CNRS Nantes University UFIP UFIP
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***  yongjian0207  ***

elNémo ID: 19020718451041685

Job options:

ID        	=	 19020718451041685
JOBID     	=	 yongjian0207
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER yongjian0207

ATOM      1  N   LEU A   1      92.525  74.388  28.577  1.00137.78           N  
ATOM      2  CA  LEU A   1      93.530  73.339  28.706  1.00140.84           C  
ATOM      3  C   LEU A   1      93.018  72.186  29.566  1.00137.55           C  
ATOM      4  O   LEU A   1      92.334  72.402  30.567  1.00142.33           O  
ATOM      5  CB  LEU A   1      94.820  73.902  29.306  1.00142.79           C  
ATOM      6  CG  LEU A   1      95.376  75.177  28.666  1.00145.03           C  
ATOM      7  CD1 LEU A   1      96.651  75.617  29.370  1.00143.80           C  
ATOM      8  CD2 LEU A   1      95.622  74.974  27.181  1.00145.88           C  
ATOM      9  N   GLU A   2      93.352  70.962  29.170  1.00200.12           N  
ANISOU    9  N   GLU A   2    26523  23628  25888   -574  -1970   2495       N  
ATOM     10  CA  GLU A   2      92.949  69.781  29.923  1.00181.04           C  
ANISOU   10  CA  GLU A   2    24046  21245  23497   -459  -1742   2287       C  
ATOM     11  C   GLU A   2      93.818  69.605  31.166  1.00169.21           C  
ANISOU   11  C   GLU A   2    22508  19781  22002   -356  -1488   2187       C  
ATOM     12  O   GLU A   2      93.428  70.005  32.263  1.00166.50           O  
ANISOU   12  O   GLU A   2    22045  19316  21900   -247  -1466   2088       O  
ATOM     13  CB  GLU A   2      93.009  68.533  29.040  1.00173.73           C  
ANISOU   13  CB  GLU A   2    23230  20481  22301   -541  -1637   2264       C  
ATOM     14  CG  GLU A   2      92.121  68.602  27.804  1.00169.31           C  
ANISOU   14  CG  GLU A   2    22718  19900  21713   -661  -1883   2359       C  
ATOM     15  CD  GLU A   2      90.660  68.845  28.141  1.00166.68           C  
ANISOU   15  CD  GLU A   2    22248  19392  21692   -577  -2051   2285       C  
ATOM     16  OE1 GLU A   2      89.837  67.934  27.915  1.00164.40           O  
ANISOU   16  OE1 GLU A   2    21948  19125  21392   -569  -2023   2186       O  
ATOM     17  OE2 GLU A   2      90.332  69.944  28.634  1.00168.23           O1-
ANISOU   17  OE2 GLU A   2    22342  19425  22152   -519  -2208   2319       O1-
ATOM     18  N   GLU A   3      94.993  69.007  30.993  1.00159.91           N  
ANISOU   18  N   GLU A   3    21427  18767  20563   -400  -1297   2210       N  
ATOM     19  CA  GLU A   3      95.943  68.874  32.092  1.00149.35           C  
ANISOU   19  CA  GLU A   3    20062  17471  19214   -319  -1076   2145       C  
ATOM     20  C   GLU A   3      97.063  69.900  31.952  1.00142.08           C  
ANISOU   20  C   GLU A   3    19188  16575  18220   -385  -1127   2301       C  
ATOM     21  O   GLU A   3      97.206  70.536  30.907  1.00144.00           O  
ANISOU   21  O   GLU A   3    19507  16834  18373   -507  -1305   2457       O  
ATOM     22  CB  GLU A   3      96.523  67.461  32.155  1.00150.30           C  
ANISOU   22  CB  GLU A   3    20236  17743  19130   -303   -816   2048       C  
ATOM     23  CG  GLU A   3      97.689  67.227  31.215  1.00157.54           C  
ANISOU   23  CG  GLU A   3    21273  18822  19763   -417   -749   2153       C  
ATOM     24  CD  GLU A   3      98.538  66.043  31.633  1.00162.89           C  
ANISOU   24  CD  GLU A   3    21969  19621  20300   -369   -470   2052       C  
ATOM     25  OE1 GLU A   3      98.115  65.300  32.543  1.00161.24           O  
ANISOU   25  OE1 GLU A   3    21696  19373  20193   -261   -345   1909       O  
ATOM     26  OE2 GLU A   3      99.630  65.859  31.054  1.00166.41           O1-
ANISOU   26  OE2 GLU A   3    22490  20198  20539   -446   -380   2114       O1-
ATOM     27  N   LYS A   4      97.856  70.057  33.006  1.00131.76           N  
ANISOU   27  N   LYS A   4    17842  15277  16946   -316   -974   2262       N  
ATOM     28  CA  LYS A   4      98.889  71.087  33.029  1.00122.96           C  
ANISOU   28  CA  LYS A   4    16757  14174  15789   -369  -1018   2399       C  
ATOM     29  C   LYS A   4     100.288  70.504  33.209  1.00117.59           C  
ANISOU   29  C   LYS A   4    16130  13657  14892   -383   -789   2405       C  
ATOM     30  O   LYS A   4     100.451  69.415  33.762  1.00123.81           O  
ANISOU   30  O   LYS A   4    16899  14507  15636   -312   -583   2280       O  
ATOM     31  CB  LYS A   4      98.596  72.100  34.139  1.00113.70           C  
ANISOU   31  CB  LYS A   4    15477  12840  14883   -288  -1081   2368       C  
ATOM     32  CG  LYS A   4      97.213  72.730  34.058  1.00108.45           C  
ANISOU   32  CG  LYS A   4    14732  11995  14481   -260  -1303   2344       C  
ATOM     33  CD  LYS A   4      96.991  73.713  35.197  1.00106.78           C  
ANISOU   33  CD  LYS A   4    14406  11625  14539   -182  -1337   2289       C  
ATOM     34  CE  LYS A   4      95.635  74.390  35.095  1.00107.22           C  
ANISOU   34  CE  LYS A   4    14364  11487  14888   -150  -1564   2258       C  
ATOM     35  NZ  LYS A   4      95.420  75.356  36.210  1.00107.20           N1+
ANISOU   35  NZ  LYS A   4    14243  11326  15162    -78  -1583   2182       N1+
ATOM     36  N   LYS A   5     101.294  71.236  32.738  1.00 98.29           N  
ANISOU   36  N   LYS A   5    13749  11276  12321   -478   -834   2551       N  
ATOM     37  CA  LYS A   5     102.684  70.825  32.894  1.00 85.05           C  
ANISOU   37  CA  LYS A   5    12108   9748  10458   -496   -631   2565       C  
ATOM     38  C   LYS A   5     103.164  71.150  34.301  1.00 80.96           C  
ANISOU   38  C   LYS A   5    11509   9178  10073   -397   -526   2518       C  
ATOM     39  O   LYS A   5     102.928  72.247  34.804  1.00 84.73           O  
ANISOU   39  O   LYS A   5    11942   9533  10718   -382   -653   2560       O  
ATOM     40  CB  LYS A   5     103.565  71.515  31.856  1.00 82.12           C  
ANISOU   40  CB  LYS A   5    11832   9471   9899   -650   -718   2735       C  
ATOM     41  CG  LYS A   5     103.127  71.257  30.426  1.00 93.64           C  
ANISOU   41  CG  LYS A   5    13385  10990  11203   -782   -831   2794       C  
ATOM     42  CD  LYS A   5     103.904  72.107  29.440  1.00107.50           C  
ANISOU   42  CD  LYS A   5    15238  12824  12782   -958   -947   2972       C  
ATOM     43  CE  LYS A   5     103.403  71.887  28.022  1.00118.89           C  
ANISOU   43  CE  LYS A   5    16783  14325  14064  -1114  -1077   3036       C  
ATOM     44  NZ  LYS A   5     104.055  72.805  27.049  1.00126.75           N1+
ANISOU   44  NZ  LYS A   5    17883  15386  14889  -1312  -1220   3221       N1+
ATOM     45  N   VAL A   6     103.838  70.194  34.934  1.00 75.80           N  
ANISOU   45  N   VAL A   6    10837   8613   9349   -336   -300   2430       N  
ATOM     46  CA  VAL A   6     104.228  70.339  36.332  1.00 78.59           C  
ANISOU   46  CA  VAL A   6    11118   8923   9821   -251   -192   2375       C  
ATOM     47  C   VAL A   6     105.738  70.417  36.536  1.00 83.93           C  
ANISOU   47  C   VAL A   6    11813   9715  10363   -281    -68   2449       C  
ATOM     48  O   VAL A   6     106.511  69.863  35.756  1.00 91.51           O  
ANISOU   48  O   VAL A   6    12826  10811  11134   -337     15   2484       O  
ATOM     49  CB  VAL A   6     103.688  69.179  37.179  1.00 65.89           C  
ANISOU   49  CB  VAL A   6     9457   7296   8282   -148    -43   2209       C  
ATOM     50  CG1 VAL A   6     102.171  69.207  37.206  1.00100.80           C  
ANISOU   50  CG1 VAL A   6    13837  11591  12871   -111   -159   2121       C  
ATOM     51  CG2 VAL A   6     104.192  67.860  36.633  1.00 69.58           C  
ANISOU   51  CG2 VAL A   6     9970   7898   8569   -153    114   2171       C  
ATOM     52  N   CYS A   7     106.145  71.112  37.594  1.00 80.37           N  
ANISOU   52  N   CYS A   7    11311   9210  10015   -250    -54   2463       N  
ATOM     53  CA  CYS A   7     107.545  71.169  38.000  1.00 77.64           C  
ANISOU   53  CA  CYS A   7    10966   8963   9572   -267     67   2523       C  
ATOM     54  C   CYS A   7     107.670  70.801  39.476  1.00 75.08           C  
ANISOU   54  C   CYS A   7    10572   8601   9354   -182    196   2431       C  
ATOM     55  O   CYS A   7     106.760  71.050  40.267  1.00 66.15           O  
ANISOU   55  O   CYS A   7     9392   7348   8392   -134    154   2349       O  
ATOM     56  CB  CYS A   7     108.134  72.556  37.739  1.00 73.61           C  
ANISOU   56  CB  CYS A   7    10482   8441   9047   -353    -61   2670       C  
ATOM     57  SG  CYS A   7     107.262  73.908  38.552  1.00154.13           S  
ANISOU   57  SG  CYS A   7    20627  18439  19496   -328   -232   2669       S  
ATOM     58  N   GLN A   8     108.803  70.209  39.841  1.00 77.15           N  
ANISOU   58  N   GLN A   8    10826   8969   9520   -172    349   2443       N  
ATOM     59  CA  GLN A   8     108.985  69.659  41.181  1.00 79.12           C  
ANISOU   59  CA  GLN A   8    11020   9198   9844   -106    474   2365       C  
ATOM     60  C   GLN A   8     108.994  70.723  42.276  1.00 77.30           C  
ANISOU   60  C   GLN A   8    10752   8880   9740   -115    424   2382       C  
ATOM     61  O   GLN A   8     108.588  70.460  43.407  1.00 74.84           O  
ANISOU   61  O   GLN A   8    10398   8506   9531    -76    480   2289       O  
ATOM     62  CB  GLN A   8     110.273  68.835  41.246  1.00 87.76           C  
ANISOU   62  CB  GLN A   8    12108  10418  10818    -99    628   2392       C  
ATOM     63  CG  GLN A   8     110.274  67.770  42.329  1.00 93.47           C  
ANISOU   63  CG  GLN A   8    12789  11128  11596    -29    757   2298       C  
ATOM     64  CD  GLN A   8     109.303  66.642  42.034  1.00 98.78           C  
ANISOU   64  CD  GLN A   8    13473  11776  12282     22    794   2180       C  
ATOM     65  NE2 GLN A   8     109.096  65.767  43.011  1.00103.97           N  
ANISOU   65  NE2 GLN A   8    14102  12402  13000     73    883   2094       N  
ATOM     66  OE1 GLN A   8     108.747  66.557  40.938  1.00 96.69           O  
ANISOU   66  OE1 GLN A   8    13247  11522  11968      5    738   2169       O  
ATOM     67  N   GLY A   9     109.461  71.921  41.938  1.00 82.82           N  
ANISOU   67  N   GLY A   9    11469   9574  10424   -179    321   2497       N  
ATOM     68  CA  GLY A   9     109.573  72.995  42.910  1.00 81.33           C  
ANISOU   68  CA  GLY A   9    11250   9305  10349   -198    275   2518       C  
ATOM     69  C   GLY A   9     110.863  72.917  43.705  1.00 81.01           C  
ANISOU   69  C   GLY A   9    11192   9348  10240   -215    390   2570       C  
ATOM     70  O   GLY A   9     111.480  71.857  43.800  1.00 89.03           O  
ANISOU   70  O   GLY A   9    12201  10458  11169   -187    519   2556       O  
ATOM     71  N   THR A  10     111.277  74.042  44.278  1.00 75.82           N  
ANISOU   71  N   THR A  10    10525   8650   9633   -261    338   2632       N  
ATOM     72  CA  THR A  10     112.512  74.086  45.051  1.00 81.99           C  
ANISOU   72  CA  THR A  10    11289   9509  10355   -290    431   2694       C  
ATOM     73  C   THR A  10     112.229  74.028  46.548  1.00 84.79           C  
ANISOU   73  C   THR A  10    11601   9796  10819   -277    492   2603       C  
ATOM     74  O   THR A  10     111.083  74.159  46.981  1.00 76.45           O  
ANISOU   74  O   THR A  10    10526   8627   9895   -255    458   2490       O  
ATOM     75  CB  THR A  10     113.338  75.350  44.739  1.00 93.13           C  
ANISOU   75  CB  THR A  10    12723  10940  11721   -370    346   2833       C  
ATOM     76  CG2 THR A  10     113.453  75.557  43.237  1.00 99.57           C  
ANISOU   76  CG2 THR A  10    13593  11811  12430   -411    262   2920       C  
ATOM     77  OG1 THR A  10     112.714  76.495  45.331  1.00 97.61           O  
ANISOU   77  OG1 THR A  10    13280  11370  12436   -392    245   2811       O  
ATOM     78  N   SER A  11     113.283  73.828  47.332  1.00 92.22           N  
ANISOU   78  N   SER A  11    12525  10809  11704   -302    581   2651       N  
ATOM     79  CA  SER A  11     113.160  73.742  48.782  1.00 94.64           C  
ANISOU   79  CA  SER A  11    12804  11072  12085   -319    643   2580       C  
ATOM     80  C   SER A  11     114.470  74.126  49.455  1.00 97.20           C  
ANISOU   80  C   SER A  11    13118  11466  12346   -381    681   2687       C  
ATOM     81  O   SER A  11     114.916  73.455  50.386  1.00102.83           O  
ANISOU   81  O   SER A  11    13813  12218  13041   -392    766   2677       O  
ATOM     82  CB  SER A  11     112.763  72.327  49.202  1.00 94.85           C  
ANISOU   82  CB  SER A  11    12816  11112  12109   -267    742   2483       C  
ATOM     83  OG  SER A  11     111.592  71.901  48.528  1.00101.54           O  
ANISOU   83  OG  SER A  11    13672  11905  13004   -212    712   2387       O  
ATOM     84  N   ASN A  12     115.081  75.207  48.981  1.00 87.69           N  
ANISOU   84  N   ASN A  12    11930  10279  11108   -431    608   2795       N  
ATOM     85  CA  ASN A  12     116.364  75.660  49.505  1.00 80.22           C  
ANISOU   85  CA  ASN A  12    10975   9406  10097   -496    634   2907       C  
ATOM     86  C   ASN A  12     116.218  76.872  50.418  1.00 80.59           C  
ANISOU   86  C   ASN A  12    11024   9367  10229   -569    584   2898       C  
ATOM     87  O   ASN A  12     117.189  77.325  51.024  1.00 84.93           O  
ANISOU   87  O   ASN A  12    11568   9966  10735   -636    603   2980       O  
ATOM     88  CB  ASN A  12     117.317  75.996  48.357  1.00 77.76           C  
ANISOU   88  CB  ASN A  12    10680   9194   9671   -518    601   3039       C  
ATOM     89  CG  ASN A  12     117.279  74.965  47.248  1.00 77.69           C  
ANISOU   89  CG  ASN A  12    10675   9256   9586   -457    641   3026       C  
ATOM     90  ND2 ASN A  12     117.116  75.429  46.015  1.00 69.49           N  
ANISOU   90  ND2 ASN A  12     9676   8229   8497   -476    562   3071       N  
ATOM     91  OD1 ASN A  12     117.397  73.765  47.495  1.00 87.76           O  
ANISOU   91  OD1 ASN A  12    11922  10575  10848   -403    738   2977       O  
ATOM     92  N   LYS A  13     115.002  77.398  50.508  1.00 78.15           N  
ANISOU   92  N   LYS A  13    10718   8927  10050   -559    522   2792       N  
ATOM     93  CA  LYS A  13     114.742  78.578  51.322  1.00 89.23           C  
ANISOU   93  CA  LYS A  13    12116  10229  11559   -625    478   2756       C  
ATOM     94  C   LYS A  13     115.649  79.740  50.925  1.00100.83           C  
ANISOU   94  C   LYS A  13    13609  11719  12982   -689    400   2899       C  
ATOM     95  O   LYS A  13     115.558  80.258  49.812  1.00106.40           O  
ANISOU   95  O   LYS A  13    14340  12407  13679   -678    297   2967       O  
ATOM     96  CB  LYS A  13     114.905  78.257  52.809  1.00 91.48           C  
ANISOU   96  CB  LYS A  13    12382  10523  11854   -681    581   2689       C  
ATOM     97  CG  LYS A  13     113.840  77.321  53.359  1.00 97.53           C  
ANISOU   97  CG  LYS A  13    13128  11242  12685   -644    648   2529       C  
ATOM     98  CD  LYS A  13     113.951  77.181  54.868  1.00104.73           C  
ANISOU   98  CD  LYS A  13    14034  12157  13603   -734    735   2463       C  
ATOM     99  CE  LYS A  13     112.883  76.250  55.417  1.00110.29           C  
ANISOU   99  CE  LYS A  13    14724  12819  14361   -717    804   2302       C  
ATOM    100  NZ  LYS A  13     111.509  76.779  55.193  1.00115.59           N1+
ANISOU  100  NZ  LYS A  13    15369  13358  15192   -684    760   2150       N1+
ATOM    101  N   LEU A  14     116.527  80.143  51.838  1.00 99.90           N  
ANISOU  101  N   LEU A  14    13489  11644  12827   -768    443   2951       N  
ATOM    102  CA  LEU A  14     117.387  81.299  51.608  1.00 96.13           C  
ANISOU  102  CA  LEU A  14    13035  11182  12309   -841    373   3080       C  
ATOM    103  C   LEU A  14     118.747  80.907  51.041  1.00100.93           C  
ANISOU  103  C   LEU A  14    13648  11954  12748   -856    406   3232       C  
ATOM    104  O   LEU A  14     119.622  81.755  50.865  1.00 99.72           O  
ANISOU  104  O   LEU A  14    13512  11841  12536   -927    363   3350       O  
ATOM    105  CB  LEU A  14     117.568  82.093  52.902  1.00 88.99           C  
ANISOU  105  CB  LEU A  14    12124  10225  11463   -932    395   3047       C  
ATOM    106  CG  LEU A  14     116.281  82.616  53.538  1.00 90.62           C  
ANISOU  106  CG  LEU A  14    12314  10266  11852   -934    375   2877       C  
ATOM    107  CD1 LEU A  14     116.567  83.249  54.890  1.00 96.48           C  
ANISOU  107  CD1 LEU A  14    13052  10980  12626  -1043    427   2832       C  
ATOM    108  CD2 LEU A  14     115.590  83.604  52.610  1.00 89.46           C  
ANISOU  108  CD2 LEU A  14    12176   9991  11823   -905    232   2879       C  
ATOM    109  N   THR A  15     118.920  79.620  50.758  1.00 99.15           N  
ANISOU  109  N   THR A  15    13402  11819  12453   -792    486   3222       N  
ATOM    110  CA  THR A  15     120.176  79.122  50.208  1.00 94.39           C  
ANISOU  110  CA  THR A  15    12784  11368  11711   -796    534   3341       C  
ATOM    111  C   THR A  15     120.416  79.641  48.795  1.00101.03           C  
ANISOU  111  C   THR A  15    13660  12249  12479   -810    458   3429       C  
ATOM    112  O   THR A  15     119.487  79.741  47.993  1.00105.80           O  
ANISOU  112  O   THR A  15    14295  12784  13122   -776    388   3385       O  
ATOM    113  CB  THR A  15     120.214  77.583  50.191  1.00 83.70           C  
ANISOU  113  CB  THR A  15    11395  10082  10325   -716    636   3292       C  
ATOM    114  CG2 THR A  15     121.352  77.088  49.317  1.00 81.87           C  
ANISOU  114  CG2 THR A  15    11139   9993   9974   -707    681   3390       C  
ATOM    115  OG1 THR A  15     120.401  77.095  51.524  1.00 82.32           O  
ANISOU  115  OG1 THR A  15    11192   9906  10181   -734    704   3259       O  
ATOM    116  N   GLN A  16     121.670  79.971  48.499  1.00 98.55           N  
ANISOU  116  N   GLN A  16    13340  12048  12055   -872    470   3554       N  
ATOM    117  CA  GLN A  16     122.050  80.454  47.178  1.00 94.05           C  
ANISOU  117  CA  GLN A  16    12807  11539  11387   -915    408   3647       C  
ATOM    118  C   GLN A  16     122.841  79.398  46.411  1.00 94.98           C  
ANISOU  118  C   GLN A  16    12890  11811  11386   -889    508   3671       C  
ATOM    119  O   GLN A  16     123.880  78.929  46.875  1.00 95.06           O  
ANISOU  119  O   GLN A  16    12842  11921  11355   -893    599   3708       O  
ATOM    120  CB  GLN A  16     122.863  81.741  47.300  1.00 89.25           C  
ANISOU  120  CB  GLN A  16    12224  10947  10741  -1026    342   3767       C  
ATOM    121  CG  GLN A  16     123.378  82.276  45.981  1.00 94.70           C  
ANISOU  121  CG  GLN A  16    12958  11714  11310  -1098    279   3875       C  
ATOM    122  CD  GLN A  16     123.858  83.706  46.089  1.00100.67           C  
ANISOU  122  CD  GLN A  16    13756  12440  12055  -1210    180   3984       C  
ATOM    123  NE2 GLN A  16     124.827  84.071  45.258  1.00100.76           N  
ANISOU  123  NE2 GLN A  16    13788  12573  11924  -1301    169   4100       N  
ATOM    124  OE1 GLN A  16     123.361  84.477  46.910  1.00104.58           O  
ANISOU  124  OE1 GLN A  16    14264  12804  12668  -1222    118   3956       O  
ATOM    125  N   LEU A  17     122.342  79.029  45.235  1.00 93.15           N  
ANISOU  125  N   LEU A  17    12691  11595  11108   -866    488   3645       N  
ATOM    126  CA  LEU A  17     122.966  77.985  44.429  1.00 90.25           C  
ANISOU  126  CA  LEU A  17    12290  11364  10636   -842    593   3638       C  
ATOM    127  C   LEU A  17     124.070  78.541  43.536  1.00 92.40           C  
ANISOU  127  C   LEU A  17    12574  11768  10765   -948    591   3751       C  
ATOM    128  O   LEU A  17     123.811  78.979  42.416  1.00 92.50           O  
ANISOU  128  O   LEU A  17    12652  11797  10699  -1012    519   3785       O  
ATOM    129  CB  LEU A  17     121.916  77.279  43.570  1.00 79.92           C  
ANISOU  129  CB  LEU A  17    11014  10022   9330   -784    584   3549       C  
ATOM    130  CG  LEU A  17     120.641  76.820  44.278  1.00 70.59           C  
ANISOU  130  CG  LEU A  17     9831   8703   8286   -691    569   3430       C  
ATOM    131  CD1 LEU A  17     119.762  76.032  43.320  1.00 67.09           C  
ANISOU  131  CD1 LEU A  17     9415   8252   7825   -641    570   3350       C  
ATOM    132  CD2 LEU A  17     120.975  75.991  45.506  1.00 63.19           C  
ANISOU  132  CD2 LEU A  17     8826   7772   7411   -630    677   3381       C  
ATOM    133  N   GLY A  18     125.302  78.514  44.034  1.00 88.99           N  
ANISOU  133  N   GLY A  18    12078  11434  10300   -977    668   3809       N  
ATOM    134  CA  GLY A  18     126.436  79.026  43.288  1.00 86.69           C  
ANISOU  134  CA  GLY A  18    11785  11279   9876  -1085    682   3909       C  
ATOM    135  C   GLY A  18     126.459  80.541  43.271  1.00 86.09           C  
ANISOU  135  C   GLY A  18    11782  11153   9776  -1197    545   4015       C  
ATOM    136  O   GLY A  18     126.119  81.184  44.264  1.00 89.79           O  
ANISOU  136  O   GLY A  18    12263  11510  10344  -1191    481   4025       O  
ATOM    137  N   THR A  19     126.861  81.115  42.142  1.00 81.53           N  
ANISOU  137  N   THR A  19    11256  10658   9065  -1310    503   4092       N  
ATOM    138  CA  THR A  19     126.870  82.564  41.988  1.00 87.24           C  
ANISOU  138  CA  THR A  19    12060  11328   9761  -1428    357   4203       C  
ATOM    139  C   THR A  19     125.510  83.042  41.494  1.00 86.96           C  
ANISOU  139  C   THR A  19    12116  11142   9784  -1423    204   4187       C  
ATOM    140  O   THR A  19     124.695  82.239  41.044  1.00 89.08           O  
ANISOU  140  O   THR A  19    12390  11384  10072  -1351    220   4100       O  
ATOM    141  CB  THR A  19     127.953  83.016  41.000  1.00 95.89           C  
ANISOU  141  CB  THR A  19    13176  12583  10676  -1575    369   4305       C  
ATOM    142  CG2 THR A  19     129.297  82.423  41.384  1.00 97.84           C  
ANISOU  142  CG2 THR A  19    13311  12985  10880  -1571    530   4306       C  
ATOM    143  OG1 THR A  19     127.604  82.586  39.678  1.00102.23           O  
ANISOU  143  OG1 THR A  19    14027  13445  11370  -1614    370   4279       O  
ATOM    144  N   PHE A  20     125.268  84.347  41.576  1.00 84.49           N  
ANISOU  144  N   PHE A  20    11869  10724   9508  -1500     50   4271       N  
ATOM    145  CA  PHE A  20     123.981  84.905  41.174  1.00 84.85           C  
ANISOU  145  CA  PHE A  20    11990  10605   9645  -1494   -118   4263       C  
ATOM    146  C   PHE A  20     123.500  84.337  39.845  1.00 92.23           C  
ANISOU  146  C   PHE A  20    12973  11590  10481  -1515   -142   4251       C  
ATOM    147  O   PHE A  20     122.324  84.007  39.693  1.00 95.01           O  
ANISOU  147  O   PHE A  20    13339  11832  10928  -1439   -201   4176       O  
ATOM    148  CB  PHE A  20     124.039  86.432  41.102  1.00 84.87           C  
ANISOU  148  CB  PHE A  20    12065  10515   9668  -1609   -290   4385       C  
ATOM    149  CG  PHE A  20     124.111  87.098  42.444  1.00 85.77           C  
ANISOU  149  CG  PHE A  20    12145  10524   9921  -1582   -297   4372       C  
ATOM    150  CD1 PHE A  20     124.737  88.323  42.592  1.00 85.79           C  
ANISOU  150  CD1 PHE A  20    12187  10506   9902  -1696   -383   4488       C  
ATOM    151  CD2 PHE A  20     123.560  86.492  43.560  1.00 89.65           C  
ANISOU  151  CD2 PHE A  20    12568  10940  10555  -1456   -215   4242       C  
ATOM    152  CE1 PHE A  20     124.803  88.937  43.826  1.00 91.25           C  
ANISOU  152  CE1 PHE A  20    12851  11103  10717  -1683   -383   4467       C  
ATOM    153  CE2 PHE A  20     123.625  87.098  44.798  1.00 91.47           C  
ANISOU  153  CE2 PHE A  20    12773  11081  10899  -1452   -213   4221       C  
ATOM    154  CZ  PHE A  20     124.248  88.322  44.932  1.00 94.48           C  
ANISOU  154  CZ  PHE A  20    13193  11443  11262  -1565   -295   4331       C  
ATOM    155  N   GLU A  21     124.412  84.223  38.885  1.00 98.50           N  
ANISOU  155  N   GLU A  21    13790  12557  11080  -1629    -91   4318       N  
ATOM    156  CA  GLU A  21     124.070  83.664  37.584  1.00106.75           C  
ANISOU  156  CA  GLU A  21    14886  13673  12001  -1678    -97   4304       C  
ATOM    157  C   GLU A  21     123.711  82.188  37.706  1.00100.22           C  
ANISOU  157  C   GLU A  21    13989  12882  11207  -1540     56   4154       C  
ATOM    158  O   GLU A  21     122.640  81.767  37.272  1.00101.30           O  
ANISOU  158  O   GLU A  21    14159  12946  11386  -1492      2   4093       O  
ATOM    159  CB  GLU A  21     125.210  83.857  36.585  1.00120.53           C  
ANISOU  159  CB  GLU A  21    16665  15611  13520  -1849    -52   4393       C  
ATOM    160  CG  GLU A  21     124.948  83.216  35.231  1.00134.14           C  
ANISOU  160  CG  GLU A  21    18443  17432  15090  -1924    -33   4365       C  
ATOM    161  CD  GLU A  21     125.931  83.665  34.170  1.00147.92           C  
ANISOU  161  CD  GLU A  21    20247  19350  16604  -2136    -25   4464       C  
ATOM    162  OE1 GLU A  21     126.150  82.905  33.203  1.00155.04           O  
ANISOU  162  OE1 GLU A  21    21158  20397  17353  -2204     78   4411       O  
ATOM    163  OE2 GLU A  21     126.485  84.777  34.303  1.00150.52           O1-
ANISOU  163  OE2 GLU A  21    20614  19674  16902  -2244   -117   4589       O1-
ATOM    164  N   ASP A  22     124.610  81.405  38.294  1.00 97.22           N  
ANISOU  164  N   ASP A  22    13512  12610  10817  -1479    239   4099       N  
ATOM    165  CA  ASP A  22     124.334  79.997  38.553  1.00102.70           C  
ANISOU  165  CA  ASP A  22    14133  13323  11564  -1342    383   3961       C  
ATOM    166  C   ASP A  22     122.938  79.858  39.147  1.00101.71           C  
ANISOU  166  C   ASP A  22    14020  13015  11609  -1223    302   3883       C  
ATOM    167  O   ASP A  22     122.080  79.171  38.594  1.00102.52           O  
ANISOU  167  O   ASP A  22    14145  13091  11718  -1177    298   3806       O  
ATOM    168  CB  ASP A  22     125.365  79.410  39.521  1.00106.28           C  
ANISOU  168  CB  ASP A  22    14472  13852  12056  -1274    541   3931       C  
ATOM    169  CG  ASP A  22     126.756  79.329  38.922  1.00103.72           C  
ANISOU  169  CG  ASP A  22    14107  13719  11582  -1374    650   3978       C  
ATOM    170  OD1 ASP A  22     127.717  79.738  39.607  1.00103.49           O  
ANISOU  170  OD1 ASP A  22    14024  13735  11563  -1399    683   4040       O  
ATOM    171  OD2 ASP A  22     126.891  78.854  37.775  1.00 99.25           O1-
ANISOU  171  OD2 ASP A  22    13561  13260  10889  -1434    708   3946       O1-
ATOM    172  N   HIS A  23     122.725  80.524  40.278  1.00 98.99           N  
ANISOU  172  N   HIS A  23    13658  12550  11402  -1184    242   3897       N  
ATOM    173  CA  HIS A  23     121.442  80.510  40.970  1.00 92.34           C  
ANISOU  173  CA  HIS A  23    12817  11533  10737  -1084    173   3813       C  
ATOM    174  C   HIS A  23     120.297  80.772  40.001  1.00 89.48           C  
ANISOU  174  C   HIS A  23    12529  11082  10387  -1105     28   3811       C  
ATOM    175  O   HIS A  23     119.382  79.959  39.873  1.00 88.24           O  
ANISOU  175  O   HIS A  23    12364  10879  10285  -1020     46   3709       O  
ATOM    176  CB  HIS A  23     121.438  81.559  42.082  1.00 89.48           C  
ANISOU  176  CB  HIS A  23    12446  11057  10496  -1093    102   3848       C  
ATOM    177  CG  HIS A  23     120.239  81.495  42.975  1.00 83.65           C  
ANISOU  177  CG  HIS A  23    11687  10150   9946   -995     67   3737       C  
ATOM    178  CD2 HIS A  23     119.040  82.120  42.906  1.00 84.17           C  
ANISOU  178  CD2 HIS A  23    11785  10050  10145   -979    -75   3704       C  
ATOM    179  ND1 HIS A  23     120.198  80.715  44.111  1.00 77.75           N  
ANISOU  179  ND1 HIS A  23    10873   9393   9274   -908    187   3639       N  
ATOM    180  CE1 HIS A  23     119.024  80.859  44.700  1.00 80.98           C  
ANISOU  180  CE1 HIS A  23    11278   9649   9842   -851    134   3543       C  
ATOM    181  NE2 HIS A  23     118.303  81.706  43.988  1.00 81.78           N  
ANISOU  181  NE2 HIS A  23    11431   9650   9992   -884    -22   3575       N  
ATOM    182  N   PHE A  24     120.357  81.910  39.318  1.00 89.31           N  
ANISOU  182  N   PHE A  24    12582  11035  10315  -1225   -125   3931       N  
ATOM    183  CA  PHE A  24     119.331  82.277  38.352  1.00 86.72           C  
ANISOU  183  CA  PHE A  24    12330  10619  10001  -1266   -296   3959       C  
ATOM    184  C   PHE A  24     119.129  81.185  37.309  1.00 90.46           C  
ANISOU  184  C   PHE A  24    12824  11200  10345  -1271   -228   3907       C  
ATOM    185  O   PHE A  24     118.000  80.885  36.925  1.00 92.99           O  
ANISOU  185  O   PHE A  24    13167  11433  10730  -1228   -306   3853       O  
ATOM    186  CB  PHE A  24     119.686  83.594  37.662  1.00 84.62           C  
ANISOU  186  CB  PHE A  24    12149  10341   9661  -1424   -466   4121       C  
ATOM    187  CG  PHE A  24     118.714  83.992  36.592  1.00 87.48           C  
ANISOU  187  CG  PHE A  24    12596  10617  10026  -1488   -664   4175       C  
ATOM    188  CD1 PHE A  24     117.593  84.743  36.901  1.00 92.49           C  
ANISOU  188  CD1 PHE A  24    13237  11034  10871  -1442   -848   4172       C  
ATOM    189  CD2 PHE A  24     118.916  83.610  35.278  1.00 89.98           C  
ANISOU  189  CD2 PHE A  24    12982  11066  10140  -1603   -669   4223       C  
ATOM    190  CE1 PHE A  24     116.694  85.109  35.917  1.00 95.18           C  
ANISOU  190  CE1 PHE A  24    13648  11285  11230  -1501  -1050   4233       C  
ATOM    191  CE2 PHE A  24     118.019  83.971  34.291  1.00 92.45           C  
ANISOU  191  CE2 PHE A  24    13379  11301  10448  -1678   -866   4286       C  
ATOM    192  CZ  PHE A  24     116.908  84.723  34.611  1.00 93.11           C  
ANISOU  192  CZ  PHE A  24    13464  11160  10752  -1624  -1066   4298       C  
ATOM    193  N   LEU A  25     120.228  80.595  36.852  1.00 96.34           N  
ANISOU  193  N   LEU A  25    13556  12134  10914  -1326    -79   3917       N  
ATOM    194  CA  LEU A  25     120.165  79.556  35.832  1.00103.74           C  
ANISOU  194  CA  LEU A  25    14512  13188  11717  -1347      9   3857       C  
ATOM    195  C   LEU A  25     119.435  78.324  36.359  1.00101.58           C  
ANISOU  195  C   LEU A  25    14175  12867  11555  -1184    114   3702       C  
ATOM    196  O   LEU A  25     118.657  77.699  35.639  1.00103.14           O  
ANISOU  196  O   LEU A  25    14406  13058  11724  -1175     99   3643       O  
ATOM    197  CB  LEU A  25     121.570  79.187  35.349  1.00109.50           C  
ANISOU  197  CB  LEU A  25    15218  14126  12261  -1437    169   3877       C  
ATOM    198  CG  LEU A  25     121.687  78.607  33.935  1.00112.24           C  
ANISOU  198  CG  LEU A  25    15619  14614  12412  -1549    219   3859       C  
ATOM    199  CD1 LEU A  25     123.098  78.787  33.393  1.00117.43           C  
ANISOU  199  CD1 LEU A  25    16271  15463  12886  -1692    323   3915       C  
ATOM    200  CD2 LEU A  25     121.275  77.143  33.893  1.00107.51           C  
ANISOU  200  CD2 LEU A  25    14968  14039  11840  -1430    367   3701       C  
ATOM    201  N   SER A  26     119.686  77.980  37.617  1.00 99.81           N  
ANISOU  201  N   SER A  26    13864  12608  11450  -1068    216   3640       N  
ATOM    202  CA  SER A  26     118.988  76.868  38.251  1.00101.85           C  
ANISOU  202  CA  SER A  26    14067  12810  11822   -921    306   3501       C  
ATOM    203  C   SER A  26     117.499  77.170  38.346  1.00102.33           C  
ANISOU  203  C   SER A  26    14160  12699  12022   -873    159   3459       C  
ATOM    204  O   SER A  26     116.663  76.326  38.028  1.00106.98           O  
ANISOU  204  O   SER A  26    14752  13263  12632   -813    178   3366       O  
ATOM    205  CB  SER A  26     119.562  76.589  39.641  1.00106.46           C  
ANISOU  205  CB  SER A  26    14564  13384  12502   -835    417   3466       C  
ATOM    206  OG  SER A  26     120.873  76.060  39.553  1.00114.23           O  
ANISOU  206  OG  SER A  26    15496  14523  13384   -856    564   3482       O  
ATOM    207  N   LEU A  27     117.177  78.383  38.786  1.00 96.58           N  
ANISOU  207  N   LEU A  27    13450  11848  11398   -900     13   3524       N  
ATOM    208  CA  LEU A  27     115.793  78.834  38.869  1.00 86.35           C  
ANISOU  208  CA  LEU A  27    12171  10375  10263   -859   -142   3487       C  
ATOM    209  C   LEU A  27     115.112  78.700  37.513  1.00 84.71           C  
ANISOU  209  C   LEU A  27    12034  10175   9978   -918   -250   3512       C  
ATOM    210  O   LEU A  27     113.973  78.244  37.416  1.00 86.13           O  
ANISOU  210  O   LEU A  27    12207  10268  10251   -851   -294   3426       O  
ATOM    211  CB  LEU A  27     115.740  80.291  39.333  1.00 79.75           C  
ANISOU  211  CB  LEU A  27    11348   9416   9539   -906   -292   3571       C  
ATOM    212  CG  LEU A  27     114.365  80.960  39.377  1.00 78.93           C  
ANISOU  212  CG  LEU A  27    11249   9110   9631   -873   -474   3540       C  
ATOM    213  CD1 LEU A  27     113.629  80.588  40.653  1.00 79.96           C  
ANISOU  213  CD1 LEU A  27    11297   9130   9952   -748   -400   3387       C  
ATOM    214  CD2 LEU A  27     114.498  82.470  39.260  1.00 79.64           C  
ANISOU  214  CD2 LEU A  27    11380   9104   9778   -964   -655   3667       C  
ATOM    215  N   GLN A  28     115.828  79.098  36.468  1.00 84.95           N  
ANISOU  215  N   GLN A  28    12134  10316   9829  -1057   -293   3631       N  
ATOM    216  CA  GLN A  28     115.301  79.093  35.108  1.00 93.75           C  
ANISOU  216  CA  GLN A  28    13332  11451  10836  -1155   -411   3680       C  
ATOM    217  C   GLN A  28     115.028  77.682  34.594  1.00 88.47           C  
ANISOU  217  C   GLN A  28    12657  10875  10082  -1111   -277   3565       C  
ATOM    218  O   GLN A  28     113.973  77.413  34.020  1.00 85.08           O  
ANISOU  218  O   GLN A  28    12261  10384   9682  -1106   -371   3532       O  
ATOM    219  CB  GLN A  28     116.276  79.814  34.176  1.00107.89           C  
ANISOU  219  CB  GLN A  28    15202  13362  12429  -1338   -464   3830       C  
ATOM    220  CG  GLN A  28     115.935  79.720  32.703  1.00115.88           C  
ANISOU  220  CG  GLN A  28    16313  14437  13278  -1478   -564   3887       C  
ATOM    221  CD  GLN A  28     116.992  80.365  31.832  1.00124.35           C  
ANISOU  221  CD  GLN A  28    17465  15650  14132  -1679   -590   4026       C  
ATOM    222  NE2 GLN A  28     117.795  81.239  32.429  1.00121.86           N  
ANISOU  222  NE2 GLN A  28    17132  15327  13840  -1705   -601   4107       N  
ATOM    223  OE1 GLN A  28     117.092  80.079  30.639  1.00132.48           O  
ANISOU  223  OE1 GLN A  28    18572  16797  14967  -1820   -597   4056       O  
ATOM    224  N   ARG A  29     115.986  76.785  34.797  1.00 89.23           N  
ANISOU  224  N   ARG A  29    12706  11114  10083  -1082    -61   3503       N  
ATOM    225  CA  ARG A  29     115.850  75.410  34.334  1.00 88.36           C  
ANISOU  225  CA  ARG A  29    12584  11092   9896  -1041     85   3386       C  
ATOM    226  C   ARG A  29     114.650  74.726  34.974  1.00 87.82           C  
ANISOU  226  C   ARG A  29    12474  10896   9998   -893     85   3262       C  
ATOM    227  O   ARG A  29     113.941  73.957  34.325  1.00 85.30           O  
ANISOU  227  O   ARG A  29    12182  10586   9644   -885     92   3192       O  
ATOM    228  CB  ARG A  29     117.130  74.620  34.617  1.00 88.90           C  
ANISOU  228  CB  ARG A  29    12587  11310   9883  -1016    312   3338       C  
ATOM    229  CG  ARG A  29     118.312  75.064  33.773  1.00101.57           C  
ANISOU  229  CG  ARG A  29    14227  13073  11291  -1176    344   3432       C  
ATOM    230  CD  ARG A  29     119.521  74.170  33.971  1.00107.62           C  
ANISOU  230  CD  ARG A  29    14910  13983  11999  -1143    575   3363       C  
ATOM    231  NE  ARG A  29     120.111  74.335  35.295  1.00115.58           N  
ANISOU  231  NE  ARG A  29    15830  14951  13135  -1046    628   3373       N  
ATOM    232  CZ  ARG A  29     121.336  73.936  35.617  1.00120.67           C  
ANISOU  232  CZ  ARG A  29    16393  15705  13750  -1033    785   3360       C  
ATOM    233  NH1 ARG A  29     122.105  73.354  34.707  1.00121.48           N1+
ANISOU  233  NH1 ARG A  29    16484  15964  13711  -1107    916   3322       N1+
ATOM    234  NH2 ARG A  29     121.796  74.124  36.846  1.00121.02           N  
ANISOU  234  NH2 ARG A  29    16366  15704  13913   -955    810   3381       N  
ATOM    235  N   MET A  30     114.422  75.025  36.248  1.00 90.97           N  
ANISOU  235  N   MET A  30    12810  11180  10575   -790     79   3231       N  
ATOM    236  CA  MET A  30     113.356  74.391  37.016  1.00 88.87           C  
ANISOU  236  CA  MET A  30    12495  10799  10473   -658     99   3103       C  
ATOM    237  C   MET A  30     111.959  74.825  36.581  1.00 90.16           C  
ANISOU  237  C   MET A  30    12693  10826  10737   -662    -88   3097       C  
ATOM    238  O   MET A  30     111.108  73.988  36.287  1.00 96.97           O  
ANISOU  238  O   MET A  30    13556  11669  11617   -614    -73   3004       O  
ATOM    239  CB  MET A  30     113.544  74.667  38.511  1.00 87.46           C  
ANISOU  239  CB  MET A  30    12245  10544  10442   -577    146   3072       C  
ATOM    240  CG  MET A  30     112.302  74.415  39.352  1.00 85.11           C  
ANISOU  240  CG  MET A  30    11905  10100  10333   -474    122   2952       C  
ATOM    241  SD  MET A  30     111.821  72.679  39.413  1.00143.67           S  
ANISOU  241  SD  MET A  30    19296  17557  17737   -376    277   2800       S  
ATOM    242  CE  MET A  30     113.158  71.995  40.387  1.00 70.29           C  
ANISOU  242  CE  MET A  30     9943   8362   8401   -336    473   2790       C  
ATOM    243  N   PHE A  31     111.728  76.133  36.538  1.00 88.36           N  
ANISOU  243  N   PHE A  31    12489  10500  10585   -719   -270   3196       N  
ATOM    244  CA  PHE A  31     110.382  76.658  36.333  1.00 86.19           C  
ANISOU  244  CA  PHE A  31    12221  10062  10464   -704   -464   3187       C  
ATOM    245  C   PHE A  31     110.050  77.022  34.886  1.00 91.05           C  
ANISOU  245  C   PHE A  31    12927  10695  10972   -829   -637   3295       C  
ATOM    246  O   PHE A  31     109.010  77.622  34.623  1.00 95.95           O  
ANISOU  246  O   PHE A  31    13554  11173  11728   -834   -834   3320       O  
ATOM    247  CB  PHE A  31     110.145  77.868  37.239  1.00 80.71           C  
ANISOU  247  CB  PHE A  31    11485   9212   9970   -679   -576   3213       C  
ATOM    248  CG  PHE A  31     110.250  77.555  38.702  1.00 77.15           C  
ANISOU  248  CG  PHE A  31    10949   8725   9637   -573   -427   3096       C  
ATOM    249  CD1 PHE A  31     111.411  77.828  39.402  1.00 78.35           C  
ANISOU  249  CD1 PHE A  31    11087   8947   9737   -592   -324   3140       C  
ATOM    250  CD2 PHE A  31     109.188  76.981  39.376  1.00 78.62           C  
ANISOU  250  CD2 PHE A  31    11074   8817   9981   -469   -391   2945       C  
ATOM    251  CE1 PHE A  31     111.508  77.536  40.749  1.00 79.45           C  
ANISOU  251  CE1 PHE A  31    11156   9057   9973   -515   -198   3042       C  
ATOM    252  CE2 PHE A  31     109.279  76.687  40.721  1.00 76.67           C  
ANISOU  252  CE2 PHE A  31    10760   8545   9825   -396   -256   2841       C  
ATOM    253  CZ  PHE A  31     110.439  76.965  41.408  1.00 75.75           C  
ANISOU  253  CZ  PHE A  31    10636   8496   9650   -423   -163   2893       C  
ATOM    254  N   ASN A  32     110.920  76.661  33.949  1.00 92.08           N  
ANISOU  254  N   ASN A  32    13124  10996  10865   -939   -567   3357       N  
ATOM    255  CA  ASN A  32     110.666  76.971  32.546  1.00102.51           C  
ANISOU  255  CA  ASN A  32    14546  12354  12051  -1089   -725   3464       C  
ATOM    256  C   ASN A  32     109.474  76.187  32.000  1.00101.89           C  
ANISOU  256  C   ASN A  32    14478  12236  11999  -1058   -771   3382       C  
ATOM    257  O   ASN A  32     109.497  74.959  31.961  1.00 99.71           O  
ANISOU  257  O   ASN A  32    14185  12050  11649  -1005   -595   3264       O  
ATOM    258  CB  ASN A  32     111.910  76.721  31.689  1.00117.00           C  
ANISOU  258  CB  ASN A  32    16445  14397  13611  -1230   -612   3527       C  
ATOM    259  CG  ASN A  32     111.842  77.422  30.341  1.00135.62           C  
ANISOU  259  CG  ASN A  32    18922  16790  15817  -1431   -805   3678       C  
ATOM    260  ND2 ASN A  32     112.949  77.401  29.602  1.00162.22           N  
ANISOU  260  ND2 ASN A  32    22351  20339  18946  -1583   -719   3740       N  
ATOM    261  OD1 ASN A  32     110.808  77.980  29.973  1.00129.05           O  
ANISOU  261  OD1 ASN A  32    18124  15823  15085  -1458  -1032   3738       O  
ATOM    262  N   ASN A  33     108.434  76.910  31.590  1.00106.16           N  
ANISOU  262  N   ASN A  33    15044  12635  12658  -1091  -1016   3448       N  
ATOM    263  CA  ASN A  33     107.220  76.311  31.030  1.00105.26           C  
ANISOU  263  CA  ASN A  33    14940  12470  12585  -1075  -1099   3389       C  
ATOM    264  C   ASN A  33     106.297  75.678  32.070  1.00108.09           C  
ANISOU  264  C   ASN A  33    15192  12716  13162   -889  -1022   3217       C  
ATOM    265  O   ASN A  33     105.178  75.276  31.751  1.00111.43           O  
ANISOU  265  O   ASN A  33    15606  13071  13663   -860  -1105   3160       O  
ATOM    266  CB  ASN A  33     107.561  75.296  29.935  1.00101.31           C  
ANISOU  266  CB  ASN A  33    14520  12155  11819  -1179   -989   3372       C  
ATOM    267  CG  ASN A  33     108.046  75.954  28.661  1.00108.81           C  
ANISOU  267  CG  ASN A  33    15591  13193  12558  -1400  -1127   3542       C  
ATOM    268  ND2 ASN A  33     107.600  77.182  28.422  1.00112.08           N  
ANISOU  268  ND2 ASN A  33    16038  13476  13074  -1470  -1396   3687       N  
ATOM    269  OD1 ASN A  33     108.815  75.368  27.900  1.00111.73           O  
ANISOU  269  OD1 ASN A  33    16026  13748  12680  -1514   -994   3540       O  
ATOM    270  N   CYS A  34     106.768  75.598  33.310  1.00101.86           N  
ANISOU  270  N   CYS A  34    14325  11912  12467   -777   -867   3137       N  
ATOM    271  CA  CYS A  34     105.989  75.006  34.392  1.00 90.74           C  
ANISOU  271  CA  CYS A  34    12818  10410  11248   -621   -777   2971       C  
ATOM    272  C   CYS A  34     104.667  75.741  34.605  1.00 91.03           C  
ANISOU  272  C   CYS A  34    12802  10243  11541   -576   -982   2951       C  
ATOM    273  O   CYS A  34     104.630  76.969  34.647  1.00 91.74           O  
ANISOU  273  O   CYS A  34    12889  10224  11746   -613  -1153   3048       O  
ATOM    274  CB  CYS A  34     106.802  75.004  35.688  1.00 84.67           C  
ANISOU  274  CB  CYS A  34    11986   9657  10527   -544   -605   2918       C  
ATOM    275  SG  CYS A  34     105.900  74.411  37.133  1.00114.51           S  
ANISOU  275  SG  CYS A  34    15654  13321  14531   -385   -498   2720       S  
ATOM    276  N   GLU A  35     103.584  74.981  34.739  1.00 93.52           N  
ANISOU  276  N   GLU A  35    13071  10504  11959   -496   -966   2821       N  
ATOM    277  CA  GLU A  35     102.263  75.557  34.972  1.00 92.04           C  
ANISOU  277  CA  GLU A  35    12811  10123  12037   -442  -1144   2775       C  
ATOM    278  C   GLU A  35     101.789  75.276  36.393  1.00 84.31           C  
ANISOU  278  C   GLU A  35    11719   9060  11256   -309  -1011   2595       C  
ATOM    279  O   GLU A  35     101.051  76.069  36.978  1.00 83.77           O  
ANISOU  279  O   GLU A  35    11568   8824  11437   -261  -1120   2548       O  
ATOM    280  CB  GLU A  35     101.250  75.003  33.970  1.00 99.34           C  
ANISOU  280  CB  GLU A  35    13763  11040  12942   -470  -1257   2765       C  
ATOM    281  CG  GLU A  35     101.690  75.105  32.521  1.00114.43           C  
ANISOU  281  CG  GLU A  35    15800  13058  14620   -627  -1369   2930       C  
ATOM    282  CD  GLU A  35     100.643  74.585  31.556  1.00124.92           C  
ANISOU  282  CD  GLU A  35    17158  14374  15931   -668  -1493   2923       C  
ATOM    283  OE1 GLU A  35      99.454  74.924  31.730  1.00130.74           O  
ANISOU  283  OE1 GLU A  35    17820  14948  16908   -610  -1651   2881       O  
ATOM    284  OE2 GLU A  35     101.009  73.842  30.621  1.00127.54           O1-
ANISOU  284  OE2 GLU A  35    17585  14861  16015   -764  -1430   2954       O1-
ATOM    285  N   VAL A  36     102.214  74.140  36.938  1.00 78.63           N  
ANISOU  285  N   VAL A  36    10995   8454  10426   -258   -778   2492       N  
ATOM    286  CA  VAL A  36     101.847  73.744  38.294  1.00 75.62           C  
ANISOU  286  CA  VAL A  36    10524   8017  10192   -157   -636   2326       C  
ATOM    287  C   VAL A  36     103.083  73.367  39.098  1.00 74.69           C  
ANISOU  287  C   VAL A  36    10416   8011   9950   -148   -431   2322       C  
ATOM    288  O   VAL A  36     103.828  72.467  38.716  1.00 75.89           O  
ANISOU  288  O   VAL A  36    10622   8307   9904   -164   -304   2343       O  
ATOM    289  CB  VAL A  36     100.885  72.544  38.291  1.00 67.54           C  
ANISOU  289  CB  VAL A  36     9475   7000   9189    -98   -562   2182       C  
ATOM    290  CG1 VAL A  36     100.658  72.044  39.709  1.00 66.84           C  
ANISOU  290  CG1 VAL A  36     9309   6879   9208    -19   -394   2017       C  
ATOM    291  CG2 VAL A  36      99.570  72.919  37.633  1.00 84.77           C  
ANISOU  291  CG2 VAL A  36    11626   9058  11526   -100   -768   2171       C  
ATOM    292  N   VAL A  37     103.299  74.053  40.214  1.00 74.89           N  
ANISOU  292  N   VAL A  37    10386   7965  10103   -125   -401   2291       N  
ATOM    293  CA  VAL A  37     104.460  73.785  41.050  1.00 80.72           C  
ANISOU  293  CA  VAL A  37    11129   8799  10740   -125   -228   2298       C  
ATOM    294  C   VAL A  37     104.098  72.830  42.178  1.00 82.80           C  
ANISOU  294  C   VAL A  37    11340   9061  11059    -59    -62   2136       C  
ATOM    295  O   VAL A  37     103.495  73.232  43.171  1.00 85.46           O  
ANISOU  295  O   VAL A  37    11609   9291  11570    -34    -57   2032       O  
ATOM    296  CB  VAL A  37     105.043  75.079  41.642  1.00 80.28           C  
ANISOU  296  CB  VAL A  37    11056   8684  10761   -161   -284   2370       C  
ATOM    297  CG1 VAL A  37     106.327  74.780  42.401  1.00 77.82           C  
ANISOU  297  CG1 VAL A  37    10755   8487  10326   -173   -116   2398       C  
ATOM    298  CG2 VAL A  37     105.295  76.096  40.538  1.00 79.26           C  
ANISOU  298  CG2 VAL A  37    10983   8538  10594   -237   -472   2534       C  
ATOM    299  N   LEU A  38     104.472  71.564  42.017  1.00 83.91           N  
ANISOU  299  N   LEU A  38    11513   9318  11052    -39     75   2111       N  
ATOM    300  CA  LEU A  38     104.127  70.524  42.981  1.00 88.56           C  
ANISOU  300  CA  LEU A  38    12066   9910  11672     12    223   1970       C  
ATOM    301  C   LEU A  38     104.712  70.802  44.361  1.00 80.72           C  
ANISOU  301  C   LEU A  38    11039   8908  10724      4    318   1946       C  
ATOM    302  O   LEU A  38     104.111  70.462  45.380  1.00 78.66           O  
ANISOU  302  O   LEU A  38    10734   8595  10560     23    389   1816       O  
ATOM    303  CB  LEU A  38     104.591  69.156  42.479  1.00 97.01           C  
ANISOU  303  CB  LEU A  38    13183  11104  12574     30    343   1968       C  
ATOM    304  CG  LEU A  38     104.008  68.726  41.132  1.00105.48           C  
ANISOU  304  CG  LEU A  38    14298  12199  13579     24    271   1976       C  
ATOM    305  CD1 LEU A  38     104.676  67.456  40.629  1.00108.85           C  
ANISOU  305  CD1 LEU A  38    14771  12754  13834     33    406   1976       C  
ATOM    306  CD2 LEU A  38     102.501  68.543  41.236  1.00108.47           C  
ANISOU  306  CD2 LEU A  38    14637  12472  14106     61    209   1850       C  
ATOM    307  N   GLY A  39     105.886  71.422  44.386  1.00 79.82           N  
ANISOU  307  N   GLY A  39    10948   8851  10532    -37    319   2071       N  
ATOM    308  CA  GLY A  39     106.542  71.757  45.635  1.00 82.87           C  
ANISOU  308  CA  GLY A  39    11307   9236  10943    -61    397   2068       C  
ATOM    309  C   GLY A  39     106.410  73.228  45.977  1.00 83.64           C  
ANISOU  309  C   GLY A  39    11377   9232  11169   -100    290   2093       C  
ATOM    310  O   GLY A  39     105.304  73.741  46.143  1.00 80.02           O  
ANISOU  310  O   GLY A  39    10874   8648  10881    -86    212   1998       O  
ATOM    311  N   ASN A  40     107.543  73.913  46.074  1.00 84.91           N  
ANISOU  311  N   ASN A  40    11560   9443  11260   -148    285   2216       N  
ATOM    312  CA  ASN A  40     107.545  75.328  46.419  1.00 83.25           C  
ANISOU  312  CA  ASN A  40    11330   9137  11165   -191    187   2247       C  
ATOM    313  C   ASN A  40     108.066  76.229  45.302  1.00 85.46           C  
ANISOU  313  C   ASN A  40    11656   9429  11386   -232     49   2408       C  
ATOM    314  O   ASN A  40     108.764  75.778  44.394  1.00 86.06           O  
ANISOU  314  O   ASN A  40    11783   9623  11294   -247     61   2509       O  
ATOM    315  CB  ASN A  40     108.351  75.554  47.695  1.00 80.18           C  
ANISOU  315  CB  ASN A  40    10926   8775  10763   -235    289   2246       C  
ATOM    316  CG  ASN A  40     107.816  74.759  48.859  1.00 78.19           C  
ANISOU  316  CG  ASN A  40    10638   8507  10565   -223    414   2093       C  
ATOM    317  ND2 ASN A  40     108.709  74.304  49.728  1.00 88.26           N  
ANISOU  317  ND2 ASN A  40    11922   9866  11747   -259    529   2118       N  
ATOM    318  OD1 ASN A  40     106.611  74.551  48.975  1.00 72.20           O  
ANISOU  318  OD1 ASN A  40     9842   7662   9929   -191    401   1955       O  
ATOM    319  N   LEU A  41     107.711  77.506  45.379  1.00 84.47           N  
ANISOU  319  N   LEU A  41    11511   9179  11405   -259    -82   2424       N  
ATOM    320  CA  LEU A  41     108.175  78.495  44.419  1.00 82.42           C  
ANISOU  320  CA  LEU A  41    11300   8912  11105   -315   -233   2584       C  
ATOM    321  C   LEU A  41     109.063  79.512  45.121  1.00 86.04           C  
ANISOU  321  C   LEU A  41    11759   9360  11573   -374   -231   2653       C  
ATOM    322  O   LEU A  41     108.586  80.531  45.619  1.00 87.31           O  
ANISOU  322  O   LEU A  41    11883   9377  11915   -384   -313   2612       O  
ATOM    323  CB  LEU A  41     106.989  79.201  43.762  1.00 82.98           C  
ANISOU  323  CB  LEU A  41    11353   8826  11351   -301   -427   2568       C  
ATOM    324  CG  LEU A  41     107.338  80.340  42.803  1.00 87.68           C  
ANISOU  324  CG  LEU A  41    12001   9384  11929   -373   -617   2739       C  
ATOM    325  CD1 LEU A  41     108.177  79.822  41.647  1.00 89.64           C  
ANISOU  325  CD1 LEU A  41    12337   9800  11921   -429   -610   2879       C  
ATOM    326  CD2 LEU A  41     106.079  81.026  42.297  1.00 89.25           C  
ANISOU  326  CD2 LEU A  41    12167   9401  12342   -353   -824   2717       C  
ATOM    327  N   GLU A  42     110.358  79.223  45.166  1.00 86.37           N  
ANISOU  327  N   GLU A  42    11837   9550  11430   -415   -133   2750       N  
ATOM    328  CA  GLU A  42     111.314  80.103  45.822  1.00 81.58           C  
ANISOU  328  CA  GLU A  42    11234   8955  10808   -479   -122   2825       C  
ATOM    329  C   GLU A  42     112.088  80.933  44.807  1.00 91.07           C  
ANISOU  329  C   GLU A  42    12498  10200  11905   -555   -239   3005       C  
ATOM    330  O   GLU A  42     112.915  80.410  44.059  1.00 97.55           O  
ANISOU  330  O   GLU A  42    13359  11168  12536   -583   -195   3098       O  
ATOM    331  CB  GLU A  42     112.279  79.293  46.685  1.00 75.38           C  
ANISOU  331  CB  GLU A  42    10438   8301   9904   -483     59   2817       C  
ATOM    332  CG  GLU A  42     111.623  78.615  47.871  1.00 78.23           C  
ANISOU  332  CG  GLU A  42    10747   8617  10360   -441    171   2653       C  
ATOM    333  CD  GLU A  42     112.541  77.622  48.551  1.00 84.30           C  
ANISOU  333  CD  GLU A  42    11512   9518  11001   -445    327   2664       C  
ATOM    334  OE1 GLU A  42     113.497  77.152  47.900  1.00 81.61           O  
ANISOU  334  OE1 GLU A  42    11194   9305  10508   -448    361   2771       O  
ATOM    335  OE2 GLU A  42     112.307  77.308  49.736  1.00 91.73           O1-
ANISOU  335  OE2 GLU A  42    12422  10432  11998   -452    414   2563       O1-
ATOM    336  N   ILE A  43     111.805  82.230  44.784  1.00 91.16           N  
ANISOU  336  N   ILE A  43    12514  10078  12046   -595   -388   3045       N  
ATOM    337  CA  ILE A  43     112.512  83.163  43.920  1.00 82.55           C  
ANISOU  337  CA  ILE A  43    11488   9011  10868   -685   -517   3221       C  
ATOM    338  C   ILE A  43     113.427  84.029  44.772  1.00 82.55           C  
ANISOU  338  C   ILE A  43    11485   9012  10868   -747   -486   3273       C  
ATOM    339  O   ILE A  43     112.977  84.982  45.408  1.00 78.11           O  
ANISOU  339  O   ILE A  43    10895   8296  10488   -752   -558   3227       O  
ATOM    340  CB  ILE A  43     111.532  84.074  43.162  1.00 79.08           C  
ANISOU  340  CB  ILE A  43    11062   8402  10581   -696   -743   3254       C  
ATOM    341  CG1 ILE A  43     110.432  83.243  42.497  1.00 80.50           C  
ANISOU  341  CG1 ILE A  43    11231   8556  10800   -630   -779   3178       C  
ATOM    342  CG2 ILE A  43     112.272  84.916  42.136  1.00 79.41           C  
ANISOU  342  CG2 ILE A  43    11189   8485  10500   -808   -884   3452       C  
ATOM    343  CD1 ILE A  43     109.306  84.073  41.918  1.00 81.42           C  
ANISOU  343  CD1 ILE A  43    11339   8482  11115   -626  -1008   3189       C  
ATOM    344  N   THR A  44     114.712  83.691  44.792  1.00 84.71           N  
ANISOU  344  N   THR A  44    11782   9457  10948   -794   -377   3361       N  
ATOM    345  CA  THR A  44     115.672  84.413  45.620  1.00 83.95           C  
ANISOU  345  CA  THR A  44    11682   9382  10831   -860   -337   3416       C  
ATOM    346  C   THR A  44     116.913  84.840  44.840  1.00 87.38           C  
ANISOU  346  C   THR A  44    12174   9947  11078   -959   -368   3594       C  
ATOM    347  O   THR A  44     117.279  84.217  43.845  1.00 91.41           O  
ANISOU  347  O   THR A  44    12716  10584  11432   -974   -349   3655       O  
ATOM    348  CB  THR A  44     116.104  83.574  46.838  1.00 74.67           C  
ANISOU  348  CB  THR A  44    10455   8286   9629   -827   -148   3328       C  
ATOM    349  CG2 THR A  44     114.908  83.275  47.728  1.00 69.56           C  
ANISOU  349  CG2 THR A  44     9756   7512   9163   -757   -112   3145       C  
ATOM    350  OG1 THR A  44     116.681  82.340  46.394  1.00 71.23           O  
ANISOU  350  OG1 THR A  44    10019   8015   9029   -798    -34   3349       O  
ATOM    351  N   TYR A  45     117.549  85.912  45.302  1.00 89.02           N  
ANISOU  351  N   TYR A  45    12396  10125  11302  -1036   -411   3669       N  
ATOM    352  CA  TYR A  45     118.806  86.391  44.728  1.00 91.37           C  
ANISOU  352  CA  TYR A  45    12743  10550  11423  -1144   -428   3834       C  
ATOM    353  C   TYR A  45     118.727  86.674  43.232  1.00 91.02           C  
ANISOU  353  C   TYR A  45    12772  10528  11285  -1208   -567   3949       C  
ATOM    354  O   TYR A  45     119.709  86.503  42.510  1.00 86.28           O  
ANISOU  354  O   TYR A  45    12205  10090  10486  -1286   -530   4054       O  
ATOM    355  CB  TYR A  45     119.940  85.402  45.009  1.00 89.50           C  
ANISOU  355  CB  TYR A  45    12472  10514  11020  -1142   -243   3847       C  
ATOM    356  CG  TYR A  45     120.113  85.072  46.472  1.00 79.84           C  
ANISOU  356  CG  TYR A  45    11186   9283   9865  -1102   -116   3756       C  
ATOM    357  CD1 TYR A  45     120.006  83.765  46.925  1.00 79.52           C  
ANISOU  357  CD1 TYR A  45    11095   9307   9811  -1019     24   3659       C  
ATOM    358  CD2 TYR A  45     120.374  86.068  47.401  1.00 76.96           C  
ANISOU  358  CD2 TYR A  45    10821   8846   9576  -1161   -143   3770       C  
ATOM    359  CE1 TYR A  45     120.161  83.460  48.262  1.00 83.93           C  
ANISOU  359  CE1 TYR A  45    11607   9860  10421  -1004    125   3588       C  
ATOM    360  CE2 TYR A  45     120.529  85.773  48.737  1.00 79.55           C  
ANISOU  360  CE2 TYR A  45    11101   9175   9950  -1149    -31   3691       C  
ATOM    361  CZ  TYR A  45     120.422  84.469  49.164  1.00 84.68           C  
ANISOU  361  CZ  TYR A  45    11704   9892  10577  -1075     99   3605       C  
ATOM    362  OH  TYR A  45     120.579  84.173  50.499  1.00 84.37           O  
ANISOU  362  OH  TYR A  45    11628   9855  10573  -1084    197   3537       O  
ATOM    363  N   VAL A  46     117.558  87.104  42.770  1.00 96.77           N  
ANISOU  363  N   VAL A  46    13519  11093  12155  -1184   -727   3926       N  
ATOM    364  CA  VAL A  46     117.399  87.514  41.380  1.00 96.18           C  
ANISOU  364  CA  VAL A  46    13525  11017  12002  -1266   -895   4050       C  
ATOM    365  C   VAL A  46     117.805  88.973  41.226  1.00105.84           C  
ANISOU  365  C   VAL A  46    14805  12159  13250  -1381  -1058   4190       C  
ATOM    366  O   VAL A  46     117.142  89.870  41.747  1.00107.00           O  
ANISOU  366  O   VAL A  46    14935  12108  13612  -1359  -1176   4160       O  
ATOM    367  CB  VAL A  46     115.956  87.338  40.894  1.00 82.48           C  
ANISOU  367  CB  VAL A  46    11785   9136  10416  -1197  -1021   3981       C  
ATOM    368  CG1 VAL A  46     115.805  87.900  39.490  1.00 78.34           C  
ANISOU  368  CG1 VAL A  46    11354   8597   9814  -1307  -1226   4131       C  
ATOM    369  CG2 VAL A  46     115.564  85.873  40.933  1.00 75.19           C  
ANISOU  369  CG2 VAL A  46    10818   8301   9451  -1095   -866   3851       C  
ATOM    370  N   GLN A  47     118.898  89.202  40.505  1.00108.67           N  
ANISOU  370  N   GLN A  47    15229  12670  13392  -1510  -1060   4335       N  
ATOM    371  CA  GLN A  47     119.482  90.532  40.388  1.00107.31           C  
ANISOU  371  CA  GLN A  47    15116  12450  13207  -1636  -1194   4480       C  
ATOM    372  C   GLN A  47     118.761  91.414  39.369  1.00114.50           C  
ANISOU  372  C   GLN A  47    16108  13216  14181  -1714  -1459   4590       C  
ATOM    373  O   GLN A  47     117.844  90.964  38.682  1.00114.85           O  
ANISOU  373  O   GLN A  47    16163  13213  14261  -1677  -1539   4563       O  
ATOM    374  CB  GLN A  47     120.966  90.418  40.033  1.00101.22           C  
ANISOU  374  CB  GLN A  47    14377  11907  12175  -1755  -1085   4588       C  
ATOM    375  CG  GLN A  47     121.748  89.520  40.974  1.00 93.63           C  
ANISOU  375  CG  GLN A  47    13330  11090  11155  -1684   -841   4497       C  
ATOM    376  CD  GLN A  47     121.706  90.011  42.406  1.00 92.87           C  
ANISOU  376  CD  GLN A  47    13178  10880  11230  -1628   -805   4428       C  
ATOM    377  NE2 GLN A  47     121.599  89.081  43.347  1.00 98.74           N  
ANISOU  377  NE2 GLN A  47    13840  11653  12025  -1516   -640   4293       N  
ATOM    378  OE1 GLN A  47     121.770  91.212  42.664  1.00 88.70           O  
ANISOU  378  OE1 GLN A  47    12683  10236  10782  -1695   -926   4494       O  
ATOM    379  N   ARG A  48     119.181  92.675  39.287  1.00123.72           N  
ANISOU  379  N   ARG A  48    17333  14309  15364  -1827  -1605   4722       N  
ATOM    380  CA  ARG A  48     118.642  93.612  38.306  1.00135.11           C  
ANISOU  380  CA  ARG A  48    18864  15613  16860  -1926  -1880   4860       C  
ATOM    381  C   ARG A  48     118.711  93.016  36.907  1.00141.74           C  
ANISOU  381  C   ARG A  48    19783  16602  17471  -2024  -1920   4949       C  
ATOM    382  O   ARG A  48     119.394  92.015  36.689  1.00145.17           O  
ANISOU  382  O   ARG A  48    20208  17259  17693  -2034  -1723   4915       O  
ATOM    383  CB  ARG A  48     119.413  94.933  38.347  1.00143.33           C  
ANISOU  383  CB  ARG A  48    19970  16609  17879  -2064  -1998   5009       C  
ATOM    384  CG  ARG A  48     119.096  95.804  39.551  1.00150.03           C  
ANISOU  384  CG  ARG A  48    20759  17249  18997  -1990  -2031   4934       C  
ATOM    385  CD  ARG A  48     117.723  96.440  39.420  1.00155.90           C  
ANISOU  385  CD  ARG A  48    21488  17708  20039  -1928  -2263   4907       C  
ATOM    386  NE  ARG A  48     117.602  97.217  38.189  1.00161.58           N  
ANISOU  386  NE  ARG A  48    22318  18359  20718  -2069  -2533   5104       N  
ATOM    387  CZ  ARG A  48     117.994  98.480  38.061  1.00164.60           C  
ANISOU  387  CZ  ARG A  48    22769  18635  21137  -2189  -2707   5248       C  
ATOM    388  NH1 ARG A  48     117.846  99.109  36.902  1.00166.93           N1+
ANISOU  388  NH1 ARG A  48    23172  18870  21384  -2329  -2964   5435       N1+
ATOM    389  NH2 ARG A  48     118.534  99.116  39.091  1.00165.20           N  
ANISOU  389  NH2 ARG A  48    22811  18664  21292  -2182  -2630   5209       N  
ATOM    390  N   ASN A  49     118.011  93.633  35.961  1.00147.27           N  
ANISOU  390  N   ASN A  49    20560  17174  18221  -2105  -2178   5063       N  
ATOM    391  CA  ASN A  49     117.934  93.097  34.609  1.00156.64           C  
ANISOU  391  CA  ASN A  49    21831  18487  19197  -2216  -2236   5145       C  
ATOM    392  C   ASN A  49     117.227  91.745  34.627  1.00144.72           C  
ANISOU  392  C   ASN A  49    20253  17031  17704  -2075  -2095   4982       C  
ATOM    393  O   ASN A  49     116.015  91.679  34.835  1.00144.26           O  
ANISOU  393  O   ASN A  49    20145  16791  17876  -1956  -2193   4900       O  
ATOM    394  CB  ASN A  49     119.335  92.958  34.013  1.00175.18           C  
ANISOU  394  CB  ASN A  49    24250  21097  21212  -2389  -2117   5248       C  
ATOM    395  CG  ASN A  49     119.314  92.586  32.541  1.00194.10           C  
ANISOU  395  CG  ASN A  49    26753  23625  23373  -2550  -2193   5345       C  
ATOM    396  ND2 ASN A  49     119.773  91.375  32.224  1.00211.20           N  
ANISOU  396  ND2 ASN A  49    28895  26015  25337  -2545  -1966   5257       N  
ATOM    397  OD1 ASN A  49     118.887  93.375  31.699  1.00194.52           O  
ANISOU  397  OD1 ASN A  49    26906  23574  23428  -2685  -2456   5497       O  
ATOM    398  N   TYR A  50     118.002  90.680  34.421  1.00130.25           N  
ANISOU  398  N   TYR A  50    18413  15442  15636  -2090  -1864   4931       N  
ATOM    399  CA  TYR A  50     117.528  89.293  34.489  1.00113.54           C  
ANISOU  399  CA  TYR A  50    16231  13402  13508  -1960  -1693   4771       C  
ATOM    400  C   TYR A  50     116.060  89.095  34.130  1.00103.75           C  
ANISOU  400  C   TYR A  50    14985  11998  12437  -1885  -1850   4723       C  
ATOM    401  O   TYR A  50     115.165  89.535  34.848  1.00 99.41           O  
ANISOU  401  O   TYR A  50    14373  11235  12164  -1768  -1946   4658       O  
ATOM    402  CB  TYR A  50     117.829  88.681  35.862  1.00112.82           C  
ANISOU  402  CB  TYR A  50    16020  13336  13510  -1796  -1456   4611       C  
ATOM    403  CG  TYR A  50     119.280  88.298  36.032  1.00122.18           C  
ANISOU  403  CG  TYR A  50    17193  14747  14484  -1852  -1244   4626       C  
ATOM    404  CD1 TYR A  50     119.811  87.203  35.362  1.00129.17           C  
ANISOU  404  CD1 TYR A  50    18082  15844  15154  -1885  -1081   4593       C  
ATOM    405  CD2 TYR A  50     120.122  89.033  36.854  1.00124.90           C  
ANISOU  405  CD2 TYR A  50    17515  15089  14851  -1876  -1207   4669       C  
ATOM    406  CE1 TYR A  50     121.140  86.851  35.507  1.00130.09           C  
ANISOU  406  CE1 TYR A  50    18169  16158  15102  -1932   -890   4598       C  
ATOM    407  CE2 TYR A  50     121.452  88.688  37.005  1.00127.74           C  
ANISOU  407  CE2 TYR A  50    17852  15653  15030  -1928  -1023   4686       C  
ATOM    408  CZ  TYR A  50     121.955  87.596  36.329  1.00128.37           C  
ANISOU  408  CZ  TYR A  50    17925  15935  14916  -1952   -866   4649       C  
ATOM    409  OH  TYR A  50     123.278  87.248  36.476  1.00128.81           O  
ANISOU  409  OH  TYR A  50    17941  16186  14816  -1998   -683   4657       O  
ATOM    410  N   ASP A  51     115.824  88.408  33.019  1.00100.72           N  
ANISOU  410  N   ASP A  51    14662  11721  11887  -1959  -1867   4746       N  
ATOM    411  CA  ASP A  51     114.472  88.182  32.529  1.00 98.88           C  
ANISOU  411  CA  ASP A  51    14433  11353  11785  -1912  -2027   4718       C  
ATOM    412  C   ASP A  51     113.745  87.099  33.325  1.00 95.93           C  
ANISOU  412  C   ASP A  51    13945  10949  11556  -1705  -1860   4508       C  
ATOM    413  O   ASP A  51     114.128  85.929  33.295  1.00 86.01           O  
ANISOU  413  O   ASP A  51    12666   9865  10148  -1668  -1639   4411       O  
ATOM    414  CB  ASP A  51     114.509  87.813  31.046  1.00102.43           C  
ANISOU  414  CB  ASP A  51    14996  11940  11981  -2087  -2100   4818       C  
ATOM    415  CG  ASP A  51     113.135  87.801  30.416  1.00109.40           C  
ANISOU  415  CG  ASP A  51    15900  12671  12994  -2076  -2323   4834       C  
ATOM    416  OD1 ASP A  51     112.142  87.954  31.155  1.00107.60           O  
ANISOU  416  OD1 ASP A  51    15582  12240  13062  -1913  -2394   4744       O  
ATOM    417  OD2 ASP A  51     113.049  87.639  29.180  1.00117.04           O1-
ANISOU  417  OD2 ASP A  51    16974  13727  13770  -2240  -2427   4934       O1-
ATOM    418  N   LEU A  52     112.693  87.501  34.032  1.00 98.97           N  
ANISOU  418  N   LEU A  52    14254  11107  12241  -1575  -1968   4433       N  
ATOM    419  CA  LEU A  52     111.864  86.567  34.790  1.00 92.96           C  
ANISOU  419  CA  LEU A  52    13387  10297  11635  -1392  -1836   4234       C  
ATOM    420  C   LEU A  52     110.510  86.363  34.114  1.00 96.15           C  
ANISOU  420  C   LEU A  52    13793  10580  12161  -1366  -2012   4216       C  
ATOM    421  O   LEU A  52     109.487  86.222  34.784  1.00 99.30           O  
ANISOU  421  O   LEU A  52    14097  10826  12807  -1224  -2025   4082       O  
ATOM    422  CB  LEU A  52     111.660  87.065  36.223  1.00 87.55           C  
ANISOU  422  CB  LEU A  52    12599   9460  11206  -1264  -1787   4125       C  
ATOM    423  CG  LEU A  52     112.833  86.929  37.198  1.00 88.64           C  
ANISOU  423  CG  LEU A  52    12705   9719  11254  -1247  -1561   4085       C  
ATOM    424  CD1 LEU A  52     112.461  87.507  38.557  1.00 74.58           C  
ANISOU  424  CD1 LEU A  52    10832   7768   9735  -1144  -1543   3976       C  
ATOM    425  CD2 LEU A  52     113.267  85.477  37.333  1.00 83.29           C  
ANISOU  425  CD2 LEU A  52    12000   9239  10408  -1190  -1306   3981       C  
ATOM    426  N   SER A  53     110.512  86.344  32.785  1.00 93.00           N  
ANISOU  426  N   SER A  53    13500  10254  11581  -1514  -2146   4350       N  
ATOM    427  CA  SER A  53     109.278  86.200  32.023  1.00 80.80           C  
ANISOU  427  CA  SER A  53    11968   8602  10129  -1517  -2341   4362       C  
ATOM    428  C   SER A  53     108.721  84.782  32.068  1.00103.28           C  
ANISOU  428  C   SER A  53    14766  11533  12943  -1410  -2167   4194       C  
ATOM    429  O   SER A  53     107.511  84.584  31.977  1.00110.22           O  
ANISOU  429  O   SER A  53    15599  12281  13998  -1336  -2280   4132       O  
ATOM    430  CB  SER A  53     109.485  86.630  30.569  1.00 91.08           C  
ANISOU  430  CB  SER A  53    13414   9966  11225  -1738  -2547   4569       C  
ATOM    431  OG  SER A  53     109.430  88.039  30.442  1.00 94.59           O  
ANISOU  431  OG  SER A  53    13896  10241  11801  -1820  -2813   4729       O  
ATOM    432  N   PHE A  54     109.599  83.795  32.208  1.00 94.93           N  
ANISOU  432  N   PHE A  54    13713  10687  11669  -1402  -1897   4120       N  
ATOM    433  CA  PHE A  54     109.158  82.404  32.201  1.00 94.88           C  
ANISOU  433  CA  PHE A  54    13669  10766  11614  -1311  -1726   3967       C  
ATOM    434  C   PHE A  54     108.222  82.083  33.363  1.00 93.65           C  
ANISOU  434  C   PHE A  54    13387  10463  11734  -1114  -1666   3789       C  
ATOM    435  O   PHE A  54     107.579  81.034  33.376  1.00 95.60           O  
ANISOU  435  O   PHE A  54    13598  10735  11991  -1032  -1572   3662       O  
ATOM    436  CB  PHE A  54     110.351  81.444  32.185  1.00 95.29           C  
ANISOU  436  CB  PHE A  54    13738  11057  11410  -1334  -1449   3919       C  
ATOM    437  CG  PHE A  54     111.299  81.628  33.333  1.00 92.52           C  
ANISOU  437  CG  PHE A  54    13324  10738  11092  -1266  -1282   3881       C  
ATOM    438  CD1 PHE A  54     111.010  81.101  34.580  1.00 92.51           C  
ANISOU  438  CD1 PHE A  54    13217  10679  11256  -1096  -1133   3722       C  
ATOM    439  CD2 PHE A  54     112.489  82.313  33.159  1.00 94.13           C  
ANISOU  439  CD2 PHE A  54    13579  11036  11151  -1387  -1274   4006       C  
ATOM    440  CE1 PHE A  54     111.885  81.264  35.636  1.00 93.64           C  
ANISOU  440  CE1 PHE A  54    13307  10853  11418  -1050   -990   3695       C  
ATOM    441  CE2 PHE A  54     113.368  82.478  34.211  1.00 98.08           C  
ANISOU  441  CE2 PHE A  54    14020  11567  11679  -1331  -1127   3976       C  
ATOM    442  CZ  PHE A  54     113.066  81.953  35.451  1.00 96.24           C  
ANISOU  442  CZ  PHE A  54    13684  11273  11610  -1164   -988   3824       C  
ATOM    443  N   LEU A  55     108.142  82.991  34.331  1.00 90.74           N  
ANISOU  443  N   LEU A  55    12951   9942  11583  -1048  -1717   3774       N  
ATOM    444  CA  LEU A  55     107.267  82.802  35.483  1.00 90.33           C  
ANISOU  444  CA  LEU A  55    12778   9748  11796   -883  -1657   3597       C  
ATOM    445  C   LEU A  55     105.803  83.030  35.121  1.00 93.86           C  
ANISOU  445  C   LEU A  55    13185  10009  12468   -842  -1870   3568       C  
ATOM    446  O   LEU A  55     104.902  82.567  35.822  1.00 92.06           O  
ANISOU  446  O   LEU A  55    12859   9693  12428   -715  -1810   3401       O  
ATOM    447  CB  LEU A  55     107.673  83.733  36.626  1.00 74.56           C  
ANISOU  447  CB  LEU A  55    10724   7651   9956   -845  -1635   3579       C  
ATOM    448  CG  LEU A  55     108.977  83.398  37.349  1.00 82.17           C  
ANISOU  448  CG  LEU A  55    11689   8775  10756   -847  -1398   3563       C  
ATOM    449  CD1 LEU A  55     109.237  84.401  38.459  1.00 79.47           C  
ANISOU  449  CD1 LEU A  55    11295   8317  10585   -822  -1402   3545       C  
ATOM    450  CD2 LEU A  55     108.938  81.985  37.904  1.00 71.68           C  
ANISOU  450  CD2 LEU A  55    10311   7557   9368   -747  -1156   3402       C  
ATOM    451  N   LYS A  56     105.574  83.740  34.022  1.00 96.55           N  
ANISOU  451  N   LYS A  56    13602  10294  12790   -960  -2125   3735       N  
ATOM    452  CA  LYS A  56     104.221  84.088  33.599  1.00 95.19           C  
ANISOU  452  CA  LYS A  56    13390   9930  12848   -935  -2369   3739       C  
ATOM    453  C   LYS A  56     103.341  82.861  33.386  1.00 96.33           C  
ANISOU  453  C   LYS A  56    13500  10118  12983   -864  -2292   3607       C  
ATOM    454  O   LYS A  56     102.116  82.949  33.464  1.00103.49           O  
ANISOU  454  O   LYS A  56    14325  10859  14136   -788  -2424   3535       O  
ATOM    455  CB  LYS A  56     104.256  84.929  32.320  1.00 93.11           C  
ANISOU  455  CB  LYS A  56    13238   9631  12509  -1105  -2660   3969       C  
ATOM    456  CG  LYS A  56     104.927  86.282  32.482  1.00 94.49           C  
ANISOU  456  CG  LYS A  56    13444   9717  12740  -1179  -2790   4109       C  
ATOM    457  CD  LYS A  56     104.713  87.156  31.259  1.00 84.45           C  
ANISOU  457  CD  LYS A  56    12274   8365  11448  -1344  -3122   4336       C  
ATOM    458  CE  LYS A  56     105.254  86.493  30.005  1.00115.60           C  
ANISOU  458  CE  LYS A  56    16363  12538  15021  -1518  -3103   4452       C  
ATOM    459  NZ  LYS A  56     105.038  87.343  28.801  1.00119.06           N1+
ANISOU  459  NZ  LYS A  56    16914  12904  15421  -1706  -3438   4685       N1+
ATOM    460  N   THR A  57     103.966  81.719  33.121  1.00 88.74           N  
ANISOU  460  N   THR A  57    12594   9374  11747   -888  -2078   3571       N  
ATOM    461  CA  THR A  57     103.224  80.502  32.816  1.00 87.34           C  
ANISOU  461  CA  THR A  57    12402   9255  11526   -839  -2000   3457       C  
ATOM    462  C   THR A  57     102.926  79.662  34.056  1.00 90.21           C  
ANISOU  462  C   THR A  57    12656   9614  12005   -674  -1765   3237       C  
ATOM    463  O   THR A  57     102.492  78.517  33.943  1.00 97.20           O  
ANISOU  463  O   THR A  57    13532  10572  12828   -628  -1650   3128       O  
ATOM    464  CB  THR A  57     103.967  79.633  31.784  1.00 88.98           C  
ANISOU  464  CB  THR A  57    12730   9694  11384   -960  -1896   3520       C  
ATOM    465  CG2 THR A  57     104.346  80.463  30.567  1.00 93.41           C  
ANISOU  465  CG2 THR A  57    13413  10282  11797  -1155  -2115   3741       C  
ATOM    466  OG1 THR A  57     105.152  79.088  32.375  1.00 89.04           O  
ANISOU  466  OG1 THR A  57    12739   9862  11230   -936  -1625   3465       O  
ATOM    467  N   ILE A  58     103.159  80.230  35.235  1.00 85.40           N  
ANISOU  467  N   ILE A  58    11970   8920  11559   -598  -1697   3172       N  
ATOM    468  CA  ILE A  58     102.859  79.533  36.481  1.00 84.22           C  
ANISOU  468  CA  ILE A  58    11720   8757  11522   -464  -1488   2968       C  
ATOM    469  C   ILE A  58     101.462  79.890  36.978  1.00 90.82           C  
ANISOU  469  C   ILE A  58    12439   9383  12686   -372  -1604   2845       C  
ATOM    470  O   ILE A  58     101.191  81.041  37.318  1.00 92.97           O  
ANISOU  470  O   ILE A  58    12659   9487  13180   -364  -1748   2866       O  
ATOM    471  CB  ILE A  58     103.893  79.846  37.576  1.00 82.89           C  
ANISOU  471  CB  ILE A  58    11532   8629  11335   -446  -1325   2947       C  
ATOM    472  CG1 ILE A  58     105.244  79.226  37.222  1.00 86.85           C  
ANISOU  472  CG1 ILE A  58    12121   9352  11527   -514  -1165   3027       C  
ATOM    473  CG2 ILE A  58     103.414  79.328  38.922  1.00 79.65           C  
ANISOU  473  CG2 ILE A  58    11016   8169  11079   -329  -1153   2741       C  
ATOM    474  CD1 ILE A  58     106.228  79.216  38.370  1.00 89.15           C  
ANISOU  474  CD1 ILE A  58    12382   9704  11788   -483   -973   2986       C  
ATOM    475  N   GLN A  59     100.580  78.895  37.019  1.00 94.15           N  
ANISOU  475  N   GLN A  59    12816   9811  13145   -304  -1537   2708       N  
ATOM    476  CA  GLN A  59      99.181  79.122  37.369  1.00 93.46           C  
ANISOU  476  CA  GLN A  59    12610   9537  13364   -223  -1644   2580       C  
ATOM    477  C   GLN A  59      98.871  78.767  38.820  1.00 89.29           C  
ANISOU  477  C   GLN A  59    11972   8969  12984   -121  -1443   2362       C  
ATOM    478  O   GLN A  59      98.055  79.423  39.463  1.00 90.96           O  
ANISOU  478  O   GLN A  59    12069   9005  13485    -65  -1510   2254       O  
ATOM    479  CB  GLN A  59      98.262  78.330  36.436  1.00 94.72           C  
ANISOU  479  CB  GLN A  59    12784   9715  13491   -227  -1727   2568       C  
ATOM    480  CG  GLN A  59      98.562  78.522  34.961  1.00102.76           C  
ANISOU  480  CG  GLN A  59    13926  10798  14320   -355  -1910   2777       C  
ATOM    481  CD  GLN A  59      97.657  77.691  34.075  1.00114.78           C  
ANISOU  481  CD  GLN A  59    15467  12348  15797   -370  -1982   2758       C  
ATOM    482  NE2 GLN A  59      98.172  77.279  32.922  1.00116.32           N  
ANISOU  482  NE2 GLN A  59    15794  12692  15712   -490  -2009   2890       N  
ATOM    483  OE1 GLN A  59      96.507  77.424  34.422  1.00122.12           O  
ANISOU  483  OE1 GLN A  59    16293  13169  16938   -284  -2008   2621       O  
ATOM    484  N   GLU A  60      99.516  77.726  39.334  1.00 82.77           N  
ANISOU  484  N   GLU A  60    11179   8304  11965   -105  -1197   2294       N  
ATOM    485  CA  GLU A  60      99.260  77.294  40.704  1.00 83.92           C  
ANISOU  485  CA  GLU A  60    11238   8431  12217    -33  -1003   2098       C  
ATOM    486  C   GLU A  60     100.483  76.679  41.381  1.00 80.50           C  
ANISOU  486  C   GLU A  60    10858   8159  11570    -47   -774   2101       C  
ATOM    487  O   GLU A  60     101.221  75.904  40.777  1.00 82.67           O  
ANISOU  487  O   GLU A  60    11220   8590  11600    -77   -699   2183       O  
ATOM    488  CB  GLU A  60      98.081  76.319  40.749  1.00 93.13           C  
ANISOU  488  CB  GLU A  60    12346   9578  13462     28   -960   1938       C  
ATOM    489  CG  GLU A  60      98.087  75.285  39.636  1.00108.45           C  
ANISOU  489  CG  GLU A  60    14374  11647  15186      3   -961   2004       C  
ATOM    490  CD  GLU A  60      97.042  74.203  39.836  1.00119.44           C  
ANISOU  490  CD  GLU A  60    15713  13037  16631     61   -880   1836       C  
ATOM    491  OE1 GLU A  60      96.945  73.670  40.962  1.00118.95           O  
ANISOU  491  OE1 GLU A  60    15599  12987  16609    105   -698   1681       O  
ATOM    492  OE2 GLU A  60      96.323  73.879  38.867  1.00124.83           O1-
ANISOU  492  OE2 GLU A  60    16411  13710  17307     50  -1000   1861       O1-
ATOM    493  N   VAL A  61     100.685  77.038  42.643  1.00 74.45           N  
ANISOU  493  N   VAL A  61    10034   7349  10905    -30   -667   2006       N  
ATOM    494  CA  VAL A  61     101.760  76.472  43.443  1.00 70.56           C  
ANISOU  494  CA  VAL A  61     9577   6990  10241    -45   -460   2001       C  
ATOM    495  C   VAL A  61     101.168  75.722  44.629  1.00 78.81           C  
ANISOU  495  C   VAL A  61    10555   8023  11368     -3   -293   1799       C  
ATOM    496  O   VAL A  61     100.399  76.286  45.408  1.00 82.62           O  
ANISOU  496  O   VAL A  61    10947   8374  12070     13   -306   1666       O  
ATOM    497  CB  VAL A  61     102.706  77.568  43.959  1.00 69.03           C  
ANISOU  497  CB  VAL A  61     9393   6778  10056    -94   -472   2087       C  
ATOM    498  CG1 VAL A  61     103.766  76.971  44.872  1.00 68.25           C  
ANISOU  498  CG1 VAL A  61     9321   6812   9801   -111   -266   2077       C  
ATOM    499  CG2 VAL A  61     103.343  78.303  42.793  1.00 67.49           C  
ANISOU  499  CG2 VAL A  61     9275   6606   9764   -153   -634   2292       C  
ATOM    500  N   ALA A  62     101.524  74.449  44.760  1.00 80.34           N  
ANISOU  500  N   ALA A  62    10789   8349  11387      8   -138   1773       N  
ATOM    501  CA  ALA A  62     100.987  73.607  45.825  1.00 79.73           C  
ANISOU  501  CA  ALA A  62    10665   8273  11356     31     17   1596       C  
ATOM    502  C   ALA A  62     101.490  74.034  47.201  1.00 83.22           C  
ANISOU  502  C   ALA A  62    11078   8704  11838     -8    127   1541       C  
ATOM    503  O   ALA A  62     100.701  74.296  48.107  1.00 83.97           O  
ANISOU  503  O   ALA A  62    11096   8704  12103    -13    163   1380       O  
ATOM    504  CB  ALA A  62     101.326  72.148  45.565  1.00 78.16           C  
ANISOU  504  CB  ALA A  62    10526   8211  10961     48    140   1602       C  
ATOM    505  N   GLY A  63     102.808  74.098  47.354  1.00 85.82           N  
ANISOU  505  N   GLY A  63    11466   9133  12008    -46    183   1668       N  
ATOM    506  CA  GLY A  63     103.408  74.480  48.618  1.00 85.55           C  
ANISOU  506  CA  GLY A  63    11418   9105  11984    -98    281   1639       C  
ATOM    507  C   GLY A  63     103.291  75.965  48.899  1.00 82.77           C  
ANISOU  507  C   GLY A  63    11021   8629  11798   -129    183   1637       C  
ATOM    508  O   GLY A  63     102.199  76.531  48.845  1.00 85.09           O  
ANISOU  508  O   GLY A  63    11246   8786  12300   -105     96   1531       O  
ATOM    509  N   TYR A  64     104.420  76.599  49.201  1.00 76.95           N  
ANISOU  509  N   TYR A  64    10319   7935  10982   -182    194   1751       N  
ATOM    510  CA  TYR A  64     104.436  78.027  49.495  1.00 72.98           C  
ANISOU  510  CA  TYR A  64     9783   7318  10629   -218    105   1758       C  
ATOM    511  C   TYR A  64     105.265  78.804  48.481  1.00 77.47           C  
ANISOU  511  C   TYR A  64    10409   7907  11120   -235    -30   1962       C  
ATOM    512  O   TYR A  64     106.108  78.241  47.784  1.00 79.82           O  
ANISOU  512  O   TYR A  64    10774   8337  11215   -238    -14   2098       O  
ATOM    513  CB  TYR A  64     104.966  78.287  50.907  1.00 70.56           C  
ANISOU  513  CB  TYR A  64     9465   7027  10318   -292    234   1695       C  
ATOM    514  CG  TYR A  64     106.416  77.907  51.103  1.00 76.11           C  
ANISOU  514  CG  TYR A  64    10239   7885  10795   -338    315   1843       C  
ATOM    515  CD1 TYR A  64     107.439  78.785  50.765  1.00 75.35           C  
ANISOU  515  CD1 TYR A  64    10180   7814  10634   -376    246   2005       C  
ATOM    516  CD2 TYR A  64     106.763  76.673  51.633  1.00 82.23           C  
ANISOU  516  CD2 TYR A  64    11037   8776  11431   -345    455   1821       C  
ATOM    517  CE1 TYR A  64     108.765  78.440  50.945  1.00 72.79           C  
ANISOU  517  CE1 TYR A  64     9907   7632  10118   -417    320   2134       C  
ATOM    518  CE2 TYR A  64     108.084  76.321  51.818  1.00 81.93           C  
ANISOU  518  CE2 TYR A  64    11048   8868  11213   -381    519   1955       C  
ATOM    519  CZ  TYR A  64     109.080  77.206  51.472  1.00 78.25           C  
ANISOU  519  CZ  TYR A  64    10610   8430  10691   -415    454   2108       C  
ATOM    520  OH  TYR A  64     110.396  76.852  51.657  1.00 80.11           O  
ANISOU  520  OH  TYR A  64    10882   8797  10761   -451    518   2236       O  
ATOM    521  N   VAL A  65     105.019  80.106  48.411  1.00 80.12           N  
ANISOU  521  N   VAL A  65    10715   8106  11622   -252   -162   1977       N  
ATOM    522  CA  VAL A  65     105.760  80.979  47.515  1.00 82.81           C  
ANISOU  522  CA  VAL A  65    11113   8450  11902   -287   -305   2171       C  
ATOM    523  C   VAL A  65     106.680  81.896  48.311  1.00 84.04           C  
ANISOU  523  C   VAL A  65    11279   8602  12051   -357   -273   2218       C  
ATOM    524  O   VAL A  65     106.221  82.709  49.112  1.00 85.52           O  
ANISOU  524  O   VAL A  65    11406   8657  12432   -373   -282   2108       O  
ATOM    525  CB  VAL A  65     104.812  81.829  46.651  1.00 90.57           C  
ANISOU  525  CB  VAL A  65    12064   9266  13082   -260   -522   2186       C  
ATOM    526  CG1 VAL A  65     105.602  82.802  45.794  1.00 92.88           C  
ANISOU  526  CG1 VAL A  65    12426   9557  13307   -318   -679   2394       C  
ATOM    527  CG2 VAL A  65     103.944  80.933  45.782  1.00 94.16           C  
ANISOU  527  CG2 VAL A  65    12516   9734  13527   -202   -567   2157       C  
ATOM    528  N   LEU A  66     107.982  81.752  48.091  1.00 84.16           N  
ANISOU  528  N   LEU A  66    11365   8765  11847   -405   -230   2375       N  
ATOM    529  CA  LEU A  66     108.972  82.584  48.762  1.00 76.56           C  
ANISOU  529  CA  LEU A  66    10420   7818  10850   -480   -203   2443       C  
ATOM    530  C   LEU A  66     109.569  83.586  47.785  1.00 75.73           C  
ANISOU  530  C   LEU A  66    10370   7698  10705   -525   -366   2629       C  
ATOM    531  O   LEU A  66     110.068  83.210  46.727  1.00 81.42           O  
ANISOU  531  O   LEU A  66    11150   8526  11260   -533   -407   2763       O  
ATOM    532  CB  LEU A  66     110.081  81.718  49.364  1.00 73.65           C  
ANISOU  532  CB  LEU A  66    10082   7628  10272   -512    -32   2484       C  
ATOM    533  CG  LEU A  66     111.202  82.467  50.087  1.00 75.82           C  
ANISOU  533  CG  LEU A  66    10377   7944  10488   -598      4   2564       C  
ATOM    534  CD1 LEU A  66     110.634  83.350  51.185  1.00 79.24           C  
ANISOU  534  CD1 LEU A  66    10760   8232  11115   -636     11   2426       C  
ATOM    535  CD2 LEU A  66     112.226  81.499  50.655  1.00 73.78           C  
ANISOU  535  CD2 LEU A  66    10137   7856  10042   -623    159   2605       C  
ATOM    536  N   ILE A  67     109.507  84.864  48.143  1.00 72.23           N  
ANISOU  536  N   ILE A  67     9909   7120  10415   -566   -456   2629       N  
ATOM    537  CA  ILE A  67     110.091  85.925  47.331  1.00 73.00           C  
ANISOU  537  CA  ILE A  67    10064   7189  10485   -625   -619   2809       C  
ATOM    538  C   ILE A  67     110.939  86.829  48.216  1.00 78.08           C  
ANISOU  538  C   ILE A  67    10714   7822  11131   -703   -579   2838       C  
ATOM    539  O   ILE A  67     110.440  87.800  48.784  1.00 75.01           O  
ANISOU  539  O   ILE A  67    10281   7265  10954   -713   -637   2756       O  
ATOM    540  CB  ILE A  67     109.008  86.773  46.637  1.00 72.30           C  
ANISOU  540  CB  ILE A  67     9949   6898  10625   -597   -835   2802       C  
ATOM    541  CG1 ILE A  67     108.125  85.895  45.750  1.00 70.81           C  
ANISOU  541  CG1 ILE A  67     9753   6718  10435   -529   -886   2775       C  
ATOM    542  CG2 ILE A  67     109.639  87.883  45.814  1.00 70.94           C  
ANISOU  542  CG2 ILE A  67     9847   6692  10416   -675  -1016   3002       C  
ATOM    543  CD1 ILE A  67     107.084  86.674  44.977  1.00 72.31           C  
ANISOU  543  CD1 ILE A  67     9917   6713  10845   -506  -1121   2792       C  
ATOM    544  N   ALA A  68     112.223  86.507  48.333  1.00 84.30           N  
ANISOU  544  N   ALA A  68    11551   8786  11691   -759   -480   2950       N  
ATOM    545  CA  ALA A  68     113.099  87.222  49.252  1.00 85.54           C  
ANISOU  545  CA  ALA A  68    11717   8959  11827   -840   -423   2978       C  
ATOM    546  C   ALA A  68     114.500  87.426  48.691  1.00 84.15           C  
ANISOU  546  C   ALA A  68    11610   8933  11428   -917   -437   3182       C  
ATOM    547  O   ALA A  68     115.029  86.567  47.988  1.00 81.63           O  
ANISOU  547  O   ALA A  68    11320   8769  10924   -906   -393   3265       O  
ATOM    548  CB  ALA A  68     113.168  86.492  50.585  1.00 87.49           C  
ANISOU  548  CB  ALA A  68    11921   9266  12054   -840   -229   2840       C  
ATOM    549  N   LEU A  69     115.091  88.572  49.015  1.00 88.18           N  
ANISOU  549  N   LEU A  69    12142   9395  11965   -999   -491   3253       N  
ATOM    550  CA  LEU A  69     116.468  88.880  48.638  1.00 86.98           C  
ANISOU  550  CA  LEU A  69    12050   9384  11612  -1089   -495   3437       C  
ATOM    551  C   LEU A  69     116.643  89.058  47.131  1.00 92.44           C  
ANISOU  551  C   LEU A  69    12806  10114  12205  -1112   -637   3594       C  
ATOM    552  O   LEU A  69     117.610  88.570  46.547  1.00 92.15           O  
ANISOU  552  O   LEU A  69    12805  10257  11951  -1152   -586   3710       O  
ATOM    553  CB  LEU A  69     117.422  87.809  49.170  1.00 75.37           C  
ANISOU  553  CB  LEU A  69    10568   8116   9953  -1094   -309   3447       C  
ATOM    554  CG  LEU A  69     117.313  87.554  50.675  1.00 72.42           C  
ANISOU  554  CG  LEU A  69    10145   7724   9647  -1096   -171   3308       C  
ATOM    555  CD1 LEU A  69     118.456  86.684  51.167  1.00 68.21           C  
ANISOU  555  CD1 LEU A  69     9606   7384   8926  -1124    -25   3364       C  
ATOM    556  CD2 LEU A  69     117.278  88.873  51.432  1.00 75.30           C  
ANISOU  556  CD2 LEU A  69    10510   7955  10146  -1171   -223   3279       C  
ATOM    557  N   ASN A  70     115.705  89.768  46.513  1.00 95.26           N  
ANISOU  557  N   ASN A  70    13173  10298  12724  -1098   -818   3595       N  
ATOM    558  CA  ASN A  70     115.752  90.027  45.079  1.00 95.90           C  
ANISOU  558  CA  ASN A  70    13323  10395  12718  -1143   -981   3749       C  
ATOM    559  C   ASN A  70     115.940  91.506  44.774  1.00 97.07           C  
ANISOU  559  C   ASN A  70    13522  10416  12944  -1235  -1171   3872       C  
ATOM    560  O   ASN A  70     115.167  92.346  45.231  1.00101.09           O  
ANISOU  560  O   ASN A  70    13995  10714  13700  -1210  -1271   3798       O  
ATOM    561  CB  ASN A  70     114.477  89.523  44.403  1.00 94.94           C  
ANISOU  561  CB  ASN A  70    13183  10184  12707  -1059  -1067   3678       C  
ATOM    562  CG  ASN A  70     114.279  88.033  44.573  1.00 97.11           C  
ANISOU  562  CG  ASN A  70    13419  10585  12895   -974   -892   3567       C  
ATOM    563  ND2 ASN A  70     113.091  87.644  45.021  1.00103.10           N  
ANISOU  563  ND2 ASN A  70    14110  11226  13838   -877   -876   3400       N  
ATOM    564  OD1 ASN A  70     115.179  87.238  44.302  1.00 91.21           O  
ANISOU  564  OD1 ASN A  70    12697  10033  11925   -997   -771   3625       O  
ATOM    565  N   THR A  71     116.970  91.821  43.998  1.00 95.31           N  
ANISOU  565  N   THR A  71    13380  10318  12517  -1346  -1218   4055       N  
ATOM    566  CA  THR A  71     117.215  93.195  43.586  1.00 92.98           C  
ANISOU  566  CA  THR A  71    13148   9913  12267  -1451  -1412   4196       C  
ATOM    567  C   THR A  71     116.505  93.482  42.269  1.00 91.25           C  
ANISOU  567  C   THR A  71    12986   9604  12080  -1479  -1638   4295       C  
ATOM    568  O   THR A  71     116.456  94.625  41.813  1.00 95.31           O  
ANISOU  568  O   THR A  71    13555   9988  12671  -1561  -1844   4415       O  
ATOM    569  CB  THR A  71     118.718  93.484  43.435  1.00 96.38           C  
ANISOU  569  CB  THR A  71    13639  10524  12455  -1581  -1357   4349       C  
ATOM    570  CG2 THR A  71     119.448  93.185  44.735  1.00 99.93           C  
ANISOU  570  CG2 THR A  71    14033  11066  12871  -1562  -1148   4265       C  
ATOM    571  OG1 THR A  71     119.260  92.671  42.388  1.00 94.74           O  
ANISOU  571  OG1 THR A  71    13477  10520  11998  -1625  -1314   4439       O  
ATOM    572  N   VAL A  72     115.956  92.434  41.662  1.00 85.67           N  
ANISOU  572  N   VAL A  72    12269   8967  11314  -1419  -1606   4250       N  
ATOM    573  CA  VAL A  72     115.185  92.577  40.435  1.00 82.27           C  
ANISOU  573  CA  VAL A  72    11891   8457  10913  -1447  -1818   4334       C  
ATOM    574  C   VAL A  72     114.025  93.538  40.675  1.00 85.05           C  
ANISOU  574  C   VAL A  72    12200   8516  11601  -1394  -2021   4287       C  
ATOM    575  O   VAL A  72     113.608  93.746  41.813  1.00 81.97           O  
ANISOU  575  O   VAL A  72    11721   8002  11422  -1305  -1948   4132       O  
ATOM    576  CB  VAL A  72     114.654  91.221  39.938  1.00 81.96           C  
ANISOU  576  CB  VAL A  72    11832   8524  10787  -1373  -1728   4254       C  
ATOM    577  CG1 VAL A  72     113.703  90.617  40.958  1.00 93.29           C  
ANISOU  577  CG1 VAL A  72    13154   9861  12431  -1213  -1615   4035       C  
ATOM    578  CG2 VAL A  72     113.972  91.376  38.589  1.00 78.91           C  
ANISOU  578  CG2 VAL A  72    11513   8079  10391  -1432  -1953   4363       C  
ATOM    579  N   GLU A  73     113.507  94.123  39.602  1.00 91.97           N  
ANISOU  579  N   GLU A  73    13136   9280  12529  -1457  -2278   4417       N  
ATOM    580  CA  GLU A  73     112.532  95.196  39.729  1.00 99.46           C  
ANISOU  580  CA  GLU A  73    14045   9935  13811  -1423  -2506   4404       C  
ATOM    581  C   GLU A  73     111.093  94.736  39.515  1.00107.69           C  
ANISOU  581  C   GLU A  73    15011  10836  15071  -1305  -2593   4288       C  
ATOM    582  O   GLU A  73     110.155  95.403  39.950  1.00113.64           O  
ANISOU  582  O   GLU A  73    15682  11340  16157  -1229  -2717   4198       O  
ATOM    583  CB  GLU A  73     112.871  96.323  38.754  1.00106.69           C  
ANISOU  583  CB  GLU A  73    15073  10776  14688  -1578  -2775   4639       C  
ATOM    584  CG  GLU A  73     112.108  97.606  38.998  1.00119.00           C  
ANISOU  584  CG  GLU A  73    16592  12020  16604  -1555  -3014   4642       C  
ATOM    585  CD  GLU A  73     112.609  98.744  38.135  1.00134.05           C  
ANISOU  585  CD  GLU A  73    18620  13862  18452  -1725  -3271   4889       C  
ATOM    586  OE1 GLU A  73     113.570  98.526  37.367  1.00135.41           O  
ANISOU  586  OE1 GLU A  73    18909  14251  18291  -1869  -3248   5050       O  
ATOM    587  OE2 GLU A  73     112.044  99.854  38.225  1.00143.25           O1-
ANISOU  587  OE2 GLU A  73    19763  14757  19911  -1719  -3496   4918       O1-
ATOM    588  N   ARG A  74     110.919  93.597  38.852  1.00106.30           N  
ANISOU  588  N   ARG A  74    14856  10815  14717  -1291  -2526   4282       N  
ATOM    589  CA BARG A  74     109.583  93.093  38.555  0.38105.35           C  
ANISOU  589  CA BARG A  74    14670  10581  14775  -1192  -2611   4184       C  
ATOM    590  CA CARG A  74     109.585  93.090  38.546  0.62103.41           C  
ANISOU  590  CA CARG A  74    14425  10336  14528  -1192  -2611   4186       C  
ATOM    591  C   ARG A  74     109.529  91.566  38.517  1.00 99.11           C  
ANISOU  591  C   ARG A  74    13863   9992  13801  -1128  -2390   4075       C  
ATOM    592  O   ARG A  74     110.454  90.911  38.038  1.00104.69           O  
ANISOU  592  O   ARG A  74    14648  10932  14197  -1204  -2268   4153       O  
ATOM    593  CB BARG A  74     109.078  93.676  37.233  0.38103.53           C  
ANISOU  593  CB BARG A  74    14516  10242  14578  -1286  -2930   4370       C  
ATOM    594  CB CARG A  74     109.096  93.652  37.210  0.62102.62           C  
ANISOU  594  CB CARG A  74    14403  10134  14453  -1288  -2928   4373       C  
ATOM    595  CG BARG A  74     107.663  93.260  36.868  0.38104.53           C  
ANISOU  595  CG BARG A  74    14572  10235  14911  -1192  -3055   4287       C  
ATOM    596  CG CARG A  74     108.141  92.730  36.475  0.62103.45           C  
ANISOU  596  CG CARG A  74    14495  10259  14552  -1243  -2977   4335       C  
ATOM    597  CD BARG A  74     107.167  93.997  35.632  0.38100.57           C  
ANISOU  597  CD BARG A  74    14143   9595  14472  -1297  -3407   4489       C  
ATOM    598  CD CARG A  74     107.480  93.427  35.303  0.62100.21           C  
ANISOU  598  CD CARG A  74    14143   9695  14236  -1333  -3327   4511       C  
ATOM    599  NE BARG A  74     106.974  95.423  35.880  0.38 96.20           N  
ANISOU  599  NE BARG A  74    13566   8784  14203  -1312  -3631   4554       N  
ATOM    600  NE CARG A  74     106.773  92.482  34.445  0.62 94.83           N  
ANISOU  600  NE CARG A  74    13478   9083  13468  -1330  -3367   4508       N  
ATOM    601  CZ BARG A  74     107.860  96.364  35.569  0.38 88.71           C  
ANISOU  601  CZ BARG A  74    12722   7836  13150  -1454  -3746   4741       C  
ATOM    602  CZ CARG A  74     105.829  92.827  33.577  0.62 87.64           C  
ANISOU  602  CZ CARG A  74    12580   8018  12702  -1364  -3659   4605       C  
ATOM    603  NH1BARG A  74     109.007  96.034  34.992  0.38109.30           N1+
ANISOU  603  NH1BARG A  74    15461  10699  15370  -1599  -3653   4878       N1+
ATOM    604  NH2BARG A  74     107.598  97.637  35.833  0.38 90.25           N  
ANISOU  604  NH2BARG A  74    12885   7772  13633  -1455  -3953   4785       N  
ATOM    605  NH1CARG A  74     105.470  94.098  33.460  0.62 89.53           N1+
ANISOU  605  NH1CARG A  74    12812   8012  13195  -1396  -3942   4713       N1+
ATOM    606  NH2CARG A  74     105.238  91.902  32.833  0.62 87.69           N  
ANISOU  606  NH2CARG A  74    12604   8108  12606  -1369  -3674   4595       N  
ATOM    607  N   ILE A  75     108.434  91.011  39.028  1.00 89.52           N  
ANISOU  607  N   ILE A  75    12541   8682  12791   -991  -2339   3888       N  
ATOM    608  CA  ILE A  75     108.221  89.569  39.039  1.00 84.70           C  
ANISOU  608  CA  ILE A  75    11908   8231  12046   -921  -2146   3771       C  
ATOM    609  C   ILE A  75     106.831  89.252  38.497  1.00 92.89           C  
ANISOU  609  C   ILE A  75    12895   9140  13258   -855  -2291   3711       C  
ATOM    610  O   ILE A  75     105.829  89.497  39.168  1.00105.64           O  
ANISOU  610  O   ILE A  75    14396  10567  15175   -750  -2324   3561       O  
ATOM    611  CB  ILE A  75     108.354  88.995  40.457  1.00 80.02           C  
ANISOU  611  CB  ILE A  75    11225   7682  11499   -821  -1877   3569       C  
ATOM    612  CG1 ILE A  75     109.683  89.428  41.081  1.00 80.00           C  
ANISOU  612  CG1 ILE A  75    11259   7781  11357   -889  -1756   3630       C  
ATOM    613  CG2 ILE A  75     108.234  87.479  40.431  1.00 76.48           C  
ANISOU  613  CG2 ILE A  75    10764   7402  10894   -760  -1683   3467       C  
ATOM    614  CD1 ILE A  75     109.818  89.068  42.543  1.00 80.87           C  
ANISOU  614  CD1 ILE A  75    11287   7910  11530   -816  -1525   3449       C  
ATOM    615  N   PRO A  76     106.769  88.708  37.274  1.00 86.06           N  
ANISOU  615  N   PRO A  76    12114   8381  12205   -923  -2374   3824       N  
ATOM    616  CA  PRO A  76     105.517  88.511  36.534  1.00 86.82           C  
ANISOU  616  CA  PRO A  76    12185   8362  12441   -893  -2559   3816       C  
ATOM    617  C   PRO A  76     104.724  87.270  36.939  1.00 88.51           C  
ANISOU  617  C   PRO A  76    12315   8618  12698   -767  -2390   3614       C  
ATOM    618  O   PRO A  76     104.335  86.503  36.061  1.00 92.43           O  
ANISOU  618  O   PRO A  76    12853   9194  13072   -790  -2425   3641       O  
ATOM    619  CB  PRO A  76     105.987  88.356  35.079  1.00 90.41           C  
ANISOU  619  CB  PRO A  76    12785   8958  12608  -1052  -2681   4024       C  
ATOM    620  CG  PRO A  76     107.457  88.703  35.078  1.00 94.19           C  
ANISOU  620  CG  PRO A  76    13354   9593  12840  -1166  -2586   4144       C  
ATOM    621  CD  PRO A  76     107.941  88.381  36.449  1.00 87.50           C  
ANISOU  621  CD  PRO A  76    12425   8795  12028  -1058  -2317   3981       C  
ATOM    622  N   LEU A  77     104.478  87.078  38.232  1.00 90.75           N  
ANISOU  622  N   LEU A  77    12488   8850  13144   -650  -2213   3415       N  
ATOM    623  CA  LEU A  77     103.647  85.964  38.684  1.00 93.64           C  
ANISOU  623  CA  LEU A  77    12770   9236  13572   -537  -2064   3217       C  
ATOM    624  C   LEU A  77     102.170  86.288  38.488  1.00 99.58           C  
ANISOU  624  C   LEU A  77    13427   9769  14641   -470  -2263   3144       C  
ATOM    625  O   LEU A  77     101.343  86.039  39.363  1.00 99.24           O  
ANISOU  625  O   LEU A  77    13261   9631  14816   -363  -2173   2939       O  
ATOM    626  CB  LEU A  77     103.920  85.643  40.153  1.00 93.71           C  
ANISOU  626  CB  LEU A  77    12702   9276  13628   -461  -1806   3033       C  
ATOM    627  CG  LEU A  77     105.269  84.995  40.463  1.00 97.82           C  
ANISOU  627  CG  LEU A  77    13293  10027  13845   -503  -1577   3070       C  
ATOM    628  CD1 LEU A  77     105.386  84.710  41.950  1.00102.39           C  
ANISOU  628  CD1 LEU A  77    13794  10613  14498   -437  -1353   2890       C  
ATOM    629  CD2 LEU A  77     105.448  83.721  39.653  1.00 95.87           C  
ANISOU  629  CD2 LEU A  77    13111   9970  13343   -516  -1489   3099       C  
ATOM    630  N   GLU A  78     101.851  86.839  37.324  1.00107.01           N  
ANISOU  630  N   GLU A  78    14423  10631  15605   -544  -2537   3315       N  
ATOM    631  CA  GLU A  78     100.510  87.333  37.037  1.00112.52           C  
ANISOU  631  CA  GLU A  78    15027  11096  16628   -492  -2778   3283       C  
ATOM    632  C   GLU A  78      99.454  86.235  36.934  1.00117.91           C  
ANISOU  632  C   GLU A  78    15643  11798  17359   -409  -2721   3138       C  
ATOM    633  O   GLU A  78      98.338  86.395  37.426  1.00126.48           O  
ANISOU  633  O   GLU A  78    16588  12706  18765   -309  -2772   2983       O  
ATOM    634  CB  GLU A  78     100.534  88.169  35.758  1.00109.57           C  
ANISOU  634  CB  GLU A  78    14750  10648  16236   -616  -3103   3535       C  
ATOM    635  CG  GLU A  78     101.683  87.813  34.831  1.00106.66           C  
ANISOU  635  CG  GLU A  78    14557  10517  15454   -767  -3068   3727       C  
ATOM    636  CD  GLU A  78     101.860  88.816  33.714  1.00112.20           C  
ANISOU  636  CD  GLU A  78    15364  11143  16125   -918  -3384   3983       C  
ATOM    637  OE1 GLU A  78     100.880  89.063  32.983  1.00122.41           O  
ANISOU  637  OE1 GLU A  78    16639  12291  17579   -934  -3647   4050       O  
ATOM    638  OE2 GLU A  78     102.978  89.355  33.566  1.00108.20           O1-
ANISOU  638  OE2 GLU A  78    14957  10721  15434  -1030  -3376   4123       O1-
ATOM    639  N   ASN A  79      99.806  85.124  36.297  1.00109.35           N  
ANISOU  639  N   ASN A  79    14653  10929  15964   -455  -2611   3179       N  
ATOM    640  CA  ASN A  79      98.846  84.051  36.061  1.00101.45           C  
ANISOU  640  CA  ASN A  79    13608   9959  14978   -395  -2570   3062       C  
ATOM    641  C   ASN A  79      98.649  83.124  37.252  1.00102.12           C  
ANISOU  641  C   ASN A  79    13603  10104  15095   -280  -2278   2818       C  
ATOM    642  O   ASN A  79      97.854  82.188  37.192  1.00104.31           O  
ANISOU  642  O   ASN A  79    13838  10408  15389   -224  -2218   2701       O  
ATOM    643  CB  ASN A  79      99.242  83.245  34.827  1.00 99.08           C  
ANISOU  643  CB  ASN A  79    13449   9855  14341   -502  -2582   3200       C  
ATOM    644  CG  ASN A  79      99.069  84.028  33.549  1.00105.12           C  
ANISOU  644  CG  ASN A  79    14296  10545  15099   -629  -2905   3425       C  
ATOM    645  ND2 ASN A  79      99.414  83.412  32.425  1.00112.12           N  
ANISOU  645  ND2 ASN A  79    15313  11603  15684   -750  -2925   3549       N  
ATOM    646  OD1 ASN A  79      98.626  85.176  33.570  1.00107.09           O  
ANISOU  646  OD1 ASN A  79    14493  10583  15615   -625  -3139   3487       O  
ATOM    647  N   LEU A  80      99.378  83.384  38.331  1.00102.90           N  
ANISOU  647  N   LEU A  80    13679  10225  15193   -256  -2101   2749       N  
ATOM    648  CA  LEU A  80      99.242  82.597  39.549  1.00 98.20           C  
ANISOU  648  CA  LEU A  80    13005   9679  14626   -169  -1834   2527       C  
ATOM    649  C   LEU A  80      97.847  82.795  40.134  1.00 96.56           C  
ANISOU  649  C   LEU A  80    12640   9274  14775    -74  -1886   2333       C  
ATOM    650  O   LEU A  80      97.484  83.902  40.529  1.00 99.02           O  
ANISOU  650  O   LEU A  80    12867   9394  15365    -53  -2006   2301       O  
ATOM    651  CB  LEU A  80     100.313  83.004  40.561  1.00 74.35           C  
ANISOU  651  CB  LEU A  80     9997   6707  11545   -185  -1671   2514       C  
ATOM    652  CG  LEU A  80     100.420  82.188  41.848  1.00 76.67           C  
ANISOU  652  CG  LEU A  80    10237   7081  11812   -129  -1389   2317       C  
ATOM    653  CD1 LEU A  80     100.730  80.735  41.539  1.00 76.60           C  
ANISOU  653  CD1 LEU A  80    10296   7276  11533   -127  -1226   2312       C  
ATOM    654  CD2 LEU A  80     101.483  82.781  42.754  1.00 75.41           C  
ANISOU  654  CD2 LEU A  80    10095   6953  11605   -167  -1275   2335       C  
ATOM    655  N   GLN A  81      97.068  81.717  40.180  1.00 93.44           N  
ANISOU  655  N   GLN A  81    12201   8925  14377    -19  -1792   2196       N  
ATOM    656  CA  GLN A  81      95.673  81.783  40.607  1.00 93.55           C  
ANISOU  656  CA  GLN A  81    12060   8768  14717     65  -1841   2006       C  
ATOM    657  C   GLN A  81      95.482  81.401  42.069  1.00 92.37           C  
ANISOU  657  C   GLN A  81    11815   8623  14658    120  -1587   1761       C  
ATOM    658  O   GLN A  81      94.680  82.009  42.776  1.00 99.36           O  
ANISOU  658  O   GLN A  81    12560   9335  15856    169  -1609   1598       O  
ATOM    659  CB  GLN A  81      94.805  80.873  39.736  1.00 76.54           C  
ANISOU  659  CB  GLN A  81     9909   6650  12523     80  -1911   2000       C  
ATOM    660  CG  GLN A  81      94.558  81.385  38.331  1.00102.82           C  
ANISOU  660  CG  GLN A  81    13293   9914  15859     22  -2214   2208       C  
ATOM    661  CD  GLN A  81      93.978  80.319  37.424  1.00105.77           C  
ANISOU  661  CD  GLN A  81    13709  10382  16095      9  -2245   2225       C  
ATOM    662  NE2 GLN A  81      93.058  80.717  36.553  1.00109.04           N  
ANISOU  662  NE2 GLN A  81    14086  10663  16680     -3  -2517   2298       N  
ATOM    663  OE1 GLN A  81      94.356  79.149  37.501  1.00104.87           O  
ANISOU  663  OE1 GLN A  81    13662  10454  15730      5  -2033   2176       O  
ATOM    664  N   ILE A  82      96.212  80.387  42.517  1.00 83.49           N  
ANISOU  664  N   ILE A  82    10764   7693  13263    104  -1348   1731       N  
ATOM    665  CA  ILE A  82      96.026  79.863  43.863  1.00 79.04           C  
ANISOU  665  CA  ILE A  82    10130   7156  12746    134  -1107   1510       C  
ATOM    666  C   ILE A  82      97.327  79.374  44.489  1.00 81.10           C  
ANISOU  666  C   ILE A  82    10488   7596  12731     89   -895   1552       C  
ATOM    667  O   ILE A  82      98.182  78.805  43.813  1.00 90.59           O  
ANISOU  667  O   ILE A  82    11807   8952  13660     56   -872   1706       O  
ATOM    668  CB  ILE A  82      95.007  78.704  43.872  1.00 82.18           C  
ANISOU  668  CB  ILE A  82    10477   7587  13162    181  -1029   1356       C  
ATOM    669  CG1 ILE A  82      94.876  78.115  45.276  1.00 91.29           C  
ANISOU  669  CG1 ILE A  82    11574   8782  14330    187   -775   1137       C  
ATOM    670  CG2 ILE A  82      95.419  77.622  42.884  1.00 77.11           C  
ANISOU  670  CG2 ILE A  82     9961   7118  12222    161  -1014   1488       C  
ATOM    671  CD1 ILE A  82      94.053  76.848  45.329  1.00 93.89           C  
ANISOU  671  CD1 ILE A  82    11877   9174  14622    217   -672    999       C  
ATOM    672  N   ILE A  83      97.471  79.612  45.788  1.00 76.45           N  
ANISOU  672  N   ILE A  83     9844   6983  12222     79   -742   1412       N  
ATOM    673  CA  ILE A  83      98.571  79.049  46.557  1.00 78.46           C  
ANISOU  673  CA  ILE A  83    10171   7398  12241     35   -533   1426       C  
ATOM    674  C   ILE A  83      97.985  78.156  47.641  1.00 82.57           C  
ANISOU  674  C   ILE A  83    10633   7949  12790     44   -334   1206       C  
ATOM    675  O   ILE A  83      97.354  78.640  48.580  1.00 87.80           O  
ANISOU  675  O   ILE A  83    11194   8501  13664     38   -284   1025       O  
ATOM    676  CB  ILE A  83      99.432  80.144  47.205  1.00 78.88           C  
ANISOU  676  CB  ILE A  83    10233   7415  12324    -17   -525   1476       C  
ATOM    677  CG1 ILE A  83      99.943  81.116  46.141  1.00 80.14           C  
ANISOU  677  CG1 ILE A  83    10449   7527  12472    -38   -738   1692       C  
ATOM    678  CG2 ILE A  83     100.590  79.523  47.974  1.00 72.80           C  
ANISOU  678  CG2 ILE A  83     9537   6815  11308    -68   -324   1505       C  
ATOM    679  CD1 ILE A  83     100.735  82.272  46.703  1.00 80.26           C  
ANISOU  679  CD1 ILE A  83    10472   7491  12532    -90   -751   1747       C  
ATOM    680  N   ARG A  84      98.185  76.851  47.503  1.00 81.21           N  
ANISOU  680  N   ARG A  84    10525   7925  12406     49   -219   1215       N  
ATOM    681  CA  ARG A  84      97.556  75.885  48.398  1.00 77.43           C  
ANISOU  681  CA  ARG A  84    10003   7480  11938     50    -48   1020       C  
ATOM    682  C   ARG A  84      98.174  75.881  49.792  1.00 78.92           C  
ANISOU  682  C   ARG A  84    10196   7717  12073    -18    132    943       C  
ATOM    683  O   ARG A  84      97.487  75.629  50.781  1.00 74.36           O  
ANISOU  683  O   ARG A  84     9551   7108  11593    -45    249    744       O  
ATOM    684  CB  ARG A  84      97.590  74.482  47.787  1.00 70.13           C  
ANISOU  684  CB  ARG A  84     9150   6687  10809     74      8   1062       C  
ATOM    685  CG  ARG A  84      96.884  74.401  46.447  1.00 68.44           C  
ANISOU  685  CG  ARG A  84     8934   6432  10639    124   -162   1122       C  
ATOM    686  CD  ARG A  84      96.316  73.022  46.194  1.00 71.43           C  
ANISOU  686  CD  ARG A  84     9331   6887  10921    149    -84   1048       C  
ATOM    687  NE  ARG A  84      95.175  73.079  45.287  1.00 78.38           N  
ANISOU  687  NE  ARG A  84    10159   7679  11941    190   -240   1021       N  
ATOM    688  CZ  ARG A  84      95.254  72.888  43.975  1.00 80.78           C  
ANISOU  688  CZ  ARG A  84    10530   8022  12139    197   -368   1166       C  
ATOM    689  NH1 ARG A  84      96.425  72.620  43.412  1.00 81.46           N1+
ANISOU  689  NH1 ARG A  84    10734   8238  11982    167   -344   1333       N1+
ATOM    690  NH2 ARG A  84      94.161  72.961  43.226  1.00 74.55           N  
ANISOU  690  NH2 ARG A  84     9688   7146  11490    224   -520   1138       N  
ATOM    691  N   GLY A  85      99.468  76.168  49.866  1.00 87.28           N  
ANISOU  691  N   GLY A  85    11335   8858  12970    -59    152   1099       N  
ATOM    692  CA  GLY A  85     100.163  76.209  51.138  1.00 89.00           C  
ANISOU  692  CA  GLY A  85    11567   9129  13120   -136    304   1055       C  
ATOM    693  C   GLY A  85     100.303  74.843  51.781  1.00 88.47           C  
ANISOU  693  C   GLY A  85    11541   9186  12889   -164    474    997       C  
ATOM    694  O   GLY A  85     100.253  74.722  53.005  1.00 88.58           O  
ANISOU  694  O   GLY A  85    11535   9209  12913   -238    605    873       O  
ATOM    695  N   ASN A  86     100.477  73.811  50.959  1.00 83.47           N  
ANISOU  695  N   ASN A  86    10966   8645  12102   -115    470   1085       N  
ATOM    696  CA  ASN A  86     100.678  72.459  51.471  1.00 85.71           C  
ANISOU  696  CA  ASN A  86    11295   9040  12231   -135    615   1051       C  
ATOM    697  C   ASN A  86     101.821  72.418  52.473  1.00 88.95           C  
ANISOU  697  C   ASN A  86    11752   9532  12512   -215    722   1111       C  
ATOM    698  O   ASN A  86     101.896  71.522  53.314  1.00 95.22           O  
ANISOU  698  O   ASN A  86    12568  10387  13223   -264    845   1051       O  
ATOM    699  CB  ASN A  86     100.935  71.475  50.329  1.00 93.65           C  
ANISOU  699  CB  ASN A  86    12365  10133  13086    -71    587   1163       C  
ATOM    700  CG  ASN A  86      99.665  71.090  49.598  1.00100.42           C  
ANISOU  700  CG  ASN A  86    13182  10930  14042    -12    523   1068       C  
ATOM    701  ND2 ASN A  86      99.778  70.142  48.675  1.00105.04           N  
ANISOU  701  ND2 ASN A  86    13823  11591  14495     32    515   1138       N  
ATOM    702  OD1 ASN A  86      98.593  71.635  49.864  1.00 96.13           O  
ANISOU  702  OD1 ASN A  86    12554  10273  13698     -9    482    927       O  
ATOM    703  N   MET A  87     102.714  73.396  52.365  1.00 84.71           N  
ANISOU  703  N   MET A  87    11233   8996  11959   -236    663   1238       N  
ATOM    704  CA  MET A  87     103.766  73.604  53.349  1.00 80.68           C  
ANISOU  704  CA  MET A  87    10754   8547  11354   -322    745   1294       C  
ATOM    705  C   MET A  87     103.866  75.092  53.649  1.00 76.68           C  
ANISOU  705  C   MET A  87    10210   7948  10975   -364    682   1289       C  
ATOM    706  O   MET A  87     103.326  75.914  52.912  1.00 77.87           O  
ANISOU  706  O   MET A  87    10321   7997  11267   -314    558   1287       O  
ATOM    707  CB  MET A  87     105.105  73.071  52.843  1.00 81.26           C  
ANISOU  707  CB  MET A  87    10900   8749  11225   -305    751   1493       C  
ATOM    708  CG  MET A  87     105.150  71.562  52.677  1.00 83.12           C  
ANISOU  708  CG  MET A  87    11172   9072  11339   -270    826   1496       C  
ATOM    709  SD  MET A  87     106.840  70.947  52.569  1.00186.77           S  
ANISOU  709  SD  MET A  87    24360  22342  24262   -276    872   1694       S  
ATOM    710  CE  MET A  87     107.479  71.453  54.165  1.00 95.96           C  
ANISOU  710  CE  MET A  87    12859  10851  12752   -403    942   1689       C  
ATOM    711  N   TYR A  88     104.546  75.441  54.734  1.00 77.94           N  
ANISOU  711  N   TYR A  88    10384   8139  11091   -462    761   1290       N  
ATOM    712  CA  TYR A  88     104.667  76.841  55.116  1.00 83.00           C  
ANISOU  712  CA  TYR A  88    10993   8691  11853   -514    716   1274       C  
ATOM    713  C   TYR A  88     106.118  77.297  55.180  1.00 91.61           C  
ANISOU  713  C   TYR A  88    12143   9863  12802   -561    703   1462       C  
ATOM    714  O   TYR A  88     107.035  76.487  55.316  1.00 93.76           O  
ANISOU  714  O   TYR A  88    12470  10263  12891   -580    763   1573       O  
ATOM    715  CB  TYR A  88     103.993  77.103  56.466  1.00 83.09           C  
ANISOU  715  CB  TYR A  88    10953   8642  11978   -613    824   1060       C  
ATOM    716  CG  TYR A  88     102.503  76.849  56.491  1.00 86.10           C  
ANISOU  716  CG  TYR A  88    11255   8928  12533   -578    841    846       C  
ATOM    717  CD1 TYR A  88     101.868  76.459  57.662  1.00 86.84           C  
ANISOU  717  CD1 TYR A  88    11317   9021  12657   -675    980    645       C  
ATOM    718  CD2 TYR A  88     101.732  76.991  55.345  1.00 93.96           C  
ANISOU  718  CD2 TYR A  88    12205   9839  13655   -462    715    846       C  
ATOM    719  CE1 TYR A  88     100.507  76.225  57.696  1.00 91.80           C  
ANISOU  719  CE1 TYR A  88    11863   9568  13448   -649   1003    440       C  
ATOM    720  CE2 TYR A  88     100.369  76.756  55.368  1.00 97.60           C  
ANISOU  720  CE2 TYR A  88    12583  10214  14286   -429    725    650       C  
ATOM    721  CZ  TYR A  88      99.763  76.374  56.547  1.00 98.18           C  
ANISOU  721  CZ  TYR A  88    12619  10291  14396   -520    875    443       C  
ATOM    722  OH  TYR A  88      98.408  76.140  56.577  1.00103.54           O  
ANISOU  722  OH  TYR A  88    13205  10888  15246   -493    893    238       O  
ATOM    723  N   TYR A  89     106.314  78.605  55.074  1.00 97.41           N  
ANISOU  723  N   TYR A  89    12860  10516  13635   -581    619   1498       N  
ATOM    724  CA  TYR A  89     107.619  79.201  55.296  1.00101.97           C  
ANISOU  724  CA  TYR A  89    13487  11159  14100   -646    613   1653       C  
ATOM    725  C   TYR A  89     107.641  79.786  56.702  1.00108.95           C  
ANISOU  725  C   TYR A  89    14351  12007  15037   -770    704   1535       C  
ATOM    726  O   TYR A  89     106.861  80.684  57.020  1.00113.17           O  
ANISOU  726  O   TYR A  89    14827  12406  15766   -789    684   1391       O  
ATOM    727  CB  TYR A  89     107.900  80.288  54.257  1.00100.28           C  
ANISOU  727  CB  TYR A  89    13279  10882  13942   -605    456   1782       C  
ATOM    728  CG  TYR A  89     109.199  81.028  54.483  1.00 94.65           C  
ANISOU  728  CG  TYR A  89    12610  10226  13126   -680    445   1934       C  
ATOM    729  CD1 TYR A  89     110.406  80.499  54.049  1.00 94.01           C  
ANISOU  729  CD1 TYR A  89    12586  10295  12838   -680    457   2118       C  
ATOM    730  CD2 TYR A  89     109.217  82.254  55.131  1.00 93.49           C  
ANISOU  730  CD2 TYR A  89    12441   9981  13098   -753    425   1885       C  
ATOM    731  CE1 TYR A  89     111.595  81.171  54.256  1.00 95.89           C  
ANISOU  731  CE1 TYR A  89    12858  10590  12985   -752    447   2255       C  
ATOM    732  CE2 TYR A  89     110.400  82.933  55.342  1.00 95.43           C  
ANISOU  732  CE2 TYR A  89    12731  10282  13247   -827    413   2024       C  
ATOM    733  CZ  TYR A  89     111.586  82.388  54.903  1.00 97.92           C  
ANISOU  733  CZ  TYR A  89    13102  10753  13351   -827    422   2212       C  
ATOM    734  OH  TYR A  89     112.768  83.063  55.114  1.00101.39           O  
ANISOU  734  OH  TYR A  89    13577  11251  13697   -905    410   2349       O  
ATOM    735  N   GLU A  90     108.525  79.259  57.543  1.00109.55           N  
ANISOU  735  N   GLU A  90    14473  12202  14948   -859    803   1591       N  
ATOM    736  CA  GLU A  90     108.623  79.688  58.935  1.00115.59           C  
ANISOU  736  CA  GLU A  90    15236  12959  15725  -1005    900   1487       C  
ATOM    737  C   GLU A  90     107.385  79.312  59.749  1.00115.64           C  
ANISOU  737  C   GLU A  90    15195  12905  15838  -1053    999   1241       C  
ATOM    738  O   GLU A  90     107.003  80.024  60.678  1.00116.75           O  
ANISOU  738  O   GLU A  90    15304  12977  16078  -1158   1060   1086       O  
ATOM    739  CB  GLU A  90     108.886  81.194  59.032  1.00122.01           C  
ANISOU  739  CB  GLU A  90    16033  13680  16643  -1050    838   1498       C  
ATOM    740  CG  GLU A  90     110.221  81.640  58.452  1.00132.33           C  
ANISOU  740  CG  GLU A  90    17393  15061  17824  -1044    758   1736       C  
ATOM    741  CD  GLU A  90     111.406  80.912  59.062  1.00140.76           C  
ANISOU  741  CD  GLU A  90    18516  16289  18675  -1122    834   1864       C  
ATOM    742  OE1 GLU A  90     111.579  79.707  58.781  1.00147.18           O  
ANISOU  742  OE1 GLU A  90    19348  17196  19378  -1070    862   1922       O  
ATOM    743  OE2 GLU A  90     112.175  81.550  59.812  1.00138.07           O1-
ANISOU  743  OE2 GLU A  90    18200  15977  18284  -1238    858   1910       O1-
ATOM    744  N   ASN A  91     106.762  78.194  59.392  1.00114.59           N  
ANISOU  744  N   ASN A  91    15057  12800  15683   -982   1021   1197       N  
ATOM    745  CA  ASN A  91     105.647  77.654  60.162  1.00114.60           C  
ANISOU  745  CA  ASN A  91    15021  12768  15755  -1038   1125    972       C  
ATOM    746  C   ASN A  91     104.467  78.608  60.255  1.00113.74           C  
ANISOU  746  C   ASN A  91    14816  12501  15898  -1031   1115    758       C  
ATOM    747  O   ASN A  91     103.785  78.656  61.277  1.00119.03           O  
ANISOU  747  O   ASN A  91    15449  13138  16638  -1140   1227    550       O  
ATOM    748  CB  ASN A  91     106.107  77.298  61.576  1.00118.28           C  
ANISOU  748  CB  ASN A  91    15533  13319  16088  -1217   1252    934       C  
ATOM    749  CG  ASN A  91     107.461  76.626  61.594  1.00127.55           C  
ANISOU  749  CG  ASN A  91    16790  14633  17043  -1236   1243   1163       C  
ATOM    750  ND2 ASN A  91     108.301  77.016  62.545  1.00126.34           N  
ANISOU  750  ND2 ASN A  91    16675  14532  16796  -1381   1285   1215       N  
ATOM    751  OD1 ASN A  91     107.751  75.765  60.763  1.00134.90           O  
ANISOU  751  OD1 ASN A  91    17743  15620  17894  -1126   1199   1288       O  
ATOM    752  N   SER A  92     104.222  79.368  59.193  1.00110.44           N  
ANISOU  752  N   SER A  92    14357  11982  15623   -911    979    807       N  
ATOM    753  CA  SER A  92     103.153  80.357  59.224  1.00112.04           C  
ANISOU  753  CA  SER A  92    14457  12013  16100   -892    945    617       C  
ATOM    754  C   SER A  92     102.639  80.730  57.840  1.00106.15           C  
ANISOU  754  C   SER A  92    13667  11163  15502   -736    772    681       C  
ATOM    755  O   SER A  92     101.470  80.513  57.525  1.00108.03           O  
ANISOU  755  O   SER A  92    13828  11318  15902   -669    750    539       O  
ATOM    756  CB  SER A  92     103.620  81.621  59.953  1.00119.67           C  
ANISOU  756  CB  SER A  92    15414  12918  17137   -995    961    586       C  
ATOM    757  OG  SER A  92     104.012  81.336  61.285  1.00122.95           O  
ANISOU  757  OG  SER A  92    15869  13425  17422  -1162   1118    512       O  
ATOM    758  N   TYR A  93     103.521  81.285  57.017  1.00 99.33           N  
ANISOU  758  N   TYR A  93    12855  10310  14577   -691    646    898       N  
ATOM    759  CA  TYR A  93     103.104  81.935  55.779  1.00 96.63           C  
ANISOU  759  CA  TYR A  93    12478   9851  14387   -578    460    969       C  
ATOM    760  C   TYR A  93     103.112  81.031  54.549  1.00 88.23           C  
ANISOU  760  C   TYR A  93    11458   8863  13203   -477    379   1111       C  
ATOM    761  O   TYR A  93     104.050  80.265  54.329  1.00 90.24           O  
ANISOU  761  O   TYR A  93    11798   9271  13219   -484    419   1264       O  
ATOM    762  CB  TYR A  93     103.979  83.161  55.523  1.00 98.19           C  
ANISOU  762  CB  TYR A  93    12707  10004  14597   -603    355   1119       C  
ATOM    763  CG  TYR A  93     104.328  83.920  56.780  1.00103.52           C  
ANISOU  763  CG  TYR A  93    13370  10650  15313   -726    456   1020       C  
ATOM    764  CD1 TYR A  93     105.611  83.872  57.308  1.00102.95           C  
ANISOU  764  CD1 TYR A  93    13383  10712  15021   -819    526   1152       C  
ATOM    765  CD2 TYR A  93     103.374  84.676  57.446  1.00109.13           C  
ANISOU  765  CD2 TYR A  93    13979  11200  16286   -754    486    787       C  
ATOM    766  CE1 TYR A  93     105.937  84.564  58.458  1.00102.11           C  
ANISOU  766  CE1 TYR A  93    13273  10586  14939   -946    617   1064       C  
ATOM    767  CE2 TYR A  93     103.690  85.370  58.598  1.00112.02           C  
ANISOU  767  CE2 TYR A  93    14336  11543  16681   -881    590    683       C  
ATOM    768  CZ  TYR A  93     104.974  85.310  59.099  1.00106.61           C  
ANISOU  768  CZ  TYR A  93    13750  10999  15759   -981    653    827       C  
ATOM    769  OH  TYR A  93     105.295  85.999  60.246  1.00105.64           O  
ANISOU  769  OH  TYR A  93    13626  10858  15653  -1121    755    726       O  
ATOM    770  N   ALA A  94     102.054  81.137  53.751  1.00 75.70           N  
ANISOU  770  N   ALA A  94     9807   7162  11792   -387    265   1053       N  
ATOM    771  CA  ALA A  94     101.993  80.481  52.452  1.00 76.55           C  
ANISOU  771  CA  ALA A  94     9956   7322  11808   -301    161   1189       C  
ATOM    772  C   ALA A  94     102.683  81.358  51.416  1.00 79.36           C  
ANISOU  772  C   ALA A  94    10362   7652  12139   -284    -15   1404       C  
ATOM    773  O   ALA A  94     103.168  80.876  50.393  1.00 79.22           O  
ANISOU  773  O   ALA A  94    10416   7729  11955   -253    -79   1572       O  
ATOM    774  CB  ALA A  94     100.553  80.229  52.055  1.00 78.44           C  
ANISOU  774  CB  ALA A  94    10107   7453  12244   -227    103   1041       C  
ATOM    775  N   LEU A  95     102.715  82.657  51.692  1.00 80.05           N  
ANISOU  775  N   LEU A  95    10412   7610  12395   -315    -90   1391       N  
ATOM    776  CA  LEU A  95     103.416  83.614  50.849  1.00 79.27           C  
ANISOU  776  CA  LEU A  95    10365   7478  12277   -322   -257   1594       C  
ATOM    777  C   LEU A  95     104.273  84.531  51.713  1.00 85.56           C  
ANISOU  777  C   LEU A  95    11179   8263  13067   -408   -207   1613       C  
ATOM    778  O   LEU A  95     103.769  85.195  52.617  1.00 91.78           O  
ANISOU  778  O   LEU A  95    11890   8928  14054   -438   -164   1442       O  
ATOM    779  CB  LEU A  95     102.422  84.440  50.034  1.00 69.92           C  
ANISOU  779  CB  LEU A  95     9114   6098  11355   -261   -468   1581       C  
ATOM    780  CG  LEU A  95     103.013  85.572  49.191  1.00 70.85           C  
ANISOU  780  CG  LEU A  95     9283   6148  11489   -283   -668   1785       C  
ATOM    781  CD1 LEU A  95     104.068  85.038  48.238  1.00 70.06           C  
ANISOU  781  CD1 LEU A  95     9308   6231  11082   -308   -694   2018       C  
ATOM    782  CD2 LEU A  95     101.922  86.302  48.426  1.00 72.51           C  
ANISOU  782  CD2 LEU A  95     9419   6150  11981   -225   -893   1768       C  
ATOM    783  N   ALA A  96     105.572  84.559  51.436  1.00 82.93           N  
ANISOU  783  N   ALA A  96    10941   8061  12506   -455   -207   1812       N  
ATOM    784  CA  ALA A  96     106.490  85.403  52.189  1.00 79.15           C  
ANISOU  784  CA  ALA A  96    10488   7589  11996   -545   -166   1854       C  
ATOM    785  C   ALA A  96     107.382  86.223  51.262  1.00 88.51           C  
ANISOU  785  C   ALA A  96    11745   8783  13102   -568   -320   2085       C  
ATOM    786  O   ALA A  96     108.303  85.694  50.641  1.00 95.73           O  
ANISOU  786  O   ALA A  96    12737   9856  13780   -580   -314   2256       O  
ATOM    787  CB  ALA A  96     107.331  84.561  53.130  1.00 70.61           C  
ANISOU  787  CB  ALA A  96     9448   6683  10697   -610     29   1850       C  
ATOM    788  N   VAL A  97     107.096  87.518  51.172  1.00 89.57           N  
ANISOU  788  N   VAL A  97    11848   8742  13444   -581   -458   2082       N  
ATOM    789  CA  VAL A  97     107.899  88.438  50.377  1.00 89.31           C  
ANISOU  789  CA  VAL A  97    11885   8696  13354   -622   -615   2295       C  
ATOM    790  C   VAL A  97     108.778  89.271  51.305  1.00 88.32           C  
ANISOU  790  C   VAL A  97    11779   8572  13207   -718   -550   2308       C  
ATOM    791  O   VAL A  97     108.283  90.138  52.023  1.00 87.28           O  
ANISOU  791  O   VAL A  97    11584   8278  13301   -736   -556   2170       O  
ATOM    792  CB  VAL A  97     107.009  89.366  49.535  1.00 90.67           C  
ANISOU  792  CB  VAL A  97    12019   8655  13777   -578   -849   2313       C  
ATOM    793  CG1 VAL A  97     107.858  90.239  48.630  1.00 94.59           C  
ANISOU  793  CG1 VAL A  97    12603   9151  14184   -638  -1022   2554       C  
ATOM    794  CG2 VAL A  97     106.023  88.548  48.718  1.00 91.73           C  
ANISOU  794  CG2 VAL A  97    12123   8778  13952   -490   -913   2280       C  
ATOM    795  N   LEU A  98     110.082  89.008  51.285  1.00 89.15           N  
ANISOU  795  N   LEU A  98    11966   8860  13048   -781   -484   2466       N  
ATOM    796  CA  LEU A  98     110.981  89.560  52.295  1.00 89.55           C  
ANISOU  796  CA  LEU A  98    12036   8949  13039   -880   -390   2471       C  
ATOM    797  C   LEU A  98     112.201  90.287  51.728  1.00 97.78           C  
ANISOU  797  C   LEU A  98    13160  10056  13934   -953   -482   2699       C  
ATOM    798  O   LEU A  98     112.793  89.853  50.741  1.00 97.43           O  
ANISOU  798  O   LEU A  98    13176  10139  13706   -946   -530   2867       O  
ATOM    799  CB  LEU A  98     111.442  88.444  53.235  1.00 77.51           C  
ANISOU  799  CB  LEU A  98    10515   7597  11339   -909   -178   2409       C  
ATOM    800  CG  LEU A  98     110.363  87.430  53.617  1.00 72.25           C  
ANISOU  800  CG  LEU A  98     9787   6917  10746   -844    -80   2219       C  
ATOM    801  CD1 LEU A  98     110.952  86.283  54.419  1.00 69.48           C  
ANISOU  801  CD1 LEU A  98     9458   6746  10196   -883    103   2202       C  
ATOM    802  CD2 LEU A  98     109.242  88.107  54.384  1.00 75.37           C  
ANISOU  802  CD2 LEU A  98    10097   7120  11422   -847    -70   1991       C  
ATOM    803  N   SER A  99     112.564  91.392  52.376  1.00102.74           N  
ANISOU  803  N   SER A  99    13791  10600  14646  -1031   -497   2691       N  
ATOM    804  CA  SER A  99     113.776  92.153  52.062  1.00102.95           C  
ANISOU  804  CA  SER A  99    13894  10689  14534  -1120   -564   2890       C  
ATOM    805  C   SER A  99     114.192  92.103  50.594  1.00100.22           C  
ANISOU  805  C   SER A  99    13615  10412  14053  -1110   -708   3102       C  
ATOM    806  O   SER A  99     115.252  91.575  50.260  1.00 97.40           O  
ANISOU  806  O   SER A  99    13311  10251  13446  -1148   -651   3243       O  
ATOM    807  CB  SER A  99     114.938  91.689  52.943  1.00106.20           C  
ANISOU  807  CB  SER A  99    14333  11290  14727  -1201   -390   2926       C  
ATOM    808  OG  SER A  99     114.639  91.866  54.316  1.00109.68           O  
ANISOU  808  OG  SER A  99    14728  11672  15274  -1247   -266   2744       O  
ATOM    809  N   ASN A 100     113.358  92.662  49.725  1.00 99.38           N  
ANISOU  809  N   ASN A 100    13502  10142  14115  -1067   -897   3121       N  
