CNRS Nantes University UFIP UFIP
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***  OXIDOREDUCTASE 07-APR-11 2YFQ  ***

elNémo ID: 22083011480152839

Job options:

ID        	=	 22083011480152839
JOBID     	=	 OXIDOREDUCTASE 07-APR-11 2YFQ
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    OXIDOREDUCTASE                          07-APR-11   2YFQ
TITLE     CRYSTAL STRUCTURE OF GLUTAMATE DEHYDROGENASE FROM
TITLE    2 PEPTONIPHILUS ASACCHAROLYTICUS
EXPDTA    X-RAY DIFFRACTION
REMARK   2 RESOLUTION.    2.94 ANGSTROMS
REMARK   3  R VALUE : 0.242350
REMARK   3  FREE R VALUE : 0.286930
REMARK   4 2YFQ COMPLIES WITH FORMAT V. 3.30,
REMARK 200  TEMPERATURE           (KELVIN) : 100.00
REMARK 200  PH                             : 7.00
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   BIOMT1  2   -0.500000 0.866025 0.000000   0.000000
REMARK 350   BIOMT2  2   -0.866025 -0.500000 0.000000   0.000000
REMARK 350   BIOMT3  2   0.000000 0.000000 1.000000   0.000000
REMARK 350   BIOMT1  3   -0.500000 -0.866025 0.000000   0.000000
REMARK 350   BIOMT2  3   0.866025 -0.500000 0.000000   0.000000
REMARK 350   BIOMT3  3   0.000000 0.000000 1.000000   0.000000
REMARK 888
REMARK 888 WRITTEN BY MAESTRO (A PRODUCT OF SCHRODINGER, LLC)
CRYST1  153.314  153.314  318.993  90.00  90.00 120.00 H 3 2        36
ATOM      1  N   ASN A   6      62.991   2.594  43.865  1.00 91.17           N  
ANISOU    1  N   ASN A   6    15048   7129  12462  -5510   2487   -635
ATOM      2  CA  ASN A   6      63.873   1.901  42.925  1.00 93.96           C  
ANISOU    2  CA  ASN A   6    15568   7308  12825  -5748   2570   -302
ATOM      3  C   ASN A   6      63.520   2.102  41.442  1.00 91.33           C  
ANISOU    3  C   ASN A   6    15114   7206  12380  -5433   2702    -84
ATOM      4  O   ASN A   6      64.386   2.589  40.718  1.00 92.87           O  
ANISOU    4  O   ASN A   6    15629   7074  12582  -5288   2720     99
ATOM      5  CB  ASN A   6      64.065   0.403  43.267  1.00 96.81           C  
ANISOU    5  CB  ASN A   6    15715   7873  13196  -6327   2600   -178
ATOM      6  CG  ASN A   6      65.100   0.155  44.369  1.00103.11           C  
ANISOU    6  CG  ASN A   6    16829   8217  14131  -6747   2461   -245
ATOM      7  OD1 ASN A   6      65.056   0.775  45.429  1.00106.96           O  
ANISOU    7  OD1 ASN A   6    17538   8417  14684  -6623   2321   -524
ATOM      8  ND2 ASN A   6      66.062  -0.732  44.108  1.00104.86           N  
ANISOU    8  ND2 ASN A   6    17080   8371  14390  -7256   2493      9
ATOM      9  H   ASN A   6      63.042   3.598  43.762  1.00 91.17           H  
ATOM     10  HA  ASN A   6      64.851   2.374  43.036  1.00 93.96           H  
ATOM     11  HB3 ASN A   6      64.365  -0.154  42.378  1.00 96.81           H  
ATOM     12  HB2 ASN A   6      63.122  -0.035  43.593  1.00 96.81           H  
ATOM     13 HD22 ASN A   6      66.771  -0.914  44.805  1.00104.86           H  
ATOM     14 HD21 ASN A   6      66.081  -1.216  43.222  1.00104.86           H  
ATOM     15  N   PRO A   7      62.314   1.732  40.940  1.00 87.60           N  
ANISOU   15  N   PRO A   7    14193   7288  11804  -5310   2779   -111
ATOM     16  CA  PRO A   7      62.020   1.746  39.494  1.00 86.19           C  
ANISOU   16  CA  PRO A   7    13880   7366  11502  -5141   2906    124
ATOM     17  C   PRO A   7      61.865   3.155  38.887  1.00 83.64           C  
ANISOU   17  C   PRO A   7    13745   6873  11160  -4637   2888    125
ATOM     18  O   PRO A   7      61.853   3.296  37.664  1.00 82.72           O  
ANISOU   18  O   PRO A   7    13595   6893  10941  -4457   2966    315
ATOM     19  CB  PRO A   7      60.736   0.915  39.348  1.00 83.38           C  
ANISOU   19  CB  PRO A   7    13011   7612  11056  -5127   2959     28
ATOM     20  CG  PRO A   7      60.029   1.065  40.682  1.00 84.17           C  
ANISOU   20  CG  PRO A   7    12976   7766  11237  -5389   2868   -193
ATOM     21  CD  PRO A   7      61.158   1.243  41.699  1.00 85.03           C  
ANISOU   21  CD  PRO A   7    13480   7368  11460  -5304   2742   -347
ATOM     22  HA  PRO A   7      62.825   1.246  38.951  1.00 86.19           H  
ATOM     23  HB3 PRO A   7      61.000  -0.133  39.199  1.00 83.38           H  
ATOM     24  HB2 PRO A   7      60.106   1.211  38.507  1.00 83.38           H  
ATOM     25  HG3 PRO A   7      59.369   0.230  40.915  1.00 84.17           H  
ATOM     26  HG2 PRO A   7      59.419   1.968  40.657  1.00 84.17           H  
ATOM     27  HD2 PRO A   7      60.856   1.928  42.487  1.00 85.03           H  
ATOM     28  HD3 PRO A   7      61.397   0.281  42.150  1.00 85.03           H  
ATOM     29  N   LEU A   8      61.784   4.187  39.742  1.00 82.88           N  
ANISOU   29  N   LEU A   8    13850   6488  11154  -4426   2781    -86
ATOM     30  CA  LEU A   8      61.639   5.598  39.401  1.00 80.70           C  
ANISOU   30  CA  LEU A   8    13696   6097  10871  -3934   2750   -134
ATOM     31  C   LEU A   8      62.938   6.173  38.802  1.00 83.15           C  
ANISOU   31  C   LEU A   8    14428   5954  11209  -3831   2745     62
ATOM     32  O   LEU A   8      62.858   7.028  37.923  1.00 81.78           O  
ANISOU   32  O   LEU A   8    14293   5796  10984  -3475   2763    167
ATOM     33  CB  LEU A   8      61.290   6.356  40.709  1.00 79.45           C  
ANISOU   33  CB  LEU A   8    13573   5839  10777  -3770   2650   -435
ATOM     34  CG  LEU A   8      60.206   7.448  40.589  1.00 76.67           C  
ANISOU   34  CG  LEU A   8    13042   5700  10389  -3329   2629   -566
ATOM     35  CD1 LEU A   8      59.987   8.104  41.959  1.00 79.57           C  
ANISOU   35  CD1 LEU A   8    13398   6045  10790  -3295   2546   -850
ATOM     36  CD2 LEU A   8      60.523   8.526  39.548  1.00 78.02           C  
ANISOU   36  CD2 LEU A   8    13437   5649  10557  -2944   2631   -462
ATOM     37  H   LEU A   8      61.807   3.967  40.728  1.00 82.88           H  
ATOM     38  HA  LEU A   8      60.830   5.700  38.675  1.00 80.70           H  
ATOM     39  HB3 LEU A   8      62.190   6.780  41.159  1.00 79.45           H  
ATOM     40  HB2 LEU A   8      60.927   5.644  41.454  1.00 79.45           H  
ATOM     41  HG  LEU A   8      59.272   6.970  40.291  1.00 76.67           H  
ATOM     42 HD11 LEU A   8      59.301   8.946  41.881  1.00 79.57           H  
ATOM     43 HD12 LEU A   8      59.578   7.395  42.679  1.00 79.57           H  
ATOM     44 HD13 LEU A   8      60.921   8.494  42.365  1.00 79.57           H  
ATOM     45 HD21 LEU A   8      59.774   9.321  39.556  1.00 78.02           H  
ATOM     46 HD22 LEU A   8      61.489   8.976  39.758  1.00 78.02           H  
ATOM     47 HD23 LEU A   8      60.540   8.123  38.536  1.00 78.02           H  
ATOM     48  N   VAL A   9      64.122   5.705  39.252  1.00 86.63           N  
ANISOU   48  N   VAL A   9    15190   5986  11738  -4144   2704    113
ATOM     49  CA  VAL A   9      65.434   6.220  38.836  1.00 89.33           C  
ANISOU   49  CA  VAL A   9    15980   5833  12127  -4057   2673    298
ATOM     50  C   VAL A   9      65.720   5.942  37.349  1.00 89.30           C  
ANISOU   50  C   VAL A   9    15928   5996  12008  -4005   2771    627
ATOM     51  O   VAL A   9      66.309   6.789  36.687  1.00 89.23           O  
ANISOU   51  O   VAL A   9    16087   5845  11972  -3636   2756    726
ATOM     52  CB  VAL A   9      66.581   5.674  39.741  1.00 94.15           C  
ANISOU   52  CB  VAL A   9    16959   5951  12864  -4465   2595    320
ATOM     53  CG1 VAL A   9      66.261   5.818  41.239  1.00 93.68           C  
ANISOU   53  CG1 VAL A   9    16869   5843  12883  -4585   2499    -28
ATOM     54  CG2 VAL A   9      67.070   4.246  39.423  1.00 96.82           C  
ANISOU   54  CG2 VAL A   9    17223   6393  13170  -4980   2671    607
ATOM     55  H   VAL A   9      64.114   4.977  39.952  1.00 86.63           H  
ATOM     56  HA  VAL A   9      65.400   7.302  38.968  1.00 89.33           H  
ATOM     57  HB  VAL A   9      67.439   6.323  39.561  1.00 94.15           H  
ATOM     58 HG11 VAL A   9      67.138   5.601  41.850  1.00 93.68           H  
ATOM     59 HG12 VAL A   9      65.941   6.833  41.477  1.00 93.68           H  
ATOM     60 HG13 VAL A   9      65.469   5.136  41.550  1.00 93.68           H  
ATOM     61 HG21 VAL A   9      67.769   3.890  40.182  1.00 96.82           H  
ATOM     62 HG22 VAL A   9      66.247   3.539  39.371  1.00 96.82           H  
ATOM     63 HG23 VAL A   9      67.598   4.203  38.469  1.00 96.82           H  
ATOM     64  N   ALA A  10      65.266   4.790  36.823  1.00 89.49           N  
ANISOU   64  N   ALA A  10    15693   6366  11944  -4350   2870    782
ATOM     65  CA  ALA A  10      65.445   4.368  35.434  1.00 89.74           C  
ANISOU   65  CA  ALA A  10    15651   6623  11824  -4325   2975   1088
ATOM     66  C   ALA A  10      64.612   5.214  34.459  1.00 85.90           C  
ANISOU   66  C   ALA A  10    15058   6335  11245  -3806   2974   1065
ATOM     67  O   ALA A  10      65.059   5.485  33.345  1.00 86.72           O  
ANISOU   67  O   ALA A  10    15380   6276  11293  -3601   2971   1276
ATOM     68  CB  ALA A  10      64.999   2.902  35.319  1.00 90.31           C  
ANISOU   68  CB  ALA A  10    15340   7189  11787  -4686   3095   1167
ATOM     69  H   ALA A  10      64.766   4.160  37.434  1.00 89.49           H  
ATOM     70  HA  ALA A  10      66.500   4.450  35.169  1.00 89.74           H  
ATOM     71  HB1 ALA A  10      65.115   2.532  34.299  1.00 90.31           H  
ATOM     72  HB2 ALA A  10      65.599   2.262  35.967  1.00 90.31           H  
ATOM     73  HB3 ALA A  10      63.953   2.774  35.602  1.00 90.31           H  
ATOM     74  N   ALA A  11      63.423   5.657  34.898  1.00 81.82           N  
ANISOU   74  N   ALA A  11    14211   6159  10717  -3603   2962    816
ATOM     75  CA  ALA A  11      62.520   6.518  34.149  1.00 78.52           C  
ANISOU   75  CA  ALA A  11    13666   5937  10231  -3145   2939    777
ATOM     76  C   ALA A  11      62.966   7.991  34.223  1.00 78.12           C  
ANISOU   76  C   ALA A  11    13899   5513  10271  -2772   2842    717
ATOM     77  O   ALA A  11      62.860   8.689  33.218  1.00 77.58           O  
ANISOU   77  O   ALA A  11    13850   5488  10141  -2435   2821    814
ATOM     78  CB  ALA A  11      61.124   6.357  34.767  1.00 74.76           C  
ANISOU   78  CB  ALA A  11    12771   5905   9731  -3056   2937    547
ATOM     79  H   ALA A  11      63.139   5.395  35.832  1.00 81.82           H  
ATOM     80  HA  ALA A  11      62.487   6.203  33.104  1.00 78.52           H  
ATOM     81  HB1 ALA A  11      60.368   6.876  34.183  1.00 74.76           H  
ATOM     82  HB2 ALA A  11      60.828   5.309  34.795  1.00 74.76           H  
ATOM     83  HB3 ALA A  11      61.085   6.724  35.793  1.00 74.76           H  
ATOM     84  N   GLN A  12      63.528   8.442  35.365  1.00 78.55           N  
ANISOU   84  N   GLN A  12    14160   5223  10461  -2818   2778    551
ATOM     85  CA  GLN A  12      64.150   9.761  35.550  1.00 78.23           C  
ANISOU   85  CA  GLN A  12    14393   4835  10497  -2445   2695    482
ATOM     86  C   GLN A  12      65.430   9.914  34.716  1.00 81.00           C  
ANISOU   86  C   GLN A  12    15092   4852  10831  -2382   2685    766
ATOM     87  O   GLN A  12      65.683  10.998  34.193  1.00 80.44           O  
ANISOU   87  O   GLN A  12    15140   4672  10753  -1986   2639    823
ATOM     88  CB  GLN A  12      64.537   9.969  37.031  1.00 79.52           C  
ANISOU   88  CB  GLN A  12    14745   4685  10786  -2522   2630    237
ATOM     89  CG  GLN A  12      63.375  10.421  37.928  1.00 76.08           C  
ANISOU   89  CG  GLN A  12    13990   4564  10352  -2499   2620    -48
ATOM     90  CD  GLN A  12      63.787  10.587  39.399  1.00 79.53           C  
ANISOU   90  CD  GLN A  12    14622   4719  10878  -2504   2547   -314
ATOM     91  OE1 GLN A  12      64.840  10.119  39.829  1.00 78.86           O  
ANISOU   91  OE1 GLN A  12    14353   4831  10780  -2323   2526   -537
ATOM     92  NE2 GLN A  12      62.950  11.264  40.183  1.00 85.15           N  
ANISOU   92  NE2 GLN A  12    15712   4970  11669  -2719   2500   -291
ATOM     93  H   GLN A  12      63.561   7.811  36.155  1.00 78.55           H  
ATOM     94  HA  GLN A  12      63.449  10.538  35.238  1.00 78.23           H  
ATOM     95  HB3 GLN A  12      65.317  10.728  37.110  1.00 79.52           H  
ATOM     96  HB2 GLN A  12      64.980   9.052  37.422  1.00 79.52           H  
ATOM     97  HG3 GLN A  12      62.555   9.710  37.860  1.00 76.08           H  
ATOM     98  HG2 GLN A  12      62.991  11.374  37.561  1.00 76.08           H  
ATOM     99 HE22 GLN A  12      63.161  11.385  41.164  1.00 85.15           H  
ATOM    100 HE21 GLN A  12      62.092  11.639  39.794  1.00 85.15           H  
ATOM    101  N   GLU A  13      66.211   8.828  34.572  1.00 83.98           N  
ANISOU  101  N   GLU A  13    15614   5096  11200  -2789   2727    964
ATOM    102  CA  GLU A  13      67.431   8.753  33.772  1.00 87.43           C  
ANISOU  102  CA  GLU A  13    16402   5201  11616  -2816   2717   1279
ATOM    103  C   GLU A  13      67.140   9.011  32.289  1.00 85.67           C  
ANISOU  103  C   GLU A  13    16050   5269  11232  -2552   2754   1487
ATOM    104  O   GLU A  13      67.901   9.739  31.660  1.00 87.06           O  
ANISOU  104  O   GLU A  13    16489   5190  11401  -2271   2695   1649
ATOM    105  CB  GLU A  13      68.097   7.368  33.956  1.00 90.92           C  
ANISOU  105  CB  GLU A  13    16945   5541  12060  -3370   2769   1472
ATOM    106  CG  GLU A  13      69.072   7.296  35.149  1.00 95.84           C  
ANISOU  106  CG  GLU A  13    17903   5651  12861  -3611   2680   1365
ATOM    107  CD  GLU A  13      70.352   8.092  34.910  1.00105.88           C  
ANISOU  107  CD  GLU A  13    19693   6318  14220  -3412   2575   1508
ATOM    108  OE1 GLU A  13      71.200   7.600  34.135  1.00110.44           O  
ANISOU  108  OE1 GLU A  13    20521   6670  14773  -3630   2583   1850
ATOM    109  OE2 GLU A  13      70.459   9.190  35.494  1.00107.12           O1-
ANISOU  109  OE2 GLU A  13    20005   6233  14464  -3026   2484   1281
ATOM    110  H   GLU A  13      65.947   7.990  35.070  1.00 83.98           H  
ATOM    111  HA  GLU A  13      68.112   9.534  34.110  1.00 87.43           H  
ATOM    112  HB3 GLU A  13      68.649   7.089  33.057  1.00 90.92           H  
ATOM    113  HB2 GLU A  13      67.335   6.599  34.066  1.00 90.92           H  
ATOM    114  HG3 GLU A  13      69.345   6.257  35.337  1.00 95.84           H  
ATOM    115  HG2 GLU A  13      68.597   7.659  36.059  1.00 95.84           H  
ATOM    116  N   LYS A  14      66.023   8.492  31.747  1.00 82.61           N  
ANISOU  116  N   LYS A  14    15262   5412  10713  -2622   2837   1471
ATOM    117  CA  LYS A  14      65.600   8.749  30.370  1.00 81.36           C  
ANISOU  117  CA  LYS A  14    14982   5549  10384  -2383   2859   1645
ATOM    118  C   LYS A  14      65.170  10.203  30.132  1.00 79.55           C  
ANISOU  118  C   LYS A  14    14787   5245  10194  -1873   2754   1547
ATOM    119  O   LYS A  14      65.394  10.700  29.030  1.00 80.73           O  
ANISOU  119  O   LYS A  14    15106   5299  10271  -1637   2711   1755
ATOM    120  CB  LYS A  14      64.442   7.810  29.978  1.00 78.99           C  
ANISOU  120  CB  LYS A  14    14247   5823   9941  -2499   2948   1584
ATOM    121  CG  LYS A  14      64.853   6.338  29.829  1.00 79.99           C  
ANISOU  121  CG  LYS A  14    14314   6117   9960  -2954   3073   1773
ATOM    122  CD  LYS A  14      65.900   6.065  28.741  1.00 79.07           C  
ANISOU  122  CD  LYS A  14    14379   5993   9669  -2976   3120   2135
ATOM    123  CE  LYS A  14      66.104   4.563  28.504  1.00 83.14           C  
ANISOU  123  CE  LYS A  14    14933   6529  10126  -3486   3239   2362
ATOM    124  NZ  LYS A  14      67.121   4.319  27.468  1.00 86.00           N1+
ANISOU  124  NZ  LYS A  14    15525   6837  10315  -3532   3282   2758
ATOM    125  H   LYS A  14      65.430   7.914  32.324  1.00 82.61           H  
ATOM    126  HA  LYS A  14      66.451   8.573  29.710  1.00 81.36           H  
ATOM    127  HB3 LYS A  14      64.005   8.133  29.031  1.00 78.99           H  
ATOM    128  HB2 LYS A  14      63.640   7.887  30.713  1.00 78.99           H  
ATOM    129  HG3 LYS A  14      63.959   5.779  29.576  1.00 79.99           H  
ATOM    130  HG2 LYS A  14      65.204   5.947  30.784  1.00 79.99           H  
ATOM    131  HD3 LYS A  14      66.856   6.507  29.023  1.00 79.07           H  
ATOM    132  HD2 LYS A  14      65.594   6.548  27.814  1.00 79.07           H  
ATOM    133  HE3 LYS A  14      65.169   4.096  28.193  1.00 83.14           H  
ATOM    134  HE2 LYS A  14      66.419   4.072  29.425  1.00 83.14           H  
ATOM    135  HZ1 LYS A  14      66.834   4.752  26.602  1.00 86.00           H  
ATOM    136  HZ2 LYS A  14      68.005   4.711  27.763  1.00 86.00           H  
ATOM    137  HZ3 LYS A  14      67.228   3.325  27.329  1.00 86.00           H  
ATOM    138  N   VAL A  15      64.613  10.896  31.147  1.00 76.76           N  
ANISOU  138  N   VAL A  15    14277   4939   9952  -1716   2711   1248
ATOM    139  CA  VAL A  15      64.292  12.324  31.069  1.00 75.40           C  
ANISOU  139  CA  VAL A  15    14094   4726   9829  -1254   2622   1139
ATOM    140  C   VAL A  15      65.597  13.131  31.047  1.00 79.25           C  
ANISOU  140  C   VAL A  15    14993   4730  10390  -1034   2551   1253
ATOM    141  O   VAL A  15      65.774  13.915  30.120  1.00 79.79           O  
ANISOU  141  O   VAL A  15    15120   4794  10404   -710   2494   1396
ATOM    142  CB  VAL A  15      63.389  12.807  32.242  1.00 72.78           C  
ANISOU  142  CB  VAL A  15    13566   4485   9603  -1167   2599    815
ATOM    143  CG1 VAL A  15      62.995  14.294  32.113  1.00 70.42           C  
ANISOU  143  CG1 VAL A  15    13218   4204   9333   -701   2523    744
ATOM    144  CG2 VAL A  15      62.091  12.001  32.382  1.00 69.77           C  
ANISOU  144  CG2 VAL A  15    12788   4550   9172  -1359   2646    683
ATOM    145  H   VAL A  15      64.464  10.428  32.030  1.00 76.76           H  
ATOM    146  HA  VAL A  15      63.757  12.504  30.133  1.00 75.40           H  
ATOM    147  HB  VAL A  15      63.939  12.690  33.176  1.00 72.78           H  
ATOM    148 HG11 VAL A  15      62.433  14.618  32.988  1.00 70.42           H  
ATOM    149 HG12 VAL A  15      63.851  14.958  32.020  1.00 70.42           H  
ATOM    150 HG13 VAL A  15      62.366  14.463  31.240  1.00 70.42           H  
ATOM    151 HG21 VAL A  15      61.542  12.302  33.274  1.00 69.77           H  
ATOM    152 HG22 VAL A  15      61.433  12.154  31.526  1.00 69.77           H  
ATOM    153 HG23 VAL A  15      62.279  10.936  32.467  1.00 69.77           H  
ATOM    154  N   ARG A  16      66.504  12.949  32.030  1.00 82.20           N  
ANISOU  154  N   ARG A  16    15655   4690  10888  -1198   2538   1181
ATOM    155  CA  ARG A  16      67.722  13.756  32.123  1.00 86.14           C  
ANISOU  155  CA  ARG A  16    16568   4684  11476   -951   2453   1245
ATOM    156  C   ARG A  16      68.750  13.468  31.015  1.00 89.82           C  
ANISOU  156  C   ARG A  16    17331   4921  11875   -975   2431   1613
ATOM    157  O   ARG A  16      69.442  14.403  30.636  1.00 92.26           O  
ANISOU  157  O   ARG A  16    17906   4929  12220   -630   2343   1707
ATOM    158  CB  ARG A  16      68.384  13.690  33.514  1.00 88.68           C  
ANISOU  158  CB  ARG A  16    17156   4590  11949  -1104   2421   1042
ATOM    159  CG  ARG A  16      68.965  12.348  33.988  1.00 91.94           C  
ANISOU  159  CG  ARG A  16    17758   4781  12394  -1644   2450   1157
ATOM    160  CD  ARG A  16      70.070  12.565  35.033  1.00 95.08           C  
ANISOU  160  CD  ARG A  16    18558   4618  12949  -1705   2363   1011
ATOM    161  NE  ARG A  16      71.307  13.018  34.379  1.00103.37           N  
ANISOU  161  NE  ARG A  16    20059   5160  14055  -1464   2269   1195
ATOM    162  CZ  ARG A  16      72.324  12.246  33.960  1.00111.93           C  
ANISOU  162  CZ  ARG A  16    21465   5916  15149  -1721   2244   1518
ATOM    163  NH1 ARG A  16      72.333  10.919  34.151  1.00112.22           N  
ANISOU  163  NH1 ARG A  16    21399   6111  15128  -2244   2324   1708
ATOM    164  NH2 ARG A  16      73.347  12.816  33.313  1.00115.77           N1+
ANISOU  164  NH2 ARG A  16    22374   5919  15696  -1445   2138   1669
ATOM    165  H   ARG A  16      66.314  12.279  32.764  1.00 82.20           H  
ATOM    166  HA  ARG A  16      67.409  14.794  32.000  1.00 86.14           H  
ATOM    167  HB3 ARG A  16      67.693  14.054  34.268  1.00 88.68           H  
ATOM    168  HB2 ARG A  16      69.183  14.434  33.508  1.00 88.68           H  
ATOM    169  HG3 ARG A  16      69.366  11.767  33.159  1.00 91.94           H  
ATOM    170  HG2 ARG A  16      68.168  11.750  34.422  1.00 91.94           H  
ATOM    171  HD3 ARG A  16      70.258  11.658  35.602  1.00 95.08           H  
ATOM    172  HD2 ARG A  16      69.758  13.314  35.761  1.00 95.08           H  
ATOM    173  HE  ARG A  16      71.357  14.005  34.174  1.00103.37           H  
ATOM    174 HH12 ARG A  16      73.097  10.354  33.815  1.00112.22           H  
ATOM    175 HH11 ARG A  16      71.571  10.454  34.640  1.00112.22           H  
ATOM    176 HH22 ARG A  16      74.121  12.259  32.985  1.00115.77           H  
ATOM    177 HH21 ARG A  16      73.299  13.789  33.022  1.00115.77           H  
ATOM    178  N   ILE A  17      68.824  12.248  30.446  1.00 90.58           N  
ANISOU  178  N   ILE A  17    17381   5170  11867  -1368   2510   1828
ATOM    179  CA  ILE A  17      69.660  11.931  29.275  1.00 93.42           C  
ANISOU  179  CA  ILE A  17    17965   5419  12113  -1386   2501   2208
ATOM    180  C   ILE A  17      69.087  12.596  28.006  1.00 91.09           C  
ANISOU  180  C   ILE A  17    17450   5482  11677   -981   2470   2266
ATOM    181  O   ILE A  17      69.857  13.115  27.196  1.00 92.99           O  
ANISOU  181  O   ILE A  17    17914   5521  11899   -666   2381   2442
ATOM    182  CB  ILE A  17      69.790  10.384  29.100  1.00 95.10           C  
ANISOU  182  CB  ILE A  17    18129   5796  12209  -1911   2616   2434
ATOM    183  CG1 ILE A  17      70.671   9.779  30.222  1.00 98.62           C  
ANISOU  183  CG1 ILE A  17    18886   5782  12803  -2329   2610   2468
ATOM    184  CG2 ILE A  17      70.341   9.951  27.719  1.00 96.89           C  
ANISOU  184  CG2 ILE A  17    18461   6113  12240  -1869   2629   2821
ATOM    185  CD1 ILE A  17      70.561   8.252  30.362  1.00 99.04           C  
ANISOU  185  CD1 ILE A  17    18753   6098  12777  -2900   2739   2579
ATOM    186  H   ILE A  17      68.244  11.507  30.817  1.00 90.58           H  
ATOM    187  HA  ILE A  17      70.658  12.344  29.438  1.00 93.42           H  
ATOM    188  HB  ILE A  17      68.788   9.958  29.184  1.00 95.10           H  
ATOM    189 HG13 ILE A  17      70.406  10.219  31.182  1.00 98.62           H  
ATOM    190 HG12 ILE A  17      71.714  10.053  30.062  1.00 98.62           H  
ATOM    191 HG21 ILE A  17      70.477   8.873  27.655  1.00 96.89           H  
ATOM    192 HG22 ILE A  17      69.660  10.208  26.909  1.00 96.89           H  
ATOM    193 HG23 ILE A  17      71.305  10.417  27.517  1.00 96.89           H  
ATOM    194 HD11 ILE A  17      71.095   7.913  31.251  1.00 99.04           H  
ATOM    195 HD12 ILE A  17      69.524   7.934  30.464  1.00 99.04           H  
ATOM    196 HD13 ILE A  17      70.992   7.729  29.511  1.00 99.04           H  
ATOM    197  N   ALA A  18      67.751  12.603  27.843  1.00 87.02           N  
ANISOU  197  N   ALA A  18    16502   5485  11076   -982   2525   2109
ATOM    198  CA  ALA A  18      67.059  13.250  26.729  1.00 84.84           C  
ANISOU  198  CA  ALA A  18    15995   5570  10669   -643   2477   2142
ATOM    199  C   ALA A  18      67.158  14.780  26.813  1.00 84.73           C  
ANISOU  199  C   ALA A  18    16060   5378  10757   -161   2356   2058
ATOM    200  O   ALA A  18      67.433  15.412  25.797  1.00 86.13           O  
ANISOU  200  O   ALA A  18    16360   5507  10860    119   2274   2257
ATOM    201  CB  ALA A  18      65.584  12.829  26.722  1.00 80.66           C  
ANISOU  201  CB  ALA A  18    15013   5558  10076   -719   2530   1934
ATOM    202  H   ALA A  18      67.177  12.159  28.546  1.00 87.02           H  
ATOM    203  HA  ALA A  18      67.520  12.925  25.795  1.00 84.84           H  
ATOM    204  HB1 ALA A  18      65.021  13.352  25.948  1.00 80.66           H  
ATOM    205  HB2 ALA A  18      65.485  11.762  26.525  1.00 80.66           H  
ATOM    206  HB3 ALA A  18      65.104  13.037  27.676  1.00 80.66           H  
ATOM    207  N   CYS A  19      67.011  15.364  28.017  1.00 83.21           N  
ANISOU  207  N   CYS A  19    15790   5106  10721    -66   2346   1770
ATOM    208  CA  CYS A  19      67.141  16.797  28.293  1.00 83.41           C  
ANISOU  208  CA  CYS A  19    15856   4991  10846    385   2255   1654
ATOM    209  C   CYS A  19      68.571  17.317  28.068  1.00 87.97           C  
ANISOU  209  C   CYS A  19    16873   5083  11470    598   2176   1845
ATOM    210  O   CYS A  19      68.744  18.463  27.656  1.00 88.68           O  
ANISOU  210  O   CYS A  19    16983   5141  11570   1033   2084   1877
ATOM    211  CB  CYS A  19      66.760  17.097  29.763  1.00 81.74           C  
ANISOU  211  CB  CYS A  19    15557   4727  10773    376   2284   1328
ATOM    212  SG  CYS A  19      64.972  16.993  30.049  1.00 78.41           S  
ANISOU  212  SG  CYS A  19    14594   4870  10328    326   2325   1078
ATOM    213  H   CYS A  19      66.778  14.769  28.803  1.00 83.21           H  
ATOM    214  HA  CYS A  19      66.474  17.335  27.619  1.00 83.41           H  
ATOM    215  HB3 CYS A  19      67.059  18.110  30.037  1.00 81.74           H  
ATOM    216  HB2 CYS A  19      67.279  16.425  30.446  1.00 81.74           H  
ATOM    217  HG  CYS A  19      64.869  15.688  29.772  1.00 78.41           H  
ATOM    218  N   GLU A  20      69.584  16.473  28.329  1.00 91.15           N  
ANISOU  218  N   GLU A  20    17620   5107  11904    283   2203   1980
ATOM    219  CA  GLU A  20      71.008  16.795  28.247  1.00 95.84           C  
ANISOU  219  CA  GLU A  20    18690   5165  12560    422   2116   2177
ATOM    220  C   GLU A  20      71.521  16.800  26.795  1.00 97.56           C  
ANISOU  220  C   GLU A  20    18998   5440  12630    605   2052   2527
ATOM    221  O   GLU A  20      72.411  17.590  26.485  1.00100.30           O  
ANISOU  221  O   GLU A  20    19604   5485  13018    975   1939   2640
ATOM    222  CB  GLU A  20      71.746  15.754  29.114  1.00 99.06           C  
ANISOU  222  CB  GLU A  20    19423   5172  13042    -47   2153   2249
ATOM    223  CG  GLU A  20      73.248  15.969  29.379  1.00104.10           C  
ANISOU  223  CG  GLU A  20    20595   5130  13828     87   2043   2312
ATOM    224  CD  GLU A  20      73.737  15.169  30.600  1.00106.44           C  
ANISOU  224  CD  GLU A  20    21122   5053  14267   -325   2058   2169
ATOM    225  OE1 GLU A  20      73.035  15.175  31.636  1.00104.21           O  
ANISOU  225  OE1 GLU A  20    20579   4992  14025   -466   2122   1859
ATOM    226  OE2 GLU A  20      74.823  14.561  30.485  1.00109.96           O1-
ANISOU  226  OE2 GLU A  20    22015   4978  14787   -512   1992   2372
ATOM    227  H   GLU A  20      69.352  15.554  28.677  1.00 91.15           H  
ATOM    228  HA  GLU A  20      71.168  17.785  28.676  1.00 95.84           H  
ATOM    229  HB3 GLU A  20      71.581  14.745  28.733  1.00 99.06           H  
ATOM    230  HB2 GLU A  20      71.257  15.808  30.083  1.00 99.06           H  
ATOM    231  HG3 GLU A  20      73.437  17.023  29.584  1.00104.10           H  
ATOM    232  HG2 GLU A  20      73.833  15.709  28.497  1.00104.10           H  
ATOM    233  N   LYS A  21      70.926  15.989  25.899  1.00 96.08           N  
ANISOU  233  N   LYS A  21    18600   5646  12259    364   2118   2691
ATOM    234  CA  LYS A  21      71.226  15.974  24.464  1.00 97.79           C  
ANISOU  234  CA  LYS A  21    18889   5974  12294    513   2059   3022
ATOM    235  C   LYS A  21      70.290  16.882  23.640  1.00 94.82           C  
ANISOU  235  C   LYS A  21    18172   6020  11836    922   1982   2935
ATOM    236  O   LYS A  21      70.667  17.268  22.535  1.00 96.36           O  
ANISOU  236  O   LYS A  21    18454   6229  11930   1217   1875   3149
ATOM    237  CB  LYS A  21      71.122  14.527  23.935  1.00 98.69           C  
ANISOU  237  CB  LYS A  21    19002   6276  12218     61   2166   3275
ATOM    238  CG  LYS A  21      72.400  13.715  24.228  1.00104.41           C  
ANISOU  238  CG  LYS A  21    20173   6492  13005   -285   2188   3520
ATOM    239  CD  LYS A  21      72.468  12.356  23.505  1.00106.84           C  
ANISOU  239  CD  LYS A  21    20503   6995  13097   -708   2295   3853
ATOM    240  CE  LYS A  21      71.841  11.189  24.278  1.00105.16           C  
ANISOU  240  CE  LYS A  21    20055   7013  12890  -1214   2456   3712
ATOM    241  NZ  LYS A  21      70.378  11.309  24.378  1.00100.17           N1+
ANISOU  241  NZ  LYS A  21    18940   6870  12249  -1113   2504   3348
ATOM    242  H   LYS A  21      70.203  15.365  26.231  1.00 96.08           H  
ATOM    243  HA  LYS A  21      72.239  16.339  24.288  1.00 97.79           H  
ATOM    244  HB3 LYS A  21      70.980  14.539  22.852  1.00 98.69           H  
ATOM    245  HB2 LYS A  21      70.240  14.037  24.347  1.00 98.69           H  
ATOM    246  HG3 LYS A  21      72.536  13.586  25.304  1.00104.41           H  
ATOM    247  HG2 LYS A  21      73.255  14.301  23.893  1.00104.41           H  
ATOM    248  HD3 LYS A  21      73.520  12.111  23.354  1.00106.84           H  
ATOM    249  HD2 LYS A  21      72.040  12.429  22.504  1.00106.84           H  
ATOM    250  HE3 LYS A  21      72.267  11.115  25.280  1.00105.16           H  
ATOM    251  HE2 LYS A  21      72.069  10.253  23.768  1.00105.16           H  
ATOM    252  HZ1 LYS A  21      70.146  12.129  24.924  1.00100.17           H  
ATOM    253  HZ2 LYS A  21      69.979  11.394  23.454  1.00100.17           H  
ATOM    254  HZ3 LYS A  21      70.010  10.487  24.832  1.00100.17           H  
ATOM    255  N   LEU A  22      69.117  17.277  24.171  1.00 90.77           N  
ANISOU  255  N   LEU A  22    17275   5841  11372    931   2023   2628
ATOM    256  CA  LEU A  22      68.267  18.328  23.592  1.00 88.41           C  
ANISOU  256  CA  LEU A  22    16646   5905  11041   1294   1936   2518
ATOM    257  C   LEU A  22      68.822  19.723  23.913  1.00 90.08           C  
ANISOU  257  C   LEU A  22    16957   5881  11389   1758   1829   2457
ATOM    258  O   LEU A  22      68.636  20.644  23.118  1.00 90.18           O  
ANISOU  258  O   LEU A  22    16831   6085  11347   2112   1716   2522
ATOM    259  CB  LEU A  22      66.844  18.264  24.198  1.00 83.81           C  
ANISOU  259  CB  LEU A  22    15645   5711  10488   1152   2001   2225
ATOM    260  CG  LEU A  22      65.916  17.203  23.573  1.00 81.83           C  
ANISOU  260  CG  LEU A  22    15147   5891  10053    911   2044   2266
ATOM    261  CD1 LEU A  22      64.689  16.980  24.465  1.00 76.45           C  
ANISOU  261  CD1 LEU A  22    14145   5469   9434    690   2123   1983
ATOM    262  CD2 LEU A  22      65.479  17.572  22.146  1.00 81.02           C  
ANISOU  262  CD2 LEU A  22    14881   6095   9810   1203   1913   2366
ATOM    263  H   LEU A  22      68.839  16.894  25.064  1.00 90.77           H  
ATOM    264  HA  LEU A  22      68.225  18.222  22.508  1.00 88.41           H  
ATOM    265  HB3 LEU A  22      66.341  19.229  24.102  1.00 83.81           H  
ATOM    266  HB2 LEU A  22      66.927  18.097  25.273  1.00 83.81           H  
ATOM    267  HG  LEU A  22      66.464  16.267  23.519  1.00 81.83           H  
ATOM    268 HD11 LEU A  22      64.055  16.192  24.072  1.00 76.45           H  
ATOM    269 HD12 LEU A  22      64.979  16.689  25.475  1.00 76.45           H  
ATOM    270 HD13 LEU A  22      64.084  17.885  24.541  1.00 76.45           H  
ATOM    271 HD21 LEU A  22      64.775  16.839  21.750  1.00 81.02           H  
ATOM    272 HD22 LEU A  22      64.995  18.548  22.116  1.00 81.02           H  
ATOM    273 HD23 LEU A  22      66.327  17.593  21.465  1.00 81.02           H  
ATOM    274  N   GLY A  23      69.484  19.878  25.074  1.00 91.67           N  
ANISOU  274  N   GLY A  23    17391   5679  11759   1762   1859   2324
ATOM    275  CA  GLY A  23      70.016  21.139  25.575  1.00 93.36           C  
ANISOU  275  CA  GLY A  23    17688   5681  12103   2221   1779   2212
ATOM    276  C   GLY A  23      68.951  22.075  26.162  1.00 90.22           C  
ANISOU  276  C   GLY A  23    16877   5633  11768   2393   1802   1913
ATOM    277  O   GLY A  23      69.213  23.270  26.291  1.00 91.27           O  
ANISOU  277  O   GLY A  23    16936   5783  11960   2823   1735   1841
ATOM    278  H   GLY A  23      69.587  19.072  25.676  1.00 91.67           H  
ATOM    279  HA3 GLY A  23      70.559  21.655  24.783  1.00 93.36           H  
ATOM    280  HA2 GLY A  23      70.741  20.912  26.357  1.00 93.36           H  
ATOM    281  N   CYS A  24      67.754  21.556  26.496  1.00 86.39           N  
ANISOU  281  N   CYS A  24    16116   5439  11270   2062   1896   1748
ATOM    282  CA  CYS A  24      66.650  22.313  27.090  1.00 83.71           C  
ANISOU  282  CA  CYS A  24    15396   5425  10985   2189   1914   1496
ATOM    283  C   CYS A  24      66.943  22.716  28.550  1.00 84.55           C  
ANISOU  283  C   CYS A  24    15624   5276  11224   2329   1958   1262
ATOM    284  O   CYS A  24      67.845  22.174  29.194  1.00 87.16           O  
ANISOU  284  O   CYS A  24    16345   5155  11617   2270   1971   1263
ATOM    285  CB  CYS A  24      65.336  21.505  26.967  1.00 80.08           C  
ANISOU  285  CB  CYS A  24    14603   5352  10473   1831   1980   1393
ATOM    286  SG  CYS A  24      65.347  19.947  27.894  1.00 81.39           S  
ANISOU  286  SG  CYS A  24    14940   5354  10632   1283   2103   1364
ATOM    287  H   CYS A  24      67.622  20.562  26.382  1.00 86.39           H  
ATOM    288  HA  CYS A  24      66.527  23.230  26.511  1.00 83.71           H  
ATOM    289  HB3 CYS A  24      65.134  21.276  25.920  1.00 80.08           H  
ATOM    290  HB2 CYS A  24      64.492  22.103  27.310  1.00 80.08           H  
ATOM    291  HG  CYS A  24      64.098  19.592  27.579  1.00 81.39           H  
ATOM    292  N   ASP A  25      66.174  23.702  29.040  1.00 82.41           N  
ANISOU  292  N   ASP A  25    15016   5308  10987   2518   1971   1068
ATOM    293  CA  ASP A  25      66.236  24.342  30.359  1.00 82.70           C  
ANISOU  293  CA  ASP A  25    15079   5232  11111   2705   2020    819
ATOM    294  C   ASP A  25      66.261  23.326  31.532  1.00 82.00           C  
ANISOU  294  C   ASP A  25    15156   4938  11063   2323   2111    641
ATOM    295  O   ASP A  25      65.581  22.305  31.435  1.00 79.53           O  
ANISOU  295  O   ASP A  25    14736   4768  10715   1916   2153    661
ATOM    296  CB  ASP A  25      65.058  25.356  30.398  1.00 80.08           C  
ANISOU  296  CB  ASP A  25    14272   5387  10770   2881   2027    704
ATOM    297  CG  ASP A  25      65.000  26.295  31.605  1.00 81.37           C  
ANISOU  297  CG  ASP A  25    14395   5541  10982   3106   2091    457
ATOM    298  OD1 ASP A  25      64.769  25.793  32.725  1.00 82.55           O  
ANISOU  298  OD1 ASP A  25    14652   5561  11152   2872   2169    269
ATOM    299  OD2 ASP A  25      65.178  27.511  31.387  1.00 82.54           O1-
ANISOU  299  OD2 ASP A  25    14374   5854  11132   3520   2062    449
ATOM    300  H   ASP A  25      65.462  24.063  28.422  1.00 82.41           H  
ATOM    301  HA  ASP A  25      67.170  24.904  30.361  1.00 82.70           H  
ATOM    302  HB3 ASP A  25      64.107  24.829  30.349  1.00 80.08           H  
ATOM    303  HB2 ASP A  25      65.089  25.977  29.502  1.00 80.08           H  
ATOM    304  N   PRO A  26      66.997  23.569  32.645  1.00 84.52           N  
ANISOU  304  N   PRO A  26    15743   4919  11453   2461   2129    459
ATOM    305  CA  PRO A  26      67.030  22.654  33.800  1.00 84.44           C  
ANISOU  305  CA  PRO A  26    15886   4719  11480   2101   2193    268
ATOM    306  C   PRO A  26      65.709  22.530  34.586  1.00 80.73           C  
ANISOU  306  C   PRO A  26    15024   4675  10976   1869   2267     92
ATOM    307  O   PRO A  26      65.546  21.556  35.321  1.00 80.20           O  
ANISOU  307  O   PRO A  26    14998   4559  10915   1463   2308     17
ATOM    308  CB  PRO A  26      68.187  23.151  34.678  1.00 87.72           C  
ANISOU  308  CB  PRO A  26    16610   4760  11958   2412   2176     67
ATOM    309  CG  PRO A  26      68.334  24.621  34.327  1.00 88.52           C  
ANISOU  309  CG  PRO A  26    16592   4994  12047   2960   2134    117
ATOM    310  CD  PRO A  26      67.874  24.722  32.873  1.00 88.01           C  
ANISOU  310  CD  PRO A  26    16411   5089  11940   2950   2076    426
ATOM    311  HA  PRO A  26      67.277  21.652  33.442  1.00 84.44           H  
ATOM    312  HB3 PRO A  26      69.099  22.622  34.402  1.00 87.72           H  
ATOM    313  HB2 PRO A  26      68.034  22.990  35.746  1.00 87.72           H  
ATOM    314  HG3 PRO A  26      69.346  24.996  34.482  1.00 88.52           H  
ATOM    315  HG2 PRO A  26      67.664  25.207  34.956  1.00 88.52           H  
ATOM    316  HD2 PRO A  26      67.403  25.683  32.685  1.00 88.01           H  
ATOM    317  HD3 PRO A  26      68.734  24.639  32.207  1.00 88.01           H  
ATOM    318  N   ALA A  27      64.743  23.446  34.377  1.00 78.52           N  
ANISOU  318  N   ALA A  27    14363   4808  10663   2112   2276     45
ATOM    319  CA  ALA A  27      63.384  23.359  34.909  1.00 74.96           C  
ANISOU  319  CA  ALA A  27    13540   4760  10182   1904   2329    -85
ATOM    320  C   ALA A  27      62.562  22.241  34.245  1.00 72.74           C  
ANISOU  320  C   ALA A  27    13135   4627   9874   1482   2329     30
ATOM    321  O   ALA A  27      61.632  21.743  34.871  1.00 71.44           O  
ANISOU  321  O   ALA A  27    12844   4595   9705   1181   2372    -98
ATOM    322  CB  ALA A  27      62.652  24.689  34.684  1.00 73.00           C  
ANISOU  322  CB  ALA A  27    12897   4931   9908   2208   2320    -86
ATOM    323  H   ALA A  27      64.938  24.229  33.762  1.00 78.52           H  
ATOM    324  HA  ALA A  27      63.448  23.183  35.982  1.00 74.96           H  
ATOM    325  HB1 ALA A  27      61.669  24.677  35.155  1.00 73.00           H  
ATOM    326  HB2 ALA A  27      63.208  25.523  35.113  1.00 73.00           H  
ATOM    327  HB3 ALA A  27      62.502  24.895  33.624  1.00 73.00           H  
ATOM    328  N   VAL A  28      62.908  21.820  33.013  1.00 72.63           N  
ANISOU  328  N   VAL A  28    13156   4611   9830   1480   2278    264
ATOM    329  CA  VAL A  28      62.240  20.748  32.267  1.00 70.20           C  
ANISOU  329  CA  VAL A  28    12723   4481   9469   1135   2281    374
ATOM    330  C   VAL A  28      62.442  19.397  32.965  1.00 70.50           C  
ANISOU  330  C   VAL A  28    12921   4343   9522    726   2347    292
ATOM    331  O   VAL A  28      61.466  18.671  33.145  1.00 67.96           O  
ANISOU  331  O   VAL A  28    12374   4267   9179    449   2379    219
ATOM    332  CB  VAL A  28      62.761  20.691  30.807  1.00 71.24           C  
ANISOU  332  CB  VAL A  28    12973   4556   9538   1193   2224    640
ATOM    333  CG1 VAL A  28      62.059  19.612  29.954  1.00 68.98           C  
ANISOU  333  CG1 VAL A  28    12493   4549   9168    898   2231    718
ATOM    334  CG2 VAL A  28      62.613  22.052  30.117  1.00 72.02           C  
ANISOU  334  CG2 VAL A  28    12945   4791   9628   1614   2138    725
ATOM    335  H   VAL A  28      63.695  22.267  32.563  1.00 72.63           H  
ATOM    336  HA  VAL A  28      61.171  20.968  32.248  1.00 70.20           H  
ATOM    337  HB  VAL A  28      63.824  20.445  30.824  1.00 71.24           H  
ATOM    338 HG11 VAL A  28      62.402  19.644  28.920  1.00 68.98           H  
ATOM    339 HG12 VAL A  28      62.260  18.606  30.319  1.00 68.98           H  
ATOM    340 HG13 VAL A  28      60.979  19.756  29.943  1.00 68.98           H  
ATOM    341 HG21 VAL A  28      63.003  22.019  29.102  1.00 72.02           H  
ATOM    342 HG22 VAL A  28      61.566  22.350  30.075  1.00 72.02           H  
ATOM    343 HG23 VAL A  28      63.149  22.840  30.636  1.00 72.02           H  
ATOM    344  N   TYR A  29      63.677  19.090  33.411  1.00 73.78           N  
ANISOU  344  N   TYR A  29    13726   4326   9982    689   2354    302
ATOM    345  CA  TYR A  29      63.954  17.907  34.220  1.00 74.29           C  
ANISOU  345  CA  TYR A  29    13944   4212  10070    275   2400    238
ATOM    346  C   TYR A  29      63.329  18.032  35.617  1.00 72.70           C  
ANISOU  346  C   TYR A  29    13605   4116   9901    200   2429    -46
ATOM    347  O   TYR A  29      62.798  17.037  36.087  1.00 71.26           O  
ANISOU  347  O   TYR A  29    13294   4072   9709   -148   2464   -120
ATOM    348  CB  TYR A  29      65.471  17.637  34.358  1.00 78.38           C  
ANISOU  348  CB  TYR A  29    14935   4206  10641    218   2376    333
ATOM    349  CG  TYR A  29      65.781  16.443  35.258  1.00 80.53           C  
ANISOU  349  CG  TYR A  29    15348   4297  10952   -239   2409    250
ATOM    350  CD1 TYR A  29      65.311  15.160  34.907  1.00 80.34           C  
ANISOU  350  CD1 TYR A  29    15206   4444  10875   -647   2459    388
ATOM    351  CD2 TYR A  29      66.430  16.624  36.498  1.00 83.02           C  
ANISOU  351  CD2 TYR A  29    15893   4303  11349   -260   2387     18
ATOM    352  CE1 TYR A  29      65.461  14.076  35.791  1.00 82.96           C  
ANISOU  352  CE1 TYR A  29    15626   4649  11247  -1083   2486    319
ATOM    353  CE2 TYR A  29      66.598  15.535  37.378  1.00 83.59           C  
ANISOU  353  CE2 TYR A  29    16076   4222  11460   -703   2396    -66
ATOM    354  CZ  TYR A  29      66.110  14.260  37.025  1.00 83.93           C  
ANISOU  354  CZ  TYR A  29    15978   4447  11463  -1121   2445     95
ATOM    355  OH  TYR A  29      66.261  13.204  37.875  1.00 85.93           O  
ANISOU  355  OH  TYR A  29    16306   4584  11758  -1571   2450     24
ATOM    356  H   TYR A  29      64.433  19.739  33.240  1.00 73.78           H  
ATOM    357  HA  TYR A  29      63.498  17.050  33.721  1.00 74.29           H  
ATOM    358  HB3 TYR A  29      65.978  18.523  34.742  1.00 78.38           H  
ATOM    359  HB2 TYR A  29      65.898  17.443  33.373  1.00 78.38           H  
ATOM    360  HD1 TYR A  29      64.803  15.010  33.971  1.00 80.34           H  
ATOM    361  HD2 TYR A  29      66.778  17.603  36.791  1.00 83.02           H  
ATOM    362  HE1 TYR A  29      65.073  13.106  35.522  1.00 82.96           H  
ATOM    363  HE2 TYR A  29      67.092  15.685  38.326  1.00 83.59           H  
ATOM    364  HH  TYR A  29      66.754  13.413  38.653  1.00 85.93           H  
ATOM    365  N   GLU A  30      63.373  19.213  36.261  1.00 73.37           N  
ANISOU  365  N   GLU A  30    13700   4167  10008    544   2417   -198
ATOM    366  CA  GLU A  30      62.848  19.457  37.610  1.00 72.81           C  
ANISOU  366  CA  GLU A  30    13534   4192   9940    520   2445   -469
ATOM    367  C   GLU A  30      61.318  19.262  37.707  1.00 69.06           C  
ANISOU  367  C   GLU A  30    12631   4189   9422    361   2467   -506
ATOM    368  O   GLU A  30      60.841  18.706  38.696  1.00 68.35           O  
ANISOU  368  O   GLU A  30    12465   4180   9324     96   2486   -656
ATOM    369  CB  GLU A  30      63.270  20.879  38.048  1.00 74.39           C  
ANISOU  369  CB  GLU A  30    13783   4343  10139    977   2440   -595
ATOM    370  CG  GLU A  30      62.831  21.353  39.453  1.00 74.71           C  
ANISOU  370  CG  GLU A  30    13728   4515  10145   1006   2477   -874
ATOM    371  CD  GLU A  30      63.534  20.681  40.638  1.00 78.55           C  
ANISOU  371  CD  GLU A  30    14586   4604  10656    866   2463  -1083
ATOM    372  OE1 GLU A  30      64.398  19.803  40.412  1.00 82.79           O  
ANISOU  372  OE1 GLU A  30    15441   4757  11257    642   2424  -1001
ATOM    373  OE2 GLU A  30      63.189  21.073  41.775  1.00 77.46           O1-
ANISOU  373  OE2 GLU A  30    14419   4546  10465    971   2485  -1328
ATOM    374  H   GLU A  30      63.831  19.988  35.802  1.00 73.37           H  
ATOM    375  HA  GLU A  30      63.317  18.731  38.275  1.00 72.81           H  
ATOM    376  HB3 GLU A  30      62.851  21.585  37.334  1.00 74.39           H  
ATOM    377  HB2 GLU A  30      64.352  20.981  37.959  1.00 74.39           H  
ATOM    378  HG3 GLU A  30      61.756  21.242  39.577  1.00 74.71           H  
ATOM    379  HG2 GLU A  30      63.025  22.421  39.534  1.00 74.71           H  
ATOM    380  N   LEU A  31      60.567  19.673  36.669  1.00 67.08           N  
ANISOU  380  N   LEU A  31    12112   4232   9145    520   2446   -365
ATOM    381  CA  LEU A  31      59.112  19.536  36.568  1.00 63.55           C  
ANISOU  381  CA  LEU A  31    11275   4201   8670    402   2440   -381
ATOM    382  C   LEU A  31      58.684  18.111  36.168  1.00 62.07           C  
ANISOU  382  C   LEU A  31    11020   4096   8466     26   2446   -322
ATOM    383  O   LEU A  31      57.650  17.648  36.643  1.00 60.00           O  
ANISOU  383  O   LEU A  31    10523   4079   8196   -153   2446   -414
ATOM    384  CB  LEU A  31      58.582  20.511  35.487  1.00 62.54           C  
ANISOU  384  CB  LEU A  31    10901   4333   8531    680   2390   -252
ATOM    385  CG  LEU A  31      58.606  22.005  35.884  1.00 63.06           C  
ANISOU  385  CG  LEU A  31    10888   4471   8599   1050   2395   -318
ATOM    386  CD1 LEU A  31      58.382  22.895  34.651  1.00 61.62           C  
ANISOU  386  CD1 LEU A  31    10465   4532   8416   1296   2329   -162
ATOM    387  CD2 LEU A  31      57.569  22.339  36.963  1.00 61.98           C  
ANISOU  387  CD2 LEU A  31    10570   4535   8443    989   2434   -502
ATOM    388  H   LEU A  31      61.035  20.138  35.903  1.00 67.08           H  
ATOM    389  HA  LEU A  31      58.655  19.762  37.532  1.00 63.55           H  
ATOM    390  HB3 LEU A  31      57.556  20.253  35.220  1.00 62.54           H  
ATOM    391  HB2 LEU A  31      59.162  20.369  34.574  1.00 62.54           H  
ATOM    392  HG  LEU A  31      59.585  22.249  36.291  1.00 63.06           H  
ATOM    393 HD11 LEU A  31      58.402  23.948  34.924  1.00 61.62           H  
ATOM    394 HD12 LEU A  31      59.155  22.735  33.900  1.00 61.62           H  
ATOM    395 HD13 LEU A  31      57.417  22.694  34.182  1.00 61.62           H  
ATOM    396 HD21 LEU A  31      57.573  23.406  37.185  1.00 61.98           H  
ATOM    397 HD22 LEU A  31      56.559  22.075  36.641  1.00 61.98           H  
ATOM    398 HD23 LEU A  31      57.773  21.811  37.894  1.00 61.98           H  
ATOM    399  N   LEU A  32      59.468  17.416  35.324  1.00 63.63           N  
ANISOU  399  N   LEU A  32    11422   4101   8652    -79   2451   -162
ATOM    400  CA  LEU A  32      59.207  16.039  34.882  1.00 62.55           C  
ANISOU  400  CA  LEU A  32    11220   4070   8475   -413   2475    -78
ATOM    401  C   LEU A  32      59.898  14.987  35.768  1.00 64.33           C  
ANISOU  401  C   LEU A  32    11615   4101   8726   -765   2521   -162
ATOM    402  O   LEU A  32      59.759  13.792  35.502  1.00 63.55           O  
ANISOU  402  O   LEU A  32    11380   4168   8598  -1067   2551   -153
ATOM    403  CB  LEU A  32      59.728  15.862  33.436  1.00 63.49           C  
ANISOU  403  CB  LEU A  32    11453   4133   8538   -354   2464    162
ATOM    404  CG  LEU A  32      58.923  16.641  32.377  1.00 60.87           C  
ANISOU  404  CG  LEU A  32    10860   4114   8154   -141   2401    243
ATOM    405  CD1 LEU A  32      59.635  16.617  31.021  1.00 61.43           C  
ANISOU  405  CD1 LEU A  32    11082   4110   8150    -32   2375    475
ATOM    406  CD2 LEU A  32      57.493  16.095  32.218  1.00 58.76           C  
ANISOU  406  CD2 LEU A  32    10294   4181   7851   -345   2401    175
ATOM    407  H   LEU A  32      60.298  17.864  34.962  1.00 63.63           H  
ATOM    408  HA  LEU A  32      58.141  15.820  34.929  1.00 62.55           H  
ATOM    409  HB3 LEU A  32      59.725  14.810  33.148  1.00 63.49           H  
ATOM    410  HB2 LEU A  32      60.772  16.171  33.402  1.00 63.49           H  
ATOM    411  HG  LEU A  32      58.864  17.683  32.690  1.00 60.87           H  
ATOM    412 HD11 LEU A  32      59.156  17.294  30.312  1.00 61.43           H  
ATOM    413 HD12 LEU A  32      60.680  16.913  31.107  1.00 61.43           H  
ATOM    414 HD13 LEU A  32      59.600  15.615  30.596  1.00 61.43           H  
ATOM    415 HD21 LEU A  32      56.924  16.717  31.531  1.00 58.76           H  
ATOM    416 HD22 LEU A  32      57.491  15.079  31.825  1.00 58.76           H  
ATOM    417 HD23 LEU A  32      56.936  16.098  33.153  1.00 58.76           H  
ATOM    418  N   LYS A  33      60.597  15.415  36.836  1.00 66.97           N  
ANISOU  418  N   LYS A  33    12240   4089   9116   -713   2518   -254
ATOM    419  CA  LYS A  33      61.326  14.591  37.801  1.00 69.02           C  
ANISOU  419  CA  LYS A  33    12695   4113   9416  -1031   2531   -368
ATOM    420  C   LYS A  33      60.395  13.599  38.500  1.00 67.16           C  
ANISOU  420  C   LYS A  33    12172   4183   9161  -1331   2546   -496
ATOM    421  O   LYS A  33      60.753  12.438  38.685  1.00 68.25           O  
ANISOU  421  O   LYS A  33    12357   4266   9308  -1695   2566   -478
ATOM    422  CB  LYS A  33      61.978  15.525  38.847  1.00 71.25           C  
ANISOU  422  CB  LYS A  33    13221   4105   9746   -818   2500   -558
ATOM    423  CG  LYS A  33      63.028  14.867  39.754  1.00 74.27           C  
ANISOU  423  CG  LYS A  33    13913   4124  10183  -1088   2478   -691
ATOM    424  CD  LYS A  33      63.826  15.930  40.524  1.00 77.29           C  
ANISOU  424  CD  LYS A  33    14589   4179  10596   -773   2437   -876
ATOM    425  CE  LYS A  33      64.937  15.341  41.399  1.00 83.84           C  
ANISOU  425  CE  LYS A  33    15835   4520  11500  -1035   2381   -968
ATOM    426  NZ  LYS A  33      65.724  16.413  42.031  1.00 87.10           N1+
ANISOU  426  NZ  LYS A  33    16657   4476  11960   -711   2322  -1085
ATOM    427  H   LYS A  33      60.662  16.415  36.965  1.00 66.97           H  
ATOM    428  HA  LYS A  33      62.102  14.045  37.261  1.00 69.02           H  
ATOM    429  HB3 LYS A  33      61.211  15.996  39.464  1.00 71.25           H  
ATOM    430  HB2 LYS A  33      62.468  16.349  38.340  1.00 71.25           H  
ATOM    431  HG3 LYS A  33      63.714  14.274  39.146  1.00 74.27           H  
ATOM    432  HG2 LYS A  33      62.550  14.178  40.449  1.00 74.27           H  
ATOM    433  HD3 LYS A  33      63.146  16.518  41.141  1.00 77.29           H  
ATOM    434  HD2 LYS A  33      64.270  16.626  39.811  1.00 77.29           H  
ATOM    435  HE3 LYS A  33      65.606  14.723  40.799  1.00 83.84           H  
ATOM    436  HE2 LYS A  33      64.514  14.701  42.174  1.00 83.84           H  
ATOM    437  HZ1 LYS A  33      65.117  16.984  42.603  1.00 87.10           H  
ATOM    438  HZ2 LYS A  33      66.452  16.012  42.606  1.00 87.10           H  
ATOM    439  HZ3 LYS A  33      66.138  16.994  41.316  1.00 87.10           H  
ATOM    440  N   GLU A  34      59.193  14.073  38.854  1.00 64.43           N  
ANISOU  440  N   GLU A  34    11524   4163   8792  -1181   2531   -609
ATOM    441  CA  GLU A  34      58.194  13.353  39.619  1.00 62.89           C  
ANISOU  441  CA  GLU A  34    11069   4243   8583  -1408   2524   -750
ATOM    442  C   GLU A  34      56.778  13.773  39.197  1.00 59.77           C  
ANISOU  442  C   GLU A  34    10306   4245   8159  -1275   2497   -758
ATOM    443  O   GLU A  34      56.606  14.836  38.595  1.00 59.33           O  
ANISOU  443  O   GLU A  34    10182   4261   8100   -973   2476   -706
ATOM    444  CB  GLU A  34      58.477  13.549  41.122  1.00 64.20           C  
ANISOU  444  CB  GLU A  34    11362   4267   8765  -1467   2502   -978
ATOM    445  CG  GLU A  34      59.291  12.379  41.711  1.00 67.95           C  
ANISOU  445  CG  GLU A  34    11992   4558   9268  -1870   2500  -1018
ATOM    446  CD  GLU A  34      59.663  12.574  43.175  1.00 70.11           C  
ANISOU  446  CD  GLU A  34    12464   4622   9554  -1926   2457  -1246
ATOM    447  OE1 GLU A  34      58.981  13.379  43.844  1.00 69.54           O  
ANISOU  447  OE1 GLU A  34    12288   4698   9438  -1714   2439  -1402
ATOM    448  OE2 GLU A  34      60.625  11.901  43.601  1.00 75.30           O1-
ANISOU  448  OE2 GLU A  34    13383   4969  10259  -2190   2435  -1266
ATOM    449  H   GLU A  34      58.969  15.027  38.606  1.00 64.43           H  
ATOM    450  HA  GLU A  34      58.292  12.296  39.361  1.00 62.89           H  
ATOM    451  HB3 GLU A  34      57.541  13.642  41.675  1.00 64.20           H  
ATOM    452  HB2 GLU A  34      58.997  14.494  41.293  1.00 64.20           H  
ATOM    453  HG3 GLU A  34      60.218  12.248  41.158  1.00 67.95           H  
ATOM    454  HG2 GLU A  34      58.739  11.444  41.620  1.00 67.95           H  
ATOM    455  N   PRO A  35      55.756  12.953  39.529  1.00 57.93           N  
ANISOU  455  N   PRO A  35     9832   4267   7912  -1502   2484   -821
ATOM    456  CA  PRO A  35      54.351  13.238  39.233  1.00 54.71           C  
ANISOU  456  CA  PRO A  35     9094   4203   7490  -1402   2436   -824
ATOM    457  C   PRO A  35      53.793  14.492  39.914  1.00 53.48           C  
ANISOU  457  C   PRO A  35     8859   4124   7339  -1157   2398   -901
ATOM    458  O   PRO A  35      54.127  14.789  41.061  1.00 54.85           O  
ANISOU  458  O   PRO A  35     9152   4187   7502  -1140   2409  -1031
ATOM    459  CB  PRO A  35      53.560  11.983  39.646  1.00 54.36           C  
ANISOU  459  CB  PRO A  35     8875   4341   7438  -1686   2422   -927
ATOM    460  CG  PRO A  35      54.518  11.120  40.440  1.00 57.38           C  
ANISOU  460  CG  PRO A  35     9455   4523   7825  -1965   2475   -917
ATOM    461  CD  PRO A  35      55.914  11.653  40.182  1.00 58.70           C  
ANISOU  461  CD  PRO A  35     9958   4331   8015  -1860   2498   -902
ATOM    462  HA  PRO A  35      54.303  13.401  38.160  1.00 54.71           H  
ATOM    463  HB3 PRO A  35      53.237  11.399  38.792  1.00 54.36           H  
ATOM    464  HB2 PRO A  35      52.658  12.206  40.219  1.00 54.36           H  
ATOM    465  HG3 PRO A  35      54.425  10.075  40.152  1.00 57.38           H  
ATOM    466  HG2 PRO A  35      54.313  11.212  41.503  1.00 57.38           H  
ATOM    467  HD2 PRO A  35      56.463  11.710  41.121  1.00 58.70           H  
ATOM    468  HD3 PRO A  35      56.447  10.971  39.517  1.00 58.70           H  
ATOM    469  N   GLN A  36      52.908  15.191  39.185  1.00 51.44           N  
ANISOU  469  N   GLN A  36     8391   4069   7086   -978   2349   -820
ATOM    470  CA  GLN A  36      52.173  16.381  39.619  1.00 49.77           C  
ANISOU  470  CA  GLN A  36     8047   3990   6875   -772   2312   -849
ATOM    471  C   GLN A  36      51.206  16.084  40.774  1.00 48.92           C  
ANISOU  471  C   GLN A  36     7780   4059   6749   -908   2278   -973
ATOM    472  O   GLN A  36      50.965  16.964  41.600  1.00 49.56           O  
ANISOU  472  O   GLN A  36     7828   4205   6798   -797   2278  -1034
ATOM    473  CB  GLN A  36      51.365  16.935  38.429  1.00 48.03           C  
ANISOU  473  CB  GLN A  36     7633   3937   6679   -609   2244   -714
ATOM    474  CG  GLN A  36      52.246  17.556  37.327  1.00 49.10           C  
ANISOU  474  CG  GLN A  36     7904   3931   6818   -396   2260   -592
ATOM    475  CD  GLN A  36      51.483  17.951  36.058  1.00 50.04           C  
ANISOU  475  CD  GLN A  36     7845   4210   6956   -280   2171   -465
ATOM    476  OE1 GLN A  36      52.100  18.146  35.016  1.00 50.23           O  
ANISOU  476  OE1 GLN A  36     7638   4437   7010   -255   2090   -460
ATOM    477  NE2 GLN A  36      50.152  18.041  36.105  1.00 54.82           N  
ANISOU  477  NE2 GLN A  36     8571   4717   7542   -215   2172   -356
ATOM    478  H   GLN A  36      52.708  14.858  38.250  1.00 51.44           H  
ATOM    479  HA  GLN A  36      52.879  17.142  39.945  1.00 49.77           H  
ATOM    480  HB3 GLN A  36      50.671  17.697  38.787  1.00 48.03           H  
ATOM    481  HB2 GLN A  36      50.751  16.135  38.010  1.00 48.03           H  
ATOM    482  HG3 GLN A  36      53.044  16.873  37.044  1.00 49.10           H  
ATOM    483  HG2 GLN A  36      52.740  18.446  37.718  1.00 49.10           H  
ATOM    484 HE22 GLN A  36      49.629  18.275  35.270  1.00 54.82           H  
ATOM    485 HE21 GLN A  36      49.669  17.862  36.972  1.00 54.82           H  
ATOM    486  N   ARG A  37      50.667  14.856  40.825  1.00 48.37           N  
ANISOU  486  N   ARG A  37     7607   4088   6684  -1139   2250  -1007
ATOM    487  CA  ARG A  37      49.703  14.389  41.809  1.00 47.92           C  
ANISOU  487  CA  ARG A  37     7380   4220   6609  -1263   2195  -1111
ATOM    488  C   ARG A  37      49.754  12.859  41.907  1.00 48.32           C  
ANISOU  488  C   ARG A  37     7385   4314   6660  -1535   2191  -1170
ATOM    489  O   ARG A  37      49.678  12.189  40.882  1.00 48.01           O  
ANISOU  489  O   ARG A  37     7287   4316   6638  -1587   2196  -1096
ATOM    490  CB  ARG A  37      48.310  14.953  41.451  1.00 46.33           C  
ANISOU  490  CB  ARG A  37     6922   4246   6434  -1143   2100  -1032
ATOM    491  CG  ARG A  37      47.154  14.485  42.352  1.00 46.57           C  
ANISOU  491  CG  ARG A  37     6770   4478   6448  -1231   2020  -1098
ATOM    492  CD  ARG A  37      45.807  15.070  41.907  1.00 45.71           C  
ANISOU  492  CD  ARG A  37     6443   4537   6389  -1123   1908   -991
ATOM    493  NE  ARG A  37      45.387  14.502  40.613  1.00 46.22           N  
ANISOU  493  NE  ARG A  37     6441   4609   6512  -1116   1858   -930
ATOM    494  CZ  ARG A  37      45.298  15.146  39.436  1.00 44.54           C  
ANISOU  494  CZ  ARG A  37     6197   4385   6343   -964   1814   -819
ATOM    495  NH1 ARG A  37      45.602  16.447  39.321  1.00 47.36           N  
ANISOU  495  NH1 ARG A  37     6559   4730   6705   -815   1819   -738
ATOM    496  NH2 ARG A  37      44.900  14.471  38.350  1.00 44.97           N1+
ANISOU  496  NH2 ARG A  37     6203   4459   6425   -955   1760   -794
ATOM    497  H   ARG A  37      50.930  14.196  40.104  1.00 48.37           H  
ATOM    498  HA  ARG A  37      49.994  14.793  42.776  1.00 47.92           H  
ATOM    499  HB3 ARG A  37      48.084  14.685  40.418  1.00 46.33           H  
ATOM    500  HB2 ARG A  37      48.343  16.043  41.473  1.00 46.33           H  
ATOM    501  HG3 ARG A  37      47.357  14.777  43.383  1.00 46.57           H  
ATOM    502  HG2 ARG A  37      47.084  13.398  42.350  1.00 46.57           H  
ATOM    503  HD3 ARG A  37      45.844  16.159  41.881  1.00 45.71           H  
ATOM    504  HD2 ARG A  37      45.046  14.813  42.645  1.00 45.71           H  
ATOM    505  HE  ARG A  37      45.154  13.519  40.632  1.00 46.22           H  
ATOM    506 HH12 ARG A  37      45.538  16.914  38.428  1.00 47.36           H  
ATOM    507 HH11 ARG A  37      45.910  16.964  40.130  1.00 47.36           H  
ATOM    508 HH22 ARG A  37      44.840  14.928  37.452  1.00 44.97           H  
ATOM    509 HH21 ARG A  37      44.661  13.491  38.414  1.00 44.97           H  
ATOM    510  N   VAL A  38      49.823  12.317  43.134  1.00 49.60           N  
ANISOU  510  N   VAL A  38     7562   4492   6790  -1707   2181  -1305
ATOM    511  CA  VAL A  38      49.659  10.898  43.457  1.00 50.43           C  
ANISOU  511  CA  VAL A  38     7551   4712   6896  -1967   2159  -1361
ATOM    512  C   VAL A  38      48.707  10.782  44.640  1.00 50.53           C  
ANISOU  512  C   VAL A  38     7400   4924   6876  -2027   2071  -1470
ATOM    513  O   VAL A  38      49.028  11.258  45.724  1.00 51.49           O  
ANISOU  513  O   VAL A  38     7627   4992   6943  -2017   2065  -1571
ATOM    514  CB  VAL A  38      50.999  10.170  43.737  1.00 53.04           C  
ANISOU  514  CB  VAL A  38     8089   4837   7226  -2211   2227  -1407
ATOM    515  CG1 VAL A  38      50.793   8.647  43.869  1.00 53.28           C  
ANISOU  515  CG1 VAL A  38     7937   5051   7257  -2490   2207  -1446
ATOM    516  CG2 VAL A  38      52.072  10.465  42.690  1.00 53.27           C  
ANISOU  516  CG2 VAL A  38     8312   4652   7278  -2155   2309  -1272
ATOM    517  H   VAL A  38      49.922  12.946  43.922  1.00 49.60           H  
ATOM    518  HA  VAL A  38      49.183  10.412  42.610  1.00 50.43           H  
ATOM    519  HB  VAL A  38      51.400  10.523  44.688  1.00 53.04           H  
ATOM    520 HG11 VAL A  38      51.744   8.133  44.007  1.00 53.28           H  
ATOM    521 HG12 VAL A  38      50.166   8.394  44.722  1.00 53.28           H  
ATOM    522 HG13 VAL A  38      50.318   8.232  42.980  1.00 53.28           H  
ATOM    523 HG21 VAL A  38      52.953   9.844  42.846  1.00 53.27           H  
ATOM    524 HG22 VAL A  38      51.701  10.286  41.685  1.00 53.27           H  
ATOM    525 HG23 VAL A  38      52.391  11.506  42.745  1.00 53.27           H  
ATOM    526  N   ILE A  39      47.567  10.114  44.440  1.00 49.43           N  
ANISOU  526  N   ILE A  39     7009   5016   6756  -2067   1997  -1454
ATOM    527  CA  ILE A  39      46.578   9.848  45.474  1.00 49.77           C  
ANISOU  527  CA  ILE A  39     6881   5261   6768  -2128   1894  -1538
ATOM    528  C   ILE A  39      46.731   8.368  45.856  1.00 51.45           C  
ANISOU  528  C   ILE A  39     7001   5574   6974  -2392   1881  -1628
ATOM    529  O   ILE A  39      46.587   7.510  44.992  1.00 52.37           O  
ANISOU  529  O   ILE A  39     7022   5751   7124  -2458   1913  -1583
ATOM    530  CB  ILE A  39      45.154  10.124  44.914  1.00 47.76           C  
ANISOU  530  CB  ILE A  39     6402   5193   6549  -1968   1786  -1457
ATOM    531  CG1 ILE A  39      45.000  11.515  44.253  1.00 47.05           C  
ANISOU  531  CG1 ILE A  39     6369   5031   6476  -1739   1788  -1347
ATOM    532  CG2 ILE A  39      44.099   9.965  46.027  1.00 48.16           C  
ANISOU  532  CG2 ILE A  39     6293   5443   6564  -2024   1666  -1522
ATOM    533  CD1 ILE A  39      43.895  11.560  43.191  1.00 46.50           C  
ANISOU  533  CD1 ILE A  39     6162   5021   6485  -1597   1714  -1234
ATOM    534  H   ILE A  39      47.387   9.731  43.520  1.00 49.43           H  
ATOM    535  HA  ILE A  39      46.736  10.480  46.344  1.00 49.77           H  
ATOM    536  HB  ILE A  39      44.954   9.383  44.139  1.00 47.76           H  
ATOM    537 HG13 ILE A  39      45.914  11.829  43.756  1.00 47.05           H  
ATOM    538 HG12 ILE A  39      44.812  12.273  45.007  1.00 47.05           H  
ATOM    539 HG21 ILE A  39      43.097  10.215  45.680  1.00 48.16           H  
ATOM    540 HG22 ILE A  39      44.073   8.944  46.394  1.00 48.16           H  
ATOM    541 HG23 ILE A  39      44.323  10.614  46.874  1.00 48.16           H  
ATOM    542 HD11 ILE A  39      43.832  12.558  42.758  1.00 46.50           H  
ATOM    543 HD12 ILE A  39      44.100  10.862  42.379  1.00 46.50           H  
ATOM    544 HD13 ILE A  39      42.918  11.315  43.606  1.00 46.50           H  
ATOM    545  N   GLU A  40      47.001   8.081  47.138  1.00 52.67           N  
ANISOU  545  N   GLU A  40     7171   5768   7073  -2539   1833  -1755
ATOM    546  CA  GLU A  40      46.924   6.761  47.762  1.00 54.41           C  
ANISOU  546  CA  GLU A  40     7263   6125   7287  -2805   1794  -1845
ATOM    547  C   GLU A  40      45.609   6.688  48.551  1.00 54.30           C  
ANISOU  547  C   GLU A  40     7023   6376   7235  -2778   1652  -1897
ATOM    548  O   GLU A  40      45.258   7.649  49.228  1.00 55.23           O  
ANISOU  548  O   GLU A  40     7208   6499   7280  -2717   1596  -1951
ATOM    549  CB  GLU A  40      48.110   6.591  48.743  1.00 56.86           C  
ANISOU  549  CB  GLU A  40     7798   6242   7564  -3035   1827  -1963
ATOM    550  CG  GLU A  40      48.090   5.264  49.537  1.00 59.68           C  
ANISOU  550  CG  GLU A  40     8005   6762   7907  -3341   1756  -2069
ATOM    551  CD  GLU A  40      49.303   5.086  50.448  1.00 63.27           C  
ANISOU  551  CD  GLU A  40     8704   6992   8345  -3602   1762  -2194
ATOM    552  OE1 GLU A  40      50.441   5.199  49.946  1.00 64.47           O  
ANISOU  552  OE1 GLU A  40     9076   6874   8546  -3681   1859  -2140
ATOM    553  OE2 GLU A  40      49.070   4.826  51.649  1.00 64.00           O1-
ANISOU  553  OE2 GLU A  40     8776   7170   8373  -3734   1653  -2345
ATOM    554  H   GLU A  40      47.126   8.864  47.771  1.00 52.67           H  
ATOM    555  HA  GLU A  40      46.965   5.982  47.006  1.00 54.41           H  
ATOM    556  HB3 GLU A  40      48.132   7.426  49.444  1.00 56.86           H  
ATOM    557  HB2 GLU A  40      49.034   6.662  48.175  1.00 56.86           H  
ATOM    558  HG3 GLU A  40      48.049   4.417  48.851  1.00 59.68           H  
ATOM    559  HG2 GLU A  40      47.197   5.196  50.157  1.00 59.68           H  
ATOM    560  N   ILE A  41      44.907   5.549  48.495  1.00 53.71           N  
ANISOU  560  N   ILE A  41     6683   6531   7194  -2811   1591  -1883
ATOM    561  CA  ILE A  41      43.631   5.303  49.171  1.00 53.27           C  
ANISOU  561  CA  ILE A  41     6410   6720   7111  -2758   1435  -1916
ATOM    562  C   ILE A  41      43.613   3.931  49.848  1.00 55.08           C  
ANISOU  562  C   ILE A  41     6424   7177   7326  -2977   1366  -2013
ATOM    563  O   ILE A  41      44.160   2.967  49.319  1.00 56.09           O  
ANISOU  563  O   ILE A  41     6503   7327   7483  -3161   1446  -2029
ATOM    564  CB  ILE A  41      42.427   5.504  48.208  1.00 51.63           C  
ANISOU  564  CB  ILE A  41     6051   6602   6965  -2511   1368  -1808
ATOM    565  CG1 ILE A  41      42.600   4.745  46.869  1.00 51.34           C  
ANISOU  565  CG1 ILE A  41     5936   6578   6991  -2495   1451  -1769
ATOM    566  CG2 ILE A  41      42.128   6.993  47.980  1.00 50.84           C  
ANISOU  566  CG2 ILE A  41     6100   6352   6866  -2308   1374  -1710
ATOM    567  CD1 ILE A  41      41.303   4.607  46.067  1.00 50.45           C  
ANISOU  567  CD1 ILE A  41     5659   6572   6938  -2262   1356  -1711
ATOM    568  H   ILE A  41      45.273   4.796  47.925  1.00 53.71           H  
ATOM    569  HA  ILE A  41      43.532   6.019  49.987  1.00 53.27           H  
ATOM    570  HB  ILE A  41      41.546   5.092  48.706  1.00 51.63           H  
ATOM    571 HG13 ILE A  41      42.977   3.739  47.054  1.00 51.34           H  
ATOM    572 HG12 ILE A  41      43.351   5.239  46.253  1.00 51.34           H  
ATOM    573 HG21 ILE A  41      41.205   7.137  47.424  1.00 50.84           H  
ATOM    574 HG22 ILE A  41      42.015   7.529  48.920  1.00 50.84           H  
ATOM    575 HG23 ILE A  41      42.928   7.467  47.422  1.00 50.84           H  
ATOM    576 HD11 ILE A  41      41.480   4.081  45.128  1.00 50.45           H  
ATOM    577 HD12 ILE A  41      40.545   4.061  46.625  1.00 50.45           H  
ATOM    578 HD13 ILE A  41      40.886   5.579  45.826  1.00 50.45           H  
ATOM    579  N   SER A  42      42.923   3.846  50.994  1.00 55.40           N  
ANISOU  579  N   SER A  42     6330   7407   7314  -2962   1214  -2064
ATOM    580  CA  SER A  42      42.554   2.604  51.667  1.00 57.22           C  
ANISOU  580  CA  SER A  42     6322   7894   7526  -3142   1118  -2155
ATOM    581  C   SER A  42      41.129   2.254  51.214  1.00 56.33           C  
ANISOU  581  C   SER A  42     5942   8002   7457  -2933   1002  -2097
ATOM    582  O   SER A  42      40.193   2.997  51.509  1.00 55.96           O  
ANISOU  582  O   SER A  42     5883   7992   7388  -2754    876  -2048
ATOM    583  CB  SER A  42      42.531   2.867  53.187  1.00 59.11           C  
ANISOU  583  CB  SER A  42     6613   8194   7654  -3263   1002  -2265
ATOM    584  OG  SER A  42      43.815   2.675  53.745  1.00 61.46           O  
ANISOU  584  OG  SER A  42     7127   8312   7913  -3509   1074  -2372
ATOM    585  H   SER A  42      42.507   4.693  51.354  1.00 55.40           H  
ATOM    586  HA  SER A  42      43.234   1.782  51.430  1.00 57.22           H  
ATOM    587  HB3 SER A  42      41.844   2.199  53.702  1.00 59.11           H  
ATOM    588  HB2 SER A  42      42.182   3.871  53.412  1.00 59.11           H  
ATOM    589  HG  SER A  42      43.769   2.883  54.667  1.00 61.46           H  
ATOM    590  N   ILE A  43      40.978   1.141  50.478  1.00 56.58           N  
ANISOU  590  N   ILE A  43     5766   8183   7547  -2949   1041  -2098
ATOM    591  CA  ILE A  43      39.713   0.677  49.911  1.00 55.68           C  
ANISOU  591  CA  ILE A  43     5412   8258   7484  -2711    935  -2066
ATOM    592  C   ILE A  43      39.219  -0.505  50.770  1.00 58.16           C  
ANISOU  592  C   ILE A  43     5428   8895   7774  -2791    802  -2150
ATOM    593  O   ILE A  43      39.766  -1.601  50.629  1.00 60.31           O  
ANISOU  593  O   ILE A  43     5518   9351   8046  -2971    870  -2208
ATOM    594  CB  ILE A  43      39.931   0.196  48.445  1.00 55.06           C  
ANISOU  594  CB  ILE A  43     5274   8185   7462  -2622   1062  -2032
ATOM    595  CG1 ILE A  43      40.535   1.295  47.546  1.00 53.42           C  
ANISOU  595  CG1 ILE A  43     5362   7669   7268  -2597   1207  -1952
ATOM    596  CG2 ILE A  43      38.600  -0.304  47.835  1.00 54.75           C  
ANISOU  596  CG2 ILE A  43     5043   8283   7478  -2316    935  -2020
ATOM    597  CD1 ILE A  43      41.211   0.739  46.289  1.00 53.32           C  
ANISOU  597  CD1 ILE A  43     5327   7657   7277  -2542   1346  -1914
ATOM    598  H   ILE A  43      41.802   0.592  50.262  1.00 56.58           H  
ATOM    599  HA  ILE A  43      38.987   1.489  49.880  1.00 55.68           H  
ATOM    600  HB  ILE A  43      40.639  -0.634  48.445  1.00 55.06           H  
ATOM    601 HG13 ILE A  43      41.289   1.873  48.078  1.00 53.42           H  
ATOM    602 HG12 ILE A  43      39.756   2.005  47.269  1.00 53.42           H  
ATOM    603 HG21 ILE A  43      38.661  -0.440  46.757  1.00 54.75           H  
ATOM    604 HG22 ILE A  43      38.288  -1.259  48.258  1.00 54.75           H  
ATOM    605 HG23 ILE A  43      37.804   0.415  48.026  1.00 54.75           H  
ATOM    606 HD11 ILE A  43      41.622   1.561  45.709  1.00 53.32           H  
ATOM    607 HD12 ILE A  43      42.033   0.069  46.543  1.00 53.32           H  
ATOM    608 HD13 ILE A  43      40.516   0.196  45.650  1.00 53.32           H  
ATOM    609  N   PRO A  44      38.183  -0.331  51.619  1.00 58.40           N  
ANISOU  609  N   PRO A  44     5393   9018   7777  -2665    608  -2143
ATOM    610  CA  PRO A  44      37.583  -1.438  52.370  1.00 60.92           C  
ANISOU  610  CA  PRO A  44     5406   9668   8073  -2711    459  -2219
ATOM    611  C   PRO A  44      36.648  -2.251  51.463  1.00 61.66           C  
ANISOU  611  C   PRO A  44     5223   9962   8243  -2480    415  -2220
ATOM    612  O   PRO A  44      35.793  -1.690  50.776  1.00 60.19           O  
ANISOU  612  O   PRO A  44     5091   9655   8122  -2194    372  -2152
ATOM    613  CB  PRO A  44      36.796  -0.754  53.492  1.00 60.53           C  
ANISOU  613  CB  PRO A  44     5412   9628   7959  -2614    262  -2182
ATOM    614  CG  PRO A  44      36.399   0.598  52.922  1.00 58.87           C  
ANISOU  614  CG  PRO A  44     5442   9143   7781  -2413    288  -2056
ATOM    615  CD  PRO A  44      37.531   0.939  51.953  1.00 56.67           C  
ANISOU  615  CD  PRO A  44     5353   8636   7543  -2484    513  -2049
ATOM    616  HA  PRO A  44      38.347  -2.089  52.802  1.00 60.92           H  
ATOM    617  HB3 PRO A  44      37.465  -0.604  54.336  1.00 60.53           H  
ATOM    618  HB2 PRO A  44      35.942  -1.331  53.850  1.00 60.53           H  
ATOM    619  HG3 PRO A  44      36.260   1.356  53.693  1.00 58.87           H  
ATOM    620  HG2 PRO A  44      35.458   0.506  52.376  1.00 58.87           H  
ATOM    621  HD2 PRO A  44      37.136   1.448  51.072  1.00 56.67           H  
ATOM    622  HD3 PRO A  44      38.250   1.595  52.443  1.00 56.67           H  
ATOM    623  N   VAL A  45      36.813  -3.578  51.488  1.00 64.33           N  
ANISOU  623  N   VAL A  45     5261  10609   8571  -2601    423  -2305
ATOM    624  CA  VAL A  45      35.928  -4.538  50.839  1.00 65.59           C  
ANISOU  624  CA  VAL A  45     5115  11025   8781  -2349    362  -2336
ATOM    625  C   VAL A  45      35.286  -5.351  51.961  1.00 67.92           C  
ANISOU  625  C   VAL A  45     5103  11656   9049  -2338    161  -2398
ATOM    626  O   VAL A  45      35.995  -5.974  52.753  1.00 69.77           O  
ANISOU  626  O   VAL A  45     5198  12084   9228  -2637    171  -2460
ATOM    627  CB  VAL A  45      36.745  -5.447  49.882  1.00 66.70           C  
ANISOU  627  CB  VAL A  45     5105  11312   8925  -2437    574  -2370
ATOM    628  CG1 VAL A  45      35.906  -6.572  49.240  1.00 68.35           C  
ANISOU  628  CG1 VAL A  45     4962  11852   9158  -2158    508  -2433
ATOM    629  CG2 VAL A  45      37.432  -4.633  48.774  1.00 64.09           C  
ANISOU  629  CG2 VAL A  45     5069  10666   8618  -2382    746  -2299
ATOM    630  H   VAL A  45      37.560  -3.960  52.053  1.00 64.33           H  
ATOM    631  HA  VAL A  45      35.144  -4.040  50.263  1.00 65.59           H  
ATOM    632  HB  VAL A  45      37.525  -5.929  50.470  1.00 66.70           H  
ATOM    633 HG11 VAL A  45      36.510  -7.165  48.551  1.00 68.35           H  
ATOM    634 HG12 VAL A  45      35.506  -7.265  49.979  1.00 68.35           H  
ATOM    635 HG13 VAL A  45      35.068  -6.165  48.675  1.00 68.35           H  
ATOM    636 HG21 VAL A  45      38.038  -5.282  48.143  1.00 64.09           H  
ATOM    637 HG22 VAL A  45      36.698  -4.135  48.139  1.00 64.09           H  
ATOM    638 HG23 VAL A  45      38.096  -3.869  49.176  1.00 64.09           H  
ATOM    639  N   LYS A  46      33.943  -5.387  51.979  1.00 68.08           N  
ANISOU  639  N   LYS A  46     5031  11724   9111  -1996    -38  -2377
ATOM    640  CA  LYS A  46      33.166  -6.330  52.772  1.00 71.23           C  
ANISOU  640  CA  LYS A  46     5109  12461   9495  -1905   -244  -2430
ATOM    641  C   LYS A  46      33.211  -7.683  52.048  1.00 73.61           C  
ANISOU  641  C   LYS A  46     5051  13100   9818  -1839   -148  -2524
ATOM    642  O   LYS A  46      32.495  -7.901  51.070  1.00 73.92           O  
ANISOU  642  O   LYS A  46     5036  13134   9917  -1513   -141  -2541
ATOM    643  CB  LYS A  46      31.710  -5.839  52.890  1.00 70.89           C  
ANISOU  643  CB  LYS A  46     5125  12309   9503  -1538   -489  -2355
ATOM    644  CG  LYS A  46      31.486  -4.899  54.083  1.00 72.53           C  
ANISOU  644  CG  LYS A  46     5494  12429   9637  -1626   -663  -2271
ATOM    645  CD  LYS A  46      30.057  -4.338  54.095  1.00 72.10           C  
ANISOU  645  CD  LYS A  46     5675  12084   9636  -1345   -822  -2121
ATOM    646  CE  LYS A  46      29.644  -3.809  55.469  1.00 75.50           C  
ANISOU  646  CE  LYS A  46     6048  12643   9995  -1283  -1100  -2046
ATOM    647  NZ  LYS A  46      28.282  -3.251  55.444  1.00 74.35           N1+
ANISOU  647  NZ  LYS A  46     6140  12224   9886  -1070  -1269  -1855
ATOM    648  H   LYS A  46      33.439  -4.838  51.296  1.00 68.08           H  
ATOM    649  HA  LYS A  46      33.591  -6.421  53.770  1.00 71.23           H  
ATOM    650  HB3 LYS A  46      31.041  -6.692  53.026  1.00 70.89           H  
ATOM    651  HB2 LYS A  46      31.388  -5.361  51.966  1.00 70.89           H  
ATOM    652  HG3 LYS A  46      32.203  -4.079  54.065  1.00 72.53           H  
ATOM    653  HG2 LYS A  46      31.676  -5.454  55.004  1.00 72.53           H  
ATOM    654  HD3 LYS A  46      29.355  -5.120  53.804  1.00 72.10           H  
ATOM    655  HD2 LYS A  46      29.970  -3.553  53.342  1.00 72.10           H  
ATOM    656  HE3 LYS A  46      30.341  -3.043  55.806  1.00 75.50           H  
ATOM    657  HE2 LYS A  46      29.672  -4.617  56.199  1.00 75.50           H  
ATOM    658  HZ1 LYS A  46      28.268  -2.441  54.838  1.00 74.35           H  
ATOM    659  HZ2 LYS A  46      27.633  -3.945  55.102  1.00 74.35           H  
ATOM    660  HZ3 LYS A  46      28.019  -2.971  56.378  1.00 74.35           H  
ATOM    661  N   MET A  47      34.092  -8.570  52.529  1.00 75.59           N  
ANISOU  661  N   MET A  47     5059  13648  10013  -2158    -72  -2588
ATOM    662  CA  MET A  47      34.370  -9.904  52.004  1.00 77.76           C  
ANISOU  662  CA  MET A  47     4980  14279  10285  -2173     72  -2656
ATOM    663  C   MET A  47      33.148 -10.820  52.202  1.00 80.72           C  
ANISOU  663  C   MET A  47     4966  15025  10680  -1830   -115  -2727
ATOM    664  O   MET A  47      32.334 -10.581  53.096  1.00 81.25           O  
ANISOU  664  O   MET A  47     5018  15099  10754  -1686   -368  -2717
ATOM    665  CB  MET A  47      35.595 -10.475  52.753  1.00 79.93           C  
ANISOU  665  CB  MET A  47     5122  14745  10505  -2672    192  -2678
ATOM    666  CG  MET A  47      36.872  -9.612  52.680  1.00 76.94           C  
ANISOU  666  CG  MET A  47     5141  13984  10111  -3011    348  -2621
ATOM    667  SD  MET A  47      37.638  -9.449  51.042  1.00 74.25           S  
ANISOU  667  SD  MET A  47     4944  13482   9784  -3010    657  -2559
ATOM    668  CE  MET A  47      38.414 -11.081  50.901  1.00 77.64           C  
ANISOU  668  CE  MET A  47     4923  14405  10170  -3319    817  -2582
ATOM    669  H   MET A  47      34.613  -8.297  53.353  1.00 75.59           H  
ATOM    670  HA  MET A  47      34.592  -9.823  50.941  1.00 77.76           H  
ATOM    671  HB3 MET A  47      35.814 -11.481  52.392  1.00 79.93           H  
ATOM    672  HB2 MET A  47      35.332 -10.588  53.803  1.00 79.93           H  
ATOM    673  HG3 MET A  47      37.622 -10.028  53.354  1.00 76.94           H  
ATOM    674  HG2 MET A  47      36.672  -8.611  53.057  1.00 76.94           H  
ATOM    675  HE1 MET A  47      38.923 -11.174  49.945  1.00 77.64           H  
ATOM    676  HE2 MET A  47      39.147 -11.226  51.696  1.00 77.64           H  
ATOM    677  HE3 MET A  47      37.669 -11.872  50.966  1.00 77.64           H  
ATOM    678  N   ASP A  48      33.007 -11.850  51.352  1.00 82.93           N  
ANISOU  678  N   ASP A  48     4926  15629  10954  -1687      8  -2795
ATOM    679  CA  ASP A  48      31.830 -12.731  51.255  1.00 85.42           C  
ANISOU  679  CA  ASP A  48     4878  16287  11292  -1271   -155  -2883
ATOM    680  C   ASP A  48      31.523 -13.544  52.524  1.00 88.51           C  
ANISOU  680  C   ASP A  48     4943  17024  11661  -1345   -375  -2914
ATOM    681  O   ASP A  48      30.363 -13.879  52.756  1.00 89.87           O  
ANISOU  681  O   ASP A  48     5018  17256  11871   -979   -626  -2936
ATOM    682  CB  ASP A  48      31.972 -13.699  50.053  1.00 87.25           C  
ANISOU  682  CB  ASP A  48     4807  16857  11488  -1126     53  -2964
ATOM    683  CG  ASP A  48      31.974 -13.035  48.670  1.00 85.06           C  
ANISOU  683  CG  ASP A  48     4832  16258  11228   -884    185  -2961
ATOM    684  OD1 ASP A  48      31.783 -11.801  48.603  1.00 83.75           O  
ANISOU  684  OD1 ASP A  48     5099  15603  11117   -862    120  -2885
ATOM    685  OD2 ASP A  48      32.127 -13.789  47.685  1.00 86.22           O1-
ANISOU  685  OD2 ASP A  48     4775  16663  11322   -717    353  -3035
ATOM    686  H   ASP A  48      33.734 -11.988  50.656  1.00 82.93           H  
ATOM    687  HA  ASP A  48      30.962 -12.092  51.085  1.00 85.42           H  
ATOM    688  HB3 ASP A  48      31.152 -14.420  50.052  1.00 87.25           H  
ATOM    689  HB2 ASP A  48      32.891 -14.279  50.150  1.00 87.25           H  
ATOM    690  N   ASP A  49      32.537 -13.817  53.360  1.00 89.92           N  
ANISOU  690  N   ASP A  49     4970  17413  11782  -1820   -300  -2911
ATOM    691  CA  ASP A  49      32.418 -14.470  54.670  1.00 92.59           C  
ANISOU  691  CA  ASP A  49     5031  18060  12087  -1954   -525  -2940
ATOM    692  C   ASP A  49      31.964 -13.491  55.781  1.00 90.86           C  
ANISOU  692  C   ASP A  49     5141  17523  11859  -1938   -776  -2881
ATOM    693  O   ASP A  49      31.768 -13.922  56.918  1.00 92.99           O  
ANISOU  693  O   ASP A  49     5227  18023  12081  -2030   -992  -2900
ATOM    694  CB  ASP A  49      33.793 -15.098  55.042  1.00 94.73           C  
ANISOU  694  CB  ASP A  49     5089  18600  12305  -2514   -390  -2954
ATOM    695  CG  ASP A  49      35.015 -14.167  55.124  1.00 91.80           C  
ANISOU  695  CG  ASP A  49     5162  17798  11921  -2936   -229  -2893
ATOM    696  OD1 ASP A  49      34.880 -12.965  54.806  1.00 88.62           O  
ANISOU  696  OD1 ASP A  49     5212  16923  11538  -2799   -232  -2840
ATOM    697  OD2 ASP A  49      36.084 -14.688  55.504  1.00 91.34           O1-
ANISOU  697  OD2 ASP A  49     4997  17873  11836  -3408   -107  -2894
ATOM    698  H   ASP A  49      33.455 -13.474  53.116  1.00 89.92           H  
ATOM    699  HA  ASP A  49      31.678 -15.269  54.605  1.00 92.59           H  
ATOM    700  HB3 ASP A  49      34.030 -15.871  54.311  1.00 94.73           H  
ATOM    701  HB2 ASP A  49      33.709 -15.618  55.996  1.00 94.73           H  
ATOM    702  N   GLY A  50      31.784 -12.196  55.469  1.00 87.09           N  
ANISOU  702  N   GLY A  50     5130  16549  11412  -1825   -746  -2803
ATOM    703  CA  GLY A  50      31.388 -11.146  56.400  1.00 85.62           C  
ANISOU  703  CA  GLY A  50     5272  16063  11195  -1824   -942  -2722
ATOM    704  C   GLY A  50      32.578 -10.622  57.206  1.00 85.31           C  
ANISOU  704  C   GLY A  50     5417  15929  11069  -2318   -877  -2726
ATOM    705  O   GLY A  50      32.544 -10.646  58.435  1.00 88.64           O  
ANISOU  705  O   GLY A  50     5677  16587  11414  -2516  -1035  -2768
ATOM    706  H   GLY A  50      31.973 -11.912  54.516  1.00 87.09           H  
ATOM    707  HA3 GLY A  50      30.606 -11.505  57.071  1.00 85.62           H  
ATOM    708  HA2 GLY A  50      30.959 -10.322  55.829  1.00 85.62           H  
ATOM    709  N   THR A  51      33.632 -10.177  56.506  1.00 82.31           N  
ANISOU  709  N   THR A  51     5372  15205  10697  -2507   -653  -2695
ATOM    710  CA  THR A  51      34.883  -9.644  57.057  1.00 82.03           C  
ANISOU  710  CA  THR A  51     5529  15041  10597  -2969   -548  -2722
ATOM    711  C   THR A  51      35.213  -8.332  56.329  1.00 78.12           C  
ANISOU  711  C   THR A  51     5481  14074  10127  -2935   -380  -2647
ATOM    712  O   THR A  51      34.625  -8.044  55.287  1.00 76.29           O  
ANISOU  712  O   THR A  51     5336  13685   9965  -2612   -336  -2585
ATOM    713  CB  THR A  51      35.997 -10.726  56.941  1.00 84.47           C  
ANISOU  713  CB  THR A  51     5583  15591  10921  -3312   -360  -2783
ATOM    714  OG1 THR A  51      35.609 -11.873  57.667  1.00 89.26           O  
ANISOU  714  OG1 THR A  51     5694  16703  11519  -3299   -492  -2845
ATOM    715  CG2 THR A  51      37.376 -10.328  57.494  1.00 84.90           C  
ANISOU  715  CG2 THR A  51     5862  15472  10924  -3810   -287  -2819
ATOM    716  H   THR A  51      33.567 -10.211  55.499  1.00 82.31           H  
ATOM    717  HA  THR A  51      34.746  -9.392  58.110  1.00 82.03           H  
ATOM    718  HB  THR A  51      36.127 -11.016  55.900  1.00 84.47           H  
ATOM    719  HG1 THR A  51      34.897 -12.287  57.200  1.00 89.26           H  
ATOM    720 HG21 THR A  51      38.050 -11.185  57.512  1.00 84.90           H  
ATOM    721 HG22 THR A  51      37.858  -9.574  56.874  1.00 84.90           H  
ATOM    722 HG23 THR A  51      37.305  -9.942  58.511  1.00 84.90           H  
ATOM    723  N   VAL A  52      36.165  -7.544  56.849  1.00 77.20           N  
ANISOU  723  N   VAL A  52     5651  13728   9954  -3259   -299  -2662
ATOM    724  CA  VAL A  52      36.747  -6.398  56.156  1.00 73.71           C  
ANISOU  724  CA  VAL A  52     5614  12860   9532  -3241   -130  -2596
ATOM    725  C   VAL A  52      38.247  -6.642  55.972  1.00 74.46           C  
ANISOU  725  C   VAL A  52     5809  12855   9627  -3634     73  -2640
ATOM    726  O   VAL A  52      38.955  -6.961  56.928  1.00 76.69           O  
ANISOU  726  O   VAL A  52     6063  13224   9854  -3978     22  -2724
ATOM    727  CB  VAL A  52      36.419  -5.069  56.883  1.00 72.01           C  
ANISOU  727  CB  VAL A  52     5722  12404   9236  -3177   -246  -2554
ATOM    728  CG1 VAL A  52      37.143  -3.845  56.285  1.00 68.01           C  
ANISOU  728  CG1 VAL A  52     5602  11487   8753  -3146    -62  -2484
ATOM    729  CG2 VAL A  52      34.906  -4.809  56.870  1.00 71.55           C  
ANISOU  729  CG2 VAL A  52     5560  12449   9176  -2824   -470  -2479
ATOM    730  H   VAL A  52      36.610  -7.828  57.711  1.00 77.20           H  
ATOM    731  HA  VAL A  52      36.321  -6.316  55.159  1.00 73.71           H  
ATOM    732  HB  VAL A  52      36.742  -5.157  57.921  1.00 72.01           H  
ATOM    733 HG11 VAL A  52      36.843  -2.928  56.789  1.00 68.01           H  
ATOM    734 HG12 VAL A  52      38.226  -3.918  56.394  1.00 68.01           H  
ATOM    735 HG13 VAL A  52      36.921  -3.729  55.222  1.00 68.01           H  
ATOM    736 HG21 VAL A  52      34.686  -3.822  57.267  1.00 71.55           H  
ATOM    737 HG22 VAL A  52      34.503  -4.844  55.856  1.00 71.55           H  
ATOM    738 HG23 VAL A  52      34.364  -5.542  57.468  1.00 71.55           H  
ATOM    739  N   LYS A  53      38.707  -6.426  54.734  1.00 72.63           N  
ANISOU  739  N   LYS A  53     5691  12444   9460  -3582    287  -2580
ATOM    740  CA  LYS A  53      40.105  -6.303  54.354  1.00 72.93           C  
ANISOU  740  CA  LYS A  53     5929  12275   9505  -3907    486  -2577
ATOM    741  C   LYS A  53      40.233  -5.005  53.556  1.00 69.69           C  
ANISOU  741  C   LYS A  53     5903  11458   9117  -3728    607  -2495
ATOM    742  O   LYS A  53      39.476  -4.776  52.610  1.00 68.39           O  
ANISOU  742  O   LYS A  53     5727  11259   8998  -3403    629  -2429
ATOM    743  CB  LYS A  53      40.577  -7.557  53.588  1.00 74.92           C  
ANISOU  743  CB  LYS A  53     5899  12771   9796  -4056    646  -2561
ATOM    744  CG  LYS A  53      42.070  -7.500  53.209  1.00 75.86           C  
ANISOU  744  CG  LYS A  53     6255  12642   9928  -4403    849  -2521
ATOM    745  CD  LYS A  53      42.606  -8.823  52.644  1.00 80.26           C  
ANISOU  745  CD  LYS A  53     6503  13494  10496  -4681    975  -2496
ATOM    746  CE  LYS A  53      44.078  -8.716  52.215  1.00 81.48           C  
ANISOU  746  CE  LYS A  53     6934  13355  10670  -5018   1168  -2419
ATOM    747  NZ  LYS A  53      44.574  -9.980  51.643  1.00 87.19           N1+
ANISOU  747  NZ  LYS A  53     7328  14404  11396  -5406   1260  -2380
ATOM    748  H   LYS A  53      38.033  -6.190  54.018  1.00 72.63           H  
ATOM    749  HA  LYS A  53      40.715  -6.210  55.255  1.00 72.93           H  
ATOM    750  HB3 LYS A  53      39.974  -7.700  52.689  1.00 74.92           H  
ATOM    751  HB2 LYS A  53      40.402  -8.432  54.213  1.00 74.92           H  
ATOM    752  HG3 LYS A  53      42.657  -7.230  54.090  1.00 75.86           H  
ATOM    753  HG2 LYS A  53      42.233  -6.706  52.479  1.00 75.86           H  
