CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 19093016532472082

Job options:

ID        	=	 19093016532472082
JOBID     	=	 
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:


CRYST1   64.920   78.100   86.220  90.00  90.00  90.00 P 21 21 21               
ATOM      1  N   THR A   2       2.157  54.960  22.247  1.00 37.51           N  
ATOM      2  CA  THR A   2       2.039  55.924  21.110  1.00 35.62           C  
ATOM      3  C   THR A   2       3.416  56.456  20.698  1.00 33.19           C  
ATOM      4  O   THR A   2       4.390  56.374  21.470  1.00 36.61           O  
ATOM      5  CB  THR A   2       1.139  57.123  21.472  1.00 37.08           C  
ATOM      6  N   GLY A   3       3.508  56.996  19.489  1.00 35.95           N  
ANISOU    6  N   GLY A   3     4630   4945   4083   -735    755   -179       N  
ATOM      7  CA  GLY A   3       4.786  57.476  18.999  1.00 30.02           C  
ANISOU    7  CA  GLY A   3     3904   4129   3370   -635    675   -145       C  
ATOM      8  C   GLY A   3       5.360  58.669  19.769  1.00 24.51           C  
ANISOU    8  C   GLY A   3     3213   3451   2648   -530    614   -111       C  
ATOM      9  O   GLY A   3       4.657  59.411  20.444  1.00 23.56           O  
ANISOU    9  O   GLY A   3     3049   3415   2485   -517    621   -132       O  
ATOM     10  N   TRP A   4       6.671  58.846  19.627  1.00 21.20           N  
ANISOU   10  N   TRP A   4     2844   2952   2258   -456    557    -68       N  
ATOM     11  CA  TRP A   4       7.373  59.970  20.259  1.00 19.02           C  
ANISOU   11  CA  TRP A   4     2574   2686   1965   -360    496    -44       C  
ATOM     12  C   TRP A   4       6.917  61.267  19.608  1.00 18.42           C  
ANISOU   12  C   TRP A   4     2404   2697   1897   -312    456    -95       C  
ATOM     13  O   TRP A   4       6.767  61.327  18.392  1.00 18.89           O  
ANISOU   13  O   TRP A   4     2413   2774   1989   -318    441   -127       O  
ATOM     14  CB  TRP A   4       8.855  59.798  20.000  1.00 18.67           C  
ANISOU   14  CB  TRP A   4     2588   2547   1959   -303    446     -2       C  
ATOM     15  CG  TRP A   4       9.756  60.725  20.768  1.00 17.57           C  
ANISOU   15  CG  TRP A   4     2470   2404   1802   -217    389     24       C  
ATOM     16  CD1 TRP A   4      10.403  60.452  21.924  1.00 18.12           C  
ANISOU   16  CD1 TRP A   4     2611   2435   1837   -192    382     77       C  
ATOM     17  CD2 TRP A   4      10.188  62.046  20.374  1.00 16.27           C  
ANISOU   17  CD2 TRP A   4     2257   2272   1653   -148    331      0       C  
ATOM     18  NE1 TRP A   4      11.172  61.517  22.323  1.00 18.69           N  
ANISOU   18  NE1 TRP A   4     2674   2524   1900   -116    325     76       N  
ATOM     19  CE2 TRP A   4      11.072  62.501  21.366  1.00 16.20           C  
ANISOU   19  CE2 TRP A   4     2289   2244   1620    -91    296     28       C  
ATOM     20  CE3 TRP A   4       9.934  62.875  19.255  1.00 15.82           C  
ANISOU   20  CE3 TRP A   4     2131   2255   1626   -130    305    -41       C  
ATOM     21  CZ2 TRP A   4      11.661  63.749  21.307  1.00 16.45           C  
ANISOU   21  CZ2 TRP A   4     2294   2293   1662    -27    244      9       C  
ATOM     22  CZ3 TRP A   4      10.524  64.105  19.206  1.00 16.08           C  
ANISOU   22  CZ3 TRP A   4     2147   2295   1667    -62    252    -48       C  
ATOM     23  CH2 TRP A   4      11.383  64.532  20.209  1.00 15.84           C  
ANISOU   23  CH2 TRP A   4     2158   2241   1620    -16    225    -27       C  
ATOM     24  N   THR A   5       6.753  62.305  20.412  1.00 17.74           N  
ANISOU   24  N   THR A   5     2299   2660   1780   -259    436   -101       N  
ATOM     25  CA  THR A   5       6.444  63.641  19.893  1.00 18.94           C  
ANISOU   25  CA  THR A   5     2376   2873   1945   -195    392   -141       C  
ATOM     26  C   THR A   5       7.277  64.663  20.645  1.00 17.93           C  
ANISOU   26  C   THR A   5     2278   2723   1812   -116    346   -124       C  
ATOM     27  O   THR A   5       7.949  64.366  21.628  1.00 17.63           O  
ANISOU   27  O   THR A   5     2304   2645   1748   -113    349    -87       O  
ATOM     28  CB  THR A   5       4.956  64.058  20.034  1.00 19.83           C  
ANISOU   28  CB  THR A   5     2404   3098   2033   -214    423   -200       C  
ATOM     29  OG1 THR A   5       4.641  64.322  21.402  1.00 22.10           O  
ANISOU   29  OG1 THR A   5     2705   3418   2274   -211    450   -204       O  
ATOM     30  CG2 THR A   5       4.020  62.995  19.442  1.00 21.63           C  
ANISOU   30  CG2 THR A   5     2594   3364   2258   -308    479   -230       C  
ATOM     31  N   ALA A   6       7.227  65.911  20.198  1.00 18.34           N  
ANISOU   31  N   ALA A   6     2283   2801   1885    -52    302   -150       N  
ATOM     32  CA  ALA A   6       7.985  66.961  20.889  1.00 18.42           C  
ANISOU   32  CA  ALA A   6     2317   2787   1893     15    263   -146       C  
ATOM     33  C   ALA A   6       7.612  67.137  22.366  1.00 19.74           C  
ANISOU   33  C   ALA A   6     2495   2995   2009     15    292   -160       C  
ATOM     34  O   ALA A   6       8.429  67.625  23.142  1.00 20.23           O  
ANISOU   34  O   ALA A   6     2596   3032   2058     52    268   -150       O  
ATOM     35  CB  ALA A   6       7.830  68.316  20.107  1.00 19.34           C  
ANISOU   35  CB  ALA A   6     2385   2917   2046     81    218   -174       C  
ATOM     36  N   ALA A   7       6.428  66.660  22.765  1.00 20.76           N  
ANISOU   36  N   ALA A   7     2591   3192   2103    -35    347   -185       N  
ATOM     37  CA  ALA A   7       6.047  66.662  24.169  1.00 21.58           C  
ANISOU   37  CA  ALA A   7     2708   3343   2146    -52    385   -196       C  
ATOM     38  C   ALA A   7       7.007  65.845  25.040  1.00 20.94           C  
ANISOU   38  C   ALA A   7     2721   3208   2026    -76    390   -133       C  
ATOM     39  O   ALA A   7       7.106  66.061  26.254  1.00 23.64           O  
ANISOU   39  O   ALA A   7     3089   3579   2312    -71    401   -133       O  
ATOM     40  CB  ALA A   7       4.593  66.175  24.347  1.00 23.17           C  
ANISOU   40  CB  ALA A   7     2854   3633   2315   -119    452   -237       C  
ATOM     41  N   ASP A   8       7.730  64.932  24.396  1.00 19.76           N  
ANISOU   41  N   ASP A   8     2619   2982   1905    -97    379    -83       N  
ATOM     42  CA  ASP A   8       8.633  64.012  25.078  1.00 20.07           C  
ANISOU   42  CA  ASP A   8     2749   2961   1916   -111    380    -17       C  
ATOM     43  C   ASP A   8      10.068  64.546  25.105  1.00 20.54           C  
ANISOU   43  C   ASP A   8     2839   2969   1997    -38    311      2       C  
ATOM     44  O   ASP A   8      10.970  63.872  25.582  1.00 21.91           O  
ANISOU   44  O   ASP A   8     3079   3093   2152    -31    296     55       O  
ATOM     45  CB  ASP A   8       8.602  62.640  24.387  1.00 20.84           C  
ANISOU   45  CB  ASP A   8     2882   2997   2039   -172    411     19       C  
ATOM     46  CG  ASP A   8       7.213  62.028  24.383  1.00 22.07           C  
ANISOU   46  CG  ASP A   8     3007   3204   2171   -260    486     -6       C  
ATOM     47  OD1 ASP A   8       6.608  61.922  25.498  1.00 25.20           O  
ANISOU   47  OD1 ASP A   8     3419   3652   2502   -297    531     -3       O  
ATOM     48  OD2 ASP A   8       6.718  61.636  23.314  1.00 21.90           O  
ANISOU   48  OD2 ASP A   8     2946   3181   2191   -299    503    -32       O  
ATOM     49  N   LEU A   9      10.292  65.759  24.608  1.00 19.50           N  
ANISOU   49  N   LEU A   9     2658   2848   1901     14    270    -40       N  
ATOM     50  CA  LEU A   9      11.663  66.281  24.617  1.00 19.57           C  
ANISOU   50  CA  LEU A   9     2690   2813   1931     70    211    -30       C  
ATOM     51  C   LEU A   9      12.237  66.387  26.020  1.00 21.18           C  
ANISOU   51  C   LEU A   9     2936   3037   2072     91    199    -16       C  
ATOM     52  O   LEU A   9      11.554  66.863  26.932  1.00 22.38           O  
ANISOU   52  O   LEU A   9     3074   3254   2174     86    223    -45       O  
ATOM     53  CB  LEU A   9      11.742  67.674  24.006  1.00 19.44           C  
ANISOU   53  CB  LEU A   9     2624   2803   1958    116    177    -80       C  
ATOM     54  CG  LEU A   9      11.940  67.845  22.560  1.00 20.07           C  
ANISOU   54  CG  LEU A   9     2679   2846   2100    122    156    -82       C  
ATOM     55  CD1 LEU A   9      11.721  69.324  22.193  1.00 22.62           C  
ANISOU   55  CD1 LEU A   9     2960   3180   2452    167    132   -126       C  
ATOM     56  CD2 LEU A   9      13.342  67.295  22.037  1.00 16.20           C  
ANISOU   56  CD2 LEU A   9     2225   2289   1640    127    123    -50       C  
ATOM     57  N   PRO A  10      13.500  65.978  26.207  1.00 19.63           N  
ANISOU   57  N   PRO A  10     2785   2797   1876    117    160     21       N  
ATOM     58  CA  PRO A  10      14.162  66.204  27.482  1.00 21.02           C  
ANISOU   58  CA  PRO A  10     2992   3005   1988    146    135     29       C  
ATOM     59  C   PRO A  10      14.588  67.671  27.647  1.00 19.00           C  
ANISOU   59  C   PRO A  10     2695   2779   1745    187    100    -36       C  
ATOM     60  O   PRO A  10      14.514  68.473  26.698  1.00 18.47           O  
ANISOU   60  O   PRO A  10     2586   2690   1742    199     91    -76       O  
ATOM     61  CB  PRO A  10      15.384  65.298  27.404  1.00 21.64           C  
ANISOU   61  CB  PRO A  10     3118   3026   2075    170     97     84       C  
ATOM     62  CG  PRO A  10      15.750  65.328  26.013  1.00 22.30           C  
ANISOU   62  CG  PRO A  10     3173   3055   2242    174     83     69       C  
ATOM     63  CD  PRO A  10      14.419  65.348  25.237  1.00 19.82           C  
ANISOU   63  CD  PRO A  10     2825   2749   1955    127    132     48       C  
ATOM     64  N   SER A  11      15.049  68.014  28.827  1.00 19.55           N  
ANISOU   64  N   SER A  11     2780   2895   1752    206     82    -47       N  
ATOM     65  CA  SER A  11      15.560  69.353  29.071  1.00 18.92           C  
ANISOU   65  CA  SER A  11     2667   2838   1684    239     52   -117       C  
ATOM     66  C   SER A  11      16.808  69.622  28.221  1.00 18.15           C  
ANISOU   66  C   SER A  11     2560   2684   1650    265      3   -123       C  
ATOM     67  O   SER A  11      17.663  68.759  28.033  1.00 19.34           O  
ANISOU   67  O   SER A  11     2736   2806   1804    275    -22    -78       O  
ATOM     68  CB  SER A  11      15.909  69.521  30.537  1.00 20.73           C  
ANISOU   68  CB  SER A  11     2914   3138   1823    249     40   -129       C  
ATOM     69  OG  SER A  11      16.448  70.822  30.805  1.00 20.56           O  
ANISOU   69  OG  SER A  11     2860   3137   1814    273     14   -208       O  
ATOM     70  N   PHE A  12      16.883  70.861  27.702  1.00 16.47           N  
ANISOU   70  N   PHE A  12     2311   2455   1490    276     -4   -184       N  
ATOM     71  CA  PHE A  12      18.078  71.392  27.054  1.00 16.44           C  
ANISOU   71  CA  PHE A  12     2296   2411   1538    290    -43   -207       C  
ATOM     72  C   PHE A  12      18.664  72.563  27.863  1.00 16.22           C  
ANISOU   72  C   PHE A  12     2253   2415   1492    303    -62   -279       C  
ATOM     73  O   PHE A  12      19.444  73.363  27.302  1.00 16.33           O  
ANISOU   73  O   PHE A  12     2252   2395   1557    304    -82   -318       O  
ATOM     74  CB  PHE A  12      17.793  71.822  25.595  1.00 15.72           C  
ANISOU   74  CB  PHE A  12     2185   2260   1526    281    -34   -211       C  
ATOM     75  CG  PHE A  12      17.851  70.678  24.604  1.00 14.81           C  
ANISOU   75  CG  PHE A  12     2079   2109   1437    265    -31   -155       C  
ATOM     76  CD1 PHE A  12      16.850  69.693  24.588  1.00 15.58           C  
ANISOU   76  CD1 PHE A  12     2187   2215   1514    246      2   -114       C  
ATOM     77  CD2 PHE A  12      18.916  70.562  23.687  1.00 15.21           C  
ANISOU   77  CD2 PHE A  12     2124   2119   1533    264    -56   -152       C  
ATOM     78  CE1 PHE A  12      16.947  68.634  23.683  1.00 15.36           C  
ANISOU   78  CE1 PHE A  12     2169   2150   1515    227      8    -73       C  
ATOM     79  CE2 PHE A  12      18.966  69.513  22.803  1.00 15.71           C  
ANISOU   79  CE2 PHE A  12     2193   2153   1621    249    -50   -112       C  
ATOM     80  CZ  PHE A  12      17.994  68.543  22.839  1.00 16.28           C  
ANISOU   80  CZ  PHE A  12     2281   2228   1675    232    -18    -73       C  
ATOM     81  N   ALA A  13      18.356  72.652  29.158  1.00 17.73           N  
ANISOU   81  N   ALA A  13     2450   2675   1610    307    -54   -300       N  
ATOM     82  CA  ALA A  13      18.861  73.735  29.981  1.00 17.70           C  
ANISOU   82  CA  ALA A  13     2429   2709   1585    313    -69   -379       C  
ATOM     83  C   ALA A  13      20.368  73.853  29.907  1.00 19.15           C  
ANISOU   83  C   ALA A  13     2604   2890   1779    320   -117   -398       C  
ATOM     84  O   ALA A  13      21.070  72.849  30.037  1.00 19.70           O  
ANISOU   84  O   ALA A  13     2688   2979   1818    333   -148   -347       O  
ATOM     85  CB  ALA A  13      18.461  73.520  31.457  1.00 19.51           C  
ANISOU   85  CB  ALA A  13     2669   3031   1713    312    -58   -389       C  
ATOM     86  N   GLN A  14      20.860  75.068  29.661  1.00 19.84           N  
ANISOU   86  N   GLN A  14     2670   2952   1915    311   -122   -473       N  
ATOM     87  CA  GLN A  14      22.308  75.349  29.615  1.00 23.01           C  
ANISOU   87  CA  GLN A  14     3052   3361   2327    305   -161   -513       C  
ATOM     88  C   GLN A  14      23.023  74.835  28.362  1.00 21.09           C  
ANISOU   88  C   GLN A  14     2804   3062   2144    300   -177   -472       C  
ATOM     89  O   GLN A  14      24.271  74.841  28.293  1.00 23.88           O  
ANISOU   89  O   GLN A  14     3135   3434   2503    296   -211   -501       O  
ATOM     90  CB  GLN A  14      23.070  74.837  30.860  1.00 25.31           C  
ANISOU   90  CB  GLN A  14     3337   3752   2527    322   -201   -521       C  
ATOM     91  CG  GLN A  14      22.565  75.305  32.202  1.00 30.46           C  
ANISOU   91  CG  GLN A  14     3988   4482   3101    321   -189   -570       C  
ATOM     92  CD  GLN A  14      22.836  76.783  32.455  1.00 37.61           C  
ANISOU   92  CD  GLN A  14     4867   5387   4035    297   -178   -687       C  
ATOM     93  OE1 GLN A  14      23.517  77.448  31.662  1.00 44.80           O  
ANISOU   93  OE1 GLN A  14     5762   6238   5019    277   -182   -727       O  
ATOM     94  NE2 GLN A  14      22.299  77.303  33.558  1.00 41.00           N  
ANISOU   94  NE2 GLN A  14     5291   5880   4405    293   -160   -746       N  
ATOM     95  N   ARG A  15      22.265  74.327  27.401  1.00 17.97           N  
ANISOU   95  N   ARG A  15     2427   2612   1789    298   -154   -411       N  
ATOM     96  CA  ARG A  15      22.849  73.781  26.180  1.00 17.42           C  
ANISOU   96  CA  ARG A  15     2352   2495   1772    290   -163   -376       C  
ATOM     97  C   ARG A  15      22.611  74.753  25.023  1.00 17.22           C  
ANISOU   97  C   ARG A  15     2325   2399   1818    262   -140   -395       C  
ATOM     98  O   ARG A  15      21.577  75.375  24.957  1.00 19.13           O  
ANISOU   98  O   ARG A  15     2577   2616   2074    264   -113   -399       O  
ATOM     99  CB  ARG A  15      22.281  72.397  25.830  1.00 17.14           C  
ANISOU   99  CB  ARG A  15     2338   2448   1727    302   -155   -293       C  
ATOM    100  CG  ARG A  15      22.428  71.397  26.971  1.00 18.53           C  
ANISOU  100  CG  ARG A  15     2532   2679   1828    331   -176   -257       C  
ATOM    101  CD  ARG A  15      21.988  69.992  26.548  1.00 20.06           C  
ANISOU  101  CD  ARG A  15     2755   2842   2023    336   -164   -177       C  
ATOM    102  NE  ARG A  15      23.084  69.438  25.787  1.00 19.61           N  
ANISOU  102  NE  ARG A  15     2684   2758   2009    348   -192   -170       N  
ATOM    103  CZ  ARG A  15      22.953  68.564  24.802  1.00 20.11           C  
ANISOU  103  CZ  ARG A  15     2755   2769   2114    341   -178   -131       C  
ATOM    104  NH1 ARG A  15      21.745  68.084  24.469  1.00 18.56           N  
ANISOU  104  NH1 ARG A  15     2583   2545   1921    318   -136    -90       N  
ATOM    105  NH2 ARG A  15      24.054  68.148  24.176  1.00 19.30           N  
ANISOU  105  NH2 ARG A  15     2632   2650   2049    355   -204   -141       N  
ATOM    106  N   THR A  16      23.563  74.864  24.118  1.00 16.02           N  
ANISOU  106  N   THR A  16     2159   2218   1709    239   -150   -406       N  
ATOM    107  CA  THR A  16      23.504  75.778  22.978  1.00 15.94           C  
ANISOU  107  CA  THR A  16     2155   2141   1760    207   -129   -416       C  
ATOM    108  C   THR A  16      23.303  74.969  21.715  1.00 14.84           C  
ANISOU  108  C   THR A  16     2019   1973   1647    198   -121   -357       C  
ATOM    109  O   THR A  16      24.012  73.985  21.433  1.00 14.50           O  
ANISOU  109  O   THR A  16     1959   1949   1600    198   -137   -340       O  
ATOM    110  CB  THR A  16      24.776  76.614  22.872  1.00 16.07           C  
ANISOU  110  CB  THR A  16     2154   2152   1799    169   -137   -482       C  
ATOM    111  OG1 THR A  16      24.899  77.442  24.055  1.00 19.32           O  
ANISOU  111  OG1 THR A  16     2562   2591   2187    171   -141   -550       O  
ATOM    112  CG2 THR A  16      24.784  77.508  21.603  1.00 17.27           C  
ANISOU  112  CG2 THR A  16     2324   2227   2010    127   -112   -480       C  
ATOM    113  N   VAL A  17      22.312  75.383  20.918  1.00 13.94           N  
ANISOU  113  N   VAL A  17     1922   1815   1559    194    -98   -327       N  
ATOM    114  CA  VAL A  17      21.957  74.729  19.663  1.00 13.81           C  
ANISOU  114  CA  VAL A  17     1906   1779   1562    181    -89   -276       C  
ATOM    115  C   VAL A  17      22.020  75.758  18.551  1.00 13.83           C  
ANISOU  115  C   VAL A  17     1921   1729   1603    151    -77   -276       C  
ATOM    116  O   VAL A  17      21.318  76.779  18.605  1.00 14.44           O  
ANISOU  116  O   VAL A  17     2018   1771   1694    164    -68   -280       O  
ATOM    117  CB  VAL A  17      20.556  74.110  19.716  1.00 13.67           C  
ANISOU  117  CB  VAL A  17     1891   1774   1526    205    -75   -233       C  
ATOM    118  CG1 VAL A  17      20.246  73.409  18.388  1.00 15.27           C  
ANISOU  118  CG1 VAL A  17     2089   1967   1746    185    -65   -191       C  
ATOM    119  CG2 VAL A  17      20.439  73.120  20.913  1.00 15.27           C  
ANISOU  119  CG2 VAL A  17     2094   2024   1682    227    -79   -226       C  
ATOM    120  N   VAL A  18      22.844  75.526  17.532  1.00 13.05           N  
ANISOU  120  N   VAL A  18     1814   1621   1521    112    -76   -271       N  
ATOM    121  CA  VAL A  18      22.873  76.346  16.339  1.00 14.10           C  
ANISOU  121  CA  VAL A  18     1968   1709   1681     77    -63   -255       C  
ATOM    122  C   VAL A  18      21.977  75.721  15.315  1.00 13.36           C  
ANISOU  122  C   VAL A  18     1873   1622   1581     80    -57   -200       C  
ATOM    123  O   VAL A  18      22.130  74.512  15.053  1.00 13.66           O  
ANISOU  123  O   VAL A  18     1887   1694   1608     75    -58   -190       O  
ATOM    124  CB  VAL A  18      24.311  76.472  15.764  1.00 14.28           C  
ANISOU  124  CB  VAL A  18     1977   1732   1716     19    -59   -289       C  
ATOM    125  CG1 VAL A  18      24.313  77.225  14.418  1.00 15.38           C  
ANISOU  125  CG1 VAL A  18     2144   1826   1870    -27    -39   -260       C  
ATOM    126  CG2 VAL A  18      25.207  77.205  16.763  1.00 15.97           C  
ANISOU  126  CG2 VAL A  18     2184   1947   1935      7    -64   -356       C  
ATOM    127  N   ILE A  19      21.071  76.487  14.709  1.00 12.86           N  
ANISOU  127  N   ILE A  19     1833   1526   1525     91    -52   -166       N  
ATOM    128  CA AILE A  19      20.108  75.988  13.708  0.50 11.87           C  
ANISOU  128  CA AILE A  19     1702   1421   1388     97    -51   -116       C  
ATOM    129  CA BILE A  19      20.213  75.946  13.678  0.50 12.94           C  
ANISOU  129  CA BILE A  19     1836   1556   1523     93    -51   -118       C  
ATOM    130  C   ILE A  19      20.179  76.872  12.486  1.00 12.79           C  
ANISOU  130  C   ILE A  19     1847   1500   1510     70    -49    -83       C  
ATOM    131  O   ILE A  19      19.914  78.074  12.592  1.00 14.23           O  
ANISOU  131  O   ILE A  19     2066   1629   1711     89    -51    -75       O  
ATOM    132  CB AILE A  19      18.619  76.014  14.232  0.50 10.90           C  
ANISOU  132  CB AILE A  19     1571   1313   1256    154    -55   -101       C  
ATOM    133  CB BILE A  19      18.814  75.619  14.226  0.50 13.58           C  
ANISOU  133  CB BILE A  19     1902   1664   1590    144    -53   -104       C  
ATOM    134  CG1AILE A  19      18.500  75.292  15.580  0.50 10.95           C  
ANISOU  134  CG1AILE A  19     1560   1354   1248    176    -52   -130       C  
ATOM    135  CG1BILE A  19      17.956  74.967  13.119  0.50 13.66           C  
ANISOU  135  CG1BILE A  19     1894   1711   1585    138    -52    -65       C  
ATOM    136  CG2AILE A  19      17.667  75.383  13.168  0.50 12.91           C  
ANISOU  136  CG2AILE A  19     1804   1606   1492    153    -55    -60       C  
ATOM    137  CG2BILE A  19      18.200  76.820  14.855  0.50 15.83           C  
ANISOU  137  CG2BILE A  19     2208   1914   1891    187    -57   -114       C  
ATOM    138  CD1AILE A  19      17.059  75.271  16.142  0.50 12.54           C  
ANISOU  138  CD1AILE A  19     1746   1582   1436    220    -47   -125       C  
ATOM    139  CD1BILE A  19      16.657  74.448  13.595  0.50 18.19           C  
ANISOU  139  CD1BILE A  19     2441   2325   2143    173    -49    -61       C  
ATOM    140  N   THR A  20      20.485  76.315  11.315  1.00 12.00           N  
ANISOU  140  N   THR A  20     1737   1426   1395     27    -43    -62       N  
ATOM    141  CA  THR A  20      20.400  77.104  10.097  1.00 12.25           C  
ANISOU  141  CA  THR A  20     1801   1433   1418      1    -42    -18       C  
ATOM    142  C   THR A  20      18.945  77.162   9.646  1.00 13.87           C  
ANISOU  142  C   THR A  20     2004   1658   1606     51    -59     30       C  
ATOM    143  O   THR A  20      18.206  76.167   9.747  1.00 13.26           O  
ANISOU  143  O   THR A  20     1885   1637   1513     70    -62     26       O  
ATOM    144  CB  THR A  20      21.292  76.566   8.998  1.00 12.68           C  
ANISOU  144  CB  THR A  20     1843   1519   1454    -68    -26    -19       C  
ATOM    145  OG1 THR A  20      20.842  75.257   8.613  1.00 12.29           O  
ANISOU  145  OG1 THR A  20     1750   1534   1385    -67    -27    -20       O  
ATOM    146  CG2 THR A  20      22.791  76.475   9.454  1.00 14.33           C  
ANISOU  146  CG2 THR A  20     2040   1722   1682   -114    -11    -79       C  
ATOM    147  N   GLY A  21      18.515  78.328   9.180  1.00 15.71           N  
ANISOU  147  N   GLY A  21     2281   1843   1842     73    -70     73       N  
ATOM    148  CA  GLY A  21      17.122  78.448   8.758  1.00 17.95           C  
ANISOU  148  CA  GLY A  21     2555   2154   2109    133    -93    117       C  
ATOM    149  C   GLY A  21      16.921  79.113   7.473  1.00 19.91           C  
ANISOU  149  C   GLY A  21     2841   2391   2332    127   -108    183       C  
ATOM    150  O   GLY A  21      17.779  79.825   6.992  1.00 20.62           O  
ANISOU  150  O   GLY A  21     2983   2426   2424     81    -96    205       O  
ATOM    151  N   ALA A  22      15.744  78.847   6.900  1.00 21.57           N  
ANISOU  151  N   ALA A  22     3019   2662   2512    171   -133    217       N  
ATOM    152  CA  ALA A  22      15.316  79.412   5.650  1.00 23.54           C  
ANISOU  152  CA  ALA A  22     3298   2921   2724    181   -158    289       C  
ATOM    153  C   ALA A  22      14.061  80.271   5.879  1.00 26.82           C  
ANISOU  153  C   ALA A  22     3720   3315   3154    288   -195    321       C  
ATOM    154  O   ALA A  22      13.350  80.577   4.913  1.00 29.06           O  
ANISOU  154  O   ALA A  22     4009   3632   3400    324   -229    382       O  
ATOM    155  CB  ALA A  22      15.065  78.252   4.655  1.00 24.66           C  
ANISOU  155  CB  ALA A  22     3385   3175   2808    138   -160    291       C  
ATOM    156  N   ASN A  23      13.851  80.706   7.132  1.00 28.00           N  
ANISOU  156  N   ASN A  23     3871   3411   3357    339   -190    279       N  
ATOM    157  CA  ASN A  23      12.689  81.535   7.593  1.00 30.43           C  
ANISOU  157  CA  ASN A  23     4175   3692   3693    449   -219    287       C  
ATOM    158  C   ASN A  23      11.371  80.868   7.193  1.00 30.13           C  
ANISOU  158  C   ASN A  23     4059   3771   3618    498   -248    291       C  
ATOM    159  O   ASN A  23      10.394  81.483   6.720  1.00 32.46           O  
ANISOU  159  O   ASN A  23     4348   4078   3905    581   -289    333       O  
ATOM    160  CB  ASN A  23      12.818  83.016   7.175  1.00 31.81           C  
ANISOU  160  CB  ASN A  23     4440   3751   3892    490   -236    350       C  
ATOM    161  CG  ASN A  23      13.604  83.872   8.219  1.00 34.06           C  
ANISOU  161  CG  ASN A  23     4782   3916   4242    481   -205    306       C  
ATOM    162  OD1 ASN A  23      13.334  83.832   9.431  1.00 36.17           O  
ANISOU  162  OD1 ASN A  23     5016   4181   4546    515   -194    237       O  
ATOM    163  ND2 ASN A  23      14.577  84.630   7.741  1.00 30.87           N  
ANISOU  163  ND2 ASN A  23     4462   3419   3847    426   -189    343       N  
ATOM    164  N   SER A  24      11.383  79.560   7.404  1.00 28.38           N  
ANISOU  164  N   SER A  24     3774   3635   3373    443   -225    244       N  
ATOM    165  CA  SER A  24      10.258  78.744   7.150  1.00 27.42           C  
ANISOU  165  CA  SER A  24     3570   3628   3217    463   -239    228       C  
ATOM    166  C   SER A  24       9.892  77.987   8.427  1.00 24.13           C  
ANISOU  166  C   SER A  24     3101   3244   2822    460   -208    153       C  
ATOM    167  O   SER A  24      10.604  77.998   9.468  1.00 22.16           O  
ANISOU  167  O   SER A  24     2878   2936   2605    440   -179    117       O  
ATOM    168  CB  SER A  24      10.564  77.800   5.995  1.00 27.70           C  
ANISOU  168  CB  SER A  24     3586   3739   3198    385   -236    244       C  
ATOM    169  OG  SER A  24       9.369  77.241   5.479  1.00 32.88           O  
ANISOU  169  OG  SER A  24     4165   4511   3814    409   -258    237       O  
ATOM    170  N   GLY A  25       8.766  77.329   8.320  1.00 22.41           N  
ANISOU  170  N   GLY A  25     2806   3128   2578    478   -215    130       N  
ATOM    171  CA  GLY A  25       8.119  76.736   9.401  1.00 21.02           C  
ANISOU  171  CA  GLY A  25     2576   2997   2413    483   -189     68       C  
ATOM    172  C   GLY A  25       8.933  75.677  10.089  1.00 18.70           C  
ANISOU  172  C   GLY A  25     2292   2691   2122    401   -143     33       C  
ATOM    173  O   GLY A  25       8.927  75.608  11.284  1.00 18.79           O  
ANISOU  173  O   GLY A  25     2303   2684   2152    408   -119     -4       O  
ATOM    174  N   LEU A  26       9.588  74.817   9.330  1.00 17.50           N  
ANISOU  174  N   LEU A  26     2145   2555   1947    327   -131     45       N  
ATOM    175  CA  LEU A  26      10.312  73.686   9.889  1.00 17.42           C  
ANISOU  175  CA  LEU A  26     2142   2536   1941    257    -92     14       C  
ATOM    176  C   LEU A  26      11.366  74.141  10.926  1.00 16.20           C  
ANISOU  176  C   LEU A  26     2042   2293   1819    261    -80      6       C  
ATOM    177  O   LEU A  26      11.404  73.659  12.062  1.00 16.20           O  
ANISOU  177  O   LEU A  26     2039   2290   1825    255    -56    -25       O  
ATOM    178  CB  LEU A  26      11.002  72.904   8.743  1.00 19.03           C  
ANISOU  178  CB  LEU A  26     2349   2758   2123    186    -86     26       C  
ATOM    179  CG  LEU A  26      11.797  71.680   9.110  1.00 17.52           C  
ANISOU  179  CG  LEU A  26     2164   2550   1940    121    -49     -2       C  
ATOM    180  CD1 LEU A  26      10.922  70.623   9.810  1.00 21.76           C  
ANISOU  180  CD1 LEU A  26     2661   3135   2473    104    -19    -39       C  
ATOM    181  CD2 LEU A  26      12.430  71.071   7.818  1.00 19.26           C  
ANISOU  181  CD2 LEU A  26     2383   2793   2142     59    -45      1       C  
ATOM    182  N   GLY A  27      12.189  75.089  10.488  1.00 16.24           N  
ANISOU  182  N   GLY A  27     2097   2234   1838    268    -98     35       N  
ATOM    183  CA  GLY A  27      13.220  75.675  11.339  1.00 16.29           C  
ANISOU  183  CA  GLY A  27     2152   2162   1874    268    -90     22       C  
ATOM    184  C   GLY A  27      12.647  76.398  12.537  1.00 14.76           C  
ANISOU  184  C   GLY A  27     1957   1947   1702    328    -90     -6       C  
ATOM    185  O   GLY A  27      13.185  76.271  13.666  1.00 15.01           O  
ANISOU  185  O   GLY A  27     2001   1959   1743    319    -73    -41       O  
ATOM    186  N   ALA A  28      11.588  77.153  12.318  1.00 15.74           N  
ANISOU  186  N   ALA A  28     2066   2083   1832    393   -110      4       N  
ATOM    187  CA  ALA A  28      10.985  77.921  13.386  1.00 15.65           C  
ANISOU  187  CA  ALA A  28     2049   2053   1844    457   -109    -31       C  
ATOM    188  C   ALA A  28      10.464  77.020  14.497  1.00 16.02           C  
ANISOU  188  C   ALA A  28     2049   2163   1872    445    -80    -79       C  
ATOM    189  O   ALA A  28      10.685  77.306  15.678  1.00 16.00           O  
ANISOU  189  O   ALA A  28     2059   2139   1880    455    -64   -119       O  
ATOM    190  CB  ALA A  28       9.879  78.808  12.865  1.00 17.72           C  
ANISOU  190  CB  ALA A  28     2294   2321   2118    538   -139    -12       C  
ATOM    191  N   VAL A  29       9.774  75.942  14.143  1.00 15.51           N  
ANISOU  191  N   VAL A  29     1935   2180   1777    416    -70    -79       N  
ATOM    192  CA  VAL A  29       9.241  75.020  15.146  1.00 15.06           C  
ANISOU  192  CA  VAL A  29     1841   2181   1697    392    -35   -118       C  
ATOM    193  C   VAL A  29      10.369  74.294  15.877  1.00 14.54           C  
ANISOU  193  C   VAL A  29     1815   2083   1623    338    -13   -122       C  
ATOM    194  O   VAL A  29      10.331  74.091  17.089  1.00 15.23           O  
ANISOU  194  O   VAL A  29     1905   2182   1699    335      8   -151       O  
ATOM    195  CB  VAL A  29       8.224  74.032  14.562  1.00 16.02           C  
ANISOU  195  CB  VAL A  29     1901   2394   1790    364    -23   -122       C  
ATOM    196  CG1 VAL A  29       7.787  72.986  15.624  1.00 17.28           C  
ANISOU  196  CG1 VAL A  29     2038   2603   1925    320     22   -157       C  
ATOM    197  CG2 VAL A  29       6.999  74.783  13.980  1.00 17.94           C  
ANISOU  197  CG2 VAL A  29     2091   2690   2037    433    -51   -127       C  
ATOM    198  N   THR A  30      11.418  73.914  15.131  1.00 13.77           N  
ANISOU  198  N   THR A  30     1749   1950   1531    296    -21    -92       N  
ATOM    199  CA  THR A  30      12.535  73.223  15.743  1.00 13.34           C  
ANISOU  199  CA  THR A  30     1726   1868   1472    256     -8    -96       C  
ATOM    200  C   THR A  30      13.160  74.140  16.836  1.00 14.05           C  
ANISOU  200  C   THR A  30     1848   1916   1574    285    -14   -121       C  
ATOM    201  O   THR A  30      13.402  73.701  17.959  1.00 14.06           O  
ANISOU  201  O   THR A  30     1856   1928   1555    277      0   -140       O  
ATOM    202  CB  THR A  30      13.588  72.830  14.705  1.00 13.14           C  
ANISOU  202  CB  THR A  30     1720   1814   1456    214    -17    -72       C  
ATOM    203  OG1 THR A  30      12.974  72.034  13.661  1.00 14.28           O  
ANISOU  203  OG1 THR A  30     1833   2003   1586    184    -11    -59       O  
ATOM    204  CG2 THR A  30      14.693  72.019  15.335  1.00 13.66           C  
ANISOU  204  CG2 THR A  30     1809   1859   1520    184     -8    -80       C  
ATOM    205  N   ALA A  31      13.375  75.406  16.482  1.00 13.36           N  
ANISOU  205  N   ALA A  31     1779   1780   1515    316    -33   -121       N  
ATOM    206  CA  ALA A  31      13.893  76.398  17.430  1.00 13.51           C  
ANISOU  206  CA  ALA A  31     1825   1754   1551    339    -36   -156       C  
ATOM    207  C   ALA A  31      12.963  76.602  18.600  1.00 15.01           C  
ANISOU  207  C   ALA A  31     1992   1982   1727    377    -20   -197       C  
ATOM    208  O   ALA A  31      13.411  76.617  19.763  1.00 15.36           O  
ANISOU  208  O   ALA A  31     2046   2032   1756    372    -10   -233       O  
ATOM    209  CB  ALA A  31      14.141  77.726  16.711  1.00 14.56           C  
ANISOU  209  CB  ALA A  31     1990   1817   1722    362    -53   -144       C  
ATOM    210  N   ARG A  32      11.676  76.768  18.301  1.00 15.11           N  
ANISOU  210  N   ARG A  32     1968   2030   1742    415    -19   -197       N  
ATOM    211  CA  ARG A  32      10.650  77.039  19.326  1.00 16.16           C  
ANISOU  211  CA  ARG A  32     2065   2208   1864    453      0   -246       C  
ATOM    212  C   ARG A  32      10.654  75.933  20.382  1.00 15.67           C  
ANISOU  212  C   ARG A  32     1994   2206   1753    409     29   -262       C  
ATOM    213  O   ARG A  32      10.609  76.210  21.600  1.00 15.75           O  
ANISOU  213  O   ARG A  32     2004   2234   1743    419     46   -306       O  
ATOM    214  CB  ARG A  32       9.262  77.191  18.669  1.00 17.36           C  
ANISOU  214  CB  ARG A  32     2165   2407   2024    498     -6   -244       C  
ATOM    215  CG  ARG A  32       8.142  77.533  19.612  1.00 21.41           C  
ANISOU  215  CG  ARG A  32     2630   2975   2530    542     14   -304       C  
ATOM    216  CD  ARG A  32       6.787  77.372  18.912  1.00 23.89           C  
ANISOU  216  CD  ARG A  32     2875   3361   2841    575      8   -305       C  
ATOM    217  NE  ARG A  32       6.411  75.945  18.797  1.00 23.59           N  
ANISOU  217  NE  ARG A  32     2802   3401   2758    504     35   -294       N  
ATOM    218  CZ  ARG A  32       5.541  75.442  17.917  1.00 26.43           C  
ANISOU  218  CZ  ARG A  32     3107   3827   3106    499     30   -284       C  
ATOM    219  NH1 ARG A  32       4.939  76.209  16.998  1.00 28.36           N  
ANISOU  219  NH1 ARG A  32     3321   4078   3376    567     -8   -275       N  
ATOM    220  NH2 ARG A  32       5.258  74.158  17.976  1.00 27.29           N  
ANISOU  220  NH2 ARG A  32     3192   3996   3178    425     64   -285       N  
ATOM    221  N   GLU A  33      10.645  74.664  19.953  1.00 14.53           N  
ANISOU  221  N   GLU A  33     1843   2094   1583    360     40   -226       N  
ATOM    222  CA  GLU A  33      10.527  73.560  20.898  1.00 14.75           C  
ANISOU  222  CA  GLU A  33     1870   2169   1562    318     71   -228       C  
ATOM    223  C   GLU A  33      11.799  73.398  21.723  1.00 14.53           C  
ANISOU  223  C   GLU A  33     1890   2111   1517    302     64   -225       C  
ATOM    224  O   GLU A  33      11.734  73.123  22.925  1.00 16.01           O  
ANISOU  224  O   GLU A  33     2085   2335   1662    294     83   -242       O  
ATOM    225  CB  GLU A  33      10.189  72.257  20.179  1.00 15.18           C  
ANISOU  225  CB  GLU A  33     1911   2250   1603    268     88   -193       C  
ATOM    226  CG  GLU A  33       8.832  72.252  19.486  1.00 16.47           C  
ANISOU  226  CG  GLU A  33     2015   2470   1770    276     98   -206       C  
ATOM    227  CD  GLU A  33       7.636  72.206  20.432  1.00 22.26           C  
ANISOU  227  CD  GLU A  33     2704   3279   2472    278    134   -251       C  
ATOM    228  OE1 GLU A  33       7.777  71.881  21.608  1.00 22.27           O  
ANISOU  228  OE1 GLU A  33     2727   3295   2438    257    161   -262       O  
ATOM    229  OE2 GLU A  33       6.495  72.420  19.944  1.00 28.00           O  
ANISOU  229  OE2 GLU A  33     3368   4063   3205    298    138   -275       O  
ATOM    230  N   LEU A  34      12.966  73.567  21.112  1.00 13.70           N  
ANISOU  230  N   LEU A  34     1814   1950   1441    297     36   -205       N  
ATOM    231  CA  LEU A  34      14.187  73.488  21.907  1.00 13.83           C  
ANISOU  231  CA  LEU A  34     1863   1950   1441    288     24   -212       C  
ATOM    232  C   LEU A  34      14.310  74.643  22.920  1.00 14.04           C  
ANISOU  232  C   LEU A  34     1892   1977   1462    318     20   -268       C  
ATOM    233  O   LEU A  34      14.720  74.450  24.086  1.00 15.71           O  
ANISOU  233  O   LEU A  34     2116   2221   1631    313     22   -287       O  
ATOM    234  CB  LEU A  34      15.421  73.453  20.991  1.00 13.56           C  
ANISOU  234  CB  LEU A  34     1848   1865   1440    272     -1   -192       C  
ATOM    235  CG  LEU A  34      15.496  72.194  20.158  1.00 13.66           C  
ANISOU  235  CG  LEU A  34     1859   1877   1452    240      3   -149       C  
ATOM    236  CD1 LEU A  34      16.547  72.347  19.049  1.00 17.08           C  
ANISOU  236  CD1 LEU A  34     2299   2268   1922    223    -16   -140       C  
ATOM    237  CD2 LEU A  34      15.814  70.974  21.069  1.00 18.06           C  
ANISOU  237  CD2 LEU A  34     2434   2455   1969    225     12   -131       C  
ATOM    238  N   ALA A  35      13.936  75.856  22.514  1.00 14.36           N  
ANISOU  238  N   ALA A  35     2023   1881   1552     79    121   -397       N  
ATOM    239  CA  ALA A  35      13.960  76.984  23.428  1.00 14.65           C  
ANISOU  239  CA  ALA A  35     2022   1948   1595    171     41   -401       C  
ATOM    240  C   ALA A  35      12.975  76.777  24.602  1.00 15.09           C  
ANISOU  240  C   ALA A  35     2060   2076   1595    184     53   -416       C  
ATOM    241  O   ALA A  35      13.262  77.173  25.729  1.00 15.26           O  
ANISOU  241  O   ALA A  35     2078   2102   1619    255     19   -412       O  
ATOM    242  CB  ALA A  35      13.646  78.316  22.668  1.00 15.56           C  
ANISOU  242  CB  ALA A  35     2097   2094   1719    202    -21   -417       C  
ATOM    243  N   ARG A  36      11.809  76.199  24.325  1.00 16.02           N  
ANISOU  243  N   ARG A  36     2159   2271   1655    104    102   -441       N  
ATOM    244  CA AARG A  36      10.815  75.911  25.389  0.50 16.19           C  
ANISOU  244  CA AARG A  36     2161   2376   1613     97    123   -459       C  
ATOM    245  CA BARG A  36      10.799  75.854  25.354  0.50 16.74           C  
ANISOU  245  CA BARG A  36     2231   2445   1681     91    128   -459       C  
ATOM    246  C   ARG A  36      11.395  74.957  26.450  1.00 15.80           C  
ANISOU  246  C   ARG A  36     2188   2244   1569    114    188   -424       C  
ATOM    247  O   ARG A  36      10.953  74.981  27.605  1.00 16.61           O  
ANISOU  247  O   ARG A  36     2279   2393   1637    154    184   -424       O  
ATOM    248  CB AARG A  36       9.528  75.317  24.765  0.50 17.65           C  
ANISOU  248  CB AARG A  36     2304   2685   1716    -30    182   -506       C  
ATOM    249  CB BARG A  36       9.626  75.119  24.652  0.50 18.64           C  
ANISOU  249  CB BARG A  36     2442   2793   1845    -48    198   -505       C  
ATOM    250  CG AARG A  36       8.434  74.868  25.720  0.50 21.15           C  
ANISOU  250  CG AARG A  36     2723   3233   2079    -75    224   -534       C  
ATOM    251  CG BARG A  36       8.599  74.423  25.539  0.50 23.41           C  
ANISOU  251  CG BARG A  36     3042   3480   2370   -118    262   -534       C  
ATOM    252  CD AARG A  36       7.266  74.054  25.064  0.50 22.21           C  
ANISOU  252  CD AARG A  36     2816   3508   2112   -256    310   -600       C  
ATOM    253  CD BARG A  36       7.492  73.669  24.751  0.50 28.87           C  
ANISOU  253  CD BARG A  36     3695   4306   2966   -302    347   -603       C  
ATOM    254  NE AARG A  36       7.680  72.855  24.270  0.50 23.14           N  
ANISOU  254  NE AARG A  36     3033   3519   2240   -407    430   -620       N  
ATOM    255  NE BARG A  36       7.457  72.215  25.022  0.50 30.98           N  
ANISOU  255  NE BARG A  36     4081   4480   3209   -450    500   -623       N  
ATOM    256  CZ AARG A  36       7.860  71.624  24.778  0.50 25.72           C  
ANISOU  256  CZ AARG A  36     3492   3719   2562   -496    565   -618       C  
ATOM    257  CZ BARG A  36       8.324  71.329  24.531  0.50 29.16           C  
ANISOU  257  CZ BARG A  36     3982   4072   3024   -502    597   -604       C  
ATOM    258  NH1AARG A  36       7.687  71.402  26.085  0.50 27.15           N  
ANISOU  258  NH1AARG A  36     3712   3875   2728   -447    590   -592       N  
ATOM    259  NH1BARG A  36       9.300  71.747  23.735  0.50 20.78           N  
ANISOU  259  NH1BARG A  36     2925   2931   2038   -429    540   -569       N  
ATOM    260  NH2AARG A  36       8.262  70.621  23.978  0.50 26.55           N  
ANISOU  260  NH2AARG A  36     3707   3706   2672   -620    687   -636       N  
ATOM    261  NH2BARG A  36       8.231  70.030  24.834  0.50 27.39           N  
ANISOU  261  NH2BARG A  36     3898   3741   2765   -623    764   -618       N  
ATOM    262  N   ARG A  37      12.365  74.128  26.037  1.00 16.16           N  
ANISOU  262  N   ARG A  37     2316   2177   1648     99    255   -388       N  
ATOM    263  CA  ARG A  37      13.040  73.174  26.928  1.00 17.56           C  
ANISOU  263  CA  ARG A  37     2581   2276   1814    154    337   -332       C  
ATOM    264  C   ARG A  37      14.349  73.718  27.505  1.00 17.01           C  
ANISOU  264  C   ARG A  37     2486   2200   1775    292    269   -288       C  
ATOM    265  O   ARG A  37      15.118  72.962  28.107  1.00 18.70           O  
ANISOU  265  O   ARG A  37     2759   2378   1967    374    334   -226       O  
ATOM    266  CB  ARG A  37      13.231  71.834  26.236  1.00 19.24           C  