ATOM    810  CA  ASN A 100     113.662  92.717  48.301  1.00101.64           C  
ANISOU  810  CA  ASN A 100    13861  10480  14278  -1082  -1054   3322       C  
ATOM    811  C   ASN A 100     114.167  94.090  47.879  1.00112.92           C  
ANISOU  811  C   ASN A 100    15350  11813  15743  -1174  -1230   3476       C  
ATOM    812  O   ASN A 100     113.568  94.744  47.024  1.00120.67           O  
ANISOU  812  O   ASN A 100    16346  12643  16859  -1168  -1442   3543       O  
ATOM    813  CB  ASN A 100     112.429  92.342  47.476  1.00100.89           C  
ANISOU  813  CB  ASN A 100    13734  10281  14317   -990  -1173   3274       C  
ATOM    814  CG  ASN A 100     112.153  90.853  47.480  1.00 98.76           C  
ANISOU  814  CG  ASN A 100    13439  10155  13930   -916  -1022   3188       C  
ATOM    815  ND2 ASN A 100     110.895  90.488  47.690  1.00102.20           N  
ANISOU  815  ND2 ASN A 100    13796  10472  14562   -825  -1021   3017       N  
ATOM    816  OD1 ASN A 100     113.056  90.040  47.288  1.00 91.64           O  
ANISOU  816  OD1 ASN A 100    12583   9463  12773   -941   -909   3271       O  
ATOM    817  N   TYR A 101     115.269  94.528  48.478  1.00115.93           N  
ANISOU  817  N   TYR A 101    15766  12280  16005  -1265  -1152   3539       N  
ATOM    818  CA  TYR A 101     115.831  95.833  48.149  1.00120.34           C  
ANISOU  818  CA  TYR A 101    16386  12755  16583  -1365  -1307   3686       C  
ATOM    819  C   TYR A 101     117.291  95.764  47.715  1.00122.55           C  
ANISOU  819  C   TYR A 101    16751  13255  16557  -1471  -1271   3885       C  
ATOM    820  O   TYR A 101     118.032  94.863  48.110  1.00116.19           O  
ANISOU  820  O   TYR A 101    15938  12653  15555  -1476  -1088   3878       O  
ATOM    821  CB  TYR A 101     115.672  96.811  49.318  1.00123.74           C  
ANISOU  821  CB  TYR A 101    16772  13020  17223  -1392  -1283   3561       C  
ATOM    822  CG  TYR A 101     116.195  96.302  50.644  1.00126.50           C  
ANISOU  822  CG  TYR A 101    17088  13493  17482  -1416  -1043   3443       C  
ATOM    823  CD1 TYR A 101     117.524  95.929  50.795  1.00126.59           C  
ANISOU  823  CD1 TYR A 101    17151  13731  17215  -1495   -932   3566       C  
ATOM    824  CD2 TYR A 101     115.362  96.215  51.751  1.00131.35           C  
ANISOU  824  CD2 TYR A 101    17618  13997  18293  -1372   -934   3207       C  
ATOM    825  CE1 TYR A 101     118.004  95.469  52.005  1.00128.56           C  
ANISOU  825  CE1 TYR A 101    17373  14089  17386  -1527   -735   3474       C  
ATOM    826  CE2 TYR A 101     115.834  95.759  52.966  1.00134.82           C  
ANISOU  826  CE2 TYR A 101    18038  14551  18635  -1418   -727   3109       C  
ATOM    827  CZ  TYR A 101     117.156  95.387  53.087  1.00134.83           C  
ANISOU  827  CZ  TYR A 101    18096  14773  18362  -1495   -637   3251       C  
ATOM    828  OH  TYR A 101     117.629  94.932  54.296  1.00140.40           O  
ANISOU  828  OH  TYR A 101    18784  15588  18973  -1550   -451   3168       O  
ATOM    829  N   ASP A 102     117.692  96.728  46.894  1.00133.38           N  
ANISOU  829  N   ASP A 102    18199  14579  17899  -1562  -1453   4061       N  
ATOM    830  CA  ASP A 102     119.074  96.852  46.458  1.00142.43           C  
ANISOU  830  CA  ASP A 102    19425  15919  18774  -1684  -1433   4249       C  
ATOM    831  C   ASP A 102     119.881  97.492  47.579  1.00151.33           C  
ANISOU  831  C   ASP A 102    20546  17057  19896  -1755  -1339   4232       C  
ATOM    832  O   ASP A 102     119.322  97.895  48.598  1.00156.11           O  
ANISOU  832  O   ASP A 102    21096  17510  20710  -1720  -1303   4079       O  
ATOM    833  CB  ASP A 102     119.146  97.718  45.200  1.00141.81           C  
ANISOU  833  CB  ASP A 102    19438  15774  18670  -1775  -1674   4441       C  
ATOM    834  CG  ASP A 102     120.450  97.554  44.448  1.00142.34           C  
ANISOU  834  CG  ASP A 102    19587  16078  18420  -1900  -1645   4628       C  
ATOM    835  OD1 ASP A 102     120.663  98.294  43.465  1.00142.88           O  
ANISOU  835  OD1 ASP A 102    19743  16116  18430  -2008  -1831   4798       O  
ATOM    836  OD2 ASP A 102     121.258  96.684  44.834  1.00142.90           O1-
ANISOU  836  OD2 ASP A 102    19629  16362  18305  -1895  -1441   4605       O1-
ATOM    837  N   ALA A 103     121.194  97.584  47.396  1.00150.56           N  
ANISOU  837  N   ALA A 103    20504  17143  19561  -1865  -1294   4381       N  
ATOM    838  CA  ALA A 103     122.037  98.281  48.358  1.00141.97           C  
ANISOU  838  CA  ALA A 103    19420  16069  18451  -1953  -1227   4393       C  
ATOM    839  C   ALA A 103     121.638  99.751  48.397  1.00140.82           C  
ANISOU  839  C   ALA A 103    19308  15680  18516  -2006  -1411   4414       C  
ATOM    840  O   ALA A 103     121.845 100.437  49.398  1.00140.61           O  
ANISOU  840  O   ALA A 103    19268  15576  18581  -2050  -1367   4350       O  
ATOM    841  CB  ALA A 103     123.503  98.132  47.992  1.00135.68           C  
ANISOU  841  CB  ALA A 103    18672  15514  17367  -2064  -1166   4563       C  
ATOM    842  N   ASN A 104     121.054 100.221  47.299  1.00141.16           N  
ANISOU  842  N   ASN A 104    19397  15597  18638  -2007  -1623   4503       N  
ATOM    843  CA  ASN A 104     120.597 101.601  47.191  1.00150.11           C  
ANISOU  843  CA  ASN A 104    20562  16476  19999  -2049  -1833   4537       C  
ATOM    844  C   ASN A 104     119.123 101.752  47.559  1.00150.55           C  
ANISOU  844  C   ASN A 104    20533  16271  20396  -1923  -1897   4348       C  
ATOM    845  O   ASN A 104     118.489 102.752  47.222  1.00152.00           O  
ANISOU  845  O   ASN A 104    20728  16214  20811  -1927  -2107   4373       O  
ATOM    846  CB  ASN A 104     120.841 102.132  45.777  1.00162.38           C  
ANISOU  846  CB  ASN A 104    22220  18026  21451  -2146  -2058   4764       C  
ATOM    847  CG  ASN A 104     122.309 102.118  45.394  1.00170.01           C  
ANISOU  847  CG  ASN A 104    23265  19238  22091  -2290  -1999   4943       C  
ATOM    848  ND2 ASN A 104     122.603 101.616  44.200  1.00172.59           N  
ANISOU  848  ND2 ASN A 104    23652  19718  22207  -2341  -2048   5080       N  
ATOM    849  OD1 ASN A 104     123.167 102.559  46.158  1.00171.90           O  
ANISOU  849  OD1 ASN A 104    23510  19533  22270  -2364  -1909   4954       O  
ATOM    850  N   LYS A 105     118.584 100.749  48.247  1.00150.56           N  
ANISOU  850  N   LYS A 105    20448  16322  20438  -1813  -1718   4160       N  
ATOM    851  CA  LYS A 105     117.197 100.773  48.708  1.00148.58           C  
ANISOU  851  CA  LYS A 105    20101  15850  20505  -1694  -1738   3951       C  
ATOM    852  C   LYS A 105     116.194 100.803  47.554  1.00144.72           C  
ANISOU  852  C   LYS A 105    19611  15220  20158  -1627  -1956   4000       C  
ATOM    853  O   LYS A 105     115.136 101.425  47.660  1.00143.63           O  
ANISOU  853  O   LYS A 105    19411  14823  20340  -1565  -2083   3895       O  
ATOM    854  CB  LYS A 105     116.959 101.962  49.645  1.00148.86           C  
ANISOU  854  CB  LYS A 105    20100  15662  20799  -1723  -1766   3837       C  
ATOM    855  CG  LYS A 105     117.948 102.061  50.800  1.00148.60           C  
ANISOU  855  CG  LYS A 105    20077  15755  20630  -1812  -1570   3796       C  
ATOM    856  CD  LYS A 105     117.782 100.916  51.789  1.00149.08           C  
ANISOU  856  CD  LYS A 105    20065  15949  20629  -1756  -1320   3611       C  
ATOM    857  CE  LYS A 105     116.466 101.018  52.547  1.00152.98           C  
ANISOU  857  CE  LYS A 105    20453  16231  21442  -1669  -1282   3347       C  
ATOM    858  NZ  LYS A 105     116.298  99.908  53.528  1.00153.06           N1+
ANISOU  858  NZ  LYS A 105    20404  16375  21379  -1636  -1042   3170       N1+
ATOM    859  N   THR A 106     116.529 100.127  46.458  1.00140.23           N  
ANISOU  859  N   THR A 106    19106  14819  19354  -1648  -1998   4156       N  
ATOM    860  CA  THR A 106     115.648 100.060  45.294  1.00136.01           C  
ANISOU  860  CA  THR A 106    18586  14183  18909  -1607  -2205   4223       C  
ATOM    861  C   THR A 106     115.741  98.708  44.595  1.00135.64           C  
ANISOU  861  C   THR A 106    18557  14362  18617  -1576  -2111   4256       C  
ATOM    862  O   THR A 106     116.660  98.468  43.812  1.00133.94           O  
ANISOU  862  O   THR A 106    18432  14340  18120  -1672  -2113   4429       O  
ATOM    863  CB  THR A 106     115.979 101.157  44.268  1.00134.36           C  
ANISOU  863  CB  THR A 106    18482  13883  18684  -1729  -2473   4456       C  
ATOM    864  CG2 THR A 106     115.722 102.536  44.853  1.00138.80           C  
ANISOU  864  CG2 THR A 106    19022  14177  19538  -1748  -2601   4420       C  
ATOM    865  OG1 THR A 106     117.355 101.052  43.882  1.00131.34           O  
ANISOU  865  OG1 THR A 106    18200  13745  17958  -1862  -2407   4631       O  
ATOM    866  N   GLY A 107     114.782  97.831  44.876  1.00135.94           N  
ANISOU  866  N   GLY A 107    18508  14374  18770  -1446  -2025   4082       N  
ATOM    867  CA  GLY A 107     114.756  96.508  44.278  1.00128.58           C  
ANISOU  867  CA  GLY A 107    17585  13636  17635  -1405  -1930   4088       C  
ATOM    868  C   GLY A 107     113.408  96.161  43.673  1.00121.88           C  
ANISOU  868  C   GLY A 107    16692  12653  16965  -1310  -2057   4023       C  
ATOM    869  O   GLY A 107     112.980  96.776  42.697  1.00126.19           O  
ANISOU  869  O   GLY A 107    17282  13073  17591  -1348  -2303   4148       O  
ATOM    870  N   LEU A 108     112.741  95.168  44.254  1.00110.24           N  
ANISOU  870  N   LEU A 108    15130  11204  15551  -1194  -1898   3832       N  
ATOM    871  CA  LEU A 108     111.428  94.741  43.781  1.00104.13           C  
ANISOU  871  CA  LEU A 108    14300  10313  14952  -1096  -1995   3747       C  
ATOM    872  C   LEU A 108     110.432  95.894  43.810  1.00104.16           C  
ANISOU  872  C   LEU A 108    14246  10010  15320  -1065  -2217   3707       C  
ATOM    873  O   LEU A 108     110.152  96.457  44.867  1.00102.76           O  
ANISOU  873  O   LEU A 108    13988   9690  15365  -1028  -2160   3554       O  
ATOM    874  CB  LEU A 108     110.910  93.577  44.627  1.00 99.37           C  
ANISOU  874  CB  LEU A 108    13606   9778  14372   -985  -1767   3528       C  
ATOM    875  CG  LEU A 108     109.467  93.135  44.382  1.00 94.32           C  
ANISOU  875  CG  LEU A 108    12884   9005  13947   -875  -1839   3396       C  
ATOM    876  CD1 LEU A 108     109.255  92.775  42.920  1.00 93.57           C  
ANISOU  876  CD1 LEU A 108    12860   8960  13731   -899  -2004   3553       C  
ATOM    877  CD2 LEU A 108     109.110  91.964  45.285  1.00 89.58           C  
ANISOU  877  CD2 LEU A 108    12208   8497  13331   -788  -1593   3187       C  
ATOM    878  N   LYS A 109     109.894  96.236  42.643  1.00107.10           N  
ANISOU  878  N   LYS A 109    14657  10278  15758  -1086  -2473   3841       N  
ATOM    879  CA  LYS A 109     109.001  97.383  42.521  1.00111.91           C  
ANISOU  879  CA  LYS A 109    15214  10582  16725  -1063  -2725   3837       C  
ATOM    880  C   LYS A 109     107.570  96.994  42.165  1.00117.29           C  
ANISOU  880  C   LYS A 109    15802  11117  17647   -951  -2837   3731       C  
ATOM    881  O   LYS A 109     106.616  97.537  42.722  1.00119.53           O  
ANISOU  881  O   LYS A 109    15963  11159  18292   -865  -2902   3575       O  
ATOM    882  CB  LYS A 109     109.547  98.374  41.489  1.00114.36           C  
ANISOU  882  CB  LYS A 109    15646  10842  16963  -1199  -2988   4105       C  
ATOM    883  CG  LYS A 109     108.602  99.519  41.163  1.00120.64           C  
ANISOU  883  CG  LYS A 109    16397  11311  18132  -1181  -3297   4137       C  
ATOM    884  CD  LYS A 109     109.292 100.578  40.316  1.00126.30           C  
ANISOU  884  CD  LYS A 109    17246  11979  18765  -1337  -3543   4407       C  
ATOM    885  CE  LYS A 109     108.291 101.571  39.748  1.00131.33           C  
ANISOU  885  CE  LYS A 109    17848  12293  19759  -1324  -3894   4476       C  
ATOM    886  NZ  LYS A 109     107.432 102.168  40.808  1.00132.51           N1+
ANISOU  886  NZ  LYS A 109    17833  12169  20345  -1191  -3884   4245       N1+
ATOM    887  N   GLU A 110     107.420  96.057  41.235  1.00120.84           N  
ANISOU  887  N   GLU A 110    16302  11711  17899   -957  -2857   3809       N  
ATOM    888  CA  GLU A 110     106.094  95.654  40.783  1.00121.97           C  
ANISOU  888  CA  GLU A 110    16366  11731  18245   -865  -2979   3732       C  
ATOM    889  C   GLU A 110     105.865  94.149  40.889  1.00116.27           C  
ANISOU  889  C   GLU A 110    15619  11207  17351   -795  -2755   3606       C  
ATOM    890  O   GLU A 110     106.647  93.348  40.374  1.00109.63           O  
ANISOU  890  O   GLU A 110    14878  10611  16167   -858  -2649   3706       O  
ATOM    891  CB  GLU A 110     105.848  96.129  39.351  1.00133.76           C  
ANISOU  891  CB  GLU A 110    17946  13146  19730   -952  -3305   3968       C  
ATOM    892  CG  GLU A 110     104.428  95.902  38.864  1.00149.50           C  
ANISOU  892  CG  GLU A 110    19851  14975  21978   -865  -3480   3906       C  
ATOM    893  CD  GLU A 110     104.175  96.534  37.512  1.00166.74           C  
ANISOU  893  CD  GLU A 110    22122  17050  24182   -969  -3838   4154       C  
ATOM    894  OE1 GLU A 110     103.069  96.342  36.961  1.00171.18           O  
ANISOU  894  OE1 GLU A 110    22626  17490  24927   -917  -4012   4141       O  
ATOM    895  OE2 GLU A 110     105.082  97.224  37.000  1.00173.57           O1-
ANISOU  895  OE2 GLU A 110    23115  17955  24878  -1111  -3952   4366       O1-
ATOM    896  N   LEU A 111     104.780  93.780  41.563  1.00113.74           N  
ANISOU  896  N   LEU A 111    15161  10774  17283   -669  -2683   3377       N  
ATOM    897  CA  LEU A 111     104.406  92.384  41.749  1.00101.57           C  
ANISOU  897  CA  LEU A 111    13582   9386  15623   -595  -2482   3237       C  
ATOM    898  C   LEU A 111     102.983  92.183  41.242  1.00 99.64           C  
ANISOU  898  C   LEU A 111    13249   8985  15623   -513  -2643   3165       C  
ATOM    899  O   LEU A 111     102.043  92.111  42.033  1.00 98.38           O  
ANISOU  899  O   LEU A 111    12950   8693  15737   -411  -2578   2942       O  
ATOM    900  CB  LEU A 111     104.495  92.014  43.228  1.00 79.41           C  
ANISOU  900  CB  LEU A 111    10691   6620  12863   -534  -2197   3004       C  
ATOM    901  CG  LEU A 111     104.448  90.529  43.586  1.00 89.83           C  
ANISOU  901  CG  LEU A 111    11998   8138  13995   -482  -1948   2878       C  
ATOM    902  CD1 LEU A 111     105.602  89.787  42.935  1.00 88.66           C  
ANISOU  902  CD1 LEU A 111    11984   8254  13451   -558  -1864   3049       C  
ATOM    903  CD2 LEU A 111     104.477  90.350  45.094  1.00 76.49           C  
ANISOU  903  CD2 LEU A 111    10227   6456  12381   -446  -1703   2657       C  
ATOM    904  N   PRO A 112     102.824  92.102  39.913  1.00104.08           N  
ANISOU  904  N   PRO A 112    13894   9566  16086   -571  -2857   3354       N  
ATOM    905  CA  PRO A 112     101.536  92.058  39.209  1.00106.86           C  
ANISOU  905  CA  PRO A 112    14179   9760  16661   -520  -3076   3345       C  
ATOM    906  C   PRO A 112     100.761  90.757  39.397  1.00110.76           C  
ANISOU  906  C   PRO A 112    14602  10343  17137   -425  -2912   3164       C  
ATOM    907  O   PRO A 112     100.260  90.213  38.414  1.00115.93           O  
ANISOU  907  O   PRO A 112    15293  11036  17721   -441  -3033   3242       O  
ATOM    908  CB  PRO A 112     101.953  92.182  37.739  1.00108.99           C  
ANISOU  908  CB  PRO A 112    14603  10107  16702   -655  -3299   3627       C  
ATOM    909  CG  PRO A 112     103.339  91.622  37.717  1.00105.58           C  
ANISOU  909  CG  PRO A 112    14300   9959  15858   -743  -3083   3708       C  
ATOM    910  CD  PRO A 112     103.944  92.181  38.961  1.00103.65           C  
ANISOU  910  CD  PRO A 112    14007   9680  15695   -714  -2921   3606       C  
ATOM    911  N   MET A 113     100.657  90.268  40.628  1.00107.99           N  
ANISOU  911  N   MET A 113    14161  10028  16845   -341  -2647   2931       N  
ATOM    912  CA  MET A 113      99.888  89.057  40.894  1.00103.17           C  
ANISOU  912  CA  MET A 113    13478   9490  16231   -256  -2490   2749       C  
ATOM    913  C   MET A 113      98.395  89.371  40.893  1.00104.57           C  
ANISOU  913  C   MET A 113    13502   9426  16804   -165  -2652   2615       C  
ATOM    914  O   MET A 113      97.741  89.344  41.935  1.00105.98           O  
ANISOU  914  O   MET A 113    13542   9509  17218    -81  -2521   2374       O  
ATOM    915  CB  MET A 113     100.312  88.427  42.223  1.00 95.52           C  
ANISOU  915  CB  MET A 113    12473   8644  15176   -220  -2160   2556       C  
ATOM    916  CG  MET A 113     101.786  88.059  42.278  1.00 93.03           C  
ANISOU  916  CG  MET A 113    12292   8566  14491   -301  -1997   2679       C  
ATOM    917  SD  MET A 113     102.223  87.015  43.682  1.00100.11           S  
ANISOU  917  SD  MET A 113    13158   9632  15248   -266  -1628   2478       S  
ATOM    918  CE  MET A 113     101.753  88.067  45.052  1.00114.07           C  
ANISOU  918  CE  MET A 113    14792  11185  17362   -235  -1590   2276       C  
ATOM    919  N   ARG A 114      97.864  89.662  39.710  1.00102.34           N  
ANISOU  919  N   ARG A 114    13244   9049  16593   -191  -2939   2773       N  
ATOM    920  CA  ARG A 114      96.490  90.133  39.569  1.00104.61           C  
ANISOU  920  CA  ARG A 114    13382   9080  17285   -112  -3150   2686       C  
ATOM    921  C   ARG A 114      95.467  89.005  39.478  1.00 99.11           C  
ANISOU  921  C   ARG A 114    12608   8429  16620    -38  -3079   2537       C  
ATOM    922  O   ARG A 114      94.263  89.257  39.410  1.00 97.63           O  
ANISOU  922  O   ARG A 114    12279   8044  16774     36  -3232   2440       O  
ATOM    923  CB  ARG A 114      96.368  91.042  38.346  1.00116.29           C  
ANISOU  923  CB  ARG A 114    14921  10415  18849   -187  -3526   2941       C  
ATOM    924  CG  ARG A 114      96.845  90.411  37.050  1.00120.33           C  
ANISOU  924  CG  ARG A 114    15607  11124  18988   -302  -3613   3175       C  
ATOM    925  CD  ARG A 114      96.528  91.309  35.870  1.00128.50           C  
ANISOU  925  CD  ARG A 114    16689  11994  20140   -386  -4010   3416       C  
ATOM    926  NE  ARG A 114      97.024  90.766  34.610  1.00131.51           N  
ANISOU  926  NE  ARG A 114    17249  12572  20146   -527  -4093   3641       N  
ATOM    927  CZ  ARG A 114      98.175  91.119  34.048  1.00129.13           C  
ANISOU  927  CZ  ARG A 114    17116  12395  19552   -674  -4130   3856       C  
ATOM    928  NH1 ARG A 114      98.955  92.018  34.634  1.00123.77           N1+
ANISOU  928  NH1 ARG A 114    16451  11663  18913   -694  -4101   3886       N1+
ATOM    929  NH2 ARG A 114      98.546  90.575  32.898  1.00130.89           N  
ANISOU  929  NH2 ARG A 114    17491  12800  19439   -811  -4192   4034       N  
ATOM    930  N   ASN A 115      95.946  87.765  39.474  1.00 95.41           N  
ANISOU  930  N   ASN A 115    12227   8216  15807    -56  -2852   2519       N  
ATOM    931  CA  ASN A 115      95.058  86.609  39.411  1.00 90.52           C  
ANISOU  931  CA  ASN A 115    11550   7662  15183      6  -2763   2379       C  
ATOM    932  C   ASN A 115      95.139  85.746  40.661  1.00 89.44           C  
ANISOU  932  C   ASN A 115    11359   7642  14981     64  -2419   2138       C  
ATOM    933  O   ASN A 115      94.428  84.751  40.785  1.00 95.20           O  
ANISOU  933  O   ASN A 115    12037   8429  15706    114  -2311   1997       O  
ATOM    934  CB  ASN A 115      95.344  85.772  38.164  1.00 90.61           C  
ANISOU  934  CB  ASN A 115    11710   7857  14863    -71  -2823   2562       C  
ATOM    935  CG  ASN A 115      94.772  86.391  36.906  1.00 98.71           C  
ANISOU  935  CG  ASN A 115    12756   8746  16004   -124  -3183   2754       C  
ATOM    936  ND2 ASN A 115      95.487  86.248  35.796  1.00108.73           N  
ANISOU  936  ND2 ASN A 115    14195  10157  16961   -250  -3280   2988       N  
ATOM    937  OD1 ASN A 115      93.697  86.991  36.930  1.00 94.01           O  
ANISOU  937  OD1 ASN A 115    12023   7919  15779    -61  -3374   2690       O  
ATOM    938  N   LEU A 116      96.010  86.134  41.586  1.00 88.71           N  
ANISOU  938  N   LEU A 116    11285   7586  14833     44  -2256   2099       N  
ATOM    939  CA  LEU A 116      96.135  85.434  42.856  1.00 90.40           C  
ANISOU  939  CA  LEU A 116    11453   7901  14994     77  -1945   1882       C  
ATOM    940  C   LEU A 116      94.896  85.690  43.699  1.00 93.75           C  
ANISOU  940  C   LEU A 116    11686   8136  15797    158  -1919   1617       C  
ATOM    941  O   LEU A 116      94.799  86.710  44.377  1.00100.89           O  
ANISOU  941  O   LEU A 116    12502   8877  16954    168  -1942   1529       O  
ATOM    942  CB  LEU A 116      97.384  85.902  43.601  1.00 87.83           C  
ANISOU  942  CB  LEU A 116    11195   7650  14526     19  -1806   1924       C  
ATOM    943  CG  LEU A 116      97.636  85.249  44.959  1.00 81.08           C  
ANISOU  943  CG  LEU A 116    10308   6902  13596     28  -1497   1723       C  
ATOM    944  CD1 LEU A 116      97.588  83.739  44.830  1.00 80.41           C  
ANISOU  944  CD1 LEU A 116    10271   7011  13269     42  -1337   1686       C  
ATOM    945  CD2 LEU A 116      98.970  85.700  45.526  1.00 79.93           C  
ANISOU  945  CD2 LEU A 116    10248   6846  13278    -44  -1390   1809       C  
ATOM    946  N   GLN A 117      93.947  84.761  43.654  1.00 94.65           N  
ANISOU  946  N   GLN A 117    11733   8274  15955    210  -1865   1482       N  
ATOM    947  CA  GLN A 117      92.663  84.961  44.315  1.00102.57           C  
ANISOU  947  CA  GLN A 117    12542   9099  17330    284  -1856   1226       C  
ATOM    948  C   GLN A 117      92.422  83.977  45.453  1.00106.70           C  
ANISOU  948  C   GLN A 117    13016   9737  17787    295  -1549    978       C  
ATOM    949  O   GLN A 117      91.484  84.145  46.231  1.00118.98           O  
ANISOU  949  O   GLN A 117    14411  11168  19629    335  -1482    731       O  
ATOM    950  CB  GLN A 117      91.524  84.867  43.298  1.00104.79           C  
ANISOU  950  CB  GLN A 117    12753   9267  17796    333  -2093   1258       C  
ATOM    951  CG  GLN A 117      91.784  85.636  42.016  1.00112.76           C  
ANISOU  951  CG  GLN A 117    13843  10196  18806    296  -2412   1540       C  
ATOM    952  CD  GLN A 117      90.608  85.604  41.065  1.00119.97           C  
ANISOU  952  CD  GLN A 117    14677  10980  19927    336  -2666   1572       C  
ATOM    953  NE2 GLN A 117      90.880  85.314  39.798  1.00120.77           N  
ANISOU  953  NE2 GLN A 117    14915  11171  19801    273  -2837   1815       N  
ATOM    954  OE1 GLN A 117      89.468  85.845  41.462  1.00125.42           O  
ANISOU  954  OE1 GLN A 117    15181  11492  20980    413  -2709   1379       O  
ATOM    955  N   GLU A 118      93.265  82.956  45.555  1.00 96.69           N  
ANISOU  955  N   GLU A 118    11884   8703  16150    251  -1365   1040       N  
ATOM    956  CA  GLU A 118      93.063  81.919  46.560  1.00 91.58           C  
ANISOU  956  CA  GLU A 118    11210   8174  15411    248  -1091    833       C  
ATOM    957  C   GLU A 118      94.350  81.500  47.259  1.00 92.19           C  
ANISOU  957  C   GLU A 118    11411   8438  15180    181   -877    882       C  
ATOM    958  O   GLU A 118      95.383  81.308  46.622  1.00 97.87           O  
ANISOU  958  O   GLU A 118    12270   9286  15632    148   -906   1099       O  
ATOM    959  CB  GLU A 118      92.398  80.692  45.933  1.00 96.68           C  
ANISOU  959  CB  GLU A 118    11870   8912  15953    280  -1084    816       C  
ATOM    960  CG  GLU A 118      92.047  79.601  46.933  1.00102.32           C  
ANISOU  960  CG  GLU A 118    12552   9731  16595    273   -823    598       C  
ATOM    961  CD  GLU A 118      90.967  80.030  47.907  1.00108.28           C  
ANISOU  961  CD  GLU A 118    13123  10333  17687    292   -758    316       C  
ATOM    962  OE1 GLU A 118      90.108  80.851  47.522  1.00114.69           O  
ANISOU  962  OE1 GLU A 118    13807  10951  18820    345   -945    273       O  
ATOM    963  OE2 GLU A 118      90.974  79.544  49.058  1.00104.64           O1-
ANISOU  963  OE2 GLU A 118    12642   9944  17174    248   -523    134       O1-
ATOM    964  N   ILE A 119      94.271  81.359  48.579  1.00 93.40           N  
ANISOU  964  N   ILE A 119    11506   8605  15377    151   -664    675       N  
ATOM    965  CA  ILE A 119      95.363  80.812  49.375  1.00 90.71           C  
ANISOU  965  CA  ILE A 119    11269   8442  14756     81   -451    698       C  
ATOM    966  C   ILE A 119      94.794  79.819  50.385  1.00 91.60           C  
ANISOU  966  C   ILE A 119    11335   8625  14846     58   -228    470       C  
ATOM    967  O   ILE A 119      94.512  80.174  51.530  1.00 95.84           O  
ANISOU  967  O   ILE A 119    11790   9105  15518     12   -100    273       O  
ATOM    968  CB  ILE A 119      96.141  81.915  50.116  1.00 87.76           C  
ANISOU  968  CB  ILE A 119    10899   8016  14430     22   -423    711       C  
ATOM    969  CG1 ILE A 119      96.743  82.905  49.118  1.00 82.65           C  
ANISOU  969  CG1 ILE A 119    10308   7302  13793     32   -647    947       C  
ATOM    970  CG2 ILE A 119      97.236  81.310  50.980  1.00 86.43           C  
ANISOU  970  CG2 ILE A 119    10831   8031  13978    -58   -210    736       C  
ATOM    971  CD1 ILE A 119      97.585  83.982  49.764  1.00 81.41           C  
ANISOU  971  CD1 ILE A 119    10169   7101  13664    -30   -629    981       C  
ATOM    972  N   LEU A 120      94.626  78.574  49.944  1.00 86.02           N  
ANISOU  972  N   LEU A 120    10682   8040  13961     80   -182    496       N  
ATOM    973  CA  LEU A 120      93.936  77.549  50.727  1.00 80.75           C  
ANISOU  973  CA  LEU A 120     9972   7431  13278     59     -1    290       C  
ATOM    974  C   LEU A 120      94.355  77.503  52.192  1.00 82.06           C  
ANISOU  974  C   LEU A 120    10140   7652  13385    -37    215    156       C  
ATOM    975  O   LEU A 120      93.512  77.393  53.081  1.00 84.95           O  
ANISOU  975  O   LEU A 120    10409   7973  13894    -74    333    -84       O  
ATOM    976  CB  LEU A 120      94.128  76.171  50.093  1.00 73.84           C  
ANISOU  976  CB  LEU A 120     9200   6713  12144     79     37    388       C  
ATOM    977  CG  LEU A 120      93.578  76.006  48.678  1.00 78.16           C  
ANISOU  977  CG  LEU A 120     9748   7224  12724    153   -154    493       C  
ATOM    978  CD1 LEU A 120      93.767  74.577  48.198  1.00 85.56           C  
ANISOU  978  CD1 LEU A 120    10785   8320  13402    160    -81    556       C  
ATOM    979  CD2 LEU A 120      92.114  76.398  48.632  1.00 76.90           C  
ANISOU  979  CD2 LEU A 120     9430   6899  12889    200   -244    314       C  
ATOM    980  N   HIS A 121      95.658  77.581  52.440  1.00 79.03           N  
ANISOU  980  N   HIS A 121     9869   7372  12787    -90    266    310       N  
ATOM    981  CA  HIS A 121      96.174  77.487  53.799  1.00 81.46           C  
ANISOU  981  CA  HIS A 121    10198   7749  13003   -198    458    215       C  
ATOM    982  C   HIS A 121      97.348  78.430  54.009  1.00 83.80           C  
ANISOU  982  C   HIS A 121    10552   8051  13238   -244    431    357       C  
ATOM    983  O   HIS A 121      97.996  78.849  53.053  1.00 91.11           O  
ANISOU  983  O   HIS A 121    11535   8978  14106   -197    287    565       O  
ATOM    984  CB  HIS A 121      96.595  76.049  54.108  1.00 85.36           C  
ANISOU  984  CB  HIS A 121    10789   8419  13224   -237    601    247       C  
ATOM    985  CG  HIS A 121      95.471  75.063  54.038  1.00 91.43           C  
ANISOU  985  CG  HIS A 121    11511   9193  14035   -211    648     97       C  
ATOM    986  CD2 HIS A 121      94.669  74.555  55.004  1.00 94.90           C  
ANISOU  986  CD2 HIS A 121    11894   9636  14529   -279    795   -130       C  
ATOM    987  ND1 HIS A 121      95.059  74.486  52.856  1.00 93.92           N  
ANISOU  987  ND1 HIS A 121    11839   9515  14330   -116    539    177       N  
ATOM    988  CE1 HIS A 121      94.052  73.664  53.096  1.00 94.60           C  
ANISOU  988  CE1 HIS A 121    11876   9605  14463   -118    613      8       C  
ATOM    989  NE2 HIS A 121      93.796  73.688  54.392  1.00 96.78           N  
ANISOU  989  NE2 HIS A 121    12108   9880  14785   -217    770   -180       N  
ATOM    990  N   GLY A 122      97.616  78.764  55.267  1.00 84.07           N  
ANISOU  990  N   GLY A 122    10574   8093  13277   -351    571    240       N  
ATOM    991  CA  GLY A 122      98.750  79.603  55.607  1.00 84.83           C  
ANISOU  991  CA  GLY A 122    10727   8205  13301   -412    566    361       C  
ATOM    992  C   GLY A 122      98.430  81.083  55.614  1.00 85.42           C  
ANISOU  992  C   GLY A 122    10712   8097  13646   -402    464    298       C  
ATOM    993  O   GLY A 122      97.367  81.504  55.158  1.00 85.25           O  
ANISOU  993  O   GLY A 122    10582   7926  13884   -328    363    191       O  
ATOM    994  N   ALA A 123      99.363  81.872  56.139  1.00 89.63           N  
ANISOU  994  N   ALA A 123    11288   8638  14130   -478    486    365       N  
ATOM    995  CA  ALA A 123      99.211  83.321  56.201  1.00 96.19           C  
ANISOU  995  CA  ALA A 123    12047   9294  15208   -479    393    317       C  
ATOM    996  C   ALA A 123     100.054  84.006  55.129  1.00 98.96           C  
ANISOU  996  C   ALA A 123    12468   9627  15506   -427    201    585       C  
ATOM    997  O   ALA A 123     100.541  83.360  54.202  1.00101.50           O  
ANISOU  997  O   ALA A 123    12874  10056  15634   -377    130    782       O  
ATOM    998  CB  ALA A 123      99.592  83.834  57.582  1.00 94.11           C  
ANISOU  998  CB  ALA A 123    11778   9037  14944   -618    553    183       C  
ATOM    999  N   VAL A 124     100.220  85.317  55.263  1.00 96.39           N  
ANISOU  999  N   VAL A 124    12107   9164  15352   -449    121    583       N  
ATOM   1000  CA  VAL A 124     101.001  86.095  54.309  1.00 98.75           C  
ANISOU 1000  CA  VAL A 124    12474   9433  15614   -420    -67    830       C  
ATOM   1001  C   VAL A 124     101.955  87.025  55.047  1.00100.61           C  
ANISOU 1001  C   VAL A 124    12749   9664  15813   -521    -21    867       C  
ATOM   1002  O   VAL A 124     101.603  87.590  56.082  1.00106.63           O  
ANISOU 1002  O   VAL A 124    13439  10336  16739   -584     80    663       O  
ATOM   1003  CB  VAL A 124     100.095  86.932  53.384  1.00102.75           C  
ANISOU 1003  CB  VAL A 124    12891   9725  16423   -326   -292    828       C  
ATOM   1004  CG1 VAL A 124     100.923  87.635  52.321  1.00106.18           C  
ANISOU 1004  CG1 VAL A 124    13416  10147  16782   -315   -495   1106       C  
ATOM   1005  CG2 VAL A 124      99.036  86.053  52.739  1.00 99.52           C  
ANISOU 1005  CG2 VAL A 124    12429   9309  16076   -235   -335    767       C  
ATOM   1006  N   ARG A 125     103.161  87.184  54.512  1.00 98.08           N  
ANISOU 1006  N   ARG A 125    12542   9446  15279   -543    -90   1118       N  
ATOM   1007  CA  ARG A 125     104.174  88.013  55.152  1.00102.45           C  
ANISOU 1007  CA  ARG A 125    13145  10015  15767   -644    -52   1180       C  
ATOM   1008  C   ARG A 125     104.859  88.958  54.169  1.00104.94           C  
ANISOU 1008  C   ARG A 125    13519  10277  16076   -629   -253   1412       C  
ATOM   1009  O   ARG A 125     105.539  88.518  53.243  1.00108.17           O  
ANISOU 1009  O   ARG A 125    14016  10810  16276   -607   -326   1629       O  
ATOM   1010  CB  ARG A 125     105.225  87.137  55.836  1.00106.65           C  
ANISOU 1010  CB  ARG A 125    13767  10771  15982   -730    121   1248       C  
ATOM   1011  CG  ARG A 125     106.429  87.903  56.360  1.00115.31           C  
ANISOU 1011  CG  ARG A 125    14929  11914  16968   -836    145   1356       C  
ATOM   1012  CD  ARG A 125     106.136  88.567  57.696  1.00121.63           C  
ANISOU 1012  CD  ARG A 125    15673  12627  17913   -940    269   1138       C  
ATOM   1013  NE  ARG A 125     107.209  89.468  58.111  1.00121.72           N  
ANISOU 1013  NE  ARG A 125    15743  12655  17851  -1041    266   1240       N  
ATOM   1014  CZ  ARG A 125     108.376  89.067  58.606  1.00116.99           C  
ANISOU 1014  CZ  ARG A 125    15232  12237  16984  -1135    359   1364       C  
ATOM   1015  NH1 ARG A 125     108.634  87.774  58.743  1.00114.31           N1+
ANISOU 1015  NH1 ARG A 125    14930  12068  16433  -1136    456   1404       N1+
ATOM   1016  NH2 ARG A 125     109.290  89.961  58.958  1.00113.84           N  
ANISOU 1016  NH2 ARG A 125    14878  11840  16536  -1228    346   1452       N  
ATOM   1017  N   PHE A 126     104.671  90.257  54.380  1.00101.54           N  
ANISOU 1017  N   PHE A 126    13038   9661  15880   -651   -339   1358       N  
ATOM   1018  CA  PHE A 126     105.387  91.277  53.623  1.00 99.54           C  
ANISOU 1018  CA  PHE A 126    12847   9349  15623   -665   -524   1573       C  
ATOM   1019  C   PHE A 126     106.245  92.102  54.574  1.00105.16           C  
ANISOU 1019  C   PHE A 126    13590  10064  16303   -780   -440   1563       C  
ATOM   1020  O   PHE A 126     105.776  92.532  55.627  1.00110.76           O  
ANISOU 1020  O   PHE A 126    14222  10672  17189   -824   -332   1341       O  
ATOM   1021  CB  PHE A 126     104.413  92.186  52.873  1.00 96.32           C  
ANISOU 1021  CB  PHE A 126    12359   8693  15547   -587   -748   1550       C  
ATOM   1022  CG  PHE A 126     103.941  91.626  51.561  1.00 95.79           C  
ANISOU 1022  CG  PHE A 126    12306   8635  15453   -498   -908   1677       C  
ATOM   1023  CD1 PHE A 126     102.807  90.836  51.496  1.00 96.20           C  
ANISOU 1023  CD1 PHE A 126    12273   8660  15620   -417   -876   1521       C  
ATOM   1024  CD2 PHE A 126     104.629  91.898  50.390  1.00 97.77           C  
ANISOU 1024  CD2 PHE A 126    12660   8928  15559   -509  -1089   1948       C  
ATOM   1025  CE1 PHE A 126     102.369  90.324  50.289  1.00 96.35           C  
ANISOU 1025  CE1 PHE A 126    12309   8690  15608   -346  -1026   1637       C  
ATOM   1026  CE2 PHE A 126     104.196  91.390  49.180  1.00 97.14           C  
ANISOU 1026  CE2 PHE A 126    12601   8864  15442   -449  -1235   2061       C  
ATOM   1027  CZ  PHE A 126     103.065  90.602  49.130  1.00 96.75           C  
ANISOU 1027  CZ  PHE A 126    12468   8785  15509   -366  -1205   1908       C  
ATOM   1028  N   SER A 127     107.501  92.323  54.203  1.00105.20           N  
ANISOU 1028  N   SER A 127    13705  10187  16078   -837   -484   1797       N  
ATOM   1029  CA  SER A 127     108.428  93.031  55.076  1.00104.87           C  
ANISOU 1029  CA  SER A 127    13704  10173  15968   -955   -404   1811       C  
ATOM   1030  C   SER A 127     109.653  93.542  54.328  1.00106.75           C  
ANISOU 1030  C   SER A 127    14050  10488  16021  -1001   -525   2090       C  
ATOM   1031  O   SER A 127     110.302  92.796  53.595  1.00110.85           O  
ANISOU 1031  O   SER A 127    14642  11180  16296   -987   -539   2269       O  
ATOM   1032  CB  SER A 127     108.865  92.122  56.226  1.00106.07           C  
ANISOU 1032  CB  SER A 127    13875  10508  15920  -1033   -163   1719       C  
ATOM   1033  OG  SER A 127     109.896  92.724  56.989  1.00110.08           O  
ANISOU 1033  OG  SER A 127    14436  11071  16318  -1159    -96   1770       O  
ATOM   1034  N   ASN A 128     109.965  94.819  54.522  1.00107.90           N  
ANISOU 1034  N   ASN A 128    14205  10505  16289  -1063   -605   2115       N  
ATOM   1035  CA  ASN A 128     111.150  95.425  53.926  1.00112.04           C  
ANISOU 1035  CA  ASN A 128    14831  11095  16643  -1129   -713   2367       C  
ATOM   1036  C   ASN A 128     111.161  95.355  52.403  1.00109.21           C  
ANISOU 1036  C   ASN A 128    14522  10743  16228  -1071   -915   2576       C  
ATOM   1037  O   ASN A 128     112.067  94.775  51.805  1.00111.75           O  
ANISOU 1037  O   ASN A 128    14927  11262  16271  -1096   -905   2762       O  
ATOM   1038  CB  ASN A 128     112.420  94.786  54.492  1.00120.39           C  
ANISOU 1038  CB  ASN A 128    15961  12404  17378  -1218   -546   2460       C  
ATOM   1039  CG  ASN A 128     112.610  95.077  55.967  1.00128.52           C  
ANISOU 1039  CG  ASN A 128    16966  13429  18435  -1318   -376   2297       C  
ATOM   1040  ND2 ASN A 128     113.372  94.227  56.646  1.00133.22           N  
ANISOU 1040  ND2 ASN A 128    17597  14233  18787  -1381   -209   2318       N  
ATOM   1041  OD1 ASN A 128     112.079  96.057  56.491  1.00128.38           O  
ANISOU 1041  OD1 ASN A 128    16898  13221  18661  -1344   -398   2152       O  
ATOM   1042  N   ASN A 129     110.148  95.951  51.783  1.00105.26           N  
ANISOU 1042  N   ASN A 129    13969  10025  16000  -1001  -1099   2541       N  
ATOM   1043  CA  ASN A 129     110.070  96.030  50.329  1.00106.97           C  
ANISOU 1043  CA  ASN A 129    14238  10221  16186   -968  -1320   2741       C  
ATOM   1044  C   ASN A 129     109.929  97.481  49.886  1.00112.03           C  
ANISOU 1044  C   ASN A 129    14885  10630  17050   -996  -1555   2824       C  
ATOM   1045  O   ASN A 129     108.856  97.903  49.454  1.00117.40           O  
ANISOU 1045  O   ASN A 129    15495  11095  18016   -924  -1722   2766       O  
ATOM   1046  CB  ASN A 129     108.898  95.197  49.810  1.00106.82           C  
ANISOU 1046  CB  ASN A 129    14152  10163  16271   -854  -1355   2649       C  
ATOM   1047  CG  ASN A 129     109.031  93.728  50.158  1.00107.27           C  
ANISOU 1047  CG  ASN A 129    14212  10442  16105   -827  -1139   2581       C  
ATOM   1048  ND2 ASN A 129     108.016  93.184  50.818  1.00110.29           N  
ANISOU 1048  ND2 ASN A 129    14494  10765  16645   -760  -1029   2349       N  
ATOM   1049  OD1 ASN A 129     110.032  93.087  49.834  1.00104.24           O  
ANISOU 1049  OD1 ASN A 129    13914  10275  15418   -869  -1072   2731       O  
ATOM   1050  N   PRO A 130     111.025  98.247  49.990  1.00111.03           N  
ANISOU 1050  N   PRO A 130    14841  10545  16802  -1103  -1576   2965       N  
ATOM   1051  CA  PRO A 130     111.051  99.699  49.784  1.00112.73           C  
ANISOU 1051  CA  PRO A 130    15071  10543  17220  -1152  -1776   3038       C  
ATOM   1052  C   PRO A 130     110.451 100.137  48.453  1.00117.39           C  
ANISOU 1052  C   PRO A 130    15679  10980  17945  -1117  -2071   3186       C  
ATOM   1053  O   PRO A 130     109.840 101.204  48.385  1.00125.77           O  
ANISOU 1053  O   PRO A 130    16693  11775  19321  -1101  -2252   3157       O  
ATOM   1054  CB  PRO A 130     112.548 100.027  49.813  1.00113.44           C  
ANISOU 1054  CB  PRO A 130    15277  10802  17021  -1282  -1737   3228       C  
ATOM   1055  CG  PRO A 130     113.160  98.932  50.607  1.00110.56           C  
ANISOU 1055  CG  PRO A 130    14914  10687  16404  -1296  -1465   3157       C  
ATOM   1056  CD  PRO A 130     112.366  97.708  50.272  1.00110.38           C  
ANISOU 1056  CD  PRO A 130    14843  10731  16365  -1189  -1412   3075       C  
ATOM   1057  N   ALA A 131     110.623  99.328  47.414  1.00114.32           N  
ANISOU 1057  N   ALA A 131    15357  10753  17327  -1113  -2122   3342       N  
ATOM   1058  CA  ALA A 131     110.186  99.712  46.075  1.00112.67           C  
ANISOU 1058  CA  ALA A 131    15191  10430  17188  -1114  -2410   3517       C  
ATOM   1059  C   ALA A 131     108.821  99.135  45.699  1.00110.97           C  
ANISOU 1059  C   ALA A 131    14881  10106  17178   -992  -2482   3401       C  
ATOM   1060  O   ALA A 131     108.248  99.506  44.675  1.00111.39           O  
ANISOU 1060  O   ALA A 131    14948  10023  17352   -985  -2741   3522       O  
ATOM   1061  CB  ALA A 131     111.238  99.321  45.041  1.00107.42           C  
ANISOU 1061  CB  ALA A 131    14669  10002  16142  -1215  -2447   3775       C  
ATOM   1062  N   LEU A 132     108.301  98.235  46.528  1.00103.57           N  
ANISOU 1062  N   LEU A 132    13849   9227  16275   -905  -2261   3173       N  
ATOM   1063  CA  LEU A 132     107.021  97.594  46.244  1.00100.30           C  
ANISOU 1063  CA  LEU A 132    13340   8730  16040   -791  -2302   3047       C  
ATOM   1064  C   LEU A 132     105.892  98.613  46.122  1.00105.98           C  
ANISOU 1064  C   LEU A 132    13953   9116  17197   -730  -2531   2973       C  
ATOM   1065  O   LEU A 132     105.663  99.411  47.031  1.00107.13           O  
ANISOU 1065  O   LEU A 132    14016   9089  17602   -718  -2494   2815       O  
ATOM   1066  CB  LEU A 132     106.680  96.560  47.317  1.00 97.81           C  
ANISOU 1066  CB  LEU A 132    12939   8522  15703   -724  -2014   2797       C  
ATOM   1067  CG  LEU A 132     105.433  95.723  47.022  1.00 96.14           C  
ANISOU 1067  CG  LEU A 132    12636   8267  15626   -614  -2027   2668       C  
ATOM   1068  CD1 LEU A 132     105.523  95.111  45.633  1.00 91.76           C  
ANISOU 1068  CD1 LEU A 132    12174   7830  14861   -623  -2167   2878       C  
ATOM   1069  CD2 LEU A 132     105.234  94.646  48.077  1.00 94.44           C  
ANISOU 1069  CD2 LEU A 132    12358   8185  15338   -573  -1734   2443       C  
ATOM   1070  N   CYS A 133     105.186  98.573  44.995  1.00108.07           N  
ANISOU 1070  N   CYS A 133    14219   9291  17552   -697  -2769   3083       N  
ATOM   1071  CA  CYS A 133     104.101  99.511  44.727  1.00104.39           C  
ANISOU 1071  CA  CYS A 133    13649   8499  17515   -638  -3028   3044       C  
ATOM   1072  C   CYS A 133     102.755  98.806  44.582  1.00102.52           C  
ANISOU 1072  C   CYS A 133    13283   8183  17486   -515  -3047   2883       C  
ATOM   1073  O   CYS A 133     102.691  97.656  44.146  1.00104.35           O  
ANISOU 1073  O   CYS A 133    13553   8610  17484   -499  -2965   2908       O  
ATOM   1074  CB  CYS A 133     104.394 100.311  43.454  1.00102.98           C  
ANISOU 1074  CB  CYS A 133    13583   8234  17309   -725  -3360   3345       C  
ATOM   1075  SG  CYS A 133     105.969 101.196  43.454  1.00201.33           S  
ANISOU 1075  SG  CYS A 133    26201  20780  29515   -886  -3373   3562       S  
ATOM   1076  N   ASN A 134     101.687  99.506  44.957  1.00101.02           N  
ANISOU 1076  N   ASN A 134    12935   7703  17746   -430  -3153   2711       N  
ATOM   1077  CA  ASN A 134     100.317  99.046  44.727  1.00104.34           C  
ANISOU 1077  CA  ASN A 134    13215   8000  18430   -315  -3227   2570       C  
ATOM   1078  C   ASN A 134      99.860  97.884  45.610  1.00107.22           C  
ANISOU 1078  C   ASN A 134    13489   8508  18741   -245  -2915   2301       C  
ATOM   1079  O   ASN A 134      98.755  97.911  46.152  1.00107.87           O  
ANISOU 1079  O   ASN A 134    13397   8424  19164   -151  -2883   2053       O  
ATOM   1080  CB  ASN A 134     100.109  98.700  43.249  1.00103.89           C  
ANISOU 1080  CB  ASN A 134    13244   7981  18247   -337  -3483   2820       C  
ATOM   1081  CG  ASN A 134     100.461  99.850  42.328  1.00105.75           C  
ANISOU 1081  CG  ASN A 134    13572   8063  18546   -423  -3819   3094       C  
ATOM   1082  ND2 ASN A 134     100.094 101.062  42.728  1.00110.08           N  
ANISOU 1082  ND2 ASN A 134    14022   8317  19487   -393  -3961   3026       N  
ATOM   1083  OD1 ASN A 134     101.064  99.653  41.274  1.00103.64           O  
ANISOU 1083  OD1 ASN A 134    13463   7939  17976   -523  -3947   3359       O  
ATOM   1084  N   VAL A 135     100.705  96.865  45.745  1.00104.94           N  
ANISOU 1084  N   VAL A 135    13314   8524  18034   -295  -2691   2348       N  
ATOM   1085  CA  VAL A 135     100.366  95.681  46.530  1.00103.47           C  
ANISOU 1085  CA  VAL A 135    13067   8494  17754   -245  -2404   2124       C  
ATOM   1086  C   VAL A 135      99.823  96.061  47.904  1.00106.39           C  
ANISOU 1086  C   VAL A 135    13284   8725  18414   -209  -2228   1811       C  
ATOM   1087  O   VAL A 135      99.012  95.340  48.487  1.00108.92           O  
ANISOU 1087  O   VAL A 135    13495   9061  18829   -148  -2069   1577       O  
ATOM   1088  CB  VAL A 135     101.584  94.752  46.701  1.00104.11           C  
ANISOU 1088  CB  VAL A 135    13293   8898  17367   -319  -2179   2220       C  
ATOM   1089  CG1 VAL A 135     101.236  93.570  47.592  1.00 96.33           C  
ANISOU 1089  CG1 VAL A 135    12246   8054  16300   -277  -1893   1990       C  
ATOM   1090  CG2 VAL A 135     102.078  94.275  45.345  1.00110.92           C  
ANISOU 1090  CG2 VAL A 135    14296   9911  17938   -361  -2322   2495       C  
ATOM   1091  N   GLU A 136     100.271  97.204  48.409  1.00110.59           N  
ANISOU 1091  N   GLU A 136    13811   9124  19083   -257  -2257   1803       N  
ATOM   1092  CA  GLU A 136      99.846  97.696  49.713  1.00121.17           C  
ANISOU 1092  CA  GLU A 136    15016  10329  20696   -246  -2089   1505       C  
ATOM   1093  C   GLU A 136      98.357  98.028  49.750  1.00118.81           C  
ANISOU 1093  C   GLU A 136    14514   9759  20871   -137  -2195   1287       C  
ATOM   1094  O   GLU A 136      97.826  98.400  50.795  1.00122.17           O  
ANISOU 1094  O   GLU A 136    14799  10055  21563   -123  -2052   1002       O  
ATOM   1095  CB  GLU A 136     100.661  98.933  50.093  1.00140.67           C  
ANISOU 1095  CB  GLU A 136    17533  12697  23219   -326  -2131   1568       C  
ATOM   1096  CG  GLU A 136     100.712  99.995  49.002  1.00157.99           C  
ANISOU 1096  CG  GLU A 136    19765  14692  25570   -326  -2482   1808       C  
ATOM   1097  CD  GLU A 136     101.769 101.053  49.264  1.00171.34           C  
ANISOU 1097  CD  GLU A 136    21550  16346  27205   -428  -2514   1926       C  
ATOM   1098  OE1 GLU A 136     102.104 101.285  50.445  1.00174.99           O  
ANISOU 1098  OE1 GLU A 136    21984  16828  27677   -474  -2290   1745       O  
ATOM   1099  OE2 GLU A 136     102.264 101.653  48.287  1.00176.50           O1-
ANISOU 1099  OE2 GLU A 136    22311  16956  27796   -473  -2763   2202       O1-
ATOM   1100  N   SER A 137      97.685  97.888  48.611  1.00116.05           N  
ANISOU 1100  N   SER A 137    14144   9326  20625    -68  -2443   1416       N  
ATOM   1101  CA  SER A 137      96.281  98.273  48.503  1.00120.22           C  
ANISOU 1101  CA  SER A 137    14472   9578  21628     39  -2591   1242       C  
ATOM   1102  C   SER A 137      95.352  97.074  48.346  1.00120.89           C  
ANISOU 1102  C   SER A 137    14481   9756  21697    113  -2513   1119       C  
ATOM   1103  O   SER A 137      94.149  97.237  48.147  1.00126.66           O  
ANISOU 1103  O   SER A 137    15043  10282  22800    206  -2643    988       O  
ATOM   1104  CB  SER A 137      96.080  99.237  47.331  1.00122.64           C  
ANISOU 1104  CB  SER A 137    14789   9655  22153     60  -2988   1480       C  
ATOM   1105  OG  SER A 137      96.239  98.573  46.088  1.00119.08           O  
ANISOU 1105  OG  SER A 137    14465   9346  21432     44  -3152   1749       O  
ATOM   1106  N   ILE A 138      95.910  95.872  48.437  1.00116.98           N  
ANISOU 1106  N   ILE A 138    14103   9561  20783     72  -2306   1161       N  
ATOM   1107  CA  ILE A 138      95.130  94.654  48.244  1.00117.31           C  
ANISOU 1107  CA  ILE A 138    14096   9713  20761    130  -2227   1066       C  
ATOM   1108  C   ILE A 138      94.388  94.228  49.506  1.00119.76           C  
ANISOU 1108  C   ILE A 138    14253  10018  21232    156  -1951    701       C  
ATOM   1109  O   ILE A 138      94.968  94.171  50.591  1.00125.26           O  
ANISOU 1109  O   ILE A 138    14976  10818  21798     86  -1699    572       O  
ATOM   1110  CB  ILE A 138      96.012  93.487  47.756  1.00115.66           C  
ANISOU 1110  CB  ILE A 138    14077   9823  20047     76  -2128   1263       C  
ATOM   1111  CG1 ILE A 138      96.079  93.473  46.230  1.00117.95           C  
ANISOU 1111  CG1 ILE A 138    14464  10115  20236     77  -2419   1562       C  
ATOM   1112  CG2 ILE A 138      95.463  92.160  48.249  1.00116.95           C  
ANISOU 1112  CG2 ILE A 138    14192  10143  20099    108  -1892   1069       C  
ATOM   1113  CD1 ILE A 138      96.671  94.722  45.632  1.00124.41           C  
ANISOU 1113  CD1 ILE A 138    15354  10794  21122     26  -2671   1788       C  
ATOM   1114  N   GLN A 139      93.100  93.933  49.356  1.00114.33           N  
ANISOU 1114  N   GLN A 139    13405   9211  20824    245  -2005    535       N  
ATOM   1115  CA  GLN A 139      92.301  93.411  50.456  1.00108.06           C  
ANISOU 1115  CA  GLN A 139    12463   8427  20168    261  -1744    184       C  
ATOM   1116  C   GLN A 139      92.532  91.912  50.572  1.00109.00           C  
ANISOU 1116  C   GLN A 139    12684   8841  19889    230  -1533    188       C  
ATOM   1117  O   GLN A 139      91.894  91.122  49.875  1.00112.20           O  
ANISOU 1117  O   GLN A 139    13074   9291  20267    286  -1606    223       O  
ATOM   1118  CB  GLN A 139      90.819  93.685  50.216  1.00101.06           C  
ANISOU 1118  CB  GLN A 139    11353   7294  19751    369  -1890      2       C  
ATOM   1119  CG  GLN A 139      90.522  95.079  49.704  1.00103.12           C  
ANISOU 1119  CG  GLN A 139    11521   7242  20417    422  -2193     74       C  
ATOM   1120  CD  GLN A 139      89.039  95.319  49.516  1.00115.89           C  
ANISOU 1120  CD  GLN A 139    12897   8610  22527    533  -2335   -119       C  
ATOM   1121  NE2 GLN A 139      88.224  94.597  50.276  1.00118.48           N  
ANISOU 1121  NE2 GLN A 139    13089   8989  22939    553  -2101   -425       N  
ATOM   1122  OE1 GLN A 139      88.630  96.139  48.695  1.00123.18           O  
ANISOU 1122  OE1 GLN A 139    13755   9295  23755    595  -2658     10       O  
ATOM   1123  N   TRP A 140      93.447  91.523  51.453  1.00106.56           N  
ANISOU 1123  N   TRP A 140    12481   8729  19279    135  -1278    157       N  
ATOM   1124  CA  TRP A 140      93.836  90.122  51.579  1.00104.39           C  
ANISOU 1124  CA  TRP A 140    12319   8733  18610     97  -1086    191       C  
ATOM   1125  C   TRP A 140      92.769  89.266  52.255  1.00103.39           C  
ANISOU 1125  C   TRP A 140    12066   8633  18583    116   -899   -102       C  
ATOM   1126  O   TRP A 140      92.870  88.040  52.276  1.00 95.06           O  
ANISOU 1126  O   TRP A 140    11087   7784  17249     98   -765    -87       O  
ATOM   1127  CB  TRP A 140      95.168  90.001  52.319  1.00 98.80           C  
ANISOU 1127  CB  TRP A 140    11759   8216  17566    -14   -893    262       C  
ATOM   1128  CG  TRP A 140      96.318  90.551  51.540  1.00 95.67           C  
ANISOU 1128  CG  TRP A 140    11511   7855  16982    -41  -1057    577       C  
ATOM   1129  CD1 TRP A 140      96.768  91.837  51.545  1.00 94.77           C  
ANISOU 1129  CD1 TRP A 140    11401   7593  17015    -67  -1180    650       C  
ATOM   1130  CD2 TRP A 140      97.161  89.833  50.632  1.00 94.05           C  
ANISOU 1130  CD2 TRP A 140    11473   7849  16413    -53  -1112    853       C  
ATOM   1131  CE2 TRP A 140      98.105  90.748  50.127  1.00 92.66           C  
ANISOU 1131  CE2 TRP A 140    11394   7642  16171    -95  -1265   1084       C  
ATOM   1132  CE3 TRP A 140      97.212  88.504  50.200  1.00 94.51           C  
ANISOU 1132  CE3 TRP A 140    11605   8106  16198    -39  -1041    919       C  
ATOM   1133  NE1 TRP A 140      97.843  91.965  50.698  1.00 92.87           N  
ANISOU 1133  NE1 TRP A 140    11323   7453  16512   -101  -1310    961       N  
ATOM   1134  CZ2 TRP A 140      99.087  90.378  49.211  1.00 88.36           C  
ANISOU 1134  CZ2 TRP A 140    11011   7266  15294   -127  -1340   1367       C  
ATOM   1135  CZ3 TRP A 140      98.189  88.139  49.291  1.00 93.20           C  
ANISOU 1135  CZ3 TRP A 140    11597   8099  15715    -64  -1115   1196       C  
ATOM   1136  CH2 TRP A 140      99.113  89.073  48.807  1.00 85.29           C  
ANISOU 1136  CH2 TRP A 140    10684   7071  14653   -110  -1259   1413       C  
ATOM   1137  N   ARG A 141      91.746  89.914  52.802  1.00110.09           N  
ANISOU 1137  N   ARG A 141    12718   9271  19840    148   -889   -371       N  
ATOM   1138  CA  ARG A 141      90.643  89.197  53.431  1.00110.32           C  
ANISOU 1138  CA  ARG A 141    12606   9309  20001    159   -717   -670       C  
ATOM   1139  C   ARG A 141      89.907  88.342  52.403  1.00107.35           C  
ANISOU 1139  C   ARG A 141    12215   8963  19610    248   -854   -586       C  
ATOM   1140  O   ARG A 141      89.193  87.404  52.756  1.00110.83           O  
ANISOU 1140  O   ARG A 141    12596   9486  20028    247   -705   -765       O  
ATOM   1141  CB  ARG A 141      89.683  90.178  54.107  1.00116.53           C  
ANISOU 1141  CB  ARG A 141    13167   9842  21269    182   -701   -976       C  
ATOM   1142  CG  ARG A 141      88.435  89.537  54.694  1.00122.86           C  
ANISOU 1142  CG  ARG A 141    13796  10630  22254    193   -539  -1304       C  
ATOM   1143  CD  ARG A 141      87.684  90.505  55.597  1.00130.35           C  
ANISOU 1143  CD  ARG A 141    14529  11358  23640    182   -454  -1644       C  
ATOM   1144  NE  ARG A 141      88.363  90.697  56.876  1.00136.03           N  
ANISOU 1144  NE  ARG A 141    15303  12171  24212     37   -185  -1792       N  
ATOM   1145  CZ  ARG A 141      89.240  91.665  57.122  1.00142.29           C  
ANISOU 1145  CZ  ARG A 141    16162  12903  24999    -11   -213  -1705       C  
ATOM   1146  NH1 ARG A 141      89.547  92.542  56.176  1.00146.93           N1+
ANISOU 1146  NH1 ARG A 141    16771  13333  25722     75   -499  -1469       N1+
ATOM   1147  NH2 ARG A 141      89.809  91.758  58.317  1.00141.41           N  
ANISOU 1147  NH2 ARG A 141    16099  12890  24739   -157     40  -1850       N  
ATOM   1148  N   ASP A 142      90.096  88.669  51.129  1.00104.54           N  
ANISOU 1148  N   ASP A 142    11922   8545  19255    310  -1139   -310       N  
ATOM   1149  CA  ASP A 142      89.466  87.932  50.039  1.00110.77           C  
ANISOU 1149  CA  ASP A 142    12713   9361  20015    381  -1297   -198       C  
ATOM   1150  C   ASP A 142      90.360  86.792  49.556  1.00111.67           C  
ANISOU 1150  C   ASP A 142    13038   9750  19640    337  -1228     22       C  
ATOM   1151  O   ASP A 142      89.877  85.707  49.226  1.00111.55           O  
ANISOU 1151  O   ASP A 142    13033   9846  19504    360  -1187      3       O  
ATOM   1152  CB  ASP A 142      89.137  88.880  48.882  1.00118.73           C  
ANISOU 1152  CB  ASP A 142    13675  10150  21285    452  -1656    -15       C  
ATOM   1153  CG  ASP A 142      88.465  88.175  47.718  1.00129.08           C  
ANISOU 1153  CG  ASP A 142    14991  11483  22571    510  -1840    108       C  
ATOM   1154  OD1 ASP A 142      89.088  87.273  47.118  1.00130.84           O  
ANISOU 1154  OD1 ASP A 142    15387  11921  22404    475  -1818    302       O  
ATOM   1155  OD2 ASP A 142      87.313  88.533  47.393  1.00134.57           O1-
ANISOU 1155  OD2 ASP A 142    15511  11975  23645    587  -2009      9       O1-
ATOM   1156  N   ILE A 143      91.664  87.043  49.523  1.00108.29           N  
ANISOU 1156  N   ILE A 143    12773   9430  18944    274  -1212    223       N  
ATOM   1157  CA  ILE A 143      92.629  86.058  49.044  1.00102.77           C  
ANISOU 1157  CA  ILE A 143    12267   8981  17799    232  -1152    438       C  
ATOM   1158  C   ILE A 143      92.943  85.001  50.100  1.00 99.94           C  
ANISOU 1158  C   ILE A 143    11953   8824  17195    173   -840    293       C  
ATOM   1159  O   ILE A 143      93.067  83.817  49.786  1.00 98.87           O  
ANISOU 1159  O   ILE A 143    11903   8864  16800    171   -766    353       O  
ATOM   1160  CB  ILE A 143      93.941  86.733  48.604  1.00107.10           C  
ANISOU 1160  CB  ILE A 143    12965   9572  18157    181  -1252    706       C  
ATOM   1161  CG1 ILE A 143      93.655  87.845  47.594  1.00113.15           C  
ANISOU 1161  CG1 ILE A 143    13697  10129  19166    221  -1576    860       C  
ATOM   1162  CG2 ILE A 143      94.898  85.711  48.015  1.00109.34           C  
ANISOU 1162  CG2 ILE A 143    13431  10107  18007    144  -1196    918       C  
ATOM   1163  CD1 ILE A 143      94.895  88.550  47.103  1.00115.71           C  
ANISOU 1163  CD1 ILE A 143    14168  10488  19307    158  -1689   1127       C  
ATOM   1164  N   VAL A 144      93.071  85.434  51.350  1.00102.48           N  
ANISOU 1164  N   VAL A 144    12220   9116  17602    114   -662    104       N  
ATOM   1165  CA  VAL A 144      93.412  84.535  52.448  1.00105.21           C  
ANISOU 1165  CA  VAL A 144    12613   9642  17719     32   -377    -27       C  
ATOM   1166  C   VAL A 144      92.161  84.032  53.169  1.00121.79           C  
ANISOU 1166  C   VAL A 144    14565  11700  20009     35   -234   -338       C  
ATOM   1167  O   VAL A 144      91.101  84.655  53.097  1.00129.66           O  
ANISOU 1167  O   VAL A 144    15395  12500  21369     93   -327   -498       O  
ATOM   1168  CB  VAL A 144      94.339  85.229  53.465  1.00 96.34           C  
ANISOU 1168  CB  VAL A 144    11532   8538  16535    -67   -248    -52       C  
ATOM   1169  CG1 VAL A 144      94.920  84.218  54.437  1.00 91.83           C  
ANISOU 1169  CG1 VAL A 144    11051   8182  15660   -167     11   -109       C  
ATOM   1170  CG2 VAL A 144      95.452  85.962  52.742  1.00100.61           C  
ANISOU 1170  CG2 VAL A 144    12189   9079  16958    -69   -412    234       C  
ATOM   1171  N   SER A 145      92.289  82.900  53.856  1.00124.45           N  
ANISOU 1171  N   SER A 145    14960  12218  20105    -32    -15   -422       N  
ATOM   1172  CA  SER A 145      91.184  82.342  54.627  1.00122.93           C  
ANISOU 1172  CA  SER A 145    14645  12015  20048    -57    147   -719       C  
ATOM   1173  C   SER A 145      91.172  82.907  56.043  1.00125.73           C  
ANISOU 1173  C   SER A 145    14931  12333  20510   -170    344   -964       C  
ATOM   1174  O   SER A 145      92.223  83.088  56.657  1.00122.94           O  
ANISOU 1174  O   SER A 145    14684  12070  19957   -263    442   -889       O  
ATOM   1175  CB  SER A 145      91.273  80.818  54.673  1.00120.18           C  
ANISOU 1175  CB  SER A 145    14398  11875  19391    -88    279   -692       C  
ATOM   1176  OG  SER A 145      90.228  80.280  55.464  1.00122.64           O  
ANISOU 1176  OG  SER A 145    14598  12184  19815   -131    442   -981       O  
ATOM   1177  N   SER A 146      89.974  83.172  56.556  1.00133.00           N  
ANISOU 1177  N   SER A 146    15667  13121  21744   -169    407  -1262       N  
ATOM   1178  CA  SER A 146      89.805  83.823  57.853  1.00138.31           C  
ANISOU 1178  CA  SER A 146    16249  13733  22570   -282    591  -1533       C  
ATOM   1179  C   SER A 146      90.614  83.174  58.975  1.00139.40           C  
ANISOU 1179  C   SER A 146    16520  14077  22368   -449    836  -1560       C  
ATOM   1180  O   SER A 146      91.034  83.847  59.917  1.00138.62           O  
ANISOU 1180  O   SER A 146    16420  13962  22288   -562    955  -1665       O  
ATOM   1181  CB  SER A 146      88.324  83.860  58.238  1.00139.42           C  
ANISOU 1181  CB  SER A 146    16173  13745  23053   -268    661  -1874       C  
ATOM   1182  OG  SER A 146      87.797  82.549  58.358  1.00139.67           O  
ANISOU 1182  OG  SER A 146    16224  13923  22923   -297    780  -1952       O  
ATOM   1183  N   ASP A 147      90.829  81.867  58.871  1.00138.58           N  
ANISOU 1183  N   ASP A 147    16532  14161  21960   -471    903  -1463       N  
ATOM   1184  CA  ASP A 147      91.510  81.120  59.923  1.00137.48           C  
ANISOU 1184  CA  ASP A 147    16516  14214  21504   -634   1119  -1482       C  
ATOM   1185  C   ASP A 147      92.952  81.573  60.140  1.00133.10           C  
ANISOU 1185  C   ASP A 147    16104  13732  20734   -695   1111  -1268       C  
ATOM   1186  O   ASP A 147      93.502  81.412  61.230  1.00130.20           O  
ANISOU 1186  O   ASP A 147    15806  13471  20191   -855   1285  -1327       O  
ATOM   1187  CB  ASP A 147      91.475  79.619  59.619  1.00139.92           C  
ANISOU 1187  CB  ASP A 147    16922  14691  21550   -625   1157  -1391       C  
ATOM   1188  CG  ASP A 147      90.085  79.028  59.761  1.00144.16           C  
ANISOU 1188  CG  ASP A 147    17330  15195  22249   -620   1230  -1645       C  
ATOM   1189  OD1 ASP A 147      89.161  79.766  60.164  1.00147.65           O  
ANISOU 1189  OD1 ASP A 147    17601  15492  23009   -630   1267  -1907       O  
ATOM   1190  OD2 ASP A 147      89.918  77.823  59.473  1.00141.86           O1-
ANISOU 1190  OD2 ASP A 147    17105  15022  21775   -607   1254  -1589       O1-
ATOM   1191  N   PHE A 148      93.560  82.145  59.107  1.00129.91           N  
ANISOU 1191  N   PHE A 148    15747  13273  20342   -581    907  -1019       N  
ATOM   1192  CA  PHE A 148      94.979  82.482  59.164  1.00125.16           C  
ANISOU 1192  CA  PHE A 148    15285  12755  19513   -630    885   -788       C  
ATOM   1193  C   PHE A 148      95.265  83.976  59.273  1.00126.67           C  
ANISOU 1193  C   PHE A 148    15426  12791  19912   -635    807   -796       C  
ATOM   1194  O   PHE A 148      96.375  84.369  59.630  1.00129.35           O  
ANISOU 1194  O   PHE A 148    15866  13195  20087   -712    832   -666       O  
ATOM   1195  CB  PHE A 148      95.713  81.911  57.951  1.00120.59           C  
ANISOU 1195  CB  PHE A 148    14830  12272  18717   -528    733   -470       C  
ATOM   1196  CG  PHE A 148      95.728  80.414  57.904  1.00115.16           C  
ANISOU 1196  CG  PHE A 148    14222  11756  17778   -536    820   -428       C  
ATOM   1197  CD1 PHE A 148      94.832  79.724  57.106  1.00113.66           C  
ANISOU 1197  CD1 PHE A 148    13986  11547  17654   -435    751   -452       C  
ATOM   1198  CD2 PHE A 148      96.638  79.695  58.660  1.00109.89           C  
ANISOU 1198  CD2 PHE A 148    13675  11262  16817   -650    963   -361       C  
ATOM   1199  CE1 PHE A 148      94.844  78.347  57.061  1.00111.84           C  
ANISOU 1199  CE1 PHE A 148    13831  11464  17198   -444    831   -417       C  
ATOM   1200  CE2 PHE A 148      96.655  78.317  58.619  1.00108.51           C  
ANISOU 1200  CE2 PHE A 148    13572  11228  16430   -656   1033   -319       C  
ATOM   1201  CZ  PHE A 148      95.757  77.642  57.818  1.00111.76           C  
ANISOU 1201  CZ  PHE A 148    13939  11617  16908   -552    971   -351       C  
ATOM   1202  N   LEU A 149      94.277  84.809  58.965  1.00122.66           N  
ANISOU 1202  N   LEU A 149    14761  12073  19773   -554    707   -946       N  
ATOM   1203  CA  LEU A 149      94.503  86.252  58.951  1.00116.54           C  
ANISOU 1203  CA  LEU A 149    13932  11123  19225   -543    605   -943       C  
ATOM   1204  C   LEU A 149      94.925  86.793  60.318  1.00111.52           C  
ANISOU 1204  C   LEU A 149    13300  10505  18569   -709    802  -1110       C  
ATOM   1205  O   LEU A 149      95.304  87.956  60.445  1.00111.78           O  
ANISOU 1205  O   LEU A 149    13314  10416  18742   -725    744  -1100       O  
ATOM   1206  CB  LEU A 149      93.285  87.005  58.399  1.00114.62           C  
ANISOU 1206  CB  LEU A 149    13501  10633  19416   -422    454  -1088       C  
ATOM   1207  CG  LEU A 149      91.891  86.663  58.925  1.00118.56           C  
ANISOU 1207  CG  LEU A 149    13826  11062  20158   -424    577  -1424       C  
ATOM   1208  CD1 LEU A 149      91.718  87.136  60.359  1.00126.11           C  
ANISOU 1208  CD1 LEU A 149    14706  11990  21219   -575    811  -1730       C  
ATOM   1209  CD2 LEU A 149      90.831  87.279  58.026  1.00116.79           C  
ANISOU 1209  CD2 LEU A 149    13434  10604  20336   -270    360  -1473       C  
ATOM   1210  N   SER A 150      94.867  85.938  61.334  1.00110.67           N  
ANISOU 1210  N   SER A 150    13224  10548  18278   -844   1029  -1259       N  
ATOM   1211  CA  SER A 150      95.333  86.300  62.666  1.00112.92           C  
ANISOU 1211  CA  SER A 150    13537  10884  18482  -1033   1226  -1402       C  
ATOM   1212  C   SER A 150      96.854  86.227  62.737  1.00109.63           C  
ANISOU 1212  C   SER A 150    13306  10622  17727  -1102   1213  -1120       C  
ATOM   1213  O   SER A 150      97.485  86.955  63.504  1.00104.44           O  
ANISOU 1213  O   SER A 150    12681   9962  17040  -1225   1287  -1150       O  
ATOM   1214  CB  SER A 150      94.708  85.384  63.720  1.00119.50           C  
ANISOU 1214  CB  SER A 150    14347  11830  19226  -1176   1464  -1654       C  
ATOM   1215  OG  SER A 150      94.900  84.020  63.389  1.00124.76           O  
ANISOU 1215  OG  SER A 150    15119  12673  19611  -1156   1470  -1501       O  
ATOM   1216  N   ASN A 151      97.436  85.341  61.934  1.00114.86           N  
ANISOU 1216  N   ASN A 151    14082  11418  18141  -1025   1123   -853       N  
ATOM   1217  CA  ASN A 151      98.887  85.201  61.860  1.00121.11           C  
ANISOU 1217  CA  ASN A 151    15036  12357  18624  -1069   1095   -572       C  
ATOM   1218  C   ASN A 151      99.504  86.089  60.783  1.00115.20           C  
ANISOU 1218  C   ASN A 151    14314  11521  17937   -954    878   -334       C  
ATOM   1219  O   ASN A 151     100.726  86.162  60.655  1.00110.45           O  
ANISOU 1219  O   ASN A 151    13832  11023  17112   -987    842   -104       O  
ATOM   1220  CB  ASN A 151      99.282  83.742  61.615  1.00131.29           C  
ANISOU 1220  CB  ASN A 151    16434  13844  19608  -1059   1128   -416       C  
ATOM   1221  CG  ASN A 151      99.349  82.931  62.895  1.00148.20           C  
ANISOU 1221  CG  ASN A 151    18622  16127  21561  -1237   1343   -547       C  
ATOM   1222  ND2 ASN A 151      99.774  81.675  62.778  1.00166.22           N  
ANISOU 1222  ND2 ASN A 151    21002  18572  23580  -1240   1370   -406       N  
ATOM   1223  OD1 ASN A 151      99.024  83.424  63.975  1.00147.15           O  
ANISOU 1223  OD1 ASN A 151    18438  15953  21517  -1379   1481   -773       O  
ATOM   1224  N   MET A 152      98.657  86.759  60.008  1.00110.11           N  
ANISOU 1224  N   MET A 152    13557  10684  17596   -828    726   -388       N  
ATOM   1225  CA  MET A 152      99.139  87.624  58.937  1.00104.03           C  
ANISOU 1225  CA  MET A 152    12812   9817  16898   -730    499   -163       C  
ATOM   1226  C   MET A 152      99.876  88.837  59.481  1.00117.39           C  
ANISOU 1226  C   MET A 152    14525  11440  18639   -818    501   -148       C  
ATOM   1227  O   MET A 152      99.285  89.685  60.147  1.00128.54           O  
ANISOU 1227  O   MET A 152    15827  12695  20316   -860    554   -380       O  
ATOM   1228  CB  MET A 152      97.990  88.086  58.042  1.00 90.46           C  
ANISOU 1228  CB  MET A 152    10962   7891  15518   -587    321   -230       C  
ATOM   1229  CG  MET A 152      97.490  87.034  57.078  1.00 75.40           C  
ANISOU 1229  CG  MET A 152     9064   6048  13536   -479    241   -142       C  
ATOM   1230  SD  MET A 152      96.847  87.772  55.568  1.00128.31           S  
ANISOU 1230  SD  MET A 152    15693  12541  20516   -319    -75    -16       S  
ATOM   1231  CE  MET A 152      95.927  89.156  56.235  1.00102.31           C  
ANISOU 1231  CE  MET A 152    12210   8967  17697   -320    -89   -298       C  
ATOM   1232  N   SER A 153     101.169  88.915  59.191  1.00120.41           N  
ANISOU 1232  N   SER A 153    15043  11939  18769   -848    448    117       N  
ATOM   1233  CA  SER A 153     101.961  90.084  59.551  1.00125.47           C  
ANISOU 1233  CA  SER A 153    15716  12518  19438   -926    423    171       C  
ATOM   1234  C   SER A 153     102.566  90.690  58.294  1.00115.20           C  
ANISOU 1234  C   SER A 153    14475  11168  18128   -837    185    452       C  
ATOM   1235  O   SER A 153     103.435  90.092  57.662  1.00101.81           O  
ANISOU 1235  O   SER A 153    12892   9633  16157   -821    139    698       O  
ATOM   1236  CB  SER A 153     103.063  89.714  60.544  1.00135.55           C  
ANISOU 1236  CB  SER A 153    17104  13991  20408  -1084    594    222       C  
ATOM   1237  OG  SER A 153     104.031  88.871  59.945  1.00139.96           O  
ANISOU 1237  OG  SER A 153    17785  14741  20653  -1059    555    492       O  
ATOM   1238  N   MET A 154     102.098  91.878  57.929  1.00121.84           N  
ANISOU 1238  N   MET A 154    15236  11782  19276   -786     34    412       N  
ATOM   1239  CA  MET A 154     102.572  92.523  56.712  1.00124.17           C  
ANISOU 1239  CA  MET A 154    15587  12011  19582   -716   -211    675       C  
ATOM   1240  C   MET A 154     102.325  94.026  56.698  1.00128.66           C  
ANISOU 1240  C   MET A 154    16083  12327  20474   -711   -346    622       C  
ATOM   1241  O   MET A 154     101.182  94.482  56.736  1.00133.97           O  
ANISOU 1241  O   MET A 154    16613  12790  21500   -647   -397    422       O  
ATOM   1242  CB  MET A 154     101.931  91.873  55.487  1.00114.80           C  
ANISOU 1242  CB  MET A 154    14385  10817  18418   -586   -364    774       C  
ATOM   1243  CG  MET A 154     100.444  91.628  55.625  1.00103.70           C  
ANISOU 1243  CG  MET A 154    12825   9275  17303   -510   -345    518       C  
ATOM   1244  SD  MET A 154      99.783  90.808  54.167  1.00123.68           S  
ANISOU 1244  SD  MET A 154    15354  11818  19819   -374   -528    657       S  
ATOM   1245  CE  MET A 154     100.029  92.080  52.934  1.00195.68           C  
ANISOU 1245  CE  MET A 154    24499  20757  29094   -326   -855    899       C  
ATOM   1246  N   ASP A 155     103.411  94.788  56.641  1.00128.62           N  
ANISOU 1246  N   ASP A 155    16175  12339  20357   -780   -407    800       N  
ATOM   1247  CA  ASP A 155     103.331  96.238  56.536  1.00139.86           C  
ANISOU 1247  CA  ASP A 155    17552  13525  22062   -780   -557    792       C  
ATOM   1248  C   ASP A 155     104.201  96.731  55.385  1.00138.57           C  
ANISOU 1248  C   ASP A 155    17505  13372  21771   -768   -785   1126       C  
ATOM   1249  O   ASP A 155     105.310  96.238  55.175  1.00136.38           O  
ANISOU 1249  O   ASP A 155    17361  13314  21144   -823   -748   1334       O  
ATOM   1250  CB  ASP A 155     103.752  96.902  57.849  1.00147.29           C  
ANISOU 1250  CB  ASP A 155    18487  14448  23030   -913   -381    628       C  
ATOM   1251  CG  ASP A 155     105.186  96.587  58.230  1.00149.48           C  
ANISOU 1251  CG  ASP A 155    18916  14967  22911  -1035   -272    808       C  
ATOM   1252  OD1 ASP A 155     105.754  97.326  59.061  1.00153.32           O  
ANISOU 1252  OD1 ASP A 155    19427  15435  23395  -1151   -189    754       O  
ATOM   1253  OD2 ASP A 155     105.747  95.604  57.700  1.00146.65           O1-
ANISOU 1253  OD2 ASP A 155    18650  14815  22254  -1016   -271    999       O1-
ATOM   1254  N   PHE A 156     103.689  97.702  54.638  1.00135.77           N  
ANISOU 1254  N   PHE A 156    17097  12778  21710   -702  -1026   1173       N  
ATOM   1255  CA  PHE A 156     104.396  98.234  53.482  1.00131.63           C  
ANISOU 1255  CA  PHE A 156    16683  12245  21087   -703  -1267   1486       C  
ATOM   1256  C   PHE A 156     104.949  99.622  53.775  1.00140.64           C  
ANISOU 1256  C   PHE A 156    17846  13235  22358   -777  -1346   1524       C  
ATOM   1257  O   PHE A 156     104.231 100.493  54.267  1.00146.68           O  
ANISOU 1257  O   PHE A 156    18491  13755  23484   -758  -1372   1327       O  
ATOM   1258  CB  PHE A 156     103.464  98.293  52.272  1.00123.64           C  
ANISOU 1258  CB  PHE A 156    15617  11076  20285   -588  -1523   1563       C  
ATOM   1259  CG  PHE A 156     102.839  96.973  51.922  1.00115.13           C  
ANISOU 1259  CG  PHE A 156    14514  10128  19101   -514  -1461   1521       C  
ATOM   1260  CD1 PHE A 156     101.799  96.460  52.677  1.00109.11           C  
ANISOU 1260  CD1 PHE A 156    13615   9321  18522   -463  -1305   1229       C  
ATOM   1261  CD2 PHE A 156     103.288  96.248  50.831  1.00114.09           C  
ANISOU 1261  CD2 PHE A 156    14496  10166  18688   -503  -1554   1767       C  
ATOM   1262  CE1 PHE A 156     101.224  95.247  52.355  1.00106.61           C  
ANISOU 1262  CE1 PHE A 156    13279   9121  18106   -399  -1251   1193       C  
ATOM   1263  CE2 PHE A 156     102.715  95.034  50.504  1.00105.90           C  
ANISOU 1263  CE2 PHE A 156    13438   9243  17556   -438  -1495   1724       C  
ATOM   1264  CZ  PHE A 156     101.682  94.534  51.266  1.00103.44           C  
ANISOU 1264  CZ  PHE A 156    12993   8881  17427   -384  -1348   1442       C  
ATOM   1265  N   GLN A 157     106.226  99.827  53.470  1.00142.89           N  
ANISOU 1265  N   GLN A 157    18277  13662  22354   -865  -1380   1772       N  
ATOM   1266  CA  GLN A 157     106.853 101.124  53.683  1.00149.45           C  
ANISOU 1266  CA  GLN A 157    19147  14366  23272   -947  -1463   1837       C  
ATOM   1267  C   GLN A 157     107.258 101.773  52.364  1.00156.14           C  
ANISOU 1267  C   GLN A 157    20085  15145  24095   -948  -1758   2138       C  
ATOM   1268  O   GLN A 157     108.198 101.332  51.704  1.00151.87           O  
ANISOU 1268  O   GLN A 157    19675  14814  23214   -997  -1785   2381       O  
ATOM   1269  CB  GLN A 157     108.058 100.999  54.615  1.00151.45           C  
ANISOU 1269  CB  GLN A 157    19490  14829  23227  -1079  -1247   1854       C  
ATOM   1270  CG  GLN A 157     108.766 102.316  54.882  1.00157.65           C  
ANISOU 1270  CG  GLN A 157    20323  15499  24078  -1176  -1318   1920       C  
ATOM   1271  CD  GLN A 157     109.499 102.324  56.207  1.00159.72           C  
ANISOU 1271  CD  GLN A 157    20612  15888  24186  -1303  -1069   1803       C  
ATOM   1272  NE2 GLN A 157     108.853 101.798  57.243  1.00156.68           N  
ANISOU 1272  NE2 GLN A 157    20135  15518  23878  -1304   -853   1524       N  
ATOM   1273  OE1 GLN A 157     110.632 102.796  56.301  1.00162.33           O  
ANISOU 1273  OE1 GLN A 157    21047  16308  24324  -1409  -1073   1963       O  
ATOM   1274  N   ASN A 158     106.534 102.822  51.990  1.00170.49           N  
ANISOU 1274  N   ASN A 158    21830  16664  26284   -901  -1981   2115       N  
ATOM   1275  CA  ASN A 158     106.786 103.540  50.747  1.00185.42           C  
ANISOU 1275  CA  ASN A 158    23803  18452  28195   -914  -2292   2395       C  
ATOM   1276  C   ASN A 158     107.528 104.851  50.997  1.00195.19           C  
ANISOU 1276  C   ASN A 158    25099  19567  29498  -1013  -2375   2476       C  
ATOM   1277  O   ASN A 158     106.954 105.933  50.870  1.00199.88           O  
ANISOU 1277  O   ASN A 158    25624  19861  30458   -985  -2568   2439       O  
ATOM   1278  CB  ASN A 158     105.465 103.814  50.024  1.00193.63           C  
ANISOU 1278  CB  ASN A 158    24729  19228  29613   -796  -2533   2353       C  
ATOM   1279  CG  ASN A 158     105.664 104.434  48.655  1.00198.77           C  
ANISOU 1279  CG  ASN A 158    25476  19785  30261   -823  -2874   2662       C  
ATOM   1280  ND2 ASN A 158     104.708 105.256  48.232  1.00198.40           N  
ANISOU 1280  ND2 ASN A 158    25332  19422  30629   -755  -3132   2639       N  
ATOM   1281  OD1 ASN A 158     106.661 104.173  47.983  1.00200.28           O  
ANISOU 1281  OD1 ASN A 158    25825  20185  30087   -911  -2909   2917       O  
ATOM   1282  N   HIS A 159     108.805 104.749  51.354  1.00196.67           N  
ANISOU 1282  N   HIS A 159    25407  19978  29341  -1129  -2233   2587       N  
ATOM   1283  CA  HIS A 159     109.609 105.929  51.659  1.00198.25           C  
ANISOU 1283  CA  HIS A 159    25672  20093  29562  -1238  -2286   2665       C  
ATOM   1284  C   HIS A 159     110.345 106.428  50.416  1.00194.04           C  
ANISOU 1284  C   HIS A 159    25281  19580  28867  -1308  -2544   3009       C  
ATOM   1285  O   HIS A 159     111.333 107.155  50.515  1.00193.63           O  
ANISOU 1285  O   HIS A 159    25325  19556  28689  -1424  -2569   3141       O  
ATOM   1286  CB  HIS A 159     110.600 105.629  52.788  1.00201.36           C  
ANISOU 1286  CB  HIS A 159    26114  20710  29684  -1342  -1998   2594       C  
ATOM   1287  CG  HIS A 159     110.973 106.829  53.604  1.00207.84           C  
ANISOU 1287  CG  HIS A 159    26934  21380  30657  -1433  -1976   2514       C  
ATOM   1288  CD2 HIS A 159     110.409 107.363  54.713  1.00210.44           C  
ANISOU 1288  CD2 HIS A 159    27152  21534  31271  -1434  -1853   2226       C  
ATOM   1289  ND1 HIS A 159     112.056 107.627  53.303  1.00209.82           N  
ANISOU 1289  ND1 HIS A 159    27309  21656  30757  -1549  -2083   2738       N  
ATOM   1290  CE1 HIS A 159     112.141 108.603  54.191  1.00210.75           C  
ANISOU 1290  CE1 HIS A 159    27396  21616  31062  -1612  -2031   2597       C  
ATOM   1291  NE2 HIS A 159     111.154 108.465  55.057  1.00211.40           N  
ANISOU 1291  NE2 HIS A 159    27336  21574  31412  -1546  -1888   2282       N  
ATOM   1292  N   LEU A 160     109.855 106.027  49.246  1.00188.93           N  
ANISOU 1292  N   LEU A 160    24648  18923  28213  -1249  -2735   3150       N  
ATOM   1293  CA  LEU A 160     110.409 106.485  47.976  1.00182.11           C  
ANISOU 1293  CA  LEU A 160    23918  18067  27207  -1328  -3000   3472       C  
ATOM   1294  C   LEU A 160     109.364 107.299  47.217  1.00178.86           C  
ANISOU 1294  C   LEU A 160    23449  17325  27184  -1267  -3329   3513       C  
ATOM   1295  O   LEU A 160     109.380 108.529  47.261  1.00180.73           O  
ANISOU 1295  O   LEU A 160    23688  17323  27660  -1307  -3500   3550       O  
ATOM   1296  CB  LEU A 160     110.889 105.300  47.137  1.00179.75           C  
ANISOU 1296  CB  LEU A 160    23714  18071  26512  -1348  -2955   3641       C  
ATOM   1297  CG  LEU A 160     111.923 104.400  47.817  1.00176.07           C  
ANISOU 1297  CG  LEU A 160    23295  17931  25672  -1399  -2646   3613       C  
ATOM   1298  CD1 LEU A 160     112.381 103.293  46.880  1.00174.09           C  
ANISOU 1298  CD1 LEU A 160    23130  17952  25063  -1416  -2622   3782       C  
ATOM   1299  CD2 LEU A 160     113.109 105.220  48.304  1.00175.16           C  
ANISOU 1299  CD2 LEU A 160    23263  17863  25427  -1532  -2601   3702       C  
ATOM   1300  N   GLY A 161     108.460 106.614  46.522  1.00175.25           N  
ANISOU 1300  N   GLY A 161    22939  16849  26797  -1173  -3424   3510       N  
ATOM   1301  CA  GLY A 161     107.310 107.274  45.927  1.00174.80           C  
ANISOU 1301  CA  GLY A 161    22795  16468  27154  -1096  -3724   3511       C  
ATOM   1302  C   GLY A 161     107.140 107.148  44.424  1.00172.17           C  
ANISOU 1302  C   GLY A 161    22553  16139  26727  -1128  -4021   3787       C  
ATOM   1303  O   GLY A 161     106.278 107.806  43.841  1.00171.60           O  
ANISOU 1303  O   GLY A 161    22423  15784  26992  -1085  -4316   3835       O  
ATOM   1304  N   SER A 162     107.945 106.302  43.790  1.00169.50           N  
ANISOU 1304  N   SER A 162    22352  16114  25938  -1210  -3947   3966       N  
ATOM   1305  CA  SER A 162     107.872 106.130  42.341  1.00168.92           C  
ANISOU 1305  CA  SER A 162    22382  16079  25719  -1273  -4208   4231       C  
ATOM   1306  C   SER A 162     106.629 105.350  41.917  1.00167.54           C  
ANISOU 1306  C   SER A 162    22105  15848  25705  -1149  -4271   4139       C  
ATOM   1307  O   SER A 162     106.530 104.898  40.776  1.00166.51           O  
ANISOU 1307  O   SER A 162    22058  15808  25402  -1197  -4428   4325       O  
ATOM   1308  CB  SER A 162     109.132 105.438  41.817  1.00169.59           C  
ANISOU 1308  CB  SER A 162    22636  16526  25275  -1405  -4082   4424       C  
ATOM   1309  OG  SER A 162     109.277 104.144  42.378  1.00169.22           O  
ANISOU 1309  OG  SER A 162    22550  16736  25011  -1339  -3757   4262       O  
ATOM   1310  N   CYS A 163     105.681 105.201  42.837  1.00168.24           N  
ANISOU 1310  N   CYS A 163    22013  15791  26118  -1000  -4146   3845       N  
ATOM   1311  CA  CYS A 163     104.463 104.441  42.573  1.00168.25           C  
ANISOU 1311  CA  CYS A 163    21896  15739  26291   -875  -4178   3723       C  
ATOM   1312  C   CYS A 163     103.378 105.294  41.924  1.00168.44           C  
ANISOU 1312  C   CYS A 163    21836  15412  26750   -826  -4548   3777       C  
ATOM   1313  O   CYS A 163     103.330 106.509  42.114  1.00168.88           O  
ANISOU 1313  O   CYS A 163    21861  15206  27101   -839  -4718   3793       O  
ATOM   1314  CB  CYS A 163     103.923 103.825  43.866  1.00166.81           C  
ANISOU 1314  CB  CYS A 163    21555  15577  26249   -750  -3861   3371       C  
ATOM   1315  SG  CYS A 163     104.971 102.550  44.592  1.00151.66           S  
ANISOU 1315  SG  CYS A 163    19714  14069  23839   -790  -3440   3297       S  
ATOM   1316  N   GLN A 164     102.508 104.642  41.159  1.00166.43           N  
ANISOU 1316  N   GLN A 164    21543  15150  26543   -769  -4676   3805       N  
ATOM   1317  CA  GLN A 164     101.364 105.306  40.549  1.00164.27           C  
ANISOU 1317  CA  GLN A 164    21168  14546  26699   -709  -5029   3845       C  
ATOM   1318  C   GLN A 164     100.126 105.055  41.399  1.00160.09           C  
ANISOU 1318  C   GLN A 164    20401  13848  26578   -529  -4911   3504       C  
ATOM   1319  O   GLN A 164     100.232 104.680  42.567  1.00161.17           O  
ANISOU 1319  O   GLN A 164    20460  14076  26702   -472  -4578   3242       O  
ATOM   1320  CB  GLN A 164     101.130 104.770  39.136  1.00165.96           C  
ANISOU 1320  CB  GLN A 164    21486  14851  26720   -774  -5265   4094       C  
ATOM   1321  CG  GLN A 164     102.397 104.594  38.316  1.00166.18           C  
ANISOU 1321  CG  GLN A 164    21753  15151  26236   -963  -5281   4388       C  
ATOM   1322  CD  GLN A 164     102.137 103.912  36.987  1.00164.18           C  
ANISOU 1322  CD  GLN A 164    21598  15021  25761  -1036  -5463   4594       C  
ATOM   1323  NE2 GLN A 164     103.191 103.378  36.379  1.00162.02           N  
ANISOU 1323  NE2 GLN A 164    21513  15055  24994  -1185  -5373   4776       N  
ATOM   1324  OE1 GLN A 164     101.002 103.865  36.512  1.00163.41           O  
ANISOU 1324  OE1 GLN A 164    21406  14744  25937   -966  -5679   4584       O  
ATOM   1325  N   LYS A 165      98.953 105.261  40.812  1.00156.34           N  
ANISOU 1325  N   LYS A 165    19810  13130  26462   -451  -5188   3509       N  
ATOM   1326  CA  LYS A 165      97.701 104.942  41.489  1.00155.08           C  
ANISOU 1326  CA  LYS A 165    19415  12820  26688   -284  -5090   3190       C  
ATOM   1327  C   LYS A 165      96.925 103.865  40.742  1.00151.74           C  
ANISOU 1327  C   LYS A 165    18969  12503  26183   -238  -5145   3216       C  
ATOM   1328  O   LYS A 165      97.293 103.476  39.633  1.00151.16           O  
ANISOU 1328  O   LYS A 165    19058  12584  25790   -338  -5297   3490       O  
ATOM   1329  CB  LYS A 165      96.835 106.190  41.670  1.00161.36           C  
ANISOU 1329  CB  LYS A 165    20034  13187  28090   -202  -5345   3099       C  
ATOM   1330  CG  LYS A 165      97.154 106.984  42.924  1.00167.46           C  
ANISOU 1330  CG  LYS A 165    20725  13835  29067   -181  -5152   2874       C  
ATOM   1331  CD  LYS A 165      96.011 107.915  43.292  1.00176.15           C  
ANISOU 1331  CD  LYS A 165    21585  14519  30825    -56  -5321   2669       C  
ATOM   1332  CE  LYS A 165      96.271 108.605  44.621  1.00179.69           C  
ANISOU 1332  CE  LYS A 165    21943  14861  31473    -39  -5082   2397       C  
ATOM   1333  NZ  LYS A 165      96.517 107.623  45.715  1.00178.58           N1+
ANISOU 1333  NZ  LYS A 165    21782  15003  31068    -30  -4622   2128       N1+
ATOM   1334  N   CYS A 166      95.851 103.386  41.359  1.00145.87           N  
ANISOU 1334  N   CYS A 166    18022  11680  25722    -96  -5013   2921       N  
ATOM   1335  CA  CYS A 166      95.025 102.347  40.762  1.00138.16           C  
ANISOU 1335  CA  CYS A 166    17003  10793  24698    -42  -5046   2909       C  
ATOM   1336  C   CYS A 166      93.951 102.961  39.877  1.00137.96           C  
ANISOU 1336  C   CYS A 166    16873  10457  25088      4  -5467   3017       C  
ATOM   1337  O   CYS A 166      93.410 104.020  40.189  1.00138.31           O  
ANISOU 1337  O   CYS A 166    16768  10171  25613     70  -5634   2929       O  
ATOM   1338  CB  CYS A 166      94.373 101.488  41.849  1.00136.91           C  
ANISOU 1338  CB  CYS A 166    16678  10710  24633     77  -4701   2539       C  
ATOM   1339  SG  CYS A 166      95.528 100.746  43.029  1.00148.80           S  
ANISOU 1339  SG  CYS A 166    18283  12556  25698     25  -4211   2388       S  
ATOM   1340  N   ASP A 167      93.651 102.291  38.769  1.00143.03           N  
ANISOU 1340  N   ASP A 167    17593  11203  25548    -36  -5640   3209       N  
ATOM   1341  CA  ASP A 167      92.585 102.721  37.875  1.00147.44           C  
ANISOU 1341  CA  ASP A 167    18056  11491  26472     -2  -6047   3325       C  
ATOM   1342  C   ASP A 167      91.304 102.931  38.675  1.00147.52           C  
ANISOU 1342  C   ASP A 167    17770  11232  27051    180  -6017   2991       C  
ATOM   1343  O   ASP A 167      90.934 102.085  39.489  1.00144.12           O  
ANISOU 1343  O   ASP A 167    17230  10929  26600    268  -5690   2701       O  
ATOM   1344  CB  ASP A 167      92.367 101.675  36.777  1.00149.35           C  
ANISOU 1344  CB  ASP A 167    18407  11941  26397    -63  -6138   3502       C  
ATOM   1345  CG  ASP A 167      91.469 102.172  35.661  1.00155.07           C  
ANISOU 1345  CG  ASP A 167    19088  12415  27418    -77  -6609   3706       C  
ATOM   1346  OD1 ASP A 167      91.883 102.083  34.485  1.00155.83           O  
ANISOU 1346  OD1 ASP A 167    19379  12619  27209   -232  -6835   4029       O  
ATOM   1347  OD2 ASP A 167      90.353 102.649  35.953  1.00159.22           O1-
ANISOU 1347  OD2 ASP A 167    19379  12634  28482     57  -6755   3544       O1-
ATOM   1348  N   PRO A 168      90.630 104.070  38.454  1.00150.50           N  
ANISOU 1348  N   PRO A 168    18011  11229  27944    230  -6359   3026       N  
ATOM   1349  CA  PRO A 168      89.405 104.440  39.174  1.00155.65           C  
ANISOU 1349  CA  PRO A 168    18359  11579  29201    401  -6363   2706       C  
ATOM   1350  C   PRO A 168      88.342 103.345  39.152  1.00165.61           C  
ANISOU 1350  C   PRO A 168    19477  12920  30525    499  -6265   2523       C  
ATOM   1351  O   PRO A 168      87.412 103.381  39.958  1.00170.03           O  
ANISOU 1351  O   PRO A 168    19784  13316  31502    636  -6145   2192       O  
ATOM   1352  CB  PRO A 168      88.909 105.664  38.403  1.00152.95           C  
ANISOU 1352  CB  PRO A 168    17953  10851  29311    403  -6860   2910       C  
ATOM   1353  CG  PRO A 168      90.141 106.265  37.834  1.00151.89           C  
ANISOU 1353  CG  PRO A 168    18080  10788  28842    235  -7005   3247       C  
ATOM   1354  CD  PRO A 168      91.046 105.114  37.501  1.00149.41           C  
ANISOU 1354  CD  PRO A 168    18004  10918  27846    115  -6768   3378       C  
ATOM   1355  N   SER A 169      88.479 102.388  38.241  1.00166.98           N  
ANISOU 1355  N   SER A 169    19810  13345  30291    420  -6310   2729       N  
ATOM   1356  CA  SER A 169      87.522 101.293  38.133  1.00164.10           C  
ANISOU 1356  CA  SER A 169    19333  13076  29941    497  -6226   2583       C  
ATOM   1357  C   SER A 169      87.767 100.227  39.197  1.00156.45           C  
ANISOU 1357  C   SER A 169    18354  12393  28697    535  -5725   2291       C  
ATOM   1358  O   SER A 169      86.843  99.524  39.606  1.00153.95           O  
ANISOU 1358  O   SER A 169    17868  12088  28537    634  -5578   2038       O  
ATOM   1359  CB  SER A 169      87.578 100.669  36.737  1.00167.24           C  
ANISOU 1359  CB  SER A 169    19913  13633  29999    386  -6465   2912       C  
ATOM   1360  OG  SER A 169      88.883 100.205  36.436  1.00168.76           O  
ANISOU 1360  OG  SER A 169    20381  14150  29589    239  -6312   3109       O  
ATOM   1361  N   CYS A 170      89.015 100.115  39.642  1.00153.44           N  
ANISOU 1361  N   CYS A 170    18152  12238  27909    447  -5474   2331       N  
ATOM   1362  CA  CYS A 170      89.391  99.121  40.642  1.00147.65           C  
ANISOU 1362  CA  CYS A 170    17436  11785  26879    461  -5014   2091       C  
ATOM   1363  C   CYS A 170      88.517  99.213  41.888  1.00152.36           C  
ANISOU 1363  C   CYS A 170    17770  12229  27889    589  -4796   1679       C  
ATOM   1364  O   CYS A 170      88.304 100.299  42.426  1.00155.75           O  
ANISOU 1364  O   CYS A 170    18064  12389  28726    635  -4863   1556       O  
ATOM   1365  CB  CYS A 170      90.865  99.274  41.021  1.00142.02           C  
ANISOU 1365  CB  CYS A 170    16925  11270  25764    352  -4820   2195       C  
ATOM   1366  SG  CYS A 170      92.010  99.102  39.635  1.00153.62           S  
ANISOU 1366  SG  CYS A 170    18706  12960  26703    180  -5016   2649       S  
ATOM   1367  N   PRO A 171      88.004  98.062  42.347  1.00154.35           N  
ANISOU 1367  N   PRO A 171    17952  12656  28036    637  -4529   1458       N  
ATOM   1368  CA  PRO A 171      87.136  97.982  43.526  1.00157.85           C  
ANISOU 1368  CA  PRO A 171    18152  12997  28825    738  -4289   1048       C  
ATOM   1369  C   PRO A 171      87.858  98.414  44.796  1.00158.37           C  
ANISOU 1369  C   PRO A 171    18222  13094  28858    705  -3988    854       C  
ATOM   1370  O   PRO A 171      88.775  97.727  45.247  1.00151.43           O  
ANISOU 1370  O   PRO A 171    17504  12504  27529    628  -3708    863       O  
ATOM   1371  CB  PRO A 171      86.791  96.491  43.606  1.00157.09           C  
ANISOU 1371  CB  PRO A 171    18072  13170  28444    747  -4054    937       C  
ATOM   1372  CG  PRO A 171      87.032  95.963  42.232  1.00156.72           C  
ANISOU 1372  CG  PRO A 171    18206  13257  28083    688  -4287   1282       C  
ATOM   1373  CD  PRO A 171      88.188  96.750  41.708  1.00154.79           C  
ANISOU 1373  CD  PRO A 171    18159  13015  27638    588  -4452   1587       C  
ATOM   1374  N   ASN A 172      87.442  99.543  45.361  1.00163.98           N  
ANISOU 1374  N   ASN A 172    18753  13503  30048    760  -4053    679       N  
ATOM   1375  CA  ASN A 172      88.029 100.050  46.597  1.00165.31           C  
ANISOU 1375  CA  ASN A 172    18906  13671  30233    723  -3777    470       C  
ATOM   1376  C   ASN A 172      89.526 100.320  46.480  1.00149.91           C  
ANISOU 1376  C   ASN A 172    17214  11886  27858    601  -3753    733       C  
ATOM   1377  O   ASN A 172      90.280 100.114  47.431  1.00144.21           O  
ANISOU 1377  O   ASN A 172    16566  11341  26887    535  -3439    614       O  
ATOM   1378  CB  ASN A 172      87.746  99.093  47.756  1.00180.50           C  
ANISOU 1378  CB  ASN A 172    20751  15787  32043    724  -3355    124       C  
ATOM   1379  CG  ASN A 172      86.281  99.064  48.140  1.00201.40           C  
ANISOU 1379  CG  ASN A 172    23106  18234  35181    834  -3336   -208       C  
ATOM   1380  ND2 ASN A 172      85.774  97.879  48.459  1.00221.06           N  
ANISOU 1380  ND2 ASN A 172    25556  20919  37517    844  -3109   -381       N  
ATOM   1381  OD1 ASN A 172      85.612 100.097  48.151  1.00202.03           O  
ANISOU 1381  OD1 ASN A 172    22994  17984  35785    909  -3524   -313       O  
ATOM   1382  N   GLY A 173      89.946 100.781  45.307  1.00143.86           N  
ANISOU 1382  N   GLY A 173    16587  11065  27010    562  -4090   1093       N  
ATOM   1383  CA  GLY A 173      91.331 101.151  45.079  1.00139.21           C  
ANISOU 1383  CA  GLY A 173    16233  10608  26053    442  -4108   1359       C  
ATOM   1384  C   GLY A 173      92.314 100.015  45.283  1.00133.38           C  
ANISOU 1384  C   GLY A 173    15690  10268  24721    356  -3811   1421       C  
ATOM   1385  O   GLY A 173      93.458 100.237  45.680  1.00133.50           O  
ANISOU 1385  O   GLY A 173    15847  10416  24460    266  -3674   1497       O  
ATOM   1386  N   SER A 174      91.868  98.793  45.011  1.00127.90           N  
ANISOU 1386  N   SER A 174    14998   9759  23841    385  -3717   1387       N  
ATOM   1387  CA  SER A 174      92.728  97.623  45.130  1.00119.28           C  
ANISOU 1387  CA  SER A 174    14081   9034  22208    314  -3453   1448       C  
ATOM   1388  C   SER A 174      93.322  97.254  43.777  1.00109.73           C  
ANISOU 1388  C   SER A 174    13074   7977  20643    242  -3657   1812       C  
ATOM   1389  O   SER A 174      92.596  96.923  42.840  1.00106.17           O  
ANISOU 1389  O   SER A 174    12599   7482  20260    274  -3868   1910       O  
ATOM   1390  CB  SER A 174      91.942  96.437  45.692  1.00124.79           C  
ANISOU 1390  CB  SER A 174    14670   9857  22887    375  -3202   1184       C  
ATOM   1391  OG  SER A 174      91.412  96.732  46.972  1.00129.83           O  
ANISOU 1391  OG  SER A 174    15126  10376  23826    418  -2988    832       O  
ATOM   1392  N   CYS A 175      94.645  97.313  43.676  1.00107.85           N  
ANISOU 1392  N   CYS A 175    13032   7922  20023    134  -3592   2007       N  
ATOM   1393  CA  CYS A 175      95.323  96.978  42.430  1.00108.08           C  
ANISOU 1393  CA  CYS A 175    13261   8118  19686     43  -3754   2339       C  
ATOM   1394  C   CYS A 175      96.722  96.436  42.686  1.00103.70           C  
ANISOU 1394  C   CYS A 175    12890   7872  18639    -55  -3508   2433       C  
ATOM   1395  O   CYS A 175      97.413  96.879  43.604  1.00103.04           O  
ANISOU 1395  O   CYS A 175    12816   7805  18529    -85  -3337   2352       O  
ATOM   1396  CB  CYS A 175      95.405  98.202  41.518  1.00108.01           C  
ANISOU 1396  CB  CYS A 175    13298   7887  19853     -9  -4140   2594       C  
ATOM   1397  SG  CYS A 175      96.661  99.401  42.015  1.00170.74           S  
ANISOU 1397  SG  CYS A 175    21343  15788  27743   -103  -4124   2692       S  
ATOM   1398  N   TRP A 176      97.136  95.479  41.863  1.00 98.29           N  
ANISOU 1398  N   TRP A 176    12345   7428  17573   -110  -3493   2601       N  
ATOM   1399  CA  TRP A 176      98.465  94.896  41.972  1.00 99.24           C  
ANISOU 1399  CA  TRP A 176    12633   7844  17230   -200  -3277   2704       C  
ATOM   1400  C   TRP A 176      99.465  95.659  41.116  1.00107.05           C  
ANISOU 1400  C   TRP A 176    13786   8854  18033   -327  -3476   3010       C  
ATOM   1401  O   TRP A 176     100.661  95.366  41.128  1.00112.58           O  
ANISOU 1401  O   TRP A 176    14624   9781  18368   -415  -3329   3119       O  
ATOM   1402  CB  TRP A 176      98.434  93.426  41.559  1.00 98.26           C  
ANISOU 1402  CB  TRP A 176    12568   7972  16793   -195  -3133   2707       C  
ATOM   1403  CG  TRP A 176      97.646  92.570  42.494  1.00100.60           C  
ANISOU 1403  CG  TRP A 176    12729   8293  17202    -93  -2894   2412       C  
ATOM   1404  CD1 TRP A 176      96.294  92.389  42.497  1.00101.73           C  
ANISOU 1404  CD1 TRP A 176    12717   8281  17655      4  -2967   2249       C  
ATOM   1405  CD2 TRP A 176      98.160  91.782  43.572  1.00 99.25           C  
ANISOU 1405  CD2 TRP A 176    12563   8312  16834    -88  -2549   2247       C  
ATOM   1406  CE2 TRP A 176      97.063  91.145  44.184  1.00 98.82           C  
ANISOU 1406  CE2 TRP A 176    12363   8212  16972      4  -2425   1987       C  
ATOM   1407  CE3 TRP A 176      99.442  91.549  44.078  1.00100.95           C  
ANISOU 1407  CE3 TRP A 176    12892   8732  16734   -160  -2342   2299       C  
ATOM   1408  NE1 TRP A 176      95.935  91.533  43.509  1.00 99.93           N  
ANISOU 1408  NE1 TRP A 176    12402   8142  17423     62  -2679   1987       N  
ATOM   1409  CZ2 TRP A 176      97.208  90.293  45.276  1.00100.55           C  
ANISOU 1409  CZ2 TRP A 176    12557   8581  17065     15  -2107   1785       C  
ATOM   1410  CZ3 TRP A 176      99.584  90.703  45.162  1.00102.15           C  
ANISOU 1410  CZ3 TRP A 176    13013   9025  16774   -141  -2036   2104       C  
ATOM   1411  CH2 TRP A 176      98.474  90.086  45.749  1.00101.10           C  
ANISOU 1411  CH2 TRP A 176    12746   8843  16826    -59  -1923   1854       C  
ATOM   1412  N   GLY A 177      98.965  96.642  40.374  1.00105.35           N  
ANISOU 1412  N   GLY A 177    13552   8399  18077   -342  -3817   3147       N  
ATOM   1413  CA  GLY A 177      99.800  97.444  39.501  1.00105.23           C  
ANISOU 1413  CA  GLY A 177    13693   8378  17911   -477  -4044   3446       C  
ATOM   1414  C   GLY A 177      98.970  98.416  38.689  1.00113.92           C  
ANISOU 1414  C   GLY A 177    14748   9181  19356   -479  -4447   3578       C  
ATOM   1415  O   GLY A 177      97.765  98.544  38.905  1.00121.02           O  
ANISOU 1415  O   GLY A 177    15474   9861  20646   -362  -4540   3418       O  
ATOM   1416  N   ALA A 178      99.612  99.102  37.749  1.00113.36           N  
ANISOU 1416  N   ALA A 178    14828   9099  19144   -620  -4694   3871       N  
ATOM   1417  CA  ALA A 178      98.923 100.080  36.916  1.00116.15           C  
ANISOU 1417  CA  ALA A 178    15159   9166  19805   -646  -5111   4038       C  
ATOM   1418  C   ALA A 178      97.995  99.402  35.916  1.00118.84           C  
ANISOU 1418  C   ALA A 178    15489   9509  20154   -639  -5295   4109       C  
ATOM   1419  O   ALA A 178      97.953  98.176  35.822  1.00119.77           O  
ANISOU 1419  O   ALA A 178    15630   9863  20013   -621  -5092   4037       O  
ATOM   1420  CB  ALA A 178      99.926 100.962  36.193  1.00122.67           C  
ANISOU 1420  CB  ALA A 178    16170  10000  20441   -824  -5318   4342       C  
ATOM   1421  N   GLY A 179      97.252 100.209  35.169  1.00126.16           N  
ANISOU 1421  N   GLY A 179    16381  10168  21386   -657  -5689   4256       N  
ATOM   1422  CA  GLY A 179      96.331  99.686  34.180  1.00137.70           C  
ANISOU 1422  CA  GLY A 179    17830  11605  22884   -664  -5908   4345       C  
ATOM   1423  C   GLY A 179      95.031  99.216  34.799  1.00145.98           C  
ANISOU 1423  C   GLY A 179    18646  12520  24299   -472  -5830   4057       C  
ATOM   1424  O   GLY A 179      94.925  99.079  36.019  1.00144.33           O  
ANISOU 1424  O   GLY A 179    18302  12298  24238   -345  -5545   3772       O  
ATOM   1425  N   GLU A 180      94.039  98.967  33.950  1.00151.82           N  
ANISOU 1425  N   GLU A 180    19341  13166  25178   -465  -6085   4133       N  
ATOM   1426  CA  GLU A 180      92.722  98.536  34.401  1.00149.78           C  
ANISOU 1426  CA  GLU A 180    18855  12771  25283   -294  -6051   3877       C  
ATOM   1427  C   GLU A 180      92.682  97.027  34.625  1.00139.51           C  
ANISOU 1427  C   GLU A 180    17568  11771  23667   -256  -5712   3716       C  
ATOM   1428  O   GLU A 180      91.752  96.503  35.238  1.00133.13           O  
ANISOU 1428  O   GLU A 180    16580  10912  23092   -114  -5578   3456       O  
ATOM   1429  CB  GLU A 180      91.661  98.947  33.379  1.00155.58           C  
ANISOU 1429  CB  GLU A 180    19529  13265  26322   -306  -6494   4040       C  
ATOM   1430  CG  GLU A 180      90.240  98.581  33.760  1.00162.80           C  
ANISOU 1430  CG  GLU A 180    20192  14014  27649   -133  -6498   3788       C  
ATOM   1431  CD  GLU A 180      89.222  99.130  32.781  1.00173.56           C  
ANISOU 1431  CD  GLU A 180    21482  15106  29358   -145  -6970   3963       C  
ATOM   1432  OE1 GLU A 180      89.572 100.054  32.016  1.00177.75           O  
ANISOU 1432  OE1 GLU A 180    22124  15503  29909   -268  -7309   4252       O  
ATOM   1433  OE2 GLU A 180      88.073  98.640  32.776  1.00174.96           O1-
ANISOU 1433  OE2 GLU A 180    21488  15201  29788    -37  -7009   3816       O1-
ATOM   1434  N   GLU A 181      93.705  96.337  34.131  1.00136.57           N  
ANISOU 1434  N   GLU A 181    17409  11711  22770   -387  -5573   3867       N  
ATOM   1435  CA  GLU A 181      93.772  94.883  34.219  1.00133.17           C  
ANISOU 1435  CA  GLU A 181    17016  11573  22010   -368  -5271   3747       C  
ATOM   1436  C   GLU A 181      94.277  94.394  35.576  1.00131.55           C  
ANISOU 1436  C   GLU A 181    16757  11507  21719   -277  -4844   3483       C  
ATOM   1437  O   GLU A 181      94.042  93.247  35.955  1.00129.72           O  
ANISOU 1437  O   GLU A 181    16491  11445  21352   -215  -4585   3308       O  
ATOM   1438  CB  GLU A 181      94.657  94.328  33.100  1.00133.68           C  
ANISOU 1438  CB  GLU A 181    17322  11909  21562   -550  -5297   4006       C  
ATOM   1439  CG  GLU A 181      96.029  94.976  33.020  1.00140.24           C  
ANISOU 1439  CG  GLU A 181    18318  12834  22132   -684  -5276   4185       C  
ATOM   1440  CD  GLU A 181      96.818  94.530  31.805  1.00146.08           C  
ANISOU 1440  CD  GLU A 181    19285  13819  22400   -883  -5337   4444       C  
ATOM   1441  OE1 GLU A 181      96.460  93.492  31.211  1.00148.94           O  
ANISOU 1441  OE1 GLU A 181    19684  14336  22571   -905  -5294   4439       O  
ATOM   1442  OE2 GLU A 181      97.797  95.219  31.446  1.00145.58           O1-
ANISOU 1442  OE2 GLU A 181    19363  13796  22153  -1026  -5421   4643       O1-
ATOM   1443  N   ASN A 182      94.965  95.265  36.306  1.00133.86           N  
ANISOU 1443  N   ASN A 182    17049  11725  22087   -280  -4779   3460       N  
ATOM   1444  CA  ASN A 182      95.551  94.885  37.589  1.00130.54           C  
ANISOU 1444  CA  ASN A 182    16596  11440  21563   -223  -4391   3236       C  
ATOM   1445  C   ASN A 182      94.658  95.195  38.789  1.00126.89           C  
ANISOU 1445  C   ASN A 182    15904  10768  21539    -73  -4283   2923       C  
ATOM   1446  O   ASN A 182      95.135  95.282  39.919  1.00128.37           O  
ANISOU 1446  O   ASN A 182    16057  10997  21720    -45  -4021   2751       O  
ATOM   1447  CB  ASN A 182      96.924  95.539  37.770  1.00128.84           C  
ANISOU 1447  CB  ASN A 182    16521  11308  21123   -328  -4334   3377       C  
ATOM   1448  CG  ASN A 182      97.949  95.021  36.781  1.00128.67           C  
ANISOU 1448  CG  ASN A 182    16721  11557  20611   -480  -4336   3631       C  
ATOM   1449  ND2 ASN A 182      99.177  95.515  36.887  1.00126.70           N  
ANISOU 1449  ND2 ASN A 182    16595  11404  20142   -581  -4277   3756       N  
ATOM   1450  OD1 ASN A 182      97.641  94.184  35.933  1.00131.64           O  
ANISOU 1450  OD1 ASN A 182    17152  12056  20807   -513  -4383   3704       O  
ATOM   1451  N   CYS A 183      93.363  95.357  38.540  1.00116.51           N  
ANISOU 1451  N   CYS A 183    14430   9232  20604     14  -4483   2844       N  
ATOM   1452  CA  CYS A 183      92.411  95.635  39.608  1.00108.82           C  
ANISOU 1452  CA  CYS A 183    13219   8052  20074    152  -4387   2528       C  
ATOM   1453  C   CYS A 183      92.007  94.347  40.318  1.00108.84           C  
ANISOU 1453  C   CYS A 183    13153   8240  19962    222  -4054   2269       C  
ATOM   1454  O   CYS A 183      91.515  93.413  39.685  1.00109.48           O  
ANISOU 1454  O   CYS A 183    13252   8431  19915    229  -4078   2300       O  
ATOM   1455  CB  CYS A 183      91.172  96.334  39.048  1.00111.17           C  
ANISOU 1455  CB  CYS A 183    13357   8028  20854    220  -4744   2543       C  
ATOM   1456  SG  CYS A 183      91.521  97.843  38.118  1.00202.66           S  
ANISOU 1456  SG  CYS A 183    25026  19368  32608    129  -5192   2872       S  
ATOM   1457  N   GLN A 184      92.216  94.300  41.631  1.00113.15           N  
ANISOU 1457  N   GLN A 184    13625   8819  20549    262  -3747   2017       N  
ATOM   1458  CA  GLN A 184      91.907  93.104  42.411  1.00117.86           C  
ANISOU 1458  CA  GLN A 184    14165   9594  21021    310  -3419   1770       C  
ATOM   1459  C   GLN A 184      90.513  92.580  42.095  1.00123.10           C  
ANISOU 1459  C   GLN A 184    14675  10163  21935    398  -3510   1642       C  
ATOM   1460  O   GLN A 184      89.519  93.283  42.266  1.00128.51           O  
ANISOU 1460  O   GLN A 184    15166  10577  23083    478  -3658   1507       O  
ATOM   1461  CB  GLN A 184      92.038  93.370  43.912  1.00121.43           C  
ANISOU 1461  CB  GLN A 184    14516  10017  21604    336  -3133   1488       C  
ATOM   1462  CG  GLN A 184      91.606  92.194  44.779  1.00124.28           C  
ANISOU 1462  CG  GLN A 184    14808  10537  21875    373  -2809   1219       C  
ATOM   1463  CD  GLN A 184      91.897  92.406  46.253  1.00125.10           C  
ANISOU 1463  CD  GLN A 184    14849  10652  22032    359  -2514    965       C  
ATOM   1464  NE2 GLN A 184      91.625  91.388  47.062  1.00120.57           N  
ANISOU 1464  NE2 GLN A 184    14235  10231  21344    366  -2226    744       N  
ATOM   1465  OE1 GLN A 184      92.362  93.471  46.661  1.00126.17           O  
ANISOU 1465  OE1 GLN A 184    14977  10660  22301    332  -2547    970       O  
ATOM   1466  N   LYS A 185      90.451  91.337  41.632  1.00123.68           N  
ANISOU 1466  N   LYS A 185    14830  10457  21706    383  -3422   1681       N  
ATOM   1467  CA  LYS A 185      89.188  90.723  41.251  1.00126.12           C  
ANISOU 1467  CA  LYS A 185    15014  10708  22197    453  -3505   1581       C  
ATOM   1468  C   LYS A 185      88.580  89.979  42.433  1.00131.27           C  
ANISOU 1468  C   LYS A 185    15525  11416  22936    521  -3185   1234       C  
ATOM   1469  O   LYS A 185      88.757  88.769  42.569  1.00138.51           O  
ANISOU 1469  O   LYS A 185    16519  12570  23538    502  -2965   1187       O  
ATOM   1470  CB  LYS A 185      89.409  89.769  40.077  1.00123.71           C  
ANISOU 1470  CB  LYS A 185    14877  10609  21519    388  -3585   1806       C  
ATOM   1471  CG  LYS A 185      90.304  90.345  38.990  1.00127.44           C  
ANISOU 1471  CG  LYS A 185    15537  11106  21777    278  -3827   2153       C  
ATOM   1472  CD  LYS A 185      90.677  89.302  37.951  1.00130.76           C  
ANISOU 1472  CD  LYS A 185    16138  11774  21772    193  -3834   2342       C  
ATOM   1473  CE  LYS A 185      91.676  89.863  36.950  1.00134.79           C  
ANISOU 1473  CE  LYS A 185    16844  12337  22033     59  -4035   2670       C  
ATOM   1474  NZ  LYS A 185      92.037  88.873  35.898  1.00135.87           N1+
ANISOU 1474  NZ  LYS A 185    17153  12714  21757    -39  -4038   2842       N1+
ATOM   1475  N   LEU A 186      87.867  90.707  43.287  1.00129.40           N  
ANISOU 1475  N   LEU A 186    15081  10956  23128    591  -3160    988       N  
ATOM   1476  CA  LEU A 186      87.265  90.115  44.478  1.00129.13           C  
ANISOU 1476  CA  LEU A 186    14904  10961  23198    636  -2854    638       C  
ATOM   1477  C   LEU A 186      86.157  89.126  44.127  1.00123.16           C  
ANISOU 1477  C   LEU A 186    14056  10242  22495    688  -2859    535       C  
ATOM   1478  O   LEU A 186      85.244  89.442  43.363  1.00119.36           O  
ANISOU 1478  O   LEU A 186    13465   9581  22305    743  -3135    582       O  
ATOM   1479  CB  LEU A 186      86.714  91.196  45.410  1.00135.53           C  
ANISOU 1479  CB  LEU A 186    15502  11510  24482    688  -2835    385       C  
ATOM   1480  CG  LEU A 186      87.681  92.238  45.973  1.00139.79           C  
ANISOU 1480  CG  LEU A 186    16099  11987  25029    639  -2797    422       C  
ATOM   1481  CD1 LEU A 186      88.001  93.288  44.926  1.00147.06           C  
ANISOU 1481  CD1 LEU A 186    17083  12735  26057    631  -3166    721       C  
ATOM   1482  CD2 LEU A 186      87.085  92.888  47.211  1.00137.44           C  
ANISOU 1482  CD2 LEU A 186    15586  11505  25128    677  -2639     71       C  
ATOM   1483  N   THR A 187      86.244  87.928  44.696  1.00120.07           N  
ANISOU 1483  N   THR A 187    13712  10082  21827    665  -2562    399       N  
ATOM   1484  CA  THR A 187      85.263  86.882  44.443  1.00122.48           C  
ANISOU 1484  CA  THR A 187    13947  10451  22140    704  -2530    292       C  
ATOM   1485  C   THR A 187      84.947  86.121  45.724  1.00122.19           C  
ANISOU 1485  C   THR A 187    13830  10524  22075    700  -2172    -31       C  
ATOM   1486  O   THR A 187      84.504  84.974  45.682  1.00125.92           O  
ANISOU 1486  O   THR A 187    14311  11140  22394    700  -2054   -106       O  
ATOM   1487  CB  THR A 187      85.773  85.881  43.392  1.00124.61           C  
ANISOU 1487  CB  THR A 187    14425  10945  21976    654  -2581    549       C  
ATOM   1488  CG2 THR A 187      85.983  86.571  42.050  1.00124.39           C  
ANISOU 1488  CG2 THR A 187    14480  10819  21962    633  -2946    867       C  
ATOM   1489  OG1 THR A 187      87.013  85.315  43.833  1.00125.00           O  
ANISOU 1489  OG1 THR A 187    14659  11236  21599    581  -2334    609       O  
ATOM   1490  N   LYS A 188      85.177  86.768  46.862  1.00118.19           N  
ANISOU 1490  N   LYS A 188    13248   9948  21711    683  -2002   -221       N  
ATOM   1491  CA  LYS A 188      84.998  86.130  48.161  1.00111.37           C  
ANISOU 1491  CA  LYS A 188    12326   9196  20792    647  -1653   -521       C  
ATOM   1492  C   LYS A 188      84.098  86.944  49.085  1.00111.79           C  
ANISOU 1492  C   LYS A 188    12130   9028  21316    681  -1590   -849       C  
ATOM   1493  O   LYS A 188      83.101  86.437  49.599  1.00112.05           O  
ANISOU 1493  O   LYS A 188    12009   9051  21513    697  -1455  -1118       O  
ATOM   1494  CB  LYS A 188      86.357  85.901  48.822  1.00105.05           C  
ANISOU 1494  CB  LYS A 188    11716   8598  19600    551  -1430   -447       C  
ATOM   1495  CG  LYS A 188      86.312  85.761  50.334  1.00101.37           C  
ANISOU 1495  CG  LYS A 188    11180   8183  19155    488  -1105   -753       C  
ATOM   1496  CD  LYS A 188      85.779  84.407  50.762  1.00 96.59           C  
ANISOU 1496  CD  LYS A 188    10567   7748  18383    461   -887   -920       C  
ATOM   1497  CE  LYS A 188      86.197  84.092  52.190  1.00 93.98           C  
ANISOU 1497  CE  LYS A 188    10263   7547  17898    352   -556  -1125       C  
ATOM   1498  NZ  LYS A 188      87.676  84.194  52.367  1.00 86.89           N1+
ANISOU 1498  NZ  LYS A 188     9566   6787  16659    280   -496   -917       N1+
ATOM   1499  N   ILE A 189      84.457  88.206  49.297  1.00110.42           N  
ANISOU 1499  N   ILE A 189    11914   8676  21362    685  -1682   -833       N  
ATOM   1500  CA  ILE A 189      83.704  89.070  50.200  1.00114.66           C  
ANISOU 1500  CA  ILE A 189    12215   8992  22357    711  -1613  -1154       C  
ATOM   1501  C   ILE A 189      82.675  89.917  49.458  1.00120.97           C  
ANISOU 1501  C   ILE A 189    12813   9490  23662    825  -1932  -1159       C  
ATOM   1502  O   ILE A 189      82.163  90.899  49.995  1.00118.52           O  
ANISOU 1502  O   ILE A 189    12305   8942  23784    862  -1948  -1371       O  
ATOM   1503  CB  ILE A 189      84.634  89.992  51.002  1.00115.35           C  
ANISOU 1503  CB  ILE A 189    12355   9042  22432    645  -1505  -1179       C  
ATOM   1504  CG1 ILE A 189      85.528  90.794  50.056  1.00120.67           C  
ANISOU 1504  CG1 ILE A 189    13172   9647  23030    656  -1786   -822       C  
ATOM   1505  CG2 ILE A 189      85.477  89.179  51.970  1.00113.57           C  
ANISOU 1505  CG2 ILE A 189    12282   9092  21777    525  -1165  -1242       C  
ATOM   1506  CD1 ILE A 189      86.461  91.749  50.763  1.00124.02           C  
ANISOU 1506  CD1 ILE A 189    13652  10026  23446    591  -1704   -825       C  
ATOM   1507  N   ILE A 190      82.379  89.531  48.222  1.00127.14           N  
ANISOU 1507  N   ILE A 190    13642  10277  24390    874  -2189   -925       N  
ATOM   1508  CA  ILE A 190      81.360  90.209  47.431  1.00131.64           C  
ANISOU 1508  CA  ILE A 190    14026  10570  25422    976  -2520   -902       C  
ATOM   1509  C   ILE A 190      80.184  89.269  47.197  1.00135.82           C  
ANISOU 1509  C   ILE A 190    14426  11135  26044   1023  -2508  -1042       C  
ATOM   1510  O   ILE A 190      79.206  89.622  46.538  1.00140.61           O  
ANISOU 1510  O   ILE A 190    14864  11535  27025   1107  -2772  -1039       O  
ATOM   1511  CB  ILE A 190      81.920  90.685  46.077  1.00133.81           C  
ANISOU 1511  CB  ILE A 190    14455  10789  25597    979  -2887   -490       C  
ATOM   1512  CG1 ILE A 190      83.218  91.465  46.286  1.00143.52           C  
ANISOU 1512  CG1 ILE A 190    15848  12035  26650    914  -2873   -328       C  
ATOM   1513  CG2 ILE A 190      80.903  91.546  45.343  1.00135.29           C  
ANISOU 1513  CG2 ILE A 190    14443  10658  26304   1075  -3254   -460       C  
ATOM   1514  CD1 ILE A 190      83.620  92.299  45.092  1.00153.37           C  
ANISOU 1514  CD1 ILE A 190    17192  13146  27937    914  -3260     26       C  
ATOM   1515  N   CYS A 191      80.284  88.067  47.753  1.00136.14           N  
ANISOU 1515  N   CYS A 191    14547  11435  25745    963  -2207  -1162       N  
ATOM   1516  CA  CYS A 191      79.264  87.047  47.555  1.00136.23           C  
ANISOU 1516  CA  CYS A 191    14466  11517  25777    991  -2168  -1286       C  
ATOM   1517  C   CYS A 191      78.066  87.260  48.472  1.00141.27           C  
ANISOU 1517  C   CYS A 191    14809  12003  26864   1031  -2027  -1698       C  
ATOM   1518  O   CYS A 191      78.218  87.617  49.640  1.00138.96           O  
ANISOU 1518  O   CYS A 191    14447  11695  26655    987  -1777  -1950       O  
ATOM   1519  CB  CYS A 191      79.858  85.657  47.780  1.00124.58           C  
ANISOU 1519  CB  CYS A 191    13199  10373  23763    906  -1907  -1247       C  
ATOM   1520  SG  CYS A 191      81.397  85.373  46.883  1.00154.58           S  
ANISOU 1520  SG  CYS A 191    17340  14374  27021    845  -2003   -811       S  
ATOM   1521  N   ALA A 192      76.873  87.039  47.930  1.00143.76           N  
ANISOU 1521  N   ALA A 192    14947  12209  27466   1106  -2186  -1768       N  
ATOM   1522  CA  ALA A 192      75.648  87.139  48.711  1.00146.57           C  
ANISOU 1522  CA  ALA A 192    15005  12431  28253   1145  -2055  -2167       C  
ATOM   1523  C   ALA A 192      75.649  86.096  49.822  1.00146.48           C  
ANISOU 1523  C   ALA A 192    15030  12664  27962   1046  -1639  -2431       C  
ATOM   1524  O   ALA A 192      76.534  85.242  49.883  1.00142.14           O  
ANISOU 1524  O   ALA A 192    14729  12375  26902    963  -1487  -2283       O  
ATOM   1525  CB  ALA A 192      74.434  86.964  47.815  1.00149.18           C  
ANISOU 1525  CB  ALA A 192    15162  12628  28890   1237  -2317  -2154       C  
ATOM   1526  N   GLN A 193      74.655  86.165  50.698  1.00152.96           N  
ANISOU 1526  N   GLN A 193    15597  13396  29124   1049  -1459  -2824       N  
ATOM   1527  CA  GLN A 193      74.571  85.240  51.821  1.00158.05           C  
ANISOU 1527  CA  GLN A 193    16260  14258  29533    934  -1065  -3099       C  
ATOM   1528  C   GLN A 193      74.313  83.805  51.364  1.00148.64           C  
ANISOU 1528  C   GLN A 193    15183  13293  27999    907  -1022  -3012       C  
ATOM   1529  O   GLN A 193      74.845  82.859  51.946  1.00141.30           O  
ANISOU 1529  O   GLN A 193    14427  12615  26647    798   -759  -3034       O  
ATOM   1530  CB  GLN A 193      73.494  85.691  52.811  1.00173.47           C  
ANISOU 1530  CB  GLN A 193    17899  16057  31956    932   -890  -3556       C  
ATOM   1531  CG  GLN A 193      73.311  84.768  54.009  1.00183.59           C  
ANISOU 1531  CG  GLN A 193    19187  17556  33012    790   -482  -3863       C  
ATOM   1532  CD  GLN A 193      74.564  84.642  54.859  1.00187.73           C  
ANISOU 1532  CD  GLN A 193    19947  18271  33111    651   -233  -3819       C  
ATOM   1533  NE2 GLN A 193      74.419  84.869  56.160  1.00192.62           N  
ANISOU 1533  NE2 GLN A 193    20465  18902  33822    538     70  -4169       N  
ATOM   1534  OE1 GLN A 193      75.646  84.334  54.357  1.00183.95           O  
ANISOU 1534  OE1 GLN A 193    19735  17932  32227    638   -311  -3479       O  
ATOM   1535  N   GLN A 194      73.503  83.649  50.321  1.00148.85           N  
ANISOU 1535  N   GLN A 194    15117  13226  28214   1003  -1289  -2908       N  
ATOM   1536  CA  GLN A 194      73.178  82.322  49.801  1.00146.81           C  
ANISOU 1536  CA  GLN A 194    14956  13164  27663    981  -1272  -2826       C  
ATOM   1537  C   GLN A 194      74.413  81.616  49.247  1.00141.90           C  
ANISOU 1537  C   GLN A 194    14674  12772  26471    928  -1281  -2475       C  
ATOM   1538  O   GLN A 194      74.402  80.403  49.044  1.00140.21           O  
ANISOU 1538  O   GLN A 194    14587  12763  25922    883  -1187  -2422       O  
ATOM   1539  CB  GLN A 194      72.095  82.399  48.720  1.00150.20           C  
ANISOU 1539  CB  GLN A 194    15219  13431  28421   1090  -1591  -2760       C  
ATOM   1540  CG  GLN A 194      70.794  83.045  49.167  1.00158.90           C  
ANISOU 1540  CG  GLN A 194    15957  14294  30122   1156  -1605  -3107       C  
ATOM   1541  CD  GLN A 194      70.782  84.545  48.948  1.00169.30           C  
ANISOU 1541  CD  GLN A 194    17124  15305  31898   1250  -1854  -3069       C  
ATOM   1542  NE2 GLN A 194      69.849  85.231  49.598  1.00173.07           N  
ANISOU 1542  NE2 GLN A 194    17285  15570  32903   1297  -1802  -3416       N  
ATOM   1543  OE1 GLN A 194      71.597  85.081  48.197  1.00173.61           O  
ANISOU 1543  OE1 GLN A 194    17831  15801  32331   1275  -2091  -2737       O  
ATOM   1544  N   CYS A 195      75.472  82.381  49.001  1.00138.38           N  
ANISOU 1544  N   CYS A 195    14368  12285  25926    932  -1393  -2243       N  
ATOM   1545  CA  CYS A 195      76.716  81.823  48.480  1.00130.98           C  
ANISOU 1545  CA  CYS A 195    13740  11555  24473    881  -1402  -1916       C  
ATOM   1546  C   CYS A 195      77.431  80.969  49.520  1.00130.29           C  
ANISOU 1546  C   CYS A 195    13805  11713  23986    767  -1040  -2019       C  
ATOM   1547  O   CYS A 195      77.626  81.391  50.660  1.00133.47           O  
ANISOU 1547  O   CYS A 195    14150  12099  24462    710   -825  -2233       O  
ATOM   1548  CB  CYS A 195      77.649  82.934  47.994  1.00128.80           C  
ANISOU 1548  CB  CYS A 195    13557  11164  24215    906  -1612  -1657       C  
ATOM   1549  SG  CYS A 195      77.220  83.632  46.386  1.00175.30           S  
ANISOU 1549  SG  CYS A 195    19401  16844  30361   1004  -2095  -1365       S  
ATOM   1550  N   SER A 196      77.825  79.767  49.115  1.00127.65           N  
ANISOU 1550  N   SER A 196    13666  11603  23231    726   -981  -1863       N  
ATOM   1551  CA  SER A 196      78.533  78.852  49.999  1.00126.56           C  
ANISOU 1551  CA  SER A 196    13689  11700  22698    617   -669  -1921       C  
ATOM   1552  C   SER A 196      80.037  79.098  49.954  1.00126.18           C  
ANISOU 1552  C   SER A 196    13867  11748  22329    578   -661  -1668       C  
ATOM   1553  O   SER A 196      80.698  79.149  50.991  1.00129.91           O  
ANISOU 1553  O   SER A 196    14398  12300  22663    494   -436  -1761       O  
ATOM   1554  CB  SER A 196      78.227  77.403  49.620  1.00130.52           C  
ANISOU 1554  CB  SER A 196    14286  12386  22921    593   -605  -1888       C  
ATOM   1555  OG  SER A 196      78.509  77.167  48.251  1.00134.88           O  
ANISOU 1555  OG  SER A 196    14966  12965  23319    646   -851  -1576       O  
ATOM   1556  N   GLY A 197      80.572  79.254  48.747  1.00121.99           N  
ANISOU 1556  N   GLY A 197    13462  11212  21676    627   -907  -1349       N  
ATOM   1557  CA  GLY A 197      81.995  79.471  48.566  1.00117.27           C  
ANISOU 1557  CA  GLY A 197    13075  10710  20772    590   -917  -1093       C  
ATOM   1558  C   GLY A 197      82.312  80.778  47.866  1.00117.17           C  
ANISOU 1558  C   GLY A 197    13045  10515  20961    644  -1192   -906       C  
ATOM   1559  O   GLY A 197      82.038  81.855  48.392  1.00116.87           O  
ANISOU 1559  O   GLY A 197    12856  10291  21260    666  -1219  -1046       O  
ATOM   1560  N   ARG A 198      82.892  80.681  46.674  1.00120.32           N  
ANISOU 1560  N   ARG A 198    13600  10966  21152    655  -1395   -593       N  
ATOM   1561  CA  ARG A 198      83.271  81.859  45.903  1.00120.47           C  
ANISOU 1561  CA  ARG A 198    13633  10828  21312    685  -1676   -375       C  
ATOM   1562  C   ARG A 198      82.130  82.287  44.990  1.00120.93           C  
ANISOU 1562  C   ARG A 198    13539  10687  21723    760  -1977   -351       C  
ATOM   1563  O   ARG A 198      81.046  81.704  45.027  1.00123.24           O  
ANISOU 1563  O   ARG A 198    13700  10961  22163    793  -1952   -522       O  
ATOM   1564  CB  ARG A 198      84.517  81.568  45.067  1.00123.19           C  
ANISOU 1564  CB  ARG A 198    14228  11337  21240    636  -1742    -47       C  
ATOM   1565  CG  ARG A 198      85.550  80.704  45.772  1.00121.81           C  
ANISOU 1565  CG  ARG A 198    14216  11404  20660    565  -1447    -51       C  
ATOM   1566  CD  ARG A 198      86.280  81.470  46.860  1.00119.27           C  
ANISOU 1566  CD  ARG A 198    13890  11055  20373    527  -1299   -133       C  
ATOM   1567  NE  ARG A 198      87.088  82.554  46.311  1.00119.01           N  
ANISOU 1567  NE  ARG A 198    13929  10938  20353    522  -1494     95       N  
ATOM   1568  CZ  ARG A 198      88.044  83.186  46.983  1.00119.34           C  
ANISOU 1568  CZ  ARG A 198    14027  10991  20325    475  -1397    117       C  
ATOM   1569  NH1 ARG A 198      88.320  82.838  48.233  1.00114.24           N1+
ANISOU 1569  NH1 ARG A 198    13378  10440  19588    425  -1113    -71       N1+
ATOM   1570  NH2 ARG A 198      88.727  84.162  46.403  1.00125.51           N  
ANISOU 1570  NH2 ARG A 198    14875  11692  21120    467  -1591    332       N  
ATOM   1571  N   CYS A 199      82.380  83.299  44.165  1.00121.53           N  
ANISOU 1571  N   CYS A 199    13633  10613  21931    780  -2271   -130       N  
ATOM   1572  CA  CYS A 199      81.352  83.819  43.268  1.00124.45           C  
ANISOU 1572  CA  CYS A 199    13860  10771  22655    844  -2598    -75       C  
ATOM   1573  C   CYS A 199      81.936  84.611  42.101  1.00115.98           C  
ANISOU 1573  C   CYS A 199    12907   9616  21543    822  -2929    270       C  
ATOM   1574  O   CYS A 199      83.076  85.073  42.157  1.00105.24           O  
ANISOU 1574  O   CYS A 199    11693   8308  19984    772  -2906    422       O  
ATOM   1575  CB  CYS A 199      80.364  84.691  44.044  1.00130.84           C  
ANISOU 1575  CB  CYS A 199    14388  11325  24001    918  -2608   -360       C  
ATOM   1576  SG  CYS A 199      81.136  86.031  44.979  1.00122.35           S  
ANISOU 1576  SG  CYS A 199    13281  10109  23096    909  -2537   -427       S  
ATOM   1577  N   ARG A 200      81.142  84.761  41.045  1.00118.97           N  
ANISOU 1577  N   ARG A 200    13224   9870  22109    850  -3241    394       N  
ATOM   1578  CA  ARG A 200      81.536  85.552  39.886  1.00126.55           C  
ANISOU 1578  CA  ARG A 200    14284  10730  23068    814  -3594    721       C  
ATOM   1579  C   ARG A 200      81.206  87.021  40.117  1.00135.01           C  
ANISOU 1579  C   ARG A 200    15183  11489  24625    873  -3800    684       C  
ATOM   1580  O   ARG A 200      82.021  87.903  39.847  1.00141.06           O  
ANISOU 1580  O   ARG A 200    16051  12191  25357    833  -3940    882       O  
ATOM   1581  CB  ARG A 200      80.819  85.057  38.629  1.00131.64           C  
ANISOU 1581  CB  ARG A 200    14947  11378  23693    798  -3856    885       C  
ATOM   1582  CG  ARG A 200      81.224  83.664  38.185  1.00136.70           C  
ANISOU 1582  CG  ARG A 200    15784  12319  23838    727  -3696    967       C  
ATOM   1583  CD  ARG A 200      80.451  83.233  36.948  1.00143.09           C  
ANISOU 1583  CD  ARG A 200    16602  13118  24647    701  -3964   1117       C  
ATOM   1584  NE  ARG A 200      79.039  82.999  37.237  1.00150.08           N  
ANISOU 1584  NE  ARG A 200    17247  13876  25899    787  -3986    882       N  
ATOM   1585  CZ  ARG A 200      78.148  82.600  36.335  1.00156.33           C  
ANISOU 1585  CZ  ARG A 200    17997  14638  26761    779  -4203    955       C  
ATOM   1586  NH1 ARG A 200      78.521  82.390  35.080  1.00158.86           N1+
ANISOU 1586  NH1 ARG A 200    18509  15050  26801    678  -4416   1257       N1+
ATOM   1587  NH2 ARG A 200      76.884  82.410  36.686  1.00157.15           N  
ANISOU 1587  NH2 ARG A 200    17868  14628  27215    861  -4205    723       N  
ATOM   1588  N   GLY A 201      80.000  87.271  40.619  1.00136.37           N  
ANISOU 1588  N   GLY A 201    15088  11466  25260    967  -3817    422       N  
ATOM   1589  CA  GLY A 201      79.549  88.620  40.904  1.00139.71           C  
ANISOU 1589  CA  GLY A 201    15309  11569  26204   1038  -3999    339       C  
ATOM   1590  C   GLY A 201      78.870  88.712  42.257  1.00136.72           C  
ANISOU 1590  C   GLY A 201    14690  11101  26155   1110  -3729    -75       C  
ATOM   1591  O   GLY A 201      79.137  87.908  43.150  1.00126.95           O  
ANISOU 1591  O   GLY A 201    13496  10069  24668   1078  -3366   -267       O  
ATOM   1592  N   LYS A 202      77.989  89.695  42.410  1.00142.63           N  
ANISOU 1592  N   LYS A 202    15183  11538  27470   1198  -3909   -215       N  
ATOM   1593  CA  LYS A 202      77.279  89.887  43.669  1.00145.74           C  
ANISOU 1593  CA  LYS A 202    15325  11824  28224   1259  -3662   -630       C  
ATOM   1594  C   LYS A 202      75.899  89.237  43.631  1.00150.39           C  
ANISOU 1594  C   LYS A 202    15698  12374  29070   1322  -3663   -844       C  
ATOM   1595  O   LYS A 202      75.367  88.829  44.664  1.00149.14           O  
ANISOU 1595  O   LYS A 202    15390  12259  29018   1335  -3362  -1196       O  
ATOM   1596  CB  LYS A 202      77.158  91.375  44.002  1.00149.23           C  
ANISOU 1596  CB  LYS A 202    15594  11941  29165   1320  -3815   -708       C  
ATOM   1597  CG  LYS A 202      76.622  91.650  45.397  1.00154.47           C  
ANISOU 1597  CG  LYS A 202    16020  12510  30163   1358  -3516  -1151       C  
ATOM   1598  CD  LYS A 202      76.544  93.140  45.682  1.00159.74           C  
ANISOU 1598  CD  LYS A 202    16521  12845  31328   1417  -3671  -1224       C  
ATOM   1599  CE  LYS A 202      75.992  93.405  47.075  1.00160.26           C  
ANISOU 1599  CE  LYS A 202    16344  12822  31727   1442  -3355  -1690       C  
ATOM   1600  NZ  LYS A 202      75.831  94.860  47.341  1.00164.00           N1+
ANISOU 1600  NZ  LYS A 202    16632  12949  32730   1507  -3508  -1788       N1+
ATOM   1601  N   SER A 203      75.326  89.142  42.436  1.00157.34           N  
ANISOU 1601  N   SER A 203    16564  13177  30040   1348  -4005   -629       N  
ATOM   1602  CA  SER A 203      74.027  88.502  42.262  1.00163.88           C  
ANISOU 1602  CA  SER A 203    17198  13974  31094   1403  -4041   -794       C  
ATOM   1603  C   SER A 203      74.127  87.009  42.549  1.00163.68           C  
ANISOU 1603  C   SER A 203    17304  14281  30606   1338  -3720   -882       C  
ATOM   1604  O   SER A 203      75.076  86.353  42.119  1.00164.37           O  
ANISOU 1604  O   SER A 203    17672  14608  30172   1255  -3663   -648       O  
ATOM   1605  CB  SER A 203      73.495  88.735  40.846  1.00169.99           C  
ANISOU 1605  CB  SER A 203    17960  14605  32025   1424  -4502   -501       C  
ATOM   1606  OG  SER A 203      74.391  88.227  39.873  1.00172.90           O  
ANISOU 1606  OG  SER A 203    18641  15182  31871   1324  -4607   -134       O  
ATOM   1607  N   PRO A 204      73.145  86.467  43.284  1.00162.06           N  
ANISOU 1607  N   PRO A 204    16891  14085  30598   1373  -3508  -1228       N  
ATOM   1608  CA  PRO A 204      73.104  85.050  43.663  1.00160.65           C  
ANISOU 1608  CA  PRO A 204    16810  14199  30031   1312  -3197  -1350       C  
ATOM   1609  C   PRO A 204      73.157  84.119  42.454  1.00157.48           C  
ANISOU 1609  C   PRO A 204    16596  13962  29275   1272  -3364  -1061       C  
ATOM   1610  O   PRO A 204      73.432  82.928  42.606  1.00148.05           O  
ANISOU 1610  O   PRO A 204    15556  13034  27664   1208  -3129  -1079       O  
ATOM   1611  CB  PRO A 204      71.754  84.919  44.373  1.00159.05           C  
ANISOU 1611  CB  PRO A 204    16291  13886  30254   1370  -3074  -1743       C  
ATOM   1612  CG  PRO A 204      71.466  86.287  44.882  1.00158.87           C  
ANISOU 1612  CG  PRO A 204    16034  13562  30766   1443  -3156  -1908       C  
ATOM   1613  CD  PRO A 204      72.011  87.221  43.846  1.00161.73           C  
ANISOU 1613  CD  PRO A 204    16499  13764  31188   1469  -3546  -1541       C  
ATOM   1614  N   SER A 205      72.897  84.662  41.269  1.00162.68           N  
ANISOU 1614  N   SER A 205    17245  14462  30102   1299  -3771   -797       N  
ATOM   1615  CA  SER A 205      72.930  83.880  40.039  1.00164.80           C  
ANISOU 1615  CA  SER A 205    17693  14873  30051   1245  -3960   -511       C  
ATOM   1616  C   SER A 205      74.364  83.645  39.578  1.00165.60           C  
ANISOU 1616  C   SER A 205    18130  15181  29607   1148  -3926   -210       C  