ATOM    754  HD3 LYS A  53      41.996  -9.129  51.793  1.00 80.26           H  
ATOM    755  HD2 LYS A  53      42.499  -9.607  53.393  1.00 80.26           H  
ATOM    756  HE3 LYS A  53      44.700  -8.450  53.070  1.00 81.48           H  
ATOM    757  HE2 LYS A  53      44.200  -7.927  51.472  1.00 81.48           H  
ATOM    758  HZ1 LYS A  53      44.066 -10.206  50.796  1.00 87.19           H  
ATOM    759  HZ2 LYS A  53      45.552  -9.890  51.409  1.00 87.19           H  
ATOM    760  HZ3 LYS A  53      44.458 -10.732  52.306  1.00 87.19           H  
ATOM    761  N   VAL A  54      41.192  -4.161  53.959  1.00 69.31           N  
ANISOU  761  N   VAL A  54     6194  11101   9040  -3930    671  -2509
ATOM    762  CA  VAL A  54      41.494  -2.883  53.331  1.00 66.49           C  
ANISOU  762  CA  VAL A  54     6190  10374   8700  -3762    783  -2431
ATOM    763  C   VAL A  54      42.712  -3.081  52.420  1.00 66.73           C  
ANISOU  763  C   VAL A  54     6359  10222   8772  -3948   1001  -2386
ATOM    764  O   VAL A  54      43.776  -3.514  52.867  1.00 68.68           O  
ANISOU  764  O   VAL A  54     6670  10416   9010  -4297   1047  -2433
ATOM    765  CB  VAL A  54      41.754  -1.828  54.436  1.00 65.78           C  
ANISOU  765  CB  VAL A  54     6401  10060   8530  -3784    708  -2473
ATOM    766  CG1 VAL A  54      42.348  -0.515  53.901  1.00 63.20           C  
ANISOU  766  CG1 VAL A  54     6394   9397   8223  -3604    830  -2387
ATOM    767  CG2 VAL A  54      40.451  -1.504  55.187  1.00 66.24           C  
ANISOU  767  CG2 VAL A  54     6331  10313   8525  -3608    492  -2486
ATOM    768  H   VAL A  54      41.776  -4.435  54.743  1.00 69.31           H  
ATOM    769  HA  VAL A  54      40.648  -2.546  52.735  1.00 66.49           H  
ATOM    770  HB  VAL A  54      42.463  -2.243  55.156  1.00 65.78           H  
ATOM    771 HG11 VAL A  54      42.443   0.213  54.707  1.00 63.20           H  
ATOM    772 HG12 VAL A  54      43.346  -0.648  53.486  1.00 63.20           H  
ATOM    773 HG13 VAL A  54      41.713  -0.090  53.124  1.00 63.20           H  
ATOM    774 HG21 VAL A  54      40.644  -0.861  56.045  1.00 66.24           H  
ATOM    775 HG22 VAL A  54      39.751  -0.978  54.538  1.00 66.24           H  
ATOM    776 HG23 VAL A  54      39.948  -2.396  55.554  1.00 66.24           H  
ATOM    777  N   PHE A  55      42.527  -2.754  51.135  1.00 64.92           N  
ANISOU  777  N   PHE A  55     6189   9890   8588  -3716   1118  -2289
ATOM    778  CA  PHE A  55      43.517  -2.855  50.069  1.00 64.88           C  
ANISOU  778  CA  PHE A  55     6324   9721   8609  -3836   1323  -2215
ATOM    779  C   PHE A  55      43.995  -1.442  49.723  1.00 62.32           C  
ANISOU  779  C   PHE A  55     6393   8995   8292  -3718   1393  -2158
ATOM    780  O   PHE A  55      43.183  -0.524  49.594  1.00 60.13           O  
ANISOU  780  O   PHE A  55     6196   8632   8018  -3428   1324  -2130
ATOM    781  CB  PHE A  55      42.824  -3.457  48.829  1.00 64.69           C  
ANISOU  781  CB  PHE A  55     6068   9906   8604  -3640   1405  -2155
ATOM    782  CG  PHE A  55      42.306  -4.868  49.042  1.00 67.51           C  
ANISOU  782  CG  PHE A  55     5999  10702   8950  -3672   1340  -2215
ATOM    783  CD1 PHE A  55      41.016  -5.072  49.577  1.00 67.28           C  
ANISOU  783  CD1 PHE A  55     5769  10868   8927  -3424   1148  -2275
ATOM    784  CD2 PHE A  55      43.121  -5.981  48.744  1.00 68.03           C  
ANISOU  784  CD2 PHE A  55     5853  10999   8998  -3945   1467  -2196
ATOM    785  CE1 PHE A  55      40.552  -6.377  49.825  1.00 68.62           C  
ANISOU  785  CE1 PHE A  55     5528  11457   9086  -3419   1079  -2335
ATOM    786  CE2 PHE A  55      42.652  -7.285  48.989  1.00 70.10           C  
ANISOU  786  CE2 PHE A  55     5684  11709   9243  -3957   1414  -2250
ATOM    787  CZ  PHE A  55      41.368  -7.482  49.532  1.00 70.04           C  
ANISOU  787  CZ  PHE A  55     5474  11894   9243  -3680   1218  -2330
ATOM    788  H   PHE A  55      41.616  -2.401  50.869  1.00 64.92           H  
ATOM    789  HA  PHE A  55      44.362  -3.481  50.364  1.00 64.88           H  
ATOM    790  HB3 PHE A  55      43.515  -3.471  47.986  1.00 64.69           H  
ATOM    791  HB2 PHE A  55      41.988  -2.825  48.523  1.00 64.69           H  
ATOM    792  HD1 PHE A  55      40.388  -4.229  49.822  1.00 67.28           H  
ATOM    793  HD2 PHE A  55      44.113  -5.837  48.340  1.00 68.03           H  
ATOM    794  HE1 PHE A  55      39.579  -6.537  50.256  1.00 68.62           H  
ATOM    795  HE2 PHE A  55      43.279  -8.136  48.773  1.00 70.10           H  
ATOM    796  HZ  PHE A  55      41.015  -8.480  49.737  1.00 70.04           H  
ATOM    797  N   LYS A  56      45.314  -1.274  49.547  1.00 62.89           N  
ANISOU  797  N   LYS A  56     6702   8824   8368  -3946   1521  -2131
ATOM    798  CA  LYS A  56      45.929  -0.010  49.150  1.00 61.06           C  
ANISOU  798  CA  LYS A  56     6835   8220   8144  -3825   1600  -2075
ATOM    799  C   LYS A  56      45.792   0.158  47.630  1.00 59.58           C  
ANISOU  799  C   LYS A  56     6657   7996   7986  -3619   1721  -1949
ATOM    800  O   LYS A  56      46.239  -0.704  46.875  1.00 60.81           O  
ANISOU  800  O   LYS A  56     6640   8324   8140  -3702   1810  -1900
ATOM    801  CB  LYS A  56      47.434  -0.042  49.486  1.00 62.62           C  
ANISOU  801  CB  LYS A  56     7318   8133   8342  -4124   1665  -2104
ATOM    802  CG  LYS A  56      47.768   0.015  50.987  1.00 64.73           C  
ANISOU  802  CG  LYS A  56     7628   8400   8568  -4334   1532  -2258
ATOM    803  CD  LYS A  56      47.922   1.433  51.566  1.00 65.33           C  
ANISOU  803  CD  LYS A  56     8030   8195   8598  -4186   1498  -2325
ATOM    804  CE  LYS A  56      46.603   2.106  51.978  1.00 63.95           C  
ANISOU  804  CE  LYS A  56     7742   8193   8362  -3904   1378  -2348
ATOM    805  NZ  LYS A  56      46.853   3.295  52.806  1.00 65.19           N1+
ANISOU  805  NZ  LYS A  56     8181   8152   8437  -3813   1346  -2433
ATOM    806  H   LYS A  56      45.924  -2.071  49.656  1.00 62.89           H  
ATOM    807  HA  LYS A  56      45.447   0.816  49.666  1.00 61.06           H  
ATOM    808  HB3 LYS A  56      47.944   0.779  48.985  1.00 62.62           H  
ATOM    809  HB2 LYS A  56      47.872  -0.951  49.071  1.00 62.62           H  
ATOM    810  HG3 LYS A  56      48.731  -0.481  51.114  1.00 64.73           H  
ATOM    811  HG2 LYS A  56      47.065  -0.575  51.576  1.00 64.73           H  
ATOM    812  HD3 LYS A  56      48.470   2.070  50.873  1.00 65.33           H  
ATOM    813  HD2 LYS A  56      48.562   1.347  52.443  1.00 65.33           H  
ATOM    814  HE3 LYS A  56      45.982   1.413  52.545  1.00 63.95           H  
ATOM    815  HE2 LYS A  56      46.039   2.414  51.101  1.00 63.95           H  
ATOM    816  HZ1 LYS A  56      47.458   3.941  52.311  1.00 65.19           H  
ATOM    817  HZ2 LYS A  56      45.978   3.741  53.042  1.00 65.19           H  
ATOM    818  HZ3 LYS A  56      47.325   2.991  53.653  1.00 65.19           H  
ATOM    819  N   GLY A  57      45.182   1.271  47.205  1.00 57.39           N  
ANISOU  819  N   GLY A  57     6568   7518   7719  -3350   1719  -1899
ATOM    820  CA  GLY A  57      45.032   1.697  45.820  1.00 56.16           C  
ANISOU  820  CA  GLY A  57     6453   7302   7584  -3133   1803  -1791
ATOM    821  C   GLY A  57      45.807   2.986  45.554  1.00 55.21           C  
ANISOU  821  C   GLY A  57     6658   6847   7472  -3021   1857  -1728
ATOM    822  O   GLY A  57      46.063   3.749  46.485  1.00 54.98           O  
ANISOU  822  O   GLY A  57     6788   6671   7430  -3012   1806  -1778
ATOM    823  H   GLY A  57      44.839   1.914  47.909  1.00 57.39           H  
ATOM    824  HA3 GLY A  57      43.977   1.882  45.621  1.00 56.16           H  
ATOM    825  HA2 GLY A  57      45.351   0.923  45.130  1.00 56.16           H  
ATOM    826  N   TRP A  58      46.153   3.235  44.282  1.00 54.55           N  
ANISOU  826  N   TRP A  58     6666   6664   7395  -2920   1960  -1622
ATOM    827  CA  TRP A  58      46.828   4.441  43.807  1.00 53.46           C  
ANISOU  827  CA  TRP A  58     6817   6226   7268  -2794   2013  -1549
ATOM    828  C   TRP A  58      46.281   4.951  42.473  1.00 51.63           C  
ANISOU  828  C   TRP A  58     6574   5996   7048  -2533   2025  -1452
ATOM    829  O   TRP A  58      45.787   4.175  41.655  1.00 52.07           O  
ANISOU  829  O   TRP A  58     6461   6239   7085  -2500   2045  -1431
ATOM    830  CB  TRP A  58      48.360   4.284  43.750  1.00 55.37           C  
ANISOU  830  CB  TRP A  58     7293   6245   7501  -3016   2136  -1506
ATOM    831  CG  TRP A  58      49.070   3.993  45.033  1.00 57.48           C  
ANISOU  831  CG  TRP A  58     7658   6416   7766  -3276   2110  -1611
ATOM    832  CD1 TRP A  58      49.552   4.918  45.891  1.00 58.16           C  
ANISOU  832  CD1 TRP A  58     7987   6264   7848  -3253   2081  -1684
ATOM    833  CD2 TRP A  58      49.386   2.699  45.619  1.00 59.70           C  
ANISOU  833  CD2 TRP A  58     7796   6846   8041  -3604   2104  -1668
ATOM    834  NE1 TRP A  58      50.119   4.284  46.976  1.00 60.69           N  
ANISOU  834  NE1 TRP A  58     8352   6547   8159  -3546   2043  -1799
ATOM    835  CE2 TRP A  58      50.042   2.915  46.869  1.00 61.31           C  
ANISOU  835  CE2 TRP A  58     8188   6861   8244  -3782   2052  -1782
ATOM    836  CE3 TRP A  58      49.169   1.359  45.230  1.00 61.17           C  
ANISOU  836  CE3 TRP A  58     7700   7327   8216  -3760   2136  -1639
ATOM    837  CZ2 TRP A  58      50.447   1.858  47.700  1.00 62.71           C  
ANISOU  837  CZ2 TRP A  58     8286   7118   8423  -4135   2011  -1864
ATOM    838  CZ3 TRP A  58      49.574   0.292  46.049  1.00 64.53           C  
ANISOU  838  CZ3 TRP A  58     8018   7858   8642  -4111   2114  -1702
ATOM    839  CH2 TRP A  58      50.207   0.535  47.286  1.00 64.12           C  
ANISOU  839  CH2 TRP A  58     8164   7595   8603  -4307   2042  -1812
ATOM    840  H   TRP A  58      45.928   2.535  43.585  1.00 54.55           H  
ATOM    841  HA  TRP A  58      46.611   5.211  44.536  1.00 53.46           H  
ATOM    842  HB3 TRP A  58      48.783   5.212  43.368  1.00 55.37           H  
ATOM    843  HB2 TRP A  58      48.629   3.509  43.032  1.00 55.37           H  
ATOM    844  HD1 TRP A  58      49.462   5.984  45.744  1.00 58.16           H  
ATOM    845  HE1 TRP A  58      50.485   4.783  47.781  1.00 60.69           H  
ATOM    846  HE3 TRP A  58      48.675   1.152  44.291  1.00 61.17           H  
ATOM    847  HZ2 TRP A  58      50.932   2.059  48.644  1.00 62.71           H  
ATOM    848  HZ3 TRP A  58      49.395  -0.717  45.715  1.00 64.53           H  
ATOM    849  HH2 TRP A  58      50.511  -0.293  47.910  1.00 64.12           H  
ATOM    850  N   ARG A  59      46.473   6.259  42.241  1.00 49.73           N  
ANISOU  850  N   ARG A  59     6501   5566   6827  -2343   2007  -1402
ATOM    851  CA  ARG A  59      46.459   6.911  40.938  1.00 48.65           C  
ANISOU  851  CA  ARG A  59     6438   5351   6698  -2143   2038  -1293
ATOM    852  C   ARG A  59      47.484   8.047  40.948  1.00 48.86           C  
ANISOU  852  C   ARG A  59     6737   5101   6727  -2091   2100  -1233
ATOM    853  O   ARG A  59      47.320   9.018  41.682  1.00 49.01           O  
ANISOU  853  O   ARG A  59     6833   5031   6756  -2038   2064  -1273
ATOM    854  CB  ARG A  59      45.038   7.333  40.514  1.00 46.67           C  
ANISOU  854  CB  ARG A  59     6047   5199   6486  -1898   1907  -1280
ATOM    855  CG  ARG A  59      44.941   7.896  39.081  1.00 45.07           C  
ANISOU  855  CG  ARG A  59     5918   4921   6286  -1709   1917  -1181
ATOM    856  CD  ARG A  59      44.955   6.785  38.021  1.00 46.32           C  
ANISOU  856  CD  ARG A  59     5968   5239   6393  -1705   1953  -1184
ATOM    857  NE  ARG A  59      45.095   7.310  36.659  1.00 44.95           N  
ANISOU  857  NE  ARG A  59     5867   5012   6199  -1520   1942  -1105
ATOM    858  CZ  ARG A  59      45.263   6.564  35.553  1.00 47.13           C  
ANISOU  858  CZ  ARG A  59     6113   5401   6392  -1493   1999  -1088
ATOM    859  NH1 ARG A  59      45.313   5.228  35.620  1.00 49.44           N  
ANISOU  859  NH1 ARG A  59     6287   5880   6617  -1646   2087  -1132
ATOM    860  NH2 ARG A  59      45.378   7.156  34.361  1.00 45.27           N1+
ANISOU  860  NH2 ARG A  59     5957   5117   6126  -1318   1969  -1024
ATOM    861  H   ARG A  59      46.830   6.815  43.007  1.00 49.73           H  
ATOM    862  HA  ARG A  59      46.807   6.173  40.216  1.00 48.65           H  
ATOM    863  HB3 ARG A  59      44.662   8.076  41.217  1.00 46.67           H  
ATOM    864  HB2 ARG A  59      44.377   6.473  40.597  1.00 46.67           H  
ATOM    865  HG3 ARG A  59      45.729   8.624  38.887  1.00 45.07           H  
ATOM    866  HG2 ARG A  59      44.005   8.447  38.987  1.00 45.07           H  
ATOM    867  HD3 ARG A  59      44.042   6.198  38.081  1.00 46.32           H  
ATOM    868  HD2 ARG A  59      45.783   6.105  38.203  1.00 46.32           H  
ATOM    869  HE  ARG A  59      45.033   8.322  36.562  1.00 44.95           H  
ATOM    870 HH12 ARG A  59      45.465   4.682  34.779  1.00 49.44           H  
ATOM    871 HH11 ARG A  59      45.233   4.759  36.509  1.00 49.44           H  
ATOM    872 HH22 ARG A  59      45.516   6.606  33.524  1.00 45.27           H  
ATOM    873 HH21 ARG A  59      45.282   8.170  34.292  1.00 45.27           H  
ATOM    874  N   SER A  60      48.521   7.907  40.115  1.00 49.30           N  
ANISOU  874  N   SER A  60     6935   5036   6761  -2088   2194  -1135
ATOM    875  CA  SER A  60      49.597   8.853  39.874  1.00 49.61           C  
ANISOU  875  CA  SER A  60     7244   4801   6806  -2013   2250  -1068
ATOM    876  C   SER A  60      49.372   9.498  38.501  1.00 48.46           C  
ANISOU  876  C   SER A  60     7123   4632   6656  -1779   2240   -952
ATOM    877  O   SER A  60      49.571   8.846  37.482  1.00 49.36           O  
ANISOU  877  O   SER A  60     7226   4803   6726  -1794   2284   -877
ATOM    878  CB  SER A  60      50.923   8.056  39.886  1.00 52.10           C  
ANISOU  878  CB  SER A  60     7759   4936   7099  -2241   2357  -1032
ATOM    879  OG  SER A  60      52.039   8.866  39.587  1.00 52.04           O  
ANISOU  879  OG  SER A  60     8008   4673   7094  -2111   2406   -924
ATOM    880  H   SER A  60      48.545   7.073  39.540  1.00 49.30           H  
ATOM    881  HA  SER A  60      49.630   9.619  40.644  1.00 49.61           H  
ATOM    882  HB3 SER A  60      50.900   7.229  39.176  1.00 52.10           H  
ATOM    883  HB2 SER A  60      51.085   7.614  40.868  1.00 52.10           H  
ATOM    884  HG  SER A  60      52.032   9.062  38.660  1.00 52.04           H  
ATOM    885  N   ALA A  61      49.002  10.785  38.478  1.00 47.16           N  
ANISOU  885  N   ALA A  61     6982   4409   6526  -1569   2182   -934
ATOM    886  CA  ALA A  61      48.994  11.632  37.291  1.00 46.70           C  
ANISOU  886  CA  ALA A  61     6962   4311   6472  -1348   2158   -819
ATOM    887  C   ALA A  61      50.394  12.256  37.181  1.00 48.28           C  
ANISOU  887  C   ALA A  61     7432   4256   6655  -1307   2246   -743
ATOM    888  O   ALA A  61      50.744  13.127  37.980  1.00 49.35           O  
ANISOU  888  O   ALA A  61     7686   4252   6812  -1241   2262   -778
ATOM    889  CB  ALA A  61      47.955  12.748  37.507  1.00 44.86           C  
ANISOU  889  CB  ALA A  61     6601   4154   6290  -1160   2048   -815
ATOM    890  H   ALA A  61      48.891  11.256  39.367  1.00 47.16           H  
ATOM    891  HA  ALA A  61      48.745  11.072  36.389  1.00 46.70           H  
ATOM    892  HB1 ALA A  61      47.967  13.469  36.689  1.00 44.86           H  
ATOM    893  HB2 ALA A  61      46.949  12.330  37.555  1.00 44.86           H  
ATOM    894  HB3 ALA A  61      48.126  13.298  38.434  1.00 44.86           H  
ATOM    895  N   HIS A  62      51.205  11.783  36.217  1.00 49.05           N  
ANISOU  895  N   HIS A  62     7639   4292   6706  -1330   2302   -639
ATOM    896  CA  HIS A  62      52.571  12.265  36.017  1.00 51.01           C  
ANISOU  896  CA  HIS A  62     8170   4265   6948  -1288   2370   -553
ATOM    897  C   HIS A  62      52.600  13.669  35.424  1.00 50.47           C  
ANISOU  897  C   HIS A  62     8142   4137   6899   -989   2321   -477
ATOM    898  O   HIS A  62      53.222  14.565  35.992  1.00 50.91           O  
ANISOU  898  O   HIS A  62     8355   4007   6982   -868   2341   -483
ATOM    899  CB  HIS A  62      53.422  11.335  35.133  1.00 52.75           C  
ANISOU  899  CB  HIS A  62     8521   4422   7101  -1427   2449   -430
ATOM    900  CG  HIS A  62      54.838  11.849  35.002  1.00 54.11           C  
ANISOU  900  CG  HIS A  62     8992   4298   7271  -1334   2488   -307
ATOM    901  ND1 HIS A  62      55.301  12.515  33.863  1.00 56.85           N  
ANISOU  901  ND1 HIS A  62     9580   4355   7667  -1404   2523   -348
ATOM    902  CD2 HIS A  62      55.828  11.879  35.965  1.00 54.22           C  
ANISOU  902  CD2 HIS A  62     9111   4249   7240  -1149   2478   -151
ATOM    903  CE1 HIS A  62      56.509  12.947  34.187  1.00 58.78           C  
ANISOU  903  CE1 HIS A  62    10072   4354   7906  -1258   2535   -218
ATOM    904  NE2 HIS A  62      56.874  12.598  35.420  1.00 57.22           N  
ANISOU  904  NE2 HIS A  62     9791   4300   7649  -1105   2510    -87
ATOM    905  H   HIS A  62      50.855  11.083  35.577  1.00 49.05           H  
ATOM    906  HA  HIS A  62      53.047  12.306  36.977  1.00 51.01           H  
ATOM    907  HB3 HIS A  62      52.984  11.194  34.145  1.00 52.75           H  
ATOM    908  HB2 HIS A  62      53.473  10.355  35.594  1.00 52.75           H  
ATOM    909  HD2 HIS A  62      55.846  11.502  36.976  1.00 54.22           H  
ATOM    910  HE1 HIS A  62      57.143  13.509  33.518  1.00 58.78           H  
ATOM    911  HE2 HIS A  62      57.756  12.821  35.866  1.00 57.22           H  
ATOM    912  N   SER A  63      51.956  13.821  34.265  1.00 49.78           N  
ANISOU  912  N   SER A  63     7905   4218   6791   -863   2249   -412
ATOM    913  CA  SER A  63      51.953  15.034  33.480  1.00 50.14           C  
ANISOU  913  CA  SER A  63     7951   4248   6853   -600   2183   -323
ATOM    914  C   SER A  63      50.545  15.278  32.961  1.00 48.65           C  
ANISOU  914  C   SER A  63     7517   4286   6683   -509   2054   -329
ATOM    915  O   SER A  63      49.827  14.339  32.617  1.00 48.84           O  
ANISOU  915  O   SER A  63     7432   4455   6670   -597   2020   -361
ATOM    916  CB  SER A  63      53.044  14.984  32.391  1.00 51.87           C  
ANISOU  916  CB  SER A  63     8368   4334   7007   -522   2216   -175
ATOM    917  OG  SER A  63      53.126  16.208  31.686  1.00 53.24           O  
ANISOU  917  OG  SER A  63     8511   4524   7194   -258   2133    -90
ATOM    918  H   SER A  63      51.454  13.027  33.888  1.00 49.78           H  
ATOM    919  HA  SER A  63      52.199  15.862  34.137  1.00 50.14           H  
ATOM    920  HB3 SER A  63      52.840  14.183  31.681  1.00 51.87           H  
ATOM    921  HB2 SER A  63      54.019  14.780  32.833  1.00 51.87           H  
ATOM    922  HG  SER A  63      53.459  16.869  32.276  1.00 53.24           H  
ATOM    923  N   SER A  64      50.194  16.561  32.863  1.00 47.60           N  
ANISOU  923  N   SER A  64     7293   4185   6606   -330   1977   -300
ATOM    924  CA  SER A  64      49.018  17.050  32.166  1.00 46.45           C  
ANISOU  924  CA  SER A  64     6956   4205   6490   -236   1829   -269
ATOM    925  C   SER A  64      49.345  18.262  31.284  1.00 47.19           C  
ANISOU  925  C   SER A  64     7071   4273   6585    -15   1769   -144
ATOM    926  O   SER A  64      48.425  18.954  30.855  1.00 46.47           O  
ANISOU  926  O   SER A  64     6817   4303   6538     72   1629   -108
ATOM    927  CB  SER A  64      47.817  17.195  33.122  1.00 45.48           C  
ANISOU  927  CB  SER A  64     6627   4207   6447   -284   1750   -338
ATOM    928  OG  SER A  64      47.950  18.321  33.970  1.00 45.36           O  
ANISOU  928  OG  SER A  64     6617   4156   6461   -235   1807   -339
ATOM    929  H   SER A  64      50.836  17.255  33.219  1.00 47.60           H  
ATOM    930  HA  SER A  64      48.753  16.272  31.453  1.00 46.45           H  
ATOM    931  HB3 SER A  64      47.691  16.296  33.726  1.00 45.48           H  
ATOM    932  HB2 SER A  64      46.897  17.314  32.546  1.00 45.48           H  
ATOM    933  HG  SER A  64      47.159  18.403  34.479  1.00 45.36           H  
ATOM    934  N   ALA A  65      50.641  18.502  31.001  1.00 49.12           N  
ANISOU  934  N   ALA A  65     7523   4354   6788     73   1861    -75
ATOM    935  CA  ALA A  65      51.178  19.631  30.240  1.00 50.31           C  
ANISOU  935  CA  ALA A  65     7702   4479   6936    308   1808     48
ATOM    936  C   ALA A  65      50.598  19.746  28.822  1.00 50.05           C  
ANISOU  936  C   ALA A  65     7547   4593   6878    371   1655    107
ATOM    937  O   ALA A  65      50.148  20.824  28.437  1.00 50.50           O  
ANISOU  937  O   ALA A  65     7441   4758   6990    496   1535    155
ATOM    938  CB  ALA A  65      52.711  19.513  30.180  1.00 52.35           C  
ANISOU  938  CB  ALA A  65     8243   4515   7132    372   1908    126
ATOM    939  H   ALA A  65      51.320  17.847  31.364  1.00 49.12           H  
ATOM    940  HA  ALA A  65      50.928  20.544  30.781  1.00 50.31           H  
ATOM    941  HB1 ALA A  65      53.145  20.355  29.639  1.00 52.35           H  
ATOM    942  HB2 ALA A  65      53.149  19.507  31.178  1.00 52.35           H  
ATOM    943  HB3 ALA A  65      53.026  18.599  29.678  1.00 52.35           H  
ATOM    944  N   VAL A  66      50.585  18.632  28.076  1.00 50.14           N  
ANISOU  944  N   VAL A  66     7632   4622   6797    276   1657     98
ATOM    945  CA  VAL A  66      50.152  18.542  26.679  1.00 50.12           C  
ANISOU  945  CA  VAL A  66     7572   4743   6727    353   1517    139
ATOM    946  C   VAL A  66      48.630  18.272  26.562  1.00 48.60           C  
ANISOU  946  C   VAL A  66     7165   4711   6588    282   1373     27
ATOM    947  O   VAL A  66      48.032  18.635  25.549  1.00 48.86           O  
ANISOU  947  O   VAL A  66     7102   4842   6620    373   1199     43
ATOM    948  CB  VAL A  66      50.980  17.400  26.016  1.00 51.27           C  
ANISOU  948  CB  VAL A  66     7905   4863   6713    299   1599    185
ATOM    949  CG1 VAL A  66      50.542  17.028  24.587  1.00 52.86           C  
ANISOU  949  CG1 VAL A  66     8043   5229   6810    369   1456    183
ATOM    950  CG2 VAL A  66      52.486  17.727  26.006  1.00 53.43           C  
ANISOU  950  CG2 VAL A  66     8411   4950   6939    395   1691    333
ATOM    951  H   VAL A  66      50.957  17.788  28.490  1.00 50.14           H  
ATOM    952  HA  VAL A  66      50.367  19.481  26.165  1.00 50.12           H  
ATOM    953  HB  VAL A  66      50.861  16.507  26.627  1.00 51.27           H  
ATOM    954 HG11 VAL A  66      51.213  16.290  24.148  1.00 52.86           H  
ATOM    955 HG12 VAL A  66      49.551  16.583  24.580  1.00 52.86           H  
ATOM    956 HG13 VAL A  66      50.531  17.899  23.932  1.00 52.86           H  
ATOM    957 HG21 VAL A  66      53.062  16.917  25.560  1.00 53.43           H  
ATOM    958 HG22 VAL A  66      52.689  18.629  25.429  1.00 53.43           H  
ATOM    959 HG23 VAL A  66      52.878  17.878  27.012  1.00 53.43           H  
ATOM    960  N   GLY A  67      47.998  17.676  27.584  1.00 47.23           N  
ANISOU  960  N   GLY A  67     6929   4553   6462    122   1428    -87
ATOM    961  CA  GLY A  67      46.569  17.359  27.618  1.00 45.49           C  
ANISOU  961  CA  GLY A  67     6535   4452   6296     53   1292   -201
ATOM    962  C   GLY A  67      46.220  16.593  28.902  1.00 44.29           C  
ANISOU  962  C   GLY A  67     6332   4298   6200   -104   1376   -297
ATOM    963  O   GLY A  67      47.035  16.581  29.818  1.00 44.78           O  
ANISOU  963  O   GLY A  67     6473   4270   6270   -160   1519   -282
ATOM    964  H   GLY A  67      48.535  17.428  28.403  1.00 47.23           H  
ATOM    965  HA3 GLY A  67      46.315  16.763  26.743  1.00 45.49           H  
ATOM    966  HA2 GLY A  67      45.983  18.277  27.577  1.00 45.49           H  
ATOM    967  N   PRO A  68      45.046  15.934  29.015  1.00 43.35           N  
ANISOU  967  N   PRO A  68     6084   4269   6118   -166   1271   -407
ATOM    968  CA  PRO A  68      44.689  15.148  30.208  1.00 42.33           C  
ANISOU  968  CA  PRO A  68     5899   4158   6024   -310   1340   -499
ATOM    969  C   PRO A  68      45.565  13.893  30.380  1.00 42.88           C  
ANISOU  969  C   PRO A  68     6075   4232   5986   -423   1521   -542
ATOM    970  O   PRO A  68      46.068  13.341  29.405  1.00 44.35           O  
ANISOU  970  O   PRO A  68     6358   4433   6058   -393   1575   -508
ATOM    971  CB  PRO A  68      43.201  14.818  30.030  1.00 42.11           C  
ANISOU  971  CB  PRO A  68     5729   4221   6051   -300   1157   -600
ATOM    972  CG  PRO A  68      42.946  14.895  28.534  1.00 41.44           C  
ANISOU  972  CG  PRO A  68     5673   4170   5903   -179   1045   -604
ATOM    973  CD  PRO A  68      43.981  15.893  28.013  1.00 43.21           C  
ANISOU  973  CD  PRO A  68     5973   4328   6119    -95   1062   -461
ATOM    974  HA  PRO A  68      44.807  15.770  31.099  1.00 42.33           H  
ATOM    975  HB3 PRO A  68      42.617  15.587  30.530  1.00 42.11           H  
ATOM    976  HB2 PRO A  68      42.907  13.858  30.456  1.00 42.11           H  
ATOM    977  HG3 PRO A  68      41.923  15.180  28.287  1.00 41.44           H  
ATOM    978  HG2 PRO A  68      43.125  13.916  28.093  1.00 41.44           H  
ATOM    979  HD2 PRO A  68      44.337  15.599  27.031  1.00 43.21           H  
ATOM    980  HD3 PRO A  68      43.541  16.887  27.927  1.00 43.21           H  
ATOM    981  N   SER A  69      45.764  13.457  31.633  1.00 42.58           N  
ANISOU  981  N   SER A  69     6011   4194   5973   -566   1608   -605
ATOM    982  CA  SER A  69      46.580  12.296  32.000  1.00 43.81           C  
ANISOU  982  CA  SER A  69     6254   4352   6041   -714   1773   -629
ATOM    983  C   SER A  69      45.946  10.987  31.492  1.00 44.69           C  
ANISOU  983  C   SER A  69     6250   4645   6088   -756   1757   -726
ATOM    984  O   SER A  69      44.727  10.914  31.328  1.00 43.96           O  
ANISOU  984  O   SER A  69     6003   4647   6051   -696   1615   -817
ATOM    985  CB  SER A  69      46.720  12.253  33.531  1.00 43.54           C  
ANISOU  985  CB  SER A  69     6243   4249   6052   -864   1861   -669
ATOM    986  OG  SER A  69      47.603  13.253  33.987  1.00 44.61           O  
ANISOU  986  OG  SER A  69     6554   4203   6192   -830   1940   -588
ATOM    987  H   SER A  69      45.300  13.943  32.387  1.00 42.58           H  
ATOM    988  HA  SER A  69      47.569  12.402  31.554  1.00 43.81           H  
ATOM    989  HB3 SER A  69      47.115  11.293  33.864  1.00 43.54           H  
ATOM    990  HB2 SER A  69      45.756  12.399  34.015  1.00 43.54           H  
ATOM    991  HG  SER A  69      48.439  13.147  33.552  1.00 44.61           H  
ATOM    992  N   LYS A  70      46.765   9.963  31.207  1.00 46.10           N  
ANISOU  992  N   LYS A  70     6500   4871   6144   -855   1900   -700
ATOM    993  CA  LYS A  70      46.295   8.693  30.661  1.00 47.20           C  
ANISOU  993  CA  LYS A  70     6513   5232   6189   -884   1920   -788
ATOM    994  C   LYS A  70      47.294   7.549  30.867  1.00 49.38           C  
ANISOU  994  C   LYS A  70     6832   5564   6366  -1092   2111   -745
ATOM    995  O   LYS A  70      48.496   7.726  30.682  1.00 50.95           O  
ANISOU  995  O   LYS A  70     7217   5635   6506  -1147   2213   -608
ATOM    996  CB  LYS A  70      45.881   8.876  29.186  1.00 47.90           C  
ANISOU  996  CB  LYS A  70     6606   5418   6177   -695   1836   -789
ATOM    997  CG  LYS A  70      45.369   7.589  28.529  1.00 47.23           C  
ANISOU  997  CG  LYS A  70     6382   5594   5969   -670   1853   -907
ATOM    998  CD  LYS A  70      44.332   7.886  27.449  1.00 47.73           C  
ANISOU  998  CD  LYS A  70     6397   5721   6016   -440   1662  -1006
ATOM    999  CE  LYS A  70      44.006   6.694  26.555  1.00 52.80           C  
ANISOU  999  CE  LYS A  70     6922   6643   6497   -370   1696  -1139
ATOM   1000  NZ  LYS A  70      43.643   5.579  27.393  1.00 52.93           N1+
ANISOU 1000  NZ  LYS A  70     6756   6790   6565   -477   1751  -1244
ATOM   1001  H   LYS A  70      47.763  10.083  31.314  1.00 46.10           H  
ATOM   1002  HA  LYS A  70      45.404   8.422  31.228  1.00 47.20           H  
ATOM   1003  HB3 LYS A  70      46.710   9.277  28.602  1.00 47.90           H  
ATOM   1004  HB2 LYS A  70      45.093   9.627  29.130  1.00 47.90           H  
ATOM   1005  HG3 LYS A  70      44.909   6.944  29.274  1.00 47.23           H  
ATOM   1006  HG2 LYS A  70      46.208   7.030  28.111  1.00 47.23           H  
ATOM   1007  HD3 LYS A  70      44.733   8.678  26.838  1.00 47.73           H  
ATOM   1008  HD2 LYS A  70      43.420   8.276  27.898  1.00 47.73           H  
ATOM   1009  HE3 LYS A  70      44.856   6.424  25.932  1.00 52.80           H  
ATOM   1010  HE2 LYS A  70      43.178   6.940  25.888  1.00 52.80           H  
ATOM   1011  HZ1 LYS A  70      43.424   4.780  26.815  1.00  0.00           H  
ATOM   1012  HZ2 LYS A  70      44.414   5.350  28.003  1.00  0.00           H  
ATOM   1013  HZ3 LYS A  70      42.835   5.823  27.948  1.00  0.00           H  
ATOM   1014  N   GLY A  71      46.757   6.361  31.182  1.00 49.98           N  
ANISOU 1014  N   GLY A  71     6731   5834   6426  -1207   2147   -851
ATOM   1015  CA  GLY A  71      47.471   5.092  31.271  1.00 51.85           C  
ANISOU 1015  CA  GLY A  71     6935   6209   6555  -1426   2321   -815
ATOM   1016  C   GLY A  71      46.767   4.102  32.198  1.00 52.36           C  
ANISOU 1016  C   GLY A  71     6750   6502   6644  -1519   2314   -957
ATOM   1017  O   GLY A  71      45.729   4.407  32.782  1.00 51.55           O  
ANISOU 1017  O   GLY A  71     6537   6397   6652  -1424   2173  -1071
ATOM   1018  H   GLY A  71      45.750   6.307  31.257  1.00 49.98           H  
ATOM   1019  HA3 GLY A  71      48.501   5.221  31.586  1.00 51.85           H  
ATOM   1020  HA2 GLY A  71      47.529   4.660  30.274  1.00 51.85           H  
ATOM   1021  N   GLY A  72      47.335   2.894  32.305  1.00 54.20           N  
ANISOU 1021  N   GLY A  72     6884   6936   6776  -1713   2461   -936
ATOM   1022  CA  GLY A  72      46.730   1.689  32.866  1.00 54.90           C  
ANISOU 1022  CA  GLY A  72     6690   7305   6863  -1775   2458  -1070
ATOM   1023  C   GLY A  72      46.450   1.652  34.382  1.00 55.15           C  
ANISOU 1023  C   GLY A  72     6641   7306   7009  -1996   2445  -1123
ATOM   1024  O   GLY A  72      46.743   2.601  35.104  1.00 54.82           O  
ANISOU 1024  O   GLY A  72     6782   6999   7048  -2140   2452  -1064
ATOM   1025  H   GLY A  72      48.209   2.754  31.820  1.00 54.20           H  
ATOM   1026  HA3 GLY A  72      47.416   0.885  32.619  1.00 54.90           H  
ATOM   1027  HA2 GLY A  72      45.825   1.489  32.305  1.00 54.90           H  
ATOM   1028  N   VAL A  73      45.886   0.529  34.861  1.00 55.98           N  
ANISOU 1028  N   VAL A  73     6466   7697   7108  -2002   2417  -1248
ATOM   1029  CA  VAL A  73      45.640   0.204  36.272  1.00 56.49           C  
ANISOU 1029  CA  VAL A  73     6408   7795   7258  -2203   2386  -1312
ATOM   1030  C   VAL A  73      46.085  -1.249  36.512  1.00 59.60           C  
ANISOU 1030  C   VAL A  73     6580   8501   7564  -2453   2526  -1302
ATOM   1031  O   VAL A  73      45.593  -2.149  35.838  1.00 60.83           O  
ANISOU 1031  O   VAL A  73     6516   8986   7609  -2351   2582  -1343
ATOM   1032  CB  VAL A  73      44.167   0.484  36.696  1.00 55.11           C  
ANISOU 1032  CB  VAL A  73     6081   7676   7182  -1998   2190  -1459
ATOM   1033  CG1 VAL A  73      43.923   0.203  38.192  1.00 56.23           C  
ANISOU 1033  CG1 VAL A  73     6145   7818   7403  -2204   2140  -1510
ATOM   1034  CG2 VAL A  73      43.711   1.918  36.385  1.00 53.27           C  
ANISOU 1034  CG2 VAL A  73     6038   7174   7030  -1765   2054  -1442
ATOM   1035  H   VAL A  73      45.643  -0.191  34.195  1.00 55.98           H  
ATOM   1036  HA  VAL A  73      46.277   0.841  36.880  1.00 56.49           H  
ATOM   1037  HB  VAL A  73      43.521  -0.186  36.127  1.00 55.11           H  
ATOM   1038 HG11 VAL A  73      42.882   0.384  38.459  1.00 56.23           H  
ATOM   1039 HG12 VAL A  73      44.148  -0.829  38.458  1.00 56.23           H  
ATOM   1040 HG13 VAL A  73      44.531   0.853  38.819  1.00 56.23           H  
ATOM   1041 HG21 VAL A  73      42.687   2.086  36.719  1.00 53.27           H  
ATOM   1042 HG22 VAL A  73      44.348   2.651  36.880  1.00 53.27           H  
ATOM   1043 HG23 VAL A  73      43.734   2.118  35.314  1.00 53.27           H  
ATOM   1044  N   ARG A  74      47.013  -1.482  37.456  1.00 61.04           N  
ANISOU 1044  N   ARG A  74     6816   8582   7792  -2783   2577  -1253
ATOM   1045  CA  ARG A  74      47.559  -2.806  37.775  1.00 64.14           C  
ANISOU 1045  CA  ARG A  74     7022   9226   8121  -3101   2707  -1208
ATOM   1046  C   ARG A  74      46.945  -3.387  39.049  1.00 64.99           C  
ANISOU 1046  C   ARG A  74     6873   9523   8298  -3236   2616  -1337
ATOM   1047  O   ARG A  74      47.046  -2.775  40.107  1.00 64.16           O  
ANISOU 1047  O   ARG A  74     6878   9200   8298  -3299   2498  -1398
ATOM   1048  CB  ARG A  74      49.062  -2.664  38.075  1.00 65.61           C  
ANISOU 1048  CB  ARG A  74     7485   9124   8321  -3422   2808  -1050
ATOM   1049  CG  ARG A  74      49.897  -2.528  36.807  1.00 67.17           C  
ANISOU 1049  CG  ARG A  74     7841   9278   8402  -3421   2953   -870
ATOM   1050  CD  ARG A  74      51.389  -2.683  37.105  1.00 70.68           C  
ANISOU 1050  CD  ARG A  74     8398   9621   8837  -3850   3076   -705
ATOM   1051  NE  ARG A  74      52.143  -2.854  35.863  1.00 71.03           N  
ANISOU 1051  NE  ARG A  74     8620   9606   8761  -3882   3216   -491
ATOM   1052  CZ  ARG A  74      53.452  -3.134  35.785  1.00 75.52           C  
ANISOU 1052  CZ  ARG A  74     9415   9942   9338  -4208   3301   -302
ATOM   1053  NH1 ARG A  74      54.205  -3.291  36.883  1.00 75.86           N  
ANISOU 1053  NH1 ARG A  74     9536   9777   9508  -4531   3252   -325
ATOM   1054  NH2 ARG A  74      54.016  -3.256  34.579  1.00 78.29           N1+
ANISOU 1054  NH2 ARG A  74     9923  10260   9562  -4212   3420    -89
ATOM   1055  H   ARG A  74      47.383  -0.695  37.969  1.00 61.04           H  
ATOM   1056  HA  ARG A  74      47.413  -3.504  36.950  1.00 64.14           H  
ATOM   1057  HB3 ARG A  74      49.415  -3.552  38.602  1.00 65.61           H  
ATOM   1058  HB2 ARG A  74      49.255  -1.822  38.744  1.00 65.61           H  
ATOM   1059  HG3 ARG A  74      49.702  -1.569  36.324  1.00 67.17           H  
ATOM   1060  HG2 ARG A  74      49.592  -3.303  36.106  1.00 67.17           H  
ATOM   1061  HD3 ARG A  74      51.562  -3.564  37.725  1.00 70.68           H  
ATOM   1062  HD2 ARG A  74      51.766  -1.821  37.655  1.00 70.68           H  
ATOM   1063  HE  ARG A  74      51.599  -2.774  35.007  1.00 71.03           H  
ATOM   1064 HH12 ARG A  74      55.197  -3.466  36.814  1.00 75.86           H  
ATOM   1065 HH11 ARG A  74      53.809  -3.149  37.803  1.00 75.86           H  
ATOM   1066 HH22 ARG A  74      55.000  -3.466  34.490  1.00 78.29           H  
ATOM   1067 HH21 ARG A  74      53.453  -3.145  33.746  1.00 78.29           H  
ATOM   1068  N   PHE A  75      46.403  -4.610  38.981  1.00 66.91           N  
ANISOU 1068  N   PHE A  75     6763  10194   8465  -3278   2673  -1379
ATOM   1069  CA  PHE A  75      45.972  -5.384  40.149  1.00 67.99           C  
ANISOU 1069  CA  PHE A  75     6621  10557   8653  -3442   2595  -1482
ATOM   1070  C   PHE A  75      46.998  -6.509  40.376  1.00 71.38           C  
ANISOU 1070  C   PHE A  75     6923  11168   9030  -3879   2750  -1369
ATOM   1071  O   PHE A  75      46.718  -7.678  40.126  1.00 74.15           O  
ANISOU 1071  O   PHE A  75     6930  11957   9286  -3917   2844  -1367
ATOM   1072  CB  PHE A  75      44.557  -5.956  39.895  1.00 67.93           C  
ANISOU 1072  CB  PHE A  75     6268  10926   8618  -3124   2510  -1632
ATOM   1073  CG  PHE A  75      43.372  -4.996  39.915  1.00 64.62           C  
ANISOU 1073  CG  PHE A  75     5958  10313   8283  -2742   2313  -1741
ATOM   1074  CD1 PHE A  75      43.515  -3.596  40.062  1.00 60.09           C  
ANISOU 1074  CD1 PHE A  75     5739   9309   7784  -2685   2247  -1693
ATOM   1075  CD2 PHE A  75      42.079  -5.540  39.767  1.00 64.26           C  
ANISOU 1075  CD2 PHE A  75     5649  10527   8241  -2435   2191  -1882
ATOM   1076  CE1 PHE A  75      42.386  -2.757  40.021  1.00 59.07           C  
ANISOU 1076  CE1 PHE A  75     5681   9033   7729  -2374   2071  -1764
ATOM   1077  CE2 PHE A  75      40.949  -4.700  39.751  1.00 60.26           C  
ANISOU 1077  CE2 PHE A  75     5249   9826   7821  -2113   1996  -1959
ATOM   1078  CZ  PHE A  75      41.101  -3.308  39.870  1.00 58.24           C  
ANISOU 1078  CZ  PHE A  75     5329   9162   7637  -2100   1939  -1890
ATOM   1079  H   PHE A  75      46.379  -5.075  38.082  1.00 66.91           H  
ATOM   1080  HA  PHE A  75      45.945  -4.786  41.060  1.00 67.99           H  
ATOM   1081  HB3 PHE A  75      44.337  -6.708  40.653  1.00 67.93           H  
ATOM   1082  HB2 PHE A  75      44.533  -6.479  38.939  1.00 67.93           H  
ATOM   1083  HD1 PHE A  75      44.478  -3.139  40.205  1.00 60.09           H  
ATOM   1084  HD2 PHE A  75      41.952  -6.606  39.654  1.00 64.26           H  
ATOM   1085  HE1 PHE A  75      42.502  -1.689  40.123  1.00 59.07           H  
ATOM   1086  HE2 PHE A  75      39.963  -5.128  39.637  1.00 60.26           H  
ATOM   1087  HZ  PHE A  75      40.233  -2.664  39.851  1.00 58.24           H  
ATOM   1088  N   HIS A  76      48.205  -6.150  40.837  1.00 71.65           N  
ANISOU 1088  N   HIS A  76     7238  10864   9123  -4203   2775  -1270
ATOM   1089  CA  HIS A  76      49.321  -7.064  41.096  1.00 75.31           C  
ANISOU 1089  CA  HIS A  76     7631  11420   9562  -4675   2895  -1141
ATOM   1090  C   HIS A  76      49.737  -6.938  42.574  1.00 76.19           C  
ANISOU 1090  C   HIS A  76     7794  11361   9793  -4978   2760  -1224
ATOM   1091  O   HIS A  76      49.527  -5.882  43.167  1.00 74.09           O  
ANISOU 1091  O   HIS A  76     7724  10818   9607  -4820   2611  -1341
ATOM   1092  CB  HIS A  76      50.467  -6.710  40.119  1.00 75.95           C  
ANISOU 1092  CB  HIS A  76     8047  11213   9598  -4817   3040   -927
ATOM   1093  CG  HIS A  76      51.412  -7.847  39.809  1.00 80.44           C  
ANISOU 1093  CG  HIS A  76     8447  12044  10072  -5191   3221   -739
ATOM   1094  ND1 HIS A  76      52.625  -8.041  40.476  1.00 83.25           N  
ANISOU 1094  ND1 HIS A  76     8982  12164  10487  -5665   3256   -593
ATOM   1095  CD2 HIS A  76      51.249  -8.869  38.898  1.00 82.35           C  
ANISOU 1095  CD2 HIS A  76     8353  12777  10158  -5168   3376   -667
ATOM   1096  CE1 HIS A  76      53.156  -9.126  39.931  1.00 86.75           C  
ANISOU 1096  CE1 HIS A  76     9200  12940  10820  -5946   3426   -413
ATOM   1097  NE2 HIS A  76      52.379  -9.660  38.988  1.00 86.08           N  
ANISOU 1097  NE2 HIS A  76     8792  13323  10593  -5642   3513   -455
ATOM   1098  H   HIS A  76      48.355  -5.176  41.061  1.00 71.65           H  
ATOM   1099  HA  HIS A  76      49.003  -8.089  40.907  1.00 75.31           H  
ATOM   1100  HB3 HIS A  76      51.035  -5.848  40.472  1.00 75.95           H  
ATOM   1101  HB2 HIS A  76      50.041  -6.409  39.161  1.00 75.95           H  
ATOM   1102  HD2 HIS A  76      50.443  -9.094  38.216  1.00 82.35           H  
ATOM   1103  HE1 HIS A  76      54.109  -9.538  40.229  1.00 86.75           H  
ATOM   1104  HE2 HIS A  76      52.579 -10.492  38.450  1.00 86.08           H  
ATOM   1105  N   PRO A  77      50.318  -7.972  43.219  1.00 79.96           N  
ANISOU 1105  N   PRO A  77     8078  12030  10274  -5417   2802  -1170
ATOM   1106  CA  PRO A  77      50.847  -7.827  44.582  1.00 80.90           C  
ANISOU 1106  CA  PRO A  77     8313  11921  10504  -5700   2648  -1267
ATOM   1107  C   PRO A  77      52.173  -7.039  44.672  1.00 81.59           C  
ANISOU 1107  C   PRO A  77     8895  11448  10657  -5920   2655  -1179
ATOM   1108  O   PRO A  77      52.549  -6.671  45.785  1.00 82.54           O  
ANISOU 1108  O   PRO A  77     9189  11313  10862  -6119   2520  -1282
ATOM   1109  CB  PRO A  77      50.999  -9.266  45.092  1.00 85.03           C  
ANISOU 1109  CB  PRO A  77     8431  12862  11013  -6106   2672  -1243
ATOM   1110  CG  PRO A  77      51.211 -10.096  43.838  1.00 86.23           C  
ANISOU 1110  CG  PRO A  77     8413  13294  11054  -6173   2892  -1049
ATOM   1111  CD  PRO A  77      50.412  -9.359  42.761  1.00 83.37           C  
ANISOU 1111  CD  PRO A  77     8118  12949  10611  -5648   2952  -1062
ATOM   1112  HA  PRO A  77      50.118  -7.315  45.214  1.00 80.90           H  
ATOM   1113  HB3 PRO A  77      50.071  -9.576  45.573  1.00 85.03           H  
ATOM   1114  HB2 PRO A  77      51.801  -9.397  45.821  1.00 85.03           H  
ATOM   1115  HG3 PRO A  77      50.901 -11.134  43.957  1.00 86.23           H  
ATOM   1116  HG2 PRO A  77      52.270 -10.091  43.575  1.00 86.23           H  
ATOM   1117  HD2 PRO A  77      50.868  -9.484  41.786  1.00 83.37           H  
ATOM   1118  HD3 PRO A  77      49.404  -9.771  42.705  1.00 83.37           H  
ATOM   1119  N   ASN A  78      52.865  -6.750  43.547  1.00 81.65           N  
ANISOU 1119  N   ASN A  78     9133  11271  10619  -5867   2802   -997
ATOM   1120  CA  ASN A  78      54.138  -6.016  43.558  1.00 82.77           C  
ANISOU 1120  CA  ASN A  78     9743  10885  10822  -6073   2818   -882
ATOM   1121  C   ASN A  78      53.938  -4.488  43.596  1.00 78.85           C  
ANISOU 1121  C   ASN A  78     9612   9984  10363  -5691   2745   -961
ATOM   1122  O   ASN A  78      54.858  -3.789  44.020  1.00 79.50           O  
ANISOU 1122  O   ASN A  78    10091   9602  10513  -5785   2708   -941
ATOM   1123  CB  ASN A  78      55.031  -6.408  42.337  1.00 85.40           C  
ANISOU 1123  CB  ASN A  78    10141  11227  11079  -6267   3011   -603
ATOM   1124  CG  ASN A  78      54.865  -5.628  41.012  1.00 83.70           C  
ANISOU 1124  CG  ASN A  78    10124  10897  10780  -5852   3102   -505
ATOM   1125  OD1 ASN A  78      53.758  -5.354  40.553  1.00 79.40           O  
ANISOU 1125  OD1 ASN A  78     9467  10505  10197  -5421   3068   -625
ATOM   1126  ND2 ASN A  78      55.985  -5.206  40.423  1.00 85.56           N  
ANISOU 1126  ND2 ASN A  78    10656  10863  10991  -5999   3205   -275
ATOM   1127  H   ASN A  78      52.517  -7.076  42.656  1.00 81.65           H  
ATOM   1128  HA  ASN A  78      54.688  -6.300  44.457  1.00 82.77           H  
ATOM   1129  HB3 ASN A  78      54.915  -7.470  42.122  1.00 85.40           H  
ATOM   1130  HB2 ASN A  78      56.071  -6.298  42.650  1.00 85.40           H  
ATOM   1131 HD22 ASN A  78      55.924  -4.630  39.595  1.00 85.56           H  
ATOM   1132 HD21 ASN A  78      56.885  -5.407  40.833  1.00 85.56           H  
ATOM   1133  N   VAL A  79      52.787  -3.973  43.106  1.00 75.42           N  
ANISOU 1133  N   VAL A  79     9038   9733   9885  -5256   2722  -1046
ATOM   1134  CA  VAL A  79      52.551  -2.538  42.946  1.00 71.80           C  
ANISOU 1134  CA  VAL A  79     8861   8963   9458  -4880   2653  -1109
ATOM   1135  C   VAL A  79      52.492  -1.827  44.306  1.00 71.20           C  
ANISOU 1135  C   VAL A  79     8971   8620   9463  -4922   2501  -1277
ATOM   1136  O   VAL A  79      51.823  -2.250  45.248  1.00 72.05           O  
ANISOU 1136  O   VAL A  79     8873   8914   9588  -5051   2396  -1417
ATOM   1137  CB  VAL A  79      51.339  -2.215  42.023  1.00 68.49           C  
ANISOU 1137  CB  VAL A  79     8236   8800   8987  -4441   2632  -1166
ATOM   1138  CG1 VAL A  79      50.054  -2.971  42.340  1.00 68.26           C  
ANISOU 1138  CG1 VAL A  79     7801   9186   8951  -4421   2551  -1304
ATOM   1139  CG2 VAL A  79      51.050  -0.709  41.906  1.00 66.28           C  
ANISOU 1139  CG2 VAL A  79     8210   8218   8753  -4108   2539  -1230
ATOM   1140  H   VAL A  79      52.077  -4.607  42.772  1.00 75.42           H  
ATOM   1141  HA  VAL A  79      53.422  -2.157  42.415  1.00 71.80           H  
ATOM   1142  HB  VAL A  79      51.631  -2.531  41.020  1.00 68.49           H  
ATOM   1143 HG11 VAL A  79      49.188  -2.506  41.867  1.00 68.26           H  
ATOM   1144 HG12 VAL A  79      50.129  -3.969  41.925  1.00 68.26           H  
ATOM   1145 HG13 VAL A  79      49.867  -3.030  43.411  1.00 68.26           H  
ATOM   1146 HG21 VAL A  79      50.340  -0.505  41.105  1.00 66.28           H  
ATOM   1147 HG22 VAL A  79      50.634  -0.295  42.826  1.00 66.28           H  
ATOM   1148 HG23 VAL A  79      51.967  -0.168  41.675  1.00 66.28           H  
ATOM   1149  N   ASN A  80      53.245  -0.728  44.344  1.00 70.35           N  
ANISOU 1149  N   ASN A  80     9255   8082   9391  -4814   2494  -1257
ATOM   1150  CA  ASN A  80      53.460   0.217  45.425  1.00 70.05           C  
ANISOU 1150  CA  ASN A  80     9452   7760   9403  -4784   2371  -1416
ATOM   1151  C   ASN A  80      53.411   1.633  44.835  1.00 67.73           C  
ANISOU 1151  C   ASN A  80     9446   7175   9112  -4418   2390  -1381
ATOM   1152  O   ASN A  80      53.120   1.796  43.646  1.00 66.68           O  
ANISOU 1152  O   ASN A  80     9330   7053   8951  -4245   2483  -1231
ATOM   1153  CB  ASN A  80      54.743  -0.148  46.220  1.00 73.41           C  
ANISOU 1153  CB  ASN A  80    10099   7911   9883  -5200   2345  -1431
ATOM   1154  CG  ASN A  80      55.999  -0.323  45.352  1.00 75.20           C  
ANISOU 1154  CG  ASN A  80    10590   7854  10130  -5349   2461  -1221
ATOM   1155  OD1 ASN A  80      56.424   0.610  44.677  1.00 73.22           O  
ANISOU 1155  OD1 ASN A  80    10572   7377   9870  -5078   2517  -1128
ATOM   1156  ND2 ASN A  80      56.581  -1.522  45.338  1.00 80.03           N  
ANISOU 1156  ND2 ASN A  80    11158   8485  10766  -5792   2490  -1128
ATOM   1157  H   ASN A  80      53.727  -0.498  43.487  1.00 70.35           H  
ATOM   1158  HA  ASN A  80      52.618   0.152  46.112  1.00 70.05           H  
ATOM   1159  HB3 ASN A  80      54.562  -1.073  46.768  1.00 73.41           H  
ATOM   1160  HB2 ASN A  80      54.951   0.606  46.980  1.00 73.41           H  
ATOM   1161 HD22 ASN A  80      57.396  -1.674  44.764  1.00 80.03           H  
ATOM   1162 HD21 ASN A  80      56.185  -2.288  45.865  1.00 80.03           H  
ATOM   1163  N   MET A  81      53.704   2.663  45.644  1.00 67.18           N  
ANISOU 1163  N   MET A  81     9592   6869   9063  -4295   2303  -1518
ATOM   1164  CA  MET A  81      53.739   4.049  45.179  1.00 65.33           C  
ANISOU 1164  CA  MET A  81     9592   6401   8828  -3940   2323  -1485
ATOM   1165  C   MET A  81      54.860   4.303  44.155  1.00 66.47           C  
ANISOU 1165  C   MET A  81    10008   6256   8991  -3940   2425  -1304
ATOM   1166  O   MET A  81      54.620   5.008  43.178  1.00 64.73           O  
ANISOU 1166  O   MET A  81     9816   6027   8752  -3651   2472  -1198
ATOM   1167  CB  MET A  81      53.882   5.011  46.368  1.00 65.37           C  
ANISOU 1167  CB  MET A  81     9804   6202   8832  -3821   2235  -1659
ATOM   1168  CG  MET A  81      53.685   6.474  45.931  1.00 62.95           C  
ANISOU 1168  CG  MET A  81     9631   5772   8513  -3418   2258  -1621
ATOM   1169  SD  MET A  81      53.371   7.661  47.255  1.00 62.43           S  
ANISOU 1169  SD  MET A  81     9659   5664   8399  -3191   2173  -1813
ATOM   1170  CE  MET A  81      51.652   7.222  47.588  1.00 61.28           C  
ANISOU 1170  CE  MET A  81     9131   5943   8209  -3290   2070  -1909
ATOM   1171  H   MET A  81      53.931   2.482  46.611  1.00 67.18           H  
ATOM   1172  HA  MET A  81      52.774   4.254  44.711  1.00 65.33           H  
ATOM   1173  HB3 MET A  81      54.848   4.891  46.864  1.00 65.37           H  
ATOM   1174  HB2 MET A  81      53.128   4.751  47.111  1.00 65.37           H  
ATOM   1175  HG3 MET A  81      52.855   6.544  45.228  1.00 62.95           H  
ATOM   1176  HG2 MET A  81      54.569   6.807  45.391  1.00 62.95           H  
ATOM   1177  HE1 MET A  81      51.199   7.840  48.357  1.00 61.28           H  
ATOM   1178  HE2 MET A  81      51.055   7.327  46.684  1.00 61.28           H  
ATOM   1179  HE3 MET A  81      51.608   6.195  47.929  1.00 61.28           H  
ATOM   1180  N   ASP A  82      56.056   3.720  44.349  1.00 69.45           N  
ANISOU 1180  N   ASP A  82    10588   6394   9407  -4269   2445  -1259
ATOM   1181  CA  ASP A  82      57.215   3.911  43.469  1.00 70.93           C  
ANISOU 1181  CA  ASP A  82    11070   6268   9612  -4271   2526  -1070
ATOM   1182  C   ASP A  82      57.026   3.227  42.103  1.00 70.36           C  
ANISOU 1182  C   ASP A  82    10807   6451   9478  -4253   2639   -856
ATOM   1183  O   ASP A  82      57.532   3.739  41.106  1.00 69.80           O  
ANISOU 1183  O   ASP A  82    10901   6236   9383  -4048   2694   -707
ATOM   1184  CB  ASP A  82      58.517   3.383  44.121  1.00 75.30           C  
ANISOU 1184  CB  ASP A  82    11908   6471  10232  -4656   2503  -1052
ATOM   1185  CG  ASP A  82      58.938   4.067  45.430  1.00 76.48           C  
ANISOU 1185  CG  ASP A  82    12323   6307  10429  -4634   2384  -1281
ATOM   1186  OD1 ASP A  82      58.130   4.829  46.007  1.00 74.57           O  
ANISOU 1186  OD1 ASP A  82    11969   6215  10151  -4392   2325  -1463
ATOM   1187  OD2 ASP A  82      60.097   3.818  45.830  1.00 81.69           O1-
ANISOU 1187  OD2 ASP A  82    13314   6567  11156  -4870   2343  -1279
ATOM   1188  H   ASP A  82      56.191   3.149  45.171  1.00 69.45           H  
ATOM   1189  HA  ASP A  82      57.337   4.981  43.296  1.00 70.93           H  
ATOM   1190  HB3 ASP A  82      59.343   3.506  43.421  1.00 75.30           H  
ATOM   1191  HB2 ASP A  82      58.440   2.313  44.314  1.00 75.30           H  
ATOM   1192  N   GLU A  83      56.256   2.125  42.049  1.00 70.82           N  
ANISOU 1192  N   GLU A  83    10512   6901   9494  -4453   2670   -849
ATOM   1193  CA  GLU A  83      55.846   1.426  40.832  1.00 70.51           C  
ANISOU 1193  CA  GLU A  83    10247   7181   9363  -4397   2781   -685
ATOM   1194  C   GLU A  83      54.936   2.329  39.980  1.00 67.05           C  
ANISOU 1194  C   GLU A  83     9770   6822   8885  -3941   2767   -694
ATOM   1195  O   GLU A  83      55.296   2.610  38.841  1.00 66.80           O  
ANISOU 1195  O   GLU A  83     9868   6712   8802  -3786   2831   -536
ATOM   1196  CB  GLU A  83      55.122   0.112  41.211  1.00 70.70           C  
ANISOU 1196  CB  GLU A  83     9846   7674   9345  -4581   2796   -741
ATOM   1197  CG  GLU A  83      56.068  -1.101  41.336  1.00 76.23           C  
ANISOU 1197  CG  GLU A  83    10484   8441  10038  -5051   2870   -621
ATOM   1198  CD  GLU A  83      56.498  -1.686  39.988  1.00 80.22           C  
ANISOU 1198  CD  GLU A  83    10985   9057  10440  -5115   3029   -363
ATOM   1199  OE1 GLU A  83      55.597  -1.956  39.163  1.00 80.96           O  
ANISOU 1199  OE1 GLU A  83    10854   9482  10426  -4854   3090   -342
ATOM   1200  OE2 GLU A  83      57.718  -1.882  39.813  1.00 80.26           O1-
ANISOU 1200  OE2 GLU A  83    11214   8819  10462  -5430   3084   -183
ATOM   1201  H   GLU A  83      55.905   1.763  42.925  1.00 70.82           H  
ATOM   1202  HA  GLU A  83      56.736   1.199  40.242  1.00 70.51           H  
ATOM   1203  HB3 GLU A  83      54.340  -0.122  40.483  1.00 70.70           H  
ATOM   1204  HB2 GLU A  83      54.591   0.245  42.152  1.00 70.70           H  
ATOM   1205  HG3 GLU A  83      55.579  -1.901  41.889  1.00 76.23           H  
ATOM   1206  HG2 GLU A  83      56.948  -0.830  41.921  1.00 76.23           H  
ATOM   1207  N   VAL A  84      53.806   2.832  40.519  1.00 64.29           N  
ANISOU 1207  N   VAL A  84     9245   6625   8559  -3743   2670   -871
ATOM   1208  CA  VAL A  84      52.882   3.715  39.785  1.00 61.35           C  
ANISOU 1208  CA  VAL A  84     8802   6343   8166  -3351   2631   -886
ATOM   1209  C   VAL A  84      53.492   5.086  39.427  1.00 60.57           C  
ANISOU 1209  C   VAL A  84     9019   5903   8091  -3118   2627   -817
ATOM   1210  O   VAL A  84      53.127   5.636  38.391  1.00 59.34           O  
ANISOU 1210  O   VAL A  84     8865   5787   7893  -2879   2644   -720
ATOM   1211  CB  VAL A  84      51.540   3.912  40.538  1.00 59.36           C  
ANISOU 1211  CB  VAL A  84     8312   6300   7942  -3220   2514  -1064
ATOM   1212  CG1 VAL A  84      50.763   2.598  40.675  1.00 60.46           C  
ANISOU 1212  CG1 VAL A  84     8100   6831   8043  -3341   2520  -1105
ATOM   1213  CG2 VAL A  84      51.677   4.590  41.910  1.00 60.21           C  
ANISOU 1213  CG2 VAL A  84     8539   6234   8103  -3339   2441  -1200
ATOM   1214  H   VAL A  84      53.572   2.590  41.471  1.00 64.29           H  
ATOM   1215  HA  VAL A  84      52.652   3.223  38.837  1.00 61.35           H  
ATOM   1216  HB  VAL A  84      50.918   4.568  39.924  1.00 59.36           H  
ATOM   1217 HG11 VAL A  84      49.754   2.776  41.045  1.00 60.46           H  
ATOM   1218 HG12 VAL A  84      50.678   2.078  39.722  1.00 60.46           H  
ATOM   1219 HG13 VAL A  84      51.258   1.939  41.385  1.00 60.46           H  
ATOM   1220 HG21 VAL A  84      50.702   4.769  42.350  1.00 60.21           H  
ATOM   1221 HG22 VAL A  84      52.234   3.956  42.593  1.00 60.21           H  
ATOM   1222 HG23 VAL A  84      52.178   5.555  41.856  1.00 60.21           H  
ATOM   1223  N   LYS A  85      54.438   5.606  40.234  1.00 61.54           N  
ANISOU 1223  N   LYS A  85     9406   5701   8274  -3177   2597   -874
ATOM   1224  CA  LYS A  85      55.201   6.829  39.964  1.00 61.39           C  
ANISOU 1224  CA  LYS A  85     9693   5355   8278  -2946   2599   -810
ATOM   1225  C   LYS A  85      56.097   6.662  38.726  1.00 63.00           C  
ANISOU 1225  C   LYS A  85    10048   5452   8438  -2964   2685   -585
ATOM   1226  O   LYS A  85      56.089   7.517  37.841  1.00 61.91           O  
ANISOU 1226  O   LYS A  85     9932   5326   8263  -2689   2689   -487
ATOM   1227  CB  LYS A  85      56.101   7.177  41.173  1.00 63.13           C  
ANISOU 1227  CB  LYS A  85    10196   5232   8557  -3034   2562   -919
ATOM   1228  CG  LYS A  85      55.439   8.007  42.286  1.00 60.94           C  
ANISOU 1228  CG  LYS A  85     9876   4985   8294  -2885   2479  -1122
ATOM   1229  CD  LYS A  85      56.464   8.418  43.359  1.00 64.89           C  
ANISOU 1229  CD  LYS A  85    10700   5125   8831  -3003   2450  -1237
ATOM   1230  CE  LYS A  85      56.067   9.642  44.200  1.00 66.06           C  
ANISOU 1230  CE  LYS A  85    10929   5209   8964  -2737   2396  -1407
ATOM   1231  NZ  LYS A  85      55.732   9.284  45.585  1.00 67.37           N1+
ANISOU 1231  NZ  LYS A  85    10947   5551   9098  -2886   2322  -1603
ATOM   1232  H   LYS A  85      54.670   5.102  41.080  1.00 61.54           H  
ATOM   1233  HA  LYS A  85      54.507   7.649  39.773  1.00 61.39           H  
ATOM   1234  HB3 LYS A  85      56.951   7.764  40.818  1.00 63.13           H  
ATOM   1235  HB2 LYS A  85      56.537   6.272  41.590  1.00 63.13           H  
ATOM   1236  HG3 LYS A  85      54.600   7.481  42.737  1.00 60.94           H  
ATOM   1237  HG2 LYS A  85      55.017   8.901  41.844  1.00 60.94           H  
ATOM   1238  HD3 LYS A  85      57.381   8.695  42.850  1.00 64.89           H  
ATOM   1239  HD2 LYS A  85      56.730   7.563  43.984  1.00 64.89           H  
ATOM   1240  HE3 LYS A  85      55.237  10.191  43.754  1.00 66.06           H  
ATOM   1241  HE2 LYS A  85      56.905  10.338  44.244  1.00 66.06           H  
ATOM   1242  HZ1 LYS A  85      55.545  10.138  46.102  1.00 67.37           H  
ATOM   1243  HZ2 LYS A  85      54.910   8.699  45.609  1.00 67.37           H  
ATOM   1244  HZ3 LYS A  85      56.508   8.802  46.016  1.00 67.37           H  
ATOM   1245  N   ALA A  86      56.836   5.542  38.664  1.00 65.73           N  
ANISOU 1245  N   ALA A  86    10481   5715   8778  -3305   2746   -492
ATOM   1246  CA  ALA A  86      57.750   5.187  37.585  1.00 67.77           C  
ANISOU 1246  CA  ALA A  86    10882   5894   8975  -3376   2835   -249
ATOM   1247  C   ALA A  86      57.004   4.863  36.284  1.00 66.23           C  
ANISOU 1247  C   ALA A  86    10440   6065   8661  -3210   2885   -156
ATOM   1248  O   ALA A  86      57.399   5.342  35.225  1.00 66.02           O  
ANISOU 1248  O   ALA A  86    10543   5970   8572  -3014   2908     -3
ATOM   1249  CB  ALA A  86      58.542   3.945  38.016  1.00 71.16           C  
ANISOU 1249  CB  ALA A  86    11378   6244   9414  -3835   2892   -155
ATOM   1250  H   ALA A  86      56.773   4.891  39.435  1.00 65.73           H  
ATOM   1251  HA  ALA A  86      58.439   6.015  37.413  1.00 67.77           H  
ATOM   1252  HB1 ALA A  86      59.261   3.656  37.250  1.00 71.16           H  
ATOM   1253  HB2 ALA A  86      59.090   4.138  38.936  1.00 71.16           H  
ATOM   1254  HB3 ALA A  86      57.896   3.088  38.204  1.00 71.16           H  
ATOM   1255  N   LEU A  87      55.917   4.079  36.372  1.00 65.21           N  
ANISOU 1255  N   LEU A  87     9962   6322   8495  -3273   2890   -260
ATOM   1256  CA  LEU A  87      55.115   3.631  35.236  1.00 64.34           C  
ANISOU 1256  CA  LEU A  87     9612   6575   8261  -3137   2934   -207
ATOM   1257  C   LEU A  87      54.242   4.750  34.632  1.00 61.67           C  
ANISOU 1257  C   LEU A  87     9277   6240   7917  -2730   2851   -244
ATOM   1258  O   LEU A  87      53.968   4.700  33.434  1.00 61.60           O  
ANISOU 1258  O   LEU A  87     9252   6356   7796  -2576   2880   -136
ATOM   1259  CB  LEU A  87      54.202   2.477  35.670  1.00 63.99           C  
ANISOU 1259  CB  LEU A  87     9194   6926   8193  -3259   2939   -340
ATOM   1260  CG  LEU A  87      54.868   1.154  36.094  1.00 67.34           C  
ANISOU 1260  CG  LEU A  87     9494   7514   8578  -3667   3041   -273
ATOM   1261  CD1 LEU A  87      53.865   0.304  36.890  1.00 68.74           C  
ANISOU 1261  CD1 LEU A  87     9306   8039   8774  -3732   3000   -457
ATOM   1262  CD2 LEU A  87      55.389   0.359  34.889  1.00 66.39           C  
ANISOU 1262  CD2 LEU A  87     9336   7594   8297  -3742   3183    -65
ATOM   1263  H   LEU A  87      55.662   3.721  37.284  1.00 65.21           H  
ATOM   1264  HA  LEU A  87      55.764   3.271  34.446  1.00 64.34           H  
ATOM   1265  HB3 LEU A  87      53.586   2.222  34.815  1.00 63.99           H  
ATOM   1266  HB2 LEU A  87      53.545   2.835  36.465  1.00 63.99           H  
ATOM   1267  HG  LEU A  87      55.721   1.364  36.738  1.00 67.34           H  
ATOM   1268 HD11 LEU A  87      54.338  -0.602  37.261  1.00 68.74           H  
ATOM   1269 HD12 LEU A  87      53.478   0.841  37.755  1.00 68.74           H  
ATOM   1270 HD13 LEU A  87      53.013   0.012  36.274  1.00 68.74           H  
ATOM   1271 HD21 LEU A  87      55.865  -0.567  35.211  1.00 66.39           H  
ATOM   1272 HD22 LEU A  87      54.583   0.095  34.203  1.00 66.39           H  
ATOM   1273 HD23 LEU A  87      56.132   0.926  34.329  1.00 66.39           H  
ATOM   1274  N   SER A  88      53.841   5.766  35.417  1.00 59.60           N  
ANISOU 1274  N   SER A  88     9032   5851   7763  -2569   2746   -388
ATOM   1275  CA  SER A  88      53.141   6.954  34.915  1.00 57.27           C  
ANISOU 1275  CA  SER A  88     8719   5559   7483  -2211   2653   -416
ATOM   1276  C   SER A  88      54.098   7.922  34.189  1.00 57.88           C  
ANISOU 1276  C   SER A  88     9079   5363   7548  -2055   2664   -265
ATOM   1277  O   SER A  88      53.668   8.593  33.252  1.00 56.62           O  
ANISOU 1277  O   SER A  88     8902   5259   7352  -1800   2613   -214
ATOM   1278  CB  SER A  88      52.403   7.667  36.067  1.00 55.24           C  
ANISOU 1278  CB  SER A  88     8384   5276   7330  -2102   2549   -582
ATOM   1279  OG  SER A  88      53.270   8.278  37.000  1.00 55.68           O  
ANISOU 1279  OG  SER A  88     8683   5021   7451  -2112   2549   -598
ATOM   1280  H   SER A  88      54.073   5.739  36.402  1.00 59.60           H  
ATOM   1281  HA  SER A  88      52.382   6.628  34.202  1.00 57.27           H  
ATOM   1282  HB3 SER A  88      51.742   6.975  36.589  1.00 55.24           H  
ATOM   1283  HB2 SER A  88      51.762   8.447  35.656  1.00 55.24           H  
ATOM   1284  HG  SER A  88      53.762   7.603  37.445  1.00 55.68           H  
ATOM   1285  N   LEU A  89      55.391   7.961  34.568  1.00 60.02           N  
ANISOU 1285  N   LEU A  89     9619   5328   7857  -2204   2713   -196
ATOM   1286  CA  LEU A  89      56.444   8.682  33.844  1.00 61.40           C  
ANISOU 1286  CA  LEU A  89    10079   5235   8016  -2058   2722    -31
ATOM   1287  C   LEU A  89      56.824   7.938  32.548  1.00 62.88           C  
ANISOU 1287  C   LEU A  89    10259   5573   8060  -2080   2786    162
ATOM   1288  O   LEU A  89      57.069   8.593  31.536  1.00 62.59           O  
ANISOU 1288  O   LEU A  89    10266   5549   7966  -1820   2745    252
ATOM   1289  CB  LEU A  89      57.659   8.884  34.788  1.00 63.84           C  
ANISOU 1289  CB  LEU A  89    10707   5146   8405  -2206   2743     -9
ATOM   1290  CG  LEU A  89      58.968   9.451  34.177  1.00 66.35           C  
ANISOU 1290  CG  LEU A  89    11379   5113   8719  -2105   2752    180
ATOM   1291  CD1 LEU A  89      58.813  10.716  33.319  1.00 64.35           C  
ANISOU 1291  CD1 LEU A  89    11137   4881   8433  -1714   2695    252
ATOM   1292  CD2 LEU A  89      59.998   9.721  35.289  1.00 69.37           C  
ANISOU 1292  CD2 LEU A  89    12050   5092   9217  -2158   2724     96
ATOM   1293  H   LEU A  89      55.676   7.401  35.358  1.00 60.02           H  
ATOM   1294  HA  LEU A  89      56.057   9.662  33.564  1.00 61.40           H  
ATOM   1295  HB3 LEU A  89      57.902   7.933  35.263  1.00 63.84           H  
ATOM   1296  HB2 LEU A  89      57.346   9.534  35.604  1.00 63.84           H  
ATOM   1297  HG  LEU A  89      59.374   8.689  33.514  1.00 66.35           H  
ATOM   1298 HD11 LEU A  89      59.636  10.790  32.612  1.00 64.35           H  
ATOM   1299 HD12 LEU A  89      57.897  10.739  32.733  1.00 64.35           H  
ATOM   1300 HD13 LEU A  89      58.844  11.616  33.928  1.00 64.35           H  
ATOM   1301 HD21 LEU A  89      60.947  10.054  34.872  1.00 69.37           H  
ATOM   1302 HD22 LEU A  89      59.649  10.499  35.968  1.00 69.37           H  
ATOM   1303 HD23 LEU A  89      60.190   8.833  35.889  1.00 69.37           H  
ATOM   1304  N   TRP A  90      56.776   6.591  32.529  1.00 64.52           N  
ANISOU 1304  N   TRP A  90    10390   5931   8196  -2387   2884    224
ATOM   1305  CA  TRP A  90      56.882   5.785  31.307  1.00 65.59           C  
ANISOU 1305  CA  TRP A  90    10462   6303   8155  -2415   2963    391
ATOM   1306  C   TRP A  90      55.691   5.993  30.346  1.00 63.43           C  
ANISOU 1306  C   TRP A  90     9974   6325   7801  -2113   2895    310
ATOM   1307  O   TRP A  90      55.871   5.866  29.135  1.00 64.11           O  
ANISOU 1307  O   TRP A  90    10126   6478   7756  -1961   2898    444
ATOM   1308  CB  TRP A  90      57.022   4.283  31.642  1.00 67.66           C  
ANISOU 1308  CB  TRP A  90    10557   6804   8348  -2774   3081    422
ATOM   1309  CG  TRP A  90      58.338   3.834  32.217  1.00 71.20           C  
ANISOU 1309  CG  TRP A  90    11240   6968   8847  -3136   3150    570
ATOM   1310  CD1 TRP A  90      58.510   3.136  33.364  1.00 72.23           C  
ANISOU 1310  CD1 TRP A  90    11310   7064   9072  -3467   3166    485
ATOM   1311  CD2 TRP A  90      59.678   3.992  31.658  1.00 72.83           C  
ANISOU 1311  CD2 TRP A  90    11787   6868   9018  -3210   3188    831
ATOM   1312  NE1 TRP A  90      59.848   2.895  33.577  1.00 75.66           N  
ANISOU 1312  NE1 TRP A  90    12030   7174   9543  -3759   3207    667
ATOM   1313  CE2 TRP A  90      60.618   3.387  32.549  1.00 76.98           C  
ANISOU 1313  CE2 TRP A  90    12456   7157   9635  -3604   3222    889
ATOM   1314  CE3 TRP A  90      60.198   4.568  30.476  1.00 73.31           C  
ANISOU 1314  CE3 TRP A  90    12052   6823   8980  -2983   3180   1025
ATOM   1315  CZ2 TRP A  90      61.998   3.366  32.294  1.00 79.51           C  
ANISOU 1315  CZ2 TRP A  90    13139   7107   9965  -3782   3246   1144
ATOM   1316  CZ3 TRP A  90      61.579   4.542  30.204  1.00 77.65           C  
ANISOU 1316  CZ3 TRP A  90    12951   7027   9526  -3139   3210   1285
ATOM   1317  CH2 TRP A  90      62.480   3.946  31.110  1.00 79.09           C  
ANISOU 1317  CH2 TRP A  90    13289   6948   9814  -3538   3242   1346
ATOM   1318  H   TRP A  90      56.590   6.105  33.395  1.00 64.52           H  
ATOM   1319  HA  TRP A  90      57.774   6.102  30.772  1.00 65.59           H  
ATOM   1320  HB3 TRP A  90      56.891   3.699  30.729  1.00 67.66           H  
ATOM   1321  HB2 TRP A  90      56.217   3.969  32.302  1.00 67.66           H  
ATOM   1322  HD1 TRP A  90      57.724   2.813  34.022  1.00 72.23           H  
ATOM   1323  HE1 TRP A  90      60.192   2.396  34.386  1.00 75.66           H  
ATOM   1324  HE3 TRP A  90      59.529   5.022  29.760  1.00 73.31           H  
ATOM   1325  HZ2 TRP A  90      62.679   2.903  32.994  1.00 79.51           H  
ATOM   1326  HZ3 TRP A  90      61.941   4.979  29.289  1.00 77.65           H  
ATOM   1327  HH2 TRP A  90      63.539   3.925  30.899  1.00 79.09           H  
ATOM   1328  N   MET A  91      54.502   6.350  30.865  1.00 61.18           N  
ANISOU 1328  N   MET A  91     9450   6203   7593  -2024   2817     94
ATOM   1329  CA  MET A  91      53.307   6.642  30.071  1.00 59.24           C  
ANISOU 1329  CA  MET A  91     9017   6192   7298  -1744   2719      1
ATOM   1330  C   MET A  91      53.332   8.040  29.435  1.00 58.60           C  
ANISOU 1330  C   MET A  91     9085   5950   7229  -1454   2619     70
ATOM   1331  O   MET A  91      52.756   8.213  28.361  1.00 58.78           O  
ANISOU 1331  O   MET A  91     9076   6127   7131  -1283   2578    116
ATOM   1332  CB  MET A  91      52.045   6.510  30.950  1.00 56.60           C  
ANISOU 1332  CB  MET A  91     8433   6005   7068  -1707   2631   -220
ATOM   1333  CG  MET A  91      51.496   5.082  30.939  1.00 58.20           C  
ANISOU 1333  CG  MET A  91     8377   6551   7184  -1825   2684   -305
ATOM   1334  SD  MET A  91      50.785   4.615  29.335  1.00 57.35           S  
ANISOU 1334  SD  MET A  91     8173   6763   6857  -1656   2707   -266
ATOM   1335  CE  MET A  91      50.384   2.885  29.666  1.00 58.67           C  
ANISOU 1335  CE  MET A  91     7993   7308   6990  -1775   2752   -438
ATOM   1336  H   MET A  91      54.421   6.424  31.869  1.00 61.18           H  
ATOM   1337  HA  MET A  91      53.254   5.924  29.256  1.00 59.24           H  
ATOM   1338  HB3 MET A  91      51.247   7.169  30.604  1.00 56.60           H  
ATOM   1339  HB2 MET A  91      52.255   6.819  31.971  1.00 56.60           H  
ATOM   1340  HG3 MET A  91      50.730   4.972  31.705  1.00 58.20           H  
ATOM   1341  HG2 MET A  91      52.286   4.376  31.198  1.00 58.20           H  
ATOM   1342  HE1 MET A  91      50.096   2.379  28.745  1.00 58.67           H  
ATOM   1343  HE2 MET A  91      51.251   2.367  30.076  1.00 58.67           H  
ATOM   1344  HE3 MET A  91      49.558   2.817  30.371  1.00 58.67           H  
ATOM   1345  N   THR A  92      54.036   9.012  30.044  1.00 58.28           N  
ANISOU 1345  N   THR A  92     9200   5620   7324  -1390   2576     69
ATOM   1346  CA  THR A  92      54.283  10.344  29.478  1.00 57.95           C  
ANISOU 1346  CA  THR A  92     9283   5435   7301  -1114   2486    146
ATOM   1347  C   THR A  92      55.172  10.243  28.221  1.00 60.11           C  
ANISOU 1347  C   THR A  92     9732   5685   7422  -1064   2525    357
ATOM   1348  O   THR A  92      54.954  10.986  27.264  1.00 59.73           O  
ANISOU 1348  O   THR A  92     9664   5723   7309   -832   2432    400
ATOM   1349  CB  THR A  92      54.933  11.240  30.566  1.00 58.04           C  
ANISOU 1349  CB  THR A  92     9452   5146   7455  -1058   2469    124
ATOM   1350  OG1 THR A  92      53.958  11.561  31.527  1.00 56.24           O  
ANISOU 1350  OG1 THR A  92     9035   4999   7334  -1051   2412    -60
ATOM   1351  CG2 THR A  92      55.463  12.593  30.077  1.00 58.34           C  
ANISOU 1351  CG2 THR A  92     9607   5057   7501   -765   2391    224
ATOM   1352  H   THR A  92      54.464   8.806  30.935  1.00 58.28           H  
ATOM   1353  HA  THR A  92      53.331  10.781  29.172  1.00 57.95           H  
ATOM   1354  HB  THR A  92      55.743  10.709  31.067  1.00 58.04           H  
ATOM   1355  HG1 THR A  92      54.393  11.953  32.274  1.00 56.24           H  
ATOM   1356 HG21 THR A  92      55.793  13.214  30.912  1.00 58.34           H  
ATOM   1357 HG22 THR A  92      56.324  12.461  29.425  1.00 58.34           H  
ATOM   1358 HG23 THR A  92      54.695  13.144  29.533  1.00 58.34           H  
ATOM   1359  N   PHE A  93      56.118   9.287  28.206  1.00 62.31           N  
ANISOU 1359  N   PHE A  93    10176   5861   7637  -1298   2651    495
ATOM   1360  CA  PHE A  93      56.951   8.965  27.052  1.00 64.29           C  
ANISOU 1360  CA  PHE A  93    10576   6143   7710  -1292   2701    720
ATOM   1361  C   PHE A  93      56.166   8.214  25.966  1.00 64.28           C  
ANISOU 1361  C   PHE A  93    10349   6548   7527  -1242   2703    680
ATOM   1362  O   PHE A  93      56.291   8.579  24.802  1.00 64.64           O  
ANISOU 1362  O   PHE A  93    10404   6691   7465  -1006   2617    727
ATOM   1363  CB  PHE A  93      58.141   8.090  27.494  1.00 66.89           C  
ANISOU 1363  CB  PHE A  93    11103   6304   8009  -1605   2837    891
ATOM   1364  CG  PHE A  93      59.244   8.840  28.210  1.00 68.42           C  
ANISOU 1364  CG  PHE A  93    11610   6047   8338  -1603   2816    976
ATOM   1365  CD1 PHE A  93      59.924   9.876  27.543  1.00 69.78           C  
ANISOU 1365  CD1 PHE A  93    12008   6013   8492  -1346   2746   1129
ATOM   1366  CD2 PHE A  93      59.639   8.473  29.515  1.00 69.51           C  
ANISOU 1366  CD2 PHE A  93    11828   5963   8619  -1845   2855    895
ATOM   1367  CE1 PHE A  93      61.025  10.504  28.152  1.00 71.00           C  
ANISOU 1367  CE1 PHE A  93    12470   5732   8776  -1302   2719   1193
ATOM   1368  CE2 PHE A  93      60.720   9.124  30.137  1.00 71.38           C  
ANISOU 1368  CE2 PHE A  93    12387   5755   8979  -1819   2823    946
ATOM   1369  CZ  PHE A  93      61.418  10.131  29.448  1.00 71.40           C  
ANISOU 1369  CZ  PHE A  93    12618   5544   8967  -1534   2758   1093
ATOM   1370  H   PHE A  93      56.237   8.720  29.032  1.00 62.31           H  
ATOM   1371  HA  PHE A  93      57.319   9.892  26.610  1.00 64.29           H  
ATOM   1372  HB3 PHE A  93      58.609   7.633  26.621  1.00 66.89           H  
ATOM   1373  HB2 PHE A  93      57.802   7.259  28.112  1.00 66.89           H  
ATOM   1374  HD1 PHE A  93      59.645  10.148  26.537  1.00 69.78           H  
ATOM   1375  HD2 PHE A  93      59.130   7.681  30.037  1.00 69.51           H  
ATOM   1376  HE1 PHE A  93      61.583  11.249  27.615  1.00 71.00           H  
ATOM   1377  HE2 PHE A  93      61.024   8.837  31.133  1.00 71.38           H  
ATOM   1378  HZ  PHE A  93      62.264  10.612  29.907  1.00 71.40           H  
ATOM   1379  N   LYS A  94      55.353   7.203  26.328  1.00 64.04           N  
ANISOU 1379  N   LYS A  94    10111   6763   7458  -1444   2788    576
ATOM   1380  CA  LYS A  94      54.529   6.414  25.399  1.00 64.08           C  
ANISOU 1380  CA  LYS A  94     9901   7168   7277  -1381   2801    511
ATOM   1381  C   LYS A  94      53.475   7.247  24.648  1.00 62.46           C  
ANISOU 1381  C   LYS A  94     9627   7044   7059  -1044   2624    402
ATOM   1382  O   LYS A  94      53.246   7.006  23.462  1.00 63.52           O  
ANISOU 1382  O   LYS A  94     9778   7359   6999   -901   2599    461
ATOM   1383  CB  LYS A  94      53.851   5.251  26.154  1.00 63.49           C  
ANISOU 1383  CB  LYS A  94     9556   7335   7231  -1557   2865    335
ATOM   1384  CG  LYS A  94      54.778   4.037  26.321  1.00 67.35           C  
ANISOU 1384  CG  LYS A  94     9980   8071   7540  -1821   3054    459
ATOM   1385  CD  LYS A  94      54.200   2.950  27.237  1.00 68.65           C  
ANISOU 1385  CD  LYS A  94     9939   8353   7793  -2103   3138    352
ATOM   1386  CE  LYS A  94      55.077   1.688  27.254  1.00 72.28           C  
ANISOU 1386  CE  LYS A  94    10384   8985   8093  -2437   3339    557
ATOM   1387  NZ  LYS A  94      54.608   0.715  28.254  1.00 72.64           N1+
ANISOU 1387  NZ  LYS A  94    10269   9087   8244  -2778   3417    506
ATOM   1388  H   LYS A  94      55.306   6.956  27.306  1.00 64.04           H  
ATOM   1389  HA  LYS A  94      55.183   5.998  24.633  1.00 64.08           H  
ATOM   1390  HB3 LYS A  94      52.962   4.916  25.617  1.00 63.49           H  
ATOM   1391  HB2 LYS A  94      53.495   5.599  27.121  1.00 63.49           H  
ATOM   1392  HG3 LYS A  94      55.736   4.365  26.727  1.00 67.35           H  
ATOM   1393  HG2 LYS A  94      54.992   3.617  25.336  1.00 67.35           H  
ATOM   1394  HD3 LYS A  94      53.192   2.691  26.910  1.00 68.65           H  
ATOM   1395  HD2 LYS A  94      54.106   3.353  28.247  1.00 68.65           H  
ATOM   1396  HE3 LYS A  94      56.112   1.946  27.485  1.00 72.28           H  
ATOM   1397  HE2 LYS A  94      55.076   1.217  26.270  1.00 72.28           H  
ATOM   1398  HZ1 LYS A  94      53.649   0.467  28.058  1.00 72.64           H  
ATOM   1399  HZ2 LYS A  94      55.182  -0.115  28.219  1.00 72.64           H  
ATOM   1400  HZ3 LYS A  94      54.667   1.123  29.176  1.00 72.64           H  
ATOM   1401  N   GLY A  95      52.876   8.246  25.319  1.00 60.15           N  
ANISOU 1401  N   GLY A  95     9271   6614   6971   -931   2495    255
ATOM   1402  CA  GLY A  95      51.912   9.174  24.737  1.00 58.30           C  
ANISOU 1402  CA  GLY A  95     8949   6433   6769   -657   2306    150
ATOM   1403  C   GLY A  95      52.572  10.254  23.875  1.00 59.22           C  
ANISOU 1403  C   GLY A  95     9248   6427   6825   -466   2229    311
ATOM   1404  O   GLY A  95      52.104  10.519  22.767  1.00 60.34           O  
ANISOU 1404  O   GLY A  95     9374   6745   6807   -315   2152    322
ATOM   1405  H   GLY A  95      53.102   8.367  26.297  1.00 60.15           H  
ATOM   1406  HA3 GLY A  95      51.364   9.657  25.546  1.00 58.30           H  
ATOM   1407  HA2 GLY A  95      51.178   8.626  24.144  1.00 58.30           H  
ATOM   1408  N   GLY A  96      53.677  10.847  24.362  1.00 59.05           N  
ANISOU 1408  N   GLY A  96     9404   6113   6921   -456   2241    427
ATOM   1409  CA  GLY A  96      54.432  11.900  23.683  1.00 59.77           C  
ANISOU 1409  CA  GLY A  96     9651   6080   6978   -242   2151    579
ATOM   1410  C   GLY A  96      55.237  11.421  22.467  1.00 62.29           C  
ANISOU 1410  C   GLY A  96    10108   6509   7049   -228   2198    760
ATOM   1411  O   GLY A  96      55.524  12.225  21.580  1.00 63.07           O  
ANISOU 1411  O   GLY A  96    10265   6643   7056    -16   2080    845
ATOM   1412  H   GLY A  96      54.008  10.566  25.275  1.00 59.05           H  
ATOM   1413  HA3 GLY A  96      55.126  12.341  24.401  1.00 59.77           H  
ATOM   1414  HA2 GLY A  96      53.752  12.698  23.378  1.00 59.77           H  
ATOM   1415  N   ALA A  97      55.554  10.115  22.400  1.00 63.44           N  
ANISOU 1415  N   ALA A  97    10294   6733   7077   -463   2367    829
ATOM   1416  CA  ALA A  97      56.237   9.447  21.289  1.00 66.35           C  
ANISOU 1416  CA  ALA A  97    10780   7247   7183   -483   2437   1021
ATOM   1417  C   ALA A  97      55.363   9.358  20.027  1.00 65.89           C  
ANISOU 1417  C   ALA A  97    10584   7499   6953   -268   2311    917
ATOM   1418  O   ALA A  97      55.891   9.392  18.917  1.00 67.88           O  
ANISOU 1418  O   ALA A  97    10959   7819   7014   -129   2261   1065
ATOM   1419  CB  ALA A  97      56.607   8.019  21.721  1.00 68.41           C  
ANISOU 1419  CB  ALA A  97    11013   7640   7339   -797   2644   1078
ATOM   1420  H   ALA A  97      55.297   9.533  23.186  1.00 63.44           H  
ATOM   1421  HA  ALA A  97      57.150   9.995  21.054  1.00 66.35           H  
ATOM   1422  HB1 ALA A  97      57.030   7.447  20.894  1.00 68.41           H  
ATOM   1423  HB2 ALA A  97      57.355   8.032  22.513  1.00 68.41           H  
ATOM   1424  HB3 ALA A  97      55.740   7.467  22.088  1.00 68.41           H  
ATOM   1425  N   LEU A  98      54.036   9.279  20.202  1.00 63.60           N  
ANISOU 1425  N   LEU A  98    10051   7384   6728   -238   2245    657
ATOM   1426  CA  LEU A  98      53.033   9.364  19.141  1.00 63.05           C  
ANISOU 1426  CA  LEU A  98     9851   7582   6524    -35   2096    503
ATOM   1427  C   LEU A  98      52.602  10.817  18.874  1.00 61.39           C  
ANISOU 1427  C   LEU A  98     9633   7246   6448    192   1860    452
ATOM   1428  O   LEU A  98      52.058  11.095  17.805  1.00 61.67           O  
ANISOU 1428  O   LEU A  98     9639   7438   6354    376   1701    391
ATOM   1429  CB  LEU A  98      51.776   8.618  19.621  1.00 61.68           C  
ANISOU 1429  CB  LEU A  98     9438   7619   6379    -88   2107    246
ATOM   1430  CG  LEU A  98      51.812   7.094  19.444  1.00 63.95           C  
ANISOU 1430  CG  LEU A  98     9663   8190   6445   -241   2309    263
ATOM   1431  CD1 LEU A  98      50.660   6.486  20.246  1.00 62.50           C  
ANISOU 1431  CD1 LEU A  98     9229   8186   6331   -261   2303     -2
ATOM   1432  CD2 LEU A  98      51.716   6.682  17.966  1.00 67.05           C  
ANISOU 1432  CD2 LEU A  98    10125   8853   6499   -105   2312    339
ATOM   1433  H   LEU A  98      53.691   9.232  21.151  1.00 63.60           H  
ATOM   1434  HA  LEU A  98      53.408   8.936  18.213  1.00 63.05           H  
ATOM   1435  HB3 LEU A  98      50.878   8.990  19.122  1.00 61.68           H  
ATOM   1436  HB2 LEU A  98      51.645   8.838  20.681  1.00 61.68           H  
ATOM   1437  HG  LEU A  98      52.745   6.706  19.857  1.00 63.95           H  
ATOM   1438 HD11 LEU A  98      50.653   5.405  20.163  1.00 62.50           H  
ATOM   1439 HD12 LEU A  98      50.758   6.737  21.303  1.00 62.50           H  
ATOM   1440 HD13 LEU A  98      49.693   6.853  19.902  1.00 62.50           H  
ATOM   1441 HD21 LEU A  98      51.544   5.612  17.868  1.00 67.05           H  
ATOM   1442 HD22 LEU A  98      50.888   7.186  17.465  1.00 67.05           H  
ATOM   1443 HD23 LEU A  98      52.629   6.918  17.423  1.00 67.05           H  
ATOM   1444  N   GLY A  99      52.821  11.730  19.834  1.00 59.95           N  
ANISOU 1444  N   GLY A  99     9470   6793   6516    174   1838    476
ATOM   1445  CA  GLY A  99      52.366  13.115  19.780  1.00 58.82           C  
ANISOU 1445  CA  GLY A  99     9287   6541   6521    364   1636    453
ATOM   1446  C   GLY A  99      50.872  13.266  20.092  1.00 56.92           C  
ANISOU 1446  C   GLY A  99     8817   6397   6412    389   1492    214
ATOM   1447  O   GLY A  99      50.222  14.143  19.522  1.00 56.35           O  
ANISOU 1447  O   GLY A  99     8668   6383   6360    543   1282    151
ATOM   1448  H   GLY A  99      53.292  11.430  20.677  1.00 59.95           H  
ATOM   1449  HA3 GLY A  99      52.586  13.547  18.803  1.00 58.82           H  
ATOM   1450  HA2 GLY A  99      52.932  13.688  20.514  1.00 58.82           H  
ATOM   1451  N   LEU A 100      50.325  12.410  20.975  1.00 55.93           N  
ANISOU 1451  N   LEU A 100     8589   6285   6378    225   1594     89
ATOM   1452  CA  LEU A 100      48.926  12.437  21.409  1.00 53.88           C  
ANISOU 1452  CA  LEU A 100     8127   6098   6246    230   1469   -128
ATOM   1453  C   LEU A 100      48.667  13.648  22.327  1.00 52.34           C  
ANISOU 1453  C   LEU A 100     7870   5716   6301    224   1402   -123
ATOM   1454  O   LEU A 100      49.583  14.064  23.041  1.00 52.47           O  
ANISOU 1454  O   LEU A 100     7987   5562   6387    170   1520     -2
ATOM   1455  CB  LEU A 100      48.598  11.162  22.222  1.00 53.80           C  
ANISOU 1455  CB  LEU A 100     8027   6201   6213     67   1612   -245
ATOM   1456  CG  LEU A 100      48.728   9.828  21.465  1.00 55.83           C  
ANISOU 1456  CG  LEU A 100     8294   6708   6211     41   1730   -262
ATOM   1457  CD1 LEU A 100      48.372   8.649  22.384  1.00 55.38           C  
ANISOU 1457  CD1 LEU A 100     8117   6745   6178   -145   1887   -349
ATOM   1458  CD2 LEU A 100      47.888   9.787  20.180  1.00 54.89           C  
ANISOU 1458  CD2 LEU A 100     8112   6786   5957    239   1553   -414
ATOM   1459  H   LEU A 100      50.926  11.719  21.405  1.00 55.93           H  
ATOM   1460  HA  LEU A 100      48.301  12.492  20.519  1.00 53.88           H  
ATOM   1461  HB3 LEU A 100      47.578  11.235  22.601  1.00 53.80           H  
ATOM   1462  HB2 LEU A 100      49.236  11.125  23.108  1.00 53.80           H  
ATOM   1463  HG  LEU A 100      49.768   9.712  21.183  1.00 55.83           H  
ATOM   1464 HD11 LEU A 100      48.475   7.692  21.870  1.00 55.38           H  
ATOM   1465 HD12 LEU A 100      49.016   8.621  23.262  1.00 55.38           H  
ATOM   1466 HD13 LEU A 100      47.345   8.722  22.735  1.00 55.38           H  
ATOM   1467 HD21 LEU A 100      47.874   8.788  19.747  1.00 54.89           H  
ATOM   1468 HD22 LEU A 100      46.861  10.083  20.382  1.00 54.89           H  
ATOM   1469 HD23 LEU A 100      48.284  10.461  19.422  1.00 54.89           H  
ATOM   1470  N   PRO A 101      47.427  14.191  22.358  1.00 51.30           N  
ANISOU 1470  N   PRO A 101     7579   5612   6301    281   1209   -251
ATOM   1471  CA  PRO A 101      47.029  15.282  23.257  1.00 49.76           C  
ANISOU 1471  CA  PRO A 101     7303   5280   6323    269   1153   -223
ATOM   1472  C   PRO A 101      46.748  14.735  24.671  1.00 49.03           C  
ANISOU 1472  C   PRO A 101     7146   5150   6334    106   1272   -303
ATOM   1473  O   PRO A 101      45.618  14.781  25.147  1.00 48.22           O  
ANISOU 1473  O   PRO A 101     6896   5063   6362     77   1161   -404
ATOM   1474  CB  PRO A 101      45.778  15.873  22.586  1.00 49.22           C  
ANISOU 1474  CB  PRO A 101     7095   5266   6339    358    889   -307
ATOM   1475  CG  PRO A 101      45.121  14.675  21.923  1.00 49.33           C  
ANISOU 1475  CG  PRO A 101     7097   5425   6222    387    816   -467
ATOM   1476  CD  PRO A 101      46.307  13.812  21.489  1.00 51.51           C  
ANISOU 1476  CD  PRO A 101     7504   5787   6280    358   1028   -424
ATOM   1477  HA  PRO A 101      47.800  16.050  23.316  1.00 49.76           H  
ATOM   1478  HB3 PRO A 101      46.084  16.586  21.819  1.00 49.22           H  
ATOM   1479  HB2 PRO A 101      45.112  16.407  23.264  1.00 49.22           H  
ATOM   1480  HG3 PRO A 101      44.469  14.948  21.091  1.00 49.33           H  
ATOM   1481  HG2 PRO A 101      44.516  14.134  22.653  1.00 49.33           H  
ATOM   1482  HD2 PRO A 101      46.069  12.751  21.568  1.00 51.51           H  
ATOM   1483  HD3 PRO A 101      46.562  14.028  20.451  1.00 51.51           H  
ATOM   1484  N   TYR A 102      47.789  14.198  25.323  1.00 49.53           N  
ANISOU 1484  N   TYR A 102     7323   5164   6333    -10   1481   -252
ATOM   1485  CA  TYR A 102      47.787  13.621  26.660  1.00 48.77           C  
ANISOU 1485  CA  TYR A 102     7181   5018   6332   -174   1593   -313
ATOM   1486  C   TYR A 102      49.123  13.895  27.348  1.00 49.52           C  
ANISOU 1486  C   TYR A 102     7442   4929   6445   -240   1750   -200
ATOM   1487  O   TYR A 102      50.144  14.086  26.687  1.00 50.81           O  
ANISOU 1487  O   TYR A 102     7755   4990   6562   -139   1769    -64
ATOM   1488  CB  TYR A 102      47.544  12.094  26.626  1.00 48.88           C  
ANISOU 1488  CB  TYR A 102     7138   5180   6254   -305   1684   -418
ATOM   1489  CG  TYR A 102      46.234  11.574  26.075  1.00 48.90           C  
ANISOU 1489  CG  TYR A 102     6986   5360   6236   -230   1541   -575
ATOM   1490  CD1 TYR A 102      44.998  12.097  26.508  1.00 48.07           C  
ANISOU 1490  CD1 TYR A 102     6748   5233   6284   -171   1354   -664
ATOM   1491  CD2 TYR A 102      46.259  10.501  25.165  1.00 48.96           C  
ANISOU 1491  CD2 TYR A 102     6981   5560   6062   -217   1595   -634
ATOM   1492  CE1 TYR A 102      43.791  11.543  26.045  1.00 45.96           C  
ANISOU 1492  CE1 TYR A 102     6369   5086   6006    -91   1204   -821
ATOM   1493  CE2 TYR A 102      45.056   9.944  24.706  1.00 46.73           C  
ANISOU 1493  CE2 TYR A 102     6574   5431   5751   -113   1463   -804
ATOM   1494  CZ  TYR A 102      43.825  10.447  25.164  1.00 44.83           C  
ANISOU 1494  CZ  TYR A 102     6231   5122   5680    -48   1262   -903
ATOM   1495  OH  TYR A 102      42.674   9.831  24.789  1.00 47.17           O  
ANISOU 1495  OH  TYR A 102     6433   5538   5950     68   1117  -1084
ATOM   1496  H   TYR A 102      48.682  14.202  24.848  1.00 49.53           H  
ATOM   1497  HA  TYR A 102      47.011  14.116  27.241  1.00 48.77           H  
ATOM   1498  HB3 TYR A 102      47.607  11.695  27.639  1.00 48.88           H  
ATOM   1499  HB2 TYR A 102      48.362  11.621  26.081  1.00 48.88           H  
ATOM   1500  HD1 TYR A 102      44.970  12.922  27.200  1.00 48.07           H  
ATOM   1501  HD2 TYR A 102      47.197  10.078  24.838  1.00 48.96           H  
ATOM   1502  HE1 TYR A 102      42.848  11.941  26.389  1.00 45.96           H  
ATOM   1503  HE2 TYR A 102      45.079   9.091  24.050  1.00 46.73           H  
ATOM   1504  HH  TYR A 102      41.901  10.237  25.153  1.00 47.17           H  
ATOM   1505  N   GLY A 103      49.120  13.775  28.679  1.00 48.80           N  
ANISOU 1505  N   GLY A 103     7327   4792   6422   -400   1845   -266
ATOM   1506  CA  GLY A 103      50.294  13.418  29.464  1.00 49.71           C  
ANISOU 1506  CA  GLY A 103     7614   4728   6544   -514   1998   -208
ATOM   1507  C   GLY A 103      50.112  12.012  30.045  1.00 49.78           C  
ANISOU 1507  C   GLY A 103     7570   4818   6526   -745   2097   -296
ATOM   1508  O   GLY A 103      49.110  11.343  29.785  1.00 49.64           O  
ANISOU 1508  O   GLY A 103     7373   4997   6491   -768   2043   -400
ATOM   1509  H   GLY A 103      48.227  13.628  29.130  1.00 48.80           H  
ATOM   1510  HA3 GLY A 103      50.428  14.154  30.251  1.00 49.71           H  
ATOM   1511  HA2 GLY A 103      51.211  13.433  28.872  1.00 49.71           H  
ATOM   1512  N   GLY A 104      51.087  11.554  30.837  1.00 50.72           N  
ANISOU 1512  N   GLY A 104     7841   4786   6643   -913   2229   -260
ATOM   1513  CA  GLY A 104      51.053  10.245  31.469  1.00 51.00           C  
ANISOU 1513  CA  GLY A 104     7815   4915   6648  -1164   2323   -324
ATOM   1514  C   GLY A 104      50.254  10.252  32.766  1.00 49.60           C  