ANISOU  266  CB  ARG A  37     2915   2377   2016     74    483   -314       C  
ATOM    267  CG  ARG A  37      11.886  71.149  25.830  1.00 23.70           C  
ANISOU  267  CG  ARG A  37     3509   2972   2523   -104    579   -380       C  
ATOM    268  CD  ARG A  37      10.977  70.904  26.934  1.00 30.23           C  
ANISOU  268  CD  ARG A  37     4337   3857   3291   -124    616   -392       C  
ATOM    269  NE  ARG A  37      11.446  69.814  27.769  1.00 34.78           N  
ANISOU  269  NE  ARG A  37     5059   4309   3845    -72    752   -326       N  
ATOM    270  CZ  ARG A  37      11.293  69.707  29.083  1.00 36.23           C  
ANISOU  270  CZ  ARG A  37     5255   4514   3995     12    765   -288       C  
ATOM    271  NH1 ARG A  37      10.673  70.653  29.812  1.00 37.86           N  
ANISOU  271  NH1 ARG A  37     5332   4861   4189     50    643   -318       N  
ATOM    272  NH2 ARG A  37      11.768  68.630  29.685  1.00 34.84           N  
ANISOU  272  NH2 ARG A  37     5233   4215   3788     74    914   -214       N  
ATOM    273  N   GLY A  38      14.573  75.028  27.383  1.00 16.27           N  
ANISOU  273  N   GLY A  38     2310   2157   1715    321    151   -322       N  
ATOM    274  CA  GLY A  38      15.688  75.692  28.035  1.00 16.24           C  
ANISOU  274  CA  GLY A  38     2264   2185   1720    412     86   -311       C  
ATOM    275  C   GLY A  38      16.944  75.875  27.221  1.00 15.59           C  
ANISOU  275  C   GLY A  38     2176   2072   1674    419     68   -297       C  
ATOM    276  O   GLY A  38      17.947  76.378  27.753  1.00 17.06           O  
ANISOU  276  O   GLY A  38     2314   2318   1848    474     22   -299       O  
ATOM    277  N   ALA A  39      16.918  75.517  25.942  1.00 15.34           N  
ANISOU  277  N   ALA A  39     2182   1969   1675    354    102   -291       N  
ATOM    278  CA  ALA A  39      18.114  75.691  25.101  1.00 15.06           C  
ANISOU  278  CA  ALA A  39     2139   1909   1672    358     86   -277       C  
ATOM    279  C   ALA A  39      18.403  77.152  24.814  1.00 14.92           C  
ANISOU  279  C   ALA A  39     2064   1915   1689    335     -7   -329       C  
ATOM    280  O   ALA A  39      17.488  77.967  24.653  1.00 15.94           O  
ANISOU  280  O   ALA A  39     2184   2039   1830    305    -43   -369       O  
ATOM    281  CB  ALA A  39      17.968  74.990  23.747  1.00 14.80           C  
ANISOU  281  CB  ALA A  39     2163   1795   1664    287    148   -265       C  
ATOM    282  N   THR A  40      19.686  77.481  24.681  1.00 15.35           N  
ANISOU  282  N   THR A  40     2087   1995   1748    349    -33   -327       N  
ATOM    283  CA  THR A  40      20.110  78.736  24.067  1.00 15.77           C  
ANISOU  283  CA  THR A  40     2119   2034   1838    294    -88   -376       C  
ATOM    284  C   THR A  40      20.216  78.440  22.575  1.00 14.56           C  
ANISOU  284  C   THR A  40     1997   1808   1727    250    -64   -352       C  
ATOM    285  O   THR A  40      21.123  77.737  22.146  1.00 15.47           O  
ANISOU  285  O   THR A  40     2111   1926   1838    264    -35   -314       O  
ATOM    286  CB  THR A  40      21.449  79.219  24.626  1.00 17.08           C  
ANISOU  286  CB  THR A  40     2224   2292   1971    297   -118   -402       C  
ATOM    287  OG1 THR A  40      21.296  79.513  26.038  1.00 20.59           O  
ANISOU  287  OG1 THR A  40     2631   2825   2365    331   -140   -435       O  
ATOM    288  CG2 THR A  40      21.912  80.471  23.908  1.00 21.21           C  
ANISOU  288  CG2 THR A  40     2752   2776   2530    211   -148   -461       C  
ATOM    289  N   VAL A  41      19.279  78.968  21.790  1.00 15.36           N  
ANISOU  289  N   VAL A  41     2120   1860   1856    213    -73   -369       N  
ATOM    290  CA  VAL A  41      19.210  78.691  20.348  1.00 14.40           C  
ANISOU  290  CA  VAL A  41     2017   1692   1762    170    -50   -350       C  
ATOM    291  C   VAL A  41      19.777  79.862  19.565  1.00 14.17           C  
ANISOU  291  C   VAL A  41     1990   1626   1766    144    -83   -368       C  
ATOM    292  O   VAL A  41      19.452  81.023  19.865  1.00 15.86           O  
ANISOU  292  O   VAL A  41     2219   1826   1981    154   -107   -400       O  
ATOM    293  CB  VAL A  41      17.772  78.419  19.875  1.00 14.51           C  
ANISOU  293  CB  VAL A  41     2036   1721   1756    147    -27   -355       C  
ATOM    294  CG1 VAL A  41      17.736  78.151  18.365  1.00 16.72           C  
ANISOU  294  CG1 VAL A  41     2319   1983   2049     94     -4   -345       C  
ATOM    295  CG2 VAL A  41      17.142  77.243  20.641  1.00 16.41           C  
ANISOU  295  CG2 VAL A  41     2291   1986   1956    141     25   -348       C  
ATOM    296  N   ILE A  42      20.672  79.573  18.635  1.00 14.13           N  
ANISOU  296  N   ILE A  42     1983   1599   1783    114    -71   -348       N  
ATOM    297  CA  ILE A  42      21.210  80.561  17.695  1.00 15.33           C  
ANISOU  297  CA  ILE A  42     2149   1709   1967     77    -86   -358       C  
ATOM    298  C   ILE A  42      20.657  80.203  16.317  1.00 14.84           C  
ANISOU  298  C   ILE A  42     2096   1624   1917     62    -64   -329       C  
ATOM    299  O   ILE A  42      21.040  79.164  15.747  1.00 15.04           O  
ANISOU  299  O   ILE A  42     2116   1653   1945     43    -35   -306       O  
ATOM    300  CB  ILE A  42      22.737  80.549  17.690  1.00 15.60           C  
ANISOU  300  CB  ILE A  42     2153   1770   2002     47    -92   -363       C  
ATOM    301  CG1 ILE A  42      23.281  80.904  19.076  1.00 18.29           C  
ANISOU  301  CG1 ILE A  42     2458   2184   2305     51   -113   -404       C  
ATOM    302  CG2 ILE A  42      23.285  81.510  16.623  1.00 18.08           C  
ANISOU  302  CG2 ILE A  42     2491   2031   2347    -11    -93   -375       C  
ATOM    303  CD1 ILE A  42      24.772  80.590  19.247  1.00 20.55           C  
ANISOU  303  CD1 ILE A  42     2678   2577   2554     38   -117   -405       C  
ATOM    304  N   MET A  43      19.712  81.011  15.827  1.00 15.40           N  
ANISOU  304  N   MET A  43     2181   1687   1979     83    -68   -330       N  
ATOM    305  CA AMET A  43      19.126  80.820  14.514  0.50 16.55           C  
ANISOU  305  CA AMET A  43     2315   1857   2114     76    -51   -306       C  
ATOM    306  CA BMET A  43      19.077  80.859  14.537  0.50 17.18           C  
ANISOU  306  CA BMET A  43     2395   1938   2192     78    -52   -307       C  
ATOM    307  C   MET A  43      19.934  81.621  13.524  1.00 16.29           C  
ANISOU  307  C   MET A  43     2310   1766   2113     64    -51   -289       C  
ATOM    308  O   MET A  43      20.055  82.843  13.649  1.00 19.01           O  
ANISOU  308  O   MET A  43     2705   2054   2464     91    -49   -293       O  
ATOM    309  CB AMET A  43      17.678  81.302  14.485  0.50 18.95           C  
ANISOU  309  CB AMET A  43     2603   2232   2364    134    -51   -303       C  
ATOM    310  CB BMET A  43      17.684  81.511  14.663  0.50 20.18           C  
ANISOU  310  CB BMET A  43     2767   2378   2521    145    -55   -305       C  
ATOM    311  CG AMET A  43      17.054  81.333  13.123  0.50 21.02           C  
ANISOU  311  CG AMET A  43     2830   2567   2587    143    -37   -279       C  
ATOM    312  CG BMET A  43      16.685  81.314  13.548  0.50 24.25           C  
ANISOU  312  CG BMET A  43     3232   2999   2979    157    -39   -287       C  
ATOM    313  SD AMET A  43      16.812  79.687  12.531  0.50 25.22           S  
ANISOU  313  SD AMET A  43     3311   3177   3094     36     -3   -303       S  
ATOM    314  SD BMET A  43      15.391  82.620  13.663  0.50 35.04           S  
ANISOU  314  SD BMET A  43     4599   4443   4271    298    -40   -260       S  
ATOM    315  CE AMET A  43      16.328  79.066  14.188  0.50 13.27           C  
ANISOU  315  CE AMET A  43     1804   1671   1566     29      1   -334       C  
ATOM    316  CE BMET A  43      14.265  81.963  14.890  0.50 34.85           C  
ANISOU  316  CE BMET A  43     4518   4534   4189    296    -49   -297       C  
ATOM    317  N   ALA A  44      20.472  80.942  12.521  1.00 14.70           N  
ANISOU  317  N   ALA A  44     2090   1569   1926     21    -38   -273       N  
ATOM    318  CA  ALA A  44      21.400  81.530  11.550  1.00 14.77           C  
ANISOU  318  CA  ALA A  44     2118   1528   1964     -3    -34   -256       C  
ATOM    319  C   ALA A  44      20.704  81.596  10.203  1.00 14.66           C  
ANISOU  319  C   ALA A  44     2089   1554   1926     15    -19   -225       C  
ATOM    320  O   ALA A  44      20.431  80.556   9.590  1.00 14.91           O  
ANISOU  320  O   ALA A  44     2079   1646   1939    -19     -5   -227       O  
ATOM    321  CB  ALA A  44      22.660  80.675  11.507  1.00 16.12           C  
ANISOU  321  CB  ALA A  44     2269   1698   2159    -51    -32   -257       C  
ATOM    322  N   VAL A  45      20.361  82.822   9.767  1.00 14.92           N  
ANISOU  322  N   VAL A  45     2162   1560   1945     75     -8   -198       N  
ATOM    323  CA  VAL A  45      19.462  83.058   8.637  1.00 15.66           C  
ANISOU  323  CA  VAL A  45     2229   1735   1983    137      8   -157       C  
ATOM    324  C   VAL A  45      19.946  84.192   7.756  1.00 16.19           C  
ANISOU  324  C   VAL A  45     2365   1725   2060    179     40   -110       C  
ATOM    325  O   VAL A  45      20.678  85.067   8.212  1.00 17.27           O  
ANISOU  325  O   VAL A  45     2592   1732   2236    164     60   -119       O  
ATOM    326  CB  VAL A  45      18.036  83.371   9.111  1.00 16.34           C  
ANISOU  326  CB  VAL A  45     2292   1919   1995    233      9   -149       C  
ATOM    327  CG1 VAL A  45      17.475  82.169   9.877  1.00 18.84           C  
ANISOU  327  CG1 VAL A  45     2542   2323   2293    172     -8   -198       C  
ATOM    328  CG2 VAL A  45      17.946  84.665   9.974  1.00 18.99           C  
ANISOU  328  CG2 VAL A  45     2726   2152   2335    319     28   -138       C  
ATOM    329  N   ARG A  46      19.512  84.193   6.495  1.00 18.15           N  
ANISOU  329  N   ARG A  46     2574   2059   2260    224     55    -66       N  
ATOM    330  CA AARG A  46      19.876  85.236   5.537  0.50 20.32           C  
ANISOU  330  CA AARG A  46     2921   2266   2531    283     99     -6       C  
ATOM    331  CA BARG A  46      19.929  85.244   5.592  0.50 20.17           C  
ANISOU  331  CA BARG A  46     2906   2240   2517    278     99     -8       C  
ATOM    332  C   ARG A  46      19.170  86.537   5.865  1.00 21.25           C  
ANISOU  332  C   ARG A  46     3138   2333   2602    429    152     42       C  
ATOM    333  O   ARG A  46      19.785  87.624   5.856  1.00 23.66           O  
ANISOU  333  O   ARG A  46     3582   2471   2935    444    214     63       O  
ATOM    334  CB AARG A  46      19.503  84.792   4.116  0.50 21.35           C  
ANISOU  334  CB AARG A  46     2964   2541   2604    307    101     31       C  
ATOM    335  CB BARG A  46      19.796  84.801   4.139  0.50 20.91           C  
ANISOU  335  CB BARG A  46     2923   2451   2569    285    101     27       C  
ATOM    336  CG AARG A  46      19.992  85.699   2.966  0.50 25.93           C  
ANISOU  336  CG AARG A  46     3611   3061   3179    364    150    102       C  
ATOM    337  CG BARG A  46      20.518  85.713   3.153  0.50 25.26           C  
ANISOU  337  CG BARG A  46     3555   2906   3134    315    149     86       C  
ATOM    338  CD AARG A  46      19.376  85.250   1.624  0.50 30.51           C  
ANISOU  338  CD AARG A  46     4079   3839   3672    410    147    140       C  
ATOM    339  CD BARG A  46      20.409  85.194   1.716  0.50 29.07           C  
ANISOU  339  CD BARG A  46     3947   3527   3571    319    145    117       C  
ATOM    340  NE AARG A  46      20.117  85.682   0.433  0.50 34.75           N  
ANISOU  340  NE AARG A  46     4652   4328   4220    418    181    193       N  
ATOM    341  NE BARG A  46      19.120  84.570   1.418  0.50 34.76           N  
ANISOU  341  NE BARG A  46     4539   4478   4188    371    125    113       N  
ATOM    342  CZ AARG A  46      20.850  84.884  -0.350  0.50 35.62           C  
ANISOU  342  CZ AARG A  46     4704   4465   4364    306    158    167       C  
ATOM    343  CZ BARG A  46      18.000  85.243   1.161  0.50 38.74           C  
ANISOU  343  CZ BARG A  46     5021   5116   4581    535    152    175       C  
ATOM    344  NH1AARG A  46      20.979  83.589  -0.087  0.50 33.66           N  
ANISOU  344  NH1AARG A  46     4374   4272   4142    181    115     89       N  
ATOM    345  NH1BARG A  46      18.000  86.569   1.179  0.50 41.65           N  
ANISOU  345  NH1BARG A  46     5516   5371   4935    682    213    256       N  
ATOM    346  NH2AARG A  46      21.473  85.392  -1.404  0.50 37.57           N  
ANISOU  346  NH2AARG A  46     4988   4671   4614    326    193    222       N  
ATOM    347  NH2BARG A  46      16.874  84.590   0.885  0.50 40.18           N  
ANISOU  347  NH2BARG A  46     5056   5558   4651    553    131    154       N  
ATOM    348  N   ASP A  47      17.867  86.445   6.135  1.00 21.01           N  
ANISOU  348  N   ASP A  47     3047   2449   2487    537    143     58       N  
ATOM    349  CA  ASP A  47      17.009  87.620   6.360  1.00 22.54           C  
ANISOU  349  CA  ASP A  47     3326   2632   2606    725    203    121       C  
ATOM    350  C   ASP A  47      16.779  87.747   7.855  1.00 22.33           C  
ANISOU  350  C   ASP A  47     3341   2539   2603    713    191     68       C  
ATOM    351  O   ASP A  47      15.846  87.152   8.443  1.00 22.67           O  
ANISOU  351  O   ASP A  47     3284   2735   2595    736    148     43       O  
ATOM    352  CB  ASP A  47      15.672  87.495   5.606  1.00 23.85           C  
ANISOU  352  CB  ASP A  47     3370   3059   2629    878    204    182       C  
ATOM    353  CG  ASP A  47      14.776  88.725   5.748  1.00 26.90           C  
ANISOU  353  CG  ASP A  47     3847   3458   2914   1122    280    271       C  
ATOM    354  OD1 ASP A  47      14.972  89.574   6.662  1.00 27.01           O  
ANISOU  354  OD1 ASP A  47     4020   3272   2968   1163    331    268       O  
ATOM    355  OD2 ASP A  47      13.842  88.858   4.903  1.00 31.73           O  
ANISOU  355  OD2 ASP A  47     4368   4298   3387   1287    299    347       O  
ATOM    356  N   THR A  48      17.660  88.502   8.481  1.00 22.20           N  
ANISOU  356  N   THR A  48     3470   2306   2658    659    232     39       N  
ATOM    357  CA  THR A  48      17.627  88.666   9.936  1.00 21.98           C  
ANISOU  357  CA  THR A  48     3487   2207   2656    626    223    -24       C  
ATOM    358  C   THR A  48      16.478  89.537  10.431  1.00 23.60           C  
ANISOU  358  C   THR A  48     3765   2421   2778    814    277     19       C  
ATOM    359  O   THR A  48      16.029  89.374  11.565  1.00 23.11           O  
ANISOU  359  O   THR A  48     3682   2388   2710    815    248    -25       O  
ATOM    360  CB  THR A  48      18.957  89.195  10.490  1.00 22.14           C  
ANISOU  360  CB  THR A  48     3623   2029   2758    480    255    -90       C  
ATOM    361  OG1 THR A  48      19.229  90.484   9.911  1.00 26.05           O  
ANISOU  361  OG1 THR A  48     4297   2358   3241    535    369    -46       O  
ATOM    362  CG2 THR A  48      20.129  88.236  10.225  1.00 22.89           C  
ANISOU  362  CG2 THR A  48     3624   2152   2921    307    193   -136       C  
ATOM    363  N   ARG A  49      15.968  90.440   9.607  1.00 24.66           N  
ANISOU  363  N   ARG A  49     3986   2545   2838    993    362    114       N  
ATOM    364  CA  ARG A  49      14.824  91.247  10.010  1.00 26.35           C  
ANISOU  364  CA  ARG A  49     4268   2791   2950   1215    425    174       C  
ATOM    365  C   ARG A  49      13.612  90.333  10.216  1.00 26.17           C  
ANISOU  365  C   ARG A  49     4037   3065   2841   1277    338    175       C  
ATOM    366  O   ARG A  49      12.915  90.420  11.244  1.00 25.50           O  
ANISOU  366  O   ARG A  49     3946   3022   2720   1337    329    152       O  
ATOM    367  CB  ARG A  49      14.549  92.343   8.969  1.00 29.09           C  
ANISOU  367  CB  ARG A  49     4753   3085   3215   1427    550    297       C  
ATOM    368  N   LYS A  50      13.347  89.467   9.245  1.00 25.67           N  
ANISOU  368  N   LYS A  50     3804   3213   2735   1249    283    191       N  
ATOM    369  CA  LYS A  50      12.244  88.519   9.342  1.00 26.03           C  
ANISOU  369  CA  LYS A  50     3645   3558   2687   1256    213    170       C  
ATOM    370  C   LYS A  50      12.497  87.555  10.511  1.00 24.59           C  
ANISOU  370  C   LYS A  50     3408   3343   2589   1064    141     62       C  
ATOM    371  O   LYS A  50      11.583  87.256  11.281  1.00 24.78           O  
ANISOU  371  O   LYS A  50     3355   3509   2550   1096    115     37       O  
ATOM    372  CB  LYS A  50      12.139  87.722   8.045  1.00 27.67           C  
ANISOU  372  CB  LYS A  50     3699   3971   2843   1202    181    180       C  
ATOM    373  CG  LYS A  50      10.961  86.784   7.928  1.00 32.23           C  
ANISOU  373  CG  LYS A  50     4060   4892   3294   1184    132    147       C  
ATOM    374  CD  LYS A  50      10.942  86.137   6.524  1.00 38.85           C  
ANISOU  374  CD  LYS A  50     4764   5925   4071   1123    120    150       C  
ATOM    375  CE  LYS A  50       9.890  85.034   6.392  1.00 42.48           C  
ANISOU  375  CE  LYS A  50     5006   6731   4404   1025     82     78       C  
ATOM    376  NZ  LYS A  50      10.145  84.167   5.177  1.00 45.35           N  
ANISOU  376  NZ  LYS A  50     5261   7224   4745    878     73     37       N  
ATOM    377  N   GLY A  51      13.726  87.070  10.619  1.00 21.54           N  
ANISOU  377  N   GLY A  51     3061   2789   2331    879    115      4       N  
ATOM    378  CA  GLY A  51      14.065  86.145  11.707  1.00 20.87           C  
ANISOU  378  CA  GLY A  51     2936   2675   2317    723     60    -81       C  
ATOM    379  C   GLY A  51      13.812  86.732  13.090  1.00 20.85           C  
ANISOU  379  C   GLY A  51     3008   2593   2321    775     68   -105       C  
ATOM    380  O   GLY A  51      13.217  86.083  13.967  1.00 20.55           O  
ANISOU  380  O   GLY A  51     2893   2653   2259    746     31   -146       O  
ATOM    381  N   GLU A  52      14.276  87.958  13.299  1.00 20.83           N  
ANISOU  381  N   GLU A  52     3165   2403   2344    840    129    -87       N  
ATOM    382  CA  GLU A  52      14.120  88.605  14.590  1.00 21.82           C  
ANISOU  382  CA  GLU A  52     3381   2435   2473    879    151   -121       C  
ATOM    383  C   GLU A  52      12.646  88.880  14.884  1.00 22.67           C  
ANISOU  383  C   GLU A  52     3449   2702   2463   1065    163    -77       C  
ATOM    384  O   GLU A  52      12.197  88.718  16.027  1.00 22.88           O  
ANISOU  384  O   GLU A  52     3450   2764   2477   1066    137   -119       O  
ATOM    385  CB  GLU A  52      14.963  89.885  14.641  1.00 23.65           C  
ANISOU  385  CB  GLU A  52     3817   2420   2748    880    241   -126       C  
ATOM    386  CG  GLU A  52      14.843  90.725  15.874  1.00 25.01           C  
ANISOU  386  CG  GLU A  52     4116   2472   2915    914    291   -171       C  
ATOM    387  CD  GLU A  52      15.338  90.041  17.126  1.00 24.62           C  
ANISOU  387  CD  GLU A  52     3995   2439   2920    758    218   -269       C  
ATOM    388  OE1 GLU A  52      15.944  88.968  17.059  1.00 24.92           O  
ANISOU  388  OE1 GLU A  52     3910   2548   3007    624    142   -299       O  
ATOM    389  OE2 GLU A  52      15.140  90.650  18.186  1.00 27.93           O  
ANISOU  389  OE2 GLU A  52     4496   2791   3324    783    251   -313       O  
ATOM    390  N   ALA A  53      11.866  89.285  13.887  1.00 23.09           N  
ANISOU  390  N   ALA A  53     3480   2877   2413   1236    203     11       N  
ATOM    391  CA  ALA A  53      10.447  89.537  14.159  1.00 25.10           C  
ANISOU  391  CA  ALA A  53     3671   3335   2528   1432    216     58       C  
ATOM    392  C   ALA A  53       9.753  88.268  14.686  1.00 25.35           C  
ANISOU  392  C   ALA A  53     3503   3601   2526   1325    126     -3       C  
ATOM    393  O   ALA A  53       8.853  88.355  15.528  1.00 27.22           O  
ANISOU  393  O   ALA A  53     3701   3951   2690   1411    120     -9       O  
ATOM    394  CB  ALA A  53       9.708  90.093  12.909  1.00 27.48           C  
ANISOU  394  CB  ALA A  53     3949   3798   2694   1652    273    173       C  
ATOM    395  N   ALA A  54      10.166  87.105  14.208  1.00 24.50           N  
ANISOU  395  N   ALA A  54     3285   3556   2465   1138     71    -49       N  
ATOM    396  CA  ALA A  54       9.603  85.835  14.698  1.00 24.70           C  
ANISOU  396  CA  ALA A  54     3158   3762   2464   1005     15   -117       C  
ATOM    397  C   ALA A  54      10.204  85.404  16.041  1.00 23.30           C  
ANISOU  397  C   ALA A  54     3033   3427   2392    880    -12   -186       C  
ATOM    398  O   ALA A  54       9.473  85.048  16.974  1.00 24.34           O  
ANISOU  398  O   ALA A  54     3106   3661   2478    878    -31   -218       O  
ATOM    399  CB  ALA A  54       9.754  84.742  13.684  1.00 24.95           C  
ANISOU  399  CB  ALA A  54     3079   3910   2491    856     -3   -143       C  
ATOM    400  N   ALA A  55      11.515  85.503  16.173  1.00 20.95           N  
ANISOU  400  N   ALA A  55     2839   2902   2217    789    -12   -207       N  
ATOM    401  CA  ALA A  55      12.200  85.016  17.367  1.00 20.35           C  
ANISOU  401  CA  ALA A  55     2790   2716   2224    676    -40   -268       C  
ATOM    402  C   ALA A  55      11.842  85.795  18.618  1.00 21.29           C  
ANISOU  402  C   ALA A  55     2973   2789   2326    763    -32   -284       C  
ATOM    403  O   ALA A  55      11.816  85.228  19.737  1.00 20.78           O  
ANISOU  403  O   ALA A  55     2877   2740   2276    703    -60   -329       O  
ATOM    404  CB  ALA A  55      13.713  85.045  17.145  1.00 20.47           C  
ANISOU  404  CB  ALA A  55     2881   2549   2347    572    -39   -285       C  
ATOM    405  N   ARG A  56      11.575  87.093  18.489  1.00 20.65           N  
ANISOU  405  N   ARG A  56     2994   2641   2208    910     18   -245       N  
ATOM    406  CA  ARG A  56      11.390  87.934  19.676  1.00 21.46           C  
ANISOU  406  CA  ARG A  56     3192   2659   2302    984     44   -270       C  
ATOM    407  C   ARG A  56      10.127  87.590  20.474  1.00 21.42           C  
ANISOU  407  C   ARG A  56     3088   2839   2208   1061     18   -272       C  
ATOM    408  O   ARG A  56      10.018  87.998  21.616  1.00 21.45           O  
ANISOU  408  O   ARG A  56     3146   2791   2212   1090     24   -307       O  
ATOM    409  CB  ARG A  56      11.412  89.433  19.337  1.00 23.89           C  
ANISOU  409  CB  ARG A  56     3674   2816   2584   1130    139   -227       C  
ATOM    410  CG  ARG A  56      10.279  89.867  18.482  1.00 26.47           C  
ANISOU  410  CG  ARG A  56     3979   3286   2792   1341    180   -131       C  
ATOM    411  CD  ARG A  56      10.512  91.290  17.956  1.00 32.47           C  
ANISOU  411  CD  ARG A  56     4950   3853   3534   1487    301    -72       C  
ATOM    412  NE  ARG A  56      10.510  92.246  19.046  1.00 36.06           N  
ANISOU  412  NE  ARG A  56     5573   4139   3989   1544    373   -107       N  
ATOM    413  CZ  ARG A  56       9.412  92.748  19.609  1.00 41.48           C  
ANISOU  413  CZ  ARG A  56     6282   4907   4571   1744    411    -70       C  
ATOM    414  NH1 ARG A  56       8.192  92.410  19.175  1.00 42.63           N  
ANISOU  414  NH1 ARG A  56     6275   5332   4590   1914    381      7       N  
ATOM    415  NH2 ARG A  56       9.541  93.605  20.607  1.00 45.42           N  
ANISOU  415  NH2 ARG A  56     6953   5223   5079   1770    486   -117       N  
ATOM    416  N   THR A  57       9.169  86.880  19.871  1.00 21.51           N  
ANISOU  416  N   THR A  57     2955   3082   2134   1085     -5   -243       N  
ATOM    417  CA  THR A  57       7.962  86.426  20.574  1.00 22.05           C  
ANISOU  417  CA  THR A  57     2908   3365   2105   1125    -29   -255       C  
ATOM    418  C   THR A  57       7.980  84.934  20.951  1.00 21.28           C  
ANISOU  418  C   THR A  57     2698   3354   2033    932    -73   -314       C  
ATOM    419  O   THR A  57       6.988  84.426  21.476  1.00 22.77           O  
ANISOU  419  O   THR A  57     2784   3727   2137    928    -85   -333       O  
ATOM    420  CB  THR A  57       6.697  86.718  19.757  1.00 24.88           C  
ANISOU  420  CB  THR A  57     3167   3979   2306   1289     -8   -192       C  
ATOM    421  OG1 THR A  57       6.720  85.947  18.570  1.00 26.71           O  
ANISOU  421  OG1 THR A  57     3293   4338   2516   1192    -20   -189       O  
ATOM    422  CG2 THR A  57       6.631  88.197  19.417  1.00 28.47           C  
ANISOU  422  CG2 THR A  57     3761   4334   2719   1520     62   -115       C  
ATOM    423  N   MET A  58       9.077  84.235  20.705  1.00 19.47           N  
ANISOU  423  N   MET A  58     2495   2994   1908    779    -84   -339       N  
ATOM    424  CA  MET A  58       9.217  82.834  21.104  1.00 19.33           C  
ANISOU  424  CA  MET A  58     2418   3010   1916    616    -96   -384       C  
ATOM    425  C   MET A  58       9.618  82.755  22.564  1.00 18.64           C  
ANISOU  425  C   MET A  58     2377   2827   1878    599   -111   -414       C  
ATOM    426  O   MET A  58      10.553  83.441  22.990  1.00 19.29           O  
ANISOU  426  O   MET A  58     2549   2751   2030    621   -118   -421       O  
ATOM    427  CB  MET A  58      10.264  82.131  20.251  1.00 20.17           C  
ANISOU  427  CB  MET A  58     2546   3017   2101    494    -88   -386       C  
ATOM    428  CG  MET A  58       9.851  81.995  18.814  1.00 20.66           C  
ANISOU  428  CG  MET A  58     2544   3198   2106    483    -73   -366       C  
ATOM    429  SD  MET A  58      11.093  81.029  17.887  1.00 23.32           S  
ANISOU  429  SD  MET A  58     2912   3413   2535    331    -56   -376       S  
ATOM    430  CE  MET A  58      10.250  80.750  16.301  1.00 24.92           C  
ANISOU  430  CE  MET A  58     3005   3828   2633    302    -34   -373       C  
ATOM    431  N   ALA A  59       8.915  81.920  23.339  1.00 17.99           N  
ANISOU  431  N   ALA A  59     2232   2854   1747    549   -109   -439       N  
ATOM    432  CA  ALA A  59       9.339  81.614  24.703  1.00 16.71           C  
ANISOU  432  CA  ALA A  59     2104   2619   1625    526   -119   -462       C  
ATOM    433  C   ALA A  59      10.742  81.001  24.745  1.00 16.33           C  
ANISOU  433  C   ALA A  59     2109   2424   1669    441   -114   -463       C  
ATOM    434  O   ALA A  59      11.138  80.224  23.834  1.00 17.00           O  
ANISOU  434  O   ALA A  59     2194   2488   1778    358    -88   -453       O  
ATOM    435  CB  ALA A  59       8.327  80.700  25.403  1.00 18.90           C  
ANISOU  435  CB  ALA A  59     2311   3039   1829    475   -101   -483       C  
ATOM    436  N   GLY A  60      11.507  81.323  25.777  1.00 16.17           N  
ANISOU  436  N   GLY A  60     2130   2325   1687    465   -133   -477       N  
ATOM    437  CA  GLY A  60      12.885  80.880  25.854  1.00 15.47           C  
ANISOU  437  CA  GLY A  60     2071   2144   1659    414   -131   -474       C  
ATOM    438  C   GLY A  60      13.813  81.803  25.047  1.00 15.98           C  
ANISOU  438  C   GLY A  60     2180   2114   1775    413   -144   -478       C  
ATOM    439  O   GLY A  60      13.435  82.927  24.705  1.00 15.85           O  
ANISOU  439  O   GLY A  60     2198   2073   1750    467   -146   -485       O  
ATOM    440  N   GLN A  61      15.011  81.308  24.772  1.00 15.92           N  
ANISOU  440  N   GLN A  61     2179   2058   1810    359   -139   -470       N  
ATOM    441  CA  GLN A  61      16.113  82.108  24.201  1.00 16.45           C  
ANISOU  441  CA  GLN A  61     2281   2047   1920    333   -148   -485       C  
ATOM    442  C   GLN A  61      16.417  81.724  22.752  1.00 15.81           C  
ANISOU  442  C   GLN A  61     2204   1932   1871    293   -132   -450       C  
ATOM    443  O   GLN A  61      17.114  80.737  22.497  1.00 17.12           O  
ANISOU  443  O   GLN A  61     2353   2099   2051    255   -117   -428       O  
ATOM    444  CB  GLN A  61      17.340  81.967  25.078  1.00 16.43           C  
ANISOU  444  CB  GLN A  61     2259   2064   1919    307   -161   -510       C  
ATOM    445  CG  GLN A  61      17.125  82.597  26.426  1.00 17.98           C  
ANISOU  445  CG  GLN A  61     2453   2299   2080    334   -177   -559       C  
ATOM    446  CD  GLN A  61      18.346  82.524  27.312  1.00 19.21           C  
ANISOU  446  CD  GLN A  61     2562   2526   2210    305   -191   -594       C  
ATOM    447  OE1 GLN A  61      18.418  81.685  28.199  1.00 18.68           O  
ANISOU  447  OE1 GLN A  61     2444   2548   2104    346   -194   -571       O  
ATOM    448  NE2 GLN A  61      19.337  83.404  27.060  1.00 18.86           N  
ANISOU  448  NE2 GLN A  61     2532   2459   2173    232   -191   -650       N  
ATOM    449  N   VAL A  62      15.832  82.454  21.783  1.00 16.68           N  
ANISOU  449  N   VAL A  62     2338   2019   1978    319   -124   -439       N  
ATOM    450  CA  VAL A  62      16.170  82.262  20.359  1.00 17.09           C  
ANISOU  450  CA  VAL A  62     2392   2045   2056    284   -110   -410       C  
ATOM    451  C   VAL A  62      16.794  83.560  19.861  1.00 17.25           C  
ANISOU  451  C   VAL A  62     2481   1969   2103    293   -102   -417       C  
ATOM    452  O   VAL A  62      16.100  84.583  19.740  1.00 18.18           O  
ANISOU  452  O   VAL A  62     2649   2062   2194    369    -83   -410       O  
ATOM    453  CB  VAL A  62      14.947  81.904  19.500  1.00 15.87           C  
ANISOU  453  CB  VAL A  62     2195   1979   1852    303    -96   -385       C  
ATOM    454  CG1 VAL A  62      15.379  81.649  18.061  1.00 18.13           C  
ANISOU  454  CG1 VAL A  62     2477   2249   2160    260    -81   -361       C  
ATOM    455  CG2 VAL A  62      14.216  80.678  20.050  1.00 18.52           C  
ANISOU  455  CG2 VAL A  62     2481   2406   2148    263    -81   -395       C  
ATOM    456  N   GLU A  63      18.108  83.520  19.619  1.00 16.67           N  
ANISOU  456  N   GLU A  63     2416   1844   2071    222   -103   -430       N  
ATOM    457  CA  GLU A  63      18.885  84.631  19.073  1.00 17.33           C  
ANISOU  457  CA  GLU A  63     2571   1831   2180    190    -80   -446       C  
ATOM    458  C   GLU A  63      18.986  84.492  17.571  1.00 18.41           C  
ANISOU  458  C   GLU A  63     2709   1948   2336    184    -66   -398       C  
ATOM    459  O   GLU A  63      19.138  83.400  17.095  1.00 19.12           O  
ANISOU  459  O   GLU A  63     2738   2091   2434    157    -79   -375       O  
ATOM    460  CB  GLU A  63      20.313  84.681  19.666  1.00 17.58           C  
ANISOU  460  CB  GLU A  63     2588   1865   2226     95    -89   -499       C  
ATOM    461  CG  GLU A  63      21.159  85.851  19.133  1.00 22.45           C  
ANISOU  461  CG  GLU A  63     3285   2386   2859     20    -48   -536       C  
ATOM    462  CD  GLU A  63      22.636  85.794  19.480  1.00 24.51           C  
ANISOU  462  CD  GLU A  63     3496   2704   3111    -96    -56   -594       C  
ATOM    463  OE1 GLU A  63      23.079  84.872  20.207  1.00 25.29           O  
ANISOU  463  OE1 GLU A  63     3494   2929   3185    -94    -96   -597       O  
ATOM    464  OE2 GLU A  63      23.352  86.722  19.013  1.00 25.16           O  
ANISOU  464  OE2 GLU A  63     3644   2715   3200   -188    -12   -636       O  
ATOM    465  N   VAL A  64      18.911  85.596  16.845  1.00 18.39           N  
ANISOU  465  N   VAL A  64     2791   1862   2335    214    -25   -383       N  
ATOM    466  CA  VAL A  64      19.065  85.590  15.387  1.00 18.71           C  
ANISOU  466  CA  VAL A  64     2835   1886   2386    216     -8   -334       C  
ATOM    467  C   VAL A  64      20.409  86.211  14.986  1.00 18.31           C  
ANISOU  467  C   VAL A  64     2844   1736   2375    123     19   -359       C  
ATOM    468  O   VAL A  64      20.765  87.321  15.434  1.00 19.80           O  
ANISOU  468  O   VAL A  64     3135   1824   2564     94     67   -400       O  
ATOM    469  CB  VAL A  64      17.915  86.360  14.768  1.00 19.82           C  
ANISOU  469  CB  VAL A  64     3024   2030   2477    347     30   -280       C  
ATOM    470  CG1 VAL A  64      18.104  86.546  13.274  1.00 21.17           C  
ANISOU  470  CG1 VAL A  64     3207   2188   2647    364     57   -225       C  
ATOM    471  CG2 VAL A  64      16.614  85.608  15.033  1.00 22.36           C  
ANISOU  471  CG2 VAL A  64     3249   2505   2740    414     -1   -264       C  
ATOM    472  N   ARG A  65      21.142  85.488  14.129  1.00 17.33           N  
ANISOU  472  N   ARG A  65     2663   1644   2277     64      1   -340       N  
ATOM    473  CA  ARG A  65      22.409  85.978  13.553  1.00 17.32           C  
ANISOU  473  CA  ARG A  65     2698   1579   2303    -29     27   -358       C  
ATOM    474  C   ARG A  65      22.373  85.784  12.048  1.00 17.38           C  
ANISOU  474  C   ARG A  65     2698   1585   2320     -7     39   -296       C  
ATOM    475  O   ARG A  65      21.694  84.892  11.528  1.00 16.95           O  
ANISOU  475  O   ARG A  65     2574   1613   2253     41     13   -257       O  
ATOM    476  CB  ARG A  65      23.611  85.243  14.130  1.00 17.59           C  
ANISOU  476  CB  ARG A  65     2648   1690   2344   -123     -8   -402       C  
ATOM    477  CG  ARG A  65      23.801  85.396  15.616  1.00 18.00           C  
ANISOU  477  CG  ARG A  65     2685   1783   2371   -152    -22   -467       C  
ATOM    478  CD  ARG A  65      25.107  84.832  16.080  1.00 19.22           C  
ANISOU  478  CD  ARG A  65     2745   2051   2504   -228    -48   -503       C  
ATOM    479  NE  ARG A  65      25.146  84.808  17.547  1.00 19.60           N  
ANISOU  479  NE  ARG A  65     2755   2179   2511   -232    -68   -557       N  
ATOM    480  CZ  ARG A  65      26.067  84.185  18.271  1.00 20.64           C  
ANISOU  480  CZ  ARG A  65     2782   2464   2595   -252    -95   -579       C  
ATOM    481  NH1 ARG A  65      27.101  83.594  17.705  1.00 20.37           N  
ANISOU  481  NH1 ARG A  65     2674   2518   2544   -272   -102   -556       N  
ATOM    482  NH2 ARG A  65      25.937  84.155  19.592  1.00 21.92           N  
ANISOU  482  NH2 ARG A  65     2907   2709   2713   -236   -112   -619       N  
ATOM    483  N   GLU A  66      23.152  86.593  11.350  1.00 19.03           N  
ANISOU  483  N   GLU A  66     2976   1708   2544    -61     84   -296       N  
ATOM    484  CA AGLU A  66      23.212  86.545   9.889  0.50 18.43           C  
ANISOU  484  CA AGLU A  66     2900   1628   2473    -40    102   -235       C  
ATOM    485  CA BGLU A  66      23.217  86.560   9.890  0.50 19.67           C  
ANISOU  485  CA BGLU A  66     3058   1784   2631    -40    102   -235       C  
ATOM    486  C   GLU A  66      24.095  85.427   9.388  1.00 18.24           C  
ANISOU  486  C   GLU A  66     2773   1685   2472   -112     58   -237       C  
ATOM    487  O   GLU A  66      25.238  85.261   9.842  1.00 19.50           O  
ANISOU  487  O   GLU A  66     2901   1864   2643   -207     45   -284       O  
ATOM    488  CB AGLU A  66      23.751  87.865   9.325  0.50 19.91           C  
ANISOU  488  CB AGLU A  66     3222   1677   2665    -73    186   -230       C  
ATOM    489  CB BGLU A  66      23.740  87.918   9.378  0.50 21.68           C  
ANISOU  489  CB BGLU A  66     3452   1895   2888    -73    188   -232       C  
ATOM    490  CG AGLU A  66      23.431  88.066   7.862  0.50 18.06           C  
ANISOU  490  CG AGLU A  66     3012   1432   2417      4    219   -146       C  
ATOM    491  CG BGLU A  66      24.494  87.914   8.060  0.50 25.76           C  
ANISOU  491  CG BGLU A  66     3965   2400   3421   -120    208   -197       C  
ATOM    492  CD AGLU A  66      24.036  89.319   7.291  0.50 26.43           C  
ANISOU  492  CD AGLU A  66     4224   2336   3479    -32    322   -134       C  
ATOM    493  CD BGLU A  66      23.642  87.603   6.888  0.50 29.10           C  
ANISOU  493  CD BGLU A  66     4355   2881   3821      1    203   -111       C  
ATOM    494  OE1AGLU A  66      24.126  90.329   8.017  0.50 31.67           O  
ANISOU  494  OE1AGLU A  66     5025   2869   4136    -62    397   -176       O  
ATOM    495  OE1BGLU A  66      22.405  87.744   7.045  0.50 34.04           O  
ANISOU  495  OE1BGLU A  66     4989   3542   4403    132    209    -73       O  
ATOM    496  OE2AGLU A  66      24.422  89.281   6.099  0.50 31.11           O  
ANISOU  496  OE2AGLU A  66     4810   2933   4077    -37    337    -87       O  
ATOM    497  OE2BGLU A  66      24.189  87.222   5.812  0.50 25.82           O  
ANISOU  497  OE2BGLU A  66     3893   2499   3415    -32    196    -83       O  
ATOM    498  N   LEU A  67      23.549  84.673   8.441  1.00 17.78           N  
ANISOU  498  N   LEU A  67     2658   1691   2404    -62     43   -190       N  
ATOM    499  CA  LEU A  67      24.272  83.626   7.727  1.00 16.87           C  
ANISOU  499  CA  LEU A  67     2470   1635   2304   -113     22   -182       C  
ATOM    500  C   LEU A  67      23.674  83.539   6.334  1.00 17.15           C  
ANISOU  500  C   LEU A  67     2492   1704   2319    -68     38   -131       C  
ATOM    501  O   LEU A  67      22.464  83.292   6.192  1.00 18.05           O  
ANISOU  501  O   LEU A  67     2576   1889   2391     -3     35   -115       O  
ATOM    502  CB  LEU A  67      24.161  82.282   8.430  1.00 17.06           C  
ANISOU  502  CB  LEU A  67     2428   1731   2323   -116     -5   -203       C  
ATOM    503  CG  LEU A  67      24.628  81.041   7.658  1.00 16.80           C  
ANISOU  503  CG  LEU A  67     2346   1745   2292   -141     -1   -188       C  
ATOM    504  CD1 LEU A  67      26.135  81.183   7.412  1.00 18.50           C  
ANISOU  504  CD1 LEU A  67     2548   1954   2524   -191     -2   -190       C  
ATOM    505  CD2 LEU A  67      24.279  79.765   8.426  1.00 18.09           C  
ANISOU  505  CD2 LEU A  67     2489   1944   2438   -128      5   -202       C  
ATOM    506  N   ASP A  68      24.518  83.633   5.296  1.00 16.95           N  
ANISOU  506  N   ASP A  68     2466   1662   2310   -109     51   -111       N  
ATOM    507  CA  ASP A  68      24.129  83.357   3.933  1.00 16.85           C  
ANISOU  507  CA  ASP A  68     2420   1709   2273    -79     61    -68       C  
ATOM    508  C   ASP A  68      24.871  82.114   3.448  1.00 15.75           C  
ANISOU  508  C   ASP A  68     2216   1618   2149   -145     47    -84       C  
ATOM    509  O   ASP A  68      26.061  82.186   3.112  1.00 16.11           O  
ANISOU  509  O   ASP A  68     2264   1633   2221   -198     50    -83       O  
ATOM    510  CB  ASP A  68      24.468  84.544   3.027  1.00 17.82           C  
ANISOU  510  CB  ASP A  68     2613   1762   2394    -57    106    -20       C  
ATOM    511  CG  ASP A  68      24.016  84.358   1.603  1.00 20.94           C  
ANISOU  511  CG  ASP A  68     2964   2243   2748     -6    117     31       C  
ATOM    512  OD1 ASP A  68      23.446  83.305   1.275  1.00 19.71           O  
ANISOU  512  OD1 ASP A  68     2719   2208   2562    -11     92     16       O  
ATOM    513  OD2 ASP A  68      24.239  85.327   0.781  1.00 25.87           O  
ANISOU  513  OD2 ASP A  68     3654   2813   3362     32    165     86       O  
ATOM    514  N   LEU A  69      24.201  80.969   3.452  1.00 15.01           N  
ANISOU  514  N   LEU A  69     2073   1598   2030   -148     43   -104       N  
ATOM    515  CA  LEU A  69      24.789  79.710   3.014  1.00 14.54           C  
ANISOU  515  CA  LEU A  69     1984   1562   1975   -199     57   -119       C  
ATOM    516  C   LEU A  69      25.226  79.704   1.564  1.00 16.03           C  
ANISOU  516  C   LEU A  69     2153   1777   2160   -218     70    -95       C  
ATOM    517  O   LEU A  69      25.989  78.841   1.189  1.00 17.58           O  
ANISOU  517  O   LEU A  69     2341   1972   2365   -253     87   -102       O  
ATOM    518  CB  LEU A  69      23.836  78.536   3.259  1.00 15.04           C  
ANISOU  518  CB  LEU A  69     2032   1680   2002   -219     82   -156       C  
ATOM    519  CG  LEU A  69      23.661  78.130   4.738  1.00 14.39           C  
ANISOU  519  CG  LEU A  69     1975   1564   1926   -208     82   -180       C  
ATOM    520  CD1 LEU A  69      22.387  77.263   4.844  1.00 14.92           C  
ANISOU  520  CD1 LEU A  69     2031   1697   1941   -244    118   -221       C  
ATOM    521  CD2 LEU A  69      24.911  77.308   5.192  1.00 15.20           C  
ANISOU  521  CD2 LEU A  69     2103   1618   2053   -208    103   -175       C  
ATOM    522  N   GLN A  70      24.766  80.666   0.763  1.00 15.55           N  
ANISOU  522  N   GLN A  70     2090   1740   2076   -180     71    -58       N  
ATOM    523  CA  GLN A  70      25.192  80.854  -0.633  1.00 16.22           C  
ANISOU  523  CA  GLN A  70     2157   1854   2152   -186     84    -24       C  
ATOM    524  C   GLN A  70      26.402  81.749  -0.796  1.00 16.66           C  
ANISOU  524  C   GLN A  70     2258   1819   2250   -203     88      4       C  
ATOM    525  O   GLN A  70      26.695  82.196  -1.915  1.00 17.58           O  
ANISOU  525  O   GLN A  70     2376   1945   2357   -197    106     44       O  
ATOM    526  CB  GLN A  70      24.036  81.393  -1.497  1.00 16.87           C  
ANISOU  526  CB  GLN A  70     2207   2040   2162   -115     96     11       C  
ATOM    527  CG  GLN A  70      22.815  80.475  -1.448  1.00 19.00           C  
ANISOU  527  CG  GLN A  70     2405   2451   2363   -130     97    -35       C  
ATOM    528  CD  GLN A  70      21.724  80.808  -2.463  1.00 26.71           C  
ANISOU  528  CD  GLN A  70     3303   3611   3234    -66    108     -7       C  
ATOM    529  OE1 GLN A  70      21.971  81.454  -3.494  1.00 33.53           O  
ANISOU  529  OE1 GLN A  70     4162   4501   4075    -11    119     51       O  
ATOM    530  NE2 GLN A  70      20.535  80.260  -2.230  1.00 26.14           N  
ANISOU  530  NE2 GLN A  70     3158   3693   3081    -82    110    -55       N  