ATOM   1617  O   SER A 205      74.598  83.026  38.540  1.00166.76           O  
ANISOU 1617  O   SER A 205    18462  15466  29432   1081  -4062     44       O  
ATOM   1618  CB  SER A 205      72.145  84.593  38.937  1.00171.15           C  
ANISOU 1618  CB  SER A 205    18370  15428  31231   1288  -4424   -327       C  
ATOM   1619  OG  SER A 205      70.845  84.941  39.380  1.00179.57           O  
ANISOU 1619  OG  SER A 205    19098  16273  32857   1389  -4471   -610       O  
ATOM   1620  N   ASP A 206      75.320  84.143  40.356  1.00163.59           N  
ANISOU 1620  N   ASP A 206    17951  14950  29257   1133  -3740   -248       N  
ATOM   1621  CA  ASP A 206      76.729  84.053  39.994  1.00156.55           C  
ANISOU 1621  CA  ASP A 206    17356  14237  27890   1045  -3706     24       C  
ATOM   1622  C   ASP A 206      77.516  83.194  40.979  1.00145.45           C  
ANISOU 1622  C   ASP A 206    16082  13089  26095    998  -3282   -120       C  
ATOM   1623  O   ASP A 206      78.735  83.069  40.865  1.00143.75           O  
ANISOU 1623  O   ASP A 206    16096  13033  25490    929  -3201     64       O  
ATOM   1624  CB  ASP A 206      77.351  85.450  39.915  1.00160.17           C  
ANISOU 1624  CB  ASP A 206    17823  14502  28533   1052  -3900    171       C  
ATOM   1625  CG  ASP A 206      76.664  86.340  38.897  1.00165.50           C  
ANISOU 1625  CG  ASP A 206    18386  14911  29584   1087  -4353    352       C  
ATOM   1626  OD1 ASP A 206      75.779  85.845  38.167  1.00168.31           O  
ANISOU 1626  OD1 ASP A 206    18680  15251  30018   1096  -4527    392       O  
ATOM   1627  OD2 ASP A 206      77.012  87.538  38.826  1.00167.37           O1-
ANISOU 1627  OD2 ASP A 206    18601  14950  30041   1100  -4543    459       O1-
ATOM   1628  N   CYS A 207      76.817  82.609  41.946  1.00138.31           N  
ANISOU 1628  N   CYS A 207    15029  12223  25301   1026  -3017   -447       N  
ATOM   1629  CA  CYS A 207      77.462  81.778  42.958  1.00130.45           C  
ANISOU 1629  CA  CYS A 207    14143  11457  23963    972  -2622   -598       C  
ATOM   1630  C   CYS A 207      78.282  80.647  42.345  1.00117.16           C  
ANISOU 1630  C   CYS A 207    12734  10049  21734    896  -2548   -380       C  
ATOM   1631  O   CYS A 207      77.817  79.940  41.450  1.00111.47           O  
ANISOU 1631  O   CYS A 207    12054   9390  20908    888  -2673   -274       O  
ATOM   1632  CB  CYS A 207      76.431  81.207  43.935  1.00133.70           C  
ANISOU 1632  CB  CYS A 207    14357  11875  24568    994  -2381   -969       C  
ATOM   1633  SG  CYS A 207      76.137  82.226  45.399  1.00110.90           S  
ANISOU 1633  SG  CYS A 207    11233   8804  22100   1023  -2196  -1323       S  
ATOM   1634  N   CYS A 208      79.505  80.484  42.838  1.00109.94           N  
ANISOU 1634  N   CYS A 208    12001   9293  20480    839  -2342   -319       N  
ATOM   1635  CA  CYS A 208      80.385  79.425  42.363  1.00104.64           C  
ANISOU 1635  CA  CYS A 208    11579   8878  19301    770  -2242   -133       C  
ATOM   1636  C   CYS A 208      80.113  78.116  43.091  1.00103.67           C  
ANISOU 1636  C   CYS A 208    11466   8937  18986    747  -1936   -342       C  
ATOM   1637  O   CYS A 208      79.740  78.113  44.265  1.00101.74           O  
ANISOU 1637  O   CYS A 208    11094   8668  18894    752  -1719   -618       O  
ATOM   1638  CB  CYS A 208      81.852  79.825  42.533  1.00 98.20           C  
ANISOU 1638  CB  CYS A 208    10946   8150  18214    719  -2170     36       C  
ATOM   1639  SG  CYS A 208      82.430  81.047  41.336  1.00120.13           S  
ANISOU 1639  SG  CYS A 208    13806  10792  21046    708  -2543    376       S  
ATOM   1640  N   HIS A 209      80.301  77.008  42.381  1.00102.47           N  
ANISOU 1640  N   HIS A 209    11471   8966  18498    709  -1920   -212       N  
ATOM   1641  CA  HIS A 209      80.126  75.679  42.954  1.00 94.68           C  
ANISOU 1641  CA  HIS A 209    10523   8158  17292    679  -1648   -373       C  
ATOM   1642  C   HIS A 209      80.938  75.526  44.236  1.00 94.49           C  
ANISOU 1642  C   HIS A 209    10555   8237  17109    637  -1343   -498       C  
ATOM   1643  O   HIS A 209      82.021  76.095  44.369  1.00 95.98           O  
ANISOU 1643  O   HIS A 209    10847   8444  17176    616  -1331   -366       O  
ATOM   1644  CB  HIS A 209      80.535  74.607  41.944  1.00 88.13           C  
ANISOU 1644  CB  HIS A 209     9895   7512  16080    637  -1677   -170       C  
ATOM   1645  CG  HIS A 209      80.223  73.212  42.386  1.00 87.10           C  
ANISOU 1645  CG  HIS A 209     9798   7542  15752    610  -1439   -323       C  
ATOM   1646  CD2 HIS A 209      79.300  72.323  41.949  1.00 88.16           C  
ANISOU 1646  CD2 HIS A 209     9897   7715  15882    611  -1460   -388       C  
ATOM   1647  ND1 HIS A 209      80.910  72.582  43.401  1.00 87.63           N  
ANISOU 1647  ND1 HIS A 209     9949   7751  15593    569  -1145   -422       N  
ATOM   1648  CE1 HIS A 209      80.422  71.367  43.573  1.00 86.52           C  
ANISOU 1648  CE1 HIS A 209     9827   7725  15321    546   -998   -539       C  
ATOM   1649  NE2 HIS A 209      79.445  71.184  42.703  1.00 88.14           N  
ANISOU 1649  NE2 HIS A 209     9962   7874  15655    572  -1179   -526       N  
ATOM   1650  N   ASN A 210      80.407  74.754  45.177  1.00101.73           N  
ANISOU 1650  N   ASN A 210    11406   9223  18025    615  -1102   -749       N  
ATOM   1651  CA  ASN A 210      81.058  74.549  46.465  1.00111.07           C  
ANISOU 1651  CA  ASN A 210    12634  10503  19064    555   -813   -885       C  
ATOM   1652  C   ASN A 210      82.534  74.187  46.341  1.00107.49           C  
ANISOU 1652  C   ASN A 210    12416  10216  18207    509   -736   -662       C  
ATOM   1653  O   ASN A 210      83.345  74.555  47.190  1.00108.06           O  
ANISOU 1653  O   ASN A 210    12532  10319  18208    469   -596   -684       O  
ATOM   1654  CB  ASN A 210      80.328  73.464  47.258  1.00126.27           C  
ANISOU 1654  CB  ASN A 210    14507  12523  20947    512   -581  -1135       C  
ATOM   1655  CG  ASN A 210      81.060  73.079  48.528  1.00135.33           C  
ANISOU 1655  CG  ASN A 210    15735  13797  21886    426   -290  -1242       C  
ATOM   1656  ND2 ASN A 210      81.107  71.782  48.815  1.00132.99           N  
ANISOU 1656  ND2 ASN A 210    15540  13669  21322    369   -114  -1284       N  
ATOM   1657  OD1 ASN A 210      81.577  73.936  49.244  1.00141.10           O  
ANISOU 1657  OD1 ASN A 210    16442  14473  22698    403   -232  -1284       O  
ATOM   1658  N   GLN A 211      82.877  73.472  45.275  1.00105.53           N  
ANISOU 1658  N   GLN A 211    12317  10078  17704    510   -828   -453       N  
ATOM   1659  CA  GLN A 211      84.227  72.942  45.110  1.00104.55           C  
ANISOU 1659  CA  GLN A 211    12406  10125  17190    467   -737   -261       C  
ATOM   1660  C   GLN A 211      85.126  73.787  44.204  1.00109.60           C  
ANISOU 1660  C   GLN A 211    13143  10736  17764    474   -935      9       C  
ATOM   1661  O   GLN A 211      86.004  73.258  43.522  1.00112.80           O  
ANISOU 1661  O   GLN A 211    13719  11278  17862    447   -939    204       O  
ATOM   1662  CB  GLN A 211      84.164  71.501  44.600  1.00 96.53           C  
ANISOU 1662  CB  GLN A 211    11505   9270  15900    448   -665   -222       C  
ATOM   1663  CG  GLN A 211      83.829  70.488  45.679  1.00 95.79           C  
ANISOU 1663  CG  GLN A 211    11395   9268  15734    409   -406   -440       C  
ATOM   1664  CD  GLN A 211      85.036  70.119  46.516  1.00 98.63           C  
ANISOU 1664  CD  GLN A 211    11884   9757  15832    354   -197   -408       C  
ATOM   1665  NE2 GLN A 211      84.896  70.215  47.834  1.00 99.87           N  
ANISOU 1665  NE2 GLN A 211    11971   9904  16071    307    -15   -607       N  
ATOM   1666  OE1 GLN A 211      86.081  69.748  45.985  1.00100.03           O  
ANISOU 1666  OE1 GLN A 211    12222  10045  15741    345   -199   -208       O  
ATOM   1667  N   CYS A 212      84.911  75.098  44.206  1.00108.40           N  
ANISOU 1667  N   CYS A 212    12880  10404  17903    504  -1096     13       N  
ATOM   1668  CA  CYS A 212      85.756  76.006  43.438  1.00104.32           C  
ANISOU 1668  CA  CYS A 212    12451   9846  17339    498  -1288    263       C  
ATOM   1669  C   CYS A 212      86.729  76.747  44.352  1.00105.33           C  
ANISOU 1669  C   CYS A 212    12604   9969  17449    472  -1171    258       C  
ATOM   1670  O   CYS A 212      86.435  76.982  45.524  1.00110.53           O  
ANISOU 1670  O   CYS A 212    13152  10573  18270    471  -1015     39       O  
ATOM   1671  CB  CYS A 212      84.903  76.993  42.642  1.00103.44           C  
ANISOU 1671  CB  CYS A 212    12216   9526  17560    542  -1595    318       C  
ATOM   1672  SG  CYS A 212      84.025  76.242  41.251  1.00101.95           S  
ANISOU 1672  SG  CYS A 212    12046   9360  17331    548  -1798    421       S  
ATOM   1673  N   ALA A 213      87.887  77.111  43.811  1.00 97.96           N  
ANISOU 1673  N   ALA A 213    11815   9096  16309    439  -1242    495       N  
ATOM   1674  CA  ALA A 213      88.936  77.732  44.611  1.00 95.03           C  
ANISOU 1674  CA  ALA A 213    11490   8744  15874    405  -1129    516       C  
ATOM   1675  C   ALA A 213      89.074  79.225  44.338  1.00106.73           C  
ANISOU 1675  C   ALA A 213    12922  10047  17586    416  -1343    615       C  
ATOM   1676  O   ALA A 213      88.737  80.051  45.185  1.00118.90           O  
ANISOU 1676  O   ALA A 213    14333  11444  19400    433  -1316    457       O  
ATOM   1677  CB  ALA A 213      90.265  77.026  44.382  1.00 90.80           C  
ANISOU 1677  CB  ALA A 213    11149   8419  14932    353  -1016    691       C  
ATOM   1678  N   ALA A 214      89.573  79.568  43.156  1.00107.22           N  
ANISOU 1678  N   ALA A 214    13090  10115  17535    396  -1554    873       N  
ATOM   1679  CA  ALA A 214      89.851  80.962  42.831  1.00114.90           C  
ANISOU 1679  CA  ALA A 214    14044  10928  18684    390  -1768   1005       C  
ATOM   1680  C   ALA A 214      88.651  81.659  42.204  1.00115.54           C  
ANISOU 1680  C   ALA A 214    13983  10785  19131    441  -2046    993       C  
ATOM   1681  O   ALA A 214      88.719  82.838  41.858  1.00122.62           O  
ANISOU 1681  O   ALA A 214    14850  11517  20223    441  -2264   1104       O  
ATOM   1682  CB  ALA A 214      91.060  81.060  41.914  1.00121.89           C  
ANISOU 1682  CB  ALA A 214    15120  11935  19259    321  -1858   1294       C  
ATOM   1683  N   GLY A 215      87.552  80.928  42.061  1.00107.32           N  
ANISOU 1683  N   GLY A 215    12851   9733  18192    483  -2045    862       N  
ATOM   1684  CA  GLY A 215      86.359  81.467  41.437  1.00104.12           C  
ANISOU 1684  CA  GLY A 215    12301   9122  18137    533  -2313    850       C  
ATOM   1685  C   GLY A 215      85.845  80.530  40.365  1.00 99.82           C  
ANISOU 1685  C   GLY A 215    11814   8668  17445    520  -2418    946       C  
ATOM   1686  O   GLY A 215      86.223  79.359  40.328  1.00103.53           O  
ANISOU 1686  O   GLY A 215    12402   9349  17586    487  -2234    947       O  
ATOM   1687  N   CYS A 216      84.989  81.039  39.486  1.00 93.43           N  
ANISOU 1687  N   CYS A 216    10923   7694  16882    539  -2721   1028       N  
ATOM   1688  CA  CYS A 216      84.416  80.209  38.434  1.00 96.27           C  
ANISOU 1688  CA  CYS A 216    11331   8127  17121    515  -2845   1119       C  
ATOM   1689  C   CYS A 216      83.930  81.027  37.244  1.00 96.77           C  
ANISOU 1689  C   CYS A 216    11372   8021  17375    495  -3241   1327       C  
ATOM   1690  O   CYS A 216      83.836  82.251  37.311  1.00102.04           O  
ANISOU 1690  O   CYS A 216    11949   8480  18340    520  -3429   1367       O  
ATOM   1691  CB  CYS A 216      83.264  79.369  38.987  1.00102.27           C  
ANISOU 1691  CB  CYS A 216    11942   8887  18031    577  -2704    853       C  
ATOM   1692  SG  CYS A 216      81.836  80.333  39.530  1.00124.15           S  
ANISOU 1692  SG  CYS A 216    14404  11352  21414    677  -2848    627       S  
ATOM   1693  N   THR A 217      83.627  80.331  36.154  1.00 95.65           N  
ANISOU 1693  N   THR A 217    11318   7969  17057    440  -3370   1462       N  
ATOM   1694  CA  THR A 217      83.068  80.955  34.965  1.00100.82           C  
ANISOU 1694  CA  THR A 217    11959   8478  17869    401  -3759   1666       C  
ATOM   1695  C   THR A 217      81.637  80.475  34.787  1.00106.12           C  
ANISOU 1695  C   THR A 217    12468   9066  18787    455  -3852   1530       C  
ATOM   1696  O   THR A 217      81.052  80.604  33.713  1.00105.86           O  
ANISOU 1696  O   THR A 217    12437   8961  18822    410  -4152   1692       O  
ATOM   1697  CB  THR A 217      83.875  80.594  33.709  1.00106.65           C  
ANISOU 1697  CB  THR A 217    12942   9392  18189    261  -3866   1956       C  
ATOM   1698  CG2 THR A 217      85.341  80.955  33.898  1.00112.25           C  
ANISOU 1698  CG2 THR A 217    13812  10210  18626    202  -3744   2077       C  
ATOM   1699  OG1 THR A 217      83.761  79.188  33.453  1.00104.38           O  
ANISOU 1699  OG1 THR A 217    12738   9315  17605    232  -3689   1899       O  
ATOM   1700  N   GLY A 218      81.084  79.912  35.857  1.00113.42           N  
ANISOU 1700  N   GLY A 218    13254  10006  19836    541  -3592   1235       N  
ATOM   1701  CA  GLY A 218      79.739  79.371  35.838  1.00119.10           C  
ANISOU 1701  CA  GLY A 218    13808  10664  20780    594  -3630   1068       C  
ATOM   1702  C   GLY A 218      79.434  78.588  37.100  1.00120.55           C  
ANISOU 1702  C   GLY A 218    13894  10930  20978    656  -3271    748       C  
ATOM   1703  O   GLY A 218      80.344  78.103  37.773  1.00120.83           O  
ANISOU 1703  O   GLY A 218    14048  11134  20730    634  -2984    697       O  
ATOM   1704  N   PRO A 219      78.142  78.461  37.430  1.00118.98           N  
ANISOU 1704  N   PRO A 219    13477  10614  21116    725  -3290    531       N  
ATOM   1705  CA  PRO A 219      77.667  77.790  38.644  1.00115.48           C  
ANISOU 1705  CA  PRO A 219    12914  10227  20737    771  -2969    205       C  
ATOM   1706  C   PRO A 219      78.068  76.320  38.707  1.00112.22           C  
ANISOU 1706  C   PRO A 219    12671  10084  19882    715  -2707    182       C  
ATOM   1707  O   PRO A 219      78.372  75.815  39.787  1.00110.81           O  
ANISOU 1707  O   PRO A 219    12501  10010  19593    717  -2395     -6       O  
ATOM   1708  CB  PRO A 219      76.141  77.898  38.516  1.00117.91           C  
ANISOU 1708  CB  PRO A 219    12975  10361  21465    834  -3131     51       C  
ATOM   1709  CG  PRO A 219      75.908  78.105  37.041  1.00120.09           C  
ANISOU 1709  CG  PRO A 219    13314  10581  21735    797  -3504    336       C  
ATOM   1710  CD  PRO A 219      77.021  79.016  36.657  1.00121.17           C  
ANISOU 1710  CD  PRO A 219    13595  10683  21760    756  -3639    586       C  
ATOM   1711  N   ARG A 220      78.069  75.649  37.560  1.00113.47           N  
ANISOU 1711  N   ARG A 220    12967  10349  19796    658  -2838    372       N  
ATOM   1712  CA  ARG A 220      78.265  74.202  37.517  1.00115.00           C  
ANISOU 1712  CA  ARG A 220    13302  10776  19616    611  -2616    338       C  
ATOM   1713  C   ARG A 220      79.575  73.726  38.140  1.00112.53           C  
ANISOU 1713  C   ARG A 220    13166  10648  18943    576  -2328    350       C  
ATOM   1714  O   ARG A 220      80.458  74.520  38.462  1.00113.48           O  
ANISOU 1714  O   ARG A 220    13330  10737  19050    575  -2315    425       O  
ATOM   1715  CB  ARG A 220      78.129  73.676  36.085  1.00119.49           C  
ANISOU 1715  CB  ARG A 220    14001  11421  19980    541  -2824    558       C  
ATOM   1716  CG  ARG A 220      76.694  73.601  35.597  1.00126.12           C  
ANISOU 1716  CG  ARG A 220    14673  12141  21105    566  -3029    493       C  
ATOM   1717  CD  ARG A 220      76.599  72.966  34.221  1.00136.04           C  
ANISOU 1717  CD  ARG A 220    16077  13498  22112    475  -3208    703       C  
ATOM   1718  NE  ARG A 220      75.223  72.944  33.733  1.00150.01           N  
ANISOU 1718  NE  ARG A 220    17682  15147  24166    493  -3429    657       N  
ATOM   1719  CZ  ARG A 220      74.856  72.475  32.545  1.00157.23           C  
ANISOU 1719  CZ  ARG A 220    18683  16116  24943    412  -3626    818       C  
ATOM   1720  NH1 ARG A 220      73.579  72.497  32.187  1.00158.04           N1+
ANISOU 1720  NH1 ARG A 220    18618  16098  25333    432  -3829    766       N1+
ATOM   1721  NH2 ARG A 220      75.766  71.985  31.714  1.00159.74           N  
ANISOU 1721  NH2 ARG A 220    19251  16608  24837    303  -3617   1024       N  
ATOM   1722  N   GLU A 221      79.678  72.412  38.301  1.00112.19           N  
ANISOU 1722  N   GLU A 221    13221  10791  18615    546  -2106    277       N  
ATOM   1723  CA  GLU A 221      80.818  71.779  38.948  1.00109.90           C  
ANISOU 1723  CA  GLU A 221    13083  10676  17997    516  -1823    268       C  
ATOM   1724  C   GLU A 221      82.033  71.747  38.028  1.00110.02           C  
ANISOU 1724  C   GLU A 221    13316  10809  17676    454  -1887    541       C  
ATOM   1725  O   GLU A 221      83.140  71.422  38.457  1.00108.16           O  
ANISOU 1725  O   GLU A 221    13207  10702  17185    430  -1692    574       O  
ATOM   1726  CB  GLU A 221      80.441  70.355  39.359  1.00112.12           C  
ANISOU 1726  CB  GLU A 221    13390  11099  18110    503  -1591    103       C  
ATOM   1727  CG  GLU A 221      81.404  69.696  40.325  1.00118.73           C  
ANISOU 1727  CG  GLU A 221    14336  12085  18692    482  -1286     37       C  
ATOM   1728  CD  GLU A 221      80.974  68.290  40.696  1.00123.95           C  
ANISOU 1728  CD  GLU A 221    15023  12869  19202    462  -1081   -116       C  
ATOM   1729  OE1 GLU A 221      80.206  67.680  39.921  1.00122.19           O  
ANISOU 1729  OE1 GLU A 221    14797  12663  18968    454  -1176   -109       O  
ATOM   1730  OE2 GLU A 221      81.402  67.796  41.760  1.00125.08           O1-
ANISOU 1730  OE2 GLU A 221    15196  13091  19237    446   -833   -237       O1-
ATOM   1731  N   SER A 222      81.821  72.090  36.762  1.00115.01           N  
ANISOU 1731  N   SER A 222    13988  11397  18313    417  -2164    736       N  
ATOM   1732  CA  SER A 222      82.878  72.020  35.759  1.00117.98           C  
ANISOU 1732  CA  SER A 222    14571  11894  18361    333  -2235    990       C  
ATOM   1733  C   SER A 222      83.399  73.401  35.383  1.00119.33           C  
ANISOU 1733  C   SER A 222    14752  11947  18643    314  -2457   1177       C  
ATOM   1734  O   SER A 222      84.413  73.526  34.695  1.00119.80           O  
ANISOU 1734  O   SER A 222    14977  12101  18440    237  -2500   1382       O  
ATOM   1735  CB  SER A 222      82.366  71.309  34.506  1.00119.20           C  
ANISOU 1735  CB  SER A 222    14804  12117  18370    267  -2380   1095       C  
ATOM   1736  OG  SER A 222      81.265  72.002  33.944  1.00118.16           O  
ANISOU 1736  OG  SER A 222    14540  11809  18547    277  -2679   1130       O  
ATOM   1737  N   ASP A 223      82.702  74.435  35.840  1.00120.10           N  
ANISOU 1737  N   ASP A 223    14666  11833  19135    379  -2594   1097       N  
ATOM   1738  CA  ASP A 223      83.026  75.804  35.460  1.00121.76           C  
ANISOU 1738  CA  ASP A 223    14865  11894  19505    365  -2842   1269       C  
ATOM   1739  C   ASP A 223      84.025  76.448  36.417  1.00122.33           C  
ANISOU 1739  C   ASP A 223    14952  11961  19567    387  -2682   1240       C  
ATOM   1740  O   ASP A 223      84.204  77.664  36.412  1.00123.27           O  
ANISOU 1740  O   ASP A 223    15025  11926  19886    394  -2853   1326       O  
ATOM   1741  CB  ASP A 223      81.752  76.649  35.392  1.00122.79           C  
ANISOU 1741  CB  ASP A 223    14780  11774  20099    426  -3100   1207       C  
ATOM   1742  CG  ASP A 223      80.690  76.034  34.499  1.00124.36           C  
ANISOU 1742  CG  ASP A 223    14947  11969  20335    404  -3268   1228       C  
ATOM   1743  OD1 ASP A 223      80.982  75.020  33.831  1.00128.79           O  
ANISOU 1743  OD1 ASP A 223    15669  12719  20545    329  -3202   1312       O  
ATOM   1744  OD2 ASP A 223      79.560  76.565  34.467  1.00121.66           O1-
ANISOU 1744  OD2 ASP A 223    14412  11430  20382    460  -3466   1156       O1-
ATOM   1745  N   CYS A 224      84.675  75.629  37.236  1.00121.11           N  
ANISOU 1745  N   CYS A 224    14865  11970  19183    392  -2364   1125       N  
ATOM   1746  CA  CYS A 224      85.646  76.132  38.202  1.00116.88           C  
ANISOU 1746  CA  CYS A 224    14348  11448  18613    403  -2195   1092       C  
ATOM   1747  C   CYS A 224      86.913  76.625  37.515  1.00113.08           C  
ANISOU 1747  C   CYS A 224    14038  11038  17887    327  -2280   1352       C  
ATOM   1748  O   CYS A 224      87.229  76.206  36.402  1.00116.20           O  
ANISOU 1748  O   CYS A 224    14572  11541  18036    254  -2375   1531       O  
ATOM   1749  CB  CYS A 224      86.001  75.048  39.220  1.00113.40           C  
ANISOU 1749  CB  CYS A 224    13940  11168  17978    414  -1849    917       C  
ATOM   1750  SG  CYS A 224      84.638  74.559  40.295  1.00112.00           S  
ANISOU 1750  SG  CYS A 224    13560  10916  18079    482  -1701    583       S  
ATOM   1751  N   LEU A 225      87.635  77.519  38.183  1.00109.84           N  
ANISOU 1751  N   LEU A 225    13619  10572  17543    335  -2240   1364       N  
ATOM   1752  CA  LEU A 225      88.931  77.971  37.692  1.00106.01           C  
ANISOU 1752  CA  LEU A 225    13293  10169  16816    259  -2282   1590       C  
ATOM   1753  C   LEU A 225      90.003  76.995  38.155  1.00104.99           C  
ANISOU 1753  C   LEU A 225    13290  10266  16335    234  -1984   1569       C  
ATOM   1754  O   LEU A 225      90.853  76.568  37.375  1.00110.71           O  
ANISOU 1754  O   LEU A 225    14172  11145  16748    162  -1974   1735       O  
ATOM   1755  CB  LEU A 225      89.246  79.380  38.201  1.00 96.37           C  
ANISOU 1755  CB  LEU A 225    12007   8784  15826    274  -2376   1617       C  
ATOM   1756  CG  LEU A 225      88.211  80.473  37.918  1.00 91.18           C  
ANISOU 1756  CG  LEU A 225    11198   7865  15580    313  -2670   1618       C  
ATOM   1757  CD1 LEU A 225      88.607  81.773  38.597  1.00 85.29           C  
ANISOU 1757  CD1 LEU A 225    10388   6964  15053    333  -2710   1611       C  
ATOM   1758  CD2 LEU A 225      88.022  80.681  36.421  1.00 91.20           C  
ANISOU 1758  CD2 LEU A 225    11285   7843  15525    241  -2982   1864       C  
ATOM   1759  N   VAL A 226      89.948  76.643  39.435  1.00100.19           N  
ANISOU 1759  N   VAL A 226    12606   9673  15788    287  -1744   1359       N  
ATOM   1760  CA  VAL A 226      90.870  75.677  40.014  1.00102.63           C  
ANISOU 1760  CA  VAL A 226    13016  10177  15804    270  -1466   1323       C  
ATOM   1761  C   VAL A 226      90.139  74.810  41.032  1.00105.04           C  
ANISOU 1761  C   VAL A 226    13228  10498  16186    318  -1258   1071       C  
ATOM   1762  O   VAL A 226      89.370  75.317  41.848  1.00114.45           O  
ANISOU 1762  O   VAL A 226    14270  11551  17663    360  -1248    896       O  
ATOM   1763  CB  VAL A 226      92.052  76.376  40.706  1.00108.26           C  
ANISOU 1763  CB  VAL A 226    13770  10910  16453    247  -1375   1378       C  
ATOM   1764  CG1 VAL A 226      92.959  75.353  41.370  1.00113.47           C  
ANISOU 1764  CG1 VAL A 226    14517  11759  16838    232  -1098   1336       C  
ATOM   1765  CG2 VAL A 226      92.831  77.215  39.708  1.00111.57           C  
ANISOU 1765  CG2 VAL A 226    14290  11326  16775    185  -1571   1629       C  
ATOM   1766  N   CYS A 227      90.372  73.503  40.979  1.00 93.75           N  
ANISOU 1766  N   CYS A 227    11885   9233  14504    305  -1091   1047       N  
ATOM   1767  CA  CYS A 227      89.745  72.589  41.924  1.00 83.50           C  
ANISOU 1767  CA  CYS A 227    10520   7965  13242    333   -891    823       C  
ATOM   1768  C   CYS A 227      90.254  72.858  43.333  1.00 89.55           C  
ANISOU 1768  C   CYS A 227    11250   8731  14043    328   -701    706       C  
ATOM   1769  O   CYS A 227      91.426  73.183  43.525  1.00 88.11           O  
ANISOU 1769  O   CYS A 227    11153   8612  13715    299   -649    821       O  
ATOM   1770  CB  CYS A 227      90.018  71.137  41.533  1.00 74.87           C  
ANISOU 1770  CB  CYS A 227     9544   7046  11858    314   -760    843       C  
ATOM   1771  SG  CYS A 227      89.263  70.636  39.973  1.00166.95           S  
ANISOU 1771  SG  CYS A 227    21245  18720  23467    302   -952    938       S  
ATOM   1772  N   ARG A 228      89.370  72.726  44.315  1.00 97.50           N  
ANISOU 1772  N   ARG A 228    12133   9673  15241    346   -595    475       N  
ATOM   1773  CA  ARG A 228      89.734  72.979  45.704  1.00103.59           C  
ANISOU 1773  CA  ARG A 228    12866  10443  16052    319   -412    343       C  
ATOM   1774  C   ARG A 228      90.262  71.717  46.382  1.00 98.78           C  
ANISOU 1774  C   ARG A 228    12349   9999  15184    280   -175    294       C  
ATOM   1775  O   ARG A 228      91.116  71.787  47.266  1.00 92.25           O  
ANISOU 1775  O   ARG A 228    11565   9228  14256    237    -36    292       O  
ATOM   1776  CB  ARG A 228      88.540  73.543  46.479  1.00112.17           C  
ANISOU 1776  CB  ARG A 228    13767  11374  17479    337   -407    102       C  
ATOM   1777  CG  ARG A 228      88.908  74.148  47.825  1.00121.93           C  
ANISOU 1777  CG  ARG A 228    14954  12579  18794    294   -255    -27       C  
ATOM   1778  CD  ARG A 228      87.737  74.901  48.436  1.00131.60           C  
ANISOU 1778  CD  ARG A 228    15980  13629  20391    312   -274   -264       C  
ATOM   1779  NE  ARG A 228      86.647  74.006  48.812  1.00143.20           N  
ANISOU 1779  NE  ARG A 228    17368  15118  21924    306   -164   -477       N  
ATOM   1780  CZ  ARG A 228      86.572  73.373  49.978  1.00152.83           C  
ANISOU 1780  CZ  ARG A 228    18582  16418  23068    235     72   -661       C  
ATOM   1781  NH1 ARG A 228      87.527  73.534  50.885  1.00154.35           N1+
ANISOU 1781  NH1 ARG A 228    18846  16677  23121    164    218   -652       N1+
ATOM   1782  NH2 ARG A 228      85.544  72.577  50.238  1.00156.22           N  
ANISOU 1782  NH2 ARG A 228    18938  16863  23555    223    158   -848       N  
ATOM   1783  N   LYS A 229      89.749  70.566  45.959  1.00 98.16           N  
ANISOU 1783  N   LYS A 229    12302   9993  15003    290   -140    260       N  
ATOM   1784  CA  LYS A 229      90.163  69.282  46.516  1.00 97.42           C  
ANISOU 1784  CA  LYS A 229    12296  10042  14679    255     64    218       C  
ATOM   1785  C   LYS A 229      90.672  68.333  45.437  1.00 96.52           C  
ANISOU 1785  C   LYS A 229    12313  10047  14314    267     41    376       C  
ATOM   1786  O   LYS A 229      91.858  68.325  45.113  1.00100.73           O  
ANISOU 1786  O   LYS A 229    12952  10664  14657    256     52    542       O  
ATOM   1787  CB  LYS A 229      89.008  68.631  47.279  1.00107.21           C  
ANISOU 1787  CB  LYS A 229    13444  11260  16033    240    177    -22       C  
ATOM   1788  CG  LYS A 229      89.016  68.886  48.778  1.00115.24           C  
ANISOU 1788  CG  LYS A 229    14401  12259  17126    178    344   -191       C  
ATOM   1789  CD  LYS A 229      90.068  68.032  49.471  1.00121.06           C  
ANISOU 1789  CD  LYS A 229    15266  13137  17594    118    519   -139       C  
ATOM   1790  CE  LYS A 229      89.871  68.021  50.980  1.00125.87           C  
ANISOU 1790  CE  LYS A 229    15826  13746  18254     28    694   -330       C  
ATOM   1791  NZ  LYS A 229      90.858  67.139  51.665  1.00124.72           N1+
ANISOU 1791  NZ  LYS A 229    15806  13730  17853    -39    845   -267       N1+
ATOM   1792  N   PHE A 230      89.768  67.529  44.887  1.00 97.40           N  
ANISOU 1792  N   PHE A 230    12412  10167  14429    285     16    313       N  
ATOM   1793  CA  PHE A 230      90.134  66.546  43.874  1.00 94.58           C  
ANISOU 1793  CA  PHE A 230    12175   9921  13841    287      8    432       C  
ATOM   1794  C   PHE A 230      89.686  66.973  42.483  1.00102.37           C  
ANISOU 1794  C   PHE A 230    13161  10861  14874    304   -212    544       C  
ATOM   1795  O   PHE A 230      88.739  67.746  42.332  1.00106.13           O  
ANISOU 1795  O   PHE A 230    13523  11209  15591    324   -359    491       O  
ATOM   1796  CB  PHE A 230      89.540  65.178  44.212  1.00 85.53           C  
ANISOU 1796  CB  PHE A 230    11042   8835  12621    279    148    294       C  
ATOM   1797  CG  PHE A 230      90.095  64.571  45.464  1.00 86.83           C  
ANISOU 1797  CG  PHE A 230    11240   9063  12689    243    355    218       C  
ATOM   1798  CD1 PHE A 230      89.605  64.941  46.705  1.00 96.69           C  
ANISOU 1798  CD1 PHE A 230    12393  10251  14094    211    439     51       C  
ATOM   1799  CD2 PHE A 230      91.107  63.632  45.403  1.00 87.24           C  
ANISOU 1799  CD2 PHE A 230    11415   9233  12500    232    463    311       C  
ATOM   1800  CE1 PHE A 230      90.116  64.384  47.863  1.00 97.94           C  
ANISOU 1800  CE1 PHE A 230    12592  10472  14149    156    618     -9       C  
ATOM   1801  CE2 PHE A 230      91.621  63.071  46.555  1.00 94.32           C  
ANISOU 1801  CE2 PHE A 230    12342  10179  13315    192    631    257       C  
ATOM   1802  CZ  PHE A 230      91.124  63.448  47.787  1.00 96.02           C  
ANISOU 1802  CZ  PHE A 230    12475  10340  13667    147    704    104       C  
ATOM   1803  N   ARG A 231      90.375  66.459  41.470  1.00104.75           N  
ANISOU 1803  N   ARG A 231    13588  11266  14948    287   -237    698       N  
ATOM   1804  CA  ARG A 231      90.057  66.771  40.085  1.00108.33           C  
ANISOU 1804  CA  ARG A 231    14067  11699  15393    273   -442    823       C  
ATOM   1805  C   ARG A 231      89.700  65.504  39.317  1.00109.25           C  
ANISOU 1805  C   ARG A 231    14256  11906  15347    257   -408    809       C  
ATOM   1806  O   ARG A 231      90.573  64.712  38.965  1.00116.21           O  
ANISOU 1806  O   ARG A 231    15255  12913  15986    235   -302    879       O  
ATOM   1807  CB  ARG A 231      91.238  67.476  39.414  1.00112.79           C  
ANISOU 1807  CB  ARG A 231    14724  12308  15824    238   -523   1031       C  
ATOM   1808  CG  ARG A 231      91.011  67.814  37.952  1.00121.70           C  
ANISOU 1808  CG  ARG A 231    15902  13429  16911    194   -741   1180       C  
ATOM   1809  CD  ARG A 231      92.243  68.458  37.339  1.00135.73           C  
ANISOU 1809  CD  ARG A 231    17777  15265  18529    140   -798   1379       C  
ATOM   1810  NE  ARG A 231      92.037  68.795  35.933  1.00154.45           N  
ANISOU 1810  NE  ARG A 231    20208  17636  20841     71  -1013   1529       N  
ATOM   1811  CZ  ARG A 231      91.537  69.951  35.507  1.00169.34           C  
ANISOU 1811  CZ  ARG A 231    22041  19390  22908     53  -1256   1614       C  
ATOM   1812  NH1 ARG A 231      91.191  70.888  36.380  1.00173.06           N1+
ANISOU 1812  NH1 ARG A 231    22392  19717  23646    109  -1304   1549       N1+
ATOM   1813  NH2 ARG A 231      91.383  70.172  34.208  1.00174.35           N  
ANISOU 1813  NH2 ARG A 231    22746  20037  23463    -31  -1455   1763       N  
ATOM   1814  N   ASP A 232      88.409  65.312  39.070  1.00107.21           N  
ANISOU 1814  N   ASP A 232    13920  11580  15233    269   -496    711       N  
ATOM   1815  CA  ASP A 232      87.946  64.168  38.298  1.00110.39           C  
ANISOU 1815  CA  ASP A 232    14386  12058  15498    247   -481    693       C  
ATOM   1816  C   ASP A 232      87.740  64.580  36.848  1.00108.25           C  
ANISOU 1816  C   ASP A 232    14160  11779  15191    200   -707    847       C  
ATOM   1817  O   ASP A 232      86.631  64.926  36.442  1.00106.38           O  
ANISOU 1817  O   ASP A 232    13839  11447  15132    202   -879    821       O  
ATOM   1818  CB  ASP A 232      86.646  63.611  38.881  1.00119.16           C  
ANISOU 1818  CB  ASP A 232    15392  13115  16770    273   -436    492       C  
ATOM   1819  CG  ASP A 232      86.201  62.333  38.196  1.00128.38           C  
ANISOU 1819  CG  ASP A 232    16631  14365  17784    248   -397    461       C  
ATOM   1820  OD1 ASP A 232      87.026  61.717  37.489  1.00134.05           O  
ANISOU 1820  OD1 ASP A 232    17485  15195  18255    215   -349    568       O  
ATOM   1821  OD2 ASP A 232      85.027  61.943  38.367  1.00129.26           O1-
ANISOU 1821  OD2 ASP A 232    16658  14429  18024    257   -409    322       O1-
ATOM   1822  N   GLU A 233      88.820  64.544  36.075  1.00110.40           N  
ANISOU 1822  N   GLU A 233    14563  12152  15232    149   -709   1008       N  
ATOM   1823  CA  GLU A 233      88.782  64.966  34.681  1.00118.00           C  
ANISOU 1823  CA  GLU A 233    15590  13124  16119     74   -918   1172       C  
ATOM   1824  C   GLU A 233      88.212  66.374  34.530  1.00121.01           C  
ANISOU 1824  C   GLU A 233    15875  13352  16753     77  -1169   1242       C  
ATOM   1825  O   GLU A 233      88.838  67.355  34.933  1.00122.99           O  
ANISOU 1825  O   GLU A 233    16104  13552  17074     90  -1201   1308       O  
ATOM   1826  CB  GLU A 233      87.979  63.976  33.833  1.00125.96           C  
ANISOU 1826  CB  GLU A 233    16640  14183  17037     34   -949   1135       C  
ATOM   1827  CG  GLU A 233      88.682  62.649  33.594  1.00134.66           C  
ANISOU 1827  CG  GLU A 233    17866  15440  17857      7   -740   1110       C  
ATOM   1828  CD  GLU A 233      87.925  61.752  32.632  1.00141.73           C  
ANISOU 1828  CD  GLU A 233    18814  16385  18651    -51   -785   1086       C  
ATOM   1829  OE1 GLU A 233      86.686  61.885  32.541  1.00141.18           O  
ANISOU 1829  OE1 GLU A 233    18658  16227  18758    -42   -922   1029       O  
ATOM   1830  OE2 GLU A 233      88.570  60.913  31.968  1.00145.10           O1-
ANISOU 1830  OE2 GLU A 233    19364  16939  18827   -108   -681   1118       O1-
ATOM   1831  N   ALA A 234      87.018  66.461  33.954  1.00119.60           N  
ANISOU 1831  N   ALA A 234    15632  13092  16718     66  -1353   1226       N  
ATOM   1832  CA  ALA A 234      86.409  67.747  33.626  1.00117.87           C  
ANISOU 1832  CA  ALA A 234    15321  12713  16750     63  -1629   1309       C  
ATOM   1833  C   ALA A 234      85.949  68.527  34.855  1.00118.49           C  
ANISOU 1833  C   ALA A 234    15228  12639  17152    158  -1614   1172       C  
ATOM   1834  O   ALA A 234      86.072  69.752  34.902  1.00119.30           O  
ANISOU 1834  O   ALA A 234    15276  12624  17428    166  -1769   1254       O  
ATOM   1835  CB  ALA A 234      85.245  67.546  32.662  1.00114.53           C  
ANISOU 1835  CB  ALA A 234    14872  12247  16398     20  -1836   1331       C  
ATOM   1836  N   THR A 235      85.423  67.816  35.846  1.00114.23           N  
ANISOU 1836  N   THR A 235    14607  12103  16692    220  -1424    960       N  
ATOM   1837  CA  THR A 235      84.799  68.457  36.999  1.00104.73           C  
ANISOU 1837  CA  THR A 235    13230  10759  15804    294  -1398    793       C  
ATOM   1838  C   THR A 235      85.624  68.333  38.276  1.00 96.68           C  
ANISOU 1838  C   THR A 235    12220   9791  14722    321  -1143    696       C  
ATOM   1839  O   THR A 235      86.453  67.433  38.408  1.00 93.98           O  
ANISOU 1839  O   THR A 235    12001   9597  14112    299   -956    713       O  
ATOM   1840  CB  THR A 235      83.400  67.875  37.261  1.00102.51           C  
ANISOU 1840  CB  THR A 235    12820  10424  15706    327  -1388    599       C  
ATOM   1841  CG2 THR A 235      82.494  68.105  36.063  1.00101.93           C  
ANISOU 1841  CG2 THR A 235    12714  10279  15737    300  -1665    692       C  
ATOM   1842  OG1 THR A 235      83.509  66.468  37.505  1.00100.42           O  
ANISOU 1842  OG1 THR A 235    12638  10305  15212    313  -1164    506       O  
ATOM   1843  N   CYS A 236      85.383  69.246  39.213  1.00 98.97           N  
ANISOU 1843  N   CYS A 236    12377   9954  15273    363  -1142    594       N  
ATOM   1844  CA  CYS A 236      86.041  69.222  40.515  1.00100.03           C  
ANISOU 1844  CA  CYS A 236    12506  10123  15377    375   -913    488       C  
ATOM   1845  C   CYS A 236      85.193  68.459  41.524  1.00102.48           C  
ANISOU 1845  C   CYS A 236    12723  10436  15781    391   -734    239       C  
ATOM   1846  O   CYS A 236      84.013  68.754  41.702  1.00109.38           O  
ANISOU 1846  O   CYS A 236    13442  11191  16926    419   -808     96       O  
ATOM   1847  CB  CYS A 236      86.278  70.645  41.027  1.00100.20           C  
ANISOU 1847  CB  CYS A 236    12442  10011  15620    394   -995    501       C  
ATOM   1848  SG  CYS A 236      87.484  71.608  40.090  1.00104.65           S  
ANISOU 1848  SG  CYS A 236    13128  10582  16053    357  -1170    791       S  
ATOM   1849  N   LYS A 237      85.798  67.480  42.187  1.00 97.26           N  
ANISOU 1849  N   LYS A 237    12149   9905  14899    368   -502    187       N  
ATOM   1850  CA  LYS A 237      85.083  66.676  43.169  1.00 92.66           C  
ANISOU 1850  CA  LYS A 237    11501   9341  14364    361   -322    -38       C  
ATOM   1851  C   LYS A 237      85.668  66.869  44.561  1.00 94.51           C  
ANISOU 1851  C   LYS A 237    11722   9590  14596    335   -130   -136       C  
ATOM   1852  O   LYS A 237      86.856  67.152  44.708  1.00 96.00           O  
ANISOU 1852  O   LYS A 237    12003   9831  14642    322    -90     -8       O  
ATOM   1853  CB  LYS A 237      85.137  65.195  42.790  1.00 82.33           C  
ANISOU 1853  CB  LYS A 237    10310   8169  12802    338   -217    -29       C  
ATOM   1854  CG  LYS A 237      84.612  64.885  41.401  1.00 79.28           C  
ANISOU 1854  CG  LYS A 237     9956   7789  12377    343   -389     67       C  
ATOM   1855  CD  LYS A 237      83.137  65.213  41.284  1.00 86.79           C  
ANISOU 1855  CD  LYS A 237    10745   8619  13614    365   -519    -64       C  
ATOM   1856  CE  LYS A 237      82.598  64.824  39.919  1.00 93.43           C  
ANISOU 1856  CE  LYS A 237    11626   9474  14399    354   -692     37       C  
ATOM   1857  NZ  LYS A 237      82.870  63.394  39.604  1.00 94.75           N1+
ANISOU 1857  NZ  LYS A 237    11934   9790  14278    321   -555     46       N1+
ATOM   1858  N   ASP A 238      84.828  66.719  45.579  1.00 92.28           N  
ANISOU 1858  N   ASP A 238    11326   9266  14470    317    -13   -366       N  
ATOM   1859  CA  ASP A 238      85.297  66.740  46.957  1.00 90.19           C  
ANISOU 1859  CA  ASP A 238    11060   9032  14177    265    185   -477       C  
ATOM   1860  C   ASP A 238      85.854  65.370  47.315  1.00 83.34           C  
ANISOU 1860  C   ASP A 238    10329   8314  13021    217    364   -465       C  
ATOM   1861  O   ASP A 238      86.780  65.251  48.115  1.00 75.20           O  
ANISOU 1861  O   ASP A 238     9371   7348  11853    172    497   -439       O  
ATOM   1862  CB  ASP A 238      84.159  67.107  47.912  1.00 95.76           C  
ANISOU 1862  CB  ASP A 238    11588   9641  15156    241    250   -742       C  
ATOM   1863  CG  ASP A 238      84.590  67.084  49.369  1.00102.07           C  
ANISOU 1863  CG  ASP A 238    12393  10481  15906    158    463   -870       C  
ATOM   1864  OD1 ASP A 238      85.766  67.393  49.651  1.00107.29           O  
ANISOU 1864  OD1 ASP A 238    13149  11187  16428    138    501   -741       O  
ATOM   1865  OD2 ASP A 238      83.750  66.759  50.233  1.00102.57           O1-
ANISOU 1865  OD2 ASP A 238    12367  10537  16068    101    592  -1099       O1-
ATOM   1866  N   THR A 239      85.277  64.338  46.706  1.00 88.77           N  
ANISOU 1866  N   THR A 239    11050   9050  13627    226    358   -482       N  
ATOM   1867  CA  THR A 239      85.671  62.959  46.961  1.00 91.48           C  
ANISOU 1867  CA  THR A 239    11517   9518  13722    186    513   -479       C  
ATOM   1868  C   THR A 239      85.476  62.125  45.701  1.00 97.29           C  
ANISOU 1868  C   THR A 239    12330  10304  14332    220    430   -384       C  
ATOM   1869  O   THR A 239      84.385  62.097  45.131  1.00107.00           O  
ANISOU 1869  O   THR A 239    13482  11483  15693    239    330   -453       O  
ATOM   1870  CB  THR A 239      84.834  62.341  48.096  1.00 96.12           C  
ANISOU 1870  CB  THR A 239    12042  10112  14368    118    672   -711       C  
ATOM   1871  CG2 THR A 239      85.318  60.937  48.414  1.00 99.10           C  
ANISOU 1871  CG2 THR A 239    12557  10607  14491     70    819   -692       C  
ATOM   1872  OG1 THR A 239      84.937  63.154  49.271  1.00102.77           O  
ANISOU 1872  OG1 THR A 239    12808  10909  15332     68    754   -820       O  
ATOM   1873  N   CYS A 240      86.533  61.446  45.268  1.00 91.16           N  
ANISOU 1873  N   CYS A 240    11701   9628  13309    222    474   -232       N  
ATOM   1874  CA  CYS A 240      86.464  60.620  44.068  1.00 87.75           C  
ANISOU 1874  CA  CYS A 240    11354   9252  12734    240    415   -146       C  
ATOM   1875  C   CYS A 240      85.360  59.571  44.178  1.00 85.30           C  
ANISOU 1875  C   CYS A 240    11020   8953  12437    218    475   -302       C  
ATOM   1876  O   CYS A 240      85.183  58.960  45.232  1.00 84.90           O  
ANISOU 1876  O   CYS A 240    10964   8923  12371    175    627   -432       O  
ATOM   1877  CB  CYS A 240      87.812  59.946  43.798  1.00 88.52           C  
ANISOU 1877  CB  CYS A 240    11602   9456  12574    239    498      2       C  
ATOM   1878  SG  CYS A 240      89.163  61.093  43.434  1.00122.67           S  
ANISOU 1878  SG  CYS A 240    15969  13790  16852    257    419    205       S  
ATOM   1879  N   PRO A 241      84.612  59.365  43.082  1.00 87.45           N  
ANISOU 1879  N   PRO A 241    11282   9213  12731    235    349   -285       N  
ATOM   1880  CA  PRO A 241      83.509  58.401  43.011  1.00 89.47           C  
ANISOU 1880  CA  PRO A 241    11514   9479  13002    214    382   -423       C  
ATOM   1881  C   PRO A 241      83.903  57.029  43.548  1.00 88.35           C  
ANISOU 1881  C   PRO A 241    11482   9426  12660    177    571   -466       C  
ATOM   1882  O   PRO A 241      84.790  56.384  42.990  1.00 86.60           O  
ANISOU 1882  O   PRO A 241    11391   9278  12235    185    604   -343       O  
ATOM   1883  CB  PRO A 241      83.222  58.317  41.512  1.00 87.38           C  
ANISOU 1883  CB  PRO A 241    11288   9223  12690    230    217   -311       C  
ATOM   1884  CG  PRO A 241      83.618  59.646  40.988  1.00 89.11           C  
ANISOU 1884  CG  PRO A 241    11473   9383  13003    258     50   -174       C  
ATOM   1885  CD  PRO A 241      84.804  60.077  41.806  1.00 89.99           C  
ANISOU 1885  CD  PRO A 241    11622   9514  13056    262    156   -121       C  
ATOM   1886  N   PRO A 242      83.244  56.588  44.628  1.00 89.14           N  
ANISOU 1886  N   PRO A 242    11527   9516  12825    131    692   -644       N  
ATOM   1887  CA  PRO A 242      83.531  55.307  45.279  1.00 87.57           C  
ANISOU 1887  CA  PRO A 242    11428   9387  12458     82    861   -692       C  
ATOM   1888  C   PRO A 242      83.409  54.140  44.309  1.00 87.49           C  
ANISOU 1888  C   PRO A 242    11518   9430  12293     89    854   -650       C  
ATOM   1889  O   PRO A 242      82.585  54.185  43.397  1.00 92.04           O  
ANISOU 1889  O   PRO A 242    12055   9988  12929    105    740   -664       O  
ATOM   1890  CB  PRO A 242      82.440  55.209  46.349  1.00 91.07           C  
ANISOU 1890  CB  PRO A 242    11765   9796  13040     16    943   -910       C  
ATOM   1891  CG  PRO A 242      82.049  56.620  46.619  1.00 97.13           C  
ANISOU 1891  CG  PRO A 242    12383  10479  14043     35    862   -965       C  
ATOM   1892  CD  PRO A 242      82.162  57.323  45.304  1.00 94.37           C  
ANISOU 1892  CD  PRO A 242    12023  10095  13739    114    672   -817       C  
ATOM   1893  N   LEU A 243      84.225  53.110  44.504  1.00 83.54           N  
ANISOU 1893  N   LEU A 243    11146   8993  11604     74    970   -600       N  
ATOM   1894  CA  LEU A 243      84.150  51.920  43.670  1.00 81.63           C  
ANISOU 1894  CA  LEU A 243    11002   8797  11215     76    986   -579       C  
ATOM   1895  C   LEU A 243      82.805  51.241  43.875  1.00 80.17           C  
ANISOU 1895  C   LEU A 243    10772   8599  11092     28   1010   -747       C  
ATOM   1896  O   LEU A 243      82.269  50.610  42.964  1.00 83.44           O  
ANISOU 1896  O   LEU A 243    11218   9030  11454     29    965   -755       O  
ATOM   1897  CB  LEU A 243      85.280  50.946  44.008  1.00 81.58           C  
ANISOU 1897  CB  LEU A 243    11124   8840  11031     71   1113   -510       C  
ATOM   1898  CG  LEU A 243      86.706  51.380  43.666  1.00 75.25           C  
ANISOU 1898  CG  LEU A 243    10381   8067  10143    118   1104   -339       C  
ATOM   1899  CD1 LEU A 243      87.689  50.267  43.994  1.00 71.37           C  
ANISOU 1899  CD1 LEU A 243    10000   7613   9505    116   1227   -292       C  
ATOM   1900  CD2 LEU A 243      86.808  51.778  42.203  1.00 70.37           C  
ANISOU 1900  CD2 LEU A 243     9780   7469   9487    157    983   -238       C  
ATOM   1901  N   MET A 244      82.266  51.375  45.081  1.00 79.86           N  
ANISOU 1901  N   MET A 244    10656   8532  11155    -27   1085   -887       N  
ATOM   1902  CA  MET A 244      80.987  50.768  45.419  1.00 82.74           C  
ANISOU 1902  CA  MET A 244    10966   8888  11584    -88   1124  -1064       C  
ATOM   1903  C   MET A 244      80.116  51.707  46.245  1.00 83.66           C  
ANISOU 1903  C   MET A 244    10918   8950  11919   -122   1118  -1218       C  
ATOM   1904  O   MET A 244      80.602  52.405  47.134  1.00 90.78           O  
ANISOU 1904  O   MET A 244    11785   9835  12871   -141   1167  -1226       O  
ATOM   1905  CB  MET A 244      81.196  49.448  46.163  1.00 82.41           C  
ANISOU 1905  CB  MET A 244    11032   8887  11392   -158   1273  -1111       C  
ATOM   1906  CG  MET A 244      81.748  48.330  45.296  1.00 63.40           C  
ANISOU 1906  CG  MET A 244     8769   6520   8802   -129   1284  -1009       C  
ATOM   1907  SD  MET A 244      81.708  46.741  46.141  1.00149.32           S  
ANISOU 1907  SD  MET A 244    19761  17424  19550   -217   1434  -1084       S  
ATOM   1908  CE  MET A 244      82.754  47.085  47.555  1.00 62.41           C  
ANISOU 1908  CE  MET A 244     8775   6413   8523   -261   1524  -1038       C  
ATOM   1909  N   LEU A 245      78.823  51.718  45.942  1.00 76.44           N  
ANISOU 1909  N   LEU A 245     9897   8007  11139   -134   1061  -1348       N  
ATOM   1910  CA  LEU A 245      77.879  52.574  46.642  1.00 78.11           C  
ANISOU 1910  CA  LEU A 245     9930   8160  11588   -163   1057  -1520       C  
ATOM   1911  C   LEU A 245      76.939  51.736  47.496  1.00 73.60           C  
ANISOU 1911  C   LEU A 245     9329   7614  11023   -270   1187  -1725       C  
ATOM   1912  O   LEU A 245      76.597  50.612  47.136  1.00 71.05           O  
ANISOU 1912  O   LEU A 245     9085   7333  10578   -298   1214  -1738       O  
ATOM   1913  CB  LEU A 245      77.074  53.404  45.643  1.00 78.45           C  
ANISOU 1913  CB  LEU A 245     9843   8137  11830    -94    870  -1517       C  
ATOM   1914  CG  LEU A 245      77.885  54.267  44.676  1.00 79.94           C  
ANISOU 1914  CG  LEU A 245    10062   8298  12014     -5    716  -1310       C  
ATOM   1915  CD1 LEU A 245      77.008  54.759  43.536  1.00 84.47           C  
ANISOU 1915  CD1 LEU A 245    10539   8815  12740     42    514  -1287       C  
ATOM   1916  CD2 LEU A 245      78.535  55.432  45.406  1.00 78.93           C  
ANISOU 1916  CD2 LEU A 245     9876   8123  11992     12    727  -1290       C  
ATOM   1917  N   TYR A 246      76.525  52.287  48.630  1.00 74.45           N  
ANISOU 1917  N   TYR A 246     9322   7696  11268   -339   1273  -1889       N  
ATOM   1918  CA  TYR A 246      75.604  51.592  49.517  1.00 73.31           C  
ANISOU 1918  CA  TYR A 246     9138   7582  11136   -462   1406  -2101       C  
ATOM   1919  C   TYR A 246      74.178  51.688  48.985  1.00 76.14           C  
ANISOU 1919  C   TYR A 246     9339   7902  11687   -450   1328  -2248       C  
ATOM   1920  O   TYR A 246      73.743  52.745  48.531  1.00 80.29           O  
ANISOU 1920  O   TYR A 246     9714   8353  12438   -374   1203  -2267       O  
ATOM   1921  CB  TYR A 246      75.699  52.165  50.932  1.00 78.90           C  
ANISOU 1921  CB  TYR A 246     9782   8285  11911   -562   1537  -2235       C  
ATOM   1922  CG  TYR A 246      74.767  51.526  51.934  1.00 68.93           C  
ANISOU 1922  CG  TYR A 246     8476   7061  10653   -718   1687  -2466       C  
ATOM   1923  CD1 TYR A 246      75.030  50.266  52.451  1.00 90.84           C  
ANISOU 1923  CD1 TYR A 246    11410   9908  13196   -827   1799  -2453       C  
ATOM   1924  CD2 TYR A 246      73.633  52.191  52.376  1.00 86.40           C  
ANISOU 1924  CD2 TYR A 246    10485   9233  13109   -764   1714  -2701       C  
ATOM   1925  CE1 TYR A 246      74.181  49.682  53.372  1.00 90.19           C  
ANISOU 1925  CE1 TYR A 246    11298   9867  13104   -990   1933  -2660       C  
ATOM   1926  CE2 TYR A 246      72.780  51.617  53.296  1.00 85.31           C  
ANISOU 1926  CE2 TYR A 246    10306   9141  12969   -922   1862  -2925       C  
ATOM   1927  CZ  TYR A 246      73.058  50.365  53.791  1.00 87.08           C  
ANISOU 1927  CZ  TYR A 246    10702   9445  12939  -1042   1970  -2899       C  
ATOM   1928  OH  TYR A 246      72.206  49.795  54.708  1.00 88.79           O  
ANISOU 1928  OH  TYR A 246    10885   9711  13140  -1218   2114  -3118       O  
ATOM   1929  N   ASN A 247      73.457  50.574  49.032  1.00 69.52           N  
ANISOU 1929  N   ASN A 247     8537   7111  10765   -525   1393  -2347       N  
ATOM   1930  CA  ASN A 247      72.082  50.533  48.555  1.00 74.91           C  
ANISOU 1930  CA  ASN A 247     9074   7769  11618   -525   1327  -2492       C  
ATOM   1931  C   ASN A 247      71.093  50.653  49.710  1.00 76.15           C  
ANISOU 1931  C   ASN A 247     9082   7926  11925   -646   1459  -2765       C  
ATOM   1932  O   ASN A 247      70.898  49.704  50.467  1.00 74.37           O  
ANISOU 1932  O   ASN A 247     8931   7766  11559   -776   1607  -2865       O  
ATOM   1933  CB  ASN A 247      71.833  49.246  47.768  1.00 79.10           C  
ANISOU 1933  CB  ASN A 247     9731   8353  11972   -535   1306  -2435       C  
ATOM   1934  CG  ASN A 247      70.483  49.231  47.081  1.00 86.45           C  
ANISOU 1934  CG  ASN A 247    10519   9258  13070   -524   1206  -2548       C  
ATOM   1935  ND2 ASN A 247      70.309  48.310  46.141  1.00 95.07           N  
ANISOU 1935  ND2 ASN A 247    11714  10385  14024   -512   1147  -2468       N  
ATOM   1936  OD1 ASN A 247      69.606  50.035  47.390  1.00 89.20           O  
ANISOU 1936  OD1 ASN A 247    10663   9552  13677   -527   1180  -2709       O  
ATOM   1937  N   PRO A 248      70.468  51.832  49.847  1.00 72.93           N  
ANISOU 1937  N   PRO A 248     8460   7441  11809   -611   1405  -2891       N  
ATOM   1938  CA  PRO A 248      69.508  52.133  50.914  1.00 74.16           C  
ANISOU 1938  CA  PRO A 248     8439   7587  12151   -721   1534  -3177       C  
ATOM   1939  C   PRO A 248      68.332  51.165  50.925  1.00 76.41           C  
ANISOU 1939  C   PRO A 248     8682   7920  12431   -812   1590  -3346       C  
ATOM   1940  O   PRO A 248      67.675  51.004  51.952  1.00 78.39           O  
ANISOU 1940  O   PRO A 248     8849   8203  12732   -952   1748  -3580       O  
ATOM   1941  CB  PRO A 248      69.009  53.533  50.549  1.00 75.45           C  
ANISOU 1941  CB  PRO A 248     8374   7632  12660   -614   1397  -3236       C  
ATOM   1942  CG  PRO A 248      70.074  54.114  49.705  1.00 74.58           C  
ANISOU 1942  CG  PRO A 248     8358   7481  12498   -479   1240  -2966       C  
ATOM   1943  CD  PRO A 248      70.666  52.976  48.942  1.00 73.30           C  
ANISOU 1943  CD  PRO A 248     8419   7397  12036   -463   1210  -2765       C  
ATOM   1944  N   THR A 249      68.070  50.530  49.790  1.00 77.96           N  
ANISOU 1944  N   THR A 249     8937   8125  12561   -745   1464  -3232       N  
ATOM   1945  CA  THR A 249      66.923  49.642  49.669  1.00 86.52           C  
ANISOU 1945  CA  THR A 249     9975   9250  13650   -822   1496  -3380       C  
ATOM   1946  C   THR A 249      67.249  48.218  50.106  1.00 89.45           C  
ANISOU 1946  C   THR A 249    10561   9721  13707   -945   1638  -3358       C  
ATOM   1947  O   THR A 249      66.518  47.623  50.897  1.00 92.03           O  
ANISOU 1947  O   THR A 249    10854  10097  14014  -1092   1778  -3555       O  
ATOM   1948  CB  THR A 249      66.380  49.621  48.229  1.00 93.80           C  
ANISOU 1948  CB  THR A 249    10851  10132  14656   -709   1286  -3280       C  
ATOM   1949  CG2 THR A 249      65.202  48.670  48.119  1.00 98.13           C  
ANISOU 1949  CG2 THR A 249    11356  10728  15202   -796   1321  -3432       C  
ATOM   1950  OG1 THR A 249      65.954  50.937  47.860  1.00 99.12           O  
ANISOU 1950  OG1 THR A 249    11310  10700  15652   -606   1137  -3310       O  
ATOM   1951  N   THR A 250      68.350  47.677  49.593  1.00 81.23           N  
ANISOU 1951  N   THR A 250     9734   8703  12426   -891   1601  -3121       N  
ATOM   1952  CA  THR A 250      68.706  46.289  49.863  1.00 77.39           C  
ANISOU 1952  CA  THR A 250     9455   8291  11657   -987   1707  -3075       C  
ATOM   1953  C   THR A 250      69.696  46.136  51.012  1.00 79.63           C  
ANISOU 1953  C   THR A 250     9866   8608  11782  -1078   1849  -3041       C  
ATOM   1954  O   THR A 250      70.105  45.023  51.342  1.00 82.93           O  
ANISOU 1954  O   THR A 250    10461   9075  11974  -1163   1930  -2988       O  
ATOM   1955  CB  THR A 250      69.286  45.613  48.616  1.00 78.44           C  
ANISOU 1955  CB  THR A 250     9752   8431  11621   -887   1595  -2853       C  
ATOM   1956  CG2 THR A 250      68.244  45.564  47.514  1.00 88.45           C  
ANISOU 1956  CG2 THR A 250    10919   9682  13007   -834   1460  -2888       C  
ATOM   1957  OG1 THR A 250      70.425  46.352  48.159  1.00 74.30           O  
ANISOU 1957  OG1 THR A 250     9278   7872  11081   -764   1509  -2654       O  
ATOM   1958  N   TYR A 251      70.074  47.256  51.619  1.00 79.90           N  
ANISOU 1958  N   TYR A 251     9809   8609  11942  -1065   1869  -3068       N  
ATOM   1959  CA  TYR A 251      71.013  47.250  52.737  1.00 80.86           C  
ANISOU 1959  CA  TYR A 251    10038   8761  11927  -1159   1992  -3035       C  
ATOM   1960  C   TYR A 251      72.301  46.507  52.397  1.00 78.17           C  
ANISOU 1960  C   TYR A 251     9925   8438  11336  -1111   1967  -2784       C  
ATOM   1961  O   TYR A 251      72.908  45.868  53.256  1.00 79.00           O  
ANISOU 1961  O   TYR A 251    10169   8583  11265  -1224   2070  -2751       O  
ATOM   1962  CB  TYR A 251      70.364  46.649  53.984  1.00 71.56           C  
ANISOU 1962  CB  TYR A 251     8855   7642  10691  -1376   2167  -3246       C  
ATOM   1963  CG  TYR A 251      69.328  47.548  54.615  1.00 78.60           C  
ANISOU 1963  CG  TYR A 251     9513   8517  11832  -1447   2232  -3514       C  
ATOM   1964  CD1 TYR A 251      69.664  48.400  55.658  1.00 81.57           C  
ANISOU 1964  CD1 TYR A 251     9831   8891  12272  -1526   2329  -3602       C  
ATOM   1965  CD2 TYR A 251      68.016  47.552  54.162  1.00 80.60           C  
ANISOU 1965  CD2 TYR A 251     9598   8757  12268  -1436   2199  -3686       C  
ATOM   1966  CE1 TYR A 251      68.721  49.227  56.238  1.00 85.66           C  
ANISOU 1966  CE1 TYR A 251    10125   9389  13033  -1592   2402  -3867       C  
ATOM   1967  CE2 TYR A 251      67.065  48.376  54.736  1.00 88.29           C  
ANISOU 1967  CE2 TYR A 251    10340   9709  13498  -1495   2264  -3947       C  
ATOM   1968  CZ  TYR A 251      67.423  49.211  55.772  1.00 90.83           C  
ANISOU 1968  CZ  TYR A 251    10604  10024  13883  -1572   2370  -4042       C  
ATOM   1969  OH  TYR A 251      66.482  50.034  56.347  1.00 98.19           O  
ANISOU 1969  OH  TYR A 251    11296  10929  15083  -1634   2447  -4321       O  
ATOM   1970  N   GLN A 252      72.711  46.592  51.137  1.00 71.64           N  
ANISOU 1970  N   GLN A 252     9136   7582  10503   -950   1826  -2609       N  
ATOM   1971  CA  GLN A 252      73.955  45.977  50.700  1.00 76.67           C  
ANISOU 1971  CA  GLN A 252     9968   8231  10932   -888   1801  -2381       C  
ATOM   1972  C   GLN A 252      74.770  46.953  49.866  1.00 85.13           C  
ANISOU 1972  C   GLN A 252    11020   9262  12063   -730   1675  -2209       C  
ATOM   1973  O   GLN A 252      74.387  48.110  49.697  1.00 90.32           O  
ANISOU 1973  O   GLN A 252    11520   9875  12921   -673   1603  -2259       O  
ATOM   1974  CB  GLN A 252      73.680  44.699  49.906  1.00 80.26           C  
ANISOU 1974  CB  GLN A 252    10537   8709  11251   -883   1779  -2339       C  
ATOM   1975  CG  GLN A 252      73.082  43.577  50.735  1.00 89.17           C  
ANISOU 1975  CG  GLN A 252    11726   9878  12275  -1048   1903  -2473       C  
ATOM   1976  CD  GLN A 252      74.020  43.090  51.821  1.00 90.94           C  
ANISOU 1976  CD  GLN A 252    12093  10122  12339  -1149   2007  -2410       C  
ATOM   1977  NE2 GLN A 252      75.319  43.262  51.601  1.00 96.01           N  
ANISOU 1977  NE2 GLN A 252    12830  10747  12904  -1056   1969  -2212       N  
ATOM   1978  OE1 GLN A 252      73.584  42.566  52.846  1.00 86.64           O  
ANISOU 1978  OE1 GLN A 252    11570   9609  11739  -1318   2116  -2535       O  
ATOM   1979  N   MET A 253      75.897  46.483  49.345  1.00 84.13           N  
ANISOU 1979  N   MET A 253    11050   9147  11769   -662   1649  -2009       N  
ATOM   1980  CA  MET A 253      76.786  47.339  48.580  1.00 65.89           C  
ANISOU 1980  CA  MET A 253     8741   6810   9483   -530   1542  -1836       C  
ATOM   1981  C   MET A 253      76.708  47.002  47.094  1.00 91.65           C  
ANISOU 1981  C   MET A 253    12047  10074  12702   -435   1424  -1733       C  
ATOM   1982  O   MET A 253      76.775  45.835  46.709  1.00 91.79           O  
ANISOU 1982  O   MET A 253    12187  10121  12569   -452   1455  -1701       O  
ATOM   1983  CB  MET A 253      78.219  47.186  49.084  1.00 80.27           C  
ANISOU 1983  CB  MET A 253    10694   8648  11157   -528   1600  -1686       C  
ATOM   1984  CG  MET A 253      78.984  48.492  49.193  1.00 83.21           C  
ANISOU 1984  CG  MET A 253    11008   8992  11615   -463   1552  -1599       C  
ATOM   1985  SD  MET A 253      78.420  49.488  50.584  1.00 81.13           S  
ANISOU 1985  SD  MET A 253    10594   8707  11523   -565   1629  -1786       S  
ATOM   1986  CE  MET A 253      78.325  48.238  51.859  1.00 91.63           C  
ANISOU 1986  CE  MET A 253    12032  10090  12693   -745   1796  -1882       C  
ATOM   1987  N   ASP A 254      76.556  48.029  46.264  1.00 93.13           N  
ANISOU 1987  N   ASP A 254    12138  10226  13023   -345   1286  -1681       N  
ATOM   1988  CA  ASP A 254      76.481  47.849  44.818  1.00 90.91           C  
ANISOU 1988  CA  ASP A 254    11896   9949  12698   -274   1159  -1576       C  
ATOM   1989  C   ASP A 254      77.701  48.457  44.143  1.00 82.17           C  
ANISOU 1989  C   ASP A 254    10853   8841  11526   -186   1085  -1374       C  
ATOM   1990  O   ASP A 254      78.275  49.421  44.642  1.00 81.14           O  
ANISOU 1990  O   ASP A 254    10675   8684  11470   -160   1079  -1333       O  
ATOM   1991  CB  ASP A 254      75.213  48.499  44.260  1.00 97.06           C  
ANISOU 1991  CB  ASP A 254    12510  10686  13681   -258   1028  -1668       C  
ATOM   1992  CG  ASP A 254      73.948  47.865  44.795  1.00104.33           C  
ANISOU 1992  CG  ASP A 254    13357  11615  14668   -346   1098  -1874       C  
ATOM   1993  OD1 ASP A 254      74.021  46.735  45.322  1.00108.71           O  
ANISOU 1993  OD1 ASP A 254    14020  12216  15070   -422   1228  -1922       O  
ATOM   1994  OD2 ASP A 254      72.878  48.499  44.686  1.00106.16           O1-
ANISOU 1994  OD2 ASP A 254    13418  11805  15113   -343   1016  -1989       O1-
ATOM   1995  N   VAL A 255      78.089  47.895  43.003  1.00 80.33           N  
ANISOU 1995  N   VAL A 255    10731   8640  11153   -150   1033  -1256       N  
ATOM   1996  CA  VAL A 255      79.235  48.406  42.260  1.00 80.68           C  
ANISOU 1996  CA  VAL A 255    10841   8695  11119    -81    969  -1071       C  
ATOM   1997  C   VAL A 255      78.899  49.697  41.525  1.00 82.62           C  
ANISOU 1997  C   VAL A 255    10976   8899  11515    -35    791  -1015       C  
ATOM   1998  O   VAL A 255      77.845  49.813  40.898  1.00 82.85           O  
ANISOU 1998  O   VAL A 255    10931   8907  11641    -44    680  -1067       O  
ATOM   1999  CB  VAL A 255      79.764  47.378  41.250  1.00 79.37           C  
ANISOU 1999  CB  VAL A 255    10826   8580  10750    -73    983   -979       C  
ATOM   2000  CG1 VAL A 255      80.686  48.053  40.248  1.00 81.17           C  
ANISOU 2000  CG1 VAL A 255    11097   8826  10919    -18    889   -806       C  
ATOM   2001  CG2 VAL A 255      80.484  46.254  41.975  1.00 79.05           C  
ANISOU 2001  CG2 VAL A 255    10903   8563  10569    -98   1146   -988       C  
ATOM   2002  N   ASN A 256      79.808  50.664  41.604  1.00 84.22           N  
ANISOU 2002  N   ASN A 256    11172   9086  11743     10    754   -902       N  
ATOM   2003  CA  ASN A 256      79.605  51.964  40.979  1.00 83.85           C  
ANISOU 2003  CA  ASN A 256    11026   8986  11845     51    577   -831       C  
ATOM   2004  C   ASN A 256      80.360  52.104  39.664  1.00 87.80           C  
ANISOU 2004  C   ASN A 256    11628   9524  12207     75    473   -644       C  
ATOM   2005  O   ASN A 256      81.589  52.116  39.648  1.00 92.28           O  
ANISOU 2005  O   ASN A 256    12289  10130  12643     94    530   -530       O  
ATOM   2006  CB  ASN A 256      80.023  53.082  41.934  1.00 76.47           C  
ANISOU 2006  CB  ASN A 256    10005   8001  11049     73    593   -838       C  
ATOM   2007  CG  ASN A 256      79.777  54.459  41.360  1.00 78.97           C  
ANISOU 2007  CG  ASN A 256    10213   8244  11546    115    402   -771       C  
ATOM   2008  ND2 ASN A 256      80.334  55.478  42.004  1.00 82.10           N  
ANISOU 2008  ND2 ASN A 256    10555   8597  12040    140    403   -744       N  
ATOM   2009  OD1 ASN A 256      79.090  54.608  40.350  1.00 82.74           O  
ANISOU 2009  OD1 ASN A 256    10657   8701  12079    121    246   -739       O  
ATOM   2010  N   PRO A 257      79.620  52.213  38.552  1.00 88.84           N  
ANISOU 2010  N   PRO A 257    11738   9648  12368     62    317   -614       N  
ATOM   2011  CA  PRO A 257      80.216  52.402  37.227  1.00 89.61           C  
ANISOU 2011  CA  PRO A 257    11930   9786  12331     57    202   -442       C  
ATOM   2012  C   PRO A 257      81.082  53.655  37.191  1.00 92.77           C  
ANISOU 2012  C   PRO A 257    12311  10157  12779     92    121   -306       C  
ATOM   2013  O   PRO A 257      82.201  53.617  36.683  1.00104.69           O  
ANISOU 2013  O   PRO A 257    13933  11726  14117     89    146   -175       O  
ATOM   2014  CB  PRO A 257      78.998  52.582  36.320  1.00 92.39           C  
ANISOU 2014  CB  PRO A 257    12214  10106  12781     26     18   -455       C  
ATOM   2015  CG  PRO A 257      77.884  51.912  37.044  1.00 94.21           C  
ANISOU 2015  CG  PRO A 257    12364  10316  13115     11     95   -647       C  
ATOM   2016  CD  PRO A 257      78.151  52.149  38.495  1.00 91.39           C  
ANISOU 2016  CD  PRO A 257    11943   9926  12853     40    238   -745       C  
ATOM   2017  N   GLU A 258      80.565  54.751  37.736  1.00 87.72           N  
ANISOU 2017  N   GLU A 258    11526   9427  12378    121     30   -347       N  
ATOM   2018  CA  GLU A 258      81.304  56.007  37.783  1.00 96.24           C  
ANISOU 2018  CA  GLU A 258    12575  10463  13528    152    -53   -228       C  
ATOM   2019  C   GLU A 258      82.527  55.890  38.687  1.00 88.68           C  
ANISOU 2019  C   GLU A 258    11682   9546  12464    172    124   -209       C  
ATOM   2020  O   GLU A 258      83.264  56.857  38.875  1.00 84.50           O  
ANISOU 2020  O   GLU A 258    11139   8992  11976    195     87   -118       O  
ATOM   2021  CB  GLU A 258      80.402  57.137  38.288  1.00116.67           C  
ANISOU 2021  CB  GLU A 258    14978  12928  16423    181   -173   -308       C  
ATOM   2022  CG  GLU A 258      79.094  57.297  37.527  1.00132.08           C  
ANISOU 2022  CG  GLU A 258    16834  14821  18530    168   -360   -341       C  
ATOM   2023  CD  GLU A 258      79.263  58.023  36.205  1.00143.70           C  
ANISOU 2023  CD  GLU A 258    18342  16275  19982    150   -595   -146       C  
ATOM   2024  OE1 GLU A 258      80.408  58.114  35.712  1.00148.22           O  
ANISOU 2024  OE1 GLU A 258    19045  16912  20358    134   -585     10       O  
ATOM   2025  OE2 GLU A 258      78.247  58.504  35.660  1.00145.27           O1-
ANISOU 2025  OE2 GLU A 258    18436  16395  20365    145   -794   -147       O1-
ATOM   2026  N   GLY A 259      82.733  54.700  39.245  1.00 85.23           N  
ANISOU 2026  N   GLY A 259    11317   9168  11896    157    309   -290       N  
ATOM   2027  CA  GLY A 259      83.805  54.464  40.194  1.00 85.80           C  
ANISOU 2027  CA  GLY A 259    11445   9274  11880    168    473   -280       C  
ATOM   2028  C   GLY A 259      85.191  54.802  39.680  1.00 87.74           C  
ANISOU 2028  C   GLY A 259    11784   9568  11984    185    466   -104       C  
ATOM   2029  O   GLY A 259      85.602  54.338  38.618  1.00 91.11           O  
ANISOU 2029  O   GLY A 259    12310  10057  12252    172    444    -14       O  
ATOM   2030  N   LYS A 260      85.910  55.616  40.446  1.00 84.60           N  
ANISOU 2030  N   LYS A 260    11354   9147  11643    205    493    -64       N  
ATOM   2031  CA  LYS A 260      87.284  55.983  40.123  1.00 78.46           C  
ANISOU 2031  CA  LYS A 260    10653   8417  10741    219    501     95       C  
ATOM   2032  C   LYS A 260      88.209  55.711  41.303  1.00 80.43           C  
ANISOU 2032  C   LYS A 260    10929   8688  10943    226    661     85       C  
ATOM   2033  O   LYS A 260      87.751  55.422  42.410  1.00 77.52           O  
ANISOU 2033  O   LYS A 260    10515   8290  10649    210    750    -40       O  
ATOM   2034  CB  LYS A 260      87.375  57.458  39.730  1.00 78.76           C  
ANISOU 2034  CB  LYS A 260    10630   8402  10893    229    334    196       C  
ATOM   2035  CG  LYS A 260      87.303  57.722  38.234  1.00 88.56           C  
ANISOU 2035  CG  LYS A 260    11918   9665  12065    206    173    318       C  
ATOM   2036  CD  LYS A 260      85.906  57.507  37.684  1.00102.18           C  
ANISOU 2036  CD  LYS A 260    13589  11348  13887    188     60    239       C  
ATOM   2037  CE  LYS A 260      85.823  57.927  36.224  1.00111.58           C  
ANISOU 2037  CE  LYS A 260    14826  12554  15017    145   -128    377       C  
ATOM   2038  NZ  LYS A 260      86.238  59.345  36.023  1.00112.28           N1+
ANISOU 2038  NZ  LYS A 260    14877  12587  15198    148   -281    508       N1+
ATOM   2039  N   TYR A 261      89.512  55.809  41.057  1.00 85.37           N  
ANISOU 2039  N   TYR A 261    11628   9368  11443    238    695    217       N  
ATOM   2040  CA  TYR A 261      90.514  55.623  42.101  1.00 83.43           C  
ANISOU 2040  CA  TYR A 261    11406   9141  11151    243    825    236       C  
ATOM   2041  C   TYR A 261      91.093  56.964  42.544  1.00 81.07           C  
ANISOU 2041  C   TYR A 261    11055   8813  10936    249    771    311       C  
ATOM   2042  O   TYR A 261      91.077  57.936  41.789  1.00 87.31           O  
ANISOU 2042  O   TYR A 261    11821   9584  11770    256    637    393       O  
ATOM   2043  CB  TYR A 261      91.625  54.688  41.616  1.00 79.25           C  
ANISOU 2043  CB  TYR A 261    10984   8691  10436    255    917    318       C  
ATOM   2044  CG  TYR A 261      91.193  53.242  41.507  1.00 77.75           C  
ANISOU 2044  CG  TYR A 261    10850   8520  10172    247   1005    228       C  
ATOM   2045  CD1 TYR A 261      90.676  52.735  40.322  1.00 76.57           C  
ANISOU 2045  CD1 TYR A 261    10742   8398   9955    239    960    216       C  
ATOM   2046  CD2 TYR A 261      91.298  52.385  42.595  1.00 79.56           C  
ANISOU 2046  CD2 TYR A 261    11096   8739  10395    237   1128    158       C  
ATOM   2047  CE1 TYR A 261      90.278  51.412  40.223  1.00 82.72           C  
ANISOU 2047  CE1 TYR A 261    11573   9188  10667    229   1042    129       C  
ATOM   2048  CE2 TYR A 261      90.902  51.063  42.506  1.00 84.86           C  
ANISOU 2048  CE2 TYR A 261    11822   9418  11003    226   1202     80       C  
ATOM   2049  CZ  TYR A 261      90.394  50.581  41.320  1.00 87.47           C  
ANISOU 2049  CZ  TYR A 261    12189   9772  11273    226   1163     61       C  
ATOM   2050  OH  TYR A 261      90.000  49.265  41.236  1.00 86.21           O  
ANISOU 2050  OH  TYR A 261    12086   9615  11053    213   1238    -21       O  
ATOM   2051  N   SER A 262      91.596  57.017  43.773  1.00 70.83           N  
ANISOU 2051  N   SER A 262     9743   7509   9659    237    869    288       N  
ATOM   2052  CA  SER A 262      92.138  58.259  44.311  1.00 79.22           C  
ANISOU 2052  CA  SER A 262    10758   8542  10802    234    832    347       C  
ATOM   2053  C   SER A 262      93.657  58.300  44.233  1.00 94.64           C  
ANISOU 2053  C   SER A 262    12779  10559  12622    245    876    496       C  
ATOM   2054  O   SER A 262      94.349  57.763  45.098  1.00100.05           O  
ANISOU 2054  O   SER A 262    13495  11272  13248    231    989    499       O  
ATOM   2055  CB  SER A 262      91.684  58.467  45.757  1.00 79.21           C  
ANISOU 2055  CB  SER A 262    10689   8492  10916    193    904    219       C  
ATOM   2056  OG  SER A 262      90.306  58.783  45.815  1.00 84.46           O  
ANISOU 2056  OG  SER A 262    11260   9087  11745    184    847     78       O  
ATOM   2057  N   PHE A 263      94.171  58.942  43.190  1.00 99.25           N  
ANISOU 2057  N   PHE A 263    13384  11167  13160    261    781    622       N  
ATOM   2058  CA  PHE A 263      95.608  59.118  43.035  1.00 95.55           C  
ANISOU 2058  CA  PHE A 263    12966  10762  12575    267    816    761       C  
ATOM   2059  C   PHE A 263      95.972  60.589  43.193  1.00 90.39           C  
ANISOU 2059  C   PHE A 263    12267  10072  12003    257    723    842       C  
ATOM   2060  O   PHE A 263      95.559  61.428  42.393  1.00 93.72           O  
ANISOU 2060  O   PHE A 263    12668  10461  12481    254    584    886       O  
ATOM   2061  CB  PHE A 263      96.072  58.595  41.675  1.00 93.61           C  
ANISOU 2061  CB  PHE A 263    12795  10591  12181    273    803    842       C  
ATOM   2062  CG  PHE A 263      97.563  58.596  41.503  1.00 92.76           C  
ANISOU 2062  CG  PHE A 263    12733  10558  11953    277    863    963       C  
ATOM   2063  CD1 PHE A 263      98.353  57.700  42.201  1.00 87.59           C  
ANISOU 2063  CD1 PHE A 263    12101   9936  11243    294   1000    956       C  
ATOM   2064  CD2 PHE A 263      98.174  59.490  40.641  1.00 98.88           C  
ANISOU 2064  CD2 PHE A 263    13524  11369  12676    257    777   1087       C  
ATOM   2065  CE1 PHE A 263      99.723  57.698  42.047  1.00 87.93           C  
ANISOU 2065  CE1 PHE A 263    12169  10045  11195    301   1054   1061       C  
ATOM   2066  CE2 PHE A 263      99.544  59.492  40.481  1.00 98.30           C  
ANISOU 2066  CE2 PHE A 263    13484  11372  12495    254    841   1188       C  
ATOM   2067  CZ  PHE A 263     100.320  58.594  41.186  1.00 95.78           C  
ANISOU 2067  CZ  PHE A 263    13173  11082  12136    281    982   1171       C  
ATOM   2068  N   GLY A 264      96.741  60.898  44.232  1.00 82.08           N  
ANISOU 2068  N   GLY A 264    11203   9024  10960    245    793    866       N  
ATOM   2069  CA  GLY A 264      97.102  62.273  44.521  1.00 79.82           C  
ANISOU 2069  CA  GLY A 264    10874   8699  10756    230    718    931       C  
ATOM   2070  C   GLY A 264      95.871  63.142  44.688  1.00 79.60           C  
ANISOU 2070  C   GLY A 264    10759   8564  10921    226    615    835       C  
ATOM   2071  O   GLY A 264      95.035  62.887  45.554  1.00 83.28           O  
ANISOU 2071  O   GLY A 264    11172   8982  11488    213    670    688       O  
ATOM   2072  N   ALA A 265      95.755  64.168  43.853  1.00 76.42           N  
ANISOU 2072  N   ALA A 265    10338   8121  10578    231    463    916       N  
ATOM   2073  CA  ALA A 265      94.594  65.047  43.889  1.00 78.78           C  
ANISOU 2073  CA  ALA A 265    10541   8301  11090    237    341    834       C  
ATOM   2074  C   ALA A 265      93.740  64.872  42.640  1.00 82.88           C  
ANISOU 2074  C   ALA A 265    11064   8802  11625    250    209    846       C  
ATOM   2075  O   ALA A 265      92.920  65.729  42.314  1.00 89.34           O  
ANISOU 2075  O   ALA A 265    11809   9520  12616    257     57    830       O  
ATOM   2076  CB  ALA A 265      95.027  66.495  44.040  1.00 79.87           C  
ANISOU 2076  CB  ALA A 265    10641   8376  11329    226    244    914       C  
ATOM   2077  N   THR A 266      93.938  63.757  41.943  1.00 79.64           N  
ANISOU 2077  N   THR A 266    10736   8483  11040    249    263    873       N  
ATOM   2078  CA  THR A 266      93.183  63.467  40.729  1.00 86.78           C  
ANISOU 2078  CA  THR A 266    11660   9388  11925    245    149    888       C  
ATOM   2079  C   THR A 266      92.444  62.138  40.834  1.00 88.67           C  
ANISOU 2079  C   THR A 266    11910   9655  12128    254    247    756       C  
ATOM   2080  O   THR A 266      92.863  61.238  41.561  1.00 89.70           O  
ANISOU 2080  O   THR A 266    12072   9836  12174    260    412    700       O  
ATOM   2081  CB  THR A 266      94.098  63.419  39.494  1.00 97.10           C  
ANISOU 2081  CB  THR A 266    13071  10788  13035    213    103   1053       C  
ATOM   2082  CG2 THR A 266      94.785  64.760  39.286  1.00104.04           C  
ANISOU 2082  CG2 THR A 266    13947  11640  13942    190    -12   1193       C  
ATOM   2083  OG1 THR A 266      95.089  62.399  39.671  1.00 98.62           O  
ANISOU 2083  OG1 THR A 266    13338  11088  13045    216    278   1063       O  
ATOM   2084  N   CYS A 267      91.344  62.022  40.097  1.00 91.00           N  
ANISOU 2084  N   CYS A 267    12178   9910  12487    250    136    714       N  
ATOM   2085  CA  CYS A 267      90.557  60.796  40.085  1.00 98.35           C  
ANISOU 2085  CA  CYS A 267    13119  10864  13384    252    213    591       C  
ATOM   2086  C   CYS A 267      90.847  59.982  38.828  1.00106.59           C  
ANISOU 2086  C   CYS A 267    14272  12000  14227    227    205    669       C  
ATOM   2087  O   CYS A 267      90.431  60.350  37.729  1.00114.77           O  
ANISOU 2087  O   CYS A 267    15320  13028  15259    197     49    738       O  
ATOM   2088  CB  CYS A 267      89.065  61.119  40.179  1.00100.23           C  
ANISOU 2088  CB  CYS A 267    13244  11000  13837    260    107    470       C  
ATOM   2089  SG  CYS A 267      88.588  61.977  41.697  1.00109.25           S  
ANISOU 2089  SG  CYS A 267    14244  12033  15231    278    144    329       S  
ATOM   2090  N   VAL A 268      91.560  58.873  38.999  1.00103.49           N  
ANISOU 2090  N   VAL A 268    13957  11692  13672    230    371    654       N  
ATOM   2091  CA  VAL A 268      91.991  58.050  37.874  1.00104.15           C  
ANISOU 2091  CA  VAL A 268    14145  11868  13559    203    399    711       C  
ATOM   2092  C   VAL A 268      91.114  56.813  37.698  1.00109.69           C  
ANISOU 2092  C   VAL A 268    14868  12580  14230    199    456    590       C  
ATOM   2093  O   VAL A 268      90.303  56.489  38.564  1.00112.60           O  
ANISOU 2093  O   VAL A 268    15177  12895  14713    218    499    462       O  
ATOM   2094  CB  VAL A 268      93.453  57.602  38.044  1.00102.97           C  
ANISOU 2094  CB  VAL A 268    14064  11802  13259    212    544    776       C  
ATOM   2095  CG1 VAL A 268      94.360  58.810  38.228  1.00102.59           C  
ANISOU 2095  CG1 VAL A 268    13998  11751  13232    209    492    898       C  
ATOM   2096  CG2 VAL A 268      93.580  56.653  39.224  1.00 98.73           C  
ANISOU 2096  CG2 VAL A 268    13520  11259  12736    247    710    674       C  
ATOM   2097  N   LYS A 269      91.285  56.126  36.573  1.00108.98           N  
ANISOU 2097  N   LYS A 269    14865  12563  13978    162    462    624       N  
ATOM   2098  CA  LYS A 269      90.524  54.914  36.287  1.00101.21           C  
ANISOU 2098  CA  LYS A 269    13915  11595  12945    150    518    516       C  
ATOM   2099  C   LYS A 269      91.221  53.697  36.880  1.00100.37           C  
ANISOU 2099  C   LYS A 269    13860  11528  12747    180    718    456       C  
ATOM   2100  O   LYS A 269      90.573  52.726  37.268  1.00105.31           O  
ANISOU 2100  O   LYS A 269    14489  12136  13387    187    792    340       O  
ATOM   2101  CB  LYS A 269      90.335  54.729  34.779  1.00104.12           C  
ANISOU 2101  CB  LYS A 269    14357  12022  13180     82    430    572       C  
ATOM   2102  CG  LYS A 269      89.469  55.791  34.110  1.00113.36           C  
ANISOU 2102  CG  LYS A 269    15480  13142  14448     41    204    634       C  
ATOM   2103  CD  LYS A 269      90.177  57.137  34.043  1.00122.37           C  
ANISOU 2103  CD  LYS A 269    16601  14268  15626     34     99    773       C  
ATOM   2104  CE  LYS A 269      91.539  57.012  33.375  1.00127.37           C  
ANISOU 2104  CE  LYS A 269    17336  15008  16050     -8    174    878       C  
ATOM   2105  NZ  LYS A 269      92.320  58.279  33.447  1.00126.41           N1+
ANISOU 2105  NZ  LYS A 269    17197  14875  15957    -15     93   1010       N1+
ATOM   2106  N   LYS A 270      92.547  53.754  36.944  1.00 98.95           N  
ANISOU 2106  N   LYS A 270    13718  11398  12481    194    799    539       N  
ATOM   2107  CA  LYS A 270      93.330  52.693  37.566  1.00 99.30           C  
ANISOU 2107  CA  LYS A 270    13798  11465  12467    228    972    500       C  
ATOM   2108  C   LYS A 270      94.600  53.253  38.196  1.00 90.63           C  
ANISOU 2108  C   LYS A 270    12684  10381  11371    256   1021    592       C  
ATOM   2109  O   LYS A 270      95.109  54.294  37.779  1.00 87.09           O  
ANISOU 2109  O   LYS A 270    12226   9955  10910    240    941    697       O  
ATOM   2110  CB  LYS A 270      93.685  51.607  36.551  1.00108.71           C  
ANISOU 2110  CB  LYS A 270    15077  12724  13504    208   1053    483       C  
ATOM   2111  CG  LYS A 270      94.789  51.996  35.582  1.00122.11           C  
ANISOU 2111  CG  LYS A 270    16819  14503  15076    178   1054    591       C  
ATOM   2112  CD  LYS A 270      95.184  50.823  34.697  1.00132.58           C  
ANISOU 2112  CD  LYS A 270    18222  15893  16259    155   1167    544       C  
ATOM   2113  CE  LYS A 270      95.654  49.634  35.525  1.00132.81           C  
ANISOU 2113  CE  LYS A 270    18255  15894  16312    218   1328    468       C  
ATOM   2114  NZ  LYS A 270      96.879  49.945  36.312  1.00130.77           N1+
ANISOU 2114  NZ  LYS A 270    17960  15635  16091    267   1391    539       N1+
ATOM   2115  N   CYS A 271      95.109  52.555  39.204  1.00 82.53           N  
ANISOU 2115  N   CYS A 271    11657   9340  10361    290   1143    557       N  
ATOM   2116  CA  CYS A 271      96.307  52.994  39.905  1.00 79.34           C  
ANISOU 2116  CA  CYS A 271    11234   8946   9964    313   1190    642       C  
ATOM   2117  C   CYS A 271      97.570  52.601  39.146  1.00 84.62           C  
ANISOU 2117  C   CYS A 271    11949   9690  10511    323   1264    713       C  
ATOM   2118  O   CYS A 271      97.615  51.550  38.507  1.00 92.22           O  
ANISOU 2118  O   CYS A 271    12961  10680  11397    325   1337    662       O  
ATOM   2119  CB  CYS A 271      96.342  52.403  41.316  1.00 68.79           C  
ANISOU 2119  CB  CYS A 271     9880   7562   8694    330   1276    587       C  
ATOM   2120  SG  CYS A 271      94.906  52.804  42.330  1.00120.23           S  
ANISOU 2120  SG  CYS A 271    16333  13999  15350    300   1222    476       S  
ATOM   2121  N   PRO A 272      98.603  53.455  39.208  1.00 77.78           N  
ANISOU 2121  N   PRO A 272    11063   8857   9632    325   1251    822       N  
ATOM   2122  CA  PRO A 272      99.913  53.119  38.644  1.00 79.24           C  
ANISOU 2122  CA  PRO A 272    11274   9114   9719    333   1337    881       C  
ATOM   2123  C   PRO A 272     100.393  51.774  39.175  1.00 79.13           C  
ANISOU 2123  C   PRO A 272    11269   9083   9713    379   1473    823       C  
ATOM   2124  O   PRO A 272     100.306  51.528  40.375  1.00 79.46           O  
ANISOU 2124  O   PRO A 272    11287   9066   9838    403   1495    805       O  
ATOM   2125  CB  PRO A 272     100.808  54.242  39.167  1.00 85.69           C  
ANISOU 2125  CB  PRO A 272    12048   9943  10566    333   1304    994       C  
ATOM   2126  CG  PRO A 272      99.887  55.396  39.344  1.00 86.98           C  
ANISOU 2126  CG  PRO A 272    12183  10059  10806    306   1165   1009       C  
ATOM   2127  CD  PRO A 272      98.574  54.813  39.777  1.00 82.04           C  
ANISOU 2127  CD  PRO A 272    11551   9367  10255    314   1155    888       C  
ATOM   2128  N   ARG A 273     100.896  50.922  38.288  1.00 84.15           N  
ANISOU 2128  N   ARG A 273    11941   9767  10265    384   1559    793       N  
ATOM   2129  CA  ARG A 273     101.270  49.556  38.650  1.00 93.99           C  
ANISOU 2129  CA  ARG A 273    13197  10980  11534    431   1679    727       C  
ATOM   2130  C   ARG A 273     102.071  49.447  39.949  1.00 86.01           C  
ANISOU 2130  C   ARG A 273    12142   9925  10615    475   1716    779       C  
ATOM   2131  O   ARG A 273     101.866  48.521  40.732  1.00 88.67           O  
ANISOU 2131  O   ARG A 273    12484  10194  11011    500   1757    730       O  
ATOM   2132  CB  ARG A 273     102.038  48.890  37.505  1.00115.34           C  
ANISOU 2132  CB  ARG A 273    15926  13749  14149    429   1778    699       C  
ATOM   2133  CG  ARG A 273     101.240  48.751  36.218  1.00133.43           C  
ANISOU 2133  CG  ARG A 273    18276  16087  16334    367   1755    636       C  
ATOM   2134  CD  ARG A 273     102.104  48.222  35.081  1.00146.42           C  
ANISOU 2134  CD  ARG A 273    19944  17810  17877    344   1866    603       C  
ATOM   2135  NE  ARG A 273     102.631  46.888  35.360  1.00154.43           N  
ANISOU 2135  NE  ARG A 273    20948  18780  18948    408   2002    521       N  
ATOM   2136  CZ  ARG A 273     103.842  46.650  35.853  1.00159.36           C  
ANISOU 2136  CZ  ARG A 273    21515  19392  19640    466   2082    553       C  
ATOM   2137  NH1 ARG A 273     104.237  45.403  36.074  1.00162.53           N1+
ANISOU 2137  NH1 ARG A 273    21904  19735  20114    526   2189    477       N1+
ATOM   2138  NH2 ARG A 273     104.661  47.658  36.124  1.00159.31           N  
ANISOU 2138  NH2 ARG A 273    21462  19428  19641    465   2048    664       N  
ATOM   2139  N   ASN A 274     102.981  50.389  40.176  1.00 78.55           N  
ANISOU 2139  N   ASN A 274    11156   9016   9674    474   1693    884       N  
ATOM   2140  CA  ASN A 274     103.861  50.327  41.341  1.00 75.66           C  
ANISOU 2140  CA  ASN A 274    10747   8616   9384    505   1721    948       C  
ATOM   2141  C   ASN A 274     103.184  50.720  42.654  1.00 79.69           C  
ANISOU 2141  C   ASN A 274    11247   9062   9970    482   1659    953       C  
ATOM   2142  O   ASN A 274     103.696  50.429  43.734  1.00 79.01           O  
ANISOU 2142  O   ASN A 274    11142   8937   9942    490   1679    990       O  
ATOM   2143  CB  ASN A 274     105.115  51.174  41.120  1.00 69.15           C  
ANISOU 2143  CB  ASN A 274     9881   7858   8534    505   1724   1058       C  
ATOM   2144  CG  ASN A 274     104.793  52.619  40.819  1.00 77.71           C  
ANISOU 2144  CG  ASN A 274    10965   8981   9582    455   1622   1118       C  
ATOM   2145  ND2 ASN A 274     105.755  53.503  41.058  1.00 82.94           N  
ANISOU 2145  ND2 ASN A 274    11589   9681  10243    447   1604   1223       N  
ATOM   2146  OD1 ASN A 274     103.692  52.940  40.375  1.00 83.24           O  
ANISOU 2146  OD1 ASN A 274    11695   9671  10262    424   1552   1073       O  
ATOM   2147  N   TYR A 275     102.033  51.377  42.559  1.00 85.85           N  
ANISOU 2147  N   TYR A 275    12037   9831  10752    445   1581    912       N  
ATOM   2148  CA  TYR A 275     101.296  51.792  43.749  1.00 88.79           C  
ANISOU 2148  CA  TYR A 275    12392  10147  11199    411   1534    888       C  
ATOM   2149  C   TYR A 275     100.438  50.670  44.332  1.00 82.48           C  
ANISOU 2149  C   TYR A 275    11621   9287  10430    401   1571    784       C  
ATOM   2150  O   TYR A 275     100.219  49.640  43.693  1.00 80.00           O  
ANISOU 2150  O   TYR A 275    11344   8970  10082    424   1618    723       O  
ATOM   2151  CB  TYR A 275     100.432  53.022  43.452  1.00 90.77           C  
ANISOU 2151  CB  TYR A 275    12621  10397  11469    378   1432    879       C  
ATOM   2152  CG  TYR A 275     101.150  54.334  43.666  1.00 91.42           C  
ANISOU 2152  CG  TYR A 275    12666  10504  11567    365   1380    985       C  
ATOM   2153  CD1 TYR A 275     101.108  54.974  44.896  1.00 91.34           C  
ANISOU 2153  CD1 TYR A 275    12621  10455  11629    334   1360    997       C  
ATOM   2154  CD2 TYR A 275     101.873  54.929  42.642  1.00 91.27           C  
ANISOU 2154  CD2 TYR A 275    12650  10548  11481    370   1354   1070       C  
ATOM   2155  CE1 TYR A 275     101.762  56.172  45.100  1.00 87.99           C  
ANISOU 2155  CE1 TYR A 275    12165  10048  11220    318   1313   1090       C  
ATOM   2156  CE2 TYR A 275     102.532  56.129  42.838  1.00 89.87           C  
ANISOU 2156  CE2 TYR A 275    12442  10390  11314    352   1303   1170       C  
ATOM   2157  CZ  TYR A 275     102.472  56.744  44.070  1.00 88.78           C  
ANISOU 2157  CZ  TYR A 275    12269  10206  11257    331   1281   1180       C  
ATOM   2158  OH  TYR A 275     103.124  57.937  44.277  1.00 93.24           O  
ANISOU 2158  OH  TYR A 275    12806  10786  11834    309   1232   1276       O  
ATOM   2159  N   VAL A 276      99.958  50.883  45.553  1.00 77.29           N  
ANISOU 2159  N   VAL A 276    10950   8585   9832    355   1553    759       N  
ATOM   2160  CA  VAL A 276      99.115  49.909  46.234  1.00 77.43           C  
ANISOU 2160  CA  VAL A 276    10997   8549   9873    321   1584    662       C  
ATOM   2161  C   VAL A 276      97.641  50.263  46.088  1.00 79.35           C  
ANISOU 2161  C   VAL A 276    11228   8776  10145    286   1539    550       C  
ATOM   2162  O   VAL A 276      97.234  51.388  46.372  1.00 89.46           O  
ANISOU 2162  O   VAL A 276    12462  10053  11475    257   1483    544       O  
ATOM   2163  CB  VAL A 276      99.453  49.826  47.731  1.00 85.51           C  
ANISOU 2163  CB  VAL A 276    12018   9539  10933    265   1600    694       C  
ATOM   2164  CG1 VAL A 276      98.310  49.186  48.495  1.00 87.49           C  
ANISOU 2164  CG1 VAL A 276    12296   9743  11204    195   1615    580       C  
ATOM   2165  CG2 VAL A 276     100.747  49.057  47.943  1.00 93.32           C  
ANISOU 2165  CG2 VAL A 276    13022  10521  11913    299   1641    790       C  
ATOM   2166  N   VAL A 277      96.843  49.299  45.646  1.00 74.48           N  
ANISOU 2166  N   VAL A 277    10649   8143   9509    288   1562    456       N  
ATOM   2167  CA  VAL A 277      95.416  49.522  45.455  1.00 81.24           C  
ANISOU 2167  CA  VAL A 277    11486   8982  10400    256   1518    343       C  
ATOM   2168  C   VAL A 277      94.615  49.028  46.655  1.00 87.90           C  
ANISOU 2168  C   VAL A 277    12332   9780  11285    185   1551    246       C  
ATOM   2169  O   VAL A 277      94.592  47.832  46.950  1.00 87.44           O  
ANISOU 2169  O   VAL A 277    12327   9699  11196    170   1607    214       O  
ATOM   2170  CB  VAL A 277      94.898  48.829  44.180  1.00 81.98           C  
ANISOU 2170  CB  VAL A 277    11617   9092  10439    284   1517    292       C  
ATOM   2171  CG1 VAL A 277      93.456  49.227  43.912  1.00 79.73           C  
ANISOU 2171  CG1 VAL A 277    11299   8793  10204    253   1450    191       C  
ATOM   2172  CG2 VAL A 277      95.777  49.179  42.993  1.00 86.48           C  
ANISOU 2172  CG2 VAL A 277    12198   9718  10944    331   1502    383       C  
ATOM   2173  N   THR A 278      93.960  49.957  47.344  1.00 94.45           N  
ANISOU 2173  N   THR A 278    13103  10595  12189    133   1517    194       N  
ATOM   2174  CA  THR A 278      93.144  49.611  48.500  1.00104.21           C  
ANISOU 2174  CA  THR A 278    14335  11800  13461     43   1556     85       C  
ATOM   2175  C   THR A 278      91.716  49.283  48.086  1.00114.75           C  
ANISOU 2175  C   THR A 278    15652  13120  14829     25   1542    -57       C  
ATOM   2176  O   THR A 278      91.303  49.565  46.960  1.00113.60           O  
ANISOU 2176  O   THR A 278    15485  12984  14694     78   1484    -65       O  
ATOM   2177  CB  THR A 278      93.121  50.744  49.545  1.00103.19           C  
ANISOU 2177  CB  THR A 278    14144  11663  13401    -21   1545     72       C  
ATOM   2178  CG2 THR A 278      94.512  50.973  50.113  1.00104.56           C  
ANISOU 2178  CG2 THR A 278    14340  11852  13536    -22   1561    212       C  
ATOM   2179  OG1 THR A 278      92.649  51.952  48.936  1.00101.54           O  
ANISOU 2179  OG1 THR A 278    13857  11449  13273     15   1470     52       O  
ATOM   2180  N   ASP A 279      90.968  48.683  49.005  1.00125.10           N  
ANISOU 2180  N   ASP A 279    16972  14409  16150    -64   1593   -166       N  
ATOM   2181  CA  ASP A 279      89.583  48.316  48.747  1.00133.23           C  
ANISOU 2181  CA  ASP A 279    17980  15427  17216    -94   1589   -312       C  
ATOM   2182  C   ASP A 279      88.713  49.557  48.579  1.00142.47           C  
ANISOU 2182  C   ASP A 279    19038  16586  18507    -92   1524   -390       C  
ATOM   2183  O   ASP A 279      87.805  49.581  47.748  1.00144.37           O  
ANISOU 2183  O   ASP A 279    19242  16821  18791    -64   1472   -456       O  
ATOM   2184  CB  ASP A 279      89.048  47.438  49.879  1.00132.90           C  
ANISOU 2184  CB  ASP A 279    17975  15370  17151   -209   1663   -410       C  
ATOM   2185  CG  ASP A 279      89.827  46.146  50.029  1.00133.03           C  
ANISOU 2185  CG  ASP A 279    18100  15377  17067   -211   1709   -332       C  
ATOM   2186  OD1 ASP A 279      90.021  45.696  51.178  1.00136.36           O  
ANISOU 2186  OD1 ASP A 279    18564  15787  17461   -309   1753   -331       O  
ATOM   2187  OD2 ASP A 279      90.251  45.583  48.998  1.00130.73           O1-
ANISOU 2187  OD2 ASP A 279    17852  15089  16732   -122   1698   -272       O1-
ATOM   2188  N   HIS A 280      89.001  50.587  49.370  1.00147.22           N  
ANISOU 2188  N   HIS A 280    19583  17180  19175   -124   1522   -380       N  
ATOM   2189  CA  HIS A 280      88.270  51.847  49.288  1.00148.53           C  
ANISOU 2189  CA  HIS A 280    19632  17318  19484   -117   1457   -453       C  
ATOM   2190  C   HIS A 280      88.182  52.324  47.843  1.00134.43           C  
ANISOU 2190  C   HIS A 280    17822  15529  17725    -18   1345   -386       C  
ATOM   2191  O   HIS A 280      87.138  52.799  47.396  1.00134.29           O  
ANISOU 2191  O   HIS A 280    17723  15481  17821     -7   1274   -473       O  
ATOM   2192  CB  HIS A 280      88.951  52.925  50.137  1.00161.23           C  
ANISOU 2192  CB  HIS A 280    21201  18918  21139   -147   1465   -410       C  
ATOM   2193  CG  HIS A 280      89.027  52.593  51.596  1.00172.42           C  
ANISOU 2193  CG  HIS A 280    22641  20344  22525   -270   1567   -474       C  
ATOM   2194  CD2 HIS A 280      88.104  52.688  52.581  1.00177.44           C  
ANISOU 2194  CD2 HIS A 280    23224  20967  23229   -384   1628   -643       C  
ATOM   2195  ND1 HIS A 280      90.172  52.105  52.189  1.00174.27           N  
ANISOU 2195  ND1 HIS A 280    22965  20605  22646   -302   1613   -356       N  
ATOM   2196  CE1 HIS A 280      89.948  51.909  53.476  1.00175.87           C  
ANISOU 2196  CE1 HIS A 280    23177  20810  22834   -438   1688   -438       C  
ATOM   2197  NE2 HIS A 280      88.701  52.255  53.740  1.00177.92           N  
ANISOU 2197  NE2 HIS A 280    23354  21052  23196   -494   1708   -619       N  
ATOM   2198  N   GLY A 281      89.287  52.188  47.119  1.00119.69           N  
ANISOU 2198  N   GLY A 281    16026  13694  15755     45   1326   -232       N  
ATOM   2199  CA  GLY A 281      89.382  52.693  45.763  1.00113.23           C  
ANISOU 2199  CA  GLY A 281    15202  12886  14934    116   1221   -149       C  
ATOM   2200  C   GLY A 281      90.327  53.876  45.704  1.00109.27           C  
ANISOU 2200  C   GLY A 281    14677  12387  14454    147   1168    -24       C  
ATOM   2201  O   GLY A 281      89.979  54.942  45.196  1.00107.08           O  
ANISOU 2201  O   GLY A 281    14333  12080  14272    169   1058     -7       O  
ATOM   2202  N   SER A 282      91.530  53.685  46.233  1.00104.78           N  
ANISOU 2202  N   SER A 282    14161  11848  13803    146   1237     68       N  
ATOM   2203  CA  SER A 282      92.521  54.750  46.287  1.00 98.50           C  
ANISOU 2203  CA  SER A 282    13349  11061  13017    165   1199    188       C  
ATOM   2204  C   SER A 282      93.940  54.192  46.239  1.00 84.21           C  
ANISOU 2204  C   SER A 282    11615   9302  11079    189   1262    316       C  
ATOM   2205  O   SER A 282      94.232  53.158  46.835  1.00 74.70           O  
ANISOU 2205  O   SER A 282    10460   8106   9817    169   1350    300       O  
ATOM   2206  CB  SER A 282      92.326  55.592  47.548  1.00100.77           C  
ANISOU 2206  CB  SER A 282    13568  11309  13412    110   1216    127       C  
ATOM   2207  OG  SER A 282      92.289  54.771  48.701  1.00104.65           O  
ANISOU 2207  OG  SER A 282    14089  11805  13870     41   1324     57       O  
ATOM   2208  N   CYS A 283      94.816  54.888  45.523  1.00 80.34           N  
ANISOU 2208  N   CYS A 283    11130   8843  10553    228   1210    442       N  
ATOM   2209  CA  CYS A 283      96.203  54.471  45.385  1.00 71.34           C  
ANISOU 2209  CA  CYS A 283    10044   7754   9308    255   1266    560       C  
ATOM   2210  C   CYS A 283      97.034  55.009  46.539  1.00 72.76           C  
ANISOU 2210  C   CYS A 283    10204   7930   9511    226   1297    619       C  
ATOM   2211  O   CYS A 283      97.092  56.218  46.757  1.00 82.33           O  
ANISOU 2211  O   CYS A 283    11368   9128  10786    211   1239    650       O  
ATOM   2212  CB  CYS A 283      96.770  54.975  44.058  1.00 69.68           C  
ANISOU 2212  CB  CYS A 283     9849   7590   9037    291   1204    663       C  
ATOM   2213  SG  CYS A 283      95.707  54.644  42.636  1.00 94.08           S  
ANISOU 2213  SG  CYS A 283    12960  10687  12099    298   1135    605       S  
ATOM   2214  N   VAL A 284      97.677  54.112  47.278  1.00 71.72           N  
ANISOU 2214  N   VAL A 284    10110   7806   9334    211   1380    639       N  
ATOM   2215  CA  VAL A 284      98.488  54.516  48.421  1.00 78.85           C  
ANISOU 2215  CA  VAL A 284    11002   8710  10248    168   1405    703       C  
ATOM   2216  C   VAL A 284      99.933  54.040  48.301  1.00 89.04           C  
ANISOU 2216  C   VAL A 284    12324  10040  11469    206   1443    832       C  
ATOM   2217  O   VAL A 284     100.276  53.288  47.388  1.00 88.88           O  
ANISOU 2217  O   VAL A 284    12332  10042  11395    263   1466    853       O  
ATOM   2218  CB  VAL A 284      97.892  54.010  49.746  1.00 72.44           C  
ANISOU 2218  CB  VAL A 284    10198   7862   9465     83   1456    609       C  
ATOM   2219  CG1 VAL A 284      96.544  54.663  50.000  1.00 73.07           C  
ANISOU 2219  CG1 VAL A 284    10223   7904   9635     38   1428    470       C  
ATOM   2220  CG2 VAL A 284      97.771  52.493  49.729  1.00 62.41           C  
ANISOU 2220  CG2 VAL A 284     8988   6584   8143     87   1512    576       C  
ATOM   2221  N   ARG A 285     100.772  54.482  49.233  1.00 88.69           N  
ANISOU 2221  N   ARG A 285    12266  10001  11430    167   1451    911       N  
ATOM   2222  CA  ARG A 285     102.195  54.167  49.197  1.00 86.58           C  
ANISOU 2222  CA  ARG A 285    12010   9769  11119    201   1477   1039       C  
ATOM   2223  C   ARG A 285     102.607  53.142  50.250  1.00 98.01           C  
ANISOU 2223  C   ARG A 285    13486  11189  12563    161   1521   1059       C  
ATOM   2224  O   ARG A 285     103.742  52.665  50.247  1.00101.03           O  
ANISOU 2224  O   ARG A 285    13870  11585  12931    195   1540   1158       O  
ATOM   2225  CB  ARG A 285     103.025  55.439  49.364  1.00 78.77           C  
ANISOU 2225  CB  ARG A 285    10984   8811  10136    188   1438   1142       C  
ATOM   2226  CG  ARG A 285     103.002  56.354  48.157  1.00 75.59           C  
ANISOU 2226  CG  ARG A 285    10561   8439   9721    232   1384   1169       C  
ATOM   2227  CD  ARG A 285     103.806  57.615  48.409  1.00 75.32           C  
ANISOU 2227  CD  ARG A 285    10494   8429   9693    209   1343   1271       C  
ATOM   2228  NE  ARG A 285     103.872  58.461  47.221  1.00 78.52           N  
ANISOU 2228  NE  ARG A 285    10891   8864  10078    239   1281   1314       N  
ATOM   2229  CZ  ARG A 285     104.307  59.716  47.225  1.00 82.45           C  
ANISOU 2229  CZ  ARG A 285    11364   9373  10589    217   1224   1390       C  
ATOM   2230  NH1 ARG A 285     104.711  60.273  48.359  1.00 88.56           N1+
ANISOU 2230  NH1 ARG A 285    12118  10133  11398    167   1229   1422       N1+
ATOM   2231  NH2 ARG A 285     104.333  60.417  46.099  1.00 76.70           N  
ANISOU 2231  NH2 ARG A 285    10638   8670   9835    232   1157   1436       N  
ATOM   2232  N   ALA A 286     101.688  52.808  51.150  1.00105.76           N  
ANISOU 2232  N   ALA A 286    14489  12131  13564     81   1533    967       N  
ATOM   2233  CA  ALA A 286     101.979  51.837  52.200  1.00113.57           C  
ANISOU 2233  CA  ALA A 286    15518  13090  14542     18   1560    991       C  
ATOM   2234  C   ALA A 286     100.713  51.236  52.800  1.00118.91           C  
ANISOU 2234  C   ALA A 286    16229  13729  15222    -64   1582    857       C  
ATOM   2235  O   ALA A 286      99.631  51.810  52.697  1.00120.70           O  
ANISOU 2235  O   ALA A 286    16431  13953  15475    -89   1578    742       O  
ATOM   2236  CB  ALA A 286     102.831  52.473  53.289  1.00115.04           C  
ANISOU 2236  CB  ALA A 286    15694  13290  14727    -59   1542   1091       C  
ATOM   2237  N   CYS A 287     100.857  50.072  53.423  1.00127.79           N  
ANISOU 2237  N   CYS A 287    17406  14819  16329   -108   1599    873       N  
ATOM   2238  CA  CYS A 287      99.752  49.435  54.126  1.00138.10           C  
ANISOU 2238  CA  CYS A 287    18754  16094  17624   -211   1622    757       C  
ATOM   2239  C   CYS A 287      99.911  49.672  55.620  1.00148.18           C  
ANISOU 2239  C   CYS A 287    20053  17370  18879   -368   1619    784       C  
ATOM   2240  O   CYS A 287     101.032  49.759  56.121  1.00153.86           O  
ANISOU 2240  O   CYS A 287    20778  18094  19589   -386   1592    921       O  
ATOM   2241  CB  CYS A 287      99.729  47.930  53.851  1.00139.15           C  
ANISOU 2241  CB  CYS A 287    18944  16183  17745   -178   1638    754       C  
ATOM   2242  SG  CYS A 287      99.943  47.462  52.118  1.00119.63           S  
ANISOU 2242  SG  CYS A 287    16457  13714  15283     -4   1652    750       S  
ATOM   2243  N   GLY A 288      98.793  49.776  56.330  1.00152.20           N  
ANISOU 2243  N   GLY A 288    20573  17876  19381   -491   1647    651       N  
ATOM   2244  CA  GLY A 288      98.833  49.930  57.771  1.00156.05           C  
ANISOU 2244  CA  GLY A 288    21092  18370  19829   -671   1655    656       C  
ATOM   2245  C   GLY A 288      99.668  48.832  58.402  1.00158.69           C  
ANISOU 2245  C   GLY A 288    21500  18675  20119   -725   1624    789       C  
ATOM   2246  O   GLY A 288      99.865  47.774  57.803  1.00157.83           O  
ANISOU 2246  O   GLY A 288    21420  18527  20021   -636   1611    827       O  
ATOM   2247  N   ALA A 289     100.165  49.081  59.609  1.00160.69           N  
ANISOU 2247  N   ALA A 289    21784  18942  20330   -876   1606    860       N  
ATOM   2248  CA  ALA A 289     100.967  48.089  60.317  1.00163.68           C  
ANISOU 2248  CA  ALA A 289    22233  19285  20675   -949   1552   1003       C  
ATOM   2249  C   ALA A 289     100.143  46.836  60.594  1.00167.31           C  
ANISOU 2249  C   ALA A 289    22769  19700  21102  -1030   1561    932       C  
ATOM   2250  O   ALA A 289     100.634  45.873  61.182  1.00167.76           O  
ANISOU 2250  O   ALA A 289    22893  19710  21137  -1102   1507   1040       O  
ATOM   2251  CB  ALA A 289     101.510  48.670  61.612  1.00162.54           C  
ANISOU 2251  CB  ALA A 289    22113  19170  20475  -1129   1526   1083       C  
ATOM   2252  N   ASP A 290      98.887  46.862  60.159  1.00167.77           N  
ANISOU 2252  N   ASP A 290    22813  19768  21165  -1020   1622    754       N  
ATOM   2253  CA  ASP A 290      97.964  45.756  60.370  1.00166.57           C  
ANISOU 2253  CA  ASP A 290    22728  19582  20978  -1102   1641    663       C  
ATOM   2254  C   ASP A 290      98.061  44.727  59.250  1.00162.29           C  
ANISOU 2254  C   ASP A 290    22195  18985  20482   -931   1627    685       C  
ATOM   2255  O   ASP A 290      97.446  43.664  59.325  1.00161.87           O  
ANISOU 2255  O   ASP A 290    22205  18891  20407   -979   1632    632       O  
ATOM   2256  CB  ASP A 290      96.528  46.278  60.452  1.00168.79           C  
ANISOU 2256  CB  ASP A 290    22978  19903  21253  -1179   1717    448       C  
ATOM   2257  CG  ASP A 290      96.388  47.460  61.389  1.00171.97           C  
ANISOU 2257  CG  ASP A 290    23347  20359  21634  -1326   1751    392       C  
ATOM   2258  OD1 ASP A 290      95.467  48.277  61.181  1.00174.00           O  
ANISOU 2258  OD1 ASP A 290    23532  20644  21935  -1323   1808    228       O  
ATOM   2259  OD2 ASP A 290      97.200  47.576  62.332  1.00172.28           O1-
ANISOU 2259  OD2 ASP A 290    23428  20409  21620  -1447   1717    510       O1-
ATOM   2260  N   SER A 291      98.831  45.042  58.213  1.00158.87           N  
ANISOU 2260  N   SER A 291    21702  18552  20107   -741   1614    755       N  
ATOM   2261  CA  SER A 291      98.895  44.182  57.036  1.00153.95           C  
ANISOU 2261  CA  SER A 291    21079  17887  19527   -580   1618    751       C  
ATOM   2262  C   SER A 291     100.218  44.270  56.280  1.00145.02           C  
ANISOU 2262  C   SER A 291    19902  16749  18452   -419   1592    884       C  
ATOM   2263  O   SER A 291     101.123  45.009  56.664  1.00143.12           O  
ANISOU 2263  O   SER A 291    19626  16534  18218   -427   1563    992       O  
ATOM   2264  CB  SER A 291      97.744  44.510  56.085  1.00156.83           C  
ANISOU 2264  CB  SER A 291    21407  18283  19899   -512   1669    587       C  
ATOM   2265  OG  SER A 291      97.777  45.874  55.700  1.00158.73           O  
ANISOU 2265  OG  SER A 291    21569  18581  20161   -460   1676    568       O  
ATOM   2266  N   TYR A 292     100.309  43.502  55.198  1.00142.37           N  
ANISOU 2266  N   TYR A 292    19563  16378  18153   -282   1609    866       N  
ATOM   2267  CA  TYR A 292     101.482  43.498  54.331  1.00146.83           C  
ANISOU 2267  CA  TYR A 292    20076  16939  18774   -128   1605    960       C  
ATOM   2268  C   TYR A 292     101.065  43.748  52.885  1.00138.64           C  
ANISOU 2268  C   TYR A 292    19001  15940  17734     -2   1656    864       C  
ATOM   2269  O   TYR A 292      99.909  44.076  52.615  1.00138.84           O  
ANISOU 2269  O   TYR A 292    19032  15995  17724    -30   1678    741       O  
ATOM   2270  CB  TYR A 292     102.221  42.164  54.443  1.00158.36           C  
ANISOU 2270  CB  TYR A 292    21568  18307  20296    -93   1577   1043       C  
ATOM   2271  CG  TYR A 292     101.303  40.964  54.459  1.00168.72           C  
ANISOU 2271  CG  TYR A 292    22954  19553  21598   -133   1588    952       C  
ATOM   2272  CD1 TYR A 292     100.778  40.449  53.281  1.00173.13           C  
ANISOU 2272  CD1 TYR A 292    23514  20104  22164    -31   1643    842       C  
ATOM   2273  CD2 TYR A 292     100.957  40.347  55.654  1.00173.86           C  
ANISOU 2273  CD2 TYR A 292    23682  20154  22224   -288   1542    977       C  
ATOM   2274  CE1 TYR A 292      99.935  39.354  53.292  1.00176.87           C  
ANISOU 2274  CE1 TYR A 292    24057  20517  22627    -71   1654    758       C  
ATOM   2275  CE2 TYR A 292     100.115  39.251  55.676  1.00177.95           C  
ANISOU 2275  CE2 TYR A 292    24273  20613  22729   -335   1549    896       C  
ATOM   2276  CZ  TYR A 292      99.607  38.759  54.492  1.00180.39           C  
ANISOU 2276  CZ  TYR A 292    24577  20911  23053   -220   1607    786       C  
ATOM   2277  OH  TYR A 292      98.769  37.667  54.507  1.00184.12           O  
ANISOU 2277  OH  TYR A 292    25123  21323  23510   -270   1615    704       O  
ATOM   2278  N   GLU A 293     102.003  43.591  51.957  1.00127.92           N  
ANISOU 2278  N   GLU A 293    17604  14584  16417    129   1672    918       N  
ATOM   2279  CA  GLU A 293     101.709  43.807  50.544  1.00124.42           C  
ANISOU 2279  CA  GLU A 293    17134  14184  15955    230   1717    838       C  
ATOM   2280  C   GLU A 293     101.638  42.496  49.767  1.00131.47           C  
ANISOU 2280  C   GLU A 293    18059  15022  16873    301   1758    779       C  
ATOM   2281  O   GLU A 293     102.662  41.909  49.421  1.00134.37           O  
ANISOU 2281  O   GLU A 293    18402  15354  17299    380   1776    837       O  
ATOM   2282  CB  GLU A 293     102.738  44.745  49.907  1.00119.66           C  
ANISOU 2282  CB  GLU A 293    16463  13644  15359    308   1720    919       C  
ATOM   2283  CG  GLU A 293     102.688  46.175  50.431  1.00114.77           C  
ANISOU 2283  CG  GLU A 293    15811  13084  14714    248   1683    957       C  
ATOM   2284  CD  GLU A 293     103.333  47.170  49.483  1.00102.65           C  
ANISOU 2284  CD  GLU A 293    14219  11620  13163    321   1687   1001       C  
ATOM   2285  OE1 GLU A 293     103.260  46.954  48.256  1.00 95.63           O  
ANISOU 2285  OE1 GLU A 293    13326  10754  12254    395   1722    952       O  
ATOM   2286  OE2 GLU A 293     103.905  48.172  49.964  1.00 96.97           O1-
ANISOU 2286  OE2 GLU A 293    13464  10935  12445    293   1656   1085       O1-
ATOM   2287  N   MET A 294     100.418  42.048  49.492  1.00140.16           N  
ANISOU 2287  N   MET A 294    19206  16112  17936    269   1777    657       N  
ATOM   2288  CA  MET A 294     100.195  40.802  48.770  1.00152.28           C  
ANISOU 2288  CA  MET A 294    20780  17593  19485    321   1819    584       C  
ATOM   2289  C   MET A 294      99.835  41.070  47.313  1.00159.89           C  
ANISOU 2289  C   MET A 294    21729  18619  20404    391   1864    498       C  
ATOM   2290  O   MET A 294      98.755  41.583  47.021  1.00166.82           O  
ANISOU 2290  O   MET A 294    22615  19543  21228    352   1854    417       O  
ATOM   2291  CB  MET A 294      99.074  39.999  49.438  1.00155.89           C  
ANISOU 2291  CB  MET A 294    21311  17997  19924    225   1809    505       C  
ATOM   2292  CG  MET A 294      98.710  38.704  48.723  1.00157.54           C  
ANISOU 2292  CG  MET A 294    21569  18146  20144    267   1850    419       C  
ATOM   2293  SD  MET A 294      99.743  37.304  49.200  1.00304.46           S  
ANISOU 2293  SD  MET A 294    40204  36622  38857    300   1838    502       S  
ATOM   2294  CE  MET A 294      99.136  36.977  50.854  1.00121.27           C  
ANISOU 2294  CE  MET A 294    17073  13366  15637    133   1766    540       C  
ATOM   2295  N   GLU A 295     100.739  40.727  46.400  1.00157.67           N  
ANISOU 2295  N   GLU A 295    21422  18340  20146    484   1912    514       N  
ATOM   2296  CA  GLU A 295     100.455  40.849  44.975  1.00155.10           C  
ANISOU 2296  CA  GLU A 295    21094  18075  19761    529   1959    433       C  
ATOM   2297  C   GLU A 295      99.229  40.016  44.622  1.00152.83           C  
ANISOU 2297  C   GLU A 295    20871  17758  19438    497   1977    307       C  
ATOM   2298  O   GLU A 295      99.160  38.831  44.946  1.00152.32           O  
ANISOU 2298  O   GLU A 295    20849  17608  19417    496   1997    275       O  
ATOM   2299  CB  GLU A 295     101.655  40.403  44.141  1.00158.77           C  
ANISOU 2299  CB  GLU A 295    21523  18539  20262    618   2027    450       C  
ATOM   2300  CG  GLU A 295     102.843  41.342  44.222  1.00166.45           C  
ANISOU 2300  CG  GLU A 295    22423  19564  21255    650   2017    564       C  
ATOM   2301  CD  GLU A 295     104.025  40.863  43.403  1.00176.98           C  
ANISOU 2301  CD  GLU A 295    23709  20899  22635    731   2096    562       C  
ATOM   2302  OE1 GLU A 295     103.906  39.807  42.746  1.00181.21           O  
ANISOU 2302  OE1 GLU A 295    24269  21392  23189    763   2164    465       O  
ATOM   2303  OE2 GLU A 295     105.073  41.543  43.417  1.00179.62           O1-
ANISOU 2303  OE2 GLU A 295    23978  21278  22991    758   2097    649       O1-
ATOM   2304  N   GLU A 296      98.262  40.639  43.959  1.00154.03           N  
ANISOU 2304  N   GLU A 296    21030  17977  19517    468   1960    239       N  
ATOM   2305  CA  GLU A 296      97.000  39.971  43.667  1.00157.00           C  
ANISOU 2305  CA  GLU A 296    21462  18335  19858    426   1966    121       C  
ATOM   2306  C   GLU A 296      96.748  39.898  42.164  1.00154.68           C  
ANISOU 2306  C   GLU A 296    21182  18096  19492    452   2001     49       C  
ATOM   2307  O   GLU A 296      95.952  40.665  41.620  1.00149.55           O  
ANISOU 2307  O   GLU A 296    20524  17508  18788    419   1956     19       O  
ATOM   2308  CB  GLU A 296      95.847  40.694  44.367  1.00164.15           C  
ANISOU 2308  CB  GLU A 296    22359  19258  20751    347   1903     89       C  
ATOM   2309  CG  GLU A 296      94.909  39.782  45.146  1.00168.67           C  
ANISOU 2309  CG  GLU A 296    22985  19768  21336    276   1905     13       C  
ATOM   2310  CD  GLU A 296      94.087  38.876  44.255  1.00173.28           C  
ANISOU 2310  CD  GLU A 296    23620  20341  21878    275   1937   -101       C  
ATOM   2311  OE1 GLU A 296      94.006  39.147  43.039  1.00176.03           O  
ANISOU 2311  OE1 GLU A 296    23960  20744  22178    311   1946   -131       O  
ATOM   2312  OE2 GLU A 296      93.517  37.893  44.775  1.00173.78           O1-
ANISOU 2312  OE2 GLU A 296    23737  20344  21949    225   1951   -159       O1-
ATOM   2313  N   ASP A 297      97.443  38.977  41.503  1.00159.02           N  
ANISOU 2313  N   ASP A 297    21750  18619  20049    503   2078     22       N  
ATOM   2314  CA  ASP A 297      97.246  38.714  40.078  1.00159.15           C  
ANISOU 2314  CA  ASP A 297    21794  18688  19988    507   2129    -60       C  
ATOM   2315  C   ASP A 297      97.847  39.779  39.160  1.00152.58           C  
ANISOU 2315  C   ASP A 297    20923  17958  19092    517   2126     -9       C  
ATOM   2316  O   ASP A 297      97.960  39.569  37.953  1.00155.81           O  
ANISOU 2316  O   ASP A 297    21353  18418  19427    510   2179    -66       O  
ATOM   2317  CB  ASP A 297      95.761  38.515  39.761  1.00162.68           C  
ANISOU 2317  CB  ASP A 297    22291  19145  20374    443   2095   -158       C  
ATOM   2318  CG  ASP A 297      95.182  37.285  40.433  1.00164.88           C  
ANISOU 2318  CG  ASP A 297    22622  19327  20696    424   2116   -226       C  
ATOM   2319  OD1 ASP A 297      95.969  36.467  40.955  1.00165.43           O  
ANISOU 2319  OD1 ASP A 297    22698  19316  20842    464   2158   -202       O  
ATOM   2320  OD2 ASP A 297      93.942  37.136  40.439  1.00164.68           O1-
ANISOU 2320  OD2 ASP A 297    22630  19305  20636    364   2083   -300       O1-
ATOM   2321  N   GLY A 298      98.232  40.918  39.725  1.00141.20           N  
ANISOU 2321  N   GLY A 298    19429  16549  17671    518   2064     95       N  
ATOM   2322  CA  GLY A 298      98.853  41.966  38.935  1.00130.75           C  
ANISOU 2322  CA  GLY A 298    18071  15318  16288    519   2052    156       C  
ATOM   2323  C   GLY A 298      98.832  43.337  39.581  1.00117.24           C  
ANISOU 2323  C   GLY A 298    16314  13637  14595    502   1958    255       C  
ATOM   2324  O   GLY A 298      99.451  44.276  39.080  1.00110.89           O  
ANISOU 2324  O   GLY A 298    15480  12903  13752    500   1938    326       O  
ATOM   2325  N   VAL A 299      98.119  43.457  40.696  1.00107.42           N  
ANISOU 2325  N   VAL A 299    15065  12341  13409    479   1903    255       N  
ATOM   2326  CA  VAL A 299      98.019  44.733  41.393  1.00 98.49           C  
ANISOU 2326  CA  VAL A 299    13887  11227  12307    456   1821    328       C  
ATOM   2327  C   VAL A 299      98.376  44.595  42.868  1.00 94.37           C  
ANISOU 2327  C   VAL A 299    13347  10645  11865    453   1822    375       C  
ATOM   2328  O   VAL A 299      97.845  43.737  43.571  1.00 88.56           O  
ANISOU 2328  O   VAL A 299    12643   9846  11160    429   1837    320       O  
ATOM   2329  CB  VAL A 299      96.613  45.348  41.252  1.00 94.15           C  
ANISOU 2329  CB  VAL A 299    13337  10688  11750    404   1739    270       C  
ATOM   2330  CG1 VAL A 299      96.355  45.751  39.806  1.00 90.79           C  
ANISOU 2330  CG1 VAL A 299    12925  10329  11241    391   1705    261       C  
ATOM   2331  CG2 VAL A 299      95.555  44.370  41.734  1.00 95.11           C  
ANISOU 2331  CG2 VAL A 299    13493  10751  11893    374   1756    163       C  
ATOM   2332  N   ARG A 300      99.289  45.442  43.328  1.00 97.69           N  
ANISOU 2332  N   ARG A 300    13722  11087  12310    465   1801    480       N  
ATOM   2333  CA  ARG A 300      99.699  45.431  44.723  1.00105.30           C  
ANISOU 2333  CA  ARG A 300    14670  12004  13337    444   1792    539       C  
ATOM   2334  C   ARG A 300      98.497  45.701  45.617  1.00109.15           C  
ANISOU 2334  C   ARG A 300    15164  12463  13844    368   1747    478       C  
ATOM   2335  O   ARG A 300      97.888  46.767  45.544  1.00116.09           O  
ANISOU 2335  O   ARG A 300    16013  13373  14724    341   1694    463       O  
ATOM   2336  CB  ARG A 300     100.784  46.481  44.961  1.00112.72           C  
ANISOU 2336  CB  ARG A 300    15557  12984  14288    458   1768    660       C  
ATOM   2337  CG  ARG A 300     102.027  46.281  44.112  1.00116.80           C  
ANISOU 2337  CG  ARG A 300    16053  13537  14789    524   1821    714       C  
ATOM   2338  CD  ARG A 300     102.818  45.069  44.573  1.00120.06           C  
ANISOU 2338  CD  ARG A 300    16468  13885  15266    563   1875    731       C  
ATOM   2339  NE  ARG A 300     103.462  45.299  45.863  1.00125.56           N  
ANISOU 2339  NE  ARG A 300    17138  14548  16023    541   1839    832       N  
ATOM   2340  CZ  ARG A 300     104.205  44.398  46.498  1.00134.44           C  
ANISOU 2340  CZ  ARG A 300    18256  15604  17221    563   1854    878       C  
ATOM   2341  NH1 ARG A 300     104.400  43.201  45.965  1.00135.44           N1+
ANISOU 2341  NH1 ARG A 300    18395  15680  17385    618   1910    823       N1+
ATOM   2342  NH2 ARG A 300     104.756  44.695  47.667  1.00139.38           N  
ANISOU 2342  NH2 ARG A 300    18863  16206  17890    524   1806    981       N  
ATOM   2343  N   LYS A 301      98.154  44.729  46.455  1.00106.97           N  
ANISOU 2343  N   LYS A 301    14928  12125  13592    329   1768    438       N  
ATOM   2344  CA  LYS A 301      97.002  44.858  47.340  1.00111.35           C  
ANISOU 2344  CA  LYS A 301    15491  12658  14160    240   1744    362       C  
ATOM   2345  C   LYS A 301      97.380  44.755  48.813  1.00112.24           C  
ANISOU 2345  C   LYS A 301    15613  12734  14300    166   1739    417       C  
ATOM   2346  O   LYS A 301      98.443  44.244  49.162  1.00108.46           O  
ANISOU 2346  O   LYS A 301    15146  12225  13837    188   1749    511       O  
ATOM   2347  CB  LYS A 301      95.945  43.804  47.004  1.00117.95           C  
ANISOU 2347  CB  LYS A 301    16378  13463  14977    220   1769    242       C  
ATOM   2348  CG  LYS A 301      94.845  44.292  46.078  1.00127.23           C  
ANISOU 2348  CG  LYS A 301    17533  14676  16132    223   1741    150       C  
ATOM   2349  CD  LYS A 301      93.824  43.195  45.821  1.00137.91           C  
ANISOU 2349  CD  LYS A 301    18937  15999  17464    195   1767     34       C  
ATOM   2350  CE  LYS A 301      92.470  43.771  45.440  1.00148.09           C  
ANISOU 2350  CE  LYS A 301    20192  17313  18761    160   1722    -67       C  
ATOM   2351  NZ  LYS A 301      92.567  44.725  44.302  1.00154.28           N1+
ANISOU 2351  NZ  LYS A 301    20937  18150  19532    210   1670    -31       N1+
ATOM   2352  N   CYS A 302      96.495  45.248  49.672  1.00121.25           N  
ANISOU 2352  N   CYS A 302    16744  13875  15449     70   1722    354       N  
ATOM   2353  CA  CYS A 302      96.686  45.157  51.113  1.00134.30           C  
ANISOU 2353  CA  CYS A 302    18417  15502  17107    -37   1719    389       C  
ATOM   2354  C   CYS A 302      95.627  44.256  51.736  1.00149.86           C  
ANISOU 2354  C   CYS A 302    20442  17437  19061   -138   1740    282       C  
ATOM   2355  O   CYS A 302      94.432  44.437  51.503  1.00153.00           O  
ANISOU 2355  O   CYS A 302    20824  17849  19461   -168   1749    154       O  
ATOM   2356  CB  CYS A 302      96.623  46.545  51.752  1.00133.34           C  
ANISOU 2356  CB  CYS A 302    18240  15419  17005    -94   1696    396       C  
ATOM   2357  SG  CYS A 302      98.046  47.595  51.409  1.00161.90           S  
ANISOU 2357  SG  CYS A 302    21805  19075  20634    -13   1666    548       S  
ATOM   2358  N   LYS A 303      96.071  43.285  52.527  1.00160.23           N  
ANISOU 2358  N   LYS A 303    21817  18699  20363   -196   1740    339       N  
ATOM   2359  CA  LYS A 303      95.152  42.391  53.219  1.00171.07           C  
ANISOU 2359  CA  LYS A 303    23254  20037  21708   -314   1755    253       C  
ATOM   2360  C   LYS A 303      95.236  42.605  54.726  1.00178.13           C  
ANISOU 2360  C   LYS A 303    24173  20930  22578   -478   1742    287       C  
ATOM   2361  O   LYS A 303      95.068  43.723  55.211  1.00180.26           O  
ANISOU 2361  O   LYS A 303    24394  21248  22849   -536   1745    263       O  
ATOM   2362  CB  LYS A 303      95.455  40.934  52.868  1.00172.20           C  
ANISOU 2362  CB  LYS A 303    23466  20109  21855   -269   1758    282       C  
ATOM   2363  CG  LYS A 303      95.609  40.682  51.376  1.00173.57           C  
ANISOU 2363  CG  LYS A 303    23618  20285  22044   -115   1781    259       C  
ATOM   2364  CD  LYS A 303      95.401  39.215  51.026  1.00175.76           C  
ANISOU 2364  CD  LYS A 303    23966  20491  22323    -97   1801    220       C  
ATOM   2365  CE  LYS A 303      93.921  38.871  50.900  1.00173.75           C  
ANISOU 2365  CE  LYS A 303    23741  20246  22028   -167   1823     68       C  
ATOM   2366  NZ  LYS A 303      93.172  39.057  52.175  1.00171.39           N1+
ANISOU 2366  NZ  LYS A 303    23463  19957  21702   -332   1814     24       N1+
ATOM   2367  N   LYS A 304      95.489  41.527  55.461  1.00179.84           N  
ANISOU 2367  N   LYS A 304    24470  21089  22772   -561   1723    343       N  
ATOM   2368  CA  LYS A 304      95.706  41.610  56.901  1.00181.07           C  
ANISOU 2368  CA  LYS A 304    24667  21243  22888   -737   1698    401       C  
ATOM   2369  C   LYS A 304      96.746  40.593  57.358  1.00189.28           C  
ANISOU 2369  C   LYS A 304    25772  22204  23939   -749   1636    560       C  
ATOM   2370  O   LYS A 304      96.908  39.538  56.746  1.00189.64           O  
ANISOU 2370  O   LYS A 304    25851  22183  24021   -661   1627    577       O  
ATOM   2371  CB  LYS A 304      94.399  41.413  57.675  1.00173.72           C  
ANISOU 2371  CB  LYS A 304    23777  20330  21898   -919   1734    257       C  
ATOM   2372  CG  LYS A 304      93.828  42.690  58.283  1.00171.18           C  
ANISOU 2372  CG  LYS A 304    23395  20083  21564  -1023   1773    160       C  
ATOM   2373  CD  LYS A 304      92.941  43.452  57.309  1.00171.34           C  
ANISOU 2373  CD  LYS A 304    23324  20142  21637   -918   1812     17       C  
ATOM   2374  CE  LYS A 304      91.586  42.779  57.149  1.00170.73           C  
ANISOU 2374  CE  LYS A 304    23265  20060  21545   -975   1853   -148       C  
ATOM   2375  NZ  LYS A 304      90.636  43.613  56.360  1.00167.61           N1+
ANISOU 2375  NZ  LYS A 304    22770  19700  21213   -900   1878   -291       N1+
ATOM   2376  N   CYS A 305      97.452  40.921  58.435  1.00197.22           N  
ANISOU 2376  N   CYS A 305    26796  23215  24925   -862   1590    675       N  
ATOM   2377  CA  CYS A 305      98.447  40.019  58.999  1.00206.11           C  
ANISOU 2377  CA  CYS A 305    27978  24260  26075   -893   1508    842       C  
ATOM   2378  C   CYS A 305      97.793  39.023  59.948  1.00214.84           C  
ANISOU 2378  C   CYS A 305    29194  25319  27118  -1087   1480    824       C  
ATOM   2379  O   CYS A 305      96.813  39.343  60.622  1.00221.69           O  
ANISOU 2379  O   CYS A 305    30090  26241  27900  -1256   1521    712       O  
ATOM   2380  CB  CYS A 305      99.538  40.802  59.732  1.00206.17           C  
ANISOU 2380  CB  CYS A 305    27958  24293  26084   -939   1456    990       C  
ATOM   2381  SG  CYS A 305     100.682  41.692  58.650  1.00299.10           S  
ANISOU 2381  SG  CYS A 305    39611  36095  37938   -710   1465   1066       S  
ATOM   2382  N   GLU A 306      98.342  37.815  59.997  1.00216.16           N  
ANISOU 2382  N   GLU A 306    29418  25379  27333  -1066   1409    931       N  
ATOM   2383  CA  GLU A 306      97.798  36.764  60.847  1.00215.70           C  
ANISOU 2383  CA  GLU A 306    29475  25261  27219  -1251   1364    936       C  
ATOM   2384  C   GLU A 306      98.410  36.838  62.242  1.00217.55           C  
ANISOU 2384  C   GLU A 306    29769  25488  27402  -1454   1270   1088       C  
ATOM   2385  O   GLU A 306      98.739  35.815  62.842  1.00221.36           O  
ANISOU 2385  O   GLU A 306    30336  25874  27895  -1549   1171   1206       O  
ATOM   2386  CB  GLU A 306      98.059  35.391  60.225  1.00214.47           C  
ANISOU 2386  CB  GLU A 306    29356  24979  27153  -1137   1321    977       C  
ATOM   2387  CG  GLU A 306      97.010  34.344  60.562  1.00215.63           C  
ANISOU 2387  CG  GLU A 306    29611  25081  27239  -1277   1320    895       C  
ATOM   2388  CD  GLU A 306      95.685  34.603  59.869  1.00216.49           C  
ANISOU 2388  CD  GLU A 306    29697  25266  27293  -1254   1435    679       C  
ATOM   2389  OE1 GLU A 306      95.600  35.572  59.086  1.00215.13           O  
ANISOU 2389  OE1 GLU A 306    29428  25172  27139  -1122   1506    601       O  
ATOM   2390  OE2 GLU A 306      94.728  33.835  60.106  1.00218.05           O1-
ANISOU 2390  OE2 GLU A 306    29975  25442  27433  -1373   1448    591       O1-
ATOM   2391  N   GLY A 307      98.559  38.057  62.751  1.00214.65           N  
ANISOU 2391  N   GLY A 307    29358  25217  26982  -1528   1296   1088       N  
ATOM   2392  CA  GLY A 307      99.163  38.277  64.052  1.00214.83           C  
ANISOU 2392  CA  GLY A 307    29433  25249  26942  -1732   1213   1229       C  
ATOM   2393  C   GLY A 307     100.052  39.505  64.057  1.00214.41           C  
ANISOU 2393  C   GLY A 307    29292  25260  26914  -1665   1215   1302       C  
ATOM   2394  O   GLY A 307      99.672  40.549  63.530  1.00214.64           O  
ANISOU 2394  O   GLY A 307    29240  25372  26940  -1584   1310   1180       O  
ATOM   2395  N   PRO A 308     101.244  39.388  64.660  1.00215.04           N  
ANISOU 2395  N   PRO A 308    29386  25297  27025  -1705   1100   1508       N  
ATOM   2396  CA  PRO A 308     102.220  40.482  64.697  1.00214.61           C  
ANISOU 2396  CA  PRO A 308    29250  25296  26997  -1646   1089   1600       C  
ATOM   2397  C   PRO A 308     102.878  40.691  63.336  1.00214.21           C  
ANISOU 2397  C   PRO A 308    29084  25228  27077  -1348   1119   1608       C  
ATOM   2398  O   PRO A 308     103.747  39.908  62.951  1.00217.98           O  
ANISOU 2398  O   PRO A 308    29542  25612  27667  -1222   1047   1729       O  
ATOM   2399  CB  PRO A 308     103.266  39.989  65.708  1.00215.73           C  
ANISOU 2399  CB  PRO A 308    29448  25375  27145  -1778    936   1830       C  
ATOM   2400  CG  PRO A 308     102.614  38.852  66.439  1.00217.27           C  
ANISOU 2400  CG  PRO A 308    29772  25506  27274  -1974    878   1835       C  
ATOM   2401  CD  PRO A 308     101.689  38.230  65.450  1.00216.49           C  
ANISOU 2401  CD  PRO A 308    29667  25376  27212  -1836    963   1670       C  
ATOM   2402  N   CYS A 309     102.467  41.733  62.621  1.00207.16           N  
ANISOU 2402  N   CYS A 309    28114  24420  26175  -1246   1223   1477       N  
ATOM   2403  CA  CYS A 309     103.030  42.027  61.307  1.00197.42           C  
ANISOU 2403  CA  CYS A 309    26780  23189  25042   -990   1259   1475       C  
ATOM   2404  C   CYS A 309     104.535  42.260  61.377  1.00189.85           C  
ANISOU 2404  C   CYS A 309    25765  22212  24159   -917   1184   1663       C  
ATOM   2405  O   CYS A 309     105.055  42.741  62.384  1.00187.75           O  
ANISOU 2405  O   CYS A 309    25515  21972  23849  -1059   1125   1772       O  
ATOM   2406  CB  CYS A 309     102.344  43.246  60.682  1.00194.10           C  
ANISOU 2406  CB  CYS A 309    26296  22866  24589   -931   1360   1324       C  
ATOM   2407  SG  CYS A 309     100.618  42.992  60.219  1.00214.56           S  
ANISOU 2407  SG  CYS A 309    28915  25473  27135   -951   1452   1091       S  
ATOM   2408  N   ARG A 310     105.232  41.912  60.301  1.00185.33           N  
ANISOU 2408  N   ARG A 310    25121  21597  23698   -703   1190   1695       N  
ATOM   2409  CA  ARG A 310     106.656  42.194  60.208  1.00183.10           C  
ANISOU 2409  CA  ARG A 310    24761  21306  23503   -612   1135   1852       C  
ATOM   2410  C   ARG A 310     106.902  43.679  60.444  1.00186.44           C  
ANISOU 2410  C   ARG A 310    25138  21839  23861   -653   1161   1864       C  
ATOM   2411  O   ARG A 310     106.082  44.520  60.072  1.00189.52           O  
ANISOU 2411  O   ARG A 310    25518  22305  24186   -650   1245   1728       O  
ATOM   2412  CB  ARG A 310     107.201  41.782  58.841  1.00177.11           C  
ANISOU 2412  CB  ARG A 310    23919  20512  22861   -375   1179   1829       C  
ATOM   2413  CG  ARG A 310     107.259  40.283  58.612  1.00176.12           C  
ANISOU 2413  CG  ARG A 310    23822  20259  22836   -316   1144   1840       C  
ATOM   2414  CD  ARG A 310     108.047  39.967  57.350  1.00177.86           C  
ANISOU 2414  CD  ARG A 310    23945  20449  23186    -94   1191   1827       C  
ATOM   2415  NE  ARG A 310     108.161  38.530  57.117  1.00182.37           N  
ANISOU 2415  NE  ARG A 310    24533  20885  23877    -30   1160   1829       N  
ATOM   2416  CZ  ARG A 310     108.874  37.981  56.138  1.00183.37           C  
ANISOU 2416  CZ  ARG A 310    24577  20955  24140    148   1198   1812       C  
ATOM   2417  NH1 ARG A 310     109.547  38.746  55.288  1.00182.26           N1+
ANISOU 2417  NH1 ARG A 310    24336  20894  24022    271   1268   1796       N1+
ATOM   2418  NH2 ARG A 310     108.914  36.662  56.010  1.00183.98           N  
ANISOU 2418  NH2 ARG A 310    24673  20896  24335    195   1168   1805       N  
ATOM   2419  N   LYS A 311     108.027  44.000  61.071  1.00186.23           N  
ANISOU 2419  N   LYS A 311    25083  21815  23862   -695   1082   2030       N  
ATOM   2420  CA  LYS A 311     108.361  45.390  61.351  1.00183.98           C  
ANISOU 2420  CA  LYS A 311    24758  21627  23519   -743   1099   2055       C  
ATOM   2421  C   LYS A 311     108.464  46.221  60.074  1.00175.57           C  
ANISOU 2421  C   LYS A 311    23603  20624  22481   -558   1186   1977       C  
ATOM   2422  O   LYS A 311     109.204  45.877  59.152  1.00176.57           O  
ANISOU 2422  O   LYS A 311    23660  20725  22702   -387   1193   2014       O  
ATOM   2423  CB  LYS A 311     109.660  45.487  62.155  1.00189.92           C  
ANISOU 2423  CB  LYS A 311    25488  22365  24306   -807    991   2261       C  