ANISOU 1514  C   GLY A 104     7484   4788   6573  -1246   2282   -477
ATOM   1515  O   GLY A 104      50.258  11.224  33.520  1.00 49.38           O  
ANISOU 1515  O   GLY A 104     7502   4627   6635  -1186   2246   -508
ATOM   1516  H   GLY A 104      51.902  12.126  31.009  1.00 50.72           H  
ATOM   1517  HA3 GLY A 104      52.062   9.921  31.705  1.00 51.00           H  
ATOM   1518  HA2 GLY A 104      50.655   9.503  30.775  1.00 51.00           H  
ATOM   1519  N   GLY A 105      49.594   9.126  33.013  1.00 49.36           N  
ANISOU 1519  N   GLY A 105     7265   4975   6517  -1364   2286   -572
ATOM   1520  CA  GLY A 105      48.924   8.760  34.242  1.00 48.86           C  
ANISOU 1520  CA  GLY A 105     7057   4980   6529  -1479   2254   -705
ATOM   1521  C   GLY A 105      49.045   7.248  34.410  1.00 50.76           C  
ANISOU 1521  C   GLY A 105     7183   5400   6704  -1703   2342   -745
ATOM   1522  O   GLY A 105      49.250   6.535  33.433  1.00 52.04           O  
ANISOU 1522  O   GLY A 105     7333   5685   6757  -1725   2415   -679
ATOM   1523  H   GLY A 105      49.629   8.399  32.309  1.00 49.36           H  
ATOM   1524  HA3 GLY A 105      47.873   9.044  34.196  1.00 48.86           H  
ATOM   1525  HA2 GLY A 105      49.385   9.273  35.082  1.00 48.86           H  
ATOM   1526  N   LYS A 106      48.921   6.744  35.640  1.00 51.19           N  
ANISOU 1526  N   LYS A 106     7145   5494   6812  -1872   2340   -845
ATOM   1527  CA  LYS A 106      48.819   5.317  35.920  1.00 52.75           C  
ANISOU 1527  CA  LYS A 106     7166   5916   6960  -2087   2403   -898
ATOM   1528  C   LYS A 106      48.356   5.082  37.352  1.00 52.70           C  
ANISOU 1528  C   LYS A 106     7031   5965   7028  -2204   2338  -1029
ATOM   1529  O   LYS A 106      48.649   5.882  38.236  1.00 51.96           O  
ANISOU 1529  O   LYS A 106     7041   5697   7003  -2171   2279  -1064
ATOM   1530  CB  LYS A 106      50.123   4.550  35.606  1.00 54.70           C  
ANISOU 1530  CB  LYS A 106     7547   6099   7137  -2338   2557   -778
ATOM   1531  CG  LYS A 106      49.808   3.180  35.002  1.00 55.84           C  
ANISOU 1531  CG  LYS A 106     7528   6536   7151  -2368   2641   -733
ATOM   1532  CD  LYS A 106      51.056   2.392  34.656  1.00 60.93           C  
ANISOU 1532  CD  LYS A 106     8326   7114   7711  -2603   2795   -557
ATOM   1533  CE  LYS A 106      50.780   1.060  33.955  1.00 62.53           C  
ANISOU 1533  CE  LYS A 106     8292   7694   7772  -2734   2910   -525
ATOM   1534  NZ  LYS A 106      50.409   1.283  32.574  1.00 63.48           N1+
ANISOU 1534  NZ  LYS A 106     8364   8010   7747  -2479   2924   -491
ATOM   1535  H   LYS A 106      48.815   7.379  36.421  1.00 51.19           H  
ATOM   1536  HA  LYS A 106      48.027   4.954  35.263  1.00 52.75           H  
ATOM   1537  HB3 LYS A 106      50.740   4.439  36.501  1.00 54.70           H  
ATOM   1538  HB2 LYS A 106      50.747   5.092  34.898  1.00 54.70           H  
ATOM   1539  HG3 LYS A 106      49.214   3.321  34.100  1.00 55.84           H  
ATOM   1540  HG2 LYS A 106      49.212   2.592  35.698  1.00 55.84           H  
ATOM   1541  HD3 LYS A 106      51.551   2.176  35.599  1.00 60.93           H  
ATOM   1542  HD2 LYS A 106      51.722   3.005  34.050  1.00 60.93           H  
ATOM   1543  HE3 LYS A 106      49.987   0.515  34.466  1.00 62.53           H  
ATOM   1544  HE2 LYS A 106      51.670   0.429  33.977  1.00 62.53           H  
ATOM   1545  HZ1 LYS A 106      50.197   0.384  32.150  1.00 63.48           H  
ATOM   1546  HZ2 LYS A 106      51.198   1.657  32.069  1.00 63.48           H  
ATOM   1547  HZ3 LYS A 106      49.557   1.824  32.537  1.00  0.00           H  
ATOM   1548  N   GLY A 107      47.652   3.972  37.579  1.00 53.74           N  
ANISOU 1548  N   GLY A 107     6923   6367   7129  -2322   2347  -1103
ATOM   1549  CA  GLY A 107      47.184   3.552  38.886  1.00 53.43           C  
ANISOU 1549  CA  GLY A 107     6732   6424   7144  -2434   2271  -1225
ATOM   1550  C   GLY A 107      47.471   2.083  39.152  1.00 55.57           C  
ANISOU 1550  C   GLY A 107     6816   6932   7366  -2690   2350  -1249
ATOM   1551  O   GLY A 107      48.191   1.414  38.408  1.00 57.20           O  
ANISOU 1551  O   GLY A 107     7018   7224   7492  -2785   2476  -1157
ATOM   1552  H   GLY A 107      47.475   3.347  36.801  1.00 53.74           H  
ATOM   1553  HA3 GLY A 107      46.110   3.729  38.939  1.00 53.43           H  
ATOM   1554  HA2 GLY A 107      47.653   4.121  39.690  1.00 53.43           H  
ATOM   1555  N   GLY A 108      46.876   1.590  40.238  1.00 56.03           N  
ANISOU 1555  N   GLY A 108     6707   7120   7462  -2806   2274  -1360
ATOM   1556  CA  GLY A 108      46.917   0.195  40.613  1.00 58.28           C  
ANISOU 1556  CA  GLY A 108     6753   7683   7708  -3052   2328  -1392
ATOM   1557  C   GLY A 108      46.325  -0.037  41.993  1.00 58.51           C  
ANISOU 1557  C   GLY A 108     6613   7833   7786  -3128   2199  -1525
ATOM   1558  O   GLY A 108      45.911   0.900  42.671  1.00 57.24           O  
ANISOU 1558  O   GLY A 108     6556   7517   7677  -3017   2083  -1578
ATOM   1559  H   GLY A 108      46.326   2.209  40.818  1.00 56.03           H  
ATOM   1560  HA3 GLY A 108      47.943  -0.179  40.591  1.00 58.28           H  
ATOM   1561  HA2 GLY A 108      46.333  -0.366  39.885  1.00 58.28           H  
ATOM   1562  N   ILE A 109      46.287  -1.314  42.384  1.00 60.40           N  
ANISOU 1562  N   ILE A 109     6571   8381   7996  -3308   2218  -1569
ATOM   1563  CA  ILE A 109      45.901  -1.823  43.690  1.00 61.17           C  
ANISOU 1563  CA  ILE A 109     6491   8624   8126  -3432   2096  -1685
ATOM   1564  C   ILE A 109      46.904  -2.920  44.058  1.00 64.95           C  
ANISOU 1564  C   ILE A 109     6848   9253   8577  -3830   2192  -1658
ATOM   1565  O   ILE A 109      47.155  -3.811  43.245  1.00 66.75           O  
ANISOU 1565  O   ILE A 109     6886   9732   8744  -3887   2316  -1592
ATOM   1566  CB  ILE A 109      44.420  -2.307  43.723  1.00 60.79           C  
ANISOU 1566  CB  ILE A 109     6117   8901   8078  -3187   1976  -1780
ATOM   1567  CG1 ILE A 109      43.421  -1.255  43.191  1.00 56.59           C  
ANISOU 1567  CG1 ILE A 109     5682   8238   7582  -2805   1874  -1784
ATOM   1568  CG2 ILE A 109      44.014  -2.762  45.139  1.00 62.45           C  
ANISOU 1568  CG2 ILE A 109     6153   9264   8314  -3325   1836  -1886
ATOM   1569  CD1 ILE A 109      41.955  -1.709  43.189  1.00 54.39           C  
ANISOU 1569  CD1 ILE A 109     5126   8221   7319  -2559   1733  -1875
ATOM   1570  H   ILE A 109      46.629  -2.008  41.728  1.00 60.40           H  
ATOM   1571  HA  ILE A 109      46.021  -1.019  44.409  1.00 61.17           H  
ATOM   1572  HB  ILE A 109      44.345  -3.176  43.067  1.00 60.79           H  
ATOM   1573 HG13 ILE A 109      43.674  -0.995  42.164  1.00 56.59           H  
ATOM   1574 HG12 ILE A 109      43.520  -0.341  43.774  1.00 56.59           H  
ATOM   1575 HG21 ILE A 109      43.050  -3.258  45.121  1.00 62.45           H  
ATOM   1576 HG22 ILE A 109      44.709  -3.481  45.569  1.00 62.45           H  
ATOM   1577 HG23 ILE A 109      43.946  -1.918  45.825  1.00 62.45           H  
ATOM   1578 HD11 ILE A 109      41.352  -1.062  42.552  1.00 54.39           H  
ATOM   1579 HD12 ILE A 109      41.855  -2.725  42.810  1.00 54.39           H  
ATOM   1580 HD13 ILE A 109      41.530  -1.674  44.190  1.00 54.39           H  
ATOM   1581  N   CYS A 110      47.431  -2.885  45.294  1.00 66.10           N  
ANISOU 1581  N   CYS A 110     7105   9251   8759  -4111   2135  -1707
ATOM   1582  CA  CYS A 110      48.214  -3.969  45.884  1.00 68.99           C  
ANISOU 1582  CA  CYS A 110     7339   9754   9120  -4533   2180  -1695
ATOM   1583  C   CYS A 110      47.217  -5.052  46.331  1.00 70.29           C  
ANISOU 1583  C   CYS A 110     7061  10379   9267  -4527   2096  -1788
ATOM   1584  O   CYS A 110      46.608  -4.963  47.398  1.00 70.52           O  
ANISOU 1584  O   CYS A 110     7009  10466   9319  -4530   1932  -1912
ATOM   1585  CB  CYS A 110      49.024  -3.435  47.084  1.00 70.43           C  
ANISOU 1585  CB  CYS A 110     7793   9618   9349  -4806   2103  -1756
ATOM   1586  SG  CYS A 110      50.208  -4.689  47.653  1.00 71.88           S  
ANISOU 1586  SG  CYS A 110     7884   9876   9551  -5394   2140  -1721
ATOM   1587  H   CYS A 110      47.160  -2.125  45.905  1.00 66.10           H  
ATOM   1588  HA  CYS A 110      48.906  -4.368  45.145  1.00 68.99           H  
ATOM   1589  HB3 CYS A 110      48.383  -3.125  47.910  1.00 70.43           H  
ATOM   1590  HB2 CYS A 110      49.606  -2.564  46.796  1.00 70.43           H  
ATOM   1591  HG  CYS A 110      50.900  -4.764  46.513  1.00 71.88           H  
ATOM   1592  N   VAL A 111      47.031  -6.045  45.455  1.00 71.36           N  
ANISOU 1592  N   VAL A 111     6910  10858   9347  -4490   2209  -1729
ATOM   1593  CA  VAL A 111      46.089  -7.147  45.580  1.00 72.97           C  
ANISOU 1593  CA  VAL A 111     6655  11546   9523  -4438   2153  -1811
ATOM   1594  C   VAL A 111      46.613  -8.319  44.752  1.00 76.14           C  
ANISOU 1594  C   VAL A 111     6793  12289   9848  -4636   2341  -1705
ATOM   1595  O   VAL A 111      47.146  -8.107  43.666  1.00 76.35           O  
ANISOU 1595  O   VAL A 111     6994  12190   9825  -4673   2508  -1566
ATOM   1596  CB  VAL A 111      44.649  -6.696  45.191  1.00 70.73           C  
ANISOU 1596  CB  VAL A 111     6260  11380   9235  -3934   2057  -1895
ATOM   1597  CG1 VAL A 111      44.508  -6.250  43.719  1.00 68.56           C  
ANISOU 1597  CG1 VAL A 111     6129  11009   8911  -3675   2185  -1814
ATOM   1598  CG2 VAL A 111      43.599  -7.772  45.501  1.00 71.71           C  
ANISOU 1598  CG2 VAL A 111     5911  12002   9333  -3834   1989  -1990
ATOM   1599  H   VAL A 111      47.566  -6.018  44.597  1.00 71.36           H  
ATOM   1600  HA  VAL A 111      46.086  -7.461  46.626  1.00 72.97           H  
ATOM   1601  HB  VAL A 111      44.401  -5.839  45.816  1.00 70.73           H  
ATOM   1602 HG11 VAL A 111      43.514  -5.854  43.516  1.00 68.56           H  
ATOM   1603 HG12 VAL A 111      45.220  -5.469  43.467  1.00 68.56           H  
ATOM   1604 HG13 VAL A 111      44.668  -7.078  43.031  1.00 68.56           H  
ATOM   1605 HG21 VAL A 111      42.601  -7.346  45.460  1.00 71.71           H  
ATOM   1606 HG22 VAL A 111      43.630  -8.588  44.781  1.00 71.71           H  
ATOM   1607 HG23 VAL A 111      43.740  -8.198  46.492  1.00 71.71           H  
ATOM   1608  N   ASP A 112      46.388  -9.552  45.221  1.00 78.76           N  
ANISOU 1608  N   ASP A 112     6693  13073  10157  -4764   2317  -1758
ATOM   1609  CA  ASP A 112      46.404 -10.730  44.365  1.00 81.29           C  
ANISOU 1609  CA  ASP A 112     6667  13844  10376  -4816   2498  -1676
ATOM   1610  C   ASP A 112      44.924 -10.997  44.023  1.00 80.45           C  
ANISOU 1610  C   ASP A 112     6243  14103  10221  -4337   2443  -1806
ATOM   1611  O   ASP A 112      44.191 -11.463  44.893  1.00 81.80           O  
ANISOU 1611  O   ASP A 112     6055  14620  10407  -4303   2331  -1914
ATOM   1612  CB  ASP A 112      47.041 -11.911  45.138  1.00 85.61           C  
ANISOU 1612  CB  ASP A 112     6922  14679  10925  -5319   2531  -1625
ATOM   1613  CG  ASP A 112      47.111 -13.221  44.341  1.00 89.43           C  
ANISOU 1613  CG  ASP A 112     7012  15683  11286  -5410   2744  -1514
ATOM   1614  OD1 ASP A 112      47.013 -13.159  43.094  1.00 88.84           O  
ANISOU 1614  OD1 ASP A 112     6962  15692  11103  -5136   2897  -1455
ATOM   1615  OD2 ASP A 112      47.279 -14.269  44.999  1.00 93.77           O1-
ANISOU 1615  OD2 ASP A 112     7210  16585  11834  -5770   2756  -1485
ATOM   1616  H   ASP A 112      45.950  -9.655  46.126  1.00 78.76           H  
ATOM   1617  HA  ASP A 112      47.007 -10.561  43.473  1.00 81.29           H  
ATOM   1618  HB3 ASP A 112      46.503 -12.097  46.068  1.00 85.61           H  
ATOM   1619  HB2 ASP A 112      48.060 -11.650  45.423  1.00 85.61           H  
ATOM   1620  N   PRO A 113      44.441 -10.677  42.799  1.00 78.37           N  
ANISOU 1620  N   PRO A 113     6125  13749   9904  -3951   2503  -1804
ATOM   1621  CA  PRO A 113      43.022 -10.807  42.437  1.00 77.79           C  
ANISOU 1621  CA  PRO A 113     5824  13926   9806  -3461   2407  -1953
ATOM   1622  C   PRO A 113      42.572 -12.266  42.228  1.00 81.86           C  
ANISOU 1622  C   PRO A 113     5805  15065  10233  -3454   2477  -2004
ATOM   1623  O   PRO A 113      41.370 -12.515  42.147  1.00 82.20           O  
ANISOU 1623  O   PRO A 113     5596  15352  10285  -3099   2346  -2156
ATOM   1624  CB  PRO A 113      42.863  -9.967  41.164  1.00 75.28           C  
ANISOU 1624  CB  PRO A 113     5756  13427   9420  -3153   2498  -1918
ATOM   1625  CG  PRO A 113      44.235  -9.992  40.517  1.00 75.93           C  
ANISOU 1625  CG  PRO A 113     6055  13350   9444  -3498   2696  -1728
ATOM   1626  CD  PRO A 113      45.211 -10.126  41.685  1.00 76.79           C  
ANISOU 1626  CD  PRO A 113     6290  13229   9658  -3940   2645  -1669
ATOM   1627  HA  PRO A 113      42.396 -10.380  43.224  1.00 77.79           H  
ATOM   1628  HB3 PRO A 113      42.620  -8.941  41.443  1.00 75.28           H  
ATOM   1629  HB2 PRO A 113      42.075 -10.316  40.495  1.00 75.28           H  
ATOM   1630  HG3 PRO A 113      44.420  -9.097  39.931  1.00 75.93           H  
ATOM   1631  HG2 PRO A 113      44.319 -10.858  39.860  1.00 75.93           H  
ATOM   1632  HD2 PRO A 113      46.059 -10.757  41.416  1.00 76.79           H  
ATOM   1633  HD3 PRO A 113      45.583  -9.143  41.964  1.00 76.79           H  
ATOM   1634  N   ALA A 114      43.515 -13.227  42.223  1.00 85.35           N  
ANISOU 1634  N   ALA A 114     6072  15762  10593  -3847   2675  -1870
ATOM   1635  CA  ALA A 114      43.258 -14.664  42.279  1.00 90.18           C  
ANISOU 1635  CA  ALA A 114     6134  17013  11119  -3913   2757  -1896
ATOM   1636  C   ALA A 114      42.747 -15.108  43.663  1.00 91.47           C  
ANISOU 1636  C   ALA A 114     6010  17359  11385  -3940   2535  -2028
ATOM   1637  O   ALA A 114      42.023 -16.099  43.746  1.00 93.86           O  
ANISOU 1637  O   ALA A 114     5888  18130  11645  -3673   2492  -2148
ATOM   1638  CB  ALA A 114      44.572 -15.402  41.978  1.00 93.56           C  
ANISOU 1638  CB  ALA A 114     6445  17642  11461  -4430   2992  -1686
ATOM   1639  H   ALA A 114      44.483 -12.942  42.291  1.00 85.35           H  
ATOM   1640  HA  ALA A 114      42.514 -14.922  41.522  1.00 90.18           H  
ATOM   1641  HB1 ALA A 114      44.418 -16.481  41.942  1.00 93.56           H  
ATOM   1642  HB2 ALA A 114      44.980 -15.099  41.013  1.00 93.56           H  
ATOM   1643  HB3 ALA A 114      45.331 -15.204  42.736  1.00 93.56           H  
ATOM   1644  N   GLU A 115      43.086 -14.360  44.732  1.00 90.15           N  
ANISOU 1644  N   GLU A 115     6081  16832  11341  -4236   2385  -2016
ATOM   1645  CA  GLU A 115      42.603 -14.542  46.104  1.00 90.67           C  
ANISOU 1645  CA  GLU A 115     5937  17021  11492  -4262   2148  -2140
ATOM   1646  C   GLU A 115      41.126 -14.118  46.276  1.00 88.00           C  
ANISOU 1646  C   GLU A 115     5614  16621  11199  -3707   1930  -2301
ATOM   1647  O   GLU A 115      40.495 -14.559  47.235  1.00 89.15           O  
ANISOU 1647  O   GLU A 115     5531  16951  11392  -3648   1729  -2400
ATOM   1648  CB  GLU A 115      43.566 -13.776  47.071  1.00 90.15           C  
ANISOU 1648  CB  GLU A 115     6173  16561  11521  -4710   2042  -2100
ATOM   1649  CG  GLU A 115      43.033 -12.511  47.797  1.00 86.14           C  
ANISOU 1649  CG  GLU A 115     6190  15452  11087  -4522   1908  -2138
ATOM   1650  CD  GLU A 115      44.078 -11.832  48.686  1.00 86.70           C  
ANISOU 1650  CD  GLU A 115     6543  15171  11227  -4920   1795  -2139
ATOM   1651  OE1 GLU A 115      44.578 -12.509  49.611  1.00 90.05           O  
ANISOU 1651  OE1 GLU A 115     6724  15827  11665  -5278   1719  -2166
ATOM   1652  OE2 GLU A 115      44.325 -10.624  48.473  1.00 80.14           O1-
ANISOU 1652  OE2 GLU A 115     6174  13846  10432  -4863   1775  -2123
ATOM   1653  H   GLU A 115      43.683 -13.562  44.573  1.00 90.15           H  
ATOM   1654  HA  GLU A 115      42.668 -15.607  46.334  1.00 90.67           H  
ATOM   1655  HB3 GLU A 115      44.498 -13.533  46.560  1.00 90.15           H  
ATOM   1656  HB2 GLU A 115      43.868 -14.484  47.844  1.00 90.15           H  
ATOM   1657  HG3 GLU A 115      42.185 -12.759  48.436  1.00 86.14           H  
ATOM   1658  HG2 GLU A 115      42.675 -11.786  47.067  1.00 86.14           H  
ATOM   1659  N   LEU A 116      40.582 -13.271  45.383  1.00 84.63           N  
ANISOU 1659  N   LEU A 116     5456  15938  10760  -3315   1952  -2318
ATOM   1660  CA  LEU A 116      39.246 -12.688  45.509  1.00 82.02           C  
ANISOU 1660  CA  LEU A 116     5211  15454  10497  -2840   1724  -2442
ATOM   1661  C   LEU A 116      38.198 -13.421  44.663  1.00 83.12           C  
ANISOU 1661  C   LEU A 116     5059  15934  10588  -2336   1695  -2567
ATOM   1662  O   LEU A 116      38.473 -13.884  43.556  1.00 84.20           O  
ANISOU 1662  O   LEU A 116     5104  16270  10618  -2205   1884  -2564
ATOM   1663  CB  LEU A 116      39.281 -11.221  45.019  1.00 77.82           C  
ANISOU 1663  CB  LEU A 116     5210  14336  10024  -2731   1684  -2394
ATOM   1664  CG  LEU A 116      40.117 -10.269  45.896  1.00 76.14           C  
ANISOU 1664  CG  LEU A 116     5312  13734   9882  -3061   1602  -2336
ATOM   1665  CD1 LEU A 116      40.036  -8.839  45.360  1.00 71.78           C  
ANISOU 1665  CD1 LEU A 116     5235  12672   9365  -2946   1615  -2274
ATOM   1666  CD2 LEU A 116      39.695 -10.295  47.372  1.00 76.09           C  
ANISOU 1666  CD2 LEU A 116     5196  13780   9935  -3012   1346  -2421
ATOM   1667  H   LEU A 116      41.140 -12.982  44.593  1.00 84.63           H  
ATOM   1668  HA  LEU A 116      38.914 -12.722  46.546  1.00 82.02           H  
ATOM   1669  HB3 LEU A 116      38.263 -10.828  44.978  1.00 77.82           H  
ATOM   1670  HB2 LEU A 116      39.650 -11.183  43.993  1.00 77.82           H  
ATOM   1671  HG  LEU A 116      41.162 -10.574  45.840  1.00 76.14           H  
ATOM   1672 HD11 LEU A 116      40.596  -8.172  46.010  1.00 71.78           H  
ATOM   1673 HD12 LEU A 116      40.452  -8.762  44.356  1.00 71.78           H  
ATOM   1674 HD13 LEU A 116      39.005  -8.480  45.329  1.00 71.78           H  
ATOM   1675 HD21 LEU A 116      40.216  -9.526  47.938  1.00 76.09           H  
ATOM   1676 HD22 LEU A 116      38.625 -10.124  47.489  1.00 76.09           H  
ATOM   1677 HD23 LEU A 116      39.943 -11.247  47.841  1.00 76.09           H  
ATOM   1678  N   SER A 117      36.964 -13.424  45.191  1.00 83.02           N  
ANISOU 1678  N   SER A 117     4923  15973  10648  -2039   1446  -2679
ATOM   1679  CA  SER A 117      35.711 -13.721  44.494  1.00 83.89           C  
ANISOU 1679  CA  SER A 117     4858  16266  10749  -1489   1345  -2819
ATOM   1680  C   SER A 117      35.383 -12.574  43.516  1.00 81.18           C  
ANISOU 1680  C   SER A 117     4937  15473  10434  -1193   1324  -2822
ATOM   1681  O   SER A 117      35.839 -11.449  43.704  1.00 78.25           O  
ANISOU 1681  O   SER A 117     4972  14639  10123  -1367   1308  -2722
ATOM   1682  CB  SER A 117      34.613 -13.836  45.574  1.00 84.38           C  
ANISOU 1682  CB  SER A 117     4773  16382  10905  -1289   1045  -2900
ATOM   1683  OG  SER A 117      33.321 -14.079  45.053  1.00 84.47           O  
ANISOU 1683  OG  SER A 117     4746  16400  10948   -728    888  -3027
ATOM   1684  H   SER A 117      36.867 -13.026  46.118  1.00 83.02           H  
ATOM   1685  HA  SER A 117      35.807 -14.661  43.948  1.00 83.89           H  
ATOM   1686  HB3 SER A 117      34.556 -12.914  46.147  1.00 84.38           H  
ATOM   1687  HB2 SER A 117      34.857 -14.629  46.281  1.00 84.38           H  
ATOM   1688  HG  SER A 117      32.722 -14.097  45.791  1.00 84.47           H  
ATOM   1689  N   GLU A 118      34.589 -12.849  42.471  1.00 82.19           N  
ANISOU 1689  N   GLU A 118     4974  15735  10521   -735   1311  -2948
ATOM   1690  CA  GLU A 118      34.246 -11.885  41.419  1.00 79.19           C  
ANISOU 1690  CA  GLU A 118     4983  14942  10165   -476   1278  -2959
ATOM   1691  C   GLU A 118      33.320 -10.746  41.901  1.00 76.78           C  
ANISOU 1691  C   GLU A 118     4971  14182  10020   -263    981  -2965
ATOM   1692  O   GLU A 118      33.323  -9.688  41.273  1.00 74.49           O  
ANISOU 1692  O   GLU A 118     5053  13476   9774   -177    948  -2924
ATOM   1693  CB  GLU A 118      33.581 -12.653  40.258  1.00 81.03           C  
ANISOU 1693  CB  GLU A 118     5082  15435  10271   -102   1389  -3093
ATOM   1694  CG  GLU A 118      34.594 -13.387  39.352  1.00 82.60           C  
ANISOU 1694  CG  GLU A 118     5201  15887  10294   -390   1725  -3002
ATOM   1695  CD  GLU A 118      35.096 -12.520  38.195  1.00 82.73           C  
ANISOU 1695  CD  GLU A 118     5516  15696  10222   -208   1825  -3011
ATOM   1696  OE1 GLU A 118      34.509 -12.650  37.099  1.00 86.47           O  
ANISOU 1696  OE1 GLU A 118     5898  16343  10613    232   1799  -3183
ATOM   1697  OE2 GLU A 118      36.049 -11.744  38.419  1.00 80.05           O1-
ANISOU 1697  OE2 GLU A 118     5505  15025   9885   -491   1922  -2855
ATOM   1698  H   GLU A 118      34.228 -13.787  42.376  1.00 82.19           H  
ATOM   1699  HA  GLU A 118      35.165 -11.421  41.058  1.00 79.19           H  
ATOM   1700  HB3 GLU A 118      32.988 -11.973  39.641  1.00 81.03           H  
ATOM   1701  HB2 GLU A 118      32.862 -13.370  40.656  1.00 81.03           H  
ATOM   1702  HG3 GLU A 118      34.110 -14.264  38.919  1.00 82.60           H  
ATOM   1703  HG2 GLU A 118      35.440 -13.766  39.927  1.00 82.60           H  
ATOM   1704  N   ARG A 119      32.582 -10.913  43.018  1.00 77.55           N  
ANISOU 1704  N   ARG A 119     4911  14353  10201   -194    761  -2994
ATOM   1705  CA  ARG A 119      31.805  -9.828  43.633  1.00 75.06           C  
ANISOU 1705  CA  ARG A 119     4907  13589  10024   -102    504  -2936
ATOM   1706  C   ARG A 119      32.670  -9.006  44.612  1.00 72.46           C  
ANISOU 1706  C   ARG A 119     4810  13012   9710   -555    560  -2778
ATOM   1707  O   ARG A 119      32.393  -7.821  44.796  1.00 69.57           O  
ANISOU 1707  O   ARG A 119     4795  12225   9413   -566    475  -2690
ATOM   1708  CB  ARG A 119      30.545 -10.394  44.336  1.00 76.80           C  
ANISOU 1708  CB  ARG A 119     4941  13914  10327    196    212  -3006
ATOM   1709  CG  ARG A 119      30.686 -10.931  45.778  1.00 79.33           C  
ANISOU 1709  CG  ARG A 119     4999  14510  10633    -64    156  -2971
ATOM   1710  CD  ARG A 119      29.356 -11.459  46.339  1.00 84.74           C  
ANISOU 1710  CD  ARG A 119     5498  15309  11391    273   -152  -3032
ATOM   1711  NE  ARG A 119      28.343 -10.395  46.436  1.00 84.81           N  
ANISOU 1711  NE  ARG A 119     5828  14875  11520    579   -404  -2995
ATOM   1712  CZ  ARG A 119      27.086 -10.544  46.881  1.00 86.76           C  
ANISOU 1712  CZ  ARG A 119     5993  15122  11849    943   -697  -3034
ATOM   1713  NH1 ARG A 119      26.650 -11.722  47.349  1.00 87.13           N  
ANISOU 1713  NH1 ARG A 119     5628  15612  11868   1085   -781  -3127
ATOM   1714  NH2 ARG A 119      26.249  -9.498  46.853  1.00 84.44           N1+
ANISOU 1714  NH2 ARG A 119     6031  14380  11672   1160   -917  -2966
ATOM   1715  H   ARG A 119      32.619 -11.802  43.497  1.00 77.55           H  
ATOM   1716  HA  ARG A 119      31.453  -9.156  42.848  1.00 75.06           H  
ATOM   1717  HB3 ARG A 119      30.104 -11.167  43.706  1.00 76.80           H  
ATOM   1718  HB2 ARG A 119      29.808  -9.590  44.349  1.00 76.80           H  
ATOM   1719  HG3 ARG A 119      31.058 -10.157  46.452  1.00 79.33           H  
ATOM   1720  HG2 ARG A 119      31.427 -11.730  45.793  1.00 79.33           H  
ATOM   1721  HD3 ARG A 119      29.507 -11.886  47.331  1.00 84.74           H  
ATOM   1722  HD2 ARG A 119      28.973 -12.260  45.705  1.00 84.74           H  
ATOM   1723  HE  ARG A 119      28.638  -9.485  46.115  1.00 84.81           H  
ATOM   1724 HH12 ARG A 119      25.704 -11.829  47.683  1.00 87.13           H  
ATOM   1725 HH11 ARG A 119      27.282 -12.509  47.383  1.00 87.13           H  
ATOM   1726 HH22 ARG A 119      25.300  -9.592  47.183  1.00 84.44           H  
ATOM   1727 HH21 ARG A 119      26.560  -8.605  46.500  1.00 84.44           H  
ATOM   1728  N   GLU A 120      33.735  -9.596  45.193  1.00 70.12           N  
ANISOU 1728  N   GLU A 120     4110  13971   8562  -2478    638  -1781
ATOM   1729  CA  GLU A 120      34.732  -8.893  46.011  1.00 69.31           C  
ANISOU 1729  CA  GLU A 120     4288  13673   8373  -2908    671  -1810
ATOM   1730  C   GLU A 120      35.670  -8.074  45.112  1.00 66.56           C  
ANISOU 1730  C   GLU A 120     4340  12854   8095  -2938    821  -1864
ATOM   1731  O   GLU A 120      36.072  -6.980  45.501  1.00 64.59           O  
ANISOU 1731  O   GLU A 120     4414  12238   7889  -2994    813  -1875
ATOM   1732  CB  GLU A 120      35.605  -9.908  46.779  1.00 72.33           C  
ANISOU 1732  CB  GLU A 120     4463  14456   8565  -3362    711  -1819
ATOM   1733  CG  GLU A 120      34.851 -10.680  47.875  1.00 75.40           C  
ANISOU 1733  CG  GLU A 120     4555  15242   8854  -3466    529  -1753
ATOM   1734  CD  GLU A 120      35.674 -11.798  48.525  1.00 78.69           C  
ANISOU 1734  CD  GLU A 120     4655  16167   9079  -3855    549  -1741
ATOM   1735  OE1 GLU A 120      36.691 -12.214  47.927  1.00 79.48           O  
ANISOU 1735  OE1 GLU A 120     4808  16282   9108  -4109    710  -1792
ATOM   1736  OE2 GLU A 120      35.256 -12.242  49.615  1.00 81.16           O1-
ANISOU 1736  OE2 GLU A 120     4659  16877   9302  -3920    396  -1670
ATOM   1737  H   GLU A 120      33.910 -10.570  44.995  1.00 70.12           H  
ATOM   1738  HA  GLU A 120      34.236  -8.227  46.717  1.00 69.31           H  
ATOM   1739  HB3 GLU A 120      36.432  -9.382  47.257  1.00 72.33           H  
ATOM   1740  HB2 GLU A 120      36.062 -10.605  46.078  1.00 72.33           H  
ATOM   1741  HG3 GLU A 120      33.959 -11.133  47.448  1.00 75.40           H  
ATOM   1742  HG2 GLU A 120      34.507  -9.988  48.642  1.00 75.40           H  
ATOM   1743  N   LEU A 121      35.979  -8.583  43.906  1.00 66.83           N  
ANISOU 1743  N   LEU A 121     4337  12920   8138  -2884    958  -1891
ATOM   1744  CA  LEU A 121      36.782  -7.930  42.877  1.00 64.29           C  
ANISOU 1744  CA  LEU A 121     4355  12193   7880  -2881   1094  -1922
ATOM   1745  C   LEU A 121      36.020  -6.749  42.253  1.00 61.43           C  
ANISOU 1745  C   LEU A 121     4226  11435   7679  -2527   1034  -1904
ATOM   1746  O   LEU A 121      36.642  -5.728  41.963  1.00 59.50           O  
ANISOU 1746  O   LEU A 121     4316  10809   7483  -2596   1092  -1908
ATOM   1747  CB  LEU A 121      37.129  -8.969  41.787  1.00 65.25           C  
ANISOU 1747  CB  LEU A 121     4337  12484   7969  -2839   1229  -1942
ATOM   1748  CG  LEU A 121      38.196  -8.520  40.762  1.00 63.88           C  
ANISOU 1748  CG  LEU A 121     4485  11981   7804  -2977   1383  -1956
ATOM   1749  CD1 LEU A 121      39.592  -8.410  41.396  1.00 66.04           C  
ANISOU 1749  CD1 LEU A 121     4921  12208   7962  -3467   1452  -1964
ATOM   1750  CD2 LEU A 121      38.231  -9.476  39.562  1.00 63.79           C  
ANISOU 1750  CD2 LEU A 121     4332  12142   7764  -2866   1500  -1971
ATOM   1751  H   LEU A 121      35.636  -9.511  43.691  1.00 66.83           H  
ATOM   1752  HA  LEU A 121      37.693  -7.561  43.350  1.00 64.29           H  
ATOM   1753  HB3 LEU A 121      36.215  -9.246  41.257  1.00 65.25           H  
ATOM   1754  HB2 LEU A 121      37.481  -9.887  42.261  1.00 65.25           H  
ATOM   1755  HG  LEU A 121      37.929  -7.539  40.368  1.00 63.88           H  
ATOM   1756 HD11 LEU A 121      40.337  -8.138  40.649  1.00 66.04           H  
ATOM   1757 HD12 LEU A 121      39.626  -7.646  42.170  1.00 66.04           H  
ATOM   1758 HD13 LEU A 121      39.901  -9.355  41.844  1.00 66.04           H  
ATOM   1759 HD21 LEU A 121      38.992  -9.181  38.841  1.00 63.79           H  
ATOM   1760 HD22 LEU A 121      38.448 -10.498  39.876  1.00 63.79           H  
ATOM   1761 HD23 LEU A 121      37.273  -9.483  39.040  1.00 63.79           H  
ATOM   1762  N   GLU A 122      34.685  -6.856  42.100  1.00 61.29           N  
ANISOU 1762  N   GLU A 122     4034  11509   7742  -2148    920  -1877
ATOM   1763  CA  GLU A 122      33.813  -5.759  41.682  1.00 58.63           C  
ANISOU 1763  CA  GLU A 122     3916  10814   7548  -1831    845  -1852
ATOM   1764  C   GLU A 122      33.741  -4.663  42.754  1.00 57.25           C  
ANISOU 1764  C   GLU A 122     3932  10440   7381  -1961    752  -1821
ATOM   1765  O   GLU A 122      33.869  -3.491  42.420  1.00 54.95           O  
ANISOU 1765  O   GLU A 122     3939   9781   7158  -1938    777  -1813
ATOM   1766  CB  GLU A 122      32.401  -6.287  41.342  1.00 59.37           C  
ANISOU 1766  CB  GLU A 122     3799  11043   7718  -1413    735  -1831
ATOM   1767  CG  GLU A 122      31.375  -5.173  41.015  1.00 57.14           C  
ANISOU 1767  CG  GLU A 122     3750  10390   7570  -1104    645  -1799
ATOM   1768  CD  GLU A 122      30.033  -5.662  40.472  1.00 58.48           C  
ANISOU 1768  CD  GLU A 122     3755  10647   7816   -691    533  -1782
ATOM   1769  OE1 GLU A 122      29.871  -6.886  40.280  1.00 62.38           O  
ANISOU 1769  OE1 GLU A 122     3966  11461   8274   -580    571  -1814
ATOM   1770  OE2 GLU A 122      29.176  -4.778  40.255  1.00 56.30           O1-
ANISOU 1770  OE2 GLU A 122     3638  10119   7634   -472    410  -1736
ATOM   1771  H   GLU A 122      34.245  -7.735  42.331  1.00 61.29           H  
ATOM   1772  HA  GLU A 122      34.233  -5.310  40.782  1.00 58.63           H  
ATOM   1773  HB3 GLU A 122      32.021  -6.880  42.176  1.00 59.37           H  
ATOM   1774  HB2 GLU A 122      32.483  -6.976  40.503  1.00 59.37           H  
ATOM   1775  HG3 GLU A 122      31.800  -4.491  40.280  1.00 57.14           H  
ATOM   1776  HG2 GLU A 122      31.160  -4.583  41.906  1.00 57.14           H  
ATOM   1777  N   GLN A 123      33.569  -5.037  44.033  1.00 59.01           N  
ANISOU 1777  N   GLN A 123     3970  10933   7520  -2112    650  -1801
ATOM   1778  CA  GLN A 123      33.473  -4.108  45.159  1.00 58.61           C  
ANISOU 1778  CA  GLN A 123     4067  10755   7448  -2244    555  -1776
ATOM   1779  C   GLN A 123      34.800  -3.373  45.432  1.00 57.57           C  
ANISOU 1779  C   GLN A 123     4266  10329   7279  -2549    685  -1829
ATOM   1780  O   GLN A 123      34.778  -2.222  45.864  1.00 55.57           O  
ANISOU 1780  O   GLN A 123     4261   9780   7073  -2520    664  -1819
ATOM   1781  CB  GLN A 123      33.017  -4.895  46.400  1.00 60.71           C  
ANISOU 1781  CB  GLN A 123     4050  11417   7598  -2390    425  -1743
ATOM   1782  CG  GLN A 123      32.610  -3.995  47.587  1.00 61.64           C  
ANISOU 1782  CG  GLN A 123     4246  11448   7727  -2334    262  -1684
ATOM   1783  CD  GLN A 123      32.072  -4.747  48.806  1.00 65.83           C  
ANISOU 1783  CD  GLN A 123     4507  12374   8131  -2491    114  -1633
ATOM   1784  OE1 GLN A 123      31.588  -4.116  49.741  1.00 66.44           O  
ANISOU 1784  OE1 GLN A 123     4617  12431   8197  -2455    -33  -1571
ATOM   1785  NE2 GLN A 123      32.146  -6.079  48.817  1.00 68.22           N  
ANISOU 1785  NE2 GLN A 123     4538  13056   8326  -2685    147  -1649
ATOM   1786  H   GLN A 123      33.466  -6.023  44.234  1.00 59.01           H  
ATOM   1787  HA  GLN A 123      32.711  -3.364  44.914  1.00 58.61           H  
ATOM   1788  HB3 GLN A 123      33.799  -5.595  46.698  1.00 60.71           H  
ATOM   1789  HB2 GLN A 123      32.153  -5.501  46.121  1.00 60.71           H  
ATOM   1790  HG3 GLN A 123      31.849  -3.283  47.264  1.00 61.64           H  
ATOM   1791  HG2 GLN A 123      33.464  -3.408  47.927  1.00 61.64           H  
ATOM   1792 HE22 GLN A 123      31.834  -6.598  49.627  1.00 68.22           H  
ATOM   1793 HE21 GLN A 123      32.541  -6.570  48.030  1.00 68.22           H  
ATOM   1794  N   LEU A 124      35.939  -4.012  45.119  1.00 58.80           N  
ANISOU 1794  N   LEU A 124     4422  10572   7349  -2830    823  -1880
ATOM   1795  CA  LEU A 124      37.275  -3.424  45.138  1.00 58.42           C  
ANISOU 1795  CA  LEU A 124     4697  10220   7279  -3085    972  -1928
ATOM   1796  C   LEU A 124      37.465  -2.439  43.970  1.00 56.22           C  
ANISOU 1796  C   LEU A 124     4677   9540   7142  -2842   1043  -1908
ATOM   1797  O   LEU A 124      38.078  -1.391  44.163  1.00 55.49           O  
ANISOU 1797  O   LEU A 124     4861   9131   7091  -2870   1078  -1912
ATOM   1798  CB  LEU A 124      38.306  -4.572  45.023  1.00 60.58           C  
ANISOU 1798  CB  LEU A 124     4897  10681   7440  -3398   1093  -1966
ATOM   1799  CG  LEU A 124      39.790  -4.147  45.020  1.00 61.07           C  
ANISOU 1799  CG  LEU A 124     5285  10463   7455  -3720   1250  -2013
ATOM   1800  CD1 LEU A 124      40.173  -3.385  46.297  1.00 61.47           C  
ANISOU 1800  CD1 LEU A 124     5522  10404   7429  -3975   1229  -2062
ATOM   1801  CD2 LEU A 124      40.698  -5.364  44.838  1.00 61.92           C  
ANISOU 1801  CD2 LEU A 124     5282  10801   7444  -4020   1350  -2029
ATOM   1802  H   LEU A 124      35.870  -4.970  44.805  1.00 58.80           H  
ATOM   1803  HA  LEU A 124      37.410  -2.893  46.081  1.00 58.42           H  
ATOM   1804  HB3 LEU A 124      38.108  -5.142  44.116  1.00 60.58           H  
ATOM   1805  HB2 LEU A 124      38.149  -5.273  45.843  1.00 60.58           H  
ATOM   1806  HG  LEU A 124      39.967  -3.499  44.164  1.00 61.07           H  
ATOM   1807 HD11 LEU A 124      41.235  -3.158  46.323  1.00 61.47           H  
ATOM   1808 HD12 LEU A 124      39.652  -2.435  46.363  1.00 61.47           H  
ATOM   1809 HD13 LEU A 124      39.937  -3.962  47.189  1.00 61.47           H  
ATOM   1810 HD21 LEU A 124      41.736  -5.064  44.724  1.00 61.92           H  
ATOM   1811 HD22 LEU A 124      40.638  -6.006  45.714  1.00 61.92           H  
ATOM   1812 HD23 LEU A 124      40.421  -5.948  43.960  1.00 61.92           H  
ATOM   1813  N   SER A 125      36.929  -2.764  42.779  1.00 55.71           N  
ANISOU 1813  N   SER A 125     4515   9507   7145  -2604   1065  -1885
ATOM   1814  CA  SER A 125      37.035  -1.945  41.573  1.00 53.50           C  
ANISOU 1814  CA  SER A 125     4452   8892   6982  -2385   1116  -1854
ATOM   1815  C   SER A 125      36.161  -0.684  41.679  1.00 51.95           C  
ANISOU 1815  C   SER A 125     4375   8478   6887  -2148   1004  -1810
ATOM   1816  O   SER A 125      36.621   0.414  41.375  1.00 50.99           O  
ANISOU 1816  O   SER A 125     4506   8038   6830  -2114   1051  -1785
ATOM   1817  CB  SER A 125      36.590  -2.762  40.342  1.00 53.53           C  
ANISOU 1817  CB  SER A 125     4308   9020   7013  -2177   1144  -1850
ATOM   1818  OG  SER A 125      37.541  -3.762  40.050  1.00 55.46           O  
ANISOU 1818  OG  SER A 125     4462   9454   7156  -2415   1265  -1881
ATOM   1819  H   SER A 125      36.437  -3.642  42.699  1.00 55.71           H  
ATOM   1820  HA  SER A 125      38.078  -1.647  41.462  1.00 53.50           H  
ATOM   1821  HB3 SER A 125      36.510  -2.123  39.462  1.00 53.53           H  
ATOM   1822  HB2 SER A 125      35.613  -3.221  40.485  1.00 53.53           H  
ATOM   1823  HG  SER A 125      37.512  -4.410  40.742  1.00 55.46           H  
ATOM   1824  N   ARG A 126      34.927  -0.829  42.187  1.00 52.17           N  
ANISOU 1824  N   ARG A 126     4213   8685   6923  -1982    851  -1787
ATOM   1825  CA  ARG A 126      34.021   0.269  42.515  1.00 50.15           C  
ANISOU 1825  CA  ARG A 126     4063   8248   6743  -1793    731  -1733
ATOM   1826  C   ARG A 126      34.580   1.130  43.659  1.00 49.98           C  
ANISOU 1826  C   ARG A 126     4215   8102   6672  -2028    754  -1747
ATOM   1827  O   ARG A 126      34.512   2.352  43.582  1.00 48.75           O  
ANISOU 1827  O   ARG A 126     4261   7685   6577  -1952    753  -1714
ATOM   1828  CB  ARG A 126      32.656  -0.309  42.927  1.00 50.99           C  
ANISOU 1828  CB  ARG A 126     3933   8584   6857  -1593    557  -1696
ATOM   1829  CG  ARG A 126      31.892  -0.955  41.763  1.00 50.47           C  
ANISOU 1829  CG  ARG A 126     3743   8577   6856  -1298    539  -1692
ATOM   1830  CD  ARG A 126      30.496  -1.419  42.185  1.00 51.80           C  
ANISOU 1830  CD  ARG A 126     3714   8915   7051  -1055    364  -1645
ATOM   1831  NE  ARG A 126      29.795  -2.049  41.062  1.00 51.71           N  
ANISOU 1831  NE  ARG A 126     3595   8955   7098   -755    363  -1663
ATOM   1832  CZ  ARG A 126      29.092  -1.418  40.111  1.00 51.81           C  
ANISOU 1832  CZ  ARG A 126     3776   8708   7201   -509    338  -1650
ATOM   1833  NH1 ARG A 126      28.952  -0.086  40.095  1.00 51.55           N  
ANISOU 1833  NH1 ARG A 126     4006   8362   7219   -522    303  -1602
ATOM   1834  NH2 ARG A 126      28.511  -2.145  39.153  1.00 51.96           N1+
ANISOU 1834  NH2 ARG A 126     3699   8791   7251   -253    350  -1689
ATOM   1835  H   ARG A 126      34.612  -1.765  42.407  1.00 52.17           H  
ATOM   1836  HA  ARG A 126      33.895   0.904  41.635  1.00 50.15           H  
ATOM   1837  HB3 ARG A 126      32.039   0.484  43.347  1.00 50.99           H  
ATOM   1838  HB2 ARG A 126      32.787  -1.039  43.728  1.00 50.99           H  
ATOM   1839  HG3 ARG A 126      32.447  -1.793  41.346  1.00 50.47           H  
ATOM   1840  HG2 ARG A 126      31.806  -0.244  40.944  1.00 50.47           H  
ATOM   1841  HD3 ARG A 126      29.906  -0.590  42.576  1.00 51.80           H  
ATOM   1842  HD2 ARG A 126      30.580  -2.153  42.987  1.00 51.80           H  
ATOM   1843  HE  ARG A 126      29.843  -3.061  41.001  1.00 51.71           H  
ATOM   1844 HH12 ARG A 126      28.385   0.335  39.363  1.00 51.55           H  
ATOM   1845 HH11 ARG A 126      29.358   0.490  40.817  1.00 51.55           H  
ATOM   1846 HH22 ARG A 126      27.956  -1.681  38.440  1.00 51.96           H  
ATOM   1847 HH21 ARG A 126      28.586  -3.157  39.177  1.00 51.96           H  
ATOM   1848  N   GLY A 127      35.189   0.493  44.674  1.00 51.62           N  
ANISOU 1848  N   GLY A 127     4348   8507   6759  -2323    785  -1800
ATOM   1849  CA  GLY A 127      35.822   1.132  45.823  1.00 52.00           C  
ANISOU 1849  CA  GLY A 127     4556   8471   6730  -2568    805  -1837
ATOM   1850  C   GLY A 127      37.072   1.956  45.487  1.00 51.14           C  
ANISOU 1850  C   GLY A 127     4754   8027   6651  -2675    976  -1874
ATOM   1851  O   GLY A 127      37.365   2.917  46.196  1.00 50.87           O  
ANISOU 1851  O   GLY A 127     4917   7806   6603  -2747   1008  -1895
ATOM   1852  H   GLY A 127      35.204  -0.517  44.657  1.00 51.62           H  
ATOM   1853  HA3 GLY A 127      36.100   0.342  46.520  1.00 52.00           H  
ATOM   1854  HA2 GLY A 127      35.099   1.758  46.340  1.00 52.00           H  
ATOM   1855  N   TRP A 128      37.777   1.615  44.393  1.00 50.87           N  
ANISOU 1855  N   TRP A 128     4757   7923   6650  -2680   1090  -1878
ATOM   1856  CA  TRP A 128      38.920   2.358  43.868  1.00 50.09           C  
ANISOU 1856  CA  TRP A 128     4942   7488   6602  -2723   1242  -1882
ATOM   1857  C   TRP A 128      38.460   3.672  43.212  1.00 47.67           C  
ANISOU 1857  C   TRP A 128     4769   6923   6420  -2445   1215  -1812
ATOM   1858  O   TRP A 128      39.068   4.708  43.468  1.00 47.43           O  
ANISOU 1858  O   TRP A 128     4948   6670   6404  -2486   1283  -1823
ATOM   1859  CB  TRP A 128      39.666   1.477  42.845  1.00 50.47           C  
ANISOU 1859  CB  TRP A 128     4984   7538   6655  -2772   1346  -1875
ATOM   1860  CG  TRP A 128      40.908   2.056  42.228  1.00 50.11           C  
ANISOU 1860  CG  TRP A 128     5234   7152   6655  -2837   1500  -1862
ATOM   1861  CD1 TRP A 128      42.153   2.011  42.756  1.00 51.52           C  
ANISOU 1861  CD1 TRP A 128     5619   7187   6769  -3119   1622  -1918
ATOM   1862  CD2 TRP A 128      41.044   2.770  40.963  1.00 46.86           C  
ANISOU 1862  CD2 TRP A 128     4946   6501   6357  -2616   1542  -1780
ATOM   1863  NE1 TRP A 128      43.045   2.627  41.906  1.00 50.66           N  
ANISOU 1863  NE1 TRP A 128     5755   6753   6742  -3059   1739  -1869
ATOM   1864  CE2 TRP A 128      42.416   3.121  40.784  1.00 47.67           C  
ANISOU 1864  CE2 TRP A 128     5315   6328   6468  -2759   1689  -1778
ATOM   1865  CE3 TRP A 128      40.140   3.179  39.956  1.00 45.52           C  
ANISOU 1865  CE3 TRP A 128     4700   6321   6276  -2321   1464  -1706
ATOM   1866  CZ2 TRP A 128      42.867   3.840  39.665  1.00 48.35           C  
ANISOU 1866  CZ2 TRP A 128     5565   6154   6653  -2604   1754  -1686
ATOM   1867  CZ3 TRP A 128      40.575   3.916  38.838  1.00 45.99           C  
ANISOU 1867  CZ3 TRP A 128     4926   6130   6420  -2195   1528  -1625
ATOM   1868  CH2 TRP A 128      41.936   4.242  38.690  1.00 46.71           C  
ANISOU 1868  CH2 TRP A 128     5254   5972   6521  -2331   1668  -1607
ATOM   1869  H   TRP A 128      37.482   0.798  43.876  1.00 50.87           H  
ATOM   1870  HA  TRP A 128      39.594   2.593  44.692  1.00 50.09           H  
ATOM   1871  HB3 TRP A 128      39.002   1.177  42.034  1.00 50.47           H  
ATOM   1872  HB2 TRP A 128      39.953   0.552  43.343  1.00 50.47           H  
ATOM   1873  HD1 TRP A 128      42.401   1.554  43.697  1.00 51.52           H  
ATOM   1874  HE1 TRP A 128      44.032   2.714  42.112  1.00 50.66           H  
ATOM   1875  HE3 TRP A 128      39.094   2.933  40.056  1.00 45.52           H  
ATOM   1876  HZ2 TRP A 128      43.910   4.096  39.565  1.00 48.35           H  
ATOM   1877  HZ3 TRP A 128      39.859   4.235  38.099  1.00 45.99           H  
ATOM   1878  HH2 TRP A 128      42.263   4.799  37.828  1.00 46.71           H  
ATOM   1879  N   VAL A 129      37.369   3.646  42.422  1.00 46.20           N  
ANISOU 1879  N   VAL A 129     4464   6776   6312  -2174   1120  -1746
ATOM   1880  CA  VAL A 129      36.772   4.834  41.801  1.00 44.06           C  
ANISOU 1880  CA  VAL A 129     4298   6299   6146  -1929   1070  -1667
ATOM   1881  C   VAL A 129      36.145   5.754  42.862  1.00 43.96           C  
ANISOU 1881  C   VAL A 129     4325   6263   6115  -1931    991  -1659
ATOM   1882  O   VAL A 129      36.355   6.960  42.796  1.00 42.92           O  
ANISOU 1882  O   VAL A 129     4366   5916   6026  -1891   1042  -1629
ATOM   1883  CB  VAL A 129      35.725   4.417  40.732  1.00 43.50           C  
ANISOU 1883  CB  VAL A 129     4086   6306   6136  -1664    953  -1613
ATOM   1884  CG1 VAL A 129      34.985   5.608  40.093  1.00 41.82           C  
ANISOU 1884  CG1 VAL A 129     3997   5878   6013  -1460    897  -1526
ATOM   1885  CG2 VAL A 129      36.379   3.604  39.610  1.00 42.41           C  
ANISOU 1885  CG2 VAL A 129     3897   6221   5995  -1655   1033  -1628
ATOM   1886  H   VAL A 129      36.910   2.760  42.264  1.00 46.20           H  
ATOM   1887  HA  VAL A 129      37.568   5.393  41.304  1.00 44.06           H  
ATOM   1888  HB  VAL A 129      34.973   3.786  41.207  1.00 43.50           H  
ATOM   1889 HG11 VAL A 129      34.255   5.250  39.369  1.00 41.82           H  
ATOM   1890 HG12 VAL A 129      34.433   6.198  40.821  1.00 41.82           H  
ATOM   1891 HG13 VAL A 129      35.675   6.276  39.577  1.00 41.82           H  
ATOM   1892 HG21 VAL A 129      35.668   3.411  38.812  1.00 42.41           H  
ATOM   1893 HG22 VAL A 129      37.217   4.141  39.166  1.00 42.41           H  
ATOM   1894 HG23 VAL A 129      36.745   2.644  39.969  1.00 42.41           H  
ATOM   1895  N   ARG A 130      35.439   5.196  43.861  1.00 44.88           N  
ANISOU 1895  N   ARG A 130     4270   6621   6162  -1976    869  -1678
ATOM   1896  CA  ARG A 130      34.834   5.915  44.990  1.00 45.13           C  
ANISOU 1896  CA  ARG A 130     4317   6683   6148  -2009    779  -1666
ATOM   1897  C   ARG A 130      35.842   6.697  45.856  1.00 46.03           C  
ANISOU 1897  C   ARG A 130     4631   6659   6198  -2224    914  -1735
ATOM   1898  O   ARG A 130      35.443   7.658  46.512  1.00 46.71           O  
ANISOU 1898  O   ARG A 130     4793   6696   6258  -2224    883  -1722
ATOM   1899  CB  ARG A 130      34.060   4.920  45.874  1.00 46.91           C  
ANISOU 1899  CB  ARG A 130     4314   7225   6287  -2073    639  -1674
ATOM   1900  CG  ARG A 130      32.749   4.419  45.248  1.00 47.44           C  
ANISOU 1900  CG  ARG A 130     4207   7395   6421  -1798    468  -1591
ATOM   1901  CD  ARG A 130      32.159   3.219  46.003  1.00 48.58           C  
ANISOU 1901  CD  ARG A 130     4087   7882   6490  -1841    352  -1594
ATOM   1902  NE  ARG A 130      31.341   3.654  47.143  1.00 48.13           N  
ANISOU 1902  NE  ARG A 130     3979   7950   6358  -1901    207  -1549
ATOM   1903  CZ  ARG A 130      30.014   3.863  47.133  1.00 49.26           C  
ANISOU 1903  CZ  ARG A 130     4074   8095   6547  -1690     33  -1449
ATOM   1904  NH1 ARG A 130      29.276   3.688  46.026  1.00 51.22           N  
ANISOU 1904  NH1 ARG A 130     4332   8212   6917  -1400    -17  -1394
ATOM   1905  NH2 ARG A 130      29.414   4.262  48.261  1.00 49.52           N1+
ANISOU 1905  NH2 ARG A 130     4065   8257   6493  -1780    -96  -1399
ATOM   1906  H   ARG A 130      35.312   4.192  43.841  1.00 44.88           H  
ATOM   1907  HA  ARG A 130      34.131   6.646  44.587  1.00 45.13           H  
ATOM   1908  HB3 ARG A 130      33.819   5.374  46.838  1.00 46.91           H  
ATOM   1909  HB2 ARG A 130      34.713   4.076  46.102  1.00 46.91           H  
ATOM   1910  HG3 ARG A 130      32.904   4.145  44.207  1.00 47.44           H  
ATOM   1911  HG2 ARG A 130      32.025   5.235  45.218  1.00 47.44           H  
ATOM   1912  HD3 ARG A 130      32.949   2.561  46.365  1.00 48.58           H  
ATOM   1913  HD2 ARG A 130      31.559   2.605  45.337  1.00 48.58           H  
ATOM   1914  HE  ARG A 130      31.848   3.822  48.000  1.00 48.13           H  
ATOM   1915 HH12 ARG A 130      28.282   3.863  46.031  1.00 51.22           H  
ATOM   1916 HH11 ARG A 130      29.698   3.334  45.173  1.00 51.22           H  
ATOM   1917 HH22 ARG A 130      28.417   4.425  48.277  1.00 49.52           H  
ATOM   1918 HH21 ARG A 130      29.951   4.396  49.106  1.00 49.52           H  
ATOM   1919  N   GLY A 131      37.131   6.319  45.835  1.00 46.41           N  
ANISOU 1919  N   GLY A 131     4776   6644   6214  -2410   1066  -1810
ATOM   1920  CA  GLY A 131      38.202   7.017  46.538  1.00 46.90           C  
ANISOU 1920  CA  GLY A 131     5069   6528   6225  -2598   1215  -1889
ATOM   1921  C   GLY A 131      38.908   8.104  45.712  1.00 46.28           C  
ANISOU 1921  C   GLY A 131     5204   6128   6252  -2450   1340  -1852
ATOM   1922  O   GLY A 131      39.571   8.950  46.311  1.00 47.52           O  
ANISOU 1922  O   GLY A 131     5539   6137   6379  -2517   1439  -1903
ATOM   1923  H   GLY A 131      37.388   5.512  45.285  1.00 46.41           H  
ATOM   1924  HA3 GLY A 131      38.941   6.275  46.837  1.00 46.90           H  
ATOM   1925  HA2 GLY A 131      37.834   7.458  47.466  1.00 46.90           H  
ATOM   1926  N   LEU A 132      38.793   8.085  44.369  1.00 44.84           N  
ANISOU 1926  N   LEU A 132     5004   5849   6185  -2247   1339  -1762
ATOM   1927  CA  LEU A 132      39.584   8.916  43.450  1.00 44.26           C  
ANISOU 1927  CA  LEU A 132     5116   5491   6210  -2121   1461  -1708
ATOM   1928  C   LEU A 132      38.776   9.865  42.554  1.00 43.11           C  
ANISOU 1928  C   LEU A 132     4916   5296   6170  -1845   1369  -1578
ATOM   1929  O   LEU A 132      39.383  10.792  42.022  1.00 42.72           O  
ANISOU 1929  O   LEU A 132     4986   5047   6199  -1726   1449  -1510
ATOM   1930  CB  LEU A 132      40.368   8.002  42.487  1.00 44.80           C  
ANISOU 1930  CB  LEU A 132     5262   5453   6307  -2185   1573  -1706
ATOM   1931  CG  LEU A 132      41.399   7.059  43.124  1.00 45.97           C  
ANISOU 1931  CG  LEU A 132     5424   5681   6360  -2462   1642  -1800
ATOM   1932  CD1 LEU A 132      41.903   6.086  42.063  1.00 46.23           C  
ANISOU 1932  CD1 LEU A 132     5397   5741   6427  -2432   1653  -1745
ATOM   1933  CD2 LEU A 132      42.565   7.798  43.787  1.00 50.07           C  
ANISOU 1933  CD2 LEU A 132     6211   5955   6859  -2614   1811  -1865
ATOM   1934  H   LEU A 132      38.211   7.370  43.954  1.00 44.84           H  
ATOM   1935  HA  LEU A 132      40.289   9.540  44.004  1.00 44.26           H  
ATOM   1936  HB3 LEU A 132      40.886   8.602  41.737  1.00 44.80           H  
ATOM   1937  HB2 LEU A 132      39.648   7.399  41.930  1.00 44.80           H  
ATOM   1938  HG  LEU A 132      40.901   6.470  43.886  1.00 45.97           H  
ATOM   1939 HD11 LEU A 132      42.693   5.445  42.454  1.00 46.23           H  
ATOM   1940 HD12 LEU A 132      41.089   5.449  41.719  1.00 46.23           H  
ATOM   1941 HD13 LEU A 132      42.282   6.616  41.193  1.00 46.23           H  
ATOM   1942 HD21 LEU A 132      43.316   7.103  44.164  1.00 50.07           H  
ATOM   1943 HD22 LEU A 132      43.052   8.473  43.084  1.00 50.07           H  
ATOM   1944 HD23 LEU A 132      42.213   8.382  44.635  1.00 50.07           H  
ATOM   1945  N   TYR A 133      37.474   9.601  42.317  1.00 42.57           N  
ANISOU 1945  N   TYR A 133     4669   5401   6103  -1741   1200  -1535
ATOM   1946  CA  TYR A 133      36.633  10.140  41.229  1.00 41.04           C  
ANISOU 1946  CA  TYR A 133     4447   5146   6000  -1513   1116  -1418
ATOM   1947  C   TYR A 133      36.727  11.643  40.911  1.00 40.74           C  
ANISOU 1947  C   TYR A 133     4532   4924   6021  -1407   1167  -1336
ATOM   1948  O   TYR A 133      36.552  12.019  39.754  1.00 40.54           O  
ANISOU 1948  O   TYR A 133     4527   4805   6071  -1263   1152  -1236
ATOM   1949  CB  TYR A 133      35.161   9.703  41.382  1.00 40.54           C  
ANISOU 1949  CB  TYR A 133     4227   5252   5926  -1412    923  -1387
ATOM   1950  CG  TYR A 133      34.404  10.376  42.514  1.00 39.84           C  
ANISOU 1950  CG  TYR A 133     4124   5225   5789  -1438    837  -1377
ATOM   1951  CD1 TYR A 133      33.643  11.537  42.262  1.00 36.47           C  
ANISOU 1951  CD1 TYR A 133     3751   4710   5395  -1336    791  -1289
ATOM   1952  CD2 TYR A 133      34.469   9.855  43.822  1.00 40.82           C  
ANISOU 1952  CD2 TYR A 133     4169   5519   5820  -1578    793  -1445
ATOM   1953  CE1 TYR A 133      32.957  12.175  43.312  1.00 37.63           C  
ANISOU 1953  CE1 TYR A 133     3884   4932   5483  -1376    711  -1271
ATOM   1954  CE2 TYR A 133      33.780  10.489  44.872  1.00 42.09           C  
ANISOU 1954  CE2 TYR A 133     4320   5751   5920  -1614    705  -1424
ATOM   1955  CZ  TYR A 133      33.029  11.653  44.618  1.00 41.41           C  
ANISOU 1955  CZ  TYR A 133     4298   5568   5867  -1513    669  -1338
ATOM   1956  OH  TYR A 133      32.373  12.281  45.636  1.00 44.22           O  
ANISOU 1956  OH  TYR A 133     4647   6006   6149  -1567    589  -1312
ATOM   1957  H   TYR A 133      37.078   8.817  42.816  1.00 42.57           H  
ATOM   1958  HA  TYR A 133      37.004   9.635  40.336  1.00 41.04           H  
ATOM   1959  HB3 TYR A 133      35.085   8.624  41.488  1.00 40.54           H  
ATOM   1960  HB2 TYR A 133      34.627   9.918  40.454  1.00 40.54           H  
ATOM   1961  HD1 TYR A 133      33.584  11.945  41.262  1.00 36.47           H  
ATOM   1962  HD2 TYR A 133      35.054   8.969  44.024  1.00 40.82           H  
ATOM   1963  HE1 TYR A 133      32.376  13.063  43.112  1.00 37.63           H  
ATOM   1964  HE2 TYR A 133      33.840  10.081  45.871  1.00 42.09           H  
ATOM   1965  HH  TYR A 133      32.451  11.827  46.461  1.00 44.22           H  
ATOM   1966  N   LYS A 134      37.004  12.493  41.914  1.00 40.71           N  
ANISOU 1966  N   LYS A 134     4605   4883   5977  -1478   1231  -1374
ATOM   1967  CA  LYS A 134      37.106  13.946  41.768  1.00 40.14           C  
ANISOU 1967  CA  LYS A 134     4602   4688   5960  -1348   1265  -1282
ATOM   1968  C   LYS A 134      38.394  14.392  41.046  1.00 40.17           C  
ANISOU 1968  C   LYS A 134     4730   4490   6042  -1285   1420  -1240
ATOM   1969  O   LYS A 134      38.469  15.539  40.613  1.00 39.89           O  
ANISOU 1969  O   LYS A 134     4719   4368   6071  -1145   1440  -1132
ATOM   1970  CB  LYS A 134      37.043  14.608  43.159  1.00 41.05           C  
ANISOU 1970  CB  LYS A 134     4757   4836   6003  -1415   1300  -1328
ATOM   1971  CG  LYS A 134      35.778  14.220  43.948  1.00 39.48           C  
ANISOU 1971  CG  LYS A 134     4446   4843   5710  -1505   1146  -1361
ATOM   1972  CD  LYS A 134      35.518  15.093  45.181  1.00 38.57           C  
ANISOU 1972  CD  LYS A 134     4370   4773   5513  -1566   1169  -1383
ATOM   1973  CE  LYS A 134      34.887  16.448  44.821  1.00 37.60           C  
ANISOU 1973  CE  LYS A 134     4225   4626   5435  -1414   1117  -1246
ATOM   1974  NZ  LYS A 134      34.633  17.258  46.022  1.00 36.80           N1+
ANISOU 1974  NZ  LYS A 134     4136   4620   5228  -1495   1123  -1265
ATOM   1975  H   LYS A 134      37.158  12.108  42.836  1.00 40.71           H  
ATOM   1976  HA  LYS A 134      36.256  14.294  41.175  1.00 40.14           H  
ATOM   1977  HB3 LYS A 134      37.069  15.690  43.029  1.00 41.05           H  
ATOM   1978  HB2 LYS A 134      37.929  14.358  43.740  1.00 41.05           H  
ATOM   1979  HG3 LYS A 134      35.864  13.182  44.269  1.00 39.48           H  
ATOM   1980  HG2 LYS A 134      34.907  14.260  43.293  1.00 39.48           H  
ATOM   1981  HD3 LYS A 134      36.443  15.226  45.742  1.00 38.57           H  
ATOM   1982  HD2 LYS A 134      34.837  14.558  45.844  1.00 38.57           H  
ATOM   1983  HE3 LYS A 134      33.942  16.298  44.297  1.00 37.60           H  
ATOM   1984  HE2 LYS A 134      35.538  17.015  44.156  1.00 37.60           H  
ATOM   1985  HZ1 LYS A 134      35.518  17.450  46.475  1.00 36.80           H  
ATOM   1986  HZ2 LYS A 134      34.196  18.129  45.760  1.00 36.80           H  
ATOM   1987  HZ3 LYS A 134      34.029  16.752  46.655  1.00 36.80           H  
ATOM   1988  N   TYR A 135      39.365  13.485  40.853  1.00 41.28           N  
ANISOU 1988  N   TYR A 135     4945   4566   6174  -1396   1523  -1312
ATOM   1989  CA  TYR A 135      40.573  13.662  40.050  1.00 41.67           C  
ANISOU 1989  CA  TYR A 135     5121   4413   6301  -1334   1655  -1251
ATOM   1990  C   TYR A 135      40.658  12.637  38.904  1.00 40.77           C  
ANISOU 1990  C   TYR A 135     4956   4328   6209  -1329   1608  -1204
ATOM   1991  O   TYR A 135      41.736  12.420  38.353  1.00 42.23           O  
ANISOU 1991  O   TYR A 135     5247   4387   6410  -1385   1717  -1199
ATOM   1992  CB  TYR A 135      41.821  13.704  40.961  1.00 43.04           C  
ANISOU 1992  CB  TYR A 135     5487   4416   6450  -1456   1847  -1354
ATOM   1993  CG  TYR A 135      42.074  15.052  41.615  1.00 45.04           C  
ANISOU 1993  CG  TYR A 135     5829   4565   6721  -1362   1946  -1355
ATOM   1994  CD1 TYR A 135      42.365  16.176  40.813  1.00 44.84           C  
ANISOU 1994  CD1 TYR A 135     5829   4412   6796  -1149   1999  -1218
ATOM   1995  CD2 TYR A 135      42.046  15.189  43.017  1.00 46.67           C  
ANISOU 1995  CD2 TYR A 135     6081   4820   6831  -1486   1990  -1489
ATOM   1996  CE1 TYR A 135      42.605  17.429  41.406  1.00 42.52           C  
ANISOU 1996  CE1 TYR A 135     5588   4053   6515  -1045   2102  -1217
ATOM   1997  CE2 TYR A 135      42.289  16.443  43.612  1.00 42.85           C  
ANISOU 1997  CE2 TYR A 135     5675   4256   6351  -1390   2100  -1499
ATOM   1998  CZ  TYR A 135      42.559  17.565  42.807  1.00 42.12           C  
ANISOU 1998  CZ  TYR A 135     5590   4048   6368  -1161   2159  -1363
ATOM   1999  OH  TYR A 135      42.766  18.785  43.381  1.00 46.36           O  
ANISOU 1999  OH  TYR A 135     6173   4533   6908  -1046   2277  -1366
ATOM   2000  H   TYR A 135      39.226  12.563  41.249  1.00 41.28           H  
ATOM   2001  HA  TYR A 135      40.515  14.612  39.520  1.00 41.67           H  
ATOM   2002  HB3 TYR A 135      42.724  13.471  40.399  1.00 43.04           H  
ATOM   2003  HB2 TYR A 135      41.742  12.926  41.722  1.00 43.04           H  
ATOM   2004  HD1 TYR A 135      42.403  16.080  39.738  1.00 44.84           H  
ATOM   2005  HD2 TYR A 135      41.847  14.329  43.638  1.00 46.67           H  
ATOM   2006  HE1 TYR A 135      42.815  18.284  40.783  1.00 42.52           H  
ATOM   2007  HE2 TYR A 135      42.263  16.547  44.688  1.00 42.85           H  
ATOM   2008  HH  TYR A 135      43.017  19.451  42.759  1.00 46.36           H  
ATOM   2009  N   LEU A 136      39.508  12.059  38.513  1.00 38.83           N  
ANISOU 2009  N   LEU A 136     4559   4240   5954  -1263   1448  -1169
ATOM   2010  CA  LEU A 136      39.300  11.300  37.282  1.00 38.88           C  
ANISOU 2010  CA  LEU A 136     4516   4283   5974  -1225   1403  -1122
ATOM   2011  C   LEU A 136      38.258  12.035  36.424  1.00 38.35           C  
ANISOU 2011  C   LEU A 136     4380   4245   5946  -1053   1264  -1009
ATOM   2012  O   LEU A 136      37.388  12.739  36.938  1.00 38.36           O  
ANISOU 2012  O   LEU A 136     4333   4293   5947   -993   1167   -987
ATOM   2013  CB  LEU A 136      38.784   9.879  37.600  1.00 39.32           C  
ANISOU 2013  CB  LEU A 136     4452   4532   5957  -1335   1350  -1227
ATOM   2014  CG  LEU A 136      39.708   9.003  38.479  1.00 42.79           C  
ANISOU 2014  CG  LEU A 136     4906   5031   6322  -1559   1444  -1349
ATOM   2015  CD1 LEU A 136      39.054   7.639  38.740  1.00 42.43           C  
ANISOU 2015  CD1 LEU A 136     4672   5239   6211  -1610   1356  -1417
ATOM   2016  CD2 LEU A 136      41.104   8.809  37.867  1.00 41.43           C  
ANISOU 2016  CD2 LEU A 136     4896   4687   6158  -1671   1607  -1339
ATOM   2017  H   LEU A 136      38.670  12.298  39.023  1.00 38.83           H  
ATOM   2018  HA  LEU A 136      40.222  11.237  36.705  1.00 38.88           H  
ATOM   2019  HB3 LEU A 136      38.601   9.352  36.661  1.00 39.32           H  
ATOM   2020  HB2 LEU A 136      37.811   9.954  38.085  1.00 39.32           H  
ATOM   2021  HG  LEU A 136      39.831   9.492  39.446  1.00 42.79           H  
ATOM   2022 HD11 LEU A 136      39.668   7.028  39.404  1.00 42.43           H  
ATOM   2023 HD12 LEU A 136      38.076   7.747  39.209  1.00 42.43           H  
ATOM   2024 HD13 LEU A 136      38.920   7.083  37.812  1.00 42.43           H  
ATOM   2025 HD21 LEU A 136      41.697   8.109  38.458  1.00 41.43           H  
ATOM   2026 HD22 LEU A 136      41.036   8.414  36.855  1.00 41.43           H  
ATOM   2027 HD23 LEU A 136      41.663   9.743  37.821  1.00 41.43           H  
ATOM   2028  N   GLY A 137      38.337  11.837  35.105  1.00 37.92           N  
ANISOU 2028  N   GLY A 137     4331   4167   5910   -996   1248   -937
ATOM   2029  CA  GLY A 137      37.422  12.407  34.127  1.00 37.06           C  
ANISOU 2029  CA  GLY A 137     4175   4087   5817   -867   1110   -845
ATOM   2030  C   GLY A 137      38.021  12.323  32.730  1.00 37.20           C  
ANISOU 2030  C   GLY A 137     4247   4036   5853   -825   1134   -739
ATOM   2031  O   GLY A 137      39.241  12.264  32.581  1.00 38.29           O  
ANISOU 2031  O   GLY A 137     4470   4063   6017   -859   1258   -692
ATOM   2032  H   GLY A 137      39.073  11.241  34.746  1.00 37.92           H  
ATOM   2033  HA3 GLY A 137      37.215  13.455  34.355  1.00 37.06           H  
ATOM   2034  HA2 GLY A 137      36.475  11.869  34.156  1.00 37.06           H  
ATOM   2035  N   ASP A 138      37.167  12.365  31.697  1.00 36.34           N  
ANISOU 2035  N   ASP A 138     4103   3982   5725   -753   1011   -698
ATOM   2036  CA  ASP A 138      37.548  12.325  30.279  1.00 36.75           C  
ANISOU 2036  CA  ASP A 138     4198   4003   5762   -736   1015   -609
ATOM   2037  C   ASP A 138      38.352  13.568  29.826  1.00 36.71           C  
ANISOU 2037  C   ASP A 138     4258   3879   5811   -694   1059   -439
ATOM   2038  O   ASP A 138      38.843  13.589  28.701  1.00 37.00           O  
ANISOU 2038  O   ASP A 138     4337   3888   5834   -692   1069   -338
ATOM   2039  CB  ASP A 138      36.287  12.098  29.402  1.00 36.75           C  
ANISOU 2039  CB  ASP A 138     4169   4081   5712   -678    872   -621
ATOM   2040  CG  ASP A 138      35.246  13.226  29.326  1.00 37.90           C  
ANISOU 2040  CG  ASP A 138     4318   4204   5878   -605    731   -531
ATOM   2041  OD1 ASP A 138      35.262  14.115  30.204  1.00 41.31           O  
ANISOU 2041  OD1 ASP A 138     4736   4606   6354   -596    733   -489
ATOM   2042  OD2 ASP A 138      34.431  13.157  28.381  1.00 40.40           O1-
ANISOU 2042  OD2 ASP A 138     4661   4537   6153   -571    619   -505
ATOM   2043  H   ASP A 138      36.178  12.439  31.895  1.00 36.34           H  
ATOM   2044  HA  ASP A 138      38.194  11.459  30.146  1.00 36.75           H  
ATOM   2045  HB3 ASP A 138      35.762  11.212  29.754  1.00 36.75           H  
ATOM   2046  HB2 ASP A 138      36.599  11.869  28.382  1.00 36.75           H  
ATOM   2047  N   ARG A 139      38.517  14.576  30.698  1.00 36.61           N  
ANISOU 2047  N   ARG A 139     4246   3812   5853   -657   1089   -404
ATOM   2048  CA  ARG A 139      39.322  15.781  30.511  1.00 36.54           C  
ANISOU 2048  CA  ARG A 139     4278   3699   5907   -586   1157   -247
ATOM   2049  C   ARG A 139      40.175  16.115  31.749  1.00 37.24           C  
ANISOU 2049  C   ARG A 139     4418   3685   6045   -586   1308   -294
ATOM   2050  O   ARG A 139      40.613  17.256  31.895  1.00 37.86           O  
ANISOU 2050  O   ARG A 139     4510   3694   6182   -491   1366   -187
ATOM   2051  CB  ARG A 139      38.456  16.952  30.004  1.00 35.55           C  
ANISOU 2051  CB  ARG A 139     4091   3626   5790   -505   1030   -108
ATOM   2052  CG  ARG A 139      37.780  16.689  28.650  1.00 34.14           C  
ANISOU 2052  CG  ARG A 139     3907   3503   5562   -510    907    -26
ATOM   2053  CD  ARG A 139      37.024  17.913  28.134  1.00 36.97           C  
ANISOU 2053  CD  ARG A 139     4212   3918   5917   -467    777    118
ATOM   2054  NE  ARG A 139      36.314  17.599  26.890  1.00 38.24           N  
ANISOU 2054  NE  ARG A 139     4392   4130   6007   -502    646    177
ATOM   2055  CZ  ARG A 139      35.672  18.488  26.118  1.00 38.98           C  
ANISOU 2055  CZ  ARG A 139     4459   4284   6066   -510    501    296
ATOM   2056  NH1 ARG A 139      35.618  19.786  26.446  1.00 36.40           N  
ANISOU 2056  NH1 ARG A 139     4065   3994   5772   -484    469    380
ATOM   2057  NH2 ARG A 139      35.068  18.062  25.001  1.00 39.39           N1+
ANISOU 2057  NH2 ARG A 139     4559   4370   6037   -563    392    328
ATOM   2058  H   ARG A 139      38.049  14.482  31.587  1.00 36.61           H  
ATOM   2059  HA  ARG A 139      40.062  15.575  29.738  1.00 36.54           H  
ATOM   2060  HB3 ARG A 139      39.073  17.846  29.907  1.00 35.55           H  
ATOM   2061  HB2 ARG A 139      37.694  17.191  30.747  1.00 35.55           H  
ATOM   2062  HG3 ARG A 139      37.078  15.860  28.736  1.00 34.14           H  
ATOM   2063  HG2 ARG A 139      38.529  16.387  27.916  1.00 34.14           H  
ATOM   2064  HD3 ARG A 139      37.719  18.734  27.958  1.00 36.97           H  
ATOM   2065  HD2 ARG A 139      36.298  18.250  28.875  1.00 36.97           H  
ATOM   2066  HE  ARG A 139      36.237  16.615  26.661  1.00 38.24           H  
ATOM   2067 HH12 ARG A 139      35.126  20.447  25.862  1.00 36.40           H  
ATOM   2068 HH11 ARG A 139      36.063  20.107  27.294  1.00 36.40           H  
ATOM   2069 HH22 ARG A 139      34.573  18.705  24.402  1.00 39.39           H  
ATOM   2070 HH21 ARG A 139      35.071  17.076  24.771  1.00 39.39           H  
ATOM   2071  N   ILE A 140      40.449  15.122  32.615  1.00 37.58           N  
ANISOU 2071  N   ILE A 140     4491   3731   6056   -695   1374   -459
ATOM   2072  CA  ILE A 140      41.351  15.220  33.767  1.00 38.37           C  
ANISOU 2072  CA  ILE A 140     4688   3711   6181   -739   1533   -531
ATOM   2073  C   ILE A 140      42.377  14.088  33.672  1.00 39.49           C  
ANISOU 2073  C   ILE A 140     4919   3787   6296   -868   1628   -594
ATOM   2074  O   ILE A 140      43.559  14.343  33.445  1.00 40.34           O  
ANISOU 2074  O   ILE A 140     5143   3738   6448   -851   1732   -512
ATOM   2075  CB  ILE A 140      40.589  15.236  35.128  1.00 37.98           C  
ANISOU 2075  CB  ILE A 140     4602   3737   6091   -804   1525   -674
ATOM   2076  CG1 ILE A 140      39.516  16.345  35.201  1.00 37.22           C  
ANISOU 2076  CG1 ILE A 140     4404   3740   5997   -709   1401   -608
ATOM   2077  CG2 ILE A 140      41.572  15.342  36.320  1.00 38.63           C  
ANISOU 2077  CG2 ILE A 140     4816   3675   6187   -852   1703   -754
ATOM   2078  CD1 ILE A 140      38.639  16.288  36.459  1.00 37.74           C  
ANISOU 2078  CD1 ILE A 140     4431   3897   6011   -776   1374   -725
ATOM   2079  H   ILE A 140      40.068  14.207  32.417  1.00 37.58           H  
ATOM   2080  HA  ILE A 140      41.921  16.149  33.704  1.00 38.37           H  
ATOM   2081  HB  ILE A 140      40.061  14.286  35.226  1.00 37.98           H  
ATOM   2082 HG13 ILE A 140      38.845  16.266  34.345  1.00 37.22           H  
ATOM   2083 HG12 ILE A 140      39.987  17.325  35.126  1.00 37.22           H  
ATOM   2084 HG21 ILE A 140      41.057  15.298  37.277  1.00 38.63           H  
ATOM   2085 HG22 ILE A 140      42.294  14.526  36.340  1.00 38.63           H  
ATOM   2086 HG23 ILE A 140      42.130  16.277  36.289  1.00 38.63           H  
ATOM   2087 HD11 ILE A 140      37.825  17.010  36.390  1.00 37.74           H  
ATOM   2088 HD12 ILE A 140      38.191  15.301  36.583  1.00 37.74           H  
ATOM   2089 HD13 ILE A 140      39.202  16.519  37.361  1.00 37.74           H  
ATOM   2090  N   ASP A 141      41.911  12.848  33.879  1.00 39.66           N  
ANISOU 2090  N   ASP A 141     4882   3942   6245   -996   1586   -724
ATOM   2091  CA  ASP A 141      42.717  11.638  33.947  1.00 40.91           C  
ANISOU 2091  CA  ASP A 141     5106   4080   6358  -1161   1678   -799
ATOM   2092  C   ASP A 141      41.882  10.436  33.488  1.00 40.53           C  
ANISOU 2092  C   ASP A 141     4929   4238   6234  -1228   1590   -869
ATOM   2093  O   ASP A 141      40.789  10.220  34.014  1.00 40.42           O  
ANISOU 2093  O   ASP A 141     4795   4374   6187  -1220   1499   -956
ATOM   2094  CB  ASP A 141      43.355  11.507  35.349  1.00 41.96           C  
ANISOU 2094  CB  ASP A 141     5319   4157   6467  -1298   1782   -934
ATOM   2095  CG  ASP A 141      44.398  10.398  35.500  1.00 44.10           C  
ANISOU 2095  CG  ASP A 141     5699   4363   6693  -1492   1893   -986
ATOM   2096  OD1 ASP A 141      44.855   9.856  34.472  1.00 42.92           O  
ANISOU 2096  OD1 ASP A 141     5575   4187   6545  -1494   1902   -893
ATOM   2097  OD2 ASP A 141      44.754  10.121  36.666  1.00 47.96           O1-
ANISOU 2097  OD2 ASP A 141     6256   4833   7133  -1661   1968  -1113
ATOM   2098  H   ASP A 141      40.917  12.727  34.013  1.00 39.66           H  
ATOM   2099  HA  ASP A 141      43.522  11.774  33.232  1.00 40.91           H  
ATOM   2100  HB3 ASP A 141      42.573  11.338  36.087  1.00 41.96           H  
ATOM   2101  HB2 ASP A 141      43.842  12.441  35.629  1.00 41.96           H  
ATOM   2102  N   ILE A 142      42.399   9.671  32.511  1.00 40.86           N  
ANISOU 2102  N   ILE A 142     4994   4291   6241  -1287   1622   -829
ATOM   2103  CA  ILE A 142      41.702   8.595  31.808  1.00 40.54           C  
ANISOU 2103  CA  ILE A 142     4823   4454   6125  -1309   1548   -885
ATOM   2104  C   ILE A 142      42.423   7.254  32.073  1.00 42.07           C  
ANISOU 2104  C   ILE A 142     5007   4737   6239  -1511   1641   -973
ATOM   2105  O   ILE A 142      43.310   6.884  31.304  1.00 43.37           O  
ANISOU 2105  O   ILE A 142     5263   4835   6380  -1598   1719   -905
ATOM   2106  CB  ILE A 142      41.635   8.943  30.289  1.00 40.29           C  
ANISOU 2106  CB  ILE A 142     4801   4418   6091  -1205   1488   -759
ATOM   2107  CG1 ILE A 142      40.917  10.284  29.999  1.00 38.74           C  
ANISOU 2107  CG1 ILE A 142     4592   4174   5954  -1034   1377   -669
ATOM   2108  CG2 ILE A 142      40.983   7.834  29.432  1.00 40.45           C  
ANISOU 2108  CG2 ILE A 142     4711   4635   6022  -1220   1439   -834
ATOM   2109  CD1 ILE A 142      41.630  11.109  28.923  1.00 39.32           C  
ANISOU 2109  CD1 ILE A 142     4752   4124   6063   -969   1382   -484
ATOM   2110  H   ILE A 142      43.314   9.924  32.159  1.00 40.86           H  
ATOM   2111  HA  ILE A 142      40.679   8.524  32.163  1.00 40.54           H  
ATOM   2112  HB  ILE A 142      42.667   9.050  29.952  1.00 40.29           H  
ATOM   2113 HG13 ILE A 142      40.840  10.905  30.888  1.00 38.74           H  
ATOM   2114 HG12 ILE A 142      39.889  10.094  29.692  1.00 38.74           H  
ATOM   2115 HG21 ILE A 142      40.886   8.150  28.393  1.00 40.45           H  
ATOM   2116 HG22 ILE A 142      41.563   6.911  29.424  1.00 40.45           H  
ATOM   2117 HG23 ILE A 142      39.986   7.590  29.796  1.00 40.45           H  
ATOM   2118 HD11 ILE A 142      41.113  12.051  28.744  1.00 39.32           H  
ATOM   2119 HD12 ILE A 142      42.651  11.349  29.220  1.00 39.32           H  
ATOM   2120 HD13 ILE A 142      41.674  10.563  27.979  1.00 39.32           H  
ATOM   2121  N   PRO A 143      42.073   6.504  33.143  1.00 42.35           N  
ANISOU 2121  N   PRO A 143     4926   4941   6224  -1601   1626  -1111
ATOM   2122  CA  PRO A 143      42.504   5.113  33.359  1.00 44.00           C  
ANISOU 2122  CA  PRO A 143     5083   5294   6341  -1813   1701  -1195
ATOM   2123  C   PRO A 143      42.172   4.137  32.205  1.00 45.13           C  
ANISOU 2123  C   PRO A 143     5097   5642   6410  -1798   1680  -1205
ATOM   2124  O   PRO A 143      41.252   4.363  31.422  1.00 45.00           O  
ANISOU 2124  O   PRO A 143     5004   5688   6407  -1614   1585  -1194
ATOM   2125  CB  PRO A 143      41.820   4.670  34.654  1.00 44.37           C  
ANISOU 2125  CB  PRO A 143     5007   5493   6359  -1873   1657  -1319
ATOM   2126  CG  PRO A 143      41.489   5.950  35.392  1.00 42.45           C  
ANISOU 2126  CG  PRO A 143     4826   5105   6196  -1736   1601  -1294
ATOM   2127  CD  PRO A 143      41.375   7.022  34.319  1.00 41.62           C  
ANISOU 2127  CD  PRO A 143     4755   4903   6156  -1533   1543  -1178
ATOM   2128  HA  PRO A 143      43.574   5.141  33.524  1.00 44.00           H  
ATOM   2129  HB3 PRO A 143      42.457   4.026  35.254  1.00 44.37           H  
ATOM   2130  HB2 PRO A 143      40.912   4.115  34.446  1.00 44.37           H  
ATOM   2131  HG3 PRO A 143      42.327   6.207  36.042  1.00 42.45           H  
ATOM   2132  HG2 PRO A 143      40.602   5.883  36.022  1.00 42.45           H  
ATOM   2133  HD2 PRO A 143      40.330   7.223  34.099  1.00 41.62           H  
ATOM   2134  HD3 PRO A 143      41.838   7.937  34.680  1.00 41.62           H  
ATOM   2135  N   ALA A 144      42.941   3.043  32.123  1.00 46.86           N  
ANISOU 2135  N   ALA A 144     5302   5962   6540  -2004   1775  -1231
ATOM   2136  CA  ALA A 144      42.870   1.999  31.098  1.00 47.11           C  
ANISOU 2136  CA  ALA A 144     5225   6198   6476  -2033   1797  -1241
ATOM   2137  C   ALA A 144      43.239   0.636  31.716  1.00 49.19           C  
ANISOU 2137  C   ALA A 144     5377   6681   6632  -2287   1877  -1329
ATOM   2138  O   ALA A 144      43.637   0.594  32.882  1.00 49.73           O  
ANISOU 2138  O   ALA A 144     5491   6704   6701  -2455   1911  -1368
ATOM   2139  CB  ALA A 144      43.776   2.413  29.926  1.00 47.35           C  
ANISOU 2139  CB  ALA A 144     5423   6067   6500  -2060   1852  -1105
ATOM   2140  H   ALA A 144      43.672   2.930  32.811  1.00 46.86           H  
ATOM   2141  HA  ALA A 144      41.841   1.937  30.739  1.00 47.11           H  
ATOM   2142  HB1 ALA A 144      43.657   1.774  29.054  1.00 47.35           H  
ATOM   2143  HB2 ALA A 144      43.558   3.431  29.603  1.00 47.35           H  
ATOM   2144  HB3 ALA A 144      44.828   2.385  30.214  1.00 47.35           H  
ATOM   2145  N   PRO A 145      43.118  -0.501  30.994  1.00 50.54           N  
ANISOU 2145  N   PRO A 145     5400   7107   6697  -2333   1913  -1363
ATOM   2146  CA  PRO A 145      43.679  -1.791  31.416  1.00 52.60           C  
ANISOU 2146  CA  PRO A 145     5536   7605   6843  -2604   1992  -1429
ATOM   2147  C   PRO A 145      45.220  -1.781  31.531  1.00 54.00           C  
ANISOU 2147  C   PRO A 145     5919   7624   6976  -2903   2102  -1354
ATOM   2148  O   PRO A 145      45.912  -1.132  30.748  1.00 54.00           O  
ANISOU 2148  O   PRO A 145     6116   7402   7000  -2893   2137  -1237
ATOM   2149  CB  PRO A 145      43.284  -2.789  30.314  1.00 53.07           C  
ANISOU 2149  CB  PRO A 145     5387   7980   6798  -2549   2016  -1475
ATOM   2150  CG  PRO A 145      42.095  -2.163  29.615  1.00 52.18           C  
ANISOU 2150  CG  PRO A 145     5247   7821   6759  -2215   1916  -1489
ATOM   2151  CD  PRO A 145      42.258  -0.658  29.826  1.00 50.03           C  
ANISOU 2151  CD  PRO A 145     5229   7180   6600  -2134   1873  -1376
ATOM   2152  HA  PRO A 145      43.212  -2.068  32.357  1.00 52.60           H  
ATOM   2153  HB3 PRO A 145      43.050  -3.773  30.716  1.00 53.07           H  
ATOM   2154  HB2 PRO A 145      44.083  -2.921  29.582  1.00 53.07           H  
ATOM   2155  HG3 PRO A 145      41.178  -2.496  30.103  1.00 52.18           H  
ATOM   2156  HG2 PRO A 145      42.028  -2.444  28.563  1.00 52.18           H  
ATOM   2157  HD2 PRO A 145      42.739  -0.218  28.956  1.00 50.03           H  
ATOM   2158  HD3 PRO A 145      41.294  -0.179  29.967  1.00 50.03           H  
ATOM   2159  N   ASP A 146      45.729  -2.587  32.470  1.00 55.50           N  
ANISOU 2159  N   ASP A 146     6066   7927   7097  -3174   2147  -1415
ATOM   2160  CA  ASP A 146      47.102  -3.081  32.578  1.00 57.61           C  
ANISOU 2160  CA  ASP A 146     6487   8126   7275  -3517   2256  -1363
ATOM   2161  C   ASP A 146      47.063  -4.540  33.060  1.00 59.53           C  
ANISOU 2161  C   ASP A 146     6482   8766   7369  -3774   2289  -1451
ATOM   2162  O   ASP A 146      46.079  -5.238  32.811  1.00 59.43           O  
ANISOU 2162  O   ASP A 146     6172   9087   7322  -3637   2243  -1527
ATOM   2163  CB  ASP A 146      48.007  -2.119  33.387  1.00 58.04           C  
ANISOU 2163  CB  ASP A 146     6836   7812   7405  -3630   2284  -1337
ATOM   2164  CG  ASP A 146      49.479  -2.178  32.968  1.00 61.27           C  
ANISOU 2164  CG  ASP A 146     7500   8020   7758  -3916   2391  -1243
ATOM   2165  OD1 ASP A 146      49.810  -1.554  31.938  1.00 62.70           O  
ANISOU 2165  OD1 ASP A 146     7850   7991   7983  -3822   2416  -1111
ATOM   2166  OD2 ASP A 146      50.255  -2.847  33.685  1.00 65.42           O1-
ANISOU 2166  OD2 ASP A 146     8066   8602   8189  -4249   2444  -1293
ATOM   2167  H   ASP A 146      45.055  -3.052  33.064  1.00 55.50           H  
ATOM   2168  HA  ASP A 146      47.486  -3.130  31.557  1.00 57.61           H  
ATOM   2169  HB3 ASP A 146      47.925  -2.314  34.456  1.00 58.04           H  
ATOM   2170  HB2 ASP A 146      47.672  -1.097  33.254  1.00 58.04           H  
ATOM   2171  N   VAL A 147      48.122  -5.010  33.741  1.00 61.71           N  
ANISOU 2171  N   VAL A 147     6880   9010   7557  -4146   2366  -1436
ATOM   2172  CA  VAL A 147      48.260  -6.349  34.322  1.00 64.25           C  
ANISOU 2172  CA  VAL A 147     6967   9728   7718  -4451   2398  -1502
ATOM   2173  C   VAL A 147      47.114  -6.660  35.304  1.00 64.04           C  
ANISOU 2173  C   VAL A 147     6636  10000   7697  -4329   2304  -1617
ATOM   2174  O   VAL A 147      46.907  -5.929  36.272  1.00 63.03           O  
ANISOU 2174  O   VAL A 147     6592   9694   7661  -4229   2234  -1658
ATOM   2175  CB  VAL A 147      49.662  -6.474  34.984  1.00 66.62           C  
ANISOU 2175  CB  VAL A 147     7506   9869   7936  -4894   2471  -1480
ATOM   2176  CG1 VAL A 147      49.851  -7.776  35.786  1.00 68.33           C  
ANISOU 2176  CG1 VAL A 147     7466  10507   7991  -5229   2473  -1561
ATOM   2177  CG2 VAL A 147      50.793  -6.356  33.946  1.00 67.93           C  
ANISOU 2177  CG2 VAL A 147     7907   9847   8056  -5058   2565  -1350
ATOM   2178  H   VAL A 147      48.898  -4.375  33.882  1.00 61.71           H  
ATOM   2179  HA  VAL A 147      48.207  -7.065  33.499  1.00 64.25           H  
ATOM   2180  HB  VAL A 147      49.779  -5.651  35.688  1.00 66.62           H  
ATOM   2181 HG11 VAL A 147      50.870  -7.852  36.165  1.00 68.33           H  
ATOM   2182 HG12 VAL A 147      49.189  -7.822  36.651  1.00 68.33           H  
ATOM   2183 HG13 VAL A 147      49.662  -8.654  35.169  1.00 68.33           H  
ATOM   2184 HG21 VAL A 147      51.771  -6.392  34.428  1.00 67.93           H  
ATOM   2185 HG22 VAL A 147      50.749  -7.169  33.220  1.00 67.93           H  
ATOM   2186 HG23 VAL A 147      50.745  -5.420  33.392  1.00 67.93           H  
ATOM   2187  N   ASN A 148      46.364  -7.738  35.015  1.00 65.37           N  
ANISOU 2187  N   ASN A 148     6450  10627   7759  -4334   2307  -1662
ATOM   2188  CA  ASN A 148      45.237  -8.275  35.788  1.00 65.60           C  
ANISOU 2188  CA  ASN A 148     6140  11004   7782  -4205   2216  -1751
ATOM   2189  C   ASN A 148      43.950  -7.432  35.723  1.00 63.05           C  
ANISOU 2189  C   ASN A 148     5775  10571   7612  -3754   2105  -1780
ATOM   2190  O   ASN A 148      43.035  -7.647  36.518  1.00 63.46           O  
ANISOU 2190  O   ASN A 148     5596  10837   7678  -3632   2010  -1837
ATOM   2191  CB  ASN A 148      45.611  -8.690  37.231  1.00 66.96           C  
ANISOU 2191  CB  ASN A 148     6306  11246   7889  -4526   2183  -1793
ATOM   2192  CG  ASN A 148      46.553  -9.890  37.334  1.00 71.31           C  
ANISOU 2192  CG  ASN A 148     6671  12175   8249  -4937   2251  -1795
ATOM   2193  OD1 ASN A 148      46.418 -10.860  36.593  1.00 74.89           O  
ANISOU 2193  OD1 ASN A 148     6856  12982   8615  -4912   2302  -1788
ATOM   2194  ND2 ASN A 148      47.515  -9.830  38.256  1.00 71.02           N  
ANISOU 2194  ND2 ASN A 148     6773  12081   8132  -5330   2255  -1809
ATOM   2195  H   ASN A 148      46.611  -8.256  34.184  1.00 65.37           H  
ATOM   2196  HA  ASN A 148      44.952  -9.183  35.254  1.00 65.60           H  
ATOM   2197  HB3 ASN A 148      44.715  -8.976  37.777  1.00 66.96           H  
ATOM   2198  HB2 ASN A 148      46.034  -7.837  37.754  1.00 66.96           H  
ATOM   2199 HD22 ASN A 148      48.152 -10.606  38.365  1.00 71.02           H  
ATOM   2200 HD21 ASN A 148      47.561  -9.033  38.878  1.00 71.02           H  
ATOM   2201  N   THR A 149      43.861  -6.501  34.763  1.00 60.51           N  
ANISOU 2201  N   THR A 149     5677   9918   7397  -3524   2106  -1727
ATOM   2202  CA  THR A 149      42.663  -5.727  34.454  1.00 58.60           C  
ANISOU 2202  CA  THR A 149     5389   9598   7279  -3119   2001  -1747
ATOM   2203  C   THR A 149      42.365  -5.820  32.955  1.00 58.71           C  
ANISOU 2203  C   THR A 149     5379   9635   7291  -2895   2033  -1727
ATOM   2204  O   THR A 149      43.241  -6.081  32.131  1.00 59.90           O  
ANISOU 2204  O   THR A 149     5639   9746   7373  -3040   2132  -1671
ATOM   2205  CB  THR A 149      42.725  -4.287  35.014  1.00 56.39           C  
ANISOU 2205  CB  THR A 149     5377   8912   7137  -3010   1934  -1714
ATOM   2206  OG1 THR A 149      43.691  -3.537  34.332  1.00 54.73           O  
ANISOU 2206  OG1 THR A 149     5471   8356   6966  -3063   2004  -1624
ATOM   2207  CG2 THR A 149      42.998  -4.186  36.520  1.00 56.59           C  
ANISOU 2207  CG2 THR A 149     5416   8942   7142  -3223   1903  -1758
ATOM   2208  H   THR A 149      44.648  -6.379  34.140  1.00 60.51           H  
ATOM   2209  HA  THR A 149      41.815  -6.213  34.934  1.00 58.60           H  
ATOM   2210  HB  THR A 149      41.765  -3.808  34.816  1.00 56.39           H  
ATOM   2211  HG1 THR A 149      44.543  -3.797  34.653  1.00 54.73           H  
ATOM   2212 HG21 THR A 149      42.925  -3.153  36.864  1.00 56.59           H  
ATOM   2213 HG22 THR A 149      42.274  -4.773  37.081  1.00 56.59           H  
ATOM   2214 HG23 THR A 149      43.994  -4.549  36.780  1.00 56.59           H  
ATOM   2215  N   ASN A 150      41.082  -5.646  32.635  1.00 57.82           N  
ANISOU 2215  N   ASN A 150     5136   9590   7245  -2553   1946  -1773
ATOM   2216  CA  ASN A 150      40.473  -5.888  31.334  1.00 57.46           C  
ANISOU 2216  CA  ASN A 150     5055   9591   7185  -2318   1967  -1786
ATOM   2217  C   ASN A 150      39.226  -5.012  31.174  1.00 55.70           C  
ANISOU 2217  C   ASN A 150     4870   9206   7088  -1956   1838  -1805
ATOM   2218  O   ASN A 150      38.907  -4.215  32.057  1.00 54.39           O  
ANISOU 2218  O   ASN A 150     4775   8870   7022  -1903   1737  -1788
ATOM   2219  CB  ASN A 150      40.220  -7.408  31.119  1.00 59.86           C  
ANISOU 2219  CB  ASN A 150     5037  10344   7364  -2321   2037  -1867
ATOM   2220  CG  ASN A 150      39.423  -8.095  32.240  1.00 62.16           C  
ANISOU 2220  CG  ASN A 150     5036  10914   7666  -2243   1960  -1935
ATOM   2221  OD1 ASN A 150      38.626  -7.462  32.926  1.00 61.77           O  
ANISOU 2221  OD1 ASN A 150     5026  10714   7729  -2084   1834  -1935
ATOM   2222  ND2 ASN A 150      39.660  -9.388  32.457  1.00 62.63           N  
ANISOU 2222  ND2 ASN A 150     4790  11406   7602  -2356   2033  -1982
ATOM   2223  H   ASN A 150      40.442  -5.406  33.378  1.00 57.82           H  
ATOM   2224  HA  ASN A 150      41.165  -5.549  30.562  1.00 57.46           H  
ATOM   2225  HB3 ASN A 150      41.186  -7.910  31.032  1.00 59.86           H  
ATOM   2226  HB2 ASN A 150      39.712  -7.591  30.172  1.00 59.86           H  
ATOM   2227 HD22 ASN A 150      39.166  -9.868  33.196  1.00 62.63           H  
ATOM   2228 HD21 ASN A 150      40.332  -9.885  31.889  1.00 62.63           H  
ATOM   2229  N   GLY A 151      38.484  -5.217  30.077  1.00 55.79           N  
ANISOU 2229  N   GLY A 151     4842   9276   7081  -1726   1843  -1844
ATOM   2230  CA  GLY A 151      37.217  -4.561  29.782  1.00 54.00           C  
ANISOU 2230  CA  GLY A 151     4670   8895   6954  -1393   1724  -1865
ATOM   2231  C   GLY A 151      36.096  -4.780  30.811  1.00 54.39           C  
ANISOU 2231  C   GLY A 151     4521   9086   7061  -1219   1619  -1926
ATOM   2232  O   GLY A 151      35.214  -3.929  30.902  1.00 53.25           O  
ANISOU 2232  O   GLY A 151     4462   8753   7019  -1010   1493  -1914
ATOM   2233  H   GLY A 151      38.812  -5.893  29.403  1.00 55.79           H  
ATOM   2234  HA3 GLY A 151      36.876  -4.928  28.813  1.00 54.00           H  
ATOM   2235  HA2 GLY A 151      37.392  -3.491  29.669  1.00 54.00           H  
ATOM   2236  N   GLN A 152      36.141  -5.862  31.614  1.00 56.06           N  
ANISOU 2236  N   GLN A 152     4461   9639   7201  -1317   1662  -1977
ATOM   2237  CA  GLN A 152      35.200  -6.108  32.711  1.00 56.24           C  
ANISOU 2237  CA  GLN A 152     4284   9812   7273  -1185   1551  -2006
ATOM   2238  C   GLN A 152      35.478  -5.178  33.907  1.00 54.71           C  
ANISOU 2238  C   GLN A 152     4221   9415   7151  -1322   1455  -1942
ATOM   2239  O   GLN A 152      34.528  -4.643  34.478  1.00 53.99           O  
ANISOU 2239  O   GLN A 152     4161   9200   7151  -1129   1320  -1927
ATOM   2240  CB  GLN A 152      35.273  -7.592  33.155  1.00 58.97           C  
ANISOU 2240  CB  GLN A 152     4282  10611   7513  -1268   1618  -2061
ATOM   2241  CG  GLN A 152      34.369  -7.991  34.344  1.00 60.46           C  
ANISOU 2241  CG  GLN A 152     4228  11008   7737  -1165   1498  -2068
ATOM   2242  CD  GLN A 152      32.878  -7.892  34.017  1.00 60.87           C  
ANISOU 2242  CD  GLN A 152     4249  10991   7890   -745   1382  -2097
ATOM   2243  OE1 GLN A 152      32.269  -8.867  33.587  1.00 59.85           O  
ANISOU 2243  OE1 GLN A 152     4353  10524   7864   -614   1273  -2059
ATOM   2244  NE2 GLN A 152      32.279  -6.721  34.234  1.00 63.25           N  
ANISOU 2244  NE2 GLN A 152     4259  11616   8159   -528   1404  -2159
ATOM   2245  H   GLN A 152      36.906  -6.513  31.505  1.00 56.06           H  
ATOM   2246  HA  GLN A 152      34.193  -5.902  32.341  1.00 56.24           H  
ATOM   2247  HB3 GLN A 152      36.292  -7.842  33.441  1.00 58.97           H  
ATOM   2248  HB2 GLN A 152      35.045  -8.232  32.301  1.00 58.97           H  
ATOM   2249  HG3 GLN A 152      34.593  -7.405  35.235  1.00 60.46           H  
ATOM   2250  HG2 GLN A 152      34.583  -9.024  34.619  1.00 60.46           H  
ATOM   2251 HE22 GLN A 152      31.294  -6.620  34.041  1.00 63.25           H  
ATOM   2252 HE21 GLN A 152      32.808  -5.945  34.612  1.00 63.25           H  
ATOM   2253  N   ILE A 153      36.760  -4.946  34.257  1.00 54.34           N  
ANISOU 2253  N   ILE A 153     4272   9317   7057  -1654   1527  -1904
ATOM   2254  CA  ILE A 153      37.165  -3.996  35.302  1.00 52.93           C  
ANISOU 2254  CA  ILE A 153     4261   8910   6939  -1771   1459  -1859
ATOM   2255  C   ILE A 153      36.851  -2.553  34.865  1.00 50.48           C  
ANISOU 2255  C   ILE A 153     4206   8228   6744  -1576   1392  -1805
ATOM   2256  O   ILE A 153      36.395  -1.767  35.691  1.00 49.72           O  
ANISOU 2256  O   ILE A 153     4156   8016   6719  -1488   1280  -1784
ATOM   2257  CB  ILE A 153      38.677  -4.147  35.646  1.00 53.56           C  
ANISOU 2257  CB  ILE A 153     4471   8926   6953  -2153   1563  -1836
ATOM   2258  CG1 ILE A 153      39.098  -5.587  36.018  1.00 55.83           C  
ANISOU 2258  CG1 ILE A 153     4518   9593   7101  -2401   1642  -1877
ATOM   2259  CG2 ILE A 153      39.140  -3.169  36.747  1.00 51.83           C  
ANISOU 2259  CG2 ILE A 153     4406   8502   6784  -2252   1499  -1817
ATOM   2260  CD1 ILE A 153      38.271  -6.249  37.125  1.00 56.32           C  
ANISOU 2260  CD1 ILE A 153     4277  10002   7121  -2413   1552  -1917
ATOM   2261  H   ILE A 153      37.493  -5.416  33.745  1.00 54.34           H  
ATOM   2262  HA  ILE A 153      36.578  -4.203  36.198  1.00 52.93           H  
ATOM   2263  HB  ILE A 153      39.247  -3.889  34.753  1.00 53.56           H  
ATOM   2264 HG13 ILE A 153      40.142  -5.586  36.330  1.00 55.83           H  
ATOM   2265 HG12 ILE A 153      39.062  -6.218  35.133  1.00 55.83           H  
ATOM   2266 HG21 ILE A 153      40.186  -3.328  37.009  1.00 51.83           H  
ATOM   2267 HG22 ILE A 153      39.057  -2.132  36.429  1.00 51.83           H  
ATOM   2268 HG23 ILE A 153      38.551  -3.280  37.654  1.00 51.83           H  
ATOM   2269 HD11 ILE A 153      38.697  -7.215  37.395  1.00 56.32           H  
ATOM   2270 HD12 ILE A 153      38.233  -5.641  38.027  1.00 56.32           H  
ATOM   2271 HD13 ILE A 153      37.250  -6.427  36.790  1.00 56.32           H  
ATOM   2272  N   MET A 154      37.038  -2.224  33.572  1.00 49.42           N  
ANISOU 2272  N   MET A 154     4228   7933   6618  -1524   1454  -1773
ATOM   2273  CA  MET A 154      36.716  -0.913  33.006  1.00 47.38           C  