ATOM    531  N   ASP A  71      27.112  82.000   0.292  1.00 16.59           N  
ANISOU  531  N   ASP A  71     2282   1742   2278   -236     78    -20       N  
ATOM    532  CA  ASP A  71      28.312  82.881   0.269  1.00 16.61           C  
ANISOU  532  CA  ASP A  71     2323   1681   2306   -293     92    -17       C  
ATOM    533  C   ASP A  71      29.291  82.334   1.310  1.00 16.75           C  
ANISOU  533  C   ASP A  71     2305   1721   2335   -346     69    -64       C  
ATOM    534  O   ASP A  71      29.093  82.505   2.502  1.00 17.34           O  
ANISOU  534  O   ASP A  71     2395   1781   2411   -345     58    -96       O  
ATOM    535  CB  ASP A  71      27.872  84.324   0.544  1.00 17.77           C  
ANISOU  535  CB  ASP A  71     2568   1733   2450   -268    130      0       C  
ATOM    536  CG  ASP A  71      29.008  85.325   0.579  1.00 20.56           C  
ANISOU  536  CG  ASP A  71     2986   2005   2819   -362    171    -16       C  
ATOM    537  OD1 ASP A  71      30.185  84.928   0.628  1.00 22.01           O  
ANISOU  537  OD1 ASP A  71     3113   2239   3010   -452    153    -50       O  
ATOM    538  OD2 ASP A  71      28.707  86.557   0.534  1.00 26.10           O  
ANISOU  538  OD2 ASP A  71     3806   2596   3513   -345    236      5       O  
ATOM    539  N   LEU A  72      30.317  81.624   0.852  1.00 15.91           N  
ANISOU  539  N   LEU A  72     2144   1675   2225   -375     64    -63       N  
ATOM    540  CA  LEU A  72      31.248  81.027   1.799  1.00 15.57           C  
ANISOU  540  CA  LEU A  72     2051   1698   2165   -388     48    -91       C  
ATOM    541  C   LEU A  72      31.923  82.031   2.721  1.00 17.04           C  
ANISOU  541  C   LEU A  72     2239   1893   2340   -462     45   -135       C  
ATOM    542  O   LEU A  72      32.296  81.694   3.855  1.00 17.11           O  
ANISOU  542  O   LEU A  72     2206   1973   2322   -455     27   -165       O  
ATOM    543  CB  LEU A  72      32.267  80.132   1.079  1.00 16.74           C  
ANISOU  543  CB  LEU A  72     2141   1925   2292   -380     55    -72       C  
ATOM    544  CG  LEU A  72      31.729  78.874   0.433  1.00 16.90           C  
ANISOU  544  CG  LEU A  72     2169   1939   2310   -319     78    -50       C  
ATOM    545  CD1 LEU A  72      32.829  78.209  -0.428  1.00 19.66           C  
ANISOU  545  CD1 LEU A  72     2479   2352   2636   -309     97    -27       C  
ATOM    546  CD2 LEU A  72      31.244  77.885   1.507  1.00 21.28           C  
ANISOU  546  CD2 LEU A  72     2744   2489   2850   -258     92    -61       C  
ATOM    547  N   SER A  73      32.100  83.282   2.282  1.00 17.44           N  
ANISOU  547  N   SER A  73     2347   1877   2401   -539     75   -143       N  
ATOM    548  CA  SER A  73      32.653  84.294   3.177  1.00 18.39           C  
ANISOU  548  CA  SER A  73     2494   1991   2503   -644     95   -207       C  
ATOM    549  C   SER A  73      31.740  84.619   4.348  1.00 18.22           C  
ANISOU  549  C   SER A  73     2525   1909   2489   -612     91   -235       C  
ATOM    550  O   SER A  73      32.212  84.842   5.455  1.00 20.36           O  
ANISOU  550  O   SER A  73     2768   2237   2729   -674     85   -298       O  
ATOM    551  CB  SER A  73      33.041  85.570   2.426  1.00 19.79           C  
ANISOU  551  CB  SER A  73     2758   2076   2685   -748    160   -214       C  
ATOM    552  OG  SER A  73      31.922  86.367   2.011  1.00 22.52           O  
ANISOU  552  OG  SER A  73     3236   2262   3058   -686    208   -170       O  
ATOM    553  N   SER A  74      30.439  84.581   4.101  1.00 18.41           N  
ANISOU  553  N   SER A  74     2607   1847   2538   -511     93   -190       N  
ATOM    554  CA  SER A  74      29.452  84.730   5.144  1.00 17.07           C  
ANISOU  554  CA  SER A  74     2476   1639   2371   -457     85   -207       C  
ATOM    555  C   SER A  74      29.426  83.515   6.090  1.00 16.41           C  
ANISOU  555  C   SER A  74     2304   1656   2273   -412     35   -222       C  
ATOM    556  O   SER A  74      29.334  83.695   7.306  1.00 17.34           O  
ANISOU  556  O   SER A  74     2422   1789   2377   -421     24   -265       O  
ATOM    557  CB  SER A  74      28.059  84.850   4.499  1.00 17.50           C  
ANISOU  557  CB  SER A  74     2583   1633   2432   -347     98   -148       C  
ATOM    558  OG  SER A  74      27.079  85.005   5.521  1.00 19.18           O  
ANISOU  558  OG  SER A  74     2825   1824   2637   -289     91   -164       O  
ATOM    559  N   VAL A  75      29.515  82.311   5.545  1.00 15.82           N  
ANISOU  559  N   VAL A  75     2170   1642   2196   -364     18   -187       N  
ATOM    560  CA  VAL A  75      29.635  81.112   6.367  1.00 15.55           C  
ANISOU  560  CA  VAL A  75     2081   1684   2140   -311      0   -189       C  
ATOM    561  C   VAL A  75      30.800  81.258   7.349  1.00 16.06           C  
ANISOU  561  C   VAL A  75     2084   1854   2162   -350    -12   -228       C  
ATOM    562  O   VAL A  75      30.666  80.955   8.531  1.00 16.48           O  
ANISOU  562  O   VAL A  75     2116   1955   2189   -313    -25   -246       O  
ATOM    563  CB  VAL A  75      29.770  79.839   5.507  1.00 14.94           C  
ANISOU  563  CB  VAL A  75     1982   1636   2058   -264     17   -149       C  
ATOM    564  CG1 VAL A  75      30.024  78.543   6.389  1.00 16.39           C  
ANISOU  564  CG1 VAL A  75     2142   1877   2206   -189     31   -138       C  
ATOM    565  CG2 VAL A  75      28.514  79.650   4.617  1.00 15.87           C  
ANISOU  565  CG2 VAL A  75     2139   1695   2195   -247     32   -131       C  
ATOM    566  N  AARG A  76      31.953  81.687   6.839  0.70 16.96           N  
ANISOU  566  N  AARG A  76     2157   2031   2255   -426     -7   -242       N  
ATOM    567  N  BARG A  76      31.945  81.700   6.845  0.30 16.83           N  
ANISOU  567  N  BARG A  76     2141   2014   2239   -427     -7   -243       N  
ATOM    568  CA AARG A  76      33.169  81.843   7.652  0.70 18.27           C  
ANISOU  568  CA AARG A  76     2231   2360   2351   -482    -17   -290       C  
ATOM    569  CA BARG A  76      33.133  81.807   7.674  0.30 17.80           C  
ANISOU  569  CA BARG A  76     2172   2299   2292   -477    -18   -288       C  
ATOM    570  C  AARG A  76      33.002  82.885   8.746  0.70 18.70           C  
ANISOU  570  C  AARG A  76     2309   2403   2389   -569    -16   -367       C  
ATOM    571  C  BARG A  76      33.008  82.882   8.751  0.30 18.72           C  
ANISOU  571  C  BARG A  76     2311   2408   2392   -569    -16   -367       C  
ATOM    572  O  AARG A  76      33.386  82.653   9.899  0.70 19.13           O  
ANISOU  572  O  AARG A  76     2289   2597   2383   -558    -35   -401       O  
ATOM    573  O  BARG A  76      33.434  82.669   9.889  0.30 19.17           O  
ANISOU  573  O  BARG A  76     2290   2606   2385   -563    -35   -403       O  
ATOM    574  CB AARG A  76      34.367  82.181   6.762  0.70 19.46           C  
ANISOU  574  CB AARG A  76     2328   2591   2472   -572     -5   -300       C  
ATOM    575  CB BARG A  76      34.367  82.053   6.821  0.30 18.57           C  
ANISOU  575  CB BARG A  76     2209   2489   2356   -558     -7   -296       C  
ATOM    576  CG AARG A  76      34.828  81.024   5.924  0.70 23.16           C  
ANISOU  576  CG AARG A  76     2747   3123   2927   -475     -5   -232       C  
ATOM    577  CG BARG A  76      35.537  82.416   7.675  0.30 20.15           C  
ANISOU  577  CG BARG A  76     2299   2893   2462   -647    -15   -365       C  
ATOM    578  CD AARG A  76      36.176  81.304   5.224  0.70 28.70           C  
ANISOU  578  CD AARG A  76     3365   3960   3577   -558      1   -245       C  
ATOM    579  CD BARG A  76      36.733  81.599   7.362  0.30 24.59           C  
ANISOU  579  CD BARG A  76     2731   3666   2943   -595    -23   -333       C  
ATOM    580  NE AARG A  76      36.794  80.032   4.904  0.70 32.72           N  
ANISOU  580  NE AARG A  76     3804   4589   4038   -428      2   -183       N  
ATOM    581  NE BARG A  76      37.489  81.361   8.584  0.30 27.57           N  
ANISOU  581  NE BARG A  76     2976   4293   3205   -574    -42   -368       N  
ATOM    582  CZ AARG A  76      37.576  79.339   5.723  0.70 31.04           C  
ANISOU  582  CZ AARG A  76     3487   4580   3727   -337     -2   -171       C  
ATOM    583  CZ BARG A  76      38.402  80.413   8.713  0.30 29.97           C  
ANISOU  583  CZ BARG A  76     3154   4825   3406   -451    -47   -320       C  
ATOM    584  NH1AARG A  76      37.941  79.799   6.923  0.70 35.53           N  
ANISOU  584  NH1AARG A  76     3978   5297   4224   -383    -21   -228       N  
ATOM    585  NH1BARG A  76      38.661  79.611   7.691  0.30 28.56           N  
ANISOU  585  NH1BARG A  76     2984   4626   3240   -350    -31   -241       N  
ATOM    586  NH2AARG A  76      38.044  78.185   5.309  0.70 33.33           N  
ANISOU  586  NH2AARG A  76     3749   4939   3973   -191     21    -99       N  
ATOM    587  NH2BARG A  76      39.052  80.274   9.860  0.30 31.53           N  
ANISOU  587  NH2BARG A  76     3218   5284   3477   -419    -62   -350       N  
ATOM    588  N   ARG A  77      32.427  84.027   8.403  1.00 18.41           N  
ANISOU  588  N   ARG A  77     2236   2140   2618   -458   -137   -156       N  
ATOM    589  CA  ARG A  77      32.210  85.107   9.380  1.00 19.72           C  
ANISOU  589  CA  ARG A  77     2455   2246   2789   -480   -160   -198       C  
ATOM    590  C   ARG A  77      31.247  84.623  10.490  1.00 18.88           C  
ANISOU  590  C   ARG A  77     2371   2147   2654   -409   -178   -227       C  
ATOM    591  O   ARG A  77      31.486  84.855  11.684  1.00 20.07           O  
ANISOU  591  O   ARG A  77     2527   2302   2793   -418   -209   -273       O  
ATOM    592  CB  ARG A  77      31.665  86.332   8.650  1.00 21.47           C  
ANISOU  592  CB  ARG A  77     2748   2376   3032   -500   -141   -179       C  
ATOM    593  CG  ARG A  77      32.715  87.135   7.904  1.00 25.13           C  
ANISOU  593  CG  ARG A  77     3204   2818   3525   -589   -129   -161       C  
ATOM    594  CD  ARG A  77      32.173  88.515   7.476  1.00 29.09           C  
ANISOU  594  CD  ARG A  77     3795   3211   4046   -610   -117   -150       C  
ATOM    595  NE  ARG A  77      30.915  88.450   6.726  1.00 27.92           N  
ANISOU  595  NE  ARG A  77     3690   3029   3888   -538    -92   -113       N  
ATOM    596  CZ  ARG A  77      30.792  88.256   5.413  1.00 30.19           C  
ANISOU  596  CZ  ARG A  77     3969   3322   4177   -530    -60    -59       C  
ATOM    597  NH1 ARG A  77      31.865  88.111   4.636  1.00 31.03           N  
ANISOU  597  NH1 ARG A  77     4027   3467   4295   -590    -43    -31       N  
ATOM    598  NH2 ARG A  77      29.583  88.225   4.862  1.00 31.20           N  
ANISOU  598  NH2 ARG A  77     4138   3423   4292   -460    -45    -32       N  
ATOM    599  N   PHE A  78      30.188  83.928  10.095  1.00 17.52           N  
ANISOU  599  N   PHE A  78     2207   1981   2467   -342   -160   -200       N  
ATOM    600  CA  PHE A  78      29.227  83.412  11.069  1.00 17.17           C  
ANISOU  600  CA  PHE A  78     2179   1950   2394   -278   -170   -220       C  
ATOM    601  C   PHE A  78      29.893  82.395  11.995  1.00 17.75           C  
ANISOU  601  C   PHE A  78     2201   2097   2446   -270   -193   -241       C  
ATOM    602  O   PHE A  78      29.789  82.468  13.223  1.00 18.57           O  
ANISOU  602  O   PHE A  78     2316   2208   2528   -255   -217   -279       O  
ATOM    603  CB  PHE A  78      28.001  82.796  10.393  1.00 16.45           C  
ANISOU  603  CB  PHE A  78     2097   1858   2292   -217   -146   -184       C  
ATOM    604  CG  PHE A  78      27.162  82.015  11.361  1.00 16.62           C  
ANISOU  604  CG  PHE A  78     2118   1912   2283   -159   -154   -198       C  
ATOM    605  CD1 PHE A  78      26.302  82.685  12.233  1.00 17.15           C  
ANISOU  605  CD1 PHE A  78     2231   1946   2337   -128   -160   -225       C  
ATOM    606  CD2 PHE A  78      27.281  80.647  11.485  1.00 16.49           C  
ANISOU  606  CD2 PHE A  78     2058   1958   2250   -135   -154   -185       C  
ATOM    607  CE1 PHE A  78      25.593  81.983  13.209  1.00 17.57           C  
ANISOU  607  CE1 PHE A  78     2280   2036   2358    -79   -165   -237       C  
ATOM    608  CE2 PHE A  78      26.575  79.957  12.473  1.00 17.42           C  
ANISOU  608  CE2 PHE A  78     2176   2103   2337    -90   -161   -196       C  
ATOM    609  CZ  PHE A  78      25.730  80.638  13.328  1.00 16.59           C  
ANISOU  609  CZ  PHE A  78     2112   1972   2219    -63   -165   -221       C  
ATOM    610  N   ALA A  79      30.608  81.434  11.423  1.00 16.59           N  
ANISOU  610  N   ALA A  79     1996   2006   2299   -275   -186   -217       N  
ATOM    611  CA  ALA A  79      31.250  80.419  12.235  1.00 18.13           C  
ANISOU  611  CA  ALA A  79     2144   2270   2471   -258   -207   -231       C  
ATOM    612  C   ALA A  79      32.240  80.988  13.217  1.00 19.27           C  
ANISOU  612  C   ALA A  79     2273   2433   2615   -302   -241   -274       C  
ATOM    613  O   ALA A  79      32.336  80.513  14.360  1.00 19.65           O  
ANISOU  613  O   ALA A  79     2311   2519   2634   -276   -267   -301       O  
ATOM    614  CB  ALA A  79      31.940  79.365  11.330  1.00 18.49           C  
ANISOU  614  CB  ALA A  79     2135   2369   2520   -253   -193   -198       C  
ATOM    615  N   ASP A  80      33.014  81.977  12.779  1.00 19.99           N  
ANISOU  615  N   ASP A  80     2360   2500   2734   -372   -243   -281       N  
ATOM    616  CA  ASP A  80      34.034  82.560  13.645  1.00 22.08           C  
ANISOU  616  CA  ASP A  80     2604   2784   2999   -426   -278   -325       C  
ATOM    617  C   ASP A  80      33.419  83.250  14.845  1.00 22.29           C  
ANISOU  617  C   ASP A  80     2689   2769   3009   -415   -303   -371       C  
ATOM    618  O   ASP A  80      34.074  83.389  15.876  1.00 23.43           O  
ANISOU  618  O   ASP A  80     2818   2946   3138   -436   -340   -414       O  
ATOM    619  CB  ASP A  80      34.891  83.528  12.845  1.00 24.06           C  
ANISOU  619  CB  ASP A  80     2844   3010   3286   -512   -271   -318       C  
ATOM    620  CG  ASP A  80      35.885  82.814  11.919  1.00 29.14           C  
ANISOU  620  CG  ASP A  80     3410   3721   3939   -531   -254   -283       C  
ATOM    621  OD1 ASP A  80      36.121  81.583  12.052  1.00 35.57           O  
ANISOU  621  OD1 ASP A  80     4175   4608   4731   -480   -257   -273       O  
ATOM    622  OD2 ASP A  80      36.442  83.519  11.046  1.00 37.38           O  
ANISOU  622  OD2 ASP A  80     4445   4746   5012   -596   -236   -265       O  
ATOM    623  N   GLY A  81      32.166  83.678  14.725  1.00 20.40           N  
ANISOU  623  N   GLY A  81     2516   2465   2769   -377   -285   -365       N  
ATOM    624  CA  GLY A  81      31.432  84.268  15.831  1.00 20.40           C  
ANISOU  624  CA  GLY A  81     2575   2429   2747   -350   -302   -407       C  
ATOM    625  C   GLY A  81      30.810  83.328  16.833  1.00 19.80           C  
ANISOU  625  C   GLY A  81     2494   2401   2628   -279   -310   -416       C  
ATOM    626  O   GLY A  81      30.267  83.802  17.847  1.00 21.30           O  
ANISOU  626  O   GLY A  81     2728   2570   2793   -254   -325   -455       O  
ATOM    627  N   VAL A  82      30.842  82.021  16.550  1.00 18.85           N  
ANISOU  627  N   VAL A  82     2325   2340   2497   -244   -299   -381       N  
ATOM    628  CA  VAL A  82      30.289  81.027  17.481  1.00 18.34           C  
ANISOU  628  CA  VAL A  82     2255   2321   2390   -180   -304   -382       C  
ATOM    629  C   VAL A  82      31.406  80.517  18.374  1.00 19.76           C  
ANISOU  629  C   VAL A  82     2390   2569   2546   -191   -340   -406       C  
ATOM    630  O   VAL A  82      32.305  79.792  17.911  1.00 20.00           O  
ANISOU  630  O   VAL A  82     2364   2649   2584   -203   -342   -386       O  
ATOM    631  CB  VAL A  82      29.644  79.850  16.728  1.00 17.37           C  
ANISOU  631  CB  VAL A  82     2115   2218   2266   -136   -273   -330       C  
ATOM    632  CG1 VAL A  82      29.079  78.833  17.713  1.00 19.35           C  
ANISOU  632  CG1 VAL A  82     2365   2511   2474    -78   -277   -327       C  
ATOM    633  CG2 VAL A  82      28.524  80.365  15.845  1.00 18.81           C  
ANISOU  633  CG2 VAL A  82     2336   2341   2467   -124   -242   -306       C  
ATOM    634  N   SER A  83      31.371  80.890  19.649  1.00 21.56           N  
ANISOU  634  N   SER A  83     2643   2807   2743   -182   -368   -451       N  
ATOM    635  CA  SER A  83      32.441  80.459  20.553  1.00 22.51           C  
ANISOU  635  CA  SER A  83     2719   2996   2835   -190   -408   -477       C  
ATOM    636  C   SER A  83      32.386  78.991  20.936  1.00 21.91           C  
ANISOU  636  C   SER A  83     2613   2986   2725   -129   -405   -447       C  
ATOM    637  O   SER A  83      33.405  78.384  21.273  1.00 22.91           O  
ANISOU  637  O   SER A  83     2689   3177   2836   -130   -431   -451       O  
ATOM    638  CB  SER A  83      32.456  81.309  21.824  1.00 24.87           C  
ANISOU  638  CB  SER A  83     3055   3287   3105   -198   -442   -538       C  
ATOM    639  OG  SER A  83      31.204  81.262  22.444  1.00 28.29           O  
ANISOU  639  OG  SER A  83     3541   3700   3507   -138   -427   -541       O  
ATOM    640  N   GLY A  84      31.194  78.401  20.869  1.00 20.46           N  
ANISOU  640  N   GLY A  84     2459   2785   2528    -76   -375   -416       N  
ATOM    641  CA  GLY A  84      31.003  76.996  21.192  1.00 20.56           C  
ANISOU  641  CA  GLY A  84     2455   2846   2510    -21   -368   -383       C  
ATOM    642  C   GLY A  84      29.540  76.656  21.041  1.00 20.09           C  
ANISOU  642  C   GLY A  84     2434   2755   2444     19   -332   -353       C  
ATOM    643  O   GLY A  84      28.677  77.533  21.118  1.00 19.75           O  
ANISOU  643  O   GLY A  84     2431   2668   2404     19   -320   -369       O  
ATOM    644  N   ALA A  85      29.249  75.387  20.776  1.00 17.93           N  
ANISOU  644  N   ALA A  85     2148   2503   2161     53   -314   -310       N  
ATOM    645  CA  ALA A  85      27.868  74.910  20.750  1.00 17.82           C  
ANISOU  645  CA  ALA A  85     2164   2470   2135     88   -282   -280       C  
ATOM    646  C   ALA A  85      27.831  73.443  21.107  1.00 17.36           C  
ANISOU  646  C   ALA A  85     2097   2450   2048    126   -278   -245       C  
ATOM    647  O   ALA A  85      28.844  72.731  21.021  1.00 17.96           O  
ANISOU  647  O   ALA A  85     2145   2558   2122    129   -294   -236       O  
ATOM    648  CB  ALA A  85      27.198  75.160  19.403  1.00 18.43           C  
ANISOU  648  CB  ALA A  85     2246   2501   2253     72   -251   -255       C  
ATOM    649  N   ASP A  86      26.675  72.978  21.559  1.00 15.85           N  
ANISOU  649  N   ASP A  86     1932   2258   1831    156   -256   -224       N  
ATOM    650  CA  ASP A  86      26.492  71.565  21.826  1.00 16.03           C  
ANISOU  650  CA  ASP A  86     1956   2303   1828    186   -247   -184       C  
ATOM    651  C   ASP A  86      25.970  70.766  20.636  1.00 14.78           C  
ANISOU  651  C   ASP A  86     1796   2118   1699    180   -220   -142       C  
ATOM    652  O   ASP A  86      26.478  69.690  20.326  1.00 15.75           O  
ANISOU  652  O   ASP A  86     1912   2250   1822    191   -222   -116       O  
ATOM    653  CB  ASP A  86      25.614  71.428  23.057  1.00 16.90           C  
ANISOU  653  CB  ASP A  86     2094   2434   1890    217   -239   -182       C  
ATOM    654  CG  ASP A  86      26.247  72.182  24.218  1.00 20.31           C  
ANISOU  654  CG  ASP A  86     2530   2896   2289    225   -271   -228       C  
ATOM    655  OD1 ASP A  86      27.470  71.943  24.536  1.00 23.83           O  
ANISOU  655  OD1 ASP A  86     2955   3374   2725    226   -304   -241       O  
ATOM    656  OD2 ASP A  86      25.658  73.101  24.777  1.00 19.55           O  
ANISOU  656  OD2 ASP A  86     2454   2793   2178    229   -268   -258       O  
ATOM    657  N   VAL A  87      24.984  71.316  19.942  1.00 14.44           N  
ANISOU  657  N   VAL A  87     1761   2042   1680    166   -196   -138       N  
ATOM    658  CA  VAL A  87      24.324  70.685  18.801  1.00 13.68           C  
ANISOU  658  CA  VAL A  87     1665   1923   1609    157   -172   -103       C  
ATOM    659  C   VAL A  87      24.316  71.666  17.644  1.00 14.10           C  
ANISOU  659  C   VAL A  87     1709   1943   1703    130   -166   -114       C  
ATOM    660  O   VAL A  87      23.958  72.848  17.833  1.00 14.02           O  
ANISOU  660  O   VAL A  87     1708   1919   1698    124   -166   -139       O  
ATOM    661  CB  VAL A  87      22.898  70.280  19.161  1.00 13.72           C  
ANISOU  661  CB  VAL A  87     1687   1930   1594    169   -146    -79       C  
ATOM    662  CG1 VAL A  87      22.159  69.639  17.970  1.00 15.23           C  
ANISOU  662  CG1 VAL A  87     1876   2099   1811    154   -125    -46       C  
ATOM    663  CG2 VAL A  87      22.892  69.305  20.354  1.00 15.49           C  
ANISOU  663  CG2 VAL A  87     1925   2185   1774    194   -148    -62       C  
ATOM    664  N   LEU A  88      24.646  71.177  16.447  1.00 12.81           N  
ANISOU  664  N   LEU A  88     1533   1766   1565    116   -160    -95       N  
ATOM    665  CA  LEU A  88      24.487  71.926  15.191  1.00 12.43           C  
ANISOU  665  CA  LEU A  88     1480   1687   1553     93   -149    -95       C  
ATOM    666  C   LEU A  88      23.422  71.228  14.374  1.00 11.83           C  
ANISOU  666  C   LEU A  88     1412   1600   1483     95   -128    -63       C  
ATOM    667  O   LEU A  88      23.538  70.011  14.141  1.00 13.13           O  
ANISOU  667  O   LEU A  88     1576   1770   1641    101   -126    -42       O  
ATOM    668  CB  LEU A  88      25.796  71.935  14.378  1.00 11.69           C  
ANISOU  668  CB  LEU A  88     1363   1595   1481     74   -159    -98       C  
ATOM    669  CG  LEU A  88      25.701  72.458  12.958  1.00 12.51           C  
ANISOU  669  CG  LEU A  88     1463   1672   1617     51   -144    -89       C  
ATOM    670  CD1 LEU A  88      25.259  73.920  12.868  1.00 14.29           C  
ANISOU  670  CD1 LEU A  88     1703   1867   1858     35   -141   -105       C  
ATOM    671  CD2 LEU A  88      27.079  72.287  12.251  1.00 14.44           C  
ANISOU  671  CD2 LEU A  88     1679   1930   1876     36   -150    -89       C  
ATOM    672  N   ILE A  89      22.403  71.961  13.965  1.00 12.02           N  
ANISOU  672  N   ILE A  89     1442   1606   1517     92   -114    -62       N  
ATOM    673  CA  ILE A  89      21.313  71.475  13.118  1.00 11.36           C  
ANISOU  673  CA  ILE A  89     1359   1517   1439     91    -97    -36       C  
ATOM    674  C   ILE A  89      21.371  72.162  11.774  1.00 11.83           C  
ANISOU  674  C   ILE A  89     1415   1552   1526     76    -92    -33       C  
ATOM    675  O   ILE A  89      21.086  73.350  11.658  1.00 12.52           O  
ANISOU  675  O   ILE A  89     1509   1623   1624     78    -90    -45       O  
ATOM    676  CB  ILE A  89      19.929  71.625  13.776  1.00 10.92           C  
ANISOU  676  CB  ILE A  89     1308   1475   1365    106    -84    -30       C  
ATOM    677  CG1 ILE A  89      19.919  71.007  15.180  1.00 12.63           C  
ANISOU  677  CG1 ILE A  89     1531   1718   1549    121    -86    -30       C  
ATOM    678  CG2 ILE A  89      18.824  70.992  12.848  1.00 11.66           C  
ANISOU  678  CG2 ILE A  89     1394   1571   1464     97    -69     -2       C  
ATOM    679  CD1 ILE A  89      18.574  71.067  15.925  1.00 13.09           C  
ANISOU  679  CD1 ILE A  89     1589   1801   1583    136    -68    -22       C  
ATOM    680  N   ASN A  90      21.752  71.389  10.747  1.00 12.09           N  
ANISOU  680  N   ASN A  90     1442   1582   1569     66    -90    -17       N  
ATOM    681  CA  ASN A  90      21.860  71.838   9.356  1.00 11.69           C  
ANISOU  681  CA  ASN A  90     1387   1513   1538     54    -84    -10       C  
ATOM    682  C   ASN A  90      20.474  71.634   8.719  1.00 11.28           C  
ANISOU  682  C   ASN A  90     1339   1462   1484     57    -74      8       C  
ATOM    683  O   ASN A  90      20.183  70.615   8.080  1.00 12.16           O  
ANISOU  683  O   ASN A  90     1449   1578   1591     52    -72     23       O  
ATOM    684  CB  ASN A  90      22.954  71.069   8.608  1.00 11.04           C  
ANISOU  684  CB  ASN A  90     1297   1435   1462     46    -87     -4       C  
ATOM    685  CG  ASN A  90      24.333  71.317   9.148  1.00 11.54           C  
ANISOU  685  CG  ASN A  90     1347   1508   1528     42    -98    -21       C  
ATOM    686  OD1 ASN A  90      24.656  72.440   9.548  1.00 13.02           O  
ANISOU  686  OD1 ASN A  90     1532   1689   1724     31   -103    -38       O  
ATOM    687  ND2 ASN A  90      25.187  70.263   9.113  1.00 12.56           N  
ANISOU  687  ND2 ASN A  90     1468   1655   1649     52   -103    -18       N  
ATOM    688  N   ASN A  91      19.591  72.584   8.971  1.00 11.63           N  
ANISOU  688  N   ASN A  91     1385   1503   1528     68    -69      4       N  
ATOM    689  CA  ASN A  91      18.176  72.540   8.593  1.00 12.51           C  
ANISOU  689  CA  ASN A  91     1491   1628   1634     77    -61     19       C  
ATOM    690  C   ASN A  91      17.781  73.316   7.369  1.00 12.51           C  
ANISOU  690  C   ASN A  91     1492   1615   1645     81    -57     28       C  
ATOM    691  O   ASN A  91      16.829  72.926   6.666  1.00 13.80           O  
ANISOU  691  O   ASN A  91     1645   1795   1803     82    -55     44       O  
ATOM    692  CB  ASN A  91      17.335  73.021   9.828  1.00 12.05           C  
ANISOU  692  CB  ASN A  91     1432   1586   1559     99    -56     10       C  
ATOM    693  CG  ASN A  91      15.940  73.437   9.482  1.00 13.58           C  
ANISOU  693  CG  ASN A  91     1614   1797   1748    118    -47     21       C  
ATOM    694  OD1 ASN A  91      14.997  72.614   9.513  1.00 14.35           O  
ANISOU  694  OD1 ASN A  91     1692   1926   1833    112    -41     37       O  
ATOM    695  ND2 ASN A  91      15.758  74.707   9.153  1.00 13.61           N  
ANISOU  695  ND2 ASN A  91     1629   1781   1760    139    -45     14       N  
ATOM    696  N   ALA A  92      18.460  74.431   7.094  1.00 11.67           N  
ANISOU  696  N   ALA A  92     1400   1480   1553     82    -58     20       N  
ATOM    697  CA  ALA A  92      18.055  75.308   6.003  1.00 12.22           C  
ANISOU  697  CA  ALA A  92     1477   1533   1631     91    -53     32       C  
ATOM    698  C   ALA A  92      18.096  74.568   4.684  1.00 13.02           C  
ANISOU  698  C   ALA A  92     1571   1644   1732     78    -53     51       C  
ATOM    699  O   ALA A  92      19.022  73.832   4.403  1.00 13.76           O  
ANISOU  699  O   ALA A  92     1662   1739   1828     59    -54     50       O  
ATOM    700  CB  ALA A  92      19.002  76.520   5.897  1.00 13.70           C  
ANISOU  700  CB  ALA A  92     1687   1681   1835     82    -52     23       C  
ATOM    701  N   GLY A  93      17.139  74.831   3.815  1.00 13.48           N  
ANISOU  701  N   GLY A  93     1626   1710   1783     93    -51     67       N  
ATOM    702  CA  GLY A  93      17.185  74.266   2.477  1.00 13.60           C  
ANISOU  702  CA  GLY A  93     1638   1733   1793     82    -53     83       C  
ATOM    703  C   GLY A  93      16.333  75.065   1.521  1.00 14.44           C  
ANISOU  703  C   GLY A  93     1749   1843   1895    105    -53    100       C  
ATOM    704  O   GLY A  93      15.393  75.784   1.920  1.00 16.76           O  
ANISOU  704  O   GLY A  93     2040   2141   2184    133    -52    102       O  
ATOM    705  N   ILE A  94      16.691  74.949   0.255  1.00 13.33           N  
ANISOU  705  N   ILE A  94     1614   1700   1749     98    -52    114       N  
ATOM    706  CA  ILE A  94      15.832  75.364  -0.836  1.00 13.23           C  
ANISOU  706  CA  ILE A  94     1602   1700   1722    119    -56    133       C  
ATOM    707  C   ILE A  94      15.498  74.123  -1.669  1.00 13.32           C  
ANISOU  707  C   ILE A  94     1599   1746   1716    105    -66    135       C  
ATOM    708  O   ILE A  94      16.256  73.165  -1.712  1.00 13.47           O  
ANISOU  708  O   ILE A  94     1619   1762   1734     81    -66    125       O  
ATOM    709  CB  ILE A  94      16.472  76.491  -1.691  1.00 13.87           C  
ANISOU  709  CB  ILE A  94     1711   1749   1808    127    -45    151       C  
ATOM    710  CG1 ILE A  94      17.783  76.072  -2.299  1.00 14.46           C  
ANISOU  710  CG1 ILE A  94     1792   1815   1885     98    -36    152       C  
ATOM    711  CG2 ILE A  94      16.643  77.778  -0.826  1.00 17.02           C  
ANISOU  711  CG2 ILE A  94     2133   2109   2226    139    -37    146       C  
ATOM    712  CD1 ILE A  94      18.374  77.129  -3.300  1.00 16.96           C  
ANISOU  712  CD1 ILE A  94     2135   2106   2203     99    -22    177       C  
ATOM    713  N   MET A  95      14.390  74.168  -2.391  1.00 13.20           N  
ANISOU  713  N   MET A  95     1572   1760   1682    122    -77    146       N  
ATOM    714  CA  MET A  95      13.805  72.978  -2.980  1.00 13.25           C  
ANISOU  714  CA  MET A  95     1561   1802   1670    104    -93    142       C  
ATOM    715  C   MET A  95      13.176  73.222  -4.358  1.00 14.27           C  
ANISOU  715  C   MET A  95     1689   1957   1775    121   -105    157       C  
ATOM    716  O   MET A  95      12.176  73.945  -4.478  1.00 15.26           O  
ANISOU  716  O   MET A  95     1800   2106   1892    152   -112    170       O  
ATOM    717  CB  MET A  95      12.732  72.345  -2.032  1.00 13.74           C  
ANISOU  717  CB  MET A  95     1593   1895   1732     94   -102    133       C  
ATOM    718  CG  MET A  95      12.153  71.058  -2.553  1.00 12.14           C  
ANISOU  718  CG  MET A  95     1376   1722   1513     63   -119    126       C  
ATOM    719  SD  MET A  95      11.045  70.219  -1.360  1.00 16.65           S  
ANISOU  719  SD  MET A  95     1912   2327   2087     36   -124    120       S  
ATOM    720  CE  MET A  95       9.598  71.297  -1.398  1.00 18.19           C  
ANISOU  720  CE  MET A  95     2065   2575   2270     76   -128    135       C  
ATOM    721  N   ALA A  96      13.730  72.545  -5.362  1.00 12.89           N  
ANISOU  721  N   ALA A  96     1528   1783   1585    106   -109    154       N  
ATOM    722  CA  ALA A  96      13.142  72.485  -6.719  1.00 13.73           C  
ANISOU  722  CA  ALA A  96     1633   1922   1660    117   -125    164       C  
ATOM    723  C   ALA A  96      12.912  73.855  -7.331  1.00 16.00           C  
ANISOU  723  C   ALA A  96     1931   2208   1938    158   -120    192       C  
ATOM    724  O   ALA A  96      11.881  74.168  -7.897  1.00 19.92           O  
ANISOU  724  O   ALA A  96     2413   2741   2414    183   -136    204       O  
ATOM    725  CB  ALA A  96      11.875  71.647  -6.697  1.00 15.13           C  
ANISOU  725  CB  ALA A  96     1779   2144   1823    102   -150    153       C  
ATOM    726  N   VAL A  97      13.933  74.682  -7.219  1.00 14.17           N  
ANISOU  726  N   VAL A  97     1726   1933   1723    164    -96    204       N  
ATOM    727  CA  VAL A  97      13.992  76.053  -7.745  1.00 14.63           C  
ANISOU  727  CA  VAL A  97     1808   1971   1777    198    -85    234       C  
ATOM    728  C   VAL A  97      14.634  76.052  -9.155  1.00 14.17           C  
ANISOU  728  C   VAL A  97     1773   1917   1693    198    -79    252       C  
ATOM    729  O   VAL A  97      15.243  75.056  -9.561  1.00 13.79           O  
ANISOU  729  O   VAL A  97     1724   1880   1634    173    -78    236       O  
ATOM    730  CB  VAL A  97      14.797  76.964  -6.806  1.00 14.51           C  
ANISOU  730  CB  VAL A  97     1813   1903   1795    194    -64    236       C  
ATOM    731  CG1 VAL A  97      14.057  77.119  -5.444  1.00 17.77           C  
ANISOU  731  CG1 VAL A  97     2208   2316   2227    204    -69    219       C  
ATOM    732  CG2 VAL A  97      16.216  76.471  -6.601  1.00 15.96           C  
ANISOU  732  CG2 VAL A  97     2004   2064   1995    155    -47    223       C  
ATOM    733  N   PRO A  98      14.479  77.144  -9.920  1.00 15.16           N  
ANISOU  733  N   PRO A  98     1922   2034   1802    231    -73    285       N  
ATOM    734  CA  PRO A  98      15.189  77.274 -11.193  1.00 15.41           C  
ANISOU  734  CA  PRO A  98     1979   2066   1807    231    -60    308       C  
ATOM    735  C   PRO A  98      16.691  77.248 -11.060  1.00 15.24           C  
ANISOU  735  C   PRO A  98     1972   2013   1805    197    -31    307       C  
ATOM    736  O   PRO A  98      17.248  77.437  -9.968  1.00 15.08           O  
ANISOU  736  O   PRO A  98     1948   1959   1822    175    -20    294       O  
ATOM    737  CB  PRO A  98      14.690  78.610 -11.753  1.00 17.34           C  
ANISOU  737  CB  PRO A  98     2251   2298   2037    275    -57    348       C  
ATOM    738  CG  PRO A  98      13.366  78.830 -11.048  1.00 18.23           C  
ANISOU  738  CG  PRO A  98     2341   2428   2156    307    -80    340       C  
ATOM    739  CD  PRO A  98      13.588  78.281  -9.677  1.00 16.59           C  
ANISOU  739  CD  PRO A  98     2110   2206   1985    274    -77    305       C  
ATOM    740  N   TYR A  99      17.354  77.000 -12.175  1.00 15.50           N  
ANISOU  740  N   TYR A  99     2017   2061   1809    193    -18    319       N  
ATOM    741  CA  TYR A  99      18.815  77.025 -12.227  1.00 14.93           C  
ANISOU  741  CA  TYR A  99     1952   1970   1750    163     12    324       C  
ATOM    742  C   TYR A  99      19.339  78.407 -11.858  1.00 14.09           C  
ANISOU  742  C   TYR A  99     1868   1813   1671    154     35    353       C  
ATOM    743  O   TYR A  99      18.905  79.404 -12.411  1.00 15.07           O  
ANISOU  743  O   TYR A  99     2020   1921   1781    178     39    388       O  
ATOM    744  CB  TYR A  99      19.292  76.662 -13.649  1.00 15.51           C  
ANISOU  744  CB  TYR A  99     2037   2077   1778    170     24    339       C  
ATOM    745  CG  TYR A  99      20.772  76.780 -13.872  1.00 14.84           C  
ANISOU  745  CG  TYR A  99     1954   1985   1699    144     60    350       C  
ATOM    746  CD1 TYR A  99      21.315  77.921 -14.456  1.00 15.42           C  
ANISOU  746  CD1 TYR A  99     2051   2039   1767    140     90    395       C  
ATOM    747  CD2 TYR A  99      21.622  75.743 -13.519  1.00 16.41           C  
ANISOU  747  CD2 TYR A  99     2130   2198   1905    125     66    318       C  
ATOM    748  CE1 TYR A  99      22.688  78.059 -14.641  1.00 16.43           C  
ANISOU  748  CE1 TYR A  99     2172   2166   1901    109    126    408       C  
ATOM    749  CE2 TYR A  99      23.010  75.845 -13.730  1.00 16.03           C  
ANISOU  749  CE2 TYR A  99     2075   2155   1861    104    101    329       C  
ATOM    750  CZ  TYR A  99      23.526  77.002 -14.304  1.00 16.28           C  
ANISOU  750  CZ  TYR A  99     2122   2173   1889     93    131    374       C  
ATOM    751  OH  TYR A  99      24.897  77.158 -14.522  1.00 18.18           O  
ANISOU  751  OH  TYR A  99     2348   2424   2132     66    168    389       O  
ATOM    752  N   ALA A 100      20.291  78.431 -10.935  1.00 15.22           N  
ANISOU  752  N   ALA A 100     2001   1931   1850    119     50    338       N  
ATOM    753  CA  ALA A 100      20.949  79.638 -10.462  1.00 15.49           C  
ANISOU  753  CA  ALA A 100     2055   1914   1915     96     70    357       C  
ATOM    754  C   ALA A 100      22.241  79.279  -9.790  1.00 16.01           C  
ANISOU  754  C   ALA A 100     2097   1978   2007     53     85    336       C  
ATOM    755  O   ALA A 100      22.404  78.159  -9.315  1.00 16.54           O  
ANISOU  755  O   ALA A 100     2134   2073   2076     49     74    303       O  
ATOM    756  CB  ALA A 100      20.026  80.415  -9.489  1.00 16.77           C  
ANISOU  756  CB  ALA A 100     2232   2039   2101    115     54    350       C  
ATOM    757  N   LEU A 101      23.167  80.235  -9.767  1.00 17.18           N  
ANISOU  757  N   LEU A 101     2258   2093   2174     19    109    358       N  
ATOM    758  CA  LEU A 101      24.469  80.051  -9.159  1.00 17.52           C  
ANISOU  758  CA  LEU A 101     2273   2140   2243    -25    123    342       C  
ATOM    759  C   LEU A 101      24.625  80.922  -7.932  1.00 18.71           C  
ANISOU  759  C   LEU A 101     2434   2240   2434    -52    117    329       C  
ATOM    760  O   LEU A 101      24.124  82.064  -7.856  1.00 21.70           O  
ANISOU  760  O   LEU A 101     2855   2567   2823    -48    117    347       O  
ATOM    761  CB  LEU A 101      25.552  80.396 -10.183  1.00 18.73           C  
ANISOU  761  CB  LEU A 101     2425   2307   2382    -53    158    377       C  
ATOM    762  CG  LEU A 101      25.651  79.494 -11.405  1.00 18.93           C  
ANISOU  762  CG  LEU A 101     2440   2390   2363    -28    169    386       C  
ATOM    763  CD1 LEU A 101      26.850  79.955 -12.290  1.00 23.51           C  
ANISOU  763  CD1 LEU A 101     3014   2987   2931    -60    210    423       C  
ATOM    764  CD2 LEU A 101      25.716  78.004 -11.094  1.00 21.43           C  
ANISOU  764  CD2 LEU A 101     2721   2750   2670    -10    152    343       C  
ATOM    765  N   THR A 102      25.371  80.402  -6.977  1.00 17.70           N  
ANISOU  765  N   THR A 102     2272   2126   2328    -78    112    296       N  
ATOM    766  CA  THR A 102      25.732  81.154  -5.774  1.00 18.27           C  
ANISOU  766  CA  THR A 102     2350   2156   2436   -110    105    277       C  
ATOM    767  C   THR A 102      26.893  82.111  -6.090  1.00 19.68           C  
ANISOU  767  C   THR A 102     2534   2313   2630   -166    131    301       C  
ATOM    768  O   THR A 102      27.477  82.062  -7.148  1.00 20.09           O  
ANISOU  768  O   THR A 102     2576   2390   2665   -179    156    332       O  
ATOM    769  CB  THR A 102      26.120  80.188  -4.624  1.00 17.20           C  
ANISOU  769  CB  THR A 102     2173   2050   2311   -115     87    234       C  
ATOM    770  OG1 THR A 102      27.407  79.575  -4.905  1.00 17.12           O  
ANISOU  770  OG1 THR A 102     2121   2086   2298   -141    102    232       O  
ATOM    771  CG2 THR A 102      25.102  79.135  -4.384  1.00 17.04           C  
ANISOU  771  CG2 THR A 102     2145   2054   2274    -70     67    214       C  
ATOM    772  N   VAL A 103      27.245  82.920  -5.077  1.00 21.65           N  
ANISOU  772  N   VAL A 103     2794   2518   2911   -203    123    284       N  
ATOM    773  CA  VAL A 103      28.390  83.821  -5.114  1.00 22.95           C  
ANISOU  773  CA  VAL A 103     2960   2660   3098   -270    142    299       C  
ATOM    774  C   VAL A 103      29.671  83.066  -5.537  1.00 21.42           C  
ANISOU  774  C   VAL A 103     2703   2536   2897   -302    161    302       C  
ATOM    775  O   VAL A 103      30.562  83.584  -6.257  1.00 22.91           O  
ANISOU  775  O   VAL A 103     2885   2731   3088   -349    190    335       O  
ATOM    776  CB  VAL A 103      28.592  84.453  -3.668  1.00 22.91           C  
ANISOU  776  CB  VAL A 103     2965   2611   3127   -303    120    260       C  
ATOM    777  CG1 VAL A 103      29.803  85.320  -3.639  1.00 29.78           C  
ANISOU  777  CG1 VAL A 103     3832   3461   4022   -383    135    270       C  
ATOM    778  CG2 VAL A 103      27.304  85.225  -3.227  1.00 27.17           C  
ANISOU  778  CG2 VAL A 103     3569   3083   3670   -262    103    254       C  
ATOM    779  N   ASP A 104      29.778  81.836  -5.038  1.00 17.98           N  
ANISOU  779  N   ASP A 104     2222   2154   2453   -275    145    269       N  
ATOM    780  CA  ASP A 104      30.943  80.991  -5.269  1.00 17.87           C  
ANISOU  780  CA  ASP A 104     2147   2211   2431   -289    159    265       C  
ATOM    781  C   ASP A 104      30.885  80.120  -6.533  1.00 17.78           C  
ANISOU  781  C   ASP A 104     2124   2248   2382   -250    179    286       C  
ATOM    782  O   ASP A 104      31.799  79.328  -6.796  1.00 20.01           O  
ANISOU  782  O   ASP A 104     2357   2592   2651   -249    192    282       O  
ATOM    783  CB  ASP A 104      31.175  80.137  -4.001  1.00 17.08           C  
ANISOU  783  CB  ASP A 104     2010   2138   2340   -277    130    218       C  
ATOM    784  CG  ASP A 104      31.334  81.013  -2.758  1.00 20.04           C  
ANISOU  784  CG  ASP A 104     2395   2470   2746   -317    110    193       C  
ATOM    785  OD1 ASP A 104      32.371  81.727  -2.690  1.00 22.77           O  
ANISOU  785  OD1 ASP A 104     2721   2818   3112   -380    120    199       O  
ATOM    786  OD2 ASP A 104      30.406  81.039  -1.927  1.00 18.81           O  
ANISOU  786  OD2 ASP A 104     2270   2281   2596   -290     85    170       O  
ATOM    787  N   GLY A 105      29.823  80.290  -7.305  1.00 18.05           N  
ANISOU  787  N   GLY A 105     2203   2257   2395   -215    180    309       N  
ATOM    788  CA  GLY A 105      29.649  79.568  -8.564  1.00 17.83           C  
ANISOU  788  CA  GLY A 105     2174   2272   2327   -178    196    328       C  
ATOM    789  C   GLY A 105      29.049  78.205  -8.475  1.00 17.85           C  
ANISOU  789  C   GLY A 105     2167   2305   2309   -125    174    297       C  
ATOM    790  O   GLY A 105      29.119  77.412  -9.431  1.00 18.93           O  
ANISOU  790  O   GLY A 105     2296   2483   2410    -96    186    303       O  
ATOM    791  N   PHE A 106      28.425  77.910  -7.334  1.00 15.65           N  
ANISOU  791  N   PHE A 106     1891   2005   2049   -113    144    264       N  
ATOM    792  CA  PHE A 106      27.814  76.606  -7.167  1.00 15.08           C  
ANISOU  792  CA  PHE A 106     1813   1955   1958    -70    123    237       C  
ATOM    793  C   PHE A 106      26.363  76.636  -7.660  1.00 14.38           C  
ANISOU  793  C   PHE A 106     1762   1848   1852    -38    108    245       C  
ATOM    794  O   PHE A 106      25.677  77.641  -7.525  1.00 14.67           O  
ANISOU  794  O   PHE A 106     1827   1846   1900    -41    103    260       O  
ATOM    795  CB  PHE A 106      27.788  76.158  -5.695  1.00 14.98           C  