ATOM   2424  CG  LYS A 311     110.323  46.852  62.079  1.00193.42           C  
ANISOU 2424  CG  LYS A 311    25862  22902  24728   -787   1011   2303       C  
ATOM   2425  CD  LYS A 311     111.200  47.119  63.289  1.00195.43           C  
ANISOU 2425  CD  LYS A 311    26134  23164  24959   -948    905   2480       C  
ATOM   2426  CE  LYS A 311     110.356  47.352  64.531  1.00198.36           C  
ANISOU 2426  CE  LYS A 311    26613  23565  25190  -1208    897   2439       C  
ATOM   2427  NZ  LYS A 311     111.173  47.791  65.695  1.00201.95           N1+
ANISOU 2427  NZ  LYS A 311    27090  24047  25594  -1388    802   2602       N1+
ATOM   2428  N   VAL A 312     107.708  47.313  60.028  1.00162.84           N  
ANISOU 2428  N   VAL A 312    21990  19090  20790   -604   1250   1865       N  
ATOM   2429  CA  VAL A 312     107.777  48.247  58.912  1.00148.54           C  
ANISOU 2429  CA  VAL A 312    20105  17340  18994   -460   1313   1807       C  
ATOM   2430  C   VAL A 312     108.705  49.406  59.260  1.00131.74           C  
ANISOU 2430  C   VAL A 312    17928  15273  16854   -489   1286   1913       C  
ATOM   2431  O   VAL A 312     108.476  50.124  60.234  1.00131.56           O  
ANISOU 2431  O   VAL A 312    17937  15286  16766   -646   1275   1914       O  
ATOM   2432  CB  VAL A 312     106.384  48.791  58.537  1.00150.36           C  
ANISOU 2432  CB  VAL A 312    20352  17606  19173   -475   1386   1621       C  
ATOM   2433  CG1 VAL A 312     105.663  49.319  59.770  1.00146.76           C  
ANISOU 2433  CG1 VAL A 312    19947  17175  18642   -680   1387   1567       C  
ATOM   2434  CG2 VAL A 312     106.505  49.872  57.474  1.00153.30           C  
ANISOU 2434  CG2 VAL A 312    20652  18038  19558   -351   1425   1586       C  
ATOM   2435  N   CYS A 313     109.756  49.582  58.467  1.00115.48           N  
ANISOU 2435  N   CYS A 313    15792  13230  14857   -348   1283   1995       N  
ATOM   2436  CA  CYS A 313     110.748  50.617  58.736  1.00101.52           C  
ANISOU 2436  CA  CYS A 313    13972  11518  13081   -368   1254   2108       C  
ATOM   2437  C   CYS A 313     110.545  51.850  57.865  1.00 91.12           C  
ANISOU 2437  C   CYS A 313    12610  10274  11737   -296   1311   2037       C  
ATOM   2438  O   CYS A 313     110.654  51.783  56.642  1.00 93.50           O  
ANISOU 2438  O   CYS A 313    12868  10587  12070   -150   1351   1999       O  
ATOM   2439  CB  CYS A 313     112.161  50.068  58.535  1.00 98.49           C  
ANISOU 2439  CB  CYS A 313    13522  11108  12790   -277   1206   2258       C  
ATOM   2440  SG  CYS A 313     112.512  48.569  59.476  1.00119.16           S  
ANISOU 2440  SG  CYS A 313    16182  13618  15476   -346   1110   2366       S  
ATOM   2441  N   ASN A 314     110.248  52.976  58.502  1.00 80.96           N  
ANISOU 2441  N   ASN A 314    11338   9031  10393   -409   1310   2018       N  
ATOM   2442  CA  ASN A 314     110.125  54.236  57.786  1.00 84.69           C  
ANISOU 2442  CA  ASN A 314    11768   9559  10851   -355   1342   1971       C  
ATOM   2443  C   ASN A 314     111.457  54.656  57.186  1.00 85.39           C  
ANISOU 2443  C   ASN A 314    11787   9690  10968   -261   1325   2097       C  
ATOM   2444  O   ASN A 314     112.482  54.654  57.864  1.00 90.08           O  
ANISOU 2444  O   ASN A 314    12363  10292  11572   -311   1278   2233       O  
ATOM   2445  CB  ASN A 314     109.594  55.332  58.708  1.00 95.42           C  
ANISOU 2445  CB  ASN A 314    13152  10942  12161   -504   1343   1923       C  
ATOM   2446  CG  ASN A 314     108.085  55.316  58.821  1.00104.22           C  
ANISOU 2446  CG  ASN A 314    14304  12032  13262   -557   1387   1744       C  
ATOM   2447  ND2 ASN A 314     107.571  55.795  59.948  1.00110.14           N  
ANISOU 2447  ND2 ASN A 314    15087  12786  13973   -726   1396   1688       N  
ATOM   2448  OD1 ASN A 314     107.388  54.884  57.903  1.00105.25           O  
ANISOU 2448  OD1 ASN A 314    14430  12143  13418   -455   1415   1650       O  
ATOM   2449  N   GLY A 315     111.439  55.012  55.907  1.00 85.20           N  
ANISOU 2449  N   GLY A 315    11724   9697  10953   -136   1360   2054       N  
ATOM   2450  CA  GLY A 315     112.645  55.440  55.227  1.00 89.53           C  
ANISOU 2450  CA  GLY A 315    12204  10296  11517    -55   1358   2156       C  
ATOM   2451  C   GLY A 315     113.067  56.841  55.624  1.00 85.05           C  
ANISOU 2451  C   GLY A 315    11621   9781  10914   -127   1331   2219       C  
ATOM   2452  O   GLY A 315     112.245  57.647  56.060  1.00 84.53           O  
ANISOU 2452  O   GLY A 315    11588   9713  10817   -209   1328   2148       O  
ATOM   2453  N   ILE A 316     114.356  57.126  55.477  1.00 79.18           N  
ANISOU 2453  N   ILE A 316    10820   9082  10184    -98   1314   2345       N  
ATOM   2454  CA  ILE A 316     114.881  58.456  55.746  1.00 78.52           C  
ANISOU 2454  CA  ILE A 316    10718   9052  10066   -159   1288   2414       C  
ATOM   2455  C   ILE A 316     114.030  59.509  55.046  1.00 82.92           C  
ANISOU 2455  C   ILE A 316    11291   9625  10590   -146   1304   2318       C  
ATOM   2456  O   ILE A 316     113.652  59.341  53.888  1.00 87.06           O  
ANISOU 2456  O   ILE A 316    11808  10155  11114    -51   1333   2253       O  
ATOM   2457  CB  ILE A 316     116.335  58.590  55.258  1.00 77.47           C  
ANISOU 2457  CB  ILE A 316    10507   8975   9953    -97   1283   2541       C  
ATOM   2458  CG1 ILE A 316     117.209  57.496  55.871  1.00 85.09           C  
ANISOU 2458  CG1 ILE A 316    11438   9909  10983    -94   1254   2640       C  
ATOM   2459  CG2 ILE A 316     116.886  59.967  55.591  1.00 76.51           C  
ANISOU 2459  CG2 ILE A 316    10372   8908   9789   -173   1253   2619       C  
ATOM   2460  CD1 ILE A 316     117.391  57.624  57.366  1.00 88.26           C  
ANISOU 2460  CD1 ILE A 316    11872  10291  11370   -242   1188   2725       C  
ATOM   2461  N   GLY A 317     113.724  60.589  55.755  1.00 80.59           N  
ANISOU 2461  N   GLY A 317    11017   9333  10272   -249   1281   2308       N  
ATOM   2462  CA  GLY A 317     112.978  61.690  55.175  1.00 78.81           C  
ANISOU 2462  CA  GLY A 317    10797   9106  10041   -241   1277   2229       C  
ATOM   2463  C   GLY A 317     111.485  61.620  55.431  1.00 82.63           C  
ANISOU 2463  C   GLY A 317    11318   9529  10547   -274   1292   2071       C  
ATOM   2464  O   GLY A 317     110.718  62.418  54.889  1.00 90.87           O  
ANISOU 2464  O   GLY A 317    12359  10555  11612   -255   1280   1991       O  
ATOM   2465  N   ILE A 318     111.066  60.667  56.258  1.00 73.15           N  
ANISOU 2465  N   ILE A 318    10151   8295   9347   -330   1311   2027       N  
ATOM   2466  CA  ILE A 318     109.655  60.530  56.591  1.00 70.87           C  
ANISOU 2466  CA  ILE A 318     9894   7956   9079   -377   1335   1869       C  
ATOM   2467  C   ILE A 318     109.461  60.128  58.049  1.00 80.28           C  
ANISOU 2467  C   ILE A 318    11127   9129  10247   -528   1347   1850       C  
ATOM   2468  O   ILE A 318     110.316  59.466  58.640  1.00 80.85           O  
ANISOU 2468  O   ILE A 318    11214   9214  10292   -569   1329   1964       O  
ATOM   2469  CB  ILE A 318     108.956  59.497  55.689  1.00 70.99           C  
ANISOU 2469  CB  ILE A 318     9918   7946   9109   -274   1359   1788       C  
ATOM   2470  CG1 ILE A 318     107.460  59.799  55.589  1.00 74.13           C  
ANISOU 2470  CG1 ILE A 318    10323   8299   9542   -291   1372   1619       C  
ATOM   2471  CG2 ILE A 318     109.191  58.086  56.208  1.00 72.63           C  
ANISOU 2471  CG2 ILE A 318    10156   8134   9305   -290   1373   1819       C  
ATOM   2472  CD1 ILE A 318     106.673  58.743  54.843  1.00 77.47           C  
ANISOU 2472  CD1 ILE A 318    10762   8697   9974   -212   1394   1532       C  
ATOM   2473  N   GLY A 319     108.334  60.540  58.621  1.00 83.10           N  
ANISOU 2473  N   GLY A 319    11501   9456  10618   -620   1374   1706       N  
ATOM   2474  CA  GLY A 319     107.985  60.193  59.986  1.00 86.21           C  
ANISOU 2474  CA  GLY A 319    11942   9840  10975   -790   1397   1661       C  
ATOM   2475  C   GLY A 319     109.095  60.427  60.993  1.00 89.60           C  
ANISOU 2475  C   GLY A 319    12389  10304  11349   -911   1367   1802       C  
ATOM   2476  O   GLY A 319     109.578  61.547  61.156  1.00 87.43           O  
ANISOU 2476  O   GLY A 319    12091  10055  11074   -945   1355   1842       O  
ATOM   2477  N   GLU A 320     109.499  59.356  61.668  1.00 92.07           N  
ANISOU 2477  N   GLU A 320    12746  10616  11620   -980   1347   1882       N  
ATOM   2478  CA  GLU A 320     110.517  59.432  62.710  1.00 98.06           C  
ANISOU 2478  CA  GLU A 320    13528  11405  12325  -1114   1302   2026       C  
ATOM   2479  C   GLU A 320     111.856  59.961  62.200  1.00103.68           C  
ANISOU 2479  C   GLU A 320    14185  12155  13053  -1023   1256   2189       C  
ATOM   2480  O   GLU A 320     112.774  60.199  62.985  1.00110.24           O  
ANISOU 2480  O   GLU A 320    15023  13016  13846  -1127   1213   2317       O  
ATOM   2481  CB  GLU A 320     110.712  58.058  63.353  1.00104.90           C  
ANISOU 2481  CB  GLU A 320    14448  12248  13162  -1184   1265   2100       C  
ATOM   2482  CG  GLU A 320     110.806  56.919  62.352  1.00114.37           C  
ANISOU 2482  CG  GLU A 320    15626  13410  14420  -1005   1253   2125       C  
ATOM   2483  CD  GLU A 320     110.996  55.568  63.016  1.00126.39           C  
ANISOU 2483  CD  GLU A 320    17201  14892  15931  -1076   1203   2203       C  
ATOM   2484  OE1 GLU A 320     110.696  54.540  62.373  1.00126.82           O  
ANISOU 2484  OE1 GLU A 320    17257  14900  16030   -965   1209   2172       O  
ATOM   2485  OE2 GLU A 320     111.444  55.534  64.183  1.00132.39           O1-
ANISOU 2485  OE2 GLU A 320    18004  15661  16636  -1251   1152   2297       O1-
ATOM   2486  N   PHE A 321     111.967  60.143  60.888  1.00100.17           N  
ANISOU 2486  N   PHE A 321    13687  11714  12659   -841   1265   2183       N  
ATOM   2487  CA  PHE A 321     113.214  60.611  60.294  1.00 95.09           C  
ANISOU 2487  CA  PHE A 321    12988  11114  12028   -754   1232   2324       C  
ATOM   2488  C   PHE A 321     112.991  61.750  59.309  1.00105.88           C  
ANISOU 2488  C   PHE A 321    14317  12497  13414   -667   1249   2271       C  
ATOM   2489  O   PHE A 321     113.767  61.932  58.373  1.00111.28           O  
ANISOU 2489  O   PHE A 321    14956  13215  14111   -555   1237   2351       O  
ATOM   2490  CB  PHE A 321     113.940  59.459  59.601  1.00 83.83           C  
ANISOU 2490  CB  PHE A 321    11528   9682  10640   -623   1215   2413       C  
ATOM   2491  CG  PHE A 321     114.212  58.293  60.501  1.00 79.84           C  
ANISOU 2491  CG  PHE A 321    11055   9144  10136   -698   1177   2484       C  
ATOM   2492  CD1 PHE A 321     115.046  58.429  61.597  1.00 82.64           C  
ANISOU 2492  CD1 PHE A 321    11420   9516  10462   -832   1118   2617       C  
ATOM   2493  CD2 PHE A 321     113.635  57.061  60.254  1.00 72.70           C  
ANISOU 2493  CD2 PHE A 321    10175   8186   9262   -643   1190   2424       C  
ATOM   2494  CE1 PHE A 321     115.296  57.358  62.429  1.00 85.17           C  
ANISOU 2494  CE1 PHE A 321    11775   9799  10787   -914   1061   2697       C  
ATOM   2495  CE2 PHE A 321     113.884  55.987  61.082  1.00 75.50           C  
ANISOU 2495  CE2 PHE A 321    10565   8498   9624   -719   1139   2499       C  
ATOM   2496  CZ  PHE A 321     114.716  56.136  62.171  1.00 82.44           C  
ANISOU 2496  CZ  PHE A 321    11454   9392  10477   -856   1069   2640       C  
ATOM   2497  N   LYS A 322     111.929  62.517  59.527  1.00110.32           N  
ANISOU 2497  N   LYS A 322    14897  13032  13986   -725   1275   2132       N  
ATOM   2498  CA  LYS A 322     111.622  63.651  58.667  1.00112.62           C  
ANISOU 2498  CA  LYS A 322    15157  13322  14313   -656   1271   2083       C  
ATOM   2499  C   LYS A 322     112.758  64.670  58.680  1.00117.48           C  
ANISOU 2499  C   LYS A 322    15746  13984  14907   -677   1236   2213       C  
ATOM   2500  O   LYS A 322     113.027  65.326  57.674  1.00125.16           O  
ANISOU 2500  O   LYS A 322    16688  14973  15894   -586   1215   2246       O  
ATOM   2501  CB  LYS A 322     110.311  64.310  59.102  1.00117.54           C  
ANISOU 2501  CB  LYS A 322    15791  13893  14977   -731   1299   1907       C  
ATOM   2502  CG  LYS A 322     109.936  65.542  58.298  1.00126.96           C  
ANISOU 2502  CG  LYS A 322    16947  15061  16229   -668   1275   1858       C  
ATOM   2503  CD  LYS A 322     109.690  65.199  56.838  1.00132.72           C  
ANISOU 2503  CD  LYS A 322    17658  15787  16983   -509   1254   1856       C  
ATOM   2504  CE  LYS A 322     109.429  66.452  56.018  1.00136.68           C  
ANISOU 2504  CE  LYS A 322    18130  16263  17540   -460   1205   1840       C  
ATOM   2505  NZ  LYS A 322     108.294  67.247  56.565  1.00139.46           N1+
ANISOU 2505  NZ  LYS A 322    18466  16541  17981   -526   1210   1684       N1+
ATOM   2506  N   ASP A 323     113.427  64.790  59.824  1.00115.71           N  
ANISOU 2506  N   ASP A 323    15539  13785  14641   -808   1225   2292       N  
ATOM   2507  CA  ASP A 323     114.498  65.769  59.993  1.00110.15           C  
ANISOU 2507  CA  ASP A 323    14814  13127  13912   -851   1192   2415       C  
ATOM   2508  C   ASP A 323     115.838  65.275  59.457  1.00 96.24           C  
ANISOU 2508  C   ASP A 323    13011  11421  12135   -767   1162   2583       C  
ATOM   2509  O   ASP A 323     116.590  66.038  58.854  1.00 92.49           O  
ANISOU 2509  O   ASP A 323    12500  10988  11655   -723   1142   2663       O  
ATOM   2510  CB  ASP A 323     114.642  66.159  61.466  1.00117.67           C  
ANISOU 2510  CB  ASP A 323    15803  14087  14820  -1046   1192   2426       C  
ATOM   2511  CG  ASP A 323     113.464  66.965  61.974  1.00122.84           C  
ANISOU 2511  CG  ASP A 323    16480  14692  15499  -1141   1234   2249       C  
ATOM   2512  OD1 ASP A 323     113.355  67.149  63.206  1.00127.13           O  
ANISOU 2512  OD1 ASP A 323    17062  15240  16001  -1319   1254   2217       O  
ATOM   2513  OD2 ASP A 323     112.648  67.416  61.143  1.00119.25           O1-
ANISOU 2513  OD2 ASP A 323    16002  14194  15112  -1045   1245   2140       O1-
ATOM   2514  N   SER A 324     116.137  64.001  59.685  1.00 91.51           N  
ANISOU 2514  N   SER A 324    12412  10818  11539   -748   1158   2632       N  
ATOM   2515  CA  SER A 324     117.415  63.434  59.267  1.00 91.21           C  
ANISOU 2515  CA  SER A 324    12318  10822  11514   -669   1132   2779       C  
ATOM   2516  C   SER A 324     117.537  63.381  57.747  1.00 79.71           C  
ANISOU 2516  C   SER A 324    10816   9386  10084   -504   1159   2761       C  
ATOM   2517  O   SER A 324     116.593  63.007  57.052  1.00 78.13           O  
ANISOU 2517  O   SER A 324    10633   9151   9900   -428   1191   2644       O  
ATOM   2518  CB  SER A 324     117.609  62.040  59.870  1.00 94.45           C  
ANISOU 2518  CB  SER A 324    12737  11202  11947   -686   1112   2825       C  
ATOM   2519  OG  SER A 324     116.429  61.266  59.752  1.00 98.42           O  
ANISOU 2519  OG  SER A 324    13284  11648  12463   -659   1146   2692       O  
ATOM   2520  N   LEU A 325     118.703  63.761  57.235  1.00 71.93           N  
ANISOU 2520  N   LEU A 325     9773   8462   9096   -461   1147   2874       N  
ATOM   2521  CA  LEU A 325     118.915  63.787  55.793  1.00 79.91           C  
ANISOU 2521  CA  LEU A 325    10742   9507  10111   -332   1177   2860       C  
ATOM   2522  C   LEU A 325     119.836  62.666  55.328  1.00 77.96           C  
ANISOU 2522  C   LEU A 325    10428   9283   9910   -238   1198   2921       C  
ATOM   2523  O   LEU A 325     120.209  62.600  54.158  1.00 80.23           O  
ANISOU 2523  O   LEU A 325    10673   9613  10197   -145   1235   2914       O  
ATOM   2524  CB  LEU A 325     119.447  65.151  55.343  1.00 89.07           C  
ANISOU 2524  CB  LEU A 325    11887  10726  11231   -355   1160   2916       C  
ATOM   2525  CG  LEU A 325     120.684  65.719  56.040  1.00 93.07           C  
ANISOU 2525  CG  LEU A 325    12357  11285  11720   -436   1125   3060       C  
ATOM   2526  CD1 LEU A 325     121.940  64.980  55.610  1.00 98.93           C  
ANISOU 2526  CD1 LEU A 325    13014  12081  12494   -364   1138   3158       C  
ATOM   2527  CD2 LEU A 325     120.815  67.203  55.742  1.00 90.46           C  
ANISOU 2527  CD2 LEU A 325    12039  10988  11345   -483   1103   3083       C  
ATOM   2528  N   SER A 326     120.201  61.786  56.251  1.00 74.34           N  
ANISOU 2528  N   SER A 326     9959   8792   9495   -272   1171   2979       N  
ATOM   2529  CA  SER A 326     121.017  60.632  55.906  1.00 87.07           C  
ANISOU 2529  CA  SER A 326    11498  10401  11185   -178   1183   3029       C  
ATOM   2530  C   SER A 326     121.071  59.625  57.042  1.00 92.07           C  
ANISOU 2530  C   SER A 326    12145  10967  11872   -232   1130   3080       C  
ATOM   2531  O   SER A 326     121.234  59.996  58.203  1.00 99.85           O  
ANISOU 2531  O   SER A 326    13161  11949  12828   -363   1071   3157       O  
ATOM   2532  CB  SER A 326     122.436  61.061  55.538  1.00 99.95           C  
ANISOU 2532  CB  SER A 326    13035  12108  12834   -153   1180   3144       C  
ATOM   2533  OG  SER A 326     123.290  59.933  55.443  1.00107.30           O  
ANISOU 2533  OG  SER A 326    13879  13021  13870    -76   1182   3195       O  
ATOM   2534  N   ILE A 327     120.929  58.350  56.701  1.00 89.84           N  
ANISOU 2534  N   ILE A 327    11843  10629  11663   -142   1150   3039       N  
ATOM   2535  CA  ILE A 327     121.108  57.293  57.681  1.00 88.20           C  
ANISOU 2535  CA  ILE A 327    11640  10348  11522   -185   1085   3106       C  
ATOM   2536  C   ILE A 327     122.475  57.484  58.330  1.00 90.25           C  
ANISOU 2536  C   ILE A 327    11826  10636  11828   -234   1012   3278       C  
ATOM   2537  O   ILE A 327     123.494  57.573  57.645  1.00 85.41           O  
ANISOU 2537  O   ILE A 327    11110  10068  11274   -147   1033   3327       O  
ATOM   2538  CB  ILE A 327     120.980  55.891  57.042  1.00 84.08           C  
ANISOU 2538  CB  ILE A 327    11087   9759  11100    -57   1116   3045       C  
ATOM   2539  CG1 ILE A 327     121.147  54.800  58.097  1.00 88.80           C  
ANISOU 2539  CG1 ILE A 327    11698  10267  11775   -112   1029   3128       C  
ATOM   2540  CG2 ILE A 327     121.987  55.709  55.918  1.00 81.92           C  
ANISOU 2540  CG2 ILE A 327    10696   9525  10905     81   1171   3055       C  
ATOM   2541  CD1 ILE A 327     120.879  53.410  57.570  1.00 90.90           C  
ANISOU 2541  CD1 ILE A 327    11948  10448  12143      2   1054   3059       C  
ATOM   2542  N   ASN A 328     122.486  57.582  59.654  1.00 94.59           N  
ANISOU 2542  N   ASN A 328    12429  11166  12347   -387    928   3366       N  
ATOM   2543  CA  ASN A 328     123.706  57.901  60.383  1.00 98.76           C  
ANISOU 2543  CA  ASN A 328    12899  11725  12901   -463    845   3538       C  
ATOM   2544  C   ASN A 328     123.899  57.030  61.615  1.00 96.65           C  
ANISOU 2544  C   ASN A 328    12660  11386  12678   -573    730   3651       C  
ATOM   2545  O   ASN A 328     123.091  56.147  61.897  1.00 96.00           O  
ANISOU 2545  O   ASN A 328    12644  11229  12605   -589    719   3594       O  
ATOM   2546  CB  ASN A 328     123.717  59.380  60.779  1.00105.31           C  
ANISOU 2546  CB  ASN A 328    13769  12633  13610   -585    847   3558       C  
ATOM   2547  CG  ASN A 328     122.465  59.792  61.530  1.00109.37           C  
ANISOU 2547  CG  ASN A 328    14411  13127  14017   -724    857   3464       C  
ATOM   2548  ND2 ASN A 328     121.719  60.736  60.965  1.00121.70           N  
ANISOU 2548  ND2 ASN A 328    16008  14720  15512   -707    929   3343       N  
ATOM   2549  OD1 ASN A 328     122.171  59.268  62.604  1.00105.61           O  
ANISOU 2549  OD1 ASN A 328    13999  12607  13523   -851    797   3498       O  
ATOM   2550  N   ALA A 329     124.977  57.291  62.346  1.00 94.03           N  
ANISOU 2550  N   ALA A 329    12280  11079  12370   -657    638   3818       N  
ATOM   2551  CA  ALA A 329     125.310  56.524  63.539  1.00 91.72           C  
ANISOU 2551  CA  ALA A 329    12009  10721  12120   -780    503   3958       C  
ATOM   2552  C   ALA A 329     124.165  56.510  64.546  1.00 88.64           C  
ANISOU 2552  C   ALA A 329    11772  10305  11601   -964    483   3908       C  
ATOM   2553  O   ALA A 329     123.992  55.543  65.287  1.00100.99           O  
ANISOU 2553  O   ALA A 329    13383  11792  13196  -1044    395   3967       O  
ATOM   2554  CB  ALA A 329     126.571  57.075  64.181  1.00 98.69           C  
ANISOU 2554  CB  ALA A 329    12825  11652  13018   -869    407   4142       C  
ATOM   2555  N   THR A 330     123.386  57.585  64.569  1.00 78.01           N  
ANISOU 2555  N   THR A 330    10502   9021  10119  -1039    565   3795       N  
ATOM   2556  CA  THR A 330     122.282  57.704  65.514  1.00 83.70           C  
ANISOU 2556  CA  THR A 330    11357   9728  10716  -1225    568   3720       C  
ATOM   2557  C   THR A 330     121.067  56.879  65.099  1.00 91.20           C  
ANISOU 2557  C   THR A 330    12362  10615  11677  -1157    631   3563       C  
ATOM   2558  O   THR A 330     120.705  55.909  65.766  1.00 83.83           O  
ANISOU 2558  O   THR A 330    11489   9615  10747  -1242    571   3587       O  
ATOM   2559  CB  THR A 330     121.845  59.169  65.682  1.00 78.79           C  
ANISOU 2559  CB  THR A 330    10783   9184   9971  -1324    640   3635       C  
ATOM   2560  CG2 THR A 330     120.677  59.265  66.652  1.00 74.90           C  
ANISOU 2560  CG2 THR A 330    10417   8677   9363  -1521    661   3530       C  
ATOM   2561  OG1 THR A 330     122.943  59.944  66.179  1.00 82.48           O  
ANISOU 2561  OG1 THR A 330    11213   9712  10415  -1413    578   3782       O  
ATOM   2562  N   ASN A 331     120.448  57.270  63.989  1.00 97.63           N  
ANISOU 2562  N   ASN A 331    13156  11447  12491  -1013    743   3410       N  
ATOM   2563  CA  ASN A 331     119.182  56.688  63.552  1.00 96.00           C  
ANISOU 2563  CA  ASN A 331    13005  11193  12279   -958    812   3244       C  
ATOM   2564  C   ASN A 331     119.275  55.264  63.004  1.00101.94           C  
ANISOU 2564  C   ASN A 331    13721  11865  13145   -819    794   3252       C  
ATOM   2565  O   ASN A 331     118.253  54.617  62.774  1.00106.02           O  
ANISOU 2565  O   ASN A 331    14292  12335  13657   -793    837   3130       O  
ATOM   2566  CB  ASN A 331     118.526  57.593  62.507  1.00 89.60           C  
ANISOU 2566  CB  ASN A 331    12181  10425  11440   -853    921   3092       C  
ATOM   2567  CG  ASN A 331     119.324  57.668  61.220  1.00 94.68           C  
ANISOU 2567  CG  ASN A 331    12720  11096  12159   -658    952   3118       C  
ATOM   2568  ND2 ASN A 331     118.940  58.585  60.339  1.00100.07           N  
ANISOU 2568  ND2 ASN A 331    13392  11823  12807   -589   1023   3022       N  
ATOM   2569  OD1 ASN A 331     120.273  56.912  61.019  1.00 92.74           O  
ANISOU 2569  OD1 ASN A 331    12402  10830  12007   -578    911   3222       O  
ATOM   2570  N   ILE A 332     120.494  54.779  62.794  1.00101.43           N  
ANISOU 2570  N   ILE A 332    13562  11784  13195   -732    733   3389       N  
ATOM   2571  CA  ILE A 332     120.691  53.466  62.184  1.00103.14           C  
ANISOU 2571  CA  ILE A 332    13724  11917  13547   -583    722   3388       C  
ATOM   2572  C   ILE A 332     120.198  52.326  63.077  1.00113.73           C  
ANISOU 2572  C   ILE A 332    15147  13162  14904   -687    639   3420       C  
ATOM   2573  O   ILE A 332     120.069  51.188  62.625  1.00116.20           O  
ANISOU 2573  O   ILE A 332    15441  13390  15320   -578    636   3390       O  
ATOM   2574  CB  ILE A 332     122.169  53.229  61.805  1.00 97.11           C  
ANISOU 2574  CB  ILE A 332    12820  11150  12926   -470    676   3521       C  
ATOM   2575  CG1 ILE A 332     122.286  52.104  60.774  1.00 88.85           C  
ANISOU 2575  CG1 ILE A 332    11699  10033  12028   -275    719   3457       C  
ATOM   2576  CG2 ILE A 332     122.998  52.930  63.045  1.00101.45           C  
ANISOU 2576  CG2 ILE A 332    13364  11663  13518   -607    522   3719       C  
ATOM   2577  CD1 ILE A 332     123.677  51.938  60.205  1.00 85.37           C  
ANISOU 2577  CD1 ILE A 332    11099   9596  11740   -145    708   3542       C  
ATOM   2578  N   LYS A 333     119.919  52.635  64.340  1.00117.40           N  
ANISOU 2578  N   LYS A 333    15707  13640  15260   -908    573   3478       N  
ATOM   2579  CA  LYS A 333     119.422  51.632  65.276  1.00114.31           C  
ANISOU 2579  CA  LYS A 333    15409  13168  14854  -1047    487   3515       C  
ATOM   2580  C   LYS A 333     118.073  51.097  64.819  1.00111.32           C  
ANISOU 2580  C   LYS A 333    15101  12753  14442  -1005    578   3329       C  
ATOM   2581  O   LYS A 333     117.750  49.932  65.039  1.00117.68           O  
ANISOU 2581  O   LYS A 333    15950  13469  15296  -1019    526   3340       O  
ATOM   2582  CB  LYS A 333     119.277  52.225  66.679  1.00117.42           C  
ANISOU 2582  CB  LYS A 333    15903  13607  15103  -1322    424   3585       C  
ATOM   2583  CG  LYS A 333     120.407  53.148  67.095  1.00126.58           C  
ANISOU 2583  CG  LYS A 333    17008  14836  16250  -1386    366   3731       C  
ATOM   2584  CD  LYS A 333     120.146  53.743  68.471  1.00128.94           C  
ANISOU 2584  CD  LYS A 333    17419  15184  16388  -1677    319   3775       C  
ATOM   2585  CE  LYS A 333     121.022  54.959  68.722  1.00130.15           C  
ANISOU 2585  CE  LYS A 333    17527  15428  16498  -1736    307   3863       C  
ATOM   2586  NZ  LYS A 333     122.465  54.667  68.499  1.00129.69           N1+
ANISOU 2586  NZ  LYS A 333    17347  15348  16580  -1630    201   4054       N1+
ATOM   2587  N   HIS A 334     117.291  51.960  64.179  1.00107.79           N  
ANISOU 2587  N   HIS A 334    14663  12373  13919   -957    705   3164       N  
ATOM   2588  CA  HIS A 334     115.922  51.628  63.802  1.00112.02           C  
ANISOU 2588  CA  HIS A 334    15264  12888  14410   -938    792   2979       C  
ATOM   2589  C   HIS A 334     115.833  50.936  62.446  1.00110.01           C  
ANISOU 2589  C   HIS A 334    14947  12591  14260   -707    854   2897       C  
ATOM   2590  O   HIS A 334     114.772  50.912  61.824  1.00112.45           O  
ANISOU 2590  O   HIS A 334    15288  12903  14535   -653    942   2733       O  
ATOM   2591  CB  HIS A 334     115.062  52.891  63.798  1.00117.99           C  
ANISOU 2591  CB  HIS A 334    16056  13725  15051  -1006    886   2837       C  
ATOM   2592  CG  HIS A 334     115.257  53.754  65.005  1.00121.39           C  
ANISOU 2592  CG  HIS A 334    16533  14209  15381  -1223    848   2902       C  
ATOM   2593  CD2 HIS A 334     114.560  53.841  66.161  1.00123.66           C  
ANISOU 2593  CD2 HIS A 334    16920  14505  15559  -1454    839   2863       C  
ATOM   2594  ND1 HIS A 334     116.285  54.667  65.107  1.00120.73           N  
ANISOU 2594  ND1 HIS A 334    16393  14182  15296  -1231    818   3014       N  
ATOM   2595  CE1 HIS A 334     116.210  55.280  66.275  1.00122.04           C  
ANISOU 2595  CE1 HIS A 334    16624  14388  15358  -1455    791   3043       C  
ATOM   2596  NE2 HIS A 334     115.173  54.797  66.934  1.00125.61           N  
ANISOU 2596  NE2 HIS A 334    17171  14813  15741  -1598    807   2949       N  
ATOM   2597  N   PHE A 335     116.947  50.376  61.990  1.00105.23           N  
ANISOU 2597  N   PHE A 335    14248  11947  13786   -576    809   3004       N  
ATOM   2598  CA  PHE A 335     116.963  49.637  60.733  1.00 99.66           C  
ANISOU 2598  CA  PHE A 335    13479  11199  13187   -369    873   2924       C  
ATOM   2599  C   PHE A 335     117.488  48.225  60.940  1.00108.11           C  
ANISOU 2599  C   PHE A 335    14525  12150  14402   -326    785   3014       C  
ATOM   2600  O   PHE A 335     117.901  47.562  59.990  1.00109.23           O  
ANISOU 2600  O   PHE A 335    14585  12247  14670   -153    822   2982       O  
ATOM   2601  CB  PHE A 335     117.817  50.360  59.693  1.00 91.61           C  
ANISOU 2601  CB  PHE A 335    12346  10251  12212   -222    934   2927       C  
ATOM   2602  CG  PHE A 335     117.231  51.657  59.228  1.00 87.24           C  
ANISOU 2602  CG  PHE A 335    11814   9797  11538   -233   1020   2825       C  
ATOM   2603  CD1 PHE A 335     117.698  52.861  59.725  1.00 85.09           C  
ANISOU 2603  CD1 PHE A 335    11532   9600  11199   -324    998   2899       C  
ATOM   2604  CD2 PHE A 335     116.207  51.673  58.297  1.00 88.93           C  
ANISOU 2604  CD2 PHE A 335    12056  10021  11713   -155   1114   2659       C  
ATOM   2605  CE1 PHE A 335     117.157  54.058  59.298  1.00 87.31           C  
ANISOU 2605  CE1 PHE A 335    11829   9955  11388   -332   1065   2807       C  
ATOM   2606  CE2 PHE A 335     115.661  52.866  57.867  1.00 89.68           C  
ANISOU 2606  CE2 PHE A 335    12165  10191  11716   -164   1172   2574       C  
ATOM   2607  CZ  PHE A 335     116.137  54.061  58.368  1.00 87.92           C  
ANISOU 2607  CZ  PHE A 335    11931  10034  11440   -250   1147   2648       C  
ATOM   2608  N   LYS A 336     117.458  47.768  62.188  1.00113.43           N  
ANISOU 2608  N   LYS A 336    15272  12769  15058   -496    667   3123       N  
ATOM   2609  CA  LYS A 336     118.054  46.490  62.554  1.00118.42           C  
ANISOU 2609  CA  LYS A 336    15881  13274  15838   -479    548   3245       C  
ATOM   2610  C   LYS A 336     117.535  45.343  61.691  1.00128.30           C  
ANISOU 2610  C   LYS A 336    17128  14433  17186   -332    602   3127       C  
ATOM   2611  O   LYS A 336     118.205  44.913  60.752  1.00138.32           O  
ANISOU 2611  O   LYS A 336    18285  15664  18605   -145    638   3110       O  
ATOM   2612  CB  LYS A 336     117.813  46.191  64.033  1.00118.47           C  
ANISOU 2612  CB  LYS A 336    16001  13241  15770   -721    414   3363       C  
ATOM   2613  CG  LYS A 336     118.960  45.456  64.705  1.00120.76           C  
ANISOU 2613  CG  LYS A 336    16243  13434  16208   -752    237   3580       C  
ATOM   2614  CD  LYS A 336     120.192  46.344  64.800  1.00118.51           C  
ANISOU 2614  CD  LYS A 336    15851  13217  15959   -736    199   3708       C  
ATOM   2615  CE  LYS A 336     121.310  45.665  65.575  1.00117.62           C  
ANISOU 2615  CE  LYS A 336    15687  13007  15997   -788      4   3937       C  
ATOM   2616  NZ  LYS A 336     122.501  46.549  65.722  1.00112.98           N1+
ANISOU 2616  NZ  LYS A 336    14995  12492  15440   -787    -38   4066       N1+
ATOM   2617  N   ASN A 337     116.344  44.849  62.010  1.00126.02           N  
ANISOU 2617  N   ASN A 337    16960  14111  16811   -426    613   3038       N  
ATOM   2618  CA  ASN A 337     115.765  43.734  61.266  1.00135.82           C  
ANISOU 2618  CA  ASN A 337    18213  15263  18131   -307    661   2924       C  
ATOM   2619  C   ASN A 337     114.702  44.169  60.262  1.00123.87           C  
ANISOU 2619  C   ASN A 337    16722  13823  16518   -229    820   2714       C  
ATOM   2620  O   ASN A 337     113.541  43.773  60.365  1.00122.88           O  
ANISOU 2620  O   ASN A 337    16694  13680  16315   -293    851   2606       O  
ATOM   2621  CB  ASN A 337     115.187  42.686  62.220  1.00159.77           C  
ANISOU 2621  CB  ASN A 337    21360  18190  21154   -455    554   2973       C  
ATOM   2622  CG  ASN A 337     116.240  41.724  62.738  1.00181.12           C  
ANISOU 2622  CG  ASN A 337    24018  20761  24040   -449    392   3161       C  
ATOM   2623  ND2 ASN A 337     115.946  41.074  63.859  1.00201.46           N  
ANISOU 2623  ND2 ASN A 337    26702  23262  26583   -637    258   3263       N  
ATOM   2624  OD1 ASN A 337     117.302  41.564  62.136  1.00179.84           O  
ANISOU 2624  OD1 ASN A 337    23720  20561  24049   -283    383   3212       O  
ATOM   2625  N   CYS A 338     115.106  44.978  59.289  1.00112.85           N  
ANISOU 2625  N   CYS A 338    15239  12513  15127    -99    913   2661       N  
ATOM   2626  CA  CYS A 338     114.191  45.434  58.250  1.00 98.24           C  
ANISOU 2626  CA  CYS A 338    13402  10731  13192    -22   1047   2478       C  
ATOM   2627  C   CYS A 338     114.292  44.553  57.014  1.00 97.13           C  
ANISOU 2627  C   CYS A 338    13205  10539  13163    161   1118   2386       C  
ATOM   2628  O   CYS A 338     115.380  44.122  56.638  1.00102.02           O  
ANISOU 2628  O   CYS A 338    13724  11115  13925    272   1105   2450       O  
ATOM   2629  CB  CYS A 338     114.487  46.884  57.873  1.00 86.23           C  
ANISOU 2629  CB  CYS A 338    11833   9336  11595     -8   1101   2472       C  
ATOM   2630  SG  CYS A 338     114.456  48.028  59.261  1.00120.89           S  
ANISOU 2630  SG  CYS A 338    16278  13792  15862   -221   1033   2566       S  
ATOM   2631  N   THR A 339     113.153  44.284  56.389  1.00 93.40           N  
ANISOU 2631  N   THR A 339    12792  10068  12627    187   1198   2228       N  
ATOM   2632  CA  THR A 339     113.129  43.536  55.141  1.00 96.25           C  
ANISOU 2632  CA  THR A 339    13111  10394  13065    345   1282   2118       C  
ATOM   2633  C   THR A 339     112.479  44.386  54.063  1.00102.08           C  
ANISOU 2633  C   THR A 339    13851  11241  13694    394   1393   1981       C  
ATOM   2634  O   THR A 339     112.449  44.013  52.892  1.00111.58           O  
ANISOU 2634  O   THR A 339    15021  12448  14927    511   1478   1880       O  
ATOM   2635  CB  THR A 339     112.349  42.218  55.277  1.00 93.01           C  
ANISOU 2635  CB  THR A 339    12776   9870  12694    333   1267   2054       C  
ATOM   2636  CG2 THR A 339     112.920  41.370  56.401  1.00 93.21           C  
ANISOU 2636  CG2 THR A 339    12814   9777  12825    263   1133   2203       C  
ATOM   2637  OG1 THR A 339     110.972  42.503  55.548  1.00 95.90           O  
ANISOU 2637  OG1 THR A 339    13249  10276  12914    224   1289   1956       O  
ATOM   2638  N   SER A 340     111.959  45.538  54.470  1.00 95.38           N  
ANISOU 2638  N   SER A 340    13041  10477  12721    297   1388   1979       N  
ATOM   2639  CA  SER A 340     111.271  46.427  53.548  1.00 92.63           C  
ANISOU 2639  CA  SER A 340    12699  10220  12275    328   1466   1864       C  
ATOM   2640  C   SER A 340     111.256  47.854  54.081  1.00 91.73           C  
ANISOU 2640  C   SER A 340    12587  10191  12076    237   1440   1912       C  
ATOM   2641  O   SER A 340     110.488  48.181  54.985  1.00 99.54           O  
ANISOU 2641  O   SER A 340    13640  11179  13000    111   1408   1896       O  
ATOM   2642  CB  SER A 340     109.843  45.934  53.305  1.00 92.52           C  
ANISOU 2642  CB  SER A 340    12767  10181  12206    305   1501   1720       C  
ATOM   2643  OG  SER A 340     109.121  46.826  52.475  1.00 93.91           O  
ANISOU 2643  OG  SER A 340    12946  10437  12296    324   1555   1619       O  
ATOM   2644  N   ILE A 341     112.118  48.698  53.525  1.00 82.56           N  
ANISOU 2644  N   ILE A 341    11353   9101  10915    293   1459   1964       N  
ATOM   2645  CA  ILE A 341     112.131  50.109  53.881  1.00 76.67           C  
ANISOU 2645  CA  ILE A 341    10605   8432  10094    218   1439   2002       C  
ATOM   2646  C   ILE A 341     110.948  50.789  53.212  1.00 74.10           C  
ANISOU 2646  C   ILE A 341    10318   8149   9689    217   1482   1870       C  
ATOM   2647  O   ILE A 341     110.844  50.801  51.985  1.00 70.79           O  
ANISOU 2647  O   ILE A 341     9878   7760   9259    309   1534   1804       O  
ATOM   2648  CB  ILE A 341     113.433  50.801  53.430  1.00 79.22           C  
ANISOU 2648  CB  ILE A 341    10839   8819  10440    275   1444   2100       C  
ATOM   2649  CG1 ILE A 341     114.653  50.074  53.998  1.00 76.82           C  
ANISOU 2649  CG1 ILE A 341    10478   8467  10244    292   1397   2228       C  
ATOM   2650  CG2 ILE A 341     113.441  52.260  53.861  1.00 60.44           C  
ANISOU 2650  CG2 ILE A 341     8466   6511   7987    189   1417   2143       C  
ATOM   2651  CD1 ILE A 341     114.727  50.104  55.507  1.00 77.47           C  
ANISOU 2651  CD1 ILE A 341    10601   8512  10320    153   1303   2333       C  
ATOM   2652  N   SER A 342     110.050  51.343  54.020  1.00 77.18           N  
ANISOU 2652  N   SER A 342    10760   8539  10027    104   1458   1829       N  
ATOM   2653  CA  SER A 342     108.863  52.006  53.497  1.00 77.86           C  
ANISOU 2653  CA  SER A 342    10870   8649  10063     99   1484   1702       C  
ATOM   2654  C   SER A 342     109.113  53.497  53.319  1.00 73.37           C  
ANISOU 2654  C   SER A 342    10267   8145   9464     83   1469   1735       C  
ATOM   2655  O   SER A 342     108.481  54.328  53.969  1.00 67.66           O  
ANISOU 2655  O   SER A 342     9561   7425   8720     -7   1452   1697       O  
ATOM   2656  CB  SER A 342     107.663  51.774  54.414  1.00 82.03           C  
ANISOU 2656  CB  SER A 342    11462   9137  10570    -14   1478   1611       C  
ATOM   2657  OG  SER A 342     106.467  52.213  53.795  1.00 88.66           O  
ANISOU 2657  OG  SER A 342    12310   9987  11389      0   1502   1476       O  
ATOM   2658  N   GLY A 343     110.043  53.824  52.429  1.00 83.14           N  
ANISOU 2658  N   GLY A 343    11454   9432  10705    167   1480   1800       N  
ATOM   2659  CA  GLY A 343     110.412  55.203  52.173  1.00 90.50           C  
ANISOU 2659  CA  GLY A 343    12355  10424  11607    155   1460   1848       C  
ATOM   2660  C   GLY A 343     111.656  55.284  51.311  1.00 92.23           C  
ANISOU 2660  C   GLY A 343    12517  10698  11828    234   1479   1935       C  
ATOM   2661  O   GLY A 343     111.794  54.547  50.337  1.00 96.47           O  
ANISOU 2661  O   GLY A 343    13041  11241  12373    318   1525   1897       O  
ATOM   2662  N   ASP A 344     112.570  56.176  51.676  1.00 84.47           N  
ANISOU 2662  N   ASP A 344    11498   9759  10838    198   1450   2043       N  
ATOM   2663  CA  ASP A 344     113.795  56.362  50.912  1.00 80.09           C  
ANISOU 2663  CA  ASP A 344    10881   9267  10282    258   1472   2123       C  
ATOM   2664  C   ASP A 344     115.020  56.063  51.767  1.00 80.82           C  
ANISOU 2664  C   ASP A 344    10923   9357  10427    240   1452   2248       C  
ATOM   2665  O   ASP A 344     114.944  56.061  52.995  1.00 86.62           O  
ANISOU 2665  O   ASP A 344    11682  10055  11174    156   1405   2293       O  
ATOM   2666  CB  ASP A 344     113.864  57.791  50.374  1.00 78.55           C  
ANISOU 2666  CB  ASP A 344    10680   9135  10028    233   1450   2149       C  
ATOM   2667  CG  ASP A 344     112.591  58.205  49.665  1.00 81.20           C  
ANISOU 2667  CG  ASP A 344    11064   9459  10328    236   1440   2041       C  
ATOM   2668  OD1 ASP A 344     111.998  57.351  48.975  1.00 81.07           O  
ANISOU 2668  OD1 ASP A 344    11068   9425  10311    290   1476   1952       O  
ATOM   2669  OD2 ASP A 344     112.183  59.379  49.796  1.00 82.44           O1-
ANISOU 2669  OD2 ASP A 344    11235   9621  10468    184   1392   2044       O1-
ATOM   2670  N   LEU A 345     116.146  55.804  51.112  1.00 74.79           N  
ANISOU 2670  N   LEU A 345    10087   8634   9695    309   1486   2302       N  
ATOM   2671  CA  LEU A 345     117.409  55.610  51.814  1.00 69.12           C  
ANISOU 2671  CA  LEU A 345     9302   7918   9043    300   1458   2429       C  
ATOM   2672  C   LEU A 345     118.457  56.612  51.335  1.00 76.84           C  
ANISOU 2672  C   LEU A 345    10216   8988   9991    300   1466   2509       C  
ATOM   2673  O   LEU A 345     118.783  56.666  50.151  1.00 81.08           O  
ANISOU 2673  O   LEU A 345    10717   9582  10509    362   1528   2470       O  
ATOM   2674  CB  LEU A 345     117.915  54.175  51.646  1.00 65.92           C  
ANISOU 2674  CB  LEU A 345     8844   7457   8746    385   1488   2420       C  
ATOM   2675  CG  LEU A 345     117.192  53.118  52.485  1.00 70.97           C  
ANISOU 2675  CG  LEU A 345     9541   7993   9433    362   1452   2392       C  
ATOM   2676  CD1 LEU A 345     117.912  51.781  52.421  1.00 71.96           C  
ANISOU 2676  CD1 LEU A 345     9601   8050   9692    444   1461   2412       C  
ATOM   2677  CD2 LEU A 345     117.071  53.585  53.923  1.00 72.99           C  
ANISOU 2677  CD2 LEU A 345     9842   8230   9663    231   1366   2479       C  
ATOM   2678  N   HIS A 346     118.970  57.412  52.263  1.00 82.88           N  
ANISOU 2678  N   HIS A 346    10973   9773  10744    216   1406   2617       N  
ATOM   2679  CA  HIS A 346     119.990  58.403  51.946  1.00 79.23           C  
ANISOU 2679  CA  HIS A 346    10455   9399  10252    201   1405   2705       C  
ATOM   2680  C   HIS A 346     121.309  58.047  52.620  1.00 87.13           C  
ANISOU 2680  C   HIS A 346    11367  10401  11336    197   1375   2832       C  
ATOM   2681  O   HIS A 346     121.447  58.171  53.836  1.00 95.84           O  
ANISOU 2681  O   HIS A 346    12488  11474  12452    112   1304   2917       O  
ATOM   2682  CB  HIS A 346     119.554  59.795  52.408  1.00 69.43           C  
ANISOU 2682  CB  HIS A 346     9272   8182   8928    100   1357   2729       C  
ATOM   2683  CG  HIS A 346     118.309  60.295  51.749  1.00 70.66           C  
ANISOU 2683  CG  HIS A 346     9497   8328   9022    102   1368   2616       C  
ATOM   2684  CD2 HIS A 346     117.079  59.739  51.622  1.00 73.31           C  
ANISOU 2684  CD2 HIS A 346     9889   8604   9360    123   1380   2499       C  
ATOM   2685  ND1 HIS A 346     118.239  61.521  51.123  1.00 75.17           N  
ANISOU 2685  ND1 HIS A 346    10083   8951   9528     76   1354   2623       N  
ATOM   2686  CE1 HIS A 346     117.023  61.699  50.638  1.00 76.82           C  
ANISOU 2686  CE1 HIS A 346    10350   9127   9711     85   1350   2518       C  
ATOM   2687  NE2 HIS A 346     116.300  60.631  50.928  1.00 74.01           N  
ANISOU 2687  NE2 HIS A 346    10018   8707   9394    114   1370   2438       N  
ATOM   2688  N   ILE A 347     122.276  57.601  51.828  1.00 81.85           N  
ANISOU 2688  N   ILE A 347    10601   9771  10728    281   1430   2841       N  
ATOM   2689  CA  ILE A 347     123.620  57.376  52.337  1.00 77.17           C  
ANISOU 2689  CA  ILE A 347     9902   9187  10232    286   1400   2962       C  
ATOM   2690  C   ILE A 347     124.528  58.496  51.845  1.00 75.05           C  
ANISOU 2690  C   ILE A 347     9578   9031   9908    259   1420   3023       C  
ATOM   2691  O   ILE A 347     125.004  58.473  50.712  1.00 79.36           O  
ANISOU 2691  O   ILE A 347    10062   9641  10451    320   1502   2973       O  
ATOM   2692  CB  ILE A 347     124.166  56.012  51.900  1.00 65.02           C  
ANISOU 2692  CB  ILE A 347     8269   7599   8837    399   1446   2925       C  
ATOM   2693  CG1 ILE A 347     123.171  54.912  52.273  1.00 74.20           C  
ANISOU 2693  CG1 ILE A 347     9501   8648  10044    422   1428   2855       C  
ATOM   2694  CG2 ILE A 347     125.520  55.751  52.536  1.00 67.19           C  
ANISOU 2694  CG2 ILE A 347     8422   7865   9242    404   1395   3057       C  
ATOM   2695  CD1 ILE A 347     123.707  53.515  52.095  1.00 76.47           C  
ANISOU 2695  CD1 ILE A 347     9698   8856  10500    525   1450   2834       C  
ATOM   2696  N   LEU A 348     124.753  59.483  52.707  1.00 70.41           N  
ANISOU 2696  N   LEU A 348     9016   8469   9267    156   1348   3128       N  
ATOM   2697  CA  LEU A 348     125.486  60.688  52.333  1.00 68.36           C  
ANISOU 2697  CA  LEU A 348     8725   8312   8937    110   1355   3190       C  
ATOM   2698  C   LEU A 348     126.855  60.770  53.008  1.00 75.68           C  
ANISOU 2698  C   LEU A 348     9548   9270   9936     80   1309   3333       C  
ATOM   2699  O   LEU A 348     127.098  60.103  54.012  1.00 81.93           O  
ANISOU 2699  O   LEU A 348    10318   9996  10817     64   1243   3404       O  
ATOM   2700  CB  LEU A 348     124.655  61.929  52.670  1.00 64.72           C  
ANISOU 2700  CB  LEU A 348     8375   7860   8356     11   1311   3189       C  
ATOM   2701  CG  LEU A 348     123.615  62.366  51.636  1.00 66.31           C  
ANISOU 2701  CG  LEU A 348     8652   8072   8472     32   1352   3072       C  
ATOM   2702  CD1 LEU A 348     122.806  61.182  51.140  1.00 66.47           C  
ANISOU 2702  CD1 LEU A 348     8692   8032   8531    119   1400   2951       C  
ATOM   2703  CD2 LEU A 348     122.703  63.441  52.209  1.00 66.55           C  
ANISOU 2703  CD2 LEU A 348     8780   8075   8432    -60   1293   3063       C  
ATOM   2704  N   PRO A 349     127.757  61.592  52.450  1.00 77.38           N  
ANISOU 2704  N   PRO A 349     9701   9587  10113     63   1338   3381       N  
ATOM   2705  CA  PRO A 349     129.100  61.779  53.006  1.00 83.21           C  
ANISOU 2705  CA  PRO A 349    10331  10367  10916     30   1297   3516       C  
ATOM   2706  C   PRO A 349     129.060  62.154  54.482  1.00 91.51           C  
ANISOU 2706  C   PRO A 349    11434  11378  11956    -83   1182   3633       C  
ATOM   2707  O   PRO A 349     129.720  61.514  55.303  1.00 91.88           O  
ANISOU 2707  O   PRO A 349    11415  11385  12112    -91   1118   3728       O  
ATOM   2708  CB  PRO A 349     129.650  62.951  52.192  1.00 80.05           C  
ANISOU 2708  CB  PRO A 349     9913  10088  10415     -9   1341   3531       C  
ATOM   2709  CG  PRO A 349     128.929  62.878  50.901  1.00 78.08           C  
ANISOU 2709  CG  PRO A 349     9709   9861  10098     46   1430   3393       C  
ATOM   2710  CD  PRO A 349     127.555  62.374  51.218  1.00 76.96           C  
ANISOU 2710  CD  PRO A 349     9676   9616   9948     65   1406   3311       C  
ATOM   2711  N   VAL A 350     128.285  63.185  54.802  1.00 93.63           N  
ANISOU 2711  N   VAL A 350    11821  11654  12100   -178   1156   3623       N  
ATOM   2712  CA  VAL A 350     128.197  63.710  56.158  1.00 91.83           C  
ANISOU 2712  CA  VAL A 350    11654  11401  11835   -311   1065   3714       C  
ATOM   2713  C   VAL A 350     127.927  62.619  57.193  1.00 86.98           C  
ANISOU 2713  C   VAL A 350    11056  10693  11300   -329   1002   3741       C  
ATOM   2714  O   VAL A 350     128.307  62.745  58.356  1.00 86.23           O  
ANISOU 2714  O   VAL A 350    10971  10587  11206   -441    916   3854       O  
ATOM   2715  CB  VAL A 350     127.103  64.790  56.258  1.00 91.34           C  
ANISOU 2715  CB  VAL A 350    11719  11333  11651   -391   1064   3646       C  
ATOM   2716  CG1 VAL A 350     125.743  64.196  55.928  1.00 89.04           C  
ANISOU 2716  CG1 VAL A 350    11505  10969  11357   -334   1101   3501       C  
ATOM   2717  CG2 VAL A 350     127.099  65.417  57.637  1.00 95.83           C  
ANISOU 2717  CG2 VAL A 350    12345  11888  12177   -544    987   3727       C  
ATOM   2718  N   ALA A 351     127.275  61.545  56.764  1.00 80.85           N  
ANISOU 2718  N   ALA A 351    10289   9850  10581   -232   1041   3641       N  
ATOM   2719  CA  ALA A 351     126.950  60.445  57.662  1.00 79.63           C  
ANISOU 2719  CA  ALA A 351    10159   9599  10500   -250    979   3662       C  
ATOM   2720  C   ALA A 351     128.205  59.710  58.119  1.00 89.48           C  
ANISOU 2720  C   ALA A 351    11286  10827  11886   -231    910   3799       C  
ATOM   2721  O   ALA A 351     128.239  59.148  59.214  1.00 95.94           O  
ANISOU 2721  O   ALA A 351    12126  11579  12747   -308    812   3886       O  
ATOM   2722  CB  ALA A 351     125.983  59.480  56.992  1.00 74.58           C  
ANISOU 2722  CB  ALA A 351     9553   8893   9891   -145   1040   3520       C  
ATOM   2723  N   PHE A 352     129.236  59.723  57.282  1.00 91.53           N  
ANISOU 2723  N   PHE A 352    11414  11143  12219   -137    957   3817       N  
ATOM   2724  CA  PHE A 352     130.458  58.981  57.576  1.00 97.49           C  
ANISOU 2724  CA  PHE A 352    12026  11873  13142    -95    897   3930       C  
ATOM   2725  C   PHE A 352     131.479  59.779  58.384  1.00100.61           C  
ANISOU 2725  C   PHE A 352    12375  12328  13524   -209    809   4097       C  
ATOM   2726  O   PHE A 352     132.095  59.246  59.306  1.00104.49           O  
ANISOU 2726  O   PHE A 352    12816  12768  14118   -255    694   4230       O  
ATOM   2727  CB  PHE A 352     131.094  58.450  56.290  1.00 96.96           C  
ANISOU 2727  CB  PHE A 352    11820  11831  13189     63   1001   3848       C  
ATOM   2728  CG  PHE A 352     130.340  57.310  55.671  1.00 89.51           C  
ANISOU 2728  CG  PHE A 352    10893  10804  12314    179   1065   3710       C  
ATOM   2729  CD1 PHE A 352     129.829  57.414  54.390  1.00 95.18           C  
ANISOU 2729  CD1 PHE A 352    11629  11568  12966    256   1197   3553       C  
ATOM   2730  CD2 PHE A 352     130.136  56.138  56.375  1.00 82.49           C  
ANISOU 2730  CD2 PHE A 352    10006   9788  11549    197    984   3742       C  
ATOM   2731  CE1 PHE A 352     129.135  56.367  53.821  1.00 97.21           C  
ANISOU 2731  CE1 PHE A 352    11904  11751  13280    354   1256   3425       C  
ATOM   2732  CE2 PHE A 352     129.443  55.090  55.813  1.00 89.87           C  
ANISOU 2732  CE2 PHE A 352    10958  10642  12546    299   1042   3614       C  
ATOM   2733  CZ  PHE A 352     128.940  55.204  54.535  1.00 96.89           C  
ANISOU 2733  CZ  PHE A 352    11863  11582  13368    379   1182   3451       C  
ATOM   2734  N   ARG A 353     131.665  61.048  58.037  1.00 97.94           N  
ANISOU 2734  N   ARG A 353    12056  12096  13062   -262    854   4097       N  
ATOM   2735  CA  ARG A 353     132.609  61.887  58.767  1.00103.40           C  
ANISOU 2735  CA  ARG A 353    12710  12852  13726   -378    777   4249       C  
ATOM   2736  C   ARG A 353     131.945  62.524  59.983  1.00105.98           C  
ANISOU 2736  C   ARG A 353    13183  13161  13923   -553    697   4302       C  
ATOM   2737  O   ARG A 353     132.583  63.254  60.740  1.00111.59           O  
ANISOU 2737  O   ARG A 353    13891  13920  14589   -679    627   4426       O  
ATOM   2738  CB  ARG A 353     133.214  62.962  57.858  1.00106.55           C  
ANISOU 2738  CB  ARG A 353    13057  13372  14054   -365    857   4234       C  
ATOM   2739  CG  ARG A 353     132.282  64.113  57.523  1.00108.32           C  
ANISOU 2739  CG  ARG A 353    13420  13639  14099   -426    909   4151       C  
ATOM   2740  CD  ARG A 353     133.005  65.176  56.707  1.00113.64           C  
ANISOU 2740  CD  ARG A 353    14042  14430  14705   -435    964   4164       C  
ATOM   2741  NE  ARG A 353     132.122  66.274  56.322  1.00124.52           N  
ANISOU 2741  NE  ARG A 353    15548  15834  15931   -488    999   4091       N  
ATOM   2742  CZ  ARG A 353     131.513  66.367  55.144  1.00132.17           C  
ANISOU 2742  CZ  ARG A 353    16549  16818  16852   -413   1084   3967       C  
ATOM   2743  NH1 ARG A 353     131.691  65.426  54.227  1.00137.93           N1+
ANISOU 2743  NH1 ARG A 353    17197  17550  17660   -289   1159   3892       N1+
ATOM   2744  NH2 ARG A 353     130.726  67.403  54.880  1.00129.31           N  
ANISOU 2744  NH2 ARG A 353    16297  16464  16369   -468   1090   3918       N  
ATOM   2745  N   GLY A 354     130.662  62.234  60.167  1.00103.24           N  
ANISOU 2745  N   GLY A 354    12960  12748  13517   -569    715   4198       N  
ATOM   2746  CA  GLY A 354     129.916  62.756  61.297  1.00 98.90           C  
ANISOU 2746  CA  GLY A 354    12549  12179  12850   -740    660   4214       C  
ATOM   2747  C   GLY A 354     129.542  64.213  61.113  1.00 96.62           C  
ANISOU 2747  C   GLY A 354    12334  11959  12419   -813    712   4162       C  
ATOM   2748  O   GLY A 354     130.317  64.995  60.561  1.00 94.72           O  
ANISOU 2748  O   GLY A 354    12029  11798  12162   -794    736   4202       O  
ATOM   2749  N   ASP A 355     128.351  64.579  61.575  1.00 94.67           N  
ANISOU 2749  N   ASP A 355    12216  11676  12077   -900    727   4067       N  
ATOM   2750  CA  ASP A 355     127.875  65.951  61.456  1.00 89.19           C  
ANISOU 2750  CA  ASP A 355    11593  11023  11272   -969    768   4004       C  
ATOM   2751  C   ASP A 355     127.890  66.660  62.805  1.00 84.93           C  
ANISOU 2751  C   ASP A 355    11127  10492  10649  -1176    707   4070       C  
ATOM   2752  O   ASP A 355     127.273  66.199  63.766  1.00 81.63           O  
ANISOU 2752  O   ASP A 355    10785  10023  10209  -1283    675   4052       O  
ATOM   2753  CB  ASP A 355     126.464  65.984  60.871  1.00 89.33           C  
ANISOU 2753  CB  ASP A 355    11689  10992  11259   -910    841   3824       C  
ATOM   2754  CG  ASP A 355     126.038  67.379  60.467  1.00 96.15           C  
ANISOU 2754  CG  ASP A 355    12602  11886  12046   -942    879   3758       C  
ATOM   2755  OD1 ASP A 355     126.922  68.252  60.329  1.00 96.91           O  
ANISOU 2755  OD1 ASP A 355    12659  12049  12113   -975    864   3846       O  
ATOM   2756  OD2 ASP A 355     124.823  67.603  60.284  1.00 98.70           O1-
ANISOU 2756  OD2 ASP A 355    12996  12159  12344   -935    918   3619       O1-
ATOM   2757  N   SER A 356     128.596  67.783  62.870  1.00 84.97           N  
ANISOU 2757  N   SER A 356    11115  10566  10603  -1246    695   4142       N  
ATOM   2758  CA  SER A 356     128.681  68.555  64.102  1.00 87.27           C  
ANISOU 2758  CA  SER A 356    11476  10874  10808  -1453    645   4200       C  
ATOM   2759  C   SER A 356     127.431  69.404  64.289  1.00 88.70           C  
ANISOU 2759  C   SER A 356    11768  11020  10912  -1528    703   4044       C  
ATOM   2760  O   SER A 356     127.027  69.699  65.414  1.00 85.85           O  
ANISOU 2760  O   SER A 356    11489  10643  10486  -1704    685   4027       O  
ATOM   2761  CB  SER A 356     129.927  69.444  64.096  1.00 83.98           C  
ANISOU 2761  CB  SER A 356    10997  10543  10369  -1503    611   4334       C  
ATOM   2762  OG  SER A 356     129.846  70.431  63.083  1.00 79.76           O  
ANISOU 2762  OG  SER A 356    10456  10042   9806  -1431    674   4269       O  
ATOM   2763  N   PHE A 357     126.817  69.789  63.176  1.00 91.01           N  
ANISOU 2763  N   PHE A 357    12060  11299  11220  -1399    771   3925       N  
ATOM   2764  CA  PHE A 357     125.637  70.641  63.209  1.00 95.06           C  
ANISOU 2764  CA  PHE A 357    12658  11767  11694  -1445    820   3772       C  
ATOM   2765  C   PHE A 357     124.446  69.930  63.846  1.00100.55           C  
ANISOU 2765  C   PHE A 357    13423  12390  12391  -1492    842   3650       C  
ATOM   2766  O   PHE A 357     123.714  70.521  64.639  1.00103.66           O  
ANISOU 2766  O   PHE A 357    13890  12755  12740  -1630    862   3559       O  
ATOM   2767  CB  PHE A 357     125.280  71.110  61.799  1.00 94.66           C  
ANISOU 2767  CB  PHE A 357    12585  11712  11669  -1292    866   3693       C  
ATOM   2768  CG  PHE A 357     124.248  72.197  61.767  1.00 96.58           C  
ANISOU 2768  CG  PHE A 357    12896  11905  11896  -1337    894   3559       C  
ATOM   2769  CD1 PHE A 357     124.573  73.486  62.153  1.00 98.27           C  
ANISOU 2769  CD1 PHE A 357    13133  12136  12069  -1450    877   3590       C  
ATOM   2770  CD2 PHE A 357     122.956  71.934  61.348  1.00 99.30           C  
ANISOU 2770  CD2 PHE A 357    13274  12177  12279  -1264    934   3401       C  
ATOM   2771  CE1 PHE A 357     123.628  74.491  62.125  1.00 99.99           C  
ANISOU 2771  CE1 PHE A 357    13402  12290  12299  -1484    898   3461       C  
ATOM   2772  CE2 PHE A 357     122.006  72.936  61.317  1.00101.97           C  
ANISOU 2772  CE2 PHE A 357    13658  12456  12631  -1299    952   3275       C  
ATOM   2773  CZ  PHE A 357     122.343  74.216  61.707  1.00100.92           C  
ANISOU 2773  CZ  PHE A 357    13543  12331  12472  -1406    933   3303       C  
ATOM   2774  N   THR A 358     124.259  68.661  63.497  1.00102.21           N  
ANISOU 2774  N   THR A 358    13608  12572  12655  -1384    844   3639       N  
ATOM   2775  CA  THR A 358     123.152  67.875  64.033  1.00101.38           C  
ANISOU 2775  CA  THR A 358    13568  12402  12551  -1424    864   3528       C  
ATOM   2776  C   THR A 358     123.590  67.026  65.221  1.00 98.33           C  
ANISOU 2776  C   THR A 358    13202  12014  12144  -1559    797   3636       C  
ATOM   2777  O   THR A 358     122.828  66.195  65.711  1.00102.74           O  
ANISOU 2777  O   THR A 358    13813  12523  12699  -1604    800   3572       O  
ATOM   2778  CB  THR A 358     122.534  66.957  62.962  1.00106.60           C  
ANISOU 2778  CB  THR A 358    14203  13021  13279  -1238    905   3438       C  
ATOM   2779  CG2 THR A 358     122.025  67.778  61.786  1.00109.08           C  
ANISOU 2779  CG2 THR A 358    14507  13334  13606  -1123    957   3337       C  
ATOM   2780  OG1 THR A 358     123.520  66.024  62.501  1.00108.25           O  
ANISOU 2780  OG1 THR A 358    14330  13250  13548  -1128    872   3557       O  
ATOM   2781  N   HIS A 359     124.821  67.239  65.677  1.00 94.82           N  
ANISOU 2781  N   HIS A 359    12717  11623  11686  -1630    727   3807       N  
ATOM   2782  CA  HIS A 359     125.361  66.511  66.822  1.00 92.29           C  
ANISOU 2782  CA  HIS A 359    12415  11303  11349  -1774    636   3941       C  
ATOM   2783  C   HIS A 359     125.270  65.002  66.643  1.00 93.92           C  
ANISOU 2783  C   HIS A 359    12595  11452  11638  -1675    602   3964       C  
ATOM   2784  O   HIS A 359     124.721  64.303  67.493  1.00102.02           O  
ANISOU 2784  O   HIS A 359    13694  12436  12634  -1793    570   3952       O  
ATOM   2785  CB  HIS A 359     124.643  66.914  68.112  1.00 90.59           C  
ANISOU 2785  CB  HIS A 359    12316  11081  11024  -2017    641   3878       C  
ATOM   2786  CG  HIS A 359     124.955  68.303  68.571  1.00 90.41           C  
ANISOU 2786  CG  HIS A 359    12318  11112  10923  -2156    653   3888       C  
ATOM   2787  CD2 HIS A 359     126.061  68.821  69.155  1.00 93.36           C  
ANISOU 2787  CD2 HIS A 359    12674  11545  11252  -2277    584   4046       C  
ATOM   2788  ND1 HIS A 359     124.063  69.346  68.444  1.00 91.29           N  
ANISOU 2788  ND1 HIS A 359    12476  11209  11002  -2184    743   3717       N  
ATOM   2789  CE1 HIS A 359     124.606  70.448  68.930  1.00 97.12           C  
ANISOU 2789  CE1 HIS A 359    13227  11993  11679  -2315    732   3766       C  
ATOM   2790  NE2 HIS A 359     125.818  70.157  69.368  1.00101.39           N  
ANISOU 2790  NE2 HIS A 359    13734  12586  12204  -2377    638   3966       N  
ATOM   2791  N   THR A 360     125.808  64.501  65.538  1.00 90.75           N  
ANISOU 2791  N   THR A 360    12092  11049  11341  -1468    611   3993       N  
ATOM   2792  CA  THR A 360     125.810  63.065  65.290  1.00 93.84           C  
ANISOU 2792  CA  THR A 360    12445  11377  11832  -1359    581   4013       C  
ATOM   2793  C   THR A 360     127.214  62.552  64.989  1.00 94.88           C  
ANISOU 2793  C   THR A 360    12447  11524  12079  -1265    512   4176       C  
ATOM   2794  O   THR A 360     127.877  63.037  64.070  1.00 90.73           O  
ANISOU 2794  O   THR A 360    11832  11052  11591  -1146    554   4186       O  
ATOM   2795  CB  THR A 360     124.853  62.678  64.145  1.00 91.59           C  
ANISOU 2795  CB  THR A 360    12161  11053  11585  -1182    680   3842       C  
ATOM   2796  CG2 THR A 360     123.407  62.790  64.601  1.00 87.00           C  
ANISOU 2796  CG2 THR A 360    11698  10433  10925  -1277    728   3686       C  
ATOM   2797  OG1 THR A 360     125.064  63.549  63.029  1.00 94.57           O  
ANISOU 2797  OG1 THR A 360    12486  11485  11963  -1064    749   3794       O  
ATOM   2798  N   PRO A 361     127.671  61.569  65.777  1.00 94.51           N  
ANISOU 2798  N   PRO A 361    12386  11428  12095  -1327    400   4304       N  
ATOM   2799  CA  PRO A 361     128.991  60.953  65.617  1.00 95.24           C  
ANISOU 2799  CA  PRO A 361    12342  11514  12331  -1242    316   4461       C  
ATOM   2800  C   PRO A 361     129.116  60.262  64.267  1.00 99.57           C  
ANISOU 2800  C   PRO A 361    12783  12035  13015   -996    391   4380       C  
ATOM   2801  O   PRO A 361     128.102  59.883  63.681  1.00102.97           O  
ANISOU 2801  O   PRO A 361    13264  12425  13434   -911    474   4228       O  
ATOM   2802  CB  PRO A 361     129.028  59.910  66.739  1.00100.56           C  
ANISOU 2802  CB  PRO A 361    13056  12109  13044  -1364    178   4579       C  
ATOM   2803  CG  PRO A 361     128.002  60.359  67.724  1.00101.74           C  
ANISOU 2803  CG  PRO A 361    13370  12266  13021  -1580    185   4518       C  
ATOM   2804  CD  PRO A 361     126.927  60.997  66.910  1.00 96.37           C  
ANISOU 2804  CD  PRO A 361    12738  11607  12269  -1497    340   4305       C  
ATOM   2805  N   PRO A 362     130.352  60.101  63.776  1.00100.05           N  
ANISOU 2805  N   PRO A 362    12693  12120  13202   -891    367   4475       N  
ATOM   2806  CA  PRO A 362     130.615  59.430  62.500  1.00102.22           C  
ANISOU 2806  CA  PRO A 362    12850  12375  13613   -671    448   4394       C  
ATOM   2807  C   PRO A 362     130.081  58.001  62.497  1.00106.75           C  
ANISOU 2807  C   PRO A 362    13434  12830  14298   -593    424   4350       C  
ATOM   2808  O   PRO A 362     130.158  57.308  63.511  1.00105.04           O  
ANISOU 2808  O   PRO A 362    13245  12539  14129   -689    297   4461       O  
ATOM   2809  CB  PRO A 362     132.143  59.425  62.420  1.00 98.89           C  
ANISOU 2809  CB  PRO A 362    12262  11990  13323   -629    390   4536       C  
ATOM   2810  CG  PRO A 362     132.565  60.573  63.266  1.00 98.64           C  
ANISOU 2810  CG  PRO A 362    12272  12037  13168   -808    328   4652       C  
ATOM   2811  CD  PRO A 362     131.588  60.602  64.399  1.00 98.77           C  
ANISOU 2811  CD  PRO A 362    12456  12011  13059   -987    270   4654       C  
ATOM   2812  N   LEU A 363     129.540  57.575  61.360  1.00107.04           N  
ANISOU 2812  N   LEU A 363    13453  12847  14370   -433    541   4192       N  
ATOM   2813  CA  LEU A 363     128.974  56.238  61.233  1.00100.86           C  
ANISOU 2813  CA  LEU A 363    12683  11951  13689   -350    534   4130       C  
ATOM   2814  C   LEU A 363     130.060  55.179  61.100  1.00 96.84           C  
ANISOU 2814  C   LEU A 363    12015  11369  13410   -238    469   4218       C  
ATOM   2815  O   LEU A 363     130.963  55.303  60.273  1.00 97.80           O  
ANISOU 2815  O   LEU A 363    11993  11538  13629   -121    528   4209       O  
ATOM   2816  CB  LEU A 363     128.038  56.171  60.026  1.00 98.05           C  
ANISOU 2816  CB  LEU A 363    12362  11604  13290   -224    683   3928       C  
ATOM   2817  CG  LEU A 363     127.495  54.785  59.675  1.00 94.99           C  
ANISOU 2817  CG  LEU A 363    11974  11104  13013   -115    699   3843       C  
ATOM   2818  CD1 LEU A 363     126.649  54.235  60.814  1.00 98.63           C  
ANISOU 2818  CD1 LEU A 363    12564  11480  13429   -246    604   3875       C  
ATOM   2819  CD2 LEU A 363     126.697  54.836  58.382  1.00 88.78           C  
ANISOU 2819  CD2 LEU A 363    11211  10346  12173      3    848   3650       C  
ATOM   2820  N   ASP A 364     129.966  54.137  61.918  1.00 96.63           N  
ANISOU 2820  N   ASP A 364    12011  11225  13479   -281    346   4300       N  
ATOM   2821  CA  ASP A 364     130.895  53.020  61.835  1.00107.84           C  
ANISOU 2821  CA  ASP A 364    13280  12545  15149   -169    268   4379       C  
ATOM   2822  C   ASP A 364     130.571  52.176  60.608  1.00109.07           C  
ANISOU 2822  C   ASP A 364    13376  12647  15417     30    395   4205       C  
ATOM   2823  O   ASP A 364     129.515  51.548  60.544  1.00113.48           O  
ANISOU 2823  O   ASP A 364    14040  13138  15939     41    422   4107       O  
ATOM   2824  CB  ASP A 364     130.821  52.164  63.101  1.00119.91           C  
ANISOU 2824  CB  ASP A 364    14867  13953  16739   -292     80   4529       C  
ATOM   2825  CG  ASP A 364     131.854  51.052  63.117  1.00128.82           C  
ANISOU 2825  CG  ASP A 364    15829  14960  18156   -184    -33   4635       C  
ATOM   2826  OD1 ASP A 364     132.765  51.073  62.262  1.00131.86           O  
ANISOU 2826  OD1 ASP A 364    16039  15371  18691    -31     35   4602       O  
ATOM   2827  OD2 ASP A 364     131.757  50.158  63.986  1.00127.65           O1-
ANISOU 2827  OD2 ASP A 364    15723  14689  18091   -259   -191   4748       O1-
ATOM   2828  N   PRO A 365     131.483  52.165  59.625  1.00103.01           N  
ANISOU 2828  N   PRO A 365    12439  11915  14783    179    479   4159       N  
ATOM   2829  CA  PRO A 365     131.289  51.436  58.367  1.00105.53           C  
ANISOU 2829  CA  PRO A 365    12690  12201  15205    360    620   3980       C  
ATOM   2830  C   PRO A 365     130.898  49.984  58.607  1.00110.72           C  
ANISOU 2830  C   PRO A 365    13356  12689  16024    419    553   3966       C  
ATOM   2831  O   PRO A 365     130.167  49.397  57.809  1.00108.79           O  
ANISOU 2831  O   PRO A 365    13144  12407  15782    515    661   3802       O  
ATOM   2832  CB  PRO A 365     132.670  51.504  57.713  1.00104.23           C  
ANISOU 2832  CB  PRO A 365    12312  12080  15213    469    664   3995       C  
ATOM   2833  CG  PRO A 365     133.281  52.738  58.262  1.00102.42           C  
ANISOU 2833  CG  PRO A 365    12081  11968  14868    344    611   4127       C  
ATOM   2834  CD  PRO A 365     132.791  52.839  59.675  1.00101.70           C  
ANISOU 2834  CD  PRO A 365    12133  11830  14679    170    449   4273       C  
ATOM   2835  N   GLN A 366     131.382  49.414  59.705  1.00116.19           N  
ANISOU 2835  N   GLN A 366    14024  13277  16846    351    367   4143       N  
ATOM   2836  CA  GLN A 366     131.093  48.026  60.038  1.00119.26           C  
ANISOU 2836  CA  GLN A 366    14421  13490  17402    392    273   4159       C  
ATOM   2837  C   GLN A 366     129.604  47.813  60.291  1.00117.44           C  
ANISOU 2837  C   GLN A 366    14399  13233  16990    310    293   4076       C  
ATOM   2838  O   GLN A 366     129.125  46.679  60.298  1.00124.21           O  
ANISOU 2838  O   GLN A 366    15286  13957  17952    358    260   4036       O  
ATOM   2839  CB  GLN A 366     131.901  47.595  61.264  1.00123.70           C  
ANISOU 2839  CB  GLN A 366    14932  13952  18117    301     40   4396       C  
ATOM   2840  CG  GLN A 366     131.823  46.109  61.571  1.00128.58           C  
ANISOU 2840  CG  GLN A 366    15529  14369  18958    355    -81   4435       C  
ATOM   2841  CD  GLN A 366     132.466  45.258  60.494  1.00133.26           C  
ANISOU 2841  CD  GLN A 366    15924  14876  19834    586      6   4317       C  
ATOM   2842  NE2 GLN A 366     131.917  44.069  60.273  1.00136.56           N  
ANISOU 2842  NE2 GLN A 366    16365  15144  20377    667      2   4237       N  
ATOM   2843  OE1 GLN A 366     133.447  45.663  59.869  1.00131.58           O  
ANISOU 2843  OE1 GLN A 366    15537  14731  19726    683     82   4291       O  
ATOM   2844  N   GLU A 367     128.873  48.905  60.491  1.00108.98           N  
ANISOU 2844  N   GLU A 367    13466  12284  15656    186    347   4043       N  
ATOM   2845  CA  GLU A 367     127.462  48.818  60.855  1.00110.32           C  
ANISOU 2845  CA  GLU A 367    13826  12439  15650     85    361   3968       C  
ATOM   2846  C   GLU A 367     126.505  48.946  59.673  1.00110.84           C  
ANISOU 2846  C   GLU A 367    13942  12556  15618    188    547   3744       C  
ATOM   2847  O   GLU A 367     125.289  48.872  59.846  1.00112.60           O  
ANISOU 2847  O   GLU A 367    14309  12768  15706    121    574   3659       O  
ATOM   2848  CB  GLU A 367     127.118  49.843  61.937  1.00114.16           C  
ANISOU 2848  CB  GLU A 367    14443  13009  15924   -134    295   4060       C  
ATOM   2849  CG  GLU A 367     127.632  49.461  63.314  1.00124.38           C  
ANISOU 2849  CG  GLU A 367    15756  14231  17272   -291     88   4275       C  
ATOM   2850  CD  GLU A 367     126.995  50.274  64.419  1.00129.05           C  
ANISOU 2850  CD  GLU A 367    16511  14892  17632   -533     40   4328       C  
ATOM   2851  OE1 GLU A 367     126.613  51.435  64.158  1.00129.28           O  
ANISOU 2851  OE1 GLU A 367    16586  15043  17492   -569    152   4239       O  
ATOM   2852  OE2 GLU A 367     126.879  49.752  65.549  1.00128.41           O1-
ANISOU 2852  OE2 GLU A 367    16510  14739  17539   -697   -112   4455       O1-
ATOM   2853  N   LEU A 368     127.049  49.136  58.476  1.00109.38           N  
ANISOU 2853  N   LEU A 368    13635  12427  15499    339    674   3648       N  
ATOM   2854  CA  LEU A 368     126.222  49.161  57.275  1.00100.95           C  
ANISOU 2854  CA  LEU A 368    12604  11401  14350    435    841   3444       C  
ATOM   2855  C   LEU A 368     125.734  47.757  56.939  1.00101.73           C  
ANISOU 2855  C   LEU A 368    12709  11366  14579    532    855   3351       C  
ATOM   2856  O   LEU A 368     124.828  47.582  56.127  1.00101.38           O  
ANISOU 2856  O   LEU A 368    12727  11333  14458    586    970   3187       O  
ATOM   2857  CB  LEU A 368     126.989  49.750  56.091  1.00 96.98           C  
ANISOU 2857  CB  LEU A 368    11975  11004  13868    544    970   3372       C  
ATOM   2858  CG  LEU A 368     127.136  51.270  56.079  1.00 95.97           C  
ANISOU 2858  CG  LEU A 368    11875  11027  13561    457   1000   3406       C  
ATOM   2859  CD1 LEU A 368     127.925  51.720  54.863  1.00 95.46           C  
ANISOU 2859  CD1 LEU A 368    11686  11062  13523    557   1126   3335       C  
ATOM   2860  CD2 LEU A 368     125.768  51.929  56.105  1.00 96.19           C  
ANISOU 2860  CD2 LEU A 368    12075  11102  13373    372   1039   3320       C  
ATOM   2861  N   ASP A 369     126.342  46.758  57.571  1.00103.30           N  
ANISOU 2861  N   ASP A 369    12840  11430  14978    549    728   3462       N  
ATOM   2862  CA  ASP A 369     125.933  45.373  57.374  1.00103.68           C  
ANISOU 2862  CA  ASP A 369    12894  11329  15171    633    719   3393       C  
ATOM   2863  C   ASP A 369     124.516  45.161  57.897  1.00 95.15           C  
ANISOU 2863  C   ASP A 369    12008  10218  13926    520    695   3351       C  
ATOM   2864  O   ASP A 369     123.879  44.149  57.605  1.00 92.66           O  
ANISOU 2864  O   ASP A 369    11733   9803  13671    576    717   3257       O  
ATOM   2865  CB  ASP A 369     126.904  44.414  58.069  1.00110.62           C  
ANISOU 2865  CB  ASP A 369    13663  12056  16312    658    557   3547       C  
ATOM   2866  CG  ASP A 369     128.264  44.364  57.393  1.00118.46           C  
ANISOU 2866  CG  ASP A 369    14436  13054  17522    802    600   3548       C  
ATOM   2867  OD1 ASP A 369     128.603  45.315  56.657  1.00119.08           O  
ANISOU 2867  OD1 ASP A 369    14458  13278  17508    834    728   3480       O  
ATOM   2868  OD2 ASP A 369     128.995  43.371  57.600  1.00121.74           O1-
ANISOU 2868  OD2 ASP A 369    14729  13321  18206    879    503   3614       O1-
ATOM   2869  N   ILE A 370     124.029  46.124  58.674  1.00 89.76           N  
ANISOU 2869  N   ILE A 370    11441   9624  13040    355    655   3411       N  
ATOM   2870  CA  ILE A 370     122.673  46.070  59.202  1.00 96.59           C  
ANISOU 2870  CA  ILE A 370    12483  10480  13737    230    647   3357       C  
ATOM   2871  C   ILE A 370     121.663  45.939  58.070  1.00 98.62           C  
ANISOU 2871  C   ILE A 370    12785  10764  13923    327    805   3144       C  
ATOM   2872  O   ILE A 370     120.676  45.210  58.180  1.00100.62           O  
ANISOU 2872  O   ILE A 370    13137  10947  14147    302    805   3070       O  
ATOM   2873  CB  ILE A 370     122.341  47.333  60.018  1.00100.25           C  
ANISOU 2873  CB  ILE A 370    13041  11057  13992     50    621   3415       C  
ATOM   2874  CG1 ILE A 370     123.163  47.370  61.306  1.00106.68           C  
ANISOU 2874  CG1 ILE A 370    13845  11840  14848    -89    447   3632       C  
ATOM   2875  CG2 ILE A 370     120.861  47.385  60.347  1.00 98.41           C  
ANISOU 2875  CG2 ILE A 370    12972  10833  13587    -62    654   3309       C  
ATOM   2876  CD1 ILE A 370     122.917  48.604  62.148  1.00108.37           C  
ANISOU 2876  CD1 ILE A 370    14148  12164  14862   -279    426   3685       C  
ATOM   2877  N   LEU A 371     121.929  46.646  56.977  1.00 91.28           N  
ANISOU 2877  N   LEU A 371    11784   9937  12960    428    934   3051       N  
ATOM   2878  CA  LEU A 371     121.015  46.700  55.842  1.00 81.82           C  
ANISOU 2878  CA  LEU A 371    10630   8785  11673    503   1079   2858       C  
ATOM   2879  C   LEU A 371     120.985  45.404  55.037  1.00 82.92           C  
ANISOU 2879  C   LEU A 371    10721   8823  11962    643   1136   2752       C  
ATOM   2880  O   LEU A 371     120.163  45.248  54.135  1.00 83.28           O  
ANISOU 2880  O   LEU A 371    10812   8889  11939    696   1246   2593       O  
ATOM   2881  CB  LEU A 371     121.391  47.864  54.927  1.00 70.50           C  
ANISOU 2881  CB  LEU A 371     9138   7493  10154    548   1184   2809       C  
ATOM   2882  CG  LEU A 371     121.553  49.214  55.623  1.00 68.82           C  
ANISOU 2882  CG  LEU A 371     8958   7379   9810    422   1135   2910       C  
ATOM   2883  CD1 LEU A 371     122.019  50.270  54.634  1.00 70.74           C  
ANISOU 2883  CD1 LEU A 371     9137   7751   9989    473   1232   2869       C  
ATOM   2884  CD2 LEU A 371     120.252  49.628  56.285  1.00 65.78           C  
ANISOU 2884  CD2 LEU A 371     8725   7005   9264    290   1113   2871       C  
ATOM   2885  N   LYS A 372     121.878  44.475  55.359  1.00 79.84           N  
ANISOU 2885  N   LYS A 372    10235   8316  11785    699   1057   2839       N  
ATOM   2886  CA  LYS A 372     121.952  43.222  54.617  1.00 76.46           C  
ANISOU 2886  CA  LYS A 372     9745   7776  11530    837   1111   2735       C  
ATOM   2887  C   LYS A 372     120.653  42.433  54.723  1.00 75.75           C  
ANISOU 2887  C   LYS A 372     9794   7608  11379    803   1110   2646       C  
ATOM   2888  O   LYS A 372     120.485  41.408  54.064  1.00 79.60           O  
ANISOU 2888  O   LYS A 372    10259   8005  11981    905   1167   2536       O  
ATOM   2889  CB  LYS A 372     123.139  42.373  55.080  1.00 76.99           C  
ANISOU 2889  CB  LYS A 372     9679   7711  11865    898   1001   2858       C  
ATOM   2890  CG  LYS A 372     124.489  42.936  54.668  1.00 87.07           C  
ANISOU 2890  CG  LYS A 372    10780   9055  13246    972   1036   2900       C  
ATOM   2891  CD  LYS A 372     125.586  41.890  54.764  1.00 97.94           C  
ANISOU 2891  CD  LYS A 372    11992  10282  14937   1080    965   2959       C  
ATOM   2892  CE  LYS A 372     126.900  42.429  54.219  1.00104.12           C  
ANISOU 2892  CE  LYS A 372    12587  11143  15832   1162   1028   2969       C  
ATOM   2893  NZ  LYS A 372     127.968  41.391  54.195  1.00108.64           N1+
ANISOU 2893  NZ  LYS A 372    12974  11563  16743   1285    975   2997       N1+
ATOM   2894  N   THR A 373     119.734  42.917  55.550  1.00 73.70           N  
ANISOU 2894  N   THR A 373     9676   7384  10942    652   1052   2684       N  
ATOM   2895  CA  THR A 373     118.438  42.271  55.703  1.00 84.68           C  
ANISOU 2895  CA  THR A 373    11202   8717  12254    599   1055   2596       C  
ATOM   2896  C   THR A 373     117.390  42.941  54.825  1.00 91.40           C  
ANISOU 2896  C   THR A 373    12122   9682  12923    607   1192   2427       C  
ATOM   2897  O   THR A 373     116.340  42.361  54.545  1.00 93.15           O  
ANISOU 2897  O   THR A 373    12429   9867  13097    606   1233   2311       O  
ATOM   2898  CB  THR A 373     117.962  42.283  57.167  1.00 82.55           C  
ANISOU 2898  CB  THR A 373    11050   8411  11903    411    913   2720       C  
ATOM   2899  CG2 THR A 373     118.802  41.335  58.006  1.00 76.76           C  
ANISOU 2899  CG2 THR A 373    10272   7532  11360    395    755   2885       C  
ATOM   2900  OG1 THR A 373     118.071  43.610  57.698  1.00 84.16           O  
ANISOU 2900  OG1 THR A 373    11274   8741  11963    301    898   2790       O  
ATOM   2901  N   VAL A 374     117.684  44.165  54.394  1.00 89.82           N  
ANISOU 2901  N   VAL A 374    11882   9617  12627    611   1252   2422       N  
ATOM   2902  CA  VAL A 374     116.767  44.923  53.551  1.00 89.19           C  
ANISOU 2902  CA  VAL A 374    11859   9645  12384    613   1361   2283       C  
ATOM   2903  C   VAL A 374     116.516  44.197  52.239  1.00 94.83           C  
ANISOU 2903  C   VAL A 374    12549  10341  13142    739   1478   2125       C  
ATOM   2904  O   VAL A 374     117.455  43.785  51.558  1.00 98.59           O  
ANISOU 2904  O   VAL A 374    12914  10799  13746    849   1529   2110       O  
ATOM   2905  CB  VAL A 374     117.307  46.327  53.244  1.00 87.81           C  
ANISOU 2905  CB  VAL A 374    11634   9605  12123    602   1394   2320       C  
ATOM   2906  CG1 VAL A 374     116.357  47.064  52.315  1.00 86.95           C  
ANISOU 2906  CG1 VAL A 374    11582   9591  11864    606   1488   2184       C  
ATOM   2907  CG2 VAL A 374     117.513  47.105  54.531  1.00 89.71           C  
ANISOU 2907  CG2 VAL A 374    11907   9871  12310    466   1288   2464       C  
ATOM   2908  N   LYS A 375     115.246  44.048  51.884  1.00 96.00           N  
ANISOU 2908  N   LYS A 375    12797  10496  13184    716   1524   2001       N  
ATOM   2909  CA  LYS A 375     114.881  43.295  50.694  1.00 96.31           C  
ANISOU 2909  CA  LYS A 375    12831  10513  13248    814   1629   1847       C  
ATOM   2910  C   LYS A 375     114.290  44.207  49.622  1.00 93.33           C  
ANISOU 2910  C   LYS A 375    12480  10265  12718    819   1723   1739       C  
ATOM   2911  O   LYS A 375     114.641  44.100  48.448  1.00 94.26           O  
ANISOU 2911  O   LYS A 375    12543  10423  12846    900   1822   1653       O  
ATOM   2912  CB  LYS A 375     113.892  42.183  51.051  1.00 98.28           C  
ANISOU 2912  CB  LYS A 375    13175  10653  13515    788   1601   1787       C  
ATOM   2913  CG  LYS A 375     114.206  40.837  50.420  1.00101.79           C  
ANISOU 2913  CG  LYS A 375    13574  10988  14115    899   1650   1711       C  
ATOM   2914  CD  LYS A 375     115.378  40.165  51.121  1.00105.38           C  
ANISOU 2914  CD  LYS A 375    13939  11328  14773    936   1564   1839       C  
ATOM   2915  CE  LYS A 375     115.596  38.750  50.606  1.00111.56           C  
ANISOU 2915  CE  LYS A 375    14678  11974  15737   1043   1601   1756       C  
ATOM   2916  NZ  LYS A 375     116.735  38.070  51.288  1.00115.71           N1+
ANISOU 2916  NZ  LYS A 375    15105  12368  16493   1086   1499   1885       N1+
ATOM   2917  N   GLU A 376     113.398  45.105  50.029  1.00 88.23           N  
ANISOU 2917  N   GLU A 376    11914   9677  11932    723   1687   1742       N  
ATOM   2918  CA  GLU A 376     112.759  46.015  49.082  1.00 84.45           C  
ANISOU 2918  CA  GLU A 376    11464   9306  11319    718   1748   1655       C  
ATOM   2919  C   GLU A 376     112.660  47.440  49.621  1.00 79.58           C  
ANISOU 2919  C   GLU A 376    10862   8769  10608    632   1695   1730       C  
ATOM   2920  O   GLU A 376     112.608  47.660  50.829  1.00 85.82           O  
ANISOU 2920  O   GLU A 376    11678   9530  11402    549   1617   1813       O  
ATOM   2921  CB  GLU A 376     111.371  45.502  48.693  1.00 86.24           C  
ANISOU 2921  CB  GLU A 376    11780   9506  11482    704   1776   1521       C  
ATOM   2922  CG  GLU A 376     110.301  45.754  49.739  1.00101.63           C  
ANISOU 2922  CG  GLU A 376    13814  11431  13371    596   1706   1526       C  
ATOM   2923  CD  GLU A 376     108.928  45.293  49.290  1.00116.70           C  
ANISOU 2923  CD  GLU A 376    15799  13321  15220    584   1736   1386       C  
ATOM   2924  OE1 GLU A 376     107.937  46.001  49.572  1.00121.90           O  
ANISOU 2924  OE1 GLU A 376    16506  14014  15797    509   1711   1348       O  
ATOM   2925  OE2 GLU A 376     108.840  44.225  48.649  1.00119.65           O1-
ANISOU 2925  OE2 GLU A 376    16179  13644  15637    647   1787   1310       O1-
ATOM   2926  N   ILE A 377     112.634  48.405  48.707  1.00 69.59           N  
ANISOU 2926  N   ILE A 377     9583   7601   9256    643   1735   1698       N  
ATOM   2927  CA  ILE A 377     112.541  49.814  49.066  1.00 69.60           C  
ANISOU 2927  CA  ILE A 377     9594   7674   9177    571   1688   1759       C  
ATOM   2928  C   ILE A 377     111.412  50.483  48.292  1.00 74.65           C  
ANISOU 2928  C   ILE A 377    10289   8361   9714    551   1701   1662       C  
ATOM   2929  O   ILE A 377     111.511  50.682  47.082  1.00 74.59           O  
ANISOU 2929  O   ILE A 377    10267   8413   9660    592   1751   1615       O  
ATOM   2930  CB  ILE A 377     113.853  50.554  48.757  1.00 69.67           C  
ANISOU 2930  CB  ILE A 377     9520   7757   9195    594   1699   1854       C  
ATOM   2931  CG1 ILE A 377     115.001  49.971  49.582  1.00 72.25           C  
ANISOU 2931  CG1 ILE A 377     9779   8033   9641    610   1668   1963       C  
ATOM   2932  CG2 ILE A 377     113.702  52.044  49.020  1.00 64.30           C  
ANISOU 2932  CG2 ILE A 377     8857   7145   8430    519   1651   1908       C  
ATOM   2933  CD1 ILE A 377     116.355  50.536  49.217  1.00 75.25           C  
ANISOU 2933  CD1 ILE A 377    10060   8485  10048    642   1690   2044       C  
ATOM   2934  N   THR A 378     110.341  50.836  48.996  1.00 74.83           N  
ANISOU 2934  N   THR A 378    10370   8358   9703    477   1653   1630       N  
ATOM   2935  CA  THR A 378     109.161  51.407  48.356  1.00 70.85           C  
ANISOU 2935  CA  THR A 378     9910   7880   9130    459   1650   1534       C  
ATOM   2936  C   THR A 378     109.463  52.708  47.620  1.00 69.62           C  
ANISOU 2936  C   THR A 378     9728   7806   8917    456   1635   1573       C  
ATOM   2937  O   THR A 378     108.779  53.055  46.660  1.00 70.15           O  
ANISOU 2937  O   THR A 378     9819   7904   8932    464   1634   1508       O  
ATOM   2938  CB  THR A 378     108.032  51.647  49.371  1.00 72.64           C  
ANISOU 2938  CB  THR A 378    10184   8063   9353    374   1604   1489       C  
ATOM   2939  CG2 THR A 378     107.714  50.363  50.111  1.00 82.02           C  
ANISOU 2939  CG2 THR A 378    11408   9172  10582    356   1612   1457       C  
ATOM   2940  OG1 THR A 378     108.433  52.649  50.312  1.00 72.39           O  
ANISOU 2940  OG1 THR A 378    10134   8048   9322    304   1557   1574       O  
ATOM   2941  N   GLY A 379     110.490  53.421  48.071  1.00 76.99           N  
ANISOU 2941  N   GLY A 379    10617   8774   9860    437   1613   1686       N  
ATOM   2942  CA  GLY A 379     110.858  54.689  47.466  1.00 80.21           C  
ANISOU 2942  CA  GLY A 379    11005   9257  10214    423   1590   1737       C  
ATOM   2943  C   GLY A 379     112.111  54.605  46.616  1.00 76.01           C  
ANISOU 2943  C   GLY A 379    10418   8793   9669    471   1643   1791       C  
ATOM   2944  O   GLY A 379     112.249  53.712  45.780  1.00 75.57           O  
ANISOU 2944  O   GLY A 379    10355   8743   9614    527   1710   1729       O  
ATOM   2945  N   PHE A 380     113.032  55.540  46.830  1.00 72.31           N  
ANISOU 2945  N   PHE A 380     9909   8376   9190    443   1618   1896       N  
ATOM   2946  CA  PHE A 380     114.267  55.568  46.058  1.00 79.67           C  
ANISOU 2946  CA  PHE A 380    10780   9383  10109    476   1672   1945       C  
ATOM   2947  C   PHE A 380     115.498  55.288  46.913  1.00 85.33           C  
ANISOU 2947  C   PHE A 380    11424  10091  10906    489   1676   2043       C  
ATOM   2948  O   PHE A 380     115.454  55.384  48.139  1.00 90.24           O  
ANISOU 2948  O   PHE A 380    12054  10664  11571    449   1619   2101       O  
ATOM   2949  CB  PHE A 380     114.423  56.902  45.318  1.00 77.43           C  
ANISOU 2949  CB  PHE A 380    10504   9183   9734    429   1642   1989       C  
ATOM   2950  CG  PHE A 380     114.739  58.068  46.214  1.00 77.23           C  
ANISOU 2950  CG  PHE A 380    10470   9164   9712    368   1569   2093       C  
ATOM   2951  CD1 PHE A 380     115.986  58.190  46.804  1.00 79.84           C  
ANISOU 2951  CD1 PHE A 380    10736   9522  10079    363   1576   2195       C  
ATOM   2952  CD2 PHE A 380     113.798  59.057  46.445  1.00 73.06           C  
ANISOU 2952  CD2 PHE A 380     9991   8609   9158    314   1492   2084       C  
ATOM   2953  CE1 PHE A 380     116.282  59.262  47.620  1.00 78.96           C  
ANISOU 2953  CE1 PHE A 380    10621   9418   9962    298   1512   2289       C  
ATOM   2954  CE2 PHE A 380     114.089  60.133  47.259  1.00 68.92           C  
ANISOU 2954  CE2 PHE A 380     9460   8087   8642    254   1433   2167       C  
ATOM   2955  CZ  PHE A 380     115.333  60.235  47.847  1.00 72.71           C  
ANISOU 2955  CZ  PHE A 380     9886   8601   9141    242   1444   2270       C  
ATOM   2956  N   LEU A 381     116.596  54.942  46.249  1.00 81.18           N  
ANISOU 2956  N   LEU A 381    10825   9616  10404    535   1744   2058       N  
ATOM   2957  CA  LEU A 381     117.864  54.705  46.920  1.00 74.52           C  
ANISOU 2957  CA  LEU A 381     9893   8769   9653    554   1745   2154       C  
ATOM   2958  C   LEU A 381     118.911  55.698  46.437  1.00 75.98           C  
ANISOU 2958  C   LEU A 381    10019   9059   9791    527   1760   2229       C  
ATOM   2959  O   LEU A 381     119.320  55.668  45.278  1.00 75.45           O  
ANISOU 2959  O   LEU A 381     9921   9065   9683    547   1838   2179       O  
ATOM   2960  CB  LEU A 381     118.345  53.276  46.671  1.00 74.91           C  
ANISOU 2960  CB  LEU A 381     9880   8767   9815    641   1815   2098       C  
ATOM   2961  CG  LEU A 381     119.727  52.933  47.232  1.00 75.00           C  
ANISOU 2961  CG  LEU A 381     9777   8766   9954    674   1813   2192       C  
ATOM   2962  CD1 LEU A 381     119.774  53.189  48.728  1.00 79.58           C  
ANISOU 2962  CD1 LEU A 381    10374   9291  10573    616   1702   2315       C  
ATOM   2963  CD2 LEU A 381     120.096  51.491  46.921  1.00 70.04           C  
ANISOU 2963  CD2 LEU A 381     9083   8068   9463    769   1880   2119       C  
ATOM   2964  N   LEU A 382     119.336  56.581  47.334  1.00 81.00           N  
ANISOU 2964  N   LEU A 382    10645   9707  10423    468   1688   2345       N  
ATOM   2965  CA  LEU A 382     120.356  57.572  47.019  1.00 80.55           C  
ANISOU 2965  CA  LEU A 382    10535   9748  10322    432   1692   2430       C  
ATOM   2966  C   LEU A 382     121.642  57.291  47.792  1.00 86.14           C  
ANISOU 2966  C   LEU A 382    11140  10453  11137    446   1683   2533       C  
ATOM   2967  O   LEU A 382     121.636  57.221  49.020  1.00 89.91           O  
ANISOU 2967  O   LEU A 382    11625  10869  11668    416   1609   2607       O  
ATOM   2968  CB  LEU A 382     119.849  58.979  47.339  1.00 73.14           C  
ANISOU 2968  CB  LEU A 382     9666   8832   9292    344   1612   2484       C  
ATOM   2969  CG  LEU A 382     120.889  60.098  47.252  1.00 72.70           C  
ANISOU 2969  CG  LEU A 382     9565   8865   9191    290   1596   2592       C  
ATOM   2970  CD1 LEU A 382     121.351  60.298  45.816  1.00 67.18           C  
ANISOU 2970  CD1 LEU A 382     8843   8267   8417    294   1668   2556       C  
ATOM   2971  CD2 LEU A 382     120.339  61.394  47.830  1.00 69.54           C  
ANISOU 2971  CD2 LEU A 382     9234   8455   8732    204   1505   2645       C  
ATOM   2972  N   ILE A 383     122.742  57.127  47.066  1.00 85.00           N  
ANISOU 2972  N   ILE A 383    10897  10377  11024    483   1757   2534       N  
ATOM   2973  CA  ILE A 383     124.035  56.868  47.687  1.00 79.75           C  
ANISOU 2973  CA  ILE A 383    10112   9711  10477    503   1748   2629       C  
ATOM   2974  C   ILE A 383     125.108  57.789  47.116  1.00 85.14           C  
ANISOU 2974  C   ILE A 383    10725  10518  11108    465   1784   2684       C  
ATOM   2975  O   ILE A 383     125.697  57.498  46.078  1.00 91.46           O  
ANISOU 2975  O   ILE A 383    11452  11383  11915    500   1887   2614       O  
ATOM   2976  CB  ILE A 383     124.476  55.406  47.489  1.00 71.53           C  
ANISOU 2976  CB  ILE A 383     8979   8606   9594    607   1812   2562       C  
ATOM   2977  CG1 ILE A 383     123.390  54.447  47.973  1.00 67.49           C  
ANISOU 2977  CG1 ILE A 383     8545   7973   9126    638   1778   2504       C  
ATOM   2978  CG2 ILE A 383     125.775  55.138  48.224  1.00 67.64           C  
ANISOU 2978  CG2 ILE A 383     8353   8094   9251    629   1777   2672       C  
ATOM   2979  CD1 ILE A 383     123.790  52.990  47.892  1.00 67.37           C  
ANISOU 2979  CD1 ILE A 383     8444   7870   9283    738   1823   2447       C  
ATOM   2980  N   GLN A 384     125.355  58.902  47.801  1.00 83.64           N  
ANISOU 2980  N   GLN A 384    10557  10362  10863    383   1704   2802       N  
ATOM   2981  CA  GLN A 384     126.353  59.869  47.358  1.00 79.64           C  
ANISOU 2981  CA  GLN A 384     9993   9971  10297    331   1725   2868       C  
ATOM   2982  C   GLN A 384     127.702  59.617  48.021  1.00 85.84           C  
ANISOU 2982  C   GLN A 384    10640  10764  11210    347   1712   2967       C  
ATOM   2983  O   GLN A 384     128.692  60.274  47.701  1.00 92.17           O  
ANISOU 2983  O   GLN A 384    11370  11665  11987    310   1738   3021       O  
ATOM   2984  CB  GLN A 384     125.882  61.295  47.648  1.00 77.52           C  
ANISOU 2984  CB  GLN A 384     9823   9733   9896    228   1644   2938       C  
ATOM   2985  CG  GLN A 384     124.587  61.666  46.945  1.00 85.05           C  
ANISOU 2985  CG  GLN A 384    10899  10676  10738    209   1640   2851       C  
ATOM   2986  CD  GLN A 384     124.174  63.104  47.190  1.00 91.28           C  
ANISOU 2986  CD  GLN A 384    11772  11483  11427    114   1556   2917       C  
ATOM   2987  NE2 GLN A 384     124.872  63.775  48.101  1.00 91.75           N  
ANISOU 2987  NE2 GLN A 384    11802  11555  11502     57   1500   3033       N  
ATOM   2988  OE1 GLN A 384     123.238  63.607  46.567  1.00 93.60           O  
ANISOU 2988  OE1 GLN A 384    12154  11772  11637     89   1535   2864       O  
ATOM   2989  N   ALA A 385     127.735  58.661  48.943  1.00 86.05           N  
ANISOU 2989  N   ALA A 385    10633  10687  11377    396   1665   2995       N  
ATOM   2990  CA  ALA A 385     128.963  58.316  49.648  1.00 90.13           C  
ANISOU 2990  CA  ALA A 385    11015  11190  12040    413   1628   3100       C  
ATOM   2991  C   ALA A 385     128.952  56.854  50.072  1.00 92.44           C  
ANISOU 2991  C   ALA A 385    11251  11358  12513    505   1614   3073       C  
ATOM   2992  O   ALA A 385     127.896  56.226  50.137  1.00 94.39           O  
ANISOU 2992  O   ALA A 385    11589  11523  12752    530   1608   2999       O  
ATOM   2993  CB  ALA A 385     129.152  59.212  50.853  1.00 92.16           C  
ANISOU 2993  CB  ALA A 385    11311  11451  12256    310   1508   3253       C  
ATOM   2994  N   TRP A 386     130.131  56.319  50.367  1.00 91.87           N  
ANISOU 2994  N   TRP A 386    11026  11267  12613    551   1601   3136       N  
ATOM   2995  CA  TRP A 386     130.265  54.912  50.715  1.00 91.97           C  
ANISOU 2995  CA  TRP A 386    10966  11151  12829    644   1578   3118       C  
ATOM   2996  C   TRP A 386     131.670  54.637  51.233  1.00103.56           C  
ANISOU 2996  C   TRP A 386    12258  12602  14489    671   1525   3230       C  
ATOM   2997  O   TRP A 386     132.632  55.253  50.772  1.00102.78           O  
ANISOU 2997  O   TRP A 386    12055  12609  14389    661   1579   3248       O  
ATOM   2998  CB  TRP A 386     129.978  54.045  49.488  1.00 86.18           C  
ANISOU 2998  CB  TRP A 386    10201  10403  12141    747   1718   2932       C  
ATOM   2999  CG  TRP A 386     129.758  52.602  49.802  1.00 80.77           C  
ANISOU 2999  CG  TRP A 386     9484   9565  11640    839   1693   2891       C  
ATOM   3000  CD1 TRP A 386     130.643  51.580  49.625  1.00 80.04           C  
ANISOU 3000  CD1 TRP A 386     9225   9403  11784    943   1725   2859       C  
ATOM   3001  CD2 TRP A 386     128.572  52.016  50.348  1.00 80.62           C  
ANISOU 3001  CD2 TRP A 386     9599   9437  11594    831   1629   2875       C  
ATOM   3002  CE2 TRP A 386     128.810  50.634  50.475  1.00 83.15           C  
ANISOU 3002  CE2 TRP A 386     9837   9624  12134    929   1618   2842       C  
ATOM   3003  CE3 TRP A 386     127.332  52.526  50.743  1.00 78.28           C  
ANISOU 3003  CE3 TRP A 386     9480   9142  11120    747   1581   2878       C  
ATOM   3004  NE1 TRP A 386     130.082  50.393  50.027  1.00 79.28           N  
ANISOU 3004  NE1 TRP A 386     9159   9154  11812   1002   1675   2831       N  
ATOM   3005  CZ2 TRP A 386     127.855  49.757  50.980  1.00 88.42           C  
ANISOU 3005  CZ2 TRP A 386    10603  10164  12830    938   1557   2822       C  
ATOM   3006  CZ3 TRP A 386     126.385  51.654  51.243  1.00 77.02           C  
ANISOU 3006  CZ3 TRP A 386     9410   8864  10991    755   1531   2848       C  
ATOM   3007  CH2 TRP A 386     126.651  50.285  51.357  1.00 84.11           C  
ANISOU 3007  CH2 TRP A 386    10233   9635  12090    846   1518   2825       C  
ATOM   3008  N   PRO A 387     131.792  53.712  52.199  1.00109.31           N  
ANISOU 3008  N   PRO A 387    12953  13195  15385    697   1411   3312       N  
ATOM   3009  CA  PRO A 387     133.084  53.330  52.778  1.00114.73           C  
ANISOU 3009  CA  PRO A 387    13466  13839  16287    726   1331   3433       C  
ATOM   3010  C   PRO A 387     134.142  53.075  51.708  1.00124.92           C  
ANISOU 3010  C   PRO A 387    14560  15184  17718    828   1464   3334       C  
ATOM   3011  O   PRO A 387     133.921  52.293  50.784  1.00127.37           O  
ANISOU 3011  O   PRO A 387    14832  15463  18099    927   1585   3169       O  
ATOM   3012  CB  PRO A 387     132.755  52.036  53.522  1.00110.53           C  
ANISOU 3012  CB  PRO A 387    12941  13130  15926    773   1226   3466       C  
ATOM   3013  CG  PRO A 387     131.336  52.204  53.926  1.00105.88           C  
ANISOU 3013  CG  PRO A 387    12566  12518  15148    693   1193   3446       C  
ATOM   3014  CD  PRO A 387     130.675  52.973  52.814  1.00105.32           C  
ANISOU 3014  CD  PRO A 387    12577  12566  14876    690   1341   3300       C  
ATOM   3015  N   GLU A 388     135.284  53.739  51.844  1.00133.87           N  
ANISOU 3015  N   GLU A 388    15571  16403  18890    794   1447   3429       N  
ATOM   3016  CA  GLU A 388     136.352  53.654  50.854  1.00143.30           C  
ANISOU 3016  CA  GLU A 388    16573  17673  20203    867   1582   3333       C  
ATOM   3017  C   GLU A 388     137.023  52.285  50.855  1.00138.24           C  
ANISOU 3017  C   GLU A 388    15742  16894  19888   1003   1579   3290       C  
ATOM   3018  O   GLU A 388     137.350  51.744  49.798  1.00132.81           O  
ANISOU 3018  O   GLU A 388    14935  16220  19306   1096   1736   3116       O  
ATOM   3019  CB  GLU A 388     137.390  54.753  51.097  1.00156.10           C  
ANISOU 3019  CB  GLU A 388    18112  19420  21779    783   1553   3456       C  
ATOM   3020  CG  GLU A 388     138.031  54.720  52.479  1.00167.17           C  
ANISOU 3020  CG  GLU A 388    19457  20749  23310    740   1357   3671       C  
ATOM   3021  CD  GLU A 388     137.074  55.131  53.582  1.00171.42           C  
ANISOU 3021  CD  GLU A 388    20205  21245  23682    625   1212   3797       C  
ATOM   3022  OE1 GLU A 388     137.170  54.572  54.695  1.00169.76           O  
ANISOU 3022  OE1 GLU A 388    19989  20917  23595    606   1050   3933       O  
ATOM   3023  OE2 GLU A 388     136.222  56.011  53.334  1.00174.07           O1-
ANISOU 3023  OE2 GLU A 388    20709  21662  23769    547   1259   3757       O1-
ATOM   3024  N   ASN A 389     137.228  51.730  52.045  1.00138.35           N  
ANISOU 3024  N   ASN A 389    15728  16772  20066   1006   1396   3447       N  
ATOM   3025  CA  ASN A 389     137.837  50.414  52.172  1.00143.02           C  
ANISOU 3025  CA  ASN A 389    16142  17205  20994   1134   1355   3430       C  
ATOM   3026  C   ASN A 389     136.983  49.337  51.517  1.00133.47           C  
ANISOU 3026  C   ASN A 389    14982  15892  19839   1234   1449   3249       C  
ATOM   3027  O   ASN A 389     137.482  48.278  51.142  1.00139.32           O  
ANISOU 3027  O   ASN A 389    15558  16524  20852   1361   1493   3155       O  
ATOM   3028  CB  ASN A 389     138.090  50.071  53.643  1.00157.91           C  
ANISOU 3028  CB  ASN A 389    18025  18960  23015   1089   1111   3658       C  
ATOM   3029  CG  ASN A 389     139.231  50.873  54.241  1.00168.50           C  
ANISOU 3029  CG  ASN A 389    19252  20380  24391   1017   1016   3831       C  
ATOM   3030  ND2 ASN A 389     139.688  50.464  55.421  1.00169.06           N  
ANISOU 3030  ND2 ASN A 389    19273  20333  24628    986    802   4028       N  
ATOM   3031  OD1 ASN A 389     139.698  51.848  53.650  1.00172.38           O  
ANISOU 3031  OD1 ASN A 389    19703  21036  24757    979   1126   3792       O  
ATOM   3032  N   ARG A 390     135.691  49.616  51.380  1.00122.56           N  
ANISOU 3032  N   ARG A 390    13822  14540  18207   1175   1480   3197       N  
ATOM   3033  CA  ARG A 390     134.776  48.688  50.729  1.00117.51           C  
ANISOU 3033  CA  ARG A 390    13251  13818  17581   1252   1572   3024       C  
ATOM   3034  C   ARG A 390     134.749  48.906  49.220  1.00109.16           C  
ANISOU 3034  C   ARG A 390    12162  12886  16428   1289   1803   2806       C  
ATOM   3035  O   ARG A 390     134.645  50.037  48.744  1.00108.51           O  
ANISOU 3035  O   ARG A 390    12150  12969  16111   1203   1875   2794       O  
ATOM   3036  CB  ARG A 390     133.367  48.819  51.311  1.00119.86           C  
ANISOU 3036  CB  ARG A 390    13792  14081  17667   1168   1490   3066       C  
ATOM   3037  CG  ARG A 390     133.159  48.061  52.614  1.00124.66           C  
ANISOU 3037  CG  ARG A 390    14441  14521  18405   1150   1289   3218       C  
ATOM   3038  CD  ARG A 390     133.285  46.560  52.400  1.00134.27           C  
ANISOU 3038  CD  ARG A 390    15554  15561  19901   1285   1293   3133       C  
ATOM   3039  NE  ARG A 390     132.687  45.798  53.493  1.00140.89           N  
ANISOU 3039  NE  ARG A 390    16495  16238  20799   1249   1114   3250       N  
ATOM   3040  CZ  ARG A 390     132.550  44.475  53.498  1.00145.18           C  
ANISOU 3040  CZ  ARG A 390    16997  16604  21561   1343   1081   3200       C  
ATOM   3041  NH1 ARG A 390     131.990  43.869  54.536  1.00145.61           N1+
ANISOU 3041  NH1 ARG A 390    17162  16523  21642   1284    908   3321       N1+
ATOM   3042  NH2 ARG A 390     132.970  43.757  52.465  1.00146.94           N  
ANISOU 3042  NH2 ARG A 390    17072  16785  21973   1488   1224   3024       N  
ATOM   3043  N   THR A 391     134.843  47.811  48.474  1.00105.20           N  
ANISOU 3043  N   THR A 391    11559  12302  16110   1407   1916   2634       N  
ATOM   3044  CA  THR A 391     134.872  47.869  47.019  1.00108.26           C  
ANISOU 3044  CA  THR A 391    11907  12802  16423   1431   2144   2412       C  
ATOM   3045  C   THR A 391     133.492  47.616  46.424  1.00113.89           C  
ANISOU 3045  C   THR A 391    12814  13512  16949   1417   2217   2281       C  
ATOM   3046  O   THR A 391     133.272  47.816  45.229  1.00113.81           O  
ANISOU 3046  O   THR A 391    12826  13612  16803   1400   2392   2111       O  
ATOM   3047  CB  THR A 391     135.849  46.826  46.450  1.00107.09           C  
ANISOU 3047  CB  THR A 391    11517  12576  16597   1562   2253   2269       C  
ATOM   3048  CG2 THR A 391     135.573  45.457  47.054  1.00 97.22           C  
ANISOU 3048  CG2 THR A 391    10242  11092  15604   1668   2149   2277       C  
ATOM   3049  OG1 THR A 391     135.697  46.751  45.028  1.00115.32           O  
ANISOU 3049  OG1 THR A 391    12550  13720  17548   1570   2485   2029       O  
ATOM   3050  N   ASP A 392     132.564  47.182  47.270  1.00116.94           N  
ANISOU 3050  N   ASP A 392    13339  13773  17320   1411   2079   2363       N  
ATOM   3051  CA  ASP A 392     131.257  46.733  46.814  1.00115.60           C  
ANISOU 3051  CA  ASP A 392    13334  13568  17019   1412   2132   2241       C  
ATOM   3052  C   ASP A 392     130.150  47.396  47.630  1.00112.48           C  
ANISOU 3052  C   ASP A 392    13153  13184  16399   1307   2000   2367       C  
ATOM   3053  O   ASP A 392     130.365  47.779  48.779  1.00118.15           O  
ANISOU 3053  O   ASP A 392    13888  13873  17131   1252   1842   2552       O  
ATOM   3054  CB  ASP A 392     131.168  45.211  46.965  1.00118.37           C  
ANISOU 3054  CB  ASP A 392    13623  13721  17630   1528   2114   2171       C  
ATOM   3055  CG  ASP A 392     130.425  44.548  45.822  1.00120.02           C  
ANISOU 3055  CG  ASP A 392    13887  13926  17790   1570   2280   1943       C  
ATOM   3056  OD1 ASP A 392     129.882  43.441  46.028  1.00114.81           O  
ANISOU 3056  OD1 ASP A 392    13259  13108  17254   1633   2245   1896       O  
ATOM   3057  OD2 ASP A 392     130.390  45.128  44.717  1.00127.53           O1-
ANISOU 3057  OD2 ASP A 392    14852  15032  18573   1531   2439   1815       O1-
ATOM   3058  N   LEU A 393     128.970  47.537  47.034  1.00102.97           N  
ANISOU 3058  N   LEU A 393    12109  12022  14992   1270   2066   2261       N  
ATOM   3059  CA  LEU A 393     127.797  47.984  47.778  1.00 97.33           C  
ANISOU 3059  CA  LEU A 393    11588  11294  14098   1183   1953   2345       C  
ATOM   3060  C   LEU A 393     127.214  46.807  48.555  1.00104.14           C  
ANISOU 3060  C   LEU A 393    12498  11978  15094   1223   1856   2365       C  
ATOM   3061  O   LEU A 393     126.057  46.431  48.368  1.00103.59           O  
ANISOU 3061  O   LEU A 393    12560  11871  14931   1214   1873   2280       O  
ATOM   3062  CB  LEU A 393     126.746  48.577  46.839  1.00 87.98           C  
ANISOU 3062  CB  LEU A 393    10546  10218  12666   1130   2049   2227       C  
ATOM   3063  CG  LEU A 393     127.092  49.931  46.219  1.00 86.09           C  
ANISOU 3063  CG  LEU A 393    10309  10155  12247   1054   2106   2241       C  
ATOM   3064  CD1 LEU A 393     125.933  50.449  45.383  1.00 83.93           C  
ANISOU 3064  CD1 LEU A 393    10188   9960  11742    996   2164   2143       C  
ATOM   3065  CD2 LEU A 393     127.459  50.930  47.302  1.00 85.64           C  
ANISOU 3065  CD2 LEU A 393    10265  10130  12146    974   1973   2433       C  
ATOM   3066  N   HIS A 394     128.035  46.236  49.431  1.00108.27           N  
ANISOU 3066  N   HIS A 394    12912  12389  15838   1259   1743   2484       N  
ATOM   3067  CA  HIS A 394     127.695  45.018  50.160  1.00108.49           C  
ANISOU 3067  CA  HIS A 394    12960  12231  16032   1298   1638   2517       C  
ATOM   3068  C   HIS A 394     126.365  45.090  50.908  1.00104.54           C  
ANISOU 3068  C   HIS A 394    12666  11697  15359   1200   1544   2564       C  
ATOM   3069  O   HIS A 394     125.545  44.180  50.810  1.00102.74           O  
ANISOU 3069  O   HIS A 394    12511  11369  15155   1229   1552   2479       O  
ATOM   3070  CB  HIS A 394     128.822  44.664  51.132  1.00110.37           C  
ANISOU 3070  CB  HIS A 394    13059  12368  16508   1318   1492   2686       C  
ATOM   3071  CG  HIS A 394     129.141  45.753  52.108  1.00111.78           C  
ANISOU 3071  CG  HIS A 394    13272  12625  16573   1197   1366   2880       C  
ATOM   3072  CD2 HIS A 394     129.010  45.811  53.454  1.00114.96           C  
ANISOU 3072  CD2 HIS A 394    13749  12965  16966   1097   1181   3065       C  
ATOM   3073  ND1 HIS A 394     129.668  46.967  51.722  1.00108.37           N  
ANISOU 3073  ND1 HIS A 394    12802  12361  16014   1155   1433   2895       N  
ATOM   3074  CE1 HIS A 394     129.845  47.727  52.788  1.00109.94           C  
ANISOU 3074  CE1 HIS A 394    13046  12590  16134   1042   1296   3076       C  
ATOM   3075  NE2 HIS A 394     129.454  47.049  53.852  1.00113.61           N  
ANISOU 3075  NE2 HIS A 394    13580  12921  16665   1000   1144   3180       N  
ATOM   3076  N   ALA A 395     126.159  46.166  51.660  1.00104.24           N  
ANISOU 3076  N   ALA A 395    12715  11741  15152   1078   1460   2690       N  
ATOM   3077  CA  ALA A 395     124.963  46.312  52.486  1.00106.45           C  
ANISOU 3077  CA  ALA A 395    13176  11995  15277    968   1371   2734       C  
ATOM   3078  C   ALA A 395     123.687  45.942  51.735  1.00103.34           C  
ANISOU 3078  C   ALA A 395    12897  11597  14770    989   1469   2562       C  
ATOM   3079  O   ALA A 395     122.776  45.338  52.302  1.00 99.81           O  
ANISOU 3079  O   ALA A 395    12560  11061  14304    948   1407   2559       O  
ATOM   3080  CB  ALA A 395     124.864  47.728  53.028  1.00112.93           C  
ANISOU 3080  CB  ALA A 395    14065  12938  15903    841   1326   2834       C  
ATOM   3081  N   PHE A 396     123.627  46.309  50.460  1.00 99.25           N  
ANISOU 3081  N   PHE A 396    12357  11181  14174   1040   1619   2422       N  
ATOM   3082  CA  PHE A 396     122.451  46.040  49.642  1.00 87.14           C  
ANISOU 3082  CA  PHE A 396    10928   9657  12523   1053   1712   2259       C  
ATOM   3083  C   PHE A 396     122.674  44.819  48.760  1.00 91.31           C  
ANISOU 3083  C   PHE A 396    11377  10107  13208   1173   1814   2117       C  
ATOM   3084  O   PHE A 396     122.258  44.786  47.602  1.00 96.19           O  
ANISOU 3084  O   PHE A 396    12016  10786  13744   1202   1946   1962       O  
ATOM   3085  CB  PHE A 396     122.105  47.263  48.796  1.00 71.97           C  
ANISOU 3085  CB  PHE A 396     9055   7897  10392   1007   1798   2199       C  
ATOM   3086  CG  PHE A 396     121.978  48.528  49.595  1.00 72.11           C  
ANISOU 3086  CG  PHE A 396     9136   7989  10276    896   1708   2327       C  
ATOM   3087  CD1 PHE A 396     123.022  49.432  49.654  1.00 78.50           C  
ANISOU 3087  CD1 PHE A 396     9860   8886  11081    873   1699   2422       C  
ATOM   3088  CD2 PHE A 396     120.818  48.805  50.298  1.00 73.97           C  
ANISOU 3088  CD2 PHE A 396     9509   8202  10393    808   1637   2342       C  
ATOM   3089  CE1 PHE A 396     122.909  50.595  50.391  1.00 82.20           C  
ANISOU 3089  CE1 PHE A 396    10387   9416  11429    767   1620   2533       C  
ATOM   3090  CE2 PHE A 396     120.699  49.965  51.037  1.00 77.32           C  
ANISOU 3090  CE2 PHE A 396     9984   8687  10705    702   1566   2442       C  
ATOM   3091  CZ  PHE A 396     121.746  50.861  51.083  1.00 79.76           C  
ANISOU 3091  CZ  PHE A 396    10215   9081  11011    682   1555   2539       C  
ATOM   3092  N   GLU A 397     123.336  43.817  49.326  1.00 91.17           N  
ANISOU 3092  N   GLU A 397    11268   9948  13422   1235   1746   2173       N  
ATOM   3093  CA  GLU A 397     123.629  42.577  48.623  1.00 96.60           C  
ANISOU 3093  CA  GLU A 397    11866  10534  14305   1354   1831   2042       C  
ATOM   3094  C   GLU A 397     122.356  41.792  48.327  1.00 97.85           C  
ANISOU 3094  C   GLU A 397    12155  10624  14401   1357   1865   1918       C  
ATOM   3095  O   GLU A 397     122.289  41.056  47.344  1.00104.00           O  
ANISOU 3095  O   GLU A 397    12898  11374  15244   1435   1990   1752       O  
ATOM   3096  CB  GLU A 397     124.586  41.724  49.458  1.00109.88           C  
ANISOU 3096  CB  GLU A 397    13422  12058  16269   1413   1714   2156       C  
ATOM   3097  CG  GLU A 397     124.749  40.293  48.983  1.00120.34           C  
ANISOU 3097  CG  GLU A 397    14667  13227  17831   1534   1766   2033       C  
ATOM   3098  CD  GLU A 397     125.484  39.435  49.994  1.00127.63           C  
ANISOU 3098  CD  GLU A 397    15494  13966  19034   1575   1602   2175       C  
ATOM   3099  OE1 GLU A 397     125.707  39.911  51.128  1.00121.90           O  
ANISOU 3099  OE1 GLU A 397    14795  13237  18286   1489   1439   2374       O  
ATOM   3100  OE2 GLU A 397     125.836  38.285  49.656  1.00136.58           O1-
ANISOU 3100  OE2 GLU A 397    16527  14954  20413   1687   1631   2087       O1-
ATOM   3101  N   ASN A 398     121.348  41.956  49.178  1.00 94.48           N  
ANISOU 3101  N   ASN A 398    11877  10174  13845   1262   1759   1991       N  
ATOM   3102  CA  ASN A 398     120.107  41.199  49.043  1.00 91.76           C  
ANISOU 3102  CA  ASN A 398    11660   9761  13444   1252   1773   1887       C  
ATOM   3103  C   ASN A 398     118.907  42.060  48.658  1.00 93.82           C  
ANISOU 3103  C   ASN A 398    12059  10145  13441   1169   1820   1819       C  
ATOM   3104  O   ASN A 398     117.760  41.637  48.803  1.00 92.31           O  
ANISOU 3104  O   ASN A 398    11989   9911  13176   1130   1804   1763       O  
ATOM   3105  CB  ASN A 398     119.811  40.436  50.334  1.00 87.95           C  
ANISOU 3105  CB  ASN A 398    11238   9126  13053   1204   1613   2006       C  
ATOM   3106  CG  ASN A 398     120.994  39.622  50.809  1.00 92.13           C  
ANISOU 3106  CG  ASN A 398    11628   9517  13860   1278   1531   2100       C  
ATOM   3107  ND2 ASN A 398     121.007  39.292  52.094  1.00 97.64           N  
ANISOU 3107  ND2 ASN A 398    12368  10110  14621   1205   1356   2263       N  
ATOM   3108  OD1 ASN A 398     121.889  39.293  50.030  1.00 92.10           O  
ANISOU 3108  OD1 ASN A 398    11478   9499  14016   1392   1622   2025       O  
ATOM   3109  N   LEU A 399     119.178  43.266  48.170  1.00 94.26           N  
ANISOU 3109  N   LEU A 399    12095  10353  13367   1141   1872   1826       N  
ATOM   3110  CA  LEU A 399     118.121  44.159  47.712  1.00 88.82           C  
ANISOU 3110  CA  LEU A 399    11520   9777  12451   1070   1908   1765       C  
ATOM   3111  C   LEU A 399     117.525  43.612  46.419  1.00 89.17           C  
ANISOU 3111  C   LEU A 399    11593   9838  12450   1118   2037   1580       C  
ATOM   3112  O   LEU A 399     118.226  43.473  45.417  1.00 92.61           O  
ANISOU 3112  O   LEU A 399    11941  10319  12929   1178   2150   1496       O  
ATOM   3113  CB  LEU A 399     118.674  45.568  47.487  1.00 84.65           C  
ANISOU 3113  CB  LEU A 399    10956   9394  11814   1027   1920   1829       C  
ATOM   3114  CG  LEU A 399     117.703  46.741  47.648  1.00 84.13           C  
ANISOU 3114  CG  LEU A 399    11003   9415  11546    928   1881   1848       C  
ATOM   3115  CD1 LEU A 399     118.397  48.055  47.329  1.00 78.29           C  
ANISOU 3115  CD1 LEU A 399    10217   8807  10724    895   1895   1912       C  
ATOM   3116  CD2 LEU A 399     116.470  46.565  46.777  1.00 91.54           C  
ANISOU 3116  CD2 LEU A 399    12037  10374  12370    923   1944   1702       C  
ATOM   3117  N   GLU A 400     116.232  43.304  46.445  1.00 83.94           N  
ANISOU 3117  N   GLU A 400    11052   9144  11696   1079   2024   1512       N  
ATOM   3118  CA  GLU A 400     115.572  42.689  45.299  1.00 87.42           C  
ANISOU 3118  CA  GLU A 400    11533   9590  12091   1113   2133   1341       C  
ATOM   3119  C   GLU A 400     114.781  43.684  44.460  1.00 92.48           C  
ANISOU 3119  C   GLU A 400    12249  10367  12522   1051   2174   1280       C  
ATOM   3120  O   GLU A 400     114.825  43.637  43.232  1.00101.40           O  
ANISOU 3120  O   GLU A 400    13367  11565  13596   1068   2283   1166       O  
ATOM   3121  CB  GLU A 400     114.641  41.565  45.752  1.00 91.89           C  
ANISOU 3121  CB  GLU A 400    12182  10027  12704   1113   2095   1292       C  
ATOM   3122  CG  GLU A 400     115.340  40.390  46.404  1.00 98.65           C  
ANISOU 3122  CG  GLU A 400    12973  10727  13784   1177   2051   1335       C  
ATOM   3123  CD  GLU A 400     114.370  39.295  46.794  1.00105.04           C  
ANISOU 3123  CD  GLU A 400    13876  11410  14624   1164   2012   1286       C  
ATOM   3124  OE1 GLU A 400     113.184  39.392  46.415  1.00101.67           O  
ANISOU 3124  OE1 GLU A 400    13556  11027  14049   1116   2041   1196       O  
ATOM   3125  OE2 GLU A 400     114.790  38.338  47.478  1.00112.42           O1-
ANISOU 3125  OE2 GLU A 400    14778  12200  15735   1198   1945   1342       O1-
ATOM   3126  N   ILE A 401     114.048  44.574  45.120  1.00 88.53           N  
ANISOU 3126  N   ILE A 401    11826   9902  11911    971   2083   1353       N  
ATOM   3127  CA  ILE A 401     113.152  45.478  44.407  1.00 87.26           C  
ANISOU 3127  CA  ILE A 401    11737   9843  11573    913   2096   1300       C  
ATOM   3128  C   ILE A 401     113.224  46.924  44.889  1.00 83.89           C  
ANISOU 3128  C   ILE A 401    11316   9495  11062    845   2020   1412       C  
ATOM   3129  O   ILE A 401     113.316  47.192  46.086  1.00 84.71           O  
ANISOU 3129  O   ILE A 401    11422   9559  11205    810   1934   1515       O  
ATOM   3130  CB  ILE A 401     111.688  44.998  44.492  1.00 85.74           C  
ANISOU 3130  CB  ILE A 401    11653   9599  11325    880   2071   1215       C  
ATOM   3131  CG1 ILE A 401     111.549  43.603  43.881  1.00 99.66           C  
ANISOU 3131  CG1 ILE A 401    13420  11288  13156    940   2152   1092       C  
ATOM   3132  CG2 ILE A 401     110.759  45.978  43.792  1.00 74.07           C  
ANISOU 3132  CG2 ILE A 401    10239   8217   9688    821   2063   1172       C  
ATOM   3133  CD1 ILE A 401     110.133  43.071  43.888  1.00107.10           C  
ANISOU 3133  CD1 ILE A 401    14467  12185  14042    906   2135   1002       C  
ATOM   3134  N   ILE A 402     113.186  47.850  43.937  1.00 77.12           N  
ANISOU 3134  N   ILE A 402    10465   8749  10087    817   2051   1392       N  
ATOM   3135  CA  ILE A 402     113.057  49.267  44.239  1.00 69.69           C  
ANISOU 3135  CA  ILE A 402     9543   7877   9059    750   1977   1480       C  
ATOM   3136  C   ILE A 402     111.803  49.796  43.553  1.00 73.62           C  
ANISOU 3136  C   ILE A 402    10125   8414   9433    701   1957   1408       C  
ATOM   3137  O   ILE A 402     111.782  49.983  42.338  1.00 79.00           O  
ANISOU 3137  O   ILE A 402    10817   9169  10032    694   2008   1352       O  
ATOM   3138  CB  ILE A 402     114.278  50.065  43.759  1.00 71.09           C  
ANISOU 3138  CB  ILE A 402     9645   8151   9216    748   2008   1549       C  
ATOM   3139  CG1 ILE A 402     115.557  49.515  44.392  1.00 70.02           C  
ANISOU 3139  CG1 ILE A 402     9408   7974   9222    801   2025   1618       C  
ATOM   3140  CG2 ILE A 402     114.111  51.541  44.087  1.00 76.15           C  
ANISOU 3140  CG2 ILE A 402    10311   8851   9771    675   1925   1641       C  
ATOM   3141  CD1 ILE A 402     116.818  50.210  43.921  1.00 65.44           C  
ANISOU 3141  CD1 ILE A 402     8739   7491   8634    800   2066   1676       C  
ATOM   3142  N   ARG A 403     110.757  50.027  44.339  1.00 73.52           N  
ANISOU 3142  N   ARG A 403    10170   8352   9412    660   1881   1407       N  
ATOM   3143  CA  ARG A 403     109.461  50.437  43.805  1.00 77.53           C  
ANISOU 3143  CA  ARG A 403    10747   8876   9835    620   1848   1334       C  
ATOM   3144  C   ARG A 403     109.481  51.834  43.190  1.00 82.27           C  
ANISOU 3144  C   ARG A 403    11349   9563  10349    574   1803   1382       C  
ATOM   3145  O   ARG A 403     108.790  52.099  42.207  1.00 84.96           O  
ANISOU 3145  O   ARG A 403    11730   9940  10610    551   1794   1327       O  
ATOM   3146  CB  ARG A 403     108.399  50.366  44.903  1.00 74.66           C  
ANISOU 3146  CB  ARG A 403    10427   8437   9504    583   1784   1314       C  
ATOM   3147  CG  ARG A 403     108.141  48.962  45.407  1.00 68.52           C  
ANISOU 3147  CG  ARG A 403     9670   7571   8793    609   1816   1258       C  
ATOM   3148  CD  ARG A 403     107.058  48.273  44.598  1.00 71.25           C  
ANISOU 3148  CD  ARG A 403    10071   7902   9099    618   1847   1129       C  
ATOM   3149  NE  ARG A 403     107.203  46.821  44.629  1.00 78.71           N  
ANISOU 3149  NE  ARG A 403    11024   8775  10107    665   1905   1074       N  
ATOM   3150  CZ  ARG A 403     107.149  46.085  45.735  1.00 76.17           C  
ANISOU 3150  CZ  ARG A 403    10715   8365   9862    655   1880   1095       C  
ATOM   3151  NH1 ARG A 403     106.961  46.662  46.915  1.00 71.96           N1+
ANISOU 3151  NH1 ARG A 403    10189   7816   9338    591   1810   1162       N1+
ATOM   3152  NH2 ARG A 403     107.293  44.770  45.660  1.00 72.43           N  
ANISOU 3152  NH2 ARG A 403    10249   7817   9455    700   1925   1047       N  
ATOM   3153  N   GLY A 404     110.270  52.726  43.777  1.00 78.70           N  
ANISOU 3153  N   GLY A 404    10854   9136   9910    554   1766   1492       N  
ATOM   3154  CA  GLY A 404     110.353  54.090  43.295  1.00 74.22           C  
ANISOU 3154  CA  GLY A 404    10290   8640   9271    505   1713   1552       C  
ATOM   3155  C   GLY A 404     109.021  54.812  43.348  1.00 76.34           C  
ANISOU 3155  C   GLY A 404    10608   8879   9516    461   1625   1517       C  
ATOM   3156  O   GLY A 404     108.698  55.594  42.456  1.00 80.82           O  
ANISOU 3156  O   GLY A 404    11199   9493  10017    427   1580   1523       O  
ATOM   3157  N   ARG A 405     108.238  54.546  44.390  1.00 77.73           N  
ANISOU 3157  N   ARG A 405    10800   8978   9756    453   1596   1479       N  
ATOM   3158  CA  ARG A 405     106.992  55.273  44.601  1.00 79.67           C  
ANISOU 3158  CA  ARG A 405    11073   9188  10010    411   1517   1435       C  
ATOM   3159  C   ARG A 405     107.311  56.739  44.847  1.00 82.34           C  
ANISOU 3159  C   ARG A 405    11388   9549  10348    369   1446   1524       C  
ATOM   3160  O   ARG A 405     106.472  57.615  44.641  1.00 85.04           O  
ANISOU 3160  O   ARG A 405    11740   9873  10698    338   1368   1503       O  
ATOM   3161  CB  ARG A 405     106.205  54.691  45.775  1.00 80.57           C  
ANISOU 3161  CB  ARG A 405    11200   9223  10190    395   1518   1370       C  
ATOM   3162  CG  ARG A 405     105.747  53.262  45.556  1.00 86.08           C  
ANISOU 3162  CG  ARG A 405    11929   9886  10891    430   1577   1279       C  
ATOM   3163  CD  ARG A 405     104.603  52.898  46.485  1.00 89.72           C  
ANISOU 3163  CD  ARG A 405    12415  10278  11398    390   1560   1195       C  
ATOM   3164  NE  ARG A 405     104.162  51.520  46.286  1.00 94.86           N  
ANISOU 3164  NE  ARG A 405    13101  10891  12049    417   1612   1111       N  
ATOM   3165  CZ  ARG A 405     104.444  50.519  47.113  1.00 96.55           C  
ANISOU 3165  CZ  ARG A 405    13328  11056  12302    415   1646   1115       C  
ATOM   3166  NH1 ARG A 405     105.161  50.742  48.204  1.00100.53           N1+
ANISOU 3166  NH1 ARG A 405    13811  11546  12839    381   1630   1203       N1+
ATOM   3167  NH2 ARG A 405     104.002  49.297  46.853  1.00 94.79           N  
ANISOU 3167  NH2 ARG A 405    13141  10793  12083    439   1688   1037       N  
ATOM   3168  N   THR A 406     108.535  56.990  45.300  1.00 82.97           N  
ANISOU 3168  N   THR A 406    11432   9662  10431    367   1467   1622       N  
ATOM   3169  CA  THR A 406     109.072  58.341  45.381  1.00 84.12           C  
ANISOU 3169  CA  THR A 406    11557   9843  10562    326   1409   1718       C  
ATOM   3170  C   THR A 406     110.473  58.352  44.784  1.00 83.48           C  
ANISOU 3170  C   THR A 406    11445   9844  10430    342   1456   1805       C  
ATOM   3171  O   THR A 406     111.233  57.397  44.946  1.00 83.92           O  
ANISOU 3171  O   THR A 406    11472   9909  10506    382   1530   1811       O  
ATOM   3172  CB  THR A 406     109.128  58.864  46.828  1.00 82.86           C  
ANISOU 3172  CB  THR A 406    11380   9639  10464    282   1379   1754       C  
ATOM   3173  CG2 THR A 406     107.730  59.116  47.356  1.00 85.67           C  
ANISOU 3173  CG2 THR A 406    11756   9922  10873    249   1335   1655       C  
ATOM   3174  OG1 THR A 406     109.780  57.901  47.663  1.00 87.29           O  
ANISOU 3174  OG1 THR A 406    11926  10187  11055    294   1435   1776       O  
ATOM   3175  N   LYS A 407     110.803  59.432  44.086  1.00 81.17           N  
ANISOU 3175  N   LYS A 407    11153   9607  10080    306   1410   1870       N  
ATOM   3176  CA  LYS A 407     112.097  59.562  43.435  1.00 85.27           C  
ANISOU 3176  CA  LYS A 407    11641  10218  10539    303   1457   1945       C  
ATOM   3177  C   LYS A 407     112.721  60.883  43.859  1.00 90.99           C  
ANISOU 3177  C   LYS A 407    12347  10967  11258    250   1394   2058       C  
ATOM   3178  O   LYS A 407     112.004  61.826  44.189  1.00 99.52           O  
ANISOU 3178  O   LYS A 407    13451  12001  12362    213   1305   2067       O  
ATOM   3179  CB  LYS A 407     111.917  59.541  41.919  1.00 82.41           C  
ANISOU 3179  CB  LYS A 407    11313   9919  10078    286   1468   1912       C  
ATOM   3180  CG  LYS A 407     110.699  58.759  41.460  1.00 77.30           C  
ANISOU 3180  CG  LYS A 407    10713   9228   9430    307   1470   1796       C  
ATOM   3181  CD  LYS A 407     110.359  59.076  40.016  1.00 79.16           C  
ANISOU 3181  CD  LYS A 407    10997   9523   9556    257   1440   1784       C  
ATOM   3182  CE  LYS A 407     108.894  58.807  39.722  1.00 80.05           C  
ANISOU 3182  CE  LYS A 407    11160   9576   9681    258   1382   1696       C  
ATOM   3183  NZ  LYS A 407     108.481  57.451  40.170  1.00 85.81           N1+
ANISOU 3183  NZ  LYS A 407    11885  10253  10465    321   1463   1591       N1+
ATOM   3184  N   GLN A 408     114.048  60.962  43.861  1.00 86.81           N  
ANISOU 3184  N   GLN A 408    11768  10506  10708    247   1441   2139       N  
ATOM   3185  CA  GLN A 408     114.691  62.225  44.199  1.00 84.80           C  
ANISOU 3185  CA  GLN A 408    11499  10282  10438    190   1383   2249       C  
ATOM   3186  C   GLN A 408     114.568  63.194  43.033  1.00 84.31           C  
ANISOU 3186  C   GLN A 408    11477  10273  10285    133   1326   2282       C  
ATOM   3187  O   GLN A 408     114.675  62.795  41.873  1.00 87.78           O  
ANISOU 3187  O   GLN A 408    11931  10775  10646    129   1369   2251       O  
ATOM   3188  CB  GLN A 408     116.155  62.041  44.588  1.00 79.47           C  
ANISOU 3188  CB  GLN A 408    10754   9665   9776    197   1444   2330       C  
ATOM   3189  CG  GLN A 408     116.725  63.274  45.267  1.00 84.73           C  
ANISOU 3189  CG  GLN A 408    11407  10345  10442    135   1380   2441       C  
ATOM   3190  CD  GLN A 408     118.208  63.172  45.517  1.00108.53           C  
ANISOU 3190  CD  GLN A 408    14346  13429  13462    134   1432   2528       C  
ATOM   3191  NE2 GLN A 408     118.802  64.255  46.005  1.00115.07           N  
ANISOU 3191  NE2 GLN A 408    15162  14282  14276     73   1381   2630       N  
ATOM   3192  OE1 GLN A 408     118.819  62.133  45.274  1.00121.76           O  
ANISOU 3192  OE1 GLN A 408    15968  15130  15163    189   1516   2500       O  
ATOM   3193  N   HIS A 409     114.338  64.465  43.352  1.00 74.42           N  
ANISOU 3193  N   HIS A 409    10243   8992   9042     80   1225   2345       N  
ATOM   3194  CA  HIS A 409     114.013  65.468  42.345  1.00 68.82           C  
ANISOU 3194  CA  HIS A 409     9580   8303   8263     18   1134   2385       C  
ATOM   3195  C   HIS A 409     112.776  65.023  41.574  1.00 70.66           C  
ANISOU 3195  C   HIS A 409     9862   8497   8487     33   1101   2293       C  
ATOM   3196  O   HIS A 409     112.370  65.659  40.602  1.00 78.33           O  
ANISOU 3196  O   HIS A 409    10880   9482   9400    -20   1017   2319       O  
ATOM   3197  CB  HIS A 409     115.184  65.692  41.386  1.00 77.93           C  
ANISOU 3197  CB  HIS A 409    10729   9581   9302    -33   1175   2459       C  
ATOM   3198  CG  HIS A 409     116.511  65.811  42.067  1.00 82.02           C  
ANISOU 3198  CG  HIS A 409    11182  10152   9830    -35   1234   2535       C  
ATOM   3199  CD2 HIS A 409     117.688  65.176  41.843  1.00 79.96           C  
ANISOU 3199  CD2 HIS A 409    10863   9981   9537    -21   1345   2547       C  
ATOM   3200  ND1 HIS A 409     116.740  66.682  43.108  1.00 85.85           N  
ANISOU 3200  ND1 HIS A 409    11652  10596  10372    -59   1176   2608       N  
ATOM   3201  CE1 HIS A 409     117.996  66.573  43.505  1.00 85.53           C  
ANISOU 3201  CE1 HIS A 409    11551  10621  10327    -62   1240   2671       C  
ATOM   3202  NE2 HIS A 409     118.592  65.666  42.752  1.00 83.43           N  
ANISOU 3202  NE2 HIS A 409    11252  10432  10016    -35   1341   2635       N  
ATOM   3203  N   GLY A 410     112.187  63.919  42.017  1.00 69.44           N  
ANISOU 3203  N   GLY A 410     9699   8294   8391     99   1161   2191       N  
ATOM   3204  CA  GLY A 410     110.991  63.380  41.403  1.00 67.25           C  
ANISOU 3204  CA  GLY A 410     9461   7977   8113    116   1138   2095       C  
ATOM   3205  C   GLY A 410     111.271  62.552  40.167  1.00 68.59           C  
ANISOU 3205  C   GLY A 410     9654   8230   8176    113   1213   2059       C  
ATOM   3206  O   GLY A 410     110.347  62.182  39.446  1.00 76.52           O  
ANISOU 3206  O   GLY A 410    10702   9219   9154    108   1186   1992       O  
ATOM   3207  N   GLN A 411     112.541  62.248  39.923  1.00 73.38           N  
ANISOU 3207  N   GLN A 411    10228   8927   8726    109   1309   2097       N  
ATOM   3208  CA  GLN A 411     112.920  61.557  38.694  1.00 77.60           C  
ANISOU 3208  CA  GLN A 411    10779   9553   9154     87   1395   2053       C  
ATOM   3209  C   GLN A 411     113.693  60.258  38.907  1.00 75.16           C  
ANISOU 3209  C   GLN A 411    10411   9267   8879    157   1548   1988       C  
ATOM   3210  O   GLN A 411     113.423  59.258  38.243  1.00 75.89           O  
ANISOU 3210  O   GLN A 411    10520   9374   8943    176   1624   1889       O  
ATOM   3211  CB  GLN A 411     113.725  62.485  37.784  1.00 77.00           C  
ANISOU 3211  CB  GLN A 411    10719   9582   8955    -12   1372   2144       C  
ATOM   3212  CG  GLN A 411     114.218  61.812  36.517  1.00 82.00           C  
ANISOU 3212  CG  GLN A 411    11366  10326   9465    -58   1479   2089       C  
ATOM   3213  CD  GLN A 411     115.067  62.728  35.666  1.00 98.86           C  
ANISOU 3213  CD  GLN A 411    13520  12577  11468   -177   1464   2178       C  
ATOM   3214  NE2 GLN A 411     115.714  62.163  34.653  1.00106.05           N  
ANISOU 3214  NE2 GLN A 411    14427  13599  12267   -231   1585   2122       N  
ATOM   3215  OE1 GLN A 411     115.141  63.932  35.913  1.00106.72           O  
ANISOU 3215  OE1 GLN A 411    14531  13559  12459   -226   1349   2290       O  
ATOM   3216  N   PHE A 412     114.656  60.273  39.822  1.00 69.86           N  
ANISOU 3216  N   PHE A 412     9670   8595   8277    191   1586   2044       N  
ATOM   3217  CA  PHE A 412     115.552  59.134  39.989  1.00 66.95           C  
ANISOU 3217  CA  PHE A 412     9231   8245   7963    255   1716   1999       C  
ATOM   3218  C   PHE A 412     115.185  58.238  41.169  1.00 69.93           C  
ANISOU 3218  C   PHE A 412     9586   8515   8470    338   1725   1961       C  
ATOM   3219  O   PHE A 412     115.012  58.707  42.293  1.00 72.57           O  
ANISOU 3219  O   PHE A 412     9916   8790   8867    338   1654   2019       O  
ATOM   3220  CB  PHE A 412     116.996  59.615  40.118  1.00 64.44           C  
ANISOU 3220  CB  PHE A 412     8839   8004   7640    234   1755   2089       C  
ATOM   3221  CG  PHE A 412     117.417  60.552  39.026  1.00 74.43           C  
ANISOU 3221  CG  PHE A 412    10131   9381   8767    134   1744   2137       C  
ATOM   3222  CD1 PHE A 412     117.358  61.923  39.210  1.00 70.93           C  
ANISOU 3222  CD1 PHE A 412     9722   8945   8282     64   1627   2247       C  
ATOM   3223  CD2 PHE A 412     117.860  60.063  37.810  1.00 74.08           C  
ANISOU 3223  CD2 PHE A 412    10081   9433   8633     97   1849   2067       C  
ATOM   3224  CE1 PHE A 412     117.741  62.788  38.205  1.00 67.42           C  
ANISOU 3224  CE1 PHE A 412     9312   8599   7707    -42   1604   2301       C  
ATOM   3225  CE2 PHE A 412     118.244  60.924  36.802  1.00 74.65           C  
ANISOU 3225  CE2 PHE A 412    10188   9615   8561    -19   1836   2114       C  
ATOM   3226  CZ  PHE A 412     118.185  62.288  37.000  1.00 70.31           C  
ANISOU 3226  CZ  PHE A 412     9678   9069   7967    -89   1707   2238       C  
ATOM   3227  N   SER A 413     115.073  56.942  40.895  1.00 69.11           N  
ANISOU 3227  N   SER A 413     9471   8387   8402    396   1813   1860       N  
ATOM   3228  CA  SER A 413     114.763  55.952  41.919  1.00 70.33           C  
ANISOU 3228  CA  SER A 413     9610   8440   8674    465   1823   1823       C  
ATOM   3229  C   SER A 413     116.026  55.244  42.403  1.00 78.50           C  
ANISOU 3229  C   SER A 413    10549   9470   9808    520   1896   1852       C  
ATOM   3230  O   SER A 413     116.055  54.693  43.502  1.00 80.14           O  
ANISOU 3230  O   SER A 413    10734   9594  10120    558   1873   1875       O  