ANISOU 2273  CA  MET A 154     4197   7349   6457  -1364   1386  -1705
ATOM   2274  C   MET A 154      35.203  -0.658  32.956  1.00 46.67           C  
ANISOU 2274  C   MET A 154     4047   7252   6435  -1074   1239  -1726
ATOM   2275  O   MET A 154      34.790   0.479  33.147  1.00 44.62           O  
ANISOU 2275  O   MET A 154     3912   6786   6255   -997   1140  -1672
ATOM   2276  CB  MET A 154      37.282  -0.774  31.579  1.00 46.53           C  
ANISOU 2276  CB  MET A 154     4244   7108   6329  -1354   1459  -1657
ATOM   2277  CG  MET A 154      38.810  -0.866  31.494  1.00 46.74           C  
ANISOU 2277  CG  MET A 154     4399   7051   6307  -1624   1587  -1598
ATOM   2278  SD  MET A 154      39.731   0.361  32.463  1.00 43.19           S  
ANISOU 2278  SD  MET A 154     4152   6338   5920  -1820   1612  -1529
ATOM   2279  CE  MET A 154      40.518  -0.749  33.662  1.00 45.90           C  
ANISOU 2279  CE  MET A 154     4338   6934   6169  -2102   1674  -1612
ATOM   2280  H   MET A 154      37.422  -2.923  32.950  1.00 49.42           H  
ATOM   2281  HA  MET A 154      37.167  -0.148  33.640  1.00 47.38           H  
ATOM   2282  HB3 MET A 154      36.982   0.189  31.162  1.00 46.53           H  
ATOM   2283  HB2 MET A 154      36.843  -1.530  30.927  1.00 46.53           H  
ATOM   2284  HG3 MET A 154      39.104  -0.777  30.450  1.00 46.74           H  
ATOM   2285  HG2 MET A 154      39.148  -1.850  31.794  1.00 46.74           H  
ATOM   2286  HE1 MET A 154      41.222  -0.193  34.279  1.00 45.90           H  
ATOM   2287  HE2 MET A 154      39.770  -1.207  34.306  1.00 45.90           H  
ATOM   2288  HE3 MET A 154      41.067  -1.540  33.154  1.00 45.90           H  
ATOM   2289  N   SER A 155      34.373  -1.697  32.757  1.00 48.02           N  
ANISOU 2289  N   SER A 155     4025   7654   6568   -918   1230  -1801
ATOM   2290  CA  SER A 155      32.911  -1.591  32.747  1.00 47.86           C  
ANISOU 2290  CA  SER A 155     3951   7628   6607   -630   1096  -1826
ATOM   2291  C   SER A 155      32.338  -1.363  34.159  1.00 47.83           C  
ANISOU 2291  C   SER A 155     3856   7670   6646   -631    980  -1804
ATOM   2292  O   SER A 155      31.352  -0.638  34.291  1.00 47.46           O  
ANISOU 2292  O   SER A 155     3877   7484   6673   -452    843  -1771
ATOM   2293  CB  SER A 155      32.307  -2.879  32.156  1.00 50.01           C  
ANISOU 2293  CB  SER A 155     4030   8146   6826   -449   1136  -1920
ATOM   2294  OG  SER A 155      32.480  -2.898  30.755  1.00 50.96           O  
ANISOU 2294  OG  SER A 155     4280   8176   6908   -389   1210  -1944
ATOM   2295  H   SER A 155      34.775  -2.611  32.605  1.00 48.02           H  
ATOM   2296  HA  SER A 155      32.615  -0.741  32.128  1.00 47.86           H  
ATOM   2297  HB3 SER A 155      31.234  -2.924  32.348  1.00 50.01           H  
ATOM   2298  HB2 SER A 155      32.748  -3.773  32.597  1.00 50.01           H  
ATOM   2299  HG  SER A 155      33.403  -3.007  30.575  1.00 50.96           H  
ATOM   2300  N   TRP A 156      32.978  -1.916  35.206  1.00 48.50           N  
ANISOU 2300  N   TRP A 156     3801   7952   6675   -853   1026  -1816
ATOM   2301  CA  TRP A 156      32.644  -1.668  36.613  1.00 48.57           C  
ANISOU 2301  CA  TRP A 156     3745   8006   6704   -899    915  -1789
ATOM   2302  C   TRP A 156      33.145  -0.300  37.089  1.00 46.61           C  
ANISOU 2302  C   TRP A 156     3747   7457   6505  -1005    889  -1724
ATOM   2303  O   TRP A 156      32.478   0.337  37.905  1.00 45.72           O  
ANISOU 2303  O   TRP A 156     3669   7263   6439   -925    762  -1683
ATOM   2304  CB  TRP A 156      33.311  -2.743  37.497  1.00 50.16           C  
ANISOU 2304  CB  TRP A 156     3729   8518   6810  -1137    963  -1823
ATOM   2305  CG  TRP A 156      32.740  -4.126  37.434  1.00 53.45           C  
ANISOU 2305  CG  TRP A 156     3842   9283   7184  -1002    957  -1870
ATOM   2306  CD1 TRP A 156      31.468  -4.453  37.105  1.00 54.64           C  
ANISOU 2306  CD1 TRP A 156     3881   9490   7390   -662    865  -1882
ATOM   2307  CD2 TRP A 156      33.409  -5.389  37.734  1.00 57.28           C  
ANISOU 2307  CD2 TRP A 156     4081  10125   7558  -1200   1049  -1909
ATOM   2308  NE1 TRP A 156      31.302  -5.817  37.194  1.00 58.02           N  
ANISOU 2308  NE1 TRP A 156     3996  10294   7754   -605    905  -1929
ATOM   2309  CE2 TRP A 156      32.466  -6.449  37.576  1.00 57.52           C  
ANISOU 2309  CE2 TRP A 156     3831  10440   7584   -943   1016  -1942
ATOM   2310  CE3 TRP A 156      34.716  -5.750  38.139  1.00 57.37           C  
ANISOU 2310  CE3 TRP A 156     4090  10238   7468  -1576   1159  -1916
ATOM   2311  CZ2 TRP A 156      32.799  -7.795  37.806  1.00 60.65           C  
ANISOU 2311  CZ2 TRP A 156     3916  11250   7878  -1046   1090  -1975
ATOM   2312  CZ3 TRP A 156      35.057  -7.095  38.387  1.00 58.38           C  
ANISOU 2312  CZ3 TRP A 156     3933  10759   7488  -1709   1221  -1948
ATOM   2313  CH2 TRP A 156      34.106  -8.117  38.217  1.00 62.32           C  
ANISOU 2313  CH2 TRP A 156     4122  11575   7983  -1446   1189  -1974
ATOM   2314  H   TRP A 156      33.775  -2.511  35.021  1.00 48.50           H  
ATOM   2315  HA  TRP A 156      31.561  -1.684  36.748  1.00 48.57           H  
ATOM   2316  HB3 TRP A 156      33.271  -2.451  38.547  1.00 50.16           H  
ATOM   2317  HB2 TRP A 156      34.372  -2.811  37.251  1.00 50.16           H  
ATOM   2318  HD1 TRP A 156      30.694  -3.746  36.841  1.00 54.64           H  
ATOM   2319  HE1 TRP A 156      30.415  -6.272  37.034  1.00 58.02           H  
ATOM   2320  HE3 TRP A 156      35.461  -4.981  38.280  1.00 57.37           H  
ATOM   2321  HZ2 TRP A 156      32.059  -8.571  37.679  1.00 60.65           H  
ATOM   2322  HZ3 TRP A 156      36.056  -7.345  38.715  1.00 58.38           H  
ATOM   2323  HH2 TRP A 156      34.376  -9.146  38.409  1.00 62.32           H  
ATOM   2324  N   PHE A 157      34.288   0.164  36.553  1.00 45.85           N  
ANISOU 2324  N   PHE A 157     3819   7207   6395  -1180   1013  -1709
ATOM   2325  CA  PHE A 157      34.840   1.486  36.814  1.00 45.02           C  
ANISOU 2325  CA  PHE A 157     3944   6821   6341  -1249   1013  -1648
ATOM   2326  C   PHE A 157      33.954   2.591  36.214  1.00 43.63           C  
ANISOU 2326  C   PHE A 157     3880   6449   6251  -1009    898  -1586
ATOM   2327  O   PHE A 157      33.706   3.582  36.895  1.00 42.74           O  
ANISOU 2327  O   PHE A 157     3839   6224   6175   -993    816  -1542
ATOM   2328  CB  PHE A 157      36.254   1.610  36.204  1.00 44.85           C  
ANISOU 2328  CB  PHE A 157     4087   6649   6303  -1420   1163  -1625
ATOM   2329  CG  PHE A 157      37.460   1.003  36.913  1.00 47.52           C  
ANISOU 2329  CG  PHE A 157     4409   7083   6563  -1719   1269  -1667
ATOM   2330  CD1 PHE A 157      37.394   0.501  38.230  1.00 46.80           C  
ANISOU 2330  CD1 PHE A 157     4194   7169   6421  -1849   1223  -1716
ATOM   2331  CD2 PHE A 157      38.703   1.005  36.246  1.00 48.99           C  
ANISOU 2331  CD2 PHE A 157     4725   7170   6719  -1891   1407  -1649
ATOM   2332  CE1 PHE A 157      38.565   0.047  38.871  1.00 47.01           C  
ANISOU 2332  CE1 PHE A 157     4229   7274   6360  -2152   1314  -1758
ATOM   2333  CE2 PHE A 157      39.870   0.550  36.891  1.00 49.57           C  
ANISOU 2333  CE2 PHE A 157     4819   7301   6714  -2189   1501  -1686
ATOM   2334  CZ  PHE A 157      39.801   0.071  38.209  1.00 49.24           C  
ANISOU 2334  CZ  PHE A 157     4657   7436   6615  -2328   1456  -1747
ATOM   2335  H   PHE A 157      34.796  -0.432  35.915  1.00 45.85           H  
ATOM   2336  HA  PHE A 157      34.866   1.639  37.890  1.00 45.02           H  
ATOM   2337  HB3 PHE A 157      36.485   2.666  36.150  1.00 44.85           H  
ATOM   2338  HB2 PHE A 157      36.248   1.266  35.171  1.00 44.85           H  
ATOM   2339  HD1 PHE A 157      36.462   0.474  38.769  1.00 46.80           H  
ATOM   2340  HD2 PHE A 157      38.771   1.378  35.235  1.00 48.99           H  
ATOM   2341  HE1 PHE A 157      38.534  -0.309  39.883  1.00 47.01           H  
ATOM   2342  HE2 PHE A 157      40.819   0.574  36.379  1.00 49.57           H  
ATOM   2343  HZ  PHE A 157      40.690  -0.277  38.712  1.00 49.24           H  
ATOM   2344  N   VAL A 158      33.453   2.407  34.977  1.00 43.71           N  
ANISOU 2344  N   VAL A 158     3901   6434   6273   -840    890  -1589
ATOM   2345  CA  VAL A 158      32.542   3.329  34.291  1.00 42.73           C  
ANISOU 2345  CA  VAL A 158     3906   6118   6212   -648    785  -1532
ATOM   2346  C   VAL A 158      31.188   3.391  35.004  1.00 43.10           C  
ANISOU 2346  C   VAL A 158     3882   6199   6293   -486    620  -1527
ATOM   2347  O   VAL A 158      30.705   4.492  35.246  1.00 41.74           O  
ANISOU 2347  O   VAL A 158     3832   5858   6171   -432    517  -1453
ATOM   2348  CB  VAL A 158      32.357   2.911  32.807  1.00 43.07           C  
ANISOU 2348  CB  VAL A 158     3988   6144   6234   -533    822  -1555
ATOM   2349  CG1 VAL A 158      31.225   3.658  32.070  1.00 43.64           C  
ANISOU 2349  CG1 VAL A 158     4167   6063   6351   -327    688  -1523
ATOM   2350  CG2 VAL A 158      33.645   3.114  32.011  1.00 43.14           C  
ANISOU 2350  CG2 VAL A 158     4129   6039   6222   -680    944  -1505
ATOM   2351  H   VAL A 158      33.721   1.572  34.474  1.00 43.71           H  
ATOM   2352  HA  VAL A 158      32.982   4.328  34.319  1.00 42.73           H  
ATOM   2353  HB  VAL A 158      32.125   1.846  32.789  1.00 43.07           H  
ATOM   2354 HG11 VAL A 158      31.230   3.427  31.004  1.00 43.64           H  
ATOM   2355 HG12 VAL A 158      30.238   3.389  32.447  1.00 43.64           H  
ATOM   2356 HG13 VAL A 158      31.338   4.737  32.174  1.00 43.64           H  
ATOM   2357 HG21 VAL A 158      33.634   2.495  31.117  1.00 43.14           H  
ATOM   2358 HG22 VAL A 158      33.773   4.153  31.709  1.00 43.14           H  
ATOM   2359 HG23 VAL A 158      34.519   2.836  32.595  1.00 43.14           H  
ATOM   2360  N   ASP A 159      30.588   2.236  35.346  1.00 44.54           N  
ANISOU 2360  N   ASP A 159     3862   6613   6448   -410    594  -1594
ATOM   2361  CA  ASP A 159      29.273   2.152  35.984  1.00 44.77           C  
ANISOU 2361  CA  ASP A 159     3813   6688   6510   -246    432  -1575
ATOM   2362  C   ASP A 159      29.199   2.927  37.311  1.00 43.94           C  
ANISOU 2362  C   ASP A 159     3746   6537   6412   -378    359  -1509
ATOM   2363  O   ASP A 159      28.257   3.692  37.516  1.00 43.37           O  
ANISOU 2363  O   ASP A 159     3770   6325   6382   -282    227  -1439
ATOM   2364  CB  ASP A 159      28.857   0.673  36.144  1.00 46.95           C  
ANISOU 2364  CB  ASP A 159     3830   7257   6751   -159    429  -1643
ATOM   2365  CG  ASP A 159      27.421   0.514  36.652  1.00 49.49           C  
ANISOU 2365  CG  ASP A 159     4087   7596   7121     85    255  -1614
ATOM   2366  OD1 ASP A 159      26.502   0.836  35.869  1.00 52.14           O  
ANISOU 2366  OD1 ASP A 159     4555   7749   7507    301    185  -1608
ATOM   2367  OD2 ASP A 159      27.268   0.089  37.816  1.00 50.43           O1-
ANISOU 2367  OD2 ASP A 159     4033   7907   7221     52    182  -1591
ATOM   2368  H   ASP A 159      31.048   1.366  35.115  1.00 44.54           H  
ATOM   2369  HA  ASP A 159      28.569   2.624  35.295  1.00 44.77           H  
ATOM   2370  HB3 ASP A 159      29.545   0.152  36.813  1.00 46.95           H  
ATOM   2371  HB2 ASP A 159      28.922   0.165  35.182  1.00 46.95           H  
ATOM   2372  N   GLU A 160      30.222   2.773  38.171  1.00 44.33           N  
ANISOU 2372  N   GLU A 160     3738   6699   6407   -614    448  -1532
ATOM   2373  CA  GLU A 160      30.306   3.483  39.443  1.00 43.89           C  
ANISOU 2373  CA  GLU A 160     3713   6629   6332   -754    393  -1492
ATOM   2374  C   GLU A 160      30.744   4.945  39.262  1.00 42.07           C  
ANISOU 2374  C   GLU A 160     3713   6128   6144   -788    414  -1428
ATOM   2375  O   GLU A 160      30.248   5.800  39.993  1.00 41.33           O  
ANISOU 2375  O   GLU A 160     3684   5955   6064   -766    311  -1363
ATOM   2376  CB  GLU A 160      31.291   2.747  40.377  1.00 44.98           C  
ANISOU 2376  CB  GLU A 160     3748   6957   6384  -1015    488  -1551
ATOM   2377  CG  GLU A 160      31.332   3.252  41.838  1.00 46.09           C  
ANISOU 2377  CG  GLU A 160     3873   7168   6471  -1167    415  -1533
ATOM   2378  CD  GLU A 160      30.017   3.047  42.599  1.00 49.24           C  
ANISOU 2378  CD  GLU A 160     4127   7709   6873  -1011    224  -1480
ATOM   2379  OE1 GLU A 160      29.061   3.805  42.332  1.00 52.58           O  
ANISOU 2379  OE1 GLU A 160     4602   8004   7371   -776    123  -1424
ATOM   2380  OE2 GLU A 160      29.988   2.143  43.461  1.00 52.34           O1-
ANISOU 2380  OE2 GLU A 160     4361   8335   7190  -1125    164  -1486
ATOM   2381  H   GLU A 160      30.970   2.136  37.932  1.00 44.33           H  
ATOM   2382  HA  GLU A 160      29.308   3.473  39.881  1.00 43.89           H  
ATOM   2383  HB3 GLU A 160      32.297   2.789  39.960  1.00 44.98           H  
ATOM   2384  HB2 GLU A 160      31.026   1.693  40.388  1.00 44.98           H  
ATOM   2385  HG3 GLU A 160      31.604   4.305  41.878  1.00 46.09           H  
ATOM   2386  HG2 GLU A 160      32.124   2.725  42.370  1.00 46.09           H  
ATOM   2387  N   TYR A 161      31.616   5.250  38.281  1.00 41.23           N  
ANISOU 2387  N   TYR A 161     3718   5894   6053   -833    544  -1434
ATOM   2388  CA  TYR A 161      32.040   6.615  37.968  1.00 39.71           C  
ANISOU 2388  CA  TYR A 161     3714   5470   5903   -845    571  -1361
ATOM   2389  C   TYR A 161      30.867   7.488  37.512  1.00 39.06           C  
ANISOU 2389  C   TYR A 161     3699   5273   5869   -672    418  -1277
ATOM   2390  O   TYR A 161      30.722   8.586  38.033  1.00 38.35           O  
ANISOU 2390  O   TYR A 161     3690   5091   5791   -703    375  -1210
ATOM   2391  CB  TYR A 161      33.155   6.644  36.903  1.00 38.75           C  
ANISOU 2391  CB  TYR A 161     3692   5238   5794   -888    711  -1356
ATOM   2392  CG  TYR A 161      33.596   8.055  36.549  1.00 39.10           C  
ANISOU 2392  CG  TYR A 161     3900   5071   5886   -882    732  -1263
ATOM   2393  CD1 TYR A 161      34.411   8.777  37.445  1.00 38.91           C  
ANISOU 2393  CD1 TYR A 161     3949   4977   5859  -1005    806  -1254
ATOM   2394  CD2 TYR A 161      33.106   8.682  35.383  1.00 40.23           C  
ANISOU 2394  CD2 TYR A 161     4121   5095   6068   -750    672  -1184
ATOM   2395  CE1 TYR A 161      34.703  10.130  37.197  1.00 36.46           C  
ANISOU 2395  CE1 TYR A 161     3761   4498   5593   -971    832  -1163
ATOM   2396  CE2 TYR A 161      33.387  10.039  35.145  1.00 37.31           C  
ANISOU 2396  CE2 TYR A 161     3868   4572   5738   -744    682  -1082
ATOM   2397  CZ  TYR A 161      34.180  10.766  36.054  1.00 36.25           C  
ANISOU 2397  CZ  TYR A 161     3778   4387   5609   -842    766  -1070
ATOM   2398  OH  TYR A 161      34.448  12.083  35.827  1.00 38.91           O  
ANISOU 2398  OH  TYR A 161     4203   4595   5985   -809    784   -965
ATOM   2399  H   TYR A 161      31.989   4.502  37.711  1.00 41.23           H  
ATOM   2400  HA  TYR A 161      32.443   7.051  38.885  1.00 39.71           H  
ATOM   2401  HB3 TYR A 161      32.836   6.126  35.998  1.00 38.75           H  
ATOM   2402  HB2 TYR A 161      34.026   6.108  37.275  1.00 38.75           H  
ATOM   2403  HD1 TYR A 161      34.784   8.305  38.342  1.00 38.91           H  
ATOM   2404  HD2 TYR A 161      32.472   8.140  34.696  1.00 40.23           H  
ATOM   2405  HE1 TYR A 161      35.316  10.682  37.893  1.00 36.46           H  
ATOM   2406  HE2 TYR A 161      32.990  10.525  34.266  1.00 37.31           H  
ATOM   2407  HH  TYR A 161      35.051  12.453  36.456  1.00 38.91           H  
ATOM   2408  N   VAL A 162      30.030   6.998  36.579  1.00 39.76           N  
ANISOU 2408  N   VAL A 162     3761   5369   5976   -501    343  -1287
ATOM   2409  CA  VAL A 162      28.819   7.660  36.081  1.00 39.41           C  
ANISOU 2409  CA  VAL A 162     3811   5193   5971   -348    191  -1214
ATOM   2410  C   VAL A 162      27.849   8.021  37.219  1.00 39.64           C  
ANISOU 2410  C   VAL A 162     3811   5252   5998   -335     47  -1162
ATOM   2411  O   VAL A 162      27.278   9.110  37.206  1.00 39.55           O  
ANISOU 2411  O   VAL A 162     3909   5116   6002   -335    -40  -1069
ATOM   2412  CB  VAL A 162      28.166   6.784  34.975  1.00 40.26           C  
ANISOU 2412  CB  VAL A 162     3901   5311   6086   -163    145  -1265
ATOM   2413  CG1 VAL A 162      26.727   7.197  34.595  1.00 40.50           C  
ANISOU 2413  CG1 VAL A 162     4052   5189   6148    -19    -30  -1198
ATOM   2414  CG2 VAL A 162      29.042   6.790  33.709  1.00 41.14           C  
ANISOU 2414  CG2 VAL A 162     4066   5384   6180   -188    275  -1299
ATOM   2415  H   VAL A 162      30.233   6.082  36.199  1.00 39.76           H  
ATOM   2416  HA  VAL A 162      29.128   8.602  35.627  1.00 39.41           H  
ATOM   2417  HB  VAL A 162      28.111   5.757  35.340  1.00 40.26           H  
ATOM   2418 HG11 VAL A 162      26.326   6.532  33.832  1.00 40.50           H  
ATOM   2419 HG12 VAL A 162      26.037   7.137  35.436  1.00 40.50           H  
ATOM   2420 HG13 VAL A 162      26.696   8.213  34.204  1.00 40.50           H  
ATOM   2421 HG21 VAL A 162      28.596   6.207  32.903  1.00 41.14           H  
ATOM   2422 HG22 VAL A 162      29.189   7.808  33.356  1.00 41.14           H  
ATOM   2423 HG23 VAL A 162      30.040   6.396  33.885  1.00 41.14           H  
ATOM   2424  N   LYS A 163      27.720   7.134  38.219  1.00 40.77           N  
ANISOU 2424  N   LYS A 163     3797   5583   6112   -341     20  -1213
ATOM   2425  CA  LYS A 163      26.849   7.305  39.376  1.00 41.59           C  
ANISOU 2425  CA  LYS A 163     3850   5756   6197   -348   -118  -1160
ATOM   2426  C   LYS A 163      27.335   8.408  40.332  1.00 41.14           C  
ANISOU 2426  C   LYS A 163     3876   5649   6108   -531    -85  -1109
ATOM   2427  O   LYS A 163      26.512   9.110  40.918  1.00 41.42           O  
ANISOU 2427  O   LYS A 163     3967   5636   6135   -529   -207  -1021
ATOM   2428  CB  LYS A 163      26.765   5.947  40.117  1.00 43.09           C  
ANISOU 2428  CB  LYS A 163     3825   6205   6344   -368   -120  -1225
ATOM   2429  CG  LYS A 163      25.448   5.723  40.878  1.00 43.96           C  
ANISOU 2429  CG  LYS A 163     3847   6404   6450   -254   -311  -1163
ATOM   2430  CD  LYS A 163      24.232   5.807  39.941  1.00 43.40           C  
ANISOU 2430  CD  LYS A 163     3913   6129   6447    -36   -444  -1096
ATOM   2431  CE  LYS A 163      22.936   5.234  40.508  1.00 42.77           C  
ANISOU 2431  CE  LYS A 163     3724   6129   6396    194   -574  -1090
ATOM   2432  NZ  LYS A 163      21.848   5.411  39.530  1.00 44.93           N1+
ANISOU 2432  NZ  LYS A 163     4188   6154   6729    372   -681  -1041
ATOM   2433  H   LYS A 163      28.246   6.273  38.162  1.00 40.77           H  
ATOM   2434  HA  LYS A 163      25.884   7.607  38.974  1.00 41.59           H  
ATOM   2435  HB3 LYS A 163      27.609   5.826  40.799  1.00 43.09           H  
ATOM   2436  HB2 LYS A 163      26.865   5.132  39.399  1.00 43.09           H  
ATOM   2437  HG3 LYS A 163      25.346   6.441  41.692  1.00 43.96           H  
ATOM   2438  HG2 LYS A 163      25.484   4.736  41.343  1.00 43.96           H  
ATOM   2439  HD3 LYS A 163      24.459   5.298  39.002  1.00 43.40           H  
ATOM   2440  HD2 LYS A 163      24.047   6.850  39.692  1.00 43.40           H  
ATOM   2441  HE3 LYS A 163      22.668   5.744  41.433  1.00 42.77           H  
ATOM   2442  HE2 LYS A 163      23.049   4.174  40.736  1.00 42.77           H  
ATOM   2443  HZ1 LYS A 163      22.065   4.904  38.685  1.00 44.93           H  
ATOM   2444  HZ2 LYS A 163      20.977   5.080  39.915  1.00 44.93           H  
ATOM   2445  HZ3 LYS A 163      21.767   6.400  39.306  1.00 44.93           H  
ATOM   2446  N   LEU A 164      28.660   8.592  40.441  1.00 40.99           N  
ANISOU 2446  N   LEU A 164     3873   5637   6065   -689     87  -1165
ATOM   2447  CA  LEU A 164      29.313   9.640  41.225  1.00 40.52           C  
ANISOU 2447  CA  LEU A 164     3898   5526   5972   -845    154  -1142
ATOM   2448  C   LEU A 164      29.414  10.964  40.438  1.00 39.87           C  
ANISOU 2448  C   LEU A 164     3960   5251   5938   -791    155  -1049
ATOM   2449  O   LEU A 164      29.504  12.026  41.051  1.00 40.48           O  
ANISOU 2449  O   LEU A 164     4092   5297   5992   -847    127   -986
ATOM   2450  CB  LEU A 164      30.746   9.162  41.555  1.00 40.61           C  
ANISOU 2450  CB  LEU A 164     3907   5575   5947  -1015    339  -1236
ATOM   2451  CG  LEU A 164      30.813   7.923  42.478  1.00 40.97           C  
ANISOU 2451  CG  LEU A 164     3797   5848   5923  -1121    331  -1319
ATOM   2452  CD1 LEU A 164      32.165   7.212  42.347  1.00 40.33           C  
ANISOU 2452  CD1 LEU A 164     3744   5773   5808  -1298    515  -1408
ATOM   2453  CD2 LEU A 164      30.527   8.277  43.944  1.00 42.04           C  
ANISOU 2453  CD2 LEU A 164     3891   6101   5980  -1225    238  -1303
ATOM   2454  H   LEU A 164      29.264   7.965  39.926  1.00 40.99           H  
ATOM   2455  HA  LEU A 164      28.758   9.825  42.146  1.00 40.52           H  
ATOM   2456  HB3 LEU A 164      31.313   9.970  42.017  1.00 40.61           H  
ATOM   2457  HB2 LEU A 164      31.267   8.941  40.622  1.00 40.61           H  
ATOM   2458  HG  LEU A 164      30.055   7.204  42.169  1.00 40.97           H  
ATOM   2459 HD11 LEU A 164      32.205   6.320  42.970  1.00 40.33           H  
ATOM   2460 HD12 LEU A 164      32.336   6.900  41.319  1.00 40.33           H  
ATOM   2461 HD13 LEU A 164      32.990   7.858  42.641  1.00 40.33           H  
ATOM   2462 HD21 LEU A 164      30.581   7.392  44.578  1.00 42.04           H  
ATOM   2463 HD22 LEU A 164      31.246   9.001  44.326  1.00 42.04           H  
ATOM   2464 HD23 LEU A 164      29.530   8.702  44.065  1.00 42.04           H  
ATOM   2465  N   ASN A 165      29.372  10.907  39.095  1.00 38.89           N  
ANISOU 2465  N   ASN A 165     3884   5026   5867   -686    175  -1035
ATOM   2466  CA  ASN A 165      29.501  12.024  38.153  1.00 37.54           C  
ANISOU 2466  CA  ASN A 165     3831   4699   5735   -650    183   -943
ATOM   2467  C   ASN A 165      28.117  12.620  37.794  1.00 37.71           C  
ANISOU 2467  C   ASN A 165     3910   4651   5766   -562     -2   -837
ATOM   2468  O   ASN A 165      27.947  13.201  36.723  1.00 37.74           O  
ANISOU 2468  O   ASN A 165     3998   4544   5796   -512    -30   -769
ATOM   2469  CB  ASN A 165      30.211  11.459  36.894  1.00 37.20           C  
ANISOU 2469  CB  ASN A 165     3813   4601   5721   -601    269   -972
ATOM   2470  CG  ASN A 165      30.778  12.502  35.931  1.00 36.06           C  
ANISOU 2470  CG  ASN A 165     3771   4322   5606   -597    314   -875
ATOM   2471  OD1 ASN A 165      31.443  13.447  36.349  1.00 34.47           O  
ANISOU 2471  OD1 ASN A 165     3603   4083   5411   -664    392   -826
ATOM   2472  ND2 ASN A 165      30.495  12.340  34.639  1.00 32.79           N  
ANISOU 2472  ND2 ASN A 165     3405   3848   5206   -516    272   -849
ATOM   2473  H   ASN A 165      29.298   9.987  38.681  1.00 38.89           H  
ATOM   2474  HA  ASN A 165      30.114  12.807  38.605  1.00 37.54           H  
ATOM   2475  HB3 ASN A 165      29.554  10.770  36.361  1.00 37.20           H  
ATOM   2476  HB2 ASN A 165      31.082  10.881  37.203  1.00 37.20           H  
ATOM   2477 HD22 ASN A 165      30.885  12.975  33.949  1.00 32.79           H  
ATOM   2478 HD21 ASN A 165      29.915  11.570  34.337  1.00 32.79           H  
ATOM   2479  N   GLY A 166      27.122  12.504  38.688  1.00 37.92           N  
ANISOU 2479  N   GLY A 166     3903   4741   5765   -558   -137   -812
ATOM   2480  CA  GLY A 166      25.798  13.114  38.547  1.00 37.48           C  
ANISOU 2480  CA  GLY A 166     3929   4598   5714   -498   -316   -701
ATOM   2481  C   GLY A 166      24.934  12.529  37.420  1.00 38.01           C  
ANISOU 2481  C   GLY A 166     4046   4578   5818   -345   -405   -719
ATOM   2482  O   GLY A 166      24.096  13.245  36.874  1.00 38.63           O  
ANISOU 2482  O   GLY A 166     4242   4533   5903   -306   -532   -634
ATOM   2483  H   GLY A 166      27.313  12.009  39.547  1.00 37.92           H  
ATOM   2484  HA3 GLY A 166      25.910  14.188  38.394  1.00 37.48           H  
ATOM   2485  HA2 GLY A 166      25.263  12.988  39.487  1.00 37.48           H  
ATOM   2486  N   GLU A 167      25.183  11.260  37.045  1.00 38.57           N  
ANISOU 2486  N   GLU A 167     4036   4718   5903   -270   -333   -835
ATOM   2487  CA  GLU A 167      24.499  10.471  36.011  1.00 39.45           C  
ANISOU 2487  CA  GLU A 167     4175   4777   6038    -99   -394   -888
ATOM   2488  C   GLU A 167      24.982  10.754  34.579  1.00 39.21           C  
ANISOU 2488  C   GLU A 167     4255   4629   6014    -90   -334   -888
ATOM   2489  O   GLU A 167      24.486  10.129  33.640  1.00 40.45           O  
ANISOU 2489  O   GLU A 167     4476   4719   6176     38   -378   -937
ATOM   2490  CB  GLU A 167      22.954  10.460  36.143  1.00 40.04           C  
ANISOU 2490  CB  GLU A 167     4330   4759   6123     18   -602   -824
ATOM   2491  CG  GLU A 167      22.397  10.053  37.525  1.00 42.09           C  
ANISOU 2491  CG  GLU A 167     4479   5141   6373     38   -696   -806
ATOM   2492  CD  GLU A 167      22.480   8.557  37.853  1.00 48.31           C  
ANISOU 2492  CD  GLU A 167     5101   6081   7174    180   -670   -913
ATOM   2493  OE1 GLU A 167      23.110   7.796  37.088  1.00 46.76           O  
ANISOU 2493  OE1 GLU A 167     4860   5919   6987    250   -551  -1020
ATOM   2494  OE2 GLU A 167      21.884   8.187  38.887  1.00 51.69           O1-
ANISOU 2494  OE2 GLU A 167     5430   6618   7593    220   -777   -879
ATOM   2495  H   GLU A 167      25.922  10.775  37.535  1.00 38.57           H  
ATOM   2496  HA  GLU A 167      24.836   9.452  36.196  1.00 39.45           H  
ATOM   2497  HB3 GLU A 167      22.527   9.799  35.387  1.00 40.04           H  
ATOM   2498  HB2 GLU A 167      22.561  11.446  35.892  1.00 40.04           H  
ATOM   2499  HG3 GLU A 167      21.343  10.327  37.561  1.00 42.09           H  
ATOM   2500  HG2 GLU A 167      22.878  10.616  38.323  1.00 42.09           H  
ATOM   2501  N   ARG A 168      25.946  11.673  34.402  1.00 38.17           N  
ANISOU 2501  N   ARG A 168     4154   4473   5878   -219   -238   -830
ATOM   2502  CA  ARG A 168      26.511  12.044  33.108  1.00 37.36           C  
ANISOU 2502  CA  ARG A 168     4145   4278   5772   -227   -190   -803
ATOM   2503  C   ARG A 168      27.442  10.924  32.637  1.00 37.27           C  
ANISOU 2503  C   ARG A 168     4068   4339   5753   -210    -41   -913
ATOM   2504  O   ARG A 168      28.417  10.584  33.314  1.00 37.35           O  
ANISOU 2504  O   ARG A 168     3988   4439   5765   -289     90   -952
ATOM   2505  CB  ARG A 168      27.296  13.359  33.257  1.00 36.39           C  
ANISOU 2505  CB  ARG A 168     4054   4120   5651   -347   -141   -684
ATOM   2506  CG  ARG A 168      26.373  14.568  33.482  1.00 35.44           C  
ANISOU 2506  CG  ARG A 168     3986   3959   5522   -390   -279   -564
ATOM   2507  CD  ARG A 168      27.144  15.857  33.803  1.00 35.30           C  
ANISOU 2507  CD  ARG A 168     3945   3960   5505   -491   -191   -464
ATOM   2508  NE  ARG A 168      27.077  16.170  35.238  1.00 39.48           N  
ANISOU 2508  NE  ARG A 168     4424   4559   6019   -549   -209   -443
ATOM   2509  CZ  ARG A 168      28.091  16.128  36.121  1.00 42.44           C  
ANISOU 2509  CZ  ARG A 168     4726   5009   6393   -603    -66   -496
ATOM   2510  NH1 ARG A 168      29.332  15.783  35.754  1.00 35.35           N  
ANISOU 2510  NH1 ARG A 168     3806   4106   5519   -605    102   -562
ATOM   2511  NH2 ARG A 168      27.849  16.436  37.401  1.00 43.72           N1+
ANISOU 2511  NH2 ARG A 168     4852   5243   6516   -668    -94   -485
ATOM   2512  H   ARG A 168      26.321  12.133  35.220  1.00 38.17           H  
ATOM   2513  HA  ARG A 168      25.706  12.185  32.382  1.00 37.36           H  
ATOM   2514  HB3 ARG A 168      27.899  13.539  32.366  1.00 36.39           H  
ATOM   2515  HB2 ARG A 168      28.000  13.280  34.086  1.00 36.39           H  
ATOM   2516  HG3 ARG A 168      25.667  14.353  34.284  1.00 35.44           H  
ATOM   2517  HG2 ARG A 168      25.767  14.723  32.588  1.00 35.44           H  
ATOM   2518  HD3 ARG A 168      26.669  16.689  33.280  1.00 35.30           H  
ATOM   2519  HD2 ARG A 168      28.168  15.818  33.433  1.00 35.30           H  
ATOM   2520  HE  ARG A 168      26.162  16.424  35.580  1.00 39.48           H  
ATOM   2521 HH12 ARG A 168      30.077  15.705  36.432  1.00 35.35           H  
ATOM   2522 HH11 ARG A 168      29.519  15.524  34.795  1.00 35.35           H  
ATOM   2523 HH22 ARG A 168      28.594  16.400  38.083  1.00 43.72           H  
ATOM   2524 HH21 ARG A 168      26.919  16.691  37.700  1.00 43.72           H  
ATOM   2525  N   MET A 169      27.096  10.337  31.481  1.00 37.56           N  
ANISOU 2525  N   MET A 169     4162   4338   5772   -117    -60   -967
ATOM   2526  CA  MET A 169      27.766   9.192  30.880  1.00 38.16           C  
ANISOU 2526  CA  MET A 169     4172   4506   5823    -99     77  -1074
ATOM   2527  C   MET A 169      28.971   9.660  30.054  1.00 37.51           C  
ANISOU 2527  C   MET A 169     4135   4395   5723   -212    195  -1019
ATOM   2528  O   MET A 169      28.991   9.563  28.827  1.00 38.27           O  
ANISOU 2528  O   MET A 169     4317   4444   5780   -196    197  -1016
ATOM   2529  CB  MET A 169      26.748   8.402  30.029  1.00 39.47           C  
ANISOU 2529  CB  MET A 169     4376   4659   5962     63     22  -1174
ATOM   2530  CG  MET A 169      25.779   7.603  30.914  1.00 40.34           C  
ANISOU 2530  CG  MET A 169     4385   4844   6099    199    -53  -1239
ATOM   2531  SD  MET A 169      24.682   6.459  30.036  1.00 42.37           S  
ANISOU 2531  SD  MET A 169     4696   5061   6342    441   -115  -1356
ATOM   2532  CE  MET A 169      25.821   5.074  29.761  1.00 42.34           C  
ANISOU 2532  CE  MET A 169     4509   5291   6289    442     94  -1492
ATOM   2533  H   MET A 169      26.278  10.687  31.001  1.00 37.56           H  
ATOM   2534  HA  MET A 169      28.143   8.529  31.654  1.00 38.16           H  
ATOM   2535  HB3 MET A 169      27.269   7.697  29.385  1.00 39.47           H  
ATOM   2536  HB2 MET A 169      26.194   9.067  29.364  1.00 39.47           H  
ATOM   2537  HG3 MET A 169      25.153   8.293  31.482  1.00 40.34           H  
ATOM   2538  HG2 MET A 169      26.341   7.022  31.644  1.00 40.34           H  
ATOM   2539  HE1 MET A 169      25.306   4.264  29.247  1.00 42.34           H  
ATOM   2540  HE2 MET A 169      26.667   5.384  29.148  1.00 42.34           H  
ATOM   2541  HE3 MET A 169      26.201   4.694  30.710  1.00 42.34           H  
ATOM   2542  N   ASP A 170      30.000  10.135  30.775  1.00 36.76           N  
ANISOU 2542  N   ASP A 170     3995   4320   5652   -323    288   -970
ATOM   2543  CA  ASP A 170      31.333  10.467  30.276  1.00 36.34           C  
ANISOU 2543  CA  ASP A 170     3972   4241   5595   -414    417   -916
ATOM   2544  C   ASP A 170      32.145   9.161  30.272  1.00 37.06           C  
ANISOU 2544  C   ASP A 170     3992   4438   5650   -452    554  -1022
ATOM   2545  O   ASP A 170      33.102   8.992  31.029  1.00 36.64           O  
ANISOU 2545  O   ASP A 170     3890   4426   5605   -553    673  -1043
ATOM   2546  CB  ASP A 170      32.005  11.520  31.203  1.00 35.23           C  
ANISOU 2546  CB  ASP A 170     3828   4061   5497   -496    475   -836
ATOM   2547  CG  ASP A 170      31.245  12.841  31.384  1.00 37.22           C  
ANISOU 2547  CG  ASP A 170     4123   4250   5770   -476    353   -728
ATOM   2548  OD1 ASP A 170      30.290  13.097  30.617  1.00 39.27           O  
ANISOU 2548  OD1 ASP A 170     4444   4467   6011   -423    218   -689
ATOM   2549  OD2 ASP A 170      31.632  13.579  32.316  1.00 38.71           O1-
ANISOU 2549  OD2 ASP A 170     4292   4433   5985   -526    396   -685
ATOM   2550  H   ASP A 170      29.866  10.211  31.774  1.00 36.76           H  
ATOM   2551  HA  ASP A 170      31.275  10.861  29.259  1.00 36.34           H  
ATOM   2552  HB3 ASP A 170      32.999  11.763  30.826  1.00 35.23           H  
ATOM   2553  HB2 ASP A 170      32.148  11.101  32.200  1.00 35.23           H  
ATOM   2554  N   ILE A 171      31.722   8.208  29.427  1.00 37.49           N  
ANISOU 2554  N   ILE A 171     4049   4540   5655   -381    541  -1093
ATOM   2555  CA  ILE A 171      32.259   6.851  29.319  1.00 38.81           C  
ANISOU 2555  CA  ILE A 171     4119   4852   5775   -413    663  -1201
ATOM   2556  C   ILE A 171      33.680   6.810  28.719  1.00 38.71           C  
ANISOU 2556  C   ILE A 171     4138   4835   5736   -556    807  -1153
ATOM   2557  O   ILE A 171      34.355   5.793  28.843  1.00 39.61           O  
ANISOU 2557  O   ILE A 171     4168   5063   5820   -645    918  -1217
ATOM   2558  CB  ILE A 171      31.261   5.972  28.515  1.00 40.06           C  
ANISOU 2558  CB  ILE A 171     4253   5088   5879   -279    630  -1310
ATOM   2559  CG1 ILE A 171      31.009   6.475  27.072  1.00 39.27           C  
ANISOU 2559  CG1 ILE A 171     4306   4885   5732   -252    590  -1268
ATOM   2560  CG2 ILE A 171      29.937   5.812  29.286  1.00 40.39           C  
ANISOU 2560  CG2 ILE A 171     4252   5133   5963   -135    498  -1355
ATOM   2561  CD1 ILE A 171      30.163   5.516  26.228  1.00 42.32           C  
ANISOU 2561  CD1 ILE A 171     4705   5312   6064   -102    554  -1394
ATOM   2562  H   ILE A 171      30.918   8.426  28.852  1.00 37.49           H  
ATOM   2563  HA  ILE A 171      32.342   6.442  30.328  1.00 38.81           H  
ATOM   2564  HB  ILE A 171      31.697   4.975  28.451  1.00 40.06           H  
ATOM   2565 HG13 ILE A 171      31.960   6.618  26.565  1.00 39.27           H  
ATOM   2566 HG12 ILE A 171      30.528   7.453  27.089  1.00 39.27           H  
ATOM   2567 HG21 ILE A 171      29.327   5.006  28.878  1.00 40.39           H  
ATOM   2568 HG22 ILE A 171      30.109   5.578  30.336  1.00 40.39           H  
ATOM   2569 HG23 ILE A 171      29.347   6.726  29.253  1.00 40.39           H  
ATOM   2570 HD11 ILE A 171      30.096   5.866  25.201  1.00 42.32           H  
ATOM   2571 HD12 ILE A 171      30.598   4.518  26.218  1.00 42.32           H  
ATOM   2572 HD13 ILE A 171      29.145   5.436  26.606  1.00 42.32           H  
ATOM   2573  N   GLY A 172      34.156   7.938  28.162  1.00 38.38           N  
ANISOU 2573  N   GLY A 172     4214   4665   5703   -583    797  -1026
ATOM   2574  CA  GLY A 172      35.541   8.192  27.785  1.00 38.87           C  
ANISOU 2574  CA  GLY A 172     4325   4681   5761   -703    917   -941
ATOM   2575  C   GLY A 172      36.480   8.441  28.973  1.00 38.78           C  
ANISOU 2575  C   GLY A 172     4307   4614   5813   -789   1000   -917
ATOM   2576  O   GLY A 172      37.682   8.554  28.766  1.00 38.69           O  
ANISOU 2576  O   GLY A 172     4371   4505   5823   -857   1084   -821
ATOM   2577  H   GLY A 172      33.527   8.726  28.109  1.00 38.38           H  
ATOM   2578  HA3 GLY A 172      35.570   9.063  27.131  1.00 38.87           H  
ATOM   2579  HA2 GLY A 172      35.932   7.352  27.212  1.00 38.87           H  
ATOM   2580  N   THR A 173      35.982   8.475  30.223  1.00 38.51           N  
ANISOU 2580  N   THR A 173     4194   4636   5802   -784    975  -1001
ATOM   2581  CA  THR A 173      36.819   8.528  31.432  1.00 38.60           C  
ANISOU 2581  CA  THR A 173     4212   4609   5846   -888   1063  -1011
ATOM   2582  C   THR A 173      37.613   7.217  31.616  1.00 39.59           C  
ANISOU 2582  C   THR A 173     4291   4838   5915  -1032   1185  -1099
ATOM   2583  O   THR A 173      38.631   7.217  32.300  1.00 40.05           O  
ANISOU 2583  O   THR A 173     4400   4838   5980  -1163   1288  -1104
ATOM   2584  CB  THR A 173      35.938   8.801  32.676  1.00 38.63           C  
ANISOU 2584  CB  THR A 173     4155   4647   5875   -854    979  -1056
ATOM   2585  OG1 THR A 173      35.298  10.050  32.512  1.00 37.08           O  
ANISOU 2585  OG1 THR A 173     4004   4367   5719   -743    862   -963
ATOM   2586  CG2 THR A 173      36.738   8.891  33.990  1.00 37.59           C  
ANISOU 2586  CG2 THR A 173     4051   4474   5756   -980   1079  -1083
ATOM   2587  H   THR A 173      34.982   8.394  30.349  1.00 38.51           H  
ATOM   2588  HA  THR A 173      37.540   9.340  31.323  1.00 38.60           H  
ATOM   2589  HB  THR A 173      35.167   8.036  32.778  1.00 38.63           H  
ATOM   2590  HG1 THR A 173      34.638   9.962  31.837  1.00 37.08           H  
ATOM   2591 HG21 THR A 173      36.134   9.272  34.809  1.00 37.59           H  
ATOM   2592 HG22 THR A 173      37.116   7.921  34.307  1.00 37.59           H  
ATOM   2593 HG23 THR A 173      37.601   9.543  33.878  1.00 37.59           H  
ATOM   2594  N   PHE A 174      37.177   6.119  30.981  1.00 40.14           N  
ANISOU 2594  N   PHE A 174     4270   5062   5920  -1014   1178  -1170
ATOM   2595  CA  PHE A 174      37.877   4.844  30.935  1.00 41.50           C  
ANISOU 2595  CA  PHE A 174     4376   5373   6017  -1164   1293  -1241
ATOM   2596  C   PHE A 174      37.905   4.374  29.491  1.00 42.01           C  
ANISOU 2596  C   PHE A 174     4446   5501   6016  -1136   1318  -1230
ATOM   2597  O   PHE A 174      36.868   4.351  28.834  1.00 41.73           O  
ANISOU 2597  O   PHE A 174     4376   5515   5966   -982   1233  -1261
ATOM   2598  CB  PHE A 174      37.189   3.817  31.843  1.00 42.07           C  
ANISOU 2598  CB  PHE A 174     4264   5669   6052  -1176   1269  -1368
ATOM   2599  CG  PHE A 174      37.172   4.228  33.300  1.00 42.35           C  
ANISOU 2599  CG  PHE A 174     4285   5684   6123  -1232   1240  -1388
ATOM   2600  CD1 PHE A 174      36.122   5.017  33.809  1.00 42.14           C  
ANISOU 2600  CD1 PHE A 174     4246   5616   6150  -1089   1110  -1374
ATOM   2601  CD2 PHE A 174      38.255   3.885  34.128  1.00 43.26           C  
ANISOU 2601  CD2 PHE A 174     4421   5810   6207  -1448   1342  -1418
ATOM   2602  CE1 PHE A 174      36.179   5.494  35.131  1.00 42.67           C  
ANISOU 2602  CE1 PHE A 174     4306   5675   6231  -1158   1086  -1390
ATOM   2603  CE2 PHE A 174      38.310   4.364  35.450  1.00 42.83           C  
ANISOU 2603  CE2 PHE A 174     4374   5734   6167  -1518   1320  -1447
ATOM   2604  CZ  PHE A 174      37.276   5.177  35.952  1.00 41.57           C  
ANISOU 2604  CZ  PHE A 174     4186   5555   6053  -1371   1195  -1433
ATOM   2605  H   PHE A 174      36.344   6.196  30.416  1.00 40.14           H  
ATOM   2606  HA  PHE A 174      38.901   4.974  31.275  1.00 41.50           H  
ATOM   2607  HB3 PHE A 174      37.689   2.850  31.759  1.00 42.07           H  
ATOM   2608  HB2 PHE A 174      36.176   3.661  31.486  1.00 42.07           H  
ATOM   2609  HD1 PHE A 174      35.292   5.300  33.177  1.00 42.14           H  
ATOM   2610  HD2 PHE A 174      39.049   3.269  33.737  1.00 43.26           H  
ATOM   2611  HE1 PHE A 174      35.391   6.128  35.500  1.00 42.67           H  
ATOM   2612  HE2 PHE A 174      39.143   4.091  36.077  1.00 42.83           H  
ATOM   2613  HZ  PHE A 174      37.317   5.544  36.967  1.00 41.57           H  
ATOM   2614  N   THR A 175      39.082   3.967  29.014  1.00 42.67           N  
ANISOU 2614  N   THR A 175     4588   5573   6050  -1292   1435  -1189
ATOM   2615  CA  THR A 175      39.267   3.289  27.735  1.00 43.56           C  
ANISOU 2615  CA  THR A 175     4701   5779   6073  -1301   1473  -1181
ATOM   2616  C   THR A 175      39.545   1.802  28.008  1.00 45.23           C  
ANISOU 2616  C   THR A 175     4764   6237   6186  -1429   1567  -1290
ATOM   2617  O   THR A 175      39.509   1.356  29.154  1.00 45.81           O  
ANISOU 2617  O   THR A 175     4733   6408   6266  -1509   1586  -1363
ATOM   2618  CB  THR A 175      40.442   3.948  26.993  1.00 43.44           C  
ANISOU 2618  CB  THR A 175     4855   5597   6054  -1375   1519  -1027
ATOM   2619  OG1 THR A 175      41.605   3.762  27.765  1.00 45.37           O  
ANISOU 2619  OG1 THR A 175     5169   5755   6313  -1555   1623   -987
ATOM   2620  CG2 THR A 175      40.200   5.434  26.682  1.00 41.96           C  
ANISOU 2620  CG2 THR A 175     4775   5211   5957  -1235   1417   -908
ATOM   2621  H   THR A 175      39.895   4.024  29.614  1.00 42.67           H  
ATOM   2622  HA  THR A 175      38.373   3.375  27.120  1.00 43.56           H  
ATOM   2623  HB  THR A 175      40.604   3.442  26.039  1.00 43.44           H  
ATOM   2624  HG1 THR A 175      42.342   4.145  27.305  1.00 45.37           H  
ATOM   2625 HG21 THR A 175      41.065   5.883  26.200  1.00 41.96           H  
ATOM   2626 HG22 THR A 175      39.349   5.555  26.010  1.00 41.96           H  
ATOM   2627 HG23 THR A 175      39.994   6.012  27.580  1.00 41.96           H  
ATOM   2628  N   GLY A 176      39.783   1.030  26.939  1.00 46.12           N  
ANISOU 2628  N   GLY A 176     4857   6474   6194  -1458   1624  -1301
ATOM   2629  CA  GLY A 176      39.951  -0.416  26.974  1.00 47.46           C  
ANISOU 2629  CA  GLY A 176     4857   6925   6249  -1571   1721  -1402
ATOM   2630  C   GLY A 176      38.655  -1.171  27.286  1.00 47.44           C  
ANISOU 2630  C   GLY A 176     4652   7133   6242  -1391   1669  -1544
ATOM   2631  O   GLY A 176      38.710  -2.323  27.711  1.00 49.67           O  
ANISOU 2631  O   GLY A 176     4740   7673   6458  -1461   1731  -1632
ATOM   2632  H   GLY A 176      39.751   1.456  26.021  1.00 46.12           H  
ATOM   2633  HA3 GLY A 176      40.718  -0.686  27.691  1.00 47.46           H  
ATOM   2634  HA2 GLY A 176      40.313  -0.734  25.999  1.00 47.46           H  
ATOM   2635  N   LYS A 177      37.501  -0.510  27.088  1.00 45.91           N  
ANISOU 2635  N   LYS A 177     4501   6826   6115  -1159   1550  -1557
ATOM   2636  CA  LYS A 177      36.163  -1.048  27.297  1.00 46.40           C  
ANISOU 2636  CA  LYS A 177     4411   7039   6178   -944   1490  -1680
ATOM   2637  C   LYS A 177      35.809  -1.987  26.127  1.00 48.07           C  
ANISOU 2637  C   LYS A 177     4550   7445   6269   -868   1567  -1775
ATOM   2638  O   LYS A 177      36.336  -1.802  25.027  1.00 48.43           O  
ANISOU 2638  O   LYS A 177     4718   7448   6235   -943   1623  -1730
ATOM   2639  CB  LYS A 177      35.138   0.110  27.278  1.00 44.92           C  
ANISOU 2639  CB  LYS A 177     4345   6632   6090   -744   1337  -1649
ATOM   2640  CG  LYS A 177      35.393   1.200  28.333  1.00 43.67           C  
ANISOU 2640  CG  LYS A 177     4254   6300   6039   -798   1266  -1563
ATOM   2641  CD  LYS A 177      34.293   2.276  28.393  1.00 43.55           C  
ANISOU 2641  CD  LYS A 177     4314   6129   6104   -611   1113  -1542
ATOM   2642  CE  LYS A 177      34.038   3.034  27.081  1.00 44.60           C  
ANISOU 2642  CE  LYS A 177     4640   6072   6232   -573   1066  -1455
ATOM   2643  NZ  LYS A 177      35.235   3.747  26.614  1.00 40.72           N1+
ANISOU 2643  NZ  LYS A 177     4270   5436   5766   -727   1111  -1317
ATOM   2644  H   LYS A 177      37.556   0.423  26.699  1.00 45.91           H  
ATOM   2645  HA  LYS A 177      36.145  -1.551  28.263  1.00 46.40           H  
ATOM   2646  HB3 LYS A 177      34.136  -0.292  27.435  1.00 44.92           H  
ATOM   2647  HB2 LYS A 177      35.119   0.560  26.285  1.00 44.92           H  
ATOM   2648  HG3 LYS A 177      36.356   1.677  28.155  1.00 43.67           H  
ATOM   2649  HG2 LYS A 177      35.472   0.732  29.316  1.00 43.67           H  
ATOM   2650  HD3 LYS A 177      34.556   3.000  29.163  1.00 43.55           H  
ATOM   2651  HD2 LYS A 177      33.359   1.814  28.715  1.00 43.55           H  
ATOM   2652  HE3 LYS A 177      33.240   3.761  27.222  1.00 44.60           H  
ATOM   2653  HE2 LYS A 177      33.703   2.354  26.305  1.00 44.60           H  
ATOM   2654  HZ1 LYS A 177      35.921   3.078  26.278  1.00 40.72           H  
ATOM   2655  HZ2 LYS A 177      34.999   4.383  25.864  1.00 40.72           H  
ATOM   2656  HZ3 LYS A 177      35.634   4.271  27.384  1.00 40.72           H  
ATOM   2657  N   PRO A 178      34.897  -2.965  26.325  1.00 49.42           N  
ANISOU 2657  N   PRO A 178     4519   7837   6419   -706   1570  -1903
ATOM   2658  CA  PRO A 178      34.329  -3.783  25.242  1.00 51.12           C  
ANISOU 2658  CA  PRO A 178     4677   8215   6532   -557   1636  -2019
ATOM   2659  C   PRO A 178      33.598  -2.898  24.216  1.00 50.51           C  
ANISOU 2659  C   PRO A 178     4831   7901   6459   -404   1555  -2016
ATOM   2660  O   PRO A 178      32.985  -1.904  24.606  1.00 49.26           O  
ANISOU 2660  O   PRO A 178     4796   7511   6411   -305   1414  -1964
ATOM   2661  CB  PRO A 178      33.302  -4.709  25.921  1.00 52.29           C  
ANISOU 2661  CB  PRO A 178     4593   8556   6717   -341   1603  -2131
ATOM   2662  CG  PRO A 178      33.601  -4.656  27.410  1.00 51.82           C  
ANISOU 2662  CG  PRO A 178     4390   8594   6704   -516   1595  -2076
ATOM   2663  CD  PRO A 178      34.380  -3.365  27.629  1.00 49.84           C  
ANISOU 2663  CD  PRO A 178     4368   8039   6529   -675   1530  -1944
ATOM   2664  HA  PRO A 178      35.127  -4.361  24.775  1.00 51.12           H  
ATOM   2665  HB3 PRO A 178      33.359  -5.727  25.532  1.00 52.29           H  
ATOM   2666  HB2 PRO A 178      32.277  -4.367  25.763  1.00 52.29           H  
ATOM   2667  HG3 PRO A 178      34.235  -5.503  27.677  1.00 51.82           H  
ATOM   2668  HG2 PRO A 178      32.701  -4.712  28.024  1.00 51.82           H  
ATOM   2669  HD2 PRO A 178      33.716  -2.586  28.005  1.00 49.84           H  
ATOM   2670  HD3 PRO A 178      35.174  -3.510  28.354  1.00 49.84           H  
ATOM   2671  N   VAL A 179      33.613  -3.278  22.926  1.00 51.73           N  
ANISOU 2671  N   VAL A 179     5048   8127   6482   -407   1641  -2069
ATOM   2672  CA  VAL A 179      32.811  -2.703  21.832  1.00 51.41           C  
ANISOU 2672  CA  VAL A 179     5215   7901   6417   -255   1565  -2101
ATOM   2673  C   VAL A 179      31.308  -2.644  22.173  1.00 51.82           C  
ANISOU 2673  C   VAL A 179     5247   7881   6560     37   1456  -2202
ATOM   2674  O   VAL A 179      30.639  -1.667  21.835  1.00 51.01           O  
ANISOU 2674  O   VAL A 179     5335   7525   6522    121   1317  -2161
ATOM   2675  CB  VAL A 179      33.111  -3.467  20.509  1.00 53.32           C  
ANISOU 2675  CB  VAL A 179     5500   8288   6473   -271   1690  -2194
ATOM   2676  CG1 VAL A 179      32.046  -3.311  19.403  1.00 52.77           C  
ANISOU 2676  CG1 VAL A 179     5584   8095   6372    -38   1625  -2314
ATOM   2677  CG2 VAL A 179      34.481  -3.065  19.940  1.00 52.74           C  
ANISOU 2677  CG2 VAL A 179     5580   8145   6315   -533   1720  -2046
ATOM   2678  H   VAL A 179      34.179  -4.091  22.688  1.00 51.73           H  
ATOM   2679  HA  VAL A 179      33.129  -1.668  21.705  1.00 51.41           H  
ATOM   2680  HB  VAL A 179      33.153  -4.532  20.742  1.00 53.32           H  
ATOM   2681 HG11 VAL A 179      32.341  -3.855  18.508  1.00 52.77           H  
ATOM   2682 HG12 VAL A 179      31.077  -3.716  19.697  1.00 52.77           H  
ATOM   2683 HG13 VAL A 179      31.908  -2.266  19.123  1.00 52.77           H  
ATOM   2684 HG21 VAL A 179      34.740  -3.672  19.072  1.00 52.74           H  
ATOM   2685 HG22 VAL A 179      34.477  -2.022  19.624  1.00 52.74           H  
ATOM   2686 HG23 VAL A 179      35.278  -3.188  20.672  1.00 52.74           H  
ATOM   2687  N   ALA A 180      30.818  -3.657  22.907  1.00 53.75           N  
ANISOU 2687  N   ALA A 180     5258   8355   6810    185   1513  -2318
ATOM   2688  CA  ALA A 180      29.467  -3.768  23.451  1.00 54.76           C  
ANISOU 2688  CA  ALA A 180     5356   8417   7034    480   1406  -2396
ATOM   2689  C   ALA A 180      29.098  -2.684  24.487  1.00 53.34           C  
ANISOU 2689  C   ALA A 180     5270   7990   7006    479   1224  -2273
ATOM   2690  O   ALA A 180      27.920  -2.557  24.817  1.00 54.14           O  
ANISOU 2690  O   ALA A 180     5433   7954   7184    697   1102  -2303
ATOM   2691  CB  ALA A 180      29.332  -5.158  24.094  1.00 56.77           C  
ANISOU 2691  CB  ALA A 180     5296   8992   7281    614   1491  -2497
ATOM   2692  H   ALA A 180      31.456  -4.409  23.132  1.00 53.75           H  
ATOM   2693  HA  ALA A 180      28.762  -3.693  22.621  1.00 54.76           H  
ATOM   2694  HB1 ALA A 180      28.323  -5.322  24.476  1.00 56.77           H  
ATOM   2695  HB2 ALA A 180      29.535  -5.946  23.368  1.00 56.77           H  
ATOM   2696  HB3 ALA A 180      30.027  -5.286  24.924  1.00 56.77           H  
ATOM   2697  N   PHE A 181      30.073  -1.898  24.979  1.00 51.83           N  
ANISOU 2697  N   PHE A 181     5096   7742   6854    237   1209  -2133
ATOM   2698  CA  PHE A 181      29.881  -0.794  25.913  1.00 50.03           C  
ANISOU 2698  CA  PHE A 181     4949   7309   6753    226   1057  -2023
ATOM   2699  C   PHE A 181      30.833   0.379  25.635  1.00 48.21           C  
ANISOU 2699  C   PHE A 181     4905   6878   6535     14   1034  -1874
ATOM   2700  O   PHE A 181      31.596   0.792  26.509  1.00 47.10           O  
ANISOU 2700  O   PHE A 181     4744   6693   6457   -132   1020  -1774
ATOM   2701  CB  PHE A 181      29.841  -1.309  27.371  1.00 49.95           C  
ANISOU 2701  CB  PHE A 181     4712   7459   6808    212   1042  -2014
ATOM   2702  CG  PHE A 181      29.424  -0.278  28.406  1.00 49.53           C  
ANISOU 2702  CG  PHE A 181     4732   7216   6871    231    880  -1917
ATOM   2703  CD1 PHE A 181      28.234   0.466  28.235  1.00 50.91           C  
ANISOU 2703  CD1 PHE A 181     5067   7174   7102    416    730  -1906
ATOM   2704  CD2 PHE A 181      30.226  -0.056  29.545  1.00 47.70           C  
ANISOU 2704  CD2 PHE A 181     4425   7020   6677     48    878  -1841
ATOM   2705  CE1 PHE A 181      27.864   1.442  29.181  1.00 47.87           C  
ANISOU 2705  CE1 PHE A 181     4746   6633   6808    412    582  -1806
ATOM   2706  CE2 PHE A 181      29.842   0.903  30.501  1.00 46.98           C  
ANISOU 2706  CE2 PHE A 181     4401   6776   6674     55    740  -1756
ATOM   2707  CZ  PHE A 181      28.669   1.660  30.315  1.00 46.23           C  
ANISOU 2707  CZ  PHE A 181     4445   6489   6632    235    592  -1733
ATOM   2708  H   PHE A 181      31.020  -2.059  24.658  1.00 51.83           H  
ATOM   2709  HA  PHE A 181      28.897  -0.378  25.692  1.00 50.03           H  
ATOM   2710  HB3 PHE A 181      30.814  -1.726  27.637  1.00 49.95           H  
ATOM   2711  HB2 PHE A 181      29.133  -2.135  27.446  1.00 49.95           H  
ATOM   2712  HD1 PHE A 181      27.599   0.301  27.378  1.00 50.91           H  
ATOM   2713  HD2 PHE A 181      31.135  -0.622  29.693  1.00 47.70           H  
ATOM   2714  HE1 PHE A 181      26.959   2.014  29.042  1.00 47.87           H  
ATOM   2715  HE2 PHE A 181      30.452   1.052  31.379  1.00 46.98           H  
ATOM   2716  HZ  PHE A 181      28.381   2.400  31.047  1.00 46.23           H  
ATOM   2717  N   GLY A 182      30.772   0.928  24.410  1.00 47.91           N  
ANISOU 2717  N   GLY A 182     5051   6724   6431      6   1030  -1862
ATOM   2718  CA  GLY A 182      31.453   2.163  24.019  1.00 46.38           C  
ANISOU 2718  CA  GLY A 182     5032   6337   6254   -146    978  -1706
ATOM   2719  C   GLY A 182      32.945   2.020  23.702  1.00 46.09           C  
ANISOU 2719  C   GLY A 182     4973   6362   6175   -372   1099  -1617
ATOM   2720  O   GLY A 182      33.648   3.027  23.643  1.00 44.91           O  
ANISOU 2720  O   GLY A 182     4922   6066   6073   -489   1067  -1469
ATOM   2721  H   GLY A 182      30.152   0.511  23.730  1.00 47.91           H  
ATOM   2722  HA3 GLY A 182      31.334   2.913  24.800  1.00 46.38           H  
ATOM   2723  HA2 GLY A 182      30.956   2.559  23.134  1.00 46.38           H  
ATOM   2724  N   GLY A 183      33.432   0.786  23.510  1.00 47.53           N  
ANISOU 2724  N   GLY A 183     5025   6766   6268   -430   1240  -1701
ATOM   2725  CA  GLY A 183      34.779   0.481  23.052  1.00 47.40           C  
ANISOU 2725  CA  GLY A 183     5023   6803   6184   -656   1358  -1616
ATOM   2726  C   GLY A 183      34.961   0.754  21.557  1.00 47.50           C  
ANISOU 2726  C   GLY A 183     5187   6779   6081   -674   1364  -1593
ATOM   2727  O   GLY A 183      33.994   1.017  20.839  1.00 47.77           O  
ANISOU 2727  O   GLY A 183     5332   6710   6108   -539   1266  -1627
ATOM   2728  H   GLY A 183      32.804   0.003  23.628  1.00 47.53           H  
ATOM   2729  HA3 GLY A 183      34.981  -0.574  23.224  1.00 47.40           H  
ATOM   2730  HA2 GLY A 183      35.508   1.040  23.633  1.00 47.40           H  
ATOM   2731  N   SER A 184      36.216   0.681  21.097  1.00 47.92           N  
ANISOU 2731  N   SER A 184     5252   6924   6032   -857   1476  -1537
ATOM   2732  CA  SER A 184      36.594   0.870  19.700  1.00 47.76           C  
ANISOU 2732  CA  SER A 184     5384   6871   5892   -930   1478  -1471
ATOM   2733  C   SER A 184      36.870  -0.484  19.034  1.00 50.60           C  
ANISOU 2733  C   SER A 184     5679   7475   6074  -1037   1631  -1546
ATOM   2734  O   SER A 184      37.365  -1.419  19.667  1.00 52.08           O  
ANISOU 2734  O   SER A 184     5714   7838   6235  -1138   1749  -1580
ATOM   2735  CB  SER A 184      37.877   1.723  19.667  1.00 46.11           C  
ANISOU 2735  CB  SER A 184     5300   6479   5741  -1073   1435  -1248
ATOM   2736  OG  SER A 184      38.347   1.971  18.355  1.00 44.26           O  
ANISOU 2736  OG  SER A 184     5161   6285   5370  -1215   1481  -1155
ATOM   2737  H   SER A 184      36.954   0.455  21.748  1.00 47.92           H  
ATOM   2738  HA  SER A 184      35.810   1.395  19.149  1.00 47.76           H  
ATOM   2739  HB3 SER A 184      38.679   1.262  20.246  1.00 46.11           H  
ATOM   2740  HB2 SER A 184      37.670   2.690  20.117  1.00 46.11           H  
ATOM   2741  HG  SER A 184      38.615   1.148  17.966  1.00 44.26           H  
ATOM   2742  N   GLU A 185      36.617  -0.527  17.717  1.00 51.92           N  
ANISOU 2742  N   GLU A 185     5963   7663   6099  -1032   1628  -1570
ATOM   2743  CA  GLU A 185      37.039  -1.575  16.792  1.00 53.61           C  
ANISOU 2743  CA  GLU A 185     6146   8108   6116  -1146   1769  -1629
ATOM   2744  C   GLU A 185      38.565  -1.547  16.607  1.00 53.76           C  
ANISOU 2744  C   GLU A 185     6203   8124   6099  -1407   1823  -1433
ATOM   2745  O   GLU A 185      39.210  -0.534  16.878  1.00 52.04           O  
ANISOU 2745  O   GLU A 185     6093   7689   5992  -1464   1731  -1248
ATOM   2746  CB  GLU A 185      36.375  -1.300  15.425  1.00 54.19           C  
ANISOU 2746  CB  GLU A 185     6387   8157   6044  -1100   1726  -1679
ATOM   2747  CG  GLU A 185      34.842  -1.468  15.407  1.00 54.49           C  
ANISOU 2747  CG  GLU A 185     6442   8157   6104   -844   1674  -1875
ATOM   2748  CD  GLU A 185      34.370  -2.902  15.653  1.00 57.50           C  
ANISOU 2748  CD  GLU A 185     6638   8790   6419   -713   1821  -2095
ATOM   2749  OE1 GLU A 185      35.107  -3.835  15.267  1.00 60.10           O  
ANISOU 2749  OE1 GLU A 185     6876   9368   6590   -841   1978  -2131
ATOM   2750  OE2 GLU A 185      33.262  -3.036  16.213  1.00 59.10           O1-
ANISOU 2750  OE2 GLU A 185     6780   8952   6724   -477   1777  -2223
ATOM   2751  H   GLU A 185      36.192   0.288  17.299  1.00 51.92           H  
ATOM   2752  HA  GLU A 185      36.745  -2.550  17.184  1.00 53.61           H  
ATOM   2753  HB3 GLU A 185      36.802  -1.961  14.671  1.00 54.19           H  
ATOM   2754  HB2 GLU A 185      36.618  -0.290  15.091  1.00 54.19           H  
ATOM   2755  HG3 GLU A 185      34.457  -1.166  14.435  1.00 54.49           H  
ATOM   2756  HG2 GLU A 185      34.380  -0.805  16.139  1.00 54.49           H  
ATOM   2757  N   GLY A 186      39.136  -2.673  16.155  1.00 55.50           N  
ANISOU 2757  N   GLY A 186     6340   8587   6160  -1561   1973  -1468
ATOM   2758  CA  GLY A 186      40.561  -2.839  15.871  1.00 56.26           C  
ANISOU 2758  CA  GLY A 186     6507   8680   6187  -1825   2025  -1276
ATOM   2759  C   GLY A 186      41.484  -2.874  17.102  1.00 56.54           C  
ANISOU 2759  C   GLY A 186     6463   8678   6343  -1950   2069  -1199
ATOM   2760  O   GLY A 186      42.699  -2.822  16.926  1.00 57.66           O  
ANISOU 2760  O   GLY A 186     6678   8784   6446  -2173   2115  -1036
ATOM   2761  H   GLY A 186      38.535  -3.460  15.953  1.00 55.50           H  
ATOM   2762  HA3 GLY A 186      40.889  -2.042  15.202  1.00 56.26           H  
ATOM   2763  HA2 GLY A 186      40.690  -3.772  15.322  1.00 56.26           H  
ATOM   2764  N   ARG A 187      40.924  -2.938  18.325  1.00 56.01           N  
ANISOU 2764  N   ARG A 187     6259   8616   6409  -1817   2052  -1315
ATOM   2765  CA  ARG A 187      41.619  -2.823  19.610  1.00 55.85           C  
ANISOU 2765  CA  ARG A 187     6170   8547   6503  -1929   2079  -1268
ATOM   2766  C   ARG A 187      42.537  -4.019  19.916  1.00 57.81           C  
ANISOU 2766  C   ARG A 187     6305   9034   6625  -2183   2230  -1274
ATOM   2767  O   ARG A 187      43.666  -3.812  20.363  1.00 57.96           O  
ANISOU 2767  O   ARG A 187     6424   8948   6648  -2408   2264  -1124
ATOM   2768  CB  ARG A 187      40.557  -2.668  20.723  1.00 55.23           C  
ANISOU 2768  CB  ARG A 187     5942   8495   6548  -1728   2027  -1415
ATOM   2769  CG  ARG A 187      41.130  -2.428  22.138  1.00 56.06           C  
ANISOU 2769  CG  ARG A 187     6028   8476   6797  -1799   2003  -1363
ATOM   2770  CD  ARG A 187      40.047  -2.349  23.220  1.00 58.88           C  
ANISOU 2770  CD  ARG A 187     6244   8864   7263  -1588   1928  -1494
ATOM   2771  NE  ARG A 187      39.600  -3.693  23.619  1.00 57.00           N  
ANISOU 2771  NE  ARG A 187     5757   8956   6945  -1584   2014  -1643
ATOM   2772  CZ  ARG A 187      38.414  -4.252  23.334  1.00 59.37           C  
ANISOU 2772  CZ  ARG A 187     5921   9396   7242  -1342   1988  -1790
ATOM   2773  NH1 ARG A 187      37.471  -3.590  22.654  1.00 57.32           N  
ANISOU 2773  NH1 ARG A 187     5774   8947   7056  -1105   1868  -1812
ATOM   2774  NH2 ARG A 187      38.170  -5.511  23.719  1.00 61.10           N1+
ANISOU 2774  NH2 ARG A 187     5888   9944   7381  -1337   2080  -1909
ATOM   2775  H   ARG A 187      39.915  -2.977  18.362  1.00 56.01           H  
ATOM   2776  HA  ARG A 187      42.238  -1.927  19.592  1.00 55.85           H  
ATOM   2777  HB3 ARG A 187      39.915  -3.549  20.737  1.00 55.23           H  
ATOM   2778  HB2 ARG A 187      39.905  -1.829  20.474  1.00 55.23           H  
ATOM   2779  HG3 ARG A 187      41.708  -1.504  22.139  1.00 56.06           H  
ATOM   2780  HG2 ARG A 187      41.832  -3.217  22.411  1.00 56.06           H  
ATOM   2781  HD3 ARG A 187      39.220  -1.705  22.919  1.00 58.88           H  
ATOM   2782  HD2 ARG A 187      40.481  -1.890  24.106  1.00 58.88           H  
ATOM   2783  HE  ARG A 187      40.273  -4.241  24.137  1.00 57.00           H  
ATOM   2784 HH12 ARG A 187      36.597  -4.078  22.439  1.00 57.32           H  
ATOM   2785 HH11 ARG A 187      37.611  -2.643  22.339  1.00 57.32           H  
ATOM   2786 HH22 ARG A 187      37.310  -5.973  23.433  1.00 61.10           H  
ATOM   2787 HH21 ARG A 187      38.860  -6.041  24.232  1.00 61.10           H  
ATOM   2788  N   ASN A 188      42.063  -5.255  19.686  1.00 59.43           N  
ANISOU 2788  N   ASN A 188     6301   9564   6717  -2141   2322  -1447
ATOM   2789  CA  ASN A 188      42.768  -6.493  20.035  1.00 61.56           C  
ANISOU 2789  CA  ASN A 188     6408  10121   6864  -2377   2464  -1472
ATOM   2790  C   ASN A 188      44.024  -6.708  19.166  1.00 62.84           C  
ANISOU 2790  C   ASN A 188     6709  10290   6877  -2671   2540  -1313
ATOM   2791  O   ASN A 188      45.033  -7.201  19.671  1.00 64.24           O  
ANISOU 2791  O   ASN A 188     6881  10500   7028  -2939   2604  -1229
ATOM   2792  CB  ASN A 188      41.786  -7.675  19.852  1.00 63.30           C  
ANISOU 2792  CB  ASN A 188     6361  10718   6971  -2238   2556  -1682
ATOM   2793  CG  ASN A 188      42.307  -8.990  20.443  1.00 67.38           C  
ANISOU 2793  CG  ASN A 188     6646  11581   7375  -2477   2694  -1713
ATOM   2794  OD1 ASN A 188      42.545  -9.084  21.644  1.00 68.45           O  
ANISOU 2794  OD1 ASN A 188     6698  11708   7602  -2586   2674  -1689
ATOM   2795  ND2 ASN A 188      42.516 -10.001  19.596  1.00 68.26           N  
ANISOU 2795  ND2 ASN A 188     6654  12012   7269  -2584   2836  -1762
ATOM   2796  H   ASN A 188      41.132  -5.343  19.303  1.00 59.43           H  
ATOM   2797  HA  ASN A 188      43.071  -6.425  21.082  1.00 61.56           H  
ATOM   2798  HB3 ASN A 188      41.534  -7.808  18.798  1.00 63.30           H  
ATOM   2799  HB2 ASN A 188      40.846  -7.449  20.359  1.00 63.30           H  
ATOM   2800 HD22 ASN A 188      42.866 -10.877  19.953  1.00 68.26           H  
ATOM   2801 HD21 ASN A 188      42.325  -9.889  18.611  1.00 68.26           H  
ATOM   2802  N   GLU A 189      43.967  -6.316  17.885  1.00 62.69           N  
ANISOU 2802  N   GLU A 189     6831  10232   6755  -2638   2525  -1262
ATOM   2803  CA  GLU A 189      45.044  -6.454  16.906  1.00 63.85           C  
ANISOU 2803  CA  GLU A 189     7109  10406   6744  -2916   2588  -1097
ATOM   2804  C   GLU A 189      45.804  -5.133  16.681  1.00 62.38           C  
ANISOU 2804  C   GLU A 189     7196   9848   6658  -2950   2472   -863
ATOM   2805  O   GLU A 189      46.625  -5.065  15.766  1.00 63.56           O  
ANISOU 2805  O   GLU A 189     7485   9988   6677  -3108   2483   -710
ATOM   2806  CB  GLU A 189      44.436  -6.905  15.559  1.00 65.49           C  
ANISOU 2806  CB  GLU A 189     7283  10882   6719  -2908   2667  -1183
ATOM   2807  CG  GLU A 189      43.455  -8.092  15.673  1.00 66.24           C  
ANISOU 2807  CG  GLU A 189     7121  11310   6737  -2736   2763  -1444
ATOM   2808  CD  GLU A 189      43.131  -8.766  14.337  1.00 68.45           C  
ANISOU 2808  CD  GLU A 189     7412  11809   6787  -2697   2843  -1546
ATOM   2809  OE1 GLU A 189      43.711  -8.368  13.302  1.00 68.16           O  
ANISOU 2809  OE1 GLU A 189     7579  11686   6634  -2833   2815  -1405
ATOM   2810  OE2 GLU A 189      42.315  -9.711  14.371  1.00 71.21           O1-
ANISOU 2810  OE2 GLU A 189     7567  12422   7068  -2520   2934  -1768
ATOM   2811  H   GLU A 189      43.105  -5.904  17.556  1.00 62.69           H  
ATOM   2812  HA  GLU A 189      45.764  -7.207  17.235  1.00 63.85           H  
ATOM   2813  HB3 GLU A 189      45.257  -7.169  14.890  1.00 65.49           H  
ATOM   2814  HB2 GLU A 189      43.911  -6.074  15.084  1.00 65.49           H  
ATOM   2815  HG3 GLU A 189      42.518  -7.768  16.126  1.00 66.24           H  
ATOM   2816  HG2 GLU A 189      43.874  -8.848  16.336  1.00 66.24           H  
ATOM   2817  N   ALA A 190      45.539  -4.094  17.495  1.00 60.17           N  
ANISOU 2817  N   ALA A 190     6980   9281   6600  -2802   2362   -826
ATOM   2818  CA  ALA A 190      46.048  -2.728  17.360  1.00 58.95           C  
ANISOU 2818  CA  ALA A 190     7055   8785   6560  -2778   2250   -609
ATOM   2819  C   ALA A 190      47.578  -2.637  17.404  1.00 60.35           C  
ANISOU 2819  C   ALA A 190     7385   8831   6713  -3046   2297   -391
ATOM   2820  O   ALA A 190      48.180  -2.046  16.510  1.00 61.17           O  
ANISOU 2820  O   ALA A 190     7647   8846   6748  -3121   2263   -200
ATOM   2821  CB  ALA A 190      45.457  -1.866  18.481  1.00 55.88           C  
ANISOU 2821  CB  ALA A 190     6677   8152   6403  -2564   2144   -631
ATOM   2822  H   ALA A 190      44.856  -4.244  18.224  1.00 60.17           H  
ATOM   2823  HA  ALA A 190      45.707  -2.336  16.400  1.00 58.95           H  
ATOM   2824  HB1 ALA A 190      45.816  -0.844  18.419  1.00 55.88           H  
ATOM   2825  HB2 ALA A 190      44.373  -1.816  18.432  1.00 55.88           H  
ATOM   2826  HB3 ALA A 190      45.717  -2.258  19.464  1.00 55.88           H  
ATOM   2827  N   THR A 191      48.204  -3.254  18.421  1.00 60.86           N  
ANISOU 2827  N   THR A 191     7411   8884   6829  -3197   2369   -415
ATOM   2828  CA  THR A 191      49.653  -3.265  18.625  1.00 62.69           C  
ANISOU 2828  CA  THR A 191     7822   8935   7061  -3446   2410   -220
ATOM   2829  C   THR A 191      50.354  -4.059  17.510  1.00 65.30           C  
ANISOU 2829  C   THR A 191     8195   9454   7161  -3689   2482   -113
ATOM   2830  O   THR A 191      51.394  -3.622  17.026  1.00 66.64           O  
ANISOU 2830  O   THR A 191     8570   9435   7314  -3779   2447    118
ATOM   2831  CB  THR A 191      49.972  -3.891  20.006  1.00 63.43           C  
ANISOU 2831  CB  THR A 191     7860   9025   7215  -3603   2481   -304
ATOM   2832  OG1 THR A 191      49.353  -3.120  21.015  1.00 61.46           O  
ANISOU 2832  OG1 THR A 191     7505   8717   7129  -3371   2421   -454
ATOM   2833  CG2 THR A 191      51.475  -3.916  20.333  1.00 65.03           C  
ANISOU 2833  CG2 THR A 191     8317   8900   7491  -3785   2493   -108
ATOM   2834  H   THR A 191      47.638  -3.711  19.122  1.00 60.86           H  
ATOM   2835  HA  THR A 191      50.017  -2.236  18.601  1.00 62.69           H  
ATOM   2836  HB  THR A 191      49.571  -4.904  20.066  1.00 63.43           H  
ATOM   2837  HG1 THR A 191      49.565  -3.497  21.856  1.00 61.46           H  
ATOM   2838 HG21 THR A 191      51.657  -4.204  21.369  1.00 65.03           H  
ATOM   2839 HG22 THR A 191      52.017  -4.621  19.704  1.00 65.03           H  
ATOM   2840 HG23 THR A 191      51.916  -2.935  20.176  1.00 65.03           H  
ATOM   2841  N   GLY A 192      49.759  -5.180  17.070  1.00 66.29           N  
ANISOU 2841  N   GLY A 192     8120   9964   7103  -3785   2582   -273
ATOM   2842  CA  GLY A 192      50.265  -6.027  15.996  1.00 68.25           C  
ANISOU 2842  CA  GLY A 192     8379  10452   7102  -4008   2661   -201
ATOM   2843  C   GLY A 192      50.256  -5.349  14.621  1.00 68.12           C  
ANISOU 2843  C   GLY A 192     8508  10360   7016  -3919   2577    -66
ATOM   2844  O   GLY A 192      51.218  -5.486  13.866  1.00 69.99           O  
ANISOU 2844  O   GLY A 192     8895  10575   7124  -4132   2587    140
ATOM   2845  H   GLY A 192      48.883  -5.450  17.493  1.00 66.29           H  
ATOM   2846  HA3 GLY A 192      49.642  -6.914  15.941  1.00 68.25           H  
ATOM   2847  HA2 GLY A 192      51.268  -6.359  16.248  1.00 68.25           H  
ATOM   2848  N   PHE A 193      49.200  -4.570  14.334  1.00 66.02           N  
ANISOU 2848  N   PHE A 193     8202  10059   6824  -3622   2487   -173
ATOM   2849  CA  PHE A 193      49.080  -3.699  13.165  1.00 65.49           C  
ANISOU 2849  CA  PHE A 193     8280   9893   6711  -3528   2376    -40
ATOM   2850  C   PHE A 193      50.119  -2.568  13.216  1.00 64.74           C  
ANISOU 2850  C   PHE A 193     8404   9437   6759  -3558   2276    254
ATOM   2851  O   PHE A 193      50.723  -2.255  12.193  1.00 65.95           O  
ANISOU 2851  O   PHE A 193     8698   9557   6805  -3659   2229    466
ATOM   2852  CB  PHE A 193      47.642  -3.128  13.113  1.00 63.17           C  
ANISOU 2852  CB  PHE A 193     7916   9595   6491  -3218   2288   -215
ATOM   2853  CG  PHE A 193      47.303  -2.314  11.872  1.00 63.25           C  
ANISOU 2853  CG  PHE A 193     8059   9556   6416  -3154   2173   -104
ATOM   2854  CD1 PHE A 193      47.682  -0.959  11.778  1.00 60.93           C  
ANISOU 2854  CD1 PHE A 193     7911   8966   6276  -3065   2024    115
ATOM   2855  CD2 PHE A 193      46.599  -2.908  10.804  1.00 64.72           C  
ANISOU 2855  CD2 PHE A 193     8220  10007   6362  -3181   2213   -223
ATOM   2856  CE1 PHE A 193      47.382  -0.215  10.624  1.00 59.98           C  
ANISOU 2856  CE1 PHE A 193     7894   8830   6067  -3027   1904    230
ATOM   2857  CE2 PHE A 193      46.319  -2.171   9.637  1.00 64.28           C  
ANISOU 2857  CE2 PHE A 193     8300   9914   6209  -3151   2096   -125
ATOM   2858  CZ  PHE A 193      46.713  -0.824   9.545  1.00 61.70           C  
ANISOU 2858  CZ  PHE A 193     8103   9306   6035  -3085   1933    111
ATOM   2859  H   PHE A 193      48.445  -4.529  15.007  1.00 66.02           H  
ATOM   2860  HA  PHE A 193      49.265  -4.293  12.269  1.00 65.49           H  
ATOM   2861  HB3 PHE A 193      47.449  -2.508  13.989  1.00 63.17           H  
ATOM   2862  HB2 PHE A 193      46.929  -3.950  13.178  1.00 63.17           H  
ATOM   2863  HD1 PHE A 193      48.210  -0.484  12.593  1.00 60.93           H  
ATOM   2864  HD2 PHE A 193      46.263  -3.930  10.879  1.00 64.72           H  
ATOM   2865  HE1 PHE A 193      47.674   0.822  10.566  1.00 59.98           H  
ATOM   2866  HE2 PHE A 193      45.785  -2.635   8.821  1.00 64.28           H  
ATOM   2867  HZ  PHE A 193      46.489  -0.252   8.656  1.00 61.70           H  
ATOM   2868  N   GLY A 194      50.347  -1.988  14.408  1.00 63.15           N  
ANISOU 2868  N   GLY A 194     8229   8978   6789  -3468   2251    267
ATOM   2869  CA  GLY A 194      51.295  -0.908  14.646  1.00 63.40           C  
ANISOU 2869  CA  GLY A 194     8462   8652   6975  -3462   2179    527
ATOM   2870  C   GLY A 194      52.752  -1.309  14.398  1.00 66.28           C  
ANISOU 2870  C   GLY A 194     8987   8970   7225  -3751   2234    751
ATOM   2871  O   GLY A 194      53.464  -0.577  13.716  1.00 67.43           O  
ANISOU 2871  O   GLY A 194     9286   8993   7340  -3771   2159   1003
ATOM   2872  H   GLY A 194      49.800  -2.298  15.200  1.00 63.15           H  
ATOM   2873  HA3 GLY A 194      51.197  -0.573  15.680  1.00 63.40           H  
ATOM   2874  HA2 GLY A 194      51.029  -0.064  14.008  1.00 63.40           H  
ATOM   2875  N   VAL A 195      53.165  -2.495  14.881  1.00 67.67           N  
ANISOU 2875  N   VAL A 195     9123   9258   7331  -3987   2359    669
ATOM   2876  CA  VAL A 195      54.481  -3.106  14.655  1.00 70.31           C  
ANISOU 2876  CA  VAL A 195     9606   9568   7539  -4311   2426    859
ATOM   2877  C   VAL A 195      54.741  -3.348  13.159  1.00 72.09           C  
ANISOU 2877  C   VAL A 195     9882   9976   7532  -4437   2405   1014
ATOM   2878  O   VAL A 195      55.825  -3.028  12.687  1.00 73.87           O  
ANISOU 2878  O   VAL A 195    10316  10013   7737  -4553   2360   1298
ATOM   2879  CB  VAL A 195      54.596  -4.422  15.474  1.00 71.78           C  
ANISOU 2879  CB  VAL A 195     9653  10010   7612  -4562   2568    682
ATOM   2880  CG1 VAL A 195      55.834  -5.284  15.132  1.00 74.48           C  
ANISOU 2880  CG1 VAL A 195    10141  10342   7814  -4919   2636    861
ATOM   2881  CG2 VAL A 195      54.577  -4.180  16.995  1.00 70.61           C  
ANISOU 2881  CG2 VAL A 195     9484   9695   7649  -4506   2584    566
ATOM   2882  H   VAL A 195      52.509  -3.024  15.439  1.00 67.67           H  
ATOM   2883  HA  VAL A 195      55.244  -2.410  15.009  1.00 70.31           H  
ATOM   2884  HB  VAL A 195      53.713  -5.010  15.228  1.00 71.78           H  
ATOM   2885 HG11 VAL A 195      55.898  -6.152  15.786  1.00 74.48           H  
ATOM   2886 HG12 VAL A 195      55.804  -5.667  14.112  1.00 74.48           H  
ATOM   2887 HG13 VAL A 195      56.758  -4.716  15.251  1.00 74.48           H  
ATOM   2888 HG21 VAL A 195      54.383  -5.106  17.537  1.00 70.61           H  
ATOM   2889 HG22 VAL A 195      55.531  -3.795  17.350  1.00 70.61           H  
ATOM   2890 HG23 VAL A 195      53.824  -3.459  17.298  1.00 70.61           H  
ATOM   2891  N   ALA A 196      53.755  -3.878  12.414  1.00 71.73           N  
ANISOU 2891  N   ALA A 196     9653  10297   7305  -4415   2443    827
ATOM   2892  CA  ALA A 196      53.873  -4.207  10.992  1.00 73.16           C  
ANISOU 2892  CA  ALA A 196     9868  10700   7229  -4546   2437    931
ATOM   2893  C   ALA A 196      54.002  -2.969  10.086  1.00 72.48           C  
ANISOU 2893  C   ALA A 196     9951  10388   7201  -4409   2273   1181
ATOM   2894  O   ALA A 196      54.754  -3.016   9.112  1.00 74.83           O  
ANISOU 2894  O   ALA A 196    10391  10690   7351  -4589   2239   1431
ATOM   2895  CB  ALA A 196      52.638  -5.003  10.577  1.00 72.89           C  
ANISOU 2895  CB  ALA A 196     9618  11057   7019  -4476   2507    646
ATOM   2896  H   ALA A 196      52.879  -4.100  12.867  1.00 71.73           H  
ATOM   2897  HA  ALA A 196      54.757  -4.833  10.851  1.00 73.16           H  
ATOM   2898  HB1 ALA A 196      52.666  -5.242   9.514  1.00 72.89           H  
ATOM   2899  HB2 ALA A 196      52.578  -5.943  11.126  1.00 72.89           H  
ATOM   2900  HB3 ALA A 196      51.725  -4.439  10.770  1.00 72.89           H  
ATOM   2901  N   VAL A 197      53.322  -1.858  10.432  1.00 69.51           N  
ANISOU 2901  N   VAL A 197     9550   9830   7030  -4102   2166   1130
ATOM   2902  CA  VAL A 197      53.460  -0.548   9.784  1.00 68.83           C  
ANISOU 2902  CA  VAL A 197     9590   9543   7018  -3960   2004   1374
ATOM   2903  C   VAL A 197      54.858   0.039  10.053  1.00 69.94           C  
ANISOU 2903  C   VAL A 197     9931   9362   7282  -4035   1972   1688
ATOM   2904  O   VAL A 197      55.487   0.543   9.122  1.00 71.18           O  
ANISOU 2904  O   VAL A 197    10218   9457   7369  -4087   1879   1976
ATOM   2905  CB  VAL A 197      52.332   0.408  10.281  1.00 66.00           C  
ANISOU 2905  CB  VAL A 197     9154   9048   6874  -3631   1906   1256
ATOM   2906  CG1 VAL A 197      52.559   1.896   9.933  1.00 64.89           C  
ANISOU 2906  CG1 VAL A 197     9135   8643   6876  -3483   1750   1549
ATOM   2907  CG2 VAL A 197      50.958  -0.016   9.732  1.00 66.43           C  
ANISOU 2907  CG2 VAL A 197     9075   9379   6789  -3543   1895   1011
ATOM   2908  H   VAL A 197      52.710  -1.910  11.235  1.00 69.51           H  
ATOM   2909  HA  VAL A 197      53.356  -0.682   8.706  1.00 68.83           H  
ATOM   2910  HB  VAL A 197      52.285   0.339  11.369  1.00 66.00           H  
ATOM   2911 HG11 VAL A 197      51.685   2.493  10.191  1.00 64.89           H  
ATOM   2912 HG12 VAL A 197      53.402   2.323  10.476  1.00 64.89           H  
ATOM   2913 HG13 VAL A 197      52.740   2.031   8.867  1.00 64.89           H  
ATOM   2914 HG21 VAL A 197      50.160   0.557  10.203  1.00 66.43           H  
ATOM   2915 HG22 VAL A 197      50.894   0.156   8.659  1.00 66.43           H  
ATOM   2916 HG23 VAL A 197      50.750  -1.071   9.905  1.00 66.43           H  
ATOM   2917  N   VAL A 198      55.344  -0.046  11.306  1.00 69.53           N  
ANISOU 2917  N   VAL A 198     9910   9101   7406  -4039   2048   1634
ATOM   2918  CA  VAL A 198      56.668   0.422  11.725  1.00 70.66           C  
ANISOU 2918  CA  VAL A 198    10272   8878   7699  -4073   2031   1899
ATOM   2919  C   VAL A 198      57.790  -0.373  11.033  1.00 73.98           C  
ANISOU 2919  C   VAL A 198    10845   9343   7920  -4405   2074   2117
ATOM   2920  O   VAL A 198      58.691   0.257  10.490  1.00 75.73           O  
ANISOU 2920  O   VAL A 198    11263   9325   8184  -4418   2002   2431
ATOM   2921  CB  VAL A 198      56.787   0.422  13.275  1.00 69.50           C  
ANISOU 2921  CB  VAL A 198    10142   8497   7767  -4016   2108   1756
ATOM   2922  CG1 VAL A 198      58.222   0.714  13.766  1.00 71.22           C  
ANISOU 2922  CG1 VAL A 198    10624   8342   8096  -4108   2124   2006
ATOM   2923  CG2 VAL A 198      55.819   1.439  13.918  1.00 67.04           C  
ANISOU 2923  CG2 VAL A 198     9722   8078   7673  -3668   2039   1623
ATOM   2924  H   VAL A 198      54.760  -0.465  12.017  1.00 69.53           H  
ATOM   2925  HA  VAL A 198      56.769   1.451  11.386  1.00 70.66           H  
ATOM   2926  HB  VAL A 198      56.507  -0.567  13.637  1.00 69.50           H  
ATOM   2927 HG11 VAL A 198      58.252   0.887  14.837  1.00 71.22           H  
ATOM   2928 HG12 VAL A 198      58.903  -0.114  13.561  1.00 71.22           H  
ATOM   2929 HG13 VAL A 198      58.627   1.607  13.290  1.00 71.22           H  
ATOM   2930 HG21 VAL A 198      55.556   1.151  14.934  1.00 67.04           H  
ATOM   2931 HG22 VAL A 198      56.261   2.433  13.967  1.00 67.04           H  
ATOM   2932 HG23 VAL A 198      54.880   1.531  13.372  1.00 67.04           H  
ATOM   2933  N   VAL A 199      57.709  -1.718  10.991  1.00 75.20           N  
ANISOU 2933  N   VAL A 199    10899   9823   7851  -4667   2190   1956
ATOM   2934  CA  VAL A 199      58.622  -2.628  10.281  1.00 78.37           C  
ANISOU 2934  CA  VAL A 199    11418  10340   8017  -5022   2240   2141
ATOM   2935  C   VAL A 199      58.811  -2.240   8.803  1.00 79.65           C  
ANISOU 2935  C   VAL A 199    11660  10582   8023  -5036   2123   2399
ATOM   2936  O   VAL A 199      59.949  -2.152   8.349  1.00 82.18           O  
ANISOU 2936  O   VAL A 199    12191  10724   8310  -5179   2074   2722
ATOM   2937  CB  VAL A 199      58.167  -4.107  10.474  1.00 79.11           C  
ANISOU 2937  CB  VAL A 199    11330  10851   7879  -5275   2394   1890
ATOM   2938  CG1 VAL A 199      58.777  -5.114   9.475  1.00 82.45           C  
ANISOU 2938  CG1 VAL A 199    11857  11445   8024  -5654   2444   2087
ATOM   2939  CG2 VAL A 199      58.460  -4.608  11.899  1.00 79.25           C  
ANISOU 2939  CG2 VAL A 199    11290  10793   8031  -5328   2497   1698
ATOM   2940  H   VAL A 199      56.937  -2.152  11.480  1.00 75.20           H  
ATOM   2941  HA  VAL A 199      59.602  -2.517  10.750  1.00 78.37           H  
ATOM   2942  HB  VAL A 199      57.087  -4.138  10.331  1.00 79.11           H  
ATOM   2943 HG11 VAL A 199      58.484  -6.135   9.721  1.00 82.45           H  
ATOM   2944 HG12 VAL A 199      58.437  -4.933   8.455  1.00 82.45           H  
ATOM   2945 HG13 VAL A 199      59.866  -5.073   9.482  1.00 82.45           H  
ATOM   2946 HG21 VAL A 199      57.915  -5.529  12.111  1.00 79.25           H  
ATOM   2947 HG22 VAL A 199      59.521  -4.823  12.021  1.00 79.25           H  
ATOM   2948 HG23 VAL A 199      58.192  -3.882  12.664  1.00 79.25           H  
ATOM   2949  N   ARG A 200      57.705  -1.981   8.079  1.00 97.74           N  
ANISOU 2949  N   ARG A 200    14827  12865   9445  -7768   1991   -883
ATOM   2950  CA  ARG A 200      57.713  -1.610   6.666  1.00101.33           C  
ANISOU 2950  CA  ARG A 200    14844  13716   9943  -7159   1659  -1564
ATOM   2951  C   ARG A 200      58.374  -0.250   6.409  1.00102.69           C  
ANISOU 2951  C   ARG A 200    15083  13934  10003  -6863   1785  -1443
ATOM   2952  O   ARG A 200      59.198  -0.152   5.503  1.00104.91           O  
ANISOU 2952  O   ARG A 200    15455  14807   9599  -6306   1804  -1608
ATOM   2953  CB  ARG A 200      56.273  -1.626   6.110  1.00105.15           C  
ANISOU 2953  CB  ARG A 200    14517  13957  11479  -7066   1086  -2320
ATOM   2954  CG  ARG A 200      56.158  -1.137   4.650  1.00111.45           C  
ANISOU 2954  CG  ARG A 200    14811  15182  12352  -6435    528  -3287
ATOM   2955  CD  ARG A 200      54.842  -1.541   3.979  1.00119.29           C  
ANISOU 2955  CD  ARG A 200    15176  15839  14309  -6251   -203  -4329
ATOM   2956  NE  ARG A 200      53.780  -0.583   4.297  1.00123.29           N  
ANISOU 2956  NE  ARG A 200    15120  15226  16499  -6836   -470  -4234
ATOM   2957  CZ  ARG A 200      52.613  -0.458   3.645  1.00131.64           C  
ANISOU 2957  CZ  ARG A 200    15548  15542  18928  -6819  -1241  -5155
ATOM   2958  NH1 ARG A 200      52.291  -1.260   2.620  1.00136.92           N  
ANISOU 2958  NH1 ARG A 200    16166  16574  19282  -6088  -1880  -6485
ATOM   2959  NH2 ARG A 200      51.757   0.490   4.034  1.00135.95           N1+
ANISOU 2959  NH2 ARG A 200    15482  14973  21199  -7459  -1386  -4706
ATOM   2960  H   ARG A 200      56.805  -2.070   8.531  1.00 97.74           H  
ATOM   2961  HA  ARG A 200      58.297  -2.362   6.135  1.00101.33           H  
ATOM   2962  HB3 ARG A 200      55.615  -1.027   6.742  1.00105.15           H  
ATOM   2963  HB2 ARG A 200      55.898  -2.648   6.184  1.00105.15           H  
ATOM   2964  HG3 ARG A 200      56.985  -1.529   4.059  1.00111.45           H  
ATOM   2965  HG2 ARG A 200      56.267  -0.053   4.610  1.00111.45           H  
ATOM   2966  HD3 ARG A 200      54.542  -2.552   4.255  1.00119.29           H  
ATOM   2967  HD2 ARG A 200      54.984  -1.537   2.899  1.00119.29           H  
ATOM   2968  HE  ARG A 200      53.948   0.013   5.096  1.00123.29           H  
ATOM   2969 HH12 ARG A 200      51.409  -1.149   2.140  1.00136.92           H  
ATOM   2970 HH11 ARG A 200      52.927  -1.988   2.329  1.00136.92           H  
ATOM   2971 HH22 ARG A 200      50.856   0.610   3.587  1.00135.95           H  
ATOM   2972 HH21 ARG A 200      51.975   1.102   4.807  1.00135.95           H  
ATOM   2973  N   GLU A 201      58.014   0.785   7.184  1.00102.64           N  
ANISOU 2973  N   GLU A 201    14947  13473  10577  -7105   1935  -1008
ATOM   2974  CA  GLU A 201      58.500   2.148   6.980  1.00105.08           C  
ANISOU 2974  CA  GLU A 201    15189  13973  10766  -6722   2104   -740
ATOM   2975  C   GLU A 201      59.956   2.325   7.454  1.00103.76           C  
ANISOU 2975  C   GLU A 201    16055  13939   9429  -6371   2625   -306
ATOM   2976  O   GLU A 201      60.679   3.148   6.898  1.00106.61           O  
ANISOU 2976  O   GLU A 201    16459  14706   9342  -5775   2757   -242
ATOM   2977  CB  GLU A 201      57.557   3.118   7.727  1.00106.97           C  
ANISOU 2977  CB  GLU A 201    14871  13880  11893  -6941   2213   -132
ATOM   2978  CG  GLU A 201      57.806   4.618   7.461  1.00112.17           C  
ANISOU 2978  CG  GLU A 201    15022  14926  12670  -6512   2279    199
ATOM   2979  CD  GLU A 201      57.741   4.982   5.974  1.00117.69           C  
ANISOU 2979  CD  GLU A 201    14803  15909  14007  -6431   1597   -578
ATOM   2980  OE1 GLU A 201      56.719   4.639   5.341  1.00121.41           O  
ANISOU 2980  OE1 GLU A 201    14508  15905  15715  -6878    990  -1102
ATOM   2981  OE2 GLU A 201      58.725   5.583   5.494  1.00119.31           O1-
ANISOU 2981  OE2 GLU A 201    15047  16807  13478  -5852   1620   -710
ATOM   2982  H   GLU A 201      57.331   0.634   7.914  1.00102.64           H  
ATOM   2983  HA  GLU A 201      58.458   2.354   5.911  1.00105.08           H  
ATOM   2984  HB3 GLU A 201      57.626   2.929   8.797  1.00106.97           H  
ATOM   2985  HB2 GLU A 201      56.524   2.890   7.458  1.00106.97           H  
ATOM   2986  HG3 GLU A 201      58.771   4.916   7.868  1.00112.17           H  
ATOM   2987  HG2 GLU A 201      57.059   5.211   7.989  1.00112.17           H  
ATOM   2988  N   SER A 202      60.402   1.510   8.425  1.00101.03           N  
ANISOU 2988  N   SER A 202    16514  13207   8664  -6728   2866    -26
ATOM   2989  CA  SER A 202      61.780   1.466   8.911  1.00102.24           C  
ANISOU 2989  CA  SER A 202    17732  13144   7970  -6508   3221    268
ATOM   2990  C   SER A 202      62.678   0.778   7.881  1.00104.31           C  
ANISOU 2990  C   SER A 202    18026  13802   7805  -6170   3231    201
ATOM   2991  O   SER A 202      63.715   1.333   7.526  1.00107.72           O  
ANISOU 2991  O   SER A 202    18741  14423   7766  -5509   3495    415
ATOM   2992  CB  SER A 202      61.831   0.665  10.219  1.00101.36           C  
ANISOU 2992  CB  SER A 202    18335  12495   7682  -7137   3235    401
ATOM   2993  OG  SER A 202      61.125   1.384  11.204  1.00 99.26           O  
ANISOU 2993  OG  SER A 202    17672  12214   7829  -7482   3133    441
ATOM   2994  H   SER A 202      59.748   0.861   8.839  1.00101.03           H  
ATOM   2995  HA  SER A 202      62.147   2.480   9.084  1.00102.24           H  
ATOM   2996  HB3 SER A 202      62.862   0.539  10.557  1.00101.36           H  
ATOM   2997  HB2 SER A 202      61.398  -0.331  10.113  1.00101.36           H  
ATOM   2998  HG  SER A 202      60.200   1.323  11.003  1.00 99.26           H  
ATOM   2999  N   ALA A 203      62.234  -0.376   7.349  1.00103.26           N  
ANISOU 2999  N   ALA A 203    17522  13951   7759  -6471   2995     16
ATOM   3000  CA  ALA A 203      62.852  -1.102   6.244  1.00106.40           C  
ANISOU 3000  CA  ALA A 203    17753  15034   7640  -6002   3042    105
ATOM   3001  C   ALA A 203      63.017  -0.214   5.003  1.00109.75           C  
ANISOU 3001  C   ALA A 203    17660  16226   7813  -5107   2965   -217
ATOM   3002  O   ALA A 203      64.127  -0.102   4.495  1.00113.77           O  
ANISOU 3002  O   ALA A 203    18435  17102   7693  -4472   3305    226
ATOM   3003  CB  ALA A 203      62.023  -2.361   5.937  1.00106.06           C  
ANISOU 3003  CB  ALA A 203    17121  15486   7690  -6188   2748   -153
ATOM   3004  H   ALA A 203      61.364  -0.755   7.702  1.00103.26           H  
ATOM   3005  HA  ALA A 203      63.845  -1.417   6.569  1.00106.40           H  
ATOM   3006  HB1 ALA A 203      62.417  -2.914   5.087  1.00106.06           H  
ATOM   3007  HB2 ALA A 203      62.022  -3.041   6.789  1.00106.06           H  
ATOM   3008  HB3 ALA A 203      60.985  -2.118   5.707  1.00106.06           H  
ATOM   3009  N   LYS A 204      61.940   0.465   4.570  1.00109.70           N  
ANISOU 3009  N   LYS A 204    16866  16414   8400  -5085   2489   -927
ATOM   3010  CA  LYS A 204      61.880   1.394   3.439  1.00114.51           C  
ANISOU 3010  CA  LYS A 204    16765  17799   8944  -4386   2185  -1412
ATOM   3011  C   LYS A 204      62.869   2.571   3.557  1.00116.23           C  
ANISOU 3011  C   LYS A 204    17383  18072   8705  -3913   2672   -771
ATOM   3012  O   LYS A 204      63.495   2.934   2.562  1.00121.32           O  
ANISOU 3012  O   LYS A 204    17816  19616   8664  -3072   2751   -723
ATOM   3013  CB  LYS A 204      60.418   1.875   3.309  1.00115.72           C  
ANISOU 3013  CB  LYS A 204    16038  17678  10252  -4775   1533  -2137
ATOM   3014  CG  LYS A 204      60.111   2.808   2.127  1.00123.15           C  
ANISOU 3014  CG  LYS A 204    16006  19423  11360  -4232    867  -2980
ATOM   3015  CD  LYS A 204      58.602   3.090   2.010  1.00127.12           C  
ANISOU 3015  CD  LYS A 204    15670  19355  13273  -4757     24  -3892
ATOM   3016  CE  LYS A 204      58.253   4.181   0.987  1.00136.32           C  
ANISOU 3016  CE  LYS A 204    15780  20802  15214  -4695   -681  -4448
ATOM   3017  NZ  LYS A 204      58.526   3.752  -0.394  1.00144.58           N1+
ANISOU 3017  NZ  LYS A 204    16315  23047  15571  -3836  -1406  -5661
ATOM   3018  H   LYS A 204      61.070   0.310   5.064  1.00109.70           H  
ATOM   3019  HA  LYS A 204      62.139   0.831   2.541  1.00114.51           H  
ATOM   3020  HB3 LYS A 204      60.117   2.369   4.233  1.00115.72           H  
ATOM   3021  HB2 LYS A 204      59.778   0.998   3.215  1.00115.72           H  
ATOM   3022  HG3 LYS A 204      60.479   2.363   1.201  1.00123.15           H  
ATOM   3023  HG2 LYS A 204      60.643   3.750   2.257  1.00123.15           H  
ATOM   3024  HD3 LYS A 204      58.233   3.414   2.984  1.00127.12           H  
ATOM   3025  HD2 LYS A 204      58.064   2.170   1.776  1.00127.12           H  
ATOM   3026  HE3 LYS A 204      58.809   5.095   1.200  1.00136.32           H  
ATOM   3027  HE2 LYS A 204      57.194   4.432   1.063  1.00136.32           H  
ATOM   3028  HZ1 LYS A 204      59.509   3.544  -0.492  1.00144.58           H  