ANISOU  795  CB  PHE A 106     1785   1936   1970    -72     97    200       C  
ATOM    796  CG  PHE A 106      29.110  76.237  -4.971  1.00 15.40           C  
ANISOU  796  CG  PHE A 106     1799   2007   2042   -104    103    188       C  
ATOM    797  CD1 PHE A 106      30.319  75.929  -5.596  1.00 14.79           C  
ANISOU  797  CD1 PHE A 106     1687   1977   1955   -113    127    197       C  
ATOM    798  CD2 PHE A 106      29.124  76.517  -3.607  1.00 14.81           C  
ANISOU  798  CD2 PHE A 106     1719   1912   1994   -119     83    164       C  
ATOM    799  CE1 PHE A 106      31.492  75.989  -4.880  1.00 15.24           C  
ANISOU  799  CE1 PHE A 106     1700   2060   2029   -141    128    184       C  
ATOM    800  CE2 PHE A 106      30.333  76.539  -2.884  1.00 15.60           C  
ANISOU  800  CE2 PHE A 106     1780   2037   2110   -148     82    148       C  
ATOM    801  CZ  PHE A 106      31.501  76.304  -3.559  1.00 15.95           C  
ANISOU  801  CZ  PHE A 106     1786   2129   2146   -160    104    160       C  
ATOM    802  N   GLU A 107      25.859  75.520  -8.192  1.00 14.33           N  
ANISOU  802  N   GLU A 107     1757   1870   1817     -5     98    234       N  
ATOM    803  CA  GLU A 107      24.416  75.391  -8.448  1.00 14.07           C  
ANISOU  803  CA  GLU A 107     1748   1828   1769     22     76    234       C  
ATOM    804  C   GLU A 107      23.709  75.608  -7.103  1.00 13.68           C  
ANISOU  804  C   GLU A 107     1698   1749   1747     19     54    215       C  
ATOM    805  O   GLU A 107      24.186  75.152  -6.050  1.00 13.61           O  
ANISOU  805  O   GLU A 107     1671   1740   1758      8     48    190       O  
ATOM    806  CB  GLU A 107      24.095  74.044  -9.098  1.00 13.31           C  
ANISOU  806  CB  GLU A 107     1652   1766   1640     47     65    216       C  
ATOM    807  CG  GLU A 107      22.633  73.789  -9.403  1.00 14.34           C  
ANISOU  807  CG  GLU A 107     1799   1897   1752     69     40    213       C  
ATOM    808  CD  GLU A 107      21.820  73.290  -8.193  1.00 13.95           C  
ANISOU  808  CD  GLU A 107     1741   1835   1723     68     14    187       C  
ATOM    809  OE1 GLU A 107      22.376  72.462  -7.434  1.00 14.39           O  
ANISOU  809  OE1 GLU A 107     1784   1892   1790     60     12    164       O  
ATOM    810  OE2 GLU A 107      20.655  73.731  -7.999  1.00 13.75           O  
ANISOU  810  OE2 GLU A 107     1722   1803   1700     77     -1    193       O  
ATOM    811  N   SER A 108      22.596  76.327  -7.111  1.00 13.60           N  
ANISOU  811  N   SER A 108     1710   1718   1738     34     44    227       N  
ATOM    812  CA  SER A 108      22.096  76.837  -5.824  1.00 13.05           C  
ANISOU  812  CA  SER A 108     1642   1619   1695     32     30    212       C  
ATOM    813  C   SER A 108      21.628  75.779  -4.828  1.00 12.99           C  
ANISOU  813  C   SER A 108     1616   1627   1693     38     10    181       C  
ATOM    814  O   SER A 108      21.792  75.966  -3.624  1.00 13.08           O  
ANISOU  814  O   SER A 108     1621   1622   1725     28      5    163       O  
ATOM    815  CB  SER A 108      21.045  77.945  -6.012  1.00 13.39           C  
ANISOU  815  CB  SER A 108     1713   1636   1737     55     26    233       C  
ATOM    816  OG  SER A 108      19.801  77.431  -6.473  1.00 15.29           O  
ANISOU  816  OG  SER A 108     1951   1904   1954     87      8    234       O  
ATOM    817  N   GLN A 109      21.066  74.681  -5.305  1.00 12.68           N  
ANISOU  817  N   GLN A 109     1570   1616   1630     52      0    173       N  
ATOM    818  CA  GLN A 109      20.574  73.658  -4.377  1.00 12.39           C  
ANISOU  818  CA  GLN A 109     1521   1589   1597     52    -18    148       C  
ATOM    819  C   GLN A 109      21.750  72.912  -3.754  1.00 12.52           C  
ANISOU  819  C   GLN A 109     1525   1608   1623     38    -13    130       C  
ATOM    820  O   GLN A 109      21.806  72.757  -2.533  1.00 12.60           O  
ANISOU  820  O   GLN A 109     1526   1610   1648     32    -20    114       O  
ATOM    821  CB  GLN A 109      19.545  72.737  -5.028  1.00 11.99           C  
ANISOU  821  CB  GLN A 109     1470   1563   1520     63    -34    144       C  
ATOM    822  CG  GLN A 109      18.339  73.500  -5.541  1.00 12.81           C  
ANISOU  822  CG  GLN A 109     1578   1674   1613     82    -43    162       C  
ATOM    823  CD  GLN A 109      17.212  72.605  -5.968  1.00 12.62           C  
ANISOU  823  CD  GLN A 109     1545   1681   1567     85    -65    154       C  
ATOM    824  OE1 GLN A 109      16.570  71.938  -5.131  1.00 12.35           O  
ANISOU  824  OE1 GLN A 109     1497   1655   1540     76    -77    139       O  
ATOM    825  NE2 GLN A 109      16.933  72.579  -7.275  1.00 13.80           N  
ANISOU  825  NE2 GLN A 109     1703   1851   1688     97    -70    165       N  
ATOM    826  N   ILE A 110      22.662  72.378  -4.554  1.00 12.61           N  
ANISOU  826  N   ILE A 110     1535   1635   1622     37     -2    131       N  
ATOM    827  CA  ILE A 110      23.837  71.714  -3.955  1.00 12.11           C  
ANISOU  827  CA  ILE A 110     1455   1579   1565     32      2    115       C  
ATOM    828  C   ILE A 110      24.634  72.722  -3.133  1.00 12.15           C  
ANISOU  828  C   ILE A 110     1446   1573   1597     12     10    116       C  
ATOM    829  O   ILE A 110      25.178  72.373  -2.065  1.00 13.22           O  
ANISOU  829  O   ILE A 110     1568   1711   1744      8      3     98       O  
ATOM    830  CB  ILE A 110      24.685  70.975  -5.010  1.00 12.01           C  
ANISOU  830  CB  ILE A 110     1441   1591   1530     44     15    115       C  
ATOM    831  CG1 ILE A 110      25.683  70.024  -4.382  1.00 12.63           C  
ANISOU  831  CG1 ILE A 110     1504   1682   1610     52     15     96       C  
ATOM    832  CG2 ILE A 110      25.440  71.944  -5.933  1.00 13.56           C  
ANISOU  832  CG2 ILE A 110     1631   1797   1722     34     40    139       C  
ATOM    833  CD1 ILE A 110      25.061  68.762  -3.759  1.00 13.63           C  
ANISOU  833  CD1 ILE A 110     1647   1798   1730     65     -5     76       C  
ATOM    834  N   GLY A 111      24.707  73.962  -3.597  1.00 13.10           N  
ANISOU  834  N   GLY A 111     1573   1677   1724      0     22    136       N  
ATOM    835  CA  GLY A 111      25.495  74.988  -2.911  1.00 13.70           C  
ANISOU  835  CA  GLY A 111     1640   1736   1825    -28     29    136       C  
ATOM    836  C   GLY A 111      24.933  75.354  -1.548  1.00 13.72           C  
ANISOU  836  C   GLY A 111     1650   1716   1846    -29     12    118       C  
ATOM    837  O   GLY A 111      25.694  75.532  -0.578  1.00 14.34           O  
ANISOU  837  O   GLY A 111     1713   1793   1940    -47      7    101       O  
ATOM    838  N   THR A 112      23.640  75.526  -1.464  1.00 13.15           N  
ANISOU  838  N   THR A 112     1596   1629   1768     -9      2    120       N  
ATOM    839  CA  THR A 112      22.967  75.912  -0.220  1.00 13.27           C  
ANISOU  839  CA  THR A 112     1619   1627   1796     -3    -11    104       C  
ATOM    840  C   THR A 112      22.847  74.714   0.717  1.00 13.08           C  
ANISOU  840  C   THR A 112     1578   1624   1765      4    -24     83       C  
ATOM    841  O   THR A 112      23.233  74.754   1.887  1.00 14.75           O  
ANISOU  841  O   THR A 112     1784   1834   1985     -1    -31     64       O  
ATOM    842  CB  THR A 112      21.543  76.439  -0.492  1.00 14.01           C  
ANISOU  842  CB  THR A 112     1733   1709   1882     22    -15    116       C  
ATOM    843  OG1 THR A 112      21.605  77.563  -1.388  1.00 15.29           O  
ANISOU  843  OG1 THR A 112     1917   1845   2046     20     -2    140       O  
ATOM    844  CG2 THR A 112      20.830  76.855   0.818  1.00 16.32           C  
ANISOU  844  CG2 THR A 112     2031   1988   2182     35    -25     98       C  
ATOM    845  N   ASN A 113      22.286  73.614   0.211  1.00 11.71           N  
ANISOU  845  N   ASN A 113     1403   1471   1574     18    -28     86       N  
ATOM    846  CA  ASN A 113      21.817  72.528   1.057  1.00 11.04           C  
ANISOU  846  CA  ASN A 113     1312   1398   1481     25    -40     73       C  
ATOM    847  C   ASN A 113      22.966  71.661   1.528  1.00 11.54           C  
ANISOU  847  C   ASN A 113     1366   1473   1545     21    -42     60       C  
ATOM    848  O   ASN A 113      22.939  71.149   2.643  1.00 12.19           O  
ANISOU  848  O   ASN A 113     1446   1559   1626     25    -51     49       O  
ATOM    849  CB  ASN A 113      20.840  71.671   0.266  1.00 11.43           C  
ANISOU  849  CB  ASN A 113     1367   1461   1513     33    -45     80       C  
ATOM    850  CG  ASN A 113      19.567  72.397  -0.152  1.00 11.59           C  
ANISOU  850  CG  ASN A 113     1391   1482   1529     43    -48     93       C  
ATOM    851  OD1 ASN A 113      19.300  73.527   0.287  1.00 12.55           O  
ANISOU  851  OD1 ASN A 113     1516   1590   1661     50    -45     96       O  
ATOM    852  ND2 ASN A 113      18.762  71.752  -1.012  1.00 11.86           N  
ANISOU  852  ND2 ASN A 113     1425   1533   1545     45    -55     99       N  
ATOM    853  N   HIS A 114      23.969  71.481   0.665  1.00 11.51           N  
ANISOU  853  N   HIS A 114     1354   1479   1537     19    -32     65       N  
ATOM    854  CA  HIS A 114      25.132  70.678   1.007  1.00 10.89           C  
ANISOU  854  CA  HIS A 114     1262   1418   1456     24    -33     54       C  
ATOM    855  C   HIS A 114      26.409  71.496   1.240  1.00 11.52           C  
ANISOU  855  C   HIS A 114     1318   1508   1551      7    -26     51       C  
ATOM    856  O   HIS A 114      27.003  71.442   2.324  1.00 12.91           O  
ANISOU  856  O   HIS A 114     1479   1692   1732      5    -36     36       O  
ATOM    857  CB  HIS A 114      25.379  69.577  -0.058  1.00 12.02           C  
ANISOU  857  CB  HIS A 114     1412   1574   1580     41    -27     57       C  
ATOM    858  CG  HIS A 114      26.658  68.848   0.129  1.00 11.55           C  
ANISOU  858  CG  HIS A 114     1337   1536   1515     56    -25     47       C  
ATOM    859  ND1 HIS A 114      26.913  68.049   1.220  1.00 13.29           N  
ANISOU  859  ND1 HIS A 114     1557   1757   1733     70    -37     36       N  
ATOM    860  CD2 HIS A 114      27.776  68.813  -0.634  1.00 12.59           C  
ANISOU  860  CD2 HIS A 114     1449   1692   1640     63    -10     50       C  
ATOM    861  CE1 HIS A 114      28.149  67.573   1.136  1.00 13.48           C  
ANISOU  861  CE1 HIS A 114     1563   1808   1751     89    -33     30       C  
ATOM    862  NE2 HIS A 114      28.699  68.020   0.008  1.00 12.94           N  
ANISOU  862  NE2 HIS A 114     1480   1757   1680     85    -15     38       N  
ATOM    863  N   LEU A 115      26.888  72.219   0.228  1.00 11.54           N  
ANISOU  863  N   LEU A 115     1314   1513   1557     -6     -9     65       N  
ATOM    864  CA  LEU A 115      28.233  72.802   0.350  1.00 12.42           C  
ANISOU  864  CA  LEU A 115     1395   1642   1680    -29     -1     63       C  
ATOM    865  C   LEU A 115      28.373  73.836   1.437  1.00 12.13           C  
ANISOU  865  C   LEU A 115     1355   1587   1664    -56    -11     51       C  
ATOM    866  O   LEU A 115      29.370  73.862   2.167  1.00 12.57           O  
ANISOU  866  O   LEU A 115     1382   1665   1727    -69    -19     37       O  
ATOM    867  CB  LEU A 115      28.758  73.347  -1.001  1.00 12.55           C  
ANISOU  867  CB  LEU A 115     1405   1668   1694    -44     23     86       C  
ATOM    868  CG  LEU A 115      28.927  72.275  -2.097  1.00 11.88           C  
ANISOU  868  CG  LEU A 115     1319   1610   1583    -14     35     92       C  
ATOM    869  CD1 LEU A 115      29.062  72.903  -3.520  1.00 14.49           C  
ANISOU  869  CD1 LEU A 115     1655   1947   1904    -25     60    119       C  
ATOM    870  CD2 LEU A 115      30.117  71.321  -1.829  1.00 13.20           C  
ANISOU  870  CD2 LEU A 115     1453   1819   1741      4     36     79       C  
ATOM    871  N   GLY A 116      27.353  74.675   1.598  1.00 12.50           N  
ANISOU  871  N   GLY A 116     1432   1597   1719    -61    -14     55       N  
ATOM    872  CA  GLY A 116      27.439  75.688   2.660  1.00 12.87           C  
ANISOU  872  CA  GLY A 116     1484   1620   1783    -83    -25     38       C  
ATOM    873  C   GLY A 116      27.420  75.032   4.056  1.00 12.00           C  
ANISOU  873  C   GLY A 116     1366   1526   1667    -67    -46     13       C  
ATOM    874  O   GLY A 116      28.129  75.463   4.947  1.00 13.23           O  
ANISOU  874  O   GLY A 116     1509   1687   1830    -86    -58     -6       O  
ATOM    875  N   HIS A 117      26.611  74.003   4.211  1.00 12.08           N  
ANISOU  875  N   HIS A 117     1385   1543   1660    -36    -51     14       N  
ATOM    876  CA  HIS A 117      26.563  73.193   5.442  1.00 12.04           C  
ANISOU  876  CA  HIS A 117     1376   1554   1644    -18    -67     -1       C  
ATOM    877  C   HIS A 117      27.852  72.416   5.700  1.00 12.09           C  
ANISOU  877  C   HIS A 117     1352   1597   1644    -13    -74     -9       C  
ATOM    878  O   HIS A 117      28.305  72.283   6.835  1.00 12.77           O  
ANISOU  878  O   HIS A 117     1428   1699   1725     -9    -90    -26       O  
ATOM    879  CB  HIS A 117      25.354  72.266   5.444  1.00 12.63           C  
ANISOU  879  CB  HIS A 117     1469   1626   1703      6    -68      7       C  
ATOM    880  CG  HIS A 117      24.062  72.958   5.781  1.00 11.66           C  
ANISOU  880  CG  HIS A 117     1365   1482   1581     10    -68      7       C  
ATOM    881  ND1 HIS A 117      22.890  72.699   5.097  1.00 12.62           N  
ANISOU  881  ND1 HIS A 117     1498   1599   1696     21    -62     23       N  
ATOM    882  CD2 HIS A 117      23.739  73.803   6.792  1.00 11.50           C  
ANISOU  882  CD2 HIS A 117     1354   1451   1564     10    -74     -7       C  
ATOM    883  CE1 HIS A 117      21.906  73.398   5.669  1.00 12.26           C  
ANISOU  883  CE1 HIS A 117     1463   1544   1651     29    -63     20       C  
ATOM    884  NE2 HIS A 117      22.405  74.116   6.678  1.00 12.00           N  
ANISOU  884  NE2 HIS A 117     1433   1504   1623     25    -69      0       N  
ATOM    885  N   PHE A 118      28.460  71.906   4.626  1.00 11.84           N  
ANISOU  885  N   PHE A 118     1306   1582   1609     -9    -61      3       N  
ATOM    886  CA  PHE A 118      29.744  71.222   4.712  1.00 12.40           C  
ANISOU  886  CA  PHE A 118     1344   1692   1672      2    -64     -2       C  
ATOM    887  C   PHE A 118      30.806  72.157   5.290  1.00 12.26           C  
ANISOU  887  C   PHE A 118     1293   1696   1669    -29    -71    -16       C  
ATOM    888  O   PHE A 118      31.531  71.795   6.229  1.00 13.16           O  
ANISOU  888  O   PHE A 118     1382   1840   1775    -19    -89    -32       O  
ATOM    889  CB  PHE A 118      30.135  70.753   3.308  1.00 12.18           C  
ANISOU  889  CB  PHE A 118     1309   1679   1638     12    -43     13       C  
ATOM    890  CG  PHE A 118      31.449  70.014   3.240  1.00 12.49           C  
ANISOU  890  CG  PHE A 118     1311   1765   1666     34    -42      8       C  
ATOM    891  CD1 PHE A 118      31.481  68.650   3.418  1.00 13.01           C  
ANISOU  891  CD1 PHE A 118     1390   1840   1712     80    -49      5       C  
ATOM    892  CD2 PHE A 118      32.646  70.681   3.036  1.00 13.97           C  
ANISOU  892  CD2 PHE A 118     1453   1990   1863      9    -34      8       C  
ATOM    893  CE1 PHE A 118      32.681  67.943   3.383  1.00 14.51           C  
ANISOU  893  CE1 PHE A 118     1548   2075   1889    111    -48      1       C  
ATOM    894  CE2 PHE A 118      33.854  69.978   2.999  1.00 14.72           C  
ANISOU  894  CE2 PHE A 118     1506   2139   1945     36    -33      4       C  
ATOM    895  CZ  PHE A 118      33.875  68.623   3.189  1.00 14.41           C  
ANISOU  895  CZ  PHE A 118     1480   2108   1884     91    -40      0       C  
ATOM    896  N   ALA A 119      30.909  73.352   4.726  1.00 13.20           N  
ANISOU  896  N   ALA A 119     1410   1797   1806    -69    -60    -10       N  
ATOM    897  CA  ALA A 119      31.858  74.328   5.207  1.00 13.60           C  
ANISOU  897  CA  ALA A 119     1433   1860   1873   -111    -68    -24       C  
ATOM    898  C   ALA A 119      31.562  74.742   6.630  1.00 13.96           C  
ANISOU  898  C   ALA A 119     1493   1892   1920   -117    -93    -51       C  
ATOM    899  O   ALA A 119      32.467  74.781   7.497  1.00 14.39           O  
ANISOU  899  O   ALA A 119     1515   1979   1971   -128   -113    -72       O  
ATOM    900  CB  ALA A 119      31.826  75.564   4.274  1.00 14.60           C  
ANISOU  900  CB  ALA A 119     1570   1955   2019   -156    -48     -7       C  
ATOM    901  N   LEU A 120      30.302  75.004   6.914  1.00 13.75           N  
ANISOU  901  N   LEU A 120     1510   1822   1891   -104    -95    -51       N  
ATOM    902  CA  LEU A 120      29.895  75.419   8.265  1.00 13.49           C  
ANISOU  902  CA  LEU A 120     1495   1775   1853   -102   -116    -77       C  
ATOM    903  C   LEU A 120      30.302  74.371   9.299  1.00 14.26           C  
ANISOU  903  C   LEU A 120     1574   1916   1929    -72   -135    -90       C  
ATOM    904  O   LEU A 120      30.828  74.689  10.398  1.00 13.74           O  
ANISOU  904  O   LEU A 120     1496   1867   1857    -82   -158   -117       O  
ATOM    905  CB  LEU A 120      28.394  75.663   8.344  1.00 13.52           C  
ANISOU  905  CB  LEU A 120     1543   1738   1853    -81   -109    -72       C  
ATOM    906  CG  LEU A 120      27.835  76.069   9.699  1.00 13.62           C  
ANISOU  906  CG  LEU A 120     1579   1740   1856    -71   -126    -98       C  
ATOM    907  CD1 LEU A 120      28.442  77.419  10.149  1.00 17.52           C  
ANISOU  907  CD1 LEU A 120     2079   2211   2365   -111   -139   -124       C  
ATOM    908  CD2 LEU A 120      26.294  76.118   9.646  1.00 16.47           C  
ANISOU  908  CD2 LEU A 120     1973   2073   2209    -42   -115    -87       C  
ATOM    909  N   THR A 121      29.998  73.114   8.992  1.00 13.64           N  
ANISOU  909  N   THR A 121     1497   1850   1834    -34   -128    -72       N  
ATOM    910  CA  THR A 121      30.270  72.017   9.923  1.00 13.05           C  
ANISOU  910  CA  THR A 121     1414   1808   1735      0   -144    -78       C  
ATOM    911  C   THR A 121      31.775  71.856  10.178  1.00 14.44           C  
ANISOU  911  C   THR A 121     1543   2035   1908     -2   -159    -90       C  
ATOM    912  O   THR A 121      32.219  71.767  11.341  1.00 15.28           O  
ANISOU  912  O   THR A 121     1637   2168   1998      6   -183   -108       O  
ATOM    913  CB  THR A 121      29.659  70.698   9.423  1.00 13.37           C  
ANISOU  913  CB  THR A 121     1474   1842   1762     37   -133    -55       C  
ATOM    914  OG1 THR A 121      28.255  70.859   9.225  1.00 12.91           O  
ANISOU  914  OG1 THR A 121     1451   1746   1705     36   -122    -45       O  
ATOM    915  CG2 THR A 121      29.917  69.566  10.458  1.00 14.25           C  
ANISOU  915  CG2 THR A 121     1588   1978   1846     75   -149    -57       C  
ATOM    916  N   ASN A 122      32.583  71.901   9.120  1.00 14.32           N  
ANISOU  916  N   ASN A 122     1496   2039   1905    -15   -145    -80       N  
ATOM    917  CA  ASN A 122      34.019  71.760   9.333  1.00 15.23           C  
ANISOU  917  CA  ASN A 122     1556   2214   2017    -17   -158    -90       C  
ATOM    918  C   ASN A 122      34.568  72.919  10.166  1.00 15.30           C  
ANISOU  918  C   ASN A 122     1543   2233   2035    -65   -180   -117       C  
ATOM    919  O   ASN A 122      35.499  72.713  10.952  1.00 16.84           O  
ANISOU  919  O   ASN A 122     1699   2481   2218    -59   -204   -135       O  
ATOM    920  CB  ASN A 122      34.781  71.708   7.997  1.00 16.44           C  
ANISOU  920  CB  ASN A 122     1674   2390   2179    -27   -134    -73       C  
ATOM    921  CG  ASN A 122      34.748  70.360   7.365  1.00 18.55           C  
ANISOU  921  CG  ASN A 122     1950   2670   2429     28   -121    -55       C  
ATOM    922  OD1 ASN A 122      34.714  69.328   8.061  1.00 18.09           O  
ANISOU  922  OD1 ASN A 122     1902   2621   2347     76   -135    -58       O  
ATOM    923  ND2 ASN A 122      34.813  70.349   6.005  1.00 18.95           N  
ANISOU  923  ND2 ASN A 122     1997   2718   2485     24    -93    -38       N  
ATOM    924  N   LEU A 123      34.030  74.112   9.998  1.00 15.15           N  
ANISOU  924  N   LEU A 123     1551   2167   2038   -110   -174   -123       N  
ATOM    925  CA  LEU A 123      34.512  75.270  10.745  1.00 16.39           C  
ANISOU  925  CA  LEU A 123     1698   2323   2206   -161   -195   -153       C  
ATOM    926  C   LEU A 123      34.069  75.240  12.213  1.00 16.92           C  
ANISOU  926  C   LEU A 123     1790   2388   2251   -140   -224   -181       C  
ATOM    927  O   LEU A 123      34.835  75.687  13.085  1.00 19.23           O  
ANISOU  927  O   LEU A 123     2057   2710   2538   -165   -253   -211       O  
ATOM    928  CB  LEU A 123      34.047  76.550  10.075  1.00 16.76           C  
ANISOU  928  CB  LEU A 123     1776   2309   2280   -211   -178   -149       C  
ATOM    929  CG  LEU A 123      34.674  76.837   8.717  1.00 18.29           C  
ANISOU  929  CG  LEU A 123     1942   2510   2495   -245   -151   -123       C  
ATOM    930  CD1 LEU A 123      33.895  77.909   7.972  1.00 20.37           C  
ANISOU  930  CD1 LEU A 123     2255   2704   2780   -276   -130   -109       C  
ATOM    931  CD2 LEU A 123      36.172  77.228   8.863  1.00 21.17           C  
ANISOU  931  CD2 LEU A 123     2243   2931   2869   -296   -164   -137       C  
ATOM    932  N   LEU A 124      32.910  74.665  12.522  1.00 15.63           N  
ANISOU  932  N   LEU A 124     1669   2197   2071    -95   -218   -171       N  
ATOM    933  CA  LEU A 124      32.420  74.588  13.909  1.00 16.15           C  
ANISOU  933  CA  LEU A 124     1760   2264   2110    -71   -240   -193       C  
ATOM    934  C   LEU A 124      32.892  73.362  14.695  1.00 16.56           C  
ANISOU  934  C   LEU A 124     1792   2371   2129    -24   -258   -190       C  
ATOM    935  O   LEU A 124      32.893  73.370  15.932  1.00 16.85           O  
ANISOU  935  O   LEU A 124     1836   2425   2139    -10   -282   -212       O  
ATOM    936  CB  LEU A 124      30.904  74.658  13.940  1.00 15.24           C  
ANISOU  936  CB  LEU A 124     1698   2099   1991    -50   -222   -182       C  
ATOM    937  CG  LEU A 124      30.291  75.984  13.528  1.00 15.90           C  
ANISOU  937  CG  LEU A 124     1813   2127   2098    -83   -211   -190       C  
ATOM    938  CD1 LEU A 124      28.728  75.928  13.572  1.00 19.14           C  
ANISOU  938  CD1 LEU A 124     2269   2502   2501    -51   -193   -178       C  
ATOM    939  CD2 LEU A 124      30.789  77.112  14.447  1.00 18.93           C  
ANISOU  939  CD2 LEU A 124     2203   2506   2483   -118   -237   -233       C  
ATOM    940  N   LEU A 125      33.233  72.269  13.999  1.00 16.46           N  
ANISOU  940  N   LEU A 125     1760   2379   2113      6   -245   -163       N  
ATOM    941  CA  LEU A 125      33.535  71.004  14.642  1.00 16.13           C  
ANISOU  941  CA  LEU A 125     1712   2376   2039     60   -258   -154       C  
ATOM    942  C   LEU A 125      34.494  71.074  15.838  1.00 16.94           C  
ANISOU  942  C   LEU A 125     1782   2535   2116     67   -296   -180       C  
ATOM    943  O   LEU A 125      34.215  70.410  16.845  1.00 17.51           O  
ANISOU  943  O   LEU A 125     1876   2621   2155    109   -310   -178       O  
ATOM    944  CB  LEU A 125      34.054  69.963  13.642  1.00 17.00           C  
ANISOU  944  CB  LEU A 125     1802   2504   2151     90   -242   -128       C  
ATOM    945  CG  LEU A 125      33.006  69.141  12.922  1.00 17.63           C  
ANISOU  945  CG  LEU A 125     1927   2539   2232    115   -216    -99       C  
ATOM    946  CD1 LEU A 125      33.638  68.366  11.763  1.00 19.13           C  
ANISOU  946  CD1 LEU A 125     2097   2743   2426    137   -199    -81       C  
ATOM    947  CD2 LEU A 125      32.249  68.150  13.822  1.00 18.29           C  
ANISOU  947  CD2 LEU A 125     2053   2610   2286    157   -221    -87       C  
ATOM    948  N   PRO A 126      35.565  71.867  15.749  1.00 17.60           N  
ANISOU  948  N   PRO A 126     1816   2654   2215     25   -312   -203       N  
ATOM    949  CA  PRO A 126      36.479  71.953  16.903  1.00 18.94           C  
ANISOU  949  CA  PRO A 126     1951   2886   2359     29   -352   -232       C  
ATOM    950  C   PRO A 126      35.861  72.522  18.179  1.00 18.17           C  
ANISOU  950  C   PRO A 126     1892   2772   2239     24   -375   -260       C  
ATOM    951  O   PRO A 126      36.490  72.405  19.256  1.00 20.32           O  
ANISOU  951  O   PRO A 126     2143   3097   2479     40   -411   -282       O  
ATOM    952  CB  PRO A 126      37.596  72.866  16.386  1.00 19.91           C  
ANISOU  952  CB  PRO A 126     2014   3041   2509    -32   -361   -251       C  
ATOM    953  CG  PRO A 126      37.524  72.756  14.927  1.00 19.87           C  
ANISOU  953  CG  PRO A 126     2003   3011   2534    -43   -322   -221       C  
ATOM    954  CD  PRO A 126      36.079  72.632  14.600  1.00 17.85           C  
ANISOU  954  CD  PRO A 126     1816   2680   2284    -27   -295   -202       C  
ATOM    955  N   ARG A 127      34.710  73.170  18.070  1.00 17.18           N  
ANISOU  955  N   ARG A 127     1818   2580   2126      5   -355   -262       N  
ATOM    956  CA  ARG A 127      34.039  73.828  19.189  1.00 18.01           C  
ANISOU  956  CA  ARG A 127     1964   2666   2210      2   -371   -291       C  
ATOM    957  C   ARG A 127      32.642  73.273  19.472  1.00 17.39           C  
ANISOU  957  C   ARG A 127     1940   2552   2113     46   -347   -268       C  
ATOM    958  O   ARG A 127      31.880  73.857  20.240  1.00 18.21           O  
ANISOU  958  O   ARG A 127     2082   2635   2201     47   -350   -288       O  
ATOM    959  CB  ARG A 127      34.002  75.331  18.956  1.00 19.06           C  
ANISOU  959  CB  ARG A 127     2108   2758   2374    -61   -373   -323       C  
ATOM    960  CG  ARG A 127      35.420  75.910  18.760  1.00 20.32           C  
ANISOU  960  CG  ARG A 127     2210   2957   2552   -116   -398   -347       C  
ATOM    961  CD  ARG A 127      35.451  77.442  18.780  1.00 22.99           C  
ANISOU  961  CD  ARG A 127     2568   3250   2916   -186   -407   -384       C  
ATOM    962  NE  ARG A 127      34.628  78.022  17.744  1.00 21.83           N  
ANISOU  962  NE  ARG A 127     2460   3028   2804   -205   -370   -363       N  
ATOM    963  CZ  ARG A 127      34.917  78.072  16.459  1.00 24.18           C  
ANISOU  963  CZ  ARG A 127     2735   3314   3135   -232   -344   -334       C  
ATOM    964  NH1 ARG A 127      36.040  77.555  15.988  1.00 25.67           N  
ANISOU  964  NH1 ARG A 127     2859   3562   3330   -244   -347   -321       N  
ATOM    965  NH2 ARG A 127      34.063  78.656  15.621  1.00 26.45           N  
ANISOU  965  NH2 ARG A 127     3067   3533   3449   -244   -313   -316       N  
ATOM    966  N   LEU A 128      32.353  72.110  18.906  1.00 16.94           N  
ANISOU  966  N   LEU A 128     1887   2494   2055     82   -325   -227       N  
ATOM    967  CA ALEU A 128      31.098  71.388  19.148  0.70 16.40           C  
ANISOU  967  CA ALEU A 128     1863   2399   1968    118   -303   -200       C  
ATOM    968  CA BLEU A 128      31.114  71.391  19.129  0.30 16.12           C  
ANISOU  968  CA BLEU A 128     1827   2363   1932    117   -303   -200       C  
ATOM    969  C   LEU A 128      31.313  70.284  20.178  1.00 17.01           C  
ANISOU  969  C   LEU A 128     1946   2517   1999    169   -318   -187       C  
ATOM    970  O   LEU A 128      32.364  69.604  20.190  1.00 18.31           O  
ANISOU  970  O   LEU A 128     2080   2723   2154    191   -336   -181       O  
ATOM    971  CB ALEU A 128      30.571  70.741  17.866  0.70 16.86           C  
ANISOU  971  CB ALEU A 128     1929   2423   2051    121   -270   -163       C  
ATOM    972  CB BLEU A 128      30.690  70.776  17.807  0.30 15.65           C  
ANISOU  972  CB BLEU A 128     1772   2272   1901    119   -271   -164       C  
ATOM    973  CG ALEU A 128      30.020  71.658  16.774  0.70 17.66           C  
ANISOU  973  CG ALEU A 128     2037   2478   2192     82   -248   -164       C  
ATOM    974  CG BLEU A 128      29.253  70.303  17.689  0.30 13.34           C  
ANISOU  974  CG BLEU A 128     1522   1942   1603    134   -244   -137       C  
ATOM    975  CD1ALEU A 128      29.466  70.825  15.582  0.70 17.82           C  
ANISOU  975  CD1ALEU A 128     2067   2473   2228     92   -219   -127       C  
ATOM    976  CD1BLEU A 128      28.232  71.463  17.820  0.30 12.39           C  
ANISOU  976  CD1BLEU A 128     1424   1789   1492    112   -233   -154       C  
ATOM    977  CD2ALEU A 128      28.970  72.659  17.312  0.70 20.78           C  
ANISOU  977  CD2ALEU A 128     2466   2842   2585     71   -243   -182       C  
ATOM    978  CD2BLEU A 128      29.137  69.588  16.330  0.30 13.49           C  
ANISOU  978  CD2BLEU A 128     1539   1940   1647    134   -221   -107       C  
ATOM    979  N   THR A 129      30.303  70.059  21.031  1.00 17.47           N  
ANISOU  979  N   THR A 129     2045   2566   2027    192   -310   -179       N  
ATOM    980  CA  THR A 129      30.421  69.063  22.107  1.00 17.67           C  
ANISOU  980  CA  THR A 129     2083   2626   2002    240   -323   -163       C  
ATOM    981  C   THR A 129      29.603  67.765  21.996  1.00 17.93           C  
ANISOU  981  C   THR A 129     2151   2637   2022    271   -296   -113       C  
ATOM    982  O   THR A 129      29.970  66.757  22.645  1.00 19.39           O  
ANISOU  982  O   THR A 129     2346   2847   2171    313   -307    -92       O  
ATOM    983  CB  THR A 129      30.084  69.655  23.479  1.00 18.70           C  
ANISOU  983  CB  THR A 129     2233   2778   2092    248   -339   -190       C  
ATOM    984  OG1 THR A 129      28.676  69.908  23.560  1.00 20.23           O  
ANISOU  984  OG1 THR A 129     2463   2937   2284    244   -308   -180       O  
ATOM    985  CG2 THR A 129      30.881  70.933  23.739  1.00 19.96           C  
ANISOU  985  CG2 THR A 129     2367   2956   2260    214   -371   -244       C  
ATOM    986  N   ASP A 130      28.517  67.763  21.222  1.00 15.81           N  
ANISOU  986  N   ASP A 130     1902   2323   1780    251   -263    -95       N  
ATOM    987  CA  ASP A 130      27.642  66.584  21.157  1.00 15.83           C  
ANISOU  987  CA  ASP A 130     1940   2304   1771    268   -238    -51       C  
ATOM    988  C   ASP A 130      27.436  66.061  19.756  1.00 14.18           C  
ANISOU  988  C   ASP A 130     1731   2055   1599    253   -218    -29       C  
ATOM    989  O   ASP A 130      27.901  64.963  19.435  1.00 15.40           O  
ANISOU  989  O   ASP A 130     1895   2205   1749    277   -219     -6       O  
ATOM    990  CB  ASP A 130      26.307  66.913  21.855  1.00 16.03           C  
ANISOU  990  CB  ASP A 130     1990   2322   1776    263   -218    -46       C  
ATOM    991  CG  ASP A 130      25.274  65.809  21.775  1.00 17.82           C  
ANISOU  991  CG  ASP A 130     2249   2527   1994    266   -190      0       C  
ATOM    992  OD1 ASP A 130      25.484  64.729  21.178  1.00 18.56           O  
ANISOU  992  OD1 ASP A 130     2355   2599   2096    273   -185     28       O  
ATOM    993  OD2 ASP A 130      24.181  66.022  22.371  1.00 21.19           O  
ANISOU  993  OD2 ASP A 130     2690   2958   2402    262   -170      7       O  
ATOM    994  N   ARG A 131      26.728  66.801  18.882  1.00 13.99           N  
ANISOU  994  N   ARG A 131     1702   2003   1609    218   -200    -36       N  
ATOM    995  CA  ARG A 131      26.315  66.212  17.627  1.00 13.39           C  
ANISOU  995  CA  ARG A 131     1633   1892   1560    205   -181    -14       C  
ATOM    996  C   ARG A 131      25.985  67.211  16.541  1.00 13.68           C  
ANISOU  996  C   ARG A 131     1654   1909   1635    172   -170    -28       C  
ATOM    997  O   ARG A 131      25.662  68.398  16.825  1.00 13.51           O  
ANISOU  997  O   ARG A 131     1625   1888   1619    156   -170    -51       O  
ATOM    998  CB  ARG A 131      25.110  65.270  17.825  1.00 14.61           C  
ANISOU  998  CB  ARG A 131     1822   2026   1699    206   -159     20       C  
ATOM    999  CG  ARG A 131      23.845  65.981  18.261  1.00 14.74           C  
ANISOU  999  CG  ARG A 131     1843   2045   1712    189   -143     17       C  
ATOM   1000  CD  ARG A 131      22.693  65.060  18.621  1.00 14.97           C  
ANISOU 1000  CD  ARG A 131     1899   2066   1721    185   -122     53       C  
ATOM   1001  NE  ARG A 131      23.014  64.188  19.765  1.00 14.83           N  
ANISOU 1001  NE  ARG A 131     1906   2064   1663    213   -128     73       N  
ATOM   1002  CZ  ARG A 131      22.182  63.284  20.277  1.00 15.13           C  
ANISOU 1002  CZ  ARG A 131     1973   2098   1678    210   -110    109       C  
ATOM   1003  NH1 ARG A 131      21.028  63.025  19.705  1.00 15.23           N  
ANISOU 1003  NH1 ARG A 131     1988   2091   1705    177    -86    128       N  
ATOM   1004  NH2 ARG A 131      22.583  62.569  21.333  1.00 16.70           N  
ANISOU 1004  NH2 ARG A 131     2197   2311   1837    239   -116    128       N  
ATOM   1005  N   VAL A 132      26.045  66.714  15.299  1.00 13.01           N  
ANISOU 1005  N   VAL A 132     1567   1801   1572    164   -159    -14       N  
ATOM   1006  CA  VAL A 132      25.566  67.387  14.088  1.00 12.22           C  
ANISOU 1006  CA  VAL A 132     1459   1678   1504    136   -145    -17       C  
ATOM   1007  C   VAL A 132      24.359  66.612  13.592  1.00 13.11           C  
ANISOU 1007  C   VAL A 132     1596   1767   1617    129   -127      8       C  
ATOM   1008  O   VAL A 132      24.432  65.401  13.425  1.00 13.78           O  
ANISOU 1008  O   VAL A 132     1700   1841   1692    141   -126     27       O  
ATOM   1009  CB  VAL A 132      26.650  67.397  13.006  1.00 13.19           C  
ANISOU 1009  CB  VAL A 132     1560   1803   1647    133   -148    -22       C  
ATOM   1010  CG1 VAL A 132      26.134  68.090  11.739  1.00 14.27           C  
ANISOU 1010  CG1 VAL A 132     1693   1916   1811    106   -132    -20       C  
ATOM   1011  CG2 VAL A 132      27.973  68.063  13.520  1.00 14.34           C  
ANISOU 1011  CG2 VAL A 132     1673   1982   1792    134   -168    -47       C  
ATOM   1012  N   VAL A 133      23.257  67.303  13.332  1.00 11.89           N  
ANISOU 1012  N   VAL A 133     1440   1603   1472    110   -114      8       N  
ATOM   1013  CA  VAL A 133      22.046  66.721  12.721  1.00 11.93           C  
ANISOU 1013  CA  VAL A 133     1458   1593   1480     96    -99     30       C  
ATOM   1014  C   VAL A 133      21.857  67.408  11.388  1.00 12.05           C  
ANISOU 1014  C   VAL A 133     1461   1595   1521     80    -94     25       C  
ATOM   1015  O   VAL A 133      21.672  68.642  11.358  1.00 12.62           O  
ANISOU 1015  O   VAL A 133     1521   1668   1603     76    -92     12       O  
ATOM   1016  CB  VAL A 133      20.793  66.943  13.584  1.00 11.74           C  
ANISOU 1016  CB  VAL A 133     1437   1582   1440     93    -88     38       C  
ATOM   1017  CG1 VAL A 133      19.556  66.349  12.908  1.00 13.61           C  
ANISOU 1017  CG1 VAL A 133     1677   1812   1681     71    -74     60       C  
ATOM   1018  CG2 VAL A 133      20.983  66.310  14.978  1.00 14.49           C  
ANISOU 1018  CG2 VAL A 133     1800   1947   1757    110    -91     45       C  
ATOM   1019  N   THR A 134      21.835  66.627  10.290  1.00 11.13           N  
ANISOU 1019  N   THR A 134     1353   1463   1412     73    -91     37       N  
ATOM   1020  CA  THR A 134      21.597  67.197   8.942  1.00 11.34           C  
ANISOU 1020  CA  THR A 134     1370   1480   1457     60    -85     35       C  
ATOM   1021  C   THR A 134      20.251  66.745   8.437  1.00 11.26           C  
ANISOU 1021  C   THR A 134     1366   1466   1444     43    -79     50       C  
ATOM   1022  O   THR A 134      19.961  65.534   8.485  1.00 12.65           O  
ANISOU 1022  O   THR A 134     1562   1634   1611     36    -79     62       O  
ATOM   1023  CB  THR A 134      22.758  66.789   8.012  1.00 11.70           C  
ANISOU 1023  CB  THR A 134     1415   1520   1509     66    -88     32       C  
ATOM   1024  OG1 THR A 134      23.999  67.287   8.552  1.00 12.22           O  
ANISOU 1024  OG1 THR A 134     1465   1600   1577     77    -95     18       O  
ATOM   1025  CG2 THR A 134      22.580  67.412   6.616  1.00 13.64           C  
ANISOU 1025  CG2 THR A 134     1654   1760   1769     54    -81     33       C  
ATOM   1026  N   VAL A 135      19.448  67.677   7.955  1.00 11.31           N  
ANISOU 1026  N   VAL A 135     1359   1478   1460     37    -74     50       N  
ATOM   1027  CA  VAL A 135      18.101  67.381   7.490  1.00 11.23           C  
ANISOU 1027  CA  VAL A 135     1344   1476   1445     22    -70     63       C  
ATOM   1028  C   VAL A 135      18.160  67.023   6.001  1.00 12.25           C  
ANISOU 1028  C   VAL A 135     1479   1594   1580     12    -74     65       C  
ATOM   1029  O   VAL A 135      18.659  67.818   5.193  1.00 13.38           O  
ANISOU 1029  O   VAL A 135     1616   1732   1732     20    -73     60       O  
ATOM   1030  CB  VAL A 135      17.104  68.516   7.818  1.00 11.87           C  
ANISOU 1030  CB  VAL A 135     1406   1576   1527     30    -63     63       C  
ATOM   1031  CG1 VAL A 135      15.674  68.067   7.462  1.00 13.38           C  
ANISOU 1031  CG1 VAL A 135     1583   1789   1711     14    -60     78       C  
ATOM   1032  CG2 VAL A 135      17.186  68.899   9.330  1.00 13.51           C  
ANISOU 1032  CG2 VAL A 135     1612   1795   1724     45    -59     55       C  
ATOM   1033  N   SER A 136      17.635  65.844   5.643  1.00 12.06           N  
ANISOU 1033  N   SER A 136     1468   1566   1548     -6    -78     73       N  
ATOM   1034  CA  SER A 136      17.525  65.371   4.274  1.00 12.21           C  
ANISOU 1034  CA  SER A 136     1497   1577   1566    -17    -84     72       C  
ATOM   1035  C   SER A 136      16.055  65.247   3.851  1.00 11.76           C  
ANISOU 1035  C   SER A 136     1425   1539   1503    -42    -88     80       C  
ATOM   1036  O   SER A 136      15.203  66.016   4.313  1.00 12.16           O  
ANISOU 1036  O   SER A 136     1448   1616   1555    -40    -83     86       O  
ATOM   1037  CB  SER A 136      18.340  64.092   4.157  1.00 12.56           C  
ANISOU 1037  CB  SER A 136     1575   1594   1604    -17    -89     68       C  
ATOM   1038  OG  SER A 136      18.372  63.580   2.813  1.00 12.50           O  
ANISOU 1038  OG  SER A 136     1583   1576   1591    -22    -95     61       O  
ATOM   1039  N   SER A 137      15.740  64.332   2.942  1.00 12.23           N  
ANISOU 1039  N   SER A 137     1500   1589   1555    -64    -98     78       N  
ATOM   1040  CA  SER A 137      14.421  64.205   2.375  1.00 12.10           C  
ANISOU 1040  CA  SER A 137     1465   1598   1533    -92   -107     83       C  
ATOM   1041  C   SER A 137      14.243  62.851   1.724  1.00 12.84           C  
ANISOU 1041  C   SER A 137     1589   1670   1617   -125   -121     76       C  
ATOM   1042  O   SER A 137      15.234  62.267   1.241  1.00 12.87           O  
ANISOU 1042  O   SER A 137     1630   1641   1619   -113   -123     65       O  
ATOM   1043  CB  SER A 137      14.261  65.264   1.277  1.00 13.06           C  
ANISOU 1043  CB  SER A 137     1567   1739   1654    -72   -111     80       C  
ATOM   1044  OG  SER A 137      13.067  65.107   0.509  1.00 13.61           O  
ANISOU 1044  OG  SER A 137     1617   1838   1713    -95   -125     83       O  
ATOM   1045  N   MET A 138      13.002  62.384   1.605  1.00 13.16           N  
ANISOU 1045  N   MET A 138     1615   1731   1652   -166   -130     81       N  
ATOM   1046  CA  MET A 138      12.665  61.260   0.726  1.00 14.06           C  
ANISOU 1046  CA  MET A 138     1756   1827   1756   -204   -149     70       C  
ATOM   1047  C   MET A 138      13.130  61.482  -0.710  1.00 14.14           C  
ANISOU 1047  C   MET A 138     1779   1835   1756   -183   -160     52       C  
ATOM   1048  O   MET A 138      13.355  60.507  -1.457  1.00 14.48           O  
ANISOU 1048  O   MET A 138     1863   1849   1789   -199   -174     36       O  
ATOM   1049  CB  MET A 138      11.156  61.005   0.742  1.00 16.54           C  
ANISOU 1049  CB  MET A 138     2036   2181   2067   -255   -159     78       C  
ATOM   1050  CG  MET A 138      10.619  60.414   2.000  1.00 19.26           C  
ANISOU 1050  CG  MET A 138     2377   2526   2415   -290   -147     96       C  
ATOM   1051  SD  MET A 138      11.131  58.783   2.397  1.00 20.96           S  
ANISOU 1051  SD  MET A 138     2663   2671   2629   -325   -149     96       S  
ATOM   1052  CE  MET A 138      10.228  57.897   1.133  1.00 22.93           C  
ANISOU 1052  CE  MET A 138     2923   2918   2870   -389   -179     78       C  
ATOM   1053  N   ALA A 139      13.265  62.730  -1.124  1.00 14.05           N  
ANISOU 1053  N   ALA A 139     1739   1852   1747   -148   -155     56       N  
ATOM   1054  CA  ALA A 139      13.770  63.043  -2.449  1.00 13.11           C  
ANISOU 1054  CA  ALA A 139     1631   1733   1615   -124   -161     45       C  
ATOM   1055  C   ALA A 139      15.174  62.557  -2.691  1.00 13.67           C  
ANISOU 1055  C   ALA A 139     1745   1765   1684   -100   -153     33       C  
ATOM   1056  O   ALA A 139      15.615  62.517  -3.848  1.00 13.82           O  
ANISOU 1056  O   ALA A 139     1780   1783   1687    -85   -157     22       O  
ATOM   1057  CB  ALA A 139      13.677  64.562  -2.734  1.00 14.54           C  
ANISOU 1057  CB  ALA A 139     1779   1946   1799    -90   -153     58       C  
ATOM   1058  N   HIS A 140      15.894  62.118  -1.659  1.00 12.79           N  
ANISOU 1058  N   HIS A 140     1650   1624   1583    -93   -142     35       N  
ATOM   1059  CA  HIS A 140      17.224  61.540  -1.897  1.00 13.51           C  
ANISOU 1059  CA  HIS A 140     1779   1684   1670    -65   -135     23       C  