ATOM   3231  CB  SER A 413     113.765  54.929  41.381  1.00 74.57           C  
ANISOU 3231  CB  SER A 413    10197   8932   9204    494   1861   1694       C  
ATOM   3232  OG  SER A 413     114.195  54.407  40.136  1.00 74.70           O  
ANISOU 3232  OG  SER A 413    10202   9019   9160    494   1962   1621       O  
ATOM   3233  N   LEU A 414     117.062  55.252  41.571  1.00 81.27           N  
ANISOU 3233  N   LEU A 414    10841   9910  10130    516   1978   1850       N  
ATOM   3234  CA  LEU A 414     118.361  54.716  41.958  1.00 78.56           C  
ANISOU 3234  CA  LEU A 414    10386   9568   9897    568   2042   1882       C  
ATOM   3235  C   LEU A 414     119.468  55.671  41.534  1.00 76.56           C  
ANISOU 3235  C   LEU A 414    10076   9429   9584    515   2062   1957       C  
ATOM   3236  O   LEU A 414     119.610  55.984  40.354  1.00 74.34           O  
ANISOU 3236  O   LEU A 414     9809   9244   9191    463   2120   1913       O  
ATOM   3237  CB  LEU A 414     118.594  53.335  41.344  1.00 66.46           C  
ANISOU 3237  CB  LEU A 414     8806   8011   8434    638   2162   1756       C  
ATOM   3238  CG  LEU A 414     119.917  52.663  41.724  1.00 75.70           C  
ANISOU 3238  CG  LEU A 414     9842   9162   9759    706   2225   1775       C  
ATOM   3239  CD1 LEU A 414     120.049  52.542  43.235  1.00 77.55           C  
ANISOU 3239  CD1 LEU A 414    10053   9297  10117    736   2125   1886       C  
ATOM   3240  CD2 LEU A 414     120.047  51.299  41.063  1.00 79.17           C  
ANISOU 3240  CD2 LEU A 414    10235   9562  10284    776   2347   1630       C  
ATOM   3241  N   ALA A 415     120.246  56.134  42.505  1.00 81.40           N  
ANISOU 3241  N   ALA A 415    10629  10034  10264    515   2013   2074       N  
ATOM   3242  CA  ALA A 415     121.310  57.090  42.235  1.00 86.99           C  
ANISOU 3242  CA  ALA A 415    11283  10848  10921    459   2023   2158       C  
ATOM   3243  C   ALA A 415     122.595  56.719  42.962  1.00 92.88           C  
ANISOU 3243  C   ALA A 415    11900  11584  11806    506   2047   2222       C  
ATOM   3244  O   ALA A 415     122.735  56.955  44.162  1.00 93.77           O  
ANISOU 3244  O   ALA A 415    12001  11641  11986    507   1959   2325       O  
ATOM   3245  CB  ALA A 415     120.874  58.488  42.620  1.00 84.49           C  
ANISOU 3245  CB  ALA A 415    11041  10548  10513    378   1905   2260       C  
ATOM   3246  N   VAL A 416     123.528  56.133  42.222  1.00 92.78           N  
ANISOU 3246  N   VAL A 416    11786  11627  11841    539   2166   2156       N  
ATOM   3247  CA  VAL A 416     124.837  55.799  42.757  1.00 84.50           C  
ANISOU 3247  CA  VAL A 416    10592  10574  10940    586   2193   2210       C  
ATOM   3248  C   VAL A 416     125.872  56.690  42.088  1.00 76.88           C  
ANISOU 3248  C   VAL A 416     9564   9752   9896    516   2248   2245       C  
ATOM   3249  O   VAL A 416     126.363  56.377  41.006  1.00 80.17           O  
ANISOU 3249  O   VAL A 416     9924  10248  10290    509   2377   2139       O  
ATOM   3250  CB  VAL A 416     125.189  54.329  42.490  1.00 87.12           C  
ANISOU 3250  CB  VAL A 416    10827  10842  11433    688   2296   2092       C  
ATOM   3251  CG1 VAL A 416     126.449  53.944  43.241  1.00 89.31           C  
ANISOU 3251  CG1 VAL A 416    10948  11083  11903    747   2289   2164       C  
ATOM   3252  CG2 VAL A 416     124.033  53.430  42.891  1.00 89.81           C  
ANISOU 3252  CG2 VAL A 416    11251  11053  11818    741   2255   2036       C  
ATOM   3253  N   VAL A 417     126.195  57.808  42.729  1.00 72.17           N  
ANISOU 3253  N   VAL A 417     8980   9190   9251    452   2155   2386       N  
ATOM   3254  CA  VAL A 417     127.084  58.793  42.130  1.00 79.59           C  
ANISOU 3254  CA  VAL A 417     9880  10267  10094    367   2190   2432       C  
ATOM   3255  C   VAL A 417     128.241  59.177  43.043  1.00 84.74           C  
ANISOU 3255  C   VAL A 417    10422  10933  10842    365   2147   2561       C  
ATOM   3256  O   VAL A 417     128.137  59.092  44.265  1.00 82.41           O  
ANISOU 3256  O   VAL A 417    10128  10545  10637    394   2046   2653       O  
ATOM   3257  CB  VAL A 417     126.322  60.077  41.753  1.00 90.79           C  
ANISOU 3257  CB  VAL A 417    11439  11738  11317    258   2113   2483       C  
ATOM   3258  CG1 VAL A 417     125.220  59.765  40.754  1.00 98.60           C  
ANISOU 3258  CG1 VAL A 417    12534  12727  12204    245   2146   2364       C  
ATOM   3259  CG2 VAL A 417     125.751  60.738  42.996  1.00 67.52           C  
ANISOU 3259  CG2 VAL A 417     8563   8709   8384    245   1966   2599       C  
ATOM   3260  N   SER A 418     129.343  59.599  42.428  1.00 96.19           N  
ANISOU 3260  N   SER A 418    11780  12504  12264    318   2224   2567       N  
ATOM   3261  CA  SER A 418     130.496  60.130  43.150  1.00 97.38           C  
ANISOU 3261  CA  SER A 418    11826  12692  12482    297   2184   2693       C  
ATOM   3262  C   SER A 418     131.105  59.125  44.123  1.00 90.32           C  
ANISOU 3262  C   SER A 418    10800  11696  11820    402   2163   2722       C  
ATOM   3263  O   SER A 418     131.696  59.509  45.132  1.00 85.26           O  
ANISOU 3263  O   SER A 418    10111  11038  11244    387   2072   2859       O  
ATOM   3264  CB  SER A 418     130.114  61.414  43.894  1.00104.34           C  
ANISOU 3264  CB  SER A 418    12817  13574  13254    210   2044   2839       C  
ATOM   3265  OG  SER A 418     129.480  62.341  43.028  1.00108.75           O  
ANISOU 3265  OG  SER A 418    13499  14203  13617    116   2039   2822       O  
ATOM   3266  N   LEU A 419     130.965  57.839  43.818  1.00 88.95           N  
ANISOU 3266  N   LEU A 419    10570  11451  11774    502   2240   2598       N  
ATOM   3267  CA  LEU A 419     131.513  56.799  44.681  1.00 94.41           C  
ANISOU 3267  CA  LEU A 419    11136  12028  12706    605   2209   2625       C  
ATOM   3268  C   LEU A 419     132.911  56.376  44.249  1.00105.72           C  
ANISOU 3268  C   LEU A 419    12361  13513  14295    649   2316   2578       C  
ATOM   3269  O   LEU A 419     133.472  56.918  43.296  1.00109.15           O  
ANISOU 3269  O   LEU A 419    12753  14086  14634    588   2425   2520       O  
ATOM   3270  CB  LEU A 419     130.587  55.583  44.729  1.00 94.04           C  
ANISOU 3270  CB  LEU A 419    11138  11848  12743    694   2215   2526       C  
ATOM   3271  CG  LEU A 419     129.246  55.778  45.437  1.00 88.20           C  
ANISOU 3271  CG  LEU A 419    10576  11027  11908    666   2097   2576       C  
ATOM   3272  CD1 LEU A 419     128.658  54.431  45.818  1.00 90.97           C  
ANISOU 3272  CD1 LEU A 419    10934  11230  12401    760   2082   2513       C  
ATOM   3273  CD2 LEU A 419     129.414  56.649  46.669  1.00 79.75           C  
ANISOU 3273  CD2 LEU A 419     9538   9948  10815    598   1953   2756       C  
ATOM   3274  N   ASN A 420     133.465  55.400  44.962  1.00113.28           N  
ANISOU 3274  N   ASN A 420    13188  14356  15498    748   2280   2601       N  
ATOM   3275  CA  ASN A 420     134.811  54.914  44.694  1.00123.77           C  
ANISOU 3275  CA  ASN A 420    14293  15708  17027    807   2366   2557       C  
ATOM   3276  C   ASN A 420     134.839  53.405  44.487  1.00114.15           C  
ANISOU 3276  C   ASN A 420    12969  14361  16042    940   2434   2421       C  
ATOM   3277  O   ASN A 420     135.900  52.815  44.290  1.00112.56           O  
ANISOU 3277  O   ASN A 420    12564  14147  16057   1010   2506   2363       O  
ATOM   3278  CB  ASN A 420     135.750  55.297  45.838  1.00148.16           C  
ANISOU 3278  CB  ASN A 420    17280  18779  20233    794   2235   2745       C  
ATOM   3279  CG  ASN A 420     137.183  54.887  45.576  1.00180.45           C  
ANISOU 3279  CG  ASN A 420    21123  22897  24544    851   2316   2706       C  
ATOM   3280  ND2 ASN A 420     137.801  54.231  46.553  1.00206.75           N  
ANISOU 3280  ND2 ASN A 420    24324  26105  28126    926   2205   2805       N  
ATOM   3281  OD1 ASN A 420     137.730  55.153  44.505  1.00184.47           O  
ANISOU 3281  OD1 ASN A 420    21553  23536  25001    821   2474   2586       O  
ATOM   3282  N   ILE A 421     133.666  52.783  44.535  1.00111.89           N  
ANISOU 3282  N   ILE A 421    12817  13974  15722    975   2408   2367       N  
ATOM   3283  CA  ILE A 421     133.557  51.338  44.369  1.00108.17           C  
ANISOU 3283  CA  ILE A 421    12270  13365  15464   1098   2462   2240       C  
ATOM   3284  C   ILE A 421     134.041  50.900  42.991  1.00105.68           C  
ANISOU 3284  C   ILE A 421    11842  13126  15187   1126   2679   2021       C  
ATOM   3285  O   ILE A 421     134.087  51.701  42.057  1.00104.24           O  
ANISOU 3285  O   ILE A 421    11699  13106  14800   1031   2787   1957       O  
ATOM   3286  CB  ILE A 421     132.108  50.863  44.562  1.00106.05           C  
ANISOU 3286  CB  ILE A 421    12189  12997  15108   1109   2407   2212       C  
ATOM   3287  CG1 ILE A 421     131.180  51.587  43.584  1.00 97.05           C  
ANISOU 3287  CG1 ILE A 421    11214  11981  13681   1018   2488   2124       C  
ATOM   3288  CG2 ILE A 421     131.660  51.099  45.994  1.00111.43           C  
ANISOU 3288  CG2 ILE A 421    12966  13588  15785   1080   2203   2406       C  
ATOM   3289  CD1 ILE A 421     129.735  51.158  43.678  1.00 91.80           C  
ANISOU 3289  CD1 ILE A 421    10724  11230  12928   1024   2443   2082       C  
ATOM   3290  N   THR A 422     134.402  49.626  42.871  1.00104.02           N  
ANISOU 3290  N   THR A 422    11490  12794  15239   1247   2740   1906       N  
ATOM   3291  CA  THR A 422     134.845  49.076  41.595  1.00101.67           C  
ANISOU 3291  CA  THR A 422    11074  12552  15002   1275   2961   1671       C  
ATOM   3292  C   THR A 422     133.753  48.218  40.971  1.00 96.81           C  
ANISOU 3292  C   THR A 422    10575  11869  14340   1307   3038   1509       C  
ATOM   3293  O   THR A 422     133.815  47.874  39.791  1.00 90.51           O  
ANISOU 3293  O   THR A 422     9740  11138  13511   1294   3230   1300       O  
ATOM   3294  CB  THR A 422     136.121  48.228  41.749  1.00101.96           C  
ANISOU 3294  CB  THR A 422    10840  12502  15398   1391   3006   1617       C  
ATOM   3295  CG2 THR A 422     137.165  48.977  42.564  1.00101.18           C  
ANISOU 3295  CG2 THR A 422    10623  12444  15374   1368   2894   1805       C  
ATOM   3296  OG1 THR A 422     135.803  46.992  42.400  1.00102.65           O  
ANISOU 3296  OG1 THR A 422    10901  12371  15731   1517   2917   1619       O  
ATOM   3297  N   SER A 423     132.752  47.877  41.776  1.00100.14           N  
ANISOU 3297  N   SER A 423    11139  12160  14750   1336   2890   1601       N  
ATOM   3298  CA  SER A 423     131.633  47.066  41.315  1.00102.82           C  
ANISOU 3298  CA  SER A 423    11601  12424  15042   1364   2938   1468       C  
ATOM   3299  C   SER A 423     130.370  47.402  42.100  1.00102.91           C  
ANISOU 3299  C   SER A 423    11827  12386  14888   1319   2772   1603       C  
ATOM   3300  O   SER A 423     130.429  47.664  43.301  1.00107.50           O  
ANISOU 3300  O   SER A 423    12424  12901  15519   1319   2601   1790       O  
ATOM   3301  CB  SER A 423     131.961  45.579  41.456  1.00102.15           C  
ANISOU 3301  CB  SER A 423    11376  12155  15282   1506   2968   1365       C  
ATOM   3302  OG  SER A 423     130.878  44.777  41.020  1.00106.38           O  
ANISOU 3302  OG  SER A 423    12033  12616  15771   1529   3015   1235       O  
ATOM   3303  N   LEU A 424     129.229  47.401  41.419  1.00 98.44           N  
ANISOU 3303  N   LEU A 424    11424  11855  14124   1272   2825   1504       N  
ATOM   3304  CA  LEU A 424     127.957  47.688  42.073  1.00 97.90           C  
ANISOU 3304  CA  LEU A 424    11552  11741  13905   1229   2685   1604       C  
ATOM   3305  C   LEU A 424     127.644  46.644  43.138  1.00 93.98           C  
ANISOU 3305  C   LEU A 424    11055  11047  13606   1316   2565   1661       C  
ATOM   3306  O   LEU A 424     127.578  46.959  44.326  1.00 89.98           O  
ANISOU 3306  O   LEU A 424    10585  10486  13119   1296   2403   1837       O  
ATOM   3307  CB  LEU A 424     126.825  47.759  41.049  1.00 99.11           C  
ANISOU 3307  CB  LEU A 424    11857  11960  13839   1170   2770   1470       C  
ATOM   3308  CG  LEU A 424     126.814  49.009  40.169  1.00 96.34           C  
ANISOU 3308  CG  LEU A 424    11570  11801  13235   1047   2827   1465       C  
ATOM   3309  CD1 LEU A 424     125.795  48.865  39.051  1.00100.88           C  
ANISOU 3309  CD1 LEU A 424    12274  12429  13628    992   2916   1318       C  
ATOM   3310  CD2 LEU A 424     126.535  50.252  41.004  1.00 86.85           C  
ANISOU 3310  CD2 LEU A 424    10460  10639  11900    973   2670   1659       C  
ATOM   3311  N   GLY A 425     127.449  45.403  42.703  1.00 93.79           N  
ANISOU 3311  N   GLY A 425    10995  10916  13722   1399   2646   1511       N  
ATOM   3312  CA  GLY A 425     127.236  44.297  43.619  1.00 93.03           C  
ANISOU 3312  CA  GLY A 425    10889  10622  13836   1482   2537   1556       C  
ATOM   3313  C   GLY A 425     125.793  44.071  44.028  1.00 89.54           C  
ANISOU 3313  C   GLY A 425    10643  10114  13263   1446   2451   1574       C  
ATOM   3314  O   GLY A 425     125.524  43.361  44.996  1.00 88.92           O  
ANISOU 3314  O   GLY A 425    10588   9883  13313   1479   2326   1655       O  
ATOM   3315  N   LEU A 426     124.862  44.674  43.295  1.00 88.95           N  
ANISOU 3315  N   LEU A 426    10708  10153  12935   1369   2512   1501       N  
ATOM   3316  CA  LEU A 426     123.440  44.480  43.556  1.00 86.31           C  
ANISOU 3316  CA  LEU A 426    10551   9768  12474   1333   2447   1494       C  
ATOM   3317  C   LEU A 426     122.957  43.217  42.858  1.00 91.48           C  
ANISOU 3317  C   LEU A 426    11216  10333  13208   1397   2548   1313       C  
ATOM   3318  O   LEU A 426     122.017  43.252  42.066  1.00 91.49           O  
ANISOU 3318  O   LEU A 426    11330  10391  13041   1354   2617   1201       O  
ATOM   3319  CB  LEU A 426     122.637  45.685  43.068  1.00 73.32           C  
ANISOU 3319  CB  LEU A 426     9041   8273  10546   1225   2454   1498       C  
ATOM   3320  CG  LEU A 426     123.124  47.057  43.533  1.00 78.65           C  
ANISOU 3320  CG  LEU A 426     9707   9054  11121   1153   2380   1652       C  
ATOM   3321  CD1 LEU A 426     122.296  48.165  42.900  1.00 71.29           C  
ANISOU 3321  CD1 LEU A 426     8904   8252   9931   1054   2390   1637       C  
ATOM   3322  CD2 LEU A 426     123.091  47.157  45.049  1.00 76.55           C  
ANISOU 3322  CD2 LEU A 426     9462   8697  10927   1140   2211   1825       C  
ATOM   3323  N   ARG A 427     123.608  42.099  43.165  1.00 97.65           N  
ANISOU 3323  N   ARG A 427    11878  10968  14255   1498   2547   1289       N  
ATOM   3324  CA  ARG A 427     123.355  40.834  42.482  1.00 98.20           C  
ANISOU 3324  CA  ARG A 427    11929  10940  14443   1570   2655   1106       C  
ATOM   3325  C   ARG A 427     121.969  40.258  42.760  1.00103.27           C  
ANISOU 3325  C   ARG A 427    12740  11495  15005   1548   2593   1084       C  
ATOM   3326  O   ARG A 427     121.634  39.178  42.274  1.00111.28           O  
ANISOU 3326  O   ARG A 427    13759  12416  16108   1601   2668    940       O  
ATOM   3327  CB  ARG A 427     124.417  39.808  42.874  1.00 93.30           C  
ANISOU 3327  CB  ARG A 427    11129  10160  14162   1688   2643   1104       C  
ATOM   3328  CG  ARG A 427     124.342  39.380  44.327  1.00 91.11           C  
ANISOU 3328  CG  ARG A 427    10870   9718  14028   1707   2435   1289       C  
ATOM   3329  CD  ARG A 427     125.449  38.400  44.664  1.00 99.09           C  
ANISOU 3329  CD  ARG A 427    11691  10564  15394   1824   2407   1297       C  
ATOM   3330  NE  ARG A 427     126.767  38.992  44.467  1.00102.04           N  
ANISOU 3330  NE  ARG A 427    11884  11021  15864   1849   2456   1322       N  
ATOM   3331  CZ  ARG A 427     127.425  39.673  45.399  1.00102.97           C  
ANISOU 3331  CZ  ARG A 427    11952  11159  16014   1819   2317   1523       C  
ATOM   3332  NH1 ARG A 427     126.888  39.847  46.599  1.00101.62           N1+
ANISOU 3332  NH1 ARG A 427    11900  10930  15781   1756   2125   1713       N1+
ATOM   3333  NH2 ARG A 427     128.621  40.179  45.133  1.00104.42           N  
ANISOU 3333  NH2 ARG A 427    11965  11424  16286   1842   2375   1530       N  
ATOM   3334  N   SER A 428     121.168  40.972  43.542  1.00 95.66           N  
ANISOU 3334  N   SER A 428    11909  10561  13878   1467   2461   1219       N  
ATOM   3335  CA  SER A 428     119.830  40.502  43.874  1.00 90.88           C  
ANISOU 3335  CA  SER A 428    11458   9882  13189   1434   2400   1200       C  
ATOM   3336  C   SER A 428     118.763  41.420  43.295  1.00 96.97           C  
ANISOU 3336  C   SER A 428    12369  10796  13681   1339   2428   1159       C  
ATOM   3337  O   SER A 428     117.576  41.096  43.318  1.00104.30           O  
ANISOU 3337  O   SER A 428    13422  11690  14518   1307   2405   1111       O  
ATOM   3338  CB  SER A 428     119.665  40.381  45.388  1.00 87.58           C  
ANISOU 3338  CB  SER A 428    11081   9354  12842   1409   2214   1378       C  
ATOM   3339  OG  SER A 428     120.572  39.431  45.917  1.00 89.03           O  
ANISOU 3339  OG  SER A 428    11143   9385  13298   1493   2165   1424       O  
ATOM   3340  N   LEU A 429     119.193  42.563  42.772  1.00 95.12           N  
ANISOU 3340  N   LEU A 429    12107  10716  13317   1293   2472   1181       N  
ATOM   3341  CA  LEU A 429     118.278  43.528  42.175  1.00 89.89           C  
ANISOU 3341  CA  LEU A 429    11564  10184  12405   1201   2484   1156       C  
ATOM   3342  C   LEU A 429     117.592  42.928  40.952  1.00 84.68           C  
ANISOU 3342  C   LEU A 429    10961   9547  11665   1198   2606    971       C  
ATOM   3343  O   LEU A 429     118.228  42.699  39.923  1.00 83.42           O  
ANISOU 3343  O   LEU A 429    10729   9445  11523   1215   2745    854       O  
ATOM   3344  CB  LEU A 429     119.027  44.804  41.789  1.00 90.81           C  
ANISOU 3344  CB  LEU A 429    11630  10453  12420   1151   2507   1218       C  
ATOM   3345  CG  LEU A 429     118.180  46.059  41.581  1.00 84.28           C  
ANISOU 3345  CG  LEU A 429    10921   9740  11362   1050   2454   1263       C  
ATOM   3346  CD1 LEU A 429     117.435  46.408  42.859  1.00 78.12           C  
ANISOU 3346  CD1 LEU A 429    10220   8895  10567   1017   2302   1385       C  
ATOM   3347  CD2 LEU A 429     119.049  47.223  41.127  1.00 79.65           C  
ANISOU 3347  CD2 LEU A 429    10278   9295  10692   1000   2482   1321       C  
ATOM   3348  N   LYS A 430     116.293  42.676  41.069  1.00 84.01           N  
ANISOU 3348  N   LYS A 430    11006   9423  11492   1165   2558    938       N  
ATOM   3349  CA  LYS A 430     115.541  42.037  39.997  1.00 90.99           C  
ANISOU 3349  CA  LYS A 430    11954  10318  12299   1154   2658    769       C  
ATOM   3350  C   LYS A 430     114.429  42.928  39.460  1.00 92.38           C  
ANISOU 3350  C   LYS A 430    12254  10603  12241   1057   2628    759       C  
ATOM   3351  O   LYS A 430     113.728  42.550  38.522  1.00 98.11           O  
ANISOU 3351  O   LYS A 430    13047  11357  12873   1026   2697    632       O  
ATOM   3352  CB  LYS A 430     114.946  40.712  40.476  1.00105.70           C  
ANISOU 3352  CB  LYS A 430    13856  12020  14287   1207   2637    713       C  
ATOM   3353  CG  LYS A 430     115.977  39.646  40.810  1.00128.57           C  
ANISOU 3353  CG  LYS A 430    16628  14785  17439   1310   2670    695       C  
ATOM   3354  CD  LYS A 430     116.767  39.227  39.577  1.00142.01           C  
ANISOU 3354  CD  LYS A 430    18232  16531  19193   1348   2848    535       C  
ATOM   3355  CE  LYS A 430     117.746  38.108  39.903  1.00145.17           C  
ANISOU 3355  CE  LYS A 430    18496  16779  19885   1461   2879    502       C  
ATOM   3356  NZ  LYS A 430     118.590  37.741  38.732  1.00146.83           N1+
ANISOU 3356  NZ  LYS A 430    18591  17034  20164   1495   3068    329       N1+
ATOM   3357  N   GLU A 431     114.262  44.106  40.051  1.00 88.68           N  
ANISOU 3357  N   GLU A 431    11816  10191  11689   1004   2520    894       N  
ATOM   3358  CA  GLU A 431     113.184  44.995  39.634  1.00 88.30           C  
ANISOU 3358  CA  GLU A 431    11874  10226  11450    918   2468    896       C  
ATOM   3359  C   GLU A 431     113.321  46.425  40.143  1.00 82.84           C  
ANISOU 3359  C   GLU A 431    11184   9605  10687    864   2368   1039       C  
ATOM   3360  O   GLU A 431     113.529  46.660  41.333  1.00 80.18           O  
ANISOU 3360  O   GLU A 431    10825   9213  10428    878   2283   1150       O  
ATOM   3361  CB  GLU A 431     111.831  44.427  40.068  1.00 95.88           C  
ANISOU 3361  CB  GLU A 431    12932  11099  12399    910   2407    855       C  
ATOM   3362  CG  GLU A 431     110.662  45.360  39.801  1.00101.34           C  
ANISOU 3362  CG  GLU A 431    13718  11857  12930    828   2332    864       C  
ATOM   3363  CD  GLU A 431     109.333  44.757  40.201  1.00100.48           C  
ANISOU 3363  CD  GLU A 431    13693  11666  12818    818   2283    808       C  
ATOM   3364  OE1 GLU A 431     109.317  43.583  40.631  1.00 96.46           O  
ANISOU 3364  OE1 GLU A 431    13181  11053  12418    868   2310    762       O  
ATOM   3365  OE2 GLU A 431     108.305  45.457  40.081  1.00 97.97           O1-
ANISOU 3365  OE2 GLU A 431    13441  11386  12399    758   2213    810       O1-
ATOM   3366  N   ILE A 432     113.200  47.375  39.220  1.00 78.06           N  
ANISOU 3366  N   ILE A 432    10610   9120   9929    793   2377   1037       N  
ATOM   3367  CA  ILE A 432     113.094  48.788  39.558  1.00 72.11           C  
ANISOU 3367  CA  ILE A 432     9877   8427   9093    732   2274   1158       C  
ATOM   3368  C   ILE A 432     111.793  49.319  38.963  1.00 74.15           C  
ANISOU 3368  C   ILE A 432    10239   8720   9213    662   2214   1123       C  
ATOM   3369  O   ILE A 432     111.768  49.836  37.846  1.00 74.26           O  
ANISOU 3369  O   ILE A 432    10283   8832   9102    597   2236   1100       O  
ATOM   3370  CB  ILE A 432     114.288  49.596  39.027  1.00 76.30           C  
ANISOU 3370  CB  ILE A 432    10341   9070   9581    702   2317   1215       C  
ATOM   3371  CG1 ILE A 432     115.595  49.047  39.600  1.00 67.58           C  
ANISOU 3371  CG1 ILE A 432     9117   7928   8633    776   2373   1246       C  
ATOM   3372  CG2 ILE A 432     114.131  51.062  39.383  1.00 65.94           C  
ANISOU 3372  CG2 ILE A 432     9058   7809   8188    637   2202   1341       C  
ATOM   3373  CD1 ILE A 432     116.825  49.782  39.125  1.00 93.91           C  
ANISOU 3373  CD1 ILE A 432    12370  11373  11937    746   2424   1294       C  
ATOM   3374  N   SER A 433     110.715  49.179  39.727  1.00 72.32           N  
ANISOU 3374  N   SER A 433    10061   8406   9011    666   2133   1121       N  
ATOM   3375  CA  SER A 433     109.359  49.426  39.244  1.00 73.60           C  
ANISOU 3375  CA  SER A 433    10310   8575   9081    615   2075   1068       C  
ATOM   3376  C   SER A 433     109.157  50.755  38.516  1.00 71.25           C  
ANISOU 3376  C   SER A 433    10041   8370   8660    536   2007   1123       C  
ATOM   3377  O   SER A 433     108.415  50.819  37.537  1.00 71.05           O  
ANISOU 3377  O   SER A 433    10076   8384   8536    484   1994   1067       O  
ATOM   3378  CB  SER A 433     108.361  49.301  40.397  1.00 83.88           C  
ANISOU 3378  CB  SER A 433    11643   9780  10447    623   1993   1073       C  
ATOM   3379  OG  SER A 433     108.436  48.017  40.993  1.00 90.67           O  
ANISOU 3379  OG  SER A 433    12493  10550  11408    680   2043   1024       O  
ATOM   3380  N   ASP A 434     109.804  51.812  38.993  1.00 74.26           N  
ANISOU 3380  N   ASP A 434    10385   8782   9049    519   1953   1239       N  
ATOM   3381  CA  ASP A 434     109.639  53.131  38.390  1.00 73.88           C  
ANISOU 3381  CA  ASP A 434    10366   8807   8900    442   1871   1307       C  
ATOM   3382  C   ASP A 434     110.813  54.039  38.731  1.00 72.01           C  
ANISOU 3382  C   ASP A 434    10071   8621   8669    429   1861   1424       C  
ATOM   3383  O   ASP A 434     111.553  53.779  39.675  1.00 72.19           O  
ANISOU 3383  O   ASP A 434    10033   8607   8788    480   1889   1465       O  
ATOM   3384  CB  ASP A 434     108.328  53.769  38.857  1.00 80.71           C  
ANISOU 3384  CB  ASP A 434    11276   9612   9780    418   1742   1316       C  
ATOM   3385  CG  ASP A 434     107.889  54.925  37.975  1.00 93.19           C  
ANISOU 3385  CG  ASP A 434    12897  11248  11262    337   1643   1363       C  
ATOM   3386  OD1 ASP A 434     106.976  55.674  38.384  1.00 93.60           O  
ANISOU 3386  OD1 ASP A 434    12965  11249  11352    319   1527   1386       O  
ATOM   3387  OD2 ASP A 434     108.453  55.083  36.872  1.00101.50           O1-
ANISOU 3387  OD2 ASP A 434    13966  12394  12207    284   1679   1375       O1-
ATOM   3388  N   GLY A 435     110.980  55.103  37.952  1.00 75.65           N  
ANISOU 3388  N   GLY A 435    10554   9163   9025    352   1812   1484       N  
ATOM   3389  CA  GLY A 435     112.045  56.061  38.179  1.00 76.23           C  
ANISOU 3389  CA  GLY A 435    10582   9293   9089    325   1795   1598       C  
ATOM   3390  C   GLY A 435     113.286  55.759  37.365  1.00 76.57           C  
ANISOU 3390  C   GLY A 435    10580   9438   9076    307   1917   1584       C  
ATOM   3391  O   GLY A 435     113.591  54.599  37.097  1.00 85.48           O  
ANISOU 3391  O   GLY A 435    11678  10562  10237    353   2036   1487       O  
ATOM   3392  N   ASP A 436     114.005  56.806  36.971  1.00 71.70           N  
ANISOU 3392  N   ASP A 436     9954   8908   8380    234   1892   1674       N  
ATOM   3393  CA  ASP A 436     115.237  56.642  36.208  1.00 74.53           C  
ANISOU 3393  CA  ASP A 436    10261   9376   8680    200   2013   1658       C  
ATOM   3394  C   ASP A 436     116.393  56.187  37.092  1.00 81.58           C  
ANISOU 3394  C   ASP A 436    11042  10249   9707    283   2090   1680       C  
ATOM   3395  O   ASP A 436     116.351  56.327  38.315  1.00 80.43           O  
ANISOU 3395  O   ASP A 436    10869  10021   9669    339   2024   1747       O  
ATOM   3396  CB  ASP A 436     115.609  57.941  35.492  1.00 75.88           C  
ANISOU 3396  CB  ASP A 436    10466   9651   8713     78   1953   1753       C  
ATOM   3397  CG  ASP A 436     114.610  58.320  34.421  1.00 89.97           C  
ANISOU 3397  CG  ASP A 436    12359  11467  10360    -22   1876   1737       C  
ATOM   3398  OD1 ASP A 436     114.748  59.415  33.834  1.00 92.48           O  
ANISOU 3398  OD1 ASP A 436    12722  11854  10564   -133   1796   1827       O  
ATOM   3399  OD2 ASP A 436     113.684  57.521  34.167  1.00 97.02           O1-
ANISOU 3399  OD2 ASP A 436    13294  12311  11257      4   1887   1641       O1-
ATOM   3400  N   VAL A 437     117.424  55.639  36.461  1.00 87.33           N  
ANISOU 3400  N   VAL A 437    11700  11051  10430    282   2229   1619       N  
ATOM   3401  CA  VAL A 437     118.602  55.175  37.177  1.00 68.62           C  
ANISOU 3401  CA  VAL A 437     9207   8663   8202    360   2301   1636       C  
ATOM   3402  C   VAL A 437     119.824  55.962  36.735  1.00 75.30           C  
ANISOU 3402  C   VAL A 437     9992   9633   8986    290   2347   1695       C  
ATOM   3403  O   VAL A 437     120.200  55.931  35.565  1.00 78.21           O  
ANISOU 3403  O   VAL A 437    10361  10110   9246    213   2445   1623       O  
ATOM   3404  CB  VAL A 437     118.867  53.685  36.915  1.00 80.18           C  
ANISOU 3404  CB  VAL A 437    10609  10088   9769    440   2441   1493       C  
ATOM   3405  CG1 VAL A 437     120.158  53.255  37.589  1.00 70.11           C  
ANISOU 3405  CG1 VAL A 437     9190   8789   8659    519   2502   1518       C  
ATOM   3406  CG2 VAL A 437     117.697  52.840  37.394  1.00 68.75           C  
ANISOU 3406  CG2 VAL A 437     9222   8515   8386    506   2398   1435       C  
ATOM   3407  N   ILE A 438     120.443  56.670  37.672  1.00 73.61           N  
ANISOU 3407  N   ILE A 438     9727   9409   8833    302   2278   1823       N  
ATOM   3408  CA  ILE A 438     121.662  57.406  37.371  1.00 75.32           C  
ANISOU 3408  CA  ILE A 438     9875   9739   9003    238   2319   1886       C  
ATOM   3409  C   ILE A 438     122.854  56.833  38.131  1.00 83.01           C  
ANISOU 3409  C   ILE A 438    10701  10688  10151    326   2384   1901       C  
ATOM   3410  O   ILE A 438     122.842  56.749  39.360  1.00 82.21           O  
ANISOU 3410  O   ILE A 438    10573  10490  10173    394   2304   1979       O  
ATOM   3411  CB  ILE A 438     121.517  58.905  37.685  1.00 73.32           C  
ANISOU 3411  CB  ILE A 438     9685   9514   8658    155   2179   2035       C  
ATOM   3412  CG1 ILE A 438     122.857  59.617  37.492  1.00 69.73           C  
ANISOU 3412  CG1 ILE A 438     9152   9174   8167     90   2222   2106       C  
ATOM   3413  CG2 ILE A 438     120.994  59.106  39.098  1.00 72.74           C  
ANISOU 3413  CG2 ILE A 438     9626   9319   8694    219   2058   2119       C  
ATOM   3414  CD1 ILE A 438     122.811  61.097  37.790  1.00 72.45           C  
ANISOU 3414  CD1 ILE A 438     9556   9544   8428      5   2088   2253       C  
ATOM   3415  N   ILE A 439     123.875  56.427  37.385  1.00 84.11           N  
ANISOU 3415  N   ILE A 439    10741  10914  10302    314   2528   1820       N  
ATOM   3416  CA  ILE A 439     125.095  55.885  37.966  1.00 81.37           C  
ANISOU 3416  CA  ILE A 439    10233  10547  10137    396   2594   1826       C  
ATOM   3417  C   ILE A 439     126.296  56.518  37.283  1.00 90.00           C  
ANISOU 3417  C   ILE A 439    11243  11791  11164    310   2682   1833       C  
ATOM   3418  O   ILE A 439     126.718  56.072  36.217  1.00 95.54           O  
ANISOU 3418  O   ILE A 439    11897  12575  11826    273   2833   1697       O  
ATOM   3419  CB  ILE A 439     125.171  54.360  37.790  1.00 75.95           C  
ANISOU 3419  CB  ILE A 439     9468   9784   9606    501   2711   1673       C  
ATOM   3420  CG1 ILE A 439     123.910  53.695  38.345  1.00 74.36           C  
ANISOU 3420  CG1 ILE A 439     9362   9443   9448    569   2631   1655       C  
ATOM   3421  CG2 ILE A 439     126.413  53.807  38.469  1.00 74.28           C  
ANISOU 3421  CG2 ILE A 439     9077   9529   9615    594   2753   1692       C  
ATOM   3422  CD1 ILE A 439     123.832  52.211  38.066  1.00 73.18           C  
ANISOU 3422  CD1 ILE A 439     9161   9212   9433    661   2739   1499       C  
ATOM   3423  N   SER A 440     126.844  57.564  37.894  1.00 91.00           N  
ANISOU 3423  N   SER A 440    11352  11954  11271    268   2594   1983       N  
ATOM   3424  CA  SER A 440     127.935  58.306  37.278  1.00 94.08           C  
ANISOU 3424  CA  SER A 440    11676  12493  11577    168   2664   2005       C  
ATOM   3425  C   SER A 440     128.946  58.824  38.296  1.00 99.03           C  
ANISOU 3425  C   SER A 440    12198  13119  12312    191   2605   2143       C  
ATOM   3426  O   SER A 440     128.752  58.689  39.503  1.00 97.32           O  
ANISOU 3426  O   SER A 440    11974  12787  12218    271   2497   2234       O  
ATOM   3427  CB  SER A 440     127.377  59.468  36.457  1.00 91.25           C  
ANISOU 3427  CB  SER A 440    11464  12235  10972     14   2608   2051       C  
ATOM   3428  OG  SER A 440     126.443  59.000  35.500  1.00 91.69           O  
ANISOU 3428  OG  SER A 440    11619  12296  10922    -20   2651   1932       O  
ATOM   3429  N   GLY A 441     130.028  59.411  37.793  1.00101.14           N  
ANISOU 3429  N   GLY A 441    12385  13520  12523    107   2677   2157       N  
ATOM   3430  CA  GLY A 441     131.054  59.991  38.641  1.00100.71           C  
ANISOU 3430  CA  GLY A 441    12228  13485  12551    109   2626   2289       C  
ATOM   3431  C   GLY A 441     131.785  58.979  39.501  1.00 99.17           C  
ANISOU 3431  C   GLY A 441    11866  13196  12619    248   2650   2279       C  
ATOM   3432  O   GLY A 441     132.427  59.338  40.489  1.00100.05           O  
ANISOU 3432  O   GLY A 441    11907  13283  12824    268   2566   2411       O  
ATOM   3433  N   ASN A 442     131.693  57.709  39.125  1.00 96.89           N  
ANISOU 3433  N   ASN A 442    11512  12848  12453    340   2757   2126       N  
ATOM   3434  CA  ASN A 442     132.344  56.644  39.876  1.00101.47           C  
ANISOU 3434  CA  ASN A 442    11929  13318  13307    477   2771   2110       C  
ATOM   3435  C   ASN A 442     133.669  56.252  39.235  1.00108.96           C  
ANISOU 3435  C   ASN A 442    12676  14351  14371    486   2935   2001       C  
ATOM   3436  O   ASN A 442     133.726  55.319  38.434  1.00110.75           O  
ANISOU 3436  O   ASN A 442    12839  14575  14666    527   3084   1817       O  
ATOM   3437  CB  ASN A 442     131.421  55.432  39.976  1.00100.33           C  
ANISOU 3437  CB  ASN A 442    11828  13030  13261    583   2774   2011       C  
ATOM   3438  CG  ASN A 442     130.039  55.795  40.485  1.00 92.07           C  
ANISOU 3438  CG  ASN A 442    10978  11912  12092    563   2633   2089       C  
ATOM   3439  ND2 ASN A 442     129.017  55.468  39.703  1.00 90.15           N  
ANISOU 3439  ND2 ASN A 442    10851  11665  11738    547   2678   1974       N  
ATOM   3440  OD1 ASN A 442     129.891  56.363  41.568  1.00 88.22           O  
ANISOU 3440  OD1 ASN A 442    10533  11374  11611    556   2487   2244       O  
ATOM   3441  N   LYS A 443     134.727  56.973  39.599  1.00116.78           N  
ANISOU 3441  N   LYS A 443    13564  15417  15389    445   2912   2107       N  
ATOM   3442  CA  LYS A 443     136.042  56.832  38.969  1.00124.44           C  
ANISOU 3442  CA  LYS A 443    14338  16494  16448    428   3068   2010       C  
ATOM   3443  C   LYS A 443     136.315  55.444  38.399  1.00121.68           C  
ANISOU 3443  C   LYS A 443    13846  16088  16298    531   3230   1799       C  
ATOM   3444  O   LYS A 443     136.330  55.254  37.183  1.00124.82           O  
ANISOU 3444  O   LYS A 443    14241  16586  16598    465   3403   1621       O  
ATOM   3445  CB  LYS A 443     137.157  57.214  39.948  1.00132.80           C  
ANISOU 3445  CB  LYS A 443    15250  17550  17659    451   2985   2160       C  
ATOM   3446  CG  LYS A 443     137.182  58.685  40.330  1.00139.11           C  
ANISOU 3446  CG  LYS A 443    16157  18440  18259    326   2865   2345       C  
ATOM   3447  CD  LYS A 443     138.420  59.020  41.151  1.00142.89           C  
ANISOU 3447  CD  LYS A 443    16471  18936  18884    336   2809   2472       C  
ATOM   3448  CE  LYS A 443     138.501  58.169  42.412  1.00146.60           C  
ANISOU 3448  CE  LYS A 443    16857  19228  19616    475   2687   2556       C  
ATOM   3449  NZ  LYS A 443     137.338  58.388  43.317  1.00146.81           N1+
ANISOU 3449  NZ  LYS A 443    17077  19144  19559    478   2515   2681       N1+
ATOM   3450  N   ASN A 444     136.534  54.479  39.284  1.00114.83           N  
ANISOU 3450  N   ASN A 444    12864  15057  15711    682   3171   1819       N  
ATOM   3451  CA  ASN A 444     136.897  53.131  38.865  1.00113.12           C  
ANISOU 3451  CA  ASN A 444    12486  14759  15734    796   3311   1626       C  
ATOM   3452  C   ASN A 444     135.774  52.113  39.053  1.00107.51           C  
ANISOU 3452  C   ASN A 444    11879  13885  15085    892   3270   1568       C  
ATOM   3453  O   ASN A 444     135.907  51.162  39.820  1.00107.27           O  
ANISOU 3453  O   ASN A 444    11754  13686  15317   1027   3203   1587       O  
ATOM   3454  CB  ASN A 444     138.168  52.676  39.587  1.00115.32           C  
ANISOU 3454  CB  ASN A 444    12515  14967  16333    900   3289   1669       C  
ATOM   3455  CG  ASN A 444     138.181  53.072  41.052  1.00113.86           C  
ANISOU 3455  CG  ASN A 444    12359  14689  16213    931   3054   1922       C  
ATOM   3456  ND2 ASN A 444     139.334  53.522  41.533  1.00107.94           N  
ANISOU 3456  ND2 ASN A 444    11452  13984  15575    921   3015   2026       N  
ATOM   3457  OD1 ASN A 444     137.169  52.972  41.742  1.00121.18           O  
ANISOU 3457  OD1 ASN A 444    13448  15509  17086    953   2912   2019       O  
ATOM   3458  N   LEU A 445     134.672  52.319  38.338  1.00101.61           N  
ANISOU 3458  N   LEU A 445    11326  13187  14094    815   3302   1503       N  
ATOM   3459  CA  LEU A 445     133.527  51.420  38.414  1.00 97.16           C  
ANISOU 3459  CA  LEU A 445    10875  12487  13555    888   3272   1439       C  
ATOM   3460  C   LEU A 445     133.252  50.756  37.068  1.00 99.37           C  
ANISOU 3460  C   LEU A 445    11163  12818  13776    861   3474   1194       C  
ATOM   3461  O   LEU A 445     133.009  51.433  36.069  1.00100.73           O  
ANISOU 3461  O   LEU A 445    11432  13146  13694    722   3559   1134       O  
ATOM   3462  CB  LEU A 445     132.285  52.178  38.884  1.00 90.44           C  
ANISOU 3462  CB  LEU A 445    10258  11624  12482    826   3108   1584       C  
ATOM   3463  CG  LEU A 445     130.971  51.394  38.857  1.00 86.82           C  
ANISOU 3463  CG  LEU A 445     9938  11049  12000    874   3081   1515       C  
ATOM   3464  CD1 LEU A 445     131.000  50.236  39.846  1.00 83.07           C  
ANISOU 3464  CD1 LEU A 445     9383  10377  11804   1022   3006   1537       C  
ATOM   3465  CD2 LEU A 445     129.795  52.314  39.139  1.00 88.59           C  
ANISOU 3465  CD2 LEU A 445    10378  11293  11990    791   2942   1637       C  
ATOM   3466  N   CYS A 446     133.286  49.428  37.051  1.00100.62           N  
ANISOU 3466  N   CYS A 446    11223  12840  14169    986   3544   1056       N  
ATOM   3467  CA  CYS A 446     133.053  48.670  35.826  1.00102.53           C  
ANISOU 3467  CA  CYS A 446    11461  13113  14381    966   3745    805       C  
ATOM   3468  C   CYS A 446     131.717  47.940  35.870  1.00105.77           C  
ANISOU 3468  C   CYS A 446    12033  13403  14754   1011   3694    765       C  
ATOM   3469  O   CYS A 446     130.968  48.059  36.839  1.00112.13           O  
ANISOU 3469  O   CYS A 446    12952  14106  15548   1051   3507    927       O  
ATOM   3470  CB  CYS A 446     134.181  47.662  35.603  1.00100.30           C  
ANISOU 3470  CB  CYS A 446    10923  12772  14414   1069   3900    634       C  
ATOM   3471  SG  CYS A 446     135.827  48.394  35.510  1.00158.29           S  
ANISOU 3471  SG  CYS A 446    18043  20259  21841   1023   3982    652       S  
ATOM   3472  N   TYR A 447     131.428  47.186  34.813  1.00103.04           N  
ANISOU 3472  N   TYR A 447    11695  13073  14383    993   3868    539       N  
ATOM   3473  CA  TYR A 447     130.223  46.361  34.737  1.00104.08           C  
ANISOU 3473  CA  TYR A 447    11962  13089  14494   1035   3845    469       C  
ATOM   3474  C   TYR A 447     128.937  47.185  34.689  1.00109.45           C  
ANISOU 3474  C   TYR A 447    12890  13830  14868    929   3722    582       C  
ATOM   3475  O   TYR A 447     127.870  46.659  34.376  1.00110.60           O  
ANISOU 3475  O   TYR A 447    13164  13923  14934    926   3723    507       O  
ATOM   3476  CB  TYR A 447     130.163  45.378  35.913  1.00104.33           C  
ANISOU 3476  CB  TYR A 447    11928  12891  14823   1208   3721    537       C  
ATOM   3477  CG  TYR A 447     131.492  44.753  36.272  1.00105.05           C  
ANISOU 3477  CG  TYR A 447    11763  12898  15254   1325   3773    497       C  
ATOM   3478  CD1 TYR A 447     132.294  45.305  37.263  1.00107.62           C  
ANISOU 3478  CD1 TYR A 447    11987  13207  15696   1360   3640    689       C  
ATOM   3479  CD2 TYR A 447     131.944  43.611  35.625  1.00105.83           C  
ANISOU 3479  CD2 TYR A 447    11715  12928  15568   1399   3951    263       C  
ATOM   3480  CE1 TYR A 447     133.509  44.742  37.595  1.00113.09           C  
ANISOU 3480  CE1 TYR A 447    12436  13818  16714   1467   3671    661       C  
ATOM   3481  CE2 TYR A 447     133.159  43.039  35.951  1.00108.24           C  
ANISOU 3481  CE2 TYR A 447    11769  13143  16214   1513   3991    221       C  
ATOM   3482  CZ  TYR A 447     133.937  43.609  36.937  1.00110.42           C  
ANISOU 3482  CZ  TYR A 447    11945  13404  16605   1548   3844    426       C  
ATOM   3483  OH  TYR A 447     135.149  43.049  37.269  1.00106.88           O  
ANISOU 3483  OH  TYR A 447    11237  12861  16510   1662   3869    393       O  
ATOM   3484  N   ALA A 448     129.040  48.474  34.997  1.00114.14           N  
ANISOU 3484  N   ALA A 448    13541  14526  15299    843   3614    758       N  
ATOM   3485  CA  ALA A 448     127.863  49.333  35.103  1.00112.79           C  
ANISOU 3485  CA  ALA A 448    13585  14391  14879    757   3471    883       C  
ATOM   3486  C   ALA A 448     127.082  49.438  33.796  1.00107.60           C  
ANISOU 3486  C   ALA A 448    13066  13844  13973    627   3566    753       C  
ATOM   3487  O   ALA A 448     125.851  49.458  33.798  1.00101.68           O  
ANISOU 3487  O   ALA A 448    12479  13053  13101    606   3476    779       O  
ATOM   3488  CB  ALA A 448     128.262  50.717  35.595  1.00114.30           C  
ANISOU 3488  CB  ALA A 448    13794  14674  14962    683   3354   1080       C  
ATOM   3489  N   ASN A 449     127.804  49.505  32.683  1.00108.40           N  
ANISOU 3489  N   ASN A 449    13101  14088  14000    530   3747    612       N  
ATOM   3490  CA  ASN A 449     127.179  49.657  31.375  1.00111.22           C  
ANISOU 3490  CA  ASN A 449    13588  14570  14100    375   3840    492       C  
ATOM   3491  C   ASN A 449     126.849  48.321  30.716  1.00102.46           C  
ANISOU 3491  C   ASN A 449    12463  13399  13067    414   3994    262       C  
ATOM   3492  O   ASN A 449     126.660  48.248  29.502  1.00103.58           O  
ANISOU 3492  O   ASN A 449    12667  13659  13031    277   4130    113       O  
ATOM   3493  CB  ASN A 449     128.078  50.488  30.458  1.00125.81           C  
ANISOU 3493  CB  ASN A 449    15394  16621  15785    209   3957    456       C  
ATOM   3494  CG  ASN A 449     129.507  49.974  30.421  1.00139.62           C  
ANISOU 3494  CG  ASN A 449    16909  18388  17753    268   4127    336       C  
ATOM   3495  ND2 ASN A 449     130.448  50.860  30.114  1.00145.02           N  
ANISOU 3495  ND2 ASN A 449    17527  19225  18349    158   4177    374       N  
ATOM   3496  OD1 ASN A 449     129.761  48.794  30.667  1.00142.96           O  
ANISOU 3496  OD1 ASN A 449    17206  18682  18428    409   4209    211       O  
ATOM   3497  N   THR A 450     126.776  47.265  31.519  1.00 93.46           N  
ANISOU 3497  N   THR A 450    11248  12073  12190    590   3969    237       N  
ATOM   3498  CA  THR A 450     126.516  45.931  30.990  1.00 89.61           C  
ANISOU 3498  CA  THR A 450    10732  11503  11812    643   4112     19       C  
ATOM   3499  C   THR A 450     125.127  45.429  31.360  1.00 85.66           C  
ANISOU 3499  C   THR A 450    10389  10876  11282    694   3990     51       C  
ATOM   3500  O   THR A 450     124.632  44.469  30.776  1.00 86.86           O  
ANISOU 3500  O   THR A 450    10573  10980  11449    701   4092   -121       O  
ATOM   3501  CB  THR A 450     127.550  44.910  31.496  1.00 91.26           C  
ANISOU 3501  CB  THR A 450    10717  11579  12379    807   4197    -71       C  
ATOM   3502  CG2 THR A 450     128.945  45.516  31.495  1.00 93.95           C  
ANISOU 3502  CG2 THR A 450    10883  12022  12792    785   4265    -49       C  
ATOM   3503  OG1 THR A 450     127.206  44.497  32.824  1.00 88.23           O  
ANISOU 3503  OG1 THR A 450    10331  11002  12190    962   4015     75       O  
ATOM   3504  N   ILE A 451     124.502  46.078  32.334  1.00 91.39           N  
ANISOU 3504  N   ILE A 451    11208  11547  11967    722   3778    263       N  
ATOM   3505  CA  ILE A 451     123.193  45.646  32.811  1.00 97.29           C  
ANISOU 3505  CA  ILE A 451    12094  12174  12699    770   3655    302       C  
ATOM   3506  C   ILE A 451     122.088  45.936  31.800  1.00 92.13           C  
ANISOU 3506  C   ILE A 451    11618  11616  11771    631   3666    242       C  
ATOM   3507  O   ILE A 451     121.993  47.040  31.267  1.00 91.22           O  
ANISOU 3507  O   ILE A 451    11581  11646  11432    493   3633    311       O  
ATOM   3508  CB  ILE A 451     122.831  46.298  34.164  1.00 99.27           C  
ANISOU 3508  CB  ILE A 451    12390  12346  12982    824   3434    534       C  
ATOM   3509  CG1 ILE A 451     123.521  45.565  35.316  1.00103.48           C  
ANISOU 3509  CG1 ILE A 451    12782  12720  13815    979   3391    584       C  
ATOM   3510  CG2 ILE A 451     121.327  46.283  34.379  1.00 77.66           C  
ANISOU 3510  CG2 ILE A 451     9830   9551  10127    807   3311    574       C  
ATOM   3511  CD1 ILE A 451     125.008  45.822  35.411  1.00105.99           C  
ANISOU 3511  CD1 ILE A 451    12917  13087  14268   1004   3456    603       C  
ATOM   3512  N   ASN A 452     121.262  44.931  31.533  1.00 81.22           N  
ANISOU 3512  N   ASN A 452    10301  10150  10411    661   3705    118       N  
ATOM   3513  CA  ASN A 452     120.073  45.131  30.723  1.00 87.10           C  
ANISOU 3513  CA  ASN A 452    11220  10961  10912    540   3682     79       C  
ATOM   3514  C   ASN A 452     118.983  45.769  31.567  1.00 80.51           C  
ANISOU 3514  C   ASN A 452    10508  10069  10012    553   3462    261       C  
ATOM   3515  O   ASN A 452     118.084  45.086  32.054  1.00 82.07           O  
ANISOU 3515  O   ASN A 452    10766  10142  10276    624   3397    250       O  
ATOM   3516  CB  ASN A 452     119.573  43.806  30.152  1.00 89.31           C  
ANISOU 3516  CB  ASN A 452    11523  11169  11242    564   3805   -124       C  
ATOM   3517  CG  ASN A 452     118.259  43.953  29.411  1.00 93.98           C  
ANISOU 3517  CG  ASN A 452    12297  11817  11595    443   3760   -151       C  
ATOM   3518  ND2 ASN A 452     117.514  42.860  29.302  1.00 92.91           N  
ANISOU 3518  ND2 ASN A 452    12209  11579  11512    488   3796   -271       N  
ATOM   3519  OD1 ASN A 452     117.917  45.040  28.944  1.00 99.98           O  
ANISOU 3519  OD1 ASN A 452    13154  12705  12131    309   3684    -59       O  
ATOM   3520  N   TRP A 453     119.071  47.081  31.750  1.00 77.92           N  
ANISOU 3520  N   TRP A 453    10216   9830   9562    482   3350    422       N  
ATOM   3521  CA  TRP A 453     118.111  47.791  32.583  1.00 82.30           C  
ANISOU 3521  CA  TRP A 453    10869  10330  10070    492   3148    587       C  
ATOM   3522  C   TRP A 453     116.692  47.619  32.058  1.00 89.15           C  
ANISOU 3522  C   TRP A 453    11886  11188  10797    431   3096    538       C  
ATOM   3523  O   TRP A 453     115.728  47.669  32.821  1.00 73.65           O  
ANISOU 3523  O   TRP A 453     9990   9133   8862    476   2960    612       O  
ATOM   3524  CB  TRP A 453     118.468  49.274  32.668  1.00 81.46           C  
ANISOU 3524  CB  TRP A 453    10776  10329   9845    408   3052    747       C  
ATOM   3525  CG  TRP A 453     119.848  49.515  33.180  1.00 80.50           C  
ANISOU 3525  CG  TRP A 453    10510  10225   9850    457   3095    803       C  
ATOM   3526  CD1 TRP A 453     120.951  49.830  32.444  1.00 76.93           C  
ANISOU 3526  CD1 TRP A 453     9978   9903   9351    385   3218    759       C  
ATOM   3527  CD2 TRP A 453     120.280  49.450  34.543  1.00 80.41           C  
ANISOU 3527  CD2 TRP A 453    10414  10104  10033    578   3012    915       C  
ATOM   3528  CE2 TRP A 453     121.657  49.742  34.559  1.00 84.35           C  
ANISOU 3528  CE2 TRP A 453    10777  10668  10602    581   3085    938       C  
ATOM   3529  CE3 TRP A 453     119.635  49.174  35.752  1.00 79.73           C  
ANISOU 3529  CE3 TRP A 453    10356   9876  10062    669   2884    998       C  
ATOM   3530  NE1 TRP A 453     122.043  49.972  33.265  1.00 88.60           N  
ANISOU 3530  NE1 TRP A 453    11317  11354  10992    464   3216    836       N  
ATOM   3531  CZ2 TRP A 453     122.401  49.768  35.735  1.00 86.98           C  
ANISOU 3531  CZ2 TRP A 453    11003  10925  11119    676   3022   1050       C  
ATOM   3532  CZ3 TRP A 453     120.374  49.200  36.919  1.00 81.72           C  
ANISOU 3532  CZ3 TRP A 453    10510  10056  10483    751   2825   1107       C  
ATOM   3533  CH2 TRP A 453     121.742  49.495  36.902  1.00 86.77           C  
ANISOU 3533  CH2 TRP A 453    11016  10759  11193    756   2888   1137       C  
ATOM   3534  N   LYS A 454     116.574  47.407  30.752  1.00 92.70           N  
ANISOU 3534  N   LYS A 454    12386  11740  11097    318   3208    407       N  
ATOM   3535  CA  LYS A 454     115.273  47.264  30.110  1.00 95.65           C  
ANISOU 3535  CA  LYS A 454    12901  12122  11321    240   3161    359       C  
ATOM   3536  C   LYS A 454     114.509  46.069  30.674  1.00 90.61           C  
ANISOU 3536  C   LYS A 454    12277  11330  10822    355   3157    282       C  
ATOM   3537  O   LYS A 454     113.332  45.876  30.378  1.00 94.05           O  
ANISOU 3537  O   LYS A 454    12823  11745  11166    313   3099    252       O  
ATOM   3538  CB  LYS A 454     115.443  47.121  28.596  1.00104.48           C  
ANISOU 3538  CB  LYS A 454    14061  13381  12256     85   3303    219       C  
ATOM   3539  CG  LYS A 454     114.173  47.361  27.800  1.00110.15           C  
ANISOU 3539  CG  LYS A 454    14938  14147  12769    -44   3219    215       C  
ATOM   3540  CD  LYS A 454     113.642  48.768  28.016  1.00113.03           C  
ANISOU 3540  CD  LYS A 454    15378  14548  13020   -111   3012    410       C  
ATOM   3541  CE  LYS A 454     112.355  48.990  27.240  1.00120.43           C  
ANISOU 3541  CE  LYS A 454    16461  15518  13778   -235   2909    413       C  
ATOM   3542  NZ  LYS A 454     111.761  50.329  27.503  1.00123.52           N1+
ANISOU 3542  NZ  LYS A 454    16915  15918  14099   -285   2692    600       N1+
ATOM   3543  N   LYS A 455     115.190  45.276  31.494  1.00 92.68           N  
ANISOU 3543  N   LYS A 455    12426  11480  11309    494   3212    257       N  
ATOM   3544  CA  LYS A 455     114.597  44.092  32.104  1.00100.87           C  
ANISOU 3544  CA  LYS A 455    13469  12359  12496    604   3207    192       C  
ATOM   3545  C   LYS A 455     114.083  44.376  33.515  1.00100.52           C  
ANISOU 3545  C   LYS A 455    13441  12205  12549    684   3032    347       C  
ATOM   3546  O   LYS A 455     113.075  43.814  33.945  1.00 99.45           O  
ANISOU 3546  O   LYS A 455    13374  11971  12441    717   2969    330       O  
ATOM   3547  CB  LYS A 455     115.620  42.954  32.139  1.00109.99           C  
ANISOU 3547  CB  LYS A 455    14493  13441  13859    702   3362     66       C  
ATOM   3548  CG  LYS A 455     115.298  41.856  33.138  1.00116.84           C  
ANISOU 3548  CG  LYS A 455    15339  14118  14936    837   3319     56       C  
ATOM   3549  CD  LYS A 455     116.405  40.816  33.188  1.00120.37           C  
ANISOU 3549  CD  LYS A 455    15638  14479  15617    939   3455    -54       C  
ATOM   3550  CE  LYS A 455     116.140  39.786  34.270  1.00120.81           C  
ANISOU 3550  CE  LYS A 455    15675  14334  15892   1066   3383    -32       C  
ATOM   3551  NZ  LYS A 455     114.816  39.132  34.088  1.00122.08           N1+
ANISOU 3551  NZ  LYS A 455    15969  14437  15977   1043   3358   -106       N1+
ATOM   3552  N   LEU A 456     114.784  45.249  34.232  1.00 97.16           N  
ANISOU 3552  N   LEU A 456    12952  11798  12165    704   2961    492       N  
ATOM   3553  CA  LEU A 456     114.412  45.594  35.600  1.00 91.42           C  
ANISOU 3553  CA  LEU A 456    12235  10978  11522    761   2806    636       C  
ATOM   3554  C   LEU A 456     113.285  46.624  35.635  1.00 86.55           C  
ANISOU 3554  C   LEU A 456    11732  10404  10748    680   2668    721       C  
ATOM   3555  O   LEU A 456     112.490  46.653  36.574  1.00 83.07           O  
ANISOU 3555  O   LEU A 456    11334   9878  10352    709   2556    781       O  
ATOM   3556  CB  LEU A 456     115.626  46.124  36.368  1.00 94.49           C  
ANISOU 3556  CB  LEU A 456    12511  11371  12019    804   2784    756       C  
ATOM   3557  CG  LEU A 456     116.891  45.263  36.362  1.00 95.98           C  
ANISOU 3557  CG  LEU A 456    12558  11519  12390    887   2907    689       C  
ATOM   3558  CD1 LEU A 456     118.030  45.981  37.071  1.00 90.08           C  
ANISOU 3558  CD1 LEU A 456    11705  10796  11726    911   2866    825       C  
ATOM   3559  CD2 LEU A 456     116.628  43.909  36.999  1.00101.84           C  
ANISOU 3559  CD2 LEU A 456    13284  12094  13318    990   2909    630       C  
ATOM   3560  N   PHE A 457     113.222  47.471  34.613  1.00 83.52           N  
ANISOU 3560  N   PHE A 457    11395  10151  10188    571   2673    723       N  
ATOM   3561  CA  PHE A 457     112.199  48.508  34.552  1.00 77.59           C  
ANISOU 3561  CA  PHE A 457    10741   9435   9307    493   2531    806       C  
ATOM   3562  C   PHE A 457     110.811  47.899  34.413  1.00 78.81           C  
ANISOU 3562  C   PHE A 457    10986   9526   9430    488   2491    728       C  
ATOM   3563  O   PHE A 457     110.672  46.717  34.099  1.00 85.19           O  
ANISOU 3563  O   PHE A 457    11799  10291  10279    521   2589    600       O  
ATOM   3564  CB  PHE A 457     112.464  49.475  33.397  1.00 78.33           C  
ANISOU 3564  CB  PHE A 457    10868   9675   9217    365   2537    829       C  
ATOM   3565  CG  PHE A 457     113.749  50.240  33.527  1.00 80.81           C  
ANISOU 3565  CG  PHE A 457    11101  10062   9542    353   2561    917       C  
ATOM   3566  CD1 PHE A 457     114.326  50.444  34.769  1.00 87.77           C  
ANISOU 3566  CD1 PHE A 457    11905  10877  10569    441   2515   1016       C  
ATOM   3567  CD2 PHE A 457     114.368  50.775  32.411  1.00 80.54           C  
ANISOU 3567  CD2 PHE A 457    11072  10169   9361    238   2626    904       C  
ATOM   3568  CE1 PHE A 457     115.506  51.152  34.894  1.00 91.04           C  
ANISOU 3568  CE1 PHE A 457    12240  11359  10991    425   2534   1099       C  
ATOM   3569  CE2 PHE A 457     115.547  51.485  32.529  1.00 85.69           C  
ANISOU 3569  CE2 PHE A 457    11647  10893  10019    219   2650    982       C  
ATOM   3570  CZ  PHE A 457     116.116  51.675  33.772  1.00 90.34           C  
ANISOU 3570  CZ  PHE A 457    12152  11410  10763    318   2604   1080       C  
ATOM   3571  N   GLY A 458     109.788  48.714  34.647  1.00 72.80           N  
ANISOU 3571  N   GLY A 458    10292   8757   8610    445   2348    800       N  
ATOM   3572  CA  GLY A 458     108.413  48.263  34.543  1.00 73.05           C  
ANISOU 3572  CA  GLY A 458    10404   8736   8616    433   2295    734       C  
ATOM   3573  C   GLY A 458     107.445  49.391  34.244  1.00 77.38           C  
ANISOU 3573  C   GLY A 458    11019   9321   9061    350   2148    804       C  
ATOM   3574  O   GLY A 458     106.249  49.283  34.517  1.00 79.00           O  
ANISOU 3574  O   GLY A 458    11270   9465   9282    352   2066    781       O  
ATOM   3575  N   THR A 459     107.963  50.477  33.679  1.00 79.81           N  
ANISOU 3575  N   THR A 459    11327   9725   9273    274   2110    888       N  
ATOM   3576  CA  THR A 459     107.140  51.639  33.362  1.00 82.03           C  
ANISOU 3576  CA  THR A 459    11664  10031   9472    193   1953    970       C  
ATOM   3577  C   THR A 459     107.690  52.389  32.153  1.00 83.26           C  
ANISOU 3577  C   THR A 459    11852  10316   9467     69   1951   1015       C  
ATOM   3578  O   THR A 459     108.897  52.394  31.910  1.00 81.47           O  
ANISOU 3578  O   THR A 459    11580  10160   9214     57   2056   1021       O  
ATOM   3579  CB  THR A 459     107.042  52.603  34.563  1.00 80.01           C  
ANISOU 3579  CB  THR A 459    11369   9712   9320    237   1835   1084       C  
ATOM   3580  CG2 THR A 459     106.160  53.796  34.225  1.00 77.93           C  
ANISOU 3580  CG2 THR A 459    11152   9455   9004    161   1666   1159       C  
ATOM   3581  OG1 THR A 459     106.488  51.913  35.691  1.00 84.05           O  
ANISOU 3581  OG1 THR A 459    11860  10112   9964    326   1836   1039       O  
ATOM   3582  N   SER A 460     106.796  53.019  31.395  1.00 83.56           N  
ANISOU 3582  N   SER A 460    11965  10383   9400    -31   1828   1048       N  
ATOM   3583  CA  SER A 460     107.188  53.787  30.220  1.00 81.91           C  
ANISOU 3583  CA  SER A 460    11806  10294   9020   -176   1798   1106       C  
ATOM   3584  C   SER A 460     108.108  54.943  30.588  1.00 79.51           C  
ANISOU 3584  C   SER A 460    11459  10025   8726   -189   1751   1239       C  
ATOM   3585  O   SER A 460     107.858  55.667  31.549  1.00 78.02           O  
ANISOU 3585  O   SER A 460    11238   9758   8648   -128   1640   1325       O  
ATOM   3586  CB  SER A 460     105.955  54.338  29.502  1.00 86.30           C  
ANISOU 3586  CB  SER A 460    12449  10850   9490   -278   1629   1144       C  
ATOM   3587  OG  SER A 460     105.017  53.314  29.224  1.00 96.77           O  
ANISOU 3587  OG  SER A 460    13815  12141  10814   -267   1658   1026       O  
ATOM   3588  N   GLY A 461     109.177  55.110  29.818  1.00 88.58           N  
ANISOU 3588  N   GLY A 461    12607  11295   9757   -278   1842   1247       N  
ATOM   3589  CA  GLY A 461     110.018  56.286  29.933  1.00 94.87           C  
ANISOU 3589  CA  GLY A 461    13378  12143  10524   -325   1788   1378       C  
ATOM   3590  C   GLY A 461     111.178  56.175  30.900  1.00 92.47           C  
ANISOU 3590  C   GLY A 461    12968  11826  10342   -219   1890   1393       C  
ATOM   3591  O   GLY A 461     111.928  57.134  31.085  1.00 98.05           O  
ANISOU 3591  O   GLY A 461    13647  12574  11033   -253   1851   1502       O  
ATOM   3592  N   GLN A 462     111.335  55.013  31.523  1.00 83.76           N  
ANISOU 3592  N   GLN A 462    11804  10659   9362    -96   2011   1290       N  
ATOM   3593  CA  GLN A 462     112.450  54.816  32.438  1.00 80.39           C  
ANISOU 3593  CA  GLN A 462    11271  10212   9061      2   2098   1308       C  
ATOM   3594  C   GLN A 462     113.778  54.897  31.688  1.00 83.02           C  
ANISOU 3594  C   GLN A 462    11559  10675   9310    -70   2228   1293       C  
ATOM   3595  O   GLN A 462     114.080  54.055  30.842  1.00 77.81           O  
ANISOU 3595  O   GLN A 462    10896  10075   8592   -106   2372   1166       O  
ATOM   3596  CB  GLN A 462     112.318  53.488  33.186  1.00 78.79           C  
ANISOU 3596  CB  GLN A 462    11019   9906   9010    136   2186   1205       C  
ATOM   3597  CG  GLN A 462     111.016  53.354  33.963  1.00 79.80           C  
ANISOU 3597  CG  GLN A 462    11189   9914   9218    195   2072   1207       C  
ATOM   3598  CD  GLN A 462     111.107  52.353  35.102  1.00 77.37           C  
ANISOU 3598  CD  GLN A 462    10821   9496   9079    324   2126   1163       C  
ATOM   3599  NE2 GLN A 462     112.183  52.434  35.876  1.00 73.25           N  
ANISOU 3599  NE2 GLN A 462    10214   8964   8653    380   2162   1223       N  
ATOM   3600  OE1 GLN A 462     110.218  51.520  35.284  1.00 75.35           O  
ANISOU 3600  OE1 GLN A 462    10599   9164   8866    364   2127   1081       O  
ATOM   3601  N   LYS A 463     114.556  55.929  31.999  1.00 87.62           N  
ANISOU 3601  N   LYS A 463    12105  11300   9884    -99   2180   1415       N  
ATOM   3602  CA  LYS A 463     115.846  56.161  31.360  1.00 85.15           C  
ANISOU 3602  CA  LYS A 463    11743  11117   9492   -177   2294   1412       C  
ATOM   3603  C   LYS A 463     116.994  55.727  32.266  1.00 85.92           C  
ANISOU 3603  C   LYS A 463    11705  11187   9754    -60   2395   1407       C  
ATOM   3604  O   LYS A 463     116.787  55.388  33.431  1.00 86.46           O  
ANISOU 3604  O   LYS A 463    11731  11136   9984     68   2354   1431       O  
ATOM   3605  CB  LYS A 463     116.002  57.641  31.010  1.00 86.28           C  
ANISOU 3605  CB  LYS A 463    11940  11338   9506   -307   2169   1558       C  
ATOM   3606  CG  LYS A 463     115.010  58.152  29.981  1.00 98.11           C  
ANISOU 3606  CG  LYS A 463    13568  12874  10834   -448   2055   1582       C  
ATOM   3607  CD  LYS A 463     114.799  59.660  30.099  1.00110.41           C  
ANISOU 3607  CD  LYS A 463    15179  14430  12343   -525   1861   1755       C  
ATOM   3608  CE  LYS A 463     116.116  60.430  30.181  1.00113.92           C  
ANISOU 3608  CE  LYS A 463    15567  14963  12753   -577   1899   1841       C  
ATOM   3609  NZ  LYS A 463     116.631  60.550  31.578  1.00107.42           N1+
ANISOU 3609  NZ  LYS A 463    14645  14059  12112   -434   1898   1894       N1+
ATOM   3610  N   THR A 464     118.207  55.747  31.723  1.00 85.55           N  
ANISOU 3610  N   THR A 464    11588  11252   9666   -115   2524   1376       N  
ATOM   3611  CA  THR A 464     119.391  55.353  32.478  1.00 85.55           C  
ANISOU 3611  CA  THR A 464    11445  11233   9829    -12   2619   1371       C  
ATOM   3612  C   THR A 464     120.569  56.284  32.201  1.00 81.62           C  
ANISOU 3612  C   THR A 464    10893  10861   9259   -104   2648   1447       C  
ATOM   3613  O   THR A 464     121.102  56.320  31.092  1.00 88.18           O  
ANISOU 3613  O   THR A 464    11724  11823   9958   -225   2760   1375       O  
ATOM   3614  CB  THR A 464     119.802  53.904  32.167  1.00 93.12           C  
ANISOU 3614  CB  THR A 464    12320  12172  10888     59   2804   1192       C  
ATOM   3615  CG2 THR A 464     119.791  53.655  30.665  1.00 91.55           C  
ANISOU 3615  CG2 THR A 464    12173  12099  10514    -80   2928   1059       C  
ATOM   3616  OG1 THR A 464     121.119  53.662  32.675  1.00103.87           O  
ANISOU 3616  OG1 THR A 464    13528  13538  12398    132   2897   1191       O  
ATOM   3617  N   LYS A 465     120.972  57.032  33.220  1.00 78.16           N  
ANISOU 3617  N   LYS A 465    10411  10385   8900    -58   2551   1589       N  
ATOM   3618  CA  LYS A 465     122.047  58.005  33.081  1.00 92.91           C  
ANISOU 3618  CA  LYS A 465    12233  12364  10704   -145   2559   1679       C  
ATOM   3619  C   LYS A 465     123.343  57.468  33.683  1.00102.10           C  
ANISOU 3619  C   LYS A 465    13228  13526  12038    -51   2673   1654       C  
ATOM   3620  O   LYS A 465     123.616  57.657  34.868  1.00108.61           O  
ANISOU 3620  O   LYS A 465    13996  14272  12998     39   2597   1755       O  
ATOM   3621  CB  LYS A 465     121.648  59.322  33.751  1.00 92.79           C  
ANISOU 3621  CB  LYS A 465    12286  12315  10655   -176   2367   1858       C  
ATOM   3622  CG  LYS A 465     122.541  60.507  33.426  1.00 93.22           C  
ANISOU 3622  CG  LYS A 465    12332  12490  10597   -300   2346   1964       C  
ATOM   3623  CD  LYS A 465     122.033  61.759  34.126  1.00 99.63           C  
ANISOU 3623  CD  LYS A 465    13215  13243  11397   -321   2151   2129       C  
ATOM   3624  CE  LYS A 465     122.924  62.960  33.855  1.00114.66           C  
ANISOU 3624  CE  LYS A 465    15116  15257  13194   -446   2120   2244       C  
ATOM   3625  NZ  LYS A 465     122.891  63.371  32.425  1.00123.91           N1+
ANISOU 3625  NZ  LYS A 465    16374  16556  14151   -623   2138   2225       N1+
ATOM   3626  N   ILE A 466     124.134  56.791  32.858  1.00 95.75           N  
ANISOU 3626  N   ILE A 466    12342  12809  11230    -79   2856   1515       N  
ATOM   3627  CA  ILE A 466     125.398  56.221  33.303  1.00 85.46           C  
ANISOU 3627  CA  ILE A 466    10860  11503  10109      9   2973   1473       C  
ATOM   3628  C   ILE A 466     126.557  56.830  32.529  1.00 82.73           C  
ANISOU 3628  C   ILE A 466    10447  11327   9660   -119   3080   1459       C  
ATOM   3629  O   ILE A 466     126.823  56.440  31.394  1.00 85.29           O  
ANISOU 3629  O   ILE A 466    10759  11754   9891   -210   3236   1311       O  
ATOM   3630  CB  ILE A 466     125.423  54.699  33.098  1.00 87.26           C  
ANISOU 3630  CB  ILE A 466    11009  11662  10485    113   3119   1288       C  
ATOM   3631  CG1 ILE A 466     124.252  54.046  33.834  1.00 90.56           C  
ANISOU 3631  CG1 ILE A 466    11500  11916  10994    227   3017   1296       C  
ATOM   3632  CG2 ILE A 466     126.752  54.122  33.562  1.00 87.34           C  
ANISOU 3632  CG2 ILE A 466    10817  11654  10713    210   3227   1247       C  
ATOM   3633  CD1 ILE A 466     124.161  52.550  33.629  1.00 94.11           C  
ANISOU 3633  CD1 ILE A 466    11890  12283  11585    325   3145   1119       C  
ATOM   3634  N   ILE A 467     127.243  57.788  33.142  1.00 81.11           N  
ANISOU 3634  N   ILE A 467    10200  11154   9464   -139   3002   1609       N  
ATOM   3635  CA  ILE A 467     128.359  58.461  32.487  1.00 86.17           C  
ANISOU 3635  CA  ILE A 467    10778  11960  10003   -271   3092   1611       C  
ATOM   3636  C   ILE A 467     129.543  58.644  33.427  1.00 87.17           C  
ANISOU 3636  C   ILE A 467    10744  12076  10301   -194   3093   1694       C  
ATOM   3637  O   ILE A 467     129.455  58.349  34.616  1.00 87.87           O  
ANISOU 3637  O   ILE A 467    10786  12030  10570    -52   3002   1769       O  
ATOM   3638  CB  ILE A 467     127.950  59.846  31.951  1.00 90.15           C  
ANISOU 3638  CB  ILE A 467    11437  12559  10256   -449   2973   1737       C  
ATOM   3639  CG1 ILE A 467     127.822  60.844  33.103  1.00 92.80           C  
ANISOU 3639  CG1 ILE A 467    11804  12821  10634   -409   2781   1941       C  
ATOM   3640  CG2 ILE A 467     126.653  59.756  31.164  1.00 94.49           C  
ANISOU 3640  CG2 ILE A 467    12155  13097  10648   -521   2924   1692       C  
ATOM   3641  CD1 ILE A 467     127.429  62.233  32.660  1.00 96.28           C  
ANISOU 3641  CD1 ILE A 467    12390  13331  10862   -571   2646   2073       C  
ATOM   3642  N   SER A 468     130.648  59.137  32.878  1.00 89.90           N  
ANISOU 3642  N   SER A 468    11007  12571  10581   -303   3193   1680       N  
ATOM   3643  CA  SER A 468     131.845  59.438  33.658  1.00 91.43           C  
ANISOU 3643  CA  SER A 468    11046  12779  10916   -256   3192   1764       C  
ATOM   3644  C   SER A 468     132.175  58.371  34.698  1.00 98.56           C  
ANISOU 3644  C   SER A 468    11798  13533  12118    -55   3200   1740       C  
ATOM   3645  O   SER A 468     132.247  58.656  35.893  1.00102.75           O  
ANISOU 3645  O   SER A 468    12308  13973  12760     25   3062   1890       O  
ATOM   3646  CB  SER A 468     131.712  60.805  34.330  1.00 89.94           C  
ANISOU 3646  CB  SER A 468    10949  12593  10630   -316   3004   1983       C  
ATOM   3647  OG  SER A 468     131.636  61.838  33.364  1.00 88.95           O  
ANISOU 3647  OG  SER A 468    10939  12609  10247   -512   2994   2017       O  
ATOM   3648  N   ASN A 469     132.370  57.142  34.233  1.00102.44           N  
ANISOU 3648  N   ASN A 469    12188  13997  12737     17   3358   1550       N  
ATOM   3649  CA  ASN A 469     132.813  56.053  35.095  1.00108.05           C  
ANISOU 3649  CA  ASN A 469    12737  14566  13753    201   3374   1515       C  
ATOM   3650  C   ASN A 469     134.147  55.501  34.614  1.00119.09           C  
ANISOU 3650  C   ASN A 469    13914  16034  15302    215   3567   1369       C  
ATOM   3651  O   ASN A 469     134.927  56.208  33.977  1.00126.52           O  
ANISOU 3651  O   ASN A 469    14810  17139  16125     84   3654   1354       O  
ATOM   3652  CB  ASN A 469     131.769  54.935  35.136  1.00104.42           C  
ANISOU 3652  CB  ASN A 469    12342  13963  13370    306   3372   1417       C  
ATOM   3653  CG  ASN A 469     130.604  55.257  36.050  1.00100.10           C  
ANISOU 3653  CG  ASN A 469    11955  13299  12780    346   3168   1570       C  
ATOM   3654  ND2 ASN A 469     129.474  54.599  35.820  1.00 95.00           N  
ANISOU 3654  ND2 ASN A 469    11419  12572  12103    380   3160   1490       N  
ATOM   3655  OD1 ASN A 469     130.720  56.083  36.955  1.00100.30           O  
ANISOU 3655  OD1 ASN A 469    12000  13307  12801    341   3024   1749       O  
ATOM   3656  N   ARG A 470     134.408  54.237  34.923  1.00120.71           N  
ANISOU 3656  N   ARG A 470    13976  16112  15777    369   3633   1259       N  
ATOM   3657  CA  ARG A 470     135.591  53.565  34.406  1.00126.28           C  
ANISOU 3657  CA  ARG A 470    14455  16862  16662    397   3831   1083       C  
ATOM   3658  C   ARG A 470     135.377  53.273  32.929  1.00124.06           C  
ANISOU 3658  C   ARG A 470    14218  16701  16217    278   4036    856       C  
ATOM   3659  O   ARG A 470     134.348  52.715  32.544  1.00124.92           O  
ANISOU 3659  O   ARG A 470    14455  16753  16255    286   4047    773       O  
ATOM   3660  CB  ARG A 470     135.837  52.261  35.162  1.00134.38           C  
ANISOU 3660  CB  ARG A 470    15324  17691  18043    601   3823   1032       C  
ATOM   3661  CG  ARG A 470     137.037  51.466  34.670  1.00137.86           C  
ANISOU 3661  CG  ARG A 470    15507  18149  18724    653   4026    834       C  
ATOM   3662  CD  ARG A 470     138.284  51.782  35.474  1.00139.06           C  
ANISOU 3662  CD  ARG A 470    15458  18297  19080    706   3969    951       C  
ATOM   3663  NE  ARG A 470     139.340  50.804  35.232  1.00145.73           N  
ANISOU 3663  NE  ARG A 470    16033  19098  20242    804   4131    765       N  
ATOM   3664  CZ  ARG A 470     140.428  50.679  35.984  1.00151.73           C  
ANISOU 3664  CZ  ARG A 470    16573  19798  21279    899   4083    836       C  
ATOM   3665  NH1 ARG A 470     140.603  51.469  37.035  1.00151.97           N1+
ANISOU 3665  NH1 ARG A 470    16633  19816  21291    897   3880   1092       N1+
ATOM   3666  NH2 ARG A 470     141.339  49.762  35.689  1.00154.53           N  
ANISOU 3666  NH2 ARG A 470    16672  20103  21939    991   4236    647       N  
ATOM   3667  N   GLY A 471     136.343  53.657  32.103  1.00122.37           N  
ANISOU 3667  N   GLY A 471    13901  16661  15933    152   4201    755       N  
ATOM   3668  CA  GLY A 471     136.241  53.439  30.672  1.00127.72           C  
ANISOU 3668  CA  GLY A 471    14618  17476  16434      4   4409    534       C  
ATOM   3669  C   GLY A 471     135.943  51.991  30.339  1.00129.84           C  
ANISOU 3669  C   GLY A 471    14821  17629  16884    116   4544    311       C  
ATOM   3670  O   GLY A 471     136.526  51.081  30.927  1.00130.16           O  
ANISOU 3670  O   GLY A 471    14668  17533  17255    291   4577    249       O  
ATOM   3671  N   GLU A 472     135.026  51.775  29.402  1.00134.45           N  
ANISOU 3671  N   GLU A 472    15569  18260  17257     11   4612    194       N  
ATOM   3672  CA  GLU A 472     134.683  50.425  28.972  1.00142.50           C  
ANISOU 3672  CA  GLU A 472    16546  19180  18418     94   4753    -33       C  
ATOM   3673  C   GLU A 472     135.911  49.713  28.415  1.00145.25           C  
ANISOU 3673  C   GLU A 472    16641  19574  18973    106   5010   -282       C  
ATOM   3674  O   GLU A 472     136.155  48.545  28.719  1.00146.95           O  
ANISOU 3674  O   GLU A 472    16701  19632  19500    278   5078   -413       O  
ATOM   3675  CB  GLU A 472     133.572  50.455  27.922  1.00149.92           C  
ANISOU 3675  CB  GLU A 472    17709  20201  19054    -64   4794   -118       C  
ATOM   3676  CG  GLU A 472     133.280  49.099  27.300  1.00158.13           C  
ANISOU 3676  CG  GLU A 472    18709  21167  20206    -14   4972   -381       C  
ATOM   3677  CD  GLU A 472     132.305  49.186  26.143  1.00163.06           C  
ANISOU 3677  CD  GLU A 472    19546  21902  20507   -206   5030   -475       C  
ATOM   3678  OE1 GLU A 472     132.383  48.332  25.234  1.00164.86           O  
ANISOU 3678  OE1 GLU A 472    19730  22162  20746   -259   5248   -735       O  
ATOM   3679  OE2 GLU A 472     131.464  50.109  26.141  1.00163.30           O1-
ANISOU 3679  OE2 GLU A 472    19784  21984  20279   -308   4856   -290       O1-
ATOM   3680  N   ASN A 473     136.682  50.425  27.600  1.00146.08           N  
ANISOU 3680  N   ASN A 473    16703  19891  18909    -82   5151   -351       N  
ATOM   3681  CA  ASN A 473     137.906  49.875  27.032  1.00148.51           C  
ANISOU 3681  CA  ASN A 473    16759  20268  19401    -95   5410   -599       C  
ATOM   3682  C   ASN A 473     138.930  49.544  28.113  1.00145.45           C  
ANISOU 3682  C   ASN A 473    16112  19747  19405    113   5361   -539       C  
ATOM   3683  O   ASN A 473     139.709  48.601  27.977  1.00148.29           O  
ANISOU 3683  O   ASN A 473    16234  20043  20064    212   5533   -751       O  
ATOM   3684  CB  ASN A 473     138.506  50.840  26.008  1.00151.28           C  
ANISOU 3684  CB  ASN A 473    17131  20887  19460   -364   5552   -657       C  
ATOM   3685  CG  ASN A 473     137.653  50.969  24.759  1.00151.68           C  
ANISOU 3685  CG  ASN A 473    17404  21078  19151   -591   5645   -770       C  
ATOM   3686  ND2 ASN A 473     137.671  52.149  24.149  1.00151.57           N  
ANISOU 3686  ND2 ASN A 473    17529  21268  18792   -835   5623   -676       N  
ATOM   3687  OD1 ASN A 473     136.990  50.018  24.345  1.00151.28           O  
ANISOU 3687  OD1 ASN A 473    17400  20949  19132   -556   5727   -934       O  
ATOM   3688  N   SER A 474     138.920  50.324  29.189  1.00140.86           N  
ANISOU 3688  N   SER A 474    15575  19119  18828    174   5121   -252       N  
ATOM   3689  CA  SER A 474     139.822  50.091  30.310  1.00139.98           C  
ANISOU 3689  CA  SER A 474    15241  18879  19067    358   5032   -153       C  
ATOM   3690  C   SER A 474     139.385  48.877  31.123  1.00137.91           C  
ANISOU 3690  C   SER A 474    14927  18353  19119    592   4939   -156       C  
ATOM   3691  O   SER A 474     140.216  48.097  31.587  1.00138.97           O  
ANISOU 3691  O   SER A 474    14818  18362  19622    749   4975   -224       O  
ATOM   3692  CB  SER A 474     139.893  51.328  31.207  1.00138.66           C  
ANISOU 3692  CB  SER A 474    15156  18748  18781    329   4802    157       C  
ATOM   3693  OG  SER A 474     140.762  51.110  32.304  1.00140.41           O  
ANISOU 3693  OG  SER A 474    15170  18850  19331    492   4705    263       O  
ATOM   3694  N   CYS A 475     138.077  48.722  31.296  1.00137.61           N  
ANISOU 3694  N   CYS A 475    15117  18228  18941    611   4812    -78       N  
ATOM   3695  CA  CYS A 475     137.539  47.587  32.035  1.00138.96           C  
ANISOU 3695  CA  CYS A 475    15272  18154  19372    810   4717    -75       C  
ATOM   3696  C   CYS A 475     137.916  46.270  31.371  1.00134.42           C  
ANISOU 3696  C   CYS A 475    14521  17503  19048    887   4941   -377       C  
ATOM   3697  O   CYS A 475     138.351  45.333  32.039  1.00135.23           O  
ANISOU 3697  O   CYS A 475    14446  17413  19522   1074   4910   -402       O  
ATOM   3698  CB  CYS A 475     136.017  47.693  32.171  1.00142.25           C  
ANISOU 3698  CB  CYS A 475    15971  18519  19557    786   4570     32       C  
ATOM   3699  SG  CYS A 475     135.456  48.732  33.541  1.00138.10           S  
ANISOU 3699  SG  CYS A 475    15604  17943  18926    807   4248    397       S  
ATOM   3700  N   LYS A 476     137.751  46.202  30.054  1.00130.67           N  
ANISOU 3700  N   LYS A 476    14100  17176  18373    735   5164   -606       N  
ATOM   3701  CA  LYS A 476     138.077  44.988  29.318  1.00131.59           C  
ANISOU 3701  CA  LYS A 476    14060  17235  18704    784   5404   -923       C  
ATOM   3702  C   LYS A 476     139.585  44.783  29.273  1.00127.50           C  
ANISOU 3702  C   LYS A 476    13222  16738  18485    834   5556  -1057       C  
ATOM   3703  O   LYS A 476     140.065  43.658  29.141  1.00123.56           O  
ANISOU 3703  O   LYS A 476    12519  16109  18321    959   5695  -1273       O  
ATOM   3704  CB  LYS A 476     137.498  45.031  27.902  1.00137.11           C  
ANISOU 3704  CB  LYS A 476    14912  18104  19078    577   5604  -1132       C  
ATOM   3705  CG  LYS A 476     138.250  45.933  26.940  1.00145.42           C  
ANISOU 3705  CG  LYS A 476    15931  19426  19896    348   5781  -1224       C  
ATOM   3706  CD  LYS A 476     137.687  45.817  25.531  1.00151.85           C  
ANISOU 3706  CD  LYS A 476    16891  20396  20409    134   5985  -1448       C  
ATOM   3707  CE  LYS A 476     138.510  46.618  24.532  1.00154.86           C  
ANISOU 3707  CE  LYS A 476    17227  21048  20567   -112   6180  -1562       C  
ATOM   3708  NZ  LYS A 476     139.900  46.097  24.399  1.00154.25           N1+
ANISOU 3708  NZ  LYS A 476    16823  20976  20810    -53   6402  -1785       N1+
ATOM   3709  N   ALA A 477     140.328  45.878  29.392  1.00132.72           N  
ANISOU 3709  N   ALA A 477    13835  17556  19036    737   5527   -930       N  
ATOM   3710  CA  ALA A 477     141.785  45.822  29.382  1.00139.93           C  
ANISOU 3710  CA  ALA A 477    14441  18508  20217    771   5660  -1038       C  
ATOM   3711  C   ALA A 477     142.318  45.102  30.617  1.00146.17           C  
ANISOU 3711  C   ALA A 477    15022  19049  21466   1027   5505   -935       C  
ATOM   3712  O   ALA A 477     143.151  44.204  30.511  1.00155.99           O  
ANISOU 3712  O   ALA A 477    15995  20195  23080   1142   5645  -1136       O  
ATOM   3713  CB  ALA A 477     142.371  47.223  29.287  1.00136.18           C  
ANISOU 3713  CB  ALA A 477    13990  18259  19493    599   5638   -896       C  
ATOM   3714  N   THR A 478     141.831  45.501  31.787  1.00142.61           N  
ANISOU 3714  N   THR A 478    14696  18494  20995   1106   5213   -622       N  
ATOM   3715  CA  THR A 478     142.264  44.896  33.040  1.00145.67           C  
ANISOU 3715  CA  THR A 478    14918  18648  21782   1323   5027   -481       C  
ATOM   3716  C   THR A 478     141.446  43.642  33.343  1.00142.06           C  
ANISOU 3716  C   THR A 478    14511  17949  21518   1479   4966   -534       C  
ATOM   3717  O   THR A 478     141.332  43.219  34.494  1.00140.29           O  
ANISOU 3717  O   THR A 478    14263  17518  21521   1632   4743   -350       O  
ATOM   3718  CB  THR A 478     142.160  45.891  34.213  1.00151.94           C  
ANISOU 3718  CB  THR A 478    15822  19444  22465   1320   4741   -122       C  
ATOM   3719  CG2 THR A 478     142.942  45.390  35.419  1.00155.20           C  
ANISOU 3719  CG2 THR A 478    16016  19659  23295   1506   4572     16       C  
ATOM   3720  OG1 THR A 478     142.688  47.160  33.808  1.00156.02           O  
ANISOU 3720  OG1 THR A 478    16357  20204  22721   1143   4797    -68       O  
ATOM   3721  N   GLY A 479     140.875  43.054  32.296  1.00140.54           N  
ANISOU 3721  N   GLY A 479    14392  17785  21223   1424   5164   -786       N  
ATOM   3722  CA  GLY A 479     140.126  41.817  32.421  1.00141.00           C  
ANISOU 3722  CA  GLY A 479    14491  17624  21459   1557   5143   -877       C  
ATOM   3723  C   GLY A 479     138.992  41.876  33.426  1.00137.33           C  
ANISOU 3723  C   GLY A 479    14261  17028  20890   1613   4860   -608       C  
ATOM   3724  O   GLY A 479     138.587  40.853  33.979  1.00138.12           O  
ANISOU 3724  O   GLY A 479    14352  16899  21228   1762   4765   -602       O  
ATOM   3725  N   GLN A 480     138.475  43.077  33.666  1.00130.10           N  
ANISOU 3725  N   GLN A 480    13553  16255  19623   1488   4727   -389       N  
ATOM   3726  CA  GLN A 480     137.357  43.250  34.583  1.00120.83           C  
ANISOU 3726  CA  GLN A 480    12609  14981  18319   1517   4475   -146       C  
ATOM   3727  C   GLN A 480     136.039  43.296  33.819  1.00112.16           C  
ANISOU 3727  C   GLN A 480    11774  13953  16889   1407   4528   -224       C  
ATOM   3728  O   GLN A 480     135.355  44.319  33.798  1.00110.66           O  
ANISOU 3728  O   GLN A 480    11792  13891  16362   1280   4437    -78       O  
ATOM   3729  CB  GLN A 480     137.533  44.521  35.415  1.00124.99           C  
ANISOU 3729  CB  GLN A 480    13203  15597  18691   1456   4280    144       C  
ATOM   3730  CG  GLN A 480     138.810  44.550  36.239  1.00132.65           C  
ANISOU 3730  CG  GLN A 480    13926  16504  19972   1551   4201    250       C  
ATOM   3731  CD  GLN A 480     138.917  45.792  37.104  1.00138.69           C  
ANISOU 3731  CD  GLN A 480    14775  17351  20571   1483   4003    540       C  
ATOM   3732  NE2 GLN A 480     140.146  46.202  37.401  1.00142.96           N  
ANISOU 3732  NE2 GLN A 480    15112  17943  21265   1491   3999    598       N  
ATOM   3733  OE1 GLN A 480     137.908  46.375  37.504  1.00135.94           O  
ANISOU 3733  OE1 GLN A 480    14666  17018  19967   1421   3856    703       O  
ATOM   3734  N   VAL A 481     135.690  42.180  33.190  1.00110.76           N  
ANISOU 3734  N   VAL A 481    11579  13685  16820   1454   4671   -455       N  
ATOM   3735  CA  VAL A 481     134.447  42.082  32.436  1.00112.47           C  
ANISOU 3735  CA  VAL A 481    12030  13955  16747   1354   4726   -545       C  
ATOM   3736  C   VAL A 481     133.523  41.030  33.039  1.00109.91           C  
ANISOU 3736  C   VAL A 481    11791  13401  16569   1487   4607   -523       C  
ATOM   3737  O   VAL A 481     133.806  40.477  34.103  1.00108.61           O  
ANISOU 3737  O   VAL A 481    11524  13040  16702   1643   4458   -408       O  
ATOM   3738  CB  VAL A 481     134.707  41.737  30.959  1.00116.56           C  
ANISOU 3738  CB  VAL A 481    12494  14604  17189   1245   5029   -866       C  
ATOM   3739  CG1 VAL A 481     135.488  42.855  30.284  1.00116.74           C  
ANISOU 3739  CG1 VAL A 481    12473  14880  17005   1073   5147   -884       C  
ATOM   3740  CG2 VAL A 481     135.448  40.415  30.848  1.00117.24           C  
ANISOU 3740  CG2 VAL A 481    12332  14525  17689   1394   5178  -1098       C  
ATOM   3741  N   CYS A 482     132.418  40.756  32.355  1.00110.25           N  
ANISOU 3741  N   CYS A 482    12025  13470  16397   1413   4665   -628       N  
ATOM   3742  CA  CYS A 482     131.451  39.775  32.831  1.00112.03           C  
ANISOU 3742  CA  CYS A 482    12350  13493  16724   1518   4564   -620       C  
ATOM   3743  C   CYS A 482     131.991  38.355  32.704  1.00118.85           C  
ANISOU 3743  C   CYS A 482    13017  14170  17970   1662   4688   -834       C  
ATOM   3744  O   CYS A 482     132.643  38.014  31.717  1.00122.94           O  
ANISOU 3744  O   CYS A 482    13399  14756  18558   1628   4931  -1089       O  
ATOM   3745  CB  CYS A 482     130.132  39.905  32.068  1.00105.34           C  
ANISOU 3745  CB  CYS A 482    11753  12735  15534   1389   4598   -680       C  
ATOM   3746  SG  CYS A 482     129.288  41.482  32.309  1.00154.39           S  
ANISOU 3746  SG  CYS A 482    18208  19118  21334   1239   4414   -420       S  
ATOM   3747  N   HIS A 483     131.715  37.531  33.710  1.00118.19           N  
ANISOU 3747  N   HIS A 483    12921  13849  18137   1814   4520   -733       N  
ATOM   3748  CA  HIS A 483     132.161  36.144  33.709  1.00119.71           C  
ANISOU 3748  CA  HIS A 483    12935  13827  18724   1965   4599   -910       C  
ATOM   3749  C   HIS A 483     131.635  35.402  32.485  1.00112.69           C  
ANISOU 3749  C   HIS A 483    12101  12961  17757   1910   4831  -1210       C  
ATOM   3750  O   HIS A 483     130.604  35.767  31.923  1.00106.05           O  
ANISOU 3750  O   HIS A 483    11484  12243  16567   1779   4855  -1224       O  
ATOM   3751  CB  HIS A 483     131.712  35.439  34.990  1.00124.46           C  
ANISOU 3751  CB  HIS A 483    13572  14174  19542   2105   4350   -723       C  
ATOM   3752  CG  HIS A 483     132.342  34.097  35.192  1.00132.19           C  
ANISOU 3752  CG  HIS A 483    14341  14906  20981   2275   4381   -854       C  
ATOM   3753  CD2 HIS A 483     133.587  33.748  35.597  1.00134.48           C  
ANISOU 3753  CD2 HIS A 483    14360  15079  21658   2397   4369   -859       C  
ATOM   3754  ND1 HIS A 483     131.668  32.916  34.965  1.00132.77           N  
ANISOU 3754  ND1 HIS A 483    14468  14811  21169   2335   4422  -1001       N  
ATOM   3755  CE1 HIS A 483     132.469  31.898  35.225  1.00133.78           C  
ANISOU 3755  CE1 HIS A 483    14368  14721  21741   2491   4432  -1092       C  
ATOM   3756  NE2 HIS A 483     133.639  32.376  35.609  1.00135.72           N  
ANISOU 3756  NE2 HIS A 483    14410  14992  22166   2533   4398  -1007       N  
ATOM   3757  N   ALA A 484     132.352  34.360  32.078  1.00112.90           N  
ANISOU 3757  N   ALA A 484    11917  12864  18117   2007   4999  -1452       N  
ATOM   3758  CA  ALA A 484     131.987  33.591  30.893  1.00112.68           C  
ANISOU 3758  CA  ALA A 484    11915  12852  18046   1952   5244  -1767       C  
ATOM   3759  C   ALA A 484     130.617  32.933  31.031  1.00111.52           C  
ANISOU 3759  C   ALA A 484    11991  12586  17794   1962   5149  -1745       C  
ATOM   3760  O   ALA A 484     129.953  32.650  30.034  1.00107.70           O  
ANISOU 3760  O   ALA A 484    11627  12180  17113   1857   5312  -1942       O  
ATOM   3761  CB  ALA A 484     133.050  32.546  30.595  1.00119.51           C  
ANISOU 3761  CB  ALA A 484    12489  13570  19349   2077   5422  -2024       C  
ATOM   3762  N   LEU A 485     130.198  32.691  32.268  1.00117.77           N  
ANISOU 3762  N   LEU A 485    12841  13195  18712   2076   4886  -1506       N  
ATOM   3763  CA  LEU A 485     128.908  32.060  32.521  1.00125.54           C  
ANISOU 3763  CA  LEU A 485    14030  14056  19611   2088   4779  -1468       C  
ATOM   3764  C   LEU A 485     127.776  33.083  32.516  1.00124.63           C  
ANISOU 3764  C   LEU A 485    14186  14119  19047   1939   4672  -1300       C  
ATOM   3765  O   LEU A 485     126.600  32.723  32.588  1.00125.96           O  
ANISOU 3765  O   LEU A 485    14546  14233  19080   1916   4601  -1279       O  
ATOM   3766  CB  LEU A 485     128.931  31.304  33.852  1.00130.37           C  
ANISOU 3766  CB  LEU A 485    14590  14390  20552   2257   4543  -1291       C  
ATOM   3767  CG  LEU A 485     129.936  30.155  33.967  1.00133.72           C  
ANISOU 3767  CG  LEU A 485    14751  14586  21472   2425   4605  -1439       C  
ATOM   3768  CD1 LEU A 485     129.949  29.595  35.381  1.00135.16           C  
ANISOU 3768  CD1 LEU A 485    14905  14510  21941   2565   4324  -1203       C  
ATOM   3769  CD2 LEU A 485     129.626  29.064  32.956  1.00133.38           C  
ANISOU 3769  CD2 LEU A 485    14699  14469  21511   2432   4827  -1761       C  
ATOM   3770  N   CYS A 486     128.135  34.359  32.430  1.00122.35           N  
ANISOU 3770  N   CYS A 486    13909  14038  18541   1838   4660  -1184       N  
ATOM   3771  CA  CYS A 486     127.145  35.429  32.427  1.00121.91           C  
ANISOU 3771  CA  CYS A 486    14090  14147  18084   1700   4551  -1020       C  
ATOM   3772  C   CYS A 486     126.471  35.569  31.067  1.00123.33           C  
ANISOU 3772  C   CYS A 486    14410  14499  17951   1536   4733  -1212       C  
ATOM   3773  O   CYS A 486     127.136  35.743  30.045  1.00124.35           O  
ANISOU 3773  O   CYS A 486    14451  14772  18026   1448   4947  -1399       O  
ATOM   3774  CB  CYS A 486     127.782  36.760  32.835  1.00121.59           C  
ANISOU 3774  CB  CYS A 486    14013  14255  17932   1647   4462   -822       C  
ATOM   3775  SG  CYS A 486     128.338  36.835  34.553  1.00187.41           S  
ANISOU 3775  SG  CYS A 486    22245  22417  26543   1796   4197   -535       S  
ATOM   3776  N   SER A 487     125.146  35.485  31.064  1.00122.35           N  
ANISOU 3776  N   SER A 487    14504  14363  17622   1485   4644  -1166       N  
ATOM   3777  CA  SER A 487     124.365  35.713  29.857  1.00122.24           C  
ANISOU 3777  CA  SER A 487    14649  14515  17281   1314   4771  -1304       C  
ATOM   3778  C   SER A 487     124.503  37.168  29.425  1.00120.59           C  
ANISOU 3778  C   SER A 487    14505  14550  16763   1154   4762  -1200       C  
ATOM   3779  O   SER A 487     124.829  38.029  30.241  1.00121.12           O  
ANISOU 3779  O   SER A 487    14549  14639  16830   1181   4608   -980       O  
ATOM   3780  CB  SER A 487     122.896  35.375  30.114  1.00122.92           C  
ANISOU 3780  CB  SER A 487    14947  14524  17233   1305   4639  -1241       C  
ATOM   3781  OG  SER A 487     122.062  35.865  29.080  1.00125.10           O  
ANISOU 3781  OG  SER A 487    15398  14978  17158   1125   4703  -1307       O  
ATOM   3782  N   PRO A 488     124.265  37.446  28.133  1.00119.70           N  
ANISOU 3782  N   PRO A 488    14476  14620  16383    976   4923  -1356       N  
ATOM   3783  CA  PRO A 488     124.311  38.812  27.599  1.00121.04           C  
ANISOU 3783  CA  PRO A 488    14731  15025  16236    798   4911  -1261       C  
ATOM   3784  C   PRO A 488     123.469  39.795  28.412  1.00124.91           C  
ANISOU 3784  C   PRO A 488    15377  15525  16557    788   4649   -974       C  
ATOM   3785  O   PRO A 488     123.573  41.006  28.209  1.00125.06           O  
ANISOU 3785  O   PRO A 488    15452  15708  16359    668   4596   -852       O  
ATOM   3786  CB  PRO A 488     123.720  38.650  26.198  1.00118.31           C  
ANISOU 3786  CB  PRO A 488    14512  14817  15625    612   5075  -1461       C  
ATOM   3787  CG  PRO A 488     124.077  37.261  25.811  1.00122.09           C  
ANISOU 3787  CG  PRO A 488    14868  15174  16344    689   5276  -1732       C  
ATOM   3788  CD  PRO A 488     124.030  36.448  27.075  1.00121.34           C  
ANISOU 3788  CD  PRO A 488    14697  14822  16587    922   5136  -1642       C  
ATOM   3789  N   GLU A 489     122.649  39.275  29.321  1.00123.40           N  
ANISOU 3789  N   GLU A 489    15255  15161  16472    906   4490   -875       N  
ATOM   3790  CA  GLU A 489     121.794  40.109  30.158  1.00120.92           C  
ANISOU 3790  CA  GLU A 489    15079  14841  16025    901   4251   -626       C  
ATOM   3791  C   GLU A 489     122.617  41.108  30.971  1.00121.95           C  
ANISOU 3791  C   GLU A 489    15122  15008  16206    932   4141   -427       C  
ATOM   3792  O   GLU A 489     122.103  42.139  31.402  1.00123.45           O  
ANISOU 3792  O   GLU A 489    15420  15256  16230    879   3979   -236       O  
ATOM   3793  CB  GLU A 489     120.957  39.238  31.097  1.00125.09           C  
ANISOU 3793  CB  GLU A 489    15661  15162  16705   1030   4121   -574       C  
ATOM   3794  CG  GLU A 489     119.677  39.896  31.598  1.00126.49           C  
ANISOU 3794  CG  GLU A 489    16024  15348  16688    983   3922   -400       C  
ATOM   3795  CD  GLU A 489     118.441  39.429  30.851  1.00126.88           C  
ANISOU 3795  CD  GLU A 489    16231  15408  16568    904   3952   -514       C  
ATOM   3796  OE1 GLU A 489     118.065  38.247  30.997  1.00125.87           O  
ANISOU 3796  OE1 GLU A 489    16105  15135  16584    984   3984   -619       O  
ATOM   3797  OE2 GLU A 489     117.835  40.248  30.130  1.00128.43           O1-
ANISOU 3797  OE2 GLU A 489    16551  15754  16492    759   3933   -492       O1-
ATOM   3798  N   GLY A 490     123.893  40.797  31.181  1.00121.76           N  
ANISOU 3798  N   GLY A 490    14896  14945  16421   1018   4229   -476       N  
ATOM   3799  CA  GLY A 490     124.781  41.674  31.926  1.00114.06           C  
ANISOU 3799  CA  GLY A 490    13821  14006  15510   1046   4137   -298       C  
ATOM   3800  C   GLY A 490     125.317  41.038  33.195  1.00107.57           C  
ANISOU 3800  C   GLY A 490    12865  12986  15022   1225   4033   -205       C  
ATOM   3801  O   GLY A 490     125.075  39.859  33.456  1.00115.54           O  
ANISOU 3801  O   GLY A 490    13846  13823  16231   1332   4041   -288       O  
ATOM   3802  N   CYS A 491     126.047  41.817  33.988  1.00 92.94           N  
ANISOU 3802  N   CYS A 491    10932  11154  13227   1249   3925    -24       N  
ATOM   3803  CA  CYS A 491     126.615  41.313  35.235  1.00 92.82           C  
ANISOU 3803  CA  CYS A 491    10791  10962  13517   1399   3803     93       C  
ATOM   3804  C   CYS A 491     126.790  42.416  36.275  1.00 90.78           C  
ANISOU 3804  C   CYS A 491    10556  10738  13200   1382   3612    354       C  
ATOM   3805  O   CYS A 491     127.159  43.541  35.943  1.00 84.63           O  
ANISOU 3805  O   CYS A 491     9784  10127  12245   1281   3630    412       O  
ATOM   3806  CB  CYS A 491     127.958  40.628  34.973  1.00103.47           C  
ANISOU 3806  CB  CYS A 491    11893  12263  15159   1486   3952    -50       C  
ATOM   3807  SG  CYS A 491     129.251  41.716  34.326  1.00118.54           S  
ANISOU 3807  SG  CYS A 491    13662  14391  16986   1389   4081    -72       S  
ATOM   3808  N   TRP A 492     126.527  42.083  37.535  1.00 92.89           N  
ANISOU 3808  N   TRP A 492    10838  10843  13611   1468   3431    509       N  
ATOM   3809  CA  TRP A 492     126.673  43.033  38.635  1.00 92.49           C  
ANISOU 3809  CA  TRP A 492    10812  10809  13522   1448   3246    752       C  
ATOM   3810  C   TRP A 492     128.077  42.994  39.224  1.00 97.82           C  
ANISOU 3810  C   TRP A 492    11276  11441  14450   1523   3224    826       C  
ATOM   3811  O   TRP A 492     128.362  43.669  40.215  1.00 95.89           O  
ANISOU 3811  O   TRP A 492    11027  11194  14213   1513   3070   1028       O  
ATOM   3812  CB  TRP A 492     125.653  42.745  39.734  1.00 86.58           C  
ANISOU 3812  CB  TRP A 492    10198   9922  12777   1474   3059    886       C  
ATOM   3813  CG  TRP A 492     124.244  42.990  39.323  1.00 84.71           C  
ANISOU 3813  CG  TRP A 492    10166   9736  12285   1393   3049    850       C  
ATOM   3814  CD1 TRP A 492     123.306  42.052  39.013  1.00 87.61           C  
ANISOU 3814  CD1 TRP A 492    10621  10015  12650   1416   3082    729       C  
ATOM   3815  CD2 TRP A 492     123.606  44.262  39.175  1.00 85.58           C  
ANISOU 3815  CD2 TRP A 492    10413   9988  12115   1276   2994    936       C  
ATOM   3816  CE2 TRP A 492     122.278  44.018  38.773  1.00 89.94           C  
ANISOU 3816  CE2 TRP A 492    11126  10532  12516   1235   2993    862       C  
ATOM   3817  CE3 TRP A 492     124.028  45.583  39.344  1.00 84.58           C  
ANISOU 3817  CE3 TRP A 492    10286   9989  11861   1200   2941   1068       C  
ATOM   3818  NE1 TRP A 492     122.120  42.660  38.681  1.00 90.83           N  
ANISOU 3818  NE1 TRP A 492    11208  10509  12795   1319   3051    736       N  
ATOM   3819  CZ2 TRP A 492     121.370  45.046  38.538  1.00 89.12           C  
ANISOU 3819  CZ2 TRP A 492    11171  10535  12156   1129   2934    917       C  
ATOM   3820  CZ3 TRP A 492     123.126  46.602  39.109  1.00 83.54           C  
ANISOU 3820  CZ3 TRP A 492    10308   9959  11473   1094   2884   1121       C  
ATOM   3821  CH2 TRP A 492     121.812  46.328  38.711  1.00 87.02           C  
ANISOU 3821  CH2 TRP A 492    10897  10381  11784   1062   2878   1046       C  
ATOM   3822  N   GLY A 493     128.946  42.198  38.610  1.00102.65           N  
ANISOU 3822  N   GLY A 493    11709  12017  15277   1594   3379    654       N  
ATOM   3823  CA  GLY A 493     130.312  42.052  39.076  1.00105.97           C  
ANISOU 3823  CA  GLY A 493    11902  12385  15975   1676   3369    698       C  
ATOM   3824  C   GLY A 493     131.071  40.999  38.294  1.00114.78           C  
ANISOU 3824  C   GLY A 493    12825  13438  17348   1762   3560    460       C  
ATOM   3825  O   GLY A 493     130.558  40.454  37.317  1.00120.89           O  
ANISOU 3825  O   GLY A 493    13651  14230  18053   1742   3717    253       O  
ATOM   3826  N   PRO A 494     132.303  40.704  38.727  1.00116.07           N  
ANISOU 3826  N   PRO A 494    12757  13524  17819   1856   3547    484       N  
ATOM   3827  CA  PRO A 494     133.198  39.768  38.039  1.00116.07           C  
ANISOU 3827  CA  PRO A 494    12531  13459  18111   1946   3732    252       C  
ATOM   3828  C   PRO A 494     132.821  38.319  38.317  1.00119.67           C  
ANISOU 3828  C   PRO A 494    12963  13668  18839   2077   3698    172       C  
ATOM   3829  O   PRO A 494     132.927  37.468  37.435  1.00120.88           O  
ANISOU 3829  O   PRO A 494    13033  13778  19117   2118   3888    -81       O  
ATOM   3830  CB  PRO A 494     134.569  40.068  38.666  1.00113.38           C  
ANISOU 3830  CB  PRO A 494    11961  13104  18015   2003   3669    364       C  
ATOM   3831  CG  PRO A 494     134.379  41.301  39.516  1.00110.09           C  
ANISOU 3831  CG  PRO A 494    11672  12785  17371   1915   3479    641       C  
ATOM   3832  CD  PRO A 494     132.946  41.307  39.903  1.00112.91           C  
ANISOU 3832  CD  PRO A 494    12292  13100  17509   1873   3354    734       C  
ATOM   3833  N   GLU A 495     132.380  38.055  39.542  1.00121.80           N  
ANISOU 3833  N   GLU A 495    13309  13777  19192   2129   3458    384       N  
ATOM   3834  CA  GLU A 495     132.090  36.699  39.997  1.00127.73           C  
ANISOU 3834  CA  GLU A 495    14037  14273  20223   2251   3381    353       C  
ATOM   3835  C   GLU A 495     130.888  36.076  39.288  1.00122.00           C  
ANISOU 3835  C   GLU A 495    13485  13527  19343   2224   3482    185       C  
ATOM   3836  O   GLU A 495     130.013  36.787  38.795  1.00120.97           O  
ANISOU 3836  O   GLU A 495    13547  13561  18854   2103   3528    174       O  
ATOM   3837  CB  GLU A 495     131.865  36.706  41.510  1.00139.25           C  
ANISOU 3837  CB  GLU A 495    15563  15593  21753   2274   3088    644       C  
ATOM   3838  CG  GLU A 495     132.988  37.378  42.284  1.00153.25           C  
ANISOU 3838  CG  GLU A 495    17184  17392  23651   2282   2967    835       C  
ATOM   3839  CD  GLU A 495     132.520  37.997  43.587  1.00161.61           C  
ANISOU 3839  CD  GLU A 495    18396  18439  24571   2214   2710   1132       C  
ATOM   3840  OE1 GLU A 495     133.310  38.741  44.207  1.00164.68           O  
ANISOU 3840  OE1 GLU A 495    18700  18884  24987   2189   2609   1301       O  
ATOM   3841  OE2 GLU A 495     131.364  37.748  43.988  1.00162.59           O1-
ANISOU 3841  OE2 GLU A 495    18722  18501  24552   2177   2615   1188       O1-
ATOM   3842  N   PRO A 496     130.849  34.735  39.235  1.00118.76           N  
ANISOU 3842  N   PRO A 496    13002  12906  19216   2337   3508     54       N  
ATOM   3843  CA  PRO A 496     129.744  33.988  38.621  1.00117.48           C  
ANISOU 3843  CA  PRO A 496    12993  12695  18948   2321   3596   -110       C  
ATOM   3844  C   PRO A 496     128.433  34.153  39.388  1.00117.30           C  
ANISOU 3844  C   PRO A 496    13226  12644  18698   2261   3404     74       C  
ATOM   3845  O   PRO A 496     127.378  33.752  38.896  1.00118.65           O  
ANISOU 3845  O   PRO A 496    13556  12813  18713   2221   3463    -36       O  
ATOM   3846  CB  PRO A 496     130.216  32.531  38.705  1.00115.79           C  
ANISOU 3846  CB  PRO A 496    12610  12222  19165   2475   3615   -238       C  
ATOM   3847  CG  PRO A 496     131.694  32.608  38.872  1.00118.33           C  
ANISOU 3847  CG  PRO A 496    12654  12513  19793   2558   3631   -233       C  
ATOM   3848  CD  PRO A 496     131.933  33.843  39.678  1.00119.07           C  
ANISOU 3848  CD  PRO A 496    12789  12736  19715   2487   3466     39       C  
ATOM   3849  N   ARG A 497     128.507  34.734  40.580  1.00117.99           N  
ANISOU 3849  N   ARG A 497    13349  12713  18770   2246   3182    343       N  
ATOM   3850  CA  ARG A 497     127.324  34.964  41.403  1.00118.32           C  
ANISOU 3850  CA  ARG A 497    13619  12735  18603   2176   3000    519       C  
ATOM   3851  C   ARG A 497     126.707  36.324  41.095  1.00112.04           C  
ANISOU 3851  C   ARG A 497    12983  12180  17408   2035   3024    575       C  
ATOM   3852  O   ARG A 497     125.621  36.649  41.576  1.00105.20           O  
ANISOU 3852  O   ARG A 497    12311  11332  16328   1962   2911    681       O  
ATOM   3853  CB  ARG A 497     127.692  34.885  42.887  1.00124.81           C  
ANISOU 3853  CB  ARG A 497    14404  13411  19605   2211   2746    779       C  
ATOM   3854  CG  ARG A 497     128.910  35.720  43.256  1.00134.15           C  
ANISOU 3854  CG  ARG A 497    15427  14675  20868   2213   2702    907       C  
ATOM   3855  CD  ARG A 497     129.341  35.509  44.701  1.00136.25           C  
ANISOU 3855  CD  ARG A 497    15646  14781  21340   2243   2446   1158       C  
ATOM   3856  NE  ARG A 497     128.529  36.273  45.643  1.00131.53           N  
ANISOU 3856  NE  ARG A 497    15249  14244  20481   2124   2275   1370       N  
ATOM   3857  CZ  ARG A 497     128.866  36.491  46.910  1.00133.30           C  
ANISOU 3857  CZ  ARG A 497    15467  14401  20778   2095   2055   1613       C  
ATOM   3858  NH1 ARG A 497     130.004  36.006  47.388  1.00137.31           N1+
ANISOU 3858  NH1 ARG A 497    15776  14775  21620   2181   1964   1691       N1+
ATOM   3859  NH2 ARG A 497     128.069  37.197  47.699  1.00132.56           N  
ANISOU 3859  NH2 ARG A 497    15562  14374  20431   1972   1927   1775       N  
ATOM   3860  N   ASP A 498     127.407  37.110  40.283  1.00111.11           N  
ANISOU 3860  N   ASP A 498    12777  12243  17199   1995   3171    497       N  
ATOM   3861  CA  ASP A 498     127.001  38.480  39.990  1.00107.58           C  
ANISOU 3861  CA  ASP A 498    12457  12017  16400   1862   3181    564       C  
ATOM   3862  C   ASP A 498     126.233  38.594  38.677  1.00108.21           C  
ANISOU 3862  C   ASP A 498    12655  12233  16228   1778   3358    369       C  
ATOM   3863  O   ASP A 498     125.939  39.697  38.219  1.00106.67           O  
ANISOU 3863  O   ASP A 498    12556  12225  15749   1662   3384    399       O  
ATOM   3864  CB  ASP A 498     128.226  39.396  39.948  1.00108.89           C  
ANISOU 3864  CB  ASP A 498    12472  12311  16589   1843   3212    627       C  
ATOM   3865  CG  ASP A 498     128.992  39.406  41.255  1.00108.69           C  
ANISOU 3865  CG  ASP A 498    12337  12170  16790   1906   3023    839       C  
ATOM   3866  OD1 ASP A 498     130.171  39.823  41.254  1.00106.14           O  
ANISOU 3866  OD1 ASP A 498    11841  11904  16585   1924   3053    867       O  
ATOM   3867  OD2 ASP A 498     128.415  38.997  42.284  1.00109.36           O1-
ANISOU 3867  OD2 ASP A 498    12511  12113  16930   1927   2842    979       O1-
ATOM   3868  N   CYS A 499     125.910  37.456  38.072  1.00107.63           N  
ANISOU 3868  N   CYS A 499    12576  12060  16260   1828   3471    174       N  
ATOM   3869  CA  CYS A 499     125.196  37.452  36.799  1.00108.41           C  
ANISOU 3869  CA  CYS A 499    12784  12278  16127   1740   3641    -21       C  
ATOM   3870  C   CYS A 499     123.744  37.896  36.943  1.00111.49           C  
ANISOU 3870  C   CYS A 499    13415  12717  16229   1649   3535     65       C  
ATOM   3871  O   CYS A 499     123.073  37.550  37.916  1.00116.84           O  
ANISOU 3871  O   CYS A 499    14178  13264  16954   1685   3371    188       O  
ATOM   3872  CB  CYS A 499     125.256  36.067  36.151  1.00106.80           C  
ANISOU 3872  CB  CYS A 499    12506  11945  16128   1816   3792   -260       C  
ATOM   3873  SG  CYS A 499     126.785  35.731  35.256  1.00 97.32           S  
ANISOU 3873  SG  CYS A 499    11037  10777  15161   1864   4031   -482       S  
ATOM   3874  N   VAL A 500     123.267  38.667  35.970  1.00109.51           N  
ANISOU 3874  N   VAL A 500    13270  12655  15682   1522   3625     -1       N  
ATOM   3875  CA  VAL A 500     121.866  39.065  35.931  1.00105.91           C  
ANISOU 3875  CA  VAL A 500    13030  12249  14964   1434   3540     51       C  
ATOM   3876  C   VAL A 500     121.011  37.859  35.562  1.00108.99           C  
ANISOU 3876  C   VAL A 500    13494  12525  15393   1462   3596   -105       C  
ATOM   3877  O   VAL A 500     120.047  37.530  36.253  1.00109.61           O  
ANISOU 3877  O   VAL A 500    13687  12500  15458   1479   3466    -28       O  
ATOM   3878  CB  VAL A 500     121.619  40.187  34.908  1.00 97.80           C  
ANISOU 3878  CB  VAL A 500    12089  11445  13624   1284   3611     24       C  
ATOM   3879  CG1 VAL A 500     120.143  40.535  34.861  1.00 80.54           C  
ANISOU 3879  CG1 VAL A 500    10110   9291  11201   1203   3513     72       C  
ATOM   3880  CG2 VAL A 500     122.450  41.414  35.251  1.00 93.00           C  
ANISOU 3880  CG2 VAL A 500    11415  10950  12968   1248   3555    179       C  
ATOM   3881  N   SER A 501     121.376  37.208  34.462  1.00114.08           N  
ANISOU 3881  N   SER A 501    18739  12344  12263   6743  -2895   1577       N  
ATOM   3882  CA  SER A 501     120.750  35.957  34.057  1.00121.51           C  
ANISOU 3882  CA  SER A 501    19709  13234  13225   6485  -2840   1346       C  
ATOM   3883  C   SER A 501     121.845  34.959  33.709  1.00129.22           C  
ANISOU 3883  C   SER A 501    20905  13725  14469   6479  -2719   1535       C  
ATOM   3884  O   SER A 501     122.929  35.347  33.275  1.00133.50           O  
ANISOU 3884  O   SER A 501    21577  14029  15118   6766  -2684   1737       O  
ATOM   3885  CB  SER A 501     119.820  36.168  32.861  1.00126.00           C  
ANISOU 3885  CB  SER A 501    20211  14093  13570   6624  -2878    953       C  
ATOM   3886  OG  SER A 501     120.552  36.314  31.658  1.00 94.99           O  
ANISOU 3886  OG  SER A 501    16426   9981   9685   6958  -2831    958       O  
ATOM   3887  N   CYS A 502     121.562  33.676  33.902  1.00133.73           N  
ANISOU 3887  N   CYS A 502    21516  14147  15147   6152  -2656   1471       N  
ATOM   3888  CA  CYS A 502     122.567  32.640  33.699  1.00135.67           C  
ANISOU 3888  CA  CYS A 502    21965  13927  15657   6101  -2543   1659       C  
ATOM   3889  C   CYS A 502     122.627  32.164  32.253  1.00139.08           C  
ANISOU 3889  C   CYS A 502    22505  14253  16088   6266  -2490   1453       C  
ATOM   3890  O   CYS A 502     121.625  32.188  31.535  1.00130.14           O  
ANISOU 3890  O   CYS A 502    21279  13401  14766   6278  -2527   1112       O  
ATOM   3891  CB  CYS A 502     122.307  31.455  34.631  1.00136.73           C  
ANISOU 3891  CB  CYS A 502    22099  13926  15924   5667  -2496   1709       C  
ATOM   3892  SG  CYS A 502     122.266  31.888  36.384  1.00181.38           S  
ANISOU 3892  SG  CYS A 502    27639  19677  21599   5447  -2550   1963       S  
ATOM   3893  N   ARG A 503     123.813  31.735  31.833  1.00151.16           N  
ANISOU 3893  N   ARG A 503    24229  15373  17831   6396  -2404   1664       N  
ATOM   3894  CA  ARG A 503     124.002  31.164  30.505  1.00161.83           C  
ANISOU 3894  CA  ARG A 503    25703  16569  19218   6538  -2342   1505       C  
ATOM   3895  C   ARG A 503     123.287  29.825  30.392  1.00170.84           C  
ANISOU 3895  C   ARG A 503    26841  17674  20396   6203  -2295   1291       C  
ATOM   3896  O   ARG A 503     122.294  29.698  29.675  1.00171.84           O  
ANISOU 3896  O   ARG A 503    26884  18054  20355   6189  -2323    948       O  
ATOM   3897  CB  ARG A 503     125.492  30.981  30.205  1.00163.84           C  
ANISOU 3897  CB  ARG A 503    26168  16373  19709   6731  -2259   1807       C  
ATOM   3898  CG  ARG A 503     126.125  32.132  29.441  1.00166.37           C  
ANISOU 3898  CG  ARG A 503    26534  16714  19966   7175  -2282   1870       C  
ATOM   3899  CD  ARG A 503     125.645  32.156  28.000  1.00169.37           C  
ANISOU 3899  CD  ARG A 503    26921  17230  20202   7381  -2283   1552       C  
ATOM   3900  NE  ARG A 503     126.336  33.164  27.202  1.00169.41           N  
ANISOU 3900  NE  ARG A 503    26990  17213  20166   7810  -2292   1623       N  
ATOM   3901  CZ  ARG A 503     126.155  33.334  25.897  1.00172.63           C  
ANISOU 3901  CZ  ARG A 503    27430  17697  20464   8060  -2288   1399       C  
ATOM   3902  NH1 ARG A 503     126.825  34.276  25.248  1.00171.63           N1+
ANISOU 3902  NH1 ARG A 503    27363  17542  20307   8448  -2294   1486       N1+
ATOM   3903  NH2 ARG A 503     125.302  32.561  25.239  1.00176.58           N  
ANISOU 3903  NH2 ARG A 503    27902  18303  20886   7925  -2277   1086       N  
ATOM   3904  N   ASN A 504     123.797  28.829  31.109  1.00177.24           N  
ANISOU 3904  N   ASN A 504    27744  18168  21430   5934  -2224   1495       N  
ATOM   3905  CA  ASN A 504     123.229  27.488  31.069  1.00186.20           C  
ANISOU 3905  CA  ASN A 504    28889  19225  22632   5603  -2170   1327       C  
ATOM   3906  C   ASN A 504     122.244  27.241  32.209  1.00176.66           C  
ANISOU 3906  C   ASN A 504    27522  18247  21352   5234  -2211   1256       C  
ATOM   3907  O   ASN A 504     121.031  27.349  32.026  1.00176.35           O  
ANISOU 3907  O   ASN A 504    27331  18562  21112   5145  -2266    942       O  
ATOM   3908  CB  ASN A 504     124.342  26.435  31.081  1.00204.83           C  
ANISOU 3908  CB  ASN A 504    31453  21091  25283   5519  -2062   1569       C  
ATOM   3909  CG  ASN A 504     125.291  26.575  29.903  1.00223.29           C  
ANISOU 3909  CG  ASN A 504    33953  23189  27697   5867  -2015   1623       C  
ATOM   3910  ND2 ASN A 504     126.253  25.665  29.804  1.00242.07           N  
ANISOU 3910  ND2 ASN A 504    36511  25141  30322   5812  -1923   1814       N  
ATOM   3911  OD1 ASN A 504     125.160  27.492  29.092  1.00223.23           O  
ANISOU 3911  OD1 ASN A 504    33910  23378  27530   6182  -2062   1495       O  
ATOM   3912  N   VAL A 505     122.771  26.913  33.384  1.00169.09           N  
ANISOU 3912  N   VAL A 505    26601  17086  20560   5024  -2182   1546       N  
ATOM   3913  CA  VAL A 505     121.935  26.652  34.552  1.00164.26           C  
ANISOU 3913  CA  VAL A 505    25849  16660  19901   4667  -2214   1516       C  
ATOM   3914  C   VAL A 505     122.456  27.385  35.783  1.00161.75           C  
ANISOU 3914  C   VAL A 505    25499  16331  19626   4664  -2252   1833       C  
ATOM   3915  O   VAL A 505     123.360  28.214  35.684  1.00159.82           O  
ANISOU 3915  O   VAL A 505    25321  15984  19421   4959  -2265   2046       O  
ATOM   3916  CB  VAL A 505     121.841  25.147  34.855  1.00164.22           C  
ANISOU 3916  CB  VAL A 505    25913  16413  20070   4299  -2128   1509       C  
ATOM   3917  CG1 VAL A 505     120.978  24.451  33.815  1.00165.10           C  
ANISOU 3917  CG1 VAL A 505    25998  16638  20096   4238  -2109   1136       C  
ATOM   3918  CG2 VAL A 505     123.229  24.529  34.908  1.00164.88           C  
ANISOU 3918  CG2 VAL A 505    26210  16003  20433   4332  -2036   1830       C  
ATOM   3919  N   SER A 506     121.886  27.073  36.944  1.00163.49           N  
ANISOU 3919  N   SER A 506    25619  16655  19843   4333  -2270   1864       N  
ATOM   3920  CA  SER A 506     122.235  27.782  38.170  1.00165.44           C  
ANISOU 3920  CA  SER A 506    25813  16937  20111   4310  -2315   2139       C  
ATOM   3921  C   SER A 506     122.104  26.921  39.423  1.00167.74           C  
ANISOU 3921  C   SER A 506    26092  17112  20529   3909  -2279   2277       C  
ATOM   3922  O   SER A 506     121.140  26.172  39.580  1.00169.13           O  
ANISOU 3922  O   SER A 506    26189  17420  20653   3612  -2270   2062       O  
ATOM   3923  CB  SER A 506     121.367  29.033  38.317  1.00167.05           C  
ANISOU 3923  CB  SER A 506    25817  17607  20048   4431  -2433   1981       C  
ATOM   3924  OG  SER A 506     119.995  28.689  38.398  1.00169.70           O  
ANISOU 3924  OG  SER A 506    25999  18260  20220   4178  -2469   1664       O  
ATOM   3925  N   ARG A 507     123.083  27.043  40.315  1.00168.20           N  
ANISOU 3925  N   ARG A 507    26229  16923  20754   3907  -2258   2637       N  
ATOM   3926  CA  ARG A 507     123.057  26.354  41.599  1.00168.84           C  
ANISOU 3926  CA  ARG A 507    26303  16891  20958   3552  -2229   2807       C  
ATOM   3927  C   ARG A 507     122.590  27.310  42.689  1.00166.99           C  
ANISOU 3927  C   ARG A 507    25897  16963  20587   3509  -2323   2876       C  
ATOM   3928  O   ARG A 507     123.405  27.926  43.377  1.00164.21           O  
ANISOU 3928  O   ARG A 507    25577  16500  20317   3625  -2341   3173       O  
ATOM   3929  CB  ARG A 507     124.447  25.822  41.952  1.00168.06           C  
ANISOU 3929  CB  ARG A 507    26405  16311  21141   3561  -2145   3167       C  
ATOM   3930  CG  ARG A 507     125.058  24.910  40.903  1.00169.13           C  
ANISOU 3930  CG  ARG A 507    26722  16110  21430   3624  -2051   3137       C  
ATOM   3931  CD  ARG A 507     124.536  23.488  41.017  1.00168.80           C  
ANISOU 3931  CD  ARG A 507    26705  15957  21474   3252  -1981   3010       C  
ATOM   3932  NE  ARG A 507     125.066  22.638  39.956  1.00166.40           N  
ANISOU 3932  NE  ARG A 507    26567  15352  21307   3319  -1898   2960       N  
ATOM   3933  CZ  ARG A 507     126.277  22.090  39.974  1.00162.00           C  
ANISOU 3933  CZ  ARG A 507    26201  14361  20990   3354  -1820   3228       C  
ATOM   3934  NH1 ARG A 507     127.088  22.303  41.001  1.00158.26           N1+
ANISOU 3934  NH1 ARG A 507    25780  13701  20650   3329  -1814   3563       N1+
ATOM   3935  NH2 ARG A 507     126.678  21.332  38.963  1.00162.99           N  
ANISOU 3935  NH2 ARG A 507    26464  14240  21225   3415  -1749   3157       N  
ATOM   3936  N   GLY A 508     121.277  27.437  42.840  1.00168.88           N  
ANISOU 3936  N   GLY A 508    25955  17590  20622   3343  -2385   2597       N  
ATOM   3937  CA  GLY A 508     120.715  28.318  43.846  1.00172.06           C  
ANISOU 3937  CA  GLY A 508    26182  18313  20879   3285  -2479   2630       C  
ATOM   3938  C   GLY A 508     120.892  29.784  43.501  1.00175.07           C  
ANISOU 3938  C   GLY A 508    26495  18913  21112   3659  -2569   2645       C  
ATOM   3939  O   GLY A 508     120.049  30.376  42.828  1.00178.02           O  
ANISOU 3939  O   GLY A 508    26750  19626  21266   3781  -2636   2360       O  
ATOM   3940  N   ARG A 509     121.992  30.371  43.961  1.00174.99           N  
ANISOU 3940  N   ARG A 509    26560  18707  21221   3844  -2570   2976       N  
ATOM   3941  CA  ARG A 509     122.256  31.787  43.724  1.00173.60           C  
ANISOU 3941  CA  ARG A 509    26323  18715  20924   4203  -2652   3025       C  
ATOM   3942  C   ARG A 509     123.541  32.004  42.930  1.00166.21           C  
ANISOU 3942  C   ARG A 509    25566  17454  20131   4540  -2600   3208       C  
ATOM   3943  O   ARG A 509     124.130  33.085  42.968  1.00162.34           O  
ANISOU 3943  O   ARG A 509    25066  16995  19618   4828  -2647   3366       O  
ATOM   3944  CB  ARG A 509     122.322  32.552  45.049  1.00176.79           C  
ANISOU 3944  CB  ARG A 509    26616  19249  21307   4152  -2721   3245       C  
ATOM   3945  CG  ARG A 509     123.475  32.141  45.950  1.00180.18           C  
ANISOU 3945  CG  ARG A 509    27180  19287  21994   4076  -2658   3632       C  
ATOM   3946  CD  ARG A 509     123.476  32.940  47.244  1.00181.82           C  
ANISOU 3946  CD  ARG A 509    27266  19650  22168   4035  -2733   3831       C  
ATOM   3947  NE  ARG A 509     124.616  32.603  48.091  1.00184.63           N  
ANISOU 3947  NE  ARG A 509    27753  19631  22769   3985  -2675   4203       N  
ATOM   3948  CZ  ARG A 509     124.622  31.610  48.976  1.00191.32           C  
ANISOU 3948  CZ  ARG A 509    28641  20300  23753   3649  -2620   4317       C  
ATOM   3949  NH1 ARG A 509     123.545  30.852  49.132  1.00193.87           N1+
ANISOU 3949  NH1 ARG A 509    28883  20786  23994   3328  -2613   4088       N1+
ATOM   3950  NH2 ARG A 509     125.704  31.375  49.704  1.00193.42           N  
ANISOU 3950  NH2 ARG A 509    29029  20224  24239   3634  -2571   4658       N  
ATOM   3951  N   GLU A 510     123.969  30.975  42.207  1.00161.88           N  
ANISOU 3951  N   GLU A 510    25181  16596  19731   4503  -2503   3184       N  
ATOM   3952  CA  GLU A 510     125.188  31.055  41.412  1.00154.91           C  
ANISOU 3952  CA  GLU A 510    24480  15381  18996   4804  -2445   3348       C  
ATOM   3953  C   GLU A 510     125.007  30.435  40.030  1.00149.35           C  
ANISOU 3953  C   GLU A 510    23861  14610  18276   4881  -2393   3097       C  
ATOM   3954  O   GLU A 510     124.384  29.384  39.891  1.00151.08           O  
ANISOU 3954  O   GLU A 510    24081  14814  18508   4613  -2350   2916       O  
ATOM   3955  CB  GLU A 510     126.344  30.369  42.141  1.00155.60           C  
ANISOU 3955  CB  GLU A 510    24730  15024  19365   4693  -2363   3701       C  
ATOM   3956  CG  GLU A 510     127.579  30.162  41.282  1.00159.25           C  
ANISOU 3956  CG  GLU A 510    25402  15098  20008   4946  -2286   3851       C  
ATOM   3957  CD  GLU A 510     128.692  29.456  42.026  1.00163.99           C  
ANISOU 3957  CD  GLU A 510    26162  15261  20886   4823  -2207   4192       C  
ATOM   3958  OE1 GLU A 510     128.730  29.556  43.270  1.00166.00           O  
ANISOU 3958  OE1 GLU A 510    26360  15529  21184   4652  -2231   4379       O  
ATOM   3959  OE2 GLU A 510     129.529  28.803  41.368  1.00166.05           O1-
ANISOU 3959  OE2 GLU A 510    26605  15166  21320   4901  -2123   4272       O1-
ATOM   3960  N   CYS A 511     125.553  31.093  39.012  1.00142.57           N  
ANISOU 3960  N   CYS A 511    23069  13712  17390   5251  -2396   3087       N  
ATOM   3961  CA  CYS A 511     125.516  30.566  37.654  1.00144.01           C  
ANISOU 3961  CA  CYS A 511    23345  13804  17567   5366  -2344   2874       C  
ATOM   3962  C   CYS A 511     126.644  29.565  37.432  1.00150.35           C  
ANISOU 3962  C   CYS A 511    24369  14112  18645   5339  -2232   3080       C  
ATOM   3963  O   CYS A 511     127.771  29.775  37.881  1.00152.54           O  
ANISOU 3963  O   CYS A 511    24753  14111  19093   5446  -2203   3403       O  
ATOM   3964  CB  CYS A 511     125.615  31.699  36.629  1.00141.63           C  
ANISOU 3964  CB  CYS A 511    23025  13673  17116   5780  -2394   2771       C  
ATOM   3965  SG  CYS A 511     124.124  32.706  36.463  1.00162.91           S  
ANISOU 3965  SG  CYS A 511    25472  16965  19460   5829  -2519   2423       S  
ATOM   3966  N   VAL A 512     126.335  28.475  36.737  1.00153.32           N  
ANISOU 3966  N   VAL A 512    24811  14379  19064   5196  -2170   2890       N  
ATOM   3967  CA  VAL A 512     127.328  27.448  36.450  1.00153.58           C  
ANISOU 3967  CA  VAL A 512    25051  13951  19352   5156  -2063   3055       C  
ATOM   3968  C   VAL A 512     127.336  27.075  34.971  1.00163.06           C  
ANISOU 3968  C   VAL A 512    26339  15081  20535   5331  -2022   2837       C  
ATOM   3969  O   VAL A 512     126.722  27.755  34.148  1.00168.51           O  
ANISOU 3969  O   VAL A 512    26943  16062  21022   5535  -2076   2592       O  
ATOM   3970  CB  VAL A 512     127.096  26.186  37.297  1.00147.34           C  
ANISOU 3970  CB  VAL A 512    24280  13003  18698   4730  -2009   3100       C  
ATOM   3971  CG1 VAL A 512     127.367  26.480  38.762  1.00144.21           C  
ANISOU 3971  CG1 VAL A 512    23839  12587  18368   4580  -2034   3377       C  
ATOM   3972  CG2 VAL A 512     125.681  25.669  37.101  1.00147.39           C  
ANISOU 3972  CG2 VAL A 512    24148  13313  18540   4485  -2032   2740       C  
ATOM   3973  N   ASP A 513     128.035  25.994  34.641  1.00163.21           N  
ANISOU 3973  N   ASP A 513    26531  14714  20767   5251  -1927   2927       N  
ATOM   3974  CA  ASP A 513     128.182  25.574  33.251  1.00161.96           C  
ANISOU 3974  CA  ASP A 513    26475  14440  20622   5419  -1879   2753       C  
ATOM   3975  C   ASP A 513     127.340  24.346  32.911  1.00160.44           C  
ANISOU 3975  C   ASP A 513    26264  14267  20427   5128  -1840   2487       C  
ATOM   3976  O   ASP A 513     127.073  24.076  31.741  1.00159.71           O  
ANISOU 3976  O   ASP A 513    26201  14203  20278   5244  -1823   2251       O  
ATOM   3977  CB  ASP A 513     129.655  25.318  32.915  1.00162.97           C  
ANISOU 3977  CB  ASP A 513    26821  14110  20989   5600  -1801   3033       C  
ATOM   3978  CG  ASP A 513     130.315  24.346  33.875  1.00166.10           C  
ANISOU 3978  CG  ASP A 513    27325  14152  21633   5316  -1733   3299       C  
ATOM   3979  OD1 ASP A 513     129.809  24.175  35.004  1.00165.77           O  
ANISOU 3979  OD1 ASP A 513    27185  14223  21579   5031  -1757   3343       O  
ATOM   3980  OD2 ASP A 513     131.350  23.755  33.501  1.00169.95           O1-
ANISOU 3980  OD2 ASP A 513    27998  14247  22329   5381  -1655   3465       O1-
ATOM   3981  N   LYS A 514     126.927  23.607  33.936  1.00162.52           N  
ANISOU 3981  N   LYS A 514    26480  14516  20753   4753  -1825   2526       N  
ATOM   3982  CA  LYS A 514     126.102  22.419  33.738  1.00166.11           C  
ANISOU 3982  CA  LYS A 514    26908  14991  21214   4448  -1787   2284       C  
ATOM   3983  C   LYS A 514     125.769  21.739  35.060  1.00165.60           C  
ANISOU 3983  C   LYS A 514    26793  14898  21230   4043  -1772   2387       C  
ATOM   3984  O   LYS A 514     126.528  21.826  36.026  1.00160.73           O  
ANISOU 3984  O   LYS A 514    26234  14085  20752   3987  -1758   2704       O  
ATOM   3985  CB  LYS A 514     126.799  21.424  32.805  1.00168.31           C  
ANISOU 3985  CB  LYS A 514    27372  14903  21675   4489  -1694   2288       C  
ATOM   3986  CG  LYS A 514     128.108  20.869  33.346  1.00165.80           C  
ANISOU 3986  CG  LYS A 514    27237  14124  21636   4436  -1619   2655       C  
ATOM   3987  CD  LYS A 514     128.752  19.913  32.355  1.00163.97           C  
ANISOU 3987  CD  LYS A 514    27181  13549  21572   4486  -1533   2638       C  
ATOM   3988  CE  LYS A 514     130.021  19.298  32.924  1.00163.27           C  
ANISOU 3988  CE  LYS A 514    27273  12999  21763   4411  -1458   2995       C  
ATOM   3989  NZ  LYS A 514     129.751  18.486  34.143  1.00162.63           N1+
ANISOU 3989  NZ  LYS A 514    27163  12847  21781   4007  -1433   3094       N1+
ATOM   3990  N   CYS A 515     124.627  21.062  35.096  1.00170.55           N  
ANISOU 3990  N   CYS A 515    27312  15720  21770   3764  -1774   2116       N  
ATOM   3991  CA  CYS A 515     124.213  20.326  36.282  1.00178.77           C  
ANISOU 3991  CA  CYS A 515    28302  16743  22881   3363  -1754   2181       C  
ATOM   3992  C   CYS A 515     124.955  18.999  36.369  1.00190.91           C  
ANISOU 3992  C   CYS A 515    30013  17840  24686   3168  -1648   2340       C  
ATOM   3993  O   CYS A 515     125.408  18.462  35.358  1.00194.77           O  
ANISOU 3993  O   CYS A 515    30626  18111  25266   3285  -1593   2284       O  
ATOM   3994  CB  CYS A 515     122.704  20.084  36.264  1.00178.67           C  
ANISOU 3994  CB  CYS A 515    28108  17101  22678   3137  -1793   1823       C  
ATOM   3995  SG  CYS A 515     121.710  21.591  36.249  1.00267.28           S  
ANISOU 3995  SG  CYS A 515    39111  28865  33576   3325  -1924   1616       S  
ATOM   3996  N   LYS A 516     125.080  18.475  37.583  1.00196.64           N  
ANISOU 3996  N   LYS A 516    30745  18434  25533   2871  -1620   2538       N  
ATOM   3997  CA  LYS A 516     125.760  17.205  37.801  1.00200.69           C  
ANISOU 3997  CA  LYS A 516    31418  18533  26301   2658  -1521   2702       C  
ATOM   3998  C   LYS A 516     124.802  16.036  37.590  1.00206.98           C  
ANISOU 3998  C   LYS A 516    32165  19385  27092   2342  -1480   2430       C  
ATOM   3999  O   LYS A 516     124.247  15.493  38.545  1.00208.81           O  
ANISOU 3999  O   LYS A 516    32327  19668  27343   2006  -1469   2434       O  
ATOM   4000  CB  LYS A 516     126.370  17.160  39.204  1.00198.49           C  
ANISOU 4000  CB  LYS A 516    31177  18075  26163   2489  -1507   3047       C  
ATOM   4001  CG  LYS A 516     127.371  18.275  39.472  1.00193.83           C  
ANISOU 4001  CG  LYS A 516    30640  17408  25599   2793  -1543   3332       C  
ATOM   4002  CD  LYS A 516     127.798  18.315  40.931  1.00189.47           C  
ANISOU 4002  CD  LYS A 516    30094  16743  25154   2616  -1542   3642       C  
ATOM   4003  CE  LYS A 516     128.747  19.477  41.190  1.00181.88           C  
ANISOU 4003  CE  LYS A 516    29172  15726  24210   2927  -1584   3911       C  
ATOM   4004  NZ  LYS A 516     129.159  19.567  42.618  1.00178.69           N1+
ANISOU 4004  NZ  LYS A 516    28767  15222  23905   2769  -1587   4210       N1+
ATOM   4005  N   LEU A 517     124.615  15.656  36.329  1.00210.93           N  
ANISOU 4005  N   LEU A 517    32701  19873  27568   2457  -1457   2191       N  
ATOM   4006  CA  LEU A 517     123.698  14.578  35.971  1.00217.92           C  
ANISOU 4006  CA  LEU A 517    33537  20818  28443   2191  -1419   1905       C  
ATOM   4007  C   LEU A 517     124.383  13.214  35.901  1.00223.13           C  
ANISOU 4007  C   LEU A 517    34367  21050  29363   2007  -1315   2027       C  
ATOM   4008  O   LEU A 517     123.954  12.262  36.553  1.00226.20           O  
ANISOU 4008  O   LEU A 517    34733  21382  29831   1653  -1272   2008       O  
ATOM   4009  CB  LEU A 517     123.010  14.884  34.640  1.00218.60           C  
ANISOU 4009  CB  LEU A 517    33556  21153  28351   2403  -1455   1550       C  
ATOM   4010  CG  LEU A 517     121.790  15.803  34.708  1.00220.34           C  
ANISOU 4010  CG  LEU A 517    33563  21868  28290   2434  -1551   1292       C  
ATOM   4011  CD1 LEU A 517     121.413  16.288  33.321  1.00221.54           C  
ANISOU 4011  CD1 LEU A 517    33681  22214  28279   2731  -1588   1003       C  
ATOM   4012  CD2 LEU A 517     120.619  15.090  35.367  1.00223.23           C  
ANISOU 4012  CD2 LEU A 517    33793  22421  28604   2039  -1547   1101       C  
ATOM   4013  N   LEU A 518     125.442  13.126  35.104  1.00221.77           N  
ANISOU 4013  N   LEU A 518    34363  20577  29322   2249  -1274   2150       N  
ATOM   4014  CA  LEU A 518     126.160  11.872  34.914  1.00219.00           C  
ANISOU 4014  CA  LEU A 518    34182  19810  29219   2110  -1178   2262       C  
ATOM   4015  C   LEU A 518     127.247  11.689  35.971  1.00217.34           C  
ANISOU 4015  C   LEU A 518    34098  19264  29216   2020  -1138   2664       C  
ATOM   4016  O   LEU A 518     127.480  10.580  36.454  1.00218.84           O  
ANISOU 4016  O   LEU A 518    34369  19191  29588   1740  -1068   2768       O  
ATOM   4017  CB  LEU A 518     126.763  11.815  33.509  1.00215.42           C  
ANISOU 4017  CB  LEU A 518    33851  19191  28809   2409  -1153   2190       C  
ATOM   4018  CG  LEU A 518     125.770  11.948  32.350  1.00214.33           C  
ANISOU 4018  CG  LEU A 518    33604  19354  28477   2524  -1188   1791       C  
ATOM   4019  CD1 LEU A 518     126.501  11.900  31.023  1.00213.56           C  
ANISOU 4019  CD1 LEU A 518    33644  19059  28442   2829  -1159   1760       C  
ATOM   4020  CD2 LEU A 518     124.710  10.861  32.414  1.00216.14           C  
ANISOU 4020  CD2 LEU A 518    33745  19680  28697   2172  -1158   1532       C  
ATOM   4021  N   GLU A 519     127.903  12.787  36.333  1.00214.58           N  
ANISOU 4021  N   GLU A 519    33765  18927  28839   2259  -1183   2887       N  
ATOM   4022  CA  GLU A 519     128.961  12.751  37.335  1.00214.43           C  
ANISOU 4022  CA  GLU A 519    33861  18606  29006   2208  -1153   3272       C  
ATOM   4023  C   GLU A 519     128.696  13.746  38.461  1.00213.41           C  
ANISOU 4023  C   GLU A 519    33607  18721  28759   2195  -1224   3397       C  
ATOM   4024  O   GLU A 519     127.546  14.081  38.746  1.00215.40           O  
ANISOU 4024  O   GLU A 519    33677  19347  28818   2079  -1281   3188       O  
ATOM   4025  CB  GLU A 519     130.320  13.020  36.689  1.00214.57           C  
ANISOU 4025  CB  GLU A 519    34063  18301  29164   2530  -1125   3485       C  
ATOM   4026  CG  GLU A 519     130.787  11.913  35.755  1.00218.29           C  
ANISOU 4026  CG  GLU A 519    34686  18454  29801   2513  -1045   3431       C  
ATOM   4027  CD  GLU A 519     132.094  12.243  35.061  1.00218.12           C  
ANISOU 4027  CD  GLU A 519    34838  18133  29903   2847  -1021   3625       C  
ATOM   4028  OE1 GLU A 519     132.439  13.440  34.979  1.00215.94           O  
ANISOU 4028  OE1 GLU A 519    34542  17970  29536   3147  -1074   3712       O  
ATOM   4029  OE2 GLU A 519     132.776  11.305  34.595  1.00219.70           O1-
ANISOU 4029  OE2 GLU A 519    35196  17984  30295   2811   -948   3688       O1-
ATOM   4030  N   GLY A 520     129.763  14.217  39.098  1.00210.93           N  
ANISOU 4030  N   GLY A 520    33387  18193  28563   2314  -1223   3736       N  
ATOM   4031  CA  GLY A 520     129.632  15.110  40.234  1.00211.10           C  
ANISOU 4031  CA  GLY A 520    33303  18405  28501   2297  -1286   3890       C  
ATOM   4032  C   GLY A 520     129.178  14.352  41.467  1.00216.11           C  
ANISOU 4032  C   GLY A 520    33890  19026  29196   1889  -1261   3957       C  
ATOM   4033  O   GLY A 520     128.402  13.402  41.367  1.00219.40           O  
ANISOU 4033  O   GLY A 520    34267  19487  29609   1617  -1226   3754       O  
ATOM   4034  N   GLU A 521     129.661  14.770  42.633  1.00217.85           N  
ANISOU 4034  N   GLU A 521    34114  19184  29475   1848  -1278   4240       N  
ATOM   4035  CA  GLU A 521     129.346  14.073  43.877  1.00221.49           C  
ANISOU 4035  CA  GLU A 521    34544  19603  30008   1471  -1251   4342       C  
ATOM   4036  C   GLU A 521     127.842  14.062  44.178  1.00217.60           C  
ANISOU 4036  C   GLU A 521    33844  19522  29312   1236  -1295   4056       C  
ATOM   4037  O   GLU A 521     127.231  12.993  44.219  1.00219.94           O  
ANISOU 4037  O   GLU A 521    34128  19793  29646    937  -1245   3909       O  