ATOM   3029  HZ2 LYS A 204      57.984   2.927  -0.606  1.00144.58           H  
ATOM   3030  HZ3 LYS A 204      58.274   4.492  -1.034  1.00144.58           H  
ATOM   3031  N   ARG A 205      63.042   3.130   4.768  1.00113.37           N  
ANISOU 3031  N   ARG A 205    17597  16883   8596  -4285   3018   -262
ATOM   3032  CA  ARG A 205      63.982   4.214   5.068  1.00116.11           C  
ANISOU 3032  CA  ARG A 205    18442  17233   8442  -3665   3521    339
ATOM   3033  C   ARG A 205      65.439   3.733   5.232  1.00118.32           C  
ANISOU 3033  C   ARG A 205    19771  17262   7924  -3223   4051    887
ATOM   3034  O   ARG A 205      66.346   4.557   5.122  1.00122.84           O  
ANISOU 3034  O   ARG A 205    20642  18086   7946  -2377   4454   1330
ATOM   3035  CB  ARG A 205      63.535   4.906   6.374  1.00114.54           C  
ANISOU 3035  CB  ARG A 205    18504  16418   8599  -3939   3715    676
ATOM   3036  CG  ARG A 205      62.344   5.856   6.152  1.00116.83           C  
ANISOU 3036  CG  ARG A 205    17572  17146   9671  -4001   3413    664
ATOM   3037  CD  ARG A 205      61.757   6.404   7.463  1.00116.28           C  
ANISOU 3037  CD  ARG A 205    17553  16670   9959  -4225   3660   1214
ATOM   3038  NE  ARG A 205      61.615   7.867   7.438  1.00121.58           N  
ANISOU 3038  NE  ARG A 205    17355  17961  10878  -3756   3794   1833
ATOM   3039  CZ  ARG A 205      60.476   8.563   7.286  1.00124.89           C  
ANISOU 3039  CZ  ARG A 205    16441  18513  12499  -4220   3457   2078
ATOM   3040  NH1 ARG A 205      59.300   7.961   7.061  1.00123.10           N  
ANISOU 3040  NH1 ARG A 205    15708  17710  13354  -5094   2959   1636
ATOM   3041  NH2 ARG A 205      60.519   9.899   7.353  1.00131.57           N1+
ANISOU 3041  NH2 ARG A 205    16398  20039  13553  -3782   3633   2882
ATOM   3042  H   ARG A 205      62.487   2.780   5.537  1.00113.37           H  
ATOM   3043  HA  ARG A 205      63.968   4.942   4.256  1.00116.11           H  
ATOM   3044  HB3 ARG A 205      64.353   5.491   6.800  1.00114.54           H  
ATOM   3045  HB2 ARG A 205      63.287   4.157   7.127  1.00114.54           H  
ATOM   3046  HG3 ARG A 205      61.554   5.337   5.609  1.00116.83           H  
ATOM   3047  HG2 ARG A 205      62.657   6.673   5.501  1.00116.83           H  
ATOM   3048  HD3 ARG A 205      62.417   6.167   8.294  1.00116.28           H  
ATOM   3049  HD2 ARG A 205      60.811   5.919   7.697  1.00116.28           H  
ATOM   3050  HE  ARG A 205      62.475   8.379   7.576  1.00121.58           H  
ATOM   3051 HH12 ARG A 205      58.451   8.497   6.962  1.00123.10           H  
ATOM   3052 HH11 ARG A 205      59.268   6.966   6.864  1.00123.10           H  
ATOM   3053 HH22 ARG A 205      59.677  10.441   7.235  1.00131.57           H  
ATOM   3054 HH21 ARG A 205      61.395  10.373   7.520  1.00131.57           H  
ATOM   3055  N   PHE A 206      65.675   2.426   5.438  1.00116.70           N  
ANISOU 3055  N   PHE A 206    20041  16545   7753  -3782   4058    976
ATOM   3056  CA  PHE A 206      67.001   1.798   5.507  1.00121.37           C  
ANISOU 3056  CA  PHE A 206    21480  16716   7918  -3531   4508   1670
ATOM   3057  C   PHE A 206      67.311   0.959   4.250  1.00125.29           C  
ANISOU 3057  C   PHE A 206    21364  18258   7981  -3027   4562   1953
ATOM   3058  O   PHE A 206      68.262   0.177   4.261  1.00130.00           O  
ANISOU 3058  O   PHE A 206    22408  18553   8433  -2982   4929   2766
ATOM   3059  CB  PHE A 206      67.113   0.953   6.803  1.00120.65           C  
ANISOU 3059  CB  PHE A 206    22289  15358   8196  -4475   4494   1829
ATOM   3060  CG  PHE A 206      67.175   1.763   8.094  1.00120.77           C  
ANISOU 3060  CG  PHE A 206    23151  14465   8272  -4547   4544   1642
ATOM   3061  CD1 PHE A 206      68.116   2.805   8.238  1.00126.98           C  
ANISOU 3061  CD1 PHE A 206    24761  14824   8663  -3686   4945   1921
ATOM   3062  CD2 PHE A 206      66.307   1.467   9.165  1.00116.73           C  
ANISOU 3062  CD2 PHE A 206    22596  13667   8088  -5274   4221   1224
ATOM   3063  CE1 PHE A 206      68.160   3.568   9.421  1.00129.13           C  
ANISOU 3063  CE1 PHE A 206    25841  14449   8773  -3466   4985   1672
ATOM   3064  CE2 PHE A 206      66.346   2.233  10.347  1.00119.26           C  
ANISOU 3064  CE2 PHE A 206    23629  13454   8230  -5090   4277   1063
ATOM   3065  CZ  PHE A 206      67.270   3.286  10.473  1.00125.59           C  
ANISOU 3065  CZ  PHE A 206    25290  13886   8541  -4143   4639   1232
ATOM   3066  H   PHE A 206      64.877   1.812   5.528  1.00116.70           H  
ATOM   3067  HA  PHE A 206      67.779   2.560   5.521  1.00121.37           H  
ATOM   3068  HB3 PHE A 206      68.021   0.350   6.789  1.00120.65           H  
ATOM   3069  HB2 PHE A 206      66.285   0.244   6.852  1.00120.65           H  
ATOM   3070  HD1 PHE A 206      68.811   3.032   7.444  1.00126.98           H  
ATOM   3071  HD2 PHE A 206      65.604   0.652   9.086  1.00116.73           H  
ATOM   3072  HE1 PHE A 206      68.880   4.366   9.523  1.00129.13           H  
ATOM   3073  HE2 PHE A 206      65.672   2.004  11.160  1.00119.26           H  
ATOM   3074  HZ  PHE A 206      67.309   3.873  11.379  1.00125.59           H  
ATOM   3075  N   GLY A 207      66.557   1.154   3.151  1.00125.16           N  
ANISOU 3075  N   GLY A 207    20269  19495   7791  -2589   4158   1304
ATOM   3076  CA  GLY A 207      66.837   0.586   1.832  1.00130.56           C  
ANISOU 3076  CA  GLY A 207    20234  21598   7774  -1742   4136   1382
ATOM   3077  C   GLY A 207      66.471  -0.895   1.658  1.00130.64           C  
ANISOU 3077  C   GLY A 207    20017  21850   7770  -2098   4032   1498
ATOM   3078  O   GLY A 207      67.135  -1.589   0.893  1.00136.83           O  
ANISOU 3078  O   GLY A 207    20635  23408   7947  -1490   4408   2335
ATOM   3079  H   GLY A 207      65.784   1.802   3.217  1.00125.16           H  
ATOM   3080  HA3 GLY A 207      67.892   0.727   1.590  1.00130.56           H  
ATOM   3081  HA2 GLY A 207      66.274   1.159   1.095  1.00130.56           H  
ATOM   3082  N   ILE A 208      65.443  -1.376   2.372  1.00124.84           N  
ANISOU 3082  N   ILE A 208    19186  20563   7686  -2990   3588    838
ATOM   3083  CA  ILE A 208      64.936  -2.748   2.350  1.00125.19           C  
ANISOU 3083  CA  ILE A 208    18886  21003   7677  -3239   3451    890
ATOM   3084  C   ILE A 208      63.466  -2.697   1.889  1.00123.68           C  
ANISOU 3084  C   ILE A 208    17950  21293   7751  -3151   2729   -417
ATOM   3085  O   ILE A 208      62.655  -1.959   2.444  1.00119.14           O  
ANISOU 3085  O   ILE A 208    17394  19876   7997  -3761   2385  -1056
ATOM   3086  CB  ILE A 208      65.107  -3.403   3.754  1.00121.79           C  
ANISOU 3086  CB  ILE A 208    19136  19313   7826  -4452   3649   1554
ATOM   3087  CG1 ILE A 208      66.581  -3.419   4.233  1.00126.06           C  
ANISOU 3087  CG1 ILE A 208    20486  19056   8356  -4602   4209   2705
ATOM   3088  CG2 ILE A 208      64.508  -4.826   3.801  1.00123.04           C  
ANISOU 3088  CG2 ILE A 208    18755  20125   7868  -4634   3537   1760
ATOM   3089  CD1 ILE A 208      66.759  -3.772   5.718  1.00124.08           C  
ANISOU 3089  CD1 ILE A 208    21021  17341   8784  -5850   4183   3021
ATOM   3090  H   ILE A 208      64.969  -0.738   3.000  1.00124.84           H  
ATOM   3091  HA  ILE A 208      65.497  -3.344   1.629  1.00125.19           H  
ATOM   3092  HB  ILE A 208      64.559  -2.792   4.468  1.00121.79           H  
ATOM   3093 HG13 ILE A 208      67.033  -2.439   4.094  1.00126.06           H  
ATOM   3094 HG12 ILE A 208      67.165  -4.106   3.618  1.00126.06           H  
ATOM   3095 HG21 ILE A 208      64.599  -5.273   4.789  1.00123.04           H  
ATOM   3096 HG22 ILE A 208      63.444  -4.837   3.563  1.00123.04           H  
ATOM   3097 HG23 ILE A 208      65.012  -5.482   3.092  1.00123.04           H  
ATOM   3098 HD11 ILE A 208      67.800  -3.652   6.018  1.00124.08           H  
ATOM   3099 HD12 ILE A 208      66.160  -3.118   6.354  1.00124.08           H  
ATOM   3100 HD13 ILE A 208      66.480  -4.802   5.934  1.00124.08           H  
ATOM   3101  N   LYS A 209      63.127  -3.505   0.877  1.00129.40           N  
ANISOU 3101  N   LYS A 209    18000  23372   7795  -2282   2509   -752
ATOM   3102  CA  LYS A 209      61.788  -3.625   0.300  1.00131.25           C  
ANISOU 3102  CA  LYS A 209    17598  24011   8261  -1973   1725  -2176
ATOM   3103  C   LYS A 209      61.105  -4.856   0.927  1.00128.42           C  
ANISOU 3103  C   LYS A 209    17290  23260   8243  -2557   1724  -2021
ATOM   3104  O   LYS A 209      61.721  -5.917   1.031  1.00130.38           O  
ANISOU 3104  O   LYS A 209    17559  24056   7923  -2484   2195   -979
ATOM   3105  CB  LYS A 209      61.994  -3.773  -1.222  1.00141.51           C  
ANISOU 3105  CB  LYS A 209    18171  27188   8410   -404   1401  -2839
ATOM   3106  CG  LYS A 209      60.727  -3.667  -2.088  1.00147.02           C  
ANISOU 3106  CG  LYS A 209    18264  28139   9458     71    325  -4758
ATOM   3107  CD  LYS A 209      61.073  -3.206  -3.516  1.00157.89           C  
ANISOU 3107  CD  LYS A 209    19034  31215   9741   1480    -37  -5432
ATOM   3108  CE  LYS A 209      59.880  -3.187  -4.483  1.00168.24           C  
ANISOU 3108  CE  LYS A 209    19669  33181  11073   2305  -1285  -7563
ATOM   3109  NZ  LYS A 209      59.552  -4.540  -4.965  1.00177.35           N1+
ANISOU 3109  NZ  LYS A 209    20470  36166  10747   3900  -1388  -7960
ATOM   3110  H   LYS A 209      63.841  -4.103   0.488  1.00129.40           H  
ATOM   3111  HA  LYS A 209      61.201  -2.726   0.498  1.00131.25           H  
ATOM   3112  HB3 LYS A 209      62.534  -4.691  -1.456  1.00141.51           H  
ATOM   3113  HB2 LYS A 209      62.665  -2.969  -1.527  1.00141.51           H  
ATOM   3114  HG3 LYS A 209      60.031  -2.953  -1.646  1.00147.02           H  
ATOM   3115  HG2 LYS A 209      60.216  -4.630  -2.104  1.00147.02           H  
ATOM   3116  HD3 LYS A 209      61.870  -3.827  -3.928  1.00157.89           H  
ATOM   3117  HD2 LYS A 209      61.482  -2.196  -3.460  1.00157.89           H  
ATOM   3118  HE3 LYS A 209      60.120  -2.575  -5.353  1.00168.24           H  
ATOM   3119  HE2 LYS A 209      59.003  -2.741  -4.013  1.00168.24           H  
ATOM   3120  HZ1 LYS A 209      59.295  -5.130  -4.187  1.00177.35           H  
ATOM   3121  HZ2 LYS A 209      58.775  -4.499  -5.609  1.00177.35           H  
ATOM   3122  HZ3 LYS A 209      60.353  -4.941  -5.432  1.00177.35           H  
ATOM   3123  N   MET A 210      59.860  -4.680   1.405  1.00125.23           N  
ANISOU 3123  N   MET A 210    16805  21937   8839  -3131   1221  -2900
ATOM   3124  CA  MET A 210      59.132  -5.589   2.305  1.00121.77           C  
ANISOU 3124  CA  MET A 210    16453  20975   8839  -3779   1284  -2630
ATOM   3125  C   MET A 210      58.920  -7.017   1.786  1.00127.86           C  
ANISOU 3125  C   MET A 210    16807  23018   8756  -2937   1304  -2549
ATOM   3126  O   MET A 210      59.168  -7.971   2.522  1.00126.83           O  
ANISOU 3126  O   MET A 210    16765  23084   8341  -3358   1789  -1383
ATOM   3127  CB  MET A 210      57.769  -4.964   2.691  1.00119.41           C  
ANISOU 3127  CB  MET A 210    16023  19523   9824  -4325    776  -3491
ATOM   3128  CG  MET A 210      57.784  -4.327   4.084  1.00111.50           C  
ANISOU 3128  CG  MET A 210    15480  17305   9581  -5478   1113  -2754
ATOM   3129  SD  MET A 210      57.868  -5.479   5.483  1.00104.77           S  
ANISOU 3129  SD  MET A 210    15024  16262   8520  -6299   1612  -1619
ATOM   3130  CE  MET A 210      56.123  -5.955   5.599  1.00107.50           C  
ANISOU 3130  CE  MET A 210    14883  16303   9660  -6310   1253  -2154
ATOM   3131  H   MET A 210      59.436  -3.775   1.256  1.00125.23           H  
ATOM   3132  HA  MET A 210      59.749  -5.685   3.203  1.00121.77           H  
ATOM   3133  HB3 MET A 210      56.967  -5.703   2.668  1.00119.41           H  
ATOM   3134  HB2 MET A 210      57.479  -4.214   1.955  1.00119.41           H  
ATOM   3135  HG3 MET A 210      56.871  -3.750   4.206  1.00111.50           H  
ATOM   3136  HG2 MET A 210      58.616  -3.628   4.156  1.00111.50           H  
ATOM   3137  HE1 MET A 210      55.980  -6.648   6.427  1.00107.50           H  
ATOM   3138  HE2 MET A 210      55.496  -5.081   5.778  1.00107.50           H  
ATOM   3139  HE3 MET A 210      55.788  -6.435   4.681  1.00107.50           H  
ATOM   3140  N   GLU A 211      58.481  -7.166   0.525  1.00135.94           N  
ANISOU 3140  N   GLU A 211    17323  24981   9347  -1697    732  -3791
ATOM   3141  CA  GLU A 211      58.271  -8.457  -0.140  1.00143.81           C  
ANISOU 3141  CA  GLU A 211    17877  27468   9297   -531    760  -3771
ATOM   3142  C   GLU A 211      59.592  -9.162  -0.518  1.00147.82           C  
ANISOU 3142  C   GLU A 211    18181  29468   8514     49   1497  -2243
ATOM   3143  O   GLU A 211      59.571 -10.344  -0.857  1.00154.77           O  
ANISOU 3143  O   GLU A 211    18576  31809   8421    983   1741  -1674
ATOM   3144  CB  GLU A 211      57.412  -8.211  -1.407  1.00154.29           C  
ANISOU 3144  CB  GLU A 211    18781  29537  10307    916   -138  -5695
ATOM   3145  CG  GLU A 211      58.088  -7.411  -2.549  1.00160.91           C  
ANISOU 3145  CG  GLU A 211    19361  31319  10460   1847   -516  -6489
ATOM   3146  CD  GLU A 211      57.391  -7.612  -3.895  1.00176.16           C  
ANISOU 3146  CD  GLU A 211    20774  34799  11359   3757  -1326  -8185
ATOM   3147  OE1 GLU A 211      57.418  -8.761  -4.387  1.00183.62           O  
ANISOU 3147  OE1 GLU A 211    21385  37588  10794   5122   -956  -7645
ATOM   3148  OE2 GLU A 211      56.873  -6.604  -4.422  1.00182.70           O1-
ANISOU 3148  OE2 GLU A 211    21471  35062  12886   3949  -2380 -10059
ATOM   3149  H   GLU A 211      58.298  -6.336  -0.020  1.00135.94           H  
ATOM   3150  HA  GLU A 211      57.719  -9.113   0.532  1.00143.81           H  
ATOM   3151  HB3 GLU A 211      56.485  -7.711  -1.125  1.00154.29           H  
ATOM   3152  HB2 GLU A 211      57.102  -9.187  -1.785  1.00154.29           H  
ATOM   3153  HG3 GLU A 211      59.123  -7.714  -2.704  1.00160.91           H  
ATOM   3154  HG2 GLU A 211      58.118  -6.351  -2.296  1.00160.91           H  
ATOM   3155  N   ASP A 212      60.718  -8.432  -0.472  1.00144.64           N  
ANISOU 3155  N   ASP A 212    18110  28669   8179   -470   1900  -1424
ATOM   3156  CA  ASP A 212      62.039  -8.816  -0.967  1.00151.39           C  
ANISOU 3156  CA  ASP A 212    18695  30880   7944    313   2542    -56
ATOM   3157  C   ASP A 212      63.033  -9.199   0.146  1.00148.57           C  
ANISOU 3157  C   ASP A 212    18692  29755   8003   -891   3307   1917
ATOM   3158  O   ASP A 212      64.167  -9.559  -0.172  1.00155.82           O  
ANISOU 3158  O   ASP A 212    19340  31561   8302   -389   3908   3366
ATOM   3159  CB  ASP A 212      62.599  -7.607  -1.764  1.00154.51           C  
ANISOU 3159  CB  ASP A 212    19062  31740   7905   1103   2397   -622
ATOM   3160  CG  ASP A 212      62.975  -7.934  -3.210  1.00167.21           C  
ANISOU 3160  CG  ASP A 212    19895  35773   7866   3058   2539   -398
ATOM   3161  OD1 ASP A 212      62.191  -8.648  -3.872  1.00174.29           O  
ANISOU 3161  OD1 ASP A 212    20238  38035   7950   4198   2240  -1013
ATOM   3162  OD2 ASP A 212      64.037  -7.432  -3.637  1.00171.49           O1-
ANISOU 3162  OD2 ASP A 212    20360  36966   7832   3621   2973    417
ATOM   3163  H   ASP A 212      60.633  -7.483  -0.138  1.00144.64           H  
ATOM   3164  HA  ASP A 212      61.939  -9.696  -1.605  1.00151.39           H  
ATOM   3165  HB3 ASP A 212      63.451  -7.140  -1.265  1.00154.51           H  
ATOM   3166  HB2 ASP A 212      61.846  -6.820  -1.836  1.00154.51           H  
ATOM   3167  N   ALA A 213      62.628  -9.152   1.425  1.00140.10           N  
ANISOU 3167  N   ALA A 213    18173  27036   8025  -2439   3241   1990
ATOM   3168  CA  ALA A 213      63.440  -9.544   2.576  1.00139.88           C  
ANISOU 3168  CA  ALA A 213    18460  26199   8490  -3664   3724   3579
ATOM   3169  C   ALA A 213      62.560 -10.247   3.608  1.00135.19           C  
ANISOU 3169  C   ALA A 213    17898  24943   8526  -4759   3502   3523
ATOM   3170  O   ALA A 213      61.563  -9.682   4.058  1.00128.17           O  
ANISOU 3170  O   ALA A 213    17286  23234   8178  -5134   3080   2354
ATOM   3171  CB  ALA A 213      64.204  -8.337   3.134  1.00136.63           C  
ANISOU 3171  CB  ALA A 213    18934  24282   8696  -4426   3888   3786
ATOM   3172  H   ALA A 213      61.683  -8.849   1.614  1.00140.10           H  
ATOM   3173  HA  ALA A 213      64.185 -10.273   2.248  1.00139.88           H  
ATOM   3174  HB1 ALA A 213      64.810  -8.617   3.997  1.00136.63           H  
ATOM   3175  HB2 ALA A 213      64.872  -7.914   2.385  1.00136.63           H  
ATOM   3176  HB3 ALA A 213      63.516  -7.552   3.451  1.00136.63           H  
ATOM   3177  N   LYS A 214      62.933 -11.484   3.969  1.00140.51           N  
ANISOU 3177  N   LYS A 214    18157  26073   9157  -5244   3808   4954
ATOM   3178  CA  LYS A 214      62.180 -12.350   4.873  1.00138.41           C  
ANISOU 3178  CA  LYS A 214    17671  25656   9264  -6101   3625   5105
ATOM   3179  C   LYS A 214      62.627 -12.114   6.322  1.00133.78           C  
ANISOU 3179  C   LYS A 214    17833  23334   9664  -7820   3480   5319
ATOM   3180  O   LYS A 214      63.777 -11.757   6.588  1.00134.65           O  
ANISOU 3180  O   LYS A 214    18579  22430  10152  -8323   3601   5674
ATOM   3181  CB  LYS A 214      62.420 -13.820   4.479  1.00148.63           C  
ANISOU 3181  CB  LYS A 214    17914  28630   9928  -5647   3968   6569
ATOM   3182  CG  LYS A 214      61.963 -14.101   3.035  1.00155.52           C  
ANISOU 3182  CG  LYS A 214    18077  31477   9535  -3602   4133   6350
ATOM   3183  CD  LYS A 214      61.927 -15.587   2.666  1.00164.19           C  
ANISOU 3183  CD  LYS A 214    18150  34389   9846  -2763   4301   7088
ATOM   3184  CE  LYS A 214      61.639 -15.779   1.169  1.00172.99           C  
ANISOU 3184  CE  LYS A 214    18684  37533   9509   -433   4349   6497
ATOM   3185  NZ  LYS A 214      61.602 -17.202   0.800  1.00184.53           N1+
ANISOU 3185  NZ  LYS A 214    18990  41237   9884    744   4742   7767
ATOM   3186  H   LYS A 214      63.783 -11.862   3.576  1.00140.51           H  
ATOM   3187  HA  LYS A 214      61.112 -12.130   4.787  1.00138.41           H  
ATOM   3188  HB3 LYS A 214      61.852 -14.461   5.154  1.00148.63           H  
ATOM   3189  HB2 LYS A 214      63.470 -14.091   4.600  1.00148.63           H  
ATOM   3190  HG3 LYS A 214      62.624 -13.580   2.342  1.00155.52           H  
ATOM   3191  HG2 LYS A 214      60.968 -13.678   2.880  1.00155.52           H  
ATOM   3192  HD3 LYS A 214      61.166 -16.094   3.262  1.00164.19           H  
ATOM   3193  HD2 LYS A 214      62.882 -16.050   2.919  1.00164.19           H  
ATOM   3194  HE3 LYS A 214      62.410 -15.290   0.574  1.00172.99           H  
ATOM   3195  HE2 LYS A 214      60.690 -15.318   0.898  1.00172.99           H  
ATOM   3196  HZ1 LYS A 214      60.864 -17.667   1.304  1.00184.53           H  
ATOM   3197  HZ2 LYS A 214      61.441 -17.292  -0.194  1.00184.53           H  
ATOM   3198  HZ3 LYS A 214      62.488 -17.632   1.031  1.00184.53           H  
ATOM   3199  N   ILE A 215      61.664 -12.263   7.241  1.00130.12           N  
ANISOU 3199  N   ILE A 215    17299  22604   9539  -8564   3198   5049
ATOM   3200  CA  ILE A 215      61.682 -11.725   8.601  1.00124.79           C  
ANISOU 3200  CA  ILE A 215    17383  20454   9576  -9802   2900   4607
ATOM   3201  C   ILE A 215      61.612 -12.874   9.624  1.00128.03           C  
ANISOU 3201  C   ILE A 215    17434  20962  10249 -10945   2701   5320
ATOM   3202  O   ILE A 215      61.031 -13.925   9.355  1.00131.23           O  
ANISOU 3202  O   ILE A 215    16957  22601  10303 -10645   2776   5846
ATOM   3203  CB  ILE A 215      60.513 -10.694   8.701  1.00116.12           C  
ANISOU 3203  CB  ILE A 215    16611  18854   8656  -9378   2674   3199
ATOM   3204  CG1 ILE A 215      60.777  -9.445   7.822  1.00113.73           C  
ANISOU 3204  CG1 ILE A 215    16677  18274   8262  -8558   2744   2511
ATOM   3205  CG2 ILE A 215      60.159 -10.244  10.135  1.00112.24           C  
ANISOU 3205  CG2 ILE A 215    16677  17306   8662 -10388   2434   2901
ATOM   3206  CD1 ILE A 215      59.498  -8.753   7.327  1.00110.04           C  
ANISOU 3206  CD1 ILE A 215    15949  17942   7918  -7746   2500   1348
ATOM   3207  H   ILE A 215      60.767 -12.595   6.918  1.00130.12           H  
ATOM   3208  HA  ILE A 215      62.618 -11.195   8.780  1.00124.79           H  
ATOM   3209  HB  ILE A 215      59.624 -11.192   8.309  1.00116.12           H  
ATOM   3210 HG13 ILE A 215      61.357  -9.698   6.938  1.00113.73           H  
ATOM   3211 HG12 ILE A 215      61.393  -8.733   8.372  1.00113.73           H  
ATOM   3212 HG21 ILE A 215      59.322  -9.546  10.135  1.00112.24           H  
ATOM   3213 HG22 ILE A 215      59.860 -11.079  10.765  1.00112.24           H  
ATOM   3214 HG23 ILE A 215      60.991  -9.739  10.618  1.00112.24           H  
ATOM   3215 HD11 ILE A 215      59.741  -7.894   6.702  1.00110.04           H  
ATOM   3216 HD12 ILE A 215      58.890  -9.433   6.728  1.00110.04           H  
ATOM   3217 HD13 ILE A 215      58.885  -8.395   8.152  1.00110.04           H  
ATOM   3218  N   ALA A 216      62.201 -12.646  10.807  1.00128.48           N  
ANISOU 3218  N   ALA A 216    18161  19807  10848 -12149   2402   5270
ATOM   3219  CA  ALA A 216      62.122 -13.493  11.991  1.00132.84           C  
ANISOU 3219  CA  ALA A 216    18425  20374  11672 -13356   2021   5702
ATOM   3220  C   ALA A 216      61.295 -12.770  13.066  1.00126.75           C  
ANISOU 3220  C   ALA A 216    18173  19024  10962 -13678   1668   4668
ATOM   3221  O   ALA A 216      61.470 -11.568  13.257  1.00123.38           O  
ANISOU 3221  O   ALA A 216    18677  17528  10673 -13693   1557   3901
ATOM   3222  CB  ALA A 216      63.545 -13.736  12.514  1.00143.56           C  
ANISOU 3222  CB  ALA A 216    19984  20903  13659 -14574   1788   6573
ATOM   3223  H   ALA A 216      62.649 -11.746  10.934  1.00128.48           H  
ATOM   3224  HA  ALA A 216      61.675 -14.448  11.744  1.00132.84           H  
ATOM   3225  HB1 ALA A 216      63.538 -14.346  13.418  1.00143.56           H  
ATOM   3226  HB2 ALA A 216      64.146 -14.260  11.772  1.00143.56           H  
ATOM   3227  HB3 ALA A 216      64.051 -12.800  12.744  1.00143.56           H  
ATOM   3228  N   VAL A 217      60.408 -13.489  13.775  1.00126.53           N  
ANISOU 3228  N   VAL A 217    17466  19864  10748 -13806   1548   4797
ATOM   3229  CA  VAL A 217      59.558 -12.948  14.841  1.00123.49           C  
ANISOU 3229  CA  VAL A 217    17346  19253  10323 -14017   1278   4112
ATOM   3230  C   VAL A 217      59.613 -13.869  16.066  1.00131.38           C  
ANISOU 3230  C   VAL A 217    17957  20652  11309 -15175    761   4532
ATOM   3231  O   VAL A 217      58.886 -14.858  16.113  1.00136.02           O  
ANISOU 3231  O   VAL A 217    17546  22384  11750 -15348    787   5371
ATOM   3232  CB  VAL A 217      58.112 -12.654  14.337  1.00117.47           C  
ANISOU 3232  CB  VAL A 217    16090  19137   9406 -12994   1583   3844
ATOM   3233  CG1 VAL A 217      57.205 -12.081  15.444  1.00117.14           C  
ANISOU 3233  CG1 VAL A 217    16020  19192   9298 -13188   1405   3601
ATOM   3234  CG2 VAL A 217      58.078 -11.724  13.107  1.00111.34           C  
ANISOU 3234  CG2 VAL A 217    15723  17770   8811 -12011   1863   3149
ATOM   3235  H   VAL A 217      60.309 -14.473  13.560  1.00126.53           H  
ATOM   3236  HA  VAL A 217      59.971 -11.996  15.162  1.00123.49           H  
ATOM   3237  HB  VAL A 217      57.665 -13.599  14.026  1.00117.47           H  
ATOM   3238 HG11 VAL A 217      56.192 -11.938  15.073  1.00117.14           H  
ATOM   3239 HG12 VAL A 217      57.128 -12.742  16.307  1.00117.14           H  
ATOM   3240 HG13 VAL A 217      57.573 -11.117  15.796  1.00117.14           H  
ATOM   3241 HG21 VAL A 217      57.077 -11.357  12.894  1.00111.34           H  
ATOM   3242 HG22 VAL A 217      58.707 -10.851  13.229  1.00111.34           H  
ATOM   3243 HG23 VAL A 217      58.435 -12.234  12.217  1.00111.34           H  
ATOM   3244  N   GLN A 218      60.439 -13.533  17.073  1.00134.33           N  
ANISOU 3244  N   GLN A 218    19078  20199  11761 -15867    244   3895
ATOM   3245  CA  GLN A 218      60.535 -14.264  18.340  1.00143.36           C  
ANISOU 3245  CA  GLN A 218    19902  21679  12888 -17030   -476   4010
ATOM   3246  C   GLN A 218      59.314 -13.941  19.212  1.00139.65           C  
ANISOU 3246  C   GLN A 218    19060  22178  11823 -16629   -535   3695
ATOM   3247  O   GLN A 218      59.068 -12.779  19.515  1.00135.65           O  
ANISOU 3247  O   GLN A 218    19196  21312  11031 -16006   -471   2923
ATOM   3248  CB  GLN A 218      61.850 -13.861  19.056  1.00151.65           C  
ANISOU 3248  CB  GLN A 218    22014  21333  14273 -17858  -1167   3254
ATOM   3249  CG  GLN A 218      62.029 -14.415  20.498  1.00165.23           C  
ANISOU 3249  CG  GLN A 218    23467  23391  15922 -18981  -2123   2975
ATOM   3250  CD  GLN A 218      62.234 -13.346  21.582  1.00172.89           C  
ANISOU 3250  CD  GLN A 218    25627  23459  16606 -18965  -2782   1543
ATOM   3251  OE1 GLN A 218      61.602 -13.398  22.633  1.00180.80           O  
ANISOU 3251  OE1 GLN A 218    27628  22924  18144 -19380  -3182    997
ATOM   3252  NE2 GLN A 218      63.116 -12.376  21.345  1.00170.89           N  
ANISOU 3252  NE2 GLN A 218    25242  24227  15463 -18361  -2892    986
ATOM   3253  H   GLN A 218      60.977 -12.683  16.986  1.00134.33           H  
ATOM   3254  HA  GLN A 218      60.549 -15.331  18.131  1.00143.36           H  
ATOM   3255  HB3 GLN A 218      61.930 -12.777  19.045  1.00151.65           H  
ATOM   3256  HB2 GLN A 218      62.688 -14.207  18.450  1.00151.65           H  
ATOM   3257  HG3 GLN A 218      62.908 -15.059  20.520  1.00165.23           H  
ATOM   3258  HG2 GLN A 218      61.205 -15.066  20.791  1.00165.23           H  
ATOM   3259 HE22 GLN A 218      63.256 -11.657  22.041  1.00170.89           H  
ATOM   3260 HE21 GLN A 218      63.621 -12.350  20.473  1.00170.89           H  
ATOM   3261  N   GLY A 219      58.567 -14.979  19.608  1.00141.66           N  
ANISOU 3261  N   GLY A 219    18193  23778  11851 -16894   -604   4452
ATOM   3262  CA  GLY A 219      57.331 -14.897  20.376  1.00138.18           C  
ANISOU 3262  CA  GLY A 219    17260  24413  10830 -16355   -541   4398
ATOM   3263  C   GLY A 219      56.096 -14.918  19.472  1.00127.66           C  
ANISOU 3263  C   GLY A 219    15462  23572   9469 -15053    285   4788
ATOM   3264  O   GLY A 219      56.119 -14.384  18.362  1.00120.17           O  
ANISOU 3264  O   GLY A 219    14928  21860   8871 -14377    731   4565
ATOM   3265  H   GLY A 219      58.830 -15.903  19.291  1.00141.66           H  
ATOM   3266  HA3 GLY A 219      57.303 -13.982  20.967  1.00138.18           H  
ATOM   3267  HA2 GLY A 219      57.302 -15.736  21.072  1.00138.18           H  
ATOM   3268  N   PHE A 220      55.006 -15.516  19.973  1.00128.45           N  
ANISOU 3268  N   PHE A 220    14687  24920   9199 -14675    429   5332
ATOM   3269  CA  PHE A 220      53.732 -15.665  19.271  1.00122.26           C  
ANISOU 3269  CA  PHE A 220    13433  24467   8554 -13436   1134   5719
ATOM   3270  C   PHE A 220      52.537 -15.467  20.215  1.00122.89           C  
ANISOU 3270  C   PHE A 220    13085  25233   8373 -12790   1346   5966
ATOM   3271  O   PHE A 220      51.535 -16.163  20.082  1.00124.13           O  
ANISOU 3271  O   PHE A 220    12464  26220   8478 -12070   1734   6654
ATOM   3272  CB  PHE A 220      53.733 -16.953  18.412  1.00126.02           C  
ANISOU 3272  CB  PHE A 220    13041  25923   8917 -13296   1321   6570
ATOM   3273  CG  PHE A 220      52.767 -16.956  17.243  1.00121.42           C  
ANISOU 3273  CG  PHE A 220    12351  25198   8584 -11899   1926   6540
ATOM   3274  CD1 PHE A 220      53.114 -16.277  16.060  1.00115.83           C  
ANISOU 3274  CD1 PHE A 220    12294  23443   8274 -11451   2071   5884
ATOM   3275  CD2 PHE A 220      51.542 -17.652  17.314  1.00125.95           C  
ANISOU 3275  CD2 PHE A 220    12184  26675   8997 -10955   2284   7084
ATOM   3276  CE1 PHE A 220      52.243 -16.302  14.956  1.00114.17           C  
ANISOU 3276  CE1 PHE A 220    12013  23051   8316 -10148   2426   5575
ATOM   3277  CE2 PHE A 220      50.663 -17.662  16.212  1.00125.32           C  
ANISOU 3277  CE2 PHE A 220    12126  26227   9263  -9600   2699   6814
ATOM   3278  CZ  PHE A 220      51.015 -16.985  15.030  1.00119.50           C  
ANISOU 3278  CZ  PHE A 220    12054  24411   8939  -9232   2699   5964
ATOM   3279  H   PHE A 220      55.072 -15.953  20.882  1.00128.45           H  
ATOM   3280  HA  PHE A 220      53.646 -14.834  18.570  1.00122.26           H  
ATOM   3281  HB3 PHE A 220      53.533 -17.827  19.028  1.00126.02           H  
ATOM   3282  HB2 PHE A 220      54.729 -17.117  17.999  1.00126.02           H  
ATOM   3283  HD1 PHE A 220      54.053 -15.747  15.991  1.00115.83           H  
ATOM   3284  HD2 PHE A 220      51.274 -18.183  18.214  1.00125.95           H  
ATOM   3285  HE1 PHE A 220      52.529 -15.795  14.055  1.00114.17           H  
ATOM   3286  HE2 PHE A 220      49.724 -18.193  16.269  1.00125.32           H  
ATOM   3287  HZ  PHE A 220      50.349 -17.003  14.180  1.00119.50           H  
ATOM   3288  N   GLY A 221      52.632 -14.505  21.154  1.00122.95           N  
ANISOU 3288  N   GLY A 221    13598  24946   8170 -12882   1140   5473
ATOM   3289  CA  GLY A 221      51.591 -14.106  22.111  1.00125.52           C  
ANISOU 3289  CA  GLY A 221    13477  26068   8146 -12173   1386   5861
ATOM   3290  C   GLY A 221      50.417 -13.375  21.441  1.00120.05           C  
ANISOU 3290  C   GLY A 221    12751  24605   8256 -11024   2142   6140
ATOM   3291  O   GLY A 221      49.979 -13.786  20.371  1.00116.86           O  
ANISOU 3291  O   GLY A 221    12208  23704   8492 -10620   2451   6251
ATOM   3292  H   GLY A 221      53.487 -13.968  21.177  1.00122.95           H  
ATOM   3293  HA3 GLY A 221      52.046 -13.462  22.863  1.00125.52           H  
ATOM   3294  HA2 GLY A 221      51.214 -14.986  22.633  1.00125.52           H  
ATOM   3295  N   ASN A 222      49.894 -12.289  22.037  1.00120.80           N  
ANISOU 3295  N   ASN A 222    12913  24619   8365 -10436   2407   6276
ATOM   3296  CA  ASN A 222      48.919 -11.420  21.358  1.00117.18           C  
ANISOU 3296  CA  ASN A 222    12403  23104   9018  -9573   3031   6581
ATOM   3297  C   ASN A 222      49.674 -10.566  20.319  1.00110.29           C  
ANISOU 3297  C   ASN A 222    12349  20755   8802  -9815   2930   5721
ATOM   3298  O   ASN A 222      49.327 -10.572  19.138  1.00106.87           O  
ANISOU 3298  O   ASN A 222    11929  19483   9191  -9600   3048   5499
ATOM   3299  CB  ASN A 222      48.211 -10.516  22.392  1.00121.57           C  
ANISOU 3299  CB  ASN A 222    12598  24100   9494  -8843   3433   7302
ATOM   3300  CG  ASN A 222      46.903  -9.940  21.839  1.00122.49           C  
ANISOU 3300  CG  ASN A 222    12205  23325  11012  -8000   4105   8115
ATOM   3301  OD1 ASN A 222      45.862 -10.587  21.905  1.00117.90           O  
ANISOU 3301  OD1 ASN A 222    11935  21374  11489  -7918   4232   7846
ATOM   3302  ND2 ASN A 222      46.957  -8.729  21.283  1.00130.63           N  
ANISOU 3302  ND2 ASN A 222    12396  25075  12164  -7378   4501   9152
ATOM   3303  H   ASN A 222      50.256 -11.995  22.932  1.00120.80           H  
ATOM   3304  HA  ASN A 222      48.177 -12.040  20.849  1.00117.18           H  
ATOM   3305  HB3 ASN A 222      48.860  -9.716  22.751  1.00121.57           H  
ATOM   3306  HB2 ASN A 222      47.954 -11.106  23.273  1.00121.57           H  
ATOM   3307 HD22 ASN A 222      46.119  -8.318  20.891  1.00130.63           H  
ATOM   3308 HD21 ASN A 222      47.831  -8.226  21.247  1.00130.63           H  
ATOM   3309  N   VAL A 223      50.773  -9.929  20.755  1.00109.52           N  
ANISOU 3309  N   VAL A 223    12940  20443   8231 -10152   2663   5162
ATOM   3310  CA  VAL A 223      51.829  -9.402  19.898  1.00104.38           C  
ANISOU 3310  CA  VAL A 223    13085  18684   7889 -10511   2472   4347
ATOM   3311  C   VAL A 223      52.699 -10.606  19.491  1.00105.40           C  
ANISOU 3311  C   VAL A 223    13256  19010   7781 -11196   2120   4113
ATOM   3312  O   VAL A 223      52.978 -11.484  20.310  1.00110.68           O  
ANISOU 3312  O   VAL A 223    13558  20681   7812 -11690   1823   4394
ATOM   3313  CB  VAL A 223      52.680  -8.377  20.694  1.00105.45           C  
ANISOU 3313  CB  VAL A 223    14018  18697   7351 -10712   2191   3787
ATOM   3314  CG1 VAL A 223      53.685  -7.657  19.784  1.00 98.15           C  
ANISOU 3314  CG1 VAL A 223    13813  16588   6891 -10757   2203   3182
ATOM   3315  CG2 VAL A 223      51.822  -7.329  21.426  1.00109.39           C  
ANISOU 3315  CG2 VAL A 223    14237  19785   7542  -9934   2509   4292
ATOM   3316  H   VAL A 223      50.990  -9.991  21.739  1.00109.52           H  
ATOM   3317  HA  VAL A 223      51.389  -8.924  19.019  1.00104.38           H  
ATOM   3318  HB  VAL A 223      53.251  -8.907  21.460  1.00105.45           H  
ATOM   3319 HG11 VAL A 223      54.269  -6.935  20.354  1.00 98.15           H  
ATOM   3320 HG12 VAL A 223      54.388  -8.354  19.331  1.00 98.15           H  
ATOM   3321 HG13 VAL A 223      53.180  -7.116  18.983  1.00 98.15           H  
ATOM   3322 HG21 VAL A 223      52.447  -6.583  21.918  1.00109.39           H  
ATOM   3323 HG22 VAL A 223      51.164  -6.809  20.729  1.00109.39           H  
ATOM   3324 HG23 VAL A 223      51.198  -7.777  22.199  1.00109.39           H  
ATOM   3325  N   GLY A 224      53.087 -10.664  18.213  1.00102.08           N  
ANISOU 3325  N   GLY A 224    13150  17807   7827 -11196   2142   3710
ATOM   3326  CA  GLY A 224      53.658 -11.842  17.579  1.00104.13           C  
ANISOU 3326  CA  GLY A 224    13289  18443   7832 -11665   1929   3768
ATOM   3327  C   GLY A 224      52.630 -12.402  16.600  1.00104.75           C  
ANISOU 3327  C   GLY A 224    12720  18791   8287 -10890   2236   4039
ATOM   3328  O   GLY A 224      52.838 -12.291  15.395  1.00102.78           O  
ANISOU 3328  O   GLY A 224    12616  18020   8415 -10411   2315   3617
ATOM   3329  H   GLY A 224      52.851  -9.890  17.611  1.00102.08           H  
ATOM   3330  HA3 GLY A 224      53.943 -12.611  18.296  1.00104.13           H  
ATOM   3331  HA2 GLY A 224      54.571 -11.562  17.054  1.00104.13           H  
ATOM   3332  N   THR A 225      51.495 -12.916  17.113  1.00109.38           N  
ANISOU 3332  N   THR A 225    12605  20228   8727 -10621   2381   4673
ATOM   3333  CA  THR A 225      50.316 -13.367  16.352  1.00111.88           C  
ANISOU 3333  CA  THR A 225    12412  20574   9525  -9634   2698   4852
ATOM   3334  C   THR A 225      49.873 -12.340  15.296  1.00109.46           C  
ANISOU 3334  C   THR A 225    12488  18876  10225  -9022   2778   4116
ATOM   3335  O   THR A 225      49.880 -12.633  14.103  1.00109.71           O  
ANISOU 3335  O   THR A 225    12570  18679  10436  -8485   2706   3583
ATOM   3336  CB  THR A 225      49.179 -13.773  17.331  1.00116.34           C  
ANISOU 3336  CB  THR A 225    12304  21806  10096  -9220   2975   5663
ATOM   3337  OG1 THR A 225      49.481 -15.042  17.874  1.00121.43           O  
ANISOU 3337  OG1 THR A 225    12393  23976   9769  -9699   2819   6314
ATOM   3338  CG2 THR A 225      47.768 -13.919  16.732  1.00118.68           C  
ANISOU 3338  CG2 THR A 225    12248  21632  11214  -8064   3306   5740
ATOM   3339  H   THR A 225      51.411 -12.943  18.119  1.00109.38           H  
ATOM   3340  HA  THR A 225      50.614 -14.253  15.792  1.00111.88           H  
ATOM   3341  HB  THR A 225      49.112 -13.043  18.134  1.00116.34           H  
ATOM   3342  HG1 THR A 225      50.200 -14.949  18.484  1.00121.43           H  
ATOM   3343 HG21 THR A 225      47.054 -14.225  17.497  1.00118.68           H  
ATOM   3344 HG22 THR A 225      47.397 -12.985  16.316  1.00118.68           H  
ATOM   3345 HG23 THR A 225      47.745 -14.669  15.949  1.00118.68           H  
ATOM   3346  N   PHE A 226      49.534 -11.121  15.738  1.00109.21           N  
ANISOU 3346  N   PHE A 226    12653  18057  10785  -9074   2877   4096
ATOM   3347  CA  PHE A 226      49.005 -10.075  14.868  1.00109.78           C  
ANISOU 3347  CA  PHE A 226    12833  16825  12053  -8589   2898   3578
ATOM   3348  C   PHE A 226      50.103  -9.222  14.206  1.00106.00           C  
ANISOU 3348  C   PHE A 226    12963  15741  11572  -8870   2658   2788
ATOM   3349  O   PHE A 226      49.768  -8.416  13.337  1.00106.75           O  
ANISOU 3349  O   PHE A 226    13072  14907  12581  -8509   2530   2203
ATOM   3350  CB  PHE A 226      48.038  -9.203  15.696  1.00112.85           C  
ANISOU 3350  CB  PHE A 226    12822  16689  13365  -8335   3218   4273
ATOM   3351  CG  PHE A 226      46.832  -9.983  16.201  1.00119.20           C  
ANISOU 3351  CG  PHE A 226    12968  17930  14392  -7802   3518   5092
ATOM   3352  CD1 PHE A 226      46.001 -10.672  15.292  1.00124.55           C  
ANISOU 3352  CD1 PHE A 226    13423  18056  15843  -7088   3486   4806
ATOM   3353  CD2 PHE A 226      46.564 -10.065  17.583  1.00123.00           C  
ANISOU 3353  CD2 PHE A 226    13061  19475  14197  -7868   3804   6091
ATOM   3354  CE1 PHE A 226      44.937 -11.466  15.761  1.00131.80           C  
ANISOU 3354  CE1 PHE A 226    13772  19348  16959  -6450   3819   5623
ATOM   3355  CE2 PHE A 226      45.502 -10.860  18.053  1.00129.74           C  
ANISOU 3355  CE2 PHE A 226    13239  20881  15176  -7267   4142   6980
ATOM   3356  CZ  PHE A 226      44.692 -11.565  17.143  1.00133.85           C  
ANISOU 3356  CZ  PHE A 226    13572  20717  16568  -6559   4192   6806
ATOM   3357  H   PHE A 226      49.555 -10.938  16.732  1.00109.21           H  
ATOM   3358  HA  PHE A 226      48.440 -10.534  14.057  1.00109.78           H  
ATOM   3359  HB3 PHE A 226      47.665  -8.366  15.103  1.00112.85           H  
ATOM   3360  HB2 PHE A 226      48.561  -8.772  16.550  1.00112.85           H  
ATOM   3361  HD1 PHE A 226      46.182 -10.608  14.232  1.00124.55           H  
ATOM   3362  HD2 PHE A 226      47.174  -9.525  18.292  1.00123.00           H  
ATOM   3363  HE1 PHE A 226      44.308 -11.995  15.060  1.00131.80           H  
ATOM   3364  HE2 PHE A 226      45.309 -10.924  19.113  1.00129.74           H  
ATOM   3365  HZ  PHE A 226      43.875 -12.172  17.503  1.00133.85           H  
ATOM   3366  N   THR A 227      51.396  -9.426  14.542  1.00103.95           N  
ANISOU 3366  N   THR A 227    13173  15965  10357  -9497   2543   2751
ATOM   3367  CA  THR A 227      52.524  -8.801  13.839  1.00101.61           C  
ANISOU 3367  CA  THR A 227    13442  15196   9968  -9618   2380   2110
ATOM   3368  C   THR A 227      52.824  -9.564  12.536  1.00103.11           C  
ANISOU 3368  C   THR A 227    13560  15740   9878  -9260   2241   1710
ATOM   3369  O   THR A 227      52.975  -8.911  11.506  1.00102.72           O  
ANISOU 3369  O   THR A 227    13671  15265  10095  -8857   2111   1047
ATOM   3370  CB  THR A 227      53.800  -8.705  14.727  1.00100.08           C  
ANISOU 3370  CB  THR A 227    13889  15087   9049 -10290   2307   2175
ATOM   3371  OG1 THR A 227      54.466  -9.933  14.916  1.00104.19           O  
ANISOU 3371  OG1 THR A 227    14412  16314   8860 -10845   2142   2455
ATOM   3372  CG2 THR A 227      53.578  -8.043  16.092  1.00101.45           C  
ANISOU 3372  CG2 THR A 227    14079  15324   9145 -10373   2421   2541
ATOM   3373  H   THR A 227      51.604 -10.127  15.237  1.00103.95           H  
ATOM   3374  HA  THR A 227      52.246  -7.782  13.570  1.00101.61           H  
ATOM   3375  HB  THR A 227      54.517  -8.082  14.191  1.00100.08           H  
ATOM   3376  HG1 THR A 227      53.869 -10.559  15.298  1.00104.19           H  
ATOM   3377 HG21 THR A 227      54.489  -8.058  16.694  1.00101.45           H  
ATOM   3378 HG22 THR A 227      53.297  -7.004  15.969  1.00101.45           H  
ATOM   3379 HG23 THR A 227      52.790  -8.527  16.663  1.00101.45           H  
ATOM   3380  N   VAL A 228      52.851 -10.916  12.546  1.00 73.95           N  
ANISOU 3380  N   VAL A 228     8233  13114   6751  -4245   1871    455
ATOM   3381  CA  VAL A 228      53.064 -11.720  11.333  1.00 76.83           C  
ANISOU 3381  CA  VAL A 228     8589  13701   6901  -4356   2057    487
ATOM   3382  C   VAL A 228      51.834 -11.672  10.408  1.00 76.52           C  
ANISOU 3382  C   VAL A 228     8516  13747   6811  -4087   2186    316
ATOM   3383  O   VAL A 228      51.998 -11.772   9.192  1.00 77.71           O  
ANISOU 3383  O   VAL A 228     8844  13935   6746  -4135   2263    314
ATOM   3384  CB  VAL A 228      53.460 -13.194  11.639  1.00 80.34           C  
ANISOU 3384  CB  VAL A 228     8780  14459   7287  -4617   2227    579
ATOM   3385  CG1 VAL A 228      54.583 -13.322  12.677  1.00 80.29           C  
ANISOU 3385  CG1 VAL A 228     8772  14372   7364  -4890   2081    708
ATOM   3386  CG2 VAL A 228      52.315 -14.153  11.986  1.00 81.77           C  
ANISOU 3386  CG2 VAL A 228     8579  14936   7555  -4439   2435    480
ATOM   3387  H   VAL A 228      52.719 -11.408  13.419  1.00 73.95           H  
ATOM   3388  HA  VAL A 228      53.900 -11.275  10.793  1.00 76.83           H  
ATOM   3389  HB  VAL A 228      53.879 -13.570  10.704  1.00 80.34           H  
ATOM   3390 HG11 VAL A 228      55.127 -14.251  12.536  1.00 80.29           H  
ATOM   3391 HG12 VAL A 228      55.291 -12.507  12.595  1.00 80.29           H  
ATOM   3392 HG13 VAL A 228      54.209 -13.327  13.695  1.00 80.29           H  
ATOM   3393 HG21 VAL A 228      52.686 -15.175  12.030  1.00 81.77           H  
ATOM   3394 HG22 VAL A 228      51.859 -13.900  12.942  1.00 81.77           H  
ATOM   3395 HG23 VAL A 228      51.535 -14.157  11.230  1.00 81.77           H  
ATOM   3396  N   LYS A 229      50.624 -11.482  10.975  1.00 75.23           N  
ANISOU 3396  N   LYS A 229     8159  13594   6831  -3826   2203    179
ATOM   3397  CA  LYS A 229      49.371 -11.301  10.240  1.00 75.14           C  
ANISOU 3397  CA  LYS A 229     8147  13609   6795  -3561   2342     -2
ATOM   3398  C   LYS A 229      49.437 -10.052   9.358  1.00 73.92           C  
ANISOU 3398  C   LYS A 229     8325  13242   6521  -3525   2204    -35
ATOM   3399  O   LYS A 229      49.137 -10.131   8.171  1.00 75.46           O  
ANISOU 3399  O   LYS A 229     8665  13509   6496  -3552   2328   -101
ATOM   3400  CB  LYS A 229      48.182 -11.169  11.219  1.00 73.47           C  
ANISOU 3400  CB  LYS A 229     7710  13373   6832  -3279   2335   -108
ATOM   3401  CG  LYS A 229      46.816 -11.072  10.502  1.00 73.45           C  
ANISOU 3401  CG  LYS A 229     7750  13335   6824  -2997   2486   -303
ATOM   3402  CD  LYS A 229      45.619 -10.893  11.444  1.00 73.32           C  
ANISOU 3402  CD  LYS A 229     7453  13347   7057  -2723   2542   -366
ATOM   3403  CE  LYS A 229      44.302 -10.819  10.656  1.00 74.36           C  
ANISOU 3403  CE  LYS A 229     7594  13482   7178  -2457   2809   -550
ATOM   3404  NZ  LYS A 229      43.153 -10.533  11.527  1.00 71.99           N1+
ANISOU 3404  NZ  LYS A 229     7379  12948   7026  -2213   2680   -664
ATOM   3405  H   LYS A 229      50.578 -11.437  11.982  1.00 75.23           H  
ATOM   3406  HA  LYS A 229      49.221 -12.178   9.607  1.00 75.14           H  
ATOM   3407  HB3 LYS A 229      48.314 -10.282  11.837  1.00 73.47           H  
ATOM   3408  HB2 LYS A 229      48.180 -12.016  11.904  1.00 73.47           H  
ATOM   3409  HG3 LYS A 229      46.669 -11.956   9.881  1.00 73.45           H  
ATOM   3410  HG2 LYS A 229      46.811 -10.226   9.815  1.00 73.45           H  
ATOM   3411  HD3 LYS A 229      45.754  -9.974  12.017  1.00 73.32           H  
ATOM   3412  HD2 LYS A 229      45.580 -11.707  12.166  1.00 73.32           H  
ATOM   3413  HE3 LYS A 229      44.120 -11.750  10.119  1.00 74.36           H  
ATOM   3414  HE2 LYS A 229      44.360 -10.025   9.911  1.00 74.36           H  
ATOM   3415  HZ1 LYS A 229      42.999 -11.300  12.164  1.00 71.99           H  
ATOM   3416  HZ2 LYS A 229      43.334  -9.698  12.079  1.00 71.99           H  
ATOM   3417  HZ3 LYS A 229      42.322 -10.386  10.972  1.00 71.99           H  
ATOM   3418  N   ASN A 230      49.824  -8.908   9.941  1.00 71.81           N  
ANISOU 3418  N   ASN A 230     8178  12716   6390  -3482   1954     25
ATOM   3419  CA  ASN A 230      49.862  -7.631   9.240  1.00 71.09           C  
ANISOU 3419  CA  ASN A 230     8332  12435   6244  -3426   1798     35
ATOM   3420  C   ASN A 230      51.133  -7.424   8.404  1.00 72.94           C  
ANISOU 3420  C   ASN A 230     8785  12653   6275  -3666   1713    229
ATOM   3421  O   ASN A 230      51.109  -6.580   7.509  1.00 73.36           O  
ANISOU 3421  O   ASN A 230     9019  12641   6211  -3669   1599    266
ATOM   3422  CB  ASN A 230      49.658  -6.477  10.238  1.00 68.31           C  
ANISOU 3422  CB  ASN A 230     7997  11814   6144  -3249   1608     37
ATOM   3423  CG  ASN A 230      48.177  -6.318  10.585  1.00 67.60           C  
ANISOU 3423  CG  ASN A 230     7804  11706   6176  -2981   1656   -164
ATOM   3424  OD1 ASN A 230      47.411  -5.822   9.762  1.00 68.25           O  
ANISOU 3424  OD1 ASN A 230     7998  11750   6186  -2893   1646   -254
ATOM   3425  ND2 ASN A 230      47.765  -6.746  11.778  1.00 65.78           N  
ANISOU 3425  ND2 ASN A 230     7369  11505   6121  -2870   1700   -223
ATOM   3426  H   ASN A 230      50.067  -8.916  10.922  1.00 71.81           H  
ATOM   3427  HA  ASN A 230      49.036  -7.615   8.534  1.00 71.09           H  
ATOM   3428  HB3 ASN A 230      49.967  -5.531   9.796  1.00 68.31           H  
ATOM   3429  HB2 ASN A 230      50.253  -6.619  11.142  1.00 68.31           H  
ATOM   3430 HD22 ASN A 230      46.794  -6.650  12.039  1.00 65.78           H  
ATOM   3431 HD21 ASN A 230      48.426  -7.166  12.421  1.00 65.78           H  
ATOM   3432  N   ILE A 231      52.193  -8.230   8.610  1.00 74.25           N  
ANISOU 3432  N   ILE A 231     8933  12891   6389  -3888   1758    371
ATOM   3433  CA  ILE A 231      53.313  -8.366   7.672  1.00 75.97           C  
ANISOU 3433  CA  ILE A 231     9352  13123   6389  -4126   1715    569
ATOM   3434  C   ILE A 231      52.822  -9.043   6.371  1.00 77.99           C  
ANISOU 3434  C   ILE A 231     9674  13613   6345  -4197   1874    474
ATOM   3435  O   ILE A 231      53.170  -8.561   5.295  1.00 79.30           O  
ANISOU 3435  O   ILE A 231    10056  13762   6311  -4291   1764    568
ATOM   3436  CB  ILE A 231      54.509  -9.107   8.353  1.00 77.55           C  
ANISOU 3436  CB  ILE A 231     9539  13341   6586  -4374   1757    734
ATOM   3437  CG1 ILE A 231      55.233  -8.165   9.348  1.00 75.15           C  
ANISOU 3437  CG1 ILE A 231     9311  12721   6523  -4342   1591    846
ATOM   3438  CG2 ILE A 231      55.530  -9.694   7.356  1.00 80.56           C  
ANISOU 3438  CG2 ILE A 231    10115  13802   6691  -4631   1774    925
ATOM   3439  CD1 ILE A 231      56.154  -8.877  10.353  1.00 75.53           C  
ANISOU 3439  CD1 ILE A 231     9386  12733   6579  -4607   1632    980
ATOM   3440  H   ILE A 231      52.158  -8.879   9.383  1.00 74.25           H  
ATOM   3441  HA  ILE A 231      53.652  -7.365   7.397  1.00 75.97           H  
ATOM   3442  HB  ILE A 231      54.100  -9.945   8.916  1.00 77.55           H  
ATOM   3443 HG13 ILE A 231      54.501  -7.590   9.914  1.00 75.15           H  
ATOM   3444 HG12 ILE A 231      55.811  -7.424   8.796  1.00 75.15           H  
ATOM   3445 HG21 ILE A 231      56.403 -10.116   7.851  1.00 80.56           H  
ATOM   3446 HG22 ILE A 231      55.088 -10.503   6.779  1.00 80.56           H  
ATOM   3447 HG23 ILE A 231      55.890  -8.940   6.657  1.00 80.56           H  
ATOM   3448 HD11 ILE A 231      56.575  -8.162  11.061  1.00 75.53           H  
ATOM   3449 HD12 ILE A 231      55.615  -9.626  10.931  1.00 75.53           H  
ATOM   3450 HD13 ILE A 231      56.990  -9.371   9.863  1.00 75.53           H  
ATOM   3451  N   GLU A 232      51.962 -10.079   6.459  1.00 78.98           N  
ANISOU 3451  N   GLU A 232     9615  13952   6441  -4151   2140    299
ATOM   3452  CA  GLU A 232      51.310 -10.723   5.310  1.00 81.27           C  
ANISOU 3452  CA  GLU A 232     9990  14435   6455  -4184   2377    157
ATOM   3453  C   GLU A 232      50.290  -9.796   4.618  1.00 80.15           C  
ANISOU 3453  C   GLU A 232    10011  14177   6266  -4025   2288      5
ATOM   3454  O   GLU A 232      50.230  -9.797   3.389  1.00 81.64           O  
ANISOU 3454  O   GLU A 232    10460  14410   6151  -4170   2276     -3
ATOM   3455  CB  GLU A 232      50.598 -12.023   5.737  1.00 82.58           C  
ANISOU 3455  CB  GLU A 232     9878  14811   6688  -4091   2718     16
ATOM   3456  CG  GLU A 232      51.549 -13.207   6.006  1.00 84.58           C  
ANISOU 3456  CG  GLU A 232     9972  15254   6912  -4314   2858    166
ATOM   3457  CD  GLU A 232      50.816 -14.522   6.303  1.00 88.02           C  
ANISOU 3457  CD  GLU A 232    10112  15939   7393  -4221   3237     60
ATOM   3458  OE1 GLU A 232      49.567 -14.538   6.226  1.00 88.42           O  
ANISOU 3458  OE1 GLU A 232    10086  15979   7529  -3948   3392   -130
ATOM   3459  OE2 GLU A 232      51.525 -15.504   6.612  1.00 89.55           O1-
ANISOU 3459  OE2 GLU A 232    10139  16332   7553  -4415   3394    185
ATOM   3460  H   GLU A 232      51.720 -10.426   7.377  1.00 78.98           H  
ATOM   3461  HA  GLU A 232      52.064 -10.976   4.570  1.00 81.27           H  
ATOM   3462  HB3 GLU A 232      49.910 -12.321   4.942  1.00 82.58           H  
ATOM   3463  HB2 GLU A 232      49.976 -11.853   6.614  1.00 82.58           H  
ATOM   3464  HG3 GLU A 232      52.212 -12.979   6.840  1.00 84.58           H  
ATOM   3465  HG2 GLU A 232      52.188 -13.370   5.138  1.00 84.58           H  
ATOM   3466  N   ARG A 233      49.532  -8.974   5.372  1.00 77.40           N  
ANISOU 3466  N   ARG A 233     9524  13682   6203  -3762   2207   -103
ATOM   3467  CA  ARG A 233      48.577  -7.999   4.819  1.00 76.01           C  
ANISOU 3467  CA  ARG A 233     9476  13373   6032  -3612   2110   -241
ATOM   3468  C   ARG A 233      49.256  -6.781   4.159  1.00 75.98           C  
ANISOU 3468  C   ARG A 233     9705  13260   5905  -3762   1804    -62
ATOM   3469  O   ARG A 233      48.570  -6.029   3.467  1.00 76.59           O  
ANISOU 3469  O   ARG A 233     9957  13308   5834  -3778   1727   -142
ATOM   3470  CB  ARG A 233      47.627  -7.467   5.913  1.00 72.85           C  
ANISOU 3470  CB  ARG A 233     8881  12815   5983  -3322   2047   -333
ATOM   3471  CG  ARG A 233      46.627  -8.505   6.454  1.00 73.29           C  
ANISOU 3471  CG  ARG A 233     8730  12969   6148  -3114   2338   -533
ATOM   3472  CD  ARG A 233      45.685  -7.931   7.525  1.00 71.44           C  
ANISOU 3472  CD  ARG A 233     8367  12560   6218  -2833   2238   -617
ATOM   3473  NE  ARG A 233      44.847  -6.853   6.977  1.00 71.89           N  
ANISOU 3473  NE  ARG A 233     8627  12460   6229  -2748   2155   -743
ATOM   3474  CZ  ARG A 233      44.209  -5.896   7.673  1.00 68.21           C  
ANISOU 3474  CZ  ARG A 233     8127  11807   5984  -2540   2035   -807
ATOM   3475  NH1 ARG A 233      44.265  -5.844   9.010  1.00 65.56           N  
ANISOU 3475  NH1 ARG A 233     7582  11407   5922  -2385   1977   -764
ATOM   3476  NH2 ARG A 233      43.499  -4.974   7.013  1.00 68.12           N1+
ANISOU 3476  NH2 ARG A 233     8309  11676   5898  -2519   1967   -910
ATOM   3477  H   ARG A 233      49.617  -9.032   6.379  1.00 77.40           H  
ATOM   3478  HA  ARG A 233      47.980  -8.494   4.050  1.00 76.01           H  
ATOM   3479  HB3 ARG A 233      47.042  -6.644   5.498  1.00 72.85           H  
ATOM   3480  HB2 ARG A 233      48.200  -7.016   6.717  1.00 72.85           H  
ATOM   3481  HG3 ARG A 233      47.155  -9.361   6.866  1.00 73.29           H  
ATOM   3482  HG2 ARG A 233      46.033  -8.898   5.628  1.00 73.29           H  
ATOM   3483  HD3 ARG A 233      46.269  -7.571   8.368  1.00 71.44           H  
ATOM   3484  HD2 ARG A 233      45.033  -8.715   7.907  1.00 71.44           H  
ATOM   3485  HE  ARG A 233      44.737  -6.855   5.973  1.00 71.89           H  
ATOM   3486 HH12 ARG A 233      43.724  -5.145   9.518  1.00 65.56           H  
ATOM   3487 HH11 ARG A 233      44.838  -6.495   9.526  1.00 65.56           H  
ATOM   3488 HH22 ARG A 233      43.053  -4.218   7.535  1.00 68.12           H  
ATOM   3489 HH21 ARG A 233      43.428  -4.985   6.008  1.00 68.12           H  
ATOM   3490  N   GLN A 234      50.578  -6.598   4.333  1.00 75.60           N  
ANISOU 3490  N   GLN A 234     9658  13149   5916  -3883   1633    200
ATOM   3491  CA  GLN A 234      51.372  -5.514   3.749  1.00 76.19           C  
ANISOU 3491  CA  GLN A 234     9907  13123   5919  -3996   1345    436
ATOM   3492  C   GLN A 234      52.502  -6.040   2.844  1.00 79.41           C  
ANISOU 3492  C   GLN A 234    10505  13671   5994  -4300   1311    641
ATOM   3493  O   GLN A 234      53.481  -5.337   2.599  1.00 79.78           O  
ANISOU 3493  O   GLN A 234    10645  13629   6038  -4389   1059    928
ATOM   3494  CB  GLN A 234      51.813  -4.507   4.838  1.00 73.97           C  
ANISOU 3494  CB  GLN A 234     9539  12581   5985  -3849   1140    616
ATOM   3495  CG  GLN A 234      50.636  -3.642   5.337  1.00 72.71           C  
ANISOU 3495  CG  GLN A 234     9381  12277   5967  -3679    955    588
ATOM   3496  CD  GLN A 234      51.031  -2.609   6.394  1.00 70.91           C  
ANISOU 3496  CD  GLN A 234     9019  11802   6123  -3436    901    596
ATOM   3497  OE1 GLN A 234      51.892  -2.862   7.235  1.00 71.56           O  
ANISOU 3497  OE1 GLN A 234     9028  11809   6351  -3409    990    610
ATOM   3498  NE2 GLN A 234      50.393  -1.438   6.364  1.00 71.75           N  
ANISOU 3498  NE2 GLN A 234     9106  11775   6379  -3284    758    588
ATOM   3499  H   GLN A 234      51.071  -7.259   4.917  1.00 75.60           H  
ATOM   3500  HA  GLN A 234      50.755  -4.953   3.045  1.00 76.19           H  
ATOM   3501  HB3 GLN A 234      52.570  -3.834   4.438  1.00 73.97           H  
ATOM   3502  HB2 GLN A 234      52.285  -5.039   5.665  1.00 73.97           H  
ATOM   3503  HG3 GLN A 234      49.867  -4.278   5.777  1.00 72.71           H  
ATOM   3504  HG2 GLN A 234      50.170  -3.132   4.492  1.00 72.71           H  
ATOM   3505 HE22 GLN A 234      50.609  -0.736   7.057  1.00 71.75           H  
ATOM   3506 HE21 GLN A 234      49.675  -1.259   5.676  1.00 71.75           H  
ATOM   3507  N   GLY A 235      52.322  -7.251   2.287  1.00 82.04           N  
ANISOU 3507  N   GLY A 235    10891  14224   6056  -4448   1579    512
ATOM   3508  CA  GLY A 235      53.099  -7.801   1.177  1.00 85.58           C  
ANISOU 3508  CA  GLY A 235    11569  14837   6112  -4763   1585    663
ATOM   3509  C   GLY A 235      54.377  -8.563   1.550  1.00 86.90           C  
ANISOU 3509  C   GLY A 235    11700  15045   6273  -4924   1649    876
ATOM   3510  O   GLY A 235      54.945  -9.224   0.684  1.00 90.10           O  
ANISOU 3510  O   GLY A 235    12275  15618   6342  -5190   1740    971
ATOM   3511  H   GLY A 235      51.504  -7.775   2.563  1.00 82.04           H  
ATOM   3512  HA3 GLY A 235      53.363  -7.007   0.476  1.00 85.58           H  
ATOM   3513  HA2 GLY A 235      52.448  -8.483   0.626  1.00 85.58           H  
ATOM   3514  N   GLY A 236      54.814  -8.506   2.818  1.00 84.63           N  
ANISOU 3514  N   GLY A 236    11224  14595   6336  -4791   1606    950
ATOM   3515  CA  GLY A 236      55.926  -9.288   3.358  1.00 85.93           C  
ANISOU 3515  CA  GLY A 236    11353  14771   6524  -4959   1687   1122
ATOM   3516  C   GLY A 236      55.481 -10.679   3.826  1.00 86.77           C  
ANISOU 3516  C   GLY A 236    11270  15088   6610  -4999   2016    938
ATOM   3517  O   GLY A 236      54.326 -11.061   3.655  1.00 87.09           O  
ANISOU 3517  O   GLY A 236    11229  15276   6584  -4890   2222    690
ATOM   3518  H   GLY A 236      54.269  -7.970   3.480  1.00 84.63           H  
ATOM   3519  HA3 GLY A 236      56.351  -8.749   4.205  1.00 85.93           H  
ATOM   3520  HA2 GLY A 236      56.725  -9.391   2.624  1.00 85.93           H  
ATOM   3521  N   LYS A 237      56.409 -11.435   4.432  1.00 87.52           N  
ANISOU 3521  N   LYS A 237    11291  15190   6773  -5158   2078   1077
ATOM   3522  CA  LYS A 237      56.154 -12.713   5.104  1.00 88.82           C  
ANISOU 3522  CA  LYS A 237    11209  15571   6970  -5213   2361    961
ATOM   3523  C   LYS A 237      57.288 -13.046   6.084  1.00 89.47           C  
ANISOU 3523  C   LYS A 237    11214  15595   7186  -5411   2338   1139
ATOM   3524  O   LYS A 237      58.407 -12.547   5.949  1.00 90.14           O  
ANISOU 3524  O   LYS A 237    11512  15497   7241  -5564   2181   1367
ATOM   3525  CB  LYS A 237      55.837 -13.846   4.106  1.00 91.89           C  
ANISOU 3525  CB  LYS A 237    11657  16239   7019  -5345   2651    879
ATOM   3526  CG  LYS A 237      57.011 -14.226   3.194  1.00 95.30           C  
ANISOU 3526  CG  LYS A 237    12113  16843   7255  -5659   2828   1038
ATOM   3527  CD  LYS A 237      56.545 -14.969   1.940  1.00 99.90           C  
ANISOU 3527  CD  LYS A 237    12895  17626   7436  -5784   3060    968
ATOM   3528  CE  LYS A 237      57.701 -15.243   0.974  1.00102.70           C  
ANISOU 3528  CE  LYS A 237    13601  17941   7480  -6064   2891   1222
ATOM   3529  NZ  LYS A 237      57.206 -15.797  -0.296  1.00106.97           N1+
ANISOU 3529  NZ  LYS A 237    14397  18678   7568  -6228   3104   1145
ATOM   3530  H   LYS A 237      57.344 -11.065   4.523  1.00 87.52           H  
ATOM   3531  HA  LYS A 237      55.260 -12.572   5.716  1.00 88.82           H  
ATOM   3532  HB3 LYS A 237      54.978 -13.556   3.498  1.00 91.89           H  
ATOM   3533  HB2 LYS A 237      55.510 -14.734   4.648  1.00 91.89           H  
ATOM   3534  HG3 LYS A 237      57.738 -14.829   3.744  1.00 95.30           H  
ATOM   3535  HG2 LYS A 237      57.536 -13.325   2.880  1.00 95.30           H  
ATOM   3536  HD3 LYS A 237      55.792 -14.365   1.429  1.00 99.90           H  
ATOM   3537  HD2 LYS A 237      56.055 -15.902   2.219  1.00 99.90           H  
ATOM   3538  HE3 LYS A 237      58.407 -15.943   1.421  1.00102.70           H  
ATOM   3539  HE2 LYS A 237      58.246 -14.323   0.759  1.00102.70           H  
ATOM   3540  HZ1 LYS A 237      56.571 -15.136  -0.725  1.00106.97           H  
ATOM   3541  HZ2 LYS A 237      57.979 -15.970  -0.921  1.00106.97           H  
ATOM   3542  HZ3 LYS A 237      56.715 -16.661  -0.117  1.00106.97           H  
ATOM   3543  N   VAL A 238      56.977 -13.899   7.071  1.00 89.56           N  
ANISOU 3543  N   VAL A 238    10925  15751   7353  -5414   2488   1050
ATOM   3544  CA  VAL A 238      57.854 -14.271   8.178  1.00 90.16           C  
ANISOU 3544  CA  VAL A 238    10929  15768   7560  -5634   2440   1192
ATOM   3545  C   VAL A 238      58.239 -15.748   8.026  1.00 93.75           C  
ANISOU 3545  C   VAL A 238    11242  16509   7868  -5932   2680   1279
ATOM   3546  O   VAL A 238      57.392 -16.625   8.204  1.00 95.05           O  
ANISOU 3546  O   VAL A 238    11107  16960   8049  -5876   2912   1168
ATOM   3547  CB  VAL A 238      57.094 -14.001   9.502  1.00 88.12           C  
ANISOU 3547  CB  VAL A 238    10427  15454   7602  -5487   2359   1080
ATOM   3548  CG1 VAL A 238      57.856 -14.492  10.742  1.00 89.49           C  
ANISOU 3548  CG1 VAL A 238    10557  15591   7854  -5795   2314   1218
ATOM   3549  CG2 VAL A 238      56.753 -12.508   9.655  1.00 84.36           C  
ANISOU 3549  CG2 VAL A 238    10103  14665   7285  -5220   2135   1016
ATOM   3550  H   VAL A 238      56.041 -14.279   7.090  1.00 89.56           H  
ATOM   3551  HA  VAL A 238      58.762 -13.666   8.170  1.00 90.16           H  
ATOM   3552  HB  VAL A 238      56.147 -14.544   9.480  1.00 88.12           H  
ATOM   3553 HG11 VAL A 238      57.327 -14.219  11.652  1.00 89.49           H  
ATOM   3554 HG12 VAL A 238      57.956 -15.576  10.752  1.00 89.49           H  
ATOM   3555 HG13 VAL A 238      58.852 -14.057  10.799  1.00 89.49           H  
ATOM   3556 HG21 VAL A 238      56.276 -12.300  10.608  1.00 84.36           H  
ATOM   3557 HG22 VAL A 238      57.648 -11.891   9.597  1.00 84.36           H  
ATOM   3558 HG23 VAL A 238      56.060 -12.176   8.881  1.00 84.36           H  
ATOM   3559  N   CYS A 239      59.518 -16.017   7.709  1.00 95.63           N  
ANISOU 3559  N   CYS A 239    11687  16662   7987  -6239   2643   1494
ATOM   3560  CA  CYS A 239      60.072 -17.359   7.526  1.00 99.26           C  
ANISOU 3560  CA  CYS A 239    12019  17381   8314  -6563   2866   1602
ATOM   3561  C   CYS A 239      60.298 -18.098   8.859  1.00 99.67           C  
ANISOU 3561  C   CYS A 239    11795  17488   8586  -6735   2844   1629
ATOM   3562  O   CYS A 239      59.886 -19.250   8.975  1.00101.07           O  
ANISOU 3562  O   CYS A 239    11585  17982   8834  -6745   3025   1573
ATOM   3563  CB  CYS A 239      61.372 -17.281   6.688  1.00101.39           C  
ANISOU 3563  CB  CYS A 239    12637  17552   8337  -6846   2852   1835
ATOM   3564  SG  CYS A 239      62.683 -16.234   7.399  1.00101.08           S  
ANISOU 3564  SG  CYS A 239    12934  17036   8436  -6957   2562   2047
ATOM   3565  H   CYS A 239      60.158 -15.241   7.623  1.00 95.63           H  
ATOM   3566  HA  CYS A 239      59.363 -17.957   6.955  1.00 99.26           H  
ATOM   3567  HB3 CYS A 239      61.137 -16.895   5.696  1.00101.39           H  
ATOM   3568  HB2 CYS A 239      61.775 -18.281   6.531  1.00101.39           H  
ATOM   3569  HG  CYS A 239      63.567 -16.426   6.418  1.00101.08           H  
ATOM   3570  N   ALA A 240      60.919 -17.446   9.857  1.00 98.55           N  
ANISOU 3570  N   ALA A 240    11853  17036   8557  -6869   2629   1725
ATOM   3571  CA  ALA A 240      61.216 -17.997  11.178  1.00 99.42           C  
ANISOU 3571  CA  ALA A 240    11783  17174   8816  -7120   2577   1760
ATOM   3572  C   ALA A 240      60.316 -17.342  12.230  1.00 96.71           C  
ANISOU 3572  C   ALA A 240    11284  16746   8714  -6886   2412   1602
ATOM   3573  O   ALA A 240      60.057 -16.144  12.159  1.00 94.00           O  
ANISOU 3573  O   ALA A 240    11191  16068   8458  -6674   2247   1544
ATOM   3574  CB  ALA A 240      62.683 -17.676  11.516  1.00100.61           C  
ANISOU 3574  CB  ALA A 240    12300  17010   8918  -7460   2480   1945
ATOM   3575  H   ALA A 240      61.198 -16.489   9.691  1.00 98.55           H  
ATOM   3576  HA  ALA A 240      61.063 -19.076  11.209  1.00 99.42           H  
ATOM   3577  HB1 ALA A 240      62.956 -18.055  12.501  1.00100.61           H  
ATOM   3578  HB2 ALA A 240      63.356 -18.136  10.793  1.00100.61           H  
ATOM   3579  HB3 ALA A 240      62.877 -16.603  11.507  1.00100.61           H  
ATOM   3580  N   ILE A 241      59.887 -18.116  13.236  1.00 97.82           N  
ANISOU 3580  N   ILE A 241    11000  17197   8972  -6921   2459   1557
ATOM   3581  CA  ILE A 241      59.145 -17.618  14.397  1.00 95.86           C  
ANISOU 3581  CA  ILE A 241    10628  16866   8929  -6789   2270   1453
ATOM   3582  C   ILE A 241      60.087 -17.740  15.609  1.00 97.61           C  
ANISOU 3582  C   ILE A 241    10958  16957   9173  -7216   2110   1552
ATOM   3583  O   ILE A 241      61.013 -16.935  15.713  1.00 97.62           O  
ANISOU 3583  O   ILE A 241    11402  16575   9116  -7365   2031   1601
ATOM   3584  CB  ILE A 241      57.730 -18.277  14.510  1.00 95.91           C  
ANISOU 3584  CB  ILE A 241    10126  17236   9078  -6528   2361   1362
ATOM   3585  CG1 ILE A 241      56.855 -18.011  13.262  1.00 94.64           C  
ANISOU 3585  CG1 ILE A 241     9939  17156   8864  -6146   2562   1240
ATOM   3586  CG2 ILE A 241      56.931 -17.887  15.774  1.00 93.54           C  
ANISOU 3586  CG2 ILE A 241     9747  16825   8968  -6375   2140   1269
ATOM   3587  CD1 ILE A 241      56.255 -16.606  13.157  1.00 88.76           C  
ANISOU 3587  CD1 ILE A 241     9493  16090   8140  -5810   2436   1095
ATOM   3588  H   ILE A 241      60.136 -19.095  13.231  1.00 97.82           H  
ATOM   3589  HA  ILE A 241      58.966 -16.550  14.286  1.00 95.86           H  
ATOM   3590  HB  ILE A 241      57.886 -19.354  14.550  1.00 95.91           H  
ATOM   3591 HG13 ILE A 241      56.041 -18.735  13.230  1.00 94.64           H  
ATOM   3592 HG12 ILE A 241      57.444 -18.175  12.370  1.00 94.64           H  
ATOM   3593 HG21 ILE A 241      55.894 -18.216  15.698  1.00 93.54           H  
ATOM   3594 HG22 ILE A 241      57.322 -18.353  16.674  1.00 93.54           H  
ATOM   3595 HG23 ILE A 241      56.923 -16.808  15.934  1.00 93.54           H  
ATOM   3596 HD11 ILE A 241      55.770 -16.477  12.188  1.00 88.76           H  
ATOM   3597 HD12 ILE A 241      55.502 -16.425  13.925  1.00 88.76           H  
ATOM   3598 HD13 ILE A 241      57.021 -15.840  13.255  1.00 88.76           H  
ATOM   3599  N   ALA A 242      59.866 -18.728  16.489  1.00 99.45           N  
ANISOU 3599  N   ALA A 242    10801  17503   9485  -7424   2073   1598
ATOM   3600  CA  ALA A 242      60.398 -18.923  17.845  1.00100.95           C  
ANISOU 3600  CA  ALA A 242    11063  17610   9682  -7855   1880   1666
ATOM   3601  C   ALA A 242      59.309 -18.725  18.903  1.00100.00           C  
ANISOU 3601  C   ALA A 242    10652  17625   9719  -7722   1705   1591
ATOM   3602  O   ALA A 242      58.565 -17.747  18.858  1.00 96.64           O  
ANISOU 3602  O   ALA A 242    10232  17089   9398  -7278   1673   1446
ATOM   3603  CB  ALA A 242      61.748 -18.252  18.164  1.00 99.86           C  
ANISOU 3603  CB  ALA A 242    11546  16930   9466  -8017   1785   1654
ATOM   3604  H   ALA A 242      59.096 -19.338  16.257  1.00 99.45           H  
ATOM   3605  HA  ALA A 242      60.628 -19.977  17.869  1.00100.95           H  
ATOM   3606  HB1 ALA A 242      62.125 -18.587  19.131  1.00 99.86           H  
ATOM   3607  HB2 ALA A 242      62.503 -18.508  17.420  1.00 99.86           H  
ATOM   3608  HB3 ALA A 242      61.675 -17.169  18.210  1.00 99.86           H  
ATOM   3609  N   GLU A 243      59.201 -19.692  19.825  1.00103.09           N  
ANISOU 3609  N   GLU A 243    10784  18267  10118  -8129   1578   1710
ATOM   3610  CA  GLU A 243      58.179 -19.807  20.865  1.00103.26           C  
ANISOU 3610  CA  GLU A 243    10430  18525  10278  -8050   1399   1709
ATOM   3611  C   GLU A 243      58.725 -20.656  22.036  1.00107.36           C  
ANISOU 3611  C   GLU A 243    10766  19283  10744  -8658   1204   1884
ATOM   3612  O   GLU A 243      59.863 -21.125  21.984  1.00110.30           O  
ANISOU 3612  O   GLU A 243    11298  19630  10980  -9120   1238   1987
ATOM   3613  CB  GLU A 243      56.848 -20.272  20.204  1.00103.00           C  
ANISOU 3613  CB  GLU A 243     9848  18877  10411  -7591   1578   1719
ATOM   3614  CG  GLU A 243      55.596 -20.447  21.091  1.00103.33           C  
ANISOU 3614  CG  GLU A 243     9437  19189  10635  -7418   1429   1760
ATOM   3615  CD  GLU A 243      55.174 -19.164  21.811  1.00100.40           C  
ANISOU 3615  CD  GLU A 243     9389  18467  10290  -7197   1223   1586
ATOM   3616  OE1 GLU A 243      54.253 -18.491  21.299  1.00 97.01           O  
ANISOU 3616  OE1 GLU A 243     9006  17901   9951  -6687   1323   1435
ATOM   3617  OE2 GLU A 243      55.774 -18.878  22.869  1.00101.26           O1-
ANISOU 3617  OE2 GLU A 243     9716  18439  10319  -7555    969   1601
ATOM   3618  H   GLU A 243      59.884 -20.441  19.802  1.00103.09           H  
ATOM   3619  HA  GLU A 243      58.027 -18.808  21.275  1.00103.26           H  
ATOM   3620  HB3 GLU A 243      57.031 -21.218  19.694  1.00103.00           H  
ATOM   3621  HB2 GLU A 243      56.583 -19.572  19.410  1.00103.00           H  
ATOM   3622  HG3 GLU A 243      55.733 -21.246  21.819  1.00103.33           H  
ATOM   3623  HG2 GLU A 243      54.765 -20.773  20.465  1.00103.33           H  
ATOM   3624  N   TRP A 244      57.940 -20.842  23.107  1.00107.93           N  
ANISOU 3624  N   TRP A 244    10519  19581  10909  -8684    984   1931
ATOM   3625  CA  TRP A 244      58.305 -21.569  24.323  1.00112.07           C  
ANISOU 3625  CA  TRP A 244    10877  20345  11359  -9298    735   2109
ATOM   3626  C   TRP A 244      57.206 -22.560  24.743  1.00115.01           C  
ANISOU 3626  C   TRP A 244    10462  21322  11914  -9264    639   2334
ATOM   3627  O   TRP A 244      56.018 -22.256  24.635  1.00112.68           O  
ANISOU 3627  O   TRP A 244     9881  21135  11798  -8755    659   2299
ATOM   3628  CB  TRP A 244      58.675 -20.553  25.422  1.00110.99           C  
ANISOU 3628  CB  TRP A 244    11298  19799  11076  -9564    474   1976
ATOM   3629  CG  TRP A 244      59.123 -21.143  26.726  1.00116.57           C  
ANISOU 3629  CG  TRP A 244    11929  20719  11644 -10276    192   2140
ATOM   3630  CD1 TRP A 244      60.407 -21.333  27.099  1.00120.62           C  
ANISOU 3630  CD1 TRP A 244    12792  21088  11950 -10924    156   2191
ATOM   3631  CD2 TRP A 244      58.308 -21.647  27.828  1.00120.13           C  
ANISOU 3631  CD2 TRP A 244    11926  21578  12141 -10447   -107   2298
ATOM   3632  NE1 TRP A 244      60.447 -21.954  28.328  1.00123.93           N  
ANISOU 3632  NE1 TRP A 244    13013  21809  12265 -11521   -156   2354
ATOM   3633  CE2 TRP A 244      59.181 -22.183  28.824  1.00123.62           C  
ANISOU 3633  CE2 TRP A 244    12466  22127  12376 -11244   -338   2438
ATOM   3634  CE3 TRP A 244      56.918 -21.729  28.079  1.00118.78           C  
ANISOU 3634  CE3 TRP A 244    11280  21690  12161 -10019   -211   2354
ATOM   3635  CZ2 TRP A 244      58.697 -22.794  29.995  1.00126.73           C  
ANISOU 3635  CZ2 TRP A 244    12483  22933  12736 -11641   -698   2643
ATOM   3636  CZ3 TRP A 244      56.421 -22.346  29.244  1.00122.00           C  
ANISOU 3636  CZ3 TRP A 244    11296  22500  12558 -10377   -555   2576
ATOM   3637  CH2 TRP A 244      57.308 -22.884  30.198  1.00125.71           C  
ANISOU 3637  CH2 TRP A 244    11860  23099  12806 -11191   -810   2724
ATOM   3638  H   TRP A 244      57.025 -20.402  23.097  1.00107.93           H  
ATOM   3639  HA  TRP A 244      59.192 -22.171  24.122  1.00112.07           H  
ATOM   3640  HB3 TRP A 244      57.833 -19.888  25.621  1.00110.99           H  
ATOM   3641  HB2 TRP A 244      59.480 -19.914  25.056  1.00110.99           H  
ATOM   3642  HD1 TRP A 244      61.258 -21.058  26.497  1.00120.62           H  
ATOM   3643  HE1 TRP A 244      61.315 -22.206  28.782  1.00123.93           H  
ATOM   3644  HE3 TRP A 244      56.222 -21.331  27.354  1.00118.78           H  
ATOM   3645  HZ2 TRP A 244      59.385 -23.203  30.721  1.00126.73           H  
ATOM   3646  HZ3 TRP A 244      55.355 -22.412  29.402  1.00122.00           H  
ATOM   3647  HH2 TRP A 244      56.922 -23.362  31.086  1.00125.71           H  
ATOM   3648  N   ASP A 245      57.626 -23.735  25.250  1.00120.48           N  
ANISOU 3648  N   ASP A 245    10799  22404  12574  -9811    549   2590
ATOM   3649  CA  ASP A 245      56.801 -24.781  25.864  1.00124.50           C  
ANISOU 3649  CA  ASP A 245    10540  23507  13256  -9902    390   2880
ATOM   3650  C   ASP A 245      57.537 -25.452  27.055  1.00129.69           C  
ANISOU 3650  C   ASP A 245    11126  24391  13761 -10716     39   3097
ATOM   3651  O   ASP A 245      58.509 -24.894  27.561  1.00129.40           O  
ANISOU 3651  O   ASP A 245    11730  23963  13475 -11138   -142   2951
ATOM   3652  CB  ASP A 245      56.134 -25.671  24.775  1.00126.42           C  
ANISOU 3652  CB  ASP A 245    10114  24190  13731  -9568    730   3058
ATOM   3653  CG  ASP A 245      55.031 -26.619  25.266  1.00129.73           C  
ANISOU 3653  CG  ASP A 245     9720  25154  14417  -9415    619   3348
ATOM   3654  OD1 ASP A 245      54.359 -26.269  26.261  1.00128.64           O  
ANISOU 3654  OD1 ASP A 245     9579  24990  14308  -9339    318   3344
ATOM   3655  OD2 ASP A 245      54.892 -27.697  24.650  1.00132.42           O1-
ANISOU 3655  OD2 ASP A 245     9421  25948  14944  -9373    842   3602
ATOM   3656  H   ASP A 245      58.623 -23.881  25.312  1.00120.48           H  
ATOM   3657  HA  ASP A 245      55.987 -24.245  26.357  1.00124.50           H  
ATOM   3658  HB3 ASP A 245      56.897 -26.241  24.245  1.00126.42           H  
ATOM   3659  HB2 ASP A 245      55.659 -25.037  24.028  1.00126.42           H  
ATOM   3660  N   ARG A 246      57.053 -26.595  27.566  1.00134.79           N  
ANISOU 3660  N   ARG A 246    11014  25650  14551 -10955    -42   3450
ATOM   3661  CA  ARG A 246      57.209 -27.018  28.961  1.00139.47           C  
ANISOU 3661  CA  ARG A 246    11407  26543  15042 -11620   -493   3689
ATOM   3662  C   ARG A 246      58.100 -28.252  29.266  1.00146.10           C  
ANISOU 3662  C   ARG A 246    11914  27801  15797 -12427   -641   4009
ATOM   3663  O   ARG A 246      58.699 -28.249  30.341  1.00148.71           O  
ANISOU 3663  O   ARG A 246    12559  28069  15874 -13112  -1007   4036
ATOM   3664  CB  ARG A 246      55.785 -27.150  29.550  1.00140.09           C  
ANISOU 3664  CB  ARG A 246    10866  27004  15357 -11260   -689   3885
ATOM   3665  CG  ARG A 246      55.703 -27.629  31.008  1.00  0.00           C  
ATOM   3666  CD  ARG A 246      54.260 -27.732  31.506  1.00  0.00           C  
ATOM   3667  NE  ARG A 246      54.229 -28.285  32.867  1.00  0.00           N  
ATOM   3668  CZ  ARG A 246      54.256 -29.590  33.187  1.00  0.00           C  
ATOM   3669  NH1 ARG A 246      54.306 -30.544  32.246  1.00  0.00           N  
ATOM   3670  NH2 ARG A 246      54.243 -29.944  34.478  1.00  0.00           N1+
ATOM   3671  H   ARG A 246      56.274 -27.009  27.069  1.00134.79           H  
ATOM   3672  HA  ARG A 246      57.675 -26.201  29.514  1.00139.47           H  
ATOM   3673  HB2 ARG A 246      55.291 -26.178  29.480  1.00140.09           H  
ATOM   3674  HB3 ARG A 246      55.185 -27.818  28.937  1.00140.09           H  
ATOM   3675  HG2 ARG A 246      56.165 -28.611  31.113  1.00  0.00           H  
ATOM   3676  HG3 ARG A 246      56.268 -26.950  31.648  1.00  0.00           H  
ATOM   3677  HD2 ARG A 246      53.798 -26.745  31.521  1.00  0.00           H  
ATOM   3678  HD3 ARG A 246      53.656 -28.351  30.841  1.00  0.00           H  
ATOM   3679  HE  ARG A 246      54.228 -27.605  33.614  1.00  0.00           H  
ATOM   3680 HH11 ARG A 246      54.329 -31.521  32.500  1.00  0.00           H  
ATOM   3681 HH12 ARG A 246      54.338 -30.285  31.271  1.00  0.00           H  
ATOM   3682 HH21 ARG A 246      54.266 -30.917  34.743  1.00  0.00           H  
ATOM   3683 HH22 ARG A 246      54.210 -29.239  35.200  1.00  0.00           H  
ATOM   3684  N   ASN A 247      58.294 -29.305  28.452  1.00149.25           N  
ANISOU 3684  N   ASN A 247    11714  28618  16377 -12426   -381   4256
ATOM   3685  CA  ASN A 247      57.806 -29.684  27.124  1.00147.27           C  
ANISOU 3685  CA  ASN A 247    11144  28443  16368 -11751    118   4231
ATOM   3686  C   ASN A 247      58.604 -29.003  26.013  1.00142.78           C  
ANISOU 3686  C   ASN A 247    11304  27315  15632 -11546    456   3885
ATOM   3687  O   ASN A 247      58.026 -28.448  25.082  1.00139.20           O  
ANISOU 3687  O   ASN A 247    10875  26715  15298 -10878    793   3719
ATOM   3688  CB  ASN A 247      56.270 -29.771  26.927  1.00145.82           C  
ANISOU 3688  CB  ASN A 247    10407  28490  16508 -11004    204   4302
ATOM   3689  CG  ASN A 247      55.586 -30.842  27.782  1.00151.57           C  
ANISOU 3689  CG  ASN A 247    10157  29929  17505 -11149     50   4785
ATOM   3690  OD1 ASN A 247      56.111 -31.939  27.964  1.00157.47           O  
ANISOU 3690  OD1 ASN A 247    10497  31066  18268 -11660     53   5079
ATOM   3691  ND2 ASN A 247      54.408 -30.525  28.320  1.00150.52           N  
ANISOU 3691  ND2 ASN A 247     9631  29967  17593 -10704    -83   4896
ATOM   3692  H   ASN A 247      58.916 -29.994  28.849  1.00149.25           H  
ATOM   3693  HA  ASN A 247      58.155 -30.713  27.028  1.00147.27           H  
ATOM   3694  HB3 ASN A 247      56.054 -30.029  25.889  1.00145.82           H  
ATOM   3695  HB2 ASN A 247      55.794 -28.810  27.083  1.00145.82           H  
ATOM   3696 HD22 ASN A 247      53.909 -31.215  28.860  1.00150.52           H  
ATOM   3697 HD21 ASN A 247      53.992 -29.625  28.125  1.00150.52           H  
ATOM   3698  N   GLU A 248      59.940 -29.052  26.153  1.00143.57           N  
ANISOU 3698  N   GLU A 248    11990  27112  15448 -12164    350   3804
ATOM   3699  CA  GLU A 248      60.969 -28.553  25.249  1.00140.97           C  
ANISOU 3699  CA  GLU A 248    12297  26319  14946 -12157    638   3589
ATOM   3700  C   GLU A 248      61.519 -27.201  25.709  1.00136.80           C  
ANISOU 3700  C   GLU A 248    12669  25111  14199 -12178    491   3267
ATOM   3701  O   GLU A 248      62.598 -27.152  26.300  1.00138.33           O  
ANISOU 3701  O   GLU A 248    13415  24984  14158 -12731    415   3217
ATOM   3702  CB  GLU A 248      60.602 -28.714  23.754  1.00138.52           C  
ANISOU 3702  CB  GLU A 248    11794  26046  14790 -11488   1097   3524
ATOM   3703  CG  GLU A 248      61.793 -28.746  22.782  1.00138.38           C  
ANISOU 3703  CG  GLU A 248    12086  25869  14623 -11674   1408   3507
ATOM   3704  CD  GLU A 248      61.439 -29.537  21.520  1.00137.15           C  
ANISOU 3704  CD  GLU A 248    11400  26079  14630 -11289   1841   3623
ATOM   3705  OE1 GLU A 248      61.188 -30.755  21.662  1.00138.56           O  
ANISOU 3705  OE1 GLU A 248    10829  26822  14995 -11421   1891   3918
ATOM   3706  OE2 GLU A 248      61.410 -28.910  20.440  1.00131.86           O1-
ANISOU 3706  OE2 GLU A 248    11069  25135  13896 -10869   2140   3433
ATOM   3707  H   GLU A 248      60.286 -29.513  26.982  1.00143.57           H  
ATOM   3708  HA  GLU A 248      61.784 -29.259  25.421  1.00140.97           H  
ATOM   3709  HB3 GLU A 248      59.924 -27.919  23.440  1.00138.52           H  
ATOM   3710  HB2 GLU A 248      60.035 -29.641  23.652  1.00138.52           H  
ATOM   3711  HG3 GLU A 248      62.649 -29.239  23.245  1.00138.38           H  
ATOM   3712  HG2 GLU A 248      62.112 -27.734  22.531  1.00138.38           H  
ATOM   3713  N   GLY A 249      60.764 -26.115  25.467  1.00131.92           N  
ANISOU 3713  N   GLY A 249    12192  24265  13666 -11587    469   3062
ATOM   3714  CA  GLY A 249      61.114 -24.745  25.838  1.00127.80           C  
ANISOU 3714  CA  GLY A 249    12482  23095  12980 -11512    389   2765
ATOM   3715  C   GLY A 249      62.170 -24.131  24.918  1.00125.44           C  
ANISOU 3715  C   GLY A 249    12783  22306  12572 -11398    670   2601
ATOM   3716  O   GLY A 249      63.174 -24.771  24.606  1.00128.13           O  
ANISOU 3716  O   GLY A 249    13100  22736  12847 -11695    838   2724
ATOM   3717  H   GLY A 249      59.885 -26.255  24.991  1.00131.92           H  
ATOM   3718  HA3 GLY A 249      61.473 -24.713  26.868  1.00127.80           H  
ATOM   3719  HA2 GLY A 249      60.217 -24.131  25.805  1.00127.80           H  
ATOM   3720  N   ASN A 250      61.939 -22.880  24.484  1.00120.57           N  
ANISOU 3720  N   ASN A 250    12692  21177  11940 -10974    718   2350
ATOM   3721  CA  ASN A 250      62.833 -22.082  23.632  1.00118.20           C  
ANISOU 3721  CA  ASN A 250    12956  20395  11560 -10810    958   2227
ATOM   3722  C   ASN A 250      63.042 -22.730  22.246  1.00118.65           C  
ANISOU 3722  C   ASN A 250    12716  20711  11654 -10672   1249   2348
ATOM   3723  O   ASN A 250      64.152 -22.728  21.716  1.00120.81           O  
ANISOU 3723  O   ASN A 250    13230  20878  11795 -11046   1366   2438
ATOM   3724  CB  ASN A 250      64.173 -21.730  24.339  1.00120.49           C  
ANISOU 3724  CB  ASN A 250    13925  20220  11636 -11387    894   2197
ATOM   3725  CG  ASN A 250      63.997 -20.898  25.612  1.00119.88           C  
ANISOU 3725  CG  ASN A 250    14284  19782  11483 -11496    675   2034
ATOM   3726  OD1 ASN A 250      63.851 -21.441  26.703  1.00117.64           O  
ANISOU 3726  OD1 ASN A 250    14490  18991  11214 -11134    751   1848
ATOM   3727  ND2 ASN A 250      64.025 -19.570  25.479  1.00125.28           N  
ANISOU 3727  ND2 ASN A 250    14783  20737  12079 -12010    404   2120
ATOM   3728  H   ASN A 250      61.091 -22.427  24.791  1.00120.57           H  
ATOM   3729  HA  ASN A 250      62.303 -21.149  23.437  1.00118.20           H  
ATOM   3730  HB3 ASN A 250      64.817 -21.168  23.662  1.00120.49           H  
ATOM   3731  HB2 ASN A 250      64.730 -22.634  24.590  1.00120.49           H  
ATOM   3732 HD22 ASN A 250      63.914 -18.987  26.296  1.00125.28           H  
ATOM   3733 HD21 ASN A 250      64.153 -19.153  24.569  1.00125.28           H  
ATOM   3734  N   TYR A 251      61.974 -23.317  21.678  1.00116.51           N  
ANISOU 3734  N   TYR A 251    11945  20772  11550 -10156   1383   2350
ATOM   3735  CA  TYR A 251      61.958 -23.970  20.369  1.00117.06           C  
ANISOU 3735  CA  TYR A 251    11775  21069  11634  -9974   1701   2430
ATOM   3736  C   TYR A 251      61.648 -22.945  19.258  1.00112.46           C  
ANISOU 3736  C   TYR A 251    11529  20157  11043  -9406   1871   2243
ATOM   3737  O   TYR A 251      61.416 -21.768  19.540  1.00108.88           O  
ANISOU 3737  O   TYR A 251    11475  19299  10595  -9180   1740   2076
ATOM   3738  CB  TYR A 251      60.893 -25.097  20.400  1.00119.68           C  
ANISOU 3738  CB  TYR A 251    11303  22025  12144  -9867   1800   2597
ATOM   3739  CG  TYR A 251      59.422 -24.699  20.395  1.00117.26           C  
ANISOU 3739  CG  TYR A 251    10674  21842  12039  -9278   1790   2500
ATOM   3740  CD1 TYR A 251      58.750 -24.405  21.600  1.00117.85           C  
ANISOU 3740  CD1 TYR A 251    10580  21985  12212  -9302   1485   2511
ATOM   3741  CD2 TYR A 251      58.708 -24.667  19.178  1.00115.91           C  
ANISOU 3741  CD2 TYR A 251    10389  21713  11939  -8720   2091   2402
ATOM   3742  CE1 TYR A 251      57.379 -24.075  21.576  1.00116.34           C  
ANISOU 3742  CE1 TYR A 251    10102  21891  12213  -8751   1487   2438
ATOM   3743  CE2 TYR A 251      57.340 -24.336  19.163  1.00114.02           C  
ANISOU 3743  CE2 TYR A 251     9885  21551  11885  -8184   2107   2308
ATOM   3744  CZ  TYR A 251      56.675 -24.031  20.361  1.00114.40           C  
ANISOU 3744  CZ  TYR A 251     9754  21658  12055  -8190   1807   2334
ATOM   3745  OH  TYR A 251      55.353 -23.695  20.345  1.00114.22           O  
ANISOU 3745  OH  TYR A 251     9482  21695  12220  -7656   1831   2257
ATOM   3746  HB2 TYR A 251      61.059 -25.759  19.549  1.00119.68           H  
ATOM   3747  HD1 TYR A 251      59.277 -24.439  22.543  1.00117.85           H  
ATOM   3748  HD2 TYR A 251      59.203 -24.907  18.249  1.00115.91           H  
ATOM   3749  HE1 TYR A 251      56.853 -23.860  22.487  1.00116.34           H  
ATOM   3750  HE2 TYR A 251      56.795 -24.329  18.236  1.00114.02           H  
ATOM   3751  HH  TYR A 251      54.961 -23.732  19.485  1.00114.22           H  
ATOM   3752  H   TYR A 251      61.091 -23.253  22.164  1.00116.51           H  
ATOM   3753  HA  TYR A 251      62.933 -24.418  20.174  1.00117.06           H  
ATOM   3754  HB3 TYR A 251      61.068 -25.730  21.272  1.00119.68           H  
ATOM   3755  N   ALA A 252      61.646 -23.390  17.990  1.00112.91           N  
ANISOU 3755  N   ALA A 252    11440  20388  11071  -9209   2162   2282
ATOM   3756  CA  ALA A 252      61.294 -22.555  16.844  1.00109.48           C  
ANISOU 3756  CA  ALA A 252    11313  19697  10589  -8736   2312   2133
ATOM   3757  C   ALA A 252      60.653 -23.326  15.691  1.00110.91           C  
ANISOU 3757  C   ALA A 252    11152  20223  10764  -8468   2639   2155
ATOM   3758  O   ALA A 252      61.149 -24.378  15.289  1.00114.47           O  
ANISOU 3758  O   ALA A 252    11429  20930  11134  -8743   2837   2308
ATOM   3759  CB  ALA A 252      62.485 -21.684  16.406  1.00108.55           C  
ANISOU 3759  CB  ALA A 252    11833  19115  10296  -8919   2297   2141
ATOM   3760  H   ALA A 252      61.852 -24.362  17.807  1.00112.91           H  
ATOM   3761  HA  ALA A 252      60.493 -21.902  17.182  1.00109.48           H  
ATOM   3762  HB1 ALA A 252      62.208 -21.026  15.583  1.00108.55           H  
ATOM   3763  HB2 ALA A 252      62.841 -21.055  17.221  1.00108.55           H  
ATOM   3764  HB3 ALA A 252      63.322 -22.300  16.073  1.00108.55           H  
ATOM   3765  N   LEU A 253      59.583 -22.737  15.128  1.00108.82           N  
ANISOU 3765  N   LEU A 253    10823  19945  10579  -7940   2714   1993
ATOM   3766  CA  LEU A 253      58.944 -23.127  13.873  1.00110.08           C  
ANISOU 3766  CA  LEU A 253    10790  20337  10700  -7643   3053   1957
ATOM   3767  C   LEU A 253      59.738 -22.538  12.698  1.00109.29           C  
ANISOU 3767  C   LEU A 253    11199  19980  10347  -7656   3154   1928
ATOM   3768  O   LEU A 253      60.312 -21.451  12.801  1.00108.03           O  
ANISOU 3768  O   LEU A 253    11487  19461  10097  -7836   2960   1953
ATOM   3769  CB  LEU A 253      57.512 -22.523  13.813  1.00107.66           C  
ANISOU 3769  CB  LEU A 253    10315  20037  10553  -7098   3074   1776
ATOM   3770  CG  LEU A 253      56.364 -23.456  14.238  1.00110.72           C  
ANISOU 3770  CG  LEU A 253    10075  20809  11185  -6868   3200   1816
ATOM   3771  CD1 LEU A 253      56.127 -24.597  13.236  1.00115.36           C  
ANISOU 3771  CD1 LEU A 253    10387  21700  11744  -6708   3655   1843
ATOM   3772  CD2 LEU A 253      56.526 -23.973  15.670  1.00115.70           C  
ANISOU 3772  CD2 LEU A 253    10300  21693  11969  -7218   2998   2021
ATOM   3773 HD13 LEU A 253      56.963 -25.298  13.213  1.00115.36           H  
ATOM   3774 HD21 LEU A 253      55.643 -24.525  15.989  1.00115.70           H  
ATOM   3775 HD22 LEU A 253      57.388 -24.635  15.768  1.00115.70           H  
ATOM   3776 HD23 LEU A 253      56.663 -23.138  16.357  1.00115.70           H  
ATOM   3777  H   LEU A 253      59.258 -21.876  15.541  1.00108.82           H  
ATOM   3778  HA  LEU A 253      58.920 -24.214  13.783  1.00110.08           H  
ATOM   3779  HB3 LEU A 253      57.274 -22.198  12.800  1.00107.66           H  
ATOM   3780  HB2 LEU A 253      57.469 -21.613  14.411  1.00107.66           H  
ATOM   3781  HG  LEU A 253      55.457 -22.849  14.227  1.00110.72           H  
ATOM   3782 HD11 LEU A 253      55.233 -25.164  13.496  1.00115.36           H  
ATOM   3783 HD12 LEU A 253      55.986 -24.213  12.224  1.00115.36           H  
ATOM   3784  N   TYR A 254      59.719 -23.259  11.568  1.00110.51           N  
ANISOU 3784  N   TYR A 254    11297  20308  10383  -7467   3468   1889
ATOM   3785  CA  TYR A 254      60.302 -22.867  10.292  1.00110.66           C  
ANISOU 3785  CA  TYR A 254    11775  20148  10124  -7495   3566   1886
ATOM   3786  C   TYR A 254      59.667 -23.733   9.198  1.00113.99           C  
ANISOU 3786  C   TYR A 254    12016  20885  10409  -7393   3980   1865
ATOM   3787  O   TYR A 254      59.986 -24.917   9.106  1.00117.84           O  
ANISOU 3787  O   TYR A 254    12289  21649  10835  -7681   4218   2019
ATOM   3788  CB  TYR A 254      61.844 -22.971  10.361  1.00112.24           C  
ANISOU 3788  CB  TYR A 254    12285  20179  10181  -7964   3459   2079
ATOM   3789  CG  TYR A 254      62.581 -22.367   9.181  1.00111.13           C  
ANISOU 3789  CG  TYR A 254    12650  19802   9772  -7996   3478   2128