ATOM   1060  C   HIS A 140      17.190  60.270  -2.736  1.00 13.45           C  
ANISOU 1060  C   HIS A 140     1818   1648   1644    -78   -150      3       C  
ATOM   1061  O   HIS A 140      18.190  59.967  -3.394  1.00 14.19           O  
ANISOU 1061  O   HIS A 140     1939   1728   1725    -46   -146     -9       O  
ATOM   1062  CB  HIS A 140      17.993  61.271  -0.587  1.00 13.40           C  
ANISOU 1062  CB  HIS A 140     1773   1649   1667    -50   -124     30       C  
ATOM   1063  CG  HIS A 140      17.724  59.930   0.054  1.00 13.19           C  
ANISOU 1063  CG  HIS A 140     1786   1587   1638    -73   -131     30       C  
ATOM   1064  ND1 HIS A 140      16.746  59.724   1.013  1.00 12.79           N  
ANISOU 1064  ND1 HIS A 140     1726   1539   1594   -109   -132     45       N  
ATOM   1065  CD2 HIS A 140      18.346  58.732  -0.109  1.00 13.54           C  
ANISOU 1065  CD2 HIS A 140     1883   1589   1672    -63   -135     18       C  
ATOM   1066  CE1 HIS A 140      16.801  58.465   1.420  1.00 12.63           C  
ANISOU 1066  CE1 HIS A 140     1753   1478   1569   -124   -136     46       C  
ATOM   1067  NE2 HIS A 140      17.750  57.833   0.742  1.00 13.02           N  
ANISOU 1067  NE2 HIS A 140     1844   1495   1608    -95   -140     28       N  
ATOM   1068  N   TRP A 141      16.080  59.547  -2.692  1.00 14.41           N  
ANISOU 1068  N   TRP A 141     1950   1763   1762   -125   -167      1       N  
ATOM   1069  CA  TRP A 141      16.029  58.193  -3.293  1.00 14.67           C  
ANISOU 1069  CA  TRP A 141     2040   1755   1778   -145   -183    -21       C  
ATOM   1070  C   TRP A 141      16.394  58.165  -4.779  1.00 15.26           C  
ANISOU 1070  C   TRP A 141     2133   1835   1828   -123   -192    -44       C  
ATOM   1071  O   TRP A 141      17.228  57.355  -5.180  1.00 16.92           O  
ANISOU 1071  O   TRP A 141     2394   2009   2025    -98   -191    -63       O  
ATOM   1072  CB  TRP A 141      14.681  57.537  -2.980  1.00 15.41           C  
ANISOU 1072  CB  TRP A 141     2134   1846   1875   -212   -201    -18       C  
ATOM   1073  CG  TRP A 141      14.574  56.936  -1.613  1.00 14.84           C  
ANISOU 1073  CG  TRP A 141     2076   1745   1818   -233   -191      0       C  
ATOM   1074  CD1 TRP A 141      14.138  57.526  -0.467  1.00 15.44           C  
ANISOU 1074  CD1 TRP A 141     2109   1849   1909   -242   -178     26       C  
ATOM   1075  CD2 TRP A 141      14.904  55.564  -1.251  1.00 16.95           C  
ANISOU 1075  CD2 TRP A 141     2411   1946   2081   -247   -195     -5       C  
ATOM   1076  NE1 TRP A 141      14.204  56.628   0.601  1.00 17.67           N  
ANISOU 1076  NE1 TRP A 141     2426   2091   2195   -260   -171     40       N  
ATOM   1077  CE2 TRP A 141      14.655  55.429   0.126  1.00 18.09           C  
ANISOU 1077  CE2 TRP A 141     2548   2084   2238   -265   -182     22       C  
ATOM   1078  CE3 TRP A 141      15.327  54.450  -1.984  1.00 18.37           C  
ANISOU 1078  CE3 TRP A 141     2662   2070   2246   -245   -208    -30       C  
ATOM   1079  CZ2 TRP A 141      14.863  54.211   0.811  1.00 20.76           C  
ANISOU 1079  CZ2 TRP A 141     2950   2361   2576   -280   -180     30       C  
ATOM   1080  CZ3 TRP A 141      15.530  53.235  -1.280  1.00 20.86           C  
ANISOU 1080  CZ3 TRP A 141     3043   2320   2563   -258   -207    -26       C  
ATOM   1081  CH2 TRP A 141      15.294  53.155   0.076  1.00 22.38           C  
ANISOU 1081  CH2 TRP A 141     3226   2507   2769   -276   -194      6       C  
ATOM   1082  N   PRO A 142      15.825  59.056  -5.611  1.00 15.26           N  
ANISOU 1082  N   PRO A 142     2096   1882   1820   -125   -199    -42       N  
ATOM   1083  CA  PRO A 142      16.248  59.072  -7.033  1.00 15.80           C  
ANISOU 1083  CA  PRO A 142     2184   1960   1858    -99   -204    -62       C  
ATOM   1084  C   PRO A 142      17.513  59.847  -7.315  1.00 15.85           C  
ANISOU 1084  C   PRO A 142     2181   1979   1862    -43   -178    -54       C  
ATOM   1085  O   PRO A 142      17.933  59.952  -8.493  1.00 18.21           O  
ANISOU 1085  O   PRO A 142     2492   2292   2133    -17   -177    -66       O  
ATOM   1086  CB  PRO A 142      15.080  59.739  -7.749  1.00 16.49           C  
ANISOU 1086  CB  PRO A 142     2234   2096   1934   -123   -223    -58       C  
ATOM   1087  CG  PRO A 142      14.440  60.622  -6.670  1.00 16.22           C  
ANISOU 1087  CG  PRO A 142     2146   2089   1928   -135   -214    -29       C  
ATOM   1088  CD  PRO A 142      14.570  59.808  -5.403  1.00 15.08           C  
ANISOU 1088  CD  PRO A 142     2020   1903   1804   -157   -207    -26       C  
ATOM   1089  N   GLY A 143      18.099  60.441  -6.279  1.00 15.15           N  
ANISOU 1089  N   GLY A 143     2067   1890   1799    -26   -158    -34       N  
ATOM   1090  CA  GLY A 143      19.274  61.282  -6.475  1.00 15.07           C  
ANISOU 1090  CA  GLY A 143     2039   1897   1790     16   -133    -24       C  
ATOM   1091  C   GLY A 143      20.501  60.477  -6.887  1.00 14.95           C  
ANISOU 1091  C   GLY A 143     2060   1862   1758     54   -123    -42       C  
ATOM   1092  O   GLY A 143      20.627  59.310  -6.587  1.00 15.87           O  
ANISOU 1092  O   GLY A 143     2217   1941   1870     54   -131    -58       O  
ATOM   1093  N   ARG A 144      21.443  61.152  -7.545  1.00 15.09           N  
ANISOU 1093  N   ARG A 144     2061   1907   1766     88   -102    -37       N  
ATOM   1094  CA AARG A 144      22.742  60.564  -7.892  0.70 16.22           C  
ANISOU 1094  CA AARG A 144     2225   2046   1892    133    -86    -50       C  
ATOM   1095  CA BARG A 144      22.727  60.577  -7.935  0.30 15.90           C  
ANISOU 1095  CA BARG A 144     2183   2006   1849    133    -86    -50       C  
ATOM   1096  C   ARG A 144      23.769  61.673  -7.789  1.00 15.42           C  
ANISOU 1096  C   ARG A 144     2077   1979   1801    154    -59    -29       C  
ATOM   1097  O   ARG A 144      23.520  62.808  -8.190  1.00 17.46           O  
ANISOU 1097  O   ARG A 144     2306   2264   2063    141    -51    -10       O  
ATOM   1098  CB AARG A 144      22.777  60.039  -9.345  0.70 18.40           C  
ANISOU 1098  CB AARG A 144     2535   2329   2125    152    -90    -73       C  
ATOM   1099  CB BARG A 144      22.678  60.126  -9.407  0.30 17.04           C  
ANISOU 1099  CB BARG A 144     2361   2159   1953    149    -91    -72       C  
ATOM   1100  CG AARG A 144      21.715  59.095  -9.761  0.70 21.84           C  
ANISOU 1100  CG AARG A 144     3016   2736   2544    124   -120    -98       C  
ATOM   1101  CG BARG A 144      22.266  58.696  -9.623  0.30 18.92           C  
ANISOU 1101  CG BARG A 144     2661   2355   2173    144   -114   -104       C  
ATOM   1102  CD AARG A 144      21.793  58.888 -11.291  0.70 26.00           C  
ANISOU 1102  CD AARG A 144     3570   3282   3024    146   -123   -119       C  
ATOM   1103  CD BARG A 144      22.104  58.390 -11.122  0.30 21.53           C  
ANISOU 1103  CD BARG A 144     3023   2699   2458    157   -121   -128       C  
ATOM   1104  NE AARG A 144      20.887  57.827 -11.719  0.70 30.17           N  
ANISOU 1104  NE AARG A 144     4150   3780   3534    118   -155   -151       N  
ATOM   1105  NE BARG A 144      21.749  56.994 -11.326  0.30 22.99           N  
ANISOU 1105  NE BARG A 144     3274   2835   2624    151   -145   -165       N  
ATOM   1106  CZ AARG A 144      21.145  56.518 -11.655  0.70 33.49           C  
ANISOU 1106  CZ AARG A 144     4631   4150   3942    129   -165   -182       C  
ATOM   1107  CZ BARG A 144      20.500  56.544 -11.417  0.30 26.03           C  
ANISOU 1107  CZ BARG A 144     3680   3200   3008     98   -178   -178       C  
ATOM   1108  NH1AARG A 144      22.309  56.053 -11.196  0.70 33.05           N  
ANISOU 1108  NH1AARG A 144     4592   4073   3890    177   -144   -185       N  
ATOM   1109  NH1BARG A 144      19.477  57.386 -11.355  0.30 27.10           N  
ANISOU 1109  NH1BARG A 144     3770   3367   3156     55   -190   -158       N  
ATOM   1110  NH2AARG A 144      20.217  55.660 -12.072  0.70 37.45           N  
ANISOU 1110  NH2AARG A 144     5179   4621   4428     92   -198   -211       N  
ATOM   1111  NH2BARG A 144      20.271  55.248 -11.581  0.30 27.99           N  
ANISOU 1111  NH2BARG A 144     3996   3396   3241     87   -199   -213       N  
ATOM   1112  N   ILE A 145      24.926  61.352  -7.250  1.00 14.14           N  
ANISOU 1112  N   ILE A 145     1910   1818   1645    185    -45    -31       N  
ATOM   1113  CA  ILE A 145      26.066  62.286  -7.221  1.00 13.75           C  
ANISOU 1113  CA  ILE A 145     1814   1807   1604    202    -18    -15       C  
ATOM   1114  C   ILE A 145      26.809  62.237  -8.534  1.00 14.90           C  
ANISOU 1114  C   ILE A 145     1962   1984   1715    235      1    -20       C  
ATOM   1115  O   ILE A 145      27.212  61.166  -8.982  1.00 17.22           O  
ANISOU 1115  O   ILE A 145     2290   2270   1982    272      1    -43       O  
ATOM   1116  CB  ILE A 145      27.051  61.948  -6.110  1.00 13.58           C  
ANISOU 1116  CB  ILE A 145     1777   1785   1598    224    -13    -16       C  
ATOM   1117  CG1 ILE A 145      26.380  61.914  -4.747  1.00 13.16           C  
ANISOU 1117  CG1 ILE A 145     1724   1702   1572    197    -32    -11       C  
ATOM   1118  CG2 ILE A 145      28.234  62.944  -6.123  1.00 14.30           C  
ANISOU 1118  CG2 ILE A 145     1813   1922   1697    233     11      0       C  
ATOM   1119  CD1 ILE A 145      25.619  63.209  -4.348  1.00 15.69           C  
ANISOU 1119  CD1 ILE A 145     2013   2029   1917    154    -34      7       C  
ATOM   1120  N   ASN A 146      26.939  63.388  -9.184  1.00 14.62           N  
ANISOU 1120  N   ASN A 146     1895   1980   1676    223     19      1       N  
ATOM   1121  CA  ASN A 146      27.737  63.540 -10.410  1.00 14.61           C  
ANISOU 1121  CA  ASN A 146     1888   2020   1642    252     46      4       C  
ATOM   1122  C   ASN A 146      29.042  64.234 -10.046  1.00 15.34           C  
ANISOU 1122  C   ASN A 146     1927   2149   1749    258     75     23       C  
ATOM   1123  O   ASN A 146      29.099  65.443  -9.864  1.00 15.63           O  
ANISOU 1123  O   ASN A 146     1931   2198   1808    225     85     49       O  
ATOM   1124  CB  ASN A 146      26.926  64.332 -11.435  1.00 14.44           C  
ANISOU 1124  CB  ASN A 146     1873   2010   1603    231     46     21       C  
ATOM   1125  CG  ASN A 146      27.531  64.287 -12.789  1.00 17.95           C  
ANISOU 1125  CG  ASN A 146     2323   2493   2002    263     70     21       C  
ATOM   1126  OD1 ASN A 146      28.766  64.435 -12.933  1.00 19.81           O  
ANISOU 1126  OD1 ASN A 146     2529   2765   2232    285    101     30       O  
ATOM   1127  ND2 ASN A 146      26.680  64.058 -13.813  1.00 19.36           N  
ANISOU 1127  ND2 ASN A 146     2537   2672   2145    265     56     12       N  
ATOM   1128  N   LEU A 147      30.120  63.445  -9.829  1.00 14.89           N  
ANISOU 1128  N   LEU A 147     1862   2110   1683    300     85      8       N  
ATOM   1129  CA  LEU A 147      31.384  64.014  -9.363  1.00 15.55           C  
ANISOU 1129  CA  LEU A 147     1888   2237   1783    303    109     22       C  
ATOM   1130  C   LEU A 147      32.053  64.901 -10.411  1.00 16.28           C  
ANISOU 1130  C   LEU A 147     1946   2382   1858    298    145     46       C  
ATOM   1131  O   LEU A 147      32.747  65.834 -10.040  1.00 19.03           O  
ANISOU 1131  O   LEU A 147     2243   2759   2229    270    161     68       O  
ATOM   1132  CB  LEU A 147      32.375  62.890  -8.986  1.00 16.16           C  
ANISOU 1132  CB  LEU A 147     1962   2330   1847    361    111      1       C  
ATOM   1133  CG  LEU A 147      31.993  62.039  -7.773  1.00 15.63           C  
ANISOU 1133  CG  LEU A 147     1924   2215   1798    369     80    -15       C  
ATOM   1134  CD1 LEU A 147      32.956  60.816  -7.710  1.00 17.14           C  
ANISOU 1134  CD1 LEU A 147     2126   2419   1964    441     85    -36       C  
ATOM   1135  CD2 LEU A 147      32.036  62.875  -6.467  1.00 18.02           C  
ANISOU 1135  CD2 LEU A 147     2186   2517   2143    328     70      0       C  
ATOM   1136  N   GLU A 148      31.832  64.608 -11.682  1.00 17.21           N  
ANISOU 1136  N   GLU A 148     2093   2511   1933    321    156     42       N  
ATOM   1137  CA  GLU A 148      32.455  65.374 -12.777  1.00 19.30           C  
ANISOU 1137  CA  GLU A 148     2330   2830   2174    319    194     69       C  
ATOM   1138  C   GLU A 148      31.753  66.693 -13.020  1.00 18.55           C  
ANISOU 1138  C   GLU A 148     2232   2720   2094    265    196    102       C  
ATOM   1139  O   GLU A 148      32.380  67.625 -13.539  1.00 20.50           O  
ANISOU 1139  O   GLU A 148     2446   3004   2337    246    228    135       O  
ATOM   1140  CB  GLU A 148      32.425  64.541 -14.070  1.00 22.08           C  
ANISOU 1140  CB  GLU A 148     2721   3200   2467    370    204     50       C  
ATOM   1141  CG  GLU A 148      33.270  63.261 -14.014  1.00 26.67           C  
ANISOU 1141  CG  GLU A 148     3309   3798   3024    436    209     17       C  
ATOM   1142  CD  GLU A 148      32.716  62.127 -13.099  1.00 32.33           C  
ANISOU 1142  CD  GLU A 148     4072   4453   3757    452    170    -17       C  
ATOM   1143  OE1 GLU A 148      31.454  62.025 -12.855  1.00 33.18           O  
ANISOU 1143  OE1 GLU A 148     4222   4505   3879    418    136    -24       O  
ATOM   1144  OE2 GLU A 148      33.565  61.303 -12.594  1.00 34.37           O  
ANISOU 1144  OE2 GLU A 148     4323   4722   4013    501    173    -35       O  
ATOM   1145  N   ASP A 149      30.481  66.797 -12.636  1.00 16.74           N  
ANISOU 1145  N   ASP A 149     2037   2440   1883    241    162     98       N  
ATOM   1146  CA  ASP A 149      29.698  67.997 -12.952  1.00 16.03           C  
ANISOU 1146  CA  ASP A 149     1952   2335   1802    202    162    129       C  
ATOM   1147  C   ASP A 149      28.643  68.202 -11.849  1.00 15.17           C  
ANISOU 1147  C   ASP A 149     1854   2175   1732    173    127    123       C  
ATOM   1148  O   ASP A 149      27.426  68.262 -12.089  1.00 15.53           O  
ANISOU 1148  O   ASP A 149     1930   2197   1772    166    104    122       O  
ATOM   1149  CB  ASP A 149      29.070  67.935 -14.344  1.00 16.89           C  
ANISOU 1149  CB  ASP A 149     2096   2456   1862    220    164    135       C  
ATOM   1150  CG  ASP A 149      28.469  69.247 -14.775  1.00 17.26           C  
ANISOU 1150  CG  ASP A 149     2147   2497   1914    189    169    174       C  
ATOM   1151  OD1 ASP A 149      28.768  70.294 -14.166  1.00 18.02           O  
ANISOU 1151  OD1 ASP A 149     2217   2581   2047    154    181    200       O  
ATOM   1152  OD2 ASP A 149      27.681  69.177 -15.753  1.00 19.43           O  
ANISOU 1152  OD2 ASP A 149     2454   2776   2151    204    160    176       O  
ATOM   1153  N   LEU A 150      29.123  68.339 -10.629  1.00 14.07           N  
ANISOU 1153  N   LEU A 150     1688   2026   1632    157    123    119       N  
ATOM   1154  CA  LEU A 150      28.251  68.498  -9.453  1.00 13.64           C  
ANISOU 1154  CA  LEU A 150     1639   1929   1611    134     93    112       C  
ATOM   1155  C   LEU A 150      27.356  69.730  -9.580  1.00 13.60           C  
ANISOU 1155  C   LEU A 150     1643   1903   1620    104     90    137       C  
ATOM   1156  O   LEU A 150      26.210  69.721  -9.095  1.00 13.44           O  
ANISOU 1156  O   LEU A 150     1641   1854   1611     97     64    131       O  
ATOM   1157  CB  LEU A 150      29.103  68.600  -8.191  1.00 13.61           C  
ANISOU 1157  CB  LEU A 150     1601   1927   1640    123     94    106       C  
ATOM   1158  CG  LEU A 150      28.337  68.456  -6.879  1.00 13.39           C  
ANISOU 1158  CG  LEU A 150     1583   1862   1641    110     65     92       C  
ATOM   1159  CD1 LEU A 150      27.986  67.000  -6.539  1.00 14.87           C  
ANISOU 1159  CD1 LEU A 150     1797   2034   1816    138     44     65       C  
ATOM   1160  CD2 LEU A 150      29.186  69.103  -5.716  1.00 15.91           C  
ANISOU 1160  CD2 LEU A 150     1863   2187   1992     88     67     94       C  
ATOM   1161  N   ASN A 151      27.877  70.784 -10.218  1.00 14.29           N  
ANISOU 1161  N   ASN A 151     1718   2006   1705     89    117    168       N  
ATOM   1162  CA  ASN A 151      27.198  72.069 -10.308  1.00 14.30           C  
ANISOU 1162  CA  ASN A 151     1731   1982   1720     65    117    196       C  
ATOM   1163  C   ASN A 151      26.393  72.271 -11.596  1.00 13.97           C  
ANISOU 1163  C   ASN A 151     1719   1946   1641     81    117    215       C  
ATOM   1164  O   ASN A 151      25.956  73.391 -11.877  1.00 15.03           O  
ANISOU 1164  O   ASN A 151     1865   2063   1779     69    122    245       O  
ATOM   1165  CB  ASN A 151      28.210  73.204 -10.078  1.00 15.06           C  
ANISOU 1165  CB  ASN A 151     1801   2079   1840     30    143    221       C  
ATOM   1166  CG  ASN A 151      28.655  73.279  -8.635  1.00 14.94           C  
ANISOU 1166  CG  ASN A 151     1760   2049   1864      8    131    202       C  
ATOM   1167  OD1 ASN A 151      27.830  73.433  -7.736  1.00 14.97           O  
ANISOU 1167  OD1 ASN A 151     1778   2019   1889      4    107    190       O  
ATOM   1168  ND2 ASN A 151      29.964  73.097  -8.369  1.00 19.23           N  
ANISOU 1168  ND2 ASN A 151     2265   2625   2414      0    148    197       N  
ATOM   1169  N   TRP A 152      26.110  71.197 -12.310  1.00 13.97           N  
ANISOU 1169  N   TRP A 152     1735   1968   1605    110    108    195       N  
ATOM   1170  CA  TRP A 152      25.151  71.220 -13.447  1.00 13.99           C  
ANISOU 1170  CA  TRP A 152     1767   1980   1569    128     98    205       C  
ATOM   1171  C   TRP A 152      25.577  72.257 -14.486  1.00 15.85           C  
ANISOU 1171  C   TRP A 152     2006   2232   1781    127    129    247       C  
ATOM   1172  O   TRP A 152      24.730  72.961 -15.057  1.00 16.08           O  
ANISOU 1172  O   TRP A 152     2056   2255   1795    131    122    272       O  
ATOM   1173  CB  TRP A 152      23.725  71.498 -12.930  1.00 13.65           C  
ANISOU 1173  CB  TRP A 152     1735   1908   1541    121     64    202       C  
ATOM   1174  CG  TRP A 152      23.139  70.476 -11.988  1.00 14.02           C  
ANISOU 1174  CG  TRP A 152     1781   1940   1605    118     34    166       C  
ATOM   1175  CD1 TRP A 152      23.361  70.371 -10.638  1.00 13.88           C  
ANISOU 1175  CD1 TRP A 152     1746   1899   1626    102     29    153       C  
ATOM   1176  CD2 TRP A 152      22.202  69.444 -12.324  1.00 13.21           C  
ANISOU 1176  CD2 TRP A 152     1696   1843   1478    127      4    140       C  
ATOM   1177  NE1 TRP A 152      22.619  69.337 -10.127  1.00 13.58           N  
ANISOU 1177  NE1 TRP A 152     1717   1852   1590    102      2    125       N  
ATOM   1178  CE2 TRP A 152      21.916  68.748 -11.140  1.00 12.29           C  
ANISOU 1178  CE2 TRP A 152     1574   1704   1390    114    -13    115       C  
ATOM   1179  CE3 TRP A 152      21.578  69.043 -13.522  1.00 13.29           C  
ANISOU 1179  CE3 TRP A 152     1727   1876   1443    143     -9    134       C  
ATOM   1180  CZ2 TRP A 152      21.033  67.669 -11.095  1.00 13.93           C  
ANISOU 1180  CZ2 TRP A 152     1796   1907   1586    109    -42     88       C  
ATOM   1181  CZ3 TRP A 152      20.700  67.964 -13.484  1.00 14.45           C  
ANISOU 1181  CZ3 TRP A 152     1889   2021   1579    138    -42    102       C  
ATOM   1182  CH2 TRP A 152      20.442  67.287 -12.276  1.00 14.71           C  
ANISOU 1182  CH2 TRP A 152     1916   2028   1645    119    -57     81       C  
ATOM   1183  N   ARG A 153      26.869  72.312 -14.772  1.00 16.62           N  
ANISOU 1183  N   ARG A 153     2083   2357   1873    123    164    258       N  
ATOM   1184  CA  ARG A 153      27.386  73.288 -15.749  1.00 17.80           C  
ANISOU 1184  CA  ARG A 153     2235   2526   2000    115    201    304       C  
ATOM   1185  C   ARG A 153      27.252  72.837 -17.198  1.00 18.96           C  
ANISOU 1185  C   ARG A 153     2405   2715   2084    151    210    309       C  
ATOM   1186  O   ARG A 153      27.149  73.687 -18.117  1.00 19.14           O  
ANISOU 1186  O   ARG A 153     2445   2746   2079    151    229    351       O  
ATOM   1187  CB  ARG A 153      28.864  73.552 -15.441  1.00 18.73           C  
ANISOU 1187  CB  ARG A 153     2313   2665   2138     90    237    315       C  
ATOM   1188  CG  ARG A 153      29.478  74.660 -16.284  1.00 24.09           C  
ANISOU 1188  CG  ARG A 153     2990   3360   2802     68    279    367       C  
ATOM   1189  CD  ARG A 153      28.853  75.991 -16.016  1.00 30.56           C  
ANISOU 1189  CD  ARG A 153     3833   4126   3649     37    274    402       C  
ATOM   1190  NE  ARG A 153      29.306  76.945 -17.030  1.00 37.28           N  
ANISOU 1190  NE  ARG A 153     4697   4991   4477     20    313    456       N  
ATOM   1191  CZ  ARG A 153      28.736  77.109 -18.225  1.00 39.77           C  
ANISOU 1191  CZ  ARG A 153     5048   5320   4742     50    319    484       C  
ATOM   1192  NH1 ARG A 153      27.644  76.409 -18.579  1.00 37.41           N  
ANISOU 1192  NH1 ARG A 153     4774   5026   4413     95    284    459       N  
ATOM   1193  NH2 ARG A 153      29.259  78.000 -19.069  1.00 42.13           N  
ANISOU 1193  NH2 ARG A 153     5357   5629   5020     31    360    538       N  
ATOM   1194  N   SER A 154      27.261  71.536 -17.418  1.00 18.02           N  
ANISOU 1194  N   SER A 154     2291   2616   1937    182    196    268       N  
ATOM   1195  CA  SER A 154      27.364  70.940 -18.777  1.00 19.37           C  
ANISOU 1195  CA  SER A 154     2483   2832   2042    220    208    263       C  
ATOM   1196  C   SER A 154      26.330  69.853 -19.031  1.00 17.93           C  
ANISOU 1196  C   SER A 154     2334   2644   1832    246    164    219       C  
ATOM   1197  O   SER A 154      26.515  68.987 -19.896  1.00 19.75           O  
ANISOU 1197  O   SER A 154     2585   2906   2013    280    167    195       O  
ATOM   1198  CB  SER A 154      28.790  70.394 -18.991  1.00 21.10           C  
ANISOU 1198  CB  SER A 154     2676   3095   2245    237    246    254       C  
ATOM   1199  OG  SER A 154      29.746  71.441 -18.822  1.00 25.07           O  
ANISOU 1199  OG  SER A 154     3142   3609   2771    204    286    297       O  
ATOM   1200  N   ARG A 155      25.224  69.907 -18.291  1.00 17.37           N  
ANISOU 1200  N   ARG A 155     2270   2535   1794    228    125    208       N  
ATOM   1201  CA  ARG A 155      24.152  68.941 -18.400  1.00 15.94           C  
ANISOU 1201  CA  ARG A 155     2115   2346   1595    238     82    169       C  
ATOM   1202  C   ARG A 155      22.822  69.661 -18.083  1.00 16.01           C  
ANISOU 1202  C   ARG A 155     2125   2335   1623    220     50    185       C  
ATOM   1203  O   ARG A 155      22.773  70.466 -17.172  1.00 16.95           O  
ANISOU 1203  O   ARG A 155     2224   2426   1788    198     55    206       O  
ATOM   1204  CB  ARG A 155      24.365  67.739 -17.434  1.00 16.34           C  
ANISOU 1204  CB  ARG A 155     2163   2371   1672    235     65    123       C  
ATOM   1205  CG  ARG A 155      24.432  68.079 -15.962  1.00 15.43           C  
ANISOU 1205  CG  ARG A 155     2021   2220   1620    206     62    128       C  
ATOM   1206  CD  ARG A 155      25.077  66.950 -15.154  1.00 16.63           C  
ANISOU 1206  CD  ARG A 155     2171   2358   1790    213     60     92       C  
ATOM   1207  NE  ARG A 155      25.250  67.234 -13.729  1.00 14.71           N  
ANISOU 1207  NE  ARG A 155     1901   2086   1601    189     57     96       N  
ATOM   1208  CZ  ARG A 155      24.493  66.729 -12.744  1.00 14.55           C  
ANISOU 1208  CZ  ARG A 155     1886   2032   1608    173     28     77       C  
ATOM   1209  NH1 ARG A 155      23.469  65.928 -13.005  1.00 16.86           N  
ANISOU 1209  NH1 ARG A 155     2208   2314   1883    171     -2     53       N  
ATOM   1210  NH2 ARG A 155      24.808  67.016 -11.497  1.00 14.94           N  
ANISOU 1210  NH2 ARG A 155     1912   2063   1700    156     30     81       N  
ATOM   1211  N   ARG A 156      21.783  69.368 -18.847  1.00 16.23           N  
ANISOU 1211  N   ARG A 156     2174   2380   1612    232     19    174       N  
ATOM   1212  CA  ARG A 156      20.474  70.005 -18.697  1.00 16.52           C  
ANISOU 1212  CA  ARG A 156     2207   2411   1657    224    -11    189       C  
ATOM   1213  C   ARG A 156      20.021  69.915 -17.241  1.00 15.81           C  
ANISOU 1213  C   ARG A 156     2095   2285   1627    197    -28    175       C  
ATOM   1214  O   ARG A 156      20.079  68.834 -16.596  1.00 16.21           O  
ANISOU 1214  O   ARG A 156     2145   2319   1693    183    -42    137       O  
ATOM   1215  CB  ARG A 156      19.439  69.330 -19.595  1.00 17.99           C  
ANISOU 1215  CB  ARG A 156     2412   2629   1793    237    -51    164       C  
ATOM   1216  CG  ARG A 156      17.993  69.771 -19.341  1.00 18.26           C  
ANISOU 1216  CG  ARG A 156     2433   2667   1837    230    -89    172       C  
ATOM   1217  CD  ARG A 156      17.016  68.907 -20.192  1.00 21.83           C  
ANISOU 1217  CD  ARG A 156     2898   3155   2238    234   -134    138       C  
ATOM   1218  NE  ARG A 156      17.127  69.253 -21.565  1.00 22.85           N  
ANISOU 1218  NE  ARG A 156     3049   3325   2305    267   -128    156       N  
ATOM   1219  CZ  ARG A 156      17.159  68.413 -22.611  1.00 22.07           C  
ANISOU 1219  CZ  ARG A 156     2978   3257   2147    281   -143    124       C  
ATOM   1220  NH1 ARG A 156      17.229  67.083 -22.465  1.00 23.35           N  
ANISOU 1220  NH1 ARG A 156     3157   3407   2308    263   -162     69       N  
ATOM   1221  NH2 ARG A 156      17.194  68.920 -23.802  1.00 20.89           N  
ANISOU 1221  NH2 ARG A 156     2847   3149   1939    314   -137    149       N  
ATOM   1222  N   TYR A 157      19.525  71.030 -16.718  1.00 15.09           N  
ANISOU 1222  N   TYR A 157     1990   2177   1564    191    -28    207       N  
ATOM   1223  CA  TYR A 157      19.055  71.093 -15.350  1.00 14.41           C  
ANISOU 1223  CA  TYR A 157     1883   2062   1529    169    -42    197       C  
ATOM   1224  C   TYR A 157      17.693  70.433 -15.170  1.00 14.68           C  
ANISOU 1224  C   TYR A 157     1910   2108   1558    163    -85    171       C  
ATOM   1225  O   TYR A 157      16.808  70.547 -16.016  1.00 15.66           O  
ANISOU 1225  O   TYR A 157     2039   2265   1647    177   -108    177       O  
ATOM   1226  CB  TYR A 157      18.941  72.553 -14.954  1.00 14.57           C  
ANISOU 1226  CB  TYR A 157     1898   2061   1576    172    -27    237       C  
ATOM   1227  CG  TYR A 157      18.627  72.863 -13.495  1.00 13.44           C  
ANISOU 1227  CG  TYR A 157     1735   1885   1484    155    -33    231       C  
ATOM   1228  CD1 TYR A 157      19.586  72.664 -12.488  1.00 14.12           C  
ANISOU 1228  CD1 TYR A 157     1811   1946   1608    133    -16    218       C  
ATOM   1229  CD2 TYR A 157      17.403  73.430 -13.144  1.00 15.70           C  
ANISOU 1229  CD2 TYR A 157     2013   2172   1778    165    -55    240       C  
ATOM   1230  CE1 TYR A 157      19.291  73.056 -11.183  1.00 14.66           C  
ANISOU 1230  CE1 TYR A 157     1866   1987   1718    121    -21    213       C  
ATOM   1231  CE2 TYR A 157      17.121  73.813 -11.863  1.00 15.26           C  
ANISOU 1231  CE2 TYR A 157     1942   2090   1764    156    -57    236       C  
ATOM   1232  CZ  TYR A 157      18.049  73.599 -10.904  1.00 15.36           C  
ANISOU 1232  CZ  TYR A 157     1950   2076   1810    133    -41    221       C  
ATOM   1233  OH  TYR A 157      17.700  74.061  -9.604  1.00 17.89           O  
ANISOU 1233  OH  TYR A 157     2257   2372   2167    127    -44    217       O  
ATOM   1234  N   SER A 158      17.497  69.807 -14.002  1.00 14.88           N  
ANISOU 1234  N   SER A 158     1921   2112   1619    139    -96    147       N  
ATOM   1235  CA  SER A 158      16.223  69.322 -13.499  1.00 15.69           C  
ANISOU 1235  CA  SER A 158     2008   2223   1729    122   -130    129       C  
ATOM   1236  C   SER A 158      16.029  69.911 -12.100  1.00 15.06           C  
ANISOU 1236  C   SER A 158     1905   2119   1698    111   -123    139       C  
ATOM   1237  O   SER A 158      16.816  69.557 -11.184  1.00 15.16           O  
ANISOU 1237  O   SER A 158     1917   2101   1739     97   -108    128       O  
ATOM   1238  CB  SER A 158      16.248  67.812 -13.426  1.00 16.01           C  
ANISOU 1238  CB  SER A 158     2062   2257   1763     99   -148     88       C  
ATOM   1239  OG  SER A 158      15.142  67.353 -12.604  1.00 17.36           O  
ANISOU 1239  OG  SER A 158     2213   2430   1953     70   -174     74       O  
ATOM   1240  N   PRO A 159      15.017  70.769 -11.875  1.00 14.38           N  
ANISOU 1240  N   PRO A 159     1799   2046   1618    123   -134    158       N  
ATOM   1241  CA  PRO A 159      14.810  71.294 -10.527  1.00 14.14           C  
ANISOU 1241  CA  PRO A 159     1750   1995   1628    117   -127    163       C  
ATOM   1242  C   PRO A 159      14.730  70.186  -9.447  1.00 13.79           C  
ANISOU 1242  C   PRO A 159     1694   1938   1605     85   -135    134       C  
ATOM   1243  O   PRO A 159      15.336  70.311  -8.378  1.00 13.58           O  
ANISOU 1243  O   PRO A 159     1665   1882   1610     77   -119    132       O  
ATOM   1244  CB  PRO A 159      13.527  72.101 -10.633  1.00 15.19           C  
ANISOU 1244  CB  PRO A 159     1863   2156   1752    141   -144    182       C  
ATOM   1245  CG  PRO A 159      13.550  72.572 -12.076  1.00 16.14           C  
ANISOU 1245  CG  PRO A 159     2002   2298   1833    168   -146    202       C  
ATOM   1246  CD  PRO A 159      14.124  71.441 -12.858  1.00 15.31           C  
ANISOU 1246  CD  PRO A 159     1914   2201   1702    150   -151    179       C  
ATOM   1247  N   TRP A 160      13.959  69.141  -9.708  1.00 13.83           N  
ANISOU 1247  N   TRP A 160     1693   1966   1593     64   -161    114       N  
ATOM   1248  CA  TRP A 160      13.785  68.077  -8.711  1.00 13.32           C  
ANISOU 1248  CA  TRP A 160     1624   1887   1548     30   -169     91       C  
ATOM   1249  C   TRP A 160      15.000  67.191  -8.611  1.00 13.35           C  
ANISOU 1249  C   TRP A 160     1659   1857   1556     21   -156     73       C  
ATOM   1250  O   TRP A 160      15.379  66.807  -7.476  1.00 13.56           O  
ANISOU 1250  O   TRP A 160     1685   1857   1609      8   -147     67       O  
ATOM   1251  CB  TRP A 160      12.490  67.262  -8.947  1.00 13.53           C  
ANISOU 1251  CB  TRP A 160     1634   1948   1558      0   -201     76       C  
ATOM   1252  CG  TRP A 160      11.295  67.992  -8.452  1.00 14.54           C  
ANISOU 1252  CG  TRP A 160     1718   2112   1693      6   -210     93       C  
ATOM   1253  CD1 TRP A 160      10.365  68.692  -9.195  1.00 16.98           C  
ANISOU 1253  CD1 TRP A 160     2002   2468   1979     29   -227    106       C  
ATOM   1254  CD2 TRP A 160      10.959  68.205  -7.084  1.00 14.73           C  
ANISOU 1254  CD2 TRP A 160     1717   2130   1746      0   -199     99       C  
ATOM   1255  NE1 TRP A 160       9.465  69.277  -8.350  1.00 19.01           N  
ANISOU 1255  NE1 TRP A 160     2220   2750   2251     38   -227    119       N  
ATOM   1256  CE2 TRP A 160       9.797  68.984  -7.050  1.00 16.86           C  
ANISOU 1256  CE2 TRP A 160     1947   2447   2010     19   -209    114       C  
ATOM   1257  CE3 TRP A 160      11.519  67.760  -5.874  1.00 16.10           C  
ANISOU 1257  CE3 TRP A 160     1900   2269   1947    -17   -182     92       C  
ATOM   1258  CZ2 TRP A 160       9.196  69.371  -5.821  1.00 16.71           C  
ANISOU 1258  CZ2 TRP A 160     1896   2439   2012     23   -199    122       C  
ATOM   1259  CZ3 TRP A 160      10.908  68.139  -4.663  1.00 16.37           C  
ANISOU 1259  CZ3 TRP A 160     1904   2314   1999    -17   -174    101       C  
ATOM   1260  CH2 TRP A 160       9.750  68.929  -4.677  1.00 17.81           C  
ANISOU 1260  CH2 TRP A 160     2047   2544   2175      2   -182    115       C  
ATOM   1261  N   LEU A 161      15.653  66.812  -9.710  1.00 13.37           N  
ANISOU 1261  N   LEU A 161     1689   1860   1532     32   -154     64       N  
ATOM   1262  CA  LEU A 161      16.850  65.974  -9.580  1.00 13.26           C  
ANISOU 1262  CA  LEU A 161     1701   1815   1519     34   -140     47       C  
ATOM   1263  C   LEU A 161      18.042  66.741  -8.965  1.00 12.21           C  
ANISOU 1263  C   LEU A 161     1560   1665   1411     51   -108     63       C  
ATOM   1264  O   LEU A 161      18.906  66.146  -8.318  1.00 13.65           O  
ANISOU 1264  O   LEU A 161     1752   1826   1607     52    -98     52       O  
ATOM   1265  CB  LEU A 161      17.223  65.222 -10.875  1.00 14.24           C  
ANISOU 1265  CB  LEU A 161     1859   1947   1604     45   -146     27       C  
ATOM   1266  CG  LEU A 161      16.279  64.095 -11.276  1.00 16.63           C  
ANISOU 1266  CG  LEU A 161     2179   2252   1885     18   -180      0       C  
ATOM   1267  CD1 LEU A 161      16.643  63.600 -12.710  1.00 22.20           C  
ANISOU 1267  CD1 LEU A 161     2920   2970   2543     37   -186    -20       C  
ATOM   1268  CD2 LEU A 161      16.326  62.931 -10.277  1.00 20.50           C  
ANISOU 1268  CD2 LEU A 161     2687   2703   2396     -9   -186    -21       C  
ATOM   1269  N   ALA A 162      18.074  68.056  -9.135  1.00 12.93           N  
ANISOU 1269  N   ALA A 162     1636   1766   1508     65    -95     90       N  
ATOM   1270  CA  ALA A 162      19.068  68.885  -8.434  1.00 12.27           C  
ANISOU 1270  CA  ALA A 162     1544   1666   1453     70    -69    104       C  
ATOM   1271  C   ALA A 162      18.791  68.910  -6.925  1.00 12.00           C  
ANISOU 1271  C   ALA A 162     1493   1613   1451     56    -73    100       C  
ATOM   1272  O   ALA A 162      19.728  68.816  -6.108  1.00 12.35           O  
ANISOU 1272  O   ALA A 162     1535   1641   1515     54    -61     94       O  
ATOM   1273  CB  ALA A 162      19.136  70.313  -9.041  1.00 13.64           C  
ANISOU 1273  CB  ALA A 162     1714   1846   1623     84    -54    136       C  
ATOM   1274  N   TYR A 163      17.516  69.007  -6.537  1.00 12.09           N  
ANISOU 1274  N   TYR A 163     1492   1634   1466     49    -91    101       N  
ATOM   1275  CA  TYR A 163      17.127  68.795  -5.131  1.00 11.49           C  
ANISOU 1275  CA  TYR A 163     1403   1548   1413     35    -95     94       C  
ATOM   1276  C   TYR A 163      17.617  67.427  -4.642  1.00 11.60           C  
ANISOU 1276  C   TYR A 163     1432   1546   1428     20    -98     74       C  
ATOM   1277  O   TYR A 163      18.276  67.310  -3.605  1.00 12.09           O  
ANISOU 1277  O   TYR A 163     1493   1591   1508     19    -89     71       O  
ATOM   1278  CB  TYR A 163      15.623  68.940  -4.931  1.00 11.60           C  
ANISOU 1278  CB  TYR A 163     1396   1586   1424     29   -112     99       C  
ATOM   1279  CG  TYR A 163      15.215  68.978  -3.463  1.00 11.81           C  
ANISOU 1279  CG  TYR A 163     1406   1608   1471     20   -110     97       C  
ATOM   1280  CD1 TYR A 163      15.745  69.931  -2.584  1.00 12.09           C  
ANISOU 1280  CD1 TYR A 163     1438   1626   1527     35    -94    103       C  
ATOM   1281  CD2 TYR A 163      14.358  68.034  -2.944  1.00 12.91           C  
ANISOU 1281  CD2 TYR A 163     1535   1760   1608     -4   -122     90       C  
ATOM   1282  CE1 TYR A 163      15.389  69.954  -1.251  1.00 12.30           C  
ANISOU 1282  CE1 TYR A 163     1453   1653   1568     31    -91    100       C  
ATOM   1283  CE2 TYR A 163      14.001  68.050  -1.629  1.00 13.07           C  
ANISOU 1283  CE2 TYR A 163     1540   1781   1642    -10   -117     91       C  
ATOM   1284  CZ  TYR A 163      14.506  69.017  -0.787  1.00 13.22           C  
ANISOU 1284  CZ  TYR A 163     1557   1787   1678     10   -101     95       C  
ATOM   1285  OH  TYR A 163      14.152  68.982   0.570  1.00 14.38           O  
ANISOU 1285  OH  TYR A 163     1691   1937   1832      6    -96     95       O  
ATOM   1286  N   SER A 164      17.286  66.394  -5.383  1.00 11.89           N  
ANISOU 1286  N   SER A 164     1486   1586   1444      9   -113     61       N  
ATOM   1287  CA  SER A 164      17.624  65.033  -4.999  1.00 11.98           C  
ANISOU 1287  CA  SER A 164     1522   1574   1454     -2   -119     42       C  
ATOM   1288  C   SER A 164      19.117  64.825  -4.855  1.00 11.89           C  
ANISOU 1288  C   SER A 164     1525   1546   1447     20   -101     37       C  
ATOM   1289  O   SER A 164      19.587  64.145  -3.913  1.00 12.00           O  
ANISOU 1289  O   SER A 164     1548   1538   1471     20    -99     30       O  
ATOM   1290  CB  SER A 164      17.060  64.035  -6.004  1.00 12.70           C  
ANISOU 1290  CB  SER A 164     1638   1668   1519    -17   -139     24       C  
ATOM   1291  OG  SER A 164      15.632  64.042  -6.031  1.00 13.96           O  
ANISOU 1291  OG  SER A 164     1778   1850   1674    -45   -159     27       O  
ATOM   1292  N   GLN A 165      19.933  65.416  -5.752  1.00 11.72           N  
ANISOU 1292  N   GLN A 165     1501   1536   1414     42    -86     42       N  
ATOM   1293  CA  GLN A 165      21.375  65.289  -5.610  1.00 12.26           C  
ANISOU 1293  CA  GLN A 165     1571   1599   1485     64    -68     38       C  
ATOM   1294  C   GLN A 165      21.813  65.865  -4.266  1.00 10.74           C  
ANISOU 1294  C   GLN A 165     1356   1401   1323     60    -60     46       C  
ATOM   1295  O   GLN A 165      22.657  65.288  -3.572  1.00 12.14           O  
ANISOU 1295  O   GLN A 165     1536   1570   1506     71    -56     38       O  
ATOM   1296  CB  GLN A 165      22.155  65.977  -6.768  1.00 12.92           C  
ANISOU 1296  CB  GLN A 165     1648   1705   1553     82    -48     48       C  
ATOM   1297  CG  GLN A 165      23.652  65.723  -6.684  1.00 13.05           C  
ANISOU 1297  CG  GLN A 165     1659   1728   1569    105    -28     44       C  
ATOM   1298  CD  GLN A 165      24.503  66.468  -7.719  1.00 13.52           C  
ANISOU 1298  CD  GLN A 165     1705   1816   1614    118     -3     58       C  
ATOM   1299  OE1 GLN A 165      25.329  65.832  -8.401  1.00 14.52           O  
ANISOU 1299  OE1 GLN A 165     1840   1957   1717    144      8     48       O  
ATOM   1300  NE2 GLN A 165      24.432  67.798  -7.727  1.00 12.80           N  
ANISOU 1300  NE2 GLN A 165     1594   1730   1538    102      6     83       N  
ATOM   1301  N   SER A 166      21.265  67.030  -3.922  1.00 10.76           N  
ANISOU 1301  N   SER A 166     1338   1408   1341     49    -58     61       N  
ATOM   1302  CA  SER A 166      21.643  67.695  -2.676  1.00 10.90           C  
ANISOU 1302  CA  SER A 166     1337   1420   1384     46    -53     65       C  
ATOM   1303  C   SER A 166      21.230  66.922  -1.425  1.00 10.58           C  
ANISOU 1303  C   SER A 166     1300   1367   1349     38    -64     56       C  
ATOM   1304  O   SER A 166      21.952  66.904  -0.432  1.00 11.46           O  
ANISOU 1304  O   SER A 166     1405   1475   1471     43    -61     52       O  
ATOM   1305  CB  SER A 166      21.124  69.150  -2.641  1.00 12.33           C  
ANISOU 1305  CB  SER A 166     1504   1602   1576     40    -48     81       C  
ATOM   1306  OG  SER A 166      19.756  69.258  -2.312  1.00 12.78           O  
ANISOU 1306  OG  SER A 166     1559   1662   1634     35    -61     84       O  
ATOM   1307  N   LYS A 167      20.067  66.296  -1.505  1.00 11.19           N  
ANISOU 1307  N   LYS A 167     1388   1443   1418     25    -78     55       N  
ATOM   1308  CA  LYS A 167      19.512  65.508  -0.371  1.00 11.62           C  
ANISOU 1308  CA  LYS A 167     1450   1488   1477     11    -86     52       C  
ATOM   1309  C   LYS A 167      20.238  64.188  -0.171  1.00 11.29           C  
ANISOU 1309  C   LYS A 167     1437   1426   1427     19    -89     42       C  
ATOM   1310  O   LYS A 167      20.455  63.716   0.949  1.00 11.70           O  
ANISOU 1310  O   LYS A 167     1494   1465   1483     20    -89     43       O  
ATOM   1311  CB  LYS A 167      18.005  65.391  -0.482  1.00 11.96           C  
ANISOU 1311  CB  LYS A 167     1486   1542   1514    -11    -97     57       C  
ATOM   1312  CG  LYS A 167      17.280  66.729  -0.410  1.00 11.67           C  
ANISOU 1312  CG  LYS A 167     1420   1527   1485     -6    -94     69       C  
ATOM   1313  CD  LYS A 167      17.329  67.328   0.983  1.00 12.50           C  
ANISOU 1313  CD  LYS A 167     1511   1631   1604     -1    -86     72       C  
ATOM   1314  CE  LYS A 167      17.965  68.689   1.063  1.00 13.11           C  
ANISOU 1314  CE  LYS A 167     1581   1705   1694     17    -76     74       C  
ATOM   1315  NZ  LYS A 167      18.058  69.115   2.501  1.00 13.60           N  
ANISOU 1315  NZ  LYS A 167     1635   1765   1766     22    -72     70       N  
ATOM   1316  N   LEU A 168      20.670  63.572  -1.267  1.00 11.47           N  
ANISOU 1316  N   LEU A 168     1480   1441   1434     29    -90     32       N  
ATOM   1317  CA  LEU A 168      21.571  62.440  -1.222  1.00 12.28           C  
ANISOU 1317  CA  LEU A 168     1614   1524   1527     50    -90     21       C  
ATOM   1318  C   LEU A 168      22.929  62.856  -0.639  1.00 11.48           C  
ANISOU 1318  C   LEU A 168     1492   1434   1433     79    -77     22       C  
ATOM   1319  O   LEU A 168      23.476  62.170   0.231  1.00 11.66           O  
ANISOU 1319  O   LEU A 168     1528   1445   1456     96    -79     20       O  
ATOM   1320  CB  LEU A 168      21.705  61.840  -2.630  1.00 12.42           C  
ANISOU 1320  CB  LEU A 168     1659   1538   1522     60    -92      6       C  
ATOM   1321  CG  LEU A 168      22.738  60.717  -2.739  1.00 12.05           C  
ANISOU 1321  CG  LEU A 168     1647   1470   1461     95    -90     -7       C  
ATOM   1322  CD1 LEU A 168      22.470  59.499  -1.811  1.00 14.44           C  
ANISOU 1322  CD1 LEU A 168     1989   1732   1764     89   -101    -10       C  
ATOM   1323  CD2 LEU A 168      22.877  60.248  -4.177  1.00 14.44           C  
ANISOU 1323  CD2 LEU A 168     1976   1772   1736    110    -90    -25       C  
ATOM   1324  N   ALA A 169      23.446  64.001  -1.075  1.00 10.84           N  