ATOM   4038  CB  GLU A 521     130.151  14.649  45.050  1.00224.01           C  
ANISOU 4038  CB  GLU A 521    34898  19800  30413   1506  -1270   4698       C  
ATOM   4039  CG  GLU A 521     131.656  14.650  44.827  1.00222.79           C  
ANISOU 4039  CG  GLU A 521    34951  19230  30470   1727  -1224   4990       C  
ATOM   4040  CD  GLU A 521     132.405  15.448  45.877  1.00218.58           C  
ANISOU 4040  CD  GLU A 521    34432  18630  29990   1824  -1258   5314       C  
ATOM   4041  OE1 GLU A 521     131.747  16.132  46.690  1.00217.03           O  
ANISOU 4041  OE1 GLU A 521    34077  18738  29648   1758  -1325   5303       O  
ATOM   4042  OE2 GLU A 521     133.652  15.395  45.886  1.00216.53           O1-
ANISOU 4042  OE2 GLU A 521    34340  18012  29918   1967  -1218   5579       O1-
ATOM   4043  N   PRO A 522     127.238  15.245  44.389  1.00207.24           N  
ANISOU 4043  N   PRO A 522    32367  18589  27784   1370  -1389   3973       N  
ATOM   4044  CA  PRO A 522     125.788  15.271  44.602  1.00204.59           C  
ANISOU 4044  CA  PRO A 522    31832  18656  27246   1162  -1435   3682       C  
ATOM   4045  C   PRO A 522     125.041  15.213  43.273  1.00206.83           C  
ANISOU 4045  C   PRO A 522    32060  19137  27390   1270  -1448   3316       C  
ATOM   4046  O   PRO A 522     125.219  16.096  42.434  1.00206.04           O  
ANISOU 4046  O   PRO A 522    31950  19149  27185   1606  -1495   3246       O  
ATOM   4047  CB  PRO A 522     125.552  16.634  45.274  1.00196.51           C  
ANISOU 4047  CB  PRO A 522    30667  17944  26053   1303  -1535   3751       C  
ATOM   4048  CG  PRO A 522     126.925  17.180  45.596  1.00192.25           C  
ANISOU 4048  CG  PRO A 522    30262  17126  25660   1535  -1531   4113       C  
ATOM   4049  CD  PRO A 522     127.830  16.578  44.578  1.00197.36           C  
ANISOU 4049  CD  PRO A 522    31100  17416  26473   1685  -1458   4153       C  
ATOM   4050  N   ARG A 523     124.220  14.185  43.086  1.00209.38           N  
ANISOU 4050  N   ARG A 523    32345  19498  27713    991  -1404   3085       N  
ATOM   4051  CA  ARG A 523     123.459  14.035  41.850  1.00209.87           C  
ANISOU 4051  CA  ARG A 523    32349  19743  27647   1068  -1413   2724       C  
ATOM   4052  C   ARG A 523     122.306  15.033  41.786  1.00207.22           C  
ANISOU 4052  C   ARG A 523    31801  19903  27030   1141  -1512   2466       C  
ATOM   4053  O   ARG A 523     121.638  15.286  42.788  1.00208.33           O  
ANISOU 4053  O   ARG A 523    31809  20269  27079    946  -1553   2468       O  
ATOM   4054  CB  ARG A 523     122.936  12.604  41.711  1.00214.75           C  
ANISOU 4054  CB  ARG A 523    32988  20244  28361    739  -1334   2558       C  
ATOM   4055  CG  ARG A 523     124.029  11.548  41.696  1.00217.57           C  
ANISOU 4055  CG  ARG A 523    33556  20115  28997    659  -1235   2787       C  
ATOM   4056  CD  ARG A 523     125.214  12.002  40.858  1.00218.08           C  
ANISOU 4056  CD  ARG A 523    33773  19942  29144   1031  -1229   2939       C  
ATOM   4057  NE  ARG A 523     126.104  10.899  40.509  1.00220.62           N  
ANISOU 4057  NE  ARG A 523    34289  19826  29711    970  -1134   3068       N  
ATOM   4058  CZ  ARG A 523     126.105  10.287  39.329  1.00223.28           C  
ANISOU 4058  CZ  ARG A 523    34691  20059  30085   1040  -1094   2881       C  
ATOM   4059  NH1 ARG A 523     125.264  10.674  38.379  1.00223.89           N1+
ANISOU 4059  NH1 ARG A 523    34657  20439  29971   1177  -1140   2554       N1+
ATOM   4060  NH2 ARG A 523     126.948   9.291  39.096  1.00224.44           N  
ANISOU 4060  NH2 ARG A 523    35015  19801  30462    976  -1011   3018       N  
ATOM   4061  N   GLU A 524     122.079  15.596  40.603  1.00202.19           N  
ANISOU 4061  N   GLU A 524    31135  19433  26256   1422  -1552   2245       N  
ATOM   4062  CA  GLU A 524     121.050  16.615  40.427  1.00195.69           C  
ANISOU 4062  CA  GLU A 524    30119  19074  25159   1533  -1651   1997       C  
ATOM   4063  C   GLU A 524     120.197  16.366  39.186  1.00193.31           C  
ANISOU 4063  C   GLU A 524    29758  18962  24728   1589  -1656   1605       C  
ATOM   4064  O   GLU A 524     120.474  15.460  38.401  1.00196.33           O  
ANISOU 4064  O   GLU A 524    30255  19108  25234   1573  -1586   1534       O  
ATOM   4065  CB  GLU A 524     121.689  18.004  40.338  1.00191.20           C  
ANISOU 4065  CB  GLU A 524    29551  18584  24511   1905  -1721   2157       C  
ATOM   4066  CG  GLU A 524     122.423  18.439  41.596  1.00189.99           C  
ANISOU 4066  CG  GLU A 524    29427  18308  24453   1874  -1732   2523       C  
ATOM   4067  CD  GLU A 524     123.182  19.738  41.407  1.00187.95           C  
ANISOU 4067  CD  GLU A 524    29189  18077  24144   2261  -1791   2692       C  
ATOM   4068  OE1 GLU A 524     123.543  20.053  40.253  1.00188.75           O  
ANISOU 4068  OE1 GLU A 524    29357  18138  24222   2560  -1790   2609       O  
ATOM   4069  OE2 GLU A 524     123.421  20.442  42.410  1.00184.77           O1-
ANISOU 4069  OE2 GLU A 524    28738  17736  23729   2269  -1836   2908       O1-
ATOM   4070  N   PHE A 525     119.156  17.176  39.024  1.00187.32           N  
ANISOU 4070  N   PHE A 525    28820  18633  23719   1654  -1743   1349       N  
ATOM   4071  CA  PHE A 525     118.314  17.130  37.834  1.00184.84           C  
ANISOU 4071  CA  PHE A 525    28437  18541  23253   1748  -1763    966       C  
ATOM   4072  C   PHE A 525     118.036  18.550  37.350  1.00188.03           C  
ANISOU 4072  C   PHE A 525    28739  19279  23426   2083  -1865    852       C  
ATOM   4073  O   PHE A 525     118.184  19.508  38.108  1.00190.62           O  
ANISOU 4073  O   PHE A 525    29004  19740  23683   2162  -1927   1021       O  
ATOM   4074  CB  PHE A 525     117.004  16.393  38.120  1.00180.31           C  
ANISOU 4074  CB  PHE A 525    27723  18185  22600   1395  -1758    682       C  
ATOM   4075  CG  PHE A 525     116.035  17.175  38.961  1.00173.45           C  
ANISOU 4075  CG  PHE A 525    26657  17718  21529   1289  -1845    592       C  
ATOM   4076  CD1 PHE A 525     115.011  17.898  38.371  1.00169.54           C  
ANISOU 4076  CD1 PHE A 525    26005  17631  20782   1413  -1927    266       C  
ATOM   4077  CD2 PHE A 525     116.144  17.184  40.341  1.00169.01           C  
ANISOU 4077  CD2 PHE A 525    26064  17124  21026   1067  -1847    832       C  
ATOM   4078  CE1 PHE A 525     114.116  18.616  39.141  1.00164.89           C  
ANISOU 4078  CE1 PHE A 525    25232  17412  20005   1314  -2010    180       C  
ATOM   4079  CE2 PHE A 525     115.252  17.900  41.117  1.00164.47           C  
ANISOU 4079  CE2 PHE A 525    25305  16920  20265    969  -1929    749       C  
ATOM   4080  CZ  PHE A 525     114.237  18.617  40.516  1.00162.46           C  
ANISOU 4080  CZ  PHE A 525    24895  17071  19762   1091  -2011    422       C  
ATOM   4081  N   VAL A 526     117.632  18.684  36.092  1.00187.40           N  
ANISOU 4081  N   VAL A 526    28641  19336  23229   2282  -1882    566       N  
ATOM   4082  CA  VAL A 526     117.464  20.004  35.494  1.00184.57           C  
ANISOU 4082  CA  VAL A 526    28205  19262  22660   2632  -1971    459       C  
ATOM   4083  C   VAL A 526     116.004  20.366  35.233  1.00188.97           C  
ANISOU 4083  C   VAL A 526    28562  20280  22957   2577  -2046     71       C  
ATOM   4084  O   VAL A 526     115.311  19.688  34.475  1.00194.19           O  
ANISOU 4084  O   VAL A 526    29198  21007  23580   2495  -2023   -228       O  
ATOM   4085  CB  VAL A 526     118.244  20.124  34.171  1.00181.37           C  
ANISOU 4085  CB  VAL A 526    27941  18669  22301   2982  -1943    449       C  
ATOM   4086  CG1 VAL A 526     118.260  21.568  33.697  1.00177.41           C  
ANISOU 4086  CG1 VAL A 526    27379  18424  21605   3358  -2032    409       C  
ATOM   4087  CG2 VAL A 526     119.660  19.600  34.342  1.00181.50           C  
ANISOU 4087  CG2 VAL A 526    28166  18208  22590   3013  -1860    805       C  
ATOM   4088  N   GLU A 527     115.548  21.442  35.868  1.00187.94           N  
ANISOU 4088  N   GLU A 527    28289  20467  22652   2625  -2139     78       N  
ATOM   4089  CA  GLU A 527     114.229  22.005  35.598  1.00189.37           C  
ANISOU 4089  CA  GLU A 527    28278  21107  22567   2628  -2224   -277       C  
ATOM   4090  C   GLU A 527     114.239  23.516  35.803  1.00183.76           C  
ANISOU 4090  C   GLU A 527    27474  20668  21677   2893  -2328   -214       C  
ATOM   4091  O   GLU A 527     114.533  24.003  36.896  1.00182.19           O  
ANISOU 4091  O   GLU A 527    27243  20480  21502   2832  -2358     35       O  
ATOM   4092  CB  GLU A 527     113.153  21.351  36.469  1.00193.11           C  
ANISOU 4092  CB  GLU A 527    28617  21749  23005   2213  -2224   -421       C  
ATOM   4093  CG  GLU A 527     112.658  20.012  35.940  1.00196.20           C  
ANISOU 4093  CG  GLU A 527    29039  22029  23480   1983  -2146   -652       C  
ATOM   4094  CD  GLU A 527     111.322  19.605  36.530  1.00196.24           C  
ANISOU 4094  CD  GLU A 527    28871  22315  23374   1637  -2168   -901       C  
ATOM   4095  OE1 GLU A 527     110.789  18.550  36.127  1.00194.20           O  
ANISOU 4095  OE1 GLU A 527    28615  22006  23167   1437  -2110  -1118       O  
ATOM   4096  OE2 GLU A 527     110.802  20.343  37.393  1.00197.69           O1-
ANISOU 4096  OE2 GLU A 527    28917  22773  23423   1566  -2242   -882       O1-
ATOM   4097  N   ASN A 528     113.918  24.251  34.741  1.00177.84           N  
ANISOU 4097  N   ASN A 528    26683  20140  20749   3191  -2383   -442       N  
ATOM   4098  CA  ASN A 528     113.959  25.709  34.766  1.00169.96           C  
ANISOU 4098  CA  ASN A 528    25605  19395  19576   3482  -2481   -400       C  
ATOM   4099  C   ASN A 528     115.373  26.240  34.970  1.00161.57           C  
ANISOU 4099  C   ASN A 528    24683  18046  18661   3721  -2461    -10       C  
ATOM   4100  O   ASN A 528     115.588  27.182  35.733  1.00160.99           O  
ANISOU 4100  O   ASN A 528    24548  18086  18535   3800  -2522    177       O  
ATOM   4101  CB  ASN A 528     113.021  26.267  35.839  1.00171.15           C  
ANISOU 4101  CB  ASN A 528    25560  19903  19566   3287  -2566   -458       C  
ATOM   4102  CG  ASN A 528     111.560  26.109  35.473  1.00176.07           C  
ANISOU 4102  CG  ASN A 528    26022  20892  19986   3145  -2611   -882       C  
ATOM   4103  ND2 ASN A 528     110.684  26.727  36.258  1.00176.90           N  
ANISOU 4103  ND2 ASN A 528    25947  21348  19920   3020  -2696   -969       N  
ATOM   4104  OD1 ASN A 528     111.220  25.442  34.496  1.00179.38           O  
ANISOU 4104  OD1 ASN A 528    26476  21279  20402   3150  -2571  -1131       O  
ATOM   4105  N   SER A 529     116.332  25.627  34.284  1.00154.98           N  
ANISOU 4105  N   SER A 529    24035  16838  18013   3837  -2375    109       N  
ATOM   4106  CA  SER A 529     117.727  26.045  34.366  1.00149.67           C  
ANISOU 4106  CA  SER A 529    23512  15861  17496   4073  -2346    469       C  
ATOM   4107  C   SER A 529     118.234  26.060  35.806  1.00145.46           C  
ANISOU 4107  C   SER A 529    22982  15192  17092   3883  -2341    808       C  
ATOM   4108  O   SER A 529     119.187  26.768  36.130  1.00141.36           O  
ANISOU 4108  O   SER A 529    22527  14540  16642   4084  -2351   1099       O  
ATOM   4109  CB  SER A 529     117.913  27.423  33.726  1.00147.42           C  
ANISOU 4109  CB  SER A 529    23195  15772  17047   4485  -2421    446       C  
ATOM   4110  OG  SER A 529     117.508  27.413  32.368  1.00145.81           O  
ANISOU 4110  OG  SER A 529    22998  15675  16728   4678  -2424    143       O  
ATOM   4111  N   GLU A 530     117.593  25.275  36.666  1.00147.81           N  
ANISOU 4111  N   GLU A 530    23211  15525  17424   3497  -2323    768       N  
ATOM   4112  CA  GLU A 530     117.995  25.182  38.065  1.00149.17           C  
ANISOU 4112  CA  GLU A 530    23385  15572  17720   3285  -2313   1073       C  
ATOM   4113  C   GLU A 530     118.442  23.770  38.418  1.00153.13           C  
ANISOU 4113  C   GLU A 530    24019  15696  18469   2995  -2204   1208       C  
ATOM   4114  O   GLU A 530     117.843  22.789  37.975  1.00157.51           O  
ANISOU 4114  O   GLU A 530    24574  16235  19038   2802  -2158    979       O  
ATOM   4115  CB  GLU A 530     116.853  25.613  38.985  1.00154.43           C  
ANISOU 4115  CB  GLU A 530    23841  16630  18203   3072  -2395    946       C  
ATOM   4116  CG  GLU A 530     116.456  27.071  38.839  1.00161.88           C  
ANISOU 4116  CG  GLU A 530    24648  17949  18911   3340  -2510    854       C  
ATOM   4117  CD  GLU A 530     115.432  27.499  39.869  1.00166.41           C  
ANISOU 4117  CD  GLU A 530    25021  18883  19323   3121  -2591    770       C  
ATOM   4118  OE1 GLU A 530     115.059  26.664  40.719  1.00168.64           O  
ANISOU 4118  OE1 GLU A 530    25276  19117  19684   2762  -2555    794       O  
ATOM   4119  OE2 GLU A 530     115.001  28.671  39.831  1.00166.45           O1-
ANISOU 4119  OE2 GLU A 530    24896  19221  19125   3308  -2690    681       O1-
ATOM   4120  N   CYS A 531     119.497  23.674  39.221  1.00152.43           N  
ANISOU 4120  N   CYS A 531    24041  15302  18574   2968  -2165   1577       N  
ATOM   4121  CA  CYS A 531     120.027  22.383  39.641  1.00151.84           C  
ANISOU 4121  CA  CYS A 531    24101  14848  18744   2702  -2063   1742       C  
ATOM   4122  C   CYS A 531     119.586  22.040  41.060  1.00150.52           C  
ANISOU 4122  C   CYS A 531    23847  14740  18605   2340  -2066   1845       C  
ATOM   4123  O   CYS A 531     119.962  22.717  42.016  1.00147.67           O  
ANISOU 4123  O   CYS A 531    23455  14401  18252   2363  -2106   2088       O  
ATOM   4124  CB  CYS A 531     121.554  22.378  39.559  1.00149.66           C  
ANISOU 4124  CB  CYS A 531    24025  14153  18687   2902  -2006   2087       C  
ATOM   4125  SG  CYS A 531     122.222  22.649  37.904  1.00120.97           S  
ANISOU 4125  SG  CYS A 531    20521  10384  15058   3317  -1985   2002       S  
ATOM   4126  N   ILE A 532     118.786  20.987  41.189  1.00153.66           N  
ANISOU 4126  N   ILE A 532    24204  15163  19018   2008  -2024   1658       N  
ATOM   4127  CA  ILE A 532     118.345  20.518  42.497  1.00155.72           C  
ANISOU 4127  CA  ILE A 532    24392  15459  19317   1641  -2015   1744       C  
ATOM   4128  C   ILE A 532     118.799  19.080  42.721  1.00161.62           C  
ANISOU 4128  C   ILE A 532    25283  15818  20308   1371  -1901   1860       C  
ATOM   4129  O   ILE A 532     118.651  18.229  41.843  1.00162.97           O  
ANISOU 4129  O   ILE A 532    25517  15874  20532   1328  -1843   1677       O  
ATOM   4130  CB  ILE A 532     116.812  20.599  42.654  1.00152.85           C  
ANISOU 4130  CB  ILE A 532    23819  15526  18733   1440  -2074   1405       C  
ATOM   4131  CG1 ILE A 532     116.308  22.013  42.354  1.00148.05           C  
ANISOU 4131  CG1 ILE A 532    23066  15315  17872   1711  -2190   1263       C  
ATOM   4132  CG2 ILE A 532     116.398  20.172  44.054  1.00152.64           C  
ANISOU 4132  CG2 ILE A 532    23718  15532  18746   1070  -2066   1514       C  
ATOM   4133  CD1 ILE A 532     116.118  22.303  40.880  1.00149.10           C  
ANISOU 4133  CD1 ILE A 532    23209  15551  17891   1995  -2208    998       C  
ATOM   4134  N   GLN A 533     119.355  18.813  43.898  1.00165.61           N  
ANISOU 4134  N   GLN A 533    25840  16123  20963   1192  -1871   2165       N  
ATOM   4135  CA  GLN A 533     119.860  17.484  44.218  1.00173.30           C  
ANISOU 4135  CA  GLN A 533    26955  16714  22176    935  -1764   2309       C  
ATOM   4136  C   GLN A 533     118.727  16.485  44.421  1.00176.55           C  
ANISOU 4136  C   GLN A 533    27276  17249  22556    560  -1730   2059       C  
ATOM   4137  O   GLN A 533     117.734  16.780  45.087  1.00172.76           O  
ANISOU 4137  O   GLN A 533    26626  17090  21924    387  -1784   1933       O  
ATOM   4138  CB  GLN A 533     120.746  17.529  45.464  1.00178.18           C  
ANISOU 4138  CB  GLN A 533    27648  17099  22952    853  -1745   2704       C  
ATOM   4139  CG  GLN A 533     121.912  18.498  45.363  1.00181.10           C  
ANISOU 4139  CG  GLN A 533    28109  17329  23370   1211  -1775   2972       C  
ATOM   4140  CD  GLN A 533     122.843  18.415  46.557  1.00182.77           C  
ANISOU 4140  CD  GLN A 533    28410  17272  23762   1122  -1746   3361       C  
ATOM   4141  NE2 GLN A 533     123.519  19.519  46.857  1.00180.89           N  
ANISOU 4141  NE2 GLN A 533    28174  17051  23505   1383  -1802   3576       N  
ATOM   4142  OE1 GLN A 533     122.957  17.371  47.199  1.00184.12           O  
ANISOU 4142  OE1 GLN A 533    28648  17220  24090    824  -1675   3467       O  
ATOM   4143  N   CYS A 534     118.883  15.300  43.839  1.00184.08           N  
ANISOU 4143  N   CYS A 534    28342  17943  23657    437  -1640   1987       N  
ATOM   4144  CA  CYS A 534     117.908  14.232  44.004  1.00192.78           C  
ANISOU 4144  CA  CYS A 534    29376  19110  24761     75  -1595   1766       C  
ATOM   4145  C   CYS A 534     117.925  13.757  45.451  1.00201.64           C  
ANISOU 4145  C   CYS A 534    30491  20136  25988   -255  -1563   1985       C  
ATOM   4146  O   CYS A 534     118.839  14.087  46.206  1.00202.12           O  
ANISOU 4146  O   CYS A 534    30632  20011  26155   -197  -1562   2320       O  
ATOM   4147  CB  CYS A 534     118.238  13.067  43.072  1.00193.26           C  
ANISOU 4147  CB  CYS A 534    29578  18870  24983     37  -1502   1681       C  
ATOM   4148  SG  CYS A 534     118.799  13.565  41.427  1.00260.92           S  
ANISOU 4148  SG  CYS A 534    38237  27386  33516    479  -1518   1568       S  
ATOM   4149  N   HIS A 535     116.914  12.987  45.839  1.00210.18           N  
ANISOU 4149  N   HIS A 535    31475  21344  27039   -598  -1536   1795       N  
ATOM   4150  CA  HIS A 535     116.864  12.432  47.186  1.00217.01           C  
ANISOU 4150  CA  HIS A 535    32333  22116  28005   -934  -1498   1984       C  
ATOM   4151  C   HIS A 535     118.066  11.518  47.404  1.00220.63           C  
ANISOU 4151  C   HIS A 535    33005  22082  28743  -1003  -1399   2285       C  
ATOM   4152  O   HIS A 535     118.366  10.673  46.561  1.00222.92           O  
ANISOU 4152  O   HIS A 535    33408  22137  29155   -999  -1330   2211       O  
ATOM   4153  CB  HIS A 535     115.560  11.662  47.407  1.00220.21           C  
ANISOU 4153  CB  HIS A 535    32607  22724  28339  -1287  -1475   1699       C  
ATOM   4154  CG  HIS A 535     115.240  11.413  48.848  1.00218.94           C  
ANISOU 4154  CG  HIS A 535    32384  22598  28207  -1609  -1464   1845       C  
ATOM   4155  CD2 HIS A 535     114.585  12.172  49.760  1.00216.67           C  
ANISOU 4155  CD2 HIS A 535    31938  22625  27762  -1687  -1538   1844       C  
ATOM   4156  ND1 HIS A 535     115.609  10.259  49.505  1.00217.41           N  
ANISOU 4156  ND1 HIS A 535    32296  22086  28222  -1899  -1366   2018       N  
ATOM   4157  CE1 HIS A 535     115.195  10.317  50.759  1.00215.79           C  
ANISOU 4157  CE1 HIS A 535    32004  21998  27988  -2139  -1379   2119       C  
ATOM   4158  NE2 HIS A 535     114.571  11.467  50.939  1.00215.22           N  
ANISOU 4158  NE2 HIS A 535    31769  22309  27695  -2017  -1483   2016       N  
ATOM   4159  N   PRO A 536     118.763  11.692  48.539  1.00218.63           N  
ANISOU 4159  N   PRO A 536    32806  21671  28594  -1061  -1394   2625       N  
ATOM   4160  CA  PRO A 536     119.984  10.940  48.852  1.00215.63           C  
ANISOU 4160  CA  PRO A 536    32630  20822  28477  -1109  -1308   2943       C  
ATOM   4161  C   PRO A 536     119.819   9.436  48.652  1.00215.03           C  
ANISOU 4161  C   PRO A 536    32633  20510  28557  -1401  -1204   2852       C  
ATOM   4162  O   PRO A 536     120.810   8.732  48.457  1.00213.70           O  
ANISOU 4162  O   PRO A 536    32648  19947  28602  -1388  -1130   3038       O  
ATOM   4163  CB  PRO A 536     120.213  11.255  50.331  1.00214.50           C  
ANISOU 4163  CB  PRO A 536    32462  20672  28366  -1247  -1326   3227       C  
ATOM   4164  CG  PRO A 536     119.600  12.596  50.521  1.00213.46           C  
ANISOU 4164  CG  PRO A 536    32153  20956  27996  -1084  -1440   3136       C  
ATOM   4165  CD  PRO A 536     118.401  12.631  49.615  1.00216.85           C  
ANISOU 4165  CD  PRO A 536    32444  21716  28235  -1088  -1473   2721       C  
ATOM   4166  N   GLU A 537     118.581   8.955  48.697  1.00216.78           N  
ANISOU 4166  N   GLU A 537    32718  20974  28675  -1659  -1199   2566       N  
ATOM   4167  CA  GLU A 537     118.305   7.532  48.532  1.00220.43           C  
ANISOU 4167  CA  GLU A 537    33235  21245  29275  -1953  -1101   2456       C  
ATOM   4168  C   GLU A 537     118.407   7.090  47.075  1.00216.63           C  
ANISOU 4168  C   GLU A 537    32824  20661  28826  -1797  -1071   2245       C  
ATOM   4169  O   GLU A 537     118.002   5.981  46.726  1.00219.01           O  
ANISOU 4169  O   GLU A 537    33143  20866  29206  -2012  -1001   2079       O  
ATOM   4170  CB  GLU A 537     116.928   7.180  49.099  1.00227.16           C  
ANISOU 4170  CB  GLU A 537    33910  22394  30006  -2285  -1105   2219       C  
ATOM   4171  CG  GLU A 537     116.838   7.305  50.611  1.00230.21           C  
ANISOU 4171  CG  GLU A 537    34246  22820  30402  -2510  -1112   2437       C  
ATOM   4172  CD  GLU A 537     117.852   6.433  51.327  1.00231.38           C  
ANISOU 4172  CD  GLU A 537    34573  22532  30807  -2670  -1022   2772       C  
ATOM   4173  OE1 GLU A 537     118.118   5.311  50.847  1.00232.75           O  
ANISOU 4173  OE1 GLU A 537    34864  22427  31145  -2787   -934   2742       O  
ATOM   4174  OE2 GLU A 537     118.381   6.870  52.370  1.00229.95           O1-
ANISOU 4174  OE2 GLU A 537    34417  22289  30665  -2677  -1040   3063       O1-
ATOM   4175  N   CYS A 538     118.947   7.960  46.229  1.00209.89           N  
ANISOU 4175  N   CYS A 538    32008  19829  27910  -1419  -1123   2253       N  
ATOM   4176  CA  CYS A 538     119.166   7.625  44.827  1.00206.49           C  
ANISOU 4176  CA  CYS A 538    31657  19286  27513  -1232  -1097   2080       C  
ATOM   4177  C   CYS A 538     120.583   7.107  44.618  1.00201.50           C  
ANISOU 4177  C   CYS A 538    31253  18182  27128  -1131  -1028   2369       C  
ATOM   4178  O   CYS A 538     121.540   7.651  45.170  1.00196.75           O  
ANISOU 4178  O   CYS A 538    30736  17420  26598   -994  -1041   2683       O  
ATOM   4179  CB  CYS A 538     118.908   8.839  43.932  1.00205.20           C  
ANISOU 4179  CB  CYS A 538    31408  19421  27139   -873  -1189   1901       C  
ATOM   4180  SG  CYS A 538     117.172   9.331  43.824  1.00266.60           S  
ANISOU 4180  SG  CYS A 538    38924  27750  34621   -967  -1268   1484       S  
ATOM   4181  N   LEU A 539     120.711   6.052  43.820  1.00201.36           N  
ANISOU 4181  N   LEU A 539    31329  17941  27238  -1198   -954   2257       N  
ATOM   4182  CA  LEU A 539     122.008   5.432  43.573  1.00198.23           C  
ANISOU 4182  CA  LEU A 539    31149  17086  27082  -1127   -884   2508       C  
ATOM   4183  C   LEU A 539     122.717   6.101  42.400  1.00197.23           C  
ANISOU 4183  C   LEU A 539    31104  16899  26934   -715   -914   2501       C  
ATOM   4184  O   LEU A 539     122.205   6.107  41.281  1.00195.77           O  
ANISOU 4184  O   LEU A 539    30873  16862  26651   -591   -930   2211       O  
ATOM   4185  CB  LEU A 539     121.840   3.933  43.311  1.00194.86           C  
ANISOU 4185  CB  LEU A 539    30789  16433  26817  -1407   -788   2404       C  
ATOM   4186  CG  LEU A 539     123.051   3.030  43.569  1.00189.29           C  
ANISOU 4186  CG  LEU A 539    30296  15237  26389  -1487   -701   2706       C  
ATOM   4187  CD1 LEU A 539     122.631   1.568  43.573  1.00191.06           C  
ANISOU 4187  CD1 LEU A 539    30543  15307  26745  -1833   -613   2586       C  
ATOM   4188  CD2 LEU A 539     124.157   3.272  42.550  1.00184.97           C  
ANISOU 4188  CD2 LEU A 539    29905  14447  25929  -1141   -698   2805       C  
ATOM   4189  N   PRO A 540     123.906   6.668  42.660  1.00198.09           N  
ANISOU 4189  N   PRO A 540    31338  16791  27137   -501   -923   2822       N  
ATOM   4190  CA  PRO A 540     124.725   7.352  41.655  1.00197.13           C  
ANISOU 4190  CA  PRO A 540    31309  16580  27013   -101   -948   2867       C  
ATOM   4191  C   PRO A 540     124.984   6.478  40.433  1.00198.95           C  
ANISOU 4191  C   PRO A 540    31650  16591  27351    -48   -888   2725       C  
ATOM   4192  O   PRO A 540     125.846   5.600  40.473  1.00198.10           O  
ANISOU 4192  O   PRO A 540    31708  16093  27469   -131   -812   2910       O  
ATOM   4193  CB  PRO A 540     126.041   7.617  42.405  1.00195.46           C  
ANISOU 4193  CB  PRO A 540    31245  16055  26967    -12   -932   3282       C  
ATOM   4194  CG  PRO A 540     125.996   6.688  43.597  1.00197.28           C  
ANISOU 4194  CG  PRO A 540    31499  16121  27336   -397   -873   3436       C  
ATOM   4195  CD  PRO A 540     124.558   6.699  43.977  1.00198.83           C  
ANISOU 4195  CD  PRO A 540    31491  16705  27349   -629   -908   3171       C  
ATOM   4196  N   GLN A 541     124.239   6.722  39.360  1.00202.56           N  
ANISOU 4196  N   GLN A 541    32014  17300  27648     92   -923   2396       N  
ATOM   4197  CA  GLN A 541     124.394   5.961  38.127  1.00206.27           C  
ANISOU 4197  CA  GLN A 541    32572  17601  28198    162   -874   2230       C  
ATOM   4198  C   GLN A 541     125.611   6.439  37.343  1.00211.76           C  
ANISOU 4198  C   GLN A 541    33424  18061  28973    532   -873   2398       C  
ATOM   4199  O   GLN A 541     125.676   7.595  36.925  1.00211.73           O  
ANISOU 4199  O   GLN A 541    33377  18249  28822    844   -941   2371       O  
ATOM   4200  CB  GLN A 541     123.136   6.082  37.265  1.00203.70           C  
ANISOU 4200  CB  GLN A 541    32087  17643  27666    187   -914   1810       C  
ATOM   4201  CG  GLN A 541     121.851   5.715  37.988  1.00203.34           C  
ANISOU 4201  CG  GLN A 541    31870  17870  27520   -159   -921   1615       C  
ATOM   4202  CD  GLN A 541     121.777   4.243  38.335  1.00205.33           C  
ANISOU 4202  CD  GLN A 541    32181  17874  27962   -523   -828   1624       C  
ATOM   4203  NE2 GLN A 541     120.935   3.905  39.305  1.00206.59           N  
ANISOU 4203  NE2 GLN A 541    32224  18187  28083   -853   -822   1572       N  
ATOM   4204  OE1 GLN A 541     122.465   3.417  37.736  1.00205.94           O  
ANISOU 4204  OE1 GLN A 541    32406  17624  28219   -509   -763   1676       O  
ATOM   4205  N   ALA A 542     126.573   5.543  37.147  1.00216.26           N  
ANISOU 4205  N   ALA A 542    34176  18213  29778    494   -796   2571       N  
ATOM   4206  CA  ALA A 542     127.784   5.870  36.404  1.00217.10           C  
ANISOU 4206  CA  ALA A 542    34446  18056  29985    824   -786   2739       C  
ATOM   4207  C   ALA A 542     127.513   5.905  34.903  1.00220.69           C  
ANISOU 4207  C   ALA A 542    34894  18604  30354   1054   -796   2452       C  
ATOM   4208  O   ALA A 542     128.352   6.352  34.121  1.00218.02           O  
ANISOU 4208  O   ALA A 542    34664  18124  30050   1373   -800   2534       O  
ATOM   4209  CB  ALA A 542     128.890   4.875  36.724  1.00214.37           C  
ANISOU 4209  CB  ALA A 542    34297  17232  29920    694   -701   3016       C  
ATOM   4210  N   MET A 543     126.337   5.429  34.509  1.00226.23           N  
ANISOU 4210  N   MET A 543    35467  19544  30946    891   -799   2115       N  
ATOM   4211  CA  MET A 543     125.951   5.406  33.103  1.00229.98           C  
ANISOU 4211  CA  MET A 543    35920  20132  31330   1085   -810   1813       C  
ATOM   4212  C   MET A 543     124.999   6.549  32.770  1.00231.15           C  
ANISOU 4212  C   MET A 543    35890  20741  31195   1268   -901   1565       C  
ATOM   4213  O   MET A 543     125.432   7.651  32.431  1.00229.30           O  
ANISOU 4213  O   MET A 543    35669  20587  30868   1599   -953   1637       O  
ATOM   4214  CB  MET A 543     125.309   4.064  32.744  1.00233.95           C  
ANISOU 4214  CB  MET A 543    36405  20575  31909    804   -750   1583       C  
ATOM   4215  CG  MET A 543     126.235   2.869  32.906  1.00235.28           C  
ANISOU 4215  CG  MET A 543    36754  20283  32358    636   -659   1797       C  
ATOM   4216  SD  MET A 543     127.716   2.987  31.883  1.00236.30           S  
ANISOU 4216  SD  MET A 543    37100  20046  32636   1001   -633   1984       S  
ATOM   4217  CE  MET A 543     126.993   3.112  30.249  1.00158.50           C  
ANISOU 4217  CE  MET A 543    27173  10428  22622   1234   -662   1573       C  
ATOM   4218  N   ASN A 544     123.701   6.281  32.868  1.00234.31           N  
ANISOU 4218  N   ASN A 544    36125  21443  31461   1051   -920   1272       N  
ATOM   4219  CA  ASN A 544     122.686   7.287  32.574  1.00234.69           C  
ANISOU 4219  CA  ASN A 544    35993  21944  31234   1192  -1007   1009       C  
ATOM   4220  C   ASN A 544     122.496   8.271  33.726  1.00237.77           C  
ANISOU 4220  C   ASN A 544    36283  22549  31509   1167  -1070   1160       C  
ATOM   4221  O   ASN A 544     123.334   8.356  34.625  1.00239.55           O  
ANISOU 4221  O   ASN A 544    36596  22557  31863   1123  -1051   1496       O  
ATOM   4222  CB  ASN A 544     121.352   6.621  32.221  1.00231.84           C  
ANISOU 4222  CB  ASN A 544    35491  21825  30773    971  -1004    625       C  
ATOM   4223  CG  ASN A 544     121.436   5.773  30.964  1.00228.05           C  
ANISOU 4223  CG  ASN A 544    35089  21185  30376   1035   -954    433       C  
ATOM   4224  ND2 ASN A 544     120.282   5.448  30.393  1.00227.33           N  
ANISOU 4224  ND2 ASN A 544    34866  21349  30159    945   -968     61       N  
ATOM   4225  OD1 ASN A 544     122.523   5.413  30.513  1.00225.94           O  
ANISOU 4225  OD1 ASN A 544    34995  20568  30284   1163   -906    615       O  
ATOM   4226  N   ILE A 545     121.393   9.013  33.693  1.00237.16           N  
ANISOU 4226  N   ILE A 545    36022  22901  31188   1197  -1145    910       N  
ATOM   4227  CA  ILE A 545     121.092   9.988  34.737  1.00232.18           C  
ANISOU 4227  CA  ILE A 545    35276  22517  30426   1176  -1214   1018       C  
ATOM   4228  C   ILE A 545     120.835   9.305  36.079  1.00231.38           C  
ANISOU 4228  C   ILE A 545    35142  22353  30420    775  -1178   1150       C  
ATOM   4229  O   ILE A 545     120.945   8.085  36.193  1.00235.35           O  
ANISOU 4229  O   ILE A 545    35719  22606  31097    522  -1098   1170       O  
ATOM   4230  CB  ILE A 545     119.879  10.863  34.363  1.00228.69           C  
ANISOU 4230  CB  ILE A 545    34636  22559  29696   1279  -1303    689       C  
ATOM   4231  CG1 ILE A 545     118.646   9.991  34.121  1.00229.56           C  
ANISOU 4231  CG1 ILE A 545    34631  22846  29747   1005  -1284    338       C  
ATOM   4232  CG2 ILE A 545     120.189  11.703  33.134  1.00225.61           C  
ANISOU 4232  CG2 ILE A 545    34278  22244  29199   1700  -1346    591       C  
ATOM   4233  CD1 ILE A 545     117.410  10.775  33.736  1.00228.43           C  
ANISOU 4233  CD1 ILE A 545    34293  23175  29324   1090  -1371     -5       C  
ATOM   4234  N   THR A 546     120.492  10.097  37.090  1.00224.58           N  
ANISOU 4234  N   THR A 546    34168  21720  29443    720  -1237   1239       N  
ATOM   4235  CA  THR A 546     120.277   9.569  38.434  1.00217.52           C  
ANISOU 4235  CA  THR A 546    33240  20779  28629    358  -1208   1385       C  
ATOM   4236  C   THR A 546     118.803   9.577  38.837  1.00212.60           C  
ANISOU 4236  C   THR A 546    32409  20549  27821    118  -1249   1099       C  
ATOM   4237  O   THR A 546     118.275   8.567  39.304  1.00214.63           O  
ANISOU 4237  O   THR A 546    32637  20760  28152   -227  -1195   1028       O  
ATOM   4238  CB  THR A 546     121.095  10.346  39.484  1.00213.29           C  
ANISOU 4238  CB  THR A 546    32745  20158  28136    433  -1236   1753       C  
ATOM   4239  CG2 THR A 546     120.907   9.736  40.865  1.00213.38           C  
ANISOU 4239  CG2 THR A 546    32733  20102  28240     56  -1201   1910       C  
ATOM   4240  OG1 THR A 546     122.484  10.309  39.134  1.00210.14           O  
ANISOU 4240  OG1 THR A 546    32544  19381  27919    649  -1196   2022       O  
ATOM   4241  N   CYS A 547     118.144  10.718  38.659  1.00202.97           N  
ANISOU 4241  N   CYS A 547    31044  19714  26362    300  -1343    935       N  
ATOM   4242  CA  CYS A 547     116.732  10.842  39.004  1.00193.10           C  
ANISOU 4242  CA  CYS A 547    29589  18862  24920     98  -1391    653       C  
ATOM   4243  C   CYS A 547     116.023  11.868  38.126  1.00182.01           C  
ANISOU 4243  C   CYS A 547    28058  17838  23261    372  -1481    363       C  
ATOM   4244  O   CYS A 547     116.649  12.534  37.302  1.00177.52           O  
ANISOU 4244  O   CYS A 547    27559  17227  22663    723  -1508    399       O  
ATOM   4245  CB  CYS A 547     116.568  11.219  40.478  1.00192.05           C  
ANISOU 4245  CB  CYS A 547    29376  18833  24761    -99  -1420    850       C  
ATOM   4246  SG  CYS A 547     116.954  12.944  40.851  1.00191.72           S  
ANISOU 4246  SG  CYS A 547    29278  19003  24562    229  -1529   1030       S  
ATOM   4247  N   THR A 548     114.712  11.988  38.311  1.00177.84           N  
ANISOU 4247  N   THR A 548    27343  17679  22549    209  -1528     76       N  
ATOM   4248  CA  THR A 548     113.909  12.934  37.545  1.00173.02           C  
ANISOU 4248  CA  THR A 548    26597  17459  21685    437  -1617   -224       C  
ATOM   4249  C   THR A 548     112.950  13.701  38.449  1.00169.43           C  
ANISOU 4249  C   THR A 548    25949  17396  21032    317  -1700   -304       C  
ATOM   4250  O   THR A 548     111.781  13.890  38.112  1.00167.10           O  
ANISOU 4250  O   THR A 548    25498  17446  20546    276  -1749   -643       O  
ATOM   4251  CB  THR A 548     113.097  12.224  36.445  1.00173.37           C  
ANISOU 4251  CB  THR A 548    26599  17593  21679    396  -1593   -611       C  
ATOM   4252  CG2 THR A 548     114.023  11.514  35.468  1.00172.84           C  
ANISOU 4252  CG2 THR A 548    26718  17157  21797    537  -1518   -549       C  
ATOM   4253  OG1 THR A 548     112.213  11.267  37.043  1.00173.79           O  
ANISOU 4253  OG1 THR A 548    26567  17701  21764     -4  -1552   -753       O  
ATOM   4254  N   GLY A 549     113.450  14.139  39.601  1.00169.82           N  
ANISOU 4254  N   GLY A 549    26008  17389  21128    262  -1716      8       N  
ATOM   4255  CA  GLY A 549     112.644  14.887  40.548  1.00172.61           C  
ANISOU 4255  CA  GLY A 549    26186  18092  21307    150  -1795    -28       C  
ATOM   4256  C   GLY A 549     113.324  15.043  41.894  1.00177.10           C  
ANISOU 4256  C   GLY A 549    26796  18505  21990     31  -1786    353       C  
ATOM   4257  O   GLY A 549     114.432  14.548  42.100  1.00179.03           O  
ANISOU 4257  O   GLY A 549    27210  18362  22452     32  -1717    646       O  
ATOM   4258  N   ARG A 550     112.658  15.734  42.814  1.00179.19           N  
ANISOU 4258  N   ARG A 550    26905  19073  22105    -70  -1858    346       N  
ATOM   4259  CA  ARG A 550     113.207  15.962  44.146  1.00181.02           C  
ANISOU 4259  CA  ARG A 550    27156  19199  22424   -183  -1860    693       C  
ATOM   4260  C   ARG A 550     112.951  14.775  45.069  1.00189.28           C  
ANISOU 4260  C   ARG A 550    28214  20089  23614   -606  -1780    756       C  
ATOM   4261  O   ARG A 550     113.869  14.268  45.715  1.00188.28           O  
ANISOU 4261  O   ARG A 550    28222  19622  23694   -700  -1716   1071       O  
ATOM   4262  CB  ARG A 550     112.623  17.238  44.756  1.00175.57           C  
ANISOU 4262  CB  ARG A 550    26293  18902  21513   -104  -1975    667       C  
ATOM   4263  CG  ARG A 550     112.933  18.499  43.968  1.00172.26           C  
ANISOU 4263  CG  ARG A 550    25861  18637  20953    318  -2057    640       C  
ATOM   4264  CD  ARG A 550     112.361  19.734  44.644  1.00170.74           C  
ANISOU 4264  CD  ARG A 550    25494  18829  20550    378  -2170    626       C  
ATOM   4265  NE  ARG A 550     112.639  20.950  43.884  1.00168.74           N  
ANISOU 4265  NE  ARG A 550    25226  18728  20160    783  -2249    595       N  
ATOM   4266  CZ  ARG A 550     111.856  21.423  42.919  1.00168.13           C  
ANISOU 4266  CZ  ARG A 550    25051  18948  19882    943  -2307    261       C  
ATOM   4267  NH1 ARG A 550     110.742  20.784  42.592  1.00169.62           N1+
ANISOU 4267  NH1 ARG A 550    25147  19316  19987    733  -2296    -75       N1+
ATOM   4268  NH2 ARG A 550     112.188  22.536  42.280  1.00165.76           N  
ANISOU 4268  NH2 ARG A 550    24747  18766  19468   1315  -2375    262       N  
ATOM   4269  N   GLY A 551     111.697  14.336  45.127  1.00196.44           N  
ANISOU 4269  N   GLY A 551    28980  21246  24412   -858  -1783    453       N  
ATOM   4270  CA  GLY A 551     111.313  13.226  45.979  1.00200.32           C  
ANISOU 4270  CA  GLY A 551    29463  21628  25021  -1269  -1709    477       C  
ATOM   4271  C   GLY A 551     111.842  11.893  45.486  1.00202.17           C  
ANISOU 4271  C   GLY A 551    29861  21474  25482  -1385  -1593    507       C  
ATOM   4272  O   GLY A 551     112.106  11.729  44.294  1.00200.93           O  
ANISOU 4272  O   GLY A 551    29778  21220  25346  -1185  -1576    379       O  
ATOM   4273  N   PRO A 552     111.999  10.930  46.406  1.00204.38           N  
ANISOU 4273  N   PRO A 552    30195  21527  25933  -1711  -1514    676       N  
ATOM   4274  CA  PRO A 552     112.503   9.583  46.112  1.00207.66           C  
ANISOU 4274  CA  PRO A 552    30764  21557  26580  -1868  -1399    731       C  
ATOM   4275  C   PRO A 552     111.632   8.848  45.098  1.00212.81           C  
ANISOU 4275  C   PRO A 552    31363  22304  27189  -1951  -1369    345       C  
ATOM   4276  O   PRO A 552     112.002   7.768  44.637  1.00215.66           O  
ANISOU 4276  O   PRO A 552    31845  22368  27728  -2042  -1280    344       O  
ATOM   4277  CB  PRO A 552     112.421   8.883  47.477  1.00206.70           C  
ANISOU 4277  CB  PRO A 552    30641  21320  26575  -2243  -1344    917       C  
ATOM   4278  CG  PRO A 552     111.423   9.700  48.256  1.00205.11           C  
ANISOU 4278  CG  PRO A 552    30240  21532  26160  -2332  -1429    813       C  
ATOM   4279  CD  PRO A 552     111.742  11.094  47.844  1.00202.89           C  
ANISOU 4279  CD  PRO A 552    29927  21433  25729  -1948  -1530    845       C  
ATOM   4280  N   ASP A 553     110.489   9.433  44.757  1.00213.23           N  
ANISOU 4280  N   ASP A 553    31238  22770  27011  -1917  -1443     20       N  
ATOM   4281  CA  ASP A 553     109.558   8.820  43.817  1.00213.63           C  
ANISOU 4281  CA  ASP A 553    31218  22952  26998  -1991  -1423   -371       C  
ATOM   4282  C   ASP A 553     110.133   8.785  42.406  1.00214.05           C  
ANISOU 4282  C   ASP A 553    31383  22855  27089  -1685  -1412   -457       C  
ATOM   4283  O   ASP A 553     109.588   8.125  41.521  1.00215.16           O  
ANISOU 4283  O   ASP A 553    31504  23020  27226  -1727  -1380   -746       O  
ATOM   4284  CB  ASP A 553     108.231   9.584  43.807  1.00211.30           C  
ANISOU 4284  CB  ASP A 553    30705  23148  26434  -1999  -1516   -691       C  
ATOM   4285  CG  ASP A 553     107.637   9.742  45.192  1.00209.89           C  
ANISOU 4285  CG  ASP A 553    30405  23147  26197  -2278  -1538   -613       C  
ATOM   4286  OD1 ASP A 553     108.203   9.183  46.153  1.00211.61           O  
ANISOU 4286  OD1 ASP A 553    30708  23107  26588  -2483  -1475   -324       O  
ATOM   4287  OD2 ASP A 553     106.600  10.428  45.318  1.00207.50           O1-
ANISOU 4287  OD2 ASP A 553    29922  23243  25674  -2292  -1618   -841       O1-
ATOM   4288  N   ASN A 554     111.236   9.497  42.201  1.00213.05           N  
ANISOU 4288  N   ASN A 554    31372  22575  27002  -1376  -1438   -205       N  
ATOM   4289  CA  ASN A 554     111.809   9.646  40.869  1.00213.79           C  
ANISOU 4289  CA  ASN A 554    31566  22553  27111  -1047  -1438   -274       C  
ATOM   4290  C   ASN A 554     113.220   9.078  40.746  1.00213.75           C  
ANISOU 4290  C   ASN A 554    31784  22072  27359   -971  -1360     43       C  
ATOM   4291  O   ASN A 554     113.990   9.495  39.881  1.00213.46           O  
ANISOU 4291  O   ASN A 554    31849  21914  27341   -647  -1371    102       O  
ATOM   4292  CB  ASN A 554     111.803  11.120  40.459  1.00212.60           C  
ANISOU 4292  CB  ASN A 554    31346  22680  26751   -684  -1546   -315       C  
ATOM   4293  CG  ASN A 554     110.443  11.769  40.638  1.00213.27           C  
ANISOU 4293  CG  ASN A 554    31211  23243  26580   -749  -1632   -612       C  
ATOM   4294  ND2 ASN A 554     109.386  10.980  40.489  1.00215.86           N  
ANISOU 4294  ND2 ASN A 554    31444  23701  26873  -1006  -1603   -914       N  
ATOM   4295  OD1 ASN A 554     110.345  12.965  40.912  1.00211.36           O  
ANISOU 4295  OD1 ASN A 554    30884  23248  26174   -573  -1722   -572       O  
ATOM   4296  N   CYS A 555     113.555   8.125  41.609  1.00213.59           N  
ANISOU 4296  N   CYS A 555    31839  21782  27533  -1270  -1280    246       N  
ATOM   4297  CA  CYS A 555     114.873   7.501  41.580  1.00211.87           C  
ANISOU 4297  CA  CYS A 555    31834  21102  27566  -1232  -1202    550       C  
ATOM   4298  C   CYS A 555     114.907   6.319  40.617  1.00214.87           C  
ANISOU 4298  C   CYS A 555    32300  21261  28079  -1299  -1122    385       C  
ATOM   4299  O   CYS A 555     113.964   5.530  40.556  1.00217.40           O  
ANISOU 4299  O   CYS A 555    32533  21684  28383  -1557  -1089    133       O  
ATOM   4300  CB  CYS A 555     115.281   7.043  42.982  1.00209.98           C  
ANISOU 4300  CB  CYS A 555    31645  20661  27477  -1512  -1154    863       C  
ATOM   4301  SG  CYS A 555     115.419   8.374  44.194  1.00186.75           S  
ANISOU 4301  SG  CYS A 555    28621  17923  24413  -1433  -1243   1109       S  
ATOM   4302  N   ILE A 556     115.997   6.202  39.866  1.00215.42           N  
ANISOU 4302  N   ILE A 556    32540  21028  28282  -1065  -1090    528       N  
ATOM   4303  CA  ILE A 556     116.175   5.082  38.949  1.00219.20           C  
ANISOU 4303  CA  ILE A 556    33118  21261  28907  -1110  -1013    406       C  
ATOM   4304  C   ILE A 556     116.464   3.803  39.729  1.00222.80           C  
ANISOU 4304  C   ILE A 556    33661  21400  29591  -1466   -915    576       C  
ATOM   4305  O   ILE A 556     116.124   2.703  39.291  1.00223.66           O  
ANISOU 4305  O   ILE A 556    33786  21401  29794  -1650   -850    405       O  
ATOM   4306  CB  ILE A 556     117.315   5.345  37.945  1.00215.72           C  
ANISOU 4306  CB  ILE A 556    32839  20576  28548   -751  -1008    527       C  
ATOM   4307  CG1 ILE A 556     117.022   6.602  37.125  1.00212.22           C  
ANISOU 4307  CG1 ILE A 556    32311  20446  27877   -390  -1102    351       C  
ATOM   4308  CG2 ILE A 556     117.509   4.148  37.026  1.00217.22           C  
ANISOU 4308  CG2 ILE A 556    33132  20506  28896   -808   -928    406       C  
ATOM   4309  CD1 ILE A 556     118.022   6.854  36.019  1.00210.13           C  
ANISOU 4309  CD1 ILE A 556    32195  19971  27675    -31  -1097    423       C  
ATOM   4310  N   GLN A 557     117.090   3.959  40.892  1.00222.98           N  
ANISOU 4310  N   GLN A 557    33742  21278  29704  -1560   -905    913       N  
ATOM   4311  CA  GLN A 557     117.400   2.829  41.759  1.00222.78           C  
ANISOU 4311  CA  GLN A 557    33801  20955  29889  -1897   -816   1104       C  
ATOM   4312  C   GLN A 557     117.781   3.315  43.155  1.00223.39           C  
ANISOU 4312  C   GLN A 557    33881  21009  29986  -1989   -833   1423       C  
ATOM   4313  O   GLN A 557     118.503   4.301  43.303  1.00220.48           O  
ANISOU 4313  O   GLN A 557    33556  20631  29585  -1729   -886   1633       O  
ATOM   4314  CB  GLN A 557     118.530   1.987  41.162  1.00218.74           C  
ANISOU 4314  CB  GLN A 557    33499  19997  29617  -1833   -738   1263       C  
ATOM   4315  CG  GLN A 557     118.736   0.647  41.849  1.00216.38           C  
ANISOU 4315  CG  GLN A 557    33285  19392  29538  -2193   -638   1397       C  
ATOM   4316  CD  GLN A 557     119.771  -0.211  41.149  1.00214.01           C  
ANISOU 4316  CD  GLN A 557    33181  18669  29463  -2128   -565   1515       C  
ATOM   4317  NE2 GLN A 557     119.808  -1.493  41.493  1.00214.34           N  
ANISOU 4317  NE2 GLN A 557    33288  18464  29689  -2439   -476   1555       N  
ATOM   4318  OE1 GLN A 557     120.530   0.273  40.309  1.00212.61           O  
ANISOU 4318  OE1 GLN A 557    33098  18389  29296  -1801   -588   1569       O  
ATOM   4319  N   CYS A 558     117.289   2.619  44.175  1.00225.90           N  
ANISOU 4319  N   CYS A 558    34152  21321  30360  -2356   -789   1456       N  
ATOM   4320  CA  CYS A 558     117.540   3.006  45.560  1.00224.89           C  
ANISOU 4320  CA  CYS A 558    34014  21187  30246  -2476   -803   1741       C  
ATOM   4321  C   CYS A 558     118.939   2.605  46.017  1.00224.85           C  
ANISOU 4321  C   CYS A 558    34217  20735  30481  -2462   -744   2133       C  
ATOM   4322  O   CYS A 558     119.514   1.639  45.517  1.00226.08           O  
ANISOU 4322  O   CYS A 558    34514  20565  30822  -2506   -668   2173       O  
ATOM   4323  CB  CYS A 558     116.490   2.389  46.486  1.00225.55           C  
ANISOU 4323  CB  CYS A 558    33973  21425  30300  -2877   -774   1631       C  
ATOM   4324  SG  CYS A 558     114.791   2.876  46.113  1.00222.83           S  
ANISOU 4324  SG  CYS A 558    33373  21619  29671  -2924   -846   1176       S  
ATOM   4325  N   ALA A 559     119.481   3.356  46.971  1.00222.83           N  
ANISOU 4325  N   ALA A 559    33977  20468  30220  -2399   -781   2420       N  
ATOM   4326  CA  ALA A 559     120.796   3.062  47.526  1.00219.71           C  
ANISOU 4326  CA  ALA A 559    33772  19666  30043  -2386   -732   2805       C  
ATOM   4327  C   ALA A 559     120.691   2.009  48.622  1.00222.29           C  
ANISOU 4327  C   ALA A 559    34129  19817  30515  -2784   -654   2936       C  
ATOM   4328  O   ALA A 559     121.651   1.292  48.904  1.00221.07           O  
ANISOU 4328  O   ALA A 559    34145  19272  30579  -2855   -584   3188       O  
ATOM   4329  CB  ALA A 559     121.441   4.329  48.064  1.00213.87           C  
ANISOU 4329  CB  ALA A 559    33035  18985  29240  -2136   -805   3055       C  
ATOM   4330  N   HIS A 560     119.516   1.924  49.238  1.00224.98           N  
ANISOU 4330  N   HIS A 560    34303  20448  30731  -3042   -666   2762       N  
ATOM   4331  CA  HIS A 560     119.263   0.939  50.282  1.00226.60           C  
ANISOU 4331  CA  HIS A 560    34517  20528  31053  -3435   -592   2854       C  
ATOM   4332  C   HIS A 560     118.008   0.124  49.980  1.00230.86           C  
ANISOU 4332  C   HIS A 560    34934  21247  31534  -3706   -556   2506       C  
ATOM   4333  O   HIS A 560     117.983  -0.671  49.040  1.00230.24           O  
ANISOU 4333  O   HIS A 560    34910  21034  31537  -3720   -505   2339       O  
ATOM   4334  CB  HIS A 560     119.130   1.617  51.648  1.00223.99           C  
ANISOU 4334  CB  HIS A 560    34108  20349  30647  -3527   -636   3048       C  
ATOM   4335  CG  HIS A 560     120.428   2.111  52.208  1.00220.25           C  
ANISOU 4335  CG  HIS A 560    33775  19621  30287  -3351   -646   3438       C  
ATOM   4336  CD2 HIS A 560     121.414   1.466  52.875  1.00219.25           C  
ANISOU 4336  CD2 HIS A 560    33817  19109  30381  -3459   -578   3756       C  
ATOM   4337  ND1 HIS A 560     120.828   3.426  52.112  1.00217.15           N  
ANISOU 4337  ND1 HIS A 560    33357  19371  29781  -3021   -736   3532       N  
ATOM   4338  CE1 HIS A 560     122.006   3.570  52.694  1.00214.39           C  
ANISOU 4338  CE1 HIS A 560    33150  18730  29578  -2932   -722   3889       C  
ATOM   4339  NE2 HIS A 560     122.383   2.395  53.164  1.00216.01           N  
ANISOU 4339  NE2 HIS A 560    33476  18612  29985  -3193   -628   4030       N  
ATOM   4340  N   TYR A 561     116.969   0.331  50.782  1.00235.08           N  
ANISOU 4340  N   TYR A 561    35302  22087  31930  -3918   -583   2395       N  
ATOM   4341  CA  TYR A 561     115.728  -0.420  50.638  1.00239.46           C  
ANISOU 4341  CA  TYR A 561    35730  22826  32428  -4199   -547   2072       C  
ATOM   4342  C   TYR A 561     114.667   0.389  49.899  1.00234.11           C  
ANISOU 4342  C   TYR A 561    34868  22583  31499  -4050   -633   1716       C  
ATOM   4343  O   TYR A 561     114.870   1.564  49.593  1.00231.25           O  
ANISOU 4343  O   TYR A 561    34471  22392  31000  -3742   -721   1732       O  
ATOM   4344  CB  TYR A 561     115.200  -0.846  52.010  1.00247.01           C  
ANISOU 4344  CB  TYR A 561    36622  23828  33404  -4566   -511   2163       C  
ATOM   4345  CG  TYR A 561     116.273  -1.370  52.938  1.00251.24           C  
ANISOU 4345  CG  TYR A 561    37327  23978  34157  -4682   -446   2555       C  
ATOM   4346  CD1 TYR A 561     116.719  -0.611  54.012  1.00251.23           C  
ANISOU 4346  CD1 TYR A 561    37330  23995  34131  -4639   -489   2840       C  
ATOM   4347  CD2 TYR A 561     116.846  -2.618  52.735  1.00253.92           C  
ANISOU 4347  CD2 TYR A 561    37822  23932  34724  -4829   -344   2638       C  
ATOM   4348  CE1 TYR A 561     117.701  -1.083  54.862  1.00252.29           C  
ANISOU 4348  CE1 TYR A 561    37620  23776  34461  -4739   -430   3195       C  
ATOM   4349  CE2 TYR A 561     117.828  -3.099  53.580  1.00255.03           C  
ANISOU 4349  CE2 TYR A 561    38120  23717  35061  -4933   -285   2993       C  
ATOM   4350  CZ  TYR A 561     118.252  -2.327  54.641  1.00255.17           C  
ANISOU 4350  CZ  TYR A 561    38142  23762  35051  -4886   -329   3269       C  
ATOM   4351  OH  TYR A 561     119.231  -2.801  55.485  1.00257.11           O  
ANISOU 4351  OH  TYR A 561    38545  23654  35490  -4985   -272   3619       O  
ATOM   4352  N   ILE A 562     113.536  -0.249  49.615  1.00232.55           N  
ANISOU 4352  N   ILE A 562    34554  22562  31244  -4271   -605   1392       N  
ATOM   4353  CA  ILE A 562     112.438   0.407  48.914  1.00229.10           C  
ANISOU 4353  CA  ILE A 562    33937  22539  30571  -4161   -681   1026       C  
ATOM   4354  C   ILE A 562     111.086   0.049  49.526  1.00225.40           C  
ANISOU 4354  C   ILE A 562    33293  22348  30002  -4498   -671    794       C  
ATOM   4355  O   ILE A 562     110.672  -1.111  49.514  1.00227.74           O  
ANISOU 4355  O   ILE A 562    33595  22530  30407  -4776   -586    675       O  
ATOM   4356  CB  ILE A 562     112.438   0.059  47.409  1.00230.96           C  
ANISOU 4356  CB  ILE A 562    34212  22722  30822  -3984   -668    776       C  
ATOM   4357  CG1 ILE A 562     111.177   0.603  46.735  1.00230.53           C  
ANISOU 4357  CG1 ILE A 562    33962  23102  30526  -3916   -738    369       C  
ATOM   4358  CG2 ILE A 562     112.553  -1.445  47.204  1.00234.51           C  
ANISOU 4358  CG2 ILE A 562    34759  22860  31485  -4235   -553    748       C  
ATOM   4359  CD1 ILE A 562     111.110   0.322  45.249  1.00230.77           C  
ANISOU 4359  CD1 ILE A 562    34019  23110  30554  -3731   -732    106       C  
ATOM   4360  N   ASP A 563     110.403   1.054  50.065  1.00218.61           N  
ANISOU 4360  N   ASP A 563    32276  21852  28935  -4470   -757    731       N  
ATOM   4361  CA  ASP A 563     109.097   0.853  50.682  1.00214.25           C  
ANISOU 4361  CA  ASP A 563    31546  21593  28267  -4771   -758    512       C  
ATOM   4362  C   ASP A 563     107.986   1.382  49.782  1.00204.67           C  
ANISOU 4362  C   ASP A 563    30163  20774  26830  -4656   -829     99       C  
ATOM   4363  O   ASP A 563     107.467   2.477  49.999  1.00200.24           O  
ANISOU 4363  O   ASP A 563    29466  20554  26061  -4540   -926     22       O  
ATOM   4364  CB  ASP A 563     109.040   1.541  52.048  1.00216.89           C  
ANISOU 4364  CB  ASP A 563    31815  22065  28529  -4864   -802    732       C  
ATOM   4365  CG  ASP A 563     107.739   1.279  52.779  1.00221.55           C  
ANISOU 4365  CG  ASP A 563    32230  22934  29015  -5196   -796    531       C  
ATOM   4366  OD1 ASP A 563     107.493   1.936  53.813  1.00220.06           O  
ANISOU 4366  OD1 ASP A 563    31955  22929  28728  -5264   -845    650       O  
ATOM   4367  OD2 ASP A 563     106.961   0.417  52.320  1.00226.18           O1-
ANISOU 4367  OD2 ASP A 563    32764  23556  29619  -5389   -741    252       O1-
ATOM   4368  N   GLY A 564     107.623   0.596  48.775  1.00202.18           N  
ANISOU 4368  N   GLY A 564    29852  20407  26558  -4689   -781   -169       N  
ATOM   4369  CA  GLY A 564     106.616   1.007  47.815  1.00201.26           C  
ANISOU 4369  CA  GLY A 564    29589  20635  26245  -4570   -843   -572       C  
ATOM   4370  C   GLY A 564     107.186   1.992  46.813  1.00200.23           C  
ANISOU 4370  C   GLY A 564    29501  20555  26022  -4137   -921   -580       C  
ATOM   4371  O   GLY A 564     108.304   1.811  46.330  1.00201.70           O  
ANISOU 4371  O   GLY A 564    29858  20423  26355  -3956   -890   -385       O  
ATOM   4372  N   PRO A 565     106.418   3.043  46.492  1.00195.39           N  
ANISOU 4372  N   PRO A 565    28734  20342  25163  -3969  -1023   -809       N  
ATOM   4373  CA  PRO A 565     106.866   4.095  45.574  1.00190.69           C  
ANISOU 4373  CA  PRO A 565    28161  19838  24453  -3550  -1106   -832       C  
ATOM   4374  C   PRO A 565     108.109   4.812  46.095  1.00191.04           C  
ANISOU 4374  C   PRO A 565    28328  19695  24561  -3347  -1133   -425       C  
ATOM   4375  O   PRO A 565     109.089   4.955  45.362  1.00190.29           O  
ANISOU 4375  O   PRO A 565    28374  19380  24549  -3076  -1128   -299       O  
ATOM   4376  CB  PRO A 565     105.672   5.060  45.550  1.00186.19           C  
ANISOU 4376  CB  PRO A 565    27379  19760  23605  -3501  -1209  -1122       C  
ATOM   4377  CG  PRO A 565     104.905   4.740  46.806  1.00187.24           C  
ANISOU 4377  CG  PRO A 565    27401  20020  23720  -3873  -1190  -1113       C  
ATOM   4378  CD  PRO A 565     105.025   3.260  46.909  1.00192.46           C  
ANISOU 4378  CD  PRO A 565    28154  20366  24606  -4167  -1065  -1088       C  
ATOM   4379  N   HIS A 566     108.063   5.249  47.350  1.00193.34           N  
ANISOU 4379  N   HIS A 566    28567  20075  24819  -3479  -1159   -225       N  
ATOM   4380  CA  HIS A 566     109.161   5.999  47.953  1.00193.32           C  
ANISOU 4380  CA  HIS A 566    28661  19927  24864  -3296  -1191    156       C  
ATOM   4381  C   HIS A 566     110.344   5.100  48.297  1.00201.55           C  
ANISOU 4381  C   HIS A 566    29909  20489  26181  -3385  -1093    488       C  
ATOM   4382  O   HIS A 566     110.165   3.985  48.784  1.00208.01           O  
ANISOU 4382  O   HIS A 566    30757  21139  27139  -3709  -1005    507       O  
ATOM   4383  CB  HIS A 566     108.685   6.713  49.221  1.00187.97           C  
ANISOU 4383  CB  HIS A 566    27854  19503  24063  -3424  -1251    256       C  
ATOM   4384  CG  HIS A 566     107.384   7.434  49.058  1.00186.08           C  
ANISOU 4384  CG  HIS A 566    27401  19741  23562  -3417  -1339    -81       C  
ATOM   4385  CD2 HIS A 566     107.111   8.736  48.801  1.00182.17           C  
ANISOU 4385  CD2 HIS A 566    26798  19566  22851  -3152  -1453   -172       C  
ATOM   4386  ND1 HIS A 566     106.164   6.803  49.169  1.00187.80           N  
ANISOU 4386  ND1 HIS A 566    27487  20152  23718  -3712  -1314   -376       N  
ATOM   4387  CE1 HIS A 566     105.196   7.683  48.982  1.00184.83           C  
ANISOU 4387  CE1 HIS A 566    26933  20195  23098  -3628  -1410   -636       C  
ATOM   4388  NE2 HIS A 566     105.744   8.863  48.757  1.00181.29           N  
ANISOU 4388  NE2 HIS A 566    26496  19833  22551  -3290  -1496   -518       N  
ATOM   4389  N   CYS A 567     111.552   5.594  48.046  1.00203.14           N  
ANISOU 4389  N   CYS A 567    30252  20472  26462  -3097  -1107    749       N  
ATOM   4390  CA  CYS A 567     112.763   4.879  48.432  1.00208.65           C  
ANISOU 4390  CA  CYS A 567    31149  20716  27414  -3153  -1024   1092       C  
ATOM   4391  C   CYS A 567     113.208   5.330  49.818  1.00215.44           C  
ANISOU 4391  C   CYS A 567    32018  21537  28303  -3233  -1042   1427       C  
ATOM   4392  O   CYS A 567     113.439   6.517  50.048  1.00215.04           O  
ANISOU 4392  O   CYS A 567    31924  21649  28133  -3005  -1128   1537       O  
ATOM   4393  CB  CYS A 567     113.877   5.110  47.410  1.00206.17           C  
ANISOU 4393  CB  CYS A 567    30991  20159  27183  -2803  -1024   1199       C  
ATOM   4394  SG  CYS A 567     113.534   4.434  45.768  1.00210.13           S  
ANISOU 4394  SG  CYS A 567    31514  20634  27691  -2709   -990    844       S  
ATOM   4395  N   VAL A 568     113.323   4.380  50.741  1.00222.35           N  
ANISOU 4395  N   VAL A 568    32950  22197  29338  -3556   -960   1589       N  
ATOM   4396  CA  VAL A 568     113.629   4.700  52.131  1.00225.30           C  
ANISOU 4396  CA  VAL A 568    33321  22543  29739  -3674   -971   1889       C  
ATOM   4397  C   VAL A 568     115.026   4.236  52.538  1.00231.92           C  
ANISOU 4397  C   VAL A 568    34373  22925  30822  -3655   -905   2276       C  
ATOM   4398  O   VAL A 568     115.588   3.321  51.936  1.00234.42           O  
ANISOU 4398  O   VAL A 568    34833  22923  31313  -3673   -827   2299       O  
ATOM   4399  CB  VAL A 568     112.589   4.079  53.085  1.00222.42           C  
ANISOU 4399  CB  VAL A 568    32836  22326  29345  -4079   -936   1787       C  
ATOM   4400  CG1 VAL A 568     112.707   4.690  54.473  1.00219.97           C  
ANISOU 4400  CG1 VAL A 568    32482  22096  29001  -4160   -974   2046       C  
ATOM   4401  CG2 VAL A 568     111.188   4.280  52.535  1.00221.76           C  
ANISOU 4401  CG2 VAL A 568    32559  22650  29052  -4130   -982   1367       C  
ATOM   4402  N   LYS A 569     115.578   4.878  53.563  1.00234.44           N  
ANISOU 4402  N   LYS A 569    34710  23216  31151  -3615   -939   2577       N  
ATOM   4403  CA  LYS A 569     116.892   4.523  54.088  1.00237.60           C  
ANISOU 4403  CA  LYS A 569    35304  23200  31774  -3600   -884   2959       C  
ATOM   4404  C   LYS A 569     116.821   3.214  54.867  1.00247.07           C  
ANISOU 4404  C   LYS A 569    36566  24164  33144  -3990   -779   3049       C  
ATOM   4405  O   LYS A 569     117.638   2.314  54.669  1.00250.89           O  
ANISOU 4405  O   LYS A 569    37223  24263  33841  -4036   -696   3193       O  
ATOM   4406  CB  LYS A 569     117.420   5.641  54.988  1.00231.51           C  
ANISOU 4406  CB  LYS A 569    34517  22498  30950  -3445   -956   3237       C  
ATOM   4407  CG  LYS A 569     118.861   5.463  55.434  1.00228.04           C  
ANISOU 4407  CG  LYS A 569    34277  21640  30726  -3362   -913   3632       C  
ATOM   4408  CD  LYS A 569     119.343   6.683  56.202  1.00224.97           C  
ANISOU 4408  CD  LYS A 569    33858  21352  30269  -3169   -995   3876       C  
ATOM   4409  CE  LYS A 569     120.814   6.571  56.564  1.00222.97           C  
ANISOU 4409  CE  LYS A 569    33805  20683  30228  -3054   -956   4261       C  
ATOM   4410  NZ  LYS A 569     121.306   7.799  57.249  1.00219.18           N1+
ANISOU 4410  NZ  LYS A 569    33293  20304  29683  -2841  -1039   4491       N1+
ATOM   4411  N   THR A 570     115.838   3.120  55.757  1.00249.95           N  
ANISOU 4411  N   THR A 570    36788  24765  33415  -4269   -783   2963       N  
ATOM   4412  CA  THR A 570     115.604   1.906  56.532  1.00250.24           C  
ANISOU 4412  CA  THR A 570    36861  24627  33593  -4659   -685   3017       C  
ATOM   4413  C   THR A 570     114.105   1.662  56.688  1.00253.05           C  
ANISOU 4413  C   THR A 570    37023  25327  33798  -4924   -688   2692       C  
ATOM   4414  O   THR A 570     113.346   2.587  56.977  1.00255.45           O  
ANISOU 4414  O   THR A 570    37159  26005  33895  -4881   -774   2573       O  
ATOM   4415  CB  THR A 570     116.262   1.981  57.924  1.00244.93           C  
ANISOU 4415  CB  THR A 570    36255  23788  33018  -4767   -671   3391       C  
ATOM   4416  CG2 THR A 570     117.776   1.881  57.807  1.00241.13           C  
ANISOU 4416  CG2 THR A 570    35992  22891  32737  -4574   -640   3716       C  
ATOM   4417  OG1 THR A 570     115.921   3.223  58.552  1.00242.02           O  
ANISOU 4417  OG1 THR A 570    35747  23745  32463  -4655   -773   3428       O  
ATOM   4418  N   CYS A 571     113.685   0.416  56.490  1.00250.73           N  
ANISOU 4418  N   CYS A 571    36752  24903  33610  -5196   -595   2547       N  
ATOM   4419  CA  CYS A 571     112.272   0.058  56.566  1.00247.73           C  
ANISOU 4419  CA  CYS A 571    36198  24820  33107  -5459   -586   2224       C  
ATOM   4420  C   CYS A 571     111.625   0.559  57.855  1.00242.64           C  
ANISOU 4420  C   CYS A 571    35417  24433  32343  -5639   -626   2287       C  
ATOM   4421  O   CYS A 571     112.238   0.508  58.922  1.00239.22           O  
ANISOU 4421  O   CYS A 571    35060  23825  32009  -5731   -603   2604       O  
ATOM   4422  CB  CYS A 571     112.095  -1.457  56.437  1.00249.81           C  
ANISOU 4422  CB  CYS A 571    36532  24838  33548  -5764   -465   2143       C  
ATOM   4423  SG  CYS A 571     112.667  -2.142  54.863  1.00279.72           S  
ANISOU 4423  SG  CYS A 571    40456  28357  37467  -5585   -418   2012       S  
ATOM   4424  N   PRO A 572     110.379   1.048  57.755  1.00242.25           N  
ANISOU 4424  N   PRO A 572    35165  24801  32077  -5687   -687   1982       N  
ATOM   4425  CA  PRO A 572     109.635   1.601  58.892  1.00244.60           C  
ANISOU 4425  CA  PRO A 572    35311  25394  32233  -5847   -735   1997       C  
ATOM   4426  C   PRO A 572     109.594   0.643  60.079  1.00252.28           C  
ANISOU 4426  C   PRO A 572    36324  26182  33347  -6222   -642   2171       C  
ATOM   4427  O   PRO A 572     109.403  -0.559  59.895  1.00257.65           O  
ANISOU 4427  O   PRO A 572    37058  26677  34161  -6457   -542   2082       O  
ATOM   4428  CB  PRO A 572     108.226   1.792  58.324  1.00242.87           C  
ANISOU 4428  CB  PRO A 572    34893  25578  31810  -5906   -779   1569       C  
ATOM   4429  CG  PRO A 572     108.435   1.974  56.865  1.00240.97           C  
ANISOU 4429  CG  PRO A 572    34688  25326  31543  -5617   -804   1381       C  
ATOM   4430  CD  PRO A 572     109.597   1.095  56.508  1.00241.34           C  
ANISOU 4430  CD  PRO A 572    34955  24904  31839  -5587   -714   1592       C  
ATOM   4431  N   ALA A 573     109.771   1.178  61.283  1.00252.91           N  
ANISOU 4431  N   ALA A 573    36380  26316  33398  -6272   -675   2416       N  
ATOM   4432  CA  ALA A 573     109.753   0.365  62.494  1.00254.29           C  
ANISOU 4432  CA  ALA A 573    36592  26330  33697  -6615   -592   2602       C  
ATOM   4433  C   ALA A 573     109.188   1.143  63.679  1.00252.80           C  
ANISOU 4433  C   ALA A 573    36260  26436  33358  -6709   -657   2671       C  
ATOM   4434  O   ALA A 573     109.901   1.430  64.641  1.00251.11           O  
ANISOU 4434  O   ALA A 573    36112  26090  33206  -6696   -664   2999       O  
ATOM   4435  CB  ALA A 573     111.151  -0.146  62.809  1.00253.45           C  
ANISOU 4435  CB  ALA A 573    36711  25760  33828  -6577   -525   2976       C  
ATOM   4436  N   GLY A 574     107.904   1.481  63.603  1.00275.41           N  
ANISOU 4436  N   GLY A 574    29775  35067  39802  -5322  -3361   1432       N  
ATOM   4437  CA  GLY A 574     107.244   2.216  64.666  1.00271.78           C  
ANISOU 4437  CA  GLY A 574    29011  34921  39331  -5169  -3481   1387       C  
ATOM   4438  C   GLY A 574     106.220   3.209  64.149  1.00267.28           C  
ANISOU 4438  C   GLY A 574    28333  34395  38826  -5331  -3642   1346       C  
ATOM   4439  O   GLY A 574     105.601   3.937  64.925  1.00265.67           O  
ANISOU 4439  O   GLY A 574    27873  34444  38624  -5226  -3757   1300       O  
ATOM   4440  N   VAL A 575     106.041   3.237  62.832  1.00264.48           N  
ANISOU 4440  N   VAL A 575    28175  33791  38523  -5588  -3648   1362       N  
ATOM   4441  CA  VAL A 575     105.094   4.152  62.205  1.00260.52           C  
ANISOU 4441  CA  VAL A 575    27599  33300  38087  -5765  -3795   1325       C  
ATOM   4442  C   VAL A 575     103.660   3.844  62.627  1.00261.44           C  
ANISOU 4442  C   VAL A 575    27654  33581  38102  -5871  -3847   1467       C  
ATOM   4443  O   VAL A 575     103.240   2.687  62.636  1.00262.06           O  
ANISOU 4443  O   VAL A 575    27901  33604  38067  -5977  -3748   1639       O  
ATOM   4444  CB  VAL A 575     105.191   4.098  60.667  1.00255.65           C  
ANISOU 4444  CB  VAL A 575    27236  32364  37537  -6033  -3776   1331       C  
ATOM   4445  CG1 VAL A 575     104.179   5.043  60.037  1.00253.37           C  
ANISOU 4445  CG1 VAL A 575    26866  32091  37312  -6215  -3930   1294       C  
ATOM   4446  CG2 VAL A 575     106.601   4.439  60.212  1.00253.33           C  
ANISOU 4446  CG2 VAL A 575    27002  31902  37348  -5934  -3729   1187       C  
ATOM   4447  N   MET A 576     102.915   4.888  62.978  1.00261.25           N  
ANISOU 4447  N   MET A 576    27387  33758  38120  -5842  -4001   1394       N  
ATOM   4448  CA  MET A 576     101.521   4.737  63.380  1.00260.45           C  
ANISOU 4448  CA  MET A 576    27204  33825  37932  -5939  -4067   1514       C  
ATOM   4449  C   MET A 576     100.664   4.244  62.218  1.00256.98           C  
ANISOU 4449  C   MET A 576    26998  33176  37466  -6273  -4058   1642       C  
ATOM   4450  O   MET A 576     100.800   4.716  61.090  1.00258.00           O  
ANISOU 4450  O   MET A 576    27235  33105  37689  -6435  -4094   1579       O  
ATOM   4451  CB  MET A 576     100.971   6.063  63.912  1.00260.44           C  
ANISOU 4451  CB  MET A 576    26891  34068  37995  -5840  -4241   1391       C  
ATOM   4452  CG  MET A 576      99.492   6.029  64.269  1.00260.80           C  
ANISOU 4452  CG  MET A 576    26842  34288  37963  -5950  -4324   1503       C  
ATOM   4453  SD  MET A 576      99.125   4.945  65.662  1.00278.84           S  
ANISOU 4453  SD  MET A 576    29069  36796  40084  -5797  -4237   1656       S  
ATOM   4454  CE  MET A 576     100.039   5.757  66.971  1.00296.91           C  
ANISOU 4454  CE  MET A 576    31051  39343  42420  -5413  -4278   1485       C  
ATOM   4455  N   GLY A 577      99.782   3.291  62.501  1.00250.88           N  
ANISOU 4455  N   GLY A 577    26305  32452  36568  -6373  -4008   1822       N  
ATOM   4456  CA  GLY A 577      98.907   2.739  61.484  1.00245.47           C  
ANISOU 4456  CA  GLY A 577    25838  31583  35845  -6685  -3995   1957       C  
ATOM   4457  C   GLY A 577      97.443   2.831  61.868  1.00242.21           C  
ANISOU 4457  C   GLY A 577    25306  31358  35365  -6781  -4090   2051       C  
ATOM   4458  O   GLY A 577      97.038   3.734  62.600  1.00241.04           O  
ANISOU 4458  O   GLY A 577    24889  31453  35244  -6652  -4212   1968       O  
ATOM   4459  N   GLU A 578      96.648   1.891  61.368  1.00242.17           N  
ANISOU 4459  N   GLU A 578    25502  31239  35272  -7011  -4032   2225       N  
ATOM   4460  CA  GLU A 578      95.221   1.854  61.666  1.00242.95           C  
ANISOU 4460  CA  GLU A 578    25516  31495  35298  -7125  -4111   2331       C  
ATOM   4461  C   GLU A 578      94.950   1.034  62.924  1.00246.29           C  
ANISOU 4461  C   GLU A 578    25863  32127  35589  -6973  -4044   2446       C  
ATOM   4462  O   GLU A 578      95.718   0.135  63.266  1.00249.02           O  
ANISOU 4462  O   GLU A 578    26321  32419  35875  -6868  -3906   2498       O  
ATOM   4463  CB  GLU A 578      94.444   1.279  60.479  1.00241.07           C  
ANISOU 4463  CB  GLU A 578    25531  31032  35034  -7456  -4088   2461       C  
ATOM   4464  CG  GLU A 578      92.933   1.313  60.646  1.00238.90           C  
ANISOU 4464  CG  GLU A 578    25178  30898  34695  -7600  -4178   2564       C  
ATOM   4465  CD  GLU A 578      92.390   2.724  60.757  1.00234.37           C  
ANISOU 4465  CD  GLU A 578    24348  30491  34210  -7572  -4361   2431       C  
ATOM   4466  OE1 GLU A 578      93.087   3.669  60.330  1.00230.83           O  
ANISOU 4466  OE1 GLU A 578    23840  29979  33885  -7519  -4420   2268       O  
ATOM   4467  OE2 GLU A 578      91.262   2.889  61.269  1.00233.68           O1-
ANISOU 4467  OE2 GLU A 578    24121  30598  34070  -7603  -4445   2489       O1-
ATOM   4468  N   ASN A 579      93.855   1.352  63.609  1.00244.95           N  
ANISOU 4468  N   ASN A 579    25503  32195  35373  -6962  -4143   2483       N  
ATOM   4469  CA  ASN A 579      93.478   0.659  64.837  1.00241.86           C  
ANISOU 4469  CA  ASN A 579    25017  32023  34857  -6821  -4095   2590       C  
ATOM   4470  C   ASN A 579      94.537   0.810  65.926  1.00242.72           C  
ANISOU 4470  C   ASN A 579    24964  32285  34972  -6494  -4056   2492       C  
ATOM   4471  O   ASN A 579      94.650  -0.032  66.818  1.00242.68           O  
ANISOU 4471  O   ASN A 579    24957  32388  34864  -6363  -3963   2582       O  
ATOM   4472  CB  ASN A 579      93.206  -0.823  64.560  1.00236.29           C  
ANISOU 4472  CB  ASN A 579    24580  31169  34030  -6977  -3950   2791       C  
ATOM   4473  CG  ASN A 579      92.490  -1.510  65.707  1.00231.66           C  
ANISOU 4473  CG  ASN A 579    23901  30810  33309  -6889  -3921   2921       C  
ATOM   4474  ND2 ASN A 579      92.836  -2.769  65.951  1.00230.34           N  
ANISOU 4474  ND2 ASN A 579    23905  30573  33042  -6869  -3767   3048       N  
ATOM   4475  OD1 ASN A 579      91.632  -0.919  66.362  1.00229.97           O  
ANISOU 4475  OD1 ASN A 579    23465  30831  33082  -6842  -4035   2909       O  
ATOM   4476  N   ASN A 580      95.311   1.889  65.843  1.00242.93           N  
ANISOU 4476  N   ASN A 580    24858  32323  35122  -6364  -4128   2305       N  
ATOM   4477  CA  ASN A 580      96.366   2.166  66.813  1.00243.88           C  
ANISOU 4477  CA  ASN A 580    24815  32583  35264  -6053  -4102   2191       C  
ATOM   4478  C   ASN A 580      97.445   1.084  66.816  1.00247.47           C  
ANISOU 4478  C   ASN A 580    25473  32881  35672  -5981  -3925   2244       C  
ATOM   4479  O   ASN A 580      98.219   0.966  67.766  1.00249.56           O  
ANISOU 4479  O   ASN A 580    25632  33271  35916  -5725  -3873   2198       O  
ATOM   4480  CB  ASN A 580      95.774   2.336  68.215  1.00241.96           C  
ANISOU 4480  CB  ASN A 580    24308  32675  34952  -5861  -4160   2209       C  
ATOM   4481  CG  ASN A 580      96.761   2.934  69.198  1.00239.41           C  
ANISOU 4481  CG  ASN A 580    23766  32522  34675  -5538  -4173   2060       C  
ATOM   4482  ND2 ASN A 580      96.429   2.870  70.482  1.00238.49           N  
ANISOU 4482  ND2 ASN A 580    23449  32680  34485  -5347  -4190   2088       N  
ATOM   4483  OD1 ASN A 580      97.808   3.450  68.808  1.00238.68           O  
ANISOU 4483  OD1 ASN A 580    23685  32318  34685  -5459  -4167   1922       O  
ATOM   4484  N   THR A 581      97.492   0.300  65.744  1.00247.28           N  
ANISOU 4484  N   THR A 581    25742  32581  35631  -6208  -3834   2340       N  
ATOM   4485  CA  THR A 581      98.462  -0.783  65.627  1.00246.11           C  
ANISOU 4485  CA  THR A 581    25813  32260  35436  -6171  -3663   2401       C  
ATOM   4486  C   THR A 581      99.774  -0.294  65.024  1.00243.36           C  
ANISOU 4486  C   THR A 581    25522  31735  35206  -6102  -3639   2248       C  
ATOM   4487  O   THR A 581      99.785   0.354  63.977  1.00243.60           O  
ANISOU 4487  O   THR A 581    25614  31604  35337  -6257  -3703   2173       O  
ATOM   4488  CB  THR A 581      97.914  -1.943  64.772  1.00246.07           C  
ANISOU 4488  CB  THR A 581    26108  32036  35350  -6448  -3566   2585       C  
ATOM   4489  CG2 THR A 581      98.965  -3.030  64.608  1.00246.08           C  
ANISOU 4489  CG2 THR A 581    26340  31850  35310  -6410  -3391   2641       C  
ATOM   4490  OG1 THR A 581      96.753  -2.499  65.402  1.00246.68           O  
ANISOU 4490  OG1 THR A 581    26139  32278  35308  -6498  -3574   2735       O  
ATOM   4491  N   LEU A 582     100.880  -0.607  65.692  1.00239.47           N  
ANISOU 4491  N   LEU A 582    25010  31275  34702  -5869  -3546   2201       N  
ATOM   4492  CA  LEU A 582     102.201  -0.219  65.215  1.00234.83           C  
ANISOU 4492  CA  LEU A 582    24476  30528  34220  -5781  -3511   2058       C  
ATOM   4493  C   LEU A 582     102.559  -0.977  63.941  1.00234.93           C  
ANISOU 4493  C   LEU A 582    24818  30204  34239  -6008  -3405   2130       C  
ATOM   4494  O   LEU A 582     102.021  -2.052  63.677  1.00236.26           O  
ANISOU 4494  O   LEU A 582    25182  30278  34308  -6173  -3320   2302       O  
ATOM   4495  CB  LEU A 582     103.260  -0.466  66.293  1.00231.89           C  
ANISOU 4495  CB  LEU A 582    24008  30278  33823  -5475  -3430   2004       C  
ATOM   4496  CG  LEU A 582     103.177   0.378  67.568  1.00228.87           C  
ANISOU 4496  CG  LEU A 582    23290  30219  33453  -5211  -3530   1902       C  
ATOM   4497  CD1 LEU A 582     101.992  -0.036  68.428  1.00227.78           C  
ANISOU 4497  CD1 LEU A 582    23046  30305  33195  -5215  -3556   2037       C  
ATOM   4498  CD2 LEU A 582     104.471   0.269  68.359  1.00228.32           C  
ANISOU 4498  CD2 LEU A 582    23153  30206  33390  -4922  -3449   1814       C  
ATOM   4499  N   VAL A 583     103.470  -0.413  63.154  1.00233.52           N  
ANISOU 4499  N   VAL A 583    24701  29846  34178  -6015  -3410   1997       N  
ATOM   4500  CA  VAL A 583     103.862  -1.018  61.885  1.00232.92           C  
ANISOU 4500  CA  VAL A 583    24932  29444  34123  -6229  -3318   2048       C  
ATOM   4501  C   VAL A 583     105.342  -1.391  61.854  1.00234.08           C  
ANISOU 4501  C   VAL A 583    25189  29452  34299  -6082  -3195   1983       C  
ATOM   4502  O   VAL A 583     106.210  -0.559  62.117  1.00232.42           O  
ANISOU 4502  O   VAL A 583    24833  29295  34182  -5891  -3235   1816       O  
ATOM   4503  CB  VAL A 583     103.552  -0.086  60.698  1.00230.09           C  
ANISOU 4503  CB  VAL A 583    24603  28939  33882  -6431  -3429   1963       C  
ATOM   4504  CG1 VAL A 583     104.195  -0.615  59.425  1.00228.92           C  
ANISOU 4504  CG1 VAL A 583    24757  28451  33770  -6612  -3331   1986       C  
ATOM   4505  CG2 VAL A 583     102.049   0.069  60.523  1.00229.30           C  
ANISOU 4505  CG2 VAL A 583    24459  28921  33742  -6629  -3530   2056       C  
ATOM   4506  N   TRP A 584     105.618  -2.650  61.530  1.00236.36           N  
ANISOU 4506  N   TRP A 584    25736  29563  34507  -6173  -3046   2118       N  
ATOM   4507  CA  TRP A 584     106.987  -3.136  61.414  1.00235.93           C  
ANISOU 4507  CA  TRP A 584    25819  29353  34470  -6060  -2917   2075       C  
ATOM   4508  C   TRP A 584     107.190  -3.816  60.065  1.00230.93           C  
ANISOU 4508  C   TRP A 584    25510  28385  33848  -6314  -2828   2150       C  
ATOM   4509  O   TRP A 584     106.335  -4.576  59.610  1.00231.06           O  
ANISOU 4509  O   TRP A 584    25691  28316  33786  -6533  -2794   2309       O  
ATOM   4510  CB  TRP A 584     107.307  -4.115  62.546  1.00240.89           C  
ANISOU 4510  CB  TRP A 584    26436  30113  34980  -5868  -2801   2165       C  
ATOM   4511  CG  TRP A 584     107.121  -3.534  63.914  1.00244.37           C  
ANISOU 4511  CG  TRP A 584    26565  30883  35402  -5613  -2878   2100       C  
ATOM   4512  CD1 TRP A 584     105.956  -3.453  64.619  1.00245.66           C  
ANISOU 4512  CD1 TRP A 584    26570  31275  35495  -5616  -2955   2174       C  
ATOM   4513  CD2 TRP A 584     108.135  -2.955  64.746  1.00245.03           C  
ANISOU 4513  CD2 TRP A 584    26459  31103  35538  -5315  -2886   1949       C  
ATOM   4514  CE2 TRP A 584     107.509  -2.542  65.940  1.00245.93           C  
ANISOU 4514  CE2 TRP A 584    26302  31530  35610  -5150  -2970   1939       C  
ATOM   4515  CE3 TRP A 584     109.509  -2.744  64.597  1.00243.91           C  
ANISOU 4515  CE3 TRP A 584    26350  30850  35476  -5171  -2831   1819       C  
ATOM   4516  NE1 TRP A 584     106.180  -2.858  65.837  1.00246.50           N  
ANISOU 4516  NE1 TRP A 584    26399  31652  35607  -5339  -3010   2079       N  
ATOM   4517  CZ2 TRP A 584     108.210  -1.932  66.978  1.00245.60           C  
ANISOU 4517  CZ2 TRP A 584    26024  31692  35603  -4848  -3000   1806       C  
ATOM   4518  CZ3 TRP A 584     110.203  -2.138  65.630  1.00243.68           C  
ANISOU 4518  CZ3 TRP A 584    26085  31022  35480  -4872  -2860   1687       C  
ATOM   4519  CH2 TRP A 584     109.553  -1.739  66.804  1.00244.62           C  
ANISOU 4519  CH2 TRP A 584    25937  31451  35555  -4713  -2944   1681       C  
ATOM   4520  N   LYS A 585     108.322  -3.539  59.425  1.00225.09           N  
ANISOU 4520  N   LYS A 585    24862  27458  33205  -6284  -2791   2035       N  
ATOM   4521  CA  LYS A 585     108.614  -4.119  58.118  1.00219.90           C  
ANISOU 4521  CA  LYS A 585    24510  26476  32568  -6515  -2709   2091       C  
ATOM   4522  C   LYS A 585     110.021  -4.704  58.043  1.00219.64           C  
ANISOU 4522  C   LYS A 585    24625  26285  32544  -6396  -2568   2057       C  
ATOM   4523  O   LYS A 585     110.885  -4.385  58.860  1.00216.85           O  
ANISOU 4523  O   LYS A 585    24121  26057  32216  -6133  -2557   1948       O  
ATOM   4524  CB  LYS A 585     108.414  -3.083  57.010  1.00214.41           C  
ANISOU 4524  CB  LYS A 585    23818  25648  32000  -6684  -2824   1986       C  
ATOM   4525  CG  LYS A 585     106.968  -2.663  56.805  1.00209.32           C  
ANISOU 4525  CG  LYS A 585    23094  25096  31342  -6866  -2948   2044       C  
ATOM   4526  CD  LYS A 585     106.815  -1.802  55.562  1.00204.86           C  
ANISOU 4526  CD  LYS A 585    22584  24356  30898  -7062  -3042   1956       C  
ATOM   4527  CE  LYS A 585     105.363  -1.420  55.333  1.00202.28           C  
ANISOU 4527  CE  LYS A 585    22187  24114  30555  -7251  -3163   2018       C  
ATOM   4528  NZ  LYS A 585     105.176  -0.666  54.065  1.00199.35           N1+
ANISOU 4528  NZ  LYS A 585    21892  23558  30295  -7460  -3247   1946       N1+
ATOM   4529  N   TYR A 586     110.241  -5.563  57.053  1.00224.02           N  
ANISOU 4529  N   TYR A 586    25476  26563  33078  -6593  -2462   2152       N  
ATOM   4530  CA  TYR A 586     111.535  -6.206  56.864  1.00230.77           C  
ANISOU 4530  CA  TYR A 586    26503  27241  33938  -6511  -2322   2134       C  
ATOM   4531  C   TYR A 586     111.937  -6.195  55.395  1.00232.43           C  
ANISOU 4531  C   TYR A 586    26954  27129  34231  -6729  -2295   2111       C  
ATOM   4532  O   TYR A 586     111.091  -6.321  54.509  1.00229.71           O  
ANISOU 4532  O   TYR A 586    26740  26658  33881  -6991  -2325   2196       O  
ATOM   4533  CB  TYR A 586     111.495  -7.647  57.375  1.00237.77           C  
ANISOU 4533  CB  TYR A 586    27535  28127  34678  -6498  -2176   2310       C  
ATOM   4534  CG  TYR A 586     110.635  -8.568  56.536  1.00243.12           C  
ANISOU 4534  CG  TYR A 586    28462  28632  35281  -6795  -2124   2493       C  
ATOM   4535  CD1 TYR A 586     111.179  -9.290  55.481  1.00244.31           C  
ANISOU 4535  CD1 TYR A 586    28908  28481  35439  -6959  -2014   2547       C  
ATOM   4536  CD2 TYR A 586     109.279  -8.715  56.798  1.00245.35           C  
ANISOU 4536  CD2 TYR A 586    28684  29052  35487  -6912  -2185   2611       C  
ATOM   4537  CE1 TYR A 586     110.398 -10.131  54.711  1.00245.16           C  
ANISOU 4537  CE1 TYR A 586    29243  28429  35480  -7230  -1967   2713       C  
ATOM   4538  CE2 TYR A 586     108.490  -9.554  56.033  1.00245.99           C  
ANISOU 4538  CE2 TYR A 586    28991  28975  35500  -7183  -2138   2777       C  
ATOM   4539  CZ  TYR A 586     109.054 -10.259  54.991  1.00245.76           C  
ANISOU 4539  CZ  TYR A 586    29251  28646  35479  -7341  -2029   2827       C  
ATOM   4540  OH  TYR A 586     108.271 -11.094  54.228  1.00246.10           O  
ANISOU 4540  OH  TYR A 586    29519  28531  35455  -7610  -1982   2993       O  
ATOM   4541  N   ALA A 587     113.233  -6.045  55.141  1.00238.10           N  
ANISOU 4541  N   ALA A 587    27728  27714  35024  -6617  -2237   1996       N  
ATOM   4542  CA  ALA A 587     113.756  -6.094  53.782  1.00241.91           C  
ANISOU 4542  CA  ALA A 587    28447  27883  35583  -6804  -2197   1971       C  
ATOM   4543  C   ALA A 587     114.009  -7.540  53.372  1.00246.63           C  
ANISOU 4543  C   ALA A 587    29344  28276  36086  -6923  -2031   2132       C  
ATOM   4544  O   ALA A 587     114.431  -8.359  54.188  1.00247.39           O  
ANISOU 4544  O   ALA A 587    29456  28448  36094  -6770  -1926   2195       O  
ATOM   4545  CB  ALA A 587     115.032  -5.279  53.675  1.00239.98           C  
ANISOU 4545  CB  ALA A 587    28132  27585  35464  -6635  -2209   1775       C  
ATOM   4546  N   ASP A 588     113.752  -7.851  52.106  1.00249.31           N  
ANISOU 4546  N   ASP A 588    29923  28358  36446  -7196  -2008   2198       N  
ATOM   4547  CA  ASP A 588     113.910  -9.215  51.615  1.00251.12           C  
ANISOU 4547  CA  ASP A 588    30448  28380  36588  -7336  -1856   2357       C  
ATOM   4548  C   ASP A 588     114.999  -9.305  50.550  1.00251.13           C  
ANISOU 4548  C   ASP A 588    30664  28083  36672  -7407  -1783   2292       C  
ATOM   4549  O   ASP A 588     116.093  -8.766  50.720  1.00249.99           O  
ANISOU 4549  O   ASP A 588    30443  27933  36609  -7223  -1778   2142       O  
ATOM   4550  CB  ASP A 588     112.581  -9.743  51.068  1.00252.39           C  
ANISOU 4550  CB  ASP A 588    30734  28487  36676  -7613  -1874   2525       C  
ATOM   4551  CG  ASP A 588     112.515 -11.258  51.058  1.00255.10           C  
ANISOU 4551  CG  ASP A 588    31313  28723  36888  -7700  -1720   2716       C  
ATOM   4552  OD1 ASP A 588     113.568 -11.904  51.241  1.00256.32           O  
ANISOU 4552  OD1 ASP A 588    31575  28794  37021  -7581  -1595   2715       O  
ATOM   4553  OD2 ASP A 588     111.408 -11.803  50.868  1.00255.57           O1-
ANISOU 4553  OD2 ASP A 588    31453  28785  36868  -7889  -1724   2867       O1-
ATOM   4554  N   ALA A 589     114.691  -9.987  49.451  1.00252.34           N  
ANISOU 4554  N   ALA A 589    31086  27988  36805  -7674  -1725   2407       N  
ATOM   4555  CA  ALA A 589     115.655 -10.192  48.375  1.00253.87           C  
ANISOU 4555  CA  ALA A 589    31510  27882  37067  -7767  -1646   2367       C  
ATOM   4556  C   ALA A 589     116.083  -8.874  47.738  1.00256.48           C  
ANISOU 4556  C   ALA A 589    31748  28147  37555  -7763  -1756   2176       C  
ATOM   4557  O   ALA A 589     117.209  -8.415  47.935  1.00256.70           O  
ANISOU 4557  O   ALA A 589    31710  28168  37658  -7576  -1741   2033       O  
ATOM   4558  CB  ALA A 589     115.082 -11.130  47.323  1.00252.61           C  
ANISOU 4558  CB  ALA A 589    31643  27485  36852  -8068  -1578   2532       C  
ATOM   4559  N   GLY A 590     115.179  -8.271  46.973  1.00257.31           N  
ANISOU 4559  N   GLY A 590    31850  28207  37710  -7971  -1865   2176       N  
ATOM   4560  CA  GLY A 590     115.470  -7.027  46.284  1.00255.36           C  
ANISOU 4560  CA  GLY A 590    31526  27889  37610  -7997  -1974   2005       C  
ATOM   4561  C   GLY A 590     115.364  -5.812  47.184  1.00253.82           C  
ANISOU 4561  C   GLY A 590    30997  27970  37474  -7785  -2108   1858       C  
ATOM   4562  O   GLY A 590     114.938  -4.743  46.747  1.00254.70           O  
ANISOU 4562  O   GLY A 590    30997  28101  37678  -7856  -2240   1761       O  
ATOM   4563  N   HIS A 591     115.754  -5.978  48.445  1.00251.57           N  
ANISOU 4563  N   HIS A 591    30552  27899  37134  -7525  -2075   1840       N  
ATOM   4564  CA  HIS A 591     115.717  -4.890  49.418  1.00248.82           C  
ANISOU 4564  CA  HIS A 591    29880  27828  36834  -7299  -2193   1703       C  
ATOM   4565  C   HIS A 591     114.330  -4.258  49.524  1.00246.47           C  
ANISOU 4565  C   HIS A 591    29423  27697  36529  -7406  -2336   1730       C  
ATOM   4566  O   HIS A 591     114.194  -3.108  49.939  1.00248.50           O  
ANISOU 4566  O   HIS A 591    29430  28129  36859  -7288  -2464   1596       O  
ATOM   4567  CB  HIS A 591     116.760  -3.821  49.075  1.00246.25           C  
ANISOU 4567  CB  HIS A 591    29473  27434  36656  -7186  -2242   1495       C  
ATOM   4568  CG  HIS A 591     118.176  -4.270  49.271  1.00243.37           C  
ANISOU 4568  CG  HIS A 591    29193  26975  36302  -7012  -2117   1440       C  
ATOM   4569  CD2 HIS A 591     119.065  -4.817  48.410  1.00241.25           C  
ANISOU 4569  CD2 HIS A 591    29173  26429  36061  -7093  -2007   1445       C  
ATOM   4570  ND1 HIS A 591     118.827  -4.170  50.482  1.00242.42           N  
ANISOU 4570  ND1 HIS A 591    28888  27059  36163  -6716  -2096   1370       N  
ATOM   4571  CE1 HIS A 591     120.056  -4.638  50.358  1.00241.03           C  
ANISOU 4571  CE1 HIS A 591    28843  26736  36002  -6622  -1979   1334       C  
ATOM   4572  NE2 HIS A 591     120.227  -5.037  49.111  1.00240.33           N  
ANISOU 4572  NE2 HIS A 591    29018  26355  35942  -6847  -1923   1378       N  
ATOM   4573  N   VAL A 592     113.304  -5.015  49.148  1.00241.12           N  
ANISOU 4573  N   VAL A 592    28890  26962  35763  -7629  -2315   1902       N  
ATOM   4574  CA  VAL A 592     111.931  -4.525  49.203  1.00237.16           C  
ANISOU 4574  CA  VAL A 592    28259  26605  35245  -7751  -2443   1945       C  
ATOM   4575  C   VAL A 592     111.352  -4.681  50.605  1.00238.80           C  
ANISOU 4575  C   VAL A 592    28254  27125  35355  -7575  -2465   1999       C  
ATOM   4576  O   VAL A 592     111.554  -5.705  51.258  1.00243.67           O  
ANISOU 4576  O   VAL A 592    28934  27785  35864  -7488  -2350   2105       O  
ATOM   4577  CB  VAL A 592     111.028  -5.260  48.194  1.00232.89           C  
ANISOU 4577  CB  VAL A 592    27964  25873  34651  -8071  -2413   2108       C  
ATOM   4578  CG1 VAL A 592     109.614  -4.703  48.242  1.00230.24           C  
ANISOU 4578  CG1 VAL A 592    27489  25689  34304  -8195  -2551   2145       C  
ATOM   4579  CG2 VAL A 592     111.602  -5.147  46.790  1.00230.48           C  
ANISOU 4579  CG2 VAL A 592    27879  25252  34441  -8249  -2387   2060       C  
ATOM   4580  N   CYS A 593     110.633  -3.661  51.064  1.00233.71           N  
ANISOU 4580  N   CYS A 593    27355  26698  34747  -7523  -2613   1925       N  
ATOM   4581  CA  CYS A 593     110.052  -3.675  52.402  1.00228.24           C  
ANISOU 4581  CA  CYS A 593    26435  26314  33970  -7351  -2650   1962       C  
ATOM   4582  C   CYS A 593     108.652  -4.282  52.409  1.00221.74           C  
ANISOU 4582  C   CYS A 593    25662  25549  33040  -7542  -2666   2141       C  
ATOM   4583  O   CYS A 593     107.815  -3.948  51.570  1.00218.76           O  
ANISOU 4583  O   CYS A 593    25337  25086  32694  -7770  -2744   2166       O  
ATOM   4584  CB  CYS A 593     110.018  -2.261  52.986  1.00227.27           C  
ANISOU 4584  CB  CYS A 593    25999  26415  33940  -7178  -2802   1788       C  
ATOM   4585  SG  CYS A 593     111.648  -1.512  53.222  1.00379.43           S  
ANISOU 4585  SG  CYS A 593    45166  45671  53329  -6910  -2788   1572       S  
ATOM   4586  N   HIS A 594     108.406  -5.175  53.364  1.00218.32           N  
ANISOU 4586  N   HIS A 594    25211  25259  32479  -7445  -2591   2263       N  
ATOM   4587  CA  HIS A 594     107.108  -5.826  53.497  1.00214.59           C  
ANISOU 4587  CA  HIS A 594    24780  24860  31896  -7604  -2596   2438       C  
ATOM   4588  C   HIS A 594     106.645  -5.838  54.951  1.00212.06           C  
ANISOU 4588  C   HIS A 594    24219  24862  31492  -7398  -2626   2466       C  
ATOM   4589  O   HIS A 594     107.461  -5.879  55.870  1.00210.79           O  
ANISOU 4589  O   HIS A 594    23947  24825  31319  -7142  -2580   2405       O  
ATOM   4590  CB  HIS A 594     107.167  -7.257  52.959  1.00213.32           C  
ANISOU 4590  CB  HIS A 594    24929  24482  31641  -7767  -2441   2612       C  
ATOM   4591  CG  HIS A 594     107.509  -7.343  51.505  1.00210.87           C  
ANISOU 4591  CG  HIS A 594    24870  23850  31401  -7991  -2407   2605       C  
ATOM   4592  CD2 HIS A 594     108.704  -7.430  50.874  1.00209.98           C  
ANISOU 4592  CD2 HIS A 594    24907  23519  31356  -7971  -2329   2531       C  
ATOM   4593  ND1 HIS A 594     106.552  -7.347  50.514  1.00208.92           N  
ANISOU 4593  ND1 HIS A 594    24748  23472  31161  -8277  -2457   2682       N  
ATOM   4594  CE1 HIS A 594     107.142  -7.432  49.335  1.00208.99           C  
ANISOU 4594  CE1 HIS A 594    24973  23195  31238  -8424  -2411   2656       C  
ATOM   4595  NE2 HIS A 594     108.448  -7.484  49.526  1.00209.31           N  
ANISOU 4595  NE2 HIS A 594    25033  23178  31317  -8243  -2333   2565       N  
ATOM   4596  N   LEU A 595     105.331  -5.805  55.150  1.00210.77           N  
ANISOU 4596  N   LEU A 595    23978  24834  31270  -7512  -2704   2558       N  
ATOM   4597  CA  LEU A 595     104.756  -5.828  56.491  1.00209.72           C  
ANISOU 4597  CA  LEU A 595    23622  25009  31054  -7339  -2739   2596       C  
ATOM   4598  C   LEU A 595     105.018  -7.157  57.193  1.00213.21           C  
ANISOU 4598  C   LEU A 595    24171  25475  31363  -7251  -2587   2735       C  
ATOM   4599  O   LEU A 595     104.725  -8.224  56.653  1.00213.66           O  
ANISOU 4599  O   LEU A 595    24471  25367  31344  -7436  -2489   2890       O  
ATOM   4600  CB  LEU A 595     103.250  -5.556  56.432  1.00205.05           C  
ANISOU 4600  CB  LEU A 595    22949  24532  30429  -7509  -2851   2674       C  
ATOM   4601  CG  LEU A 595     102.817  -4.117  56.145  1.00199.36           C  
ANISOU 4601  CG  LEU A 595    22034  23890  29824  -7537  -3026   2531       C  
ATOM   4602  CD1 LEU A 595     101.329  -4.052  55.839  1.00197.18           C  
ANISOU 4602  CD1 LEU A 595    21749  23663  29508  -7759  -3115   2633       C  
ATOM   4603  CD2 LEU A 595     103.165  -3.214  57.315  1.00198.80           C  
ANISOU 4603  CD2 LEU A 595    21649  24095  29790  -7241  -3106   2389       C  
ATOM   4604  N   CYS A 596     105.570  -7.085  58.401  1.00215.46           N  
ANISOU 4604  N   CYS A 596    24274  25968  31622  -6967  -2568   2679       N  
ATOM   4605  CA  CYS A 596     105.836  -8.279  59.194  1.00217.24           C  
ANISOU 4605  CA  CYS A 596    24573  26246  31723  -6855  -2430   2801       C  
ATOM   4606  C   CYS A 596     104.537  -8.887  59.707  1.00218.37           C  
ANISOU 4606  C   CYS A 596    24691  26538  31741  -6944  -2440   2968       C  
ATOM   4607  O   CYS A 596     103.452  -8.369  59.445  1.00216.81           O  
ANISOU 4607  O   CYS A 596    24418  26402  31557  -7090  -2554   2987       O  
ATOM   4608  CB  CYS A 596     106.755  -7.950  60.372  1.00217.56           C  
ANISOU 4608  CB  CYS A 596    24408  26481  31775  -6520  -2418   2686       C  
ATOM   4609  SG  CYS A 596     108.422  -7.432  59.907  1.00360.75           S  
ANISOU 4609  SG  CYS A 596    42586  44443  50039  -6385  -2379   2500       S  
ATOM   4610  N   HIS A 597     104.655  -9.989  60.440  1.00222.73           N  
ANISOU 4610  N   HIS A 597    25307  27148  32173  -6855  -2319   3090       N  
ATOM   4611  CA  HIS A 597     103.494 -10.636  61.036  1.00227.33           C  
ANISOU 4611  CA  HIS A 597    25862  27882  32629  -6915  -2316   3251       C  
ATOM   4612  C   HIS A 597     102.978  -9.784  62.192  1.00230.17           C  
ANISOU 4612  C   HIS A 597    25893  28572  32991  -6723  -2439   3180       C  
ATOM   4613  O   HIS A 597     103.755  -9.355  63.044  1.00231.47           O  
ANISOU 4613  O   HIS A 597    25882  28883  33183  -6457  -2445   3065       O  
ATOM   4614  CB  HIS A 597     103.862 -12.038  61.528  1.00228.12           C  
ANISOU 4614  CB  HIS A 597    26119  27952  32603  -6855  -2148   3392       C  
ATOM   4615  CG  HIS A 597     102.700 -12.978  61.608  1.00226.98           C  
ANISOU 4615  CG  HIS A 597    26074  27836  32333  -7023  -2112   3592       C  
ATOM   4616  CD2 HIS A 597     102.192 -13.846  60.700  1.00225.86           C  
ANISOU 4616  CD2 HIS A 597    26192  27485  32139  -7289  -2045   3740       C  
ATOM   4617  ND1 HIS A 597     101.917 -13.103  62.735  1.00227.22           N  
ANISOU 4617  ND1 HIS A 597    25925  28135  32272  -6916  -2145   3659       N  
ATOM   4618  CE1 HIS A 597     100.975 -14.004  62.518  1.00226.84           C  
ANISOU 4618  CE1 HIS A 597    26023  28044  32123  -7110  -2099   3839       C  
ATOM   4619  NE2 HIS A 597     101.121 -14.470  61.291  1.00226.25           N  
ANISOU 4619  NE2 HIS A 597    26214  27680  32069  -7338  -2039   3891       N  
ATOM   4620  N   PRO A 598     101.661  -9.531  62.217  1.00229.43           N  
ANISOU 4620  N   PRO A 598    25714  28594  32867  -6858  -2539   3245       N  
ATOM   4621  CA  PRO A 598     101.021  -8.687  63.235  1.00230.72           C  
ANISOU 4621  CA  PRO A 598    25565  29067  33031  -6706  -2667   3185       C  
ATOM   4622  C   PRO A 598     101.342  -9.120  64.666  1.00235.30           C  
ANISOU 4622  C   PRO A 598    26003  29877  33523  -6432  -2608   3207       C  
ATOM   4623  O   PRO A 598     101.163  -8.331  65.595  1.00234.47           O  
ANISOU 4623  O   PRO A 598    25624  30028  33437  -6245  -2705   3119       O  
ATOM   4624  CB  PRO A 598      99.529  -8.870  62.947  1.00227.98           C  
ANISOU 4624  CB  PRO A 598    25245  28753  32624  -6940  -2729   3317       C  
ATOM   4625  CG  PRO A 598      99.470  -9.197  61.496  1.00226.03           C  
ANISOU 4625  CG  PRO A 598    25272  28198  32412  -7224  -2693   3369       C  
ATOM   4626  CD  PRO A 598     100.694 -10.020  61.218  1.00226.77           C  
ANISOU 4626  CD  PRO A 598    25577  28089  32496  -7174  -2537   3381       C  
ATOM   4627  N   ASN A 599     101.808 -10.353  64.837  1.00238.98           N  
ANISOU 4627  N   ASN A 599    26652  30253  33896  -6410  -2451   3321       N  
ATOM   4628  CA  ASN A 599     102.153 -10.869  66.159  1.00238.69           C  
ANISOU 4628  CA  ASN A 599    26504  30417  33770  -6157  -2381   3352       C  
ATOM   4629  C   ASN A 599     103.454 -10.281  66.698  1.00240.37           C  
ANISOU 4629  C   ASN A 599    26582  30690  34058  -5878  -2374   3181       C  
ATOM   4630  O   ASN A 599     103.568  -9.988  67.888  1.00237.68           O  
ANISOU 4630  O   ASN A 599    26015  30599  33694  -5634  -2403   3130       O  
ATOM   4631  CB  ASN A 599     102.248 -12.396  66.134  1.00235.69           C  
ANISOU 4631  CB  ASN A 599    26373  29912  33265  -6228  -2212   3530       C  
ATOM   4632  CG  ASN A 599     100.918 -13.060  65.838  1.00232.28           C  
ANISOU 4632  CG  ASN A 599    26050  29465  32741  -6470  -2213   3711       C  
ATOM   4633  ND2 ASN A 599     100.886 -14.384  65.932  1.00232.02           N  
ANISOU 4633  ND2 ASN A 599    26211  29356  32591  -6524  -2073   3873       N  
ATOM   4634  OD1 ASN A 599      99.932 -12.392  65.528  1.00230.04           O  
ANISOU 4634  OD1 ASN A 599    25677  29238  32490  -6607  -2337   3703       O  
ATOM   4635  N   CYS A 600     104.432 -10.114  65.814  1.00246.06           N  
ANISOU 4635  N   CYS A 600    27443  31178  34869  -5916  -2336   3092       N  
ATOM   4636  CA  CYS A 600     105.738  -9.593  66.201  1.00252.14           C  
ANISOU 4636  CA  CYS A 600    28113  31972  35717  -5668  -2321   2929       C  
ATOM   4637  C   CYS A 600     105.654  -8.150  66.692  1.00256.79           C  
ANISOU 4637  C   CYS A 600    28394  32772  36403  -5515  -2480   2757       C  
ATOM   4638  O   CYS A 600     105.623  -7.212  65.895  1.00254.91           O  
ANISOU 4638  O   CYS A 600    28130  32447  36279  -5615  -2579   2650       O  
ATOM   4639  CB  CYS A 600     106.722  -9.694  65.033  1.00252.08           C  
ANISOU 4639  CB  CYS A 600    28333  31656  35791  -5770  -2252   2874       C  
ATOM   4640  SG  CYS A 600     107.090 -11.386  64.508  1.00252.15           S  
ANISOU 4640  SG  CYS A 600    28703  31410  35693  -5909  -2050   3055       S  
ATOM   4641  N   THR A 601     105.617  -7.983  68.011  1.00262.94           N  
ANISOU 4641  N   THR A 601    28942  33828  37137  -5271  -2505   2732       N  
ATOM   4642  CA  THR A 601     105.568  -6.659  68.617  1.00267.53           C  
ANISOU 4642  CA  THR A 601    29216  34631  37802  -5099  -2651   2572       C  
ATOM   4643  C   THR A 601     106.950  -6.014  68.604  1.00271.76           C  
ANISOU 4643  C   THR A 601    29695  35115  38447  -4907  -2643   2389       C  
ATOM   4644  O   THR A 601     107.079  -4.796  68.479  1.00272.49           O  
ANISOU 4644  O   THR A 601    29617  35264  38654  -4853  -2765   2232       O  
ATOM   4645  CB  THR A 601     105.051  -6.721  70.067  1.00268.41           C  
ANISOU 4645  CB  THR A 601    29097  35062  37823  -4898  -2678   2611       C  
ATOM   4646  CG2 THR A 601     104.857  -5.319  70.626  1.00266.97           C  
ANISOU 4646  CG2 THR A 601    28599  35109  37729  -4748  -2841   2452       C  
ATOM   4647  OG1 THR A 601     103.803  -7.423  70.103  1.00269.95           O  
ANISOU 4647  OG1 THR A 601    29359  35300  37909  -5073  -2672   2790       O  
ATOM   4648  N   TYR A 602     107.982  -6.842  68.733  1.00274.41           N  
ANISOU 4648  N   TYR A 602    30175  35342  38747  -4805  -2499   2411       N  
ATOM   4649  CA  TYR A 602     109.359  -6.365  68.707  1.00274.37           C  
ANISOU 4649  CA  TYR A 602    30142  35271  38838  -4625  -2473   2248       C  
ATOM   4650  C   TYR A 602     109.890  -6.353  67.280  1.00273.88           C  
ANISOU 4650  C   TYR A 602    30314  34887  38860  -4823  -2439   2214       C  
ATOM   4651  O   TYR A 602     111.100  -6.301  67.057  1.00273.34           O  
ANISOU 4651  O   TYR A 602    30310  34693  38853  -4720  -2377   2117       O  
ATOM   4652  CB  TYR A 602     110.249  -7.250  69.582  1.00274.75           C  
ANISOU 4652  CB  TYR A 602    30223  35364  38805  -4406  -2333   2282       C  
ATOM   4653  CG  TYR A 602     109.706  -7.482  70.972  1.00276.42           C  
ANISOU 4653  CG  TYR A 602    30239  35872  38914  -4227  -2344   2344       C  
ATOM   4654  CD1 TYR A 602     108.915  -8.589  71.253  1.00277.82           C  
ANISOU 4654  CD1 TYR A 602    30526  36079  38953  -4325  -2271   2537       C  
ATOM   4655  CD2 TYR A 602     109.982  -6.596  72.003  1.00276.97           C  
ANISOU 4655  CD2 TYR A 602    30017  36194  39026  -3961  -2427   2209       C  
ATOM   4656  CE1 TYR A 602     108.415  -8.806  72.522  1.00279.03           C  
ANISOU 4656  CE1 TYR A 602    30503  36504  39013  -4162  -2279   2594       C  
ATOM   4657  CE2 TYR A 602     109.487  -6.805  73.276  1.00278.31           C  
ANISOU 4657  CE2 TYR A 602    30008  36635  39102  -3796  -2437   2265       C  
ATOM   4658  CZ  TYR A 602     108.704  -7.911  73.530  1.00279.15           C  
ANISOU 4658  CZ  TYR A 602    30228  36765  39071  -3897  -2363   2458       C  
ATOM   4659  OH  TYR A 602     108.209  -8.123  74.796  1.00279.77           O  
ANISOU 4659  OH  TYR A 602    30130  37114  39057  -3734  -2372   2514       O  
ATOM   4660  N   GLY A 603     108.977  -6.403  66.316  1.00273.62           N  
ANISOU 4660  N   GLY A 603    30411  34723  38830  -5107  -2481   2296       N  
ATOM   4661  CA  GLY A 603     109.350  -6.446  64.915  1.00271.83           C  
ANISOU 4661  CA  GLY A 603    30420  34188  38676  -5321  -2450   2281       C  
ATOM   4662  C   GLY A 603     109.783  -7.837  64.499  1.00269.98           C  
ANISOU 4662  C   GLY A 603    30484  33737  38358  -5417  -2278   2420       C  
ATOM   4663  O   GLY A 603     109.708  -8.780  65.286  1.00269.70           O  
ANISOU 4663  O   GLY A 603    30474  33795  38204  -5331  -2185   2536       O  
ATOM   4664  N   CYS A 604     110.240  -7.966  63.258  1.00268.24           N  
ANISOU 4664  N   CYS A 604    30492  33229  38200  -5596  -2234   2408       N  
ATOM   4665  CA  CYS A 604     110.683  -9.254  62.740  1.00266.91           C  
ANISOU 4665  CA  CYS A 604    30621  32831  37961  -5704  -2072   2535       C  
ATOM   4666  C   CYS A 604     111.748  -9.089  61.660  1.00265.61           C  
ANISOU 4666  C   CYS A 604    30632  32388  37900  -5768  -2027   2440       C  
ATOM   4667  O   CYS A 604     111.573  -8.321  60.715  1.00266.36           O  
ANISOU 4667  O   CYS A 604    30746  32362  38096  -5920  -2113   2366       O  
ATOM   4668  CB  CYS A 604     109.495 -10.048  62.193  1.00266.66           C  
ANISOU 4668  CB  CYS A 604    30762  32715  37840  -5982  -2052   2725       C  
ATOM   4669  SG  CYS A 604     108.519  -9.175  60.946  1.00228.38           S  
ANISOU 4669  SG  CYS A 604    25938  27751  33084  -6275  -2193   2700       S  
ATOM   4670  N   THR A 605     112.852  -9.814  61.810  1.00263.14           N  
ANISOU 4670  N   THR A 605    30445  31973  37561  -5651  -1890   2444       N  
ATOM   4671  CA  THR A 605     113.928  -9.780  60.827  1.00258.25           C  
ANISOU 4671  CA  THR A 605    30008  31085  37032  -5703  -1831   2364       C  
ATOM   4672  C   THR A 605     113.610 -10.698  59.652  1.00255.24           C  
ANISOU 4672  C   THR A 605    29944  30425  36612  -5999  -1748   2508       C  
ATOM   4673  O   THR A 605     114.438 -10.899  58.764  1.00254.85           O  
ANISOU 4673  O   THR A 605    30090  30124  36617  -6075  -1678   2475       O  
ATOM   4674  CB  THR A 605     115.277 -10.194  61.446  1.00256.37           C  
ANISOU 4674  CB  THR A 605    29781  30844  36782  -5456  -1715   2306       C  
ATOM   4675  CG2 THR A 605     115.678  -9.224  62.547  1.00254.18           C  
ANISOU 4675  CG2 THR A 605    29192  30828  36555  -5159  -1799   2149       C  
ATOM   4676  OG1 THR A 605     115.170 -11.514  61.993  1.00257.56           O  
ANISOU 4676  OG1 THR A 605    30055  31016  36792  -5436  -1585   2472       O  
ATOM   4677  N   GLY A 606     112.401 -11.251  59.657  1.00251.69           N  
ANISOU 4677  N   GLY A 606    29543  30021  36067  -6166  -1756   2668       N  
ATOM   4678  CA  GLY A 606     111.957 -12.132  58.593  1.00249.44           C  
ANISOU 4678  CA  GLY A 606    29547  29491  35738  -6455  -1685   2816       C  
ATOM   4679  C   GLY A 606     110.447 -12.270  58.567  1.00249.38           C  
ANISOU 4679  C   GLY A 606    29517  29575  35661  -6641  -1753   2947       C  
ATOM   4680  O   GLY A 606     109.762 -11.780  59.464  1.00250.10           O  
ANISOU 4680  O   GLY A 606    29370  29929  35727  -6533  -1845   2933       O  
ATOM   4681  N   PRO A 607     109.921 -12.939  57.531  1.00249.54           N  
ANISOU 4681  N   PRO A 607    29786  29377  35651  -6922  -1708   3075       N  
ATOM   4682  CA  PRO A 607     108.479 -13.150  57.352  1.00249.46           C  
ANISOU 4682  CA  PRO A 607    29791  29418  35576  -7131  -1765   3209       C  
ATOM   4683  C   PRO A 607     107.877 -14.024  58.450  1.00249.55           C  
ANISOU 4683  C   PRO A 607    29751  29627  35440  -7048  -1709   3355       C  
ATOM   4684  O   PRO A 607     108.507 -14.990  58.882  1.00250.80           O  
ANISOU 4684  O   PRO A 607    30014  29757  35521  -6947  -1574   3423       O  
ATOM   4685  CB  PRO A 607     108.394 -13.878  56.005  1.00248.68           C  
ANISOU 4685  CB  PRO A 607    30012  29004  35473  -7420  -1689   3313       C  
ATOM   4686  CG  PRO A 607     109.693 -13.595  55.322  1.00247.54           C  
ANISOU 4686  CG  PRO A 607    29971  28651  35432  -7380  -1645   3186       C  
ATOM   4687  CD  PRO A 607     110.702 -13.497  56.416  1.00248.22           C  
ANISOU 4687  CD  PRO A 607    29905  28893  35517  -7062  -1604   3092       C  
ATOM   4688  N   GLY A 608     106.669 -13.683  58.889  1.00247.38           N  
ANISOU 4688  N   GLY A 608    29315  29549  35128  -7090  -1812   3400       N  
ATOM   4689  CA  GLY A 608     105.955 -14.472  59.877  1.00245.30           C  
ANISOU 4689  CA  GLY A 608    29001  29475  34727  -7035  -1771   3544       C  
ATOM   4690  C   GLY A 608     106.699 -14.652  61.186  1.00242.69           C  
ANISOU 4690  C   GLY A 608    28521  29340  34351  -6722  -1715   3502       C  
ATOM   4691  O   GLY A 608     107.657 -13.934  61.474  1.00241.74           O  
ANISOU 4691  O   GLY A 608    28274  29262  34315  -6523  -1739   3341       O  
ATOM   4692  N   LEU A 609     106.252 -15.618  61.984  1.00238.41           N  
ANISOU 4692  N   LEU A 609    27994  28917  33673  -6679  -1639   3649       N  
ATOM   4693  CA  LEU A 609     106.879 -15.905  63.269  1.00232.51           C  
ANISOU 4693  CA  LEU A 609    27116  28361  32868  -6389  -1577   3629       C  
ATOM   4694  C   LEU A 609     108.249 -16.548  63.082  1.00237.54           C  
ANISOU 4694  C   LEU A 609    27928  28818  33510  -6297  -1434   3606       C  
ATOM   4695  O   LEU A 609     109.100 -16.489  63.970  1.00238.20           O  
ANISOU 4695  O   LEU A 609    27893  29022  33590  -6034  -1397   3529       O  
ATOM   4696  CB  LEU A 609     105.985 -16.816  64.112  1.00222.29           C  
ANISOU 4696  CB  LEU A 609    25807  27229  31424  -6386  -1531   3802       C  
ATOM   4697  CG  LEU A 609     104.615 -16.256  64.495  1.00216.40           C  
ANISOU 4697  CG  LEU A 609    24870  26695  30657  -6446  -1666   3833       C  
ATOM   4698  CD1 LEU A 609     103.844 -17.262  65.332  1.00214.45           C  
ANISOU 4698  CD1 LEU A 609    24629  26594  30258  -6435  -1602   4008       C  
ATOM   4699  CD2 LEU A 609     104.764 -14.938  65.239  1.00216.50           C  
ANISOU 4699  CD2 LEU A 609    24564  26941  30754  -6227  -1801   3657       C  
ATOM   4700  N   GLU A 610     108.455 -17.162  61.921  1.00240.67           N  
ANISOU 4700  N   GLU A 610    28606  28924  33914  -6515  -1355   3672       N  
ATOM   4701  CA  GLU A 610     109.727 -17.801  61.607  1.00241.30           C  
ANISOU 4701  CA  GLU A 610    28876  28806  34000  -6458  -1218   3657       C  
ATOM   4702  C   GLU A 610     110.795 -16.766  61.268  1.00245.80           C  
ANISOU 4702  C   GLU A 610    29368  29309  34714  -6343  -1268   3452       C  
ATOM   4703  O   GLU A 610     111.923 -17.114  60.918  1.00244.66           O  
ANISOU 4703  O   GLU A 610    29370  28992  34600  -6294  -1170   3412       O  
ATOM   4704  CB  GLU A 610     109.560 -18.788  60.449  1.00234.78           C  
ANISOU 4704  CB  GLU A 610    28379  27691  33137  -6737  -1119   3798       C  
ATOM   4705  CG  GLU A 610     108.952 -18.180  59.194  1.00224.85           C  
ANISOU 4705  CG  GLU A 610    27197  26269  31965  -7003  -1214   3777       C  
ATOM   4706  CD  GLU A 610     108.778 -19.194  58.080  1.00214.14           C  
ANISOU 4706  CD  GLU A 610    26167  24631  30566  -7276  -1113   3921       C  
ATOM   4707  OE1 GLU A 610     109.301 -20.320  58.214  1.00212.68           O  
ANISOU 4707  OE1 GLU A 610    26155  24354  30298  -7249   -966   4019       O  
ATOM   4708  OE2 GLU A 610     108.119 -18.866  57.072  1.00207.31           O1-
ANISOU 4708  OE2 GLU A 610    25383  23635  29751  -7516  -1181   3937       O1-
ATOM   4709  N   GLY A 611     110.431 -15.492  61.373  1.00250.98           N  
ANISOU 4709  N   GLY A 611    29795  30104  35462  -6300  -1423   3324       N  
ATOM   4710  CA  GLY A 611     111.353 -14.408  61.091  1.00255.50           C  
ANISOU 4710  CA  GLY A 611    30269  30634  36174  -6190  -1486   3123       C  
ATOM   4711  C   GLY A 611     111.738 -13.638  62.339  1.00260.86           C  
ANISOU 4711  C   GLY A 611    30646  31590  36878  -5879  -1550   2992       C  
ATOM   4712  O   GLY A 611     112.767 -12.963  62.370  1.00259.87           O  
ANISOU 4712  O   GLY A 611    30441  31448  36848  -5720  -1565   2831       O  
ATOM   4713  N   CYS A 612     110.906 -13.738  63.370  1.00266.87           N  
ANISOU 4713  N   CYS A 612    31238  32608  37553  -5793  -1588   3061       N  
ATOM   4714  CA  CYS A 612     111.176 -13.082  64.645  1.00270.40           C  
ANISOU 4714  CA  CYS A 612    31393  33338  38009  -5497  -1647   2952       C  
ATOM   4715  C   CYS A 612     111.431 -14.109  65.744  1.00271.93           C  
ANISOU 4715  C   CYS A 612    31589  33658  38075  -5319  -1528   3050       C  
ATOM   4716  O   CYS A 612     110.506 -14.524  66.441  1.00272.43           O  
ANISOU 4716  O   CYS A 612    31582  33894  38037  -5321  -1536   3167       O  
ATOM   4717  CB  CYS A 612     110.019 -12.157  65.033  1.00271.91           C  
ANISOU 4717  CB  CYS A 612    31341  33755  38219  -5513  -1809   2925       C  
ATOM   4718  SG  CYS A 612     108.376 -12.906  64.912  1.00465.68           S  
ANISOU 4718  SG  CYS A 612    55966  58332  62637  -5764  -1819   3141       S  
ATOM   4719  N   PRO A 613     112.699 -14.521  65.897  1.00271.67           N  
ANISOU 4719  N   PRO A 613    31638  33535  38048  -5166  -1416   3003       N  
ATOM   4720  CA  PRO A 613     113.112 -15.536  66.874  1.00272.70           C  
ANISOU 4720  CA  PRO A 613    31794  33757  38062  -4991  -1289   3088       C  
ATOM   4721  C   PRO A 613     112.876 -15.090  68.315  1.00273.22           C  
ANISOU 4721  C   PRO A 613    31561  34158  38093  -4732  -1353   3042       C  
ATOM   4722  O   PRO A 613     112.461 -13.956  68.552  1.00274.35           O  
ANISOU 4722  O   PRO A 613    31472  34460  38308  -4679  -1497   2934       O  
ATOM   4723  CB  PRO A 613     114.617 -15.681  66.613  1.00271.12           C  
ANISOU 4723  CB  PRO A 613    31706  33389  37919  -4871  -1191   2991       C  
ATOM   4724  CG  PRO A 613     114.826 -15.153  65.231  1.00269.23           C  
ANISOU 4724  CG  PRO A 613    31601  32899  37796  -5073  -1231   2920       C  
ATOM   4725  CD  PRO A 613     113.830 -14.051  65.082  1.00269.33           C  
ANISOU 4725  CD  PRO A 613    31429  33032  37873  -5159  -1401   2864       C  
ATOM   4726  N   THR A 614     113.142 -15.984  69.262  1.00270.87           N  
ANISOU 4726  N   THR A 614    31269  33964  37686  -4573  -1247   3124       N  
ATOM   4727  CA  THR A 614     112.987 -15.676  70.679  1.00266.38           C  
ANISOU 4727  CA  THR A 614    30429  33710  37074  -4315  -1292   3088       C  
ATOM   4728  C   THR A 614     114.097 -16.323  71.501  1.00265.82           C  
ANISOU 4728  C   THR A 614    30371  33676  36951  -4067  -1165   3075       C  
ATOM   4729  O   THR A 614     114.460 -17.477  71.275  1.00266.24           O  
ANISOU 4729  O   THR A 614    30656  33575  36928  -4125  -1022   3189       O  
ATOM   4730  CB  THR A 614     111.623 -16.152  71.216  1.00262.38           C  
ANISOU 4730  CB  THR A 614    29873  33370  36450  -4400  -1316   3248       C  
ATOM   4731  CG2 THR A 614     111.518 -15.891  72.711  1.00260.88           C  
ANISOU 4731  CG2 THR A 614    29409  33502  36211  -4124  -1354   3214       C  
ATOM   4732  OG1 THR A 614     110.570 -15.454  70.539  1.00259.98           O  
ANISOU 4732  OG1 THR A 614    29527  33057  36198  -4611  -1446   3249       O  
ATOM   4733  OXT THR A 614     114.655 -15.710  72.411  1.00264.72           O1-
ANISOU 4733  OXT THR A 614    30013  33724  36846  -3803  -1203   2951       O1-
TER    4734      THR A 614 
ATOM   4735  N   LEU B   1      63.685  67.583  64.765  1.00173.33           N  
ANISOU 4735  N   LEU B   1    20136  19636  26084    192    -64  -3209       N  
ATOM   4736  CA  LEU B   1      63.130  67.574  66.114  1.00175.74           C  
ANISOU 4736  CA  LEU B   1    20297  20158  26319    278    -32  -3476       C  
ATOM   4737  C   LEU B   1      62.431  66.253  66.416  1.00179.28           C  
ANISOU 4737  C   LEU B   1    20733  20877  26508    360      1  -3354       C  
ATOM   4738  O   LEU B   1      62.849  65.502  67.298  1.00181.07           O  
ANISOU 4738  O   LEU B   1    20878  21422  26497    361     50  -3408       O  
ATOM   4739  CB  LEU B   1      62.152  68.737  66.299  1.00173.62           C  
ANISOU 4739  CB  LEU B   1    19964  19663  26341    350    -75  -3670       C  
ATOM   4740  CG  LEU B   1      62.738  70.151  66.282  1.00171.78           C  
ANISOU 4740  CG  LEU B   1    19693  19158  26418    282   -114  -3858       C  
ATOM   4741  CD1 LEU B   1      61.628  71.191  66.327  1.00169.66           C  
ANISOU 4741  CD1 LEU B   1    19365  18633  26467    370   -170  -4013       C  
ATOM   4742  CD2 LEU B   1      63.708  70.347  67.439  1.00171.11           C  
ANISOU 4742  CD2 LEU B   1    19478  19297  26237    234    -71  -4152       C  
ATOM   4743  N   GLU B   2      61.363  65.977  65.676  1.00179.98           N  
ANISOU 4743  N   GLU B   2    20893  20836  26656    426    -32  -3177       N  
ATOM   4744  CA  GLU B   2      60.565  64.774  65.882  1.00177.21           C  
ANISOU 4744  CA  GLU B   2    20526  20697  26109    503    -11  -3050       C  
ATOM   4745  C   GLU B   2      60.658  63.850  64.674  1.00169.82           C  
ANISOU 4745  C   GLU B   2    19727  19693  25104    476    -33  -2738       C  
ATOM   4746  O   GLU B   2      60.065  64.123  63.631  1.00172.16           O  
ANISOU 4746  O   GLU B   2    20113  19756  25543    492    -81  -2600       O  
ATOM   4747  CB  GLU B   2      59.106  65.155  66.142  1.00179.84           C  
ANISOU 4747  CB  GLU B   2    20799  20974  26558    616    -32  -3140       C  
ATOM   4748  CG  GLU B   2      58.116  64.007  66.015  1.00181.06           C  
ANISOU 4748  CG  GLU B   2    20961  21261  26575    689    -28  -2955       C  
ATOM   4749  CD  GLU B   2      56.679  64.490  65.961  1.00183.80           C  
ANISOU 4749  CD  GLU B   2    21274  21488  27073    793    -59  -3009       C  
ATOM   4750  OE1 GLU B   2      55.796  63.701  65.561  1.00183.12           O  
ANISOU 4750  OE1 GLU B   2    21218  21428  26933    846    -71  -2832       O  
ATOM   4751  OE2 GLU B   2      56.432  65.662  66.314  1.00185.87           O1-
ANISOU 4751  OE2 GLU B   2    21473  21623  27525    823    -75  -3237       O1-
ATOM   4752  N   GLU B   3      61.406  62.759  64.816  1.00157.53           N  
ANISOU 4752  N   GLU B   3    18173  18348  23333    438     -1  -2634       N  
ATOM   4753  CA  GLU B   3      61.563  61.806  63.724  1.00144.34           C  
ANISOU 4753  CA  GLU B   3    16610  16639  21594    417    -23  -2376       C  
ATOM   4754  C   GLU B   3      60.202  61.306  63.252  1.00132.04           C  
ANISOU 4754  C   GLU B   3    15075  15023  20071    505    -54  -2248       C  
ATOM   4755  O   GLU B   3      59.379  60.863  64.054  1.00130.03           O  
ANISOU 4755  O   GLU B   3    14731  14920  19753    578    -36  -2291       O  
ATOM   4756  CB  GLU B   3      62.448  60.632  64.145  1.00146.41           C  
ANISOU 4756  CB  GLU B   3    16838  17152  21638    384     13  -2312       C  
ATOM   4757  CG  GLU B   3      61.897  59.814  65.298  1.00151.18           C  
ANISOU 4757  CG  GLU B   3    17318  18024  22101    451     45  -2339       C  
ATOM   4758  CD  GLU B   3      62.727  58.579  65.577  1.00157.42           C  
ANISOU 4758  CD  GLU B   3    18075  19029  22709    422     66  -2225       C  
ATOM   4759  OE1 GLU B   3      63.809  58.440  64.968  1.00158.14           O  
ANISOU 4759  OE1 GLU B   3    18234  19074  22777    351     61  -2169       O  
ATOM   4760  OE2 GLU B   3      62.298  57.747  66.404  1.00161.17           O1-
ANISOU 4760  OE2 GLU B   3    18444  19721  23071    470     84  -2182       O1-
ATOM   4761  N   LYS B   4      59.973  61.388  61.946  1.00120.86           N  
ANISOU 4761  N   LYS B   4    13769  13406  18747    494   -102  -2087       N  
ATOM   4762  CA  LYS B   4      58.681  61.041  61.367  1.00113.63           C  
ANISOU 4762  CA  LYS B   4    12879  12413  17884    574   -140  -1972       C  
ATOM   4763  C   LYS B   4      58.202  59.657  61.802  1.00115.56           C  
ANISOU 4763  C   LYS B   4    13068  12861  17978    625   -125  -1896       C  
ATOM   4764  O   LYS B   4      59.008  58.775  62.100  1.00120.80           O  
ANISOU 4764  O   LYS B   4    13708  13689  18501    588    -99  -1856       O  
ATOM   4765  CB  LYS B   4      58.744  61.124  59.840  1.00107.91           C  
ANISOU 4765  CB  LYS B   4    12268  11509  17224    541   -192  -1789       C  
ATOM   4766  CG  LYS B   4      59.068  62.510  59.300  1.00104.35           C  
ANISOU 4766  CG  LYS B   4    11863  10833  16953    489   -219  -1807       C  
ATOM   4767  CD  LYS B   4      59.061  62.516  57.779  1.00107.80           C  
ANISOU 4767  CD  LYS B   4    12391  11146  17422    459   -271  -1593       C  
ATOM   4768  CE  LYS B   4      59.212  63.921  57.221  1.00116.88           C  
ANISOU 4768  CE  LYS B   4    13569  12058  18781    411   -307  -1564       C  
ATOM   4769  NZ  LYS B   4      59.139  63.933  55.731  1.00120.24           N1+
ANISOU 4769  NZ  LYS B   4    14065  12404  19217    383   -360  -1330       N1+
ATOM   4770  N   LYS B   5      56.885  59.480  61.840  1.00111.01           N  
ANISOU 4770  N   LYS B   5    12462  12268  17451    709   -144  -1869       N  
ATOM   4771  CA  LYS B   5      56.288  58.201  62.209  1.00107.79           C  
ANISOU 4771  CA  LYS B   5    11991  12028  16938    755   -137  -1777       C  
ATOM   4772  C   LYS B   5      56.195  57.293  60.990  1.00101.44           C  
ANISOU 4772  C   LYS B   5    11264  11146  16131    749   -184  -1589       C  
ATOM   4773  O   LYS B   5      55.733  57.712  59.930  1.00101.94           O  
ANISOU 4773  O   LYS B   5    11406  11035  16292    762   -230  -1529       O  
ATOM   4774  CB  LYS B   5      54.904  58.420  62.822  1.00115.28           C  
ANISOU 4774  CB  LYS B   5    12855  13009  17937    844   -135  -1839       C  
ATOM   4775  CG  LYS B   5      54.919  59.336  64.035  1.00123.96           C  
ANISOU 4775  CG  LYS B   5    13852  14209  19039    862    -92  -2063       C  
ATOM   4776  CD  LYS B   5      53.518  59.692  64.500  1.00126.96           C  
ANISOU 4776  CD  LYS B   5    14147  14605  19486    956    -96  -2144       C  
ATOM   4777  CE  LYS B   5      53.568  60.670  65.663  1.00131.05           C  
ANISOU 4777  CE  LYS B   5    14549  15230  20015    979    -58  -2410       C  
ATOM   4778  NZ  LYS B   5      52.210  61.111  66.082  1.00137.29           N1+
ANISOU 4778  NZ  LYS B   5    15248  16037  20881   1078    -63  -2517       N1+
ATOM   4779  N   VAL B   6      56.633  56.049  61.144  1.00 97.42           N  
ANISOU 4779  N   VAL B   6    10721  10776  15517    733   -177  -1502       N  
ATOM   4780  CA  VAL B   6      56.732  55.136  60.010  1.00 93.31           C  
ANISOU 4780  CA  VAL B   6    10257  10197  14998    724   -224  -1365       C  
ATOM   4781  C   VAL B   6      55.821  53.916  60.116  1.00 87.05           C  
ANISOU 4781  C   VAL B   6     9396   9466  14213    778   -249  -1264       C  
ATOM   4782  O   VAL B   6      55.664  53.331  61.188  1.00 82.73           O  
ANISOU 4782  O   VAL B   6     8745   9073  13617    793   -220  -1254       O  
ATOM   4783  CB  VAL B   6      58.181  54.656  59.808  1.00 92.04           C  
ANISOU 4783  CB  VAL B   6    10120  10102  14751    653   -213  -1348       C  
ATOM   4784  CG1 VAL B   6      59.043  55.787  59.273  1.00 94.65           C  
ANISOU 4784  CG1 VAL B   6    10533  10335  15095    589   -206  -1405       C  
ATOM   4785  CG2 VAL B   6      58.744  54.116  61.113  1.00 88.83           C  
ANISOU 4785  CG2 VAL B   6     9611   9892  14247    641   -166  -1379       C  
ATOM   4786  N   CYS B   7      55.226  53.543  58.988  1.00 87.37           N  
ANISOU 4786  N   CYS B   7     9485   9395  14318    803   -305  -1185       N  
ATOM   4787  CA  CYS B   7      54.412  52.337  58.896  1.00 84.30           C  
ANISOU 4787  CA  CYS B   7     9032   9033  13965    846   -341  -1091       C  
ATOM   4788  C   CYS B   7      54.987  51.423  57.821  1.00 83.21           C  
ANISOU 4788  C   CYS B   7     8926   8858  13830    823   -390  -1035       C  
ATOM   4789  O   CYS B   7      55.586  51.892  56.853  1.00 77.42           O  
ANISOU 4789  O   CYS B   7     8277   8063  13076    791   -406  -1055       O  
ATOM   4790  CB  CYS B   7      52.958  52.687  58.573  1.00 77.38           C  
ANISOU 4790  CB  CYS B   7     8156   8069  13176    910   -371  -1076       C  
ATOM   4791  SG  CYS B   7      52.738  53.631  57.048  1.00159.80           S  
ANISOU 4791  SG  CYS B   7    18717  18329  23671    915   -421  -1073       S  
ATOM   4792  N   GLN B   8      54.806  50.118  57.991  1.00 83.01           N  
ANISOU 4792  N   GLN B   8     8820   8880  13842    838   -417   -967       N  
ATOM   4793  CA  GLN B   8      55.407  49.153  57.079  1.00 80.49           C  
ANISOU 4793  CA  GLN B   8     8504   8535  13545    824   -467   -947       C  
ATOM   4794  C   GLN B   8      54.829  49.262  55.670  1.00 78.78           C  
ANISOU 4794  C   GLN B   8     8344   8220  13368    847   -526   -956       C  
ATOM   4795  O   GLN B   8      55.568  49.275  54.688  1.00 80.78           O  
ANISOU 4795  O   GLN B   8     8646   8468  13578    821   -549   -989       O  
ATOM   4796  CB  GLN B   8      55.258  47.728  57.615  1.00 81.74           C  
ANISOU 4796  CB  GLN B   8     8543   8736  13780    839   -492   -870       C  
ATOM   4797  CG  GLN B   8      56.408  46.811  57.227  1.00 87.61           C  
ANISOU 4797  CG  GLN B   8     9264   9493  14533    812   -520   -879       C  
ATOM   4798  CD  GLN B   8      57.748  47.313  57.742  1.00 93.18           C  
ANISOU 4798  CD  GLN B   8    10000  10289  15117    760   -463   -920       C  
ATOM   4799  NE2 GLN B   8      58.806  47.070  56.976  1.00 94.10           N  
ANISOU 4799  NE2 GLN B   8    10148  10404  15201    733   -482   -973       N  
ATOM   4800  OE1 GLN B   8      57.830  47.910  58.815  1.00 94.15           O  
ANISOU 4800  OE1 GLN B   8    10107  10496  15170    746   -404   -917       O  
ATOM   4801  N   GLY B   9      53.507  49.347  55.577  1.00 79.58           N  
ANISOU 4801  N   GLY B   9     8427   8268  13541    898   -551   -927       N  
ATOM   4802  CA  GLY B   9      52.845  49.457  54.291  1.00 79.76           C  
ANISOU 4802  CA  GLY B   9     8490   8221  13597    926   -611   -929       C  
ATOM   4803  C   GLY B   9      52.373  48.109  53.788  1.00 84.18           C  
ANISOU 4803  C   GLY B   9     8969   8768  14249    954   -678   -916       C  
ATOM   4804  O   GLY B   9      53.003  47.086  54.048  1.00 92.87           O  
ANISOU 4804  O   GLY B   9    10005   9897  15384    938   -689   -918       O  
ATOM   4805  N   THR B  10      51.260  48.106  53.063  1.00 80.59           N  
ANISOU 4805  N   THR B  10     8508   8264  13850    998   -729   -908       N  
ATOM   4806  CA  THR B  10      50.672  46.863  52.579  1.00 84.52           C  
ANISOU 4806  CA  THR B  10     8916   8738  14460   1027   -800   -915       C  
ATOM   4807  C   THR B  10      51.304  46.399  51.269  1.00 83.37           C  
ANISOU 4807  C   THR B  10     8774   8618  14286   1019   -857   -997       C  
ATOM   4808  O   THR B  10      51.980  47.166  50.586  1.00 80.45           O  
ANISOU 4808  O   THR B  10     8481   8294  13793    995   -844  -1024       O  
ATOM   4809  CB  THR B  10      49.150  46.998  52.390  1.00 94.91           C  
ANISOU 4809  CB  THR B  10    10205  10006  15849   1079   -833   -883       C  
ATOM   4810  CG2 THR B  10      48.496  47.470  53.679  1.00 97.35           C  
ANISOU 4810  CG2 THR B  10    10493  10320  16176   1092   -775   -819       C  
ATOM   4811  OG1 THR B  10      48.874  47.941  51.346  1.00 99.69           O  
ANISOU 4811  OG1 THR B  10    10889  10606  16383   1095   -854   -902       O  
ATOM   4812  N   SER B  11      51.080  45.133  50.931  1.00 87.21           N  
ANISOU 4812  N   SER B  11     9160   9081  14894   1039   -923  -1040       N  
ATOM   4813  CA  SER B  11      51.575  44.565  49.682  1.00 86.18           C  
ANISOU 4813  CA  SER B  11     9000   8995  14750   1043   -987  -1156       C  
ATOM   4814  C   SER B  11      50.658  43.442  49.210  1.00 86.51           C  
ANISOU 4814  C   SER B  11     8926   8984  14961   1084  -1074  -1212       C  
ATOM   4815  O   SER B  11      51.100  42.316  48.981  1.00 84.15           O  
ANISOU 4815  O   SER B  11     8532   8665  14776   1088  -1126  -1300       O  
ATOM   4816  CB  SER B  11      53.001  44.045  49.855  1.00 82.41           C  
ANISOU 4816  CB  SER B  11     8504   8556  14251   1008   -972  -1210       C  
ATOM   4817  OG  SER B  11      53.875  45.094  50.228  1.00 89.64           O  
ANISOU 4817  OG  SER B  11     9522   9526  15012    964   -895  -1170       O  
ATOM   4818  N   ASN B  12      49.377  43.765  49.067  1.00 80.14           N  
ANISOU 4818  N   ASN B  12     8117   8146  14185   1117  -1093  -1169       N  
ATOM   4819  CA  ASN B  12      48.372  42.789  48.675  1.00 76.31           C  
ANISOU 4819  CA  ASN B  12     7519   7606  13870   1153  -1175  -1217       C  
ATOM   4820  C   ASN B  12      47.871  43.053  47.262  1.00 83.78           C  
ANISOU 4820  C   ASN B  12     8465   8631  14738   1185  -1235  -1312       C  
ATOM   4821  O   ASN B  12      47.212  42.207  46.657  1.00 86.18           O  
ANISOU 4821  O   ASN B  12     8663   8917  15164   1214  -1316  -1404       O  
ATOM   4822  CB  ASN B  12      47.198  42.830  49.651  1.00 74.76           C  
ANISOU 4822  CB  ASN B  12     7293   7335  13779   1166  -1155  -1092       C  
ATOM   4823  CG  ASN B  12      47.639  43.049  51.085  1.00 74.60           C  
ANISOU 4823  CG  ASN B  12     7292   7304  13748   1134  -1073   -973       C  
ATOM   4824  ND2 ASN B  12      46.925  43.912  51.798  1.00 67.21           N  
ANISOU 4824  ND2 ASN B  12     6398   6379  12760   1145  -1017   -881       N  
ATOM   4825  OD1 ASN B  12      48.610  42.449  51.549  1.00 78.94           O  
ANISOU 4825  OD1 ASN B  12     7810   7850  14335   1104  -1061   -971       O  
ATOM   4826  N   LYS B  13      48.185  44.237  46.746  1.00 88.63           N  
ANISOU 4826  N   LYS B  13     9185   9336  15154   1177  -1200  -1283       N  
ATOM   4827  CA  LYS B  13      47.730  44.654  45.423  1.00 94.38           C  
ANISOU 4827  CA  LYS B  13     9912  10173  15773   1204  -1252  -1331       C  
ATOM   4828  C   LYS B  13      46.203  44.681  45.321  1.00 94.83           C  
ANISOU 4828  C   LYS B  13     9931  10185  15917   1251  -1293  -1295       C  
ATOM   4829  O   LYS B  13      45.537  45.412  46.056  1.00 99.18           O  
ANISOU 4829  O   LYS B  13    10538  10664  16484   1261  -1248  -1173       O  
ATOM   4830  CB  LYS B  13      48.328  43.755  44.338  1.00 95.15           C  
ANISOU 4830  CB  LYS B  13     9915  10384  15854   1209  -1321  -1510       C  
ATOM   4831  CG  LYS B  13      49.843  43.833  44.240  1.00 92.32           C  
ANISOU 4831  CG  LYS B  13     9591  10109  15378   1166  -1283  -1555       C  
ATOM   4832  CD  LYS B  13      50.371  42.891  43.173  1.00 98.65           C  
ANISOU 4832  CD  LYS B  13    10274  11038  16170   1182  -1357  -1763       C  
ATOM   4833  CE  LYS B  13      51.868  43.054  42.978  1.00 97.52           C  
ANISOU 4833  CE  LYS B  13    10158  11009  15884   1141  -1318  -1810       C  
ATOM   4834  NZ  LYS B  13      52.211  44.382  42.401  1.00 95.51           N1+
ANISOU 4834  NZ  LYS B  13    10002  10904  15384   1108  -1273  -1702       N1+
ATOM   4835  N   LEU B  14      45.654  43.883  44.412  1.00 83.99           N  
ANISOU 4835  N   LEU B  14     8449   8861  14602   1282  -1381  -1417       N  
ATOM   4836  CA  LEU B  14      44.216  43.883  44.170  1.00 80.74           C  
ANISOU 4836  CA  LEU B  14     7989   8428  14263   1327  -1429  -1397       C  
ATOM   4837  C   LEU B  14      43.467  42.916  45.084  1.00 90.57           C  
ANISOU 4837  C   LEU B  14     9143   9521  15747   1332  -1445  -1386       C  
ATOM   4838  O   LEU B  14      42.261  42.723  44.937  1.00 97.90           O  
ANISOU 4838  O   LEU B  14    10008  10423  16765   1364  -1490  -1383       O  
ATOM   4839  CB  LEU B  14      43.919  43.556  42.706  1.00 75.86           C  
ANISOU 4839  CB  LEU B  14     7282   7962  13578   1358  -1519  -1538       C  
ATOM   4840  CG  LEU B  14      44.584  44.460  41.668  1.00 76.16           C  
ANISOU 4840  CG  LEU B  14     7378   8196  13364   1350  -1512  -1528       C  
ATOM   4841  CD1 LEU B  14      44.208  44.023  40.264  1.00 79.09           C  
ANISOU 4841  CD1 LEU B  14     7629   8760  13661   1384  -1606  -1679       C  
ATOM   4842  CD2 LEU B  14      44.199  45.910  41.899  1.00 82.17           C  
ANISOU 4842  CD2 LEU B  14     8261   8937  14022   1353  -1459  -1327       C  
ATOM   4843  N   THR B  15      44.183  42.310  46.024  1.00 89.98           N  
ANISOU 4843  N   THR B  15     9054   9358  15777   1296  -1411  -1366       N  
ATOM   4844  CA  THR B  15      43.564  41.383  46.965  1.00 93.15           C  
ANISOU 4844  CA  THR B  15     9357   9626  16411   1289  -1424  -1315       C  
ATOM   4845  C   THR B  15      42.742  42.124  48.014  1.00 95.46           C  