ATOM   3790  CD1 TYR A 254      62.639 -20.967   9.038  1.00107.14           C  
ANISOU 3790  CD1 TYR A 254    12497  18972   9239  -7699   3293   2031
ATOM   3791  CD2 TYR A 254      63.231 -23.189   8.240  1.00116.23           C  
ANISOU 3791  CD2 TYR A 254    13407  20561  10193  -8341   3667   2304
ATOM   3792  CE1 TYR A 254      63.336 -20.388   7.964  1.00109.28           C  
ANISOU 3792  CE1 TYR A 254    13196  19057   9268  -7744   3275   2131
ATOM   3793  CE2 TYR A 254      63.935 -22.612   7.166  1.00117.05           C  
ANISOU 3793  CE2 TYR A 254    13973  20466  10036  -8389   3662   2392
ATOM   3794  CZ  TYR A 254      63.985 -21.212   7.025  1.00115.47           C  
ANISOU 3794  CZ  TYR A 254    14096  19963   9816  -8091   3453   2317
ATOM   3795  OH  TYR A 254      64.666 -20.655   5.984  1.00116.02           O  
ANISOU 3795  OH  TYR A 254    14582  19870   9629  -8156   3419   2455
ATOM   3796  HB2 TYR A 254      62.219 -22.461  11.250  1.00112.24           H  
ATOM   3797  HD1 TYR A 254      62.161 -20.335   9.769  1.00107.14           H  
ATOM   3798  HD2 TYR A 254      63.190 -24.265   8.333  1.00116.23           H  
ATOM   3799  HE1 TYR A 254      63.383 -19.314   7.877  1.00109.28           H  
ATOM   3800  HE2 TYR A 254      64.427 -23.247   6.444  1.00117.05           H  
ATOM   3801  HH  TYR A 254      64.642 -19.710   5.987  1.00116.02           H  
ATOM   3802  H   TYR A 254      59.225 -24.140  11.580  1.00110.51           H  
ATOM   3803  HA  TYR A 254      60.047 -21.825  10.097  1.00110.66           H  
ATOM   3804  HB3 TYR A 254      62.146 -24.012  10.482  1.00112.24           H  
ATOM   3805  N   ASN A 255      58.779 -23.148   8.373  1.00112.51           N  
ANISOU 3805  N   ASN A 255    11918  20651  10181  -6993   4087   1670
ATOM   3806  CA  ASN A 255      58.126 -23.788   7.217  1.00115.29           C  
ANISOU 3806  CA  ASN A 255    12204  21233  10367  -6858   4519   1595
ATOM   3807  C   ASN A 255      58.478 -23.065   5.905  1.00114.86           C  
ANISOU 3807  C   ASN A 255    12705  20985   9953  -6848   4535   1521
ATOM   3808  O   ASN A 255      57.688 -23.033   4.959  1.00115.50           O  
ANISOU 3808  O   ASN A 255    12872  21132   9880  -6635   4804   1362
ATOM   3809  CB  ASN A 255      56.606 -24.046   7.432  1.00115.07           C  
ANISOU 3809  CB  ASN A 255    11778  21369  10573  -6436   4730   1439
ATOM   3810  CG  ASN A 255      56.214 -25.224   8.342  1.00117.23           C  
ANISOU 3810  CG  ASN A 255    11407  22025  11111  -6497   4950   1597
ATOM   3811  OD1 ASN A 255      55.031 -25.538   8.443  1.00116.09           O  
ANISOU 3811  OD1 ASN A 255    11080  22024  11006  -6881   4868   1812
ATOM   3812  ND2 ASN A 255      57.160 -25.903   8.996  1.00113.68           N  
ANISOU 3812  ND2 ASN A 255    10608  21733  10852  -6116   5232   1505
ATOM   3813  H   ASN A 255      58.571 -22.172   8.525  1.00112.51           H  
ATOM   3814  HA  ASN A 255      58.584 -24.764   7.050  1.00115.29           H  
ATOM   3815  HB3 ASN A 255      56.132 -24.268   6.475  1.00115.07           H  
ATOM   3816  HB2 ASN A 255      56.112 -23.143   7.788  1.00115.07           H  
ATOM   3817 HD22 ASN A 255      56.897 -26.683   9.579  1.00113.68           H  
ATOM   3818 HD21 ASN A 255      58.134 -25.642   8.906  1.00113.68           H  
ATOM   3819  N   GLU A 256      59.722 -22.564   5.835  1.00113.99           N  
ANISOU 3819  N   GLU A 256    12975  20618   9719  -7079   4234   1649
ATOM   3820  CA  GLU A 256      60.520 -22.368   4.627  1.00116.24           C  
ANISOU 3820  CA  GLU A 256    13709  20830   9628  -7300   4271   1754
ATOM   3821  C   GLU A 256      60.395 -20.970   4.001  1.00113.96           C  
ANISOU 3821  C   GLU A 256    13874  20265   9161  -7151   4028   1702
ATOM   3822  O   GLU A 256      61.150 -20.066   4.357  1.00113.00           O  
ANISOU 3822  O   GLU A 256    14030  19877   9030  -7266   3723   1859
ATOM   3823  CB  GLU A 256      60.452 -23.581   3.654  1.00120.82           C  
ANISOU 3823  CB  GLU A 256    14217  21732   9959  -7434   4739   1763
ATOM   3824  CG  GLU A 256      61.811 -23.984   3.053  1.00123.98           C  
ANISOU 3824  CG  GLU A 256    14902  22147  10056  -7853   4790   1994
ATOM   3825  CD  GLU A 256      62.719 -24.763   4.020  1.00127.48           C  
ANISOU 3825  CD  GLU A 256    15086  22689  10662  -8198   4792   2207
ATOM   3826  OE1 GLU A 256      62.393 -24.834   5.225  1.00125.09           O  
ANISOU 3826  OE1 GLU A 256    14441  22391  10696  -8148   4646   2195
ATOM   3827  OE2 GLU A 256      63.738 -25.286   3.520  1.00130.76           O1-
ANISOU 3827  OE2 GLU A 256    15657  23181  10844  -8553   4934   2394
ATOM   3828  H   GLU A 256      60.261 -22.607   6.688  1.00113.99           H  
ATOM   3829  HA  GLU A 256      61.530 -22.369   5.042  1.00116.24           H  
ATOM   3830  HB3 GLU A 256      59.748 -23.384   2.844  1.00120.82           H  
ATOM   3831  HB2 GLU A 256      60.042 -24.458   4.156  1.00120.82           H  
ATOM   3832  HG3 GLU A 256      62.345 -23.107   2.688  1.00123.98           H  
ATOM   3833  HG2 GLU A 256      61.638 -24.623   2.185  1.00123.98           H  
ATOM   3834  N   ASN A 257      59.457 -20.801   3.052  1.00113.86           N  
ANISOU 3834  N   ASN A 257    13943  20319   9000  -6918   4183   1503
ATOM   3835  CA  ASN A 257      59.199 -19.563   2.303  1.00111.52           C  
ANISOU 3835  CA  ASN A 257    13998  19798   8578  -6758   3927   1434
ATOM   3836  C   ASN A 257      58.040 -18.791   2.954  1.00107.77           C  
ANISOU 3836  C   ASN A 257    13324  19202   8420  -6383   3788   1232
ATOM   3837  O   ASN A 257      57.072 -18.408   2.294  1.00106.86           O  
ANISOU 3837  O   ASN A 257    13296  19075   8229  -6155   3847   1029
ATOM   3838  CB  ASN A 257      58.856 -19.901   0.824  1.00114.32           C  
ANISOU 3838  CB  ASN A 257    14633  20286   8517  -6799   4169   1332
ATOM   3839  CG  ASN A 257      60.035 -20.328  -0.060  1.00119.11           C  
ANISOU 3839  CG  ASN A 257    15541  20962   8752  -7179   4221   1560
ATOM   3840  OD1 ASN A 257      59.948 -20.200  -1.278  1.00123.88           O  
ANISOU 3840  OD1 ASN A 257    16110  21530   9428  -7410   4131   1794
ATOM   3841  ND2 ASN A 257      61.133 -20.826   0.512  1.00121.57           N  
ANISOU 3841  ND2 ASN A 257    16187  21363   8641  -7271   4368   1495
ATOM   3842  H   ASN A 257      58.853 -21.586   2.853  1.00113.86           H  
ATOM   3843  HA  ASN A 257      60.070 -18.910   2.335  1.00111.52           H  
ATOM   3844  HB3 ASN A 257      58.431 -19.028   0.327  1.00114.32           H  
ATOM   3845  HB2 ASN A 257      58.090 -20.677   0.779  1.00114.32           H  
ATOM   3846 HD22 ASN A 257      61.901 -21.131  -0.067  1.00121.57           H  
ATOM   3847 HD21 ASN A 257      61.171 -20.952   1.515  1.00121.57           H  
ATOM   3848  N   GLY A 258      58.144 -18.580   4.272  1.00105.75           N  
ANISOU 3848  N   GLY A 258    12828  18850   8503  -6347   3609   1286
ATOM   3849  CA  GLY A 258      57.085 -18.048   5.110  1.00102.40           C  
ANISOU 3849  CA  GLY A 258    12192  18328   8389  -6019   3484   1119
ATOM   3850  C   GLY A 258      56.284 -19.186   5.738  1.00103.63           C  
ANISOU 3850  C   GLY A 258    11893  18745   8737  -5881   3768   1008
ATOM   3851  O   GLY A 258      55.899 -20.128   5.045  1.00106.69           O  
ANISOU 3851  O   GLY A 258    12180  19374   8984  -5887   4141    954
ATOM   3852  H   GLY A 258      58.966 -18.933   4.741  1.00105.75           H  
ATOM   3853  HA3 GLY A 258      56.402 -17.411   4.544  1.00102.40           H  
ATOM   3854  HA2 GLY A 258      57.529 -17.408   5.861  1.00102.40           H  
ATOM   3855  N   ILE A 259      55.988 -19.070   7.040  1.00101.50           N  
ANISOU 3855  N   ILE A 259    11352  18422   8791  -5755   3599    993
ATOM   3856  CA  ILE A 259      54.988 -19.896   7.712  1.00102.62           C  
ANISOU 3856  CA  ILE A 259    11023  18799   9170  -5577   3799    928
ATOM   3857  C   ILE A 259      53.661 -19.153   7.530  1.00100.69           C  
ANISOU 3857  C   ILE A 259    10790  18466   9002  -5164   3852    698
ATOM   3858  O   ILE A 259      53.563 -17.969   7.861  1.00 97.43           O  
ANISOU 3858  O   ILE A 259    10570  17790   8660  -5014   3565    621
ATOM   3859  CB  ILE A 259      55.325 -20.018   9.221  1.00101.63           C  
ANISOU 3859  CB  ILE A 259    10624  18667   9323  -5681   3551   1042
ATOM   3860  CG1 ILE A 259      56.665 -20.748   9.450  1.00103.22           C  
ANISOU 3860  CG1 ILE A 259    10876  18913   9431  -6138   3493   1262
ATOM   3861  CG2 ILE A 259      54.217 -20.752  10.006  1.00103.61           C  
ANISOU 3861  CG2 ILE A 259    10338  19195   9834  -5492   3723   1030
ATOM   3862  CD1 ILE A 259      57.386 -20.245  10.694  1.00 98.88           C  
ANISOU 3862  CD1 ILE A 259    10191  18297   9081  -6330   3217   1364
ATOM   3863 HG23 ILE A 259      53.943 -21.687   9.516  1.00103.61           H  
ATOM   3864 HD11 ILE A 259      58.277 -20.826  10.901  1.00 98.88           H  
ATOM   3865 HD12 ILE A 259      57.699 -19.215  10.537  1.00 98.88           H  
ATOM   3866 HD13 ILE A 259      56.744 -20.293  11.571  1.00 98.88           H  
ATOM   3867  H   ILE A 259      56.338 -18.268   7.546  1.00101.50           H  
ATOM   3868  HA  ILE A 259      54.934 -20.893   7.272  1.00102.62           H  
ATOM   3869  HB  ILE A 259      55.415 -19.010   9.631  1.00101.63           H  
ATOM   3870 HG13 ILE A 259      57.338 -20.621   8.603  1.00103.22           H  
ATOM   3871 HG12 ILE A 259      56.500 -21.820   9.542  1.00103.22           H  
ATOM   3872 HG21 ILE A 259      54.552 -21.009  11.010  1.00103.61           H  
ATOM   3873 HG22 ILE A 259      53.314 -20.149  10.104  1.00103.61           H  
ATOM   3874  N   ASP A 260      52.652 -19.857   6.996  1.00103.07           N  
ANISOU 3874  N   ASP A 260    10894  18967   9300  -4975   4241    593
ATOM   3875  CA  ASP A 260      51.320 -19.324   6.746  1.00101.82           C  
ANISOU 3875  CA  ASP A 260    10746  18705   9236  -4584   4327    373
ATOM   3876  C   ASP A 260      50.622 -19.041   8.085  1.00 98.92           C  
ANISOU 3876  C   ASP A 260    10076  18272   9235  -4361   4091    375
ATOM   3877  O   ASP A 260      50.393 -19.965   8.867  1.00100.17           O  
ANISOU 3877  O   ASP A 260     9778  18649   9633  -4318   4189    484
ATOM   3878  CB  ASP A 260      50.530 -20.344   5.894  1.00105.79           C  
ANISOU 3878  CB  ASP A 260    11104  19405   9686  -4417   4857    271
ATOM   3879  CG  ASP A 260      49.161 -19.814   5.465  1.00107.21           C  
ANISOU 3879  CG  ASP A 260    11514  19405   9816  -4094   4989      8
ATOM   3880  OD1 ASP A 260      49.145 -18.949   4.563  1.00108.55           O  
ANISOU 3880  OD1 ASP A 260    12150  19376   9719  -4175   4820   -100
ATOM   3881  OD2 ASP A 260      48.162 -20.261   6.062  1.00113.03           O1-
ANISOU 3881  OD2 ASP A 260    11963  20197  10785  -3770   5258    -70
ATOM   3882  H   ASP A 260      52.813 -20.823   6.750  1.00103.07           H  
ATOM   3883  HA  ASP A 260      51.422 -18.394   6.181  1.00101.82           H  
ATOM   3884  HB3 ASP A 260      50.403 -21.284   6.432  1.00105.79           H  
ATOM   3885  HB2 ASP A 260      51.091 -20.587   4.991  1.00105.79           H  
ATOM   3886  N   PHE A 261      50.316 -17.758   8.342  1.00 95.08           N  
ANISOU 3886  N   PHE A 261     9837  17502   8789  -4233   3776    278
ATOM   3887  CA  PHE A 261      49.677 -17.281   9.567  1.00 92.56           C  
ANISOU 3887  CA  PHE A 261     9290  17100   8779  -4025   3560    267
ATOM   3888  C   PHE A 261      48.294 -17.910   9.784  1.00 93.99           C  
ANISOU 3888  C   PHE A 261     9131  17423   9159  -3678   3853    182
ATOM   3889  O   PHE A 261      47.990 -18.321  10.902  1.00 94.94           O  
ANISOU 3889  O   PHE A 261     8820  17718   9536  -3620   3844    309
ATOM   3890  CB  PHE A 261      49.543 -15.743   9.527  1.00 88.51           C  
ANISOU 3890  CB  PHE A 261     9113  16250   8267  -3914   3241    163
ATOM   3891  CG  PHE A 261      48.694 -15.187  10.657  1.00 87.35           C  
ANISOU 3891  CG  PHE A 261     8778  16009   8404  -3643   3096    103
ATOM   3892  CD1 PHE A 261      49.130 -15.319  11.988  1.00 86.90           C  
ANISOU 3892  CD1 PHE A 261     8546  15946   8524  -3755   2846    232
ATOM   3893  CD2 PHE A 261      47.404 -14.679  10.389  1.00 88.16           C  
ANISOU 3893  CD2 PHE A 261     8899  16023   8575  -3300   3220    -80
ATOM   3894  CE1 PHE A 261      48.290 -14.941  13.046  1.00 85.36           C  
ANISOU 3894  CE1 PHE A 261     8196  15678   8560  -3527   2707    191
ATOM   3895  CE2 PHE A 261      46.559 -14.310  11.452  1.00 86.76           C  
ANISOU 3895  CE2 PHE A 261     8551  15759   8655  -3051   3091   -116
ATOM   3896  CZ  PHE A 261      47.011 -14.418  12.781  1.00 85.52           C  
ANISOU 3896  CZ  PHE A 261     8215  15616   8663  -3163   2827     26
ATOM   3897  HD1 PHE A 261      50.094 -15.755  12.204  1.00 86.90           H  
ATOM   3898  HD2 PHE A 261      47.046 -14.606   9.372  1.00 88.16           H  
ATOM   3899  HE1 PHE A 261      48.640 -15.060  14.057  1.00 85.36           H  
ATOM   3900  HE2 PHE A 261      45.568 -13.934  11.246  1.00 86.76           H  
ATOM   3901  HZ  PHE A 261      46.375 -14.115  13.600  1.00 85.52           H  
ATOM   3902  H   PHE A 261      50.577 -17.059   7.656  1.00 95.08           H  
ATOM   3903  HA  PHE A 261      50.314 -17.558  10.410  1.00 92.56           H  
ATOM   3904  HB3 PHE A 261      49.087 -15.443   8.584  1.00 88.51           H  
ATOM   3905  HB2 PHE A 261      50.528 -15.278   9.545  1.00 88.51           H  
ATOM   3906  N   LYS A 262      47.473 -17.956   8.721  1.00 94.36           N  
ANISOU 3906  N   LYS A 262     9388  17387   9079  -3466   4114    -15
ATOM   3907  CA  LYS A 262      46.096 -18.445   8.716  1.00 96.02           C  
ANISOU 3907  CA  LYS A 262     9358  17662   9464  -3101   4462   -116
ATOM   3908  C   LYS A 262      45.990 -19.886   9.247  1.00 99.71           C  
ANISOU 3908  C   LYS A 262     9275  18463  10146  -3078   4725     82
ATOM   3909  O   LYS A 262      45.149 -20.159  10.103  1.00 99.65           O  
ANISOU 3909  O   LYS A 262     8870  18536  10456  -2839   4718    166
ATOM   3910  CB  LYS A 262      45.539 -18.296   7.284  1.00 97.60           C  
ANISOU 3910  CB  LYS A 262     9923  17766   9393  -3013   4813   -340
ATOM   3911  CG  LYS A 262      44.065 -18.700   7.112  1.00  0.00           C  
ATOM   3912  CD  LYS A 262      43.618 -18.632   5.645  1.00  0.00           C  
ATOM   3913  CE  LYS A 262      42.165 -19.087   5.456  1.00  0.00           C  
ATOM   3914  NZ  LYS A 262      41.780 -19.073   4.036  1.00  0.00           N1+
ATOM   3915  HA  LYS A 262      45.521 -17.799   9.381  1.00 96.02           H  
ATOM   3916  HB2 LYS A 262      45.654 -17.259   6.965  1.00 97.60           H  
ATOM   3917  HB3 LYS A 262      46.143 -18.883   6.595  1.00 97.60           H  
ATOM   3918  H   LYS A 262      47.833 -17.616   7.841  1.00 94.36           H  
ATOM   3919  HG2 LYS A 262      43.911 -19.717   7.468  1.00  0.00           H  
ATOM   3920  HG3 LYS A 262      43.435 -18.055   7.726  1.00  0.00           H  
ATOM   3921  HD2 LYS A 262      43.737 -17.614   5.272  1.00  0.00           H  
ATOM   3922  HD3 LYS A 262      44.275 -19.262   5.044  1.00  0.00           H  
ATOM   3923  HE2 LYS A 262      42.034 -20.099   5.842  1.00  0.00           H  
ATOM   3924  HE3 LYS A 262      41.488 -18.440   6.014  1.00  0.00           H  
ATOM   3925  HZ1 LYS A 262      41.875 -18.135   3.670  1.00  0.00           H  
ATOM   3926  HZ2 LYS A 262      42.383 -19.696   3.519  1.00  0.00           H  
ATOM   3927  HZ3 LYS A 262      40.822 -19.376   3.940  1.00  0.00           H  
ATOM   3928  N   GLU A 263      46.873 -20.779   8.772  1.00102.90           N  
ANISOU 3928  N   GLU A 263     9644  19072  10380  -3342   4940    185
ATOM   3929  CA  GLU A 263      46.922 -22.190   9.146  1.00107.42           C  
ANISOU 3929  CA  GLU A 263     9680  19990  11143  -3344   5241    392
ATOM   3930  C   GLU A 263      47.712 -22.433  10.451  1.00107.20           C  
ANISOU 3930  C   GLU A 263     9276  20151  11305  -3605   4884    662
ATOM   3931  O   GLU A 263      47.402 -23.401  11.145  1.00110.21           O  
ANISOU 3931  O   GLU A 263     9100  20810  11963  -3527   4998    866
ATOM   3932  CB  GLU A 263      47.596 -22.962   7.995  1.00111.27           C  
ANISOU 3932  CB  GLU A 263    10288  20628  11363  -3533   5661    392
ATOM   3933  CG  GLU A 263      46.675 -23.078   6.757  1.00113.61           C  
ANISOU 3933  CG  GLU A 263    10931  20777  11458  -3297   6107    129
ATOM   3934  CD  GLU A 263      47.342 -23.685   5.520  1.00119.98           C  
ANISOU 3934  CD  GLU A 263    11977  21698  11911  -3553   6477    112
ATOM   3935  OE1 GLU A 263      48.531 -24.066   5.608  1.00120.77           O  
ANISOU 3935  OE1 GLU A 263    12018  21963  11907  -3923   6344    301
ATOM   3936  OE2 GLU A 263      46.632 -23.768   4.493  1.00123.12           O1-
ANISOU 3936  OE2 GLU A 263    12655  22006  12117  -3401   6916    -96
ATOM   3937  HG3 GLU A 263      46.294 -22.097   6.473  1.00113.61           H  
ATOM   3938  HG2 GLU A 263      45.803 -23.683   7.005  1.00113.61           H  
ATOM   3939  H   GLU A 263      47.513 -20.477   8.047  1.00102.90           H  
ATOM   3940  HA  GLU A 263      45.909 -22.571   9.284  1.00107.42           H  
ATOM   3941  HB3 GLU A 263      47.858 -23.970   8.322  1.00111.27           H  
ATOM   3942  HB2 GLU A 263      48.538 -22.478   7.728  1.00111.27           H  
ATOM   3943  N   LEU A 264      48.679 -21.570  10.827  1.00103.98           N  
ANISOU 3943  N   LEU A 264     9172  19589  10748  -3923   4462    680
ATOM   3944  CA  LEU A 264      49.412 -21.659  12.101  1.00103.71           C  
ANISOU 3944  CA  LEU A 264     8876  19680  10850  -4214   4121    901
ATOM   3945  C   LEU A 264      48.524 -21.239  13.284  1.00102.09           C  
ANISOU 3945  C   LEU A 264     8408  19447  10935  -3973   3885    926
ATOM   3946  O   LEU A 264      48.540 -21.909  14.316  1.00104.50           O  
ANISOU 3946  O   LEU A 264     8210  20032  11464  -4023   3844   1146
ATOM   3947  CB  LEU A 264      50.684 -20.770  12.063  1.00101.22           C  
ANISOU 3947  CB  LEU A 264     8997  19150  10311  -4592   3784    908
ATOM   3948  CG  LEU A 264      51.483 -20.666  13.396  1.00100.94           C  
ANISOU 3948  CG  LEU A 264     8891  19088  10373  -4888   3375   1057
ATOM   3949  CD1 LEU A 264      51.980 -22.029  13.908  1.00105.98           C  
ANISOU 3949  CD1 LEU A 264     8965  20111  11190  -5090   3398   1307
ATOM   3950  CD2 LEU A 264      52.654 -19.681  13.280  1.00100.90           C  
ANISOU 3950  CD2 LEU A 264     9343  18858  10136  -5251   3179   1078
ATOM   3951  HA  LEU A 264      49.716 -22.696  12.249  1.00103.71           H  
ATOM   3952  HB3 LEU A 264      50.399 -19.763  11.753  1.00101.22           H  
ATOM   3953  HB2 LEU A 264      51.345 -21.143  11.282  1.00101.22           H  
ATOM   3954  HG  LEU A 264      50.835 -20.244  14.163  1.00100.94           H  
ATOM   3955 HD11 LEU A 264      52.548 -21.917  14.832  1.00105.98           H  
ATOM   3956 HD12 LEU A 264      51.157 -22.711  14.119  1.00105.98           H  
ATOM   3957 HD13 LEU A 264      52.632 -22.510  13.178  1.00105.98           H  
ATOM   3958 HD21 LEU A 264      53.130 -19.522  14.248  1.00100.90           H  
ATOM   3959 HD22 LEU A 264      53.419 -20.042  12.599  1.00100.90           H  
ATOM   3960 HD23 LEU A 264      52.317 -18.710  12.917  1.00100.90           H  
ATOM   3961  H   LEU A 264      48.909 -20.803  10.207  1.00103.98           H  
ATOM   3962  N   LEU A 265      47.731 -20.162  13.134  1.00 98.24           N  
ANISOU 3962  N   LEU A 265     8243  18642  10441  -3723   3731    723
ATOM   3963  CA  LEU A 265      46.751 -19.694  14.118  1.00 96.88           C  
ANISOU 3963  CA  LEU A 265     7868  18417  10523  -3465   3534    731
ATOM   3964  C   LEU A 265      45.663 -20.753  14.360  1.00100.78           C  
ANISOU 3964  C   LEU A 265     7797  19203  11292  -3181   3824    871
ATOM   3965  O   LEU A 265      45.275 -20.979  15.505  1.00102.13           O  
ANISOU 3965  O   LEU A 265     7548  19573  11684  -3210   3637   1084
ATOM   3966  CB  LEU A 265      46.120 -18.373  13.617  1.00 93.17           C  
ANISOU 3966  CB  LEU A 265     7808  17582  10011  -3179   3453    477
ATOM   3967  CG  LEU A 265      45.056 -17.750  14.557  1.00 90.35           C  
ANISOU 3967  CG  LEU A 265     7282  17142   9903  -2878   3290    469
ATOM   3968  CD1 LEU A 265      45.686 -17.211  15.851  1.00 86.95           C  
ANISOU 3968  CD1 LEU A 265     6874  16651   9513  -3122   2842    573
ATOM   3969  CD2 LEU A 265      44.245 -16.664  13.838  1.00 86.69           C  
ANISOU 3969  CD2 LEU A 265     7177  16363   9399  -2563   3357    212
ATOM   3970  HA  LEU A 265      47.280 -19.514  15.056  1.00 96.88           H  
ATOM   3971  HB3 LEU A 265      45.664 -18.554  12.642  1.00 93.17           H  
ATOM   3972  HB2 LEU A 265      46.907 -17.642  13.438  1.00 93.17           H  
ATOM   3973  HG  LEU A 265      44.325 -18.506  14.840  1.00 90.35           H  
ATOM   3974 HD11 LEU A 265      44.940 -16.727  16.481  1.00 86.95           H  
ATOM   3975 HD12 LEU A 265      46.137 -18.011  16.439  1.00 86.95           H  
ATOM   3976 HD13 LEU A 265      46.462 -16.483  15.631  1.00 86.95           H  
ATOM   3977 HD21 LEU A 265      43.473 -16.254  14.489  1.00 86.69           H  
ATOM   3978 HD22 LEU A 265      44.875 -15.842  13.513  1.00 86.69           H  
ATOM   3979 HD23 LEU A 265      43.746 -17.067  12.955  1.00 86.69           H  
ATOM   3980  H   LEU A 265      47.783 -19.650  12.261  1.00 98.24           H  
ATOM   3981  N   ALA A 266      45.225 -21.427  13.282  1.00103.27           N  
ANISOU 3981  N   ALA A 266     8112  19540  11586  -2919   4291    766
ATOM   3982  CA  ALA A 266      44.246 -22.507  13.298  1.00108.05           C  
ANISOU 3982  CA  ALA A 266     8179  20414  12461  -2625   4688    919
ATOM   3983  C   ALA A 266      44.774 -23.804  13.940  1.00112.22           C  
ANISOU 3983  C   ALA A 266     8106  21366  13168  -2869   4645   1277
ATOM   3984  O   ALA A 266      43.956 -24.642  14.308  1.00115.26           O  
ANISOU 3984  O   ALA A 266     7940  21982  13872  -2624   4774   1494
ATOM   3985  CB  ALA A 266      43.828 -22.802  11.849  1.00110.37           C  
ANISOU 3985  CB  ALA A 266     8656  20664  12616  -2440   5254    749
ATOM   3986  HB2 ALA A 266      43.413 -21.912  11.374  1.00110.37           H  
ATOM   3987  HB3 ALA A 266      44.670 -23.138  11.246  1.00110.37           H  
ATOM   3988  H   ALA A 266      45.608 -21.175  12.381  1.00103.27           H  
ATOM   3989  HA  ALA A 266      43.371 -22.177  13.860  1.00108.05           H  
ATOM   3990  HB1 ALA A 266      43.060 -23.575  11.807  1.00110.37           H  
ATOM   3991  N   TYR A 267      46.103 -23.959  14.105  1.00112.93           N  
ANISOU 3991  N   TYR A 267     8288  21559  13060  -3354   4467   1363
ATOM   3992  CA  TYR A 267      46.732 -25.051  14.855  1.00117.66           C  
ANISOU 3992  CA  TYR A 267     8334  22569  13802  -3660   4411   1707
ATOM   3993  C   TYR A 267      46.902 -24.672  16.340  1.00116.92           C  
ANISOU 3993  C   TYR A 267     8058  22549  13819  -3906   3861   1885
ATOM   3994  O   TYR A 267      46.898 -25.565  17.185  1.00120.85           O  
ANISOU 3994  O   TYR A 267     7976  23424  14515  -4068   3781   2210
ATOM   3995  CB  TYR A 267      48.127 -25.344  14.252  1.00119.31           C  
ANISOU 3995  CB  TYR A 267     8700  22879  13753  -4093   4531   1741
ATOM   3996  CG  TYR A 267      48.854 -26.534  14.864  1.00  0.00           C  
ATOM   3997  CD1 TYR A 267      49.773 -26.341  15.920  1.00  0.00           C  
ATOM   3998  CD2 TYR A 267      48.596 -27.840  14.400  1.00  0.00           C  
ATOM   3999  CE1 TYR A 267      50.399 -27.445  16.529  1.00  0.00           C  
ATOM   4000  CE2 TYR A 267      49.235 -28.944  14.998  1.00  0.00           C  
ATOM   4001  CZ  TYR A 267      50.126 -28.749  16.074  1.00  0.00           C  
ATOM   4002  OH  TYR A 267      50.712 -29.819  16.684  1.00  0.00           O  
ATOM   4003  H   TYR A 267      46.710 -23.235  13.751  1.00112.93           H  
ATOM   4004  HA  TYR A 267      46.122 -25.953  14.786  1.00117.66           H  
ATOM   4005  HB2 TYR A 267      48.018 -25.530  13.183  1.00119.31           H  
ATOM   4006  HB3 TYR A 267      48.773 -24.470  14.331  1.00119.31           H  
ATOM   4007  HD1 TYR A 267      49.977 -25.345  16.283  1.00  0.00           H  
ATOM   4008  HD2 TYR A 267      47.895 -28.000  13.593  1.00  0.00           H  
ATOM   4009  HE1 TYR A 267      51.084 -27.291  17.351  1.00  0.00           H  
ATOM   4010  HE2 TYR A 267      49.021 -29.942  14.643  1.00  0.00           H  
ATOM   4011  HH  TYR A 267      50.471 -30.645  16.295  1.00  0.00           H  
ATOM   4012  N   LYS A 268      47.008 -23.373  16.681  1.00112.43           N  
ANISOU 4012  N   LYS A 268     7968  21631  13119  -3943   3496   1690
ATOM   4013  CA  LYS A 268      47.055 -22.907  18.071  1.00111.90           C  
ANISOU 4013  CA  LYS A 268     7794  21582  13140  -4116   3018   1817
ATOM   4014  C   LYS A 268      45.685 -23.066  18.761  1.00114.11           C  
ANISOU 4014  C   LYS A 268     7560  22047  13747  -3721   3058   1981
ATOM   4015  O   LYS A 268      45.635 -23.359  19.954  1.00116.22           O  
ANISOU 4015  O   LYS A 268     7405  22589  14166  -3892   2783   2261
ATOM   4016  CB  LYS A 268      47.531 -21.437  18.131  1.00106.55           C  
ANISOU 4016  CB  LYS A 268     7744  20460  12280  -4153   2708   1561
ATOM   4017  CG  LYS A 268      48.588 -21.257  19.233  1.00106.35           C  
ANISOU 4017  CG  LYS A 268     8040  20332  12036  -4696   2394   1581
ATOM   4018  CD  LYS A 268      48.898 -19.799  19.587  1.00105.27           C  
ANISOU 4018  CD  LYS A 268     8290  19862  11847  -4726   2023   1454
ATOM   4019  CE  LYS A 268      50.054 -19.717  20.597  1.00106.97           C  
ANISOU 4019  CE  LYS A 268     8830  19949  11863  -5271   1743   1487
ATOM   4020  NZ  LYS A 268      50.190 -18.370  21.171  1.00105.62           N1+
ANISOU 4020  NZ  LYS A 268     9144  19365  11623  -5239   1486   1312
ATOM   4021  HE2 LYS A 268      49.888 -20.412  21.421  1.00106.97           H  
ATOM   4022  HZ1 LYS A 268      50.943 -18.373  21.845  1.00105.62           H  
ATOM   4023  HZ2 LYS A 268      50.415 -17.700  20.447  1.00105.62           H  
ATOM   4024  HZ3 LYS A 268      49.330 -18.101  21.625  1.00105.62           H  
ATOM   4025  H   LYS A 268      47.005 -22.677  15.950  1.00112.43           H  
ATOM   4026  HA  LYS A 268      47.775 -23.540  18.597  1.00111.90           H  
ATOM   4027  HB3 LYS A 268      46.691 -20.759  18.296  1.00106.55           H  
ATOM   4028  HB2 LYS A 268      47.967 -21.131  17.180  1.00106.55           H  
ATOM   4029  HG3 LYS A 268      49.505 -21.764  18.927  1.00106.35           H  
ATOM   4030  HG2 LYS A 268      48.254 -21.763  20.140  1.00106.35           H  
ATOM   4031  HD3 LYS A 268      48.003 -19.339  20.006  1.00105.27           H  
ATOM   4032  HD2 LYS A 268      49.147 -19.236  18.688  1.00105.27           H  
ATOM   4033  HE3 LYS A 268      50.996 -20.002  20.126  1.00106.97           H  
ATOM   4034  N   GLU A 269      44.588 -22.988  17.987  1.00114.07           N  
ANISOU 4034  N   GLU A 269     7613  21885  13845  -3205   3398   1818
ATOM   4035  CA  GLU A 269      43.295 -23.571  18.336  1.00117.64           C  
ANISOU 4035  CA  GLU A 269     7528  22526  14643  -2773   3583   2009
ATOM   4036  C   GLU A 269      43.385 -25.086  18.076  1.00123.62           C  
ANISOU 4036  C   GLU A 269     7721  23689  15558  -2790   3964   2276
ATOM   4037  O   GLU A 269      43.867 -25.502  17.025  1.00124.78           O  
ANISOU 4037  O   GLU A 269     8044  23817  15548  -2847   4325   2153
ATOM   4038  CB  GLU A 269      42.202 -22.929  17.451  1.00115.77           C  
ANISOU 4038  CB  GLU A 269     7588  21949  14452  -2234   3880   1731
ATOM   4039  CG  GLU A 269      40.793 -23.522  17.656  1.00  0.00           C  
ATOM   4040  CD  GLU A 269      39.725 -22.734  16.900  1.00  0.00           C  
ATOM   4041  OE1 GLU A 269      39.407 -23.149  15.765  1.00  0.00           O  
ATOM   4042  OE2 GLU A 269      39.245 -21.730  17.471  1.00  0.00           O1-
ATOM   4043  H   GLU A 269      44.716 -22.727  17.020  1.00114.07           H  
ATOM   4044  HA  GLU A 269      43.069 -23.379  19.386  1.00117.64           H  
ATOM   4045  HB2 GLU A 269      42.175 -21.857  17.654  1.00115.77           H  
ATOM   4046  HB3 GLU A 269      42.475 -23.025  16.398  1.00115.77           H  
ATOM   4047  HG2 GLU A 269      40.754 -24.560  17.324  1.00  0.00           H  
ATOM   4048  HG3 GLU A 269      40.537 -23.523  18.716  1.00  0.00           H  
ATOM   4049  N   ALA A 270      42.952 -25.892  19.054  1.00128.08           N  
ANISOU 4049  N   ALA A 270     7598  24636  16432  -2760   3873   2668
ATOM   4050  CA  ALA A 270      43.021 -27.354  19.123  1.00134.34           C  
ANISOU 4050  CA  ALA A 270     7721  25893  17430  -2836   4162   3022
ATOM   4051  C   ALA A 270      44.229 -27.865  19.918  1.00136.10           C  
ANISOU 4051  C   ALA A 270     7767  26417  17526  -3510   3751   3255
ATOM   4052  O   ALA A 270      44.042 -28.642  20.853  1.00140.16           O  
ANISOU 4052  O   ALA A 270     7640  27343  18271  -3659   3543   3664
ATOM   4053  CB  ALA A 270      42.792 -28.093  17.786  1.00135.79           C  
ANISOU 4053  CB  ALA A 270     8033  26016  17546  -2640   4811   2854
ATOM   4054  HA  ALA A 270      42.153 -27.604  19.734  1.00134.34           H  
ATOM   4055  HB1 ALA A 270      42.621 -29.156  17.960  1.00135.79           H  
ATOM   4056  HB2 ALA A 270      41.917 -27.704  17.262  1.00135.79           H  
ATOM   4057  HB3 ALA A 270      43.651 -28.017  17.118  1.00135.79           H  
ATOM   4058  H   ALA A 270      42.567 -25.439  19.870  1.00128.08           H  
ATOM   4059  N   ASN A 271      45.456 -27.453  19.553  1.00133.46           N  
ANISOU 4059  N   ASN A 271     8010  25872  16826  -3931   3615   3012
ATOM   4060  CA  ASN A 271      46.694 -28.018  20.112  1.00135.91           C  
ANISOU 4060  CA  ASN A 271     8219  26429  16992  -4598   3316   3206
ATOM   4061  C   ASN A 271      47.345 -27.129  21.182  1.00133.07           C  
ANISOU 4061  C   ASN A 271     8194  25926  16439  -5046   2692   3173
ATOM   4062  O   ASN A 271      48.154 -27.643  21.955  1.00135.51           O  
ANISOU 4062  O   ASN A 271     8362  26466  16660  -5617   2410   3378
ATOM   4063  CB  ASN A 271      47.730 -28.257  18.988  1.00135.98           C  
ANISOU 4063  CB  ASN A 271     8582  26348  16735  -4842   3610   3042
ATOM   4064  CG  ASN A 271      47.197 -29.189  17.895  1.00141.01           C  
ANISOU 4064  CG  ASN A 271     8844  27202  17533  -4532   4243   3130
ATOM   4065  OD1 ASN A 271      46.672 -28.731  16.884  1.00145.18           O  
ANISOU 4065  OD1 ASN A 271     8634  28147  18381  -4434   4407   3489
ATOM   4066  ND2 ASN A 271      47.332 -30.500  18.094  1.00142.24           N  
ANISOU 4066  ND2 ASN A 271     9509  27076  17459  -4387   4611   2818
ATOM   4067  H   ASN A 271      45.541 -26.825  18.764  1.00133.46           H  
ATOM   4068  HA  ASN A 271      46.492 -28.983  20.582  1.00135.91           H  
ATOM   4069  HB3 ASN A 271      48.640 -28.698  19.399  1.00135.98           H  
ATOM   4070  HB2 ASN A 271      48.040 -27.318  18.536  1.00135.98           H  
ATOM   4071 HD22 ASN A 271      46.994 -31.146  17.396  1.00142.24           H  
ATOM   4072 HD21 ASN A 271      47.774 -30.842  18.936  1.00142.24           H  
ATOM   4073  N   LYS A 272      47.037 -25.817  21.227  1.00128.51           N  
ANISOU 4073  N   LYS A 272     8079  24959  15788  -4809   2500   2912
ATOM   4074  CA  LYS A 272      47.520 -24.834  22.217  1.00125.90           C  
ANISOU 4074  CA  LYS A 272     8165  24417  15255  -5191   1973   2830
ATOM   4075  C   LYS A 272      49.026 -24.506  22.103  1.00124.82           C  
ANISOU 4075  C   LYS A 272     8485  24139  14803  -5774   1842   2731
ATOM   4076  O   LYS A 272      49.566 -23.796  22.950  1.00123.47           O  
ANISOU 4076  O   LYS A 272     8657  23805  14451  -6176   1449   2691
ATOM   4077  CB  LYS A 272      47.075 -25.199  23.656  1.00129.19           C  
ANISOU 4077  CB  LYS A 272     8075  25180  15832  -5378   1581   3178
ATOM   4078  CG  LYS A 272      45.555 -25.073  23.855  1.00130.12           C  
ANISOU 4078  CG  LYS A 272     7971  25273  16198  -4828   1565   3221
ATOM   4079  CD  LYS A 272      45.085 -25.654  25.196  1.00139.88           C  
ANISOU 4079  CD  LYS A 272     8483  27006  17659  -4976   1278   3693
ATOM   4080  CE  LYS A 272      43.578 -25.462  25.418  1.00141.82           C  
ANISOU 4080  CE  LYS A 272     8540  27206  18140  -4453   1218   3766
ATOM   4081  NZ  LYS A 272      43.124 -26.149  26.637  1.00149.28           N1+
ANISOU 4081  NZ  LYS A 272     8631  28714  19373  -4516   1020   4317
ATOM   4082  H   LYS A 272      46.370 -25.473  20.550  1.00128.51           H  
ATOM   4083  HA  LYS A 272      47.032 -23.892  21.973  1.00125.90           H  
ATOM   4084  HB3 LYS A 272      47.560 -24.544  24.382  1.00129.19           H  
ATOM   4085  HB2 LYS A 272      47.402 -26.205  23.916  1.00129.19           H  
ATOM   4086  HG3 LYS A 272      45.033 -25.590  23.049  1.00130.12           H  
ATOM   4087  HG2 LYS A 272      45.265 -24.023  23.780  1.00130.12           H  
ATOM   4088  HD3 LYS A 272      45.639 -25.189  26.013  1.00139.88           H  
ATOM   4089  HD2 LYS A 272      45.327 -26.717  25.222  1.00139.88           H  
ATOM   4090  HE3 LYS A 272      43.016 -25.856  24.569  1.00141.82           H  
ATOM   4091  HE2 LYS A 272      43.338 -24.401  25.496  1.00141.82           H  
ATOM   4092  HZ1 LYS A 272      43.627 -25.789  27.437  1.00149.28           H  
ATOM   4093  HZ2 LYS A 272      42.135 -25.992  26.764  1.00149.28           H  
ATOM   4094  HZ3 LYS A 272      43.298 -27.140  26.550  1.00149.28           H  
ATOM   4095  N   THR A 273      49.695 -25.029  21.063  1.00125.59           N  
ANISOU 4095  N   THR A 273     8605  24282  14831  -5811   2203   2696
ATOM   4096  CA  THR A 273      51.134 -24.970  20.818  1.00124.58           C  
ANISOU 4096  CA  THR A 273     8944  23977  14412  -6284   2161   2596
ATOM   4097  C   THR A 273      51.350 -24.837  19.307  1.00123.30           C  
ANISOU 4097  C   THR A 273     9039  23661  14148  -6039   2604   2405
ATOM   4098  O   THR A 273      52.324 -24.291  18.794  1.00120.79           O  
ANISOU 4098  O   THR A 273     9288  23028  13579  -6226   2586   2225
ATOM   4099  CB  THR A 273      51.838 -26.199  21.462  1.00129.66           C  
ANISOU 4099  CB  THR A 273     9204  25019  15043  -6891   2033   2917
ATOM   4100  OG1 THR A 273      51.668 -26.177  22.865  1.00130.90           O  
ANISOU 4100  OG1 THR A 273     9151  25333  15252  -7173   1586   3100
ATOM   4101  CG2 THR A 273      53.359 -26.257  21.239  1.00128.94           C  
ANISOU 4101  CG2 THR A 273     9646  24695  14650  -7388   1991   2814
ATOM   4102  H   THR A 273      49.157 -25.591  20.418  1.00125.59           H  
ATOM   4103  HA  THR A 273      51.534 -24.065  21.279  1.00124.58           H   
ATOM   4105  HB  THR A 273      51.391 -27.118  21.081  1.00129.66           H  
ATOM   4106  HG1 THR A 273      50.743 -26.191  23.055  1.00130.90           H  
ATOM   4107 HG21 THR A 273      53.790 -27.134  21.726  1.00128.94           H  
ATOM   4108 HG22 THR A 273      53.619 -26.319  20.183  1.00128.94           H  
ATOM   4109 HG23 THR A 273      53.849 -25.382  21.661  1.00128.94           H  
ATOM   4110  N   ILE A 295      64.995  -9.810   8.887  1.00 86.46           N  
ANISOU 4110  N   ILE A 295    12202  13156   7494  -6016   1665   2574
ATOM   4111  CA  ILE A 295      65.319  -9.011  10.072  1.00 86.00           C  
ANISOU 4111  CA  ILE A 295    12320  12669   7688  -5993   1682   2592
ATOM   4112  C   ILE A 295      64.445  -9.412  11.276  1.00 84.20           C  
ANISOU 4112  C   ILE A 295    11908  12522   7561  -6005   1718   2280
ATOM   4113  O   ILE A 295      63.425 -10.073  11.099  1.00 83.64           O  
ANISOU 4113  O   ILE A 295    11544  12847   7389  -6016   1739   2088
ATOM   4114  CG2 ILE A 295      66.427  -7.192   8.691  1.00 87.76           C  
ANISOU 4114  CG2 ILE A 295    12913  12369   8063  -5722   1548   3162
ATOM   4115  CD1 ILE A 295      63.031  -6.495  10.444  1.00 77.81           C  
ANISOU 4115  CD1 ILE A 295    11044  11433   7089  -5203   1471   2285
ATOM   4116  CB  ILE A 295      65.325  -7.497   9.727  1.00 85.27           C  
ANISOU 4116  CB  ILE A 295    12381  12197   7822  -5663   1579   2767
ATOM   4117  CG1 ILE A 295      63.963  -6.898   9.290  1.00 82.37           C  
ANISOU 4117  CG1 ILE A 295    11781  12002   7515  -5333   1448   2613
ATOM   4117  H   ILE A 295      65.601  -9.595   8.108  1.00 86.46           H  
ATOM   4120  HA  ILE A 295      66.335  -9.285  10.356  1.00 86.00           H  
ATOM   4121  HB  ILE A 295      65.613  -6.964  10.625  1.00 85.27           H  
ATOM   4122 HG13 ILE A 295      63.449  -7.572   8.607  1.00 82.37           H  
ATOM   4123 HG12 ILE A 295      64.150  -5.992   8.711  1.00 82.37           H  
ATOM   4124 HG21 ILE A 295      66.542  -6.122   8.524  1.00 87.76           H  
ATOM   4125 HG22 ILE A 295      67.393  -7.574   9.019  1.00 87.76           H  
ATOM   4126 HG23 ILE A 295      66.203  -7.641   7.723  1.00 87.76           H  
ATOM   4127 HD11 ILE A 295      62.162  -5.959  10.062  1.00 77.81           H  
ATOM   4128 HD12 ILE A 295      62.653  -7.356  10.993  1.00 77.81           H  
ATOM   4129 HD13 ILE A 295      63.535  -5.837  11.153  1.00 77.81           H  
ATOM   4130  N   ILE A 296      64.872  -9.084  12.509  1.00 83.71           N  
ANISOU 4130  N   ILE A 296    12027  12087   7690  -6004   1736   2242
ATOM   4131  CA  ILE A 296      64.348  -9.696  13.740  1.00 82.75           C  
ANISOU 4131  CA  ILE A 296    11790  12049   7602  -6162   1760   2002
ATOM   4132  C   ILE A 296      63.375  -8.745  14.465  1.00 79.61           C  
ANISOU 4132  C   ILE A 296    11327  11523   7398  -5881   1693   1794
ATOM   4133  O   ILE A 296      63.709  -7.596  14.740  1.00 78.74           O  
ANISOU 4133  O   ILE A 296    11468  10985   7463  -5704   1702   1835
ATOM   4134  CB  ILE A 296      65.545 -10.104  14.656  1.00 85.45           C  
ANISOU 4134  CB  ILE A 296    12407  12157   7902  -6579   1851   2075
ATOM   4135  CG1 ILE A 296      66.486 -11.104  13.930  1.00  0.00           C  
ATOM   4136  CG2 ILE A 296      65.080 -10.711  16.000  1.00  0.00           C  
ATOM   4137  CD1 ILE A 296      67.795 -11.419  14.667  1.00  0.00           C  
ATOM   4138  HA  ILE A 296      63.813 -10.612  13.499  1.00 82.75           H  
ATOM   4139  HB  ILE A 296      66.119  -9.202  14.881  1.00 85.45           H  
ATOM   4140  H   ILE A 296      65.690  -8.497  12.600  1.00 83.71           H  
ATOM   4141 HG12 ILE A 296      65.958 -12.037  13.741  1.00  0.00           H  
ATOM   4142 HG13 ILE A 296      66.766 -10.719  12.951  1.00  0.00           H  
ATOM   4143 HG21 ILE A 296      65.921 -10.957  16.648  1.00  0.00           H  
ATOM   4144 HG22 ILE A 296      64.456 -10.032  16.575  1.00  0.00           H  
ATOM   4145 HG23 ILE A 296      64.506 -11.625  15.840  1.00  0.00           H  
ATOM   4146 HD11 ILE A 296      68.440 -12.040  14.046  1.00  0.00           H  
ATOM   4147 HD12 ILE A 296      68.345 -10.508  14.903  1.00  0.00           H  
ATOM   4148 HD13 ILE A 296      67.627 -11.962  15.596  1.00  0.00           H  
ATOM   4149  N   VAL A 297      62.190  -9.264  14.824  1.00 77.92           N  
ANISOU 4149  N   VAL A 297    10771  11681   7156  -5839   1651   1585
ATOM   4150  CA  VAL A 297      61.164  -8.608  15.635  1.00 75.06           C  
ANISOU 4150  CA  VAL A 297    10312  11267   6941  -5635   1585   1382
ATOM   4151  C   VAL A 297      61.043  -9.391  16.961  1.00 75.90           C  
ANISOU 4151  C   VAL A 297    10337  11494   7008  -5947   1570   1265
ATOM   4152  O   VAL A 297      60.335 -10.398  16.993  1.00 75.90           O  
ANISOU 4152  O   VAL A 297     9987  11921   6932  -6056   1558   1202
ATOM   4153  CB  VAL A 297      59.806  -8.621  14.866  1.00 72.65           C  
ANISOU 4153  CB  VAL A 297     9678  11269   6656  -5308   1534   1249
ATOM   4154  CG1 VAL A 297      58.628  -8.004  15.645  1.00 70.32           C  
ANISOU 4154  CG1 VAL A 297     9290  10915   6513  -5106   1468   1056
ATOM   4155  CG2 VAL A 297      59.882  -7.976  13.471  1.00 72.34           C  
ANISOU 4155  CG2 VAL A 297     9723  11133   6629  -5053   1505   1369
ATOM   4156  HB  VAL A 297      59.552  -9.663  14.709  1.00 72.65           H  
ATOM   4157 HG11 VAL A 297      57.695  -8.127  15.094  1.00 70.32           H  
ATOM   4158 HG12 VAL A 297      58.480  -8.468  16.619  1.00 70.32           H  
ATOM   4159 HG13 VAL A 297      58.768  -6.935  15.797  1.00 70.32           H  
ATOM   4160 HG21 VAL A 297      58.935  -8.082  12.941  1.00 72.34           H  
ATOM   4161 HG22 VAL A 297      60.098  -6.914  13.539  1.00 72.34           H  
ATOM   4162 HG23 VAL A 297      60.646  -8.436  12.844  1.00 72.34           H  
ATOM   4163  H   VAL A 297      61.985 -10.209  14.522  1.00 77.92           H  
ATOM   4164  HA  VAL A 297      61.444  -7.578  15.824  1.00 75.06           H  
ATOM   4165  N   PRO A 298      61.690  -8.969  18.070  1.00 77.04           N  
ANISOU 4165  N   PRO A 298    10812  11261   7198  -6110   1581   1256
ATOM   4166  CA  PRO A 298      61.467  -9.591  19.377  1.00 78.63           C  
ANISOU 4166  CA  PRO A 298    10937  11590   7348  -6400   1514   1135
ATOM   4167  C   PRO A 298      60.146  -9.103  20.005  1.00 76.41           C  
ANISOU 4167  C   PRO A 298    10442  11422   7169  -6133   1411    956
ATOM   4168  O   PRO A 298      60.070  -7.996  20.535  1.00 74.74           O  
ANISOU 4168  O   PRO A 298    10458  10867   7073  -5906   1416    885
ATOM   4169  CB  PRO A 298      62.697  -9.190  20.206  1.00 80.87           C  
ANISOU 4169  CB  PRO A 298    11738  11376   7612  -6681   1582   1168
ATOM   4170  CG  PRO A 298      63.161  -7.872  19.609  1.00 79.90           C  
ANISOU 4170  CG  PRO A 298    11919  10818   7620  -6372   1696   1282
ATOM   4171  CD  PRO A 298      62.732  -7.943  18.141  1.00 78.41           C  
ANISOU 4171  CD  PRO A 298    11452  10921   7420  -6159   1680   1400
ATOM   4172  HA  PRO A 298      61.440 -10.676  19.298  1.00 78.63           H  
ATOM   4173  HB3 PRO A 298      63.483  -9.933  20.065  1.00 80.87           H  
ATOM   4174  HB2 PRO A 298      62.501  -9.127  21.276  1.00 80.87           H  
ATOM   4175  HG3 PRO A 298      64.233  -7.711  19.728  1.00 79.90           H  
ATOM   4176  HG2 PRO A 298      62.652  -7.050  20.106  1.00 79.90           H  
ATOM   4177  HD2 PRO A 298      62.380  -6.974  17.801  1.00 78.41           H  
ATOM   4178  HD3 PRO A 298      63.575  -8.225  17.516  1.00 78.41           H  
ATOM   4179  N   ALA A 299      59.127  -9.978  19.975  1.00 77.04           N  
ANISOU 4179  N   ALA A 299    10075  11977   7219  -6143   1341    904
ATOM   4180  CA  ALA A 299      57.967  -9.978  20.866  1.00 76.59           C  
ANISOU 4180  CA  ALA A 299     9813  12057   7232  -6016   1227    771
ATOM   4181  C   ALA A 299      58.316 -10.860  22.089  1.00 80.59           C  
ANISOU 4181  C   ALA A 299    10356  12641   7625  -6504   1126    788
ATOM   4182  O   ALA A 299      59.491 -11.132  22.345  1.00 83.56           O  
ANISOU 4182  O   ALA A 299    11103  12748   7898  -6865   1165    844
ATOM   4183  CB  ALA A 299      56.755 -10.562  20.104  1.00 75.30           C  
ANISOU 4183  CB  ALA A 299     9148  12344   7118  -5751   1227    738
ATOM   4184  HB1 ALA A 299      55.835 -10.438  20.674  1.00 75.30           H  
ATOM   4185  HB2 ALA A 299      56.608 -10.047  19.154  1.00 75.30           H  
ATOM   4186  HB3 ALA A 299      56.860 -11.623  19.884  1.00 75.30           H  
ATOM   4187  H   ALA A 299      59.284 -10.850  19.484  1.00 77.04           H  
ATOM   4188  HA  ALA A 299      57.732  -8.969  21.199  1.00 76.59           H  
ATOM   4189  N   ALA A 300      57.314 -11.242  22.897  1.00 81.71           N  
ANISOU 4189  N   ALA A 300    10126  13143   7778  -6538    995    759
ATOM   4190  CA  ALA A 300      57.449 -12.057  24.109  1.00 85.50           C  
ANISOU 4190  CA  ALA A 300    10583  13768   8134  -7039    841    805
ATOM   4191  C   ALA A 300      58.048 -11.254  25.278  1.00 86.88           C  
ANISOU 4191  C   ALA A 300    11336  13467   8208  -7303    802    723
ATOM   4192  O   ALA A 300      57.421 -10.296  25.727  1.00 84.97           O  
ANISOU 4192  O   ALA A 300    11292  12960   8031  -7037    793    599
ATOM   4193  CB  ALA A 300      58.081 -13.447  23.862  1.00 88.61           C  
ANISOU 4193  CB  ALA A 300    10765  14477   8424  -7453    863    966
ATOM   4194  HB1 ALA A 300      58.140 -14.020  24.788  1.00 88.61           H  
ATOM   4195  HB2 ALA A 300      57.471 -14.031  23.178  1.00 88.61           H  
ATOM   4196  HB3 ALA A 300      59.088 -13.390  23.451  1.00 88.61           H  
ATOM   4197  H   ALA A 300      56.380 -10.946  22.655  1.00 81.71           H  
ATOM   4198  HA  ALA A 300      56.423 -12.255  24.417  1.00 85.50           H  
ATOM   4199  N   LEU A 301      59.224 -11.662  25.791  1.00 90.74           N  
ANISOU 4199  N   LEU A 301    12119  13823   8533  -7826    810    785
ATOM   4200  CA  LEU A 301      59.803 -11.184  27.049  1.00 93.31           C  
ANISOU 4200  CA  LEU A 301    12973  13774   8706  -8210    760    700
ATOM   4201  C   LEU A 301      61.025 -10.273  26.862  1.00 93.90           C  
ANISOU 4201  C   LEU A 301    13728  13189   8760  -8236    983    647
ATOM   4202  O   LEU A 301      61.604 -10.167  25.781  1.00 92.93           O  
ANISOU 4202  O   LEU A 301    13675  12892   8743  -7990   1159    717
ATOM   4203  CB  LEU A 301      60.194 -12.412  27.909  1.00 97.71           C  
ANISOU 4203  CB  LEU A 301    13419  14648   9059  -8877    566    790
ATOM   4204  CG  LEU A 301      58.993 -13.193  28.486  1.00 99.25           C  
ANISOU 4204  CG  LEU A 301    13114  15350   9248  -8933    294    833
ATOM   4205  CD1 LEU A 301      59.468 -14.490  29.158  1.00104.36           C  
ANISOU 4205  CD1 LEU A 301    13606  16348   9699  -9636     79    979
ATOM   4206  CD2 LEU A 301      58.168 -12.357  29.482  1.00 98.90           C  
ANISOU 4206  CD2 LEU A 301    13320  15064   9194  -8735    216    677
ATOM   4207  H   LEU A 301      59.703 -12.422  25.328  1.00 90.74           H  
ATOM   4208  HA  LEU A 301      59.074 -10.582  27.590  1.00 93.31           H  
ATOM   4209  HB3 LEU A 301      60.826 -12.108  28.745  1.00 97.71           H  
ATOM   4210  HB2 LEU A 301      60.812 -13.081  27.309  1.00 97.71           H  
ATOM   4211  HG  LEU A 301      58.335 -13.480  27.664  1.00 99.25           H  
ATOM   4212 HD11 LEU A 301      58.625 -15.074  29.527  1.00104.36           H  
ATOM   4213 HD12 LEU A 301      60.016 -15.119  28.455  1.00104.36           H  
ATOM   4214 HD13 LEU A 301      60.127 -14.283  30.002  1.00104.36           H  
ATOM   4215 HD21 LEU A 301      57.380 -12.957  29.936  1.00 98.90           H  
ATOM   4216 HD22 LEU A 301      58.793 -11.970  30.288  1.00 98.90           H  
ATOM   4217 HD23 LEU A 301      57.677 -11.511  29.001  1.00 98.90           H  
ATOM   4218  N   GLU A 302      61.388  -9.610  27.974  1.00 96.11           N  
ANISOU 4218  N   GLU A 302    14517  13102   8897  -8544    983    538
ATOM   4219  CA  GLU A 302      62.460  -8.629  28.117  1.00 97.32           C  
ANISOU 4219  CA  GLU A 302    15355  12564   9059  -8514   1243    471
ATOM   4220  C   GLU A 302      63.836  -9.297  28.225  1.00101.40           C  
ANISOU 4220  C   GLU A 302    16233  12858   9439  -8995   1359    558
ATOM   4221  O   GLU A 302      63.949 -10.457  28.622  1.00104.18           O  
ANISOU 4221  O   GLU A 302    16332  13600   9653  -9436   1211    653
ATOM   4222  CB  GLU A 302      62.270  -7.843  29.438  1.00 98.22           C  
ANISOU 4222  CB  GLU A 302    15922  12347   9050  -8656   1242    294
ATOM   4223  CG  GLU A 302      60.819  -7.487  29.815  1.00 96.00           C  
ANISOU 4223  CG  GLU A 302    15415  12145   8916  -8148   1185    199
ATOM   4224  CD  GLU A 302      60.750  -6.388  30.877  1.00 99.55           C  
ANISOU 4224  CD  GLU A 302    16395  12199   9230  -8284   1241     25
ATOM   4225  OE1 GLU A 302      61.602  -6.417  31.793  1.00101.66           O  
ANISOU 4225  OE1 GLU A 302    17185  12193   9250  -8837   1286    -34
ATOM   4226  OE2 GLU A 302      59.835  -5.543  30.764  1.00 98.95           O1-
ANISOU 4226  OE2 GLU A 302    16239  12080   9280  -7859   1251    -58
ATOM   4227  HB2 GLU A 302      62.689  -8.400  30.279  1.00 98.22           H  
ATOM   4228  HG3 GLU A 302      60.303  -8.366  30.200  1.00 96.00           H  
ATOM   4229  HG2 GLU A 302      60.261  -7.169  28.937  1.00 96.00           H  
ATOM   4230  H   GLU A 302      60.846  -9.781  28.808  1.00 96.11           H  
ATOM   4231  HA  GLU A 302      62.430  -7.945  27.265  1.00 97.32           H  
ATOM   4232  HB3 GLU A 302      62.863  -6.928  29.370  1.00 98.22           H  
ATOM   4233  N   ASN A 303      64.886  -8.523  27.907  1.00102.41           N  
ANISOU 4233  N   ASN A 303    16945  12341   9623  -8895   1645    544
ATOM   4234  CA  ASN A 303      66.303  -8.820  28.158  1.00106.62           C  
ANISOU 4234  CA  ASN A 303    17982  12502  10029  -9349   1816    609
ATOM   4235  C   ASN A 303      66.878  -9.943  27.276  1.00108.36           C  
ANISOU 4235  C   ASN A 303    17895  13063  10214  -9581   1764    803
ATOM   4236  O   ASN A 303      68.036 -10.319  27.446  1.00112.55           O  
ANISOU 4236  O   ASN A 303    18819  13334  10610 -10038   1876    862
ATOM   4237  CB  ASN A 303      66.643  -8.971  29.667  1.00110.64           C  
ANISOU 4237  CB  ASN A 303    19009  12781  10249  -9984   1784    458
ATOM   4238  CG  ASN A 303      66.341  -7.738  30.536  1.00110.26           C  
ANISOU 4238  CG  ASN A 303    19512  12163  10219  -9781   1984    272
ATOM   4239  OD1 ASN A 303      66.101  -7.880  31.732  1.00108.07           O  
ANISOU 4239  OD1 ASN A 303    19456  11427  10177  -9271   2269    294
ATOM   4240  ND2 ASN A 303      66.376  -6.527  29.974  1.00112.47           N  
ANISOU 4240  ND2 ASN A 303    20010  12478  10245 -10194   1839    109
ATOM   4241  H   ASN A 303      64.688  -7.594  27.563  1.00102.41           H  
ATOM   4242  HA  ASN A 303      66.838  -7.938  27.808  1.00106.62           H  
ATOM   4243  HB3 ASN A 303      67.705  -9.186  29.788  1.00110.64           H  
ATOM   4244  HB2 ASN A 303      66.118  -9.830  30.085  1.00110.64           H  
ATOM   4245 HD22 ASN A 303      66.174  -5.714  30.538  1.00112.47           H  
ATOM   4246 HD21 ASN A 303      66.571  -6.425  28.989  1.00112.47           H  
ATOM   4247  N   VAL A 304      66.093 -10.436  26.302  1.00105.72           N  
ANISOU 4247  N   VAL A 304    16888  13290   9989  -9282   1620    895
ATOM   4248  CA  VAL A 304      66.541 -11.283  25.201  1.00106.50           C  
ANISOU 4248  CA  VAL A 304    16722  13639  10103  -9327   1654   1088
ATOM   4249  C   VAL A 304      67.129 -10.312  24.170  1.00105.53           C  
ANISOU 4249  C   VAL A 304    16909  13032  10155  -8896   1898   1185
ATOM   4250  O   VAL A 304      66.443  -9.382  23.756  1.00102.48           O  
ANISOU 4250  O   VAL A 304    16536  12455   9949  -8380   1951   1130
ATOM   4251  CB  VAL A 304      65.334 -12.038  24.570  1.00103.86           C  
ANISOU 4251  CB  VAL A 304    15633  13979   9848  -9041   1496   1142
ATOM   4252  CG1 VAL A 304      65.812 -13.067  23.527  1.00106.55           C  
ANISOU 4252  CG1 VAL A 304    15735  14628  10121  -9276   1533   1328
ATOM   4253  CG2 VAL A 304      64.445 -12.734  25.615  1.00102.55           C  
ANISOU 4253  CG2 VAL A 304    15074  14266   9624  -9181   1251   1045
ATOM   4254  HB  VAL A 304      64.688 -11.323  24.056  1.00103.86           H  
ATOM   4255 HG11 VAL A 304      64.973 -13.629  23.115  1.00106.55           H  
ATOM   4256 HG12 VAL A 304      66.321 -12.592  22.690  1.00106.55           H  
ATOM   4257 HG13 VAL A 304      66.501 -13.787  23.972  1.00106.55           H  
ATOM   4258 HG21 VAL A 304      63.636 -13.286  25.135  1.00102.55           H  
ATOM   4259 HG22 VAL A 304      65.020 -13.439  26.216  1.00102.55           H  
ATOM   4260 HG23 VAL A 304      63.976 -12.019  26.292  1.00102.55           H  
ATOM   4261  H   VAL A 304      65.151 -10.079  26.242  1.00105.72           H  
ATOM   4262  HA  VAL A 304      67.291 -11.993  25.555  1.00106.50           H  
ATOM   4263  N   ILE A 305      68.401 -10.521  23.809  1.00108.22           N  
ANISOU 4263  N   ILE A 305    17468  13195  10454  -9104   2036   1356
ATOM   4264  CA  ILE A 305      69.307  -9.610  23.107  1.00108.67           C  
ANISOU 4264  CA  ILE A 305    17919  12702  10668  -8785   2280   1502
ATOM   4265  C   ILE A 305      70.158  -8.843  24.141  1.00111.40           C  
ANISOU 4265  C   ILE A 305    18982  12338  11006  -8952   2498   1411
ATOM   4266  O   ILE A 305      70.043  -7.627  24.285  1.00109.72           O  
ANISOU 4266  O   ILE A 305    18969  11773  10946  -8576   2607   1320
ATOM   4267  CB  ILE A 305      68.714  -8.769  21.921  1.00104.57           C  
ANISOU 4267  CB  ILE A 305    17123  12215  10395  -8064   2284   1565
ATOM   4268  CG1 ILE A 305      67.783  -9.517  20.926  1.00102.54           C  
ANISOU 4268  CG1 ILE A 305    16188  12648  10122  -7878   2082   1578
ATOM   4269  CG2 ILE A 305      69.842  -8.076  21.125  1.00105.04           C  
ANISOU 4269  CG2 ILE A 305    17504  11795  10611  -7799   2498   1809
ATOM   4270  CD1 ILE A 305      68.359 -10.798  20.316  1.00105.63           C  
ANISOU 4270  CD1 ILE A 305    16363  13392  10380  -8138   2068   1755
ATOM   4271  H   ILE A 305      68.840 -11.338  24.207  1.00108.22           H  
ATOM   4272  HA  ILE A 305      70.019 -10.280  22.630  1.00108.67           H  
ATOM   4273  HB  ILE A 305      68.106  -7.973  22.354  1.00104.57           H  
ATOM   4274 HG13 ILE A 305      67.518  -8.837  20.116  1.00102.54           H  
ATOM   4275 HG12 ILE A 305      66.828  -9.766  21.383  1.00102.54           H  
ATOM   4276 HG21 ILE A 305      69.461  -7.569  20.239  1.00105.04           H  
ATOM   4277 HG22 ILE A 305      70.363  -7.325  21.719  1.00105.04           H  
ATOM   4278 HG23 ILE A 305      70.583  -8.799  20.786  1.00105.04           H  
ATOM   4279 HD11 ILE A 305      67.706 -11.176  19.529  1.00105.63           H  
ATOM   4280 HD12 ILE A 305      69.343 -10.634  19.875  1.00105.63           H  
ATOM   4281 HD13 ILE A 305      68.443 -11.580  21.069  1.00105.63           H  
ATOM   4282  N   THR A 306      71.022  -9.571  24.865  1.00116.03           N  
ANISOU 4282  N   THR A 306    19964  12718  11403  -9544   2578   1430
ATOM   4283  CA  THR A 306      72.104  -9.034  25.695  1.00119.78           C  
ANISOU 4283  CA  THR A 306    21227  12439  11846  -9760   2859   1369
ATOM   4284  C   THR A 306      73.349  -8.748  24.824  1.00122.50           C  
ANISOU 4284  C   THR A 306    21902  12344  12297  -9689   3119   1628
ATOM   4285  O   THR A 306      73.311  -8.919  23.604  1.00121.63           O  
ANISOU 4285  O   THR A 306    21403  12568  12244  -9529   3039   1842
ATOM   4286  CB  THR A 306      72.429 -10.057  26.811  1.00123.63           C  
ANISOU 4286  CB  THR A 306    22021  12939  12014 -10548   2776   1204
ATOM   4287  OG1 THR A 306      72.922 -11.275  26.286  1.00126.63           O  
ANISOU 4287  OG1 THR A 306    22151  13720  12241 -11013   2647   1347
ATOM   4288  CG2 THR A 306      71.252 -10.355  27.744  1.00121.33           C  
ANISOU 4288  CG2 THR A 306    21434  13058  11609 -10638   2506    987
ATOM   4289  H   THR A 306      71.031 -10.571  24.734  1.00116.03           H  
ATOM   4290  HA  THR A 306      71.781  -8.109  26.156  1.00119.78           H  
ATOM   4291  HB  THR A 306      73.220  -9.639  27.437  1.00123.63           H  
ATOM   4292  HG1 THR A 306      73.762 -11.444  26.704  1.00126.63           H  
ATOM   4293 HG21 THR A 306      71.574 -10.944  28.604  1.00121.33           H  
ATOM   4294 HG22 THR A 306      70.798  -9.439  28.120  1.00121.33           H  
ATOM   4295 HG23 THR A 306      70.484 -10.928  27.226  1.00121.33           H  
ATOM   4296  N   GLY A 307      74.460  -8.312  25.443  1.00126.17           N  
ANISOU 4296  N   GLY A 307    23104  12056  12780  -9812   3443   1617
ATOM   4297  CA  GLY A 307      75.715  -7.968  24.773  1.00129.45           C  
ANISOU 4297  CA  GLY A 307    23895  11976  13314  -9746   3722   1888
ATOM   4298  C   GLY A 307      76.373  -9.122  23.998  1.00131.25           C  
ANISOU 4298  C   GLY A 307    23866  12595  13407 -10087   3592   2092
ATOM   4299  O   GLY A 307      76.965  -8.884  22.948  1.00131.04           O  
ANISOU 4299  O   GLY A 307    23719  12538  13532  -9769   3657   2382
ATOM   4300  H   GLY A 307      74.442  -8.213  26.450  1.00126.17           H  
ATOM   4301  HA3 GLY A 307      76.418  -7.619  25.530  1.00129.45           H  
ATOM   4302  HA2 GLY A 307      75.545  -7.129  24.098  1.00129.45           H  
ATOM   4303  N   GLU A 308      76.228 -10.363  24.489  1.00133.21           N  
ANISOU 4303  N   GLU A 308    24015  13231  13367 -10746   3401   1963
ATOM   4304  CA  GLU A 308      76.757 -11.591  23.889  1.00135.65           C  
ANISOU 4304  CA  GLU A 308    24091  13921  13528 -11150   3303   2147
ATOM   4305  C   GLU A 308      75.682 -12.401  23.133  1.00131.89           C  
ANISOU 4305  C   GLU A 308    22759  14321  13033 -11001   2994   2190
ATOM   4306  O   GLU A 308      76.018 -13.438  22.565  1.00133.60           O  
ANISOU 4306  O   GLU A 308    22720  14909  13131 -11299   2928   2341
ATOM   4307  CB  GLU A 308      77.436 -12.459  24.984  1.00140.80           C  
ANISOU 4307  CB  GLU A 308    25167  14441  13890 -12013   3323   2050
ATOM   4308  CG  GLU A 308      76.579 -12.859  26.208  1.00142.36           C  
ANISOU 4308  CG  GLU A 308    25301  14914  13876 -12454   3097   1756
ATOM   4309  CD  GLU A 308      76.518 -11.768  27.278  1.00143.24           C  
ANISOU 4309  CD  GLU A 308    25968  14440  14019 -12300   3262   1519
ATOM   4310  OE1 GLU A 308      77.587 -11.463  27.850  1.00150.85           O  
ANISOU 4310  OE1 GLU A 308    27721  14664  14931 -12538   3574   1480
ATOM   4311  OE2 GLU A 308      75.405 -11.240  27.483  1.00133.99           O1-
ANISOU 4311  OE2 GLU A 308    24468  13529  12913 -11957   3104   1368
ATOM   4312  HB2 GLU A 308      77.815 -13.372  24.525  1.00140.80           H  
ATOM   4313  HG3 GLU A 308      77.022 -13.737  26.678  1.00142.36           H  
ATOM   4314  HG2 GLU A 308      75.573 -13.152  25.906  1.00142.36           H  
ATOM   4315  H   GLU A 308      75.739 -10.464  25.369  1.00133.21           H  
ATOM   4316  HA  GLU A 308      77.524 -11.342  23.155  1.00135.65           H  
ATOM   4317  HB3 GLU A 308      78.333 -11.942  25.325  1.00140.80           H  
ATOM   4318  N   ARG A 309      74.424 -11.929  23.072  1.00127.20           N  
ANISOU 4318  N   ARG A 309    21751  14025  12554 -10543   2840   2058
ATOM   4319  CA  ARG A 309      73.365 -12.470  22.209  1.00123.55           C  
ANISOU 4319  CA  ARG A 309    20534  14294  12115 -10280   2615   2099
ATOM   4320  C   ARG A 309      73.192 -11.600  20.947  1.00120.52           C  
ANISOU 4320  C   ARG A 309    20032  13819  11942  -9632   2691   2288
ATOM   4321  O   ARG A 309      72.812 -12.122  19.900  1.00119.87           O  
ANISOU 4321  O   ARG A 309    19570  14145  11829  -9534   2624   2447
ATOM   4322  NH1 ARG A 309      70.085 -16.889  20.484  1.00127.38           N  
ANISOU 4322  NH1 ARG A 309    18388  17684  12328 -10598   1995   2168
ATOM   4323  NH2 ARG A 309      68.130 -15.947  19.681  1.00120.46           N1+
ANISOU 4323  NH2 ARG A 309    16899  17202  11667  -9642   1903   2021
ATOM   4324  CB  ARG A 309      72.051 -12.515  23.020  1.00120.58           C  
ANISOU 4324  CB  ARG A 309    19761  14321  11733 -10185   2392   1858
ATOM   4325  CG  ARG A 309      70.775 -12.933  22.257  1.00118.07           C  
ANISOU 4325  CG  ARG A 309    18707  14674  11480  -9809   2212   1875
ATOM   4326  CD  ARG A 309      70.790 -14.371  21.725  1.00125.67           C  
ANISOU 4326  CD  ARG A 309    19197  16271  12282 -10229   2083   1936
ATOM   4327  NE  ARG A 309      69.572 -14.655  20.953  1.00125.18           N  
ANISOU 4327  NE  ARG A 309    18480  16797  12287  -9848   1977   1941
ATOM   4328  CZ  ARG A 309      69.268 -15.831  20.376  1.00126.95           C  
ANISOU 4328  CZ  ARG A 309    18248  17563  12425 -10027   1949   2043
ATOM   4329  H   ARG A 309      74.212 -11.085  23.588  1.00127.20           H  
ATOM   4330  HA  ARG A 309      73.614 -13.483  21.888  1.00123.55           H  
ATOM   4331  HB3 ARG A 309      71.882 -11.529  23.442  1.00120.58           H  
ATOM   4332  HB2 ARG A 309      72.184 -13.179  23.875  1.00120.58           H  
ATOM   4333  HG3 ARG A 309      70.588 -12.245  21.434  1.00118.07           H  
ATOM   4334  HG2 ARG A 309      69.924 -12.824  22.930  1.00118.07           H  
ATOM   4335  HD3 ARG A 309      70.873 -15.078  22.551  1.00125.67           H  
ATOM   4336  HD2 ARG A 309      71.650 -14.527  21.074  1.00125.67           H  
ATOM   4337  HE  ARG A 309      68.933 -13.882  20.836  1.00125.18           H  
ATOM   4338 HH12 ARG A 309      69.849 -17.768  20.047  1.00127.38           H  
ATOM   4339 HH11 ARG A 309      70.943 -16.812  21.009  1.00127.38           H  
ATOM   4340 HH22 ARG A 309      67.885 -16.823  19.242  1.00120.46           H  
ATOM   4341 HH21 ARG A 309      67.503 -15.159  19.588  1.00120.46           H  
ATOM   4342  N   ALA A 310      73.499 -10.295  21.020  1.00118.91           N  
ANISOU 4342  N   ALA A 310    20162  13078  11939  -9213   2836   2282
ATOM   4343  CA  ALA A 310      73.481  -9.362  19.893  1.00116.61           C  
ANISOU 4343  CA  ALA A 310    19814  12621  11870  -8624   2907   2510
ATOM   4344  C   ALA A 310      74.652  -9.602  18.920  1.00119.10           C  
ANISOU 4344  C   ALA A 310    20286  12809  12156  -8725   3016   2838
ATOM   4345  O   ALA A 310      74.523  -9.305  17.733  1.00117.49           O  
ANISOU 4345  O   ALA A 310    19773  12874  11995  -8421   2932   3040
ATOM   4346  CB  ALA A 310      73.590  -7.935  20.452  1.00116.28           C  
ANISOU 4346  CB  ALA A 310    20170  11944  12068  -8237   3103   2482
ATOM   4347  HB1 ALA A 310      73.603  -7.193  19.652  1.00116.28           H  
ATOM   4348  HB2 ALA A 310      72.745  -7.697  21.098  1.00116.28           H  
ATOM   4349  HB3 ALA A 310      74.493  -7.810  21.049  1.00116.28           H  
ATOM   4350  H   ALA A 310      73.767  -9.916  21.920  1.00118.91           H  
ATOM   4351  HA  ALA A 310      72.542  -9.467  19.347  1.00116.61           H  
ATOM   4352  N   LYS A 311      75.765 -10.177  19.413  1.00123.17           N  
ANISOU 4352  N   LYS A 311    21306  12918  12575  -9184   3198   2890
ATOM   4353  CA  LYS A 311      76.963 -10.521  18.648  1.00126.25           C  
ANISOU 4353  CA  LYS A 311    21916  13121  12932  -9324   3326   3214
ATOM   4354  C   LYS A 311      76.814 -11.798  17.797  1.00126.18           C  
ANISOU 4354  C   LYS A 311    21455  13779  12707  -9592   3156   3307
ATOM   4355  O   LYS A 311      77.652 -12.020  16.924  1.00128.35           O  
ANISOU 4355  O   LYS A 311    21819  14002  12946  -9628   3226   3601
ATOM   4356  CB  LYS A 311      78.129 -10.736  19.645  1.00131.15           C  
ANISOU 4356  CB  LYS A 311    23232  13107  13493  -9787   3586   3222
ATOM   4357  CG  LYS A 311      78.746  -9.409  20.102  1.00131.64           C  
ANISOU 4357  CG  LYS A 311    23851  12370  13795  -9467   3872   3228
ATOM   4358  CD  LYS A 311      79.893  -9.562  21.113  1.00134.02           C  
ANISOU 4358  CD  LYS A 311    24903  11974  14046  -9889   4191   3300
ATOM   4359  CE  LYS A 311      80.431  -8.201  21.580  1.00133.50           C  
ANISOU 4359  CE  LYS A 311    25413  11173  14137  -9725   4489   3138
ATOM   4360  NZ  LYS A 311      81.580  -8.351  22.489  1.00136.99           N1+
ANISOU 4360  NZ  LYS A 311    26629  10774  14647  -9879   4899   3304
ATOM   4361  HG3 LYS A 311      77.963  -8.784  20.532  1.00131.64           H  
ATOM   4362  HG2 LYS A 311      79.119  -8.886  19.222  1.00131.64           H  
ATOM   4363  HD3 LYS A 311      80.697 -10.144  20.660  1.00134.02           H  
ATOM   4364  HD2 LYS A 311      79.545 -10.132  21.975  1.00134.02           H  
ATOM   4365  HE3 LYS A 311      79.647  -7.637  22.087  1.00133.50           H  
ATOM   4366  HE2 LYS A 311      80.751  -7.609  20.722  1.00133.50           H  
ATOM   4367  HZ1 LYS A 311      81.916  -7.438  22.762  1.00136.99           H  
ATOM   4368  HZ2 LYS A 311      81.295  -8.862  23.311  1.00136.99           H  
ATOM   4369  HZ3 LYS A 311      82.319  -8.854  22.019  1.00136.99           H  
ATOM   4370  H   LYS A 311      75.779 -10.392  20.399  1.00123.17           H  
ATOM   4371  HA  LYS A 311      77.205  -9.704  17.967  1.00126.25           H  
ATOM   4372  HB3 LYS A 311      78.926 -11.325  19.186  1.00131.15           H  
ATOM   4373  HB2 LYS A 311      77.791 -11.314  20.506  1.00131.15           H  
ATOM   4374  N   THR A 312      75.785 -12.630  18.036  1.00124.00           N  
ANISOU 4374  N   THR A 312    20698  14118  12297  -9760   2954   3077
ATOM   4375  CA  THR A 312      75.624 -13.949  17.412  1.00124.55           C  
ANISOU 4375  CA  THR A 312    20334  14823  12167 -10045   2847   3142
ATOM   4376  C   THR A 312      74.603 -13.978  16.256  1.00121.30           C  
ANISOU 4376  C   THR A 312    19389  14933  11768  -9607   2716   3200
ATOM   4377  O   THR A 312      74.512 -15.010  15.592  1.00122.34           O  
ANISOU 4377  O   THR A 312    19251  15496  11736  -9783   2701   3313
ATOM   4378  CB  THR A 312      75.229 -14.984  18.500  1.00125.51           C  
ANISOU 4378  CB  THR A 312    20217  15348  12121 -10584   2736   2917
ATOM   4379  OG1 THR A 312      73.964 -14.713  19.069  1.00121.70           O  
ANISOU 4379  OG1 THR A 312    19456  15063  11720 -10346   2585   2658
ATOM   4380  CG2 THR A 312      76.276 -15.123  19.615  1.00129.52           C  
ANISOU 4380  CG2 THR A 312    21274  15413  12526 -11186   2856   2899
ATOM   4381  H   THR A 312      75.121 -12.385  18.757  1.00124.00           H  
ATOM   4382  HA  THR A 312      76.576 -14.275  16.989  1.00124.55           H  
ATOM   4383  HB  THR A 312      75.141 -15.963  18.025  1.00125.51           H  
ATOM   4384  HG1 THR A 312      73.764 -15.396  19.689  1.00121.70           H  
ATOM   4385 HG21 THR A 312      75.984 -15.879  20.343  1.00129.52           H  
ATOM   4386 HG22 THR A 312      77.243 -15.415  19.206  1.00129.52           H  
ATOM   4387 HG23 THR A 312      76.418 -14.185  20.148  1.00129.52           H  
ATOM   4388  N   ILE A 313      73.869 -12.883  15.983  1.00117.67           N  
ANISOU 4388  N   ILE A 313    18793  14435  11482  -9067   2638   3120
ATOM   4389  CA  ILE A 313      72.817 -12.823  14.957  1.00114.93           C  
ANISOU 4389  CA  ILE A 313    17979  14575  11114  -8704   2512   3150
ATOM   4390  C   ILE A 313      73.193 -11.905  13.786  1.00114.77           C  
ANISOU 4390  C   ILE A 313    18068  14363  11174  -8306   2517   3437
ATOM   4391  O   ILE A 313      74.145 -11.127  13.854  1.00117.18           O  
ANISOU 4391  O   ILE A 313    18796  14139  11590  -8260   2635   3670
ATOM   4392  CB  ILE A 313      71.421 -12.518  15.577  1.00110.88           C  
ANISOU 4392  CB  ILE A 313    17038  14428  10664  -8448   2365   2856
ATOM   4393  CG1 ILE A 313      71.364 -11.335  16.573  1.00108.96           C  
ANISOU 4393  CG1 ILE A 313    17031  13753  10614  -8258   2368   2690
ATOM   4394  CG2 ILE A 313      70.850 -13.788  16.234  1.00111.61           C  
ANISOU 4394  CG2 ILE A 313    16734  15081  10590  -8826   2315   2704
ATOM   4395  CD1 ILE A 313      71.524  -9.945  15.943  1.00107.32           C  
ANISOU 4395  CD1 ILE A 313    17024  13127  10627  -7749   2405   2830
ATOM   4396  H   ILE A 313      74.022 -12.051  16.536  1.00117.67           H  
ATOM   4397  HA  ILE A 313      72.729 -13.803  14.484  1.00114.93           H  
ATOM   4398  HB  ILE A 313      70.733 -12.283  14.764  1.00110.88           H  
ATOM   4399 HG13 ILE A 313      72.098 -11.462  17.368  1.00108.96           H  
ATOM   4400 HG12 ILE A 313      70.393 -11.347  17.071  1.00108.96           H  
ATOM   4401 HG21 ILE A 313      69.838 -13.621  16.601  1.00111.61           H  
ATOM   4402 HG22 ILE A 313      70.805 -14.617  15.528  1.00111.61           H  
ATOM   4403 HG23 ILE A 313      71.461 -14.104  17.081  1.00111.61           H  
ATOM   4404 HD11 ILE A 313      71.331  -9.166  16.680  1.00107.32           H  
ATOM   4405 HD12 ILE A 313      72.535  -9.786  15.571  1.00107.32           H  
ATOM   4406 HD13 ILE A 313      70.828  -9.798  15.115  1.00107.32           H  
ATOM   4407  N   ASN A 314      72.453 -12.083  12.678  1.00112.15           N  
ANISOU 4407  N   ASN A 314    17351  14483  10778  -8043   2392   3430
ATOM   4408  CA  ASN A 314      72.742 -11.570  11.343  1.00112.51           C  
ANISOU 4408  CA  ASN A 314    17415  14549  10785  -7808   2346   3726
ATOM   4409  C   ASN A 314      71.474 -10.902  10.797  1.00108.82           C  
ANISOU 4409  C   ASN A 314    16611  14370  10367  -7388   2186   3608
ATOM   4410  O   ASN A 314      70.594 -11.573  10.258  1.00107.88           O  
ANISOU 4410  O   ASN A 314    16154  14764  10072  -7419   2133   3462
ATOM   4411  CB  ASN A 314      73.244 -12.724  10.437  1.00115.16           C  
ANISOU 4411  CB  ASN A 314    17679  15248  10829  -8157   2390   3869
ATOM   4412  CG  ASN A 314      74.536 -13.385  10.938  1.00118.97           C  
ANISOU 4412  CG  ASN A 314    18490  15469  11246  -8623   2549   3993
ATOM   4413  OD1 ASN A 314      75.627 -12.871  10.710  1.00123.19           O  
ANISOU 4413  OD1 ASN A 314    19382  15624  11802  -8652   2620   4307
ATOM   4414  ND2 ASN A 314      74.416 -14.522  11.626  1.00117.18           N  
ANISOU 4414  ND2 ASN A 314    18136  15447  10941  -9006   2599   3769
ATOM   4415  H   ASN A 314      71.675 -12.722  12.743  1.00112.15           H  
ATOM   4416  HA  ASN A 314      73.525 -10.811  11.394  1.00112.51           H  
ATOM   4417  HB3 ASN A 314      73.430 -12.345   9.431  1.00115.16           H  
ATOM   4418  HB2 ASN A 314      72.473 -13.489  10.332  1.00115.16           H  
ATOM   4419 HD22 ASN A 314      75.245 -14.980  11.977  1.00117.18           H  
ATOM   4420 HD21 ASN A 314      73.504 -14.920  11.795  1.00117.18           H  
ATOM   4421  N   ALA A 315      71.387  -9.576  10.960  1.00106.94           N  
ANISOU 4421  N   ALA A 315    16475  13779  10380  -6996   2137   3670
ATOM   4422  CA  ALA A 315      70.287  -8.722  10.522  1.00103.15           C  
ANISOU 4422  CA  ALA A 315    15712  13498   9982  -6594   1980   3572
ATOM   4423  C   ALA A 315      70.794  -7.288  10.344  1.00103.23           C  
ANISOU 4423  C   ALA A 315    15905  13050  10267  -6220   1955   3831
ATOM   4424  O   ALA A 315      71.748  -6.892  11.008  1.00105.11           O  
ANISOU 4424  O   ALA A 315    16478  12776  10682  -6233   2104   3965
ATOM   4425  CB  ALA A 315      69.109  -8.818  11.507  1.00 99.76           C  
ANISOU 4425  CB  ALA A 315    15061  13222   9622  -6542   1964   3181
ATOM   4426  HB1 ALA A 315      68.291  -8.162  11.212  1.00 99.76           H  
ATOM   4427  HB2 ALA A 315      68.713  -9.832  11.554  1.00 99.76           H  
ATOM   4428  HB3 ALA A 315      69.411  -8.532  12.516  1.00 99.76           H  
ATOM   4429  H   ALA A 315      72.155  -9.105  11.419  1.00106.94           H  
ATOM   4430  HA  ALA A 315      69.949  -9.068   9.543  1.00103.15           H  
ATOM   4431  N   LYS A 316      70.146  -6.508   9.465  1.00101.57           N  
ANISOU 4431  N   LYS A 316    15480  13016  10096  -5899   1782   3916
ATOM   4432  CA  LYS A 316      70.421  -5.079   9.263  1.00101.76           C  
ANISOU 4432  CA  LYS A 316    15585  12662  10417  -5515   1740   4188
ATOM   4433  C   LYS A 316      69.441  -4.183  10.047  1.00 98.42           C  
ANISOU 4433  C   LYS A 316    15037  12120  10237  -5218   1741   3921
ATOM   4434  O   LYS A 316      69.635  -2.968  10.088  1.00 98.89           O  
ANISOU 4434  O   LYS A 316    15155  11824  10594  -4887   1762   4102
ATOM   4435  CB  LYS A 316      70.280  -4.763   7.756  1.00102.64           C  
ANISOU 4435  CB  LYS A 316    15542  13022  10435  -5372   1519   4506
ATOM   4436  CG  LYS A 316      71.427  -5.325   6.896  1.00107.44           C  
ANISOU 4436  CG  LYS A 316    16330  13658  10835  -5615   1509   4885
ATOM   4437  CD  LYS A 316      72.762  -4.583   7.088  1.00111.18           C  
ANISOU 4437  CD  LYS A 316    17093  13565  11585  -5471   1612   5330
ATOM   4438  CE  LYS A 316      73.895  -5.172   6.236  1.00114.09           C  
ANISOU 4438  CE  LYS A 316    17692  13923  11737  -5775   1652   5659
ATOM   4439  NZ  LYS A 316      75.151  -4.432   6.438  1.00117.86           N1+
ANISOU 4439  NZ  LYS A 316    18443  13833  12507  -5593   1762   6127
ATOM   4440  HG3 LYS A 316      71.136  -5.255   5.846  1.00107.44           H  
ATOM   4441  HG2 LYS A 316      71.559  -6.388   7.100  1.00107.44           H  
ATOM   4442  HD3 LYS A 316      73.063  -4.616   8.136  1.00111.18           H  
ATOM   4443  HD2 LYS A 316      72.627  -3.530   6.841  1.00111.18           H  
ATOM   4444  HE3 LYS A 316      73.631  -5.139   5.179  1.00114.09           H  
ATOM   4445  HE2 LYS A 316      74.058  -6.219   6.495  1.00114.09           H  
ATOM   4446  HZ1 LYS A 316      75.420  -4.476   7.411  1.00117.86           H  
ATOM   4447  HZ2 LYS A 316      75.880  -4.840   5.869  1.00117.86           H  
ATOM   4448  HZ3 LYS A 316      75.019  -3.466   6.172  1.00117.86           H  
ATOM   4449  H   LYS A 316      69.384  -6.908   8.938  1.00101.57           H  
ATOM   4450  HA  LYS A 316      71.422  -4.820   9.609  1.00101.76           H  
ATOM   4451  HB3 LYS A 316      70.228  -3.685   7.591  1.00102.64           H  
ATOM   4452  HB2 LYS A 316      69.331  -5.158   7.391  1.00102.64           H  
ATOM   4453  N   LEU A 317      68.411  -4.773  10.673  1.00 95.59           N  
ANISOU 4453  N   LEU A 317    14498  12055   9766  -5328   1732   3516
ATOM   4454  CA  LEU A 317      67.357  -4.091  11.413  1.00 92.28           C  
ANISOU 4454  CA  LEU A 317    13943  11577   9542  -5057   1712   3257
ATOM   4455  C   LEU A 317      66.873  -4.967  12.578  1.00 90.49           C  
ANISOU 4455  C   LEU A 317    13648  11500   9232  -5253   1770   2858
ATOM   4456  O   LEU A 317      66.898  -6.196  12.501  1.00 90.22           O  
ANISOU 4456  O   LEU A 317    13438  11880   8960  -5508   1739   2709
ATOM   4457  CB  LEU A 317      66.258  -3.620  10.425  1.00 90.13           C  
ANISOU 4457  CB  LEU A 317    13356  11626   9262  -4788   1507   3255
ATOM   4458  CG  LEU A 317      65.059  -2.841  11.009  1.00 86.49           C  
ANISOU 4458  CG  LEU A 317    12720  11155   8985  -4502   1467   3000
ATOM   4459  CD1 LEU A 317      65.476  -1.528  11.691  1.00 86.94           C  
ANISOU 4459  CD1 LEU A 317    12953  10682   9396  -4216   1575   3147
ATOM   4460  CD2 LEU A 317      64.018  -2.562   9.911  1.00 84.24           C  
ANISOU 4460  CD2 LEU A 317    12144  11252   8610  -4346   1262   2977
ATOM   4461  H   LEU A 317      68.344  -5.780  10.626  1.00 95.59           H  
ATOM   4462  HA  LEU A 317      67.801  -3.203  11.859  1.00 92.28           H  
ATOM   4463  HB3 LEU A 317      65.864  -4.494   9.911  1.00 90.13           H  
ATOM   4464  HB2 LEU A 317      66.718  -3.008   9.650  1.00 90.13           H  
ATOM   4465  HG  LEU A 317      64.568  -3.464  11.756  1.00 86.49           H  
ATOM   4466 HD11 LEU A 317      64.602  -0.987  12.053  1.00 86.94           H  
ATOM   4467 HD12 LEU A 317      66.118  -1.704  12.553  1.00 86.94           H  
ATOM   4468 HD13 LEU A 317      66.010  -0.874  11.004  1.00 86.94           H  
ATOM   4469 HD21 LEU A 317      63.139  -2.064  10.319  1.00 84.24           H  
ATOM   4470 HD22 LEU A 317      64.425  -1.924   9.127  1.00 84.24           H  
ATOM   4471 HD23 LEU A 317      63.677  -3.486   9.445  1.00 84.24           H  
ATOM   4472  N   VAL A 318      66.419  -4.315  13.654  1.00 89.31           N  
ANISOU 4472  N   VAL A 318    13630  11017   9285  -5128   1860   2707
ATOM   4473  CA  VAL A 318      65.735  -4.899  14.800  1.00 87.56           C  
ANISOU 4473  CA  VAL A 318    13337  10931   9001  -5289   1873   2357
ATOM   4474  C   VAL A 318      64.503  -4.026  15.075  1.00 84.13           C  
ANISOU 4474  C   VAL A 318    12714  10525   8725  -4948   1803   2163
ATOM   4475  O   VAL A 318      64.599  -2.800  15.038  1.00 83.92           O  
ANISOU 4475  O   VAL A 318    12821  10129   8937  -4655   1863   2249
ATOM   4476  CB  VAL A 318      66.687  -5.080  16.017  1.00 89.75           C  
ANISOU 4476  CB  VAL A 318    14003  10806   9292  -5574   2047   2302
ATOM   4477  CG1 VAL A 318      65.970  -5.696  17.235  1.00 88.93           C  
ANISOU 4477  CG1 VAL A 318    13771  10975   9043  -5855   1998   1993
ATOM   4478  CG2 VAL A 318      67.931  -5.925  15.690  1.00 93.25           C  
ANISOU 4478  CG2 VAL A 318    14708  11095   9627  -5876   2149   2544
ATOM   4479  HB  VAL A 318      67.044  -4.092  16.302  1.00 89.75           H  
ATOM   4480 HG11 VAL A 318      66.658  -5.830  18.070  1.00 88.93           H  
ATOM   4481 HG12 VAL A 318      65.156  -5.065  17.595  1.00 88.93           H  
ATOM   4482 HG13 VAL A 318      65.550  -6.673  16.994  1.00 88.93           H  
ATOM   4483 HG21 VAL A 318      68.577  -6.031  16.563  1.00 93.25           H  
ATOM   4484 HG22 VAL A 318      67.653  -6.926  15.357  1.00 93.25           H  
ATOM   4485 HG23 VAL A 318      68.531  -5.471  14.905  1.00 93.25           H  
ATOM   4486  H   VAL A 318      66.487  -3.307  13.653  1.00 89.31           H  
ATOM   4487  HA  VAL A 318      65.384  -5.885  14.509  1.00 87.56           H  
ATOM   4488  N   CYS A 319      63.346  -4.649  15.333  1.00 81.82           N  
ANISOU 4488  N   CYS A 319    12107  10666   8313  -4981   1696   1919
ATOM   4489  CA  CYS A 319      62.066  -3.969  15.527  1.00 78.64           C  
ANISOU 4489  CA  CYS A 319    11520  10323   8037  -4690   1627   1721
ATOM   4490  C   CYS A 319      61.370  -4.506  16.776  1.00 77.76           C  
ANISOU 4490  C   CYS A 319    11371  10298   7877  -4858   1633   1450
ATOM   4491  O   CYS A 319      60.622  -5.474  16.689  1.00 77.16           O  
ANISOU 4491  O   CYS A 319    11026  10637   7655  -5010   1566   1318
ATOM   4492  CB  CYS A 319      61.200  -4.086  14.252  1.00 76.91           C  
ANISOU 4492  CB  CYS A 319    10961  10515   7744  -4512   1492   1693
ATOM   4493  SG  CYS A 319      61.753  -2.966  12.938  1.00 78.82           S  
ANISOU 4493  SG  CYS A 319    11239  10664   8046  -4305   1419   2027
ATOM   4494  H   CYS A 319      63.338  -5.661  15.337  1.00 81.82           H  
ATOM   4495  HA  CYS A 319      62.234  -2.918  15.736  1.00 78.64           H  
ATOM   4496  HB3 CYS A 319      60.159  -3.843  14.469  1.00 76.91           H  
ATOM   4497  HB2 CYS A 319      61.222  -5.104  13.871  1.00 76.91           H  
ATOM   4498  HG  CYS A 319      61.677  -1.850  13.675  1.00 78.82           H  
ATOM   4499  N   GLU A 320      61.618  -3.884  17.940  1.00 78.13           N  
ANISOU 4499  N   GLU A 320    11696   9940   8048  -4833   1724   1390
ATOM   4500  CA  GLU A 320      61.132  -4.332  19.247  1.00 78.15           C  
ANISOU 4500  CA  GLU A 320    11728   9976   7989  -5019   1710   1159
ATOM   4501  C   GLU A 320      59.605  -4.245  19.354  1.00 75.30           C  
ANISOU 4501  C   GLU A 320    11011   9944   7657  -4797   1580    973
ATOM   4502  O   GLU A 320      59.047  -3.155  19.407  1.00 73.26           O  
ANISOU 4502  O   GLU A 320    10717   9554   7563  -4443   1576    946
ATOM   4503  CB  GLU A 320      61.740  -3.445  20.341  1.00 79.09           C  
ANISOU 4503  CB  GLU A 320    12287   9541   8224  -5006   1867   1131
ATOM   4504  CG  GLU A 320      63.260  -3.571  20.477  1.00 82.64           C  
ANISOU 4504  CG  GLU A 320    13163   9579   8659  -5231   2045   1296
ATOM   4505  CD  GLU A 320      63.752  -2.905  21.758  1.00 84.60           C  
ANISOU 4505  CD  GLU A 320    13890   9317   8935  -5350   2231   1190
ATOM   4506  OE1 GLU A 320      63.357  -1.744  22.004  1.00 83.00           O  
ANISOU 4506  OE1 GLU A 320    13771   8855   8909  -5029   2318   1132
ATOM   4507  OE2 GLU A 320      64.536  -3.563  22.475  1.00 87.92           O1-
ANISOU 4507  OE2 GLU A 320    14622   9594   9189  -5786   2301   1160
ATOM   4508  HB2 GLU A 320      61.491  -2.405  20.136  1.00 79.09           H  
ATOM   4509  HG3 GLU A 320      63.747  -3.114  19.618  1.00 82.64           H  
ATOM   4510  HG2 GLU A 320      63.551  -4.622  20.489  1.00 82.64           H  
ATOM   4511  H   GLU A 320      62.224  -3.074  17.932  1.00 78.13           H  
ATOM   4512  HA  GLU A 320      61.439  -5.364  19.405  1.00 78.15           H  
ATOM   4513  HB3 GLU A 320      61.279  -3.696  21.297  1.00 79.09           H  
ATOM   4514  N   ALA A 321      58.936  -5.402  19.407  1.00 75.38           N  
ANISOU 4514  N   ALA A 321    10746  10375   7522  -5004   1484    864
ATOM   4515  CA  ALA A 321      57.487  -5.498  19.559  1.00 73.11           C  
ANISOU 4515  CA  ALA A 321    10134  10377   7269  -4804   1382    701
ATOM   4516  C   ALA A 321      57.102  -5.703  21.035  1.00 73.89           C  
ANISOU 4516  C   ALA A 321    10299  10454   7321  -5009   1329    569
ATOM   4517  O   ALA A 321      56.057  -5.214  21.461  1.00 72.37           O  
ANISOU 4517  O   ALA A 321    10019  10270   7206  -4800   1274    446
ATOM   4518  CB  ALA A 321      57.020  -6.701  18.735  1.00 73.29           C  
ANISOU 4518  CB  ALA A 321     9760  10893   7195  -4818   1336    700
ATOM   4519  HB1 ALA A 321      55.936  -6.761  18.712  1.00 73.29           H  
ATOM   4520  HB2 ALA A 321      57.342  -6.597  17.701  1.00 73.29           H  
ATOM   4521  HB3 ALA A 321      57.415  -7.643  19.113  1.00 73.29           H  
ATOM   4522  H   ALA A 321      59.461  -6.266  19.370  1.00 75.38           H  
ATOM   4523  HA  ALA A 321      56.993  -4.602  19.181  1.00 73.11           H  
ATOM   4524  N   ALA A 322      57.961  -6.364  21.828  1.00 76.58           N  
ANISOU 4524  N   ALA A 322    10808  10770   7517  -5447   1334    604
ATOM   4525  CA  ALA A 322      57.883  -6.420  23.286  1.00 77.69           C  
ANISOU 4525  CA  ALA A 322    11093  10854   7570  -5720   1264    498
ATOM   4526  C   ALA A 322      58.600  -5.205  23.883  1.00 78.14           C  
ANISOU 4526  C   ALA A 322    11680  10323   7685  -5678   1409    463
ATOM   4527  O   ALA A 322      59.448  -4.590  23.236  1.00 78.80           O  
ANISOU 4527  O   ALA A 322    12011  10082   7847  -5587   1563    575
ATOM   4528  CB  ALA A 322      58.620  -7.674  23.780  1.00 80.73           C  
ANISOU 4528  CB  ALA A 322    11467  11441   7766  -6248   1206    558
ATOM   4529  HB1 ALA A 322      58.768  -7.670  24.862  1.00 80.73           H  
ATOM   4530  HB2 ALA A 322      58.034  -8.560  23.556  1.00 80.73           H  
ATOM   4531  HB3 ALA A 322      59.598  -7.789  23.313  1.00 80.73           H  
ATOM   4532  H   ALA A 322      58.799  -6.741  21.407  1.00 76.58           H  
ATOM   4533  HA  ALA A 322      56.845  -6.442  23.624  1.00 77.69           H  
ATOM   4534  N   ASN A 323      58.264  -4.887  25.141  1.00 78.08           N  
ANISOU 4534  N   ASN A 323    11848  10173   7647  -5723   1377    326
ATOM   4535  CA  ASN A 323      58.928  -3.856  25.933  1.00 79.77           C  
ANISOU 4535  CA  ASN A 323    12649   9808   7853  -5815   1562    276
ATOM   4536  C   ASN A 323      60.215  -4.441  26.526  1.00 83.65           C  
ANISOU 4536  C   ASN A 323    13477  10165   8140  -6365   1605    313
ATOM   4537  O   ASN A 323      60.186  -5.498  27.152  1.00 85.15           O  
ANISOU 4537  O   ASN A 323    13476  10734   8144  -6770   1421    311
ATOM   4538  CB  ASN A 323      58.017  -3.402  27.096  1.00 79.25           C  
ANISOU 4538  CB  ASN A 323    12744   9622   7745  -5799   1531    110
ATOM   4539  CG  ASN A 323      56.704  -2.791  26.600  1.00 77.10           C  
ANISOU 4539  CG  ASN A 323    12051   9626   7616  -5370   1415     61
ATOM   4540  OD1 ASN A 323      55.697  -3.485  26.493  1.00 79.12           O  
ANISOU 4540  OD1 ASN A 323    11860  10376   7825  -5402   1210     66
ATOM   4541  ND2 ASN A 323      56.712  -1.493  26.290  1.00 74.72           N  
ANISOU 4541  ND2 ASN A 323    11888   8997   7505  -4966   1563     26
ATOM   4542  H   ASN A 323      57.561  -5.442  25.607  1.00 78.08           H  
ATOM   4543  HA  ASN A 323      59.158  -3.003  25.302  1.00 79.77           H  
ATOM   4544  HB3 ASN A 323      58.535  -2.669  27.718  1.00 79.25           H  
ATOM   4545  HB2 ASN A 323      57.781  -4.242  27.751  1.00 79.25           H  
ATOM   4546 HD22 ASN A 323      55.881  -1.070  25.904  1.00 74.72           H  
ATOM   4547 HD21 ASN A 323      57.568  -0.962  26.373  1.00 74.72           H  
ATOM   4548  N   GLY A 324      61.344  -3.763  26.284  1.00 85.46           N  
ANISOU 4548  N   GLY A 324    14193   9857   8422  -6377   1856    369
ATOM   4549  CA  GLY A 324      62.644  -4.045  26.879  1.00 89.89           C  
ANISOU 4549  CA  GLY A 324    15186  10178   8789  -6906   1944    385
ATOM   4550  C   GLY A 324      63.634  -5.057  26.259  1.00 91.74           C  
ANISOU 4550  C   GLY A 324    15455  10343   9058  -6978   2045    580
ATOM   4551  O   GLY A 324      64.674  -5.177  26.907  1.00 94.12           O  
ANISOU 4551  O   GLY A 324    16257  10099   9406  -7013   2303    642
ATOM   4552  H   GLY A 324      61.265  -2.901  25.755  1.00 85.46           H  
ATOM   4553  HA3 GLY A 324      62.495  -4.327  27.923  1.00 89.89           H  
ATOM   4554  HA2 GLY A 324      63.166  -3.088  26.916  1.00 89.89           H  
ATOM   4555  N   PRO A 325      63.423  -5.783  25.119  1.00 90.83           N  
ANISOU 4555  N   PRO A 325    14821  10758   8931  -6968   1873    688
ATOM   4556  CA  PRO A 325      64.360  -6.783  24.556  1.00 92.91           C  
ANISOU 4556  CA  PRO A 325    15079  11122   9099  -7278   1893    847
ATOM   4557  C   PRO A 325      65.861  -6.465  24.636  1.00 96.22           C  
ANISOU 4557  C   PRO A 325    16120  10929   9510  -7471   2151    931
ATOM   4558  O   PRO A 325      66.573  -7.083  25.428  1.00 99.88           O  
ANISOU 4558  O   PRO A 325    16916  11262   9774  -8003   2173    880
ATOM   4559  CB  PRO A 325      63.904  -7.043  23.112  1.00 90.23           C  
ANISOU 4559  CB  PRO A 325    14300  11079   8903  -6859   1854    987
ATOM   4560  CG  PRO A 325      62.416  -6.804  23.168  1.00 87.26           C  
ANISOU 4560  CG  PRO A 325    13493  11081   8579  -6587   1688    859
ATOM   4561  CD  PRO A 325      62.238  -5.747  24.255  1.00 87.14           C  
ANISOU 4561  CD  PRO A 325    13797  10711   8602  -6521   1734    694
ATOM   4562  HA  PRO A 325      64.194  -7.698  25.126  1.00 92.91           H  
ATOM   4563  HB3 PRO A 325      64.154  -8.047  22.772  1.00 90.23           H  
ATOM   4564  HB2 PRO A 325      64.343  -6.338  22.406  1.00 90.23           H  
ATOM   4565  HG3 PRO A 325      61.924  -7.729  23.471  1.00 87.26           H  
ATOM   4566  HG2 PRO A 325      61.986  -6.494  22.216  1.00 87.26           H  