ANISOU 1324  N   ALA A 169     1380   1378   1359     84    -65     27       N  
ATOM   1325  CA  ALA A 169      24.683  64.538  -0.517  1.00 11.25           C  
ANISOU 1325  CA  ALA A 169     1404   1447   1421    100    -55     28       C  
ATOM   1326  C   ALA A 169      24.617  64.716   0.997  1.00 11.35           C  
ANISOU 1326  C   ALA A 169     1406   1456   1447     94    -62     30       C  
ATOM   1327  O   ALA A 169      25.555  64.384   1.718  1.00 11.98           O  
ANISOU 1327  O   ALA A 169     1480   1545   1527    114    -64     26       O  
ATOM   1328  CB  ALA A 169      25.089  65.841  -1.210  1.00 11.61           C  
ANISOU 1328  CB  ALA A 169     1420   1515   1474     92    -41     37       C  
ATOM   1329  N   ASN A 170      23.455  65.153   1.510  1.00 10.79           N  
ANISOU 1329  N   ASN A 170     1335   1378   1385     70    -68     37       N  
ATOM   1330  CA  ASN A 170      23.282  65.332   2.953  1.00 11.51           C  
ANISOU 1330  CA  ASN A 170     1419   1470   1484     66    -74     38       C  
ATOM   1331  C   ASN A 170      23.496  64.022   3.711  1.00 11.02           C  
ANISOU 1331  C   ASN A 170     1382   1393   1409     80    -81     37       C  
ATOM   1332  O   ASN A 170      24.057  64.002   4.817  1.00 11.87           O  
ANISOU 1332  O   ASN A 170     1484   1509   1517     93    -85     36       O  
ATOM   1333  CB  ASN A 170      21.866  65.814   3.300  1.00 11.41           C  
ANISOU 1333  CB  ASN A 170     1403   1454   1475     44    -76     46       C  
ATOM   1334  CG  ASN A 170      21.525  67.240   2.881  1.00 12.31           C  
ANISOU 1334  CG  ASN A 170     1497   1578   1600     36    -70     49       C  
ATOM   1335  OD1 ASN A 170      20.344  67.503   2.567  1.00 12.99           O  
ANISOU 1335  OD1 ASN A 170     1582   1667   1685     26    -72     56       O  
ATOM   1336  ND2 ASN A 170      22.469  68.189   2.959  1.00 12.21           N  
ANISOU 1336  ND2 ASN A 170     1468   1569   1598     40    -64     45       N  
ATOM   1337  N   LEU A 171      23.044  62.909   3.137  1.00 11.11           N  
ANISOU 1337  N   LEU A 171     1428   1383   1410     78    -85     37       N  
ATOM   1338  CA  LEU A 171      23.215  61.591   3.753  1.00 11.10           C  
ANISOU 1338  CA  LEU A 171     1463   1357   1396     92    -91     39       C  
ATOM   1339  C   LEU A 171      24.650  61.057   3.641  1.00 11.78           C  
ANISOU 1339  C   LEU A 171     1555   1446   1472    137    -90     31       C  
ATOM   1340  O   LEU A 171      25.205  60.522   4.607  1.00 12.68           O  
ANISOU 1340  O   LEU A 171     1680   1557   1580    161    -95     35       O  
ATOM   1341  CB  LEU A 171      22.189  60.579   3.187  1.00 12.14           C  
ANISOU 1341  CB  LEU A 171     1634   1457   1519     67    -97     41       C  
ATOM   1342  CG  LEU A 171      20.776  60.868   3.655  1.00 12.69           C  
ANISOU 1342  CG  LEU A 171     1693   1531   1595     25    -99     52       C  
ATOM   1343  CD1 LEU A 171      19.771  59.978   2.924  1.00 14.69           C  
ANISOU 1343  CD1 LEU A 171     1977   1762   1842     -8   -107     51       C  
ATOM   1344  CD2 LEU A 171      20.614  60.540   5.163  1.00 18.55           C  
ANISOU 1344  CD2 LEU A 171     2442   2269   2334     23    -98     67       C  
ATOM   1345  N   LEU A 172      25.233  61.185   2.451  1.00 11.76           N  
ANISOU 1345  N   LEU A 172     1545   1454   1466    151    -83     21       N  
ATOM   1346  CA  LEU A 172      26.623  60.771   2.248  1.00 11.83           C  
ANISOU 1346  CA  LEU A 172     1551   1478   1465    198    -79     13       C  
ATOM   1347  C   LEU A 172      27.557  61.591   3.133  1.00 12.34           C  
ANISOU 1347  C   LEU A 172     1567   1580   1538    209    -78     15       C  
ATOM   1348  O   LEU A 172      28.575  61.081   3.631  1.00 13.15           O  
ANISOU 1348  O   LEU A 172     1666   1698   1631    249    -81     13       O  
ATOM   1349  CB  LEU A 172      26.972  60.916   0.780  1.00 12.32           C  
ANISOU 1349  CB  LEU A 172     1608   1553   1519    208    -67      4       C  
ATOM   1350  CG  LEU A 172      26.287  59.947  -0.183  1.00 12.37           C  
ANISOU 1350  CG  LEU A 172     1666   1524   1509    206    -71     -4       C  
ATOM   1351  CD1 LEU A 172      26.529  60.401  -1.630  1.00 14.60           C  
ANISOU 1351  CD1 LEU A 172     1935   1829   1780    211    -59    -11       C  
ATOM   1352  CD2 LEU A 172      26.764  58.494   0.012  1.00 14.09           C  
ANISOU 1352  CD2 LEU A 172     1935   1708   1708    248    -77    -13       C  
ATOM   1353  N   PHE A 173      27.235  62.868   3.311  1.00 11.50           N  
ANISOU 1353  N   PHE A 173     1427   1491   1450    175    -75     18       N  
ATOM   1354  CA  PHE A 173      27.947  63.773   4.254  1.00 11.85           C  
ANISOU 1354  CA  PHE A 173     1430   1567   1505    172    -79     16       C  
ATOM   1355  C   PHE A 173      27.919  63.199   5.659  1.00 12.11           C  
ANISOU 1355  C   PHE A 173     1477   1594   1529    187    -93     19       C  
ATOM   1356  O   PHE A 173      28.938  63.098   6.364  1.00 12.97           O  
ANISOU 1356  O   PHE A 173     1565   1730   1631    214   -101     14       O  
ATOM   1357  CB  PHE A 173      27.297  65.152   4.221  1.00 11.56           C  
ANISOU 1357  CB  PHE A 173     1373   1532   1487    132    -75     18       C  
ATOM   1358  CG  PHE A 173      27.788  66.073   5.282  1.00 11.88           C  
ANISOU 1358  CG  PHE A 173     1383   1592   1537    122    -82     12       C  
ATOM   1359  CD1 PHE A 173      29.042  66.608   5.268  1.00 12.55           C  
ANISOU 1359  CD1 PHE A 173     1430   1710   1628    124    -81      4       C  
ATOM   1360  CD2 PHE A 173      26.915  66.447   6.278  1.00 13.83           C  
ANISOU 1360  CD2 PHE A 173     1640   1827   1787    107    -90     12       C  
ATOM   1361  CE1 PHE A 173      29.455  67.487   6.266  1.00 13.32           C  
ANISOU 1361  CE1 PHE A 173     1502   1824   1734    108    -92     -5       C  
ATOM   1362  CE2 PHE A 173      27.298  67.355   7.238  1.00 14.94           C  
ANISOU 1362  CE2 PHE A 173     1759   1983   1934     97    -98      1       C  
ATOM   1363  CZ  PHE A 173      28.591  67.848   7.239  1.00 15.24           C  
ANISOU 1363  CZ  PHE A 173     1761   2050   1977     96   -101     -8       C  
ATOM   1364  N   THR A 174      26.712  62.836   6.104  1.00 11.47           N  
ANISOU 1364  N   THR A 174     1428   1483   1446    169    -96     28       N  
ATOM   1365  CA  THR A 174      26.521  62.289   7.446  1.00 12.14           C  
ANISOU 1365  CA  THR A 174     1531   1561   1518    180   -106     35       C  
ATOM   1366  C   THR A 174      27.312  60.994   7.671  1.00 12.96           C  
ANISOU 1366  C   THR A 174     1664   1656   1602    226   -112     39       C  
ATOM   1367  O   THR A 174      28.003  60.851   8.696  1.00 12.91           O  
ANISOU 1367  O   THR A 174     1649   1670   1584    254   -123     41       O  
ATOM   1368  CB  THR A 174      25.050  62.051   7.688  1.00 11.81           C  
ANISOU 1368  CB  THR A 174     1517   1493   1476    148   -103     48       C  
ATOM   1369  OG1 THR A 174      24.315  63.290   7.613  1.00 12.49           O  
ANISOU 1369  OG1 THR A 174     1575   1592   1577    116    -98     45       O  
ATOM   1370  CG2 THR A 174      24.767  61.381   9.086  1.00 14.39           C  
ANISOU 1370  CG2 THR A 174     1868   1812   1786    156   -109     62       C  
ATOM   1371  N   SER A 175      27.273  60.078   6.714  1.00 12.71           N  
ANISOU 1371  N   SER A 175     1666   1596   1564    239   -108     39       N  
ATOM   1372  CA ASER A 175      28.009  58.803   6.833  0.50 12.93           C  
ANISOU 1372  CA ASER A 175     1732   1608   1573    291   -113     42       C  
ATOM   1373  CA BSER A 175      27.994  58.813   6.900  0.50 13.57           C  
ANISOU 1373  CA BSER A 175     1812   1688   1653    290   -113     42       C  
ATOM   1374  C   SER A 175      29.510  59.016   6.893  1.00 13.40           C  
ANISOU 1374  C   SER A 175     1750   1715   1626    339   -116     32       C  
ATOM   1375  O   SER A 175      30.199  58.431   7.726  1.00 13.98           O  
ANISOU 1375  O   SER A 175     1831   1798   1682    383   -126     38       O  
ATOM   1376  CB ASER A 175      27.677  57.894   5.658  0.50 13.91           C  
ANISOU 1376  CB ASER A 175     1903   1690   1691    294   -108     36       C  
ATOM   1377  CB BSER A 175      27.541  57.771   5.885  0.50 14.48           C  
ANISOU 1377  CB BSER A 175     1982   1755   1762    292   -109     40       C  
ATOM   1378  OG ASER A 175      26.319  57.496   5.689  0.50 13.67           O  
ANISOU 1378  OG ASER A 175     1912   1616   1664    249   -109     46       O  
ATOM   1379  OG BSER A 175      27.820  58.174   4.563  0.50 18.29           O  
ANISOU 1379  OG BSER A 175     2445   2253   2250    292   -100     24       O  
ATOM   1380  N   GLU A 176      30.037  59.853   5.990  1.00 13.20           N  
ANISOU 1380  N   GLU A 176     1678   1723   1611    330   -106     20       N  
ATOM   1381  CA  GLU A 176      31.479  60.072   5.951  1.00 13.72           C  
ANISOU 1381  CA  GLU A 176     1695   1844   1672    370   -106     11       C  
ATOM   1382  C   GLU A 176      31.940  60.883   7.154  1.00 13.50           C  
ANISOU 1382  C   GLU A 176     1622   1858   1649    360   -120     10       C  
ATOM   1383  O   GLU A 176      32.993  60.605   7.710  1.00 14.70           O  
ANISOU 1383  O   GLU A 176     1749   2048   1786    403   -131      8       O  
ATOM   1384  CB  GLU A 176      31.917  60.687   4.633  1.00 15.01           C  
ANISOU 1384  CB  GLU A 176     1824   2033   1843    360    -88      2       C  
ATOM   1385  CG  GLU A 176      33.393  61.020   4.502  1.00 14.79           C  
ANISOU 1385  CG  GLU A 176     1734   2073   1812    391    -84     -4       C  
ATOM   1386  CD  GLU A 176      34.343  59.865   4.457  1.00 16.47           C  
ANISOU 1386  CD  GLU A 176     1956   2301   1998    467    -86     -6       C  
ATOM   1387  OE1 GLU A 176      33.908  58.705   4.439  1.00 19.94           O  
ANISOU 1387  OE1 GLU A 176     2462   2691   2422    501    -90     -4       O  
ATOM   1388  OE2 GLU A 176      35.572  60.175   4.410  1.00 20.58           O  
ANISOU 1388  OE2 GLU A 176     2414   2889   2514    493    -83    -11       O  
ATOM   1389  N   LEU A 177      31.146  61.849   7.582  1.00 13.01           N  
ANISOU 1389  N   LEU A 177     1551   1789   1603    308   -122     10       N  
ATOM   1390  CA  LEU A 177      31.482  62.627   8.795  1.00 13.10           C  
ANISOU 1390  CA  LEU A 177     1527   1833   1615    296   -137      4       C  
ATOM   1391  C   LEU A 177      31.568  61.652   9.979  1.00 13.79           C  
ANISOU 1391  C   LEU A 177     1645   1917   1677    338   -153     14       C  
ATOM   1392  O   LEU A 177      32.525  61.692  10.766  1.00 14.10           O  
ANISOU 1392  O   LEU A 177     1653   2000   1702    367   -170      8       O  
ATOM   1393  CB  LEU A 177      30.434  63.715   9.075  1.00 13.69           C  
ANISOU 1393  CB  LEU A 177     1601   1891   1708    241   -135      2       C  
ATOM   1394  CG  LEU A 177      30.653  64.522  10.348  1.00 13.03           C  
ANISOU 1394  CG  LEU A 177     1494   1835   1622    229   -152     -8       C  
ATOM   1395  CD1 LEU A 177      32.055  65.158  10.445  1.00 14.33           C  
ANISOU 1395  CD1 LEU A 177     1600   2054   1790    231   -163    -24       C  
ATOM   1396  CD2 LEU A 177      29.590  65.606  10.458  1.00 14.18           C  
ANISOU 1396  CD2 LEU A 177     1644   1958   1784    182   -146    -12       C  
ATOM   1397  N   GLN A 178      30.594  60.747  10.133  1.00 13.41           N  
ANISOU 1397  N   GLN A 178     1657   1818   1620    341   -150     30       N  
ATOM   1398  CA  GLN A 178      30.666  59.815  11.238  1.00 14.12           C  
ANISOU 1398  CA  GLN A 178     1781   1899   1682    379   -162     45       C  
ATOM   1399  C   GLN A 178      31.897  58.926  11.141  1.00 14.64           C  
ANISOU 1399  C   GLN A 178     1847   1984   1728    448   -170     46       C  
ATOM   1400  O   GLN A 178      32.561  58.668  12.153  1.00 14.96           O  
ANISOU 1400  O   GLN A 178     1880   2055   1746    489   -188     51       O  
ATOM   1401  CB  GLN A 178      29.388  58.980  11.344  1.00 14.61           C  
ANISOU 1401  CB  GLN A 178     1910   1901   1740    361   -154     66       C  
ATOM   1402  CG  GLN A 178      29.419  58.060  12.580  1.00 14.59           C  
ANISOU 1402  CG  GLN A 178     1949   1886   1707    397   -165     88       C  
ATOM   1403  CD  GLN A 178      29.484  58.842  13.859  1.00 15.98           C  
ANISOU 1403  CD  GLN A 178     2094   2105   1872    390   -176     86       C  
ATOM   1404  OE1 GLN A 178      28.582  59.595  14.174  1.00 16.32           O  
ANISOU 1404  OE1 GLN A 178     2128   2148   1924    344   -170     85       O  
ATOM   1405  NE2 GLN A 178      30.550  58.642  14.640  1.00 19.18           N  
ANISOU 1405  NE2 GLN A 178     2483   2549   2252    442   -196     86       N  
ATOM   1406  N   ARG A 179      32.217  58.455   9.933  1.00 13.63           N  
ANISOU 1406  N   ARG A 179     1728   1843   1605    468   -158     41       N  
ATOM   1407  CA  ARG A 179      33.423  57.603   9.757  1.00 15.64           C  
ANISOU 1407  CA  ARG A 179     1982   2122   1839    545   -163     40       C  
ATOM   1408  C   ARG A 179      34.662  58.358  10.242  1.00 15.56           C  
ANISOU 1408  C   ARG A 179     1891   2194   1825    564   -177     27       C  
ATOM   1409  O   ARG A 179      35.509  57.774  10.956  1.00 17.01           O  
ANISOU 1409  O   ARG A 179     2069   2409   1982    626   -194     32       O  
ATOM   1410  CB  ARG A 179      33.589  57.181   8.323  1.00 16.27           C  
ANISOU 1410  CB  ARG A 179     2075   2183   1922    561   -146     30       C  
ATOM   1411  CG  ARG A 179      34.677  56.151   8.114  1.00 17.25           C  
ANISOU 1411  CG  ARG A 179     2211   2321   2021    649   -148     29       C  
ATOM   1412  CD  ARG A 179      34.926  55.897   6.646  1.00 19.36           C  
ANISOU 1412  CD  ARG A 179     2483   2583   2288    666   -128     15       C  
ATOM   1413  NE  ARG A 179      35.580  57.005   5.979  1.00 21.83           N  
ANISOU 1413  NE  ARG A 179     2714   2964   2616    642   -117      2       N  
ATOM   1414  CZ  ARG A 179      36.876  57.303   6.092  1.00 30.11           C  
ANISOU 1414  CZ  ARG A 179     3691   4093   3656    681   -119     -3       C  
ATOM   1415  NH1 ARG A 179      37.692  56.560   6.863  1.00 33.54           N  
ANISOU 1415  NH1 ARG A 179     4125   4553   4066    756   -135      1       N  
ATOM   1416  NH2 ARG A 179      37.392  58.331   5.420  1.00 31.13           N  
ANISOU 1416  NH2 ARG A 179     3747   4278   3799    647   -104    -12       N  
ATOM   1417  N   ARG A 180      34.772  59.625   9.888  1.00 15.19           N  
ANISOU 1417  N   ARG A 180     1785   2184   1802    510   -172     12       N  
ATOM   1418  CA AARG A 180      35.914  60.436  10.292  0.50 15.77           C  
ANISOU 1418  CA AARG A 180     1780   2336   1876    512   -185     -1       C  
ATOM   1419  CA BARG A 180      35.919  60.444  10.276  0.50 16.71           C  
ANISOU 1419  CA BARG A 180     1898   2455   1995    512   -185     -1       C  
ATOM   1420  C   ARG A 180      35.949  60.733  11.782  1.00 16.65           C  
ANISOU 1420  C   ARG A 180     1882   2471   1974    509   -212     -2       C  
ATOM   1421  O   ARG A 180      37.024  60.739  12.399  1.00 17.59           O  
ANISOU 1421  O   ARG A 180     1953   2654   2075    545   -233     -8       O  
ATOM   1422  CB AARG A 180      35.957  61.699   9.454  0.50 14.61           C  
ANISOU 1422  CB AARG A 180     1582   2208   1758    448   -170    -14       C  
ATOM   1423  CB BARG A 180      35.961  61.732   9.449  0.50 16.26           C  
ANISOU 1423  CB BARG A 180     1790   2418   1968    447   -170    -14       C  
ATOM   1424  CG AARG A 180      36.440  61.431   8.038  0.50 12.33           C  
ANISOU 1424  CG AARG A 180     1280   1929   1473    467   -146    -15       C  
ATOM   1425  CG BARG A 180      36.024  61.552   7.906  0.50 18.02           C  
ANISOU 1425  CG BARG A 180     2015   2630   2200    450   -142    -13       C  
ATOM   1426  CD AARG A 180      36.290  62.663   7.180  0.50 13.40           C  
ANISOU 1426  CD AARG A 180     1381   2073   1637    400   -128    -20       C  
ATOM   1427  CD BARG A 180      37.253  60.863   7.384  0.50 22.18           C  
ANISOU 1427  CD BARG A 180     2511   3206   2708    516   -137    -16       C  
ATOM   1428  NE AARG A 180      36.838  62.525   5.842  0.50 14.10           N  
ANISOU 1428  NE AARG A 180     1449   2182   1724    416   -103    -20       N  
ATOM   1429  NE BARG A 180      38.403  61.354   8.066  0.50 24.58           N  
ANISOU 1429  NE BARG A 180     2741   3590   3007    525   -154    -24       N  
ATOM   1430  CZ AARG A 180      37.998  63.054   5.433  0.50 13.40           C  
ANISOU 1430  CZ AARG A 180     1288   2165   1638    414    -95    -25       C  
ATOM   1431  CZ BARG A 180      39.102  62.415   7.720  0.50 25.21           C  
ANISOU 1431  CZ BARG A 180     2746   3728   3104    482   -148    -33       C  
ATOM   1432  NH1AARG A 180      38.740  63.748   6.243  0.50 15.87           N  
ANISOU 1432  NH1AARG A 180     1540   2532   1957    393   -112    -33       N  
ATOM   1433  NH1BARG A 180      38.833  63.111   6.612  0.50 24.01           N  
ANISOU 1433  NH1BARG A 180     2586   3563   2973    432   -121    -32       N  
ATOM   1434  NH2AARG A 180      38.371  62.953   4.169  0.50 14.12           N  
ANISOU 1434  NH2AARG A 180     1364   2274   1725    427    -67    -22       N  
ATOM   1435  NH2BARG A 180      40.103  62.735   8.496  0.50 22.60           N  
ANISOU 1435  NH2BARG A 180     2350   3470   2766    490   -170    -42       N  
ATOM   1436  N   LEU A 181      34.781  60.964  12.379  1.00 15.64           N  
ANISOU 1436  N   LEU A 181     1794   2296   1849    470   -212      4       N  
ATOM   1437  CA  LEU A 181      34.700  61.224  13.812  1.00 15.91           C  
ANISOU 1437  CA  LEU A 181     1828   2351   1865    469   -235      3       C  
ATOM   1438  C   LEU A 181      35.151  59.996  14.564  1.00 16.84           C  
ANISOU 1438  C   LEU A 181     1977   2475   1945    544   -251     21       C  
ATOM   1439  O   LEU A 181      35.943  60.091  15.515  1.00 18.04           O  
ANISOU 1439  O   LEU A 181     2096   2683   2073    575   -277     15       O  
ATOM   1440  CB  LEU A 181      33.268  61.633  14.211  1.00 15.53           C  
ANISOU 1440  CB  LEU A 181     1821   2253   1825    418   -226      9       C  
ATOM   1441  CG  LEU A 181      32.790  63.003  13.742  1.00 15.31           C  
ANISOU 1441  CG  LEU A 181     1765   2221   1830    350   -216     -9       C  
ATOM   1442  CD1 LEU A 181      31.305  63.168  14.005  1.00 15.90           C  
ANISOU 1442  CD1 LEU A 181     1884   2247   1909    315   -204      0       C  
ATOM   1443  CD2 LEU A 181      33.619  64.142  14.425  1.00 16.78           C  
ANISOU 1443  CD2 LEU A 181     1892   2464   2017    330   -239    -35       C  
ATOM   1444  N   THR A 182      34.666  58.826  14.167  1.00 16.76           N  
ANISOU 1444  N   THR A 182     2032   2406   1927    575   -237     43       N  
ATOM   1445  CA  THR A 182      35.052  57.563  14.832  1.00 17.71           C  
ANISOU 1445  CA  THR A 182     2198   2519   2011    652   -249     65       C  
ATOM   1446  C   THR A 182      36.552  57.327  14.686  1.00 19.79           C  
ANISOU 1446  C   THR A 182     2409   2851   2259    720   -264     56       C  
ATOM   1447  O   THR A 182      37.227  57.011  15.691  1.00 20.60           O  
ANISOU 1447  O   THR A 182     2501   2996   2328    774   -289     62       O  
ATOM   1448  CB  THR A 182      34.239  56.405  14.270  1.00 18.71           C  
ANISOU 1448  CB  THR A 182     2410   2560   2136    663   -230     88       C  
ATOM   1449  OG1 THR A 182      32.842  56.599  14.580  1.00 18.86           O  
ANISOU 1449  OG1 THR A 182     2469   2529   2166    599   -219    100       O  
ATOM   1450  CG2 THR A 182      34.715  55.045  14.854  1.00 19.45           C  
ANISOU 1450  CG2 THR A 182     2560   2636   2193    748   -242    113       C  
ATOM   1451  N   ALA A 183      37.091  57.539  13.493  1.00 18.69           N  
ANISOU 1451  N   ALA A 183     2231   2730   2139    720   -250     40       N  
ATOM   1452  CA  ALA A 183      38.535  57.354  13.285  1.00 19.77           C  
ANISOU 1452  CA  ALA A 183     2307   2944   2261    785   -260     31       C  
ATOM   1453  C   ALA A 183      39.379  58.307  14.116  1.00 20.60           C  
ANISOU 1453  C   ALA A 183     2326   3139   2360    770   -287     14       C  
ATOM   1454  O   ALA A 183      40.498  57.927  14.521  1.00 22.65           O  
ANISOU 1454  O   ALA A 183     2544   3467   2592    839   -308     13       O  
ATOM   1455  CB  ALA A 183      38.864  57.504  11.829  1.00 19.43           C  
ANISOU 1455  CB  ALA A 183     2236   2907   2239    777   -234     18       C  
ATOM   1456  N   ALA A 184      38.888  59.518  14.380  1.00 19.87           N  
ANISOU 1456  N   ALA A 184     2206   3050   2290    686   -290     -1       N  
ATOM   1457  CA  ALA A 184      39.584  60.519  15.195  1.00 20.98           C  
ANISOU 1457  CA  ALA A 184     2273   3269   2429    659   -318    -22       C  
ATOM   1458  C   ALA A 184      39.424  60.277  16.681  1.00 22.23           C  
ANISOU 1458  C   ALA A 184     2457   3436   2551    685   -348    -16       C  
ATOM   1459  O   ALA A 184      40.020  61.014  17.462  1.00 24.76           O  
ANISOU 1459  O   ALA A 184     2721   3822   2861    668   -377    -37       O  
ATOM   1460  CB  ALA A 184      39.049  61.926  14.865  1.00 21.93           C  
ANISOU 1460  CB  ALA A 184     2369   3376   2587    559   -308    -43       C  
ATOM   1461  N   GLY A 185      38.638  59.290  17.095  1.00 21.27           N  
ANISOU 1461  N   GLY A 185     2420   3251   2408    721   -342     11       N  
ATOM   1462  CA  GLY A 185      38.343  59.077  18.518  1.00 22.75           C  
ANISOU 1462  CA  GLY A 185     2640   3443   2558    741   -366     23       C  
ATOM   1463  C   GLY A 185      37.505  60.177  19.144  1.00 21.85           C  
ANISOU 1463  C   GLY A 185     2527   3319   2456    665   -368      7       C  
ATOM   1464  O   GLY A 185      37.542  60.406  20.357  1.00 24.40           O  
ANISOU 1464  O   GLY A 185     2848   3674   2747    672   -394      2       O  
ATOM   1465  N   SER A 186      36.696  60.843  18.318  1.00 21.53           N  
ANISOU 1465  N   SER A 186     2493   3231   2456    596   -341     -1       N  
ATOM   1466  CA  SER A 186      35.833  61.907  18.827  1.00 21.31           C  
ANISOU 1466  CA  SER A 186     2469   3187   2438    529   -340    -17       C  
ATOM   1467  C   SER A 186      34.578  61.323  19.467  1.00 20.15           C  
ANISOU 1467  C   SER A 186     2398   2983   2272    532   -327     10       C  
ATOM   1468  O   SER A 186      34.034  60.329  18.949  1.00 22.65           O  
ANISOU 1468  O   SER A 186     2768   3245   2592    550   -305     39       O  
ATOM   1469  CB  SER A 186      35.425  62.827  17.675  1.00 20.23           C  
ANISOU 1469  CB  SER A 186     2313   3022   2351    461   -316    -33       C  
ATOM   1470  OG  SER A 186      34.481  63.795  18.086  1.00 18.97           O  
ANISOU 1470  OG  SER A 186     2167   2838   2201    405   -312    -47       O  
ATOM   1471  N   PRO A 187      34.059  61.973  20.528  1.00 20.75           N  
ANISOU 1471  N   PRO A 187     2481   3071   2331    508   -337      0       N  
ATOM   1472  CA  PRO A 187      32.760  61.538  21.063  1.00 20.67           C  
ANISOU 1472  CA  PRO A 187     2537   3012   2305    501   -317     27       C  
ATOM   1473  C   PRO A 187      31.563  62.117  20.292  1.00 19.53           C  
ANISOU 1473  C   PRO A 187     2406   2815   2199    439   -286     24       C  
ATOM   1474  O   PRO A 187      30.420  61.766  20.586  1.00 20.41           O  
ANISOU 1474  O   PRO A 187     2563   2888   2301    426   -266     47       O  
ATOM   1475  CB  PRO A 187      32.789  62.053  22.489  1.00 22.73           C  
ANISOU 1475  CB  PRO A 187     2792   3317   2525    508   -341     14       C  
ATOM   1476  CG  PRO A 187      33.557  63.308  22.399  1.00 22.35           C  
ANISOU 1476  CG  PRO A 187     2679   3316   2495    475   -363    -32       C  
ATOM   1477  CD  PRO A 187      34.634  63.063  21.343  1.00 21.14           C  
ANISOU 1477  CD  PRO A 187     2482   3181   2368    489   -368    -37       C  
ATOM   1478  N   LEU A 188      31.831  62.968  19.322  1.00 17.75           N  
ANISOU 1478  N   LEU A 188     2139   2591   2013    401   -282     -1       N  
ATOM   1479  CA  LEU A 188      30.744  63.573  18.541  1.00 16.48           C  
ANISOU 1479  CA  LEU A 188     1988   2385   1886    348   -255     -3       C  
ATOM   1480  C   LEU A 188      30.078  62.551  17.661  1.00 16.01           C  
ANISOU 1480  C   LEU A 188     1969   2272   1838    351   -230     26       C  
ATOM   1481  O   LEU A 188      30.721  61.611  17.167  1.00 16.89           O  
ANISOU 1481  O   LEU A 188     2090   2379   1947    388   -231     39       O  
ATOM   1482  CB  LEU A 188      31.243  64.731  17.673  1.00 16.85           C  
ANISOU 1482  CB  LEU A 188     1986   2443   1971    308   -256    -34       C  
ATOM   1483  CG  LEU A 188      31.882  65.921  18.385  1.00 18.88           C  
ANISOU 1483  CG  LEU A 188     2203   2745   2225    288   -281    -70       C  
ATOM   1484  CD1 LEU A 188      32.451  66.916  17.341  1.00 21.56           C  
ANISOU 1484  CD1 LEU A 188     2498   3088   2604    245   -278    -92       C  
ATOM   1485  CD2 LEU A 188      30.894  66.609  19.317  1.00 21.36           C  
ANISOU 1485  CD2 LEU A 188     2542   3047   2524    269   -280    -81       C  
ATOM   1486  N   ARG A 189      28.789  62.761  17.428  1.00 14.65           N  
ANISOU 1486  N   ARG A 189     1821   2063   1680    313   -208     35       N  
ATOM   1487  CA  ARG A 189      27.997  61.935  16.482  1.00 14.71           C  
ANISOU 1487  CA  ARG A 189     1864   2019   1703    301   -185     59       C  
ATOM   1488  C   ARG A 189      27.467  62.810  15.360  1.00 14.53           C  
ANISOU 1488  C   ARG A 189     1821   1982   1717    257   -171     44       C  
ATOM   1489  O   ARG A 189      27.123  63.982  15.560  1.00 15.11           O  
ANISOU 1489  O   ARG A 189     1870   2067   1801    229   -170     25       O  
ATOM   1490  CB  ARG A 189      26.823  61.236  17.163  1.00 16.33           C  
ANISOU 1490  CB  ARG A 189     2117   2198   1888    294   -171     89       C  
ATOM   1491  CG  ARG A 189      27.245  60.082  17.959  1.00 19.25           C  
ANISOU 1491  CG  ARG A 189     2525   2566   2223    338   -180    114       C  
ATOM   1492  CD  ARG A 189      26.101  59.574  18.830  1.00 21.00           C  
ANISOU 1492  CD  ARG A 189     2789   2770   2420    324   -164    146       C  
ATOM   1493  NE  ARG A 189      25.989  60.385  20.044  1.00 19.07           N  
ANISOU 1493  NE  ARG A 189     2524   2570   2149    327   -171    136       N  
ATOM   1494  CZ  ARG A 189      25.215  60.076  21.070  1.00 21.29           C  
ANISOU 1494  CZ  ARG A 189     2834   2856   2398    325   -159    162       C  
ATOM   1495  NH1 ARG A 189      24.348  59.077  20.975  1.00 21.51           N  
ANISOU 1495  NH1 ARG A 189     2907   2843   2423    307   -137    200       N  
ATOM   1496  NH2 ARG A 189      25.303  60.796  22.184  1.00 24.12           N  
ANISOU 1496  NH2 ARG A 189     3176   3260   2727    338   -168    148       N  
ATOM   1497  N   ALA A 190      27.361  62.213  14.182  1.00 12.87           N  
ANISOU 1497  N   ALA A 190     1625   1741   1524    253   -159     52       N  
ATOM   1498  CA  ALA A 190      26.670  62.785  13.023  1.00 12.48           C  
ANISOU 1498  CA  ALA A 190     1566   1670   1503    214   -144     46       C  
ATOM   1499  C   ALA A 190      25.429  61.978  12.737  1.00 12.68           C  
ANISOU 1499  C   ALA A 190     1632   1657   1528    194   -130     68       C  
ATOM   1500  O   ALA A 190      25.496  60.769  12.542  1.00 13.50           O  
ANISOU 1500  O   ALA A 190     1773   1732   1621    211   -129     84       O  
ATOM   1501  CB  ALA A 190      27.622  62.783  11.783  1.00 14.00           C  
ANISOU 1501  CB  ALA A 190     1738   1868   1713    224   -144     35       C  
ATOM   1502  N   LEU A 191      24.281  62.656  12.706  1.00 12.58           N  
ANISOU 1502  N   LEU A 191     1612   1642   1525    159   -119     69       N  
ATOM   1503  CA  LEU A 191      22.965  62.033  12.524  1.00 12.47           C  
ANISOU 1503  CA  LEU A 191     1624   1601   1509    130   -106     89       C  
ATOM   1504  C   LEU A 191      22.229  62.764  11.446  1.00 12.24           C  
ANISOU 1504  C   LEU A 191     1576   1571   1505    100    -98     81       C  
ATOM   1505  O   LEU A 191      22.564  63.891  11.077  1.00 12.40           O  
ANISOU 1505  O   LEU A 191     1565   1606   1539     99    -99     62       O  
ATOM   1506  CB  LEU A 191      22.149  62.119  13.841  1.00 13.10           C  
ANISOU 1506  CB  LEU A 191     1709   1697   1569    123    -99    103       C  
ATOM   1507  CG  LEU A 191      22.853  61.633  15.104  1.00 14.77           C  
ANISOU 1507  CG  LEU A 191     1938   1923   1751    157   -109    112       C  
ATOM   1508  CD1 LEU A 191      22.019  61.926  16.377  1.00 18.08           C  
ANISOU 1508  CD1 LEU A 191     2357   2366   2145    151    -99    124       C  
ATOM   1509  CD2 LEU A 191      23.126  60.147  15.009  1.00 16.53           C  
ANISOU 1509  CD2 LEU A 191     2208   2110   1962    172   -110    136       C  
ATOM   1510  N   ALA A 192      21.186  62.145  10.915  1.00 12.04           N  
ANISOU 1510  N   ALA A 192     1567   1524   1481     72    -90     95       N  
ATOM   1511  CA  ALA A 192      20.327  62.790   9.932  1.00 12.44           C  
ANISOU 1511  CA  ALA A 192     1597   1578   1548     44    -84     89       C  
ATOM   1512  C   ALA A 192      18.867  62.567  10.278  1.00 11.45           C  
ANISOU 1512  C   ALA A 192     1472   1460   1417     12    -75    107       C  
ATOM   1513  O   ALA A 192      18.520  61.662  11.031  1.00 12.41           O  
ANISOU 1513  O   ALA A 192     1617   1573   1524      3    -71    126       O  
ATOM   1514  CB  ALA A 192      20.649  62.259   8.488  1.00 13.00           C  
ANISOU 1514  CB  ALA A 192     1683   1626   1630     41    -88     83       C  
ATOM   1515  N   ALA A 193      18.006  63.427   9.728  1.00 11.20           N  
ANISOU 1515  N   ALA A 193     1411   1447   1397     -3    -70    102       N  
ATOM   1516  CA  ALA A 193      16.552  63.347   9.882  1.00 11.95           C  
ANISOU 1516  CA  ALA A 193     1492   1561   1487    -33    -61    117       C  
ATOM   1517  C   ALA A 193      15.914  63.817   8.607  1.00 11.17           C  
ANISOU 1517  C   ALA A 193     1371   1469   1401    -47    -64    110       C  
ATOM   1518  O   ALA A 193      16.528  64.537   7.812  1.00 11.56           O  
ANISOU 1518  O   ALA A 193     1415   1514   1463    -30    -70     95       O  
ATOM   1519  CB  ALA A 193      16.079  64.244  11.076  1.00 12.02           C  
ANISOU 1519  CB  ALA A 193     1476   1606   1485    -18    -49    118       C  
ATOM   1520  N   HIS A 194      14.650  63.452   8.381  1.00 11.11           N  
ANISOU 1520  N   HIS A 194     1351   1479   1391    -81    -61    123       N  
ATOM   1521  CA  HIS A 194      13.888  64.054   7.302  1.00 11.86           C  
ANISOU 1521  CA  HIS A 194     1416   1594   1493    -89    -66    118       C  
ATOM   1522  C   HIS A 194      12.438  64.241   7.720  1.00 12.12           C  
ANISOU 1522  C   HIS A 194     1412   1673   1518   -109    -57    132       C  
ATOM   1523  O   HIS A 194      11.936  63.463   8.534  1.00 12.57           O  
ANISOU 1523  O   HIS A 194     1472   1737   1564   -136    -48    149       O  
ATOM   1524  CB  HIS A 194      14.010  63.233   5.992  1.00 11.88           C  
ANISOU 1524  CB  HIS A 194     1442   1572   1500   -112    -81    112       C  
ATOM   1525  CG  HIS A 194      13.163  62.011   5.948  1.00 11.59           C  
ANISOU 1525  CG  HIS A 194     1416   1529   1455   -161    -85    123       C  
ATOM   1526  ND1 HIS A 194      11.883  62.023   5.423  1.00 12.46           N  
ANISOU 1526  ND1 HIS A 194     1494   1674   1564   -196    -90    128       N  
ATOM   1527  CD2 HIS A 194      13.396  60.751   6.384  1.00 12.74           C  
ANISOU 1527  CD2 HIS A 194     1604   1638   1595   -185    -85    132       C  
ATOM   1528  CE1 HIS A 194      11.377  60.809   5.534  1.00 12.70           C  
ANISOU 1528  CE1 HIS A 194     1545   1689   1589   -246    -94    138       C  
ATOM   1529  NE2 HIS A 194      12.259  60.009   6.125  1.00 13.14           N  
ANISOU 1529  NE2 HIS A 194     1650   1697   1643   -240    -90    142       N  
ATOM   1530  N   PRO A 195      11.754  65.233   7.109  1.00 11.98           N  
ANISOU 1530  N   PRO A 195     1358   1687   1504    -96    -59    127       N  
ATOM   1531  CA  PRO A 195      10.467  65.675   7.675  1.00 12.52           C  
ANISOU 1531  CA  PRO A 195     1383   1811   1563    -97    -47    139       C  
ATOM   1532  C   PRO A 195       9.270  64.944   7.116  1.00 14.15           C  
ANISOU 1532  C   PRO A 195     1562   2050   1765   -144    -53    151       C  
ATOM   1533  O   PRO A 195       8.134  65.293   7.500  1.00 15.92           O  
ANISOU 1533  O   PRO A 195     1738   2329   1979   -146    -43    162       O  
ATOM   1534  CB  PRO A 195      10.418  67.155   7.282  1.00 12.81           C  
ANISOU 1534  CB  PRO A 195     1400   1862   1604    -49    -47    128       C  
ATOM   1535  CG  PRO A 195      11.204  67.199   6.013  1.00 13.35           C  
ANISOU 1535  CG  PRO A 195     1491   1894   1684    -48    -63    117       C  
ATOM   1536  CD  PRO A 195      12.367  66.295   6.277  1.00 12.07           C  
ANISOU 1536  CD  PRO A 195     1371   1688   1526    -61    -65    113       C  
ATOM   1537  N   GLY A 196       9.454  63.965   6.236  1.00 13.17           N  
ANISOU 1537  N   GLY A 196     1462   1895   1644   -182    -70    148       N  
ATOM   1538  CA  GLY A 196       8.305  63.341   5.579  1.00 14.11           C  
ANISOU 1538  CA  GLY A 196     1554   2047   1760   -233    -81    154       C  
ATOM   1539  C   GLY A 196       7.786  64.145   4.408  1.00 13.65           C  
ANISOU 1539  C   GLY A 196     1461   2023   1700   -214    -97    145       C  
ATOM   1540  O   GLY A 196       8.536  64.759   3.661  1.00 14.73           O  
ANISOU 1540  O   GLY A 196     1617   2135   1842   -178   -105    132       O  
ATOM   1541  N   TYR A 197       6.465  64.159   4.265  1.00 15.17           N  
ANISOU 1541  N   TYR A 197     1600   2278   1885   -239   -101    154       N  
ATOM   1542  CA  TYR A 197       5.807  64.634   3.055  1.00 16.33           C  
ANISOU 1542  CA  TYR A 197     1713   2465   2026   -232   -122    148       C  
ATOM   1543  C   TYR A 197       6.097  66.078   2.660  1.00 16.92           C  
ANISOU 1543  C   TYR A 197     1781   2546   2101   -159   -120    143       C  
ATOM   1544  O   TYR A 197       6.032  66.430   1.477  1.00 17.53           O  
ANISOU 1544  O   TYR A 197     1855   2631   2173   -144   -140    136       O  
ATOM   1545  CB  TYR A 197       4.268  64.439   3.166  1.00 17.21           C  
ANISOU 1545  CB  TYR A 197     1754   2657   2126   -269   -125    161       C  
ATOM   1546  CG  TYR A 197       3.635  65.258   4.280  1.00 17.31           C  
ANISOU 1546  CG  TYR A 197     1719   2725   2133   -231    -98    176       C  
ATOM   1547  CD1 TYR A 197       3.209  66.564   4.040  1.00 20.87           C  
ANISOU 1547  CD1 TYR A 197     2132   3219   2576   -164    -97    176       C  
ATOM   1548  CD2 TYR A 197       3.461  64.746   5.550  1.00 17.11           C  
ANISOU 1548  CD2 TYR A 197     1689   2705   2104   -257    -73    192       C  
ATOM   1549  CE1 TYR A 197       2.661  67.336   5.060  1.00 20.07           C  
ANISOU 1549  CE1 TYR A 197     1993   3165   2466   -121    -71    186       C  
ATOM   1550  CE2 TYR A 197       2.923  65.521   6.596  1.00 17.98           C  
ANISOU 1550  CE2 TYR A 197     1758   2868   2203   -216    -46    203       C  
ATOM   1551  CZ  TYR A 197       2.510  66.809   6.329  1.00 19.74           C  
ANISOU 1551  CZ  TYR A 197     1945   3133   2419   -147    -46    198       C  
ATOM   1552  OH  TYR A 197       1.940  67.521   7.428  1.00 21.45           O  
ANISOU 1552  OH  TYR A 197     2124   3402   2622   -102    -17    207       O  
ATOM   1553  N   SER A 198       6.357  66.944   3.625  1.00 16.62           N  
ANISOU 1553  N   SER A 198     1741   2506   2066   -112    -98    147       N  
ATOM   1554  CA  SER A 198       6.478  68.389   3.286  1.00 17.22           C  
ANISOU 1554  CA  SER A 198     1812   2586   2142    -45    -97    144       C  
ATOM   1555  C   SER A 198       7.567  68.721   2.308  1.00 17.57           C  
ANISOU 1555  C   SER A 198     1902   2578   2194    -27   -107    133       C  
ATOM   1556  O   SER A 198       7.447  69.699   1.566  1.00 19.42           O  
ANISOU 1556  O   SER A 198     2131   2821   2425     13   -113    135       O  
ATOM   1557  CB  SER A 198       6.712  69.200   4.547  1.00 17.80           C  
ANISOU 1557  CB  SER A 198     1889   2655   2217     -2    -72    144       C  
ATOM   1558  OG  SER A 198       7.867  68.841   5.210  1.00 17.06           O  
ANISOU 1558  OG  SER A 198     1841   2506   2133    -12    -64    136       O  
ATOM   1559  N   HIS A 199       8.627  67.925   2.310  1.00 16.33           N  
ANISOU 1559  N   HIS A 199     1868   2228   2108      2   -162    -41       N  
ATOM   1560  CA  HIS A 199       9.790  68.194   1.425  1.00 16.22           C  
ANISOU 1560  CA  HIS A 199     1894   2184   2084     18   -168    -24       C  
ATOM   1561  C   HIS A 199       9.941  67.123   0.392  1.00 17.50           C  
ANISOU 1561  C   HIS A 199     2071   2352   2225     -7   -178    -34       C  
ATOM   1562  O   HIS A 199      10.993  66.529   0.188  1.00 19.99           O  
ANISOU 1562  O   HIS A 199     2421   2638   2536    -18   -167    -32       O  
ATOM   1563  CB  HIS A 199      11.032  68.417   2.282  1.00 16.47           C  
ANISOU 1563  CB  HIS A 199     1955   2174   2127     21   -146    -16       C  
ATOM   1564  CG  HIS A 199      10.986  69.719   3.012  1.00 15.88           C  
ANISOU 1564  CG  HIS A 199     1871   2091   2070     51   -140    -12       C  
ATOM   1565  ND1 HIS A 199      10.128  69.960   4.062  1.00 17.63           N  
ANISOU 1565  ND1 HIS A 199     2064   2333   2302     55   -132    -26       N  
ATOM   1566  CD2 HIS A 199      11.655  70.884   2.803  1.00 19.82           C  
ANISOU 1566  CD2 HIS A 199     2386   2563   2582     80   -140      1       C  
ATOM   1567  CE1 HIS A 199      10.320  71.187   4.514  1.00 20.01           C  
ANISOU 1567  CE1 HIS A 199     2366   2616   2620     86   -127    -26       C  
ATOM   1568  NE2 HIS A 199      11.251  71.768   3.776  1.00 20.82           N  
ANISOU 1568  NE2 HIS A 199     2496   2685   2727     99   -132     -9       N  
ATOM   1569  N   THR A 200       8.874  66.940  -0.361  1.00 17.61           N  
ANISOU 1569  N   THR A 200     2055   2408   2226    -12   -202    -47       N  
ATOM   1570  CA  THR A 200       8.802  65.926  -1.391  1.00 18.83           C  
ANISOU 1570  CA  THR A 200     2219   2576   2359    -40   -216    -67       C  
ATOM   1571  C   THR A 200       8.006  66.520  -2.558  1.00 19.48           C  
ANISOU 1571  C   THR A 200     2275   2710   2414    -15   -251    -66       C  
ATOM   1572  O   THR A 200       7.357  67.557  -2.424  1.00 20.93           O  
ANISOU 1572  O   THR A 200     2429   2916   2604     20   -262    -50       O  
ATOM   1573  CB  THR A 200       8.100  64.632  -0.938  1.00 18.87           C  
ANISOU 1573  CB  THR A 200     2207   2587   2376    -93   -210    -97       C  
ATOM   1574  OG1 THR A 200       6.702  64.897  -0.756  1.00 20.61           O  
ANISOU 1574  OG1 THR A 200     2371   2857   2602    -98   -225   -108       O  
ATOM   1575  CG2 THR A 200       8.724  64.091   0.326  1.00 19.93           C  
ANISOU 1575  CG2 THR A 200     2363   2675   2532   -112   -177    -89       C  
ATOM   1576  N   ASN A 201       8.039  65.815  -3.682  1.00 21.47           N  
ANISOU 1576  N   ASN A 201     2539   2982   2636    -31   -269    -85       N  
ATOM   1577  CA AASN A 201       7.354  66.247  -4.909  0.50 22.83           C  
ANISOU 1577  CA AASN A 201     2690   3212   2771     -7   -307    -85       C  
ATOM   1578  CA BASN A 201       7.336  66.296  -4.879  0.50 22.73           C  
ANISOU 1578  CA BASN A 201     2677   3200   2760     -6   -307    -84       C  
ATOM   1579  C   ASN A 201       5.826  66.056  -4.964  1.00 26.04           C  
ANISOU 1579  C   ASN A 201     3035   3681   3178    -22   -337   -112       C  
ATOM   1580  O   ASN A 201       5.196  66.312  -6.003  1.00 28.65           O  
ANISOU 1580  O   ASN A 201     3342   4069   3473     -3   -374   -116       O  
ATOM   1581  CB AASN A 201       8.052  65.588  -6.114  0.50 23.52           C  
ANISOU 1581  CB AASN A 201     2815   3304   2818    -18   -313   -100       C  
ATOM   1582  CB BASN A 201       8.037  65.797  -6.135  0.50 23.25           C  
ANISOU 1582  CB BASN A 201     2779   3271   2782    -10   -315    -94       C  
ATOM   1583  CG AASN A 201       7.797  64.085  -6.193  0.50 23.55           C  
ANISOU 1583  CG AASN A 201     2819   3306   2823    -75   -314   -154       C  
ATOM   1584  CG BASN A 201       7.492  66.450  -7.377  0.50 23.76           C  
ANISOU 1584  CG BASN A 201     2829   3398   2799     25   -353    -82       C  
ATOM   1585  OD1AASN A 201       6.954  63.567  -5.479  0.50 26.14           O  
ANISOU 1585  OD1AASN A 201     3113   3638   3180   -111   -314   -176       O  
ATOM   1586  OD1BASN A 201       6.596  67.284  -7.286  0.50 25.26           O  
ANISOU 1586  OD1BASN A 201     2980   3623   2993     56   -375    -63       O  
ATOM   1587  ND2AASN A 201       8.523  63.392  -7.072  0.50 27.15           N  
ANISOU 1587  ND2AASN A 201     3312   3752   3249    -86   -312   -175       N  
ATOM   1588  ND2BASN A 201       8.024  66.087  -8.532  0.50 25.94           N  
ANISOU 1588  ND2BASN A 201     3135   3692   3027     25   -361    -91       N  