ANISOU 4845  C   THR B  15     9698   9880  16692   1294  -1357  -1144       C  
ATOM   4846  O   THR B  15      43.131  43.195  48.479  1.00104.11           O  
ANISOU 4846  O   THR B  15    10908  11010  17638   1286  -1279  -1065       O  
ATOM   4847  CB  THR B  15      44.614  40.506  47.667  1.00 95.32           C  
ANISOU 4847  CB  THR B  15     9585   9830  16802   1251  -1412  -1319       C  
ATOM   4848  CG2 THR B  15      44.016  39.834  48.893  1.00 91.60           C  
ANISOU 4848  CG2 THR B  15     9027   9240  16536   1232  -1403  -1183       C  
ATOM   4849  OG1 THR B  15      45.077  39.500  46.759  1.00102.58           O  
ANISOU 4849  OG1 THR B  15    10405  10751  17821   1259  -1499  -1505       O  
ATOM   4850  N   GLN B  16      41.601  41.549  48.377  1.00 88.88           N  
ANISOU 4850  N   GLN B  16     8764   8980  16027   1305  -1391  -1100       N  
ATOM   4851  CA  GLN B  16      40.728  42.139  49.383  1.00 84.64           C  
ANISOU 4851  CA  GLN B  16     8241   8431  15488   1314  -1332   -955       C  
ATOM   4852  C   GLN B  16      40.771  41.357  50.690  1.00 90.09           C  
ANISOU 4852  C   GLN B  16     8840   9061  16328   1274  -1302   -838       C  
ATOM   4853  O   GLN B  16      40.572  40.143  50.703  1.00 96.50           O  
ANISOU 4853  O   GLN B  16     9521   9794  17350   1255  -1366   -845       O  
ATOM   4854  CB  GLN B  16      39.292  42.205  48.868  1.00 79.89           C  
ANISOU 4854  CB  GLN B  16     7584   7832  14939   1357  -1385   -965       C  
ATOM   4855  CG  GLN B  16      38.279  42.569  49.935  1.00 81.42           C  
ANISOU 4855  CG  GLN B  16     7750   8017  15168   1368  -1335   -830       C  
ATOM   4856  CD  GLN B  16      36.887  42.745  49.370  1.00 85.14           C  
ANISOU 4856  CD  GLN B  16     8174   8501  15674   1415  -1386   -846       C  
ATOM   4857  NE2 GLN B  16      35.903  42.878  50.252  1.00 90.32           N  
ANISOU 4857  NE2 GLN B  16     8774   9159  16386   1426  -1353   -742       N  
ATOM   4858  OE1 GLN B  16      36.698  42.765  48.155  1.00 82.85           O  
ANISOU 4858  OE1 GLN B  16     7886   8240  15351   1444  -1454   -951       O  
ATOM   4859  N   LEU B  17      41.022  42.060  51.789  1.00 89.31           N  
ANISOU 4859  N   LEU B  17     8797   9008  16128   1261  -1210   -728       N  
ATOM   4860  CA  LEU B  17      41.128  41.424  53.096  1.00 87.58           C  
ANISOU 4860  CA  LEU B  17     8486   8784  16008   1221  -1173   -592       C  
ATOM   4861  C   LEU B  17      39.785  41.388  53.815  1.00 92.26           C  
ANISOU 4861  C   LEU B  17     8982   9399  16673   1231  -1161   -478       C  
ATOM   4862  O   LEU B  17      39.452  42.302  54.569  1.00 93.50           O  
ANISOU 4862  O   LEU B  17     9176   9645  16704   1248  -1086   -420       O  
ATOM   4863  CB  LEU B  17      42.161  42.147  53.960  1.00 80.02           C  
ANISOU 4863  CB  LEU B  17     7614   7903  14888   1199  -1079   -547       C  
ATOM   4864  CG  LEU B  17      43.492  42.456  53.275  1.00 75.67           C  
ANISOU 4864  CG  LEU B  17     7174   7353  14224   1189  -1075   -655       C  
ATOM   4865  CD1 LEU B  17      44.483  43.043  54.268  1.00 73.93           C  
ANISOU 4865  CD1 LEU B  17     7013   7207  13871   1159   -986   -604       C  
ATOM   4866  CD2 LEU B  17      44.056  41.207  52.621  1.00 79.54           C  
ANISOU 4866  CD2 LEU B  17     7589   7768  14866   1171  -1156   -726       C  
ATOM   4867  N   GLY B  18      39.020  40.327  53.579  1.00 90.45           N  
ANISOU 4867  N   GLY B  18     8619   9094  16656   1221  -1237   -456       N  
ATOM   4868  CA  GLY B  18      37.743  40.142  54.244  1.00 88.80           C  
ANISOU 4868  CA  GLY B  18     8294   8911  16535   1221  -1233   -335       C  
ATOM   4869  C   GLY B  18      36.635  40.990  53.653  1.00 88.01           C  
ANISOU 4869  C   GLY B  18     8240   8846  16355   1280  -1240   -401       C  
ATOM   4870  O   GLY B  18      36.665  41.333  52.472  1.00 92.92           O  
ANISOU 4870  O   GLY B  18     8940   9439  16924   1316  -1287   -538       O  
ATOM   4871  N   THR B  19      35.650  41.326  54.480  1.00 81.18           N  
ANISOU 4871  N   THR B  19     7312   8060  15474   1292  -1196   -298       N  
ATOM   4872  CA  THR B  19      34.534  42.153  54.040  1.00 81.29           C  
ANISOU 4872  CA  THR B  19     7354   8108  15423   1355  -1202   -348       C  
ATOM   4873  C   THR B  19      34.990  43.594  53.868  1.00 80.43           C  
ANISOU 4873  C   THR B  19     7411   8047  15102   1405  -1144   -424       C  
ATOM   4874  O   THR B  19      36.018  43.993  54.411  1.00 80.84           O  
ANISOU 4874  O   THR B  19     7534   8131  15049   1384  -1082   -417       O  
ATOM   4875  CB  THR B  19      33.369  42.109  55.042  1.00 82.99           C  
ANISOU 4875  CB  THR B  19     7439   8412  15680   1356  -1166   -223       C  
ATOM   4876  CG2 THR B  19      33.047  40.674  55.417  1.00 81.59           C  
ANISOU 4876  CG2 THR B  19     7083   8188  15730   1289  -1215   -100       C  
ATOM   4877  OG1 THR B  19      33.721  42.842  56.223  1.00 88.28           O  
ANISOU 4877  OG1 THR B  19     8130   9211  16200   1357  -1064   -161       O  
ATOM   4878  N   PHE B  20      34.223  44.376  53.117  1.00 82.09           N  
ANISOU 4878  N   PHE B  20     7673   8256  15262   1468  -1170   -490       N  
ATOM   4879  CA  PHE B  20      34.588  45.763  52.860  1.00 84.00           C  
ANISOU 4879  CA  PHE B  20     8059   8513  15344   1515  -1131   -547       C  
ATOM   4880  C   PHE B  20      34.965  46.505  54.136  1.00 88.59           C  
ANISOU 4880  C   PHE B  20     8663   9166  15832   1513  -1031   -510       C  
ATOM   4881  O   PHE B  20      35.867  47.340  54.128  1.00 96.32           O  
ANISOU 4881  O   PHE B  20     9758  10137  16704   1515   -992   -555       O  
ATOM   4882  CB  PHE B  20      33.469  46.499  52.126  1.00 89.92           C  
ANISOU 4882  CB  PHE B  20     8823   9261  16083   1589  -1171   -581       C  
ATOM   4883  CG  PHE B  20      33.361  46.139  50.674  1.00 87.77           C  
ANISOU 4883  CG  PHE B  20     8563   8951  15834   1600  -1266   -648       C  
ATOM   4884  CD1 PHE B  20      32.134  46.135  50.034  1.00 87.79           C  
ANISOU 4884  CD1 PHE B  20     8504   8965  15888   1649  -1328   -662       C  
ATOM   4885  CD2 PHE B  20      34.490  45.793  49.952  1.00 79.79           C  
ANISOU 4885  CD2 PHE B  20     7612   7921  14786   1563  -1293   -706       C  
ATOM   4886  CE1 PHE B  20      32.036  45.804  48.698  1.00 86.38           C  
ANISOU 4886  CE1 PHE B  20     8320   8789  15713   1660  -1417   -737       C  
ATOM   4887  CE2 PHE B  20      34.399  45.458  48.617  1.00 82.49           C  
ANISOU 4887  CE2 PHE B  20     7944   8271  15128   1575  -1379   -787       C  
ATOM   4888  CZ  PHE B  20      33.170  45.463  47.989  1.00 85.15           C  
ANISOU 4888  CZ  PHE B  20     8216   8631  15508   1623  -1442   -804       C  
ATOM   4889  N   GLU B  21      34.280  46.200  55.233  1.00 91.22           N  
ANISOU 4889  N   GLU B  21     8871   9584  16203   1507   -992   -433       N  
ATOM   4890  CA  GLU B  21      34.600  46.827  56.509  1.00 97.61           C  
ANISOU 4890  CA  GLU B  21     9670  10507  16910   1506   -898   -415       C  
ATOM   4891  C   GLU B  21      35.924  46.302  57.045  1.00 99.01           C  
ANISOU 4891  C   GLU B  21     9860  10707  17054   1436   -863   -375       C  
ATOM   4892  O   GLU B  21      36.779  47.073  57.479  1.00104.10           O  
ANISOU 4892  O   GLU B  21    10583  11388  17582   1435   -804   -425       O  
ATOM   4893  CB  GLU B  21      33.490  46.603  57.535  1.00104.92           C  
ANISOU 4893  CB  GLU B  21    10434  11567  17864   1517   -864   -336       C  
ATOM   4894  CG  GLU B  21      33.863  47.067  58.934  1.00111.21           C  
ANISOU 4894  CG  GLU B  21    11180  12533  18541   1509   -768   -322       C  
ATOM   4895  CD  GLU B  21      32.661  47.221  59.840  1.00119.57           C  
ANISOU 4895  CD  GLU B  21    12085  13760  19584   1543   -729   -286       C  
ATOM   4896  OE1 GLU B  21      32.725  46.761  61.000  1.00123.87           O  
ANISOU 4896  OE1 GLU B  21    12496  14486  20083   1500   -675   -187       O  
ATOM   4897  OE2 GLU B  21      31.650  47.800  59.392  1.00124.28           O1-
ANISOU 4897  OE2 GLU B  21    12685  14326  20210   1613   -754   -350       O1-
ATOM   4898  N   ASP B  22      36.085  44.984  57.017  1.00 95.14           N  
ANISOU 4898  N   ASP B  22     9282  10186  16683   1378   -905   -289       N  
ATOM   4899  CA  ASP B  22      37.343  44.371  57.413  1.00 97.62           C  
ANISOU 4899  CA  ASP B  22     9598  10503  16991   1315   -887   -244       C  
ATOM   4900  C   ASP B  22      38.480  45.041  56.654  1.00 91.28           C  
ANISOU 4900  C   ASP B  22     8964   9628  16089   1321   -886   -363       C  
ATOM   4901  O   ASP B  22      39.382  45.626  57.251  1.00 91.13           O  
ANISOU 4901  O   ASP B  22     9003   9669  15951   1307   -821   -383       O  
ATOM   4902  CB  ASP B  22      37.330  42.869  57.114  1.00103.91           C  
ANISOU 4902  CB  ASP B  22    10287  11212  17984   1264   -962   -162       C  
ATOM   4903  CG  ASP B  22      36.170  42.150  57.777  1.00105.59           C  
ANISOU 4903  CG  ASP B  22    10318  11479  18321   1247   -973    -21       C  
ATOM   4904  OD1 ASP B  22      35.873  41.005  57.379  1.00 99.54           O  
ANISOU 4904  OD1 ASP B  22     9454  10609  17758   1213  -1051     32       O  
ATOM   4905  OD2 ASP B  22      35.554  42.731  58.693  1.00113.54           O1-
ANISOU 4905  OD2 ASP B  22    11271  12639  19232   1266   -907     31       O1-
ATOM   4906  N   HIS B  23      38.414  44.961  55.329  1.00 88.60           N  
ANISOU 4906  N   HIS B  23     8689   9179  15794   1340   -958   -443       N  
ATOM   4907  CA  HIS B  23      39.444  45.509  54.456  1.00 86.87           C  
ANISOU 4907  CA  HIS B  23     8612   8911  15483   1340   -966   -539       C  
ATOM   4908  C   HIS B  23      39.757  46.963  54.784  1.00 81.70           C  
ANISOU 4908  C   HIS B  23     8067   8293  14684   1366   -898   -580       C  
ATOM   4909  O   HIS B  23      40.918  47.373  54.776  1.00 86.00           O  
ANISOU 4909  O   HIS B  23     8699   8836  15140   1339   -866   -617       O  
ATOM   4910  CB  HIS B  23      39.012  45.392  52.994  1.00 90.73           C  
ANISOU 4910  CB  HIS B  23     9130   9331  16013   1369  -1053   -614       C  
ATOM   4911  CG  HIS B  23      40.066  45.808  52.017  1.00 88.59           C  
ANISOU 4911  CG  HIS B  23     8976   9042  15642   1361  -1069   -695       C  
ATOM   4912  CD2 HIS B  23      40.556  47.029  51.699  1.00 90.75           C  
ANISOU 4912  CD2 HIS B  23     9373   9325  15782   1376  -1036   -723       C  
ATOM   4913  ND1 HIS B  23      40.746  44.905  51.229  1.00 83.74           N  
ANISOU 4913  ND1 HIS B  23     8343   8404  15071   1333  -1126   -758       N  
ATOM   4914  CE1 HIS B  23      41.609  45.552  50.466  1.00 83.91           C  
ANISOU 4914  CE1 HIS B  23     8470   8448  14964   1329  -1123   -817       C  
ATOM   4915  NE2 HIS B  23      41.515  46.842  50.733  1.00 89.86           N  
ANISOU 4915  NE2 HIS B  23     9313   9215  15615   1350  -1070   -783       N  
ATOM   4916  N   PHE B  24      38.717  47.741  55.063  1.00 72.83           N  
ANISOU 4916  N   PHE B  24     6927   7193  13550   1421   -880   -583       N  
ATOM   4917  CA  PHE B  24      38.892  49.144  55.411  1.00 74.84           C  
ANISOU 4917  CA  PHE B  24     7264   7461  13712   1455   -825   -639       C  
ATOM   4918  C   PHE B  24      39.521  49.279  56.781  1.00 80.44           C  
ANISOU 4918  C   PHE B  24     7935   8276  14353   1424   -741   -635       C  
ATOM   4919  O   PHE B  24      40.455  50.055  56.974  1.00 90.92           O  
ANISOU 4919  O   PHE B  24     9345   9600  15600   1410   -699   -694       O  
ATOM   4920  CB  PHE B  24      37.553  49.876  55.411  1.00 81.44           C  
ANISOU 4920  CB  PHE B  24     8067   8294  14581   1531   -833   -655       C  
ATOM   4921  CG  PHE B  24      37.627  51.266  55.978  1.00 83.12           C  
ANISOU 4921  CG  PHE B  24     8328   8513  14741   1572   -778   -728       C  
ATOM   4922  CD1 PHE B  24      37.843  52.355  55.151  1.00 86.17           C  
ANISOU 4922  CD1 PHE B  24     8829   8789  15125   1603   -802   -771       C  
ATOM   4923  CD2 PHE B  24      37.488  51.483  57.339  1.00 80.41           C  
ANISOU 4923  CD2 PHE B  24     7898   8293  14361   1579   -706   -754       C  
ATOM   4924  CE1 PHE B  24      37.914  53.634  55.670  1.00 85.23           C  
ANISOU 4924  CE1 PHE B  24     8740   8642  15002   1641   -761   -847       C  
ATOM   4925  CE2 PHE B  24      37.559  52.760  57.862  1.00 82.07           C  
ANISOU 4925  CE2 PHE B  24     8136   8505  14542   1622   -661   -858       C  
ATOM   4926  CZ  PHE B  24      37.772  53.836  57.027  1.00 81.95           C  
ANISOU 4926  CZ  PHE B  24     8238   8340  14561   1654   -692   -909       C  
ATOM   4927  N   LEU B  25      38.994  48.523  57.735  1.00 83.72           N  
ANISOU 4927  N   LEU B  25     8211   8800  14797   1411   -718   -558       N  
ATOM   4928  CA  LEU B  25      39.437  48.622  59.116  1.00 92.88           C  
ANISOU 4928  CA  LEU B  25     9301  10117  15872   1387   -638   -542       C  
ATOM   4929  C   LEU B  25      40.904  48.205  59.262  1.00 90.75           C  
ANISOU 4929  C   LEU B  25     9076   9852  15552   1320   -620   -526       C  
ATOM   4930  O   LEU B  25      41.591  48.641  60.186  1.00 88.05           O  
ANISOU 4930  O   LEU B  25     8724   9623  15107   1303   -554   -556       O  
ATOM   4931  CB  LEU B  25      38.521  47.800  60.029  1.00 94.56           C  
ANISOU 4931  CB  LEU B  25     9334  10472  16124   1379   -625   -426       C  
ATOM   4932  CG  LEU B  25      38.407  48.254  61.486  1.00 98.48           C  
ANISOU 4932  CG  LEU B  25     9720  11192  16504   1387   -539   -431       C  
ATOM   4933  CD1 LEU B  25      38.514  49.767  61.600  1.00100.43           C  
ANISOU 4933  CD1 LEU B  25    10052  11438  16668   1445   -498   -610       C  
ATOM   4934  CD2 LEU B  25      37.107  47.756  62.100  1.00 97.20           C  
ANISOU 4934  CD2 LEU B  25     9384  11168  16381   1402   -536   -332       C  
ATOM   4935  N   SER B  26      41.379  47.373  58.338  1.00 86.82           N  
ANISOU 4935  N   SER B  26     8617   9242  15128   1288   -682   -496       N  
ATOM   4936  CA  SER B  26      42.790  46.997  58.298  1.00 87.48           C  
ANISOU 4936  CA  SER B  26     8749   9314  15175   1233   -674   -497       C  
ATOM   4937  C   SER B  26      43.615  48.118  57.684  1.00 85.28           C  
ANISOU 4937  C   SER B  26     8625   8973  14803   1238   -659   -612       C  
ATOM   4938  O   SER B  26      44.699  48.439  58.165  1.00 90.13           O  
ANISOU 4938  O   SER B  26     9279   9638  15330   1203   -611   -643       O  
ATOM   4939  CB  SER B  26      42.995  45.710  57.495  1.00 95.94           C  
ANISOU 4939  CB  SER B  26     9790  10288  16374   1204   -752   -452       C  
ATOM   4940  OG  SER B  26      42.441  44.591  58.164  1.00109.47           O  
ANISOU 4940  OG  SER B  26    11347  12044  18204   1183   -768   -321       O  
ATOM   4941  N   LEU B  27      43.093  48.706  56.613  1.00 82.64           N  
ANISOU 4941  N   LEU B  27     8370   8538  14492   1278   -703   -663       N  
ATOM   4942  CA  LEU B  27      43.748  49.828  55.955  1.00 80.79           C  
ANISOU 4942  CA  LEU B  27     8269   8239  14189   1280   -696   -739       C  
ATOM   4943  C   LEU B  27      43.948  50.972  56.940  1.00 81.89           C  
ANISOU 4943  C   LEU B  27     8424   8425  14264   1290   -623   -798       C  
ATOM   4944  O   LEU B  27      44.878  51.766  56.805  1.00 87.99           O  
ANISOU 4944  O   LEU B  27     9286   9164  14982   1265   -600   -854       O  
ATOM   4945  CB  LEU B  27      42.916  50.306  54.762  1.00 82.56           C  
ANISOU 4945  CB  LEU B  27     8543   8371  14455   1329   -758   -750       C  
ATOM   4946  CG  LEU B  27      43.427  51.533  54.004  1.00 84.73           C  
ANISOU 4946  CG  LEU B  27     8939   8573  14680   1332   -762   -786       C  
ATOM   4947  CD1 LEU B  27      44.721  51.211  53.275  1.00 91.86           C  
ANISOU 4947  CD1 LEU B  27     9906   9476  15518   1272   -775   -792       C  
ATOM   4948  CD2 LEU B  27      42.377  52.035  53.031  1.00 80.33           C  
ANISOU 4948  CD2 LEU B  27     8399   7951  14171   1391   -822   -767       C  
ATOM   4949  N   GLN B  28      43.069  51.047  57.934  1.00 78.36           N  
ANISOU 4949  N   GLN B  28     7877   8067  13828   1325   -589   -796       N  
ATOM   4950  CA  GLN B  28      43.135  52.104  58.935  1.00 79.89           C  
ANISOU 4950  CA  GLN B  28     8054   8332  13967   1346   -523   -889       C  
ATOM   4951  C   GLN B  28      44.183  51.810  60.002  1.00 87.26           C  
ANISOU 4951  C   GLN B  28     8943   9409  14805   1291   -461   -896       C  
ATOM   4952  O   GLN B  28      44.876  52.715  60.467  1.00 85.30           O  
ANISOU 4952  O   GLN B  28     8729   9184  14499   1282   -416   -999       O  
ATOM   4953  CB  GLN B  28      41.770  52.308  59.595  1.00 82.35           C  
ANISOU 4953  CB  GLN B  28     8255   8724  14310   1411   -510   -903       C  
ATOM   4954  CG  GLN B  28      41.745  53.463  60.584  1.00 87.16           C  
ANISOU 4954  CG  GLN B  28     8829   9413  14876   1447   -449  -1041       C  
ATOM   4955  CD  GLN B  28      40.418  53.602  61.301  1.00 87.03           C  
ANISOU 4955  CD  GLN B  28     8679   9515  14875   1515   -432  -1069       C  
ATOM   4956  NE2 GLN B  28      40.277  54.672  62.074  1.00 86.37           N  
ANISOU 4956  NE2 GLN B  28     8550   9495  14770   1561   -387  -1226       N  
ATOM   4957  OE1 GLN B  28      39.531  52.759  61.167  1.00 88.13           O  
ANISOU 4957  OE1 GLN B  28     8744   9690  15050   1524   -459   -963       O  
ATOM   4958  N   ARG B  29      44.295  50.542  60.386  1.00 93.29           N  
ANISOU 4958  N   ARG B  29     9616  10266  15564   1254   -464   -782       N  
ATOM   4959  CA  ARG B  29      45.224  50.137  61.437  1.00 90.52           C  
ANISOU 4959  CA  ARG B  29     9198  10074  15121   1204   -411   -755       C  
ATOM   4960  C   ARG B  29      46.679  50.220  60.990  1.00 89.20           C  
ANISOU 4960  C   ARG B  29     9139   9841  14911   1151   -410   -791       C  
ATOM   4961  O   ARG B  29      47.584  50.344  61.815  1.00 90.38           O  
ANISOU 4961  O   ARG B  29     9262  10112  14966   1116   -359   -819       O  
ATOM   4962  CB  ARG B  29      44.900  48.722  61.922  1.00 91.73           C  
ANISOU 4962  CB  ARG B  29     9211  10326  15315   1178   -426   -588       C  
ATOM   4963  CG  ARG B  29      43.558  48.608  62.626  1.00107.93           C  
ANISOU 4963  CG  ARG B  29    11124  12503  17383   1216   -412   -534       C  
ATOM   4964  CD  ARG B  29      43.278  47.184  63.076  1.00115.24           C  
ANISOU 4964  CD  ARG B  29    11900  13512  18373   1177   -434   -336       C  
ATOM   4965  NE  ARG B  29      43.357  46.236  61.970  1.00116.85           N  
ANISOU 4965  NE  ARG B  29    12150  13518  18730   1157   -515   -271       N  
ATOM   4966  CZ  ARG B  29      42.989  44.962  62.051  1.00120.30           C  
ANISOU 4966  CZ  ARG B  29    12467  13945  19298   1127   -560   -110       C  
ATOM   4967  NH1 ARG B  29      42.509  44.480  63.190  1.00122.68           N1+
ANISOU 4967  NH1 ARG B  29    12596  14434  19584   1108   -528     38       N1+
ATOM   4968  NH2 ARG B  29      43.099  44.170  60.993  1.00122.72           N  
ANISOU 4968  NH2 ARG B  29    12810  14062  19755   1115   -640    -98       N  
ATOM   4969  N   MET B  30      46.898  50.158  59.681  1.00 90.93           N  
ANISOU 4969  N   MET B  30     9467   9892  15189   1146   -467   -794       N  
ATOM   4970  CA  MET B  30      48.247  50.192  59.128  1.00 88.44           C  
ANISOU 4970  CA  MET B  30     9248   9525  14831   1095   -471   -824       C  
ATOM   4971  C   MET B  30      48.741  51.617  58.893  1.00 85.31           C  
ANISOU 4971  C   MET B  30     8958   9065  14388   1092   -444   -936       C  
ATOM   4972  O   MET B  30      49.927  51.902  59.056  1.00100.07           O  
ANISOU 4972  O   MET B  30    10873  10960  16191   1044   -414   -979       O  
ATOM   4973  CB  MET B  30      48.310  49.388  57.824  1.00 87.38           C  
ANISOU 4973  CB  MET B  30     9155   9279  14768   1088   -545   -782       C  
ATOM   4974  CG  MET B  30      49.596  49.568  57.026  1.00 85.14           C  
ANISOU 4974  CG  MET B  30     8972   8949  14430   1044   -554   -828       C  
ATOM   4975  SD  MET B  30      51.037  48.806  57.796  1.00104.68           S  
ANISOU 4975  SD  MET B  30    11401  11526  16845    983   -519   -810       S  
ATOM   4976  CE  MET B  30      50.539  47.087  57.824  1.00164.23           C  
ANISOU 4976  CE  MET B  30    18815  19065  24519    993   -577   -702       C  
ATOM   4977  N   PHE B  31      47.835  52.513  58.519  1.00 69.12           N  
ANISOU 4977  N   PHE B  31     6942   6928  12393   1143   -461   -976       N  
ATOM   4978  CA  PHE B  31      48.233  53.865  58.145  1.00 72.18           C  
ANISOU 4978  CA  PHE B  31     7426   7212  12787   1140   -453  -1059       C  
ATOM   4979  C   PHE B  31      47.766  54.941  59.119  1.00 86.29           C  
ANISOU 4979  C   PHE B  31     9167   9025  14593   1181   -409  -1172       C  
ATOM   4980  O   PHE B  31      47.871  56.131  58.827  1.00 91.27           O  
ANISOU 4980  O   PHE B  31     9861   9536  15281   1190   -413  -1243       O  
ATOM   4981  CB  PHE B  31      47.752  54.189  56.731  1.00 70.82           C  
ANISOU 4981  CB  PHE B  31     7334   6892  12681   1163   -520  -1012       C  
ATOM   4982  CG  PHE B  31      48.365  53.321  55.675  1.00 73.94           C  
ANISOU 4982  CG  PHE B  31     7770   7278  13044   1123   -564   -944       C  
ATOM   4983  CD1 PHE B  31      47.722  52.177  55.240  1.00 78.11           C  
ANISOU 4983  CD1 PHE B  31     8245   7826  13605   1144   -611   -886       C  
ATOM   4984  CD2 PHE B  31      49.591  53.646  55.125  1.00 79.44           C  
ANISOU 4984  CD2 PHE B  31     8545   7955  13684   1063   -559   -953       C  
ATOM   4985  CE1 PHE B  31      48.289  51.375  54.271  1.00 79.76           C  
ANISOU 4985  CE1 PHE B  31     8474   8036  13795   1114   -656   -862       C  
ATOM   4986  CE2 PHE B  31      50.163  52.849  54.157  1.00 82.02           C  
ANISOU 4986  CE2 PHE B  31     8892   8301  13970   1032   -599   -915       C  
ATOM   4987  CZ  PHE B  31      49.512  51.712  53.729  1.00 81.33           C  
ANISOU 4987  CZ  PHE B  31     8747   8236  13920   1061   -649   -882       C  
ATOM   4988  N   ASN B  32      47.255  54.529  60.273  1.00 94.32           N  
ANISOU 4988  N   ASN B  32    10062  10205  15571   1205   -369  -1189       N  
ATOM   4989  CA  ASN B  32      46.832  55.490  61.283  1.00106.55           C  
ANISOU 4989  CA  ASN B  32    11540  11824  17120   1248   -325  -1330       C  
ATOM   4990  C   ASN B  32      48.030  56.236  61.865  1.00111.05           C  
ANISOU 4990  C   ASN B  32    12129  12428  17637   1202   -278  -1457       C  
ATOM   4991  O   ASN B  32      48.920  55.626  62.458  1.00111.52           O  
ANISOU 4991  O   ASN B  32    12153  12634  17588   1149   -242  -1437       O  
ATOM   4992  CB  ASN B  32      46.041  54.801  62.397  1.00117.45           C  
ANISOU 4992  CB  ASN B  32    12761  13425  18440   1279   -290  -1308       C  
ATOM   4993  CG  ASN B  32      45.346  55.788  63.316  1.00131.66           C  
ANISOU 4993  CG  ASN B  32    14466  15314  20244   1343   -253  -1473       C  
ATOM   4994  ND2 ASN B  32      45.003  55.337  64.519  1.00156.72           N  
ANISOU 4994  ND2 ASN B  32    17481  18751  23314   1354   -204  -1481       N  
ATOM   4995  OD1 ASN B  32      45.116  56.940  62.949  1.00124.11           O  
ANISOU 4995  OD1 ASN B  32    13566  14200  19389   1384   -271  -1592       O  
ATOM   4996  N   ASN B  33      48.046  57.554  61.678  1.00112.82           N  
ANISOU 4996  N   ASN B  33    12402  12509  17954   1223   -285  -1582       N  
ATOM   4997  CA  ASN B  33      49.117  58.414  62.185  1.00109.15           C  
ANISOU 4997  CA  ASN B  33    11950  12046  17476   1179   -248  -1726       C  
ATOM   4998  C   ASN B  33      50.409  58.315  61.379  1.00101.52           C  
ANISOU 4998  C   ASN B  33    11102  10984  16488   1093   -261  -1652       C  
ATOM   4999  O   ASN B  33      51.363  59.048  61.631  1.00 99.00           O  
ANISOU 4999  O   ASN B  33    10805  10638  16173   1046   -238  -1755       O  
ATOM   5000  CB  ASN B  33      49.399  58.125  63.661  1.00114.76           C  
ANISOU 5000  CB  ASN B  33    12523  13033  18049   1173   -181  -1829       C  
ATOM   5001  CG  ASN B  33      48.166  58.266  64.527  1.00127.06           C  
ANISOU 5001  CG  ASN B  33    13939  14732  19604   1256   -161  -1917       C  
ATOM   5002  ND2 ASN B  33      47.301  59.211  64.176  1.00134.65           N  
ANISOU 5002  ND2 ASN B  33    14916  15530  20717   1325   -193  -2007       N  
ATOM   5003  OD1 ASN B  33      47.989  57.531  65.498  1.00129.98           O  
ANISOU 5003  OD1 ASN B  33    14179  15368  19841   1259   -119  -1895       O  
ATOM   5004  N   CYS B  34      50.429  57.407  60.408  1.00 96.71           N  
ANISOU 5004  N   CYS B  34    10555  10333  15857   1073   -300  -1485       N  
ATOM   5005  CA  CYS B  34      51.614  57.176  59.591  1.00 85.12           C  
ANISOU 5005  CA  CYS B  34     9182   8811  14349    996   -314  -1413       C  
ATOM   5006  C   CYS B  34      52.025  58.428  58.817  1.00 87.25           C  
ANISOU 5006  C   CYS B  34     9545   8888  14719    969   -338  -1438       C  
ATOM   5007  O   CYS B  34      51.182  59.132  58.262  1.00 91.32           O  
ANISOU 5007  O   CYS B  34    10084   9257  15356   1016   -379  -1421       O  
ATOM   5008  CB  CYS B  34      51.367  56.015  58.626  1.00 70.45           C  
ANISOU 5008  CB  CYS B  34     7353   6947  12470    997   -361  -1261       C  
ATOM   5009  SG  CYS B  34      52.778  55.590  57.585  1.00122.77           S  
ANISOU 5009  SG  CYS B  34    14069  13550  19029    912   -380  -1191       S  
ATOM   5010  N   GLU B  35      53.325  58.701  58.788  1.00 82.21           N  
ANISOU 5010  N   GLU B  35     8948   8251  14037    889   -316  -1465       N  
ATOM   5011  CA  GLU B  35      53.850  59.854  58.066  1.00 82.09           C  
ANISOU 5011  CA  GLU B  35     9009   8058  14123    844   -339  -1462       C  
ATOM   5012  C   GLU B  35      54.771  59.421  56.933  1.00 79.66           C  
ANISOU 5012  C   GLU B  35     8781   7746  13742    772   -362  -1328       C  
ATOM   5013  O   GLU B  35      54.968  60.155  55.964  1.00 77.68           O  
ANISOU 5013  O   GLU B  35     8591   7361  13562    739   -398  -1249       O  
ATOM   5014  CB  GLU B  35      54.603  60.787  59.016  1.00 90.91           C  
ANISOU 5014  CB  GLU B  35    10092   9171  15277    806   -296  -1631       C  
ATOM   5015  CG  GLU B  35      53.753  61.342  60.146  1.00105.97           C  
ANISOU 5015  CG  GLU B  35    11902  11105  17257    881   -274  -1805       C  
ATOM   5016  CD  GLU B  35      54.506  62.343  61.000  1.00112.88           C  
ANISOU 5016  CD  GLU B  35    12732  11969  18190    844   -240  -2005       C  
ATOM   5017  OE1 GLU B  35      55.562  62.832  60.549  1.00114.90           O  
ANISOU 5017  OE1 GLU B  35    13048  12128  18480    760   -245  -1986       O  
ATOM   5018  OE2 GLU B  35      54.040  62.644  62.120  1.00114.32           O1-
ANISOU 5018  OE2 GLU B  35    12806  12250  18380    898   -210  -2188       O1-
ATOM   5019  N   VAL B  36      55.340  58.227  57.064  1.00 79.22           N  
ANISOU 5019  N   VAL B  36     8707   7846  13546    748   -343  -1301       N  
ATOM   5020  CA  VAL B  36      56.259  57.699  56.063  1.00 74.29           C  
ANISOU 5020  CA  VAL B  36     8136   7253  12839    686   -361  -1207       C  
ATOM   5021  C   VAL B  36      56.013  56.220  55.810  1.00 75.92           C  
ANISOU 5021  C   VAL B  36     8310   7569  12967    716   -381  -1148       C  
ATOM   5022  O   VAL B  36      56.296  55.381  56.664  1.00 77.80           O  
ANISOU 5022  O   VAL B  36     8489   7928  13145    718   -351  -1182       O  
ATOM   5023  CB  VAL B  36      57.722  57.868  56.495  1.00 68.97           C  
ANISOU 5023  CB  VAL B  36     7467   6646  12091    601   -316  -1269       C  
ATOM   5024  CG1 VAL B  36      58.648  57.274  55.444  1.00 70.38           C  
ANISOU 5024  CG1 VAL B  36     7687   6880  12176    544   -335  -1182       C  
ATOM   5025  CG2 VAL B  36      58.042  59.333  56.730  1.00 70.10           C  
ANISOU 5025  CG2 VAL B  36     7631   6662  12340    562   -303  -1339       C  
ATOM   5026  N   VAL B  37      55.491  55.903  54.631  1.00 75.40           N  
ANISOU 5026  N   VAL B  37     8272   7464  12912    739   -437  -1058       N  
ATOM   5027  CA  VAL B  37      55.225  54.520  54.263  1.00 73.50           C  
ANISOU 5027  CA  VAL B  37     7991   7304  12632    768   -469  -1021       C  
ATOM   5028  C   VAL B  37      56.484  53.888  53.684  1.00 70.42           C  
ANISOU 5028  C   VAL B  37     7611   7000  12145    709   -472  -1017       C  
ATOM   5029  O   VAL B  37      56.858  54.166  52.545  1.00 62.97           O  
ANISOU 5029  O   VAL B  37     6709   6054  11161    678   -501   -975       O  
ATOM   5030  CB  VAL B  37      54.087  54.424  53.230  1.00 76.38           C  
ANISOU 5030  CB  VAL B  37     8363   7611  13046    823   -533   -953       C  
ATOM   5031  CG1 VAL B  37      53.677  52.978  53.029  1.00 75.28           C  
ANISOU 5031  CG1 VAL B  37     8160   7539  12904    859   -569   -945       C  
ATOM   5032  CG2 VAL B  37      52.898  55.258  53.674  1.00 77.88           C  
ANISOU 5032  CG2 VAL B  37     8547   7703  13339    881   -534   -957       C  
ATOM   5033  N   LEU B  38      57.137  53.042  54.476  1.00 76.16           N  
ANISOU 5033  N   LEU B  38     8288   7818  12831    696   -443  -1057       N  
ATOM   5034  CA  LEU B  38      58.389  52.411  54.066  1.00 77.03           C  
ANISOU 5034  CA  LEU B  38     8394   8014  12859    646   -443  -1072       C  
ATOM   5035  C   LEU B  38      58.186  51.494  52.868  1.00 81.68           C  
ANISOU 5035  C   LEU B  38     8963   8627  13446    672   -508  -1053       C  
ATOM   5036  O   LEU B  38      59.090  51.317  52.052  1.00 82.47           O  
ANISOU 5036  O   LEU B  38     9071   8793  13469    634   -521  -1070       O  
ATOM   5037  CB  LEU B  38      58.993  51.618  55.226  1.00 73.82           C  
ANISOU 5037  CB  LEU B  38     7920   7696  12432    640   -408  -1103       C  
ATOM   5038  CG  LEU B  38      59.204  52.392  56.528  1.00 75.73           C  
ANISOU 5038  CG  LEU B  38     8152   7965  12656    619   -344  -1146       C  
ATOM   5039  CD1 LEU B  38      59.517  51.445  57.675  1.00 72.33           C  
ANISOU 5039  CD1 LEU B  38     7627   7653  12203    627   -319  -1142       C  
ATOM   5040  CD2 LEU B  38      60.300  53.435  56.363  1.00 75.82           C  
ANISOU 5040  CD2 LEU B  38     8225   7971  12612    545   -310  -1193       C  
ATOM   5041  N   GLY B  39      56.995  50.913  52.771  1.00 87.02           N  
ANISOU 5041  N   GLY B  39     9599   9263  14203    737   -549  -1031       N  
ATOM   5042  CA  GLY B  39      56.670  50.006  51.686  1.00 89.34           C  
ANISOU 5042  CA  GLY B  39     9854   9579  14512    768   -618  -1041       C  
ATOM   5043  C   GLY B  39      55.684  50.597  50.699  1.00 90.15           C  
ANISOU 5043  C   GLY B  39     9989   9642  14624    799   -661  -1001       C  
ATOM   5044  O   GLY B  39      55.896  51.692  50.179  1.00 91.45           O  
ANISOU 5044  O   GLY B  39    10217   9798  14732    766   -651   -959       O  
ATOM   5045  N   ASN B  40      54.599  49.873  50.443  1.00 87.75           N  
ANISOU 5045  N   ASN B  40     9629   9311  14400    858   -712  -1002       N  
ATOM   5046  CA  ASN B  40      53.598  50.308  49.474  1.00 83.55           C  
ANISOU 5046  CA  ASN B  40     9111   8760  13873    895   -762   -964       C  
ATOM   5047  C   ASN B  40      52.351  50.907  50.116  1.00 81.34           C  
ANISOU 5047  C   ASN B  40     8844   8380  13683    940   -752   -913       C  
ATOM   5048  O   ASN B  40      51.916  50.471  51.181  1.00 83.57           O  
ANISOU 5048  O   ASN B  40     9082   8630  14041    963   -729   -920       O  
ATOM   5049  CB  ASN B  40      53.198  49.146  48.562  1.00 80.98           C  
ANISOU 5049  CB  ASN B  40     8706   8490  13573    932   -837  -1023       C  
ATOM   5050  CG  ASN B  40      54.317  48.719  47.637  1.00 82.04           C  
ANISOU 5050  CG  ASN B  40     8818   8750  13604    899   -858  -1095       C  
ATOM   5051  ND2 ASN B  40      54.396  47.423  47.364  1.00 96.34           N  
ANISOU 5051  ND2 ASN B  40    10536  10596  15474    925   -907  -1197       N  
ATOM   5052  OD1 ASN B  40      55.100  49.544  47.170  1.00 70.91           O  
ANISOU 5052  OD1 ASN B  40     7462   7407  12072    850   -833  -1062       O  
ATOM   5053  N   LEU B  41      51.784  51.912  49.455  1.00 76.41           N  
ANISOU 5053  N   LEU B  41     8264   7718  13048    954   -771   -853       N  
ATOM   5054  CA  LEU B  41      50.513  52.492  49.865  1.00 70.18           C  
ANISOU 5054  CA  LEU B  41     7476   6837  12351   1010   -775   -815       C  
ATOM   5055  C   LEU B  41      49.415  51.974  48.949  1.00 73.69           C  
ANISOU 5055  C   LEU B  41     7874   7301  12825   1066   -849   -799       C  
ATOM   5056  O   LEU B  41      49.263  52.449  47.825  1.00 78.14           O  
ANISOU 5056  O   LEU B  41     8456   7898  13337   1069   -892   -748       O  
ATOM   5057  CB  LEU B  41      50.567  54.018  49.786  1.00 70.08           C  
ANISOU 5057  CB  LEU B  41     7535   6745  12347    995   -756   -755       C  
ATOM   5058  CG  LEU B  41      49.253  54.753  50.069  1.00 72.20           C  
ANISOU 5058  CG  LEU B  41     7800   6909  12725   1062   -769   -724       C  
ATOM   5059  CD1 LEU B  41      48.853  54.610  51.529  1.00 70.33           C  
ANISOU 5059  CD1 LEU B  41     7524   6645  12554   1090   -718   -794       C  
ATOM   5060  CD2 LEU B  41      49.356  56.219  49.686  1.00 74.09           C  
ANISOU 5060  CD2 LEU B  41     8098   7052  13003   1047   -774   -650       C  
ATOM   5061  N   GLU B  42      48.655  50.995  49.427  1.00 71.70           N  
ANISOU 5061  N   GLU B  42     7547   7040  12654   1105   -865   -833       N  
ATOM   5062  CA  GLU B  42      47.607  50.385  48.617  1.00 69.81           C  
ANISOU 5062  CA  GLU B  42     7248   6820  12458   1155   -938   -838       C  
ATOM   5063  C   GLU B  42      46.211  50.638  49.178  1.00 77.06           C  
ANISOU 5063  C   GLU B  42     8137   7666  13477   1215   -941   -803       C  
ATOM   5064  O   GLU B  42      45.743  49.918  50.060  1.00 83.50           O  
ANISOU 5064  O   GLU B  42     8887   8463  14375   1229   -927   -816       O  
ATOM   5065  CB  GLU B  42      47.853  48.884  48.477  1.00 67.69           C  
ANISOU 5065  CB  GLU B  42     6892   6597  12229   1150   -974   -917       C  
ATOM   5066  CG  GLU B  42      49.071  48.531  47.643  1.00 76.03           C  
ANISOU 5066  CG  GLU B  42     7952   7750  13186   1108   -991   -980       C  
ATOM   5067  CD  GLU B  42      49.508  47.094  47.845  1.00 88.16           C  
ANISOU 5067  CD  GLU B  42     9399   9296  14801   1102  -1015  -1071       C  
ATOM   5068  OE1 GLU B  42      49.280  46.555  48.947  1.00 88.82           O  
ANISOU 5068  OE1 GLU B  42     9441   9307  14998   1104   -992  -1047       O  
ATOM   5069  OE2 GLU B  42      50.083  46.505  46.906  1.00 95.72           O1-
ANISOU 5069  OE2 GLU B  42    10313  10341  15714   1095  -1061  -1165       O1-
ATOM   5070  N   ILE B  43      45.556  51.668  48.652  1.00 74.69           N  
ANISOU 5070  N   ILE B  43     7875   7331  13171   1249   -961   -746       N  
ATOM   5071  CA  ILE B  43      44.185  51.992  49.021  1.00 69.20           C  
ANISOU 5071  CA  ILE B  43     7148   6576  12568   1314   -973   -719       C  
ATOM   5072  C   ILE B  43      43.227  51.391  48.001  1.00 74.73           C  
ANISOU 5072  C   ILE B  43     7786   7321  13286   1357  -1054   -717       C  
ATOM   5073  O   ILE B  43      43.065  51.925  46.902  1.00 67.23           O  
ANISOU 5073  O   ILE B  43     6857   6407  12280   1372  -1102   -671       O  
ATOM   5074  CB  ILE B  43      43.957  53.507  49.039  1.00 65.81           C  
ANISOU 5074  CB  ILE B  43     6783   6064  12156   1337   -958   -660       C  
ATOM   5075  CG1 ILE B  43      45.168  54.232  49.628  1.00 71.68           C  
ANISOU 5075  CG1 ILE B  43     7595   6773  12866   1279   -893   -672       C  
ATOM   5076  CG2 ILE B  43      42.691  53.844  49.807  1.00 67.95           C  
ANISOU 5076  CG2 ILE B  43     7012   6274  12534   1406   -949   -665       C  
ATOM   5077  CD1 ILE B  43      45.136  55.735  49.411  1.00 75.10           C  
ANISOU 5077  CD1 ILE B  43     8087   7104  13344   1288   -895   -611       C  
ATOM   5078  N   THR B  44      42.594  50.281  48.368  1.00 78.58           N  
ANISOU 5078  N   THR B  44     8185   7816  13854   1374  -1073   -759       N  
ATOM   5079  CA  THR B  44      41.682  49.589  47.464  1.00 79.76           C  
ANISOU 5079  CA  THR B  44     8258   8009  14040   1411  -1154   -784       C  
ATOM   5080  C   THR B  44      40.417  49.128  48.183  1.00 83.32           C  
ANISOU 5080  C   THR B  44     8625   8415  14617   1452  -1160   -776       C  
ATOM   5081  O   THR B  44      40.431  48.895  49.390  1.00 87.46           O  
ANISOU 5081  O   THR B  44     9125   8908  15199   1438  -1104   -763       O  
ATOM   5082  CB  THR B  44      42.362  48.372  46.809  1.00 81.46           C  
ANISOU 5082  CB  THR B  44     8417   8293  14241   1376  -1198   -875       C  
ATOM   5083  CG2 THR B  44      43.452  48.819  45.847  1.00 81.67           C  
ANISOU 5083  CG2 THR B  44     8504   8410  14118   1343  -1205   -886       C  
ATOM   5084  OG1 THR B  44      42.948  47.546  47.823  1.00 84.13           O  
ANISOU 5084  OG1 THR B  44     8723   8590  14651   1338  -1158   -901       O  
ATOM   5085  N   TYR B  45      39.326  49.014  47.431  1.00 83.65           N  
ANISOU 5085  N   TYR B  45     8613   8479  14692   1500  -1227   -777       N  
ATOM   5086  CA  TYR B  45      38.057  48.497  47.949  1.00 76.12           C  
ANISOU 5086  CA  TYR B  45     7564   7499  13861   1536  -1244   -771       C  
ATOM   5087  C   TYR B  45      37.439  49.332  49.070  1.00 71.43           C  
ANISOU 5087  C   TYR B  45     6982   6858  13300   1569  -1180   -714       C  
ATOM   5088  O   TYR B  45      36.719  48.804  49.916  1.00 74.27           O  
ANISOU 5088  O   TYR B  45     7256   7216  13749   1577  -1164   -701       O  
ATOM   5089  CB  TYR B  45      38.215  47.047  48.407  1.00 69.35           C  
ANISOU 5089  CB  TYR B  45     6609   6631  13111   1494  -1255   -813       C  
ATOM   5090  CG  TYR B  45      38.674  46.120  47.313  1.00 75.62           C  
ANISOU 5090  CG  TYR B  45     7358   7465  13909   1474  -1329   -910       C  
ATOM   5091  CD1 TYR B  45      39.922  45.516  47.365  1.00 81.23           C  
ANISOU 5091  CD1 TYR B  45     8077   8179  14609   1422  -1317   -962       C  
ATOM   5092  CD2 TYR B  45      37.864  45.856  46.219  1.00 83.66           C  
ANISOU 5092  CD2 TYR B  45     8313   8534  14940   1510  -1414   -967       C  
ATOM   5093  CE1 TYR B  45      40.345  44.666  46.361  1.00 81.53           C  
ANISOU 5093  CE1 TYR B  45     8057   8264  14657   1412  -1388  -1082       C  
ATOM   5094  CE2 TYR B  45      38.279  45.010  45.213  1.00 87.60           C  
ANISOU 5094  CE2 TYR B  45     8750   9095  15439   1497  -1485  -1091       C  
ATOM   5095  CZ  TYR B  45      39.518  44.419  45.286  1.00 80.81           C  
ANISOU 5095  CZ  TYR B  45     7896   8233  14576   1449  -1472  -1155       C  
ATOM   5096  OH  TYR B  45      39.925  43.578  44.278  1.00 78.43           O  
ANISOU 5096  OH  TYR B  45     7516   8002  14280   1444  -1545  -1308       O  
ATOM   5097  N   VAL B  46      37.716  50.631  49.073  1.00 66.36           N  
ANISOU 5097  N   VAL B  46     6433   6185  12596   1589  -1148   -683       N  
ATOM   5098  CA  VAL B  46      37.115  51.526  50.053  1.00 74.97           C  
ANISOU 5098  CA  VAL B  46     7525   7233  13729   1633  -1097   -665       C  
ATOM   5099  C   VAL B  46      35.783  52.040  49.520  1.00 89.02           C  
ANISOU 5099  C   VAL B  46     9269   8996  15557   1713  -1150   -638       C  
ATOM   5100  O   VAL B  46      35.734  52.695  48.479  1.00 91.33           O  
ANISOU 5100  O   VAL B  46     9609   9276  15818   1738  -1200   -599       O  
ATOM   5101  CB  VAL B  46      38.026  52.719  50.371  1.00 75.34           C  
ANISOU 5101  CB  VAL B  46     7672   7227  13728   1620  -1044   -664       C  
ATOM   5102  CG1 VAL B  46      37.527  53.443  51.608  1.00 73.40           C  
ANISOU 5102  CG1 VAL B  46     7399   6955  13536   1661   -984   -695       C  
ATOM   5103  CG2 VAL B  46      39.457  52.253  50.570  1.00 76.12           C  
ANISOU 5103  CG2 VAL B  46     7815   7352  13756   1539  -1006   -687       C  
ATOM   5104  N   GLN B  47      34.707  51.743  50.239  1.00 92.23           N  
ANISOU 5104  N   GLN B  47     9582   9420  16040   1750  -1140   -646       N  
ATOM   5105  CA  GLN B  47      33.363  52.043  49.758  1.00 90.33           C  
ANISOU 5105  CA  GLN B  47     9288   9178  15854   1826  -1195   -626       C  
ATOM   5106  C   GLN B  47      32.884  53.436  50.156  1.00101.20           C  
ANISOU 5106  C   GLN B  47    10692  10493  17268   1899  -1171   -622       C  
ATOM   5107  O   GLN B  47      33.537  54.133  50.931  1.00107.78           O  
ANISOU 5107  O   GLN B  47    11573  11286  18093   1890  -1108   -652       O  
ATOM   5108  CB  GLN B  47      32.376  50.981  50.244  1.00 88.44           C  
ANISOU 5108  CB  GLN B  47     8917   8994  15690   1828  -1204   -634       C  
ATOM   5109  CG  GLN B  47      32.723  49.571  49.794  1.00 87.01           C  
ANISOU 5109  CG  GLN B  47     8687   8844  15529   1763  -1245   -648       C  
ATOM   5110  CD  GLN B  47      32.621  49.396  48.291  1.00 89.53           C  
ANISOU 5110  CD  GLN B  47     9017   9182  15818   1776  -1336   -669       C  
ATOM   5111  NE2 GLN B  47      33.615  48.742  47.703  1.00 88.47           N  
ANISOU 5111  NE2 GLN B  47     8907   9066  15642   1720  -1359   -709       N  
ATOM   5112  OE1 GLN B  47      31.659  49.840  47.668  1.00 94.71           O  
ANISOU 5112  OE1 GLN B  47     9649   9854  16483   1838  -1387   -653       O  
ATOM   5113  N   ARG B  48      31.734  53.829  49.615  1.00104.99           N  
ANISOU 5113  N   ARG B  48    11130  10963  17799   1976  -1227   -596       N  
ATOM   5114  CA  ARG B  48      31.165  55.152  49.850  1.00100.70           C  
ANISOU 5114  CA  ARG B  48    10596  10341  17324   2060  -1224   -595       C  
ATOM   5115  C   ARG B  48      31.072  55.489  51.334  1.00 97.00           C  
ANISOU 5115  C   ARG B  48    10085   9877  16895   2078  -1140   -679       C  
ATOM   5116  O   ARG B  48      30.938  54.601  52.174  1.00102.81           O  
ANISOU 5116  O   ARG B  48    10743  10709  17611   2043  -1095   -710       O  
ATOM   5117  CB  ARG B  48      29.770  55.240  49.225  1.00106.33           C  
ANISOU 5117  CB  ARG B  48    11235  11071  18094   2142  -1295   -561       C  
ATOM   5118  CG  ARG B  48      29.734  55.043  47.717  1.00120.21           C  
ANISOU 5118  CG  ARG B  48    13015  12860  19800   2139  -1385   -484       C  
ATOM   5119  CD  ARG B  48      30.087  56.326  46.981  1.00134.15           C  
ANISOU 5119  CD  ARG B  48    14859  14539  21571   2172  -1421   -394       C  
ATOM   5120  NE  ARG B  48      29.127  57.393  47.252  1.00145.69           N  
ANISOU 5120  NE  ARG B  48    16287  15912  23157   2274  -1437   -380       N  
ATOM   5121  CZ  ARG B  48      29.240  58.636  46.793  1.00148.64           C  
ANISOU 5121  CZ  ARG B  48    16707  16172  23598   2319  -1472   -293       C  
ATOM   5122  NH1 ARG B  48      28.317  59.541  47.092  1.00148.77           N1+
ANISOU 5122  NH1 ARG B  48    16675  16095  23755   2420  -1492   -297       N1+
ATOM   5123  NH2 ARG B  48      30.276  58.976  46.036  1.00145.82           N  
ANISOU 5123  NH2 ARG B  48    16432  15794  23178   2261  -1490   -196       N  
ATOM   5124  N   ASN B  49      31.151  56.780  51.646  1.00 95.35           N  
ANISOU 5124  N   ASN B  49     9910   9569  16748   2131  -1123   -715       N  
ATOM   5125  CA  ASN B  49      30.898  57.283  52.996  1.00 99.17           C  
ANISOU 5125  CA  ASN B  49    10329  10074  17277   2171  -1053   -830       C  
ATOM   5126  C   ASN B  49      31.844  56.777  54.084  1.00 94.85           C  
ANISOU 5126  C   ASN B  49     9775   9618  16645   2093   -967   -892       C  
ATOM   5127  O   ASN B  49      31.613  57.006  55.273  1.00 90.95           O  
ANISOU 5127  O   ASN B  49     9200   9204  16154   2120   -904   -993       O  
ATOM   5128  CB  ASN B  49      29.445  57.024  53.396  1.00102.70           C  
ANISOU 5128  CB  ASN B  49    10642  10608  17770   2245  -1061   -859       C  
ATOM   5129  CG  ASN B  49      28.462  57.751  52.504  1.00113.42           C  
ANISOU 5129  CG  ASN B  49    11993  11876  19227   2340  -1142   -817       C  
ATOM   5130  ND2 ASN B  49      28.748  59.017  52.214  1.00110.14           N  
ANISOU 5130  ND2 ASN B  49    11641  11305  18901   2388  -1166   -821       N  
ATOM   5131  OD1 ASN B  49      27.460  57.181  52.075  1.00123.90           O  
ANISOU 5131  OD1 ASN B  49    13250  13265  20561   2370  -1187   -773       O  
ATOM   5132  N   TYR B  50      32.905  56.089  53.680  1.00 89.95           N  
ANISOU 5132  N   TYR B  50     9229   9006  15943   2001   -964   -836       N  
ATOM   5133  CA  TYR B  50      33.941  55.697  54.625  1.00 86.84           C  
ANISOU 5133  CA  TYR B  50     8838   8685  15471   1927   -889   -880       C  
ATOM   5134  C   TYR B  50      34.919  56.841  54.847  1.00 88.63           C  
ANISOU 5134  C   TYR B  50     9149   8816  15709   1920   -858   -946       C  
ATOM   5135  O   TYR B  50      35.182  57.634  53.943  1.00 93.09           O  
ANISOU 5135  O   TYR B  50     9802   9243  16325   1932   -905   -906       O  
ATOM   5136  CB  TYR B  50      34.676  54.446  54.150  1.00 88.70           C  
ANISOU 5136  CB  TYR B  50     9103   8965  15635   1837   -903   -804       C  
ATOM   5137  CG  TYR B  50      34.058  53.161  54.643  1.00 89.55           C  
ANISOU 5137  CG  TYR B  50     9091   9194  15741   1814   -896   -768       C  
ATOM   5138  CD1 TYR B  50      33.465  52.268  53.762  1.00 92.04           C  
ANISOU 5138  CD1 TYR B  50     9373   9505  16093   1809   -965   -707       C  
ATOM   5139  CD2 TYR B  50      34.062  52.843  55.994  1.00 89.11           C  
ANISOU 5139  CD2 TYR B  50     8939   9265  15653   1796   -824   -791       C  
ATOM   5140  CE1 TYR B  50      32.899  51.093  54.212  1.00 96.03           C  
ANISOU 5140  CE1 TYR B  50     9758  10096  16632   1781   -966   -665       C  
ATOM   5141  CE2 TYR B  50      33.497  51.671  56.453  1.00 90.73           C  
ANISOU 5141  CE2 TYR B  50     9020   9580  15873   1766   -821   -723       C  
ATOM   5142  CZ  TYR B  50      32.917  50.800  55.559  1.00 96.64           C  
ANISOU 5142  CZ  TYR B  50     9742  10288  16688   1757   -894   -657       C  
ATOM   5143  OH  TYR B  50      32.352  49.631  56.012  1.00100.80           O  
ANISOU 5143  OH  TYR B  50    10135  10900  17264   1721   -898   -581       O  
ATOM   5144  N   ASP B  51      35.456  56.925  56.057  1.00 88.21           N  
ANISOU 5144  N   ASP B  51     9058   8848  15612   1895   -782  -1041       N  
ATOM   5145  CA  ASP B  51      36.327  58.034  56.418  1.00 91.33           C  
ANISOU 5145  CA  ASP B  51     9509   9157  16034   1890   -750  -1136       C  
ATOM   5146  C   ASP B  51      37.802  57.707  56.205  1.00 87.70           C  
ANISOU 5146  C   ASP B  51     9144   8689  15488   1788   -730  -1097       C  
ATOM   5147  O   ASP B  51      38.393  56.924  56.950  1.00 84.34           O  
ANISOU 5147  O   ASP B  51     8684   8399  14962   1730   -676  -1110       O  
ATOM   5148  CB  ASP B  51      36.075  58.451  57.865  1.00 98.73           C  
ANISOU 5148  CB  ASP B  51    10334  10212  16968   1930   -681  -1297       C  
ATOM   5149  CG  ASP B  51      36.726  59.768  58.209  1.00104.61           C  
ANISOU 5149  CG  ASP B  51    11114  10842  17792   1946   -663  -1436       C  
ATOM   5150  OD1 ASP B  51      37.319  60.390  57.304  1.00103.44           O  
ANISOU 5150  OD1 ASP B  51    11079  10505  17717   1924   -707  -1379       O  
ATOM   5151  OD2 ASP B  51      36.641  60.180  59.384  1.00111.34           O1-
ANISOU 5151  OD2 ASP B  51    11867  11802  18637   1978   -607  -1603       O1-
ATOM   5152  N   LEU B  52      38.390  58.316  55.180  1.00 90.42           N  
ANISOU 5152  N   LEU B  52     9599   8885  15872   1767   -774  -1038       N  
ATOM   5153  CA  LEU B  52      39.803  58.125  54.880  1.00 93.47           C  
ANISOU 5153  CA  LEU B  52    10074   9262  16179   1672   -758  -1003       C  
ATOM   5154  C   LEU B  52      40.612  59.341  55.315  1.00102.93           C  
ANISOU 5154  C   LEU B  52    11312  10358  17437   1658   -728  -1094       C  
ATOM   5155  O   LEU B  52      41.654  59.646  54.734  1.00104.28           O  
ANISOU 5155  O   LEU B  52    11572  10458  17593   1593   -737  -1044       O  
ATOM   5156  CB  LEU B  52      40.004  57.880  53.385  1.00 81.13           C  
ANISOU 5156  CB  LEU B  52     8589   7642  14594   1644   -828   -865       C  
ATOM   5157  CG  LEU B  52      39.442  56.579  52.817  1.00 69.51           C  
ANISOU 5157  CG  LEU B  52     7078   6269  13064   1642   -866   -796       C  
ATOM   5158  CD1 LEU B  52      39.649  56.531  51.314  1.00 69.35           C  
ANISOU 5158  CD1 LEU B  52     7119   6219  13013   1624   -937   -690       C  
ATOM   5159  CD2 LEU B  52      40.099  55.389  53.487  1.00 64.14           C  
ANISOU 5159  CD2 LEU B  52     6365   5711  12296   1578   -819   -820       C  
ATOM   5160  N   SER B  53      40.127  60.030  56.342  1.00101.37           N  
ANISOU 5160  N   SER B  53    11038  10164  17313   1718   -694  -1238       N  
ATOM   5161  CA  SER B  53      40.757  61.262  56.803  1.00 99.41           C  
ANISOU 5161  CA  SER B  53    10805   9802  17165   1716   -674  -1361       C  
ATOM   5162  C   SER B  53      42.127  61.025  57.425  1.00101.91           C  
ANISOU 5162  C   SER B  53    11147  10204  17371   1624   -612  -1421       C  
ATOM   5163  O   SER B  53      42.919  61.957  57.562  1.00108.89           O  
ANISOU 5163  O   SER B  53    12065  10978  18330   1594   -604  -1496       O  
ATOM   5164  CB  SER B  53      39.849  61.990  57.794  1.00106.48           C  
ANISOU 5164  CB  SER B  53    11586  10707  18166   1813   -656  -1542       C  
ATOM   5165  OG  SER B  53      38.713  62.526  57.138  1.00117.23           O  
ANISOU 5165  OG  SER B  53    12933  11936  19673   1903   -723  -1496       O  
ATOM   5166  N   PHE B  54      42.407  59.783  57.800  1.00 99.43           N  
ANISOU 5166  N   PHE B  54    10806  10078  16894   1577   -573  -1382       N  
ATOM   5167  CA  PHE B  54      43.687  59.462  58.420  1.00 96.80           C  
ANISOU 5167  CA  PHE B  54    10486   9847  16448   1494   -516  -1426       C  
ATOM   5168  C   PHE B  54      44.819  59.426  57.400  1.00 94.30           C  
ANISOU 5168  C   PHE B  54    10291   9434  16106   1411   -542  -1319       C  
ATOM   5169  O   PHE B  54      45.992  59.401  57.767  1.00 99.18           O  
ANISOU 5169  O   PHE B  54    10933  10098  16653   1340   -502  -1359       O  
ATOM   5170  CB  PHE B  54      43.613  58.141  59.193  1.00 94.34           C  
ANISOU 5170  CB  PHE B  54    10088   9765  15992   1474   -473  -1398       C  
ATOM   5171  CG  PHE B  54      43.208  56.962  58.354  1.00 85.35           C  
ANISOU 5171  CG  PHE B  54     8967   8640  14821   1463   -517  -1235       C  
ATOM   5172  CD1 PHE B  54      44.132  56.310  57.557  1.00 87.34           C  
ANISOU 5172  CD1 PHE B  54     9300   8867  15017   1391   -538  -1139       C  
ATOM   5173  CD2 PHE B  54      41.906  56.496  58.378  1.00 81.96           C  
ANISOU 5173  CD2 PHE B  54     8459   8258  14424   1524   -539  -1196       C  
ATOM   5174  CE1 PHE B  54      43.761  55.221  56.791  1.00 88.42           C  
ANISOU 5174  CE1 PHE B  54     9436   9018  15143   1386   -584  -1025       C  
ATOM   5175  CE2 PHE B  54      41.530  55.409  57.615  1.00 85.41           C  
ANISOU 5175  CE2 PHE B  54     8899   8700  14853   1511   -585  -1067       C  
ATOM   5176  CZ  PHE B  54      42.459  54.770  56.820  1.00 86.04           C  
ANISOU 5176  CZ  PHE B  54     9055   8747  14888   1444   -609   -991       C  
ATOM   5177  N   LEU B  55      44.462  59.431  56.119  1.00 90.78           N  
ANISOU 5177  N   LEU B  55     9909   8878  15704   1421   -608  -1185       N  
ATOM   5178  CA  LEU B  55      45.456  59.390  55.053  1.00 88.61           C  
ANISOU 5178  CA  LEU B  55     9732   8548  15387   1345   -636  -1074       C  
ATOM   5179  C   LEU B  55      46.049  60.766  54.777  1.00 94.81           C  
ANISOU 5179  C   LEU B  55    10573   9164  16289   1320   -648  -1084       C  
ATOM   5180  O   LEU B  55      46.796  60.948  53.817  1.00102.78           O  
ANISOU 5180  O   LEU B  55    11653  10120  17277   1258   -676   -973       O  
ATOM   5181  CB  LEU B  55      44.852  58.814  53.770  1.00 80.76           C  
ANISOU 5181  CB  LEU B  55     8763   7549  14373   1364   -704   -929       C  
ATOM   5182  CG  LEU B  55      44.480  57.330  53.806  1.00 74.65           C  
ANISOU 5182  CG  LEU B  55     7938   6920  13504   1367   -705   -904       C  
ATOM   5183  CD1 LEU B  55      44.036  56.857  52.433  1.00 65.98           C  
ANISOU 5183  CD1 LEU B  55     6861   5819  12389   1378   -779   -791       C  
ATOM   5184  CD2 LEU B  55      45.647  56.496  54.308  1.00 76.57           C  
ANISOU 5184  CD2 LEU B  55     8184   7275  13636   1291   -657   -933       C  
ATOM   5185  N   LYS B  56      45.718  61.734  55.624  1.00 92.26           N  
ANISOU 5185  N   LYS B  56    10201   8759  16095   1367   -630  -1222       N  
ATOM   5186  CA  LYS B  56      46.226  63.090  55.450  1.00 98.87           C  
ANISOU 5186  CA  LYS B  56    11071   9400  17095   1345   -650  -1246       C  
ATOM   5187  C   LYS B  56      47.616  63.257  56.055  1.00 93.41           C  
ANISOU 5187  C   LYS B  56    10397   8745  16350   1254   -595  -1339       C  
ATOM   5188  O   LYS B  56      48.319  64.218  55.748  1.00 99.18           O  
ANISOU 5188  O   LYS B  56    11166   9320  17198   1204   -612  -1326       O  
ATOM   5189  CB  LYS B  56      45.265  64.113  56.063  1.00103.92           C  
ANISOU 5189  CB  LYS B  56    11635   9914  17935   1442   -665  -1383       C  
ATOM   5190  CG  LYS B  56      43.894  64.146  55.413  1.00106.86           C  
ANISOU 5190  CG  LYS B  56    11987  10225  18390   1535   -728  -1288       C  
ATOM   5191  CD  LYS B  56      43.101  65.366  55.857  1.00114.80           C  
ANISOU 5191  CD  LYS B  56    12923  11059  19638   1629   -756  -1418       C  
ATOM   5192  CE  LYS B  56      42.911  65.389  57.364  1.00120.86           C  
ANISOU 5192  CE  LYS B  56    13582  11951  20388   1673   -689  -1684       C  
ATOM   5193  NZ  LYS B  56      42.107  66.565  57.801  1.00125.07           N1+
ANISOU 5193  NZ  LYS B  56    14028  12325  21168   1775   -720  -1847       N1+
ATOM   5194  N   THR B  57      48.009  62.321  56.911  1.00 80.43           N  
ANISOU 5194  N   THR B  57     8717   7305  14539   1231   -533  -1421       N  
ATOM   5195  CA  THR B  57      49.281  62.427  57.618  1.00 77.10           C  
ANISOU 5195  CA  THR B  57     8294   6948  14051   1153   -477  -1525       C  
ATOM   5196  C   THR B  57      50.444  61.803  56.852  1.00 83.83           C  
ANISOU 5196  C   THR B  57     9228   7849  14774   1055   -476  -1392       C  
ATOM   5197  O   THR B  57      51.604  62.024  57.195  1.00 92.47           O  
ANISOU 5197  O   THR B  57    10337   8967  15832    980   -441  -1451       O  
ATOM   5198  CB  THR B  57      49.204  61.812  59.029  1.00 70.59           C  
ANISOU 5198  CB  THR B  57     7367   6345  13107   1176   -410  -1678       C  
ATOM   5199  CG2 THR B  57      48.509  62.768  59.983  1.00 69.09           C  
ANISOU 5199  CG2 THR B  57     7081   6125  13045   1252   -398  -1884       C  
ATOM   5200  OG1 THR B  57      48.471  60.582  58.979  1.00 69.03           O  
ANISOU 5200  OG1 THR B  57     7140   6291  12798   1211   -411  -1581       O  
ATOM   5201  N   ILE B  58      50.133  61.027  55.818  1.00 79.93           N  
ANISOU 5201  N   ILE B  58     8775   7381  14212   1058   -516  -1229       N  
ATOM   5202  CA  ILE B  58      51.170  60.412  54.997  1.00 80.71           C  
ANISOU 5202  CA  ILE B  58     8936   7542  14186    976   -521  -1118       C  
ATOM   5203  C   ILE B  58      51.910  61.470  54.188  1.00 89.85           C  
ANISOU 5203  C   ILE B  58    10156   8559  15424    910   -547  -1040       C  
ATOM   5204  O   ILE B  58      51.311  62.171  53.371  1.00 95.49           O  
ANISOU 5204  O   ILE B  58    10890   9139  16254    936   -604   -934       O  
ATOM   5205  CB  ILE B  58      50.591  59.361  54.033  1.00 78.76           C  
ANISOU 5205  CB  ILE B  58     8698   7367  13859   1003   -566   -991       C  
ATOM   5206  CG1 ILE B  58      49.978  58.197  54.815  1.00 75.38           C  
ANISOU 5206  CG1 ILE B  58     8199   7074  13367   1050   -542  -1044       C  
ATOM   5207  CG2 ILE B  58      51.671  58.858  53.087  1.00 73.50           C  
ANISOU 5207  CG2 ILE B  58     8081   6769  13075    924   -577   -901       C  
ATOM   5208  CD1 ILE B  58      49.399  57.113  53.935  1.00 65.00           C  
ANISOU 5208  CD1 ILE B  58     6877   5817  12003   1075   -591   -947       C  
ATOM   5209  N   GLN B  59      53.213  61.580  54.420  1.00 90.15           N  
ANISOU 5209  N   GLN B  59    10215   8633  15404    822   -509  -1077       N  
ATOM   5210  CA  GLN B  59      54.026  62.585  53.749  1.00 93.32           C  
ANISOU 5210  CA  GLN B  59    10661   8910  15886    743   -529   -996       C  
ATOM   5211  C   GLN B  59      54.814  61.995  52.588  1.00 96.82           C  
ANISOU 5211  C   GLN B  59    11149   9458  16179    672   -546   -842       C  
ATOM   5212  O   GLN B  59      55.032  62.658  51.576  1.00105.92           O  
ANISOU 5212  O   GLN B  59    12330  10535  17380    627   -587   -691       O  
ATOM   5213  CB  GLN B  59      54.984  63.245  54.739  1.00 97.86           C  
ANISOU 5213  CB  GLN B  59    11218   9452  16511    684   -479  -1149       C  
ATOM   5214  CG  GLN B  59      54.302  63.867  55.941  1.00106.93           C  
ANISOU 5214  CG  GLN B  59    12300  10531  17797    754   -461  -1343       C  
ATOM   5215  CD  GLN B  59      55.270  64.631  56.820  1.00118.26           C  
ANISOU 5215  CD  GLN B  59    13704  11931  19298    692   -421  -1511       C  
ATOM   5216  NE2 GLN B  59      55.126  64.477  58.130  1.00123.40           N  
ANISOU 5216  NE2 GLN B  59    14277  12697  19911    733   -372  -1720       N  
ATOM   5217  OE1 GLN B  59      56.135  65.355  56.327  1.00120.33           O  
ANISOU 5217  OE1 GLN B  59    14000  12077  19642    606   -436  -1452       O  
ATOM   5218  N   GLU B  60      55.244  60.747  52.735  1.00 90.82           N  
ANISOU 5218  N   GLU B  60    10382   8882  15244    663   -517   -878       N  
ATOM   5219  CA  GLU B  60      56.046  60.104  51.702  1.00 91.15           C  
ANISOU 5219  CA  GLU B  60    10448   9049  15137    603   -531   -776       C  
ATOM   5220  C   GLU B  60      55.842  58.592  51.651  1.00 83.63           C  
ANISOU 5220  C   GLU B  60     9467   8258  14052    644   -532   -806       C  
ATOM   5221  O   GLU B  60      55.708  57.935  52.683  1.00 80.03           O  
ANISOU 5221  O   GLU B  60     8974   7853  13581    677   -497   -911       O  
ATOM   5222  CB  GLU B  60      57.529  60.435  51.895  1.00100.30           C  
ANISOU 5222  CB  GLU B  60    11623  10241  16247    499   -489   -804       C  
ATOM   5223  CG  GLU B  60      57.982  60.436  53.348  1.00106.35           C  
ANISOU 5223  CG  GLU B  60    12362  11022  17025    492   -427   -978       C  
ATOM   5224  CD  GLU B  60      59.491  60.512  53.492  1.00104.45           C  
ANISOU 5224  CD  GLU B  60    12129  10852  16703    391   -387  -1010       C  
ATOM   5225  OE1 GLU B  60      60.190  59.654  52.911  1.00101.48           O  
ANISOU 5225  OE1 GLU B  60    11758  10620  16179    357   -386   -964       O  
ATOM   5226  OE2 GLU B  60      59.976  61.425  54.194  1.00100.70           O1-
ANISOU 5226  OE2 GLU B  60    11647  10294  16320    347   -359  -1096       O1-
ATOM   5227  N   VAL B  61      55.816  58.051  50.438  1.00 78.34           N  
ANISOU 5227  N   VAL B  61     8798   7674  13294    641   -577   -712       N  
ATOM   5228  CA  VAL B  61      55.692  56.614  50.236  1.00 75.11           C  
ANISOU 5228  CA  VAL B  61     8350   7401  12789    676   -591   -752       C  
ATOM   5229  C   VAL B  61      56.894  56.092  49.457  1.00 71.36           C  
ANISOU 5229  C   VAL B  61     7870   7070  12171    610   -592   -741       C  
ATOM   5230  O   VAL B  61      57.132  56.505  48.322  1.00 73.80           O  
ANISOU 5230  O   VAL B  61     8190   7429  12423    575   -624   -643       O  
ATOM   5231  CB  VAL B  61      54.405  56.261  49.472  1.00 74.44           C  
ANISOU 5231  CB  VAL B  61     8241   7314  12730    751   -654   -696       C  
ATOM   5232  CG1 VAL B  61      54.343  54.766  49.207  1.00 79.30           C  
ANISOU 5232  CG1 VAL B  61     8801   8054  13274    780   -677   -754       C  
ATOM   5233  CG2 VAL B  61      53.186  56.719  50.252  1.00 69.32           C  
ANISOU 5233  CG2 VAL B  61     7584   6537  12217    822   -653   -715       C  
ATOM   5234  N   ALA B  62      57.645  55.183  50.072  1.00 60.77           N  
ANISOU 5234  N   ALA B  62     6503   5814  10774    596   -559   -836       N  
ATOM   5235  CA  ALA B  62      58.876  54.667  49.478  1.00 63.36           C  
ANISOU 5235  CA  ALA B  62     6816   6283  10976    538   -555   -854       C  
ATOM   5236  C   ALA B  62      58.626  53.757  48.277  1.00 68.86           C  
ANISOU 5236  C   ALA B  62     7465   7101  11597    571   -615   -853       C  
ATOM   5237  O   ALA B  62      59.343  53.822  47.280  1.00 63.79           O  
ANISOU 5237  O   ALA B  62     6811   6585  10841    525   -629   -824       O  
ATOM   5238  CB  ALA B  62      59.705  53.944  50.527  1.00 66.33           C  
ANISOU 5238  CB  ALA B  62     7166   6706  11332    523   -509   -954       C  
ATOM   5239  N   GLY B  63      57.612  52.904  48.376  1.00 76.79           N  
ANISOU 5239  N   GLY B  63     8427   8082  12666    648   -651   -892       N  
ATOM   5240  CA  GLY B  63      57.273  52.001  47.292  1.00 79.37           C  
ANISOU 5240  CA  GLY B  63     8693   8519  12947    687   -715   -925       C  
ATOM   5241  C   GLY B  63      56.460  52.686  46.211  1.00 79.94           C  
ANISOU 5241  C   GLY B  63     8773   8608  12991    704   -762   -825       C  
ATOM   5242  O   GLY B  63      56.876  53.709  45.667  1.00 84.60           O  
ANISOU 5242  O   GLY B  63     9400   9226  13518    650   -754   -721       O  
ATOM   5243  N   TYR B  64      55.299  52.118  45.897  1.00 79.69           N  
ANISOU 5243  N   TYR B  64     8698   8566  13015    776   -816   -845       N  
ATOM   5244  CA  TYR B  64      54.387  52.709  44.923  1.00 79.50           C  
ANISOU 5244  CA  TYR B  64     8670   8566  12970    804   -867   -748       C  
ATOM   5245  C   TYR B  64      53.032  52.975  45.563  1.00 82.86           C  
ANISOU 5245  C   TYR B  64     9113   8831  13541    869   -876   -714       C  
ATOM   5246  O   TYR B  64      52.741  52.483  46.653  1.00 84.78           O  
ANISOU 5246  O   TYR B  64     9349   8979  13883    896   -849   -780       O  
ATOM   5247  CB  TYR B  64      54.211  51.790  43.714  1.00 76.49           C  
ANISOU 5247  CB  TYR B  64     8198   8370  12496    835   -935   -819       C  
ATOM   5248  CG  TYR B  64      53.682  50.419  44.070  1.00 85.20           C  
ANISOU 5248  CG  TYR B  64     9231   9444  13698    895   -966   -964       C  
ATOM   5249  CD1 TYR B  64      52.344  50.229  44.391  1.00 82.64           C  
ANISOU 5249  CD1 TYR B  64     8891   9009  13499    959   -996   -954       C  
ATOM   5250  CD2 TYR B  64      54.521  49.315  44.087  1.00 92.02           C  
ANISOU 5250  CD2 TYR B  64    10032  10383  14548    887   -971  -1106       C  
ATOM   5251  CE1 TYR B  64      51.859  48.977  44.720  1.00 79.03           C  
ANISOU 5251  CE1 TYR B  64     8358   8514  13156   1004  -1028  -1068       C  
ATOM   5252  CE2 TYR B  64      54.046  48.062  44.412  1.00 89.78           C  
ANISOU 5252  CE2 TYR B  64     9671  10045  14396    938  -1008  -1224       C  
ATOM   5253  CZ  TYR B  64      52.716  47.897  44.728  1.00 80.22           C  
ANISOU 5253  CZ  TYR B  64     8445   8721  13313    992  -1037  -1197       C  
ATOM   5254  OH  TYR B  64      52.247  46.646  45.054  1.00 76.02           O  
ANISOU 5254  OH  TYR B  64     7824   8127  12933   1033  -1078  -1296       O  
ATOM   5255  N   VAL B  65      52.204  53.752  44.875  1.00 81.58           N  
ANISOU 5255  N   VAL B  65     8958   8654  13384    894   -916   -603       N  
ATOM   5256  CA  VAL B  65      50.870  54.068  45.365  1.00 75.84           C  
ANISOU 5256  CA  VAL B  65     8238   7787  12792    962   -930   -572       C  
ATOM   5257  C   VAL B  65      49.796  53.497  44.445  1.00 77.91           C  
ANISOU 5257  C   VAL B  65     8432   8132  13039   1026  -1005   -574       C  
ATOM   5258  O   VAL B  65      49.609  53.964  43.321  1.00 80.20           O  
ANISOU 5258  O   VAL B  65     8705   8522  13247   1026  -1053   -479       O  
ATOM   5259  CB  VAL B  65      50.669  55.585  45.519  1.00 69.33           C  
ANISOU 5259  CB  VAL B  65     7476   6830  12039    951   -916   -441       C  
ATOM   5260  CG1 VAL B  65      49.210  55.901  45.793  1.00 67.75           C  
ANISOU 5260  CG1 VAL B  65     7264   6512  11966   1034   -944   -414       C  
ATOM   5261  CG2 VAL B  65      51.551  56.121  46.633  1.00 69.13           C  
ANISOU 5261  CG2 VAL B  65     7504   6701  12062    899   -842   -478       C  
ATOM   5262  N   LEU B  66      49.098  52.478  44.932  1.00 73.30           N  
ANISOU 5262  N   LEU B  66     7797   7518  12536   1076  -1019   -676       N  
ATOM   5263  CA  LEU B  66      48.033  51.842  44.173  1.00 75.41           C  
ANISOU 5263  CA  LEU B  66     7988   7852  12814   1136  -1092   -705       C  
ATOM   5264  C   LEU B  66      46.669  52.258  44.709  1.00 79.79           C  
ANISOU 5264  C   LEU B  66     8545   8274  13496   1199  -1101   -654       C  
ATOM   5265  O   LEU B  66      46.354  52.028  45.875  1.00 81.62           O  
ANISOU 5265  O   LEU B  66     8780   8395  13837   1215  -1061   -691       O  
ATOM   5266  CB  LEU B  66      48.175  50.320  44.230  1.00 79.64           C  
ANISOU 5266  CB  LEU B  66     8440   8442  13378   1145  -1116   -860       C  
ATOM   5267  CG  LEU B  66      47.044  49.499  43.607  1.00 75.03           C  
ANISOU 5267  CG  LEU B  66     7759   7904  12845   1205  -1194   -927       C  
ATOM   5268  CD1 LEU B  66      46.948  49.755  42.110  1.00 71.65           C  
ANISOU 5268  CD1 LEU B  66     7289   7664  12269   1214  -1257   -911       C  
ATOM   5269  CD2 LEU B  66      47.247  48.021  43.888  1.00 68.05           C  
ANISOU 5269  CD2 LEU B  66     6788   7015  12052   1208  -1216  -1078       C  
ATOM   5270  N   ILE B  67      45.868  52.876  43.849  1.00 84.76           N  
ANISOU 5270  N   ILE B  67     9163   8936  14105   1237  -1153   -562       N  
ATOM   5271  CA  ILE B  67      44.516  53.286  44.203  1.00 83.90           C  
ANISOU 5271  CA  ILE B  67     9046   8719  14114   1306  -1171   -516       C  
ATOM   5272  C   ILE B  67      43.537  52.722  43.183  1.00 80.16           C  
ANISOU 5272  C   ILE B  67     8487   8359  13612   1358  -1255   -531       C  
ATOM   5273  O   ILE B  67      43.321  53.315  42.127  1.00 73.77           O  
ANISOU 5273  O   ILE B  67     7665   7645  12720   1369  -1304   -432       O  
ATOM   5274  CB  ILE B  67      44.386  54.818  44.230  1.00 90.08           C  
ANISOU 5274  CB  ILE B  67     9894   9397  14937   1311  -1160   -372       C  
ATOM   5275  CG1 ILE B  67      45.386  55.422  45.216  1.00 90.44           C  
ANISOU 5275  CG1 ILE B  67    10014   9333  15018   1256  -1082   -381       C  
ATOM   5276  CG2 ILE B  67      42.968  55.226  44.591  1.00 97.77           C  
ANISOU 5276  CG2 ILE B  67    10847  10262  16041   1393  -1182   -343       C  
ATOM   5277  CD1 ILE B  67      45.335  56.930  45.287  1.00 96.11           C  
ANISOU 5277  CD1 ILE B  67    10785   9916  15819   1257  -1076   -260       C  
ATOM   5278  N   ALA B  68      42.948  51.572  43.500  1.00 83.88           N  
ANISOU 5278  N   ALA B  68     8885   8828  14156   1386  -1274   -647       N  
ATOM   5279  CA  ALA B  68      42.088  50.873  42.550  1.00 87.74           C  
ANISOU 5279  CA  ALA B  68     9276   9432  14628   1429  -1357   -701       C  
ATOM   5280  C   ALA B  68      40.833  50.290  43.194  1.00 90.53           C  
ANISOU 5280  C   ALA B  68     9569   9692  15135   1481  -1373   -746       C  
ATOM   5281  O   ALA B  68      40.840  49.912  44.365  1.00 95.05           O  
ANISOU 5281  O   ALA B  68    10147  10151  15815   1470  -1322   -776       O  
ATOM   5282  CB  ALA B  68      42.873  49.779  41.840  1.00 86.43           C  
ANISOU 5282  CB  ALA B  68     9042   9417  14381   1396  -1390   -839       C  
ATOM   5283  N   LEU B  69      39.758  50.223  42.414  1.00 86.04           N  
ANISOU 5283  N   LEU B  69     8932   9193  14567   1534  -1445   -740       N  
ATOM   5284  CA  LEU B  69      38.514  49.593  42.847  1.00 80.69           C  
ANISOU 5284  CA  LEU B  69     8177   8454  14029   1580  -1471   -786       C  
ATOM   5285  C   LEU B  69      37.926  50.239  44.097  1.00 87.57           C  
ANISOU 5285  C   LEU B  69     9093   9169  15011   1605  -1410   -711       C  
ATOM   5286  O   LEU B  69      37.491  49.545  45.016  1.00 90.59           O  
ANISOU 5286  O   LEU B  69     9427   9482  15512   1606  -1388   -754       O  
ATOM   5287  CB  LEU B  69      38.729  48.097  43.076  1.00 72.86           C  
ANISOU 5287  CB  LEU B  69     7097   7462  13123   1551  -1489   -934       C  
ATOM   5288  CG  LEU B  69      39.432  47.393  41.915  1.00 75.94           C  
ANISOU 5288  CG  LEU B  69     7427   8012  13414   1529  -1547  -1057       C  
ATOM   5289  CD1 LEU B  69      39.613  45.910  42.194  1.00 71.75           C  
ANISOU 5289  CD1 LEU B  69     6798   7441  13023   1507  -1574  -1213       C  
ATOM   5290  CD2 LEU B  69      38.661  47.615  40.623  1.00 81.04           C  
ANISOU 5290  CD2 LEU B  69     8006   8820  13964   1575  -1630  -1063       C  
ATOM   5291  N   ASN B  70      37.911  51.568  44.120  1.00 90.94           N  
ANISOU 5291  N   ASN B  70     9597   9547  15408   1626  -1387   -598       N  
ATOM   5292  CA  ASN B  70      37.336  52.318  45.231  1.00 92.34           C  
ANISOU 5292  CA  ASN B  70     9804   9590  15689   1662  -1335   -553       C  
ATOM   5293  C   ASN B  70      36.070  53.054  44.817  1.00 94.20           C  
ANISOU 5293  C   ASN B  70    10011   9810  15971   1743  -1385   -481       C  
ATOM   5294  O   ASN B  70      36.067  53.787  43.828  1.00 93.13           O  
ANISOU 5294  O   ASN B  70     9896   9717  15771   1761  -1432   -388       O  
ATOM   5295  CB  ASN B  70      38.350  53.324  45.776  1.00 94.49           C  
ANISOU 5295  CB  ASN B  70    10180   9782  15942   1627  -1268   -507       C  
ATOM   5296  CG  ASN B  70      39.555  52.658  46.402  1.00 95.27           C  
ANISOU 5296  CG  ASN B  70    10303   9890  16005   1554  -1210   -577       C  
ATOM   5297  ND2 ASN B  70      40.740  52.989  45.903  1.00 93.74           N  
ANISOU 5297  ND2 ASN B  70    10173   9733  15713   1499  -1199   -553       N  
ATOM   5298  OD1 ASN B  70      39.424  51.862  47.330  1.00 97.11           O  
ANISOU 5298  OD1 ASN B  70    10491  10107  16300   1544  -1177   -639       O  
ATOM   5299  N   THR B  71      34.995  52.859  45.574  1.00 95.98           N  
ANISOU 5299  N   THR B  71    10177   9985  16305   1791  -1376   -509       N  
ATOM   5300  CA  THR B  71      33.753  53.576  45.315  1.00 93.33           C  
ANISOU 5300  CA  THR B  71     9808   9625  16029   1875  -1419   -450       C  
ATOM   5301  C   THR B  71      33.686  54.824  46.183  1.00 93.18           C  
ANISOU 5301  C   THR B  71     9840   9472  16090   1913  -1366   -414       C  
ATOM   5302  O   THR B  71      32.842  55.690  45.972  1.00 97.56           O  
ANISOU 5302  O   THR B  71    10381   9977  16712   1988  -1401   -354       O  
ATOM   5303  CB  THR B  71      32.514  52.705  45.581  1.00 92.84           C  
ANISOU 5303  CB  THR B  71     9633   9596  16045   1912  -1445   -507       C  
ATOM   5304  CG2 THR B  71      32.665  51.342  44.921  1.00 94.59           C  
ANISOU 5304  CG2 THR B  71     9788   9922  16231   1867  -1494   -582       C  
ATOM   5305  OG1 THR B  71      32.338  52.538  46.993  1.00 93.27           O  
ANISOU 5305  OG1 THR B  71     9665   9590  16182   1908  -1371   -550       O  
ATOM   5306  N   VAL B  72      34.582  54.907  47.162  1.00 95.25           N  
ANISOU 5306  N   VAL B  72    10153   9681  16356   1864  -1287   -461       N  
ATOM   5307  CA  VAL B  72      34.669  56.081  48.021  1.00 97.45           C  
ANISOU 5307  CA  VAL B  72    10472   9840  16715   1894  -1237   -466       C  
ATOM   5308  C   VAL B  72      34.813  57.322  47.153  1.00 92.94           C  
ANISOU 5308  C   VAL B  72     9957   9188  16168   1920  -1284   -354       C  
ATOM   5309  O   VAL B  72      35.311  57.246  46.031  1.00 92.82           O  
ANISOU 5309  O   VAL B  72     9970   9236  16061   1883  -1331   -268       O  
ATOM   5310  CB  VAL B  72      35.865  55.989  48.986  1.00102.34           C  
ANISOU 5310  CB  VAL B  72    11140  10443  17303   1823  -1153   -532       C  
ATOM   5311  CG1 VAL B  72      37.172  56.161  48.229  1.00102.17           C  
ANISOU 5311  CG1 VAL B  72    11204  10425  17191   1750  -1159   -479       C  
ATOM   5312  CG2 VAL B  72      35.743  57.030  50.086  1.00107.04           C  
ANISOU 5312  CG2 VAL B  72    11736  10941  17992   1864  -1098   -590       C  
ATOM   5313  N   GLU B  73      34.381  58.465  47.668  1.00 95.10           N  
ANISOU 5313  N   GLU B  73    10232   9331  16573   1982  -1275   -353       N  
ATOM   5314  CA  GLU B  73      34.330  59.672  46.854  1.00104.43           C  
ANISOU 5314  CA  GLU B  73    11444  10409  17826   2017  -1334   -220       C  
ATOM   5315  C   GLU B  73      35.605  60.513  46.923  1.00109.05           C  
ANISOU 5315  C   GLU B  73    12113  10889  18433   1952  -1304   -181       C  
ATOM   5316  O   GLU B  73      36.067  61.023  45.903  1.00113.80           O  
ANISOU 5316  O   GLU B  73    12749  11481  19008   1923  -1353    -27       O  
ATOM   5317  CB  GLU B  73      33.109  60.513  47.221  1.00110.92           C  
ANISOU 5317  CB  GLU B  73    12206  11119  18818   2130  -1361   -233       C  
ATOM   5318  CG  GLU B  73      32.721  61.524  46.161  1.00121.19           C  
ANISOU 5318  CG  GLU B  73    13506  12336  20203   2181  -1449    -58       C  
ATOM   5319  CD  GLU B  73      31.321  62.060  46.361  1.00130.45           C  
ANISOU 5319  CD  GLU B  73    14598  13436  21530   2304  -1490    -73       C  
ATOM   5320  OE1 GLU B  73      30.568  61.462  47.158  1.00130.98           O  
ANISOU 5320  OE1 GLU B  73    14602  13564  21599   2344  -1455   -212       O  
ATOM   5321  OE2 GLU B  73      30.974  63.075  45.722  1.00134.93           O1-
ANISOU 5321  OE2 GLU B  73    15155  13891  22221   2360  -1561     66       O1-
ATOM   5322  N   ARG B  74      36.171  60.657  48.117  1.00107.61           N  
ANISOU 5322  N   ARG B  74    11950  10645  18291   1927  -1226   -312       N  
ATOM   5323  CA  ARG B  74      37.360  61.488  48.284  1.00107.63           C  
ANISOU 5323  CA  ARG B  74    12023  10538  18335   1865  -1197   -296       C  
ATOM   5324  C   ARG B  74      38.487  60.783  49.030  1.00107.84           C  
ANISOU 5324  C   ARG B  74    12085  10644  18246   1776  -1115   -405       C  
ATOM   5325  O   ARG B  74      38.267  60.182  50.082  1.00112.73           O  
ANISOU 5325  O   ARG B  74    12663  11326  18846   1788  -1059   -542       O  
ATOM   5326  CB  ARG B  74      37.012  62.790  49.006  1.00116.76           C  
ANISOU 5326  CB  ARG B  74    13157  11495  19710   1931  -1193   -357       C  
ATOM   5327  CG  ARG B  74      38.186  63.747  49.117  1.00131.46           C  
ANISOU 5327  CG  ARG B  74    15079  13214  21655   1866  -1176   -338       C  
ATOM   5328  CD  ARG B  74      38.004  64.725  50.261  1.00143.15           C  
ANISOU 5328  CD  ARG B  74    16521  14530  23341   1921  -1147   -504       C  
ATOM   5329  NE  ARG B  74      36.794  65.526  50.110  1.00158.46           N  
ANISOU 5329  NE  ARG B  74    18395  16334  25478   2037  -1211   -483       N  
ATOM   5330  CZ  ARG B  74      36.391  66.434  50.991  1.00171.50           C  
ANISOU 5330  CZ  ARG B  74    19986  17835  27340   2112  -1204   -641       C  
ATOM   5331  NH1 ARG B  74      37.105  66.655  52.087  1.00176.87           N1+
ANISOU 5331  NH1 ARG B  74    20661  18498  28045   2079  -1134   -837       N1+
ATOM   5332  NH2 ARG B  74      35.277  67.121  50.778  1.00173.20           N  
ANISOU 5332  NH2 ARG B  74    20136  17928  27743   2224  -1271   -616       N  
ATOM   5333  N   ILE B  75      39.694  60.871  48.479  1.00100.00           N  
ANISOU 5333  N   ILE B  75    11158   9662  17174   1688  -1111   -331       N  
ATOM   5334  CA  ILE B  75      40.886  60.330  49.122  1.00 87.51           C  
ANISOU 5334  CA  ILE B  75     9613   8144  15493   1602  -1039   -422       C  
ATOM   5335  C   ILE B  75      41.875  61.457  49.403  1.00 88.14           C  
ANISOU 5335  C   ILE B  75     9744   8087  15658   1553  -1014   -420       C  
ATOM   5336  O   ILE B  75      42.465  62.015  48.480  1.00 97.60           O  
ANISOU 5336  O   ILE B  75    10983   9244  16855   1505  -1051   -277       O  
ATOM   5337  CB  ILE B  75      41.563  59.263  48.249  1.00 84.48           C  
ANISOU 5337  CB  ILE B  75     9249   7922  14927   1533  -1053   -365       C  
ATOM   5338  CG1 ILE B  75      40.588  58.123  47.951  1.00 73.00           C  
ANISOU 5338  CG1 ILE B  75     7731   6588  13418   1579  -1086   -385       C  
ATOM   5339  CG2 ILE B  75      42.809  58.729  48.934  1.00 92.88           C  
ANISOU 5339  CG2 ILE B  75    10345   9042  15903   1451   -982   -456       C  
ATOM   5340  CD1 ILE B  75      41.183  57.020  47.108  1.00 66.18           C  
ANISOU 5340  CD1 ILE B  75     6865   5880  12400   1522  -1108   -371       C  
ATOM   5341  N   PRO B  76      42.054  61.795  50.688  1.00 79.69           N  
ANISOU 5341  N   PRO B  76     8657   6959  14662   1561   -952   -579       N  
ATOM   5342  CA  PRO B  76      42.818  62.967  51.131  1.00 80.54           C  
ANISOU 5342  CA  PRO B  76     8791   6911  14900   1528   -932   -623       C  
ATOM   5343  C   PRO B  76      44.332  62.763  51.206  1.00 82.32           C  
ANISOU 5343  C   PRO B  76     9074   7190  15016   1414   -884   -630       C  
ATOM   5344  O   PRO B  76      44.927  63.099  52.229  1.00 84.12           O  
ANISOU 5344  O   PRO B  76     9294   7387  15281   1389   -828   -775       O  
ATOM   5345  CB  PRO B  76      42.274  63.224  52.546  1.00 65.08           C  
ANISOU 5345  CB  PRO B  76     6763   4930  13035   1594   -883   -834       C  
ATOM   5346  CG  PRO B  76      41.125  62.265  52.734  1.00 80.00           C  
ANISOU 5346  CG  PRO B  76     8590   6956  14850   1663   -884   -859       C  
ATOM   5347  CD  PRO B  76      41.394  61.127  51.817  1.00 75.63           C  
ANISOU 5347  CD  PRO B  76     8075   6536  14126   1610   -904   -731       C  
ATOM   5348  N   LEU B  77      44.947  62.236  50.152  1.00 80.85           N  
ANISOU 5348  N   LEU B  77     8932   7098  14691   1348   -907   -490       N  
ATOM   5349  CA  LEU B  77      46.403  62.136  50.111  1.00 83.19           C  
ANISOU 5349  CA  LEU B  77     9277   7443  14889   1240   -868   -485       C  
ATOM   5350  C   LEU B  77      47.004  63.498  49.795  1.00 93.38           C  
ANISOU 5350  C   LEU B  77    10597   8558  16326   1193   -890   -397       C  
ATOM   5351  O   LEU B  77      47.768  63.645  48.842  1.00 99.44           O  
ANISOU 5351  O   LEU B  77    11397   9357  17028   1118   -913   -243       O  
ATOM   5352  CB  LEU B  77      46.854  61.114  49.067  1.00 78.33           C  
ANISOU 5352  CB  LEU B  77     8681   7007  14076   1191   -888   -384       C  
ATOM   5353  CG  LEU B  77      46.611  59.643  49.403  1.00 75.72           C  
ANISOU 5353  CG  LEU B  77     8318   6840  13615   1211   -865   -480       C  
ATOM   5354  CD1 LEU B  77      47.203  58.751  48.322  1.00 80.08           C  
ANISOU 5354  CD1 LEU B  77     8876   7551  13998   1160   -891   -411       C  
ATOM   5355  CD2 LEU B  77      47.192  59.300  50.766  1.00 63.16           C  
ANISOU 5355  CD2 LEU B  77     6717   5274  12007   1186   -786   -635       C  
ATOM   5356  N   GLU B  78      46.655  64.491  50.604  1.00 98.25           N  
ANISOU 5356  N   GLU B  78    11187   8995  17151   1237   -885   -499       N  
ATOM   5357  CA  GLU B  78      47.038  65.872  50.334  1.00110.12           C  
ANISOU 5357  CA  GLU B  78    12697  10278  18864   1205   -922   -416       C  
ATOM   5358  C   GLU B  78      48.458  66.210  50.776  1.00119.94           C  
ANISOU 5358  C   GLU B  78    13970  11496  20106   1097   -872   -479       C  
ATOM   5359  O   GLU B  78      49.173  66.931  50.079  1.00129.49           O  
ANISOU 5359  O   GLU B  78    15202  12610  21387   1019   -902   -324       O  
ATOM   5360  CB  GLU B  78      46.031  66.835  50.967  1.00113.66           C  
ANISOU 5360  CB  GLU B  78    13087  10522  19576   1306   -950   -520       C  
ATOM   5361  CG  GLU B  78      45.324  66.276  52.191  1.00113.99           C  
ANISOU 5361  CG  GLU B  78    13075  10658  19579   1388   -897   -762       C  
ATOM   5362  CD  GLU B  78      44.205  67.177  52.676  1.00114.99           C  
ANISOU 5362  CD  GLU B  78    13128  10612  19952   1503   -932   -866       C  
ATOM   5363  OE1 GLU B  78      44.419  68.404  52.744  1.00122.38           O  
ANISOU 5363  OE1 GLU B  78    14046  11316  21137   1501   -966   -884       O  
ATOM   5364  OE2 GLU B  78      43.114  66.661  52.993  1.00108.22           O1-
ANISOU 5364  OE2 GLU B  78    12221   9846  19053   1594   -930   -934       O1-
ATOM   5365  N   ASN B  79      48.866  65.689  51.928  1.00114.84           N  
ANISOU 5365  N   ASN B  79    13312  10948  19373   1088   -797   -695       N  
ATOM   5366  CA  ASN B  79      50.195  65.969  52.462  1.00103.80           C  
ANISOU 5366  CA  ASN B  79    11932   9545  17964    991   -747   -782       C  
ATOM   5367  C   ASN B  79      51.271  65.056  51.886  1.00 99.18           C  
ANISOU 5367  C   ASN B  79    11396   9149  17137    895   -719   -687       C  
ATOM   5368  O   ASN B  79      52.406  65.039  52.362  1.00104.73           O  
ANISOU 5368  O   ASN B  79    12112   9897  17783    815   -670   -767       O  
ATOM   5369  CB  ASN B  79      50.189  65.882  53.987  1.00 98.01           C  
ANISOU 5369  CB  ASN B  79    11144   8858  17239   1026   -682  -1058       C  
ATOM   5370  CG  ASN B  79      49.335  66.955  54.624  1.00 97.89           C  
ANISOU 5370  CG  ASN B  79    11061   8651  17481   1112   -707  -1198       C  
ATOM   5371  ND2 ASN B  79      49.265  66.948  55.950  1.00 97.91           N  
ANISOU 5371  ND2 ASN B  79    10994   8724  17483   1150   -652  -1453       N  
ATOM   5372  OD1 ASN B  79      48.744  67.782  53.932  1.00103.26           O  
ANISOU 5372  OD1 ASN B  79    11739   9135  18361   1148   -777  -1079       O  
ATOM   5373  N   LEU B  80      50.908  64.296  50.860  1.00 89.00           N  
ANISOU 5373  N   LEU B  80    10126   7982  15709    908   -754   -533       N  
ATOM   5374  CA  LEU B  80      51.855  63.428  50.180  1.00 78.47           C  
ANISOU 5374  CA  LEU B  80     8824   6836  14155    829   -739   -454       C  
ATOM   5375  C   LEU B  80      52.802  64.267  49.329  1.00 86.21           C  
ANISOU 5375  C   LEU B  80     9829   7758  15170    729   -762   -286       C  
ATOM   5376  O   LEU B  80      52.373  64.940  48.394  1.00 88.66           O  
ANISOU 5376  O   LEU B  80    10133   7986  15569    733   -826    -96       O  
ATOM   5377  CB  LEU B  80      51.111  62.424  49.303  1.00 74.03           C  
ANISOU 5377  CB  LEU B  80     8251   6422  13453    880   -778   -365       C  
ATOM   5378  CG  LEU B  80      51.958  61.337  48.646  1.00 76.89           C  
ANISOU 5378  CG  LEU B  80     8625   7002  13590    820   -767   -334       C  
ATOM   5379  CD1 LEU B  80      52.638  60.490  49.708  1.00 79.51           C  
ANISOU 5379  CD1 LEU B  80     8953   7423  13834    800   -697   -508       C  
ATOM   5380  CD2 LEU B  80      51.101  60.478  47.733  1.00 74.38           C  
ANISOU 5380  CD2 LEU B  80     8278   6810  13172    878   -819   -269       C  
ATOM   5381  N   GLN B  81      54.089  64.225  49.661  1.00 92.12           N  
ANISOU 5381  N   GLN B  81    10594   8558  15848    635   -712   -342       N  
ATOM   5382  CA  GLN B  81      55.094  65.036  48.976  1.00 89.54           C  
ANISOU 5382  CA  GLN B  81    10281   8183  15559    524   -726   -189       C  
ATOM   5383  C   GLN B  81      55.828  64.283  47.872  1.00 88.69           C  
ANISOU 5383  C   GLN B  81    10180   8309  15210    458   -730    -54       C  
ATOM   5384  O   GLN B  81      56.044  64.816  46.785  1.00 88.58           O  
ANISOU 5384  O   GLN B  81    10155   8308  15193    403   -774    165       O  
ATOM   5385  CB  GLN B  81      56.120  65.571  49.975  1.00 80.71           C  
ANISOU 5385  CB  GLN B  81     9163   6980  14522    453   -672   -336       C  
ATOM   5386  CG  GLN B  81      55.704  66.832  50.699  1.00 86.13           C  
ANISOU 5386  CG  GLN B  81     9824   7395  15507    479   -689   -419       C  
ATOM   5387  CD  GLN B  81      56.710  67.237  51.754  1.00 96.59           C  
ANISOU 5387  CD  GLN B  81    11135   8672  16892    413   -634   -609       C  
ATOM   5388  NE2 GLN B  81      57.128  68.497  51.722  1.00101.99           N  
ANISOU 5388  NE2 GLN B  81    11799   9134  17818    349   -662   -569       N  
ATOM   5389  OE1 GLN B  81      57.108  66.426  52.589  1.00 98.57           O  
ANISOU 5389  OE1 GLN B  81    11383   9084  16983    418   -572   -785       O  
ATOM   5390  N   ILE B  82      56.223  63.047  48.155  1.00 87.07           N  
ANISOU 5390  N   ILE B  82     9979   8298  14807    464   -686   -182       N  
ATOM   5391  CA  ILE B  82      57.052  62.300  47.221  1.00 89.35           C  
ANISOU 5391  CA  ILE B  82    10260   8816  14873    403   -685   -108       C  
ATOM   5392  C   ILE B  82      56.757  60.805  47.224  1.00 85.20           C  
ANISOU 5392  C   ILE B  82     9717   8474  14181    467   -678   -223       C  
ATOM   5393  O   ILE B  82      56.446  60.220  48.262  1.00 82.03           O  
ANISOU 5393  O   ILE B  82     9316   8047  13805    521   -646   -384       O  
ATOM   5394  CB  ILE B  82      58.550  62.511  47.520  1.00 98.69           C  
ANISOU 5394  CB  ILE B  82    11453  10040  16006    291   -633   -143       C  
ATOM   5395  CG1 ILE B  82      59.412  61.737  46.522  1.00106.40           C  
ANISOU 5395  CG1 ILE B  82    12407  11275  16745    234   -633    -79       C  
ATOM   5396  CG2 ILE B  82      58.874  62.093  48.946  1.00 94.93           C  
ANISOU 5396  CG2 ILE B  82    10985   9538  15544    308   -570   -372       C  
ATOM   5397  CD1 ILE B  82      60.892  61.817  46.812  1.00111.88           C  
ANISOU 5397  CD1 ILE B  82    13103  12035  17371    128   -580   -124       C  
ATOM   5398  N   ILE B  83      56.852  60.201  46.045  1.00 87.77           N  
ANISOU 5398  N   ILE B  83    10014   8992  14344    459   -714   -137       N  
ATOM   5399  CA  ILE B  83      56.781  58.755  45.905  1.00 89.62           C  
ANISOU 5399  CA  ILE B  83    10215   9403  14433    505   -716   -256       C  
ATOM   5400  C   ILE B  83      58.119  58.259  45.375  1.00 88.31           C  
ANISOU 5400  C   ILE B  83    10027   9437  14090    427   -694   -271       C  
ATOM   5401  O   ILE B  83      58.475  58.517  44.227  1.00 94.44           O  
ANISOU 5401  O   ILE B  83    10772  10355  14756    379   -723   -142       O  
ATOM   5402  CB  ILE B  83      55.661  58.330  44.940  1.00 91.86           C  
ANISOU 5402  CB  ILE B  83    10458   9768  14676    579   -784   -194       C  
ATOM   5403  CG1 ILE B  83      54.308  58.840  45.438  1.00 92.65           C  
ANISOU 5403  CG1 ILE B  83    10573   9676  14952    660   -806   -176       C  
ATOM   5404  CG2 ILE B  83      55.638  56.819  44.787  1.00 88.40           C  
ANISOU 5404  CG2 ILE B  83     9972   9495  14122    622   -793   -338       C  
ATOM   5405  CD1 ILE B  83      53.155  58.502  44.521  1.00 94.52           C  
ANISOU 5405  CD1 ILE B  83    10767   9987  15159    734   -876   -111       C  
ATOM   5406  N   ARG B  84      58.864  57.558  46.222  1.00 83.99           N  
ANISOU 5406  N   ARG B  84     9482   8918  13511    414   -645   -424       N  
ATOM   5407  CA  ARG B  84      60.205  57.105  45.869  1.00 83.64           C  
ANISOU 5407  CA  ARG B  84     9412   9051  13315    343   -620   -461       C  
ATOM   5408  C   ARG B  84      60.199  56.219  44.628  1.00 83.88           C  
ANISOU 5408  C   ARG B  84     9374   9313  13184    365   -667   -465       C  
ATOM   5409  O   ARG B  84      60.911  56.487  43.662  1.00 88.71           O  
ANISOU 5409  O   ARG B  84     9952  10093  13662    300   -675   -379       O  
ATOM   5410  CB  ARG B  84      60.848  56.368  47.047  1.00 78.93           C  
ANISOU 5410  CB  ARG B  84     8818   8443  12726    346   -568   -627       C  
ATOM   5411  CG  ARG B  84      61.135  57.254  48.248  1.00 77.93           C  
ANISOU 5411  CG  ARG B  84     8739   8152  12719    309   -516   -651       C  
ATOM   5412  CD  ARG B  84      62.496  57.920  48.130  1.00 86.59           C  
ANISOU 5412  CD  ARG B  84     9846   9294  13761    196   -480   -614       C  
ATOM   5413  NE  ARG B  84      62.591  59.142  48.926  1.00 88.94           N  
ANISOU 5413  NE  ARG B  84    10180   9407  14206    153   -451   -603       N  
ATOM   5414  CZ  ARG B  84      62.571  59.177  50.254  1.00 85.73           C  
ANISOU 5414  CZ  ARG B  84     9780   8913  13880    174   -411   -736       C  
ATOM   5415  NH1 ARG B  84      62.444  58.055  50.951  1.00 85.37           N1+
ANISOU 5415  NH1 ARG B  84     9709   8945  13782    234   -393   -854       N1+
ATOM   5416  NH2 ARG B  84      62.667  60.338  50.886  1.00 81.24           N  
ANISOU 5416  NH2 ARG B  84     9229   8185  13453    134   -392   -750       N  
ATOM   5417  N   GLY B  85      59.394  55.164  44.658  1.00 77.68           N  
ANISOU 5417  N   GLY B  85     8554   8547  12414    454   -699   -571       N  
ATOM   5418  CA  GLY B  85      59.324  54.239  43.543  1.00 82.34           C  
ANISOU 5418  CA  GLY B  85     9061   9351  12872    486   -750   -625       C  
ATOM   5419  C   GLY B  85      60.298  53.085  43.681  1.00 87.94           C  
ANISOU 5419  C   GLY B  85     9719  10187  13510    482   -735   -796       C  
ATOM   5420  O   GLY B  85      60.728  52.501  42.686  1.00 88.47           O  
ANISOU 5420  O   GLY B  85     9704  10473  13436    481   -766   -855       O  
ATOM   5421  N   ASN B  86      60.648  52.755  44.920  1.00 88.61           N  
ANISOU 5421  N   ASN B  86     9834  10144  13688    484   -690   -879       N  
ATOM   5422  CA  ASN B  86      61.545  51.638  45.188  1.00 87.60           C  
ANISOU 5422  CA  ASN B  86     9651  10104  13528    488   -680  -1030       C  
ATOM   5423  C   ASN B  86      61.026  50.351  44.563  1.00 89.06           C  
ANISOU 5423  C   ASN B  86     9742  10375  13720    566   -746  -1157       C  
ATOM   5424  O   ASN B  86      61.796  49.446  44.246  1.00 95.58           O  
ANISOU 5424  O   ASN B  86    10492  11330  14495    572   -760  -1289       O  
ATOM   5425  CB  ASN B  86      61.734  51.454  46.692  1.00 91.50           C  
ANISOU 5425  CB  ASN B  86    10182  10444  14140    492   -631  -1073       C  
ATOM   5426  CG  ASN B  86      62.453  52.622  47.333  1.00 92.82           C  
ANISOU 5426  CG  ASN B  86    10420  10550  14297    412   -567   -999       C  
ATOM   5427  ND2 ASN B  86      62.744  52.502  48.624  1.00 95.60           N  
ANISOU 5427  ND2 ASN B  86    10788  10816  14718    409   -522  -1048       N  
ATOM   5428  OD1 ASN B  86      62.748  53.621  46.675  1.00 87.65           O  
ANISOU 5428  OD1 ASN B  86     9795   9931  13578    349   -561   -896       O  
ATOM   5429  N   MET B  87      59.710  50.281  44.398  1.00 89.26           N  
ANISOU 5429  N   MET B  87     9764  10324  13827    628   -790  -1129       N  
ATOM   5430  CA  MET B  87      59.069  49.178  43.695  1.00 95.85           C  
ANISOU 5430  CA  MET B  87    10501  11235  14683    700   -862  -1249       C  
ATOM   5431  C   MET B  87      58.024  49.736  42.740  1.00 93.57           C  
ANISOU 5431  C   MET B  87    10206  11001  14345    724   -909  -1160       C  
ATOM   5432  O   MET B  87      57.515  50.837  42.944  1.00 97.03           O  
ANISOU 5432  O   MET B  87    10723  11339  14805    706   -888  -1003       O  
ATOM   5433  CB  MET B  87      58.408  48.214  44.683  1.00102.17           C  
ANISOU 5433  CB  MET B  87    11278  11864  15678    761   -876  -1322       C  
ATOM   5434  CG  MET B  87      59.382  47.399  45.518  1.00105.49           C  
ANISOU 5434  CG  MET B  87    11669  12255  16159    751   -850  -1413       C  
ATOM   5435  SD  MET B  87      58.538  46.153  46.512  1.00157.76           S  
ANISOU 5435  SD  MET B  87    18225  18699  23019    820   -883  -1462       S  
ATOM   5436  CE  MET B  87      57.645  45.258  45.243  1.00120.83           C  
ANISOU 5436  CE  MET B  87    13436  14089  18386    887   -986  -1589       C  
ATOM   5437  N   TYR B  88      57.707  48.982  41.693  1.00 91.06           N  
ANISOU 5437  N   TYR B  88     9783  10847  13967    769   -977  -1270       N  
ATOM   5438  CA  TYR B  88      56.684  49.405  40.747  1.00 92.83           C  
ANISOU 5438  CA  TYR B  88     9982  11157  14133    798  -1029  -1193       C  
ATOM   5439  C   TYR B  88      55.473  48.485  40.795  1.00 93.70           C  
ANISOU 5439  C   TYR B  88    10032  11185  14386    883  -1091  -1300       C  
ATOM   5440  O   TYR B  88      55.594  47.297  41.091  1.00 99.71           O  
ANISOU 5440  O   TYR B  88    10724  11909  15253    918  -1115  -1473       O  
ATOM   5441  CB  TYR B  88      57.231  49.436  39.317  1.00 96.46           C  
ANISOU 5441  CB  TYR B  88    10346  11937  14366    776  -1062  -1220       C  
ATOM   5442  CG  TYR B  88      58.486  50.254  39.136  1.00100.60           C  
ANISOU 5442  CG  TYR B  88    10905  12581  14738    683  -1006  -1113       C  
ATOM   5443  CD1 TYR B  88      59.450  49.879  38.210  1.00103.33           C  
ANISOU 5443  CD1 TYR B  88    11146  13224  14892    656  -1017  -1211       C  
ATOM   5444  CD2 TYR B  88      58.713  51.394  39.892  1.00106.31           C  
ANISOU 5444  CD2 TYR B  88    11750  13127  15517    622   -945   -926       C  
ATOM   5445  CE1 TYR B  88      60.600  50.620  38.037  1.00107.00           C  
ANISOU 5445  CE1 TYR B  88    11630  13809  15215    565   -965  -1102       C  
ATOM   5446  CE2 TYR B  88      59.862  52.141  39.727  1.00111.11           C  
ANISOU 5446  CE2 TYR B  88    12379  13832  16005    530   -898   -825       C  
ATOM   5447  CZ  TYR B  88      60.801  51.749  38.797  1.00112.14           C  
ANISOU 5447  CZ  TYR B  88    12408  14262  15937    498   -906   -902       C  
ATOM   5448  OH  TYR B  88      61.949  52.486  38.626  1.00118.53           O  
ANISOU 5448  OH  TYR B  88    13229  15181  16626    399   -858   -791       O  
ATOM   5449  N   TYR B  89      54.304  49.045  40.504  1.00 86.93           N  
ANISOU 5449  N   TYR B  89     9192  10291  13547    915  -1121  -1191       N  
ATOM   5450  CA  TYR B  89      53.105  48.245  40.317  1.00 92.59           C  
ANISOU 5450  CA  TYR B  89     9834  10973  14373    991  -1189  -1287       C  
ATOM   5451  C   TYR B  89      53.013  47.843  38.848  1.00107.66           C  
ANISOU 5451  C   TYR B  89    11615  13165  16125   1014  -1262  -1391       C  
ATOM   5452  O   TYR B  89      53.024  48.698  37.961  1.00112.49           O  
ANISOU 5452  O   TYR B  89    12224  13956  16560    991  -1270  -1264       O  
ATOM   5453  CB  TYR B  89      51.863  49.028  40.746  1.00 88.81           C  
ANISOU 5453  CB  TYR B  89     9426  10328  13990   1019  -1187  -1130       C  
ATOM   5454  CG  TYR B  89      50.561  48.313  40.473  1.00 84.58           C  
ANISOU 5454  CG  TYR B  89     8810   9773  13553   1093  -1258  -1210       C  
ATOM   5455  CD1 TYR B  89      50.109  47.308  41.316  1.00 84.60           C  
ANISOU 5455  CD1 TYR B  89     8778   9613  13753   1126  -1267  -1315       C  
ATOM   5456  CD2 TYR B  89      49.783  48.645  39.374  1.00 84.67           C  
ANISOU 5456  CD2 TYR B  89     8768   9937  13466   1124  -1318  -1167       C  
ATOM   5457  CE1 TYR B  89      48.921  46.651  41.069  1.00 87.46           C  
ANISOU 5457  CE1 TYR B  89     9058   9950  14221   1185  -1334  -1386       C  
ATOM   5458  CE2 TYR B  89      48.594  47.994  39.120  1.00 91.34           C  
ANISOU 5458  CE2 TYR B  89     9533  10771  14403   1189  -1385  -1250       C  
ATOM   5459  CZ  TYR B  89      48.167  46.997  39.970  1.00 94.47           C  
ANISOU 5459  CZ  TYR B  89     9899  10989  15007   1217  -1393  -1364       C  
ATOM   5460  OH  TYR B  89      46.982  46.345  39.721  1.00101.38           O  
ANISOU 5460  OH  TYR B  89    10686  11846  15989   1274  -1462  -1445       O  
ATOM   5461  N   GLU B  90      52.939  46.540  38.597  1.00112.12           N  
ANISOU 5461  N   GLU B  90    12062  13778  16763   1060  -1318  -1622       N  
ATOM   5462  CA  GLU B  90      52.947  46.011  37.236  1.00119.40           C  
ANISOU 5462  CA  GLU B  90    12833  14995  17537   1088  -1391  -1785       C  
ATOM   5463  C   GLU B  90      54.280  46.274  36.539  1.00120.35           C  
ANISOU 5463  C   GLU B  90    12919  15382  17428   1035  -1364  -1808       C  
ATOM   5464  O   GLU B  90      54.364  46.256  35.311  1.00118.56           O  
ANISOU 5464  O   GLU B  90    12576  15472  16999   1043  -1409  -1875       O  
ATOM   5465  CB  GLU B  90      51.794  46.590  36.412  1.00124.34           C  
ANISOU 5465  CB  GLU B  90    13431  15738  18074   1119  -1440  -1681       C  
ATOM   5466  CG  GLU B  90      50.407  46.254  36.942  1.00128.53           C  
ANISOU 5466  CG  GLU B  90    13969  16049  18818   1177  -1476  -1683       C  
ATOM   5467  CD  GLU B  90      50.182  44.762  37.108  1.00130.74           C  
ANISOU 5467  CD  GLU B  90    14133  16253  19289   1224  -1534  -1947       C  
ATOM   5468  OE1 GLU B  90      50.810  44.157  38.002  1.00130.60           O  
ANISOU 5468  OE1 GLU B  90    14137  16063  19423   1209  -1502  -2012       O  
ATOM   5469  OE2 GLU B  90      49.362  44.198  36.352  1.00130.26           O1-
ANISOU 5469  OE2 GLU B  90    13949  16301  19242   1275  -1615  -2083       O1-
ATOM   5470  N   ASN B  91      55.317  46.522  37.332  1.00126.63           N  
ANISOU 5470  N   ASN B  91    13802  16070  18242    981  -1291  -1753       N  
ATOM   5471  CA  ASN B  91      56.667  46.700  36.805  1.00134.59           C  
ANISOU 5471  CA  ASN B  91    14774  17313  19051    926  -1260  -1782       C  
ATOM   5472  C   ASN B  91      56.796  47.871  35.834  1.00132.38           C  
ANISOU 5472  C   ASN B  91    14495  17287  18517    873  -1250  -1582       C  
ATOM   5473  O   ASN B  91      57.533  47.787  34.851  1.00130.80           O  
ANISOU 5473  O   ASN B  91    14185  17414  18098    851  -1262  -1651       O  
ATOM   5474  CB  ASN B  91      57.142  45.414  36.126  1.00140.86           C  
ANISOU 5474  CB  ASN B  91    15396  18305  19821    971  -1319  -2095       C  
ATOM   5475  CG  ASN B  91      56.967  44.194  37.005  1.00145.03           C  
ANISOU 5475  CG  ASN B  91    15897  18572  20635   1025  -1345  -2279       C  
ATOM   5476  ND2 ASN B  91      56.579  43.079  36.398  1.00146.77           N  
ANISOU 5476  ND2 ASN B  91    15960  18874  20934   1093  -1431  -2538       N  
ATOM   5477  OD1 ASN B  91      57.180  44.252  38.216  1.00145.86           O  
ANISOU 5477  OD1 ASN B  91    16110  18413  20897   1003  -1292  -2187       O  
ATOM   5478  N   SER B  92      56.089  48.962  36.111  1.00129.49           N  
ANISOU 5478  N   SER B  92    14239  16776  18185    854  -1230  -1327       N  
ATOM   5479  CA  SER B  92      56.117  50.120  35.225  1.00127.38           C  
ANISOU 5479  CA  SER B  92    13967  16715  17718    803  -1229  -1091       C  
ATOM   5480  C   SER B  92      55.749  51.423  35.927  1.00121.73           C  
ANISOU 5480  C   SER B  92    13402  15740  17111    763  -1186   -807       C  
ATOM   5481  O   SER B  92      56.251  52.488  35.570  1.00127.04           O  
ANISOU 5481  O   SER B  92    14100  16496  17672    690  -1160   -587       O  
ATOM   5482  CB  SER B  92      55.181  49.901  34.035  1.00131.83           C  
ANISOU 5482  CB  SER B  92    14400  17532  18157    859  -1313  -1124       C  
ATOM   5483  OG  SER B  92      55.551  48.748  33.301  1.00136.36           O  
ANISOU 5483  OG  SER B  92    14812  18375  18625    896  -1359  -1414       O  
ATOM   5484  N   TYR B  93      54.874  51.340  36.923  1.00109.70           N  
ANISOU 5484  N   TYR B  93    11963  13904  15813    812  -1181   -816       N  
ATOM   5485  CA  TYR B  93      54.336  52.543  37.546  1.00 96.77           C  
ANISOU 5485  CA  TYR B  93    10446  12026  14297    794  -1153   -585       C  
ATOM   5486  C   TYR B  93      54.632  52.645  39.038  1.00 81.28           C  
ANISOU 5486  C   TYR B  93     8601   9758  12525    778  -1084   -609       C  
ATOM   5487  O   TYR B  93      54.685  51.641  39.745  1.00 82.00           O  
ANISOU 5487  O   TYR B  93     8684   9758  12714    812  -1075   -791       O  
ATOM   5488  CB  TYR B  93      52.827  52.625  37.312  1.00 96.08           C  
ANISOU 5488  CB  TYR B  93    10340  11877  14288    871  -1212   -535       C  
ATOM   5489  CG  TYR B  93      52.423  52.344  35.886  1.00 98.36           C  
ANISOU 5489  CG  TYR B  93    10493  12491  14389    900  -1288   -549       C  
ATOM   5490  CD1 TYR B  93      51.854  51.129  35.534  1.00 99.45           C  
ANISOU 5490  CD1 TYR B  93    10526  12730  14531    971  -1346   -782       C  
ATOM   5491  CD2 TYR B  93      52.621  53.289  34.890  1.00105.95           C  
ANISOU 5491  CD2 TYR B  93    11414  13669  15171    854  -1305   -327       C  
ATOM   5492  CE1 TYR B  93      51.485  50.865  34.230  1.00105.56           C  
ANISOU 5492  CE1 TYR B  93    11158  13828  15122   1000  -1417   -824       C  
ATOM   5493  CE2 TYR B  93      52.256  53.034  33.582  1.00112.80           C  
ANISOU 5493  CE2 TYR B  93    12139  14882  15839    880  -1374   -336       C  
ATOM   5494  CZ  TYR B  93      51.688  51.821  33.258  1.00110.21           C  
ANISOU 5494  CZ  TYR B  93    11706  14663  15503    956  -1430   -600       C  
ATOM   5495  OH  TYR B  93      51.323  51.561  31.958  1.00110.57           O  
ANISOU 5495  OH  TYR B  93    11594  15077  15340    986  -1501   -637       O  
ATOM   5496  N   ALA B  94      54.824  53.873  39.506  1.00 68.13           N  
ANISOU 5496  N   ALA B  94     7029   7941  10917    726  -1041   -422       N  
ATOM   5497  CA  ALA B  94      54.988  54.135  40.927  1.00 70.64           C  
ANISOU 5497  CA  ALA B  94     7446   7986  11407    715   -979   -442       C  
ATOM   5498  C   ALA B  94      53.691  54.707  41.480  1.00 75.46           C  
ANISOU 5498  C   ALA B  94     8107   8376  12190    773   -993   -363       C  
ATOM   5499  O   ALA B  94      53.534  54.869  42.690  1.00 80.74           O  
ANISOU 5499  O   ALA B  94     8838   8833  13007    785   -949   -400       O  
ATOM   5500  CB  ALA B  94      56.136  55.098  41.161  1.00 71.10           C  
ANISOU 5500  CB  ALA B  94     7563   8017  11437    618   -923   -330       C  
ATOM   5501  N   LEU B  95      52.765  55.016  40.577  1.00 71.10           N  
ANISOU 5501  N   LEU B  95     7513   7897  11606    813  -1055   -258       N  
ATOM   5502  CA  LEU B  95      51.458  55.545  40.951  1.00 73.39           C  
ANISOU 5502  CA  LEU B  95     7833   8001  12051    878  -1079   -184       C  
ATOM   5503  C   LEU B  95      50.385  55.045  39.991  1.00 75.84           C  
ANISOU 5503  C   LEU B  95     8057   8455  12303    948  -1157   -190       C  
ATOM   5504  O   LEU B  95      50.370  55.412  38.817  1.00 84.07           O  
ANISOU 5504  O   LEU B  95     9042   9692  13208    934  -1203    -66       O  
ATOM   5505  CB  LEU B  95      51.478  57.074  40.959  1.00 77.80           C  
ANISOU 5505  CB  LEU B  95     8447   8427  12686    840  -1071     35       C  
ATOM   5506  CG  LEU B  95      50.134  57.758  41.225  1.00 80.42           C  
ANISOU 5506  CG  LEU B  95     8796   8571  13186    914  -1104    122       C  
ATOM   5507  CD1 LEU B  95      49.577  57.333  42.575  1.00 80.74           C  
ANISOU 5507  CD1 LEU B  95     8874   8420  13382    969  -1065    -40       C  
ATOM   5508  CD2 LEU B  95      50.265  59.271  41.147  1.00 76.50           C  
ANISOU 5508  CD2 LEU B  95     8339   7933  12795    873  -1107    338       C  
ATOM   5509  N   ALA B  96      49.485  54.208  40.494  1.00 70.53           N  
ANISOU 5509  N   ALA B  96     7364   7702  11733   1020  -1173   -327       N  
ATOM   5510  CA  ALA B  96      48.437  53.634  39.662  1.00 76.36           C  
ANISOU 5510  CA  ALA B  96     8012   8568  12434   1087  -1249   -365       C  
ATOM   5511  C   ALA B  96      47.046  53.884  40.237  1.00 84.03           C  
ANISOU 5511  C   ALA B  96     9002   9352  13575   1161  -1267   -331       C  
ATOM   5512  O   ALA B  96      46.671  53.304  41.254  1.00 91.70           O  
ANISOU 5512  O   ALA B  96     9987  10174  14679   1190  -1240   -444       O  
ATOM   5513  CB  ALA B  96      48.673  52.143  39.469  1.00 76.11           C  
ANISOU 5513  CB  ALA B  96     7894   8665  12358   1102  -1271   -594       C  
ATOM   5514  N   VAL B  97      46.287  54.753  39.580  1.00 81.56           N  
ANISOU 5514  N   VAL B  97     8677   9059  13254   1191  -1314   -165       N  
ATOM   5515  CA  VAL B  97      44.902  55.004  39.957  1.00 84.72           C  
ANISOU 5515  CA  VAL B  97     9076   9312  13801   1269  -1341   -133       C  
ATOM   5516  C   VAL B  97      43.984  54.332  38.941  1.00 88.86           C  
ANISOU 5516  C   VAL B  97     9492  10025  14246   1326  -1424   -176       C  
ATOM   5517  O   VAL B  97      43.747  54.866  37.857  1.00 96.13           O  
ANISOU 5517  O   VAL B  97    10363  11105  15055   1333  -1479    -36       O  
ATOM   5518  CB  VAL B  97      44.600  56.514  40.020  1.00 85.38           C  
ANISOU 5518  CB  VAL B  97     9215   9250  13977   1275  -1342     82       C  
ATOM   5519  CG1 VAL B  97      43.140  56.754  40.361  1.00 89.86           C  
ANISOU 5519  CG1 VAL B  97     9768   9682  14694   1367  -1375    100       C  
ATOM   5520  CG2 VAL B  97      45.501  57.189  41.038  1.00 80.05           C  
ANISOU 5520  CG2 VAL B  97     8634   8385  13396   1218  -1265     94       C  
ATOM   5521  N   LEU B  98      43.470  53.158  39.296  1.00 80.34           N  
ANISOU 5521  N   LEU B  98     8362   8934  13229   1363  -1436   -363       N  
ATOM   5522  CA  LEU B  98      42.737  52.327  38.346  1.00 82.94           C  
ANISOU 5522  CA  LEU B  98     8572   9454  13490   1409  -1516   -458       C  
ATOM   5523  C   LEU B  98      41.280  52.099  38.733  1.00 96.47           C  
ANISOU 5523  C   LEU B  98    10251  11051  15352   1484  -1549   -485       C  
ATOM   5524  O   LEU B  98      40.935  52.081  39.913  1.00101.58           O  
ANISOU 5524  O   LEU B  98    10949  11483  16162   1498  -1502   -506       O  
ATOM   5525  CB  LEU B  98      43.433  50.974  38.190  1.00 80.00           C  
ANISOU 5525  CB  LEU B  98     8130   9198  13070   1383  -1522   -684       C  
ATOM   5526  CG  LEU B  98      44.936  51.008  37.911  1.00 79.06           C  
ANISOU 5526  CG  LEU B  98     8031   9200  12809   1311  -1485   -699       C  
ATOM   5527  CD1 LEU B  98      45.530  49.612  38.015  1.00 74.60           C  
ANISOU 5527  CD1 LEU B  98     7397   8685  12265   1300  -1490   -943       C  
ATOM   5528  CD2 LEU B  98      45.216  51.621  36.548  1.00 80.45           C  
ANISOU 5528  CD2 LEU B  98     8151   9655  12761   1293  -1527   -581       C  
ATOM   5529  N   SER B  99      40.442  51.916  37.715  1.00104.76           N  
ANISOU 5529  N   SER B  99    11202  12272  16330   1531  -1631   -487       N  
ATOM   5530  CA  SER B  99      39.028  51.575  37.877  1.00104.34           C  
ANISOU 5530  CA  SER B  99    11091  12156  16397   1602  -1675   -529       C  
ATOM   5531  C   SER B  99      38.443  51.931  39.243  1.00 97.35           C  
ANISOU 5531  C   SER B  99    10282  10995  15713   1627  -1619   -490       C  
ATOM   5532  O   SER B  99      38.152  51.051  40.053  1.00 88.53           O  
ANISOU 5532  O   SER B  99     9140   9774  14721   1630  -1600   -618       O  
ATOM   5533  CB  SER B  99      38.804  50.089  37.583  1.00106.37           C  
ANISOU 5533  CB  SER B  99    11230  12515  16671   1610  -1724   -765       C  
ATOM   5534  OG  SER B  99      39.231  49.759  36.272  1.00103.59           O  
ANISOU 5534  OG  SER B  99    10781  12455  16125   1600  -1783   -836       O  
ATOM   5535  N   ASN B 100      38.272  53.226  39.487  1.00 98.82           N  
ANISOU 5535  N   ASN B 100    10543  11070  15936   1644  -1597   -312       N  
ATOM   5536  CA  ASN B 100      37.652  53.703  40.717  1.00 97.93           C  
ANISOU 5536  CA  ASN B 100    10483  10725  16002   1679  -1549   -288       C  
ATOM   5537  C   ASN B 100      36.230  54.191  40.477  1.00103.16           C  
ANISOU 5537  C   ASN B 100    11096  11363  16735   1765  -1605   -210       C  
ATOM   5538  O   ASN B 100      35.916  55.355  40.723  1.00106.66           O  
ANISOU 5538  O   ASN B 100    11586  11683  17257   1800  -1597    -78       O  
ATOM   5539  CB  ASN B 100      38.483  54.828  41.334  1.00 93.58           C  
ANISOU 5539  CB  ASN B 100    10041  10030  15486   1644  -1484   -183       C  
ATOM   5540  CG  ASN B 100      39.720  54.320  42.034  1.00 93.68           C  
ANISOU 5540  CG  ASN B 100    10105  10013  15476   1569  -1411   -282       C  
ATOM   5541  ND2 ASN B 100      40.848  54.971  41.785  1.00 98.03           N  
ANISOU 5541  ND2 ASN B 100    10718  10580  15950   1509  -1385   -203       N  
ATOM   5542  OD1 ASN B 100      39.664  53.357  42.797  1.00 94.09           O  
ANISOU 5542  OD1 ASN B 100    10133  10030  15587   1564  -1382   -415       O  
ATOM   5543  N   TYR B 101      35.374  53.301  39.988  1.00102.58           N  
ANISOU 5543  N   TYR B 101    10921  11403  16651   1800  -1665   -300       N  
ATOM   5544  CA  TYR B 101      33.991  53.666  39.711  1.00108.11           C  
ANISOU 5544  CA  TYR B 101    11561  12105  17411   1882  -1723   -237       C  
ATOM   5545  C   TYR B 101      32.993  52.737  40.390  1.00118.06           C  
ANISOU 5545  C   TYR B 101    12750  13308  18797   1914  -1725   -371       C  
ATOM   5546  O   TYR B 101      33.283  51.568  40.649  1.00108.56           O  
ANISOU 5546  O   TYR B 101    11508  12126  17612   1872  -1714   -517       O  
ATOM   5547  CB  TYR B 101      33.728  53.714  38.203  1.00108.43           C  
ANISOU 5547  CB  TYR B 101    11519  12383  17295   1903  -1815   -173       C  
ATOM   5548  CG  TYR B 101      34.127  52.461  37.460  1.00113.30           C  
ANISOU 5548  CG  TYR B 101    12048  13211  17789   1864  -1854   -343       C  
ATOM   5549  CD1 TYR B 101      33.428  51.274  37.632  1.00111.78           C  
ANISOU 5549  CD1 TYR B 101    11764  13029  17678   1881  -1882   -526       C  
ATOM   5550  CD2 TYR B 101      35.197  52.468  36.575  1.00121.96           C  
ANISOU 5550  CD2 TYR B 101    13140  14501  18701   1812  -1865   -328       C  
ATOM   5551  CE1 TYR B 101      33.790  50.128  36.952  1.00118.35           C  
ANISOU 5551  CE1 TYR B 101    12501  14033  18433   1850  -1926   -708       C  
ATOM   5552  CE2 TYR B 101      35.565  51.327  35.889  1.00124.22           C  
ANISOU 5552  CE2 TYR B 101    13328  14989  18881   1786  -1904   -517       C  
ATOM   5553  CZ  TYR B 101      34.859  50.161  36.081  1.00124.35           C  
ANISOU 5553  CZ  TYR B 101    13254  14989  19005   1808  -1937   -716       C  
ATOM   5554  OH  TYR B 101      35.224  49.023  35.399  1.00128.01           O  
ANISOU 5554  OH  TYR B 101    13606  15634  19399   1787  -1985   -930       O  
ATOM   5555  N   ASP B 102      31.814  53.280  40.674  1.00134.68           N  
ANISOU 5555  N   ASP B 102    14830  15338  21004   1989  -1742   -312       N  
ATOM   5556  CA  ASP B 102      30.726  52.519  41.266  1.00142.35           C  
ANISOU 5556  CA  ASP B 102    15719  16273  22093   2022  -1748   -410       C  
ATOM   5557  C   ASP B 102      30.012  51.754  40.161  1.00141.74           C  
ANISOU 5557  C   ASP B 102    15522  16374  21958   2043  -1843   -472       C  
ATOM   5558  O   ASP B 102      30.315  51.932  38.982  1.00142.31           O  
ANISOU 5558  O   ASP B 102    15574  16612  21886   2042  -1901   -432       O  
ATOM   5559  CB  ASP B 102      29.747  53.470  41.957  1.00149.71           C  
ANISOU 5559  CB  ASP B 102    16659  17076  23147   2099  -1731   -331       C  
ATOM   5560  CG  ASP B 102      28.987  52.808  43.086  1.00156.17           C  
ANISOU 5560  CG  ASP B 102    17419  17823  24094   2110  -1691   -424       C  
ATOM   5561  OD1 ASP B 102      28.152  53.491  43.717  1.00157.05           O  
ANISOU 5561  OD1 ASP B 102    17518  17853  24302   2176  -1673   -390       O  
ATOM   5562  OD2 ASP B 102      29.226  51.611  43.347  1.00159.42           O1-
ANISOU 5562  OD2 ASP B 102    17786  18266  24521   2053  -1680   -527       O1-
ATOM   5563  N   ALA B 103      29.068  50.899  40.539  1.00141.60           N  
ANISOU 5563  N   ALA B 103    15410  16341  22050   2060  -1861   -571       N  
ATOM   5564  CA  ALA B 103      28.246  50.213  39.553  1.00141.05           C  
ANISOU 5564  CA  ALA B 103    15211  16431  21952   2086  -1957   -647       C  
ATOM   5565  C   ALA B 103      27.494  51.251  38.727  1.00140.59           C  
ANISOU 5565  C   ALA B 103    15135  16462  21820   2165  -2017   -510       C  
ATOM   5566  O   ALA B 103      27.314  51.092  37.520  1.00136.32           O  
ANISOU 5566  O   ALA B 103    14516  16123  21155   2180  -2099   -522       O  
ATOM   5567  CB  ALA B 103      27.275  49.265  40.235  1.00139.79           C  
ANISOU 5567  CB  ALA B 103    14952  16206  21956   2089  -1961   -748       C  
ATOM   5568  N   ASN B 104      27.068  52.321  39.392  1.00142.14           N  
ANISOU 5568  N   ASN B 104    15393  16516  22097   2217  -1979   -383       N  
ATOM   5569  CA  ASN B 104      26.369  53.415  38.731  1.00142.43           C  
ANISOU 5569  CA  ASN B 104    15416  16595  22106   2299  -2036   -227       C  
ATOM   5570  C   ASN B 104      27.339  54.375  38.048  1.00137.22           C  
ANISOU 5570  C   ASN B 104    14834  15975  21326   2281  -2041    -70       C  
ATOM   5571  O   ASN B 104      26.979  55.505  37.719  1.00135.96           O  
ANISOU 5571  O   ASN B 104    14687  15788  21184   2341  -2074    105       O  
ATOM   5572  CB  ASN B 104      25.504  54.178  39.737  1.00149.10           C  
ANISOU 5572  CB  ASN B 104    16277  17259  23117   2370  -1999   -174       C  
ATOM   5573  CG  ASN B 104      24.539  53.274  40.480  1.00155.15           C  
ANISOU 5573  CG  ASN B 104    16954  17999  23996   2381  -1987   -306       C  
ATOM   5574  ND2 ASN B 104      24.089  53.722  41.647  1.00157.78           N  
ANISOU 5574  ND2 ASN B 104    17304  18185  24460   2418  -1925   -303       N  
ATOM   5575  OD1 ASN B 104      24.200  52.188  40.011  1.00156.44           O  
ANISOU 5575  OD1 ASN B 104    17022  18282  24134   2355  -2034   -412       O  
ATOM   5576  N   LYS B 105      28.570  53.916  37.840  1.00135.60           N  
ANISOU 5576  N   LYS B 105    14674  15835  21015   2198  -2013   -124       N  
ATOM   5577  CA  LYS B 105      29.607  54.734  37.218  1.00135.14           C  
ANISOU 5577  CA  LYS B 105    14681  15831  20834   2163  -2011     26       C  
ATOM   5578  C   LYS B 105      29.857  56.012  38.014  1.00128.41           C  
ANISOU 5578  C   LYS B 105    13938  14742  20110   2180  -1956    170       C  
ATOM   5579  O   LYS B 105      29.926  57.103  37.447  1.00126.75           O  
ANISOU 5579  O   LYS B 105    13743  14532  19883   2204  -1991    371       O  
ATOM   5580  CB  LYS B 105      29.232  55.080  35.774  1.00137.26           C  
ANISOU 5580  CB  LYS B 105    14859  16346  20947   2199  -2110    155       C  
ATOM   5581  CG  LYS B 105      28.876  53.876  34.914  1.00137.99           C  
ANISOU 5581  CG  LYS B 105    14818  16698  20915   2194  -2178    -14       C  
ATOM   5582  CD  LYS B 105      30.082  52.983  34.662  1.00135.74           C  
ANISOU 5582  CD  LYS B 105    14534  16533  20508   2107  -2153   -167       C  
ATOM   5583  CE  LYS B 105      31.084  53.645  33.727  1.00134.83           C  
ANISOU 5583  CE  LYS B 105    14434  16606  20190   2068  -2166    -13       C  
ATOM   5584  NZ  LYS B 105      32.215  52.732  33.387  1.00131.91           N1+
ANISOU 5584  NZ  LYS B 105    14042  16391  19687   1993  -2149   -186       N1+
ATOM   5585  N   THR B 106      29.992  55.868  39.329  1.00120.22           N  
ANISOU 5585  N   THR B 106    12961  13509  19207   2167  -1873     68       N  
ATOM   5586  CA  THR B 106      30.219  57.008  40.211  1.00115.34           C  
ANISOU 5586  CA  THR B 106    12431  12667  18727   2185  -1818    148       C  
ATOM   5587  C   THR B 106      31.094  56.624  41.395  1.00113.97           C  
ANISOU 5587  C   THR B 106    12331  12377  18594   2120  -1718     21       C  
ATOM   5588  O   THR B 106      30.589  56.272  42.461  1.00111.15           O  
ANISOU 5588  O   THR B 106    11956  11933  18341   2140  -1671    -90       O  
ATOM   5589  CB  THR B 106      28.898  57.563  40.759  1.00115.99           C  
ANISOU 5589  CB  THR B 106    12469  12627  18975   2287  -1833    161       C  
ATOM   5590  CG2 THR B 106      28.115  58.263  39.662  1.00120.02           C  
ANISOU 5590  CG2 THR B 106    12917  13214  19471   2360  -1932    331       C  
ATOM   5591  OG1 THR B 106      28.117  56.486  41.292  1.00117.36           O  
ANISOU 5591  OG1 THR B 106    12571  12842  19179   2300  -1820      1       O  
ATOM   5592  N   GLY B 107      32.406  56.702  41.206  1.00116.80           N  
ANISOU 5592  N   GLY B 107    12761  12755  18863   2040  -1686     46       N  
ATOM   5593  CA  GLY B 107      33.346  56.350  42.254  1.00112.48           C  
ANISOU 5593  CA  GLY B 107    12280  12120  18338   1974  -1596    -63       C  
ATOM   5594  C   GLY B 107      34.200  57.522  42.693  1.00102.36           C  
ANISOU 5594  C   GLY B 107    11092  10688  17112   1949  -1548     20       C  
ATOM   5595  O   GLY B 107      33.690  58.619  42.927  1.00 99.63           O  
ANISOU 5595  O   GLY B 107    10755  10202  16897   2009  -1560    100       O  
ATOM   5596  N   LEU B 108      35.504  57.286  42.808  1.00 95.10           N  
ANISOU 5596  N   LEU B 108    10233   9789  16110   1862  -1500    -10       N  
ATOM   5597  CA  LEU B 108      36.439  58.321  43.230  1.00 92.01           C  
ANISOU 5597  CA  LEU B 108     9927   9261  15773   1823  -1454     54       C  
ATOM   5598  C   LEU B 108      36.226  59.593  42.424  1.00 92.21           C  
ANISOU 5598  C   LEU B 108     9954   9229  15851   1854  -1515    256       C  
ATOM   5599  O   LEU B 108      36.218  59.565  41.195  1.00 95.65           O  
ANISOU 5599  O   LEU B 108    10355   9820  16169   1846  -1581    384       O  
ATOM   5600  CB  LEU B 108      37.882  57.840  43.079  1.00 90.56           C  
ANISOU 5600  CB  LEU B 108     9792   9163  15454   1720  -1413     23       C  
ATOM   5601  CG  LEU B 108      38.976  58.861  43.399  1.00 90.16           C  
ANISOU 5601  CG  LEU B 108     9822   8989  15444   1663  -1369     92       C  
ATOM   5602  CD1 LEU B 108      38.931  59.263  44.866  1.00 86.63           C  
ANISOU 5602  CD1 LEU B 108     9406   8358  15150   1682  -1298    -20       C  
ATOM   5603  CD2 LEU B 108      40.343  58.308  43.035  1.00 92.29           C  
ANISOU 5603  CD2 LEU B 108    10125   9387  15555   1565  -1340     73       C  
ATOM   5604  N   LYS B 109      36.053  60.707  43.125  1.00 90.98           N  
ANISOU 5604  N   LYS B 109     9827   8859  15882   1892  -1498    285       N  
ATOM   5605  CA  LYS B 109      35.777  61.981  42.477  1.00 93.96           C  
ANISOU 5605  CA  LYS B 109    10195   9133  16373   1930  -1563    489       C  
ATOM   5606  C   LYS B 109      36.914  62.975  42.679  1.00 97.31           C  
ANISOU 5606  C   LYS B 109    10686   9406  16883   1862  -1535    570       C  
ATOM   5607  O   LYS B 109      37.317  63.668  41.746  1.00102.98           O  
ANISOU 5607  O   LYS B 109    11403  10135  17591   1828  -1586    787       O  
ATOM   5608  CB  LYS B 109      34.464  62.565  43.004  1.00 96.75           C  
ANISOU 5608  CB  LYS B 109    10498   9335  16926   2047  -1590    461       C  
ATOM   5609  CG  LYS B 109      34.119  63.936  42.446  1.00106.26           C  
ANISOU 5609  CG  LYS B 109    11682  10387  18304   2098  -1665    671       C  
ATOM   5610  CD  LYS B 109      32.772  64.416  42.962  1.00114.26           C  
ANISOU 5610  CD  LYS B 109    12632  11264  19516   2226  -1695    615       C  
ATOM   5611  CE  LYS B 109      32.506  65.858  42.557  1.00121.70           C  
ANISOU 5611  CE  LYS B 109    13550  12003  20689   2281  -1770    814       C  
ATOM   5612  NZ  LYS B 109      32.513  66.030  41.079  1.00126.39           N1+
ANISOU 5612  NZ  LYS B 109    14112  12735  21178   2262  -1859   1098       N1+
ATOM   5613  N   GLU B 110      37.435  63.037  43.898  1.00 96.08           N  
ANISOU 5613  N   GLU B 110    10576   9124  16808   1838  -1455    402       N  
ATOM   5614  CA  GLU B 110      38.448  64.025  44.236  1.00103.59           C  
ANISOU 5614  CA  GLU B 110    11580   9905  17874   1778  -1427    444       C  
ATOM   5615  C   GLU B 110      39.716  63.387  44.797  1.00 99.79           C  
ANISOU 5615  C   GLU B 110    11158   9495  17262   1678  -1342    317       C  
ATOM   5616  O   GLU B 110      39.663  62.604  45.744  1.00103.14           O  
ANISOU 5616  O   GLU B 110    11583   9961  17644   1685  -1280    120       O  
ATOM   5617  CB  GLU B 110      37.877  65.026  45.239  1.00121.55           C  
ANISOU 5617  CB  GLU B 110    13837  11926  20421   1856  -1420    352       C  
ATOM   5618  CG  GLU B 110      38.739  66.251  45.462  1.00140.38           C  
ANISOU 5618  CG  GLU B 110    16253  14092  22991   1808  -1417    410       C  
ATOM   5619  CD  GLU B 110      38.074  67.257  46.375  1.00152.23           C  
ANISOU 5619  CD  GLU B 110    17713  15342  24788   1900  -1425    292       C  
ATOM   5620  OE1 GLU B 110      38.669  68.329  46.617  1.00160.55           O  
ANISOU 5620  OE1 GLU B 110    18775  16179  26047   1872  -1432    314       O  
ATOM   5621  OE2 GLU B 110      36.952  66.973  46.848  1.00150.14           O1-
ANISOU 5621  OE2 GLU B 110    17394  15096  24556   2001  -1426    167       O1-
ATOM   5622  N   LEU B 111      40.856  63.729  44.204  1.00 91.97           N  
ANISOU 5622  N   LEU B 111    10206   8528  16209   1583  -1343    444       N  
ATOM   5623  CA  LEU B 111      42.145  63.230  44.669  1.00 88.82           C  
ANISOU 5623  CA  LEU B 111     9861   8193  15695   1485  -1267    339       C  
ATOM   5624  C   LEU B 111      43.102  64.396  44.914  1.00 95.11           C  
ANISOU 5624  C   LEU B 111    10696   8809  16632   1418  -1251    405       C  
ATOM   5625  O   LEU B 111      44.006  64.646  44.116  1.00 95.79           O  
ANISOU 5625  O   LEU B 111    10799   8958  16639   1331  -1265    565       O  
ATOM   5626  CB  LEU B 111      42.736  62.253  43.651  1.00 85.95           C  
ANISOU 5626  CB  LEU B 111     9493   8091  15074   1421  -1279    398       C  
ATOM   5627  CG  LEU B 111      43.984  61.475  44.078  1.00 82.96           C  
ANISOU 5627  CG  LEU B 111     9156   7811  14555   1333  -1206    270       C  
ATOM   5628  CD1 LEU B 111      43.709  60.639  45.320  1.00 79.18           C  
ANISOU 5628  CD1 LEU B 111     8677   7315  14093   1367  -1145     43       C  
ATOM   5629  CD2 LEU B 111      44.478  60.600  42.939  1.00 80.51           C  
ANISOU 5629  CD2 LEU B 111     8819   7762  14009   1284  -1231    322       C  
ATOM   5630  N   PRO B 112      42.901  65.114  46.028  1.00 98.61           N  
ANISOU 5630  N   PRO B 112    11141   9038  17290   1458  -1222    273       N  
ATOM   5631  CA  PRO B 112      43.626  66.349  46.348  1.00 99.79           C  
ANISOU 5631  CA  PRO B 112    11308   8967  17642   1409  -1219    308       C  
ATOM   5632  C   PRO B 112      45.099  66.129  46.668  1.00 97.74           C  
ANISOU 5632  C   PRO B 112    11099   8765  17273   1290  -1151    247       C  
ATOM   5633  O   PRO B 112      45.525  66.465  47.770  1.00102.14           O  
ANISOU 5633  O   PRO B 112    11665   9208  17936   1278  -1098     67       O  
ATOM   5634  CB  PRO B 112      42.910  66.861  47.606  1.00102.88           C  
ANISOU 5634  CB  PRO B 112    11665   9174  18252   1500  -1198     94       C  
ATOM   5635  CG  PRO B 112      41.610  66.123  47.655  1.00103.58           C  
ANISOU 5635  CG  PRO B 112    11712   9370  18276   1605  -1213     33       C  
ATOM   5636  CD  PRO B 112      41.892  64.792  47.048  1.00 97.77           C  
ANISOU 5636  CD  PRO B 112    10998   8898  17252   1556  -1196     72       C  
ATOM   5637  N   MET B 113      45.864  65.585  45.727  1.00 95.56           N  
ANISOU 5637  N   MET B 113    10844   8679  16785   1207  -1155    383       N  
ATOM   5638  CA  MET B 113      47.298  65.407  45.932  1.00 94.87           C  
ANISOU 5638  CA  MET B 113    10798   8655  16592   1093  -1095    342       C  
ATOM   5639  C   MET B 113      48.048  66.668  45.522  1.00 97.82           C  
ANISOU 5639  C   MET B 113    11175   8869  17122   1012  -1124    524       C  
ATOM   5640  O   MET B 113      48.854  66.654  44.593  1.00 98.54           O  
ANISOU 5640  O   MET B 113    11269   9089  17083    921  -1137    704       O  
ATOM   5641  CB  MET B 113      47.813  64.195  45.156  1.00 81.49           C  
ANISOU 5641  CB  MET B 113     9111   7252  14601   1044  -1084    373       C  
ATOM   5642  CG  MET B 113      47.184  62.886  45.590  1.00 71.90           C  
ANISOU 5642  CG  MET B 113     7884   6175  13261   1110  -1059    193       C  
ATOM   5643  SD  MET B 113      47.998  61.450  44.874  1.00 92.25           S  
ANISOU 5643  SD  MET B 113    10456   9054  15540   1049  -1043    167       S  
ATOM   5644  CE  MET B 113      47.824  61.798  43.127  1.00 91.69           C  
ANISOU 5644  CE  MET B 113    10342   9129  15369   1033  -1129    430       C  
ATOM   5645  N   ARG B 114      47.775  67.755  46.234  1.00 98.59           N  
ANISOU 5645  N   ARG B 114    11259   8691  17511   1045  -1136    469       N  
ATOM   5646  CA  ARG B 114      48.287  69.072  45.877  1.00105.61           C  
ANISOU 5646  CA  ARG B 114    12132   9365  18630    979  -1181    652       C  
ATOM   5647  C   ARG B 114      49.739  69.273  46.289  1.00111.36           C  
ANISOU 5647  C   ARG B 114    12890  10077  19343    854  -1123    592       C  
ATOM   5648  O   ARG B 114      50.345  70.292  45.960  1.00113.03           O  
ANISOU 5648  O   ARG B 114    13085  10126  19734    775  -1156    755       O  
ATOM   5649  CB  ARG B 114      47.419  70.152  46.519  1.00108.61           C  
ANISOU 5649  CB  ARG B 114    12469   9433  19366   1071  -1224    580       C  
ATOM   5650  CG  ARG B 114      47.433  70.117  48.035  1.00107.65           C  
ANISOU 5650  CG  ARG B 114    12346   9224  19330   1112  -1156    229       C  
ATOM   5651  CD  ARG B 114      46.120  70.617  48.600  1.00112.35           C  
ANISOU 5651  CD  ARG B 114    12884   9646  20158   1252  -1193    105       C  
ATOM   5652  NE  ARG B 114      46.138  70.670  50.057  1.00115.79           N  