ATOM   4567  HD2 PRO A 325      62.128  -4.754  23.816  1.00 87.14           H  
ATOM   4568  HD3 PRO A 325      61.341  -6.010  24.802  1.00 87.14           H  
ATOM   4569  N   THR A 326      66.331  -5.488  23.851  1.00 95.62           N  
ANISOU 4569  N   THR A 326    16206  10472   9654  -7053   2345   1074
ATOM   4570  CA  THR A 326      67.727  -5.076  23.818  1.00 99.29           C  
ANISOU 4570  CA  THR A 326    17225  10342  10158  -7167   2622   1213
ATOM   4571  C   THR A 326      68.083  -4.324  25.117  1.00101.58           C  
ANISOU 4571  C   THR A 326    18161  10016  10419  -7324   2863   1056
ATOM   4572  O   THR A 326      67.468  -3.314  25.462  1.00 99.67           O  
ANISOU 4572  O   THR A 326    18010   9556  10305  -7003   2952    945
ATOM   4573  CB  THR A 326      67.992  -4.230  22.549  1.00 98.23           C  
ANISOU 4573  CB  THR A 326    17019  10013  10291  -6656   2744   1479
ATOM   4574  OG1 THR A 326      67.260  -3.030  22.554  1.00 97.61           O  
ANISOU 4574  OG1 THR A 326    16803   9846  10438  -6137   2764   1439
ATOM   4575  CG2 THR A 326      67.678  -4.952  21.233  1.00 97.75           C  
ANISOU 4575  CG2 THR A 326    16452  10506  10184  -6612   2539   1630
ATOM   4576  H   THR A 326      65.677  -4.977  23.269  1.00 95.62           H  
ATOM   4577  HA  THR A 326      68.338  -5.971  23.743  1.00 99.29           H  
ATOM   4578  HB  THR A 326      69.051  -3.972  22.538  1.00 98.23           H  
ATOM   4579  HG1 THR A 326      66.333  -3.242  22.562  1.00 97.61           H  
ATOM   4580 HG21 THR A 326      67.970  -4.343  20.377  1.00 97.75           H  
ATOM   4581 HG22 THR A 326      68.219  -5.889  21.165  1.00 97.75           H  
ATOM   4582 HG23 THR A 326      66.614  -5.172  21.131  1.00 97.75           H  
ATOM   4583  N   THR A 327      69.079  -4.852  25.842  1.00106.04           N  
ANISOU 4583  N   THR A 327    19200  10296  10793  -7853   2985   1042
ATOM   4584  CA  THR A 327      69.656  -4.248  27.042  1.00109.20           C  
ANISOU 4584  CA  THR A 327    20325  10049  11115  -8083   3265    889
ATOM   4585  C   THR A 327      70.599  -3.088  26.640  1.00110.51           C  
ANISOU 4585  C   THR A 327    20905   9512  11572  -7657   3669   1065
ATOM   4586  O   THR A 327      71.041  -3.046  25.489  1.00110.44           O  
ANISOU 4586  O   THR A 327    20709   9513  11742  -7400   3702   1342
ATOM   4587  CB  THR A 327      70.462  -5.337  27.798  1.00113.67           C  
ANISOU 4587  CB  THR A 327    21290  10535  11366  -8843   3264    829
ATOM   4588  OG1 THR A 327      71.495  -5.843  26.987  1.00114.81           O  
ANISOU 4588  OG1 THR A 327    21281  10807  11534  -8936   3250   1072
ATOM   4589  CG2 THR A 327      69.617  -6.510  28.307  1.00113.21           C  
ANISOU 4589  CG2 THR A 327    20934  11065  11016  -9323   2901    648
ATOM   4590  H   THR A 327      69.522  -5.697  25.505  1.00106.04           H  
ATOM   4591  HA  THR A 327      68.844  -3.889  27.673  1.00109.20           H  
ATOM   4592  HB  THR A 327      70.944  -4.889  28.665  1.00113.67           H  
ATOM   4593  HG1 THR A 327      72.014  -6.441  27.507  1.00114.81           H  
ATOM   4594 HG21 THR A 327      70.223  -7.204  28.892  1.00113.21           H  
ATOM   4595 HG22 THR A 327      68.818  -6.151  28.952  1.00113.21           H  
ATOM   4596 HG23 THR A 327      69.166  -7.073  27.489  1.00113.21           H  
ATOM   4597  N   PRO A 328      70.944  -2.158  27.562  1.00111.99           N  
ANISOU 4597  N   PRO A 328    21656   9086  11809  -7580   3991    926
ATOM   4598  CA  PRO A 328      71.959  -1.107  27.354  1.00114.16           C  
ANISOU 4598  CA  PRO A 328    22365   8627  12382  -7188   4441   1114
ATOM   4599  C   PRO A 328      73.319  -1.575  26.791  1.00117.78           C  
ANISOU 4599  C   PRO A 328    23089   8812  12852  -7391   4594   1360
ATOM   4600  O   PRO A 328      73.918  -0.850  26.001  1.00118.61           O  
ANISOU 4600  O   PRO A 328    23214   8579  13274  -6938   4818   1662
ATOM   4601  CB  PRO A 328      72.152  -0.462  28.734  1.00116.94           C  
ANISOU 4601  CB  PRO A 328    23432   8372  12628  -7365   4780    851
ATOM   4602  CG  PRO A 328      70.839  -0.701  29.457  1.00114.32           C  
ANISOU 4602  CG  PRO A 328    22830   8538  12068  -7542   4457    570
ATOM   4603  CD  PRO A 328      70.298  -2.001  28.867  1.00111.63           C  
ANISOU 4603  CD  PRO A 328    21815   9029  11571  -7779   3956    611
ATOM   4604  HA  PRO A 328      71.525  -0.377  26.667  1.00114.16           H  
ATOM   4605  HB3 PRO A 328      72.399   0.598  28.667  1.00116.94           H  
ATOM   4606  HB2 PRO A 328      72.954  -0.954  29.289  1.00116.94           H  
ATOM   4607  HG3 PRO A 328      70.151   0.113  29.226  1.00114.32           H  
ATOM   4608  HG2 PRO A 328      70.953  -0.741  30.541  1.00114.32           H  
ATOM   4609  HD2 PRO A 328      70.563  -2.838  29.514  1.00111.63           H  
ATOM   4610  HD3 PRO A 328      69.210  -1.961  28.786  1.00111.63           H  
ATOM   4611  N   GLU A 329      73.785  -2.784  27.160  1.00120.06           N  
ANISOU 4611  N   GLU A 329    23558   9259  12802  -8073   4461   1258
ATOM   4612  CA  GLU A 329      75.007  -3.416  26.645  1.00123.33           C  
ANISOU 4612  CA  GLU A 329    24170   9504  13185  -8333   4556   1487
ATOM   4613  C   GLU A 329      74.797  -4.017  25.237  1.00120.61           C  
ANISOU 4613  C   GLU A 329    23138   9715  12974  -8042   4288   1783
ATOM   4614  O   GLU A 329      75.744  -4.050  24.452  1.00122.46           O  
ANISOU 4614  O   GLU A 329    23453   9665  13410  -7790   4461   2100
ATOM   4615  CB  GLU A 329      75.462  -4.525  27.629  1.00127.08           C  
ANISOU 4615  CB  GLU A 329    25027  10005  13251  -9194   4485   1303
ATOM   4616  CG  GLU A 329      74.397  -5.597  27.948  1.00123.38           C  
ANISOU 4616  CG  GLU A 329    24243  10168  12468  -9634   4089   1021
ATOM   4617  CD  GLU A 329      74.873  -6.771  28.801  1.00119.81           C  
ANISOU 4617  CD  GLU A 329    23963   9917  11642 -10488   3926    947
ATOM   4618  OE1 GLU A 329      76.082  -7.082  28.751  1.00123.02           O  
ANISOU 4618  OE1 GLU A 329    24727   9992  12024 -10747   4115   1098
ATOM   4619  OE2 GLU A 329      73.992  -7.366  29.458  1.00113.09           O1-
ANISOU 4619  OE2 GLU A 329    22871   9567  10533 -10905   3600    762
ATOM   4620  HB2 GLU A 329      76.357  -5.002  27.225  1.00127.08           H  
ATOM   4621  HG3 GLU A 329      74.030  -6.036  27.023  1.00123.38           H  
ATOM   4622  HG2 GLU A 329      73.552  -5.132  28.453  1.00123.38           H  
ATOM   4623  H   GLU A 329      73.239  -3.322  27.816  1.00120.06           H  
ATOM   4624  HA  GLU A 329      75.796  -2.666  26.580  1.00123.33           H  
ATOM   4625  HB3 GLU A 329      75.778  -4.060  28.564  1.00127.08           H  
ATOM   4626  N   GLY A 330      73.567  -4.447  24.902  1.00116.61           N  
ANISOU 4626  N   GLY A 330    21976   9979  12351  -8071   3883   1690
ATOM   4627  CA  GLY A 330      73.170  -4.969  23.596  1.00113.91           C  
ANISOU 4627  CA  GLY A 330    21002  10199  12080  -7835   3634   1920
ATOM   4628  C   GLY A 330      73.103  -3.882  22.518  1.00112.28           C  
ANISOU 4628  C   GLY A 330    20621   9817  12225  -7140   3733   2187
ATOM   4629  O   GLY A 330      73.558  -4.116  21.401  1.00113.44           O  
ANISOU 4629  O   GLY A 330    20694   9945  12464  -7012   3755   2501
ATOM   4630  H   GLY A 330      72.835  -4.373  25.595  1.00116.61           H  
ATOM   4631  HA3 GLY A 330      72.182  -5.422  23.693  1.00113.91           H  
ATOM   4632  HA2 GLY A 330      73.849  -5.762  23.283  1.00113.91           H  
ATOM   4633  N   ASP A 331      72.601  -2.682  22.865  1.00109.98           N  
ANISOU 4633  N   ASP A 331    20255   9409  12121  -6714   3781   2081
ATOM   4634  CA  ASP A 331      72.518  -1.500  21.994  1.00108.85           C  
ANISOU 4634  CA  ASP A 331    19948   9068  12342  -6057   3885   2338
ATOM   4635  C   ASP A 331      73.881  -0.980  21.524  1.00113.12           C  
ANISOU 4635  C   ASP A 331    20860   9024  13096  -5897   4193   2699
ATOM   4636  O   ASP A 331      73.978  -0.489  20.399  1.00112.99           O  
ANISOU 4636  O   ASP A 331    20544   9090  13298  -5498   4133   3040
ATOM   4637  CB  ASP A 331      71.782  -0.339  22.705  1.00107.48           C  
ANISOU 4637  CB  ASP A 331    19894   8603  12339  -5732   4046   2158
ATOM   4638  CG  ASP A 331      70.296  -0.571  22.974  1.00103.72           C  
ANISOU 4638  CG  ASP A 331    18894   8731  11785  -5633   3719   1927
ATOM   4639  OD1 ASP A 331      69.733  -1.502  22.366  1.00102.97           O  
ANISOU 4639  OD1 ASP A 331    18366   9262  11495  -5837   3391   1890
ATOM   4640  OD2 ASP A 331      69.729   0.233  23.743  1.00100.66           O1-
ANISOU 4640  OD2 ASP A 331    18539   8169  11538  -5343   3820   1793
ATOM   4641  HA  ASP A 331      71.964  -1.776  21.096  1.00108.85           H  
ATOM   4642  HB3 ASP A 331      71.845   0.568  22.103  1.00107.48           H  
ATOM   4643  HB2 ASP A 331      72.272  -0.112  23.654  1.00107.48           H  
ATOM   4644  H   ASP A 331      72.231  -2.584  23.802  1.00109.98           H  
ATOM   4645  N   LYS A 332      74.923  -1.096  22.367  1.00117.28           N  
ANISOU 4645  N   LYS A 332    22052   8956  13553  -6221   4521   2635
ATOM   4646  CA  LYS A 332      76.279  -0.620  22.091  1.00121.73           C  
ANISOU 4646  CA  LYS A 332    23053   8852  14346  -6055   4887   2973
ATOM   4647  C   LYS A 332      76.925  -1.365  20.917  1.00122.61           C  
ANISOU 4647  C   LYS A 332    22923   9234  14430  -6112   4715   3330
ATOM   4648  O   LYS A 332      77.457  -0.723  20.011  1.00123.76           O  
ANISOU 4648  O   LYS A 332    22946   9209  14868  -5662   4788   3735
ATOM   4649  CB  LYS A 332      77.153  -0.784  23.352  1.00126.56           C  
ANISOU 4649  CB  LYS A 332    24484   8776  14827  -6481   5279   2788
ATOM   4650  CG  LYS A 332      76.824   0.242  24.443  1.00127.41           C  
ANISOU 4650  CG  LYS A 332    24991   8389  15029  -6319   5598   2525
ATOM   4651  CD  LYS A 332      77.638   0.013  25.728  1.00133.39           C  
ANISOU 4651  CD  LYS A 332    26659   8387  15637  -6759   6039   2354
ATOM   4652  CE  LYS A 332      77.187   0.901  26.896  1.00133.52           C  
ANISOU 4652  CE  LYS A 332    27093   7996  15643  -6704   6324   2021
ATOM   4653  NZ  LYS A 332      77.460   2.325  26.642  1.00133.45           N1+
ANISOU 4653  NZ  LYS A 332    27145   7453  16105  -5965   6733   2236
ATOM   4654  HG3 LYS A 332      75.761   0.200  24.671  1.00127.41           H  
ATOM   4655  HG2 LYS A 332      77.008   1.246  24.062  1.00127.41           H  
ATOM   4656  HD3 LYS A 332      78.700   0.163  25.529  1.00133.39           H  
ATOM   4657  HD2 LYS A 332      77.531  -1.028  26.030  1.00133.39           H  
ATOM   4658  HE3 LYS A 332      77.712   0.608  27.806  1.00133.52           H  
ATOM   4659  HE2 LYS A 332      76.121   0.767  27.087  1.00133.52           H  
ATOM   4660  HZ1 LYS A 332      76.954   2.622  25.819  1.00133.45           H  
ATOM   4661  HZ2 LYS A 332      77.159   2.874  27.435  1.00133.45           H  
ATOM   4662  HZ3 LYS A 332      78.450   2.460  26.497  1.00133.45           H  
ATOM   4663  H   LYS A 332      74.756  -1.521  23.268  1.00117.28           H  
ATOM   4664  HA  LYS A 332      76.228   0.438  21.827  1.00121.73           H  
ATOM   4665  HB3 LYS A 332      78.206  -0.672  23.092  1.00126.56           H  
ATOM   4666  HB2 LYS A 332      77.049  -1.794  23.748  1.00126.56           H  
ATOM   4667  N   VAL A 333      76.842  -2.706  20.916  1.00122.45           N  
ANISOU 4667  N   VAL A 333    22819   9650  14058  -6671   4484   3199
ATOM   4668  CA  VAL A 333      77.385  -3.540  19.850  1.00123.28           C  
ANISOU 4668  CA  VAL A 333    22724  10042  14073  -6806   4330   3506
ATOM   4669  C   VAL A 333      76.509  -3.510  18.584  1.00119.48           C  
ANISOU 4669  C   VAL A 333    21557  10163  13676  -6401   4002   3703
ATOM   4670  O   VAL A 333      77.078  -3.595  17.502  1.00120.94           O  
ANISOU 4670  O   VAL A 333    21648  10327  13975  -6191   3984   4103
ATOM   4671  CB  VAL A 333      77.618  -4.987  20.356  1.00124.58           C  
ANISOU 4671  CB  VAL A 333    22978  10512  13843  -7542   4205   3323
ATOM   4672  CG1 VAL A 333      76.377  -5.678  20.942  1.00121.01           C  
ANISOU 4672  CG1 VAL A 333    22221  10602  13156  -7824   3945   2915
ATOM   4673  CG2 VAL A 333      78.281  -5.867  19.283  1.00125.13           C  
ANISOU 4673  CG2 VAL A 333    22746  10997  13802  -7650   4020   3619
ATOM   4674  HB  VAL A 333      78.340  -4.910  21.171  1.00124.58           H  
ATOM   4675 HG11 VAL A 333      76.619  -6.686  21.276  1.00121.01           H  
ATOM   4676 HG12 VAL A 333      75.993  -5.142  21.809  1.00121.01           H  
ATOM   4677 HG13 VAL A 333      75.575  -5.756  20.208  1.00121.01           H  
ATOM   4678 HG21 VAL A 333      78.697  -6.756  19.742  1.00125.13           H  
ATOM   4679 HG22 VAL A 333      77.574  -6.185  18.515  1.00125.13           H  
ATOM   4680 HG23 VAL A 333      79.106  -5.349  18.795  1.00125.13           H  
ATOM   4681  H   VAL A 333      76.373  -3.166  21.684  1.00122.45           H  
ATOM   4682  HA  VAL A 333      78.361  -3.135  19.575  1.00123.28           H  
ATOM   4683  N   LEU A 334      75.176  -3.327  18.682  1.00114.87           N  
ANISOU 4683  N   LEU A 334    20529  10086  13032  -6296   3751   3435
ATOM   4684  CA  LEU A 334      74.288  -3.153  17.522  1.00111.33           C  
ANISOU 4684  CA  LEU A 334    19479  10176  12646  -5928   3457   3570
ATOM   4685  C   LEU A 334      74.673  -1.923  16.683  1.00112.53           C  
ANISOU 4685  C   LEU A 334    19609   9997  13149  -5382   3556   3985
ATOM   4686  O   LEU A 334      74.704  -2.015  15.459  1.00112.96           O  
ANISOU 4686  O   LEU A 334    19377  10340  13204  -5248   3370   4299
ATOM   4687  CB  LEU A 334      72.805  -3.047  17.960  1.00106.51           C  
ANISOU 4687  CB  LEU A 334    18500   9969  12000  -5809   3265   3221
ATOM   4688  CG  LEU A 334      72.149  -4.365  18.426  1.00104.91           C  
ANISOU 4688  CG  LEU A 334    18093  10299  11469  -6268   3064   2880
ATOM   4689  CD1 LEU A 334      70.809  -4.094  19.130  1.00101.15           C  
ANISOU 4689  CD1 LEU A 334    17377  10037  11018  -6105   2951   2563
ATOM   4690  CD2 LEU A 334      71.927  -5.358  17.277  1.00104.91           C  
ANISOU 4690  CD2 LEU A 334    17677  10917  11266  -6412   2824   2987
ATOM   4691  H   LEU A 334      74.762  -3.265  19.602  1.00114.87           H  
ATOM   4692  HA  LEU A 334      74.410  -4.022  16.874  1.00111.33           H  
ATOM   4693  HB3 LEU A 334      72.203  -2.647  17.140  1.00106.51           H  
ATOM   4694  HB2 LEU A 334      72.731  -2.307  18.757  1.00106.51           H  
ATOM   4695  HG  LEU A 334      72.810  -4.849  19.142  1.00104.91           H  
ATOM   4696 HD11 LEU A 334      70.354  -5.020  19.477  1.00101.15           H  
ATOM   4697 HD12 LEU A 334      70.938  -3.456  20.004  1.00101.15           H  
ATOM   4698 HD13 LEU A 334      70.100  -3.604  18.462  1.00101.15           H  
ATOM   4699 HD21 LEU A 334      71.469  -6.279  17.639  1.00104.91           H  
ATOM   4700 HD22 LEU A 334      71.267  -4.937  16.518  1.00104.91           H  
ATOM   4701 HD23 LEU A 334      72.865  -5.634  16.804  1.00104.91           H  
ATOM   4702  N   THR A 335      75.034  -0.807  17.341  1.00113.66           N  
ANISOU 4702  N   THR A 335    20065   9536  13584  -5086   3858   4004
ATOM   4703  CA  THR A 335      75.438   0.450  16.708  1.00115.48           C  
ANISOU 4703  CA  THR A 335    20261   9405  14212  -4537   3996   4434
ATOM   4704  C   THR A 335      76.781   0.304  15.961  1.00119.92           C  
ANISOU 4704  C   THR A 335    21042   9684  14837  -4567   4107   4895
ATOM   4705  O   THR A 335      76.915   0.829  14.855  1.00120.70           O  
ANISOU 4705  O   THR A 335    20860   9881  15118  -4232   3980   5334
ATOM   4706  CB  THR A 335      75.537   1.549  17.800  1.00116.74           C  
ANISOU 4706  CB  THR A 335    20775   8903  14677  -4239   4390   4352
ATOM   4707  OG1 THR A 335      74.278   1.706  18.426  1.00114.02           O  
ANISOU 4707  OG1 THR A 335    20348   8777  14197  -4338   4314   3879
ATOM   4708  CG2 THR A 335      75.909   2.942  17.258  1.00117.59           C  
ANISOU 4708  CG2 THR A 335    20631   8817  15232  -3598   4459   4776
ATOM   4709  H   THR A 335      75.011  -0.828  18.351  1.00113.66           H  
ATOM   4710  HA  THR A 335      74.670   0.732  15.983  1.00115.48           H  
ATOM   4711  HB  THR A 335      76.259   1.261  18.565  1.00116.74           H  
ATOM   4712  HG1 THR A 335      74.079   0.919  18.915  1.00114.02           H  
ATOM   4713 HG21 THR A 335      75.881   3.689  18.051  1.00117.59           H  
ATOM   4714 HG22 THR A 335      76.916   2.959  16.843  1.00117.59           H  
ATOM   4715 HG23 THR A 335      75.218   3.262  16.476  1.00117.59           H  
ATOM   4716  N   GLU A 336      77.756  -0.424  16.540  1.00123.19           N  
ANISOU 4716  N   GLU A 336    21965   9754  15089  -4992   4331   4812
ATOM   4717  CA  GLU A 336      79.093  -0.614  15.972  1.00127.96           C  
ANISOU 4717  CA  GLU A 336    22835  10042  15740  -5054   4466   5240
ATOM   4718  C   GLU A 336      79.137  -1.746  14.923  1.00127.22           C  
ANISOU 4718  C   GLU A 336    22409  10596  15332  -5352   4104   5366
ATOM   4719  O   GLU A 336      79.941  -1.681  13.994  1.00130.03           O  
ANISOU 4719  O   GLU A 336    22720  10920  15765  -5220   4059   5835
ATOM   4720  CB  GLU A 336      80.071  -0.905  17.132  1.00132.17           C  
ANISOU 4720  CB  GLU A 336    24095   9901  16224  -5411   4877   5113
ATOM   4721  CG  GLU A 336      81.551  -1.005  16.694  1.00137.90           C  
ANISOU 4721  CG  GLU A 336    25185  10089  17122  -5337   5133   5607
ATOM   4722  CD  GLU A 336      82.575  -0.759  17.810  1.00143.09           C  
ANISOU 4722  CD  GLU A 336    26622   9847  17897  -5454   5672   5530
ATOM   4723  OE1 GLU A 336      82.234  -0.063  18.791  1.00141.99           O  
ANISOU 4723  OE1 GLU A 336    26708   9356  17885  -5309   5921   5244
ATOM   4724  OE2 GLU A 336      83.708  -1.262  17.645  1.00147.08           O1-
ANISOU 4724  OE2 GLU A 336    27546   9978  18359  -5698   5865   5758
ATOM   4725  HB2 GLU A 336      79.947  -0.105  17.863  1.00132.17           H  
ATOM   4726  HG3 GLU A 336      81.754  -0.260  15.923  1.00137.90           H  
ATOM   4727  HG2 GLU A 336      81.744  -1.978  16.242  1.00137.90           H  
ATOM   4728  H   GLU A 336      77.574  -0.837  17.444  1.00123.19           H  
ATOM   4729  HA  GLU A 336      79.404   0.312  15.486  1.00127.96           H  
ATOM   4730  HB3 GLU A 336      79.784  -1.823  17.649  1.00132.17           H  
ATOM   4731  N   ARG A 337      78.245  -2.747  15.029  1.00123.82           N  
ANISOU 4731  N   ARG A 337    21745  10748  14551  -5743   3861   4968
ATOM   4732  CA  ARG A 337      78.043  -3.827  14.056  1.00122.73           C  
ANISOU 4732  CA  ARG A 337    21278  11258  14094  -6034   3556   5029
ATOM   4733  C   ARG A 337      77.213  -3.348  12.838  1.00119.84           C  
ANISOU 4733  C   ARG A 337    20360  11394  13780  -5649   3238   5223
ATOM   4734  O   ARG A 337      77.129  -4.063  11.840  1.00119.72           O  
ANISOU 4734  O   ARG A 337    20090  11872  13526  -5801   3004   5355
ATOM   4735  NH1 ARG A 337      80.975  -7.403  12.239  1.00131.64           N  
ANISOU 4735  NH1 ARG A 337    22881  12745  14392  -7411   3542   5747
ATOM   4736  NH2 ARG A 337      79.741  -7.798  10.324  1.00129.56           N1+
ANISOU 4736  NH2 ARG A 337    21829  13559  13839  -7249   3044   5885
ATOM   4737  CB  ARG A 337      77.325  -4.990  14.792  1.00120.72           C  
ANISOU 4737  CB  ARG A 337    20950  11426  13492  -6562   3453   4561
ATOM   4738  CG  ARG A 337      77.162  -6.315  14.023  1.00119.92           C  
ANISOU 4738  CG  ARG A 337    20549  11966  13051  -6918   3221   4581
ATOM   4739  CD  ARG A 337      78.495  -7.031  13.731  1.00125.56           C  
ANISOU 4739  CD  ARG A 337    21606  12445  13656  -7240   3358   4877
ATOM   4740  NE  ARG A 337      78.632  -7.340  12.300  1.00125.94           N  
ANISOU 4740  NE  ARG A 337    21378  12902  13569  -7187   3164   5202
ATOM   4741  CZ  ARG A 337      79.784  -7.511  11.630  1.00128.81           C  
ANISOU 4741  CZ  ARG A 337    21990  13044  13909  -7279   3247   5610
ATOM   4742  H   ARG A 337      77.635  -2.747  15.836  1.00123.82           H  
ATOM   4743  HA  ARG A 337      79.016  -4.163  13.697  1.00122.73           H  
ATOM   4744  HB3 ARG A 337      76.337  -4.653  15.113  1.00120.72           H  
ATOM   4745  HB2 ARG A 337      77.874  -5.217  15.707  1.00120.72           H  
ATOM   4746  HG3 ARG A 337      76.582  -6.169  13.112  1.00119.92           H  
ATOM   4747  HG2 ARG A 337      76.551  -6.979  14.635  1.00119.92           H  
ATOM   4748  HD3 ARG A 337      78.556  -7.961  14.297  1.00125.56           H  
ATOM   4749  HD2 ARG A 337      79.336  -6.420  14.055  1.00125.56           H  
ATOM   4750  HE  ARG A 337      77.764  -7.464  11.799  1.00125.94           H  
ATOM   4751 HH12 ARG A 337      81.833  -7.533  11.723  1.00131.64           H  
ATOM   4752 HH11 ARG A 337      81.020  -7.185  13.223  1.00131.64           H  
ATOM   4753 HH22 ARG A 337      80.594  -7.932   9.801  1.00129.56           H  
ATOM   4754 HH21 ARG A 337      78.854  -7.887   9.849  1.00129.56           H  
ATOM   4755  N   GLY A 338      76.645  -2.130  12.895  1.00117.84           N  
ANISOU 4755  N   GLY A 338    19950  10994  13828  -5170   3245   5248
ATOM   4756  CA  GLY A 338      75.928  -1.469  11.805  1.00115.90           C  
ANISOU 4756  CA  GLY A 338    19222  11151  13664  -4808   2951   5471
ATOM   4757  C   GLY A 338      74.453  -1.869  11.683  1.00110.87           C  
ANISOU 4757  C   GLY A 338    18155  11151  12820  -4859   2676   5078
ATOM   4758  O   GLY A 338      73.860  -1.679  10.620  1.00109.14           O  
ANISOU 4758  O   GLY A 338    17554  11383  12532  -4715   2394   5204
ATOM   4759  H   GLY A 338      76.763  -1.598  13.747  1.00117.84           H  
ATOM   4760  HA3 GLY A 338      76.435  -1.653  10.857  1.00115.90           H  
ATOM   4761  HA2 GLY A 338      75.973  -0.394  11.978  1.00115.90           H  
ATOM   4762  N   ILE A 339      73.876  -2.442  12.748  1.00108.68           N  
ANISOU 4762  N   ILE A 339    17958  10899  12437  -5078   2759   4612
ATOM   4763  CA  ILE A 339      72.506  -2.936  12.814  1.00104.48           C  
ANISOU 4763  CA  ILE A 339    17043  10932  11724  -5135   2537   4233
ATOM   4764  C   ILE A 339      71.650  -1.836  13.462  1.00101.69           C  
ANISOU 4764  C   ILE A 339    16562  10453  11620  -4760   2555   4043
ATOM   4765  O   ILE A 339      71.906  -1.408  14.588  1.00102.09           O  
ANISOU 4765  O   ILE A 339    16916  10037  11837  -4713   2797   3903
ATOM   4766  CB  ILE A 339      72.462  -4.238  13.668  1.00103.94           C  
ANISOU 4766  CB  ILE A 339    17044  11098  11350  -5642   2557   3882
ATOM   4767  CG1 ILE A 339      73.520  -5.261  13.173  1.00108.10           C  
ANISOU 4767  CG1 ILE A 339    17753  11647  11672  -6009   2599   4108
ATOM   4768  CG2 ILE A 339      71.037  -4.835  13.667  1.00100.24           C  
ANISOU 4768  CG2 ILE A 339    16126  11271  10690  -5684   2326   3573
ATOM   4769  CD1 ILE A 339      73.499  -6.641  13.850  1.00108.92           C  
ANISOU 4769  CD1 ILE A 339    17928  11960  11496  -6554   2637   3834
ATOM   4770  H   ILE A 339      74.421  -2.515  13.598  1.00108.68           H  
ATOM   4771  HA  ILE A 339      72.136  -3.157  11.810  1.00104.48           H  
ATOM   4772  HB  ILE A 339      72.718  -3.994  14.700  1.00103.94           H  
ATOM   4773 HG13 ILE A 339      74.516  -4.852  13.331  1.00108.10           H  
ATOM   4774 HG12 ILE A 339      73.429  -5.387  12.095  1.00108.10           H  
ATOM   4775 HG21 ILE A 339      70.968  -5.736  14.274  1.00100.24           H  
ATOM   4776 HG22 ILE A 339      70.309  -4.139  14.079  1.00100.24           H  
ATOM   4777 HG23 ILE A 339      70.710  -5.087  12.659  1.00100.24           H  
ATOM   4778 HD11 ILE A 339      74.297  -7.269  13.456  1.00108.92           H  
ATOM   4779 HD12 ILE A 339      73.652  -6.560  14.924  1.00108.92           H  
ATOM   4780 HD13 ILE A 339      72.566  -7.175  13.673  1.00108.92           H  
ATOM   4781  N   ASN A 340      70.617  -1.398  12.731  1.00 98.85           N  
ANISOU 4781  N   ASN A 340    15784  10506  11269  -4518   2308   4043
ATOM   4782  CA  ASN A 340      69.654  -0.382  13.153  1.00 96.36           C  
ANISOU 4782  CA  ASN A 340    15290  10147  11174  -4168   2288   3893
ATOM   4783  C   ASN A 340      68.607  -1.008  14.089  1.00 93.23           C  
ANISOU 4783  C   ASN A 340    14794  10024  10605  -4352   2246   3404
ATOM   4784  O   ASN A 340      68.437  -2.225  14.118  1.00 92.70           O  
ANISOU 4784  O   ASN A 340    14651  10327  10243  -4703   2158   3224
ATOM   4785  CB  ASN A 340      68.950   0.184  11.901  1.00 95.27           C  
ANISOU 4785  CB  ASN A 340    14756  10351  11093  -3887   2022   4107
ATOM   4786  CG  ASN A 340      69.936   0.877  10.955  1.00 99.15           C  
ANISOU 4786  CG  ASN A 340    15285  10653  11736  -3725   1999   4651
ATOM   4787  OD1 ASN A 340      70.464   1.939  11.276  1.00 98.93           O  
ANISOU 4787  OD1 ASN A 340    15150  10955  11485  -3885   1804   4858
ATOM   4788  ND2 ASN A 340      70.208   0.266   9.800  1.00101.83           N  
ANISOU 4788  ND2 ASN A 340    15778  10453  12458  -3402   2213   4907
ATOM   4789  H   ASN A 340      70.469  -1.817  11.823  1.00 98.85           H  
ATOM   4790  HA  ASN A 340      70.171   0.420  13.684  1.00 96.36           H  
ATOM   4791  HB3 ASN A 340      68.196   0.915  12.192  1.00 95.27           H  
ATOM   4792  HB2 ASN A 340      68.421  -0.608  11.366  1.00 95.27           H  
ATOM   4793 HD22 ASN A 340      70.860   0.688   9.158  1.00101.83           H  
ATOM   4794 HD21 ASN A 340      69.774  -0.620   9.580  1.00101.83           H  
ATOM   4795  N   LEU A 341      67.931  -0.169  14.882  1.00 91.08           N  
ANISOU 4795  N   LEU A 341    14504   9578  10524  -4107   2314   3216
ATOM   4796  CA  LEU A 341      67.050  -0.592  15.964  1.00 88.72           C  
ANISOU 4796  CA  LEU A 341    14161   9462  10087  -4274   2293   2788
ATOM   4797  C   LEU A 341      65.923   0.423  16.128  1.00 85.98           C  
ANISOU 4797  C   LEU A 341    13613   9133   9923  -3927   2250   2636
ATOM   4798  O   LEU A 341      66.195   1.544  16.550  1.00 86.96           O  
ANISOU 4798  O   LEU A 341    13910   8810  10321  -3652   2436   2721
ATOM   4799  CB  LEU A 341      67.901  -0.811  17.237  1.00 90.91           C  
ANISOU 4799  CB  LEU A 341    14895   9327  10320  -4567   2536   2647
ATOM   4800  CG  LEU A 341      67.135  -1.044  18.557  1.00 90.04           C  
ANISOU 4800  CG  LEU A 341    14859   9216  10137  -4696   2566   2260
ATOM   4801  CD1 LEU A 341      66.381  -2.380  18.572  1.00 89.10           C  
ANISOU 4801  CD1 LEU A 341    14457   9673   9725  -5031   2348   2028
ATOM   4802  CD2 LEU A 341      68.105  -0.966  19.739  1.00 94.11           C  
ANISOU 4802  CD2 LEU A 341    15942   9150  10667  -4912   2860   2204
ATOM   4803  H   LEU A 341      68.108   0.821  14.801  1.00 91.08           H  
ATOM   4804  HA  LEU A 341      66.599  -1.547  15.706  1.00 88.72           H  
ATOM   4805  HB3 LEU A 341      68.537   0.066  17.370  1.00 90.91           H  
ATOM   4806  HB2 LEU A 341      68.588  -1.642  17.073  1.00 90.91           H  
ATOM   4807  HG  LEU A 341      66.406  -0.247  18.708  1.00 90.04           H  
ATOM   4808 HD11 LEU A 341      65.910  -2.537  19.541  1.00 89.10           H  
ATOM   4809 HD12 LEU A 341      65.603  -2.415  17.810  1.00 89.10           H  
ATOM   4810 HD13 LEU A 341      67.063  -3.212  18.408  1.00 89.10           H  
ATOM   4811 HD21 LEU A 341      67.581  -1.098  20.683  1.00 94.11           H  
ATOM   4812 HD22 LEU A 341      68.873  -1.738  19.680  1.00 94.11           H  
ATOM   4813 HD23 LEU A 341      68.607  -0.000  19.782  1.00 94.11           H  
ATOM   4814  N   THR A 342      64.670   0.026  15.854  1.00 82.82           N  
ANISOU 4814  N   THR A 342    12860   9232   9377  -3938   2034   2413
ATOM   4815  CA  THR A 342      63.490   0.836  16.157  1.00 79.99           C  
ANISOU 4815  CA  THR A 342    12323   8916   9152  -3666   1990   2224
ATOM   4816  C   THR A 342      63.030   0.424  17.571  1.00 78.72           C  
ANISOU 4816  C   THR A 342    12308   8704   8896  -3856   2068   1880
ATOM   4817  O   THR A 342      62.857  -0.770  17.833  1.00 78.20           O  
ANISOU 4817  O   THR A 342    12146   8977   8589  -4160   1969   1698
ATOM   4818  CB  THR A 342      62.381   0.636  15.093  1.00 77.89           C  
ANISOU 4818  CB  THR A 342    11630   9173   8791  -3557   1734   2168
ATOM   4819  OG1 THR A 342      61.722  -0.608  15.148  1.00 77.45           O  
ANISOU 4819  OG1 THR A 342    11433   9536   8460  -3837   1643   1918
ATOM   4820  CG2 THR A 342      62.882   0.885  13.663  1.00 79.38           C  
ANISOU 4820  CG2 THR A 342    11705   9474   8983  -3479   1614   2515
ATOM   4821  H   THR A 342      64.514  -0.918  15.524  1.00 82.82           H  
ATOM   4822  HA  THR A 342      63.773   1.885  16.097  1.00 79.99           H  
ATOM   4823  HB  THR A 342      61.594   1.367  15.289  1.00 77.89           H  
ATOM   4824  HG1 THR A 342      61.218  -0.648  15.948  1.00 77.45           H  
ATOM   4825 HG21 THR A 342      62.676   1.911  13.355  1.00 79.38           H  
ATOM   4826 HG22 THR A 342      63.953   0.731  13.542  1.00 79.38           H  
ATOM   4827 HG23 THR A 342      62.397   0.206  12.965  1.00 79.38           H  
ATOM   4828  N   PRO A 343      62.871   1.388  18.500  1.00 78.67           N  
ANISOU 4828  N   PRO A 343    12528   8285   9079  -3684   2248   1810
ATOM   4829  CA  PRO A 343      62.634   1.112  19.918  1.00 78.67           C  
ANISOU 4829  CA  PRO A 343    12766   8149   8975  -3891   2342   1515
ATOM   4830  C   PRO A 343      61.175   0.738  20.187  1.00 75.76           C  
ANISOU 4830  C   PRO A 343    12098   8186   8502  -3883   2153   1239
ATOM   4831  O   PRO A 343      60.266   1.210  19.501  1.00 73.22           O  
ANISOU 4831  O   PRO A 343    11482   8033   8307  -3568   2051   1235
ATOM   4832  CB  PRO A 343      62.982   2.429  20.623  1.00 79.76           C  
ANISOU 4832  CB  PRO A 343    13245   7690   9372  -3639   2631   1577
ATOM   4833  CG  PRO A 343      62.634   3.487  19.590  1.00 78.75           C  
ANISOU 4833  CG  PRO A 343    12833   7571   9518  -3200   2592   1828
ATOM   4834  CD  PRO A 343      62.977   2.828  18.262  1.00 79.32           C  
ANISOU 4834  CD  PRO A 343    12657   7989   9491  -3279   2389   2042
ATOM   4835  HA  PRO A 343      63.297   0.317  20.268  1.00 78.67           H  
ATOM   4836  HB3 PRO A 343      64.051   2.449  20.836  1.00 79.76           H  
ATOM   4837  HB2 PRO A 343      62.457   2.578  21.568  1.00 79.76           H  
ATOM   4838  HG3 PRO A 343      63.158   4.427  19.727  1.00 78.75           H  
ATOM   4839  HG2 PRO A 343      61.565   3.701  19.627  1.00 78.75           H  
ATOM   4840  HD2 PRO A 343      62.316   3.169  17.464  1.00 79.32           H  
ATOM   4841  HD3 PRO A 343      64.006   3.068  17.997  1.00 79.32           H  
ATOM   4842  N   ASP A 344      60.993  -0.088  21.225  1.00 76.49           N  
ANISOU 4842  N   ASP A 344    12272   8422   8369  -4245   2105   1030
ATOM   4843  CA  ASP A 344      59.742  -0.562  21.816  1.00 74.38           C  
ANISOU 4843  CA  ASP A 344    11722   8544   7997  -4271   1926    801
ATOM   4844  C   ASP A 344      58.634   0.501  21.883  1.00 71.78           C  
ANISOU 4844  C   ASP A 344    11283   8131   7861  -3870   1934    734
ATOM   4845  O   ASP A 344      57.615   0.345  21.216  1.00 69.71           O  
ANISOU 4845  O   ASP A 344    10649   8188   7650  -3644   1790    732
ATOM   4846  CB  ASP A 344      60.016  -1.283  23.160  1.00 76.06           C  
ANISOU 4846  CB  ASP A 344    12151   8754   7995  -4691   1914    622
ATOM   4847  CG  ASP A 344      60.744  -0.500  24.269  1.00 78.90           C  
ANISOU 4847  CG  ASP A 344    13089   8519   8371  -4815   2163    594
ATOM   4848  OD1 ASP A 344      61.308   0.580  23.988  1.00 80.68           O  
ANISOU 4848  OD1 ASP A 344    13529   8314   8812  -4533   2380    728
ATOM   4849  OD2 ASP A 344      60.720  -1.011  25.409  1.00 79.81           O1-
ANISOU 4849  OD2 ASP A 344    13452   8595   8278  -5207   2152    449
ATOM   4850  HA  ASP A 344      59.372  -1.325  21.134  1.00 74.38           H  
ATOM   4851  HB3 ASP A 344      60.611  -2.175  22.970  1.00 76.06           H  
ATOM   4852  HB2 ASP A 344      59.067  -1.633  23.562  1.00 76.06           H  
ATOM   4853  H   ASP A 344      61.832  -0.421  21.686  1.00 76.49           H  
ATOM   4854  N   ILE A 345      58.865   1.589  22.636  1.00 72.51           N  
ANISOU 4854  N   ILE A 345    11725   7771   8054  -3797   2130    684
ATOM   4855  CA  ILE A 345      57.985   2.745  22.845  1.00 70.69           C  
ANISOU 4855  CA  ILE A 345    11438   7408   8012  -3439   2182    619
ATOM   4856  C   ILE A 345      57.361   3.368  21.579  1.00 68.09           C  
ANISOU 4856  C   ILE A 345    10704   7299   7869  -3069   2063    743
ATOM   4857  O   ILE A 345      56.250   3.882  21.673  1.00 65.82           O  
ANISOU 4857  O   ILE A 345    10190   7194   7625  -2887   1964    624
ATOM   4858  CB  ILE A 345      58.688   3.761  23.800  1.00 72.80           C  
ANISOU 4858  CB  ILE A 345    12184   7051   8428  -3348   2511    645
ATOM   4859  CG1 ILE A 345      58.545   3.256  25.256  1.00 74.57           C  
ANISOU 4859  CG1 ILE A 345    12731   7158   8445  -3629   2563    392
ATOM   4860  CG2 ILE A 345      58.223   5.231  23.662  1.00 71.34           C  
ANISOU 4860  CG2 ILE A 345    11883   6668   8556  -2881   2628    751
ATOM   4861  CD1 ILE A 345      59.176   4.159  26.318  1.00 78.46           C  
ANISOU 4861  CD1 ILE A 345    13774   7016   9020  -3597   2933    369
ATOM   4862  H   ILE A 345      59.748   1.602  23.133  1.00 72.51           H  
ATOM   4863  HA  ILE A 345      57.119   2.343  23.373  1.00 70.69           H  
ATOM   4864  HB  ILE A 345      59.752   3.767  23.555  1.00 72.80           H  
ATOM   4865 HG13 ILE A 345      59.003   2.268  25.334  1.00 74.57           H  
ATOM   4866 HG12 ILE A 345      57.493   3.119  25.504  1.00 74.57           H  
ATOM   4867 HG21 ILE A 345      58.776   5.898  24.323  1.00 71.34           H  
ATOM   4868 HG22 ILE A 345      58.385   5.616  22.656  1.00 71.34           H  
ATOM   4869 HG23 ILE A 345      57.167   5.336  23.897  1.00 71.34           H  
ATOM   4870 HD11 ILE A 345      59.231   3.651  27.281  1.00 78.46           H  
ATOM   4871 HD12 ILE A 345      60.185   4.423  26.017  1.00 78.46           H  
ATOM   4872 HD13 ILE A 345      58.606   5.076  26.465  1.00 78.46           H  
ATOM   4873  N   LEU A 346      58.035   3.318  20.417  1.00 68.92           N  
ANISOU 4873  N   LEU A 346    10736   7390   8061  -2990   2062    988
ATOM   4874  CA  LEU A 346      57.471   3.742  19.134  1.00 67.23           C  
ANISOU 4874  CA  LEU A 346    10155   7429   7960  -2730   1906   1121
ATOM   4875  C   LEU A 346      56.767   2.559  18.450  1.00 66.12           C  
ANISOU 4875  C   LEU A 346     9705   7824   7593  -2883   1676   1018
ATOM   4876  O   LEU A 346      55.656   2.718  17.947  1.00 64.25           O  
ANISOU 4876  O   LEU A 346     9206   7851   7356  -2742   1550    896
ATOM   4877  CB  LEU A 346      58.622   4.225  18.216  1.00 69.12           C  
ANISOU 4877  CB  LEU A 346    10435   7458   8368  -2600   1972   1465
ATOM   4878  CG  LEU A 346      58.206   4.703  16.801  1.00 67.66           C  
ANISOU 4878  CG  LEU A 346     9900   7531   8277  -2384   1783   1649
ATOM   4879  CD1 LEU A 346      57.237   5.899  16.838  1.00 66.50           C  
ANISOU 4879  CD1 LEU A 346     9610   7292   8367  -2065   1797   1627
ATOM   4880  CD2 LEU A 346      59.447   5.032  15.961  1.00 69.94           C  
ANISOU 4880  CD2 LEU A 346    10230   7669   8673  -2339   1805   2027
ATOM   4881  H   LEU A 346      58.943   2.875  20.408  1.00 68.92           H  
ATOM   4882  HA  LEU A 346      56.759   4.554  19.283  1.00 67.23           H  
ATOM   4883  HB3 LEU A 346      59.362   3.428  18.113  1.00 69.12           H  
ATOM   4884  HB2 LEU A 346      59.151   5.039  18.709  1.00 69.12           H  
ATOM   4885  HG  LEU A 346      57.702   3.888  16.282  1.00 67.66           H  
ATOM   4886 HD11 LEU A 346      57.021   6.258  15.831  1.00 66.50           H  
ATOM   4887 HD12 LEU A 346      56.281   5.629  17.288  1.00 66.50           H  
ATOM   4888 HD13 LEU A 346      57.647   6.733  17.406  1.00 66.50           H  
ATOM   4889 HD21 LEU A 346      59.172   5.302  14.942  1.00 69.94           H  
ATOM   4890 HD22 LEU A 346      60.003   5.865  16.389  1.00 69.94           H  
ATOM   4891 HD23 LEU A 346      60.121   4.177  15.902  1.00 69.94           H  
ATOM   4892  N   THR A 347      57.426   1.392  18.402  1.00 67.63           N  
ANISOU 4892  N   THR A 347     9945   8153   7597  -3172   1652   1067
ATOM   4893  CA  THR A 347      57.066   0.255  17.559  1.00 67.01           C  
ANISOU 4893  CA  THR A 347     9591   8559   7312  -3317   1494   1011
ATOM   4894  C   THR A 347      55.782  -0.461  18.032  1.00 65.25           C  
ANISOU 4894  C   THR A 347     9142   8661   6988  -3341   1404    749
ATOM   4895  O   THR A 347      55.008  -0.903  17.184  1.00 64.46           O  
ANISOU 4895  O   THR A 347     8766   8911   6815  -3275   1305    693
ATOM   4896  CB  THR A 347      58.275  -0.711  17.520  1.00 69.43           C  
ANISOU 4896  CB  THR A 347    10028   8911   7443  -3660   1530   1101
ATOM   4897  OG1 THR A 347      59.414  -0.046  17.013  1.00 71.59           O  
ANISOU 4897  OG1 THR A 347    10551   8818   7832  -3625   1640   1359
ATOM   4898  CG2 THR A 347      58.087  -1.948  16.625  1.00 69.77           C  
ANISOU 4898  CG2 THR A 347     9796   9423   7291  -3776   1415   1106
ATOM   4899  H   THR A 347      58.308   1.331  18.894  1.00 67.63           H  
ATOM   4900  HA  THR A 347      56.883   0.627  16.555  1.00 67.01           H  
ATOM   4901  HB  THR A 347      58.515  -1.003  18.539  1.00 69.43           H  
ATOM   4902  HG1 THR A 347      59.688   0.600  17.650  1.00 71.59           H  
ATOM   4903 HG21 THR A 347      59.010  -2.524  16.554  1.00 69.77           H  
ATOM   4904 HG22 THR A 347      57.331  -2.618  17.026  1.00 69.77           H  
ATOM   4905 HG23 THR A 347      57.789  -1.672  15.613  1.00 69.77           H  
ATOM   4906  N   ASN A 348      55.525  -0.533  19.352  1.00 65.15           N  
ANISOU 4906  N   ASN A 348     9264   8526   6965  -3441   1447    603
ATOM   4907  CA  ASN A 348      54.351  -1.188  19.946  1.00 63.92           C  
ANISOU 4907  CA  ASN A 348     8886   8685   6715  -3489   1350    408
ATOM   4908  C   ASN A 348      53.266  -0.201  20.423  1.00 62.25           C  
ANISOU 4908  C   ASN A 348     8645   8366   6642  -3216   1341    285
ATOM   4909  O   ASN A 348      52.355  -0.601  21.147  1.00 62.14           O  
ANISOU 4909  O   ASN A 348     8551   8489   6570  -3268   1282    145
ATOM   4910  CB  ASN A 348      54.773  -2.164  21.080  1.00 65.36           C  
ANISOU 4910  CB  ASN A 348     9190   8909   6735  -3869   1344    353
ATOM   4911  CG  ASN A 348      55.498  -1.582  22.308  1.00 66.59           C  
ANISOU 4911  CG  ASN A 348     9759   8623   6919  -3966   1454    320
ATOM   4912  OD1 ASN A 348      55.228  -0.468  22.753  1.00 66.31           O  
ANISOU 4912  OD1 ASN A 348     9883   8262   7050  -3704   1555    321
ATOM   4913  ND2 ASN A 348      56.443  -2.345  22.861  1.00 70.09           N  
ANISOU 4913  ND2 ASN A 348    10390   9049   7191  -4363   1450    291
ATOM   4914  H   ASN A 348      56.201  -0.131  19.991  1.00 65.15           H  
ATOM   4915  HA  ASN A 348      53.860  -1.800  19.187  1.00 63.92           H  
ATOM   4916  HB3 ASN A 348      55.426  -2.908  20.625  1.00 65.36           H  
ATOM   4917  HB2 ASN A 348      53.911  -2.722  21.445  1.00 65.36           H  
ATOM   4918 HD22 ASN A 348      56.951  -2.011  23.666  1.00 70.09           H  
ATOM   4919 HD21 ASN A 348      56.644  -3.257  22.472  1.00 70.09           H  
ATOM   4920  N   SER A 349      53.345   1.081  20.025  1.00 61.24           N  
ANISOU 4920  N   SER A 349     8564   8004   6699  -2933   1393    362
ATOM   4921  CA  SER A 349      52.416   2.134  20.445  1.00 59.66           C  
ANISOU 4921  CA  SER A 349     8386   7635   6647  -2691   1422    266
ATOM   4922  C   SER A 349      51.064   2.125  19.700  1.00 57.85           C  
ANISOU 4922  C   SER A 349     7843   7688   6450  -2477   1309    170
ATOM   4923  O   SER A 349      50.214   2.962  20.000  1.00 56.57           O  
ANISOU 4923  O   SER A 349     7675   7405   6414  -2267   1326     96
ATOM   4924  CB  SER A 349      53.110   3.500  20.283  1.00 60.14           C  
ANISOU 4924  CB  SER A 349     8649   7272   6929  -2490   1569    417
ATOM   4925  OG  SER A 349      53.263   3.904  18.940  1.00 60.08           O  
ANISOU 4925  OG  SER A 349     8483   7333   7012  -2354   1515    608
ATOM   4926  H   SER A 349      54.113   1.346  19.425  1.00 61.24           H  
ATOM   4927  HA  SER A 349      52.207   1.999  21.508  1.00 59.66           H  
ATOM   4928  HB3 SER A 349      54.087   3.472  20.752  1.00 60.14           H  
ATOM   4929  HB2 SER A 349      52.548   4.269  20.811  1.00 60.14           H  
ATOM   4930  HG  SER A 349      53.928   3.365  18.532  1.00 60.08           H  
ATOM   4931  N   GLY A 350      50.822   1.169  18.784  1.00 57.67           N  
ANISOU 4931  N   GLY A 350     7588   8016   6307  -2534   1221    168
ATOM   4932  CA  GLY A 350      49.543   0.982  18.094  1.00 56.00           C  
ANISOU 4932  CA  GLY A 350     7125   8049   6105  -2351   1151     67
ATOM   4933  C   GLY A 350      48.367   0.701  19.042  1.00 54.83           C  
ANISOU 4933  C   GLY A 350     6884   7987   5961  -2287   1133   -101
ATOM   4934  O   GLY A 350      47.257   1.164  18.787  1.00 53.11           O  
ANISOU 4934  O   GLY A 350     6581   7758   5839  -2066   1118   -182
ATOM   4935  H   GLY A 350      51.562   0.514  18.579  1.00 57.67           H  
ATOM   4936  HA3 GLY A 350      49.641   0.141  17.407  1.00 56.00           H  
ATOM   4937  HA2 GLY A 350      49.326   1.860  17.483  1.00 56.00           H  
ATOM   4938  N   GLY A 351      48.628   0.014  20.168  1.00 55.93           N  
ANISOU 4938  N   GLY A 351     7040   8220   5992  -2502   1121   -131
ATOM   4939  CA  GLY A 351      47.666  -0.270  21.230  1.00 55.71           C  
ANISOU 4939  CA  GLY A 351     6934   8276   5956  -2482   1074   -237
ATOM   4940  C   GLY A 351      47.123   0.982  21.921  1.00 54.35           C  
ANISOU 4940  C   GLY A 351     6920   7812   5917  -2287   1105   -291
ATOM   4941  O   GLY A 351      45.905   1.135  22.016  1.00 53.33           O  
ANISOU 4941  O   GLY A 351     6651   7760   5854  -2087   1076   -373
ATOM   4942  H   GLY A 351      49.570  -0.323  20.309  1.00 55.93           H  
ATOM   4943  HA3 GLY A 351      48.154  -0.889  21.983  1.00 55.71           H  
ATOM   4944  HA2 GLY A 351      46.840  -0.854  20.829  1.00 55.71           H  
ATOM   4945  N   VAL A 352      48.016   1.888  22.362  1.00 54.78           N  
ANISOU 4945  N   VAL A 352     7280   7513   6020  -2336   1193   -240
ATOM   4946  CA  VAL A 352      47.652   3.144  23.030  1.00 54.08           C  
ANISOU 4946  CA  VAL A 352     7368   7121   6059  -2161   1271   -284
ATOM   4947  C   VAL A 352      47.110   4.196  22.033  1.00 52.38           C  
ANISOU 4947  C   VAL A 352     7026   6844   6032  -1860   1293   -253
ATOM   4948  O   VAL A 352      46.403   5.115  22.442  1.00 51.14           O  
ANISOU 4948  O   VAL A 352     6867   6581   5983  -1672   1318   -313
ATOM   4949  CB  VAL A 352      48.855   3.699  23.851  1.00 55.57           C  
ANISOU 4949  CB  VAL A 352     7959   6895   6260  -2280   1429   -240
ATOM   4950  CG1 VAL A 352      49.430   2.646  24.815  1.00 57.94           C  
ANISOU 4950  CG1 VAL A 352     8440   7235   6339  -2654   1398   -269
ATOM   4951  CG2 VAL A 352      49.994   4.335  23.039  1.00 56.21           C  
ANISOU 4951  CG2 VAL A 352     8118   6756   6484  -2187   1543    -83
ATOM   4952  HB  VAL A 352      48.453   4.500  24.472  1.00 55.57           H  
ATOM   4953 HG11 VAL A 352      50.101   3.105  25.542  1.00 57.94           H  
ATOM   4954 HG12 VAL A 352      48.637   2.146  25.368  1.00 57.94           H  
ATOM   4955 HG13 VAL A 352      49.994   1.879  24.285  1.00 57.94           H  
ATOM   4956 HG21 VAL A 352      50.741   4.777  23.700  1.00 56.21           H  
ATOM   4957 HG22 VAL A 352      50.503   3.598  22.425  1.00 56.21           H  
ATOM   4958 HG23 VAL A 352      49.627   5.132  22.398  1.00 56.21           H  
ATOM   4959  H   VAL A 352      48.999   1.703  22.229  1.00 54.78           H  
ATOM   4960  HA  VAL A 352      46.859   2.917  23.742  1.00 54.08           H  
ATOM   4961  N   LEU A 353      47.399   4.042  20.728  1.00 52.60           N  
ANISOU 4961  N   LEU A 353     6955   6946   6083  -1845   1274   -146
ATOM   4962  CA  LEU A 353      46.887   4.877  19.643  1.00 51.63           C  
ANISOU 4962  CA  LEU A 353     6684   6840   6093  -1629   1243   -106
ATOM   4963  C   LEU A 353      45.414   4.547  19.323  1.00 50.34           C  
ANISOU 4963  C   LEU A 353     6324   6905   5898  -1518   1172   -264
ATOM   4964  O   LEU A 353      44.654   5.464  19.018  1.00 49.04           O  
ANISOU 4964  O   LEU A 353     6128   6646   5860  -1333   1180   -303
ATOM   4965  CB  LEU A 353      47.783   4.653  18.404  1.00 52.44           C  
ANISOU 4965  CB  LEU A 353     6711   7063   6150  -1702   1190     38
ATOM   4966  CG  LEU A 353      47.432   5.458  17.133  1.00 52.26           C  
ANISOU 4966  CG  LEU A 353     6550   7087   6219  -1559   1116    118
ATOM   4967  CD1 LEU A 353      47.403   6.975  17.374  1.00 49.51           C  
ANISOU 4967  CD1 LEU A 353     6243   6446   6122  -1356   1176    207
ATOM   4968  CD2 LEU A 353      48.423   5.123  16.013  1.00 53.73           C  
ANISOU 4968  CD2 LEU A 353     6714   7378   6323  -1682   1052    299
ATOM   4969  H   LEU A 353      48.006   3.276  20.469  1.00 52.60           H  
ATOM   4970  HA  LEU A 353      46.955   5.921  19.955  1.00 51.63           H  
ATOM   4971  HB3 LEU A 353      47.777   3.595  18.146  1.00 52.44           H  
ATOM   4972  HB2 LEU A 353      48.814   4.879  18.676  1.00 52.44           H  
ATOM   4973  HG  LEU A 353      46.447   5.145  16.790  1.00 52.26           H  
ATOM   4974 HD11 LEU A 353      47.197   7.517  16.451  1.00 49.51           H  
ATOM   4975 HD12 LEU A 353      46.628   7.255  18.085  1.00 49.51           H  
ATOM   4976 HD13 LEU A 353      48.357   7.334  17.760  1.00 49.51           H  
ATOM   4977 HD21 LEU A 353      48.095   5.534  15.059  1.00 53.73           H  
ATOM   4978 HD22 LEU A 353      49.414   5.525  16.228  1.00 53.73           H  
ATOM   4979 HD23 LEU A 353      48.530   4.047  15.892  1.00 53.73           H  
ATOM   4980  N   VAL A 354      44.983   3.277  19.446  1.00 51.07           N  
ANISOU 4980  N   VAL A 354     6281   7288   5835  -1626   1123   -342
ATOM   4981  CA  VAL A 354      43.572   2.881  19.332  1.00 50.33           C  
ANISOU 4981  CA  VAL A 354     6008   7380   5734  -1491   1098   -471
ATOM   4982  C   VAL A 354      42.822   3.105  20.661  1.00 50.14           C  
ANISOU 4982  C   VAL A 354     6033   7245   5772  -1402   1104   -541
ATOM   4983  O   VAL A 354      41.610   3.325  20.632  1.00 49.94           O  
ANISOU 4983  O   VAL A 354     5923   7233   5819  -1216   1105   -622
ATOM   4984  CB  VAL A 354      43.463   1.408  18.850  1.00 50.95           C  
ANISOU 4984  CB  VAL A 354     5897   7794   5668  -1587   1091   -508
ATOM   4985  CG1 VAL A 354      42.024   0.851  18.860  1.00 49.81           C  
ANISOU 4985  CG1 VAL A 354     5585   7795   5546  -1440   1103   -613
ATOM   4986  CG2 VAL A 354      44.012   1.283  17.420  1.00 51.14           C  
ANISOU 4986  CG2 VAL A 354     5876   7921   5634  -1589   1101   -492
ATOM   4987  HB  VAL A 354      44.069   0.778  19.503  1.00 50.95           H  
ATOM   4988 HG11 VAL A 354      41.966  -0.096  18.326  1.00 49.81           H  
ATOM   4989 HG12 VAL A 354      41.653   0.675  19.868  1.00 49.81           H  
ATOM   4990 HG13 VAL A 354      41.335   1.534  18.359  1.00 49.81           H  
ATOM   4991 HG21 VAL A 354      43.984   0.253  17.065  1.00 51.14           H  
ATOM   4992 HG22 VAL A 354      43.441   1.888  16.717  1.00 51.14           H  
ATOM   4993 HG23 VAL A 354      45.045   1.619  17.365  1.00 51.14           H  
ATOM   4994  H   VAL A 354      45.656   2.556  19.673  1.00 51.07           H  
ATOM   4995  HA  VAL A 354      43.083   3.508  18.589  1.00 50.33           H  
ATOM   4996  N   SER A 355      43.529   3.134  21.804  1.00 50.30           N  
ANISOU 4996  N   SER A 355     6222   7145   5745  -1554   1110   -510
ATOM   4997  CA  SER A 355      42.980   3.515  23.107  1.00 49.91           C  
ANISOU 4997  CA  SER A 355     6276   6983   5705  -1523   1106   -563
ATOM   4998  C   SER A 355      42.659   5.027  23.144  1.00 48.90           C  
ANISOU 4998  C   SER A 355     6260   6571   5749  -1304   1189   -580
ATOM   4999  O   SER A 355      41.652   5.425  23.727  1.00 48.12           O  
ANISOU 4999  O   SER A 355     6147   6439   5696  -1169   1185   -643
ATOM   5000  CB  SER A 355      44.014   3.137  24.187  1.00 51.27           C  
ANISOU 5000  CB  SER A 355     6685   7041   5753  -1789   1112   -530
ATOM   5001  OG  SER A 355      43.458   3.148  25.479  1.00 52.98           O  
ANISOU 5001  OG  SER A 355     6949   7298   5884  -1856   1045   -571
ATOM   5002  H   SER A 355      44.516   2.924  21.763  1.00 50.30           H  
ATOM   5003  HA  SER A 355      42.062   2.949  23.273  1.00 49.91           H  
ATOM   5004  HB3 SER A 355      44.855   3.825  24.175  1.00 51.27           H  
ATOM   5005  HB2 SER A 355      44.409   2.136  24.014  1.00 51.27           H  
ATOM   5006  HG  SER A 355      44.159   2.964  26.096  1.00 52.98           H  
ATOM   5007  N   TYR A 356      43.456   5.850  22.436  1.00 48.92           N  
ANISOU 5007  N   TYR A 356     6352   6378   5857  -1269   1264   -495
ATOM   5008  CA  TYR A 356      43.189   7.257  22.131  1.00 47.40           C  
ANISOU 5008  CA  TYR A 356     6217   5932   5861  -1074   1353   -458
ATOM   5009  C   TYR A 356      41.969   7.419  21.207  1.00 46.66           C  
ANISOU 5009  C   TYR A 356     5913   5981   5837   -909   1285   -513
ATOM   5010  O   TYR A 356      41.156   8.308  21.446  1.00 46.70           O  
ANISOU 5010  O   TYR A 356     5934   5861   5950   -761   1325   -556
ATOM   5011  CB  TYR A 356      44.441   7.881  21.468  1.00 47.56           C  
ANISOU 5011  CB  TYR A 356     6310   5768   5993  -1078   1429   -296
ATOM   5012  CG  TYR A 356      44.234   9.211  20.750  1.00 47.97           C  
ANISOU 5012  CG  TYR A 356     6278   5675   6273   -879   1470   -194
ATOM   5013  CD1 TYR A 356      43.799  10.351  21.456  1.00 47.40           C  
ANISOU 5013  CD1 TYR A 356     6308   5338   6363   -729   1608   -193
ATOM   5014  CD2 TYR A 356      44.425   9.296  19.356  1.00 48.43           C  
ANISOU 5014  CD2 TYR A 356     6154   5869   6376   -865   1368    -77
ATOM   5015  CE1 TYR A 356      43.563  11.563  20.783  1.00 44.46           C  
ANISOU 5015  CE1 TYR A 356     5815   4857   6222   -562   1643    -69
ATOM   5016  CE2 TYR A 356      44.197  10.510  18.680  1.00 46.55           C  
ANISOU 5016  CE2 TYR A 356     5808   5531   6349   -722   1369     55
ATOM   5017  CZ  TYR A 356      43.765  11.645  19.394  1.00 46.15           C  
ANISOU 5017  CZ  TYR A 356     5819   5232   6485   -567   1507     63
ATOM   5018  OH  TYR A 356      43.535  12.821  18.745  1.00 50.00           O  
ANISOU 5018  OH  TYR A 356     6155   5646   7199   -441   1505    221
ATOM   5019  HB2 TYR A 356      45.224   8.002  22.212  1.00 47.56           H  
ATOM   5020  HD1 TYR A 356      43.616  10.296  22.511  1.00 47.40           H  
ATOM   5021  HD2 TYR A 356      44.744   8.428  18.799  1.00 48.43           H  
ATOM   5022  HE1 TYR A 356      43.223  12.425  21.335  1.00 44.46           H  
ATOM   5023  HE2 TYR A 356      44.350  10.561  17.612  1.00 46.55           H  
ATOM   5024  HH  TYR A 356      43.711  12.774  17.817  1.00 50.00           H  
ATOM   5025  H   TYR A 356      44.284   5.447  22.017  1.00 48.92           H  
ATOM   5026  HA  TYR A 356      42.981   7.782  23.064  1.00 47.40           H  
ATOM   5027  HB3 TYR A 356      44.864   7.181  20.754  1.00 47.56           H  
ATOM   5028  N   TYR A 357      41.827   6.579  20.166  1.00 46.58           N  
ANISOU 5028  N   TYR A 357     5736   6216   5748   -952   1202   -519
ATOM   5029  CA  TYR A 357      40.714   6.650  19.214  1.00 45.77           C  
ANISOU 5029  CA  TYR A 357     5486   6237   5667   -837   1159   -597
ATOM   5030  C   TYR A 357      39.373   6.311  19.868  1.00 45.10           C  
ANISOU 5030  C   TYR A 357     5367   6191   5579   -725   1173   -726
ATOM   5031  O   TYR A 357      38.377   6.947  19.534  1.00 44.74           O  
ANISOU 5031  O   TYR A 357     5306   6062   5630   -585   1190   -779
ATOM   5032  CB  TYR A 357      40.939   5.682  18.039  1.00 46.56           C  
ANISOU 5032  CB  TYR A 357     5470   6598   5622   -937   1106   -613
ATOM   5033  CG  TYR A 357      42.107   5.978  17.116  1.00 48.19           C  
ANISOU 5033  CG  TYR A 357     5697   6801   5813  -1051   1063   -463
ATOM   5034  CD1 TYR A 357      42.653   7.276  16.991  1.00 47.04           C  
ANISOU 5034  CD1 TYR A 357     5600   6438   5836  -1000   1060   -309
ATOM   5035  CD2 TYR A 357      42.643   4.925  16.352  1.00 47.80           C  
ANISOU 5035  CD2 TYR A 357     5599   6975   5589  -1203   1034   -448
ATOM   5036  CE1 TYR A 357      43.741   7.503  16.132  1.00 47.75           C  
ANISOU 5036  CE1 TYR A 357     5681   6535   5926  -1091   1005   -120
ATOM   5037  CE2 TYR A 357      43.736   5.148  15.499  1.00 49.06           C  
ANISOU 5037  CE2 TYR A 357     5784   7141   5717  -1317    978   -283
ATOM   5038  CZ  TYR A 357      44.285   6.436  15.397  1.00 49.11           C  
ANISOU 5038  CZ  TYR A 357     5829   6932   5899  -1257    951   -109
ATOM   5039  OH  TYR A 357      45.356   6.652  14.593  1.00 50.40           O  
ANISOU 5039  OH  TYR A 357     5993   7113   6045  -1357    881    102
ATOM   5040  HB2 TYR A 357      41.047   4.666  18.418  1.00 46.56           H  
ATOM   5041  HD1 TYR A 357      42.262   8.112  17.547  1.00 47.04           H  
ATOM   5042  HD2 TYR A 357      42.224   3.935  16.434  1.00 47.80           H  
ATOM   5043  HE1 TYR A 357      44.164   8.493  16.050  1.00 47.75           H  
ATOM   5044  HE2 TYR A 357      44.153   4.331  14.931  1.00 49.06           H  
ATOM   5045  HH  TYR A 357      45.576   7.573  14.492  1.00 50.40           H  
ATOM   5046  H   TYR A 357      42.538   5.878  20.007  1.00 46.58           H  
ATOM   5047  HA  TYR A 357      40.624   7.671  18.844  1.00 45.77           H  
ATOM   5048  HB3 TYR A 357      40.050   5.658  17.409  1.00 46.56           H  
ATOM   5049  N   GLU A 358      39.362   5.373  20.828  1.00 45.41           N  
ANISOU 5049  N   GLU A 358     5387   6358   5508   -798   1156   -751
ATOM   5050  CA  GLU A 358      38.217   5.040  21.672  1.00 45.35           C  
ANISOU 5050  CA  GLU A 358     5324   6407   5500   -694   1149   -818
ATOM   5051  C   GLU A 358      37.703   6.260  22.447  1.00 45.14           C  
ANISOU 5051  C   GLU A 358     5448   6117   5588   -580   1191   -827
ATOM   5052  O   GLU A 358      36.508   6.537  22.412  1.00 45.08           O  
ANISOU 5052  O   GLU A 358     5400   6072   5657   -416   1212   -885
ATOM   5053  CB  GLU A 358      38.606   3.881  22.609  1.00 45.93           C  
ANISOU 5053  CB  GLU A 358     5354   6654   5444   -843   1090   -779
ATOM   5054  CG  GLU A 358      37.500   3.457  23.595  1.00 46.64           C  
ANISOU 5054  CG  GLU A 358     5372   6817   5534   -754   1048   -784
ATOM   5055  CD  GLU A 358      37.897   2.276  24.478  1.00 49.71           C  
ANISOU 5055  CD  GLU A 358     5710   7393   5784   -959    944   -701
ATOM   5056  OE1 GLU A 358      38.954   1.660  24.220  1.00 51.78           O  
ANISOU 5056  OE1 GLU A 358     5972   7749   5953  -1167    922   -662
ATOM   5057  OE2 GLU A 358      37.125   2.011  25.422  1.00 50.14           O1-
ANISOU 5057  OE2 GLU A 358     5724   7510   5816   -937    868   -656
ATOM   5058  HB2 GLU A 358      38.913   3.026  22.008  1.00 45.93           H  
ATOM   5059  HG3 GLU A 358      36.595   3.191  23.046  1.00 46.64           H  
ATOM   5060  HG2 GLU A 358      37.235   4.280  24.258  1.00 46.64           H  
ATOM   5061  H   GLU A 358      40.228   4.890  21.028  1.00 45.41           H  
ATOM   5062  HA  GLU A 358      37.406   4.711  21.020  1.00 45.35           H  
ATOM   5063  HB3 GLU A 358      39.488   4.161  23.185  1.00 45.93           H  
ATOM   5064  N   TRP A 359      38.620   7.011  23.078  1.00 44.98           N  
ANISOU 5064  N   TRP A 359     5621   5892   5576   -669   1234   -769
ATOM   5065  CA  TRP A 359      38.356   8.262  23.782  1.00 44.22           C  
ANISOU 5065  CA  TRP A 359     5696   5520   5586   -576   1325   -767
ATOM   5066  C   TRP A 359      37.778   9.358  22.867  1.00 43.55           C  
ANISOU 5066  C   TRP A 359     5541   5324   5684   -412   1371   -762
ATOM   5067  O   TRP A 359      36.836  10.033  23.278  1.00 43.24           O  
ANISOU 5067  O   TRP A 359     5537   5162   5728   -287   1417   -796
ATOM   5068  CE2 TRP A 359      39.779  12.335  25.679  1.00 46.15           C  
ANISOU 5068  CE2 TRP A 359     6644   4708   6182   -433   1901   -620
ATOM   5069  CE3 TRP A 359      40.596  11.856  23.453  1.00 46.61           C  
ANISOU 5069  CE3 TRP A 359     6334   5021   6353   -437   1739   -482
ATOM   5070  CZ2 TRP A 359      40.125  13.688  25.545  1.00 45.14           C  
ANISOU 5070  CZ2 TRP A 359     6570   4297   6284   -293   2109   -522
ATOM   5071  CZ3 TRP A 359      40.941  13.212  23.300  1.00 44.67           C  
ANISOU 5071  CZ3 TRP A 359     6119   4510   6343   -304   1908   -357
ATOM   5072  CH2 TRP A 359      40.712  14.128  24.347  1.00 45.49           C  
ANISOU 5072  CH2 TRP A 359     6420   4347   6516   -223   2107   -379
ATOM   5073  CB  TRP A 359      39.655   8.733  24.457  1.00 44.95           C  
ANISOU 5073  CB  TRP A 359     6027   5387   5663   -701   1423   -703
ATOM   5074  CG  TRP A 359      39.592  10.067  25.134  1.00 44.03           C  
ANISOU 5074  CG  TRP A 359     6119   4956   5656   -611   1580   -692
ATOM   5075  CD1 TRP A 359      39.132  10.270  26.379  1.00 41.84           C  
ANISOU 5075  CD1 TRP A 359     6032   4571   5293   -633   1622   -742
ATOM   5076  CD2 TRP A 359      40.011  11.378  24.648  1.00 46.60           C  
ANISOU 5076  CD2 TRP A 359     6480   5032   6194   -493   1732   -603
ATOM   5077  NE1 TRP A 359      39.205  11.605  26.693  1.00 43.10           N  
ANISOU 5077  NE1 TRP A 359     6374   4413   5588   -536   1824   -715
ATOM   5078  H   TRP A 359      39.583   6.703  23.043  1.00 44.98           H  
ATOM   5079  HA  TRP A 359      37.620   8.056  24.562  1.00 44.22           H  
ATOM   5080  HB3 TRP A 359      40.473   8.766  23.744  1.00 44.95           H  
ATOM   5081  HB2 TRP A 359      39.954   7.997  25.203  1.00 44.95           H  
ATOM   5082  HD1 TRP A 359      38.772   9.478  27.000  1.00 41.84           H  
ATOM   5083  HE1 TRP A 359      38.911  11.986  27.584  1.00 43.10           H  
ATOM   5084  HE3 TRP A 359      40.801  11.160  22.654  1.00 46.61           H  
ATOM   5085  HZ2 TRP A 359      39.942  14.383  26.351  1.00 45.14           H  
ATOM   5086  HZ3 TRP A 359      41.392  13.552  22.379  1.00 44.67           H  
ATOM   5087  HH2 TRP A 359      40.987  15.165  24.228  1.00 45.49           H  
ATOM   5088  N   VAL A 360      38.300   9.516  21.634  1.00 43.42           N  
ANISOU 5088  N   VAL A 360     5424   5355   5717   -436   1346   -704
ATOM   5089  CA  VAL A 360      37.776  10.447  20.623  1.00 43.11           C  
ANISOU 5089  CA  VAL A 360     5301   5247   5832   -335   1349   -676
ATOM   5090  C   VAL A 360      36.343  10.064  20.201  1.00 42.66           C  
ANISOU 5090  C   VAL A 360     5165   5298   5745   -251   1311   -809
ATOM   5091  O   VAL A 360      35.498  10.950  20.076  1.00 41.81           O  
ANISOU 5091  O   VAL A 360     5083   5053   5750   -145   1356   -833
ATOM   5092  CB  VAL A 360      38.732  10.529  19.395  1.00 44.05           C  
ANISOU 5092  CB  VAL A 360     5321   5440   5976   -416   1282   -559
ATOM   5093  CG1 VAL A 360      38.154  11.342  18.217  1.00 42.84           C  
ANISOU 5093  CG1 VAL A 360     5052   5313   5910   -384   1218   -548
ATOM   5094  CG2 VAL A 360      40.099  11.127  19.769  1.00 44.23           C  
ANISOU 5094  CG2 VAL A 360     5424   5265   6118   -428   1366   -386
ATOM   5095  HB  VAL A 360      38.908   9.518  19.029  1.00 44.05           H  
ATOM   5096 HG11 VAL A 360      38.886  11.450  17.416  1.00 42.84           H  
ATOM   5097 HG12 VAL A 360      37.277  10.868  17.776  1.00 42.84           H  
ATOM   5098 HG13 VAL A 360      37.867  12.346  18.534  1.00 42.84           H  
ATOM   5099 HG21 VAL A 360      40.764  11.157  18.906  1.00 44.23           H  
ATOM   5100 HG22 VAL A 360      39.997  12.145  20.145  1.00 44.23           H  
ATOM   5101 HG23 VAL A 360      40.604  10.544  20.532  1.00 44.23           H  
ATOM   5102  H   VAL A 360      39.083   8.933  21.368  1.00 43.42           H  
ATOM   5103  HA  VAL A 360      37.727  11.438  21.081  1.00 43.11           H  
ATOM   5104  N   GLN A 361      36.059   8.761  20.033  1.00 43.51           N  
ANISOU 5104  N   GLN A 361     4590   5646   6298    231    192   -667
ATOM   5105  CA  GLN A 361      34.738   8.227  19.689  1.00 44.06           C  
ANISOU 5105  CA  GLN A 361     4576   5766   6397    324    151   -799
ATOM   5106  C   GLN A 361      33.713   8.380  20.829  1.00 43.62           C  
ANISOU 5106  C   GLN A 361     4490   5632   6451    423     41   -849
ATOM   5107  O   GLN A 361      32.523   8.489  20.543  1.00 43.77           O  
ANISOU 5107  O   GLN A 361     4523   5620   6488    521    -25   -909
ATOM   5108  CD  GLN A 361      35.978   5.011  17.815  1.00 49.59           C  
ANISOU 5108  CD  GLN A 361     5052   6857   6931    115    455   -975
ATOM   5109  OE1 GLN A 361      35.118   4.136  17.768  1.00 50.51           O  
ANISOU 5109  OE1 GLN A 361     5068   7068   7053    184    486  -1107
ATOM   5110  NE2 GLN A 361      37.276   4.726  17.722  1.00 49.93           N  
ANISOU 5110  NE2 GLN A 361     5100   6928   6944    -28    520   -911
ATOM   5111  CB  GLN A 361      34.864   6.735  19.310  1.00 45.32           C  
ANISOU 5111  CB  GLN A 361     4609   6075   6534    287    245   -913
ATOM   5112  CG  GLN A 361      35.594   6.483  17.977  1.00 46.28           C  
ANISOU 5112  CG  GLN A 361     4764   6284   6535    189    349   -882
ATOM   5113  H   GLN A 361      36.809   8.092  20.150  1.00 43.51           H  
ATOM   5114  HA  GLN A 361      34.354   8.773  18.831  1.00 44.06           H  
ATOM   5115  HB3 GLN A 361      33.868   6.300  19.230  1.00 45.32           H  
ATOM   5116  HB2 GLN A 361      35.361   6.193  20.116  1.00 45.32           H  
ATOM   5117  HG3 GLN A 361      36.482   7.108  17.889  1.00 46.28           H  
ATOM   5118  HG2 GLN A 361      34.957   6.768  17.140  1.00 46.28           H  
ATOM   5119 HE22 GLN A 361      37.577   3.762  17.649  1.00 49.93           H  
ATOM   5120 HE21 GLN A 361      37.954   5.472  17.776  1.00 49.93           H  
ATOM   5121  N   ASN A 362      34.158   8.435  22.099  1.00 43.20           N  
ANISOU 5121  N   ASN A 362     4417   5541   6457    383     22   -820
ATOM   5122  CA  ASN A 362      33.309   8.661  23.273  1.00 42.84           C  
ANISOU 5122  CA  ASN A 362     4348   5425   6503    453    -87   -849
ATOM   5123  C   ASN A 362      33.019  10.153  23.516  1.00 41.54           C  
ANISOU 5123  C   ASN A 362     4309   5129   6347    505   -176   -777
ATOM   5124  O   ASN A 362      32.009  10.462  24.145  1.00 40.94           O  
ANISOU 5124  O   ASN A 362     4235   4990   6330    576   -277   -806
ATOM   5125  CB  ASN A 362      34.013   8.138  24.552  1.00 43.53           C  
ANISOU 5125  CB  ASN A 362     4399   5517   6622    354    -74   -827
ATOM   5126  CG  ASN A 362      34.216   6.623  24.608  1.00 46.84           C  
ANISOU 5126  CG  ASN A 362     4643   6095   7058    322    -34   -923
ATOM   5127  OD1 ASN A 362      35.274   6.156  25.021  1.00 51.19           O  
ANISOU 5127  OD1 ASN A 362     5084   6718   7647    439    -65  -1017
ATOM   5128  ND2 ASN A 362      33.200   5.840  24.246  1.00 45.27           N  
ANISOU 5128  ND2 ASN A 362     4420   5957   6824    166     41   -901
ATOM   5129  H   ASN A 362      35.150   8.315  22.261  1.00 43.20           H  
ATOM   5130  HA  ASN A 362      32.351   8.157  23.141  1.00 42.84           H  
ATOM   5131  HB3 ASN A 362      33.432   8.408  25.435  1.00 43.53           H  
ATOM   5132  HB2 ASN A 362      34.984   8.620  24.670  1.00 43.53           H  
ATOM   5133 HD22 ASN A 362      33.323   4.836  24.231  1.00 45.27           H  
ATOM   5134 HD21 ASN A 362      32.335   6.242  23.906  1.00 45.27           H  
ATOM   5135  N   GLN A 363      33.874  11.066  23.022  1.00 41.63           N  
ANISOU 5135  N   GLN A 363     4419   5107   6291    466   -139   -673
ATOM   5136  CA  GLN A 363      33.753  12.516  23.201  1.00 39.99           C  
ANISOU 5136  CA  GLN A 363     4313   4800   6083    496   -206   -583
ATOM   5137  C   GLN A 363      32.634  13.130  22.338  1.00 39.55           C  
ANISOU 5137  C   GLN A 363     4285   4747   5995    555   -273   -608
ATOM   5138  O   GLN A 363      32.031  14.115  22.762  1.00 39.45           O  
ANISOU 5138  O   GLN A 363     4318   4663   6008    595   -366   -602
ATOM   5139  CD  GLN A 363      36.348  14.362  24.678  1.00 44.14           C  
ANISOU 5139  CD  GLN A 363     5052   5131   6590    424   -107   -320
ATOM   5140  OE1 GLN A 363      35.536  14.663  25.547  1.00 44.14           O  
ANISOU 5140  OE1 GLN A 363     5118   5116   6536    448    -59   -206
ATOM   5141  NE2 GLN A 363      37.396  15.135  24.391  1.00 43.08           N  
ANISOU 5141  NE2 GLN A 363     4924   4929   6515    434   -180   -358
ATOM   5142  CB  GLN A 363      35.089  13.179  22.800  1.00 39.44           C  
ANISOU 5142  CB  GLN A 363     4322   4710   5955    450   -133   -451
ATOM   5143  CG  GLN A 363      36.202  13.075  23.864  1.00 40.79           C  
ANISOU 5143  CG  GLN A 363     4526   4813   6159    392    -87   -419
ATOM   5144  H   GLN A 363      34.691  10.730  22.529  1.00 41.63           H  
ATOM   5145  HA  GLN A 363      33.536  12.738  24.248  1.00 39.99           H  
ATOM   5146  HB3 GLN A 363      34.931  14.231  22.555  1.00 39.44           H  
ATOM   5147  HB2 GLN A 363      35.449  12.740  21.871  1.00 39.44           H  
ATOM   5148  HG3 GLN A 363      37.153  12.855  23.375  1.00 40.79           H  
ATOM   5149  HG2 GLN A 363      36.018  12.246  24.546  1.00 40.79           H  
ATOM   5150 HE22 GLN A 363      37.555  15.989  24.906  1.00 43.08           H  
ATOM   5151 HE21 GLN A 363      38.049  14.845  23.679  1.00 43.08           H  
ATOM   5152  N   TYR A 364      32.335  12.537  21.168  1.00 40.01           N  
ANISOU 5152  N   TYR A 364     4329   4888   5985    544   -224   -641
ATOM   5153  CA  TYR A 364      31.277  12.966  20.244  1.00 39.95           C  
ANISOU 5153  CA  TYR A 364     4370   4880   5930    578   -281   -685
ATOM   5154  C   TYR A 364      30.256  11.864  19.931  1.00 41.24           C  
ANISOU 5154  C   TYR A 364     4484   5062   6124    640   -274   -838
ATOM   5155  O   TYR A 364      29.321  12.102  19.166  1.00 42.44           O  
ANISOU 5155  O   TYR A 364     4700   5190   6235    672   -309   -900
ATOM   5156  CB  TYR A 364      31.855  13.699  19.011  1.00 39.36           C  
ANISOU 5156  CB  TYR A 364     4348   4878   5731    516   -251   -600
ATOM   5157  CG  TYR A 364      32.440  12.895  17.850  1.00 39.25           C  
ANISOU 5157  CG  TYR A 364     4301   4972   5640    461   -148   -616
ATOM   5158  CD1 TYR A 364      33.123  11.672  18.040  1.00 41.94           C  
ANISOU 5158  CD1 TYR A 364     4566   5352   6016    443    -60   -661
ATOM   5159  CD2 TYR A 364      32.328  13.421  16.545  1.00 42.85           C  
ANISOU 5159  CD2 TYR A 364     4805   5506   5970    404   -140   -580
ATOM   5160  CE1 TYR A 364      33.705  11.004  16.943  1.00 43.48           C  
ANISOU 5160  CE1 TYR A 364     4738   5655   6126    375     40   -674
ATOM   5161  CE2 TYR A 364      32.898  12.749  15.448  1.00 44.32           C  
ANISOU 5161  CE2 TYR A 364     4974   5799   6068    338    -46   -588
ATOM   5162  CZ  TYR A 364      33.594  11.543  15.649  1.00 46.52           C  
ANISOU 5162  CZ  TYR A 364     5182   6107   6387    327     46   -637
ATOM   5163  OH  TYR A 364      34.153  10.901  14.584  1.00 49.04           O  
ANISOU 5163  OH  TYR A 364     5489   6536   6607    246    141   -645
ATOM   5164  HB2 TYR A 364      31.057  14.319  18.600  1.00 39.36           H  
ATOM   5165  HD1 TYR A 364      33.212  11.238  19.024  1.00 41.94           H  
ATOM   5166  HD2 TYR A 364      31.811  14.355  16.379  1.00 42.85           H  
ATOM   5167  HE1 TYR A 364      34.236  10.076  17.089  1.00 43.48           H  
ATOM   5168  HE2 TYR A 364      32.805  13.168  14.458  1.00 44.32           H  
ATOM   5169  HH  TYR A 364      34.025  11.367  13.771  1.00 49.04           H  
ATOM   5170  H   TYR A 364      32.889  11.738  20.897  1.00 40.01           H  
ATOM   5171  HA  TYR A 364      30.672  13.714  20.760  1.00 39.95           H  
ATOM   5172  HB3 TYR A 364      32.618  14.406  19.340  1.00 39.36           H  
ATOM   5173  N   GLY A 365      30.405  10.683  20.553  1.00 41.53           N  
ANISOU 5173  N   GLY A 365     4411   5147   6223    655   -222   -898
ATOM   5174  CA  GLY A 365      29.443   9.584  20.531  1.00 42.84           C  
ANISOU 5174  CA  GLY A 365     4499   5343   6435    750   -215  -1038
ATOM   5175  C   GLY A 365      29.284   8.857  19.190  1.00 43.84           C  
ANISOU 5175  C   GLY A 365     4634   5542   6481    760   -132  -1126
ATOM   5176  O   GLY A 365      28.288   8.155  19.020  1.00 44.72           O  
ANISOU 5176  O   GLY A 365     4750   5629   6611    868   -141  -1241
ATOM   5177  H   GLY A 365      31.202  10.568  21.163  1.00 41.53           H  
ATOM   5178  HA3 GLY A 365      28.468   9.955  20.850  1.00 42.84           H  
ATOM   5179  HA2 GLY A 365      29.754   8.852  21.278  1.00 42.84           H  
ATOM   5180  N   TYR A 366      30.225   9.026  18.248  1.00 43.87           N  
ANISOU 5180  N   TYR A 366     4651   5628   6390    652    -48  -1073
ATOM   5181  CA  TYR A 366      30.219   8.381  16.937  1.00 45.36           C  
ANISOU 5181  CA  TYR A 366     4841   5910   6485    629     50  -1155
ATOM   5182  C   TYR A 366      31.396   7.405  16.866  1.00 46.24           C  
ANISOU 5182  C   TYR A 366     4831   6159   6580    552    170  -1160
ATOM   5183  O   TYR A 366      32.532   7.783  17.150  1.00 46.48           O  
ANISOU 5183  O   TYR A 366     4858   6200   6602    459    184  -1046
ATOM   5184  CB  TYR A 366      30.313   9.458  15.840  1.00 45.16           C  
ANISOU 5184  CB  TYR A 366     4948   5881   6329    539     36  -1076
ATOM   5185  CG  TYR A 366      30.021   8.929  14.448  1.00 46.81           C  
ANISOU 5185  CG  TYR A 366     5200   6163   6423    506    117  -1173
ATOM   5186  CD1 TYR A 366      28.703   8.557  14.110  1.00 46.91           C  
ANISOU 5186  CD1 TYR A 366     5258   6122   6443    605    121  -1324
ATOM   5187  CD2 TYR A 366      31.054   8.787  13.498  1.00 49.11           C  
ANISOU 5187  CD2 TYR A 366     5503   6569   6587    378    194  -1112
ATOM   5188  CE1 TYR A 366      28.418   8.039  12.833  1.00 49.72           C  
ANISOU 5188  CE1 TYR A 366     5673   6534   6683    572    211  -1427
ATOM   5189  CE2 TYR A 366      30.767   8.271  12.218  1.00 50.35           C  
ANISOU 5189  CE2 TYR A 366     5708   6799   6622    330    274  -1207
ATOM   5190  CZ  TYR A 366      29.449   7.896  11.886  1.00 52.03           C  
ANISOU 5190  CZ  TYR A 366     5969   6956   6845    425    289  -1372
ATOM   5191  OH  TYR A 366      29.168   7.394  10.649  1.00 54.75           O  
ANISOU 5191  OH  TYR A 366     6382   7362   7060    376    384  -1483
ATOM   5192  HB2 TYR A 366      29.593  10.251  16.044  1.00 45.16           H  
ATOM   5193  HD1 TYR A 366      27.908   8.661  14.833  1.00 46.91           H  
ATOM   5194  HD2 TYR A 366      32.068   9.060  13.752  1.00 49.11           H  
ATOM   5195  HE1 TYR A 366      27.407   7.752  12.581  1.00 49.72           H  
ATOM   5196  HE2 TYR A 366      31.564   8.158  11.498  1.00 50.35           H  
ATOM   5197  HH  TYR A 366      29.935   7.293  10.107  1.00 54.75           H  
ATOM   5198  H   TYR A 366      31.021   9.607  18.471  1.00 43.87           H  
ATOM   5199  HA  TYR A 366      29.290   7.825  16.795  1.00 45.36           H  
ATOM   5200  HB3 TYR A 366      31.291   9.938  15.856  1.00 45.16           H  
ATOM   5201  N   TYR A 367      31.101   6.149  16.502  1.00 47.32           N  
ANISOU 5201  N   TYR A 367     4877   6399   6704    589    262  -1291
ATOM   5202  CA  TYR A 367      32.015   5.014  16.594  1.00 47.79           C  
ANISOU 5202  CA  TYR A 367     4795   6605   6756    514    370  -1311
ATOM   5203  C   TYR A 367      32.397   4.535  15.195  1.00 49.15           C  
ANISOU 5203  C   TYR A 367     4990   6894   6792    408    492  -1333
ATOM   5204  O   TYR A 367      31.557   4.449  14.298  1.00 50.79           O  
ANISOU 5204  O   TYR A 367     5250   7113   6936    450    528  -1424
ATOM   5205  CB  TYR A 367      31.351   3.894  17.415  1.00 48.46           C  
ANISOU 5205  CB  TYR A 367     4706   6758   6947    633    379  -1429
ATOM   5206  CG  TYR A 367      31.118   4.331  18.848  1.00 47.08           C  
ANISOU 5206  CG  TYR A 367     4521   6481   6886    682    252  -1367
ATOM   5207  CD1 TYR A 367      29.903   4.950  19.206  1.00 45.92           C  
ANISOU 5207  CD1 TYR A 367     4460   6190   6798    814    136  -1379
ATOM   5208  CD2 TYR A 367      32.155   4.218  19.798  1.00 47.71           C  
ANISOU 5208  CD2 TYR A 367     4539   6594   6993    569    247  -1286
ATOM   5209  CE1 TYR A 367      29.743   5.498  20.492  1.00 47.14           C  
ANISOU 5209  CE1 TYR A 367     4623   6248   7039    842     19  -1316
ATOM   5210  CE2 TYR A 367      31.997   4.774  21.081  1.00 47.54           C  
ANISOU 5210  CE2 TYR A 367     4531   6472   7059    596    132  -1229
ATOM   5211  CZ  TYR A 367      30.796   5.425  21.424  1.00 47.32           C  
ANISOU 5211  CZ  TYR A 367     4576   6313   7091    735     17  -1243
ATOM   5212  OH  TYR A 367      30.649   5.997  22.652  1.00 46.00           O  
ANISOU 5212  OH  TYR A 367     4431   6050   6998    756    -98  -1188
ATOM   5213  HB2 TYR A 367      30.404   3.592  16.964  1.00 48.46           H  
ATOM   5214  HD1 TYR A 367      29.106   5.048  18.483  1.00 45.92           H  
ATOM   5215  HD2 TYR A 367      33.093   3.752  19.532  1.00 47.71           H  
ATOM   5216  HE1 TYR A 367      28.818   5.993  20.749  1.00 47.14           H  
ATOM   5217  HE2 TYR A 367      32.811   4.718  21.788  1.00 47.54           H  
ATOM   5218  HH  TYR A 367      29.803   6.405  22.764  1.00 46.00           H  
ATOM   5219  H   TYR A 367      30.148   5.941  16.240  1.00 47.32           H  
ATOM   5220  HA  TYR A 367      32.925   5.315  17.113  1.00 47.79           H  
ATOM   5221  HB3 TYR A 367      31.986   3.006  17.422  1.00 48.46           H  
ATOM   5222  N   TRP A 368      33.696   4.265  15.026  1.00 49.35           N  
ANISOU 5222  N   TRP A 368     4997   6996   6759    258    559  -1246
ATOM   5223  CA  TRP A 368      34.344   3.982  13.752  1.00 50.25           C  
ANISOU 5223  CA  TRP A 368     5149   7220   6726    133    667  -1240
ATOM   5224  C   TRP A 368      34.470   2.469  13.554  1.00 51.84           C  
ANISOU 5224  C   TRP A 368     5203   7602   6890    101    808  -1377
ATOM   5225  O   TRP A 368      34.645   1.716  14.513  1.00 52.72           O  
ANISOU 5225  O   TRP A 368     5160   7782   7091    147    828  -1445
ATOM   5226  CE2 TRP A 368      36.575   8.191  14.786  1.00 48.19           C  
ANISOU 5226  CE2 TRP A 368     5254   6592   6464     67    400   -673
ATOM   5227  CE3 TRP A 368      38.325   6.524  14.917  1.00 46.44           C  
ANISOU 5227  CE3 TRP A 368     4975   6483   6187   -126    578   -661
ATOM   5228  CZ2 TRP A 368      37.439   9.180  15.286  1.00 47.93           C  
ANISOU 5228  CZ2 TRP A 368     5303   6468   6440     66    359   -506
ATOM   5229  CZ3 TRP A 368      39.205   7.511  15.407  1.00 47.44           C  
ANISOU 5229  CZ3 TRP A 368     5213   6489   6323   -126    537   -497
ATOM   5230  CH2 TRP A 368      38.766   8.833  15.600  1.00 48.57           C  
ANISOU 5230  CH2 TRP A 368     5415   6536   6502    -18    432   -421
ATOM   5231  CB  TRP A 368      35.760   4.602  13.792  1.00 50.04           C  
ANISOU 5231  CB  TRP A 368     5210   7165   6637     -8    665  -1059
ATOM   5232  CG  TRP A 368      35.843   6.076  14.085  1.00 47.98           C  
ANISOU 5232  CG  TRP A 368     5070   6754   6408     38    542   -923
ATOM   5233  CD1 TRP A 368      34.836   6.974  13.959  1.00 48.59           C  
ANISOU 5233  CD1 TRP A 368     5210   6748   6505    137    445   -938
ATOM   5234  CD2 TRP A 368      36.984   6.837  14.592  1.00 46.50           C  
ANISOU 5234  CD2 TRP A 368     4959   6486   6222    -15    513   -753
ATOM   5235  NE1 TRP A 368      35.260   8.212  14.382  1.00 46.63           N  
ANISOU 5235  NE1 TRP A 368     5045   6399   6274    144    356   -788
ATOM   5236  H   TRP A 368      34.298   4.318  15.837  1.00 49.35           H  
ATOM   5237  HA  TRP A 368      33.773   4.418  12.930  1.00 50.25           H  
ATOM   5238  HB3 TRP A 368      36.278   4.420  12.851  1.00 50.04           H  
ATOM   5239  HB2 TRP A 368      36.349   4.100  14.563  1.00 50.04           H  
ATOM   5240  HD1 TRP A 368      33.839   6.741  13.610  1.00 48.59           H  
ATOM   5241  HE1 TRP A 368      34.656   9.025  14.407  1.00 46.63           H  
ATOM   5242  HE3 TRP A 368      38.684   5.514  14.781  1.00 46.44           H  
ATOM   5243  HZ2 TRP A 368      37.088  10.192  15.422  1.00 47.93           H  
ATOM   5244  HZ3 TRP A 368      40.228   7.253  15.625  1.00 47.44           H  
ATOM   5245  HH2 TRP A 368      39.448   9.579  15.977  1.00 48.57           H  
ATOM   5246  N   THR A 369      34.403   2.042  12.284  1.00 52.63           N  
ANISOU 5246  N   THR A 369     5346   7800   6852     17    907  -1414
ATOM   5247  CA  THR A 369      34.597   0.662  11.839  1.00 54.41           C  
ANISOU 5247  CA  THR A 369     5433   8213   7025    -23   1056  -1545
ATOM   5248  C   THR A 369      36.082   0.267  11.928  1.00 55.15           C  
ANISOU 5248  C   THR A 369     5502   8408   7046   -228   1128  -1448
ATOM   5249  O   THR A 369      36.959   1.130  11.994  1.00 54.39           O  
ANISOU 5249  O   THR A 369     5539   8223   6905   -329   1076  -1283
ATOM   5250  CB  THR A 369      34.088   0.513  10.379  1.00 55.72           C  
ANISOU 5250  CB  THR A 369     5670   8446   7056    -34   1151  -1653
ATOM   5251  OG1 THR A 369      34.876   1.235   9.453  1.00 55.27           O  
ANISOU 5251  OG1 THR A 369     5777   8365   6856   -189   1133  -1521
ATOM   5252  CG2 THR A 369      32.611   0.896  10.196  1.00 54.14           C  
ANISOU 5252  CG2 THR A 369     5521   8139   6911    159   1106  -1774
ATOM   5253  H   THR A 369      34.264   2.743  11.564  1.00 52.63           H  
ATOM   5254  HA  THR A 369      34.014   0.003  12.482  1.00 54.41           H  
ATOM   5255  HB  THR A 369      34.184  -0.537  10.099  1.00 55.72           H  
ATOM   5256  HG1 THR A 369      34.744   2.161   9.610  1.00 55.27           H  
ATOM   5257 HG21 THR A 369      32.274   0.680   9.181  1.00 54.14           H  
ATOM   5258 HG22 THR A 369      31.975   0.335  10.879  1.00 54.14           H  
ATOM   5259 HG23 THR A 369      32.441   1.957  10.379  1.00 54.14           H  
ATOM   5260  N   GLU A 370      36.362  -1.045  11.898  1.00 57.05           N  
ANISOU 5260  N   GLU A 370     5573   8835   7267   -285   1250  -1548
ATOM   5261  CA  GLU A 370      37.705  -1.632  11.893  1.00 58.07           C  
ANISOU 5261  CA  GLU A 370     5682   9083   7299   -510   1339  -1478
ATOM   5262  C   GLU A 370      38.603  -1.114  10.750  1.00 58.46           C  
ANISOU 5262  C   GLU A 370     5924   9104   7185   -664   1366  -1359
ATOM   5263  O   GLU A 370      39.787  -0.876  10.972  1.00 58.46           O  
ANISOU 5263  O   GLU A 370     6025   9049   7136   -809   1352  -1202
ATOM   5264  CB  GLU A 370      37.560  -3.168  11.905  1.00 60.09           C  
ANISOU 5264  CB  GLU A 370     5722   9587   7523   -546   1486  -1633
ATOM   5265  CG  GLU A 370      38.887  -3.958  11.900  1.00 61.74           C  
ANISOU 5265  CG  GLU A 370     5884   9947   7629   -803   1587  -1579
ATOM   5266  CD  GLU A 370      38.679  -5.465  12.061  1.00 66.58           C  
ANISOU 5266  CD  GLU A 370     6224  10836   8237   -820   1717  -1737
ATOM   5267  OE1 GLU A 370      37.829  -5.851  12.893  1.00 68.44           O  
ANISOU 5267  OE1 GLU A 370     6277  11121   8607   -633   1683  -1836
ATOM   5268  OE2 GLU A 370      39.383  -6.216  11.351  1.00 67.93           O1-
ANISOU 5268  OE2 GLU A 370     6355  11189   8265  -1018   1854  -1759
ATOM   5269  HB2 GLU A 370      36.978  -3.443  12.786  1.00 60.09           H  
ATOM   5270  HG3 GLU A 370      39.525  -3.618  12.717  1.00 61.74           H  
ATOM   5271  HG2 GLU A 370      39.439  -3.779  10.976  1.00 61.74           H  
ATOM   5272  H   GLU A 370      35.588  -1.692  11.863  1.00 57.05           H  
ATOM   5273  HA  GLU A 370      38.186  -1.335  12.828  1.00 58.07           H  
ATOM   5274  HB3 GLU A 370      36.965  -3.480  11.047  1.00 60.09           H  
ATOM   5275  N   ALA A 371      38.023  -0.872   9.560  1.00 58.77           N  
ANISOU 5275  N   ALA A 371     6028   9171   7132   -630   1399  -1425
ATOM   5276  CA  ALA A 371      38.701  -0.320   8.388  1.00 58.72           C  
ANISOU 5276  CA  ALA A 371     6193   9160   6957   -777   1411  -1307
ATOM   5277  C   ALA A 371      39.035   1.176   8.539  1.00 57.08           C  
ANISOU 5277  C   ALA A 371     6143   8765   6781   -746   1261  -1111
ATOM   5278  O   ALA A 371      40.098   1.601   8.093  1.00 57.13           O  
ANISOU 5278  O   ALA A 371     6266   8745   6694   -872   1250   -940
ATOM   5279  CB  ALA A 371      37.775  -0.496   7.173  1.00 59.60           C  
ANISOU 5279  CB  ALA A 371     6343   9343   6958   -757   1472  -1430
ATOM   5280  HB1 ALA A 371      38.238  -0.108   6.264  1.00 59.60           H  
ATOM   5281  HB2 ALA A 371      37.554  -1.548   7.000  1.00 59.60           H  
ATOM   5282  HB3 ALA A 371      36.825   0.024   7.309  1.00 59.60           H  
ATOM   5283  H   ALA A 371      37.037  -1.071   9.467  1.00 58.77           H  
ATOM   5284  HA  ALA A 371      39.626  -0.875   8.218  1.00 58.72           H  
ATOM   5285  N   GLU A 372      38.159   1.960   9.196  1.00 55.95           N  
ANISOU 5285  N   GLU A 372     6002   8491   6764   -571   1147  -1133
ATOM   5286  CA  GLU A 372      38.352   3.389   9.471  1.00 54.25           C  
ANISOU 5286  CA  GLU A 372     5910   8117   6584   -526   1010   -961
ATOM   5287  C   GLU A 372      39.375   3.608  10.599  1.00 53.72           C  
ANISOU 5287  C   GLU A 372     5855   7967   6588   -564    985   -828
ATOM   5288  O   GLU A 372      40.120   4.586  10.552  1.00 53.05           O  
ANISOU 5288  O   GLU A 372     5892   7786   6479   -581    922   -648
ATOM   5289  CB  GLU A 372      37.009   4.000   9.924  1.00 52.99           C  
ANISOU 5289  CB  GLU A 372     5745   7846   6543   -346    903  -1030
ATOM   5290  CG  GLU A 372      36.028   4.247   8.759  1.00 53.88           C  
ANISOU 5290  CG  GLU A 372     5933   7978   6562   -326    893  -1104
ATOM   5291  CD  GLU A 372      34.610   4.607   9.212  1.00 55.65           C  
ANISOU 5291  CD  GLU A 372     6150   8099   6896   -155    821  -1225
ATOM   5292  OE1 GLU A 372      34.227   4.191  10.327  1.00 54.27           O  
ANISOU 5292  OE1 GLU A 372     5881   7861   6878    -35    788  -1273
ATOM   5293  OE2 GLU A 372      33.912   5.268   8.412  1.00 56.32           O1-
ANISOU 5293  OE2 GLU A 372     6337   8165   6895   -153    796  -1270
ATOM   5294  HB2 GLU A 372      36.563   3.354  10.678  1.00 52.99           H  
ATOM   5295  HG3 GLU A 372      35.957   3.359   8.130  1.00 53.88           H  
ATOM   5296  HG2 GLU A 372      36.412   5.043   8.118  1.00 53.88           H  
ATOM   5297  H   GLU A 372      37.311   1.536   9.544  1.00 55.95           H  
ATOM   5298  HA  GLU A 372      38.707   3.898   8.573  1.00 54.25           H  
ATOM   5299  HB3 GLU A 372      37.178   4.958  10.419  1.00 52.99           H  
ATOM   5300  N   VAL A 373      39.437   2.692  11.583  1.00 54.39           N  
ANISOU 5300  N   VAL A 373     5815   8094   6756   -576   1037   -916
ATOM   5301  CA  VAL A 373      40.443   2.671  12.646  1.00 54.25           C  
ANISOU 5301  CA  VAL A 373     5824   7993   6796   -639   1023   -810
ATOM   5302  C   VAL A 373      41.830   2.344  12.067  1.00 55.22           C  
ANISOU 5302  C   VAL A 373     6051   8152   6777   -834   1108   -690
ATOM   5303  O   VAL A 373      42.783   3.028  12.421  1.00 54.70           O  
ANISOU 5303  O   VAL A 373     6130   7950   6705   -864   1073   -523
ATOM   5304  CB  VAL A 373      40.033   1.671  13.764  1.00 54.94           C  
ANISOU 5304  CB  VAL A 373     5738   8138   6998   -622   1044   -936
ATOM   5305  CG1 VAL A 373      41.179   1.355  14.751  1.00 53.30           C  
ANISOU 5305  CG1 VAL A 373     5583   7856   6811   -743   1047   -834
ATOM   5306  CG2 VAL A 373      38.818   2.199  14.551  1.00 54.12           C  
ANISOU 5306  CG2 VAL A 373     5566   7958   7038   -416    937  -1016
ATOM   5307  HB  VAL A 373      39.739   0.731  13.298  1.00 54.94           H  
ATOM   5308 HG11 VAL A 373      40.833   0.799  15.616  1.00 53.30           H  
ATOM   5309 HG12 VAL A 373      41.963   0.753  14.292  1.00 53.30           H  
ATOM   5310 HG13 VAL A 373      41.636   2.270  15.120  1.00 53.30           H  
ATOM   5311 HG21 VAL A 373      38.449   1.454  15.254  1.00 54.12           H  
ATOM   5312 HG22 VAL A 373      39.077   3.089  15.124  1.00 54.12           H  
ATOM   5313 HG23 VAL A 373      37.991   2.464  13.896  1.00 54.12           H  
ATOM   5314  H   VAL A 373      38.767   1.934  11.569  1.00 54.39           H  
ATOM   5315  HA  VAL A 373      40.500   3.670  13.083  1.00 54.25           H  
ATOM   5316  N   GLU A 374      41.939   1.352  11.164  1.00 56.80           N  
ANISOU 5316  N   GLU A 374     6192   8530   6861   -959   1225   -774
ATOM   5317  CA  GLU A 374      43.193   0.927  10.533  1.00 58.00           C  
ANISOU 5317  CA  GLU A 374     6457   8728   6854  -1164   1309   -662
ATOM   5318  C   GLU A 374      43.763   1.989   9.581  1.00 57.58           C  