ATOM   1589  N   LEU A 202       5.212  65.702  -3.853  1.00 26.83           N  
ANISOU 1589  N   LEU A 202     3104   3776   3315    -51   -321   -126       N  
ATOM   1590  CA  LEU A 202       3.757  65.521  -3.806  1.00 29.67           C  
ANISOU 1590  CA  LEU A 202     3395   4197   3679    -69   -344   -153       C  
ATOM   1591  C   LEU A 202       2.915  66.803  -4.016  1.00 32.71           C  
ANISOU 1591  C   LEU A 202     3734   4635   4059     -8   -371   -130       C  
ATOM   1592  O   LEU A 202       3.260  67.881  -3.515  1.00 35.30           O  
ANISOU 1592  O   LEU A 202     4073   4935   4401     40   -356    -95       O  
ATOM   1593  CB  LEU A 202       3.385  64.887  -2.475  1.00 29.07           C  
ANISOU 1593  CB  LEU A 202     3299   4101   3644   -114   -310   -166       C  
ATOM   1594  CG  LEU A 202       3.925  63.490  -2.234  1.00 27.74           C  
ANISOU 1594  CG  LEU A 202     3168   3885   3487   -177   -287   -189       C  
ATOM   1595  CD1 LEU A 202       3.373  63.029  -0.900  1.00 29.48           C  
ANISOU 1595  CD1 LEU A 202     3361   4095   3743   -216   -254   -192       C  
ATOM   1596  CD2 LEU A 202       3.531  62.525  -3.355  1.00 28.85           C  
ANISOU 1596  CD2 LEU A 202     3301   4052   3606   -219   -315   -233       C  
ATOM   1597  N   ALA A 223       0.986  75.290  10.024  1.00 38.35           N  
ANISOU 1597  N   ALA A 223     4305   5253   5013    311    -32   -213       N  
ATOM   1598  CA  ALA A 223       1.397  74.904  11.387  1.00 37.26           C  
ANISOU 1598  CA  ALA A 223     4183   5123   4850    279      5   -233       C  
ATOM   1599  C   ALA A 223       1.641  73.400  11.546  1.00 35.68           C  
ANISOU 1599  C   ALA A 223     3990   4943   4621    203     14   -212       C  
ATOM   1600  O   ALA A 223       2.647  72.964  12.122  1.00 33.13           O  
ANISOU 1600  O   ALA A 223     3716   4593   4279    171     25   -205       O  
ATOM   1601  CB  ALA A 223       0.342  75.349  12.384  1.00 38.26           C  
ANISOU 1601  CB  ALA A 223     4254   5305   4975    310     38   -271       C  
ATOM   1602  N   THR A 224       0.686  72.623  11.061  1.00 34.75           N  
ANISOU 1602  N   THR A 224     3823   4875   4504    174     11   -204       N  
ATOM   1603  CA  THR A 224       0.633  71.187  11.280  1.00 32.49           C  
ANISOU 1603  CA  THR A 224     3535   4611   4198    101     26   -187       C  
ATOM   1604  C   THR A 224       1.822  70.546  10.579  1.00 29.87           C  
ANISOU 1604  C   THR A 224     3266   4220   3861     69      3   -160       C  
ATOM   1605  O   THR A 224       2.488  69.655  11.157  1.00 27.64           O  
ANISOU 1605  O   THR A 224     3019   3920   3559     25     21   -145       O  
ATOM   1606  CB  THR A 224      -0.725  70.591  10.745  1.00 35.06           C  
ANISOU 1606  CB  THR A 224     3785   5001   4532     76     22   -191       C  
ATOM   1607  N   ASP A 225       2.096  70.997   9.350  1.00 27.38           N  
ANISOU 1607  N   ASP A 225     2965   3875   3561     95    -34   -151       N  
ATOM   1608  CA  ASP A 225       3.159  70.425   8.528  1.00 25.92           C  
ANISOU 1608  CA  ASP A 225     2834   3641   3371     69    -55   -128       C  
ATOM   1609  C   ASP A 225       4.499  70.707   9.180  1.00 23.71           C  
ANISOU 1609  C   ASP A 225     2613   3309   3084     75    -44   -123       C  
ATOM   1610  O   ASP A 225       5.373  69.820   9.214  1.00 22.07           O  
ANISOU 1610  O   ASP A 225     2445   3075   2864     37    -42   -107       O  
ATOM   1611  CB  ASP A 225       3.173  70.971   7.081  1.00 26.36           C  
ANISOU 1611  CB  ASP A 225     2893   3684   3438    101    -96   -117       C  
ATOM   1612  CG  ASP A 225       1.914  70.625   6.286  1.00 29.19           C  
ANISOU 1612  CG  ASP A 225     3191   4099   3798     94   -117   -123       C  
ATOM   1613  OD1 ASP A 225       1.067  69.827   6.742  1.00 28.27           O  
ANISOU 1613  OD1 ASP A 225     3031   4030   3680     54   -100   -136       O  
ATOM   1614  OD2 ASP A 225       1.789  71.206   5.190  1.00 35.72           O  
ANISOU 1614  OD2 ASP A 225     4014   4927   4628    131   -150   -114       O  
ATOM   1615  N   ALA A 226       4.677  71.931   9.701  1.00 22.08           N  
ANISOU 1615  N   ALA A 226     2411   3089   2887    122    -39   -139       N  
ATOM   1616  CA  ALA A 226       5.915  72.277  10.349  1.00 20.26           C  
ANISOU 1616  CA  ALA A 226     2230   2817   2651    125    -32   -142       C  
ATOM   1617  C   ALA A 226       6.084  71.474  11.632  1.00 18.89           C  
ANISOU 1617  C   ALA A 226     2061   2667   2448     91     -2   -146       C  
ATOM   1618  O   ALA A 226       7.204  71.031  11.910  1.00 18.52           O  
ANISOU 1618  O   ALA A 226     2055   2592   2387     71     -3   -134       O  
ATOM   1619  CB  ALA A 226       5.970  73.791  10.626  1.00 21.79           C  
ANISOU 1619  CB  ALA A 226     2425   2987   2865    180    -32   -166       C  
ATOM   1620  N   ASP A 227       5.043  71.306  12.440  1.00 18.24           N  
ANISOU 1620  N   ASP A 227     1937   2638   2354     87     23   -160       N  
ATOM   1621  CA  ASP A 227       5.179  70.477  13.640  1.00 17.32           C  
ANISOU 1621  CA  ASP A 227     1828   2549   2203     53     53   -155       C  
ATOM   1622  C   ASP A 227       5.593  69.045  13.317  1.00 15.96           C  
ANISOU 1622  C   ASP A 227     1680   2360   2021      0     52   -118       C  
ATOM   1623  O   ASP A 227       6.474  68.456  13.979  1.00 15.48           O  
ANISOU 1623  O   ASP A 227     1658   2285   1936    -17     60   -101       O  
ATOM   1624  CB  ASP A 227       3.908  70.417  14.506  1.00 18.69           C  
ANISOU 1624  CB  ASP A 227     1948   2789   2362     51     89   -171       C  
ATOM   1625  CG  ASP A 227       3.543  71.713  15.197  1.00 24.02           C  
ANISOU 1625  CG  ASP A 227     2603   3485   3038    104    102   -213       C  
ATOM   1626  OD1 ASP A 227       4.402  72.400  15.765  1.00 24.77           O  
ANISOU 1626  OD1 ASP A 227     2732   3554   3123    127     99   -233       O  
ATOM   1627  OD2 ASP A 227       2.308  71.966  15.271  1.00 31.83           O  
ANISOU 1627  OD2 ASP A 227     3535   4524   4036    120    118   -231       O  
ATOM   1628  N   PHE A 228       4.948  68.435  12.331  1.00 15.56           N  
ANISOU 1628  N   PHE A 228     1608   2314   1988    -23     40   -108       N  
ATOM   1629  CA  PHE A 228       5.239  67.059  11.974  1.00 14.85           C  
ANISOU 1629  CA  PHE A 228     1542   2203   1895    -75     40    -80       C  
ATOM   1630  C   PHE A 228       6.683  66.903  11.473  1.00 14.09           C  
ANISOU 1630  C   PHE A 228     1503   2049   1800    -69     18    -65       C  
ATOM   1631  O   PHE A 228       7.427  65.983  11.867  1.00 14.23           O  
ANISOU 1631  O   PHE A 228     1558   2043   1804    -93     27    -42       O  
ATOM   1632  CB  PHE A 228       4.249  66.533  10.921  1.00 15.38           C  
ANISOU 1632  CB  PHE A 228     1572   2288   1984   -102     28    -83       C  
ATOM   1633  CG  PHE A 228       4.432  65.076  10.623  1.00 16.31           C  
ANISOU 1633  CG  PHE A 228     1713   2381   2103   -160     32    -63       C  
ATOM   1634  CD1 PHE A 228       3.956  64.103  11.498  1.00 17.08           C  
ANISOU 1634  CD1 PHE A 228     1804   2494   2192   -207     69    -47       C  
ATOM   1635  CD2 PHE A 228       5.155  64.652   9.525  1.00 16.86           C  
ANISOU 1635  CD2 PHE A 228     1818   2405   2182   -166      5    -57       C  
ATOM   1636  CE1 PHE A 228       4.158  62.753  11.217  1.00 18.98           C  
ANISOU 1636  CE1 PHE A 228     2073   2698   2440   -260     75    -28       C  
ATOM   1637  CE2 PHE A 228       5.369  63.309   9.277  1.00 17.55           C  
ANISOU 1637  CE2 PHE A 228     1933   2461   2274   -215     11    -44       C  
ATOM   1638  CZ  PHE A 228       4.903  62.378  10.110  1.00 17.62           C  
ANISOU 1638  CZ  PHE A 228     1937   2476   2280   -261     44    -29       C  
ATOM   1639  N   GLY A 229       7.118  67.820  10.621  1.00 14.13           N  
ANISOU 1639  N   GLY A 229     1516   2030   1820    -34     -8    -74       N  
ATOM   1640  CA  GLY A 229       8.467  67.745  10.125  1.00 13.24           C  
ANISOU 1640  CA  GLY A 229     1451   1869   1709    -29    -25    -62       C  
ATOM   1641  C   GLY A 229       9.513  67.974  11.198  1.00 13.61           C  
ANISOU 1641  C   GLY A 229     1527   1905   1740    -18    -16    -61       C  
ATOM   1642  O   GLY A 229      10.542  67.276  11.276  1.00 13.36           O  
ANISOU 1642  O   GLY A 229     1529   1847   1699    -30    -18    -43       O  
ATOM   1643  N   ALA A 230       9.261  68.967  12.057  1.00 13.12           N  
ANISOU 1643  N   ALA A 230     1447   1864   1671      7     -6    -84       N  
ATOM   1644  CA  ALA A 230      10.224  69.323  13.104  1.00 13.33           C  
ANISOU 1644  CA  ALA A 230     1497   1888   1679     19     -1    -93       C  
ATOM   1645  C   ALA A 230      10.392  68.191  14.086  1.00 13.02           C  
ANISOU 1645  C   ALA A 230     1471   1870   1605     -6     17    -71       C  
ATOM   1646  O   ALA A 230      11.470  68.023  14.679  1.00 13.15           O  
ANISOU 1646  O   ALA A 230     1515   1879   1602     -3     12    -63       O  
ATOM   1647  CB  ALA A 230       9.792  70.621  13.835  1.00 15.01           C  
ANISOU 1647  CB  ALA A 230     1689   2121   1892     52      6   -131       C  
ATOM   1648  N   ARG A 231       9.324  67.430  14.315  1.00 13.72           N  
ANISOU 1648  N   ARG A 231     1538   1987   1685    -32     39    -58       N  
ATOM   1649  CA  ARG A 231       9.372  66.293  15.229  1.00 13.18           C  
ANISOU 1649  CA  ARG A 231     1485   1935   1585    -60     62    -27       C  
ATOM   1650  C   ARG A 231      10.547  65.370  14.941  1.00 12.33           C  
ANISOU 1650  C   ARG A 231     1422   1785   1478    -70     49      3       C  
ATOM   1651  O   ARG A 231      11.212  64.854  15.827  1.00 13.19           O  
ANISOU 1651  O   ARG A 231     1555   1898   1555    -69     56     26       O  
ATOM   1652  CB  ARG A 231       8.066  65.520  15.149  1.00 13.76           C  
ANISOU 1652  CB  ARG A 231     1529   2033   1665    -96     87    -15       C  
ATOM   1653  CG  ARG A 231       7.956  64.298  16.061  1.00 14.80           C  
ANISOU 1653  CG  ARG A 231     1678   2177   1768   -132    119     23       C  
ATOM   1654  CD  ARG A 231       6.719  63.452  15.746  1.00 15.28           C  
ANISOU 1654  CD  ARG A 231     1709   2249   1847   -181    142     35       C  
ATOM   1655  NE  ARG A 231       5.507  64.198  15.989  1.00 16.44           N  
ANISOU 1655  NE  ARG A 231     1799   2454   1995   -175    160      5       N  
ATOM   1656  CZ  ARG A 231       4.309  63.789  15.585  1.00 20.34           C  
ANISOU 1656  CZ  ARG A 231     2247   2970   2509   -211    174      2       C  
ATOM   1657  NH1 ARG A 231       4.197  62.686  14.873  1.00 20.97           N  
ANISOU 1657  NH1 ARG A 231     2339   3015   2614   -259    171     21       N  
ATOM   1658  NH2 ARG A 231       3.237  64.531  15.849  1.00 23.69           N  
ANISOU 1658  NH2 ARG A 231     2613   3453   2934   -198    190    -26       N  
ATOM   1659  N   GLN A 232      10.761  65.146  13.649  1.00 11.86           N  
ANISOU 1659  N   GLN A 232     1370   1685   1450    -76     29      5       N  
ATOM   1660  CA  GLN A 232      11.775  64.197  13.205  1.00 12.22           C  
ANISOU 1660  CA  GLN A 232     1454   1688   1501    -83     19     31       C  
ATOM   1661  C   GLN A 232      13.164  64.714  13.594  1.00 12.42           C  
ANISOU 1661  C   GLN A 232     1499   1705   1513    -52      2     28       C  
ATOM   1662  O   GLN A 232      14.005  63.976  14.149  1.00 13.14           O  
ANISOU 1662  O   GLN A 232     1617   1788   1586    -48      2     54       O  
ATOM   1663  CB  GLN A 232      11.646  63.946  11.704  1.00 12.51           C  
ANISOU 1663  CB  GLN A 232     1490   1691   1569    -94      3     25       C  
ATOM   1664  CG  GLN A 232      10.226  63.776  11.137  1.00 12.09           C  
ANISOU 1664  CG  GLN A 232     1404   1657   1531   -121      9     13       C  
ATOM   1665  CD  GLN A 232       9.364  62.769  11.845  1.00 12.34           C  
ANISOU 1665  CD  GLN A 232     1428   1703   1556   -162     38     31       C  
ATOM   1666  OE1 GLN A 232       9.860  61.701  12.266  1.00 13.95           O  
ANISOU 1666  OE1 GLN A 232     1666   1879   1753   -180     51     61       O  
ATOM   1667  NE2 GLN A 232       8.040  63.080  11.957  1.00 13.65           N  
ANISOU 1667  NE2 GLN A 232     1546   1912   1725   -177     51     15       N  
ATOM   1668  N   THR A 233      13.426  65.975  13.281  1.00 11.84           N  
ANISOU 1668  N   THR A 233     1413   1634   1452    -28    -13     -1       N  
ATOM   1669  CA  THR A 233      14.684  66.618  13.657  1.00 12.19           C  
ANISOU 1669  CA  THR A 233     1467   1674   1489     -5    -29    -12       C  
ATOM   1670  C   THR A 233      14.890  66.630  15.176  1.00 12.46           C  
ANISOU 1670  C   THR A 233     1503   1748   1482      1    -21    -13       C  
ATOM   1671  O   THR A 233      15.985  66.371  15.663  1.00 13.11           O  
ANISOU 1671  O   THR A 233     1601   1833   1546     12    -33     -3       O  
ATOM   1672  CB  THR A 233      14.742  68.042  13.140  1.00 12.71           C  
ANISOU 1672  CB  THR A 233     1518   1730   1580     11    -41    -46       C  
ATOM   1673  OG1 THR A 233      14.538  68.058  11.725  1.00 12.95           O  
ANISOU 1673  OG1 THR A 233     1548   1730   1639      7    -49    -40       O  
ATOM   1674  CG2 THR A 233      16.080  68.700  13.451  1.00 13.46           C  
ANISOU 1674  CG2 THR A 233     1621   1817   1674     25    -57    -61       C  
ATOM   1675  N   LEU A 234      13.819  66.935  15.903  1.00 11.88           N  
ANISOU 1675  N   LEU A 234     1410   1711   1390     -1     -1    -26       N  
ATOM   1676  CA  LEU A 234      13.890  67.039  17.364  1.00 12.81           C  
ANISOU 1676  CA  LEU A 234     1528   1877   1460      7      9    -32       C  
ATOM   1677  C   LEU A 234      14.248  65.704  18.029  1.00 12.83           C  
ANISOU 1677  C   LEU A 234     1556   1890   1427     -2     18     17       C  
ATOM   1678  O   LEU A 234      14.966  65.655  19.016  1.00 13.55           O  
ANISOU 1678  O   LEU A 234     1658   2011   1476     12     11     22       O  
ATOM   1679  CB  LEU A 234      12.570  67.625  17.899  1.00 13.01           C  
ANISOU 1679  CB  LEU A 234     1524   1942   1474      7     34    -58       C  
ATOM   1680  CG  LEU A 234      12.325  69.111  17.580  1.00 13.03           C  
ANISOU 1680  CG  LEU A 234     1505   1938   1505     30     25   -111       C  
ATOM   1681  CD1 LEU A 234      10.844  69.522  17.826  1.00 15.03           C  
ANISOU 1681  CD1 LEU A 234     1724   2227   1759     34     52   -131       C  
ATOM   1682  CD2 LEU A 234      13.303  70.011  18.362  1.00 14.14           C  
ANISOU 1682  CD2 LEU A 234     1654   2089   1626     51      9   -148       C  
ATOM   1683  N   TYR A 235      13.742  64.604  17.454  1.00 12.82           N  
ANISOU 1683  N   TYR A 235     1565   1861   1443    -27     32     53       N  
ATOM   1684  CA  TYR A 235      14.114  63.268  17.903  1.00 13.37           C  
ANISOU 1684  CA  TYR A 235     1666   1920   1491    -36     42    106       C  
ATOM   1685  C   TYR A 235      15.615  63.010  17.650  1.00 12.94           C  
ANISOU 1685  C   TYR A 235     1635   1838   1442    -11     12    118       C  
ATOM   1686  O   TYR A 235      16.356  62.617  18.554  1.00 13.48           O  
ANISOU 1686  O   TYR A 235     1720   1927   1471      7      6    144       O  
ATOM   1687  CB  TYR A 235      13.238  62.239  17.187  1.00 14.24           C  
ANISOU 1687  CB  TYR A 235     1781   1995   1632    -73     63    132       C  
ATOM   1688  CG  TYR A 235      13.402  60.793  17.597  1.00 14.66           C  
ANISOU 1688  CG  TYR A 235     1871   2024   1674    -89     80    190       C  
ATOM   1689  CD1 TYR A 235      14.415  60.026  17.063  1.00 16.39           C  
ANISOU 1689  CD1 TYR A 235     2123   2191   1912    -76     63    213       C  
ATOM   1690  CD2 TYR A 235      12.485  60.182  18.412  1.00 16.91           C  
ANISOU 1690  CD2 TYR A 235     2157   2332   1935   -117    117    222       C  
ATOM   1691  CE1 TYR A 235      14.513  58.653  17.326  1.00 18.63           C  
ANISOU 1691  CE1 TYR A 235     2445   2437   2194    -88     81    267       C  
ATOM   1692  CE2 TYR A 235      12.582  58.816  18.677  1.00 18.91           C  
ANISOU 1692  CE2 TYR A 235     2449   2549   2187   -135    136    280       C  
ATOM   1693  CZ  TYR A 235      13.592  58.087  18.121  1.00 20.05           C  
ANISOU 1693  CZ  TYR A 235     2630   2634   2354   -118    117    301       C  
ATOM   1694  OH  TYR A 235      13.666  56.719  18.394  1.00 26.10           O  
ANISOU 1694  OH  TYR A 235     3438   3354   3122   -133    138    360       O  
ATOM   1695  N   ALA A 236      16.093  63.315  16.447  1.00 12.77           N  
ANISOU 1695  N   ALA A 236     1611   1777   1463     -7     -6     98       N  
ATOM   1696  CA  ALA A 236      17.519  63.166  16.137  1.00 12.81           C  
ANISOU 1696  CA  ALA A 236     1629   1762   1476     16    -31    104       C  
ATOM   1697  C   ALA A 236      18.417  64.050  17.014  1.00 13.28           C  
ANISOU 1697  C   ALA A 236     1676   1864   1506     41    -52     80       C  
ATOM   1698  O   ALA A 236      19.506  63.644  17.396  1.00 14.80           O  
ANISOU 1698  O   ALA A 236     1877   2063   1681     62    -69     98       O  
ATOM   1699  CB  ALA A 236      17.787  63.459  14.653  1.00 13.45           C  
ANISOU 1699  CB  ALA A 236     1705   1801   1604     13    -43     84       C  
ATOM   1700  N   ALA A 237      17.927  65.230  17.380  1.00 12.90           N  
ANISOU 1700  N   ALA A 237     1604   1845   1451     38    -51     38       N  
ATOM   1701  CA  ALA A 237      18.715  66.164  18.208  1.00 12.89           C  
ANISOU 1701  CA  ALA A 237     1589   1882   1423     56    -72      3       C  
ATOM   1702  C   ALA A 237      18.796  65.788  19.654  1.00 13.67           C  
ANISOU 1702  C   ALA A 237     1695   2038   1459     68    -70     19       C  
ATOM   1703  O   ALA A 237      19.690  66.282  20.343  1.00 14.92           O  
ANISOU 1703  O   ALA A 237     1845   2232   1590     84    -94     -4       O  
ATOM   1704  CB  ALA A 237      18.136  67.572  18.096  1.00 14.61           C  
ANISOU 1704  CB  ALA A 237     1785   2103   1660     52    -69    -50       C  
ATOM   1705  N   SER A 238      17.884  64.927  20.121  1.00 13.50           N  
ANISOU 1705  N   SER A 238     1689   2028   1412     58    -42     58       N  
ATOM   1706  CA  SER A 238      17.720  64.691  21.551  1.00 15.00           C  
ANISOU 1706  CA  SER A 238     1885   2280   1532     67    -32     74       C  
ATOM   1707  C   SER A 238      17.949  63.262  22.043  1.00 16.50           C  
ANISOU 1707  C   SER A 238     2108   2471   1690     74    -23    147       C  
ATOM   1708  O   SER A 238      18.148  63.087  23.251  1.00 18.95           O  
ANISOU 1708  O   SER A 238     2426   2839   1935     90    -24    166       O  
ATOM   1709  CB  SER A 238      16.342  65.170  22.000  1.00 15.13           C  
ANISOU 1709  CB  SER A 238     1886   2328   1533     51      1     52       C  
ATOM   1710  OG  SER A 238      15.304  64.427  21.409  1.00 15.22           O  
ANISOU 1710  OG  SER A 238     1902   2307   1573     23     31     85       O  
ATOM   1711  N   GLN A 239      17.783  62.255  21.180  1.00 15.13           N  
ANISOU 1711  N   GLN A 239     1953   2235   1558     60    -11    188       N  
ATOM   1712  CA  GLN A 239      17.769  60.860  21.637  1.00 15.84           C  
ANISOU 1712  CA  GLN A 239     2080   2312   1626     61      5    262       C  
ATOM   1713  C   GLN A 239      19.144  60.231  21.561  1.00 16.47           C  
ANISOU 1713  C   GLN A 239     2178   2372   1705     98    -25    292       C  
ATOM   1714  O   GLN A 239      19.984  60.660  20.814  1.00 16.53           O  
ANISOU 1714  O   GLN A 239     2170   2360   1747    112    -52    260       O  
ATOM   1715  CB  GLN A 239      16.766  60.052  20.818  1.00 16.41           C  
ANISOU 1715  CB  GLN A 239     2164   2324   1744     22     38    285       C  
ATOM   1716  CG  GLN A 239      15.349  60.591  20.876  1.00 17.53           C  
ANISOU 1716  CG  GLN A 239     2280   2491   1888    -12     69    258       C  
ATOM   1717  CD  GLN A 239      14.799  60.744  22.284  1.00 20.31           C  
ANISOU 1717  CD  GLN A 239     2628   2916   2172    -12     93    272       C  
ATOM   1718  OE1 GLN A 239      14.581  61.885  22.827  1.00 22.48           O  
ANISOU 1718  OE1 GLN A 239     2874   3249   2418     -1     90    221       O  
ATOM   1719  NE2 GLN A 239      14.584  59.604  22.930  1.00 19.98           N  
ANISOU 1719  NE2 GLN A 239     2617   2871   2101    -23    121    340       N  
ATOM   1720  N   ASP A 240      19.344  59.164  22.339  1.00 18.58           N  
ANISOU 1720  N   ASP A 240     2479   2644   1935    115    -16    359       N  
ATOM   1721  CA  ASP A 240      20.657  58.490  22.413  1.00 18.73           C  
ANISOU 1721  CA  ASP A 240     2516   2651   1949    162    -46    396       C  
ATOM   1722  C   ASP A 240      20.748  57.490  21.276  1.00 20.16           C  
ANISOU 1722  C   ASP A 240     2722   2740   2195    156    -35    422       C  
ATOM   1723  O   ASP A 240      20.390  56.321  21.436  1.00 23.31           O  
ANISOU 1723  O   ASP A 240     3162   3096   2598    151    -10    483       O  
ATOM   1724  CB  ASP A 240      20.833  57.779  23.767  1.00 21.05           C  
ANISOU 1724  CB  ASP A 240     2838   2990   2169    190    -43    463       C  
ATOM   1725  CG  ASP A 240      22.196  57.182  23.926  1.00 23.67           C  
ANISOU 1725  CG  ASP A 240     3181   3321   2491    247    -79    499       C  
ATOM   1726  OD1 ASP A 240      23.073  57.345  23.066  1.00 23.19           O  
ANISOU 1726  OD1 ASP A 240     3101   3232   2477    265   -106    469       O  
ATOM   1727  OD2 ASP A 240      22.401  56.486  24.951  1.00 26.64           O  
ANISOU 1727  OD2 ASP A 240     3585   3727   2809    278    -79    565       O  
ATOM   1728  N   LEU A 241      21.137  57.973  20.097  1.00 17.39           N  
ANISOU 1728  N   LEU A 241     2349   2357   1898    152    -51    372       N  
ATOM   1729  CA  LEU A 241      21.135  57.206  18.849  1.00 17.26           C  
ANISOU 1729  CA  LEU A 241     2353   2258   1944    142    -40    378       C  
ATOM   1730  C   LEU A 241      22.558  56.877  18.428  1.00 17.56           C  
ANISOU 1730  C   LEU A 241     2390   2279   2000    191    -69    382       C  
ATOM   1731  O   LEU A 241      23.472  57.701  18.626  1.00 17.66           O  
ANISOU 1731  O   LEU A 241     2369   2343   1997    217   -100    352       O  
ATOM   1732  CB  LEU A 241      20.486  58.018  17.723  1.00 16.43           C  
ANISOU 1732  CB  LEU A 241     2222   2137   1882    104    -35    318       C  
ATOM   1733  CG  LEU A 241      19.006  58.309  17.919  1.00 18.65           C  
ANISOU 1733  CG  LEU A 241     2496   2431   2158     57     -6    309       C  
ATOM   1734  CD1 LEU A 241      18.519  59.469  17.054  1.00 19.34           C  
ANISOU 1734  CD1 LEU A 241     2548   2526   2274     35    -11    247       C  
ATOM   1735  CD2 LEU A 241      18.184  57.048  17.572  1.00 26.01           C  
ANISOU 1735  CD2 LEU A 241     3462   3302   3118     24     26    347       C  
ATOM   1736  N   PRO A 242      22.769  55.700  17.819  1.00 17.35           N  
ANISOU 1736  N   PRO A 242     2399   2181   2010    203    -57    414       N  
ATOM   1737  CA  PRO A 242      24.069  55.423  17.250  1.00 18.35           C  
ANISOU 1737  CA  PRO A 242     2520   2290   2162    251    -80    410       C  
ATOM   1738  C   PRO A 242      24.442  56.429  16.154  1.00 16.78           C  
ANISOU 1738  C   PRO A 242     2280   2100   1994    239    -93    343       C  
ATOM   1739  O   PRO A 242      23.592  56.971  15.459  1.00 16.61           O  
ANISOU 1739  O   PRO A 242     2250   2066   1993    194    -79    307       O  
ATOM   1740  CB  PRO A 242      23.888  54.041  16.612  1.00 19.56           C  
ANISOU 1740  CB  PRO A 242     2722   2352   2358    253    -55    443       C  
ATOM   1741  CG  PRO A 242      22.669  53.475  17.121  1.00 22.12           C  
ANISOU 1741  CG  PRO A 242     3080   2650   2673    212    -23    479       C  
ATOM   1742  CD  PRO A 242      21.813  54.607  17.646  1.00 18.52           C  
ANISOU 1742  CD  PRO A 242     2592   2263   2182    172    -21    451       C  
ATOM   1743  N   GLY A 243      25.737  56.682  16.019  1.00 16.78           N  
ANISOU 1743  N   GLY A 243     2252   2126   1997    281   -119    330       N  
ATOM   1744  CA  GLY A 243      26.234  57.509  14.940  1.00 16.18           C  
ANISOU 1744  CA  GLY A 243     2140   2054   1952    272   -127    276       C  
ATOM   1745  C   GLY A 243      25.779  57.010  13.579  1.00 15.68           C  
ANISOU 1745  C   GLY A 243     2100   1923   1936    251   -102    262       C  
ATOM   1746  O   GLY A 243      25.587  55.806  13.377  1.00 17.61           O  
ANISOU 1746  O   GLY A 243     2384   2109   2196    261    -86    291       O  
ATOM   1747  N   ASP A 244      25.521  57.957  12.680  1.00 15.01           N  
ANISOU 1747  N   ASP A 244     1990   1843   1867    219    -99    216       N  
ATOM   1748  CA  ASP A 244      24.963  57.677  11.344  1.00 14.88           C  
ANISOU 1748  CA  ASP A 244     1991   1777   1886    193    -79    194       C  
ATOM   1749  C   ASP A 244      23.570  57.083  11.355  1.00 15.72           C  
ANISOU 1749  C   ASP A 244     2130   1846   1995    155    -59    207       C  
ATOM   1750  O   ASP A 244      23.170  56.417  10.399  1.00 19.37           O  
ANISOU 1750  O   ASP A 244     2616   2259   2484    140    -44    196       O  
ATOM   1751  CB  ASP A 244      25.931  56.836  10.456  1.00 16.07           C  
ANISOU 1751  CB  ASP A 244     2151   1890   2062    230    -75    193       C  
ATOM   1752  CG  ASP A 244      25.602  56.914   8.966  1.00 17.86           C  
ANISOU 1752  CG  ASP A 244     2382   2087   2314    206    -60    156       C  
ATOM   1753  OD1 ASP A 244      24.960  57.825   8.529  1.00 20.13           O  
ANISOU 1753  OD1 ASP A 244     2655   2394   2600    171    -59    132       O  
ATOM   1754  OD2 ASP A 244      26.013  55.950   8.268  1.00 25.50           O  
ANISOU 1754  OD2 ASP A 244     3372   3012   3303    229    -48    154       O  
ATOM   1755  N   SER A 245      22.779  57.371  12.377  1.00 15.63           N  
ANISOU 1755  N   SER A 245     2118   1862   1957    134    -57    222       N  
ATOM   1756  CA  SER A 245      21.361  57.056  12.335  1.00 14.99           C  
ANISOU 1756  CA  SER A 245     2055   1759   1882     88    -35    226       C  
ATOM   1757  C   SER A 245      20.642  58.085  11.488  1.00 14.79           C  
ANISOU 1757  C   SER A 245     2002   1751   1867     56    -36    181       C  
ATOM   1758  O   SER A 245      21.024  59.257  11.489  1.00 15.32           O  
ANISOU 1758  O   SER A 245     2038   1857   1926     64    -51    157       O  
ATOM   1759  CB  SER A 245      20.746  57.092  13.721  1.00 15.40           C  
ANISOU 1759  CB  SER A 245     2109   1844   1897     79    -28    257       C  
ATOM   1760  OG  SER A 245      21.251  56.086  14.571  1.00 17.30           O  
ANISOU 1760  OG  SER A 245     2380   2070   2122    108    -25    309       O  
ATOM   1761  N   PHE A 246      19.594  57.670  10.802  1.00 14.04           N  
ANISOU 1761  N   PHE A 246     1917   1626   1791     18    -22    171       N  
ATOM   1762  CA  PHE A 246      18.714  58.524  10.004  1.00 13.41           C  
ANISOU 1762  CA  PHE A 246     1812   1563   1718    -10    -24    134       C  
ATOM   1763  C   PHE A 246      17.290  58.337  10.561  1.00 14.09           C  
ANISOU 1763  C   PHE A 246     1894   1658   1799    -50     -7    143       C  
ATOM   1764  O   PHE A 246      16.843  57.176  10.637  1.00 15.52           O  
ANISOU 1764  O   PHE A 246     2102   1801   1992    -73      9    162       O  
ATOM   1765  CB  PHE A 246      18.746  58.022   8.558  1.00 13.52           C  
ANISOU 1765  CB  PHE A 246     1839   1539   1758    -18    -23    111       C  
ATOM   1766  CG  PHE A 246      17.989  58.849   7.541  1.00 12.83           C  
ANISOU 1766  CG  PHE A 246     1728   1471   1675    -40    -31     76       C  
ATOM   1767  CD1 PHE A 246      17.771  60.201   7.681  1.00 12.91           C  
ANISOU 1767  CD1 PHE A 246     1706   1524   1674    -36    -41     65       C  
ATOM   1768  CD2 PHE A 246      17.527  58.226   6.384  1.00 12.53           C  
ANISOU 1768  CD2 PHE A 246     1702   1407   1652    -61    -29     54       C  
ATOM   1769  CE1 PHE A 246      17.150  60.974   6.663  1.00 12.79           C  
ANISOU 1769  CE1 PHE A 246     1671   1524   1662    -47    -49     40       C  
ATOM   1770  CE2 PHE A 246      16.924  58.976   5.374  1.00 13.79           C  
ANISOU 1770  CE2 PHE A 246     1839   1590   1808    -74    -40     25       C  
ATOM   1771  CZ  PHE A 246      16.722  60.330   5.511  1.00 12.48           C  
ANISOU 1771  CZ  PHE A 246     1643   1466   1632    -65    -50     22       C  
ATOM   1772  N   VAL A 247      16.649  59.431  10.993  1.00 13.84           N  
ANISOU 1772  N   VAL A 247     1830   1674   1752    -58    -10    128       N  
ATOM   1773  CA  VAL A 247      15.373  59.425  11.714  1.00 14.00           C  
ANISOU 1773  CA  VAL A 247     1836   1719   1761    -89      8    135       C  
ATOM   1774  C   VAL A 247      14.299  60.010  10.801  1.00 13.13           C  
ANISOU 1774  C   VAL A 247     1696   1622   1668   -114      4    101       C  
ATOM   1775  O   VAL A 247      14.490  61.037  10.136  1.00 13.65           O  
ANISOU 1775  O   VAL A 247     1743   1704   1739    -96    -13     74       O  
ATOM   1776  CB  VAL A 247      15.483  60.339  13.003  1.00 14.82           C  
ANISOU 1776  CB  VAL A 247     1923   1877   1831    -70      7    139       C  
ATOM   1777  CG1 VAL A 247      14.094  60.569  13.690  1.00 19.85           C  
ANISOU 1777  CG1 VAL A 247     2535   2551   2453    -98     29    137       C  
ATOM   1778  CG2 VAL A 247      16.509  59.644  13.985  1.00 19.43           C  
ANISOU 1778  CG2 VAL A 247     2535   2456   2389    -43      7    179       C  
ATOM   1779  N   GLY A 248      13.112  59.404  10.808  1.00 13.01           N  
ANISOU 1779  N   GLY A 248     1673   1606   1661   -155     22    103       N  
ATOM   1780  CA  GLY A 248      11.981  59.963  10.093  1.00 12.82           C  
ANISOU 1780  CA  GLY A 248     1611   1609   1649   -176     16     72       C  
ATOM   1781  C   GLY A 248      10.726  59.152  10.335  1.00 13.23           C  
ANISOU 1781  C   GLY A 248     1649   1665   1711   -228     40     78       C  
ATOM   1782  O   GLY A 248      10.702  58.271  11.167  1.00 13.61           O  
ANISOU 1782  O   GLY A 248     1720   1695   1754   -247     64    110       O  
ATOM   1783  N   PRO A 249       9.664  59.457   9.568  1.00 12.53           N  
ANISOU 1783  N   PRO A 249     1523   1602   1636   -251     32     47       N  
ATOM   1784  CA  PRO A 249       8.397  58.742   9.765  1.00 13.59           C  
ANISOU 1784  CA  PRO A 249     1632   1747   1782   -306     54     47       C  
ATOM   1785  C   PRO A 249       8.515  57.314   9.238  1.00 13.90           C  
ANISOU 1785  C   PRO A 249     1708   1725   1846   -347     61     52       C  
ATOM   1786  O   PRO A 249       9.159  57.039   8.219  1.00 14.50           O  
ANISOU 1786  O   PRO A 249     1809   1764   1933   -337     40     34       O  
ATOM   1787  CB  PRO A 249       7.416  59.558   8.932  1.00 14.07           C  
ANISOU 1787  CB  PRO A 249     1639   1855   1850   -308     33      9       C  
ATOM   1788  CG  PRO A 249       8.061  60.899   8.740  1.00 14.10           C  
ANISOU 1788  CG  PRO A 249     1638   1877   1840   -248     10      0       C  
ATOM   1789  CD  PRO A 249       9.517  60.580   8.628  1.00 13.27           C  
ANISOU 1789  CD  PRO A 249     1587   1722   1731   -224      3     16       C  
ATOM   1790  N   ARG A 250       7.884  56.392   9.950  1.00 14.18           N  
ANISOU 1790  N   ARG A 250     1748   1747   1892   -396     94     75       N  
ATOM   1791  CA  ARG A 250       7.995  54.952   9.661  1.00 14.82           C  
ANISOU 1791  CA  ARG A 250     1872   1756   2002   -439    108     85       C  
ATOM   1792  C   ARG A 250       7.722  54.613   8.201  1.00 14.47           C  
ANISOU 1792  C   ARG A 250     1821   1691   1983   -464     83     34       C  
ATOM   1793  O   ARG A 250       8.426  53.780   7.620  1.00 16.88           O  
ANISOU 1793  O   ARG A 250     2175   1932   2306   -464     79     28       O  
ATOM   1794  CB  ARG A 250       7.058  54.149  10.565  1.00 15.63           C  
ANISOU 1794  CB  ARG A 250     1966   1855   2115   -500    151    115       C  
ATOM   1795  CG  ARG A 250       7.003  52.657  10.265  1.00 16.82           C  
ANISOU 1795  CG  ARG A 250     2161   1924   2306   -554    170    123       C  
ATOM   1796  CD  ARG A 250       6.216  51.904  11.304  1.00 20.03           C  
ANISOU 1796  CD  ARG A 250     2568   2322   2721   -612    218    166       C  
ATOM   1797  NE  ARG A 250       6.099  50.502  10.942  1.00 23.69           N  
ANISOU 1797  NE  ARG A 250     3073   2697   3231   -670    237    169       N  
ATOM   1798  CZ  ARG A 250       5.174  49.685  11.448  1.00 28.33           C  
ANISOU 1798  CZ  ARG A 250     3655   3265   3844   -747    279    192       C  
ATOM   1799  NH1 ARG A 250       4.301  50.136  12.342  1.00 29.78           N  
ANISOU 1799  NH1 ARG A 250     3788   3520   4005   -770    308    215       N  
ATOM   1800  NH2 ARG A 250       5.098  48.422  11.029  1.00 33.06           N  
ANISOU 1800  NH2 ARG A 250     4296   3773   4492   -802    295    189       N  
ATOM   1801  N   PHE A 251       6.717  55.259   7.586  1.00 14.59           N  
ANISOU 1801  N   PHE A 251     1778   1766   1999   -481     65     -4       N  
ATOM   1802  CA  PHE A 251       6.320  54.944   6.205  1.00 14.32           C  
ANISOU 1802  CA  PHE A 251     1731   1727   1981   -509     38    -55       C  
ATOM   1803  C   PHE A 251       6.777  55.998   5.220  1.00 14.78           C  
ANISOU 1803  C   PHE A 251     1779   1821   2017   -453     -2    -81       C  
ATOM   1804  O   PHE A 251       6.169  56.184   4.142  1.00 16.36           O  
ANISOU 1804  O   PHE A 251     1947   2053   2215   -466    -30   -123       O  
ATOM   1805  CB  PHE A 251       4.823  54.637   6.120  1.00 14.48           C  
ANISOU 1805  CB  PHE A 251     1694   1785   2021   -578     44    -80       C  
ATOM   1806  CG  PHE A 251       4.445  53.455   6.969  1.00 15.19           C  
ANISOU 1806  CG  PHE A 251     1803   1828   2138   -642     89    -52       C  
ATOM   1807  CD1 PHE A 251       4.888  52.184   6.607  1.00 16.46           C  
ANISOU 1807  CD1 PHE A 251     2023   1902   2330   -676     98    -57       C  
ATOM   1808  CD2 PHE A 251       3.770  53.603   8.151  1.00 16.69           C  
ANISOU 1808  CD2 PHE A 251     1962   2054   2323   -662    124    -17       C  
ATOM   1809  CE1 PHE A 251       4.618  51.099   7.388  1.00 16.53           C  
ANISOU 1809  CE1 PHE A 251     2057   1855   2366   -732    142    -23       C  
ATOM   1810  CE2 PHE A 251       3.475  52.485   8.939  1.00 16.95           C  
ANISOU 1810  CE2 PHE A 251     2019   2039   2380   -723    170     17       C  
ATOM   1811  CZ  PHE A 251       3.902  51.238   8.521  1.00 16.83           C  
ANISOU 1811  CZ  PHE A 251     2063   1931   2398   -758    177     15       C  
ATOM   1812  N   GLY A 252       7.809  56.707   5.603  1.00 14.18           N  
ANISOU 1812  N   GLY A 252     1725   1740   1920   -394     -4    -55       N  
ATOM   1813  CA  GLY A 252       8.456  57.695   4.719  1.00 14.45           C  
ANISOU 1813  CA  GLY A 252     1759   1796   1935   -340    -35    -70       C  
ATOM   1814  C   GLY A 252       7.770  59.029   4.734  1.00 13.97           C  
ANISOU 1814  C   GLY A 252     1644   1802   1859   -315    -51    -75       C  
ATOM   1815  O   GLY A 252       8.294  60.030   5.249  1.00 15.73           O  
ANISOU 1815  O   GLY A 252     1867   2038   2069   -269    -51    -57       O  
ATOM   1816  N   TYR A 253       6.561  59.071   4.240  1.00 14.33           N  
ANISOU 1816  N   TYR A 253     1643   1891   1911   -345    -63   -102       N  
ATOM   1817  CA  TYR A 253       5.801  60.305   4.156  1.00 14.63           C  
ANISOU 1817  CA  TYR A 253     1626   1994   1937   -315    -81   -109       C  
ATOM   1818  C   TYR A 253       5.082  60.658   5.457  1.00 14.64           C  
ANISOU 1818  C   TYR A 253     1590   2027   1943   -321    -53    -93       C  
ATOM   1819  O   TYR A 253       4.914  61.821   5.796  1.00 15.75           O  
ANISOU 1819  O   TYR A 253     1705   2204   2075   -277    -57    -88       O  
ATOM   1820  CB  TYR A 253       4.831  60.189   2.990  1.00 15.88           C  
ANISOU 1820  CB  TYR A 253     1744   2194   2096   -339   -112   -146       C  
ATOM   1821  CG  TYR A 253       5.528  59.974   1.669  1.00 17.35           C  
ANISOU 1821  CG  TYR A 253     1965   2359   2267   -327   -139   -165       C  
ATOM   1822  CD1 TYR A 253       5.885  61.059   0.909  1.00 23.81           C  
ANISOU 1822  CD1 TYR A 253     2781   3201   3061   -271   -166   -160       C  
ATOM   1823  CD2 TYR A 253       5.818  58.705   1.198  1.00 17.46           C  
ANISOU 1823  CD2 TYR A 253     2013   2328   2290   -370   -135   -187       C  
ATOM   1824  CE1 TYR A 253       6.543  60.900  -0.293  1.00 28.41           C  
ANISOU 1824  CE1 TYR A 253     3396   3773   3623   -259   -186   -175       C  
ATOM   1825  CE2 TYR A 253       6.471  58.514  -0.003  1.00 29.27           C  
ANISOU 1825  CE2 TYR A 253     3542   3811   3768   -355   -157   -209       C  
ATOM   1826  CZ  TYR A 253       6.822  59.624  -0.740  1.00 27.82           C  
ANISOU 1826  CZ  TYR A 253     3354   3661   3554   -300   -182   -201       C  
ATOM   1827  OH  TYR A 253       7.454  59.474  -1.989  1.00 34.82           O  
ANISOU 1827  OH  TYR A 253     4271   4544   4414   -285   -201   -222       O  
ATOM   1828  N   LEU A 254       4.599  59.626   6.153  1.00 14.24           N  
ANISOU 1828  N   LEU A 254     1538   1965   1907   -376    -23    -86       N  
ATOM   1829  CA  LEU A 254       3.836  59.682   7.398  1.00 14.18           C  
ANISOU 1829  CA  LEU A 254     1496   1991   1901   -395     11    -69       C  
ATOM   1830  C   LEU A 254       4.261  58.489   8.260  1.00 14.98           C  
ANISOU 1830  C   LEU A 254     1644   2038   2008   -435     49    -37       C  
ATOM   1831  O   LEU A 254       4.922  57.552   7.762  1.00 15.11           O  
ANISOU 1831  O   LEU A 254     1710   1992   2037   -454     45    -35       O  
ATOM   1832  CB  LEU A 254       2.334  59.616   7.165  1.00 13.84           C  
ANISOU 1832  CB  LEU A 254     1378   2007   1871   -436     10    -96       C  
ATOM   1833  CG  LEU A 254       1.690  60.827   6.469  1.00 15.19           C  
ANISOU 1833  CG  LEU A 254     1493   2243   2036   -391    -24   -122       C  
ATOM   1834  CD1 LEU A 254       0.239  60.493   6.120  1.00 16.68           C  
ANISOU 1834  CD1 LEU A 254     1605   2491   2241   -440    -29   -152       C  
ATOM   1835  CD2 LEU A 254       1.765  62.102   7.366  1.00 16.66           C  
ANISOU 1835  CD2 LEU A 254     1664   2458   2207   -329    -12   -108       C  
ATOM   1836  N   GLY A 255       3.800  58.484   9.508  1.00 15.27           N  
ANISOU 1836  N   GLY A 255     1663   2101   2037   -449     86    -12       N  
ATOM   1837  CA  GLY A 255       4.114  57.420  10.436  1.00 15.56           C  
ANISOU 1837  CA  GLY A 255     1743   2093   2074   -484    125     28       C  
ATOM   1838  C   GLY A 255       4.894  57.867  11.651  1.00 15.53           C  
ANISOU 1838  C   GLY A 255     1769   2094   2037   -439    143     65       C  
ATOM   1839  O   GLY A 255       5.411  58.983  11.707  1.00 15.39           O  
ANISOU 1839  O   GLY A 255     1747   2100   1998   -380    123     54       O  
ATOM   1840  N   ARG A 256       5.014  56.959  12.622  1.00 16.11           N  
ANISOU 1840  N   ARG A 256     1874   2141   2103   -468    181    109       N  
ATOM   1841  CA AARG A 256       5.735  57.232  13.869  0.50 16.44           C  
ANISOU 1841  CA AARG A 256     1946   2193   2104   -429    199    148       C  
ATOM   1842  CA BARG A 256       5.704  57.350  13.844  0.50 16.99           C  
ANISOU 1842  CA BARG A 256     2012   2269   2174   -425    197    145       C  
ATOM   1843  C   ARG A 256       7.209  57.504  13.629  1.00 14.95           C  
ANISOU 1843  C   ARG A 256     1806   1967   1906   -371    167    152       C  
ATOM   1844  O   ARG A 256       7.819  56.927  12.718  1.00 15.17           O  
ANISOU 1844  O   ARG A 256     1867   1937   1958   -372    147    146       O  
ATOM   1845  CB AARG A 256       5.616  56.049  14.829  0.50 17.48           C  
ANISOU 1845  CB AARG A 256     2111   2298   2231   -472    245    204       C  
ATOM   1846  CB BARG A 256       5.373  56.441  15.022  0.50 19.40           C  
ANISOU 1846  CB BARG A 256     2335   2572   2465   -465    247    197       C  
ATOM   1847  CG AARG A 256       6.198  54.740  14.395  0.50 21.09           C  
ANISOU 1847  CG AARG A 256     2628   2665   2719   -498    246    229       C  
ATOM   1848  CG BARG A 256       6.068  55.125  15.166  0.50 22.95           C  
ANISOU 1848  CG BARG A 256     2852   2941   2926   -486    261    245       C  
ATOM   1849  CD AARG A 256       5.845  53.651  15.448  0.50 26.22           C  
ANISOU 1849  CD AARG A 256     3306   3292   3364   -545    299    292       C  
ATOM   1850  CD BARG A 256       5.336  54.423  16.345  0.50 27.40           C  
ANISOU 1850  CD BARG A 256     3416   3521   3474   -534    318    297       C  
ATOM   1851  NE AARG A 256       6.382  53.970  16.779  0.50 29.90           N  
ANISOU 1851  NE AARG A 256     3793   3794   3774   -502    316    339       N  
ATOM   1852  NE BARG A 256       3.982  54.971  16.407  0.50 32.31           N  
ANISOU 1852  NE BARG A 256     3962   4217   4099   -569    337    265       N  
ATOM   1853  CZ AARG A 256       5.848  53.572  17.938  0.50 34.02           C  
ANISOU 1853  CZ AARG A 256     4315   4342   4266   -531    365    389       C  