ANISOU 5652  NE  ARG B 114    13295  10029  20672   1292  -1129   -237       N  
ATOM   5653  CZ  ARG B 114      45.054  70.809  50.811  1.00113.40           C  
ANISOU 5653  CZ  ARG B 114    12932   9662  20491   1417  -1133   -429       C  
ATOM   5654  NH1 ARG B 114      43.858  70.901  50.246  1.00107.37           N1+
ANISOU 5654  NH1 ARG B 114    12137   8860  19800   1516  -1199   -311       N1+
ATOM   5655  NH2 ARG B 114      45.165  70.852  52.132  1.00115.45           N  
ANISOU 5655  NH2 ARG B 114    13153   9923  20791   1444  -1072   -741       N  
ATOM   5656  N   ASN B 115      50.293  68.305  47.011  1.00114.32           N  
ANISOU 5656  N   ASN B 115    13302  10617  19517    834  -1041    371       N  
ATOM   5657  CA  ASN B 115      51.672  68.407  47.480  1.00113.09           C  
ANISOU 5657  CA  ASN B 115    13171  10469  19329    721   -981    290       C  
ATOM   5658  C   ASN B 115      52.595  67.359  46.868  1.00102.21           C  
ANISOU 5658  C   ASN B 115    11822   9385  17627    640   -943    345       C  
ATOM   5659  O   ASN B 115      53.800  67.357  47.118  1.00 95.47           O  
ANISOU 5659  O   ASN B 115    10987   8574  16713    541   -895    301       O  
ATOM   5660  CB  ASN B 115      51.727  68.357  49.008  1.00113.25           C  
ANISOU 5660  CB  ASN B 115    13190  10415  19426    757   -917    -32       C  
ATOM   5661  CG  ASN B 115      51.265  69.653  49.645  1.00114.40           C  
ANISOU 5661  CG  ASN B 115    13290  10249  19927    803   -951   -116       C  
ATOM   5662  ND2 ASN B 115      50.273  69.562  50.524  1.00116.79           N  
ANISOU 5662  ND2 ASN B 115    13560  10510  20306    920   -941   -325       N  
ATOM   5663  OD1 ASN B 115      51.794  70.725  49.349  1.00110.49           O  
ANISOU 5663  OD1 ASN B 115    12778   9556  19648    732   -989      4       O  
ATOM   5664  N   LEU B 116      52.020  66.470  46.065  1.00 97.67           N  
ANISOU 5664  N   LEU B 116    11241   9015  16853    686   -967    426       N  
ATOM   5665  CA  LEU B 116      52.805  65.500  45.316  1.00 92.25           C  
ANISOU 5665  CA  LEU B 116    10561   8615  15874    621   -947    478       C  
ATOM   5666  C   LEU B 116      53.541  66.219  44.197  1.00 93.34           C  
ANISOU 5666  C   LEU B 116    10676   8794  15995    516   -984    754       C  
ATOM   5667  O   LEU B 116      52.936  66.612  43.202  1.00 95.23           O  
ANISOU 5667  O   LEU B 116    10875   9055  16252    535  -1054    982       O  
ATOM   5668  CB  LEU B 116      51.900  64.419  44.730  1.00 92.01           C  
ANISOU 5668  CB  LEU B 116    10511   8781  15669    704   -975    471       C  
ATOM   5669  CG  LEU B 116      52.588  63.382  43.842  1.00 91.36           C  
ANISOU 5669  CG  LEU B 116    10411   9005  15296    654   -968    501       C  
ATOM   5670  CD1 LEU B 116      53.488  62.488  44.674  1.00 91.36           C  
ANISOU 5670  CD1 LEU B 116    10439   9088  15184    620   -892    282       C  
ATOM   5671  CD2 LEU B 116      51.561  62.556  43.089  1.00 95.66           C  
ANISOU 5671  CD2 LEU B 116    10914   9714  15717    738  -1018    518       C  
ATOM   5672  N   GLN B 117      54.848  66.389  44.360  1.00 99.33           N  
ANISOU 5672  N   GLN B 117    11448   9580  16712    404   -939    745       N  
ATOM   5673  CA  GLN B 117      55.637  67.146  43.398  1.00102.86           C  
ANISOU 5673  CA  GLN B 117    11861  10063  17158    289   -968   1017       C  
ATOM   5674  C   GLN B 117      56.766  66.315  42.802  1.00108.16           C  
ANISOU 5674  C   GLN B 117    12520  11051  17524    202   -928   1027       C  
ATOM   5675  O   GLN B 117      57.271  66.625  41.723  1.00115.31           O  
ANISOU 5675  O   GLN B 117    13376  12107  18329    120   -957   1272       O  
ATOM   5676  CB  GLN B 117      56.209  68.400  44.060  1.00102.65           C  
ANISOU 5676  CB  GLN B 117    11838   9741  17422    216   -962   1032       C  
ATOM   5677  CG  GLN B 117      55.220  69.110  44.965  1.00110.11           C  
ANISOU 5677  CG  GLN B 117    12789  10368  18680    312   -987    911       C  
ATOM   5678  CD  GLN B 117      55.779  70.383  45.559  1.00119.62           C  
ANISOU 5678  CD  GLN B 117    13977  11270  20202    242   -992    907       C  
ATOM   5679  NE2 GLN B 117      55.623  70.541  46.868  1.00121.25           N  
ANISOU 5679  NE2 GLN B 117    14197  11308  20564    293   -956    613       N  
ATOM   5680  OE1 GLN B 117      56.340  71.219  44.851  1.00125.16           O  
ANISOU 5680  OE1 GLN B 117    14642  11900  21013    140  -1032   1164       O  
ATOM   5681  N   GLU B 118      57.158  65.257  43.503  1.00104.01           N  
ANISOU 5681  N   GLU B 118    12029  10637  16853    223   -865    768       N  
ATOM   5682  CA  GLU B 118      58.293  64.450  43.076  1.00101.44           C  
ANISOU 5682  CA  GLU B 118    11688  10591  16265    149   -825    735       C  
ATOM   5683  C   GLU B 118      57.962  62.964  43.006  1.00 94.05           C  
ANISOU 5683  C   GLU B 118    10746   9873  15117    230   -814    556       C  
ATOM   5684  O   GLU B 118      57.364  62.405  43.924  1.00 89.89           O  
ANISOU 5684  O   GLU B 118    10251   9254  14650    314   -794    359       O  
ATOM   5685  CB  GLU B 118      59.485  64.673  44.010  1.00108.03           C  
ANISOU 5685  CB  GLU B 118    12554  11344  17150     64   -758    604       C  
ATOM   5686  CG  GLU B 118      60.748  63.931  43.602  1.00112.58           C  
ANISOU 5686  CG  GLU B 118    13107  12196  17472    -16   -716    572       C  
ATOM   5687  CD  GLU B 118      61.448  64.569  42.417  1.00119.91           C  
ANISOU 5687  CD  GLU B 118    13978  13265  18320   -130   -741    845       C  
ATOM   5688  OE1 GLU B 118      61.425  65.814  42.308  1.00124.25           O  
ANISOU 5688  OE1 GLU B 118    14517  13617  19074   -189   -771   1041       O  
ATOM   5689  OE2 GLU B 118      62.028  63.826  41.597  1.00118.54           O1-
ANISOU 5689  OE2 GLU B 118    13753  13402  17884   -160   -735    864       O1-
ATOM   5690  N   ILE B 119      58.356  62.335  41.903  1.00 97.58           N  
ANISOU 5690  N   ILE B 119    11136  10617  15323    203   -831    625       N  
ATOM   5691  CA  ILE B 119      58.249  60.889  41.749  1.00 98.39           C  
ANISOU 5691  CA  ILE B 119    11213  10935  15236    266   -825    438       C  
ATOM   5692  C   ILE B 119      59.563  60.342  41.196  1.00103.51           C  
ANISOU 5692  C   ILE B 119    11814  11854  15659    185   -796    409       C  
ATOM   5693  O   ILE B 119      59.729  60.195  39.984  1.00109.64           O  
ANISOU 5693  O   ILE B 119    12514  12895  16251    160   -830    522       O  
ATOM   5694  CB  ILE B 119      57.088  60.495  40.820  1.00 96.15           C  
ANISOU 5694  CB  ILE B 119    10875  10776  14879    351   -895    501       C  
ATOM   5695  CG1 ILE B 119      55.757  60.969  41.405  1.00 94.88           C  
ANISOU 5695  CG1 ILE B 119    10754  10355  14940    439   -923    512       C  
ATOM   5696  CG2 ILE B 119      57.061  58.990  40.611  1.00 95.35           C  
ANISOU 5696  CG2 ILE B 119    10731  10892  14607    408   -897    291       C  
ATOM   5697  CD1 ILE B 119      54.548  60.520  40.612  1.00 94.55           C  
ANISOU 5697  CD1 ILE B 119    10660  10426  14839    530   -990    550       C  
ATOM   5698  N   LEU B 120      60.490  60.048  42.102  1.00 96.92           N  
ANISOU 5698  N   LEU B 120    11016  10973  14836    147   -734    251       N  
ATOM   5699  CA  LEU B 120      61.855  59.675  41.741  1.00 93.35           C  
ANISOU 5699  CA  LEU B 120    10523  10744  14201     63   -699    218       C  
ATOM   5700  C   LEU B 120      61.944  58.597  40.663  1.00102.13           C  
ANISOU 5700  C   LEU B 120    11544  12187  15073     95   -729    157       C  
ATOM   5701  O   LEU B 120      62.618  58.779  39.650  1.00109.04           O  
ANISOU 5701  O   LEU B 120    12346  13311  15774     25   -737    275       O  
ATOM   5702  CB  LEU B 120      62.629  59.232  42.984  1.00 83.68           C  
ANISOU 5702  CB  LEU B 120     9344   9427  13023     52   -634     13       C  
ATOM   5703  CG  LEU B 120      62.759  60.273  44.094  1.00 83.25           C  
ANISOU 5703  CG  LEU B 120     9359   9090  13182     10   -598     26       C  
ATOM   5704  CD1 LEU B 120      63.603  59.738  45.238  1.00 85.81           C  
ANISOU 5704  CD1 LEU B 120     9706   9394  13504     -3   -535   -177       C  
ATOM   5705  CD2 LEU B 120      63.356  61.555  43.546  1.00 87.40           C  
ANISOU 5705  CD2 LEU B 120     9872   9582  13752   -106   -603    250       C  
ATOM   5706  N   HIS B 121      61.271  57.473  40.886  1.00100.30           N  
ANISOU 5706  N   HIS B 121    11302  11968  14838    199   -747    -33       N  
ATOM   5707  CA  HIS B 121      61.356  56.348  39.963  1.00101.39           C  
ANISOU 5707  CA  HIS B 121    11341  12401  14782    239   -781   -150       C  
ATOM   5708  C   HIS B 121      59.978  55.799  39.614  1.00 99.44           C  
ANISOU 5708  C   HIS B 121    11064  12151  14566    347   -843   -196       C  
ATOM   5709  O   HIS B 121      59.060  55.836  40.431  1.00101.17           O  
ANISOU 5709  O   HIS B 121    11347  12127  14966    409   -846   -224       O  
ATOM   5710  CB  HIS B 121      62.226  55.240  40.558  1.00109.76           C  
ANISOU 5710  CB  HIS B 121    12386  13510  15807    250   -744   -390       C  
ATOM   5711  CG  HIS B 121      63.567  55.711  41.029  1.00119.88           C  
ANISOU 5711  CG  HIS B 121    13697  14786  17066    150   -680   -369       C  
ATOM   5712  CD2 HIS B 121      64.750  55.827  40.382  1.00122.54           C  
ANISOU 5712  CD2 HIS B 121    13974  15356  17230     65   -659   -335       C  
ATOM   5713  ND1 HIS B 121      63.796  56.129  42.323  1.00122.78           N  
ANISOU 5713  ND1 HIS B 121    14155  14902  17595    128   -630   -393       N  
ATOM   5714  CE1 HIS B 121      65.062  56.484  42.451  1.00122.44           C  
ANISOU 5714  CE1 HIS B 121    14110  14924  17489     32   -583   -376       C  
ATOM   5715  NE2 HIS B 121      65.663  56.309  41.288  1.00123.69           N  
ANISOU 5715  NE2 HIS B 121    14180  15370  17448     -9   -598   -335       N  
ATOM   5716  N   GLY B 122      59.842  55.285  38.396  1.00 97.90           N  
ANISOU 5716  N   GLY B 122    10761  12249  14189    370   -894   -213       N  
ATOM   5717  CA  GLY B 122      58.583  54.724  37.940  1.00 94.77           C  
ANISOU 5717  CA  GLY B 122    10315  11888  13804    468   -959   -270       C  
ATOM   5718  C   GLY B 122      57.769  55.705  37.120  1.00 92.71           C  
ANISOU 5718  C   GLY B 122    10036  11675  13515    464  -1006    -20       C  
ATOM   5719  O   GLY B 122      58.128  56.877  37.000  1.00 93.76           O  
ANISOU 5719  O   GLY B 122    10200  11765  13659    386   -989    216       O  
ATOM   5720  N   ALA B 123      56.670  55.221  36.551  1.00 91.81           N  
ANISOU 5720  N   ALA B 123     9860  11645  13379    549  -1071    -65       N  
ATOM   5721  CA  ALA B 123      55.782  56.059  35.755  1.00 98.14           C  
ANISOU 5721  CA  ALA B 123    10630  12506  14154    560  -1125    171       C  
ATOM   5722  C   ALA B 123      54.408  56.170  36.413  1.00102.53           C  
ANISOU 5722  C   ALA B 123    11252  12778  14928    647  -1151    170       C  
ATOM   5723  O   ALA B 123      54.194  55.655  37.510  1.00106.53           O  
ANISOU 5723  O   ALA B 123    11827  13053  15596    688  -1120      3       O  
ATOM   5724  CB  ALA B 123      55.657  55.507  34.344  1.00 98.49           C  
ANISOU 5724  CB  ALA B 123    10517  12961  13943    582  -1186    140       C  
ATOM   5725  N   VAL B 124      53.480  56.842  35.742  1.00 97.83           N  
ANISOU 5725  N   VAL B 124    10623  12217  14330    675  -1208    367       N  
ATOM   5726  CA  VAL B 124      52.139  57.025  36.285  1.00105.10           C  
ANISOU 5726  CA  VAL B 124    11594  12888  15450    760  -1236    379       C  
ATOM   5727  C   VAL B 124      51.083  56.399  35.378  1.00108.61           C  
ANISOU 5727  C   VAL B 124    11932  13540  15795    841  -1314    329       C  
ATOM   5728  O   VAL B 124      51.266  56.312  34.163  1.00114.34           O  
ANISOU 5728  O   VAL B 124    12543  14603  16297    824  -1357    392       O  
ATOM   5729  CB  VAL B 124      51.820  58.515  36.501  1.00115.42           C  
ANISOU 5729  CB  VAL B 124    12965  13971  16919    734  -1239    657       C  
ATOM   5730  CG1 VAL B 124      50.533  58.675  37.299  1.00115.49           C  
ANISOU 5730  CG1 VAL B 124    13031  13694  17157    826  -1254    622       C  
ATOM   5731  CG2 VAL B 124      52.975  59.201  37.212  1.00116.15           C  
ANISOU 5731  CG2 VAL B 124    13138  13904  17092    640  -1170    710       C  
ATOM   5732  N   ARG B 125      49.978  55.966  35.977  1.00104.47           N  
ANISOU 5732  N   ARG B 125    11433  12830  15429    928  -1332    213       N  
ATOM   5733  CA  ARG B 125      48.907  55.310  35.237  1.00102.08           C  
ANISOU 5733  CA  ARG B 125    11031  12693  15063   1008  -1407    137       C  
ATOM   5734  C   ARG B 125      47.536  55.672  35.799  1.00 97.66           C  
ANISOU 5734  C   ARG B 125    10517  11883  14708   1085  -1432    192       C  
ATOM   5735  O   ARG B 125      47.220  55.350  36.944  1.00102.21           O  
ANISOU 5735  O   ARG B 125    11164  12204  15468   1116  -1395     66       O  
ATOM   5736  CB  ARG B 125      49.095  53.792  35.271  1.00105.94           C  
ANISOU 5736  CB  ARG B 125    11453  13293  15506   1037  -1413   -179       C  
ATOM   5737  CG  ARG B 125      47.901  52.998  34.764  1.00109.65           C  
ANISOU 5737  CG  ARG B 125    11822  13863  15976   1124  -1489   -310       C  
ATOM   5738  CD  ARG B 125      47.948  52.802  33.258  1.00115.78           C  
ANISOU 5738  CD  ARG B 125    12445  15056  16492   1126  -1555   -311       C  
ATOM   5739  NE  ARG B 125      46.735  52.163  32.752  1.00119.02           N  
ANISOU 5739  NE  ARG B 125    12753  15563  16908   1209  -1634   -428       N  
ATOM   5740  CZ  ARG B 125      46.466  50.866  32.870  1.00111.18           C  
ANISOU 5740  CZ  ARG B 125    11688  14575  15980   1255  -1662   -725       C  
ATOM   5741  NH1 ARG B 125      47.322  50.060  33.484  1.00112.17           N1+
ANISOU 5741  NH1 ARG B 125    11834  14610  16175   1230  -1620   -923       N1+
ATOM   5742  NH2 ARG B 125      45.336  50.374  32.379  1.00 99.61           N  
ANISOU 5742  NH2 ARG B 125    10123  13197  14528   1325  -1738   -819       N  
ATOM   5743  N   PHE B 126      46.730  56.346  34.987  1.00 89.95           N  
ANISOU 5743  N   PHE B 126     9486  10999  13691   1117  -1495    387       N  
ATOM   5744  CA  PHE B 126      45.350  56.649  35.346  1.00 89.27           C  
ANISOU 5744  CA  PHE B 126     9418  10721  13779   1201  -1530    434       C  
ATOM   5745  C   PHE B 126      44.410  56.009  34.331  1.00101.03           C  
ANISOU 5745  C   PHE B 126    10777  12467  15141   1267  -1614    379       C  
ATOM   5746  O   PHE B 126      44.630  56.109  33.124  1.00105.16           O  
ANISOU 5746  O   PHE B 126    11197  13311  15447   1247  -1662    478       O  
ATOM   5747  CB  PHE B 126      45.120  58.160  35.393  1.00 93.19           C  
ANISOU 5747  CB  PHE B 126     9966  11046  14396   1191  -1539    731       C  
ATOM   5748  CG  PHE B 126      45.522  58.798  36.692  1.00 97.13           C  
ANISOU 5748  CG  PHE B 126    10591  11198  15114   1164  -1467    730       C  
ATOM   5749  CD1 PHE B 126      46.856  58.935  37.029  1.00105.30           C  
ANISOU 5749  CD1 PHE B 126    11680  12216  16115   1072  -1403    717       C  
ATOM   5750  CD2 PHE B 126      44.563  59.273  37.570  1.00 97.15           C  
ANISOU 5750  CD2 PHE B 126    10646  10914  15351   1232  -1465    729       C  
ATOM   5751  CE1 PHE B 126      47.226  59.527  38.222  1.00105.29           C  
ANISOU 5751  CE1 PHE B 126    11780  11916  16309   1047  -1340    697       C  
ATOM   5752  CE2 PHE B 126      44.927  59.865  38.762  1.00 97.49           C  
ANISOU 5752  CE2 PHE B 126    10785  10670  15585   1211  -1402    700       C  
ATOM   5753  CZ  PHE B 126      46.260  59.992  39.088  1.00100.39           C  
ANISOU 5753  CZ  PHE B 126    11203  11024  15915   1118  -1340    681       C  
ATOM   5754  N   SER B 127      43.364  55.352  34.823  1.00106.12           N  
ANISOU 5754  N   SER B 127    11414  12989  15915   1343  -1634    221       N  
ATOM   5755  CA  SER B 127      42.450  54.623  33.951  1.00109.96           C  
ANISOU 5755  CA  SER B 127    11771  13705  16305   1406  -1714    124       C  
ATOM   5756  C   SER B 127      41.106  54.342  34.617  1.00113.20           C  
ANISOU 5756  C   SER B 127    12191  13908  16914   1489  -1735     45       C  
ATOM   5757  O   SER B 127      41.042  54.054  35.812  1.00118.72           O  
ANISOU 5757  O   SER B 127    12969  14344  17795   1495  -1680    -62       O  
ATOM   5758  CB  SER B 127      43.090  53.308  33.499  1.00110.72           C  
ANISOU 5758  CB  SER B 127    11774  14036  16258   1387  -1723   -145       C  
ATOM   5759  OG  SER B 127      42.136  52.459  32.887  1.00115.79           O  
ANISOU 5759  OG  SER B 127    12290  14842  16865   1452  -1800   -304       O  
ATOM   5760  N   ASN B 128      40.036  54.428  33.832  1.00112.35           N  
ANISOU 5760  N   ASN B 128    11989  13943  16757   1551  -1814    106       N  
ATOM   5761  CA  ASN B 128      38.696  54.105  34.311  1.00115.77           C  
ANISOU 5761  CA  ASN B 128    12406  14226  17355   1631  -1843     27       C  
ATOM   5762  C   ASN B 128      38.314  54.835  35.594  1.00109.65           C  
ANISOU 5762  C   ASN B 128    11754  13088  16820   1652  -1786    110       C  
ATOM   5763  O   ASN B 128      37.939  54.210  36.586  1.00108.00           O  
ANISOU 5763  O   ASN B 128    11572  12699  16765   1672  -1752    -47       O  
ATOM   5764  CB  ASN B 128      38.552  52.596  34.508  1.00124.68           C  
ANISOU 5764  CB  ASN B 128    13466  15392  18514   1641  -1852   -280       C  
ATOM   5765  CG  ASN B 128      38.829  51.816  33.240  1.00132.64           C  
ANISOU 5765  CG  ASN B 128    14328  16765  19304   1633  -1917   -417       C  
ATOM   5766  ND2 ASN B 128      39.164  50.540  33.391  1.00139.11           N  
ANISOU 5766  ND2 ASN B 128    15092  17610  20155   1621  -1918   -694       N  
ATOM   5767  OD1 ASN B 128      38.742  52.355  32.136  1.00129.77           O  
ANISOU 5767  OD1 ASN B 128    13888  16668  18751   1640  -1970   -277       O  
ATOM   5768  N   ASN B 129      38.413  56.159  35.567  1.00105.11           N  
ANISOU 5768  N   ASN B 129    11236  12417  16284   1647  -1781    357       N  
ATOM   5769  CA  ASN B 129      38.029  56.985  36.704  1.00101.49           C  
ANISOU 5769  CA  ASN B 129    10874  11629  16058   1677  -1737    424       C  
ATOM   5770  C   ASN B 129      37.039  58.056  36.264  1.00106.00           C  
ANISOU 5770  C   ASN B 129    11414  12156  16703   1745  -1801    646       C  
ATOM   5771  O   ASN B 129      37.415  59.207  36.049  1.00113.80           O  
ANISOU 5771  O   ASN B 129    12435  13075  17729   1723  -1807    871       O  
ATOM   5772  CB  ASN B 129      39.265  57.622  37.339  1.00101.78           C  
ANISOU 5772  CB  ASN B 129    11017  11515  16138   1600  -1661    480       C  
ATOM   5773  CG  ASN B 129      40.294  56.593  37.770  1.00102.66           C  
ANISOU 5773  CG  ASN B 129    11155  11675  16177   1535  -1600    275       C  
ATOM   5774  ND2 ASN B 129      41.543  56.804  37.372  1.00105.06           N  
ANISOU 5774  ND2 ASN B 129    11481  12083  16354   1454  -1575    334       N  
ATOM   5775  OD1 ASN B 129      39.971  55.622  38.455  1.00 98.84           O  
ANISOU 5775  OD1 ASN B 129    10663  11133  15758   1557  -1578     77       O  
ATOM   5776  N   PRO B 130      35.764  57.668  36.122  1.00104.16           N  
ANISOU 5776  N   PRO B 130    11108  11959  16508   1827  -1854    588       N  
ATOM   5777  CA  PRO B 130      34.690  58.503  35.571  1.00105.03           C  
ANISOU 5777  CA  PRO B 130    11162  12073  16672   1906  -1930    782       C  
ATOM   5778  C   PRO B 130      34.418  59.766  36.380  1.00108.98           C  
ANISOU 5778  C   PRO B 130    11736  12255  17415   1943  -1909    920       C  
ATOM   5779  O   PRO B 130      34.112  60.806  35.797  1.00120.50           O  
ANISOU 5779  O   PRO B 130    13166  13697  18920   1974  -1968   1164       O  
ATOM   5780  CB  PRO B 130      33.467  57.581  35.629  1.00107.58           C  
ANISOU 5780  CB  PRO B 130    11405  12454  17018   1978  -1967    609       C  
ATOM   5781  CG  PRO B 130      34.027  56.202  35.672  1.00108.26           C  
ANISOU 5781  CG  PRO B 130    11469  12670  16995   1924  -1939    362       C  
ATOM   5782  CD  PRO B 130      35.290  56.317  36.460  1.00105.60           C  
ANISOU 5782  CD  PRO B 130    11245  12188  16691   1847  -1849    329       C  
ATOM   5783  N   ALA B 131      34.523  59.674  37.701  1.00104.18           N  
ANISOU 5783  N   ALA B 131    11208  11407  16967   1943  -1832    763       N  
ATOM   5784  CA  ALA B 131      34.182  60.796  38.569  1.00109.08           C  
ANISOU 5784  CA  ALA B 131    11881  11732  17834   1991  -1812    829       C  
ATOM   5785  C   ALA B 131      35.381  61.690  38.870  1.00107.09           C  
ANISOU 5785  C   ALA B 131    11712  11330  17647   1918  -1767    929       C  
ATOM   5786  O   ALA B 131      35.235  62.751  39.476  1.00107.10           O  
ANISOU 5786  O   ALA B 131    11745  11080  17867   1951  -1760    991       O  
ATOM   5787  CB  ALA B 131      33.558  60.293  39.861  1.00112.56           C  
ANISOU 5787  CB  ALA B 131    12336  12025  18406   2038  -1755    605       C  
ATOM   5788  N   LEU B 132      36.562  61.260  38.440  1.00107.55           N  
ANISOU 5788  N   LEU B 132    11794  11543  17525   1819  -1739    930       N  
ATOM   5789  CA  LEU B 132      37.794  61.989  38.719  1.00105.46           C  
ANISOU 5789  CA  LEU B 132    11604  11159  17306   1735  -1692   1011       C  
ATOM   5790  C   LEU B 132      37.758  63.398  38.136  1.00110.98           C  
ANISOU 5790  C   LEU B 132    12286  11752  18128   1740  -1752   1306       C  
ATOM   5791  O   LEU B 132      37.502  63.583  36.946  1.00111.25           O  
ANISOU 5791  O   LEU B 132    12244  11976  18048   1746  -1829   1514       O  
ATOM   5792  CB  LEU B 132      39.004  61.224  38.179  1.00100.48           C  
ANISOU 5792  CB  LEU B 132    10980  10762  16434   1633  -1662    972       C  
ATOM   5793  CG  LEU B 132      40.375  61.756  38.599  1.00 96.98           C  
ANISOU 5793  CG  LEU B 132    10616  10213  16019   1535  -1599   1007       C  
ATOM   5794  CD1 LEU B 132      40.447  61.911  40.110  1.00 95.41           C  
ANISOU 5794  CD1 LEU B 132    10495   9741  16017   1548  -1524    829       C  
ATOM   5795  CD2 LEU B 132      41.480  60.842  38.092  1.00 93.20           C  
ANISOU 5795  CD2 LEU B 132    10130   9990  15292   1448  -1570    931       C  
ATOM   5796  N   CYS B 133      38.021  64.387  38.985  1.00113.78           N  
ANISOU 5796  N   CYS B 133    12698  11808  18725   1738  -1722   1324       N  
ATOM   5797  CA  CYS B 133      37.976  65.785  38.576  1.00115.08           C  
ANISOU 5797  CA  CYS B 133    12840  11805  19082   1744  -1784   1599       C  
ATOM   5798  C   CYS B 133      39.325  66.474  38.755  1.00108.66           C  
ANISOU 5798  C   CYS B 133    12082  10872  18331   1633  -1745   1687       C  
ATOM   5799  O   CYS B 133      40.042  66.214  39.721  1.00102.25           O  
ANISOU 5799  O   CYS B 133    11343   9968  17541   1588  -1661   1479       O  
ATOM   5800  CB  CYS B 133      36.907  66.540  39.374  1.00119.03           C  
ANISOU 5800  CB  CYS B 133    13328  12010  19887   1858  -1807   1547       C  
ATOM   5801  SG  CYS B 133      35.210  65.962  39.124  1.00137.89           S  
ANISOU 5801  SG  CYS B 133    15636  14511  22245   1995  -1866   1488       S  
ATOM   5802  N   ASN B 134      39.661  67.347  37.809  1.00110.77           N  
ANISOU 5802  N   ASN B 134    12305  11158  18625   1587  -1809   2009       N  
ATOM   5803  CA  ASN B 134      40.817  68.236  37.927  1.00113.02           C  
ANISOU 5803  CA  ASN B 134    12623  11285  19034   1483  -1789   2145       C  
ATOM   5804  C   ASN B 134      42.170  67.585  37.643  1.00111.18           C  
ANISOU 5804  C   ASN B 134    12423  11286  18533   1354  -1726   2115       C  
ATOM   5805  O   ASN B 134      43.031  68.191  37.006  1.00110.78           O  
ANISOU 5805  O   ASN B 134    12349  11280  18461   1256  -1743   2359       O  
ATOM   5806  CB  ASN B 134      40.832  68.914  39.300  1.00118.12           C  
ANISOU 5806  CB  ASN B 134    13327  11548  20003   1512  -1746   1959       C  
ATOM   5807  CG  ASN B 134      39.488  69.512  39.669  1.00123.07           C  
ANISOU 5807  CG  ASN B 134    13912  11949  20900   1650  -1804   1941       C  
ATOM   5808  ND2 ASN B 134      38.718  69.908  38.660  1.00125.46           N  
ANISOU 5808  ND2 ASN B 134    14134  12314  21222   1701  -1902   2211       N  
ATOM   5809  OD1 ASN B 134      39.141  69.610  40.845  1.00122.96           O  
ANISOU 5809  OD1 ASN B 134    13927  11728  21064   1711  -1762   1686       O  
ATOM   5810  N   VAL B 135      42.355  66.357  38.118  1.00110.01           N  
ANISOU 5810  N   VAL B 135    12319  11285  18195   1354  -1656   1823       N  
ATOM   5811  CA  VAL B 135      43.613  65.638  37.931  1.00105.71           C  
ANISOU 5811  CA  VAL B 135    11800  10957  17407   1246  -1595   1751       C  
ATOM   5812  C   VAL B 135      44.017  65.598  36.462  1.00108.94           C  
ANISOU 5812  C   VAL B 135    12124  11695  17571   1183  -1647   2008       C  
ATOM   5813  O   VAL B 135      45.197  65.482  36.130  1.00109.36           O  
ANISOU 5813  O   VAL B 135    12180  11901  17469   1076  -1612   2054       O  
ATOM   5814  CB  VAL B 135      43.517  64.197  38.462  1.00101.81           C  
ANISOU 5814  CB  VAL B 135    11335  10601  16748   1275  -1537   1426       C  
ATOM   5815  CG1 VAL B 135      44.856  63.490  38.328  1.00100.34           C  
ANISOU 5815  CG1 VAL B 135    11171  10611  16343   1171  -1478   1340       C  
ATOM   5816  CG2 VAL B 135      43.055  64.199  39.908  1.00102.34           C  
ANISOU 5816  CG2 VAL B 135    11463  10393  17027   1337  -1486   1192       C  
ATOM   5817  N   GLU B 136      43.024  65.703  35.587  1.00115.80           N  
ANISOU 5817  N   GLU B 136    12908  12696  18396   1252  -1732   2174       N  
ATOM   5818  CA  GLU B 136      43.247  65.675  34.149  1.00126.04           C  
ANISOU 5818  CA  GLU B 136    14096  14355  19439   1205  -1790   2426       C  
ATOM   5819  C   GLU B 136      44.013  66.903  33.663  1.00128.42           C  
ANISOU 5819  C   GLU B 136    14367  14595  19831   1108  -1817   2785       C  
ATOM   5820  O   GLU B 136      44.417  66.970  32.503  1.00135.26           O  
ANISOU 5820  O   GLU B 136    15135  15785  20474   1046  -1855   3028       O  
ATOM   5821  CB  GLU B 136      41.905  65.575  33.422  1.00138.98           C  
ANISOU 5821  CB  GLU B 136    15642  16132  21034   1311  -1879   2521       C  
ATOM   5822  CG  GLU B 136      40.868  66.573  33.919  1.00150.78           C  
ANISOU 5822  CG  GLU B 136    17148  17271  22871   1403  -1928   2631       C  
ATOM   5823  CD  GLU B 136      39.446  66.150  33.602  1.00160.91           C  
ANISOU 5823  CD  GLU B 136    18365  18651  24122   1527  -1991   2584       C  
ATOM   5824  OE1 GLU B 136      39.260  65.319  32.689  1.00168.82           O  
ANISOU 5824  OE1 GLU B 136    19284  20030  24832   1532  -2021   2565       O  
ATOM   5825  OE2 GLU B 136      38.515  66.650  34.268  1.00159.44           O1-
ANISOU 5825  OE2 GLU B 136    18201  18174  24206   1621  -2012   2550       O1-
ATOM   5826  N   SER B 137      44.214  67.869  34.553  1.00122.70           N  
ANISOU 5826  N   SER B 137    13714  13469  19439   1094  -1799   2816       N  
ATOM   5827  CA  SER B 137      44.862  69.123  34.181  1.00120.77           C  
ANISOU 5827  CA  SER B 137    13434  13097  19357   1002  -1834   3165       C  
ATOM   5828  C   SER B 137      46.258  69.261  34.780  1.00121.39           C  
ANISOU 5828  C   SER B 137    13583  13074  19465    880  -1752   3081       C  
ATOM   5829  O   SER B 137      46.837  70.346  34.770  1.00127.36           O  
ANISOU 5829  O   SER B 137    14325  13631  20433    799  -1771   3316       O  
ATOM   5830  CB  SER B 137      44.000  70.313  34.606  1.00120.00           C  
ANISOU 5830  CB  SER B 137    13331  12592  19673   1078  -1899   3305       C  
ATOM   5831  OG  SER B 137      44.015  70.475  36.014  1.00115.96           O  
ANISOU 5831  OG  SER B 137    12921  11714  19425   1112  -1840   3010       O  
ATOM   5832  N   ILE B 138      46.797  68.164  35.299  1.00116.77           N  
ANISOU 5832  N   ILE B 138    13065  12619  18684    864  -1666   2752       N  
ATOM   5833  CA  ILE B 138      48.117  68.190  35.923  1.00116.10           C  
ANISOU 5833  CA  ILE B 138    13047  12458  18609    755  -1585   2641       C  
ATOM   5834  C   ILE B 138      49.239  67.971  34.912  1.00122.96           C  
ANISOU 5834  C   ILE B 138    13850  13687  19182    631  -1574   2815       C  
ATOM   5835  O   ILE B 138      49.266  66.959  34.210  1.00125.76           O  
ANISOU 5835  O   ILE B 138    14154  14421  19209    641  -1570   2737       O  
ATOM   5836  CB  ILE B 138      48.235  67.147  37.055  1.00107.27           C  
ANISOU 5836  CB  ILE B 138    12024  11294  17439    795  -1497   2216       C  
ATOM   5837  CG1 ILE B 138      47.713  67.724  38.372  1.00100.54           C  
ANISOU 5837  CG1 ILE B 138    11242  10028  16931    862  -1479   2052       C  
ATOM   5838  CG2 ILE B 138      49.681  66.714  37.233  1.00107.87           C  
ANISOU 5838  CG2 ILE B 138    12134  11499  17352    679  -1419   2112       C  
ATOM   5839  CD1 ILE B 138      46.252  68.090  38.347  1.00 99.52           C  
ANISOU 5839  CD1 ILE B 138    11080   9756  16978    989  -1550   2103       C  
ATOM   5840  N   GLN B 139      50.160  68.929  34.841  1.00123.50           N  
ANISOU 5840  N   GLN B 139    13906  13640  19377    514  -1571   3040       N  
ATOM   5841  CA  GLN B 139      51.339  68.801  33.993  1.00122.13           C  
ANISOU 5841  CA  GLN B 139    13666  13800  18937    383  -1550   3205       C  
ATOM   5842  C   GLN B 139      52.338  67.863  34.654  1.00119.14           C  
ANISOU 5842  C   GLN B 139    13363  13509  18396    339  -1450   2867       C  
ATOM   5843  O   GLN B 139      53.292  68.311  35.288  1.00122.48           O  
ANISOU 5843  O   GLN B 139    13837  13750  18949    250  -1399   2838       O  
ATOM   5844  CB  GLN B 139      51.995  70.163  33.769  1.00121.94           C  
ANISOU 5844  CB  GLN B 139    13598  13595  19137    264  -1581   3569       C  
ATOM   5845  CG  GLN B 139      51.057  71.247  33.269  1.00121.49           C  
ANISOU 5845  CG  GLN B 139    13467  13363  19331    304  -1687   3927       C  
ATOM   5846  CD  GLN B 139      51.761  72.579  33.090  1.00120.12           C  
ANISOU 5846  CD  GLN B 139    13240  12977  19422    177  -1722   4292       C  
ATOM   5847  NE2 GLN B 139      53.040  72.530  32.736  1.00116.93           N  
ANISOU 5847  NE2 GLN B 139    12803  12788  18837     32  -1676   4389       N  
ATOM   5848  OE1 GLN B 139      51.165  73.640  33.275  1.00121.13           O  
ANISOU 5848  OE1 GLN B 139    13349  12746  19930    208  -1793   4483       O  
ATOM   5849  N   TRP B 140      52.116  66.562  34.504  1.00116.20           N  
ANISOU 5849  N   TRP B 140    12987  13408  17754    403  -1427   2610       N  
ATOM   5850  CA  TRP B 140      52.942  65.564  35.175  1.00112.82           C  
ANISOU 5850  CA  TRP B 140    12624  13048  17194    381  -1340   2274       C  
ATOM   5851  C   TRP B 140      54.420  65.676  34.812  1.00111.77           C  
ANISOU 5851  C   TRP B 140    12457  13105  16904    240  -1296   2365       C  
ATOM   5852  O   TRP B 140      55.277  65.129  35.504  1.00107.57           O  
ANISOU 5852  O   TRP B 140    11986  12558  16329    204  -1222   2126       O  
ATOM   5853  CB  TRP B 140      52.423  64.154  34.887  1.00108.94           C  
ANISOU 5853  CB  TRP B 140    12104  12830  16457    471  -1342   2020       C  
ATOM   5854  CG  TRP B 140      51.117  63.866  35.557  1.00104.36           C  
ANISOU 5854  CG  TRP B 140    11575  12033  16045    603  -1362   1853       C  
ATOM   5855  CD1 TRP B 140      49.871  64.135  35.072  1.00102.42           C  
ANISOU 5855  CD1 TRP B 140    11281  11779  15854    689  -1438   1984       C  
ATOM   5856  CD2 TRP B 140      50.927  63.261  36.842  1.00 99.36           C  
ANISOU 5856  CD2 TRP B 140    11039  11176  15539    660  -1306   1536       C  
ATOM   5857  CE2 TRP B 140      49.538  63.192  37.069  1.00 95.97           C  
ANISOU 5857  CE2 TRP B 140    10613  10617  15235    778  -1349   1489       C  
ATOM   5858  CE3 TRP B 140      51.796  62.769  37.821  1.00 93.80           C  
ANISOU 5858  CE3 TRP B 140    10408  10387  14846    623  -1225   1300       C  
ATOM   5859  NE1 TRP B 140      48.916  63.732  35.974  1.00 99.60           N  
ANISOU 5859  NE1 TRP B 140    10986  11205  15652    795  -1430   1758       N  
ATOM   5860  CZ2 TRP B 140      48.999  62.651  38.234  1.00 86.69           C  
ANISOU 5860  CZ2 TRP B 140     9506   9243  14191    853  -1311   1223       C  
ATOM   5861  CZ3 TRP B 140      51.258  62.233  38.977  1.00 87.41           C  
ANISOU 5861  CZ3 TRP B 140     9665   9383  14166    700  -1190   1046       C  
ATOM   5862  CH2 TRP B 140      49.872  62.178  39.173  1.00 82.97           C  
ANISOU 5862  CH2 TRP B 140     9099   8706  13721    811  -1232   1013       C  
ATOM   5863  N   ARG B 141      54.712  66.392  33.732  1.00115.05           N  
ANISOU 5863  N   ARG B 141    12768  13711  17235    158  -1342   2724       N  
ATOM   5864  CA  ARG B 141      56.090  66.596  33.297  1.00118.18           C  
ANISOU 5864  CA  ARG B 141    13112  14313  17480     14  -1305   2856       C  
ATOM   5865  C   ARG B 141      56.958  67.142  34.432  1.00113.54           C  
ANISOU 5865  C   ARG B 141    12626  13377  17138    -63  -1242   2768       C  
ATOM   5866  O   ARG B 141      58.178  66.976  34.431  1.00111.88           O  
ANISOU 5866  O   ARG B 141    12404  13309  16797   -166  -1186   2731       O  
ATOM   5867  CB  ARG B 141      56.129  67.533  32.086  1.00129.05           C  
ANISOU 5867  CB  ARG B 141    14351  15877  18803    -67  -1373   3323       C  
ATOM   5868  CG  ARG B 141      57.526  67.939  31.644  1.00138.95           C  
ANISOU 5868  CG  ARG B 141    15537  17321  19937   -231  -1339   3521       C  
ATOM   5869  CD  ARG B 141      57.522  68.482  30.222  1.00148.84           C  
ANISOU 5869  CD  ARG B 141    16614  18932  21006   -300  -1405   3963       C  
ATOM   5870  NE  ARG B 141      57.385  67.416  29.233  1.00158.03           N  
ANISOU 5870  NE  ARG B 141    17664  20639  21741   -253  -1415   3862       N  
ATOM   5871  CZ  ARG B 141      56.228  67.024  28.707  1.00164.79           C  
ANISOU 5871  CZ  ARG B 141    18470  21645  22499   -136  -1477   3848       C  
ATOM   5872  NH1 ARG B 141      55.097  67.613  29.071  1.00168.65           N1+
ANISOU 5872  NH1 ARG B 141    19015  21780  23284    -53  -1534   3945       N1+
ATOM   5873  NH2 ARG B 141      56.203  66.043  27.814  1.00164.87           N  
ANISOU 5873  NH2 ARG B 141    18360  22162  22119   -101  -1485   3723       N  
ATOM   5874  N   ASP B 142      56.316  67.782  35.403  1.00111.15           N  
ANISOU 5874  N   ASP B 142    12411  12635  17188     -8  -1252   2715       N  
ATOM   5875  CA  ASP B 142      57.016  68.360  36.544  1.00112.12           C  
ANISOU 5875  CA  ASP B 142    12619  12414  17569    -68  -1200   2604       C  
ATOM   5876  C   ASP B 142      57.175  67.341  37.669  1.00115.33           C  
ANISOU 5876  C   ASP B 142    13124  12768  17928     -6  -1123   2175       C  
ATOM   5877  O   ASP B 142      58.222  67.270  38.313  1.00119.93           O  
ANISOU 5877  O   ASP B 142    13747  13307  18513    -81  -1058   2036       O  
ATOM   5878  CB  ASP B 142      56.266  69.597  37.049  1.00110.25           C  
ANISOU 5878  CB  ASP B 142    12404  11737  17750    -36  -1254   2738       C  
ATOM   5879  CG  ASP B 142      56.940  70.248  38.243  1.00106.52           C  
ANISOU 5879  CG  ASP B 142    12001  10907  17564    -93  -1208   2594       C  
ATOM   5880  OD1 ASP B 142      57.031  69.602  39.308  1.00104.79           O  
ANISOU 5880  OD1 ASP B 142    11866  10611  17339    -43  -1143   2238       O  
ATOM   5881  OD2 ASP B 142      57.367  71.415  38.121  1.00105.30           O1-
ANISOU 5881  OD2 ASP B 142    11805  10551  17653   -190  -1241   2842       O1-
ATOM   5882  N   ILE B 143      56.131  66.551  37.897  1.00111.64           N  
ANISOU 5882  N   ILE B 143    12685  12314  17418    127  -1135   1980       N  
ATOM   5883  CA  ILE B 143      56.120  65.590  38.995  1.00110.29           C  
ANISOU 5883  CA  ILE B 143    12595  12081  17231    193  -1072   1607       C  
ATOM   5884  C   ILE B 143      56.939  64.341  38.683  1.00104.81           C  
ANISOU 5884  C   ILE B 143    11879  11727  16219    167  -1026   1439       C  
ATOM   5885  O   ILE B 143      57.631  63.809  39.550  1.00 96.44           O  
ANISOU 5885  O   ILE B 143    10870  10627  15144    151   -960   1206       O  
ATOM   5886  CB  ILE B 143      54.683  65.166  39.345  1.00113.10           C  
ANISOU 5886  CB  ILE B 143    12974  12333  17667    339  -1103   1474       C  
ATOM   5887  CG1 ILE B 143      53.796  66.398  39.522  1.00121.59           C  
ANISOU 5887  CG1 ILE B 143    14052  13093  19055    378  -1160   1645       C  
ATOM   5888  CG2 ILE B 143      54.669  64.304  40.599  1.00109.11           C  
ANISOU 5888  CG2 ILE B 143    12540  11733  17182    396  -1038   1127       C  
ATOM   5889  CD1 ILE B 143      52.336  66.072  39.719  1.00126.11           C  
ANISOU 5889  CD1 ILE B 143    14630  13590  19698    520  -1198   1552       C  
ATOM   5890  N   VAL B 144      56.855  63.880  37.441  1.00109.37           N  
ANISOU 5890  N   VAL B 144    12363  12648  16544    167  -1065   1552       N  
ATOM   5891  CA  VAL B 144      57.512  62.643  37.037  1.00110.68           C  
ANISOU 5891  CA  VAL B 144    12484  13153  16415    161  -1035   1367       C  
ATOM   5892  C   VAL B 144      58.864  62.916  36.381  1.00120.27           C  
ANISOU 5892  C   VAL B 144    13634  14606  17456     28  -1009   1509       C  
ATOM   5893  O   VAL B 144      59.083  63.984  35.809  1.00124.16           O  
ANISOU 5893  O   VAL B 144    14081  15099  17994    -56  -1036   1821       O  
ATOM   5894  CB  VAL B 144      56.625  61.840  36.063  1.00102.76           C  
ANISOU 5894  CB  VAL B 144    11395  12431  15219    249  -1094   1343       C  
ATOM   5895  CG1 VAL B 144      57.158  60.429  35.893  1.00101.01           C  
ANISOU 5895  CG1 VAL B 144    11130  12486  14764    271  -1067   1064       C  
ATOM   5896  CG2 VAL B 144      55.193  61.806  36.564  1.00101.27           C  
ANISOU 5896  CG2 VAL B 144    11254  12006  15218    370  -1131   1278       C  
ATOM   5897  N   SER B 145      59.771  61.948  36.479  1.00120.84           N  
ANISOU 5897  N   SER B 145    13693  14878  17344      8   -959   1287       N  
ATOM   5898  CA  SER B 145      61.062  62.037  35.808  1.00123.68           C  
ANISOU 5898  CA  SER B 145    13974  15520  17498   -110   -931   1385       C  
ATOM   5899  C   SER B 145      60.882  61.821  34.311  1.00128.33           C  
ANISOU 5899  C   SER B 145    14417  16536  17808   -112   -985   1538       C  
ATOM   5900  O   SER B 145      59.953  61.136  33.883  1.00132.43           O  
ANISOU 5900  O   SER B 145    14895  17181  18242     -9  -1030   1439       O  
ATOM   5901  CB  SER B 145      62.033  61.001  36.373  1.00129.33           C  
ANISOU 5901  CB  SER B 145    14710  16326  18106   -114   -867   1077       C  
ATOM   5902  OG  SER B 145      63.230  60.960  35.616  1.00137.02           O  
ANISOU 5902  OG  SER B 145    15587  17628  18847   -215   -844   1147       O  
ATOM   5903  N   SER B 146      61.774  62.404  33.516  1.00127.92           N  
ANISOU 5903  N   SER B 146    14270  16724  17607   -233   -980   1778       N  
ATOM   5904  CA  SER B 146      61.671  62.316  32.064  1.00127.59           C  
ANISOU 5904  CA  SER B 146    14065  17138  17276   -249  -1029   1959       C  
ATOM   5905  C   SER B 146      62.045  60.930  31.547  1.00130.62           C  
ANISOU 5905  C   SER B 146    14354  17925  17352   -197  -1018   1653       C  
ATOM   5906  O   SER B 146      61.653  60.545  30.446  1.00136.66           O  
ANISOU 5906  O   SER B 146    14980  19071  17875   -161  -1067   1684       O  
ATOM   5907  CB  SER B 146      62.550  63.376  31.402  1.00123.34           C  
ANISOU 5907  CB  SER B 146    13439  16753  16672   -404  -1025   2331       C  
ATOM   5908  OG  SER B 146      63.900  63.228  31.799  1.00123.87           O  
ANISOU 5908  OG  SER B 146    13518  16863  16684   -497   -952   2220       O  
ATOM   5909  N   ASP B 147      62.803  60.185  32.345  1.00125.99           N  
ANISOU 5909  N   ASP B 147    13830  17257  16785   -191   -957   1352       N  
ATOM   5910  CA  ASP B 147      63.237  58.849  31.952  1.00127.51           C  
ANISOU 5910  CA  ASP B 147    13929  17784  16736   -139   -949   1034       C  
ATOM   5911  C   ASP B 147      62.065  57.879  31.859  1.00130.62           C  
ANISOU 5911  C   ASP B 147    14309  18184  17136      7  -1003    803       C  
ATOM   5912  O   ASP B 147      62.126  56.889  31.130  1.00135.88           O  
ANISOU 5912  O   ASP B 147    14847  19198  17584     60  -1028    592       O  
ATOM   5913  CB  ASP B 147      64.279  58.313  32.934  1.00127.74           C  
ANISOU 5913  CB  ASP B 147    14032  17672  16830   -160   -878    782       C  
ATOM   5914  CG  ASP B 147      65.556  59.125  32.928  1.00135.88           C  
ANISOU 5914  CG  ASP B 147    15050  18760  17817   -308   -825    970       C  
ATOM   5915  OD1 ASP B 147      65.606  60.149  32.214  1.00139.26           O  
ANISOU 5915  OD1 ASP B 147    15417  19303  18193   -399   -844   1316       O  
ATOM   5916  OD2 ASP B 147      66.509  58.738  33.637  1.00138.56           O1-
ANISOU 5916  OD2 ASP B 147    15433  19032  18181   -336   -768    784       O1-
ATOM   5917  N   PHE B 148      60.998  58.170  32.596  1.00125.83           N  
ANISOU 5917  N   PHE B 148    13822  17197  16790     72  -1022    830       N  
ATOM   5918  CA  PHE B 148      59.840  57.286  32.643  1.00121.92           C  
ANISOU 5918  CA  PHE B 148    13324  16659  16341    204  -1070    619       C  
ATOM   5919  C   PHE B 148      58.640  57.886  31.924  1.00124.46           C  
ANISOU 5919  C   PHE B 148    13602  17027  16660    243  -1141    851       C  
ATOM   5920  O   PHE B 148      57.602  57.239  31.784  1.00124.74           O  
ANISOU 5920  O   PHE B 148    13612  17072  16712    347  -1191    709       O  
ATOM   5921  CB  PHE B 148      59.473  56.968  34.093  1.00116.88           C  
ANISOU 5921  CB  PHE B 148    12840  15580  15989    263  -1038    434       C  
ATOM   5922  CG  PHE B 148      60.598  56.363  34.881  1.00113.18           C  
ANISOU 5922  CG  PHE B 148    12413  15052  15539    233   -972    217       C  
ATOM   5923  CD1 PHE B 148      61.365  57.143  35.728  1.00113.61           C  
ANISOU 5923  CD1 PHE B 148    12567  14878  15721    148   -911    316       C  
ATOM   5924  CD2 PHE B 148      60.890  55.014  34.770  1.00110.15           C  
ANISOU 5924  CD2 PHE B 148    11956  14839  15057    291   -978    -91       C  
ATOM   5925  CE1 PHE B 148      62.401  56.589  36.452  1.00115.27           C  
ANISOU 5925  CE1 PHE B 148    12807  15051  15938    122   -853    123       C  
ATOM   5926  CE2 PHE B 148      61.923  54.454  35.490  1.00110.81           C  
ANISOU 5926  CE2 PHE B 148    12069  14867  15168    269   -924   -276       C  
ATOM   5927  CZ  PHE B 148      62.680  55.242  36.333  1.00115.78           C  
ANISOU 5927  CZ  PHE B 148    12801  15288  15901    184   -860   -163       C  
ATOM   5928  N   LEU B 149      58.790  59.126  31.469  1.00126.47           N  
ANISOU 5928  N   LEU B 149    13838  17308  16907    155  -1150   1218       N  
ATOM   5929  CA  LEU B 149      57.708  59.835  30.796  1.00125.29           C  
ANISOU 5929  CA  LEU B 149    13641  17190  16775    184  -1222   1492       C  
ATOM   5930  C   LEU B 149      57.182  59.027  29.615  1.00123.92           C  
ANISOU 5930  C   LEU B 149    13301  17464  16319    252  -1284   1396       C  
ATOM   5931  O   LEU B 149      55.997  59.085  29.288  1.00123.61           O  
ANISOU 5931  O   LEU B 149    13235  17417  16313    330  -1347   1458       O  
ATOM   5932  CB  LEU B 149      58.185  61.215  30.337  1.00128.37           C  
ANISOU 5932  CB  LEU B 149    13997  17603  17173     62  -1226   1921       C  
ATOM   5933  CG  LEU B 149      57.116  62.239  29.943  1.00138.50           C  
ANISOU 5933  CG  LEU B 149    15265  18772  18589     81  -1297   2266       C  
ATOM   5934  CD1 LEU B 149      57.626  63.656  30.161  1.00137.56           C  
ANISOU 5934  CD1 LEU B 149    15183  18412  18671    -37  -1287   2629       C  
ATOM   5935  CD2 LEU B 149      56.658  62.041  28.504  1.00147.11           C  
ANISOU 5935  CD2 LEU B 149    16167  20357  19372    103  -1367   2409       C  
ATOM   5936  N   SER B 150      58.071  58.265  28.987  1.00124.82           N  
ANISOU 5936  N   SER B 150    13293  17977  16156    225  -1266   1225       N  
ATOM   5937  CA  SER B 150      57.709  57.442  27.839  1.00127.97           C  
ANISOU 5937  CA  SER B 150    13507  18849  16267    286  -1324   1082       C  
ATOM   5938  C   SER B 150      56.798  56.279  28.226  1.00123.57           C  
ANISOU 5938  C   SER B 150    12973  18163  15814    421  -1357    714       C  
ATOM   5939  O   SER B 150      55.864  55.949  27.497  1.00119.61           O  
ANISOU 5939  O   SER B 150    12365  17870  15210    495  -1426    676       O  
ATOM   5940  CB  SER B 150      58.968  56.914  27.148  1.00137.90           C  
ANISOU 5940  CB  SER B 150    14617  20559  17217    226  -1294    953       C  
ATOM   5941  OG  SER B 150      59.824  56.269  28.075  1.00141.42           O  
ANISOU 5941  OG  SER B 150    15156  20801  17775    221  -1229    672       O  
ATOM   5942  N   ASN B 151      57.075  55.659  29.369  1.00127.58           N  
ANISOU 5942  N   ASN B 151    13609  18338  16530    448  -1308    454       N  
ATOM   5943  CA  ASN B 151      56.281  54.524  29.833  1.00133.32           C  
ANISOU 5943  CA  ASN B 151    14354  18911  17389    563  -1337    120       C  
ATOM   5944  C   ASN B 151      54.979  54.931  30.515  1.00125.78           C  
ANISOU 5944  C   ASN B 151    13519  17572  16699    626  -1361    220       C  
ATOM   5945  O   ASN B 151      54.233  54.080  31.000  1.00121.55           O  
ANISOU 5945  O   ASN B 151    13007  16871  16305    714  -1383    -18       O  
ATOM   5946  CB  ASN B 151      57.099  53.632  30.770  1.00147.74           C  
ANISOU 5946  CB  ASN B 151    16246  20559  19331    568  -1281   -182       C  
ATOM   5947  CG  ASN B 151      57.907  52.588  30.025  1.00169.81           C  
ANISOU 5947  CG  ASN B 151    18875  23749  21897    578  -1293   -464       C  
ATOM   5948  ND2 ASN B 151      58.537  51.684  30.771  1.00195.28           N  
ANISOU 5948  ND2 ASN B 151    22135  26826  25235    598  -1260   -743       N  
ATOM   5949  OD1 ASN B 151      57.968  52.595  28.796  1.00167.02           O  
ANISOU 5949  OD1 ASN B 151    18353  23840  21268    570  -1333   -432       O  
ATOM   5950  N   MET B 152      54.709  56.231  30.554  1.00124.49           N  
ANISOU 5950  N   MET B 152    13421  17265  16615    579  -1360    573       N  
ATOM   5951  CA  MET B 152      53.488  56.729  31.178  1.00121.61           C  
ANISOU 5951  CA  MET B 152    13159  16545  16503    640  -1385    677       C  
ATOM   5952  C   MET B 152      52.270  56.543  30.285  1.00127.53           C  
ANISOU 5952  C   MET B 152    13797  17498  17160    722  -1471    707       C  
ATOM   5953  O   MET B 152      52.262  56.962  29.128  1.00133.70           O  
ANISOU 5953  O   MET B 152    14448  18633  17719    695  -1516    908       O  
ATOM   5954  CB  MET B 152      53.626  58.203  31.558  1.00116.80           C  
ANISOU 5954  CB  MET B 152    12646  15679  16052    569  -1362   1026       C  
ATOM   5955  CG  MET B 152      54.357  58.436  32.862  1.00116.21           C  
ANISOU 5955  CG  MET B 152    12721  15243  16189    522  -1282    957       C  
ATOM   5956  SD  MET B 152      53.822  59.960  33.652  1.00127.48           S  
ANISOU 5956  SD  MET B 152    14275  16222  17941    504  -1279   1243       S  
ATOM   5957  CE  MET B 152      54.118  61.135  32.336  1.00155.43           C  
ANISOU 5957  CE  MET B 152    17700  20020  21335    412  -1326   1678       C  
ATOM   5958  N   SER B 153      51.239  55.911  30.835  1.00128.59           N  
ANISOU 5958  N   SER B 153    13972  17424  17461    819  -1495    515       N  
ATOM   5959  CA  SER B 153      49.981  55.740  30.125  1.00134.69           C  
ANISOU 5959  CA  SER B 153    14650  18343  18184    901  -1578    529       C  
ATOM   5960  C   SER B 153      48.827  56.215  30.997  1.00126.65           C  
ANISOU 5960  C   SER B 153    13750  16917  17454    964  -1587    609       C  
ATOM   5961  O   SER B 153      48.620  55.707  32.099  1.00119.26           O  
ANISOU 5961  O   SER B 153    12913  15674  16725    999  -1550    414       O  
ATOM   5962  CB  SER B 153      49.778  54.278  29.722  1.00142.22           C  
ANISOU 5962  CB  SER B 153    15483  19527  19027    967  -1615    158       C  
ATOM   5963  OG  SER B 153      49.684  53.439  30.859  1.00142.72           O  
ANISOU 5963  OG  SER B 153    15641  19267  19318   1006  -1581   -108       O  
ATOM   5964  N   MET B 154      48.080  57.195  30.504  1.00129.50           N  
ANISOU 5964  N   MET B 154    14087  17290  17828    978  -1637    904       N  
ATOM   5965  CA  MET B 154      46.970  57.745  31.267  1.00132.62           C  
ANISOU 5965  CA  MET B 154    14579  17315  18496   1042  -1650    990       C  
ATOM   5966  C   MET B 154      46.031  58.595  30.417  1.00138.40           C  
ANISOU 5966  C   MET B 154    15232  18158  19196   1078  -1730   1286       C  
ATOM   5967  O   MET B 154      46.469  59.462  29.661  1.00141.30           O  
ANISOU 5967  O   MET B 154    15541  18698  19448   1015  -1750   1588       O  
ATOM   5968  CB  MET B 154      47.495  58.559  32.450  1.00127.65           C  
ANISOU 5968  CB  MET B 154    14108  16283  18110    993  -1578   1078       C  
ATOM   5969  CG  MET B 154      48.532  59.599  32.075  1.00123.08           C  
ANISOU 5969  CG  MET B 154    13529  15765  17471    885  -1557   1360       C  
ATOM   5970  SD  MET B 154      49.414  60.217  33.519  1.00122.85           S  
ANISOU 5970  SD  MET B 154    13669  15309  17699    818  -1464   1342       S  
ATOM   5971  CE  MET B 154      48.064  60.895  34.476  1.00136.79           C  
ANISOU 5971  CE  MET B 154    15525  16643  19806    912  -1484   1382       C  
ATOM   5972  N   ASP B 155      44.736  58.329  30.550  1.00139.85           N  
ANISOU 5972  N   ASP B 155    15405  18246  19487   1177  -1778   1211       N  
ATOM   5973  CA  ASP B 155      43.709  59.115  29.878  1.00148.74           C  
ANISOU 5973  CA  ASP B 155    16461  19432  20620   1227  -1858   1480       C  
ATOM   5974  C   ASP B 155      42.494  59.282  30.787  1.00143.00           C  
ANISOU 5974  C   ASP B 155    15818  18333  20181   1320  -1868   1431       C  
ATOM   5975  O   ASP B 155      42.072  58.338  31.456  1.00135.15           O  
ANISOU 5975  O   ASP B 155    14858  17225  19269   1370  -1847   1137       O  
ATOM   5976  CB  ASP B 155      43.310  58.474  28.545  1.00158.42           C  
ANISOU 5976  CB  ASP B 155    17501  21143  21548   1259  -1934   1439       C  
ATOM   5977  CG  ASP B 155      42.866  57.032  28.697  1.00162.93           C  
ANISOU 5977  CG  ASP B 155    18031  21785  22089   1323  -1942   1032       C  
ATOM   5978  OD1 ASP B 155      42.328  56.473  27.718  1.00167.69           O  
ANISOU 5978  OD1 ASP B 155    18478  22742  22496   1367  -2013    951       O  
ATOM   5979  OD2 ASP B 155      43.054  56.456  29.789  1.00161.59           O1-
ANISOU 5979  OD2 ASP B 155    17973  21323  22100   1328  -1882    798       O1-
ATOM   5980  N   PHE B 156      41.941  60.490  30.811  1.00143.10           N  
ANISOU 5980  N   PHE B 156    15853  18161  20358   1341  -1902   1727       N  
ATOM   5981  CA  PHE B 156      40.847  60.811  31.718  1.00143.89           C  
ANISOU 5981  CA  PHE B 156    16028  17897  20745   1429  -1908   1694       C  
ATOM   5982  C   PHE B 156      39.518  60.926  30.983  1.00156.27           C  
ANISOU 5982  C   PHE B 156    17488  19599  22286   1522  -2004   1806       C  
ATOM   5983  O   PHE B 156      39.476  60.941  29.753  1.00158.87           O  
ANISOU 5983  O   PHE B 156    17685  20296  22381   1513  -2068   1959       O  
ATOM   5984  CB  PHE B 156      41.138  62.117  32.460  1.00137.86           C  
ANISOU 5984  CB  PHE B 156    15368  16762  20251   1400  -1880   1901       C  
ATOM   5985  CG  PHE B 156      42.486  62.152  33.125  1.00131.21           C  
ANISOU 5985  CG  PHE B 156    14621  15802  19433   1301  -1791   1824       C  
ATOM   5986  CD1 PHE B 156      43.608  62.565  32.426  1.00130.68           C  
ANISOU 5986  CD1 PHE B 156    14517  15923  19212   1196  -1785   2019       C  
ATOM   5987  CD2 PHE B 156      42.630  61.779  34.451  1.00123.85           C  
ANISOU 5987  CD2 PHE B 156    13802  14589  18667   1311  -1716   1567       C  
ATOM   5988  CE1 PHE B 156      44.847  62.600  33.035  1.00125.34           C  
ANISOU 5988  CE1 PHE B 156    13922  15143  18557   1104  -1705   1945       C  
ATOM   5989  CE2 PHE B 156      43.866  61.812  35.065  1.00116.89           C  
ANISOU 5989  CE2 PHE B 156    12999  13613  17799   1223  -1638   1496       C  
ATOM   5990  CZ  PHE B 156      44.975  62.224  34.356  1.00119.85           C  
ANISOU 5990  CZ  PHE B 156    13344  14163  18031   1120  -1632   1679       C  
ATOM   5991  N   GLN B 157      38.436  61.007  31.751  1.00167.86           N  
ANISOU 5991  N   GLN B 157    19003  20790  23985   1612  -2012   1726       N  
ATOM   5992  CA  GLN B 157      37.102  61.210  31.197  1.00183.95           C  
ANISOU 5992  CA  GLN B 157    20949  22904  26042   1708  -2100   1834       C  
ATOM   5993  C   GLN B 157      36.234  61.998  32.172  1.00199.22           C  
ANISOU 5993  C   GLN B 157    22960  24427  28309   1785  -2099   1881       C  
ATOM   5994  O   GLN B 157      36.454  61.960  33.382  1.00203.15           O  
ANISOU 5994  O   GLN B 157    23570  24624  28993   1781  -2025   1712       O  
ATOM   5995  CB  GLN B 157      36.441  59.871  30.861  1.00181.96           C  
ANISOU 5995  CB  GLN B 157    20611  22895  25633   1759  -2128   1554       C  
ATOM   5996  CG  GLN B 157      36.999  59.195  29.618  1.00184.06           C  
ANISOU 5996  CG  GLN B 157    20744  23634  25556   1712  -2163   1522       C  
ATOM   5997  CD  GLN B 157      36.820  60.034  28.366  1.00188.28           C  
ANISOU 5997  CD  GLN B 157    21153  24457  25927   1711  -2246   1873       C  
ATOM   5998  NE2 GLN B 157      37.660  59.792  27.366  1.00188.88           N  
ANISOU 5998  NE2 GLN B 157    21125  24936  25704   1643  -2258   1920       N  
ATOM   5999  OE1 GLN B 157      35.936  60.887  28.297  1.00190.63           O  
ANISOU 5999  OE1 GLN B 157    21435  24630  26367   1774  -2301   2104       O  
ATOM   6000  N   ASN B 158      35.250  62.715  31.639  1.00209.91           N  
ANISOU 6000  N   ASN B 158    24237  25787  29731   1859  -2184   2106       N  
ATOM   6001  CA  ASN B 158      34.366  63.527  32.465  1.00221.14           C  
ANISOU 6001  CA  ASN B 158    25708  26838  31476   1945  -2196   2154       C  
ATOM   6002  C   ASN B 158      32.906  63.118  32.302  1.00224.89           C  
ANISOU 6002  C   ASN B 158    26103  27379  31964   2060  -2257   2073       C  
ATOM   6003  O   ASN B 158      32.059  63.934  31.939  1.00230.25           O  
ANISOU 6003  O   ASN B 158    26720  28005  32759   2135  -2334   2294       O  
ATOM   6004  CB  ASN B 158      34.539  65.011  32.131  1.00233.19           C  
ANISOU 6004  CB  ASN B 158    27221  28213  33167   1934  -2246   2533       C  
ATOM   6005  CG  ASN B 158      33.826  65.919  33.114  1.00242.08           C  
ANISOU 6005  CG  ASN B 158    28401  28909  34669   2018  -2250   2544       C  
ATOM   6006  ND2 ASN B 158      33.426  67.097  32.649  1.00245.70           N  
ANISOU 6006  ND2 ASN B 158    28799  29256  35300   2057  -2333   2871       N  
ATOM   6007  OD1 ASN B 158      33.640  65.567  34.279  1.00244.80           O  
ANISOU 6007  OD1 ASN B 158    28827  29034  35152   2049  -2182   2263       O  
ATOM   6008  N   HIS B 159      32.616  61.850  32.573  1.00222.00           N  
ANISOU 6008  N   HIS B 159    25730  27124  31495   2073  -2227   1761       N  
ATOM   6009  CA  HIS B 159      31.259  61.336  32.436  1.00221.09           C  
ANISOU 6009  CA  HIS B 159    25532  27086  31388   2172  -2282   1656       C  
ATOM   6010  C   HIS B 159      30.429  61.658  33.676  1.00213.90           C  
ANISOU 6010  C   HIS B 159    24685  25814  30772   2251  -2250   1553       C  
ATOM   6011  O   HIS B 159      29.404  61.028  33.932  1.00213.35           O  
ANISOU 6011  O   HIS B 159    24569  25758  30735   2319  -2265   1387       O  
ATOM   6012  CB  HIS B 159      31.277  59.827  32.184  1.00224.52           C  
ANISOU 6012  CB  HIS B 159    25913  27779  31617   2148  -2272   1366       C  
ATOM   6013  CG  HIS B 159      30.042  59.313  31.511  1.00231.00           C  
ANISOU 6013  CG  HIS B 159    26600  28813  32358   2227  -2356   1315       C  
ATOM   6014  CD2 HIS B 159      29.751  59.131  30.202  1.00235.08           C  
ANISOU 6014  CD2 HIS B 159    26973  29705  32643   2241  -2443   1405       C  
ATOM   6015  ND1 HIS B 159      28.922  58.917  32.212  1.00232.93           N  
ANISOU 6015  ND1 HIS B 159    26837  28904  32763   2303  -2356   1150       N  
ATOM   6016  CE1 HIS B 159      27.995  58.514  31.362  1.00234.93           C  
ANISOU 6016  CE1 HIS B 159    26954  29409  32901   2358  -2441   1138       C  
ATOM   6017  NE2 HIS B 159      28.472  58.633  30.136  1.00236.58           N  
ANISOU 6017  NE2 HIS B 159    27076  29946  32867   2324  -2496   1284       N  
ATOM   6018  N   LEU B 160      30.884  62.645  34.441  1.00206.80           N  
ANISOU 6018  N   LEU B 160    23879  24607  30089   2240  -2208   1643       N  
ATOM   6019  CA  LEU B 160      30.180  63.074  35.643  1.00196.12           C  
ANISOU 6019  CA  LEU B 160    22574  22926  29018   2317  -2176   1536       C  
ATOM   6020  C   LEU B 160      29.597  64.469  35.446  1.00184.58           C  
ANISOU 6020  C   LEU B 160    21077  21278  27777   2394  -2249   1798       C  
ATOM   6021  O   LEU B 160      28.433  64.717  35.758  1.00181.90           O  
ANISOU 6021  O   LEU B 160    20692  20827  27595   2502  -2284   1769       O  
ATOM   6022  CB  LEU B 160      31.123  63.056  36.849  1.00195.27           C  
ANISOU 6022  CB  LEU B 160    22586  22596  29012   2253  -2069   1369       C  
ATOM   6023  CG  LEU B 160      30.497  63.306  38.223  1.00193.19           C  
ANISOU 6023  CG  LEU B 160    22358  22049  28996   2324  -2019   1194       C  
ATOM   6024  CD1 LEU B 160      29.406  62.286  38.516  1.00190.98           C  
ANISOU 6024  CD1 LEU B 160    22019  21870  28676   2385  -2018    995       C  
ATOM   6025  CD2 LEU B 160      31.563  63.283  39.308  1.00189.70           C  
ANISOU 6025  CD2 LEU B 160    22020  21446  28612   2250  -1916   1044       C  
ATOM   6026  N   GLY B 161      30.416  65.378  34.926  1.00178.43           N  
ANISOU 6026  N   GLY B 161    20310  20462  27023   2337  -2273   2061       N  
ATOM   6027  CA  GLY B 161      29.972  66.726  34.623  1.00177.02           C  
ANISOU 6027  CA  GLY B 161    20084  20100  27075   2399  -2355   2353       C  
ATOM   6028  C   GLY B 161      29.989  67.665  35.814  1.00173.56           C  
ANISOU 6028  C   GLY B 161    19713  19236  26996   2438  -2319   2286       C  
ATOM   6029  O   GLY B 161      30.038  68.885  35.649  1.00175.31           O  
ANISOU 6029  O   GLY B 161    19911  19246  27453   2458  -2377   2529       O  
ATOM   6030  N   SER B 162      29.953  67.102  37.017  1.00167.23           N  
ANISOU 6030  N   SER B 162    18980  18315  26245   2448  -2229   1956       N  
ATOM   6031  CA  SER B 162      29.904  67.907  38.232  1.00165.23           C  
ANISOU 6031  CA  SER B 162    18771  17698  26312   2494  -2190   1833       C  
ATOM   6032  C   SER B 162      31.291  68.344  38.698  1.00164.24           C  
ANISOU 6032  C   SER B 162    18735  17418  26250   2385  -2126   1828       C  
ATOM   6033  O   SER B 162      31.490  68.656  39.872  1.00167.52           O  
ANISOU 6033  O   SER B 162    19199  17596  26855   2397  -2064   1626       O  
ATOM   6034  CB  SER B 162      29.187  67.150  39.352  1.00162.57           C  
ANISOU 6034  CB  SER B 162    18443  17335  25991   2557  -2122   1493       C  
ATOM   6035  OG  SER B 162      29.892  65.973  39.703  1.00159.87           O  
ANISOU 6035  OG  SER B 162    18163  17159  25420   2465  -2033   1294       O  
ATOM   6036  N   CYS B 163      32.248  68.363  37.775  1.00156.55           N  
ANISOU 6036  N   CYS B 163    17771  16601  25108   2279  -2142   2044       N  
ATOM   6037  CA  CYS B 163      33.596  68.824  38.086  1.00143.53           C  
ANISOU 6037  CA  CYS B 163    16197  14822  23516   2167  -2090   2075       C  
ATOM   6038  C   CYS B 163      33.657  70.346  38.043  1.00140.14           C  
ANISOU 6038  C   CYS B 163    15738  14077  23433   2186  -2156   2312       C  
ATOM   6039  O   CYS B 163      33.025  70.975  37.196  1.00143.24           O  
ANISOU 6039  O   CYS B 163    16043  14470  23912   2240  -2259   2594       O  
ATOM   6040  CB  CYS B 163      34.610  68.228  37.108  1.00137.55           C  
ANISOU 6040  CB  CYS B 163    15448  14379  22437   2043  -2079   2209       C  
ATOM   6041  SG  CYS B 163      34.768  66.430  37.197  1.00331.30           S  
ANISOU 6041  SG  CYS B 163    40016  39250  46615   2008  -2003   1905       S  
ATOM   6042  N   GLN B 164      34.418  70.934  38.961  1.00135.78           N  
ANISOU 6042  N   GLN B 164    15246  13252  23091   2142  -2103   2199       N  
ATOM   6043  CA  GLN B 164      34.551  72.385  39.020  1.00135.85           C  
ANISOU 6043  CA  GLN B 164    15221  12917  23480   2154  -2167   2389       C  
ATOM   6044  C   GLN B 164      35.709  72.879  38.156  1.00131.94           C  
ANISOU 6044  C   GLN B 164    14724  12466  22941   2017  -2193   2715       C  
ATOM   6045  O   GLN B 164      36.379  72.090  37.489  1.00130.59           O  
ANISOU 6045  O   GLN B 164    14576  12620  22424   1921  -2160   2780       O  
ATOM   6046  CB  GLN B 164      34.726  72.850  40.467  1.00137.73           C  
ANISOU 6046  CB  GLN B 164    15500  12830  24000   2182  -2106   2081       C  
ATOM   6047  CG  GLN B 164      33.621  72.385  41.400  1.00138.85           C  
ANISOU 6047  CG  GLN B 164    15627  12952  24175   2312  -2072   1756       C  
ATOM   6048  CD  GLN B 164      33.642  73.104  42.735  1.00143.16           C  
ANISOU 6048  CD  GLN B 164    16172  13176  25044   2363  -2036   1483       C  
ATOM   6049  NE2 GLN B 164      32.933  72.554  43.714  1.00145.15           N  
ANISOU 6049  NE2 GLN B 164    16416  13470  25265   2448  -1977   1159       N  
ATOM   6050  OE1 GLN B 164      34.283  74.145  42.884  1.00142.16           O  
ANISOU 6050  OE1 GLN B 164    16040  12779  25197   2324  -2062   1558       O  
ATOM   6051  N   LYS B 165      35.938  74.187  38.170  1.00130.84           N  
ANISOU 6051  N   LYS B 165    14547  12001  23166   2007  -2255   2915       N  
ATOM   6052  CA  LYS B 165      36.993  74.781  37.358  1.00135.69           C  
ANISOU 6052  CA  LYS B 165    15140  12632  23783   1873  -2288   3265       C  
ATOM   6053  C   LYS B 165      38.183  75.180  38.226  1.00132.14           C  
ANISOU 6053  C   LYS B 165    14762  11950  23495   1772  -2217   3112       C  
ATOM   6054  O   LYS B 165      38.045  75.377  39.433  1.00126.37           O  
ANISOU 6054  O   LYS B 165    14068  10960  22986   1828  -2172   2787       O  
ATOM   6055  CB  LYS B 165      36.456  75.991  36.591  1.00147.18           C  
ANISOU 6055  CB  LYS B 165    16478  13898  25547   1917  -2426   3674       C  
ATOM   6056  CG  LYS B 165      37.231  76.322  35.324  1.00157.47           C  
ANISOU 6056  CG  LYS B 165    17718  15394  26717   1789  -2479   4137       C  
ATOM   6057  CD  LYS B 165      36.513  77.381  34.499  1.00166.12           C  
ANISOU 6057  CD  LYS B 165    18678  16354  28085   1847  -2625   4571       C  
ATOM   6058  CE  LYS B 165      37.179  77.582  33.145  1.00170.51           C  
ANISOU 6058  CE  LYS B 165    19148  17199  28438   1721  -2678   5060       C  
ATOM   6059  NZ  LYS B 165      37.110  76.357  32.300  1.00169.33           N1+
ANISOU 6059  NZ  LYS B 165    18988  17613  27734   1701  -2646   5054       N1+
ATOM   6060  N   CYS B 166      39.353  75.294  37.606  1.00135.68           N  
ANISOU 6060  N   CYS B 166    15217  12516  23820   1622  -2206   3341       N  
ATOM   6061  CA  CYS B 166      40.569  75.629  38.336  1.00138.01           C  
ANISOU 6061  CA  CYS B 166    15575  12626  24238   1511  -2138   3215       C  
ATOM   6062  C   CYS B 166      40.687  77.129  38.583  1.00142.49           C  
ANISOU 6062  C   CYS B 166    16082  12736  25322   1506  -2215   3376       C  
ATOM   6063  O   CYS B 166      40.516  77.935  37.668  1.00141.46           O  
ANISOU 6063  O   CYS B 166    15856  12535  25356   1492  -2321   3788       O  
ATOM   6064  CB  CYS B 166      41.805  75.125  37.585  1.00137.31           C  
ANISOU 6064  CB  CYS B 166    15508  12858  23806   1350  -2093   3383       C  
ATOM   6065  SG  CYS B 166      41.886  73.330  37.394  1.00200.52           S  
ANISOU 6065  SG  CYS B 166    23578  21366  31244   1344  -2000   3136       S  
ATOM   6066  N   ASP B 167      40.975  77.491  39.829  1.00145.31           N  
ANISOU 6066  N   ASP B 167    16481  12790  25940   1518  -2166   3046       N  
ATOM   6067  CA  ASP B 167      41.216  78.881  40.196  1.00149.85           C  
ANISOU 6067  CA  ASP B 167    16996  12906  27035   1505  -2233   3126       C  
ATOM   6068  C   ASP B 167      42.206  79.505  39.219  1.00156.12           C  
ANISOU 6068  C   ASP B 167    17743  13701  27873   1346  -2283   3574       C  
ATOM   6069  O   ASP B 167      43.220  78.894  38.888  1.00157.95           O  
ANISOU 6069  O   ASP B 167    18028  14215  27769   1213  -2212   3624       O  
ATOM   6070  CB  ASP B 167      41.755  78.956  41.627  1.00146.17           C  
ANISOU 6070  CB  ASP B 167    16587  12228  26722   1497  -2146   2676       C  
ATOM   6071  CG  ASP B 167      41.947  80.381  42.112  1.00150.39           C  
ANISOU 6071  CG  ASP B 167    17046  12267  27830   1496  -2219   2684       C  
ATOM   6072  OD1 ASP B 167      41.408  80.718  43.187  1.00152.51           O  
ANISOU 6072  OD1 ASP B 167    17291  12288  28368   1609  -2214   2325       O  
ATOM   6073  OD2 ASP B 167      42.637  81.164  41.427  1.00152.69           O1-
ANISOU 6073  OD2 ASP B 167    17286  12420  28309   1382  -2283   3043       O1-
ATOM   6074  N   PRO B 168      41.906  80.724  38.743  1.00158.79           N  
ANISOU 6074  N   PRO B 168    17971  13730  28633   1359  -2409   3914       N  
ATOM   6075  CA  PRO B 168      42.764  81.427  37.781  1.00160.81           C  
ANISOU 6075  CA  PRO B 168    18154  13970  28976   1207  -2471   4400       C  
ATOM   6076  C   PRO B 168      44.240  81.406  38.176  1.00162.34           C  
ANISOU 6076  C   PRO B 168    18407  14158  29116   1037  -2386   4303       C  
ATOM   6077  O   PRO B 168      45.098  81.227  37.313  1.00167.08           O  
ANISOU 6077  O   PRO B 168    18993  15026  29463    893  -2374   4612       O  
ATOM   6078  CB  PRO B 168      42.225  82.856  37.823  1.00159.32           C  
ANISOU 6078  CB  PRO B 168    17846  13276  29414   1269  -2608   4602       C  
ATOM   6079  CG  PRO B 168      40.786  82.692  38.163  1.00159.74           C  
ANISOU 6079  CG  PRO B 168    17885  13269  29542   1472  -2642   4394       C  
ATOM   6080  CD  PRO B 168      40.701  81.501  39.081  1.00156.29           C  
ANISOU 6080  CD  PRO B 168    17575  13063  28746   1524  -2505   3868       C  
ATOM   6081  N   SER B 169      44.524  81.575  39.464  1.00155.06           N  
ANISOU 6081  N   SER B 169    17540  12961  28415   1057  -2327   3872       N  
ATOM   6082  CA  SER B 169      45.901  81.616  39.950  1.00145.70           C  
ANISOU 6082  CA  SER B 169    16405  11741  27215    904  -2249   3746       C  
ATOM   6083  C   SER B 169      46.657  80.322  39.657  1.00137.40           C  
ANISOU 6083  C   SER B 169    15449  11189  25567    813  -2133   3682       C  
ATOM   6084  O   SER B 169      47.883  80.273  39.764  1.00133.70           O  
ANISOU 6084  O   SER B 169    15011  10778  25010    667  -2073   3673       O  
ATOM   6085  CB  SER B 169      45.934  81.918  41.450  1.00141.40           C  
ANISOU 6085  CB  SER B 169    15891  10866  26970    965  -2204   3240       C  
ATOM   6086  OG  SER B 169      45.248  80.922  42.186  1.00138.43           O  
ANISOU 6086  OG  SER B 169    15592  10683  26321   1092  -2123   2828       O  
ATOM   6087  N   CYS B 170      45.923  79.278  39.292  1.00135.79           N  
ANISOU 6087  N   CYS B 170    15282  11338  24974    901  -2106   3627       N  
ATOM   6088  CA  CYS B 170      46.532  77.999  38.952  1.00134.37           C  
ANISOU 6088  CA  CYS B 170    15175  11631  24246    832  -2008   3555       C  
ATOM   6089  C   CYS B 170      47.301  78.097  37.640  1.00136.78           C  
ANISOU 6089  C   CYS B 170    15418  12202  24349    688  -2040   4015       C  
ATOM   6090  O   CYS B 170      46.735  78.459  36.608  1.00136.77           O  
ANISOU 6090  O   CYS B 170    15323  12283  24363    706  -2134   4401       O  
ATOM   6091  CB  CYS B 170      45.470  76.902  38.860  1.00131.86           C  
ANISOU 6091  CB  CYS B 170    14892  11595  23613    967  -1987   3383       C  
ATOM   6092  SG  CYS B 170      44.557  76.627  40.394  1.00156.63           S  
ANISOU 6092  SG  CYS B 170    18089  14508  26914   1131  -1937   2848       S  
ATOM   6093  N   PRO B 171      48.600  77.773  37.680  1.00137.77           N  
ANISOU 6093  N   PRO B 171    15585  12487  24276    543  -1961   3977       N  
ATOM   6094  CA  PRO B 171      49.480  77.836  36.509  1.00140.75           C  
ANISOU 6094  CA  PRO B 171    15892  13153  24432    390  -1976   4384       C  
ATOM   6095  C   PRO B 171      48.945  76.993  35.357  1.00139.51           C  
ANISOU 6095  C   PRO B 171    15692  13476  23840    430  -1995   4568       C  
ATOM   6096  O   PRO B 171      48.718  75.795  35.529  1.00133.52           O  
ANISOU 6096  O   PRO B 171    15002  12994  22734    494  -1926   4267       O  
ATOM   6097  CB  PRO B 171      50.792  77.243  37.027  1.00141.85           C  
ANISOU 6097  CB  PRO B 171    16112  13431  24352    274  -1859   4137       C  
ATOM   6098  CG  PRO B 171      50.751  77.464  38.501  1.00140.15           C  
ANISOU 6098  CG  PRO B 171    15977  12841  24435    331  -1815   3713       C  
ATOM   6099  CD  PRO B 171      49.313  77.316  38.885  1.00136.65           C  
ANISOU 6099  CD  PRO B 171    15545  12278  24096    517  -1850   3535       C  
ATOM   6100  N   ASN B 172      48.751  77.617  34.199  1.00147.40           N  
ANISOU 6100  N   ASN B 172    16563  14574  24868    390  -2092   5058       N  
ATOM   6101  CA AASN B 172      48.237  76.918  33.027  0.50146.25           C  
ANISOU 6101  CA AASN B 172    16347  14910  24313    424  -2122   5256       C  
ATOM   6102  CA BASN B 172      48.230  76.924  33.027  0.50146.33           C  
ANISOU 6102  CA BASN B 172    16356  14918  24325    425  -2123   5258       C  
ATOM   6103  C   ASN B 172      46.960  76.138  33.340  1.00146.53           C  
ANISOU 6103  C   ASN B 172    16433  14996  24245    605  -2121   4954       C  
ATOM   6104  O   ASN B 172      46.698  75.092  32.745  1.00144.34           O  
ANISOU 6104  O   ASN B 172    16145  15149  23547    639  -2099   4884       O  
ATOM   6105  CB AASN B 172      49.306  75.984  32.453  0.50149.05           C  
ANISOU 6105  CB AASN B 172    16701  15761  24171    307  -2040   5235       C  
ATOM   6106  CB BASN B 172      49.294  76.003  32.424  0.50149.67           C  
ANISOU 6106  CB BASN B 172    16776  15842  24251    307  -2043   5248       C  
ATOM   6107  CG AASN B 172      48.947  75.460  31.075  0.50148.42           C  
ANISOU 6107  CG AASN B 172    16502  16208  23682    315  -2085   5505       C  
ATOM   6108  CG BASN B 172      50.450  76.770  31.811  0.50146.69           C  
ANISOU 6108  CG BASN B 172    16307  15515  23915    123  -2059   5646       C  
ATOM   6109  ND2AASN B 172      49.675  74.447  30.619  0.50146.77           N  
ANISOU 6109  ND2AASN B 172    16289  16465  23011    252  -2014   5388       N  
ATOM   6110  OD1AASN B 172      48.028  75.961  30.427  0.50154.59           O  
ANISOU 6110  OD1AASN B 172    17187  16989  24563    380  -2186   5806       O  
ATOM   6111  ND2BASN B 172      51.496  76.051  31.419  0.50147.36           N  
ANISOU 6111  ND2BASN B 172    16387  16001  23604     14  -1983   5605       N  
ATOM   6112  OD1BASN B 172      50.403  77.994  31.688  0.50147.00           O  
ANISOU 6112  OD1BASN B 172    16270  15234  24350     80  -2143   5988       O  
ATOM   6113  N   GLY B 173      46.174  76.652  34.281  1.00139.81           N  
ANISOU 6113  N   GLY B 173    15626  13709  23787    719  -2146   4762       N  
ATOM   6114  CA  GLY B 173      44.924  76.023  34.670  1.00133.68           C  
ANISOU 6114  CA  GLY B 173    14889  12940  22963    888  -2147   4483       C  
ATOM   6115  C   GLY B 173      45.093  74.637  35.262  1.00124.46           C  
ANISOU 6115  C   GLY B 173    13830  12010  21447    914  -2033   4033       C  
ATOM   6116  O   GLY B 173      44.182  73.811  35.194  1.00121.96           O  
ANISOU 6116  O   GLY B 173    13523  11876  20939   1024  -2031   3868       O  
ATOM   6117  N   SER B 174      46.258  74.383  35.849  1.00116.84           N  
ANISOU 6117  N   SER B 174    12940  11038  20416    810  -1941   3843       N  
ATOM   6118  CA  SER B 174      46.554  73.084  36.444  1.00106.75           C  
ANISOU 6118  CA  SER B 174    11758   9970  18832    822  -1834   3438       C  
ATOM   6119  C   SER B 174      46.193  73.057  37.926  1.00105.20           C  
ANISOU 6119  C   SER B 174    11651   9450  18872    908  -1782   3035       C  
ATOM   6120  O   SER B 174      46.668  73.884  38.704  1.00108.15           O  
ANISOU 6120  O   SER B 174    12045   9488  19557    870  -1770   2973       O  
ATOM   6121  CB  SER B 174      48.033  72.743  36.265  1.00101.88           C  
ANISOU 6121  CB  SER B 174    11164   9562  17985    668  -1762   3446       C  
ATOM   6122  OG  SER B 174      48.402  72.781  34.898  1.00101.38           O  
ANISOU 6122  OG  SER B 174    10998   9838  17682    584  -1806   3816       O  
ATOM   6123  N   CYS B 175      45.355  72.099  38.313  1.00 98.22           N  
ANISOU 6123  N   CYS B 175    10804   8680  17837   1021  -1752   2760       N  
ATOM   6124  CA  CYS B 175      44.928  71.981  39.702  1.00 98.35           C  
ANISOU 6124  CA  CYS B 175    10884   8453  18032   1107  -1700   2384       C  
ATOM   6125  C   CYS B 175      44.466  70.568  40.031  1.00 99.09           C  
ANISOU 6125  C   CYS B 175    11021   8795  17832   1175  -1639   2091       C  
ATOM   6126  O   CYS B 175      43.892  69.880  39.187  1.00101.76           O  
ANISOU 6126  O   CYS B 175    11322   9405  17938   1213  -1671   2175       O  
ATOM   6127  CB  CYS B 175      43.799  72.968  39.998  1.00102.01           C  
ANISOU 6127  CB  CYS B 175    11297   8583  18877   1225  -1779   2429       C  
ATOM   6128  SG  CYS B 175      42.226  72.529  39.229  1.00109.47           S  
ANISOU 6128  SG  CYS B 175    12179   9704  19710   1367  -1856   2534       S  
ATOM   6129  N   TRP B 176      44.712  70.145  41.267  1.00 99.24           N  
ANISOU 6129  N   TRP B 176    11106   8724  17875   1187  -1554   1750       N  
ATOM   6130  CA  TRP B 176      44.301  68.824  41.727  1.00102.12           C  
ANISOU 6130  CA  TRP B 176    11504   9287  18009   1245  -1496   1475       C  
ATOM   6131  C   TRP B 176      42.848  68.827  42.186  1.00106.59           C  
ANISOU 6131  C   TRP B 176    12041   9741  18716   1391  -1527   1358       C  
ATOM   6132  O   TRP B 176      42.181  67.792  42.174  1.00108.69           O  
ANISOU 6132  O   TRP B 176    12302  10194  18799   1452  -1514   1232       O  
ATOM   6133  CB  TRP B 176      45.201  68.354  42.871  1.00101.96           C  
ANISOU 6133  CB  TRP B 176    11552   9246  17944   1192  -1394   1190       C  
ATOM   6134  CG  TRP B 176      46.614  68.106  42.460  1.00101.01           C  
ANISOU 6134  CG  TRP B 176    11459   9283  17637   1055  -1353   1262       C  
ATOM   6135  CD1 TRP B 176      47.647  68.996  42.497  1.00101.44           C  
ANISOU 6135  CD1 TRP B 176    11522   9198  17823    951  -1346   1371       C  
ATOM   6136  CD2 TRP B 176      47.156  66.883  41.948  1.00 97.63           C  
ANISOU 6136  CD2 TRP B 176    11042   9185  16868   1007  -1317   1220       C  
ATOM   6137  CE2 TRP B 176      48.523  67.106  41.697  1.00 96.03           C  
ANISOU 6137  CE2 TRP B 176    10855   9041  16590    878  -1286   1308       C  
ATOM   6138  CE3 TRP B 176      46.617  65.622  41.678  1.00 97.39           C  
ANISOU 6138  CE3 TRP B 176    11000   9397  16607   1062  -1312   1108       C  
ATOM   6139  NE1 TRP B 176      48.798  68.403  42.040  1.00101.52           N  
ANISOU 6139  NE1 TRP B 176    11550   9447  17577    841  -1303   1407       N  
ATOM   6140  CZ2 TRP B 176      49.359  66.114  41.190  1.00 90.07           C  
ANISOU 6140  CZ2 TRP B 176    10103   8589  15530    810  -1248   1277       C  
ATOM   6141  CZ3 TRP B 176      47.449  64.640  41.174  1.00 94.36           C  
ANISOU 6141  CZ3 TRP B 176    10617   9295  15942    994  -1280   1070       C  
ATOM   6142  CH2 TRP B 176      48.804  64.892  40.935  1.00 89.10           C  
ANISOU 6142  CH2 TRP B 176     9964   8691  15198    873  -1248   1150       C  
ATOM   6143  N   GLY B 177      42.364  69.996  42.592  1.00104.76           N  
ANISOU 6143  N   GLY B 177    11779   9197  18827   1448  -1572   1392       N  
ATOM   6144  CA  GLY B 177      41.006  70.130  43.083  1.00102.26           C  
ANISOU 6144  CA  GLY B 177    11423   8757  18675   1591  -1603   1271       C  
ATOM   6145  C   GLY B 177      40.561  71.577  43.150  1.00106.24           C  
ANISOU 6145  C   GLY B 177    11870   8918  19576   1646  -1681   1392       C  
ATOM   6146  O   GLY B 177      41.163  72.448  42.522  1.00112.88           O  
ANISOU 6146  O   GLY B 177    12692   9642  20556   1573  -1733   1654       O  
ATOM   6147  N   ALA B 178      39.507  71.834  43.917  1.00106.24           N  
ANISOU 6147  N   ALA B 178    11832   8758  19775   1775  -1693   1205       N  
ATOM   6148  CA  ALA B 178      38.965  73.182  44.049  1.00110.39           C  
ANISOU 6148  CA  ALA B 178    12289   8939  20717   1850  -1775   1278       C  
ATOM   6149  C   ALA B 178      39.846  74.059  44.935  1.00114.10           C  
ANISOU 6149  C   ALA B 178    12766   9128  21460   1796  -1746   1132       C  
ATOM   6150  O   ALA B 178      40.877  73.614  45.437  1.00116.84           O  
ANISOU 6150  O   ALA B 178    13176   9568  21652   1698  -1661    985       O  
ATOM   6151  CB  ALA B 178      37.547  73.131  44.593  1.00110.64           C  
ANISOU 6151  CB  ALA B 178    12264   8915  20860   2012  -1795   1095       C  
ATOM   6152  N   GLY B 179      39.433  75.309  45.119  1.00116.07           N  
ANISOU 6152  N   GLY B 179    12941   9031  22129   1861  -1824   1165       N  
ATOM   6153  CA  GLY B 179      40.172  76.246  45.947  1.00121.05           C  
ANISOU 6153  CA  GLY B 179    13554   9361  23076   1821  -1814   1007       C  
ATOM   6154  C   GLY B 179      41.489  76.681  45.334  1.00124.85           C  
ANISOU 6154  C   GLY B 179    14065   9791  23580   1657  -1824   1261       C  
ATOM   6155  O   GLY B 179      41.945  76.108  44.344  1.00125.95           O  
ANISOU 6155  O   GLY B 179    14246  10184  23425   1567  -1819   1526       O  
ATOM   6156  N   GLU B 180      42.102  77.701  45.927  1.00127.52           N  
ANISOU 6156  N   GLU B 180    14369   9810  24274   1617  -1839   1167       N  
ATOM   6157  CA  GLU B 180      43.389  78.207  45.459  1.00135.46           C  
ANISOU 6157  CA  GLU B 180    15388  10734  25346   1454  -1849   1392       C  
ATOM   6158  C   GLU B 180      44.535  77.372  46.020  1.00139.49           C  
ANISOU 6158  C   GLU B 180    15987  11475  25537   1342  -1726   1181       C  
ATOM   6159  O   GLU B 180      45.673  77.465  45.560  1.00145.30           O  
ANISOU 6159  O   GLU B 180    16751  12255  26201   1195  -1712   1363       O  
ATOM   6160  CB  GLU B 180      43.562  79.674  45.860  1.00137.73           C  
ANISOU 6160  CB  GLU B 180    15587  10555  26189   1455  -1926   1374       C  
ATOM   6161  CG  GLU B 180      44.851  80.314  45.367  1.00141.79           C  
ANISOU 6161  CG  GLU B 180    16097  10946  26831   1281  -1948   1634       C  
ATOM   6162  CD  GLU B 180      44.830  81.825  45.489  1.00154.22           C  
ANISOU 6162  CD  GLU B 180    17558  12025  29012   1288  -2058   1711       C  
ATOM   6163  OE1 GLU B 180      43.761  82.378  45.822  1.00158.46           O  
ANISOU 6163  OE1 GLU B 180    18019  12324  29867   1439  -2127   1594       O  
ATOM   6164  OE2 GLU B 180      45.879  82.460  45.249  1.00158.00           O1-
ANISOU 6164  OE2 GLU B 180    18017  12348  29668   1144  -2079   1886       O1-
ATOM   6165  N   GLU B 181      44.221  76.550  47.015  1.00131.75           N  
ANISOU 6165  N   GLU B 181    15041  10652  24365   1413  -1639    810       N  
ATOM   6166  CA  GLU B 181      45.223  75.731  47.683  1.00122.38           C  
ANISOU 6166  CA  GLU B 181    13927   9681  22893   1324  -1524    587       C  
ATOM   6167  C   GLU B 181      45.596  74.507  46.856  1.00123.13           C  
ANISOU 6167  C   GLU B 181    14098  10155  22531   1254  -1479    760       C  
ATOM   6168  O   GLU B 181      46.707  73.988  46.966  1.00127.33           O  
ANISOU 6168  O   GLU B 181    14685  10848  22848   1141  -1408    718       O  
ATOM   6169  CB  GLU B 181      44.711  75.296  49.056  1.00121.81           C  
ANISOU 6169  CB  GLU B 181    13841   9657  22785   1426  -1453    153       C  
ATOM   6170  CG  GLU B 181      43.316  74.692  49.026  1.00128.62           C  
ANISOU 6170  CG  GLU B 181    14683  10649  23537   1569  -1465    107       C  
ATOM   6171  CD  GLU B 181      42.757  74.446  50.414  1.00135.65           C  
ANISOU 6171  CD  GLU B 181    15530  11573  24438   1671  -1403   -303       C  
ATOM   6172  OE1 GLU B 181      43.509  74.619  51.396  1.00143.75           O  
ANISOU 6172  OE1 GLU B 181    16547  12568  25505   1628  -1343   -560       O  
ATOM   6173  OE2 GLU B 181      41.567  74.080  50.522  1.00130.50           O1-
ANISOU 6173  OE2 GLU B 181    14842  10999  23744   1793  -1414   -367       O1-
ATOM   6174  N   ASN B 182      44.666  74.050  46.025  1.00121.11           N  
ANISOU 6174  N   ASN B 182    13834  10047  22137   1324  -1524    940       N  
ATOM   6175  CA  ASN B 182      44.878  72.838  45.242  1.00118.24           C  
ANISOU 6175  CA  ASN B 182    13522  10053  21351   1276  -1489   1060       C  
ATOM   6176  C   ASN B 182      45.547  73.087  43.892  1.00119.91           C  
ANISOU 6176  C   ASN B 182    13726  10359  21478   1164  -1540   1451       C  
ATOM   6177  O   ASN B 182      45.467  72.254  42.990  1.00123.43           O  
ANISOU 6177  O   ASN B 182    14179  11105  21611   1149  -1542   1596       O  
ATOM   6178  CB  ASN B 182      43.559  72.086  45.052  1.00112.64           C  
ANISOU 6178  CB  ASN B 182    12797   9501  20501   1403  -1507   1022       C  
ATOM   6179  CG  ASN B 182      43.001  71.553  46.357  1.00107.66           C  
ANISOU 6179  CG  ASN B 182    12170   8880  19856   1494  -1439    646       C  
ATOM   6180  ND2 ASN B 182      41.819  70.952  46.294  1.00108.09           N  
ANISOU 6180  ND2 ASN B 182    12200   9048  19821   1603  -1454    601       N  
ATOM   6181  OD1 ASN B 182      43.626  71.679  47.409  1.00105.49           O  
ANISOU 6181  OD1 ASN B 182    11909   8528  19643   1464  -1375    405       O  
ATOM   6182  N   CYS B 183      46.207  74.232  43.757  1.00114.37           N  
ANISOU 6182  N   CYS B 183    12992   9409  21055   1085  -1581   1616       N  
ATOM   6183  CA  CYS B 183      46.929  74.545  42.531  1.00114.79           C  
ANISOU 6183  CA  CYS B 183    13020   9560  21036    963  -1626   2008       C  
ATOM   6184  C   CYS B 183      48.238  73.770  42.474  1.00115.59           C  
ANISOU 6184  C   CYS B 183    13180   9926  20814    831  -1538   1956       C  
ATOM   6185  O   CYS B 183      48.988  73.734  43.449  1.00117.98           O  
ANISOU 6185  O   CYS B 183    13525  10146  21155    785  -1466   1700       O  
ATOM   6186  CB  CYS B 183      47.201  76.048  42.429  1.00119.96           C  
ANISOU 6186  CB  CYS B 183    13605   9839  22133    914  -1706   2221       C  
ATOM   6187  SG  CYS B 183      45.761  77.046  41.976  1.00160.48           S  
ANISOU 6187  SG  CYS B 183    18638  14693  27643   1050  -1843   2445       S  
ATOM   6188  N   GLN B 184      48.507  73.144  41.334  1.00117.68           N  
ANISOU 6188  N   GLN B 184    13435  10523  20754    774  -1545   2188       N  
ATOM   6189  CA  GLN B 184      49.744  72.394  41.166  1.00121.38           C  
ANISOU 6189  CA  GLN B 184    13944  11264  20910    654  -1468   2149       C  
ATOM   6190  C   GLN B 184      50.942  73.317  41.329  1.00122.12           C  
ANISOU 6190  C   GLN B 184    14028  11174  21199    516  -1460   2252       C  
ATOM   6191  O   GLN B 184      51.087  74.295  40.597  1.00125.53           O  
ANISOU 6191  O   GLN B 184    14390  11487  21819    453  -1534   2594       O  
ATOM   6192  CB  GLN B 184      49.797  71.710  39.800  1.00125.68           C  
ANISOU 6192  CB  GLN B 184    14449  12204  21098    620  -1491   2395       C  
ATOM   6193  CG  GLN B 184      51.076  70.919  39.565  1.00124.93           C  
ANISOU 6193  CG  GLN B 184    14380  12409  20679    503  -1417   2345       C  
ATOM   6194  CD  GLN B 184      51.160  70.338  38.168  1.00124.26           C  
ANISOU 6194  CD  GLN B 184    14229  12732  20251    468  -1446   2578       C  
ATOM   6195  NE2 GLN B 184      52.276  69.685  37.867  1.00124.45           N  
ANISOU 6195  NE2 GLN B 184    14256  13036  19993    370  -1388   2542       N  
ATOM   6196  OE1 GLN B 184      50.234  70.475  37.369  1.00122.49           O  
ANISOU 6196  OE1 GLN B 184    13941  12588  20010    533  -1522   2779       O  
ATOM   6197  N   LYS B 185      51.793  73.004  42.299  1.00120.86           N  
ANISOU 6197  N   LYS B 185    13927  10993  21003    467  -1373   1966       N  
ATOM   6198  CA  LYS B 185      52.999  73.782  42.538  1.00119.86           C  
ANISOU 6198  CA  LYS B 185    13790  10709  21043    330  -1356   2019       C  
ATOM   6199  C   LYS B 185      54.147  73.228  41.703  1.00115.46           C  
ANISOU 6199  C   LYS B 185    13231  10488  20150    196  -1318   2186       C  
ATOM   6200  O   LYS B 185      54.656  72.142  41.979  1.00111.55           O  
ANISOU 6200  O   LYS B 185    12789  10246  19350    186  -1238   1971       O  
ATOM   6201  CB  LYS B 185      53.367  73.746  44.022  1.00119.98           C  
ANISOU 6201  CB  LYS B 185    13854  10556  21176    345  -1284   1616       C  
ATOM   6202  CG  LYS B 185      52.203  74.025  44.956  1.00120.28           C  
ANISOU 6202  CG  LYS B 185    13888  10352  21462    495  -1303   1371       C  
ATOM   6203  CD  LYS B 185      52.578  73.745  46.402  1.00121.41           C  
ANISOU 6203  CD  LYS B 185    14067  10447  21618    512  -1219    956       C  
ATOM   6204  CE  LYS B 185      51.364  73.829  47.313  1.00124.85           C  
ANISOU 6204  CE  LYS B 185    14484  10733  22222    669  -1228    695       C  
ATOM   6205  NZ  LYS B 185      51.702  73.491  48.722  1.00125.11           N1+
ANISOU 6205  NZ  LYS B 185    14532  10782  22222    688  -1143    298       N1+
ATOM   6206  N   LEU B 186      54.549  73.974  40.680  1.00115.29           N  
ANISOU 6206  N   LEU B 186    13136  10477  20191     94  -1378   2577       N  
ATOM   6207  CA  LEU B 186      55.638  73.541  39.813  1.00116.62           C  
ANISOU 6207  CA  LEU B 186    13279  10992  20041    -38  -1345   2759       C  
ATOM   6208  C   LEU B 186      56.988  73.962  40.382  1.00112.97           C  
ANISOU 6208  C   LEU B 186    12829  10417  19679   -177  -1292   2689       C  
ATOM   6209  O   LEU B 186      57.180  75.118  40.761  1.00113.16           O  
ANISOU 6209  O   LEU B 186    12821  10085  20089   -229  -1330   2765       O  
ATOM   6210  CB  LEU B 186      55.469  74.097  38.397  1.00125.89           C  
ANISOU 6210  CB  LEU B 186    14345  12296  21190    -93  -1432   3239       C  
ATOM   6211  CG  LEU B 186      54.141  73.832  37.686  1.00130.83           C  
ANISOU 6211  CG  LEU B 186    14934  13044  21731     34  -1500   3368       C  
ATOM   6212  CD1 LEU B 186      53.111  74.862  38.107  1.00137.27           C  
ANISOU 6212  CD1 LEU B 186    15732  13429  22994    126  -1580   3422       C  
ATOM   6213  CD2 LEU B 186      54.325  73.858  36.178  1.00132.09           C  
ANISOU 6213  CD2 LEU B 186    14982  13559  21645    -40  -1551   3788       C  
ATOM   6214  N   THR B 187      57.917  73.014  40.439  1.00108.43           N  
ANISOU 6214  N   THR B 187    12290  10139  18768   -235  -1208   2533       N  
ATOM   6215  CA  THR B 187      59.254  73.269  40.959  1.00108.04           C  
ANISOU 6215  CA  THR B 187    12251  10039  18762   -367  -1150   2449       C  
ATOM   6216  C   THR B 187      60.297  72.538  40.122  1.00111.82           C  
ANISOU 6216  C   THR B 187    12701  10941  18845   -472  -1104   2559       C  
ATOM   6217  O   THR B 187      61.377  72.207  40.609  1.00116.18           O  
ANISOU 6217  O   THR B 187    13280  11571  19291   -549  -1032   2388       O  
ATOM   6218  CB  THR B 187      59.384  72.813  42.424  1.00103.11           C  
ANISOU 6218  CB  THR B 187    11712   9286  18178   -307  -1075   1996       C  
ATOM   6219  CG2 THR B 187      58.543  73.693  43.335  1.00106.89           C  
ANISOU 6219  CG2 THR B 187    12195   9345  19072   -222  -1116   1861       C  
ATOM   6220  OG1 THR B 187      58.942  71.455  42.545  1.00 91.84           O  
ANISOU 6220  OG1 THR B 187    10338   8127  16430   -202  -1029   1775       O  
ATOM   6221  N   LYS B 188      59.967  72.292  38.859  1.00109.62           N  
ANISOU 6221  N   LYS B 188    12355  10953  18345   -471  -1148   2838       N  
ATOM   6222  CA  LYS B 188      60.822  71.497  37.986  1.00107.60           C  
ANISOU 6222  CA  LYS B 188    12052  11154  17679   -548  -1109   2914       C  
ATOM   6223  C   LYS B 188      60.992  72.142  36.616  1.00110.42           C  
ANISOU 6223  C   LYS B 188    12279  11705  17972   -648  -1172   3387       C  
ATOM   6224  O   LYS B 188      62.108  72.459  36.204  1.00115.36           O  
ANISOU 6224  O   LYS B 188    12840  12468  18524   -797  -1151   3567       O  
ATOM   6225  CB  LYS B 188      60.245  70.087  37.838  1.00105.78           C  
ANISOU 6225  CB  LYS B 188    11853  11222  17116   -422  -1083   2675       C  
ATOM   6226  CG  LYS B 188      60.735  69.318  36.623  1.00106.48           C  
ANISOU 6226  CG  LYS B 188    11854  11813  16789   -467  -1076   2795       C  
ATOM   6227  CD  LYS B 188      62.142  68.794  36.821  1.00109.65           C  
ANISOU 6227  CD  LYS B 188    12259  12410  16992   -566   -996   2645       C  
ATOM   6228  CE  LYS B 188      62.477  67.735  35.782  1.00113.05           C  
ANISOU 6228  CE  LYS B 188    12606  13357  16991   -565   -983   2634       C  
ATOM   6229  NZ  LYS B 188      61.553  66.568  35.860  1.00110.62           N1+
ANISOU 6229  NZ  LYS B 188    12334  13159  16539   -410   -988   2364       N1+
ATOM   6230  N   ILE B 189      59.881  72.338  35.914  1.00106.85           N  
ANISOU 6230  N   ILE B 189    11777  11280  17542   -569  -1251   3600       N  
ATOM   6231  CA  ILE B 189      59.923  72.858  34.553  1.00108.74           C  
ANISOU 6231  CA  ILE B 189    11874  11762  17678   -650  -1317   4069       C  
ATOM   6232  C   ILE B 189      59.937  74.383  34.513  1.00116.31           C  
ANISOU 6232  C   ILE B 189    12774  12349  19070   -739  -1389   4433       C  
ATOM   6233  O   ILE B 189      59.939  74.984  33.438  1.00113.59           O  
ANISOU 6233  O   ILE B 189    12299  12156  18705   -815  -1455   4881       O  
ATOM   6234  CB  ILE B 189      58.742  72.336  33.718  1.00105.37           C  
ANISOU 6234  CB  ILE B 189    11401  11587  17049   -526  -1374   4152       C  
ATOM   6235  CG1 ILE B 189      57.416  72.721  34.374  1.00106.59           C  
ANISOU 6235  CG1 ILE B 189    11622  11340  17538   -384  -1427   4060       C  
ATOM   6236  CG2 ILE B 189      58.835  70.828  33.554  1.00 98.57           C  
ANISOU 6236  CG2 ILE B 189    10563  11135  15756   -459  -1313   3831       C  
ATOM   6237  CD1 ILE B 189      56.202  72.223  33.624  1.00109.82           C  
ANISOU 6237  CD1 ILE B 189    11985  11972  17769   -258  -1486   4125       C  
ATOM   6238  N   ILE B 190      59.948  75.005  35.687  1.00125.83           N  
ANISOU 6238  N   ILE B 190    14060  13074  20674   -728  -1381   4240       N  
ATOM   6239  CA  ILE B 190      60.001  76.458  35.779  1.00134.77           C  
ANISOU 6239  CA  ILE B 190    15132  13792  22282   -809  -1454   4530       C  
ATOM   6240  C   ILE B 190      61.235  76.898  36.555  1.00141.53           C  
ANISOU 6240  C   ILE B 190    16012  14444  23319   -943  -1399   4403       C  
ATOM   6241  O   ILE B 190      61.128  77.495  37.626  1.00146.91           O  
ANISOU 6241  O   ILE B 190    16746  14684  24388   -917  -1405   4189       O  
ATOM   6242  CB  ILE B 190      58.747  77.031  36.462  1.00135.19           C  
ANISOU 6242  CB  ILE B 190    15228  13396  22742   -665  -1519   4422       C  
ATOM   6243  CG1 ILE B 190      57.492  76.330  35.943  1.00140.63           C  
ANISOU 6243  CG1 ILE B 190    15923  14301  23209   -508  -1552   4415       C  
ATOM   6244  CG2 ILE B 190      58.659  78.534  36.240  1.00140.08           C  
ANISOU 6244  CG2 ILE B 190    15747  13624  23854   -740  -1622   4806       C  
ATOM   6245  CD1 ILE B 190      56.204  76.904  36.489  1.00147.66           C  
ANISOU 6245  CD1 ILE B 190    16836  14787  24481   -364  -1623   4345       C  
ATOM   6246  N   CYS B 191      62.407  76.594  36.011  1.00141.32           N  
ANISOU 6246  N   CYS B 191    15934  14757  23003  -1084  -1348   4521       N  
ATOM   6247  CA  CYS B 191      63.660  76.925  36.674  1.00141.36           C  
ANISOU 6247  CA  CYS B 191    15954  14626  23133  -1220  -1291   4404       C  
ATOM   6248  C   CYS B 191      64.684  77.435  35.669  1.00146.06           C  
ANISOU 6248  C   CYS B 191    16410  15447  23640  -1416  -1304   4843       C  
ATOM   6249  O   CYS B 191      64.615  77.110  34.484  1.00150.84           O  
ANISOU 6249  O   CYS B 191    16922  16470  23921  -1439  -1323   5138       O  
ATOM   6250  CB  CYS B 191      64.208  75.701  37.409  1.00136.48           C  
ANISOU 6250  CB  CYS B 191    15443  14220  22192  -1174  -1179   3933       C  
ATOM   6251  SG  CYS B 191      63.010  74.898  38.499  1.00121.66           S  
ANISOU 6251  SG  CYS B 191    13709  12182  20333   -948  -1156   3446       S  
ATOM   6252  N   ALA B 192      65.629  78.237  36.146  1.00147.61           N  
ANISOU 6252  N   ALA B 192    16580  15383  24123  -1560  -1295   4881       N  
ATOM   6253  CA  ALA B 192      66.684  78.765  35.291  1.00157.38           C  
ANISOU 6253  CA  ALA B 192    17678  16814  25306  -1764  -1303   5296       C  
ATOM   6254  C   ALA B 192      67.435  77.635  34.595  1.00161.56           C  
ANISOU 6254  C   ALA B 192    18181  17965  25241  -1803  -1221   5262       C  
ATOM   6255  O   ALA B 192      67.473  76.508  35.087  1.00162.03           O  
ANISOU 6255  O   ALA B 192    18346  18208  25010  -1701  -1144   4839       O  
ATOM   6256  CB  ALA B 192      67.643  79.624  36.100  1.00161.15           C  
ANISOU 6256  CB  ALA B 192    18148  16916  26166  -1904  -1291   5234       C  
ATOM   6257  N   GLN B 193      68.031  77.943  33.448  1.00166.27           N  
ANISOU 6257  N   GLN B 193    18619  18889  25666  -1951  -1241   5712       N  
ATOM   6258  CA  GLN B 193      68.775  76.952  32.681  1.00166.99           C  
ANISOU 6258  CA  GLN B 193    18650  19603  25194  -1996  -1170   5702       C  
ATOM   6259  C   GLN B 193      69.978  76.447  33.472  1.00161.66           C  
ANISOU 6259  C   GLN B 193    18044  18970  24410  -2058  -1067   5335       C  
ATOM   6260  O   GLN B 193      70.568  75.420  33.137  1.00159.48           O  
ANISOU 6260  O   GLN B 193    17753  19159  23683  -2054   -996   5170       O  
ATOM   6261  CB  GLN B 193      69.225  77.544  31.342  1.00176.00           C  
ANISOU 6261  CB  GLN B 193    19583  21081  26208  -2160  -1215   6289       C  
ATOM   6262  CG  GLN B 193      69.778  76.527  30.355  1.00176.78           C  
ANISOU 6262  CG  GLN B 193    19583  21892  25692  -2183  -1157   6306       C  
ATOM   6263  CD  GLN B 193      70.095  77.140  29.003  1.00179.05           C  
ANISOU 6263  CD  GLN B 193    19643  22552  25836  -2337  -1207   6912       C  
ATOM   6264  NE2 GLN B 193      70.526  76.308  28.061  1.00180.75           N  
ANISOU 6264  NE2 GLN B 193    19742  23431  25504  -2354  -1163   6940       N  
ATOM   6265  OE1 GLN B 193      69.954  78.348  28.808  1.00177.28           O  
ANISOU 6265  OE1 GLN B 193    19334  22030  25995  -2438  -1287   7352       O  
ATOM   6266  N   GLN B 194      70.331  77.174  34.529  1.00159.75           N  
ANISOU 6266  N   GLN B 194    17865  18241  24591  -2111  -1064   5197       N  
ATOM   6267  CA  GLN B 194      71.467  76.809  35.367  1.00156.25           C  
ANISOU 6267  CA  GLN B 194    17482  17799  24089  -2174   -973   4856       C  
ATOM   6268  C   GLN B 194      71.024  76.157  36.673  1.00146.65           C  
ANISOU 6268  C   GLN B 194    16441  16344  22936  -2009   -929   4304       C  
ATOM   6269  O   GLN B 194      71.789  76.091  37.635  1.00142.82           O  
ANISOU 6269  O   GLN B 194    16014  15717  22532  -2047   -870   4005       O  
ATOM   6270  CB  GLN B 194      72.335  78.035  35.659  1.00161.51           C  
ANISOU 6270  CB  GLN B 194    18074  18138  25154  -2366   -995   5063       C  
ATOM   6271  CG  GLN B 194      71.634  79.120  36.458  1.00162.98           C  
ANISOU 6271  CG  GLN B 194    18302  17686  25938  -2334  -1072   5047       C  
ATOM   6272  CD  GLN B 194      72.543  80.294  36.758  1.00168.10           C  
ANISOU 6272  CD  GLN B 194    18864  18003  27002  -2528  -1098   5220       C  
ATOM   6273  NE2 GLN B 194      72.122  81.145  37.685  1.00168.17           N  
ANISOU 6273  NE2 GLN B 194    18912  17442  27541  -2498  -1151   5073       N  
ATOM   6274  OE1 GLN B 194      73.613  80.435  36.164  1.00172.43           O  
ANISOU 6274  OE1 GLN B 194    19301  18810  27403  -2705  -1071   5472       O  
ATOM   6275  N   CYS B 195      69.783  75.680  36.704  1.00142.69           N  
ANISOU 6275  N   CYS B 195    16010  15812  22391  -1830   -958   4181       N  
ATOM   6276  CA  CYS B 195      69.273  74.958  37.863  1.00135.89           C  
ANISOU 6276  CA  CYS B 195    15300  14787  21546  -1667   -915   3686       C  
ATOM   6277  C   CYS B 195      69.521  73.465  37.713  1.00132.94           C  
ANISOU 6277  C   CYS B 195    14966  14864  20680  -1588   -840   3417       C  
ATOM   6278  O   CYS B 195      69.032  72.838  36.774  1.00135.25           O  
ANISOU 6278  O   CYS B 195    15217  15497  20676  -1527   -858   3531       O  
ATOM   6279  CB  CYS B 195      67.779  75.220  38.057  1.00132.96           C  
ANISOU 6279  CB  CYS B 195    14980  14129  21411  -1513   -986   3675       C  
ATOM   6280  SG  CYS B 195      67.396  76.750  38.931  1.00157.96           S  
ANISOU 6280  SG  CYS B 195    18147  16627  25242  -1537  -1058   3713       S  
ATOM   6281  N   SER B 196      70.285  72.901  38.642  1.00129.78           N  
ANISOU 6281  N   SER B 196    14637  14465  20209  -1589   -762   3056       N  
ATOM   6282  CA  SER B 196      70.611  71.482  38.604  1.00127.35           C  
ANISOU 6282  CA  SER B 196    14360  14542  19484  -1515   -695   2782       C  
ATOM   6283  C   SER B 196      69.357  70.614  38.679  1.00125.36           C  
ANISOU 6283  C   SER B 196    14181  14324  19127  -1322   -712   2592       C  
ATOM   6284  O   SER B 196      69.165  69.715  37.859  1.00122.28           O  
ANISOU 6284  O   SER B 196    13751  14308  18403  -1266   -711   2600       O  
ATOM   6285  CB  SER B 196      71.578  71.123  39.734  1.00124.94           C  
ANISOU 6285  CB  SER B 196    14118  14170  19183  -1542   -617   2434       C  
ATOM   6286  OG  SER B 196      71.147  71.670  40.968  1.00126.35           O  
ANISOU 6286  OG  SER B 196    14382  13906  19721  -1494   -625   2232       O  
ATOM   6287  N   GLY B 197      68.505  70.891  39.661  1.00125.61           N  
ANISOU 6287  N   GLY B 197    14305  13973  19449  -1222   -731   2413       N  
ATOM   6288  CA  GLY B 197      67.304  70.102  39.869  1.00120.16           C  
ANISOU 6288  CA  GLY B 197    13684  13282  18691  -1043   -745   2221       C  
ATOM   6289  C   GLY B 197      66.044  70.930  40.028  1.00117.36           C  
ANISOU 6289  C   GLY B 197    13350  12578  18664   -968   -818   2332       C  
ATOM   6290  O   GLY B 197      65.520  71.474  39.056  1.00117.22           O  
ANISOU 6290  O   GLY B 197    13262  12593  18684   -984   -886   2666       O  
ATOM   6291  N   ARG B 198      65.555  71.024  41.260  1.00114.84           N  
ANISOU 6291  N   ARG B 198    13115  11942  18578   -881   -806   2051       N  
ATOM   6292  CA  ARG B 198      64.310  71.729  41.543  1.00114.29           C  
ANISOU 6292  CA  ARG B 198    13064  11537  18824   -788   -872   2091       C  
ATOM   6293  C   ARG B 198      64.580  73.171  41.959  1.00115.69           C  
ANISOU 6293  C   ARG B 198    13208  11319  19430   -881   -910   2208       C  
ATOM   6294  O   ARG B 198      65.732  73.584  42.074  1.00122.68           O  
ANISOU 6294  O   ARG B 198    14061  12191  20361  -1021   -881   2246       O  
ATOM   6295  CB  ARG B 198      63.529  71.004  42.640  1.00115.19           C  
ANISOU 6295  CB  ARG B 198    13268  11553  18945   -632   -840   1712       C  
ATOM   6296  CG  ARG B 198      63.592  69.484  42.554  1.00117.34           C  
ANISOU 6296  CG  ARG B 198    13575  12179  18831   -561   -787   1514       C  
ATOM   6297  CD  ARG B 198      62.753  68.935  41.409  1.00115.56           C  
ANISOU 6297  CD  ARG B 198    13314  12193  18400   -489   -834   1683       C  
ATOM   6298  NE  ARG B 198      61.324  69.123  41.641  1.00110.77           N  
ANISOU 6298  NE  ARG B 198    12735  11380  17974   -358   -886   1660       N  
ATOM   6299  CZ  ARG B 198      60.368  68.513  40.948  1.00108.71           C  
ANISOU 6299  CZ  ARG B 198    12457  11288  17559   -261   -924   1713       C  
ATOM   6300  NH1 ARG B 198      60.684  67.666  39.978  1.00109.59           N1+
ANISOU 6300  NH1 ARG B 198    12522  11782  17336   -277   -919   1775       N1+
ATOM   6301  NH2 ARG B 198      59.094  68.747  41.228  1.00108.10           N  
ANISOU 6301  NH2 ARG B 198    12401  11008  17664   -144   -969   1688       N  
ATOM   6302  N   CYS B 199      63.513  73.933  42.188  1.00114.24           N  
ANISOU 6302  N   CYS B 199    13024  10806  19577   -801   -978   2253       N  
ATOM   6303  CA  CYS B 199      63.644  75.336  42.572  1.00114.74           C  
ANISOU 6303  CA  CYS B 199    13039  10451  20105   -874  -1031   2350       C  
ATOM   6304  C   CYS B 199      62.432  75.842  43.354  1.00113.86           C  
ANISOU 6304  C   CYS B 199    12952   9973  20337   -734  -1080   2177       C  
ATOM   6305  O   CYS B 199      61.422  75.148  43.474  1.00104.97           O  
ANISOU 6305  O   CYS B 199    11875   8931  19078   -585  -1077   2040       O  
ATOM   6306  CB  CYS B 199      63.866  76.207  41.335  1.00115.19           C  
ANISOU 6306  CB  CYS B 199    12990  10509  20270   -998  -1105   2850       C  
ATOM   6307  SG  CYS B 199      62.561  76.074  40.093  1.00132.68           S  
ANISOU 6307  SG  CYS B 199    15162  12878  22371   -897  -1187   3186       S  
ATOM   6308  N   ARG B 200      62.545  77.056  43.886  1.00121.50           N  
ANISOU 6308  N   ARG B 200    13873  10535  21758   -782  -1126   2174       N  
ATOM   6309  CA  ARG B 200      61.446  77.686  44.610  1.00124.10           C  
ANISOU 6309  CA  ARG B 200    14199  10495  22459   -653  -1182   2007       C  
ATOM   6310  C   ARG B 200      60.686  78.632  43.689  1.00126.04           C  
ANISOU 6310  C   ARG B 200    14365  10528  22997   -648  -1298   2407       C  
ATOM   6311  O   ARG B 200      59.465  78.758  43.777  1.00125.84           O  
ANISOU 6311  O   ARG B 200    14342  10358  23114   -505  -1350   2373       O  
ATOM   6312  CB  ARG B 200      61.967  78.461  45.823  1.00123.87           C  
ANISOU 6312  CB  ARG B 200    14147  10134  22786   -692  -1172   1708       C  
ATOM   6313  CG  ARG B 200      62.972  77.703  46.670  1.00122.33           C  
ANISOU 6313  CG  ARG B 200    14005  10149  22327   -736  -1063   1374       C  
ATOM   6314  CD  ARG B 200      63.124  78.326  48.051  1.00120.24           C  
ANISOU 6314  CD  ARG B 200    13715   9587  22384   -717  -1054    985       C  
ATOM   6315  NE  ARG B 200      63.464  79.746  47.997  1.00115.86           N  
ANISOU 6315  NE  ARG B 200    13062   8635  22323   -821  -1134   1121       N  
ATOM   6316  CZ  ARG B 200      64.706  80.216  47.932  1.00110.73           C  
ANISOU 6316  CZ  ARG B 200    12365   7944  21761   -994  -1123   1202       C  
ATOM   6317  NH1 ARG B 200      65.735  79.381  47.904  1.00108.34           N1+
ANISOU 6317  NH1 ARG B 200    12107   7988  21069  -1078  -1033   1158       N1+
ATOM   6318  NH2 ARG B 200      64.921  81.524  47.890  1.00109.94           N  
ANISOU 6318  NH2 ARG B 200    12165   7450  22158  -1084  -1206   1329       N  
ATOM   6319  N   GLY B 201      61.424  79.300  42.810  1.00127.30           N  
ANISOU 6319  N   GLY B 201    14443  10678  23247   -806  -1340   2801       N  
ATOM   6320  CA  GLY B 201      60.839  80.234  41.868  1.00132.61           C  
ANISOU 6320  CA  GLY B 201    15020  11166  24200   -824  -1455   3246       C  
ATOM   6321  C   GLY B 201      61.490  80.126  40.505  1.00136.06           C  
ANISOU 6321  C   GLY B 201    15389  11938  24368   -965  -1464   3716       C  
ATOM   6322  O   GLY B 201      62.089  79.103  40.174  1.00135.60           O  
ANISOU 6322  O   GLY B 201    15372  12313  23835  -1000  -1383   3669       O  
ATOM   6323  N   LYS B 202      61.378  81.186  39.711  1.00137.12           N  
ANISOU 6323  N   LYS B 202    15406  11882  24811  -1044  -1567   4173       N  
ATOM   6324  CA  LYS B 202      61.938  81.188  38.367  1.00143.07           C  
ANISOU 6324  CA  LYS B 202    16066  12973  25320  -1182  -1585   4668       C  
ATOM   6325  C   LYS B 202      63.332  81.808  38.350  1.00142.90           C  
ANISOU 6325  C   LYS B 202    15974  12888  25435  -1394  -1568   4821       C  
ATOM   6326  O   LYS B 202      64.202  81.382  37.589  1.00139.54           O  
ANISOU 6326  O   LYS B 202    15507  12867  24647  -1518  -1522   5031       O  
ATOM   6327  CB  LYS B 202      61.010  81.932  37.407  1.00157.45           C  
ANISOU 6327  CB  LYS B 202    17779  14685  27359  -1153  -1710   5142       C  
ATOM   6328  CG  LYS B 202      61.329  81.720  35.937  1.00170.92           C  
ANISOU 6328  CG  LYS B 202    19381  16856  28705  -1257  -1727   5645       C  
ATOM   6329  CD  LYS B 202      60.275  82.369  35.055  1.00181.28           C  
ANISOU 6329  CD  LYS B 202    20586  18083  30209  -1202  -1852   6091       C  
ATOM   6330  CE  LYS B 202      60.492  82.041  33.589  1.00184.40           C  
ANISOU 6330  CE  LYS B 202    20866  19022  30175  -1286  -1864   6563       C  
ATOM   6331  NZ  LYS B 202      59.404  82.598  32.739  1.00187.65           N1+
ANISOU 6331  NZ  LYS B 202    21170  19392  30738  -1220  -1987   6992       N1+
ATOM   6332  N   SER B 203      63.539  82.813  39.193  1.00148.71           N  
ANISOU 6332  N   SER B 203    16684  13120  26697  -1435  -1608   4699       N  
ATOM   6333  CA  SER B 203      64.838  83.468  39.292  1.00155.70           C  
ANISOU 6333  CA  SER B 203    17497  13889  27772  -1639  -1598   4810       C  
ATOM   6334  C   SER B 203      65.908  82.471  39.720  1.00156.61           C  
ANISOU 6334  C   SER B 203    17696  14362  27449  -1693  -1465   4488       C  
ATOM   6335  O   SER B 203      65.645  81.583  40.531  1.00156.99           O  
ANISOU 6335  O   SER B 203    17866  14510  27273  -1561  -1390   4027       O  
ATOM   6336  CB  SER B 203      64.781  84.638  40.277  1.00159.91           C  
ANISOU 6336  CB  SER B 203    17992  13802  28965  -1647  -1664   4630       C  
ATOM   6337  OG  SER B 203      64.450  84.195  41.581  1.00158.61           O  
ANISOU 6337  OG  SER B 203    17940  13513  28811  -1503  -1605   4031       O  
ATOM   6338  N   PRO B 204      67.120  82.612  39.165  1.00155.11           N  
ANISOU 6338  N   PRO B 204    17427  14371  27136  -1888  -1438   4745       N  
ATOM   6339  CA  PRO B 204      68.245  81.722  39.475  1.00152.72           C  
ANISOU 6339  CA  PRO B 204    17182  14418  26427  -1955  -1317   4483       C  
ATOM   6340  C   PRO B 204      68.653  81.802  40.944  1.00153.51           C  
ANISOU 6340  C   PRO B 204    17356  14227  26743  -1934  -1268   3966       C  
ATOM   6341  O   PRO B 204      69.457  80.992  41.404  1.00150.46           O  
ANISOU 6341  O   PRO B 204    17033  14102  26034  -1955  -1167   3675       O  
ATOM   6342  CB  PRO B 204      69.370  82.257  38.583  1.00149.37           C  
ANISOU 6342  CB  PRO B 204    16619  14146  25987  -2185  -1328   4934       C  
ATOM   6343  CG  PRO B 204      68.672  82.988  37.484  1.00151.51           C  
ANISOU 6343  CG  PRO B 204    16771  14358  26437  -2209  -1440   5485       C  
ATOM   6344  CD  PRO B 204      67.468  83.597  38.127  1.00154.02           C  
ANISOU 6344  CD  PRO B 204    17127  14174  27220  -2058  -1523   5340       C  
ATOM   6345  N   SER B 205      68.099  82.771  41.666  1.00156.24           N  
ANISOU 6345  N   SER B 205    17682  14052  27631  -1889  -1342   3848       N  
ATOM   6346  CA  SER B 205      68.382  82.930  43.087  1.00155.08           C  
ANISOU 6346  CA  SER B 205    17581  13629  27712  -1857  -1306   3339       C  
ATOM   6347  C   SER B 205      67.432  82.084  43.926  1.00153.02           C  
ANISOU 6347  C   SER B 205    17445  13423  27273  -1638  -1260   2889       C  
ATOM   6348  O   SER B 205      67.334  82.263  45.140  1.00154.76           O  
ANISOU 6348  O   SER B 205    17692  13402  27708  -1571  -1245   2460       O  
ATOM   6349  CB  SER B 205      68.261  84.400  43.493  1.00160.34           C  
ANISOU 6349  CB  SER B 205    18143  13709  29071  -1912  -1412   3388       C  
ATOM   6350  OG  SER B 205      69.112  85.217  42.708  1.00167.07           O  
ANISOU 6350  OG  SER B 205    18866  14488  30126  -2124  -1462   3840       O  
ATOM   6351  N   ASP B 206      66.733  81.162  43.270  1.00148.51           N  
ANISOU 6351  N   ASP B 206    16933  13187  26306  -1530  -1241   2990       N  
ATOM   6352  CA  ASP B 206      65.745  80.325  43.941  1.00139.91           C  
ANISOU 6352  CA  ASP B 206    15951  12167  25042  -1325  -1205   2623       C  
ATOM   6353  C   ASP B 206      66.048  78.839  43.772  1.00129.46           C  
ANISOU 6353  C   ASP B 206    14715  11353  23121  -1286  -1102   2489       C  
ATOM   6354  O   ASP B 206      65.284  77.989  44.227  1.00125.75           O  
ANISOU 6354  O   ASP B 206    14328  10996  22454  -1128  -1067   2219       O  
ATOM   6355  CB  ASP B 206      64.341  80.630  43.413  1.00143.24           C  
ANISOU 6355  CB  ASP B 206    16356  12443  25626  -1197  -1295   2825       C  
ATOM   6356  CG  ASP B 206      63.910  82.059  43.687  1.00148.93           C  
ANISOU 6356  CG  ASP B 206    16986  12621  26980  -1204  -1404   2908       C  
ATOM   6357  OD1 ASP B 206      64.616  82.765  44.437  1.00152.24           O  
ANISOU 6357  OD1 ASP B 206    17362  12759  27722  -1291  -1406   2732       O  
ATOM   6358  OD2 ASP B 206      62.860  82.475  43.151  1.00148.58           O1-
ANISOU 6358  OD2 ASP B 206    16904  12427  27122  -1120  -1492   3141       O1-
ATOM   6359  N   CYS B 207      67.161  78.532  43.114  1.00126.83           N  
ANISOU 6359  N   CYS B 207    14351  11323  22514  -1431  -1059   2678       N  
ATOM   6360  CA  CYS B 207      67.555  77.145  42.882  1.00119.99           C  
ANISOU 6360  CA  CYS B 207    13547  10939  21105  -1402   -969   2557       C  
ATOM   6361  C   CYS B 207      67.666  76.358  44.182  1.00116.34           C  
ANISOU 6361  C   CYS B 207    13181  10501  20524  -1307   -888   2049       C  
ATOM   6362  O   CYS B 207      68.332  76.786  45.123  1.00116.39           O  
ANISOU 6362  O   CYS B 207    13181  10319  20725  -1365   -862   1821       O  
ATOM   6363  CB  CYS B 207      68.884  77.078  42.126  1.00121.18           C  
ANISOU 6363  CB  CYS B 207    13630  11379  21034  -1584   -933   2795       C  
ATOM   6364  SG  CYS B 207      68.749  77.302  40.340  1.00117.86           S  
ANISOU 6364  SG  CYS B 207    13097  11231  20454  -1666   -996   3389       S  
ATOM   6365  N   CYS B 208      67.007  75.204  44.224  1.00116.44           N  
ANISOU 6365  N   CYS B 208    13267  10756  20219  -1164   -852   1881       N  
ATOM   6366  CA  CYS B 208      67.099  74.315  45.374  1.00109.85           C  
ANISOU 6366  CA  CYS B 208    12511  10001  19226  -1074   -774   1445       C  
ATOM   6367  C   CYS B 208      68.428  73.576  45.347  1.00107.90           C  
ANISOU 6367  C   CYS B 208    12266  10072  18659  -1171   -695   1372       C  
ATOM   6368  O   CYS B 208      69.150  73.620  44.351  1.00106.78           O  
ANISOU 6368  O   CYS B 208    12069  10135  18369  -1290   -696   1650       O  
ATOM   6369  CB  CYS B 208      65.945  73.312  45.375  1.00101.93           C  
ANISOU 6369  CB  CYS B 208    11573   9144  18013   -897   -769   1323       C  
ATOM   6370  SG  CYS B 208      64.317  74.042  45.651  1.00119.97           S  
ANISOU 6370  SG  CYS B 208    13860  11068  20657   -754   -852   1320       S  
ATOM   6371  N   HIS B 209      68.750  72.898  46.443  1.00110.05           N  
ANISOU 6371  N   HIS B 209    12590  10404  18819  -1119   -626   1005       N  
ATOM   6372  CA  HIS B 209      69.985  72.129  46.514  1.00114.80           C  
ANISOU 6372  CA  HIS B 209    13192  11302  19124  -1194   -552    905       C  
ATOM   6373  C   HIS B 209      69.912  70.903  45.608  1.00114.33           C  
ANISOU 6373  C   HIS B 209    13148  11633  18659  -1143   -531    991       C  
ATOM   6374  O   HIS B 209      68.837  70.344  45.387  1.00108.90           O  
ANISOU 6374  O   HIS B 209    12497  10992  17890  -1013   -554    978       O  
ATOM   6375  CB  HIS B 209      70.284  71.708  47.953  1.00113.88           C  
ANISOU 6375  CB  HIS B 209    13116  11155  18999  -1142   -491    502       C  
ATOM   6376  CG  HIS B 209      71.638  71.096  48.130  1.00110.63           C  
ANISOU 6376  CG  HIS B 209    12692  11000  18342  -1229   -421    400       C  
ATOM   6377  CD2 HIS B 209      72.836  71.652  48.427  1.00110.12           C  
ANISOU 6377  CD2 HIS B 209    12580  10903  18359  -1370   -396    375       C  
ATOM   6378  ND1 HIS B 209      71.868  69.744  47.991  1.00108.41           N  
ANISOU 6378  ND1 HIS B 209    12440  11052  17696  -1168   -372    308       N  
ATOM   6379  CE1 HIS B 209      73.149  69.494  48.198  1.00106.29           C  
ANISOU 6379  CE1 HIS B 209    12145  10949  17292  -1263   -320    231       C  
ATOM   6380  NE2 HIS B 209      73.758  70.634  48.465  1.00107.45           N  
ANISOU 6380  NE2 HIS B 209    12247  10888  17693  -1389   -331    271       N  
ATOM   6381  N   ASN B 210      71.062  70.491  45.087  1.00118.02           N  
ANISOU 6381  N   ASN B 210    13577  12385  18882  -1247   -490   1061       N  
ATOM   6382  CA  ASN B 210      71.135  69.350  44.183  1.00116.38           C  
ANISOU 6382  CA  ASN B 210    13358  12567  18293  -1208   -472   1117       C  
ATOM   6383  C   ASN B 210      70.477  68.100  44.764  1.00104.10           C  
ANISOU 6383  C   ASN B 210    11872  11107  16574  -1042   -446    831       C  
ATOM   6384  O   ASN B 210      69.996  67.241  44.027  1.00 99.12           O  
ANISOU 6384  O   ASN B 210    11237  10706  15719   -966   -459    869       O  
ATOM   6385  CB  ASN B 210      72.594  69.064  43.817  1.00125.86           C  
ANISOU 6385  CB  ASN B 210    14500  14048  19271  -1336   -422   1149       C  
ATOM   6386  CG  ASN B 210      72.729  68.132  42.629  1.00134.36           C  
ANISOU 6386  CG  ASN B 210    15526  15539  19984  -1320   -418   1261       C  
ATOM   6387  ND2 ASN B 210      73.565  68.516  41.671  1.00138.90           N  
ANISOU 6387  ND2 ASN B 210    16006  16322  20448  -1459   -419   1517       N  
ATOM   6388  OD1 ASN B 210      72.098  67.077  42.574  1.00136.47           O  
ANISOU 6388  OD1 ASN B 210    15827  15948  20075  -1185   -417   1111       O  
ATOM   6389  N   GLN B 211      70.449  68.010  46.089  1.00102.27           N  
ANISOU 6389  N   GLN B 211    11691  10706  16461   -991   -413    547       N  
ATOM   6390  CA  GLN B 211      69.917  66.832  46.764  1.00105.20           C  
ANISOU 6390  CA  GLN B 211    12113  11165  16692   -848   -385    289       C  
ATOM   6391  C   GLN B 211      68.554  67.088  47.399  1.00104.41           C  
ANISOU 6391  C   GLN B 211    12058  10815  16799   -726   -418    202       C  
ATOM   6392  O   GLN B 211      68.319  66.726  48.552  1.00105.72           O  
ANISOU 6392  O   GLN B 211    12254  10914  17001   -651   -387    -50       O  
ATOM   6393  CB  GLN B 211      70.904  66.340  47.823  1.00109.24           C  
ANISOU 6393  CB  GLN B 211    12633  11748  17127   -869   -319     32       C  
ATOM   6394  CG  GLN B 211      72.220  65.838  47.253  1.00110.86           C  
ANISOU 6394  CG  GLN B 211    12791  12239  17091   -964   -282     73       C  
ATOM   6395  CD  GLN B 211      72.082  64.490  46.573  1.00105.59           C  
ANISOU 6395  CD  GLN B 211    12116  11868  16136   -881   -279     49       C  
ATOM   6396  NE2 GLN B 211      72.583  64.393  45.346  1.00112.81           N  
ANISOU 6396  NE2 GLN B 211    12969  13018  16874   -949   -290    231       N  
ATOM   6397  OE1 GLN B 211      71.539  63.545  47.145  1.00 89.81           O  
ANISOU 6397  OE1 GLN B 211    10150   9892  14080   -760   -271   -135       O  
ATOM   6398  N   CYS B 212      67.657  67.712  46.642  1.00102.44           N  
ANISOU 6398  N   CYS B 212    11799  10446  16678   -706   -481    419       N  
ATOM   6399  CA  CYS B 212      66.304  67.974  47.120  1.00 97.82           C  
ANISOU 6399  CA  CYS B 212    11245   9633  16287   -586   -518    354       C  
ATOM   6400  C   CYS B 212      65.277  67.228  46.274  1.00100.13           C  
ANISOU 6400  C   CYS B 212    11547  10074  16425   -482   -555    454       C  
ATOM   6401  O   CYS B 212      65.417  67.130  45.055  1.00100.01           O  
ANISOU 6401  O   CYS B 212    11494  10242  16264   -525   -583    681       O  
ATOM   6402  CB  CYS B 212      66.010  69.476  47.110  1.00 97.22           C  
ANISOU 6402  CB  CYS B 212    11142   9228  16568   -637   -573    498       C  
ATOM   6403  SG  CYS B 212      66.881  70.418  48.387  1.00104.61           S  
ANISOU 6403  SG  CYS B 212    12059   9916  17771   -724   -541    289       S  
ATOM   6404  N   ALA B 213      64.245  66.702  46.927  1.00103.00           N  
ANISOU 6404  N   ALA B 213    11947  10376  16814   -348   -556    281       N  
ATOM   6405  CA  ALA B 213      63.228  65.916  46.237  1.00107.72           C  
ANISOU 6405  CA  ALA B 213    12547  11106  17274   -244   -591    338       C  
ATOM   6406  C   ALA B 213      62.201  66.799  45.535  1.00115.61           C  
ANISOU 6406  C   ALA B 213    13529  11944  18452   -215   -666    563       C  
ATOM   6407  O   ALA B 213      62.366  67.145  44.366  1.00122.42           O  
ANISOU 6407  O   ALA B 213    14350  12907  19257   -278   -706    828       O  
ATOM   6408  CB  ALA B 213      62.542  64.965  47.203  1.00106.43           C  
ANISOU 6408  CB  ALA B 213    12417  10951  17069   -120   -563     83       C  
ATOM   6409  N   ALA B 214      61.141  67.160  46.251  1.00112.93           N  
ANISOU 6409  N   ALA B 214    13211  11373  18323   -118   -687    464       N  
ATOM   6410  CA  ALA B 214      60.071  67.960  45.667  1.00115.30           C  
ANISOU 6410  CA  ALA B 214    13490  11504  18812    -72   -763    660       C  
ATOM   6411  C   ALA B 214      60.485  69.419  45.513  1.00117.73           C  
ANISOU 6411  C   ALA B 214    13764  11565  19404   -172   -801    844       C  
ATOM   6412  O   ALA B 214      60.640  69.917  44.398  1.00122.01           O  
ANISOU 6412  O   ALA B 214    14261  12152  19945   -242   -849   1150       O  
ATOM   6413  CB  ALA B 214      58.807  67.850  46.506  1.00115.97           C  
ANISOU 6413  CB  ALA B 214    13597  11433  19033     69   -773    478       C  
ATOM   6414  N   GLY B 215      60.660  70.100  46.639  1.00112.51           N  
ANISOU 6414  N   GLY B 215    13108  10650  18991   -179   -782    657       N  
ATOM   6415  CA  GLY B 215      61.053  71.496  46.632  1.00110.70           C  
ANISOU 6415  CA  GLY B 215    12835  10139  19087   -272   -822    788       C  
ATOM   6416  C   GLY B 215      61.953  71.819  47.806  1.00109.28           C  
ANISOU 6416  C   GLY B 215    12654   9843  19023   -332   -769    530       C  
ATOM   6417  O   GLY B 215      62.501  70.920  48.442  1.00112.95           O  
ANISOU 6417  O   GLY B 215    13151  10502  19262   -327   -696    308       O  
ATOM   6418  N   CYS B 216      62.105  73.105  48.099  1.00104.17           N  
ANISOU 6418  N   CYS B 216    11961   8877  18743   -388   -810    555       N  
ATOM   6419  CA  CYS B 216      62.953  73.529  49.204  1.00102.83           C  
ANISOU 6419  CA  CYS B 216    11771   8585  18713   -450   -768    296       C  
ATOM   6420  C   CYS B 216      62.507  74.870  49.773  1.00102.81           C  
ANISOU 6420  C   CYS B 216    11710   8175  19180   -434   -829    216       C  
ATOM   6421  O   CYS B 216      61.829  75.647  49.101  1.00 99.34           O  
ANISOU 6421  O   CYS B 216    11235   7520  18989   -419   -912    451       O  
ATOM   6422  CB  CYS B 216      64.410  73.613  48.752  1.00105.10           C  
ANISOU 6422  CB  CYS B 216    12042   8996  18896   -621   -738    434       C  
ATOM   6423  SG  CYS B 216      64.710  74.848  47.472  1.00116.41           S  
ANISOU 6423  SG  CYS B 216    13403  10246  20583   -761   -824    891       S  
ATOM   6424  N   THR B 217      62.892  75.130  51.018  1.00102.88           N  
ANISOU 6424  N   THR B 217    11693   8084  19312   -433   -792   -124       N  
ATOM   6425  CA  THR B 217      62.585  76.393  51.675  1.00103.09           C  
ANISOU 6425  CA  THR B 217    11643   7729  19798   -419   -849   -273       C  
ATOM   6426  C   THR B 217      63.732  77.372  51.460  1.00106.84           C  
ANISOU 6426  C   THR B 217    12059   8017  20520   -591   -875   -155       C  
ATOM   6427  O   THR B 217      63.568  78.583  51.605  1.00104.74           O  
ANISOU 6427  O   THR B 217    11713   7383  20699   -613   -949   -157       O  
ATOM   6428  CB  THR B 217      62.375  76.201  53.188  1.00102.01           C  
ANISOU 6428  CB  THR B 217    11484   7609  19668   -324   -798   -737       C  
ATOM   6429  CG2 THR B 217      61.591  74.925  53.461  1.00 91.11           C  
ANISOU 6429  CG2 THR B 217    10164   6518  17935   -189   -745   -845       C  
ATOM   6430  OG1 THR B 217      63.647  76.132  53.846  1.00107.59           O  
ANISOU 6430  OG1 THR B 217    12172   8417  20291   -431   -738   -922       O  
ATOM   6431  N   GLY B 218      64.895  76.831  51.112  1.00114.89           N  
ANISOU 6431  N   GLY B 218    13105   9287  21260   -714   -818    -56       N  
ATOM   6432  CA  GLY B 218      66.081  77.631  50.873  1.00121.41           C  
ANISOU 6432  CA  GLY B 218    13873   9988  22268   -892   -833     71       C  
ATOM   6433  C   GLY B 218      67.054  76.921  49.952  1.00123.50           C  
ANISOU 6433  C   GLY B 218    14172  10585  22169  -1009   -787    330       C  
ATOM   6434  O   GLY B 218      66.878  75.741  49.648  1.00128.39           O  
ANISOU 6434  O   GLY B 218    14860  11533  22391   -945   -737    345       O  
ATOM   6435  N   PRO B 219      68.091  77.639  49.499  1.00117.19           N  
ANISOU 6435  N   PRO B 219    13312   9701  21515  -1183   -805    530       N  
ATOM   6436  CA  PRO B 219      69.084  77.121  48.552  1.00114.53           C  
ANISOU 6436  CA  PRO B 219    12981   9676  20860  -1311   -767    798       C  
ATOM   6437  C   PRO B 219      69.943  76.008  49.143  1.00115.31           C  
ANISOU 6437  C   PRO B 219    13128  10114  20570  -1314   -665    536       C  
ATOM   6438  O   PRO B 219      70.327  75.084  48.427  1.00118.03           O  
ANISOU 6438  O   PRO B 219    13505  10805  20538  -1332   -623    673       O  
ATOM   6439  CB  PRO B 219      69.960  78.349  48.277  1.00117.44           C  
ANISOU 6439  CB  PRO B 219    13252   9798  21573  -1495   -814    998       C  
ATOM   6440  CG  PRO B 219      69.773  79.206  49.496  1.00119.76           C  
ANISOU 6440  CG  PRO B 219    13502   9717  22285  -1464   -842    660       C  
ATOM   6441  CD  PRO B 219      68.320  79.063  49.787  1.00117.60           C  
ANISOU 6441  CD  PRO B 219    13268   9334  22081  -1272   -875    535       C  
ATOM   6442  N   ARG B 220      70.233  76.098  50.437  1.00114.63           N  
ANISOU 6442  N   ARG B 220    13035   9939  20580  -1292   -628    156       N  
ATOM   6443  CA  ARG B 220      71.198  75.205  51.075  1.00111.96           C  
ANISOU 6443  CA  ARG B 220    12721   9893  19925  -1316   -539    -80       C  
ATOM   6444  C   ARG B 220      70.728  73.757  51.220  1.00110.75           C  
ANISOU 6444  C   ARG B 220    12648  10061  19372  -1177   -483   -201       C  
ATOM   6445  O   ARG B 220      69.558  73.442  51.010  1.00114.01           O  
ANISOU 6445  O   ARG B 220    13100  10456  19761  -1048   -509   -164       O  
ATOM   6446  CB  ARG B 220      71.640  75.775  52.426  1.00116.86           C  
ANISOU 6446  CB  ARG B 220    13290  10343  20768  -1335   -522   -446       C  
ATOM   6447  CG  ARG B 220      72.416  77.077  52.299  1.00124.98           C  
ANISOU 6447  CG  ARG B 220    14227  11091  22171  -1502   -569   -348       C  
ATOM   6448  CD  ARG B 220      72.922  77.576  53.640  1.00129.40           C  
ANISOU 6448  CD  ARG B 220    14721  11518  22926  -1523   -552   -749       C  
ATOM   6449  NE  ARG B 220      73.773  78.752  53.485  1.00137.96           N  
ANISOU 6449  NE  ARG B 220    15710  12344  24366  -1698   -597   -657       N  
ATOM   6450  CZ  ARG B 220      74.317  79.421  54.496  1.00146.80           C  
ANISOU 6450  CZ  ARG B 220    16745  13299  25733  -1749   -600   -973       C  
ATOM   6451  NH1 ARG B 220      75.079  80.480  54.258  1.00150.18           N1+
ANISOU 6451  NH1 ARG B 220    17079  13476  26505  -1917   -648   -860       N1+
ATOM   6452  NH2 ARG B 220      74.099  79.032  55.744  1.00149.24           N  
ANISOU 6452  NH2 ARG B 220    17051  13706  25948  -1636   -557  -1401       N  
ATOM   6453  N   GLU B 221      71.667  72.887  51.583  1.00113.16           N  
ANISOU 6453  N   GLU B 221    12967  10649  19379  -1206   -409   -343       N  
ATOM   6454  CA  GLU B 221      71.436  71.447  51.664  1.00109.87           C  
ANISOU 6454  CA  GLU B 221    12611  10545  18589  -1096   -358   -435       C  
ATOM   6455  C   GLU B 221      70.456  71.059  52.766  1.00104.30           C  
ANISOU 6455  C   GLU B 221    11929   9797  17902   -938   -346   -718       C  
ATOM   6456  O   GLU B 221      69.850  69.988  52.719  1.00 94.59           O  
ANISOU 6456  O   GLU B 221    10747   8751  16443   -826   -328   -742       O  
ATOM   6457  CB  GLU B 221      72.766  70.731  51.899  1.00114.58           C  
ANISOU 6457  CB  GLU B 221    13197  11418  18919  -1171   -290   -531       C  
ATOM   6458  CG  GLU B 221      73.525  71.264  53.105  1.00130.11           C  
ANISOU 6458  CG  GLU B 221    15116  13294  21028  -1229   -260   -802       C  
ATOM   6459  CD  GLU B 221      74.906  70.659  53.249  1.00143.