ANISOU 5318  C   GLU A 374     6590   8583   6706  -1153   1247   -477
ATOM   5319  O   GLU A 374      44.982   2.157   9.542  1.00 58.22           O  
ANISOU 5319  O   GLU A 374     6823   8574   6726  -1241   1251   -302
ATOM   5320  CB  GLU A 374      42.944  -0.358   9.725  1.00 59.65           C  
ANISOU 5320  CB  GLU A 374     6558   9163   6942  -1296   1447   -798
ATOM   5321  CG  GLU A 374      42.936  -1.628  10.592  1.00 61.32           C  
ANISOU 5321  CG  GLU A 374     6580   9513   7207  -1358   1531   -940
ATOM   5322  CD  GLU A 374      42.691  -2.905   9.785  1.00 64.60           C  
ANISOU 5322  CD  GLU A 374     6865  10178   7501  -1467   1680  -1088
ATOM   5323  OE1 GLU A 374      42.580  -2.818   8.541  1.00 65.50           O  
ANISOU 5323  OE1 GLU A 374     7073  10345   7471  -1532   1726  -1068
ATOM   5324  OE2 GLU A 374      42.651  -3.975  10.425  1.00 65.38           O1-
ANISOU 5324  OE2 GLU A 374     6760  10437   7642  -1491   1754  -1223
ATOM   5325  HB2 GLU A 374      42.010  -0.272   9.165  1.00 59.65           H  
ATOM   5326  HG3 GLU A 374      42.182  -1.559  11.375  1.00 61.32           H  
ATOM   5327  HG2 GLU A 374      43.891  -1.731  11.108  1.00 61.32           H  
ATOM   5328  H   GLU A 374      41.106   0.832  10.922  1.00 56.80           H  
ATOM   5329  HA  GLU A 374      43.935   0.729  11.309  1.00 58.00           H  
ATOM   5330  HB3 GLU A 374      43.728  -0.477   8.974  1.00 59.65           H  
ATOM   5331  N   GLU A 375      42.898   2.719   8.848  1.00 56.71           N  
ANISOU 5331  N   GLU A 375     6473   8497   6576  -1048   1190   -510
ATOM   5332  CA  GLU A 375      43.277   3.811   7.950  1.00 56.41           C  
ANISOU 5332  CA  GLU A 375     6579   8419   6435  -1046   1121   -333
ATOM   5333  C   GLU A 375      43.920   4.977   8.719  1.00 55.07           C  
ANISOU 5333  C   GLU A 375     6518   8063   6343   -956   1028   -137
ATOM   5334  O   GLU A 375      44.979   5.463   8.322  1.00 55.28           O  
ANISOU 5334  O   GLU A 375     6682   8045   6278  -1015   1028     52
ATOM   5335  CB  GLU A 375      42.037   4.279   7.151  1.00 56.02           C  
ANISOU 5335  CB  GLU A 375     6503   8422   6359   -959   1061   -412
ATOM   5336  CG  GLU A 375      42.292   5.482   6.218  1.00 57.51           C  
ANISOU 5336  CG  GLU A 375     6814   8612   6425   -974    978   -223
ATOM   5337  CD  GLU A 375      41.029   5.919   5.483  1.00 61.19           C  
ANISOU 5337  CD  GLU A 375     7271   9134   6846   -925    914   -300
ATOM   5338  OE1 GLU A 375      40.730   5.299   4.438  1.00 63.68           O  
ANISOU 5338  OE1 GLU A 375     7592   9584   7018  -1034    981   -398
ATOM   5339  OE2 GLU A 375      40.385   6.870   5.978  1.00 60.30           O1-
ANISOU 5339  OE2 GLU A 375     7157   8929   6827   -794    800   -263
ATOM   5340  HB2 GLU A 375      41.662   3.441   6.560  1.00 56.02           H  
ATOM   5341  HG3 GLU A 375      43.059   5.229   5.485  1.00 57.51           H  
ATOM   5342  HG2 GLU A 375      42.664   6.345   6.771  1.00 57.51           H  
ATOM   5343  H   GLU A 375      41.914   2.502   8.920  1.00 56.71           H  
ATOM   5344  HA  GLU A 375      44.015   3.426   7.243  1.00 56.41           H  
ATOM   5345  HB3 GLU A 375      41.235   4.533   7.846  1.00 56.02           H  
ATOM   5346  N   LYS A 376      43.300   5.380   9.842  1.00 53.83           N  
ANISOU 5346  N   LYS A 376     6305   7797   6352   -808    954   -186
ATOM   5347  CA  LYS A 376      43.810   6.404  10.749  1.00 52.98           C  
ANISOU 5347  CA  LYS A 376     6288   7510   6334   -709    882    -34
ATOM   5348  C   LYS A 376      45.064   5.929  11.496  1.00 53.79           C  
ANISOU 5348  C   LYS A 376     6483   7523   6432   -815    958     40
ATOM   5349  O   LYS A 376      45.988   6.720  11.671  1.00 53.64           O  
ANISOU 5349  O   LYS A 376     6615   7371   6396   -786    941    224
ATOM   5350  CB  LYS A 376      42.728   6.772  11.782  1.00 51.56           C  
ANISOU 5350  CB  LYS A 376     6020   7246   6324   -558    803   -133
ATOM   5351  CG  LYS A 376      41.608   7.647  11.201  1.00 51.47           C  
ANISOU 5351  CG  LYS A 376     5949   7282   6324   -454    719   -203
ATOM   5352  CD  LYS A 376      40.615   8.089  12.286  1.00 49.14           C  
ANISOU 5352  CD  LYS A 376     5626   6864   6179   -303    619   -221
ATOM   5353  CE  LYS A 376      39.501   9.007  11.765  1.00 51.45           C  
ANISOU 5353  CE  LYS A 376     5926   7180   6444   -225    521   -206
ATOM   5354  NZ  LYS A 376      38.513   8.258  10.970  1.00 54.70           N1+
ANISOU 5354  NZ  LYS A 376     6266   7673   6842   -223    530   -402
ATOM   5355  HG3 LYS A 376      41.086   7.105  10.413  1.00 51.47           H  
ATOM   5356  HG2 LYS A 376      42.044   8.529  10.732  1.00 51.47           H  
ATOM   5357  HD3 LYS A 376      41.162   8.616  13.069  1.00 49.14           H  
ATOM   5358  HD2 LYS A 376      40.180   7.209  12.760  1.00 49.14           H  
ATOM   5359  HE3 LYS A 376      39.914   9.820  11.167  1.00 51.45           H  
ATOM   5360  HE2 LYS A 376      38.978   9.464  12.604  1.00 51.45           H  
ATOM   5361  HZ1 LYS A 376      38.099   7.536  11.542  1.00 54.70           H  
ATOM   5362  HZ2 LYS A 376      37.791   8.883  10.643  1.00 54.70           H  
ATOM   5363  HZ3 LYS A 376      38.972   7.831  10.177  1.00 54.70           H  
ATOM   5364  H   LYS A 376      42.436   4.923  10.100  1.00 53.83           H  
ATOM   5365  HA  LYS A 376      44.076   7.292  10.172  1.00 52.98           H  
ATOM   5366  HB3 LYS A 376      43.188   7.324  12.605  1.00 51.56           H  
ATOM   5367  HB2 LYS A 376      42.306   5.870  12.228  1.00 51.56           H  
ATOM   5368  N   GLN A 377      45.108   4.647  11.905  1.00 54.64           N  
ANISOU 5368  N   GLN A 377     6504   7709   6549   -937   1045   -104
ATOM   5369  CA  GLN A 377      46.219   4.028  12.628  1.00 55.67           C  
ANISOU 5369  CA  GLN A 377     6722   7768   6662  -1080   1121    -57
ATOM   5370  C   GLN A 377      47.506   4.042  11.803  1.00 57.01           C  
ANISOU 5370  C   GLN A 377     7076   7917   6670  -1212   1181    113
ATOM   5371  O   GLN A 377      48.541   4.446  12.320  1.00 57.50           O  
ANISOU 5371  O   GLN A 377     7315   7814   6718  -1252   1201    249
ATOM   5372  CD  GLN A 377      46.405   0.725  14.760  1.00 59.38           C  
ANISOU 5372  CD  GLN A 377     6910   8469   7184  -1469   1312   -389
ATOM   5373  OE1 GLN A 377      46.815   0.485  15.890  1.00 61.01           O  
ANISOU 5373  OE1 GLN A 377     7066   8596   7520  -1377   1245   -427
ATOM   5374  NE2 GLN A 377      45.526  -0.073  14.151  1.00 62.89           N  
ANISOU 5374  NE2 GLN A 377     7227   9131   7539  -1628   1413   -494
ATOM   5375  CB  GLN A 377      45.862   2.591  13.060  1.00 56.54           C  
ANISOU 5375  CB  GLN A 377     6667   8026   6791  -1207   1201   -246
ATOM   5376  CG  GLN A 377      46.877   1.994  14.052  1.00 58.30           C  
ANISOU 5376  CG  GLN A 377     6974   8203   6976  -1401   1281   -212
ATOM   5377  H   GLN A 377      44.295   4.067  11.736  1.00 54.64           H  
ATOM   5378  HA  GLN A 377      46.396   4.615  13.528  1.00 55.67           H  
ATOM   5379  HB3 GLN A 377      45.752   1.945  12.189  1.00 56.54           H  
ATOM   5380  HB2 GLN A 377      44.897   2.610  13.561  1.00 56.54           H  
ATOM   5381  HG3 GLN A 377      47.084   2.729  14.828  1.00 58.30           H  
ATOM   5382  HG2 GLN A 377      47.827   1.783  13.561  1.00 58.30           H  
ATOM   5383 HE22 GLN A 377      45.194  -0.901  14.622  1.00 62.89           H  
ATOM   5384 HE21 GLN A 377      45.191   0.154  13.225  1.00 62.89           H  
ATOM   5385  N   GLU A 378      47.426   3.661  10.518  1.00 57.74           N  
ANISOU 5385  N   GLU A 378     7143   8166   6631  -1281   1211    106
ATOM   5386  CA  GLU A 378      48.535   3.685   9.571  1.00 59.24           C  
ANISOU 5386  CA  GLU A 378     7509   8348   6653  -1400   1252    282
ATOM   5387  C   GLU A 378      49.047   5.112   9.290  1.00 58.54           C  
ANISOU 5387  C   GLU A 378     7570   8106   6567  -1237   1156    511
ATOM   5388  O   GLU A 378      50.259   5.310   9.203  1.00 59.38           O  
ANISOU 5388  O   GLU A 378     7873   8074   6616  -1270   1180    690
ATOM   5389  CB  GLU A 378      48.089   2.952   8.287  1.00 60.26           C  
ANISOU 5389  CB  GLU A 378     7566   8698   6632  -1513   1300    212
ATOM   5390  CG  GLU A 378      49.109   3.003   7.132  1.00 62.79           C  
ANISOU 5390  CG  GLU A 378     8055   9045   6758  -1688   1359    369
ATOM   5391  CD  GLU A 378      48.838   2.018   5.993  1.00 67.21           C  
ANISOU 5391  CD  GLU A 378     8533   9840   7163  -1835   1429    262
ATOM   5392  OE1 GLU A 378      47.920   1.180   6.121  1.00 66.29           O  
ANISOU 5392  OE1 GLU A 378     8228   9859   7101  -1818   1466     39
ATOM   5393  OE2 GLU A 378      49.583   2.118   4.996  1.00 70.78           O1-
ANISOU 5393  OE2 GLU A 378     9118  10340   7435  -1959   1449    403
ATOM   5394  HB2 GLU A 378      47.883   1.916   8.549  1.00 60.26           H  
ATOM   5395  HG3 GLU A 378      50.110   2.797   7.513  1.00 62.79           H  
ATOM   5396  HG2 GLU A 378      49.123   4.005   6.706  1.00 62.79           H  
ATOM   5397  H   GLU A 378      46.529   3.348  10.168  1.00 57.74           H  
ATOM   5398  HA  GLU A 378      49.358   3.122  10.013  1.00 59.24           H  
ATOM   5399  HB3 GLU A 378      47.141   3.366   7.936  1.00 60.26           H  
ATOM   5400  N   ALA A 379      48.137   6.099   9.199  1.00 57.13           N  
ANISOU 5400  N   ALA A 379     7301   7955   6452  -1061   1052    504
ATOM   5401  CA  ALA A 379      48.446   7.507   8.955  1.00 56.66           C  
ANISOU 5401  CA  ALA A 379     7332   7795   6402   -890    954    712
ATOM   5402  C   ALA A 379      49.172   8.169  10.141  1.00 56.56           C  
ANISOU 5402  C   ALA A 379     7458   7546   6487   -795    960    827
ATOM   5403  O   ALA A 379      50.164   8.864   9.930  1.00 57.20           O  
ANISOU 5403  O   ALA A 379     7705   7517   6512   -737    956   1041
ATOM   5404  CB  ALA A 379      47.134   8.260   8.673  1.00 54.86           C  
ANISOU 5404  CB  ALA A 379     6963   7636   6245   -743    848    645
ATOM   5405  HB1 ALA A 379      47.321   9.311   8.450  1.00 54.86           H  
ATOM   5406  HB2 ALA A 379      46.617   7.833   7.813  1.00 54.86           H  
ATOM   5407  HB3 ALA A 379      46.450   8.220   9.520  1.00 54.86           H  
ATOM   5408  H   ALA A 379      47.161   5.854   9.290  1.00 57.13           H  
ATOM   5409  HA  ALA A 379      49.087   7.573   8.074  1.00 56.66           H  
ATOM   5410  N   ASP A 380      48.702   7.930  11.379  1.00 56.09           N  
ANISOU 5410  N   ASP A 380     7336   7408   6566   -779    974    681
ATOM   5411  CA  ASP A 380      49.260   8.504  12.608  1.00 55.92           C  
ANISOU 5411  CA  ASP A 380     7436   7165   6648   -684    975    751
ATOM   5412  C   ASP A 380      50.495   7.741  13.120  1.00 57.54           C  
ANISOU 5412  C   ASP A 380     7842   7234   6787   -837   1081    816
ATOM   5413  O   ASP A 380      51.326   8.349  13.797  1.00 58.66           O  
ANISOU 5413  O   ASP A 380     8182   7173   6934   -751   1096    977
ATOM   5414  CB  ASP A 380      48.194   8.515  13.725  1.00 54.33           C  
ANISOU 5414  CB  ASP A 380     7093   6944   6606   -620    935    575
ATOM   5415  CG  ASP A 380      47.005   9.451  13.464  1.00 54.74           C  
ANISOU 5415  CG  ASP A 380     7013   7060   6726   -439    819    559
ATOM   5416  OD1 ASP A 380      47.135  10.356  12.610  1.00 56.53           O  
ANISOU 5416  OD1 ASP A 380     7274   7315   6889   -343    767    715
ATOM   5417  OD2 ASP A 380      45.983   9.263  14.159  1.00 54.92           O1-
ANISOU 5417  OD2 ASP A 380     6898   7113   6855   -400    776    399
ATOM   5418  HA  ASP A 380      49.565   9.531  12.412  1.00 55.92           H  
ATOM   5419  HB3 ASP A 380      48.638   8.823  14.673  1.00 54.33           H  
ATOM   5420  HB2 ASP A 380      47.812   7.506  13.876  1.00 54.33           H  
ATOM   5421  H   ASP A 380      47.872   7.359  11.471  1.00 56.09           H  
ATOM   5422  N   MET A 381      50.665   6.456  12.757  1.00 58.26           N  
ANISOU 5422  N   MET A 381     7895   7433   6809  -1065   1163    696
ATOM   5423  CA  MET A 381      51.894   5.696  12.999  1.00 59.80           C  
ANISOU 5423  CA  MET A 381     8299   7518   6904  -1259   1269    766
ATOM   5424  C   MET A 381      53.025   6.230  12.112  1.00 61.29           C  
ANISOU 5424  C   MET A 381     8706   7615   6968  -1215   1273   1012
ATOM   5425  O   MET A 381      54.115   6.468  12.623  1.00 62.60           O  
ANISOU 5425  O   MET A 381     9120   7551   7113  -1194   1313   1159
ATOM   5426  SD  MET A 381      51.878   2.521  15.050  1.00 60.94           S  
ANISOU 5426  SD  MET A 381     8153   7860   7142  -1694   1399    299
ATOM   5427  CE  MET A 381      53.110   3.732  15.579  1.00 62.34           C  
ANISOU 5427  CE  MET A 381     8732   7737   7218  -1779   1466    520
ATOM   5428  CB  MET A 381      51.678   4.191  12.713  1.00 60.87           C  
ANISOU 5428  CB  MET A 381     8330   7849   6948  -1525   1356    613
ATOM   5429  CG  MET A 381      50.915   3.460  13.832  1.00 59.43           C  
ANISOU 5429  CG  MET A 381     7906   7806   6868  -1580   1361    375
ATOM   5430  H   MET A 381      49.930   6.004  12.229  1.00 58.26           H  
ATOM   5431  HA  MET A 381      52.191   5.831  14.040  1.00 59.80           H  
ATOM   5432  HB3 MET A 381      52.627   3.679  12.544  1.00 60.87           H  
ATOM   5433  HB2 MET A 381      51.127   4.093  11.777  1.00 60.87           H  
ATOM   5434  HG3 MET A 381      50.243   2.733  13.376  1.00 59.43           H  
ATOM   5435  HG2 MET A 381      50.280   4.162  14.363  1.00 59.43           H  
ATOM   5436  HE1 MET A 381      53.750   3.290  16.339  1.00 62.34           H  
ATOM   5437  HE2 MET A 381      53.743   4.035  14.746  1.00 62.34           H  
ATOM   5438  HE3 MET A 381      52.630   4.613  16.002  1.00 62.34           H  
ATOM   5439  N   MET A 382      52.758   6.486  10.818  1.00 61.66           N  
ANISOU 5439  N   MET A 382     8666   7838   6924  -1193   1229   1061
ATOM   5440  CA  MET A 382      53.717   7.069   9.877  1.00 63.22           C  
ANISOU 5440  CA  MET A 382     9039   7990   6991  -1146   1213   1307
ATOM   5441  C   MET A 382      54.070   8.537  10.177  1.00 62.92           C  
ANISOU 5441  C   MET A 382     9111   7766   7029   -873   1148   1499
ATOM   5442  O   MET A 382      55.194   8.941   9.889  1.00 64.61           O  
ANISOU 5442  O   MET A 382     9553   7833   7164   -826   1171   1715
ATOM   5443  SD  MET A 382      53.466   5.435   6.049  1.00 70.01           S  
ANISOU 5443  SD  MET A 382     9816   9415   7369  -1573   1252   1355
ATOM   5444  CE  MET A 382      51.702   5.603   5.692  1.00 66.54           C  
ANISOU 5444  CE  MET A 382     9085   9261   6935  -1553   1195   1154
ATOM   5445  CB  MET A 382      53.200   6.926   8.431  1.00 63.32           C  
ANISOU 5445  CB  MET A 382     8914   8257   6888  -1186   1166   1307
ATOM   5446  CG  MET A 382      53.453   5.522   7.859  1.00 65.63           C  
ANISOU 5446  CG  MET A 382     9183   8706   7049  -1468   1263   1186
ATOM   5447  H   MET A 382      51.834   6.274  10.464  1.00 61.66           H  
ATOM   5448  HA  MET A 382      54.657   6.527   9.958  1.00 63.22           H  
ATOM   5449  HB3 MET A 382      53.730   7.634   7.791  1.00 63.32           H  
ATOM   5450  HB2 MET A 382      52.145   7.193   8.358  1.00 63.32           H  
ATOM   5451  HG3 MET A 382      52.735   4.804   8.254  1.00 65.63           H  
ATOM   5452  HG2 MET A 382      54.437   5.169   8.173  1.00 65.63           H  
ATOM   5453  HE1 MET A 382      51.527   5.584   4.617  1.00 66.54           H  
ATOM   5454  HE2 MET A 382      51.160   4.777   6.146  1.00 66.54           H  
ATOM   5455  HE3 MET A 382      51.312   6.540   6.092  1.00 66.54           H  
ATOM   5456  N   LYS A 383      53.164   9.307  10.806  1.00 60.90           N  
ANISOU 5456  N   LYS A 383     8698   7520   6922   -689   1072   1425
ATOM   5457  CA  LYS A 383      53.426  10.651  11.332  1.00 60.57           C  
ANISOU 5457  CA  LYS A 383     8734   7318   6963   -428   1024   1583
ATOM   5458  C   LYS A 383      54.407  10.602  12.522  1.00 61.53           C  
ANISOU 5458  C   LYS A 383     9106   7146   7126   -426   1118   1627
ATOM   5459  O   LYS A 383      55.319  11.425  12.590  1.00 63.17           O  
ANISOU 5459  O   LYS A 383     9518   7178   7306   -277   1136   1837
ATOM   5460  CB  LYS A 383      52.078  11.283  11.753  1.00 58.54           C  
ANISOU 5460  CB  LYS A 383     8254   7142   6845   -276    932   1466
ATOM   5461  CG  LYS A 383      52.160  12.567  12.606  1.00 58.08           C  
ANISOU 5461  CG  LYS A 383     8254   6917   6897    -26    903   1574
ATOM   5462  CD  LYS A 383      50.778  13.177  12.900  1.00 57.98           C  
ANISOU 5462  CD  LYS A 383     8009   7032   6987     88    802   1468
ATOM   5463  CE  LYS A 383      50.738  13.981  14.210  1.00 59.78           C  
ANISOU 5463  CE  LYS A 383     8269   7079   7364    226    811   1423
ATOM   5464  NZ  LYS A 383      51.655  15.133  14.184  1.00 60.00           N1+
ANISOU 5464  NZ  LYS A 383     8458   6934   7404    448    836   1638
ATOM   5465  HG3 LYS A 383      52.795  13.306  12.119  1.00 58.08           H  
ATOM   5466  HG2 LYS A 383      52.635  12.329  13.559  1.00 58.08           H  
ATOM   5467  HD3 LYS A 383      50.043  12.375  12.985  1.00 57.98           H  
ATOM   5468  HD2 LYS A 383      50.453  13.789  12.058  1.00 57.98           H  
ATOM   5469  HE3 LYS A 383      50.994  13.343  15.056  1.00 59.78           H  
ATOM   5470  HE2 LYS A 383      49.726  14.348  14.386  1.00 59.78           H  
ATOM   5471  HZ1 LYS A 383      52.603  14.805  14.058  1.00 60.00           H  
ATOM   5472  HZ2 LYS A 383      51.406  15.745  13.420  1.00 60.00           H  
ATOM   5473  HZ3 LYS A 383      51.588  15.637  15.056  1.00 60.00           H  
ATOM   5474  H   LYS A 383      52.251   8.913  10.985  1.00 60.90           H  
ATOM   5475  HA  LYS A 383      53.872  11.262  10.546  1.00 60.57           H  
ATOM   5476  HB3 LYS A 383      51.513  10.551  12.324  1.00 58.54           H  
ATOM   5477  HB2 LYS A 383      51.488  11.481  10.856  1.00 58.54           H  
ATOM   5478  N   ALA A 384      54.226   9.635  13.438  1.00 60.74           N  
ANISOU 5478  N   ALA A 384     8997   6999   7082   -595   1179   1433
ATOM   5479  CA  ALA A 384      55.062   9.435  14.621  1.00 61.71           C  
ANISOU 5479  CA  ALA A 384     9363   6853   7232   -642   1270   1443
ATOM   5480  C   ALA A 384      56.460   8.914  14.253  1.00 64.58           C  
ANISOU 5480  C   ALA A 384    10021   7076   7438   -789   1366   1592
ATOM   5481  O   ALA A 384      57.443   9.396  14.814  1.00 66.18           O  
ANISOU 5481  O   ALA A 384    10509   7004   7630   -700   1425   1736
ATOM   5482  CB  ALA A 384      54.370   8.433  15.553  1.00 60.71           C  
ANISOU 5482  CB  ALA A 384     9123   6764   7180   -821   1298   1202
ATOM   5483  HB1 ALA A 384      54.948   8.281  16.466  1.00 60.71           H  
ATOM   5484  HB2 ALA A 384      53.382   8.794  15.843  1.00 60.71           H  
ATOM   5485  HB3 ALA A 384      54.235   7.458  15.084  1.00 60.71           H  
ATOM   5486  H   ALA A 384      53.448   9.000  13.313  1.00 60.74           H  
ATOM   5487  HA  ALA A 384      55.167  10.389  15.144  1.00 61.71           H  
ATOM   5488  N   ILE A 385      56.556   7.988  13.277  1.00 65.07           N  
ANISOU 5488  N   ILE A 385    10030   7320   7373  -1012   1387   1557
ATOM   5489  CA  ILE A 385      57.807   7.469  12.709  1.00 67.65           C  
ANISOU 5489  CA  ILE A 385    10628   7543   7532  -1169   1467   1707
ATOM   5490  C   ILE A 385      58.612   8.601  12.048  1.00 69.05           C  
ANISOU 5490  C   ILE A 385    10991   7577   7670   -913   1432   1989
ATOM   5491  O   ILE A 385      59.796   8.738  12.348  1.00 71.25           O  
ANISOU 5491  O   ILE A 385    11600   7582   7891   -897   1506   2143
ATOM   5492  CB  ILE A 385      57.515   6.308  11.710  1.00 68.36           C  
ANISOU 5492  CB  ILE A 385    10588   7902   7482  -1416   1481   1637
ATOM   5493  CG1 ILE A 385      56.919   5.070  12.419  1.00 68.31           C  
ANISOU 5493  CG1 ILE A 385    10427   8031   7499  -1678   1541   1377
ATOM   5494  CG2 ILE A 385      58.756   5.872  10.895  1.00 69.98           C  
ANISOU 5494  CG2 ILE A 385    11080   8014   7495  -1554   1543   1834
ATOM   5495  CD1 ILE A 385      56.121   4.163  11.469  1.00 68.18           C  
ANISOU 5495  CD1 ILE A 385    10133   8351   7422  -1812   1530   1232
ATOM   5496  H   ILE A 385      55.695   7.630  12.885  1.00 65.07           H  
ATOM   5497  HA  ILE A 385      58.409   7.077  13.530  1.00 67.65           H  
ATOM   5498  HB  ILE A 385      56.776   6.678  10.998  1.00 68.36           H  
ATOM   5499 HG13 ILE A 385      56.266   5.370  13.236  1.00 68.31           H  
ATOM   5500 HG12 ILE A 385      57.713   4.493  12.897  1.00 68.31           H  
ATOM   5501 HG21 ILE A 385      58.541   5.010  10.267  1.00 69.98           H  
ATOM   5502 HG22 ILE A 385      59.112   6.655  10.226  1.00 69.98           H  
ATOM   5503 HG23 ILE A 385      59.577   5.592  11.554  1.00 69.98           H  
ATOM   5504 HD11 ILE A 385      55.574   3.401  12.017  1.00 68.18           H  
ATOM   5505 HD12 ILE A 385      55.381   4.716  10.898  1.00 68.18           H  
ATOM   5506 HD13 ILE A 385      56.771   3.661  10.758  1.00 68.18           H  
ATOM   5507  N   LYS A 386      57.966   9.429  11.202  1.00 67.90           N  
ANISOU 5507  N   LYS A 386    10634   7616   7548   -713   1321   2056
ATOM   5508  CA  LYS A 386      58.560  10.586  10.522  1.00 69.00           C  
ANISOU 5508  CA  LYS A 386    10876   7708   7633   -473   1267   2334
ATOM   5509  C   LYS A 386      59.183  11.592  11.508  1.00 69.45           C  
ANISOU 5509  C   LYS A 386    11148   7454   7784   -227   1308   2453
ATOM   5510  O   LYS A 386      60.256  12.124  11.230  1.00 71.49           O  
ANISOU 5510  O   LYS A 386    11677   7517   7968   -110   1345   2685
ATOM   5511  CB  LYS A 386      57.486  11.266   9.639  1.00 67.66           C  
ANISOU 5511  CB  LYS A 386    10398   7818   7490   -320   1132   2345
ATOM   5512  CG  LYS A 386      58.002  12.391   8.716  1.00 69.05           C  
ANISOU 5512  CG  LYS A 386    10613   8064   7558   -146   1056   2631
ATOM   5513  CD  LYS A 386      56.876  13.336   8.262  1.00 67.50           C  
ANISOU 5513  CD  LYS A 386    10145   8063   7437     79    928   2657
ATOM   5514  CE  LYS A 386      57.365  14.493   7.378  1.00 70.25           C  
ANISOU 5514  CE  LYS A 386    10531   8455   7706    316    852   2972
ATOM   5515  NZ  LYS A 386      57.601  14.061   5.989  1.00 71.70           N1+
ANISOU 5515  NZ  LYS A 386    10591   8931   7721    196    761   3055
ATOM   5516  HG3 LYS A 386      58.501  11.953   7.852  1.00 69.05           H  
ATOM   5517  HG2 LYS A 386      58.752  12.995   9.223  1.00 69.05           H  
ATOM   5518  HD3 LYS A 386      56.412  13.762   9.152  1.00 67.50           H  
ATOM   5519  HD2 LYS A 386      56.089  12.776   7.754  1.00 67.50           H  
ATOM   5520  HE3 LYS A 386      58.273  14.940   7.785  1.00 70.25           H  
ATOM   5521  HE2 LYS A 386      56.610  15.279   7.355  1.00 70.25           H  
ATOM   5522  HZ1 LYS A 386      58.321  13.354   5.972  1.00 71.70           H  
ATOM   5523  HZ2 LYS A 386      56.747  13.683   5.605  1.00 71.70           H  
ATOM   5524  HZ3 LYS A 386      57.894  14.852   5.435  1.00 71.70           H  
ATOM   5525  H   LYS A 386      56.987   9.250  11.021  1.00 67.90           H  
ATOM   5526  HA  LYS A 386      59.355  10.207   9.879  1.00 69.00           H  
ATOM   5527  HB3 LYS A 386      56.700  11.658  10.285  1.00 67.66           H  
ATOM   5528  HB2 LYS A 386      57.007  10.518   9.008  1.00 67.66           H  
ATOM   5529  N   GLY A 387      58.534  11.807  12.665  1.00 67.50           N  
ANISOU 5529  N   GLY A 387    10796   7156   7697   -154   1308   2289
ATOM   5530  CA  GLY A 387      58.981  12.695  13.730  1.00 68.26           C  
ANISOU 5530  CA  GLY A 387    11079   6965   7891     69   1360   2357
ATOM   5531  C   GLY A 387      60.225  12.194  14.473  1.00 70.64           C  
ANISOU 5531  C   GLY A 387    11781   6934   8125    -53   1499   2405
ATOM   5532  O   GLY A 387      61.155  12.971  14.673  1.00 72.62           O  
ANISOU 5532  O   GLY A 387    12304   6940   8347    147   1550   2614
ATOM   5533  H   GLY A 387      57.662  11.318  12.814  1.00 67.50           H  
ATOM   5534  HA3 GLY A 387      58.165  12.793  14.443  1.00 68.26           H  
ATOM   5535  HA2 GLY A 387      59.166  13.690  13.324  1.00 68.26           H  
ATOM   5536  N   VAL A 388      60.267  10.901  14.843  1.00 70.51           N  
ANISOU 5536  N   VAL A 388    11804   6911   8075   -385   1564   2214
ATOM   5537  CA  VAL A 388      61.410  10.264  15.516  1.00 72.61           C  
ANISOU 5537  CA  VAL A 388    12454   6883   8253   -580   1697   2233
ATOM   5538  C   VAL A 388      62.635  10.166  14.583  1.00 75.46           C  
ANISOU 5538  C   VAL A 388    13113   7107   8450   -577   1739   2482
ATOM   5539  O   VAL A 388      63.757  10.367  15.047  1.00 77.52           O  
ANISOU 5539  O   VAL A 388    13763   7024   8666   -526   1838   2609
ATOM   5540  CB  VAL A 388      60.991   8.870  16.062  1.00 72.22           C  
ANISOU 5540  CB  VAL A 388    12331   6949   8162   -983   1742   1994
ATOM   5541  CG1 VAL A 388      62.166   8.061  16.656  1.00 73.71           C  
ANISOU 5541  CG1 VAL A 388    12930   6840   8235  -1230   1880   2013
ATOM   5542  CG2 VAL A 388      59.896   9.007  17.135  1.00 69.99           C  
ANISOU 5542  CG2 VAL A 388    11770   6785   8037   -969   1694   1767
ATOM   5543  HB  VAL A 388      60.577   8.286  15.238  1.00 72.22           H  
ATOM   5544 HG11 VAL A 388      61.825   7.127  17.100  1.00 73.71           H  
ATOM   5545 HG12 VAL A 388      62.906   7.790  15.904  1.00 73.71           H  
ATOM   5546 HG13 VAL A 388      62.678   8.625  17.437  1.00 73.71           H  
ATOM   5547 HG21 VAL A 388      59.597   8.032  17.518  1.00 69.99           H  
ATOM   5548 HG22 VAL A 388      60.244   9.603  17.976  1.00 69.99           H  
ATOM   5549 HG23 VAL A 388      59.000   9.494  16.758  1.00 69.99           H  
ATOM   5550  H   VAL A 388      59.464  10.320  14.645  1.00 70.51           H  
ATOM   5551  HA  VAL A 388      61.696  10.892  16.363  1.00 72.61           H  
ATOM   5552  N   PHE A 389      62.426   9.908  13.278  1.00 75.49           N  
ANISOU 5552  N   PHE A 389    12951   7373   8358   -637   1666   2551
ATOM   5553  CA  PHE A 389      63.472   9.894  12.253  1.00 78.06           C  
ANISOU 5553  CA  PHE A 389    13519   7620   8519   -627   1679   2805
ATOM   5554  C   PHE A 389      64.024  11.298  11.955  1.00 79.26           C  
ANISOU 5554  C   PHE A 389    13803   7604   8710   -208   1648   3074
ATOM   5555  O   PHE A 389      65.218  11.420  11.693  1.00 81.43           O  
ANISOU 5555  O   PHE A 389    14452   7594   8894   -140   1719   3278
ATOM   5556  CB  PHE A 389      62.928   9.268  10.947  1.00 77.65           C  
ANISOU 5556  CB  PHE A 389    13219   7926   8357   -781   1598   2802
ATOM   5557  CG  PHE A 389      63.240   7.789  10.796  1.00 78.92           C  
ANISOU 5557  CG  PHE A 389    13462   8153   8371  -1206   1677   2686
ATOM   5558  CD1 PHE A 389      62.394   6.811  11.359  1.00 76.35           C  
ANISOU 5558  CD1 PHE A 389    12916   7999   8095  -1461   1705   2397
ATOM   5559  CD2 PHE A 389      64.393   7.384  10.090  1.00 83.02           C  
ANISOU 5559  CD2 PHE A 389    14279   8570   8695  -1351   1725   2874
ATOM   5560  CE1 PHE A 389      62.685   5.443  11.202  1.00 76.62           C  
ANISOU 5560  CE1 PHE A 389    12996   8127   7989  -1853   1785   2289
ATOM   5561  CE2 PHE A 389      64.688   6.015   9.939  1.00 84.51           C  
ANISOU 5561  CE2 PHE A 389    14542   8836   8733  -1767   1806   2766
ATOM   5562  CZ  PHE A 389      63.831   5.044  10.489  1.00 83.05           C  
ANISOU 5562  CZ  PHE A 389    14105   8848   8601  -2019   1839   2468
ATOM   5563  HE1 PHE A 389      62.032   4.698  11.630  1.00 76.62           H  
ATOM   5564  HE2 PHE A 389      65.570   5.708   9.396  1.00 84.51           H  
ATOM   5565  HZ  PHE A 389      64.053   3.994  10.367  1.00 83.05           H  
ATOM   5566  H   PHE A 389      61.475   9.739  12.972  1.00 75.49           H  
ATOM   5567  HA  PHE A 389      64.307   9.290  12.615  1.00 78.06           H  
ATOM   5568  HB3 PHE A 389      63.353   9.764  10.073  1.00 77.65           H  
ATOM   5569  HB2 PHE A 389      61.852   9.425  10.854  1.00 77.65           H  
ATOM   5570  HD1 PHE A 389      61.522   7.098  11.919  1.00 76.35           H  
ATOM   5571  HD2 PHE A 389      65.056   8.121   9.663  1.00 83.02           H  
ATOM   5572  N   ALA A 390      63.187  12.350  12.026  1.00 77.53           N  
ANISOU 5572  N   ALA A 390    13275   7562   8621     71   1546   3072
ATOM   5573  CA  ALA A 390      63.587  13.743  11.819  1.00 78.38           C  
ANISOU 5573  CA  ALA A 390    13421   7589   8773    489   1504   3322
ATOM   5574  C   ALA A 390      64.442  14.274  12.983  1.00 79.97           C  
ANISOU 5574  C   ALA A 390    13979   7373   9033    666   1632   3381
ATOM   5575  O   ALA A 390      65.406  14.992  12.733  1.00 82.68           O  
ANISOU 5575  O   ALA A 390    14587   7502   9324    909   1668   3639
ATOM   5576  CB  ALA A 390      62.330  14.615  11.674  1.00 75.77           C  
ANISOU 5576  CB  ALA A 390    12683   7541   8567    692   1382   3266
ATOM   5577  HB1 ALA A 390      62.591  15.665  11.538  1.00 75.77           H  
ATOM   5578  HB2 ALA A 390      61.745  14.316  10.803  1.00 75.77           H  
ATOM   5579  HB3 ALA A 390      61.682  14.547  12.548  1.00 75.77           H  
ATOM   5580  H   ALA A 390      62.213  12.177  12.235  1.00 77.53           H  
ATOM   5581  HA  ALA A 390      64.170  13.811  10.899  1.00 78.38           H  
ATOM   5582  N   VAL A 391      64.135  13.873  14.231  1.00 78.35           N  
ANISOU 5582  N   VAL A 391    13793   7052   8926    537   1702   3142
ATOM   5583  CA  VAL A 391      64.928  14.159  15.434  1.00 79.86           C  
ANISOU 5583  CA  VAL A 391    14347   6837   9157    626   1841   3143
ATOM   5584  C   VAL A 391      66.261  13.385  15.414  1.00 83.09           C  
ANISOU 5584  C   VAL A 391    15238   6926   9407    445   1963   3255
ATOM   5585  O   VAL A 391      67.289  13.957  15.768  1.00 85.57           O  
ANISOU 5585  O   VAL A 391    15908   6900   9703    681   2053   3436
ATOM   5586  CB  VAL A 391      64.088  13.821  16.701  1.00 77.69           C  
ANISOU 5586  CB  VAL A 391    13979   6546   8995    452   1878   2849
ATOM   5587  CG1 VAL A 391      64.886  13.773  18.025  1.00 79.44           C  
ANISOU 5587  CG1 VAL A 391    14640   6335   9209    433   2039   2828
ATOM   5588  CG2 VAL A 391      62.940  14.829  16.876  1.00 75.36           C  
ANISOU 5588  CG2 VAL A 391    13307   6466   8862    697   1781   2774
ATOM   5589  HB  VAL A 391      63.646  12.833  16.565  1.00 77.69           H  
ATOM   5590 HG11 VAL A 391      64.228  13.567  18.868  1.00 79.44           H  
ATOM   5591 HG12 VAL A 391      65.647  12.992  18.028  1.00 79.44           H  
ATOM   5592 HG13 VAL A 391      65.378  14.723  18.227  1.00 79.44           H  
ATOM   5593 HG21 VAL A 391      62.347  14.580  17.754  1.00 75.36           H  
ATOM   5594 HG22 VAL A 391      63.323  15.839  17.018  1.00 75.36           H  
ATOM   5595 HG23 VAL A 391      62.272  14.850  16.016  1.00 75.36           H  
ATOM   5596  H   VAL A 391      63.314  13.295  14.351  1.00 78.35           H  
ATOM   5597  HA  VAL A 391      65.167  15.224  15.446  1.00 79.86           H  
ATOM   5598  N   ALA A 392      66.258  12.114  14.976  1.00 83.11           N  
ANISOU 5598  N   ALA A 392    15256   7034   9289     32   1971   3150
ATOM   5599  CA  ALA A 392      67.448  11.265  14.871  1.00 86.14           C  
ANISOU 5599  CA  ALA A 392    16088   7145   9495   -203   2081   3249
ATOM   5600  C   ALA A 392      68.436  11.756  13.800  1.00 89.04           C  
ANISOU 5600  C   ALA A 392    16665   7406   9760     44   2061   3582
ATOM   5601  O   ALA A 392      69.643  11.604  13.978  1.00 92.02           O  
ANISOU 5601  O   ALA A 392    17509   7403  10050     91   2169   3739
ATOM   5602  CB  ALA A 392      67.008   9.834  14.527  1.00 85.45           C  
ANISOU 5602  CB  ALA A 392    15898   7279   9291   -685   2079   3080
ATOM   5603  HB1 ALA A 392      67.864   9.163  14.445  1.00 85.45           H  
ATOM   5604  HB2 ALA A 392      66.353   9.425  15.296  1.00 85.45           H  
ATOM   5605  HB3 ALA A 392      66.469   9.794  13.581  1.00 85.45           H  
ATOM   5606  H   ALA A 392      65.373  11.702  14.709  1.00 83.11           H  
ATOM   5607  HA  ALA A 392      67.959  11.256  15.836  1.00 86.14           H  
ATOM   5608  N   ASP A 393      67.926  12.371  12.718  1.00 88.37           N  
ANISOU 5608  N   ASP A 393    16241   7658   9679    200   1920   3691
ATOM   5609  CA  ASP A 393      68.704  12.963  11.631  1.00 91.00           C  
ANISOU 5609  CA  ASP A 393    16693   7968   9916    452   1867   4020
ATOM   5610  C   ASP A 393      69.260  14.350  12.020  1.00 92.58           C  
ANISOU 5610  C   ASP A 393    17059   7903  10215    946   1904   4220
ATOM   5611  O   ASP A 393      70.372  14.690  11.620  1.00 95.69           O  
ANISOU 5611  O   ASP A 393    17755   8082  10520   1157   1929   4502
ATOM   5612  CB  ASP A 393      67.768  13.076  10.400  1.00 89.45           C  
ANISOU 5612  CB  ASP A 393    16042   8241   9703    475   1698   4054
ATOM   5613  CG  ASP A 393      68.454  13.568   9.123  1.00 92.75           C  
ANISOU 5613  CG  ASP A 393    16559   8701   9979    640   1626   4389
ATOM   5614  OD1 ASP A 393      69.280  12.794   8.591  1.00 95.44           O  
ANISOU 5614  OD1 ASP A 393    17168   8953  10142    393   1664   4480
ATOM   5615  OD2 ASP A 393      68.129  14.696   8.695  1.00 94.27           O1-
ANISOU 5615  OD2 ASP A 393    16549   9038  10229   1007   1525   4567
ATOM   5616  HA  ASP A 393      69.540  12.302  11.390  1.00 91.00           H  
ATOM   5617  HB3 ASP A 393      66.922  13.728  10.625  1.00 89.45           H  
ATOM   5618  HB2 ASP A 393      67.343  12.099  10.176  1.00 89.45           H  
ATOM   5619  H   ASP A 393      66.921  12.431  12.640  1.00 88.37           H  
ATOM   5620  N   GLU A 394      68.502  15.133  12.810  1.00 90.63           N  
ANISOU 5620  N   GLU A 394    16613   7676  10147   1134   1909   4074
ATOM   5621  CA  GLU A 394      68.845  16.495  13.225  1.00 91.85           C  
ANISOU 5621  CA  GLU A 394    16846   7645  10409   1618   1944   4235
ATOM   5622  C   GLU A 394      69.877  16.500  14.368  1.00 94.18           C  
ANISOU 5622  C   GLU A 394    17660   7423  10703   1659   2135   4227
ATOM   5623  O   GLU A 394      70.909  17.158  14.249  1.00 97.38           O  
ANISOU 5623  O   GLU A 394    18396   7537  11068   1962   2204   4476
ATOM   5624  CB  GLU A 394      67.546  17.216  13.657  1.00 88.54           C  
ANISOU 5624  CB  GLU A 394    15983   7491  10166   1785   1868   4081
ATOM   5625  CG  GLU A 394      67.734  18.668  14.155  1.00 90.31           C  
ANISOU 5625  CG  GLU A 394    16115   7717  10480   2306   1846   4294
ATOM   5626  CD  GLU A 394      66.431  19.379  14.536  1.00 89.77           C  
ANISOU 5626  CD  GLU A 394    15660   7867  10580   2434   1796   4119
ATOM   5627  OE1 GLU A 394      65.346  18.776  14.380  1.00 85.78           O  
ANISOU 5627  OE1 GLU A 394    14819   7666  10108   2171   1699   3905
ATOM   5628  OE2 GLU A 394      66.545  20.531  15.010  1.00 92.11           O1-
ANISOU 5628  OE2 GLU A 394    15998   8026  10972   2806   1859   4199
ATOM   5629  HB2 GLU A 394      66.864  17.229  12.806  1.00 88.54           H  
ATOM   5630  HG3 GLU A 394      68.235  19.259  13.389  1.00 90.31           H  
ATOM   5631  HG2 GLU A 394      68.376  18.689  15.037  1.00 90.31           H  
ATOM   5632  H   GLU A 394      67.594  14.787  13.087  1.00 90.63           H  
ATOM   5633  HA  GLU A 394      69.268  17.027  12.372  1.00 91.85           H  
ATOM   5634  HB3 GLU A 394      67.047  16.635  14.433  1.00 88.54           H  
ATOM   5635  N   TYR A 395      69.611  15.762  15.459  1.00 92.79           N  
ANISOU 5635  N   TYR A 395    17557   7135  10565   1356   2219   3943
ATOM   5636  CA  TYR A 395      70.487  15.661  16.631  1.00 94.83           C  
ANISOU 5636  CA  TYR A 395    18320   6909  10802   1313   2405   3894
ATOM   5637  C   TYR A 395      71.537  14.538  16.490  1.00 97.36           C  
ANISOU 5637  C   TYR A 395    19076   6989  10926    941   2489   3932
ATOM   5638  O   TYR A 395      72.404  14.425  17.356  1.00 99.32           O  
ANISOU 5638  O   TYR A 395    19778   6840  11120    799   2645   3869
ATOM   5639  CB  TYR A 395      69.630  15.395  17.885  1.00 92.34           C  
ANISOU 5639  CB  TYR A 395    17890   6595  10601   1141   2451   3580
ATOM   5640  CG  TYR A 395      68.796  16.589  18.326  1.00 90.24           C  
ANISOU 5640  CG  TYR A 395    17295   6472  10519   1509   2405   3541
ATOM   5641  CD1 TYR A 395      69.352  17.564  19.181  1.00 91.73           C  
ANISOU 5641  CD1 TYR A 395    17732   6345  10778   1890   2526   3628
ATOM   5642  CD2 TYR A 395      67.468  16.735  17.879  1.00 86.41           C  
ANISOU 5642  CD2 TYR A 395    16269   6434  10129   1470   2251   3413
ATOM   5643  CE1 TYR A 395      68.584  18.674  19.585  1.00 90.15           C  
ANISOU 5643  CE1 TYR A 395    17221   6297  10735   2214   2490   3592
ATOM   5644  CE2 TYR A 395      66.697  17.839  18.285  1.00 85.81           C  
ANISOU 5644  CE2 TYR A 395    15901   6496  10206   1777   2208   3378
ATOM   5645  CZ  TYR A 395      67.255  18.813  19.136  1.00 88.03           C  
ANISOU 5645  CZ  TYR A 395    16411   6485  10553   2143   2326   3468
ATOM   5646  OH  TYR A 395      66.503  19.880  19.536  1.00 86.28           O  
ANISOU 5646  OH  TYR A 395    15879   6430  10473   2426   2286   3428
ATOM   5647  HB2 TYR A 395      68.981  14.532  17.736  1.00 92.34           H  
ATOM   5648  HD1 TYR A 395      70.369  17.463  19.532  1.00 91.73           H  
ATOM   5649  HD2 TYR A 395      67.034  16.007  17.213  1.00 86.41           H  
ATOM   5650  HE1 TYR A 395      69.017  19.412  20.245  1.00 90.15           H  
ATOM   5651  HE2 TYR A 395      65.680  17.933  17.933  1.00 85.81           H  
ATOM   5652  HH  TYR A 395      66.977  20.460  20.115  1.00 86.28           H  
ATOM   5653  H   TYR A 395      68.744  15.239  15.484  1.00 92.79           H  
ATOM   5654  HA  TYR A 395      71.031  16.596  16.773  1.00 94.83           H  
ATOM   5655  HB3 TYR A 395      70.274  15.132  18.726  1.00 92.34           H  
ATOM   5656  N   ASN A 396      71.489  13.747  15.399  1.00 97.29           N  
ANISOU 5656  N   ASN A 396    18935   7232  10799    760   2388   4029
ATOM   5657  CA  ASN A 396      72.530  12.824  14.926  1.00100.17           C  
ANISOU 5657  CA  ASN A 396    19712   7393  10956    462   2453   4135
ATOM   5658  C   ASN A 396      72.787  11.687  15.938  1.00100.41           C  
ANISOU 5658  C   ASN A 396    20031   7215  10904    -21   2582   3900
ATOM   5659  O   ASN A 396      73.912  11.508  16.404  1.00103.44           O  
ANISOU 5659  O   ASN A 396    20966   7163  11174   -104   2724   3978
ATOM   5660  CB  ASN A 396      73.806  13.627  14.540  1.00104.08           C  
ANISOU 5660  CB  ASN A 396    20649   7512  11384    834   2517   4471
ATOM   5661  CG  ASN A 396      74.842  12.904  13.662  1.00107.58           C  
ANISOU 5661  CG  ASN A 396    21462   7812  11602    572   2542   4640
ATOM   5662  OD1 ASN A 396      75.919  13.446  13.430  1.00108.38           O  
ANISOU 5662  OD1 ASN A 396    21505   8087  11588     90   2527   4496
ATOM   5663  ND2 ASN A 396      74.552  11.700  13.160  1.00111.98           N  
ANISOU 5663  ND2 ASN A 396    22410   8050  12089    892   2586   4951
ATOM   5664  H   ASN A 396      70.719  13.902  14.765  1.00 97.29           H  
ATOM   5665  HA  ASN A 396      72.120  12.372  14.023  1.00100.17           H  
ATOM   5666  HB3 ASN A 396      74.313  13.995  15.434  1.00104.08           H  
ATOM   5667  HB2 ASN A 396      73.506  14.518  13.984  1.00104.08           H  
ATOM   5668 HD22 ASN A 396      75.233  11.228  12.583  1.00111.98           H  
ATOM   5669 HD21 ASN A 396      73.662  11.267  13.355  1.00111.98           H  
ATOM   5670  N   VAL A 397      71.731  10.944  16.304  1.00 97.26           N  
ANISOU 5670  N   VAL A 397    19264   7133  10557   -340   2533   3617
ATOM   5671  CA  VAL A 397      71.777   9.894  17.323  1.00 97.28           C  
ANISOU 5671  CA  VAL A 397    19461   7019  10484   -818   2637   3381
ATOM   5672  C   VAL A 397      70.795   8.752  16.991  1.00 94.48           C  
ANISOU 5672  C   VAL A 397    18678   7111  10107  -1236   2556   3147
ATOM   5673  O   VAL A 397      70.039   8.841  16.023  1.00 92.61           O  
ANISOU 5673  O   VAL A 397    18011   7259   9916  -1153   2425   3157
ATOM   5674  CB  VAL A 397      71.676  10.539  18.738  1.00 97.29           C  
ANISOU 5674  CB  VAL A 397    19656   6715  10595   -707   2746   3247
ATOM   5675  CG1 VAL A 397      70.235  10.889  19.152  1.00 92.28           C  
ANISOU 5675  CG1 VAL A 397    18510   6407  10145   -674   2658   3007
ATOM   5676  CG2 VAL A 397      72.392   9.712  19.816  1.00100.47           C  
ANISOU 5676  CG2 VAL A 397    20586   6754  10836  -1127   2908   3157
ATOM   5677  HB  VAL A 397      72.218  11.484  18.712  1.00 97.29           H  
ATOM   5678 HG11 VAL A 397      70.219  11.414  20.107  1.00 92.28           H  
ATOM   5679 HG12 VAL A 397      69.763  11.540  18.415  1.00 92.28           H  
ATOM   5680 HG13 VAL A 397      69.612  10.001  19.253  1.00 92.28           H  
ATOM   5681 HG21 VAL A 397      72.362  10.215  20.783  1.00100.47           H  
ATOM   5682 HG22 VAL A 397      71.931   8.737  19.942  1.00100.47           H  
ATOM   5683 HG23 VAL A 397      73.441   9.552  19.563  1.00100.47           H  
ATOM   5684  H   VAL A 397      70.838  11.122  15.862  1.00 97.26           H  
ATOM   5685  HA  VAL A 397      72.759   9.425  17.246  1.00 97.28           H  
ATOM   5686  N   THR A 398      70.825   7.674  17.797  1.00 94.59           N  
ANISOU 5686  N   THR A 398    18825   7074  10040  -1683   2641   2945
ATOM   5687  CA  THR A 398      70.037   6.439  17.648  1.00 92.79           C  
ANISOU 5687  CA  THR A 398    18233   7248   9774  -2098   2590   2723
ATOM   5688  C   THR A 398      68.528   6.734  17.768  1.00 88.89           C  
ANISOU 5688  C   THR A 398    17154   7144   9474  -1940   2463   2555
ATOM   5689  O   THR A 398      68.137   7.669  18.468  1.00 87.46           O  
ANISOU 5689  O   THR A 398    16877   6892   9461  -1614   2437   2533
ATOM   5690  CB  THR A 398      70.440   5.402  18.743  1.00 93.73           C  
ANISOU 5690  CB  THR A 398    18553   7248   9812  -2545   2698   2517
ATOM   5691  OG1 THR A 398      71.829   5.426  19.020  1.00 97.95           O  
ANISOU 5691  OG1 THR A 398    19708   7277  10231  -2577   2839   2639
ATOM   5692  CG2 THR A 398      70.084   3.953  18.376  1.00 93.80           C  
ANISOU 5692  CG2 THR A 398    18382   7585   9673  -3044   2692   2391
ATOM   5693  H   THR A 398      71.479   7.692  18.564  1.00 94.59           H  
ATOM   5694  HA  THR A 398      70.254   6.033  16.658  1.00 92.79           H  
ATOM   5695  HB  THR A 398      69.929   5.618  19.677  1.00 93.73           H  
ATOM   5696  HG1 THR A 398      72.020   6.154  19.594  1.00 97.95           H  
ATOM   5697 HG21 THR A 398      70.406   3.262  19.157  1.00 93.80           H  
ATOM   5698 HG22 THR A 398      69.010   3.815  18.254  1.00 93.80           H  
ATOM   5699 HG23 THR A 398      70.567   3.647  17.449  1.00 93.80           H  
ATOM   5700  N   LEU A 399      67.687   5.905  17.125  1.00 87.25           N  
ANISOU 5700  N   LEU A 399    16573   7345   9235  -2185   2393   2429
ATOM   5701  CA  LEU A 399      66.223   5.975  17.187  1.00 83.60           C  
ANISOU 5701  CA  LEU A 399    15581   7247   8936  -2102   2284   2242
ATOM   5702  C   LEU A 399      65.660   5.799  18.610  1.00 82.31           C  
ANISOU 5702  C   LEU A 399    15369   7026   8879  -2193   2315   2024
ATOM   5703  O   LEU A 399      64.635   6.408  18.914  1.00 80.12           O  
ANISOU 5703  O   LEU A 399    14812   6850   8778  -1938   2238   1944
ATOM   5704  CB  LEU A 399      65.598   4.915  16.259  1.00 82.79           C  
ANISOU 5704  CB  LEU A 399    15140   7561   8756  -2380   2234   2134
ATOM   5705  CG  LEU A 399      65.796   5.139  14.746  1.00 83.58           C  
ANISOU 5705  CG  LEU A 399    15168   7816   8775  -2262   2169   2319
ATOM   5706  CD1 LEU A 399      65.462   3.855  13.970  1.00 84.43           C  
ANISOU 5706  CD1 LEU A 399    15092   8249   8740  -2639   2178   2217
ATOM   5707  CD2 LEU A 399      64.948   6.308  14.215  1.00 81.26           C  
ANISOU 5707  CD2 LEU A 399    14536   7699   8639  -1854   2038   2364
ATOM   5708  H   LEU A 399      68.083   5.165  16.565  1.00 87.25           H  
ATOM   5709  HA  LEU A 399      65.925   6.963  16.840  1.00 83.60           H  
ATOM   5710  HB3 LEU A 399      64.526   4.836  16.450  1.00 82.79           H  
ATOM   5711  HB2 LEU A 399      66.020   3.955  16.536  1.00 82.79           H  
ATOM   5712  HG  LEU A 399      66.845   5.368  14.558  1.00 83.58           H  
ATOM   5713 HD11 LEU A 399      65.546   4.010  12.896  1.00 84.43           H  
ATOM   5714 HD12 LEU A 399      66.137   3.041  14.237  1.00 84.43           H  
ATOM   5715 HD13 LEU A 399      64.443   3.525  14.173  1.00 84.43           H  
ATOM   5716 HD21 LEU A 399      65.115   6.458  13.148  1.00 81.26           H  
ATOM   5717 HD22 LEU A 399      63.883   6.125  14.355  1.00 81.26           H  
ATOM   5718 HD23 LEU A 399      65.193   7.247  14.709  1.00 81.26           H  
ATOM   5719  N   ARG A 400      66.335   5.021  19.487  1.00 83.80           N  
ANISOU 5719  N   ARG A 400    15836   7057   8948  -2569   2423   1935
ATOM   5720  CA  ARG A 400      66.003   4.885  20.908  1.00 82.74           C  
ANISOU 5720  CA  ARG A 400    15666   6883   8886  -2703   2448   1733
ATOM   5721  C   ARG A 400      66.114   6.221  21.648  1.00 82.75           C  
ANISOU 5721  C   ARG A 400    15863   6562   9014  -2340   2472   1792
ATOM   5722  O   ARG A 400      65.172   6.625  22.322  1.00 80.66           O  
ANISOU 5722  O   ARG A 400    15346   6397   8903  -2208   2415   1657
ATOM   5723  NH1 ARG A 400      64.675   1.173  23.590  1.00 85.32           N  
ANISOU 5723  NH1 ARG A 400    15481   7913   9025  -4080   2494   1041
ATOM   5724  NH2 ARG A 400      65.809  -0.583  22.645  1.00 85.84           N1+
ANISOU 5724  NH2 ARG A 400    15784   8090   8742  -4692   2618   1108
ATOM   5725  CB  ARG A 400      66.875   3.810  21.603  1.00 85.11           C  
ANISOU 5725  CB  ARG A 400    16270   7061   9006  -3194   2563   1648
ATOM   5726  CG  ARG A 400      66.574   3.696  23.120  1.00 84.62           C  
ANISOU 5726  CG  ARG A 400    16215   6934   9001  -3333   2588   1460
ATOM   5727  CD  ARG A 400      67.295   2.567  23.865  1.00 87.87           C  
ANISOU 5727  CD  ARG A 400    16920   7250   9217  -3859   2696   1371
ATOM   5728  NE  ARG A 400      67.021   1.243  23.307  1.00 89.08           N  
ANISOU 5728  NE  ARG A 400    16868   7747   9232  -4246   2689   1311
ATOM   5729  CZ  ARG A 400      65.833   0.630  23.186  1.00 86.70           C  
ANISOU 5729  CZ  ARG A 400    16036   7910   8995  -4341   2599   1152
ATOM   5730  H   ARG A 400      67.163   4.547  19.157  1.00 83.80           H  
ATOM   5731  HA  ARG A 400      64.966   4.567  20.984  1.00 82.74           H  
ATOM   5732  HB3 ARG A 400      67.934   4.026  21.457  1.00 85.11           H  
ATOM   5733  HB2 ARG A 400      66.691   2.850  21.120  1.00 85.11           H  
ATOM   5734  HG3 ARG A 400      65.499   3.614  23.264  1.00 84.62           H  
ATOM   5735  HG2 ARG A 400      66.860   4.618  23.624  1.00 84.62           H  
ATOM   5736  HD3 ARG A 400      67.008   2.566  24.916  1.00 87.87           H  
ATOM   5737  HD2 ARG A 400      68.373   2.731  23.833  1.00 87.87           H  
ATOM   5738  HE  ARG A 400      67.855   0.712  23.067  1.00 89.08           H  
ATOM   5739 HH12 ARG A 400      63.809   0.657  23.499  1.00 85.32           H  
ATOM   5740 HH11 ARG A 400      64.661   2.085  24.019  1.00 85.32           H  
ATOM   5741 HH22 ARG A 400      64.923  -1.066  22.507  1.00 85.84           H  
ATOM   5742 HH21 ARG A 400      66.668  -1.072  22.423  1.00 85.84           H  
ATOM   5743  N   GLU A 401      67.257   6.906  21.522  1.00 85.36           N  
ANISOU 5743  N   GLU A 401    16647   6508   9280  -2166   2560   1996
ATOM   5744  CA  GLU A 401      67.516   8.176  22.196  1.00 85.64           C  
ANISOU 5744  CA  GLU A 401    16867   6239   9433  -1783   2599   2060
ATOM   5745  C   GLU A 401      66.656   9.299  21.582  1.00 83.53           C  
ANISOU 5745  C   GLU A 401    16248   6153   9337  -1301   2480   2156
ATOM   5746  O   GLU A 401      66.253  10.208  22.301  1.00 82.72           O  
ANISOU 5746  O   GLU A 401    16134   5928   9367   -994   2486   2151
ATOM   5747  CB  GLU A 401      69.026   8.546  22.163  1.00 89.09           C  
ANISOU 5747  CB  GLU A 401    17945   6160   9746  -1751   2756   2223
ATOM   5748  CG  GLU A 401      70.009   7.393  21.829  1.00 93.39           C  
ANISOU 5748  CG  GLU A 401    18790   6606  10089  -1966   2806   2382
ATOM   5749  CD  GLU A 401      71.329   7.400  22.597  1.00100.39           C  
ANISOU 5749  CD  GLU A 401    20288   7065  10790  -2295   2975   2381
ATOM   5750  OE1 GLU A 401      71.283   7.612  23.828  1.00100.67           O  
ANISOU 5750  OE1 GLU A 401    20434   6982  10833  -2487   3040   2200
ATOM   5751  OE2 GLU A 401      72.360   7.145  21.937  1.00100.72           O1-
ANISOU 5751  OE2 GLU A 401    20714   6887  10667  -2375   3040   2565
ATOM   5752  HB2 GLU A 401      69.207   9.344  21.443  1.00 89.09           H  
ATOM   5753  HG3 GLU A 401      70.212   7.427  20.762  1.00 93.39           H  
ATOM   5754  HG2 GLU A 401      69.593   6.412  22.051  1.00 93.39           H  
ATOM   5755  H   GLU A 401      67.991   6.529  20.940  1.00 85.36           H  
ATOM   5756  HA  GLU A 401      67.226   8.058  23.241  1.00 85.64           H  
ATOM   5757  HB3 GLU A 401      69.270   8.992  23.126  1.00 89.09           H  
ATOM   5758  N   ALA A 402      66.322   9.189  20.282  1.00 82.72           N  
ANISOU 5758  N   ALA A 402    15844   6364   9221  -1266   2374   2229
ATOM   5759  CA  ALA A 402      65.519  10.140  19.524  1.00 80.49           C  
ANISOU 5759  CA  ALA A 402    15191   6316   9078   -875   2246   2309
ATOM   5760  C   ALA A 402      64.016  10.082  19.847  1.00 77.12           C  
ANISOU 5760  C   ALA A 402    14297   6201   8804   -867   2143   2091
ATOM   5761  O   ALA A 402      63.386  11.133  19.781  1.00 75.54           O  
ANISOU 5761  O   ALA A 402    13911   6046   8744   -532   2081   2114
ATOM   5762  CB  ALA A 402      65.690   9.859  18.025  1.00 80.76           C  
ANISOU 5762  CB  ALA A 402    15093   6571   9021   -868   2171   2461
ATOM   5763  HB1 ALA A 402      65.168  10.605  17.423  1.00 80.76           H  
ATOM   5764  HB2 ALA A 402      66.741   9.891  17.738  1.00 80.76           H  
ATOM   5765  HB3 ALA A 402      65.291   8.885  17.749  1.00 80.76           H  
ATOM   5766  H   ALA A 402      66.697   8.403  19.767  1.00 82.72           H  
ATOM   5767  HA  ALA A 402      65.890  11.144  19.729  1.00 80.49           H  
ATOM   5768  N   VAL A 403      63.426   8.919  20.205  1.00 76.13           N  
ANISOU 5768  N   VAL A 403    13976   6302   8648  -1231   2122   1888
ATOM   5769  CA  VAL A 403      61.999   8.833  20.570  1.00 73.13           C  
ANISOU 5769  CA  VAL A 403    13159   6222   8407  -1229   2020   1685
ATOM   5770  C   VAL A 403      61.737   9.432  21.964  1.00 72.49           C  
ANISOU 5770  C   VAL A 403    13132   5965   8444  -1108   2043   1589
ATOM   5771  O   VAL A 403      60.703  10.070  22.159  1.00 70.30           O  
ANISOU 5771  O   VAL A 403    12570   5830   8311   -878   1952   1537
ATOM   5772  CB  VAL A 403      61.443   7.380  20.479  1.00 72.63           C  
ANISOU 5772  CB  VAL A 403    12867   6446   8283  -1628   2001   1491
ATOM   5773  CG1 VAL A 403      62.074   6.366  21.448  1.00 73.94           C  
ANISOU 5773  CG1 VAL A 403    13313   6439   8341  -1999   2113   1394
ATOM   5774  CG2 VAL A 403      59.912   7.341  20.637  1.00 69.39           C  
ANISOU 5774  CG2 VAL A 403    11998   6344   8021  -1561   1884   1310
ATOM   5775  HB  VAL A 403      61.653   7.021  19.471  1.00 72.63           H  
ATOM   5776 HG11 VAL A 403      61.570   5.403  21.387  1.00 73.94           H  
ATOM   5777 HG12 VAL A 403      63.111   6.197  21.184  1.00 73.94           H  
ATOM   5778 HG13 VAL A 403      62.025   6.680  22.490  1.00 73.94           H  
ATOM   5779 HG21 VAL A 403      59.522   6.342  20.461  1.00 69.39           H  
ATOM   5780 HG22 VAL A 403      59.605   7.623  21.644  1.00 69.39           H  
ATOM   5781 HG23 VAL A 403      59.417   8.016  19.938  1.00 69.39           H  
ATOM   5782  H   VAL A 403      63.976   8.071  20.220  1.00 76.13           H  
ATOM   5783  HA  VAL A 403      61.442   9.436  19.853  1.00 73.13           H  
ATOM   5784  N   TYR A 404      62.687   9.277  22.905  1.00 74.46           N  
ANISOU 5784  N   TYR A 404    13771   5900   8619  -1277   2168   1568
ATOM   5785  CA  TYR A 404      62.640   9.904  24.223  1.00 73.88           C  
ANISOU 5785  CA  TYR A 404    13818   5625   8628  -1198   2212   1478
ATOM   5786  C   TYR A 404      62.827  11.422  24.099  1.00 73.89           C  
ANISOU 5786  C   TYR A 404    13894   5455   8727   -732   2220   1635
ATOM   5787  O   TYR A 404      62.097  12.169  24.741  1.00 72.43           O  
ANISOU 5787  O   TYR A 404    13551   5299   8671   -545   2182   1560
ATOM   5788  CB  TYR A 404      63.732   9.305  25.139  1.00 76.57           C  
ANISOU 5788  CB  TYR A 404    14612   5650   8832  -1509   2357   1436
ATOM   5789  CG  TYR A 404      63.469   7.871  25.570  1.00 76.59           C  
ANISOU 5789  CG  TYR A 404    14485   5867   8750  -1984   2342   1250
ATOM   5790  CD1 TYR A 404      62.320   7.564  26.321  1.00 73.15           C  
ANISOU 5790  CD1 TYR A 404    13741   5648   8404  -2093   2266   1049
ATOM   5791  CD2 TYR A 404      64.365   6.836  25.238  1.00 78.35           C  
ANISOU 5791  CD2 TYR A 404    14882   6094   8796  -2326   2402   1283
ATOM   5792  CE1 TYR A 404      62.053   6.246  26.724  1.00 73.49           C  
ANISOU 5792  CE1 TYR A 404    13630   5921   8372  -2505   2246    890
ATOM   5793  CE2 TYR A 404      64.084   5.506  25.604  1.00 78.00           C  
ANISOU 5793  CE2 TYR A 404    14682   6289   8667  -2765   2391   1114
ATOM   5794  CZ  TYR A 404      62.929   5.209  26.352  1.00 77.18           C  
ANISOU 5794  CZ  TYR A 404    14247   6413   8665  -2838   2311    920
ATOM   5795  OH  TYR A 404      62.676   3.921  26.723  1.00 77.70           O  
ANISOU 5795  OH  TYR A 404    14119   6746   8656  -3240   2292    761
ATOM   5796  HB2 TYR A 404      64.708   9.372  24.655  1.00 76.57           H  
ATOM   5797  HD1 TYR A 404      61.637   8.345  26.590  1.00 73.15           H  
ATOM   5798  HD2 TYR A 404      65.275   7.063  24.707  1.00 78.35           H  
ATOM   5799  HE1 TYR A 404      61.169   6.042  27.309  1.00 73.49           H  
ATOM   5800  HE2 TYR A 404      64.767   4.717  25.331  1.00 78.00           H  
ATOM   5801  HH  TYR A 404      61.846   3.811  27.160  1.00 77.70           H  
ATOM   5802  H   TYR A 404      63.507   8.732  22.675  1.00 74.46           H  
ATOM   5803  HA  TYR A 404      61.657   9.728  24.665  1.00 73.88           H  
ATOM   5804  HB3 TYR A 404      63.811   9.897  26.053  1.00 76.57           H  
ATOM   5805  N   MET A 405      63.731  11.879  23.216  1.00 75.76           N  
ANISOU 5805  N   MET A 405    14351   5536   8898   -543   2264   1859
ATOM   5806  CA  MET A 405      63.953  13.291  22.905  1.00 76.10           C  
ANISOU 5806  CA  MET A 405    14429   5461   9025    -73   2267   2039
ATOM   5807  C   MET A 405      62.767  13.929  22.152  1.00 73.56           C  
ANISOU 5807  C   MET A 405    13607   5510   8831    158   2108   2036
ATOM   5808  O   MET A 405      62.471  15.091  22.403  1.00 72.70           O  
ANISOU 5808  O   MET A 405    13394   5393   8838    463   2090   2057
ATOM   5809  SD  MET A 405      68.060  12.961  22.044  1.00 80.75           S  
ANISOU 5809  SD  MET A 405    16358   5123   9200   -140   2598   2552
ATOM   5810  CE  MET A 405      68.211  14.528  21.155  1.00 82.18           C  
ANISOU 5810  CE  MET A 405    16516   5275   9433    433   2559   2870
ATOM   5811  CB  MET A 405      65.249  13.420  22.081  1.00 78.90           C  
ANISOU 5811  CB  MET A 405    15125   5586   9270     74   2340   2297
ATOM   5812  CG  MET A 405      66.511  13.239  22.946  1.00 81.47           C  
ANISOU 5812  CG  MET A 405    16030   5431   9496      6   2524   2339
ATOM   5813  H   MET A 405      64.293  11.204  22.716  1.00 75.76           H  
ATOM   5814  HA  MET A 405      64.076  13.838  23.841  1.00 76.10           H  
ATOM   5815  HB3 MET A 405      65.299  14.398  21.601  1.00 78.90           H  
ATOM   5816  HB2 MET A 405      65.243  12.691  21.273  1.00 78.90           H  
ATOM   5817  HG3 MET A 405      66.384  12.388  23.612  1.00 81.47           H  
ATOM   5818  HG2 MET A 405      66.641  14.095  23.603  1.00 81.47           H  
ATOM   5819  HE1 MET A 405      69.188  14.584  20.680  1.00 82.18           H  
ATOM   5820  HE2 MET A 405      67.441  14.616  20.388  1.00 82.18           H  
ATOM   5821  HE3 MET A 405      68.119  15.369  21.842  1.00 82.18           H  
ATOM   5822  N   TYR A 406      62.052  13.180  21.292  1.00 72.48           N  
ANISOU 5822  N   TYR A 406    13174   5701   8665     -7   2000   2002
ATOM   5823  CA  TYR A 406      60.847  13.626  20.579  1.00 69.93           C  
ANISOU 5823  CA  TYR A 406    12394   5735   8441    145   1849   1974
ATOM   5824  C   TYR A 406      59.668  13.859  21.544  1.00 67.57           C  
ANISOU 5824  C   TYR A 406    11869   5525   8278    162   1801   1777
ATOM   5825  O   TYR A 406      58.930  14.830  21.376  1.00 66.23           O  
ANISOU 5825  O   TYR A 406    11494   5458   8211    439   1732   1811
ATOM   5826  CB  TYR A 406      60.470  12.568  19.515  1.00 69.39           C  
ANISOU 5826  CB  TYR A 406    12103   5965   8298   -110   1772   1920
ATOM   5827  CG  TYR A 406      59.271  12.888  18.632  1.00 67.25           C  
ANISOU 5827  CG  TYR A 406    11420   6046   8086     26   1626   1921
ATOM   5828  CD1 TYR A 406      59.300  14.007  17.773  1.00 68.36           C  
ANISOU 5828  CD1 TYR A 406    11504   6244   8226    330   1570   2133
ATOM   5829  CD2 TYR A 406      58.129  12.060  18.646  1.00 65.84           C  
ANISOU 5829  CD2 TYR A 406    10917   6150   7949   -163   1545   1715
ATOM   5830  CE1 TYR A 406      58.207  14.290  16.931  1.00 67.05           C  
ANISOU 5830  CE1 TYR A 406    10979   6407   8089    412   1436   2131
ATOM   5831  CE2 TYR A 406      57.034  12.343  17.806  1.00 64.96           C  
ANISOU 5831  CE2 TYR A 406    10464   6341   7876    -59   1419   1707
ATOM   5832  CZ  TYR A 406      57.075  13.454  16.943  1.00 65.33           C  
ANISOU 5832  CZ  TYR A 406    10475   6436   7909    211   1365   1911
ATOM   5833  OH  TYR A 406      56.024  13.715  16.111  1.00 63.97           O  
ANISOU 5833  OH  TYR A 406     9987   6561   7756    277   1242   1897
ATOM   5834  HB2 TYR A 406      61.316  12.422  18.844  1.00 69.39           H  
ATOM   5835  HD1 TYR A 406      60.158  14.658  17.753  1.00 68.36           H  
ATOM   5836  HD2 TYR A 406      58.094  11.197  19.295  1.00 65.84           H  
ATOM   5837  HE1 TYR A 406      58.243  15.144  16.272  1.00 67.05           H  
ATOM   5838  HE2 TYR A 406      56.166  11.702  17.819  1.00 64.96           H  
ATOM   5839  HH  TYR A 406      55.331  13.077  16.186  1.00 63.97           H  
ATOM   5840  H   TYR A 406      62.365  12.235  21.114  1.00 72.48           H  
ATOM   5841  HA  TYR A 406      61.077  14.569  20.081  1.00 69.93           H  
ATOM   5842  HB3 TYR A 406      60.306  11.603  19.994  1.00 69.39           H  
ATOM   5843  N   ALA A 407      59.534  13.005  22.572  1.00 67.13           N  
ANISOU 5843  N   ALA A 407    11858   5437   8212   -144   1836   1582
ATOM   5844  CA  ALA A 407      58.528  13.115  23.623  1.00 65.16           C  
ANISOU 5844  CA  ALA A 407    11425   5260   8075   -164   1790   1396
ATOM   5845  C   ALA A 407      58.814  14.303  24.556  1.00 65.92           C  
ANISOU 5845  C   ALA A 407    11713   5096   8237     94   1862   1441
ATOM   5846  O   ALA A 407      57.922  15.128  24.741  1.00 64.31           O  
ANISOU 5846  O   ALA A 407    11283   5007   8145    302   1790   1412
ATOM   5847  CB  ALA A 407      58.499  11.809  24.425  1.00 65.15           C  
ANISOU 5847  CB  ALA A 407    11449   5280   8025   -554   1815   1204
ATOM   5848  HB1 ALA A 407      57.774  11.860  25.239  1.00 65.15           H  
ATOM   5849  HB2 ALA A 407      58.219  10.968  23.790  1.00 65.15           H  
ATOM   5850  HB3 ALA A 407      59.475  11.584  24.855  1.00 65.15           H  
ATOM   5851  H   ALA A 407      60.184  12.233  22.639  1.00 67.13           H  
ATOM   5852  HA  ALA A 407      57.552  13.268  23.158  1.00 65.16           H  
ATOM   5853  N   ILE A 408      60.046  14.432  25.095  1.00 68.34           N  
ANISOU 5853  N   ILE A 408    12449   5050   8466     81   2011   1512
ATOM   5854  CA  ILE A 408      60.463  15.549  25.960  1.00 69.15           C  
ANISOU 5854  CA  ILE A 408    12764   4888   8623    337   2105   1550
ATOM   5855  C   ILE A 408      60.370  16.906  25.244  1.00 69.30           C  
ANISOU 5855  C   ILE A 408    12622   4988   8719    770   2062   1725
ATOM   5856  O   ILE A 408      59.947  17.870  25.876  1.00 68.77           O  
ANISOU 5856  O   ILE A 408    12436   4942   8750    980   2050   1692
ATOM   5857  CB  ILE A 408      61.896  15.323  26.535  1.00 72.03           C  
ANISOU 5857  CB  ILE A 408    13668   4822   8879    269   2292   1605
ATOM   5858  CG1 ILE A 408      62.004  14.078  27.438  1.00 72.78           C  
ANISOU 5858  CG1 ILE A 408    13917   4857   8881   -197   2333   1423
ATOM   5859  CG2 ILE A 408      62.491  16.542  27.281  1.00 71.24           C  
ANISOU 5859  CG2 ILE A 408    13781   4451   8836    565   2403   1635
ATOM   5860  CD1 ILE A 408      61.068  14.047  28.649  1.00 71.83           C  
ANISOU 5860  CD1 ILE A 408    13573   4887   8834   -360   2267   1202
ATOM   5861  H   ILE A 408      60.735  13.719  24.896  1.00 68.34           H  
ATOM   5862  HA  ILE A 408      59.758  15.599  26.790  1.00 69.15           H  
ATOM   5863  HB  ILE A 408      62.555  15.140  25.687  1.00 72.03           H  
ATOM   5864 HG13 ILE A 408      63.029  13.977  27.792  1.00 72.78           H  
ATOM   5865 HG12 ILE A 408      61.808  13.195  26.849  1.00 72.78           H  
ATOM   5866 HG21 ILE A 408      63.477  16.303  27.676  1.00 71.24           H  
ATOM   5867 HG22 ILE A 408      62.630  17.405  26.630  1.00 71.24           H  
ATOM   5868 HG23 ILE A 408      61.862  16.857  28.114  1.00 71.24           H  
ATOM   5869 HD11 ILE A 408      61.282  13.181  29.275  1.00 71.83           H  
ATOM   5870 HD12 ILE A 408      61.209  14.933  29.261  1.00 71.83           H  
ATOM   5871 HD13 ILE A 408      60.020  13.986  28.357  1.00 71.83           H  
ATOM   5872  N   LYS A 409      60.747  16.985  23.955  1.00 70.36           N  
ANISOU 5872  N   LYS A 409    12732   5201   8802    884   2029   1911
ATOM   5873  CA  LYS A 409      60.757  18.222  23.172  1.00 70.86           C  
ANISOU 5873  CA  LYS A 409    12666   5345   8914   1291   1992   2111
ATOM   5874  C   LYS A 409      59.354  18.833  23.019  1.00 68.20           C  
ANISOU 5874  C   LYS A 409    11896   5324   8692   1404   1857   2030
ATOM   5875  O   LYS A 409      59.207  20.031  23.236  1.00 68.24           O  
ANISOU 5875  O   LYS A 409    11851   5306   8771   1697   1877   2083
ATOM   5876  CB  LYS A 409      61.425  17.973  21.803  1.00 72.23           C  
ANISOU 5876  CB  LYS A 409    12825   5620   8997   1339   1945   2315
ATOM   5877  CG  LYS A 409      61.656  19.245  20.966  1.00 73.77           C  
ANISOU 5877  CG  LYS A 409    12985   5830   9213   1772   1937   2566
ATOM   5878  CD  LYS A 409      62.589  19.012  19.767  1.00 75.15           C  
ANISOU 5878  CD  LYS A 409    13247   6031   9274   1814   1913   2794
ATOM   5879  CE  LYS A 409      62.891  20.307  18.996  1.00 77.17           C  
ANISOU 5879  CE  LYS A 409    13460   6312   9550   2267   1903   3060
ATOM   5880  NZ  LYS A 409      63.888  20.092  17.933  1.00 81.30           N1+
ANISOU 5880  NZ  LYS A 409    14234   6707   9951   2352   1933   3313
ATOM   5881  HG3 LYS A 409      62.093  20.013  21.607  1.00 73.77           H  
ATOM   5882  HG2 LYS A 409      60.702  19.642  20.616  1.00 73.77           H  
ATOM   5883  HD3 LYS A 409      62.147  18.276  19.095  1.00 75.15           H  
ATOM   5884  HD2 LYS A 409      63.528  18.580  20.119  1.00 75.15           H  
ATOM   5885  HE3 LYS A 409      63.276  21.069  19.675  1.00 77.17           H  
ATOM   5886  HE2 LYS A 409      61.977  20.703  18.552  1.00 77.17           H  
ATOM   5887  HZ1 LYS A 409      64.768  19.811  18.346  1.00 81.30           H  
ATOM   5888  HZ2 LYS A 409      63.571  19.376  17.295  1.00 81.30           H  
ATOM   5889  HZ3 LYS A 409      64.032  20.949  17.417  1.00 81.30           H  
ATOM   5890  H   LYS A 409      61.090  16.149  23.502  1.00 70.36           H  
ATOM   5891  HA  LYS A 409      61.373  18.936  23.721  1.00 70.86           H  
ATOM   5892  HB3 LYS A 409      60.864  17.238  21.224  1.00 72.23           H  
ATOM   5893  HB2 LYS A 409      62.406  17.536  21.989  1.00 72.23           H  
ATOM   5894  N   SER A 410      58.322  18.028  22.710  1.00 65.92           N  
ANISOU 5894  N   SER A 410    11307   5325   8413   1172   1728   1898
ATOM   5895  CA  SER A 410      56.937  18.492  22.575  1.00 63.28           C  
ANISOU 5895  CA  SER A 410    10590   5276   8177   1255   1597   1817
ATOM   5896  C   SER A 410      56.262  18.791  23.932  1.00 61.91           C  
ANISOU 5896  C   SER A 410    10413   5022   8089   1216   1620   1638
ATOM   5897  O   SER A 410      55.440  19.708  23.998  1.00 61.43           O  
ANISOU 5897  O   SER A 410    10173   5064   8105   1417   1574   1643
ATOM   5898  CB  SER A 410      56.142  17.447  21.762  1.00 61.47           C  
ANISOU 5898  CB  SER A 410    10050   5375   7932   1068   1455   1744
ATOM   5899  OG  SER A 410      55.990  16.216  22.438  1.00 62.39           O  
ANISOU 5899  OG  SER A 410    10243   5470   7993    734   1478   1611
ATOM   5900  H   SER A 410      58.496  17.041  22.570  1.00 65.92           H  
ATOM   5901  HA  SER A 410      56.946  19.419  21.998  1.00 63.28           H  
ATOM   5902  HB3 SER A 410      56.635  17.260  20.808  1.00 61.47           H  
ATOM   5903  HB2 SER A 410      55.149  17.833  21.527  1.00 61.47           H  
ATOM   5904  HG  SER A 410      55.591  15.593  21.849  1.00 62.39           H  
ATOM   5905  N   ILE A 411      56.640  18.086  25.016  1.00 61.93           N  
ANISOU 5905  N   ILE A 411    10619   4848   8065    955   1693   1490
ATOM   5906  CA  ILE A 411      56.187  18.358  26.388  1.00 61.15           C  
ANISOU 5906  CA  ILE A 411    10564   4643   8028    919   1726   1337
ATOM   5907  C   ILE A 411      56.806  19.666  26.920  1.00 62.37           C  
ANISOU 5907  C   ILE A 411    10914   4576   8210   1235   1843   1444
ATOM   5908  O   ILE A 411      56.129  20.405  27.634  1.00 60.86           O  
ANISOU 5908  O   ILE A 411    10620   4413   8090   1344   1831   1374
ATOM   5909  CB  ILE A 411      56.535  17.156  27.317  1.00 61.88           C  
ANISOU 5909  CB  ILE A 411    10880   4571   8061    569   1796   1180
ATOM   5910  CG1 ILE A 411      55.743  15.889  26.919  1.00 60.84           C  
ANISOU 5910  CG1 ILE A 411    10492   4704   7920    274   1677   1047
ATOM   5911  CG2 ILE A 411      56.296  17.457  28.814  1.00 61.32           C  
ANISOU 5911  CG2 ILE A 411    10900   4365   8034    544   1842   1045
ATOM   5912  CD1 ILE A 411      56.348  14.592  27.475  1.00 63.20           C  
ANISOU 5912  CD1 ILE A 411    11005   4885   8123    -86   1749    946
ATOM   5913  H   ILE A 411      57.305  17.334  24.887  1.00 61.93           H  
ATOM   5914  HA  ILE A 411      55.107  18.492  26.377  1.00 61.15           H  
ATOM   5915  HB  ILE A 411      57.599  16.940  27.193  1.00 61.88           H  
ATOM   5916 HG13 ILE A 411      55.684  15.794  25.835  1.00 60.84           H  
ATOM   5917 HG12 ILE A 411      54.710  15.981  27.254  1.00 60.84           H  
ATOM   5918 HG21 ILE A 411      56.452  16.571  29.422  1.00 61.32           H  
ATOM   5919 HG22 ILE A 411      56.975  18.216  29.203  1.00 61.32           H  
ATOM   5920 HG23 ILE A 411      55.275  17.796  28.991  1.00 61.32           H  
ATOM   5921 HD11 ILE A 411      55.785  13.725  27.130  1.00 63.20           H  
ATOM   5922 HD12 ILE A 411      57.384  14.459  27.171  1.00 63.20           H  
ATOM   5923 HD13 ILE A 411      56.335  14.589  28.560  1.00 63.20           H  
ATOM   5924  N   ASP A 412      58.066  19.958  26.557  1.00 64.80           N  
ANISOU 5924  N   ASP A 412    11501   4665   8453   1392   1958   1619
ATOM   5925  CA  ASP A 412      58.811  21.156  26.936  1.00 66.83           C  
ANISOU 5925  CA  ASP A 412    11953   4707   8733   1732   2085   1737
ATOM   5926  C   ASP A 412      58.159  22.448  26.399  1.00 66.03           C  
ANISOU 5926  C   ASP A 412    11517   4856   8713   2053   2002   1830
ATOM   5927  O   ASP A 412      58.019  23.408  27.158  1.00 65.68           O  
ANISOU 5927  O   ASP A 412    11455   4772   8728   2216   2051   1787
ATOM   5928  CB  ASP A 412      60.287  20.989  26.485  1.00 69.65           C  
ANISOU 5928  CB  ASP A 412    12653   4803   9006   1875   2210   1933
ATOM   5929  CG  ASP A 412      61.159  22.236  26.633  1.00 72.96           C  
ANISOU 5929  CG  ASP A 412    13272   4997   9453   2270   2354   2061
ATOM   5930  OD1 ASP A 412      60.989  22.917  27.664  1.00 72.37           O  
ANISOU 5930  OD1 ASP A 412    13263   4811   9424   2308   2430   1937
ATOM   5931  OD2 ASP A 412      61.976  22.491  25.724  1.00 77.95           O1-
ANISOU 5931  OD2 ASP A 412    13996   5567  10056   2552   2395   2289
ATOM   5932  HA  ASP A 412      58.798  21.217  28.027  1.00 66.83           H  
ATOM   5933  HB3 ASP A 412      60.325  20.680  25.442  1.00 69.65           H  
ATOM   5934  HB2 ASP A 412      60.756  20.188  27.057  1.00 69.65           H  
ATOM   5935  H   ASP A 412      58.561  19.283  25.990  1.00 64.80           H  
ATOM   5936  N   VAL A 413      57.725  22.457  25.122  1.00 65.71           N  
ANISOU 5936  N   VAL A 413    11220   5085   8664   2123   1878   1957
ATOM   5937  CA  VAL A 413      57.029  23.589  24.493  1.00 64.64           C  
ANISOU 5937  CA  VAL A 413    10743   5235   8582   2382   1779   2056
ATOM   5938  C   VAL A 413      55.705  23.895  25.214  1.00 62.12           C  
ANISOU 5938  C   VAL A 413    10199   5061   8344   2311   1711   1874
ATOM   5939  O   VAL A 413      55.424  25.061  25.480  1.00 62.97           O  
ANISOU 5939  O   VAL A 413    10241   5187   8497   2553   1750   1913
ATOM   5940  CB  VAL A 413      56.797  23.344  22.972  1.00 63.60           C  
ANISOU 5940  CB  VAL A 413    10339   5414   8412   2359   1626   2168
ATOM   5941  CG1 VAL A 413      56.057  24.509  22.282  1.00 64.16           C  
ANISOU 5941  CG1 VAL A 413    10125   5742   8513   2653   1553   2313
ATOM   5942  CG2 VAL A 413      58.111  23.106  22.212  1.00 66.96           C  
ANISOU 5942  CG2 VAL A 413    10995   5702   8745   2379   1681   2337
ATOM   5943  HB  VAL A 413      56.186  22.448  22.856  1.00 63.60           H  
ATOM   5944 HG11 VAL A 413      55.970  24.343  21.208  1.00 64.16           H  
ATOM   5945 HG12 VAL A 413      55.045  24.630  22.659  1.00 64.16           H  
ATOM   5946 HG13 VAL A 413      56.584  25.453  22.429  1.00 64.16           H  
ATOM   5947 HG21 VAL A 413      57.924  22.906  21.156  1.00 66.96           H  
ATOM   5948 HG22 VAL A 413      58.763  23.978  22.276  1.00 66.96           H  
ATOM   5949 HG23 VAL A 413      58.667  22.266  22.607  1.00 66.96           H  
ATOM   5950  H   VAL A 413      57.875  21.631  24.559  1.00 65.71           H  
ATOM   5951  HA  VAL A 413      57.673  24.464  24.601  1.00 64.64           H  
ATOM   5952  N   ALA A 414      54.933  22.855  25.575  1.00 59.36           N  
ANISOU 5952  N   ALA A 414     9744   4805   8006   1989   1619   1681
ATOM   5953  CA  ALA A 414      53.665  22.968  26.293  1.00 56.97           C  
ANISOU 5953  CA  ALA A 414     9231   4642   7774   1900   1536   1510
ATOM   5954  C   ALA A 414      53.838  23.509  27.723  1.00 57.33           C  
ANISOU 5954  C   ALA A 414     9464   4469   7851   1960   1656   1425
ATOM   5955  O   ALA A 414      53.035  24.336  28.147  1.00 56.47           O  
ANISOU 5955  O   ALA A 414     9195   4471   7791   2102   1631   1413
ATOM   5956  CB  ALA A 414      52.994  21.589  26.335  1.00 55.15           C  
ANISOU 5956  CB  ALA A 414     8880   4528   7545   1565   1426   1331
ATOM   5957  HB1 ALA A 414      52.008  21.655  26.793  1.00 55.15           H  
ATOM   5958  HB2 ALA A 414      52.856  21.189  25.330  1.00 55.15           H  
ATOM   5959  HB3 ALA A 414      53.578  20.864  26.903  1.00 55.15           H  
ATOM   5960  H   ALA A 414      55.246  21.925  25.336  1.00 59.36           H  
ATOM   5961  HA  ALA A 414      53.021  23.653  25.737  1.00 56.97           H  
ATOM   5962  N   MET A 415      54.904  23.102  28.437  1.00 58.78           N  
ANISOU 5962  N   MET A 415     9995   4346   7992   1838   1791   1367
ATOM   5963  CA  MET A 415      55.250  23.593  29.773  1.00 59.76           C  
ANISOU 5963  CA  MET A 415    10354   4228   8124   1890   1930   1291
ATOM   5964  C   MET A 415      55.652  25.080  29.765  1.00 61.57           C  
ANISOU 5964  C   MET A 415    10597   4420   8377   2289   2029   1445
ATOM   5965  O   MET A 415      55.222  25.815  30.653  1.00 61.34           O  
ANISOU 5965  O   MET A 415    10505   4413   8387   2381   2056   1378
ATOM   5966  SD  MET A 415      57.213  20.459  31.787  1.00 62.73           S  
ANISOU 5966  SD  MET A 415    11649   3912   8274   1031   2173   1008
ATOM   5967  CE  MET A 415      56.175  19.293  32.704  1.00 64.08           C  
ANISOU 5967  CE  MET A 415    11660   4242   8446    612   2051    766
ATOM   5968  CB  MET A 415      56.398  22.743  30.365  1.00 61.97           C  
ANISOU 5968  CB  MET A 415    11053   4164   8327   1700   2075   1233
ATOM   5969  CG  MET A 415      55.922  21.398  30.926  1.00 60.66           C  
ANISOU 5969  CG  MET A 415    10877   4044   8128   1285   1995   1067
ATOM   5970  H   MET A 415      55.524  22.420  28.021  1.00 58.78           H  
ATOM   5971  HA  MET A 415      54.371  23.500  30.414  1.00 59.76           H  
ATOM   5972  HB3 MET A 415      56.869  23.288  31.184  1.00 61.97           H  
ATOM   5973  HB2 MET A 415      57.181  22.583  29.624  1.00 61.97           H  
ATOM   5974  HG3 MET A 415      55.510  20.773  30.135  1.00 60.66           H  
ATOM   5975  HG2 MET A 415      55.110  21.574  31.626  1.00 60.66           H  
ATOM   5976  HE1 MET A 415      56.795  18.626  33.301  1.00 64.08           H  
ATOM   5977  HE2 MET A 415      55.519  19.827  33.386  1.00 64.08           H  
ATOM   5978  HE3 MET A 415      55.567  18.699  32.022  1.00 64.08           H  
ATOM   5979  N   LYS A 416      56.422  25.536  28.758  1.00 63.48           N  
ANISOU 5979  N   LYS A 416    10904   4624   8590   2531   2079   1654
ATOM   5980  CA  LYS A 416      56.808  26.942  28.611  1.00 65.35           C  
ANISOU 5980  CA  LYS A 416    11113   4867   8851   2945   2168   1820
ATOM   5981  C   LYS A 416      55.625  27.831  28.181  1.00 63.88           C  
ANISOU 5981  C   LYS A 416    10492   5059   8718   3075   2033   1851
ATOM   5982  O   LYS A 416      55.493  28.930  28.719  1.00 64.58           O  
ANISOU 5982  O   LYS A 416    10533   5166   8838   3295   2107   1865
ATOM   5983  CB  LYS A 416      57.968  27.088  27.599  1.00 68.15           C  
ANISOU 5983  CB  LYS A 416    11630   5104   9161   3205   2248   2059
ATOM   5984  CG  LYS A 416      58.395  28.562  27.393  1.00 69.70           C  
ANISOU 5984  CG  LYS A 416    11582   5514   9388   3618   2242   2259
ATOM   5985  CD  LYS A 416      59.862  28.786  27.006  1.00 74.63           C  
ANISOU 5985  CD  LYS A 416    12440   5927   9989   4012   2407   2477
ATOM   5986  CE  LYS A 416      60.230  28.277  25.611  1.00 77.91           C  
ANISOU 5986  CE  LYS A 416    13051   6216  10335   4023   2407   2649
ATOM   5987  NZ  LYS A 416      61.600  28.684  25.259  1.00 78.42           N1+
ANISOU 5987  NZ  LYS A 416    13210   6197  10388   4496   2519   2917
ATOM   5988  HG3 LYS A 416      58.245  29.101  28.330  1.00 69.70           H  
ATOM   5989  HG2 LYS A 416      57.740  29.044  26.665  1.00 69.70           H  
ATOM   5990  HD3 LYS A 416      60.511  28.327  27.753  1.00 74.63           H  
ATOM   5991  HD2 LYS A 416      60.060  29.857  27.054  1.00 74.63           H  
ATOM   5992  HE3 LYS A 416      59.542  28.675  24.864  1.00 77.91           H  
ATOM   5993  HE2 LYS A 416      60.158  27.190  25.571  1.00 77.91           H  
ATOM   5994  HZ1 LYS A 416      62.246  28.307  25.940  1.00 78.42           H  
ATOM   5995  HZ2 LYS A 416      61.833  28.323  24.345  1.00 78.42           H  
ATOM   5996  HZ3 LYS A 416      61.666  29.691  25.253  1.00 78.42           H  
ATOM   5997  H   LYS A 416      56.751  24.880  28.062  1.00 63.48           H  
ATOM   5998  HA  LYS A 416      57.163  27.297  29.583  1.00 65.35           H  
ATOM   5999  HB3 LYS A 416      57.705  26.643  26.639  1.00 68.15           H  
ATOM   6000  HB2 LYS A 416      58.817  26.516  27.971  1.00 68.15           H  
ATOM   6001  N   LEU A 417      54.767  27.370  27.250  1.00 62.36           N  
ANISOU 6001  N   LEU A 417     9999   5168   8528   2933   1844   1859
ATOM   6002  CA  LEU A 417      53.597  28.110  26.756  1.00 61.39           C  
ANISOU 6002  CA  LEU A 417     9480   5407   8437   2995   1702   1874
ATOM   6003  C   LEU A 417      52.553  28.359  27.853  1.00 60.42           C  
ANISOU 6003  C   LEU A 417     9286   5311   8361   2871   1685   1681
ATOM   6004  O   LEU A 417      51.993  29.452  27.924  1.00 59.82           O  
ANISOU 6004  O   LEU A 417     9034   5390   8307   3039   1685   1711
ATOM   6005  CB  LEU A 417      52.915  27.339  25.602  1.00 59.39           C  
ANISOU 6005  CB  LEU A 417     8980   5421   8163   2797   1510   1874
ATOM   6006  CG  LEU A 417      53.577  27.485  24.220  1.00 60.70           C  
ANISOU 6006  CG  LEU A 417     9049   5738   8276   2954   1464   2100
ATOM   6007  CD1 LEU A 417      52.964  26.471  23.242  1.00 56.83           C  
ANISOU 6007  CD1 LEU A 417     8407   5435   7751   2691   1307   2053
ATOM   6008  CD2 LEU A 417      53.443  28.907  23.650  1.00 60.68           C  
ANISOU 6008  CD2 LEU A 417     8790   5991   8275   3242   1434   2259
ATOM   6009  H   LEU A 417      54.945  26.461  26.840  1.00 62.36           H  
ATOM   6010  HA  LEU A 417      53.934  29.086  26.410  1.00 61.39           H  
ATOM   6011  HB3 LEU A 417      51.876  27.661  25.499  1.00 59.39           H  
ATOM   6012  HB2 LEU A 417      52.859  26.284  25.874  1.00 59.39           H  
ATOM   6013  HG  LEU A 417      54.640  27.259  24.313  1.00 60.70           H  
ATOM   6014 HD11 LEU A 417      53.452  26.514  22.269  1.00 56.83           H  
ATOM   6015 HD12 LEU A 417      53.066  25.452  23.618  1.00 56.83           H  
ATOM   6016 HD13 LEU A 417      51.901  26.661  23.091  1.00 56.83           H  
ATOM   6017 HD21 LEU A 417      53.866  28.966  22.647  1.00 60.68           H  
ATOM   6018 HD22 LEU A 417      52.398  29.214  23.585  1.00 60.68           H  
ATOM   6019 HD23 LEU A 417      53.970  29.642  24.257  1.00 60.68           H  
ATOM   6020  N   ARG A 418      52.331  27.363  28.724  1.00 60.39           N  
ANISOU 6020  N   ARG A 418     9413   5171   8362   2565   1666   1489
ATOM   6021  CA  ARG A 418      51.437  27.443  29.877  1.00 60.14           C  
ANISOU 6021  CA  ARG A 418     9327   5160   8364   2396   1626   1298
ATOM   6022  C   ARG A 418      52.055  28.204  31.064  1.00 63.60           C  
ANISOU 6022  C   ARG A 418     9979   5383   8804   2542   1804   1265
ATOM   6023  O   ARG A 418      51.349  28.472  32.036  1.00 61.82           O  
ANISOU 6023  O   ARG A 418     9702   5190   8597   2448   1785   1132
ATOM   6024  NH1 ARG A 418      48.220  21.743  30.857  1.00 47.90           N  
ANISOU 6024  NH1 ARG A 418     7549   3808   6842    993   1133    584
ATOM   6025  NH2 ARG A 418      47.292  23.169  32.424  1.00 46.26           N1+
ANISOU 6025  NH2 ARG A 418     7294   3603   6678   1100   1122    511
ATOM   6026  CB  ARG A 418      51.102  26.011  30.325  1.00 58.05           C  
ANISOU 6026  CB  ARG A 418     9142   4820   8095   2039   1558   1122
ATOM   6027  CG  ARG A 418      50.193  25.283  29.320  1.00 54.71           C  
ANISOU 6027  CG  ARG A 418     8471   4640   7676   1879   1378   1111
ATOM   6028  CD  ARG A 418      49.808  23.886  29.802  1.00 51.11           C  
ANISOU 6028  CD  ARG A 418     8051   4146   7222   1547   1312    929
ATOM   6029  NE  ARG A 418      48.852  23.975  30.913  1.00 48.74           N  
ANISOU 6029  NE  ARG A 418     7692   3871   6957   1434   1259    778
ATOM   6030  CZ  ARG A 418      48.124  22.961  31.396  1.00 47.09           C  
ANISOU 6030  CZ  ARG A 418     7446   3687   6759   1175   1171    623
ATOM   6031  H   ARG A 418      52.831  26.494  28.589  1.00 60.39           H  
ATOM   6032  HA  ARG A 418      50.517  27.959  29.593  1.00 60.14           H  
ATOM   6033  HB3 ARG A 418      50.591  26.041  31.288  1.00 58.05           H  
ATOM   6034  HB2 ARG A 418      52.018  25.439  30.490  1.00 58.05           H  
ATOM   6035  HG3 ARG A 418      50.670  25.213  28.344  1.00 54.71           H  
ATOM   6036  HG2 ARG A 418      49.288  25.870  29.158  1.00 54.71           H  
ATOM   6037  HD3 ARG A 418      50.687  23.311  30.102  1.00 51.11           H  
ATOM   6038  HD2 ARG A 418      49.335  23.350  28.978  1.00 51.11           H  
ATOM   6039  HE  ARG A 418      48.767  24.882  31.345  1.00 48.74           H  
ATOM   6040 HH12 ARG A 418      47.703  20.955  31.222  1.00 47.90           H  
ATOM   6041 HH11 ARG A 418      48.832  21.589  30.066  1.00 47.90           H  
ATOM   6042 HH22 ARG A 418      46.734  22.412  32.787  1.00 46.26           H  
ATOM   6043 HH21 ARG A 418      47.198  24.089  32.829  1.00 46.26           H  
ATOM   6044  N   GLY A 419      53.342  28.581  30.982  1.00 41.68           N  
ATOM   6045  CA  GLY A 419      54.032  29.422  31.951  1.00 44.56           C  
ATOM   6046  C   GLY A 419      54.459  28.687  33.225  1.00 46.82           C  
ATOM   6047  O   GLY A 419      54.483  29.302  34.289  1.00 47.18           O  
ATOM   6048  H   GLY A 419      53.854  28.334  30.146  1.00 41.68           H  
ATOM   6049  HA3 GLY A 419      53.406  30.277  32.210  1.00 44.56           H  
ATOM   6050  HA2 GLY A 419      54.926  29.823  31.474  1.00 44.56           H  
ATOM   6051  N   TRP A 420      54.775  27.384  33.135  1.00 49.33           N  
ATOM   6052  CA  TRP A 420      55.199  26.558  34.272  1.00 51.96           C  
ATOM   6053  C   TRP A 420      56.698  26.726  34.594  1.00 53.81           C  
ATOM   6054  O   TRP A 420      57.132  26.319  35.673  1.00 54.45           O  
ATOM   6055  CE2 TRP A 420      51.513  23.361  33.710  1.00 61.32           C  
ATOM   6056  CE3 TRP A 420      53.526  22.019  33.796  1.00 60.61           C  
ATOM   6057  CZ2 TRP A 420      50.715  22.208  33.637  1.00 59.61           C  
ATOM   6058  CZ3 TRP A 420      52.738  20.858  33.700  1.00 61.49           C  
ATOM   6059  CH2 TRP A 420      51.334  20.947  33.626  1.00 59.21           C  
ATOM   6060  CB  TRP A 420      54.908  25.075  33.962  1.00 52.03           C  
ATOM   6061  CG  TRP A 420      53.464  24.659  33.854  1.00 53.83           C  
ATOM   6062  CD1 TRP A 420      52.375  25.466  33.830  1.00 58.43           C  
ATOM   6063  CD2 TRP A 420      52.939  23.302  33.787  1.00 57.52           C  
ATOM   6064  NE1 TRP A 420      51.228  24.708  33.739  1.00 61.72           N  
ATOM   6065  H   TRP A 420      54.723  26.935  32.229  1.00 49.33           H  
ATOM   6066  HA  TRP A 420      54.638  26.843  35.163  1.00 51.96           H  
ATOM   6067  HB3 TRP A 420      55.336  24.458  34.753  1.00 52.03           H  
ATOM   6068  HB2 TRP A 420      55.418  24.768  33.049  1.00 52.03           H  
ATOM   6069  HD1 TRP A 420      52.397  26.544  33.882  1.00 58.43           H  
ATOM   6070  HE1 TRP A 420      50.307  25.118  33.723  1.00 61.72           H  
ATOM   6071  HE3 TRP A 420      54.600  21.933  33.869  1.00 60.61           H  
ATOM   6072  HZ2 TRP A 420      49.639  22.286  33.587  1.00 59.61           H  
ATOM   6073  HZ3 TRP A 420      53.221  19.894  33.683  1.00 61.49           H  
ATOM   6074  HH2 TRP A 420      50.737  20.051  33.560  1.00 59.21           H  
ATOM   6075  N   TYR A 421      57.469  27.374  33.704  1.00 55.01           N  
ATOM   6076  CA  TYR A 421      58.835  27.831  33.938  1.00 55.89           C  
ATOM   6077  C   TYR A 421      59.114  29.126  33.165  1.00 56.41           C  
ATOM   6078  O   TYR A 421      58.515  29.468  32.144  1.00 56.69           O  
ATOM   6079  CB  TYR A 421      59.872  26.709  33.717  1.00 56.22           C  
ATOM   6080  CG  TYR A 421      60.217  26.361  32.282  1.00 57.01           C  
ATOM   6081  CD1 TYR A 421      61.238  27.081  31.631  1.00 57.11           C  
ATOM   6082  CD2 TYR A 421      59.558  25.311  31.607  1.00 60.63           C  
ATOM   6083  CE1 TYR A 421      61.587  26.774  30.308  1.00 60.85           C  
ATOM   6084  CE2 TYR A 421      59.922  24.989  30.283  1.00 61.89           C  
ATOM   6085  CZ  TYR A 421      60.934  25.728  29.635  1.00 63.09           C  
ATOM   6086  OH  TYR A 421      61.295  25.452  28.351  1.00 63.09           O  
ATOM   6087  HA  TYR A 421      58.898  28.101  34.994  1.00 55.89           H  
ATOM   6088  HB3 TYR A 421      59.557  25.800  34.226  1.00 56.22           H  
ATOM   6089  HB2 TYR A 421      60.803  26.999  34.206  1.00 56.22           H  
ATOM   6090  HD1 TYR A 421      61.761  27.875  32.145  1.00 57.11           H  
ATOM   6091  HD2 TYR A 421      58.780  24.748  32.102  1.00 60.63           H  
ATOM   6092  HE1 TYR A 421      62.368  27.333  29.815  1.00 60.85           H  
ATOM   6093  HE2 TYR A 421      59.419  24.185  29.766  1.00 61.89           H  
ATOM   6094  HH  TYR A 421      61.060  24.570  28.075  1.00 63.09           H  
ATOM   6095  H   TYR A 421      57.042  27.662  32.835  1.00 55.01           H  
TER    6096      TYR A 421
CONECT    1    9
CONECT    9    1
CONECT 1000 1012
CONECT 1534 1547
CONECT 4097 4104
CONECT 4104 4097
CONECT 4134 4139
CONECT 4139 4134
CONECT 1012 1000
CONECT 1547 1534
END   



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