ATOM   1854  CZ BARG A 256       3.026  54.615  17.261  0.50 35.14           C  
ANISOU 1854  CZ BARG A 256     4293   4613   4446   -618    389    294       C  
ATOM   1855  NH1AARG A 256       4.738  52.853  17.967  0.50 36.12           N  
ANISOU 1855  NH1AARG A 256     4560   4602   4561   -608    406    401       N  
ATOM   1856  NH1BARG A 256       3.242  53.704  18.206  0.50 35.60           N  
ANISOU 1856  NH1BARG A 256     4398   4640   4485   -641    431    362       N  
ATOM   1857  NH2AARG A 256       6.422  53.912  19.084  0.50 34.40           N  
ANISOU 1857  NH2AARG A 256     4384   4429   4255   -486    374    427       N  
ATOM   1858  NH2BARG A 256       1.841  55.203  17.184  0.50 38.05           N  
ANISOU 1858  NH2BARG A 256     4582   5053   4819   -641    401    256       N  
ATOM   1859  N   THR A 257       7.795  58.336  14.475  1.00 15.04           N  
ANISOU 1859  N   THR A 257     1820   2012   1879   -322    164    160       N  
ATOM   1860  CA  THR A 257       9.228  58.693  14.366  1.00 14.48           C  
ANISOU 1860  CA  THR A 257     1788   1917   1797   -268    134    162       C  
ATOM   1861  C   THR A 257      10.114  57.574  14.882  1.00 15.79           C  
ANISOU 1861  C   THR A 257     2011   2033   1954   -266    145    212       C  
ATOM   1862  O   THR A 257       9.928  57.033  15.978  1.00 17.14           O  
ANISOU 1862  O   THR A 257     2196   2214   2099   -279    176    256       O  
ATOM   1863  CB  THR A 257       9.476  59.986  15.152  1.00 14.38           C  
ANISOU 1863  CB  THR A 257     1754   1960   1748   -223    127    147       C  
ATOM   1864  OG1 THR A 257       8.682  61.039  14.607  1.00 15.12           O  
ANISOU 1864  OG1 THR A 257     1799   2090   1856   -217    117    102       O  
ATOM   1865  CG2 THR A 257      10.955  60.363  15.107  1.00 16.22           C  
ANISOU 1865  CG2 THR A 257     2019   2172   1970   -175     98    147       C  
ATOM   1866  N   GLN A 258      11.058  57.170  14.056  1.00 14.87           N  
ANISOU 1866  N   GLN A 258     1926   1861   1859   -248    121    209       N  
ATOM   1867  CA  GLN A 258      11.964  56.065  14.367  1.00 15.18           C  
ANISOU 1867  CA  GLN A 258     2021   1845   1900   -238    128    254       C  
ATOM   1868  C   GLN A 258      13.178  56.126  13.441  1.00 15.37           C  
ANISOU 1868  C   GLN A 258     2066   1832   1941   -198     95    235       C  
ATOM   1869  O   GLN A 258      13.177  56.836  12.434  1.00 14.76           O  
ANISOU 1869  O   GLN A 258     1965   1764   1879   -191     72    191       O  
ATOM   1870  CB  GLN A 258      11.251  54.708  14.212  1.00 16.97           C  
ANISOU 1870  CB  GLN A 258     2271   2016   2158   -294    158    279       C  
ATOM   1871  CG  GLN A 258      10.662  54.513  12.800  1.00 17.89           C  
ANISOU 1871  CG  GLN A 258     2372   2105   2320   -332    146    229       C  
ATOM   1872  CD  GLN A 258      10.171  53.144  12.492  1.00 25.82           C  
ANISOU 1872  CD  GLN A 258     3406   3042   3363   -388    170    242       C  
ATOM   1873  OE1 GLN A 258       9.241  52.728  13.072  1.00 25.50           O  
ANISOU 1873  OE1 GLN A 258     3353   3008   3325   -437    202    263       O  
ATOM   1874  NE2 GLN A 258      10.793  52.472  11.525  1.00 28.72           N  
ANISOU 1874  NE2 GLN A 258     3808   3342   3761   -382    155    224       N  
ATOM   1875  N   PRO A 259      14.232  55.369  13.738  1.00 15.48           N  
ANISOU 1875  N   PRO A 259     2123   1805   1952   -168     93    271       N  
ATOM   1876  CA  PRO A 259      15.261  55.147  12.727  1.00 14.71           C  
ANISOU 1876  CA  PRO A 259     2044   1663   1878   -137     70    252       C  
ATOM   1877  C   PRO A 259      14.669  54.497  11.477  1.00 14.42           C  
ANISOU 1877  C   PRO A 259     2015   1578   1884   -177     74    221       C  
ATOM   1878  O   PRO A 259      13.849  53.574  11.575  1.00 16.78           O  
ANISOU 1878  O   PRO A 259     2330   1841   2203   -224     99    235       O  
ATOM   1879  CB  PRO A 259      16.230  54.190  13.449  1.00 16.83           C  
ANISOU 1879  CB  PRO A 259     2360   1895   2140   -103     76    305       C  
ATOM   1880  CG  PRO A 259      16.038  54.526  14.902  1.00 17.48           C  
ANISOU 1880  CG  PRO A 259     2435   2032   2175    -96     86    343       C  
ATOM   1881  CD  PRO A 259      14.542  54.632  14.977  1.00 17.05           C  
ANISOU 1881  CD  PRO A 259     2355   1996   2124   -156    112    333       C  
ATOM   1882  N   VAL A 260      15.106  54.992  10.318  1.00 14.98           N  
ANISOU 1882  N   VAL A 260     2075   1649   1967   -160     51    178       N  
ATOM   1883  CA  VAL A 260      14.583  54.551   9.029  1.00 14.49           C  
ANISOU 1883  CA  VAL A 260     2014   1555   1934   -193     48    138       C  
ATOM   1884  C   VAL A 260      15.741  54.207   8.080  1.00 15.15           C  
ANISOU 1884  C   VAL A 260     2124   1600   2031   -157     35    120       C  
ATOM   1885  O   VAL A 260      16.898  54.468   8.390  1.00 16.25           O  
ANISOU 1885  O   VAL A 260     2270   1745   2158   -106     26    137       O  
ATOM   1886  CB  VAL A 260      13.673  55.600   8.395  1.00 14.04           C  
ANISOU 1886  CB  VAL A 260     1908   1553   1871   -214     34     98       C  
ATOM   1887  CG1 VAL A 260      12.405  55.788   9.246  1.00 16.36           C  
ANISOU 1887  CG1 VAL A 260     2172   1885   2159   -253     52    110       C  
ATOM   1888  CG2 VAL A 260      14.409  56.928   8.168  1.00 14.80           C  
ANISOU 1888  CG2 VAL A 260     1982   1693   1948   -167     10     85       C  
ATOM   1889  N   GLY A 261      15.395  53.586   6.972  1.00 16.08           N  
ANISOU 1889  N   GLY A 261     2254   1682   2173   -184     35     83       N  
ATOM   1890  CA  GLY A 261      16.359  53.218   5.944  1.00 15.59           C  
ANISOU 1890  CA  GLY A 261     2216   1586   2121   -152     26     57       C  
ATOM   1891  C   GLY A 261      16.633  54.331   4.957  1.00 14.89           C  
ANISOU 1891  C   GLY A 261     2095   1548   2012   -133      4     22       C  
ATOM   1892  O   GLY A 261      16.117  55.451   5.052  1.00 15.78           O  
ANISOU 1892  O   GLY A 261     2169   1717   2107   -139     -6     19       O  
ATOM   1893  N   ARG A 262      17.535  54.024   4.036  1.00 14.86           N  
ANISOU 1893  N   ARG A 262     2111   1522   2013   -103      1      0       N  
ATOM   1894  CA  ARG A 262      17.965  54.975   3.013  1.00 13.81           C  
ANISOU 1894  CA  ARG A 262     1954   1431   1859    -82    -13    -28       C  
ATOM   1895  C   ARG A 262      18.344  54.198   1.728  1.00 13.99           C  
ANISOU 1895  C   ARG A 262     2004   1422   1888    -77    -10    -70       C  
ATOM   1896  O   ARG A 262      18.434  52.965   1.726  1.00 15.54           O  
ANISOU 1896  O   ARG A 262     2237   1556   2109    -82      3    -78       O  
ATOM   1897  CB  ARG A 262      19.146  55.828   3.501  1.00 13.92           C  
ANISOU 1897  CB  ARG A 262     1952   1474   1860    -33    -17     -2       C  
ATOM   1898  CG  ARG A 262      20.439  55.053   3.677  1.00 14.05           C  
ANISOU 1898  CG  ARG A 262     1994   1454   1888     10     -7      9       C  
ATOM   1899  CD  ARG A 262      21.476  55.881   4.429  1.00 16.52           C  
ANISOU 1899  CD  ARG A 262     2282   1803   2189     49    -15     37       C  
ATOM   1900  NE  ARG A 262      21.194  55.804   5.854  1.00 16.76           N  
ANISOU 1900  NE  ARG A 262     2314   1837   2217     45    -15     75       N  
ATOM   1901  CZ  ARG A 262      21.967  56.336   6.815  1.00 18.76           C  
ANISOU 1901  CZ  ARG A 262     2549   2121   2456     76    -24    101       C  
ATOM   1902  NH1 ARG A 262      23.022  57.059   6.515  1.00 18.91           N  
ANISOU 1902  NH1 ARG A 262     2543   2169   2470    105    -33     91       N  
ATOM   1903  NH2 ARG A 262      21.646  56.069   8.075  1.00 20.54           N  
ANISOU 1903  NH2 ARG A 262     2783   2348   2672     72    -22    136       N  
ATOM   1904  N   SER A 263      18.564  54.929   0.642  1.00 14.22           N  
ANISOU 1904  N   SER A 263     2016   1492   1894    -65    -21    -97       N  
ATOM   1905  CA  SER A 263      18.807  54.321  -0.649  1.00 14.42           C  
ANISOU 1905  CA  SER A 263     2062   1501   1913    -62    -18   -143       C  
ATOM   1906  C   SER A 263      20.149  53.580  -0.719  1.00 14.28           C  
ANISOU 1906  C   SER A 263     2072   1442   1909    -15      0   -144       C  
ATOM   1907  O   SER A 263      21.071  53.819   0.074  1.00 15.18           O  
ANISOU 1907  O   SER A 263     2180   1557   2030     22      4   -107       O  
ATOM   1908  CB  SER A 263      18.778  55.381  -1.752  1.00 14.70           C  
ANISOU 1908  CB  SER A 263     2072   1599   1912    -55    -32   -162       C  
ATOM   1909  OG  SER A 263      19.967  56.174  -1.715  1.00 13.93           O  
ANISOU 1909  OG  SER A 263     1962   1527   1804    -12    -26   -138       O  
ATOM   1910  N   ARG A 264      20.256  52.689  -1.700  1.00 15.29           N  
ANISOU 1910  N   ARG A 264     2229   1538   2040    -15      7   -191       N  
ATOM   1911  CA  ARG A 264      21.485  51.970  -1.941  1.00 17.33           C  
ANISOU 1911  CA  ARG A 264     2513   1760   2311     34     26   -201       C  
ATOM   1912  C   ARG A 264      22.621  52.951  -2.245  1.00 15.92           C  
ANISOU 1912  C   ARG A 264     2304   1638   2107     79     29   -187       C  
ATOM   1913  O   ARG A 264      23.725  52.808  -1.737  1.00 17.51           O  
ANISOU 1913  O   ARG A 264     2502   1827   2321    125     40   -164       O  
ATOM   1914  CB  ARG A 264      21.305  50.980  -3.086  1.00 19.96           C  
ANISOU 1914  CB  ARG A 264     2880   2056   2646     23     34   -266       C  
ATOM   1915  CG  ARG A 264      20.349  49.849  -2.769  1.00 25.37           C  
ANISOU 1915  CG  ARG A 264     3599   2670   3368    -23     36   -284       C  
ATOM   1916  CD  ARG A 264      20.009  49.108  -4.087  1.00 34.27           C  
ANISOU 1916  CD  ARG A 264     4753   3779   4488    -45     38   -363       C  
ATOM   1917  NE  ARG A 264      19.116  47.970  -3.867  1.00 41.93           N  
ANISOU 1917  NE  ARG A 264     5757   4673   5500    -97     42   -388       N  
ATOM   1918  CZ  ARG A 264      18.244  47.487  -4.756  1.00 48.20           C  
ANISOU 1918  CZ  ARG A 264     6562   5462   6290   -149     32   -456       C  
ATOM   1919  NH1 ARG A 264      18.097  48.048  -5.964  1.00 50.85           N  
ANISOU 1919  NH1 ARG A 264     6876   5869   6574   -151     15   -505       N  
ATOM   1920  NH2 ARG A 264      17.495  46.432  -4.431  1.00 50.30           N  
ANISOU 1920  NH2 ARG A 264     6858   5650   6602   -201     40   -475       N  
ATOM   1921  N   ARG A 265      22.341  53.980  -3.053  1.00 15.71           N  
ANISOU 1921  N   ARG A 265     2251   1673   2044     66     18   -199       N  
ATOM   1922  CA  ARG A 265      23.379  54.978  -3.335  1.00 15.10           C  
ANISOU 1922  CA  ARG A 265     2143   1647   1945    100     25   -181       C  
ATOM   1923  C   ARG A 265      23.816  55.757  -2.102  1.00 15.39           C  
ANISOU 1923  C   ARG A 265     2152   1698   1996    112     19   -130       C  
ATOM   1924  O   ARG A 265      24.968  56.150  -1.976  1.00 15.46           O  
ANISOU 1924  O   ARG A 265     2140   1727   2005    146     29   -114       O  
ATOM   1925  CB  ARG A 265      22.949  55.905  -4.472  1.00 15.41           C  
ANISOU 1925  CB  ARG A 265     2167   1745   1942     83     17   -196       C  
ATOM   1926  CG  ARG A 265      22.981  55.184  -5.787  1.00 16.53           C  
ANISOU 1926  CG  ARG A 265     2334   1887   2060     86     27   -251       C  
ATOM   1927  CD  ARG A 265      22.845  56.084  -7.004  1.00 21.02           C  
ANISOU 1927  CD  ARG A 265     2889   2522   2576     82     24   -260       C  
ATOM   1928  NE  ARG A 265      21.521  56.653  -7.140  1.00 22.09           N  
ANISOU 1928  NE  ARG A 265     3014   2685   2692     44     -5   -257       N  
ATOM   1929  CZ  ARG A 265      20.483  56.100  -7.777  1.00 22.26           C  
ANISOU 1929  CZ  ARG A 265     3049   2710   2697     13    -22   -300       C  
ATOM   1930  NH1 ARG A 265      19.342  56.782  -7.887  1.00 22.35           N  
ANISOU 1930  NH1 ARG A 265     3040   2759   2690    -14    -51   -291       N  
ATOM   1931  NH2 ARG A 265      20.555  54.893  -8.338  1.00 24.20           N  
ANISOU 1931  NH2 ARG A 265     3326   2924   2943     11    -14   -357       N  
ATOM   1932  N   ALA A 266      22.905  55.986  -1.161  1.00 13.85           N  
ANISOU 1932  N   ALA A 266     1953   1498   1811     82      4   -106       N  
ATOM   1933  CA  ALA A 266      23.296  56.623   0.101  1.00 13.61           C  
ANISOU 1933  CA  ALA A 266     1899   1481   1791     94     -1    -64       C  
ATOM   1934  C   ALA A 266      24.182  55.751   0.975  1.00 14.70           C  
ANISOU 1934  C   ALA A 266     2050   1584   1951    130      6    -44       C  
ATOM   1935  O   ALA A 266      24.836  56.278   1.880  1.00 16.56           O  
ANISOU 1935  O   ALA A 266     2261   1840   2188    150      0    -15       O  
ATOM   1936  CB  ALA A 266      22.021  57.061   0.900  1.00 14.09           C  
ANISOU 1936  CB  ALA A 266     1951   1549   1851     55    -16    -47       C  
ATOM   1937  N   LYS A 267      24.214  54.447   0.721  1.00 15.55           N  
ANISOU 1937  N   LYS A 267     2195   1637   2076    140     18    -61       N  
ATOM   1938  CA  LYS A 267      25.052  53.502   1.471  1.00 16.36           C  
ANISOU 1938  CA  LYS A 267     2315   1698   2203    184     26    -39       C  
ATOM   1939  C   LYS A 267      26.386  53.215   0.812  1.00 17.58           C  
ANISOU 1939  C   LYS A 267     2463   1855   2361    238     40    -57       C  
ATOM   1940  O   LYS A 267      27.119  52.346   1.279  1.00 20.86           O  
ANISOU 1940  O   LYS A 267     2894   2234   2798    283     47    -43       O  
ATOM   1941  CB  LYS A 267      24.260  52.211   1.765  1.00 16.87           C  
ANISOU 1941  CB  LYS A 267     2428   1688   2292    164     33    -39       C  
ATOM   1942  CG  LYS A 267      23.057  52.501   2.671  1.00 19.29           C  
ANISOU 1942  CG  LYS A 267     2732   2000   2596    114     23    -12       C  
ATOM   1943  CD  LYS A 267      22.297  51.260   3.092  1.00 25.95           C  
ANISOU 1943  CD  LYS A 267     3620   2770   3468     88     35     -3       C  
ATOM   1944  CE  LYS A 267      21.074  51.005   2.279  1.00 27.93           C  
ANISOU 1944  CE  LYS A 267     3882   3007   3723     28     36    -46       C  
ATOM   1945  NZ  LYS A 267      20.273  49.876   2.883  1.00 31.11           N  
ANISOU 1945  NZ  LYS A 267     4324   3338   4158     -8     50    -31       N  
ATOM   1946  N   ASP A 268      26.730  53.936  -0.257  1.00 16.18           N  
ANISOU 1946  N   ASP A 268     2262   1724   2161    237     46    -85       N  
ATOM   1947  CA  ASP A 268      27.975  53.725  -0.992  1.00 16.68           C  
ANISOU 1947  CA  ASP A 268     2313   1800   2224    286     66   -106       C  
ATOM   1948  C   ASP A 268      29.111  54.489  -0.291  1.00 16.28           C  
ANISOU 1948  C   ASP A 268     2212   1796   2174    317     61    -73       C  
ATOM   1949  O   ASP A 268      29.199  55.714  -0.361  1.00 16.37           O  
ANISOU 1949  O   ASP A 268     2187   1861   2169    295     56    -64       O  
ATOM   1950  CB  ASP A 268      27.791  54.183  -2.439  1.00 16.53           C  
ANISOU 1950  CB  ASP A 268     2290   1815   2173    266     77   -145       C  
ATOM   1951  CG  ASP A 268      28.995  53.873  -3.331  1.00 20.65           C  
ANISOU 1951  CG  ASP A 268     2801   2353   2689    314    105   -174       C  
ATOM   1952  OD1 ASP A 268      30.127  53.841  -2.863  1.00 17.74           O  
ANISOU 1952  OD1 ASP A 268     2406   1997   2337    359    113   -157       O  
ATOM   1953  OD2 ASP A 268      28.791  53.748  -4.565  1.00 26.86           O  
ANISOU 1953  OD2 ASP A 268     3603   3152   3450    306    119   -216       O  
ATOM   1954  N   ALA A 269      29.951  53.757   0.436  1.00 16.52           N  
ANISOU 1954  N   ALA A 269     2241   1806   2227    368     62    -55       N  
ATOM   1955  CA  ALA A 269      31.003  54.369   1.216  1.00 14.80           C  
ANISOU 1955  CA  ALA A 269     1973   1636   2011    397     51    -28       C  
ATOM   1956  C   ALA A 269      32.078  55.002   0.344  1.00 15.37           C  
ANISOU 1956  C   ALA A 269     1999   1763   2075    415     70    -48       C  
ATOM   1957  O   ALA A 269      32.635  56.029   0.714  1.00 15.97           O  
ANISOU 1957  O   ALA A 269     2026   1894   2147    406     61    -34       O  
ATOM   1958  CB  ALA A 269      31.646  53.320   2.170  1.00 17.60           C  
ANISOU 1958  CB  ALA A 269     2339   1957   2389    456     45     -1       C  
ATOM   1959  N   GLY A 270      32.373  54.403  -0.800  1.00 15.67           N  
ANISOU 1959  N   GLY A 270     2051   1789   2111    436     97    -85       N  
ATOM   1960  CA  GLY A 270      33.305  55.016  -1.735  1.00 15.53           C  
ANISOU 1960  CA  GLY A 270     1990   1829   2080    447    122   -104       C  
ATOM   1961  C   GLY A 270      32.840  56.360  -2.257  1.00 14.81           C  
ANISOU 1961  C   GLY A 270     1881   1782   1962    389    122   -101       C  
ATOM   1962  O   GLY A 270      33.615  57.299  -2.341  1.00 15.05           O  
ANISOU 1962  O   GLY A 270     1863   1866   1990    384    131    -91       O  
ATOM   1963  N   MET A 271      31.567  56.443  -2.612  1.00 14.68           N  
ANISOU 1963  N   MET A 271     1906   1742   1929    347    114   -108       N  
ATOM   1964  CA  MET A 271      31.026  57.718  -3.057  1.00 14.28           C  
ANISOU 1964  CA  MET A 271     1842   1728   1853    298    111    -98       C  
ATOM   1965  C   MET A 271      30.998  58.734  -1.928  1.00 13.76           C  
ANISOU 1965  C   MET A 271     1746   1680   1802    275     87    -63       C  
ATOM   1966  O   MET A 271      31.287  59.900  -2.155  1.00 14.07           O  
ANISOU 1966  O   MET A 271     1754   1758   1834    252     93    -51       O  
ATOM   1967  CB  MET A 271      29.631  57.568  -3.670  1.00 14.92           C  
ANISOU 1967  CB  MET A 271     1967   1786   1913    262    102   -115       C  
ATOM   1968  CG  MET A 271      29.050  58.861  -4.195  1.00 14.82           C  
ANISOU 1968  CG  MET A 271     1943   1811   1874    221     97   -101       C  
ATOM   1969  SD  MET A 271      30.011  59.620  -5.528  1.00 16.57           S  
ANISOU 1969  SD  MET A 271     2139   2091   2064    228    134   -104       S  
ATOM   1970  CE  MET A 271      29.466  58.635  -6.832  1.00 19.36           C  
ANISOU 1970  CE  MET A 271     2536   2437   2381    236    145   -151       C  
ATOM   1971  N   ALA A 272      30.685  58.325  -0.703  1.00 13.65           N  
ANISOU 1971  N   ALA A 272     1741   1638   1805    280     63    -46       N  
ATOM   1972  CA  ALA A 272      30.705  59.280   0.398  1.00 12.86           C  
ANISOU 1972  CA  ALA A 272     1612   1560   1713    261     41    -20       C  
ATOM   1973  C   ALA A 272      32.103  59.886   0.572  1.00 13.67           C  
ANISOU 1973  C   ALA A 272     1658   1709   1826    278     48    -16       C  
ATOM   1974  O   ALA A 272      32.265  61.093   0.781  1.00 14.20           O  
ANISOU 1974  O   ALA A 272     1693   1806   1895    248     43     -8       O  
ATOM   1975  CB  ALA A 272      30.252  58.587   1.706  1.00 14.50           C  
ANISOU 1975  CB  ALA A 272     1839   1737   1930    271     18     -2       C  
ATOM   1976  N   ALA A 273      33.144  59.054   0.520  1.00 13.76           N  
ANISOU 1976  N   ALA A 273     1652   1726   1847    328     59    -23       N  
ATOM   1977  CA  ALA A 273      34.484  59.506   0.630  1.00 13.62           C  
ANISOU 1977  CA  ALA A 273     1574   1758   1842    346     66    -23       C  
ATOM   1978  C   ALA A 273      34.959  60.381  -0.554  1.00 14.55           C  
ANISOU 1978  C   ALA A 273     1663   1913   1951    321     99    -34       C  
ATOM   1979  O   ALA A 273      35.650  61.388  -0.337  1.00 14.50           O  
ANISOU 1979  O   ALA A 273     1606   1948   1955    299    100    -27       O  
ATOM   1980  CB  ALA A 273      35.431  58.300   0.920  1.00 15.17           C  
ANISOU 1980  CB  ALA A 273     1758   1951   2053    415     68    -26       C  
ATOM   1981  N   ALA A 274      34.547  60.034  -1.794  1.00 14.33           N  
ANISOU 1981  N   ALA A 274     1669   1871   1902    320    125    -50       N  
ATOM   1982  CA  ALA A 274      34.889  60.832  -2.967  1.00 13.98           C  
ANISOU 1982  CA  ALA A 274     1607   1864   1840    297    159    -54       C  
ATOM   1983  C   ALA A 274      34.186  62.184  -2.939  1.00 13.56           C  
ANISOU 1983  C   ALA A 274     1556   1813   1781    239    150    -32       C  
ATOM   1984  O   ALA A 274      34.798  63.220  -3.216  1.00 13.47           O  
ANISOU 1984  O   ALA A 274     1507   1835   1774    213    168    -20       O  
ATOM   1985  CB  ALA A 274      34.476  60.083  -4.257  1.00 14.85           C  
ANISOU 1985  CB  ALA A 274     1759   1961   1919    311    185    -79       C  
ATOM   1986  N   LEU A 275      32.908  62.179  -2.557  1.00 13.53           N  
ANISOU 1986  N   LEU A 275     1595   1773   1771    220    122    -26       N  
ATOM   1987  CA  LEU A 275      32.151  63.432  -2.433  1.00 13.61           C  
ANISOU 1987  CA  LEU A 275     1610   1781   1779    174    110     -7       C  
ATOM   1988  C   LEU A 275      32.786  64.343  -1.383  1.00 13.57           C  
ANISOU 1988  C   LEU A 275     1561   1791   1804    156     97      4       C  
ATOM   1989  O   LEU A 275      32.824  65.559  -1.556  1.00 13.93           O  
ANISOU 1989  O   LEU A 275     1591   1844   1856    120    105     17       O  
ATOM   1990  CB  LEU A 275      30.678  63.163  -2.093  1.00 13.90           C  
ANISOU 1990  CB  LEU A 275     1692   1781   1807    162     83     -6       C  
ATOM   1991  CG  LEU A 275      29.852  64.422  -1.791  1.00 13.22           C  
ANISOU 1991  CG  LEU A 275     1608   1689   1723    124     67     11       C  
ATOM   1992  CD1 LEU A 275      29.689  65.335  -3.019  1.00 14.22           C  
ANISOU 1992  CD1 LEU A 275     1741   1831   1830    104     88     25       C  
ATOM   1993  CD2 LEU A 275      28.487  63.974  -1.268  1.00 15.29           C  
ANISOU 1993  CD2 LEU A 275     1905   1922   1981    118     40      8       C  
ATOM   1994  N   TRP A 276      33.271  63.763  -0.280  1.00 13.14           N  
ANISOU 1994  N   TRP A 276     1487   1739   1766    181     77     -1       N  
ATOM   1995  CA  TRP A 276      33.948  64.552   0.730  1.00 13.06           C  
ANISOU 1995  CA  TRP A 276     1431   1752   1779    166     60      1       C  
ATOM   1996  C   TRP A 276      35.160  65.272   0.167  1.00 13.59           C  
ANISOU 1996  C   TRP A 276     1444   1858   1860    151     89      0       C  
ATOM   1997  O   TRP A 276      35.370  66.479   0.408  1.00 13.63           O  
ANISOU 1997  O   TRP A 276     1423   1872   1883    109     88      3       O  
ATOM   1998  CB  TRP A 276      34.344  63.649   1.913  1.00 13.32           C  
ANISOU 1998  CB  TRP A 276     1450   1790   1818    205     33     -1       C  
ATOM   1999  CG  TRP A 276      34.820  64.444   3.094  1.00 13.34           C  
ANISOU 1999  CG  TRP A 276     1411   1821   1836    188      6     -3       C  
ATOM   2000  CD1 TRP A 276      36.037  65.039   3.248  1.00 13.97           C  
ANISOU 2000  CD1 TRP A 276     1427   1945   1934    179     10    -13       C  
ATOM   2001  CD2 TRP A 276      34.044  64.818   4.252  1.00 13.37           C  
ANISOU 2001  CD2 TRP A 276     1430   1813   1835    171    -25     -1       C  
ATOM   2002  NE1 TRP A 276      36.052  65.776   4.409  1.00 14.71           N  
ANISOU 2002  NE1 TRP A 276     1498   2053   2035    155    -21    -21       N  
ATOM   2003  CE2 TRP A 276      34.850  65.639   5.043  1.00 13.51           C  
ANISOU 2003  CE2 TRP A 276     1396   1869   1867    153    -42    -14       C  
ATOM   2004  CE3 TRP A 276      32.739  64.514   4.695  1.00 14.82           C  
ANISOU 2004  CE3 TRP A 276     1665   1963   2003    168    -40      6       C  
ATOM   2005  CZ2 TRP A 276      34.366  66.223   6.237  1.00 15.42           C  
ANISOU 2005  CZ2 TRP A 276     1640   2113   2103    134    -73    -21       C  
ATOM   2006  CZ3 TRP A 276      32.275  65.076   5.853  1.00 15.25           C  
ANISOU 2006  CZ3 TRP A 276     1719   2022   2052    151    -66      4       C  
ATOM   2007  CH2 TRP A 276      33.105  65.905   6.629  1.00 15.98           C  
ANISOU 2007  CH2 TRP A 276     1762   2152   2155    137    -83    -11       C  
ATOM   2008  N   ALA A 277      35.968  64.562  -0.626  1.00 13.13           N  
ANISOU 2008  N   ALA A 277     1369   1823   1796    183    117     -7       N  
ATOM   2009  CA  ALA A 277      37.143  65.155  -1.236  1.00 13.91           C  
ANISOU 2009  CA  ALA A 277     1412   1965   1907    169    151     -8       C  
ATOM   2010  C   ALA A 277      36.768  66.296  -2.171  1.00 13.98           C  
ANISOU 2010  C   ALA A 277     1436   1967   1908    118    179      9       C  
ATOM   2011  O   ALA A 277      37.359  67.379  -2.134  1.00 15.58           O  
ANISOU 2011  O   ALA A 277     1600   2187   2133     77    193     17       O  
ATOM   2012  CB  ALA A 277      37.961  64.078  -2.011  1.00 15.17           C  
ANISOU 2012  CB  ALA A 277     1555   2150   2056    220    182    -23       C  
ATOM   2013  N   LEU A 278      35.790  66.068  -3.035  1.00 14.14           N  
ANISOU 2013  N   LEU A 278     1512   1962   1896    121    188     16       N  
ATOM   2014  CA  LEU A 278      35.307  67.119  -3.928  1.00 14.01           C  
ANISOU 2014  CA  LEU A 278     1518   1938   1866     81    210     41       C  
ATOM   2015  C   LEU A 278      34.797  68.328  -3.129  1.00 14.29           C  
ANISOU 2015  C   LEU A 278     1555   1945   1928     39    186     56       C  
ATOM   2016  O   LEU A 278      35.065  69.481  -3.496  1.00 14.62           O  
ANISOU 2016  O   LEU A 278     1584   1986   1984      0    209     77       O  
ATOM   2017  CB  LEU A 278      34.227  66.563  -4.834  1.00 14.26           C  
ANISOU 2017  CB  LEU A 278     1609   1954   1855     97    212     42       C  
ATOM   2018  CG  LEU A 278      33.455  67.555  -5.706  1.00 15.00           C  
ANISOU 2018  CG  LEU A 278     1735   2038   1925     67    223     73       C  
ATOM   2019  CD1 LEU A 278      34.327  68.413  -6.582  1.00 15.87           C  
ANISOU 2019  CD1 LEU A 278     1819   2178   2031     42    270     99       C  
ATOM   2020  CD2 LEU A 278      32.366  66.814  -6.490  1.00 16.31           C  
ANISOU 2020  CD2 LEU A 278     1953   2196   2044     88    214     64       C  
ATOM   2021  N   SER A 279      34.100  68.058  -2.031  1.00 13.34           N  
ANISOU 2021  N   SER A 279     1451   1800   1817     48    145     44       N  
ATOM   2022  CA  SER A 279      33.521  69.122  -1.213  1.00 12.94           C  
ANISOU 2022  CA  SER A 279     1405   1721   1788     14    121     49       C  
ATOM   2023  C   SER A 279      34.595  69.978  -0.517  1.00 13.66           C  
ANISOU 2023  C   SER A 279     1442   1829   1919    -17    122     40       C  
ATOM   2024  O   SER A 279      34.462  71.214  -0.383  1.00 14.03           O  
ANISOU 2024  O   SER A 279     1487   1852   1990    -58    125     48       O  
ATOM   2025  CB  SER A 279      32.530  68.551  -0.196  1.00 13.01           C  
ANISOU 2025  CB  SER A 279     1442   1708   1791     33     80     37       C  
ATOM   2026  OG  SER A 279      31.448  67.898  -0.886  1.00 13.20           O  
ANISOU 2026  OG  SER A 279     1516   1715   1784     50     80     43       O  
ATOM   2027  N   GLU A 280      35.673  69.328  -0.065  1.00 14.43           N  
ANISOU 2027  N   GLU A 280     1491   1965   2025      3    119     21       N  
ATOM   2028  CA  GLU A 280      36.804  70.050   0.509  1.00 15.18           C  
ANISOU 2028  CA  GLU A 280     1522   2088   2155    -27    120      7       C  
ATOM   2029  C   GLU A 280      37.414  70.965  -0.561  1.00 16.38           C  
ANISOU 2029  C   GLU A 280     1654   2246   2322    -70    168     26       C  
ATOM   2030  O   GLU A 280      37.753  72.116  -0.291  1.00 17.14           O  
ANISOU 2030  O   GLU A 280     1726   2332   2454   -121    173     25       O  
ATOM   2031  CB  GLU A 280      37.890  69.086   1.069  1.00 15.70           C  
ANISOU 2031  CB  GLU A 280     1534   2205   2223     11    107    -12       C  
ATOM   2032  CG  GLU A 280      37.496  68.351   2.337  1.00 15.84           C  
ANISOU 2032  CG  GLU A 280     1563   2222   2231     46     59    -26       C  
ATOM   2033  CD  GLU A 280      38.654  67.765   3.121  1.00 20.40           C  
ANISOU 2033  CD  GLU A 280     2078   2854   2817     78     38    -44       C  
ATOM   2034  OE1 GLU A 280      39.787  67.725   2.575  1.00 23.33           O  
ANISOU 2034  OE1 GLU A 280     2394   3267   3203     81     64    -49       O  
ATOM   2035  OE2 GLU A 280      38.437  67.332   4.272  1.00 18.16           O  
ANISOU 2035  OE2 GLU A 280     1798   2576   2523    103     -2    -51       O  
ATOM   2036  N   GLN A 281      37.568  70.460  -1.773  1.00 16.70           N  
ANISOU 2036  N   GLN A 281     1705   2301   2336    -50    205     43       N  
ATOM   2037  CA AGLN A 281      38.168  71.265  -2.837  0.50 16.97           C  
ANISOU 2037  CA AGLN A 281     1722   2347   2377    -89    257     68       C  
ATOM   2038  CA BGLN A 281      38.147  71.223  -2.885  0.50 17.85           C  
ANISOU 2038  CA BGLN A 281     1835   2459   2487    -87    258     69       C  
ATOM   2039  C   GLN A 281      37.283  72.455  -3.205  1.00 17.49           C  
ANISOU 2039  C   GLN A 281     1835   2360   2448   -129    265    100       C  
ATOM   2040  O   GLN A 281      37.788  73.543  -3.397  1.00 18.87           O  
ANISOU 2040  O   GLN A 281     1988   2525   2654   -181    291    116       O  
ATOM   2041  CB AGLN A 281      38.477  70.423  -4.069  0.50 17.77           C  
ANISOU 2041  CB AGLN A 281     1827   2483   2439    -54    297     77       C  
ATOM   2042  CB BGLN A 281      38.287  70.297  -4.111  0.50 18.99           C  
ANISOU 2042  CB BGLN A 281     1993   2633   2587    -47    294     77       C  
ATOM   2043  CG AGLN A 281      39.504  69.366  -3.810  0.50 16.67           C  
ANISOU 2043  CG AGLN A 281     1635   2395   2302    -12    299     47       C  
ATOM   2044  CG BGLN A 281      38.855  70.907  -5.386  0.50 22.57           C  
ANISOU 2044  CG BGLN A 281     2434   3110   3029    -77    355    108       C  
ATOM   2045  CD AGLN A 281      39.553  68.357  -4.921  0.50 22.30           C  
ANISOU 2045  CD AGLN A 281     2368   3132   2972     34    331     46       C  
ATOM   2046  CD BGLN A 281      38.880  69.884  -6.542  0.50 26.49           C  
ANISOU 2046  CD BGLN A 281     2951   3641   3473    -30    386    106       C  
ATOM   2047  OE1AGLN A 281      38.990  68.567  -5.996  0.50 26.62           O  
ANISOU 2047  OE1AGLN A 281     2959   3669   3484     25    358     68       O  
ATOM   2048  OE1BGLN A 281      39.605  68.899  -6.488  0.50 31.55           O  
ANISOU 2048  OE1BGLN A 281     3557   4320   4110      9    392     77       O  
ATOM   2049  NE2AGLN A 281      40.195  67.236  -4.658  0.50 25.10           N  
ANISOU 2049  NE2AGLN A 281     2692   3516   3327     86    325     18       N  
ATOM   2050  NE2BGLN A 281      38.073  70.120  -7.570  0.50 29.19           N  
ANISOU 2050  NE2BGLN A 281     3349   3969   3772    -33    403    135       N  
ATOM   2051  N   LEU A 282      35.971  72.258  -3.296  1.00 15.74           N  
ANISOU 2051  N   LEU A 282     1677   2104   2199   -107    241    110       N  
ATOM   2052  CA  LEU A 282      35.089  73.331  -3.677  1.00 15.60           C  
ANISOU 2052  CA  LEU A 282     1704   2038   2184   -134    246    142       C  
ATOM   2053  C   LEU A 282      34.975  74.408  -2.608  1.00 16.01           C  
ANISOU 2053  C   LEU A 282     1747   2049   2286   -172    223    130       C  
ATOM   2054  O   LEU A 282      34.831  75.618  -2.920  1.00 17.41           O  
ANISOU 2054  O   LEU A 282     1940   2186   2488   -210    243    157       O  
ATOM   2055  CB  LEU A 282      33.694  72.772  -4.010  1.00 15.22           C  
ANISOU 2055  CB  LEU A 282     1717   1973   2094    -96    223    150       C  
ATOM   2056  CG  LEU A 282      33.553  71.960  -5.301  1.00 14.62           C  
ANISOU 2056  CG  LEU A 282     1663   1927   1962    -66    247    163       C  
ATOM   2057  CD1 LEU A 282      32.175  71.289  -5.347  1.00 15.78           C  
ANISOU 2057  CD1 LEU A 282     1860   2058   2074    -33    212    156       C  
ATOM   2058  CD2 LEU A 282      33.740  72.894  -6.538  1.00 18.41           C  
ANISOU 2058  CD2 LEU A 282     2157   2409   2428    -91    292    212       C  
ATOM   2059  N   THR A 283      34.969  73.984  -1.344  1.00 16.37           N  
ANISOU 2059  N   THR A 283     1773   2101   2344   -159    182     90       N  
ATOM   2060  CA  THR A 283      34.701  74.921  -0.229  1.00 15.28           C  
ANISOU 2060  CA  THR A 283     1633   1927   2245   -189    155     68       C  
ATOM   2061  C   THR A 283      35.957  75.501   0.434  1.00 17.14           C  
ANISOU 2061  C   THR A 283     1805   2181   2526   -233    158     40       C  
ATOM   2062  O   THR A 283      35.836  76.444   1.215  1.00 18.07           O  
ANISOU 2062  O   THR A 283     1920   2265   2679   -268    142     18       O  
ATOM   2063  CB  THR A 283      33.822  74.318   0.865  1.00 14.64           C  
ANISOU 2063  CB  THR A 283     1571   1842   2148   -156    107     41       C  
ATOM   2064  OG1 THR A 283      34.501  73.231   1.516  1.00 14.84           O  
ANISOU 2064  OG1 THR A 283     1560   1917   2161   -128     88     15       O  
ATOM   2065  CG2 THR A 283      32.459  73.856   0.299  1.00 15.69           C  
ANISOU 2065  CG2 THR A 283     1763   1954   2242   -121    101     64       C  
ATOM   2066  N   LYS A 284      37.129  74.944   0.113  1.00 17.58           N  
ANISOU 2066  N   LYS A 284     1807   2291   2579   -232    178     36       N  
ATOM   2067  CA  LYS A 284      38.384  75.301   0.797  1.00 18.83           C  
ANISOU 2067  CA  LYS A 284     1892   2485   2778   -269    175      2       C  
ATOM   2068  C   LYS A 284      38.252  75.186   2.308  1.00 18.71           C  
ANISOU 2068  C   LYS A 284     1861   2478   2768   -260    119    -43       C  
ATOM   2069  O   LYS A 284      38.766  76.022   3.065  1.00 21.33           O  
ANISOU 2069  O   LYS A 284     2156   2808   3139   -307    106    -77       O  
ATOM   2070  CB  LYS A 284      38.881  76.670   0.314  1.00 20.17           C  
ANISOU 2070  CB  LYS A 284     2046   2621   2994   -341    214     17       C  
ATOM   2071  CG  LYS A 284      39.111  76.719  -1.232  1.00 25.57           C  
ANISOU 2071  CG  LYS A 284     2743   3309   3663   -347    275     70       C  
ATOM   2072  CD  LYS A 284      39.926  75.526  -1.689  1.00 32.12           C  
ANISOU 2072  CD  LYS A 284     3529   4213   4461   -307    291     67       C  
ATOM   2073  CE  LYS A 284      40.190  75.459  -3.200  1.00 36.08           C  
ANISOU 2073  CE  LYS A 284     4040   4731   4936   -308    353    112       C  
ATOM   2074  NZ  LYS A 284      40.515  74.031  -3.543  1.00 35.71           N  
ANISOU 2074  NZ  LYS A 284     3977   4745   4846   -244    355    100       N  
ATOM   2075  N   THR A 285      37.555  74.135   2.744  1.00 17.39           N  
ANISOU 2075  N   THR A 285     1724   2321   2561   -202     88    -46       N  
ATOM   2076  CA  THR A 285      37.499  73.721   4.153  1.00 17.61           C  
ANISOU 2076  CA  THR A 285     1736   2375   2579   -180     36    -83       C  
ATOM   2077  C   THR A 285      37.853  72.243   4.205  1.00 19.41           C  
ANISOU 2077  C   THR A 285     1949   2651   2773   -119     25    -78       C  
ATOM   2078  O   THR A 285      37.771  71.523   3.209  1.00 20.77           O  
ANISOU 2078  O   THR A 285     2142   2824   2926    -89     52    -52       O  
ATOM   2079  CB  THR A 285      36.124  73.959   4.851  1.00 17.44           C  
ANISOU 2079  CB  THR A 285     1773   2308   2543   -171      8    -89       C  
ATOM   2080  OG1 THR A 285      35.150  73.064   4.305  1.00 17.62           O  
ANISOU 2080  OG1 THR A 285     1850   2316   2529   -126     12    -59       O  
ATOM   2081  CG2 THR A 285      35.696  75.404   4.677  1.00 17.60           C  
ANISOU 2081  CG2 THR A 285     1816   2269   2599   -223     23    -91       C  
ATOM   2082  N   GLU A 286      38.332  71.802   5.353  1.00 19.79           N  
ANISOU 2082  N   GLU A 286     1960   2743   2814    -98    -14   -106       N  
ATOM   2083  CA  GLU A 286      38.717  70.417   5.553  1.00 21.03           C  
ANISOU 2083  CA  GLU A 286     2103   2942   2944    -34    -29    -99       C  
ATOM   2084  C   GLU A 286      38.300  69.898   6.912  1.00 19.10           C  
ANISOU 2084  C   GLU A 286     1871   2712   2672     -2    -78   -112       C  
ATOM   2085  O   GLU A 286      38.112  70.678   7.846  1.00 20.09           O  
ANISOU 2085  O   GLU A 286     1991   2840   2803    -32   -105   -139       O  
ATOM   2086  CB  GLU A 286      40.219  70.213   5.371  1.00 23.42           C  
ANISOU 2086  CB  GLU A 286     2324   3307   3264    -30    -19   -111       C  
ATOM   2087  CG  GLU A 286      41.094  70.839   6.379  1.00 29.27           C  
ANISOU 2087  CG  GLU A 286     2996   4097   4027    -60    -51   -149       C  
ATOM   2088  CD  GLU A 286      42.593  70.558   6.147  1.00 37.99           C  
ANISOU 2088  CD  GLU A 286     4009   5273   5150    -52    -41   -160       C  
ATOM   2089  OE1 GLU A 286      42.988  70.158   5.021  1.00 40.48           O  
ANISOU 2089  OE1 GLU A 286     4316   5594   5470    -37      3   -139       O  
ATOM   2090  OE2 GLU A 286      43.366  70.733   7.118  1.00 44.59           O  
ANISOU 2090  OE2 GLU A 286     4781   6167   5994    -58    -79   -193       O  
ATOM   2091  N   PHE A 287      38.170  68.590   7.029  1.00 18.39           N  
ANISOU 2091  N   PHE A 287     1800   2633   2554     59    -89    -93       N  
ATOM   2092  CA  PHE A 287      37.892  67.949   8.313  1.00 18.39           C  
ANISOU 2092  CA  PHE A 287     1810   2652   2523     97   -133    -95       C  
ATOM   2093  C   PHE A 287      39.012  68.312   9.294  1.00 18.91           C  
ANISOU 2093  C   PHE A 287     1802   2787   2594     91   -168   -126       C  
ATOM   2094  O   PHE A 287      40.188  68.060   8.984  1.00 20.61           O  
ANISOU 2094  O   PHE A 287     1956   3049   2826    105   -162   -130       O  
ATOM   2095  CB  PHE A 287      37.785  66.423   8.157  1.00 18.36           C  
ANISOU 2095  CB  PHE A 287     1835   2644   2496    165   -132    -64       C  
ATOM   2096  CG  PHE A 287      37.448  65.714   9.426  1.00 17.23           C  
ANISOU 2096  CG  PHE A 287     1709   2515   2319    204   -172    -54       C  
ATOM   2097  CD1 PHE A 287      36.156  65.731   9.924  1.00 17.98           C  
ANISOU 2097  CD1 PHE A 287     1864   2573   2392    195   -179    -45       C  
ATOM   2098  CD2 PHE A 287      38.420  65.042  10.148  1.00 18.07           C  
ANISOU 2098  CD2 PHE A 287     1772   2678   2415    253   -201    -52       C  
ATOM   2099  CE1 PHE A 287      35.835  65.057  11.093  1.00 18.28           C  
ANISOU 2099  CE1 PHE A 287     1922   2628   2394    229   -211    -30       C  
ATOM   2100  CE2 PHE A 287      38.093  64.381  11.304  1.00 18.01           C  
ANISOU 2100  CE2 PHE A 287     1787   2685   2371    292   -236    -34       C  
ATOM   2101  CZ  PHE A 287      36.821  64.404  11.806  1.00 18.46           C  
ANISOU 2101  CZ  PHE A 287     1906   2705   2403    277   -240    -23       C  
ATOM   2102  N   PRO A 288      38.684  68.874  10.472  1.00 18.85           N  
ANISOU 2102  N   PRO A 288     1795   2793   2571     71   -204   -150       N  
ATOM   2103  CA  PRO A 288      39.722  69.498  11.319  1.00 19.97           C  
ANISOU 2103  CA  PRO A 288     1863   3002   2721     48   -238   -192       C  
ATOM   2104  C   PRO A 288      40.158  68.669  12.509  1.00 22.40           C  
ANISOU 2104  C   PRO A 288     2146   3377   2988    104   -288   -191       C  
ATOM   2105  O   PRO A 288      41.064  69.115  13.257  1.00 24.68           O  
ANISOU 2105  O   PRO A 288     2366   3733   3276     90   -323   -229       O  
ATOM   2106  CB  PRO A 288      38.992  70.742  11.821  1.00 20.84           C  
ANISOU 2106  CB  PRO A 288     1998   3081   2839    -10   -245   -226       C  
ATOM   2107  CG  PRO A 288      37.640  70.242  12.014  1.00 19.14           C  
ANISOU 2107  CG  PRO A 288     1861   2822   2590     17   -243   -199       C  
ATOM   2108  CD  PRO A 288      37.347  69.382  10.831  1.00 19.28           C  
ANISOU 2108  CD  PRO A 288     1913   2800   2613     48   -206   -153       C  
ATOM   2109  N   LEU A 289      39.583  67.487  12.721  1.00 22.13           N  
ANISOU 2109  N   LEU A 289     2161   3329   2917    166   -293   -149       N  
ATOM   2110  CA  LEU A 289      39.904  66.701  13.912  1.00 24.21           C  
ANISOU 2110  CA  LEU A 289     2410   3651   3135    223   -341   -138       C  
ATOM   2111  C   LEU A 289      40.858  65.565  13.594  1.00 26.77           C  
ANISOU 2111  C   LEU A 289     2699   4007   3462    291   -342   -109       C  
ATOM   2112  O   LEU A 289      41.259  65.345  12.439  1.00 27.53           O  
ANISOU 2112  O   LEU A 289     2783   4081   3594    295   -304   -101       O  
ATOM   2113  CB  LEU A 289      38.642  66.173  14.592  1.00 23.40           C  
ANISOU 2113  CB  LEU A 289     2385   3515   2988    246   -348   -109       C  
ATOM   2114  CG  LEU A 289      37.513  67.173  14.856  1.00 23.87           C  
ANISOU 2114  CG  LEU A 289     2487   3538   3044    189   -340   -134       C  
ATOM   2115  CD1 LEU A 289      36.283  66.519  15.522  1.00 24.52           C  
ANISOU 2115  CD1 LEU A 289     2639   3596   3080    215   -343   -100       C  
ATOM   2116  CD2 LEU A 289      38.014  68.350  15.699  1.00 27.77           C  
ANISOU 2116  CD2 LEU A 289     2930   4085   3535    145   -373   -193       C  
ATOM   2117  OXT LEU A 289      41.278  64.876  14.562  1.00 31.69           O  
ANISOU 2117  OXT LEU A 289     3304   4686   4050    348   -384    -94       O  
END



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