CNRS Nantes University US2B US2B
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***  hsp90  ***

elNémo ID: 2407052049042402197

Job options:

ID        	=	 2407052049042402197
JOBID     	=	 hsp90
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER hsp90

ATOM      1  N   LYS A 294      -5.567 -29.875  -8.809  1.00103.51           N  
ANISOU    1  N   LYS A 294    10470  12403  16454  -1529   3907   2595       N  
ATOM      2  CA  LYS A 294      -4.575 -31.009  -8.876  1.00102.79           C  
ANISOU    2  CA  LYS A 294     9977  12689  16388  -1595   3957   2269       C  
ATOM      3  C   LYS A 294      -5.122 -32.359  -8.292  1.00 96.88           C  
ANISOU    3  C   LYS A 294     9207  12314  15287  -1344   3417   1844       C  
ATOM      4  O   LYS A 294      -5.278 -33.339  -9.040  1.00 96.24           O  
ANISOU    4  O   LYS A 294     9201  12640  14725  -1127   3498   1814       O  
ATOM      5  CB  LYS A 294      -3.208 -30.579  -8.294  1.00105.96           C  
ANISOU    5  CB  LYS A 294     9843  12800  17614  -2015   4116   2068       C  
ATOM      6  CG  LYS A 294      -2.014 -31.457  -8.657  1.00107.06           C  
ANISOU    6  CG  LYS A 294     9487  13241  17946  -2083   4374   1895       C  
ATOM      7  CD  LYS A 294      -1.889 -31.691 -10.154  1.00109.13           C  
ANISOU    7  CD  LYS A 294     9939  13784  17740  -1948   5019   2250       C  
ATOM      8  CE  LYS A 294      -0.519 -32.220 -10.521  1.00111.78           C  
ANISOU    8  CE  LYS A 294     9705  14267  18496  -2099   5477   2095       C  
ATOM      9  NZ  LYS A 294       0.463 -31.111 -10.627  1.00117.18           N1+
ANISOU    9  NZ  LYS A 294    10056  14560  19905  -2527   5988   2309       N1+
ATOM     10  N   PRO A 295      -5.439 -32.422  -6.979  1.00 93.19           N  
ANISOU   10  N   PRO A 295     8675  11701  15031  -1386   2907   1512       N  
ATOM     11  CA  PRO A 295      -6.007 -33.687  -6.558  1.00 88.50           C  
ANISOU   11  CA  PRO A 295     8116  11425  14084  -1145   2500   1226       C  
ATOM     12  C   PRO A 295      -7.458 -33.782  -7.003  1.00 86.52           C  
ANISOU   12  C   PRO A 295     8302  11309  13263   -858   2384   1379       C  
ATOM     13  O   PRO A 295      -8.096 -32.760  -7.225  1.00 88.27           O  
ANISOU   13  O   PRO A 295     8775  11310  13452   -830   2469   1667       O  
ATOM     14  CB  PRO A 295      -5.909 -33.624  -5.033  1.00 86.43           C  
ANISOU   14  CB  PRO A 295     7706  10986  14145  -1296   2037    893       C  
ATOM     15  CG  PRO A 295      -5.970 -32.224  -4.707  1.00 88.53           C  
ANISOU   15  CG  PRO A 295     8073  10834  14730  -1522   2131    978       C  
ATOM     16  CD  PRO A 295      -5.334 -31.479  -5.852  1.00 94.09           C  
ANISOU   16  CD  PRO A 295     8719  11393  15637  -1648   2698   1347       C  
ATOM     17  N   ILE A 296      -7.967 -35.002  -7.117  1.00 83.84           N  
ANISOU   17  N   ILE A 296     8009  11297  12549   -646   2185   1184       N  
ATOM     18  CA  ILE A 296      -9.271 -35.250  -7.696  1.00 82.80           C  
ANISOU   18  CA  ILE A 296     8194  11377  11887   -399   2065   1279       C  
ATOM     19  C   ILE A 296     -10.402 -34.458  -7.007  1.00 81.35           C  
ANISOU   19  C   ILE A 296     8204  10950  11753   -333   1810   1360       C  
ATOM     20  O   ILE A 296     -11.314 -33.964  -7.674  1.00 82.90           O  
ANISOU   20  O   ILE A 296     8622  11197  11678   -157   1817   1644       O  
ATOM     21  CB  ILE A 296      -9.570 -36.770  -7.704  1.00 80.23           C  
ANISOU   21  CB  ILE A 296     7821  11353  11307   -258   1875    940       C  
ATOM     22  CG1 ILE A 296     -10.744 -37.103  -8.629  1.00 80.81           C  
ANISOU   22  CG1 ILE A 296     8156  11737  10809    -56   1798    991       C  
ATOM     23  CG2 ILE A 296      -9.855 -37.263  -6.301  1.00 77.50           C  
ANISOU   23  CG2 ILE A 296     7388  10859  11200   -277   1498    670       C  
ATOM     24  CD1 ILE A 296     -11.035 -38.583  -8.757  1.00 78.69           C  
ANISOU   24  CD1 ILE A 296     7844  11710  10343     30   1672    605       C  
ATOM     25  N   TRP A 297     -10.331 -34.324  -5.684  1.00 79.28           N  
ANISOU   25  N   TRP A 297     7850  10441  11829   -461   1592   1112       N  
ATOM     26  CA  TRP A 297     -11.433 -33.750  -4.914  1.00 77.86           C  
ANISOU   26  CA  TRP A 297     7842  10044  11696   -390   1404   1073       C  
ATOM     27  C   TRP A 297     -11.483 -32.253  -5.107  1.00 82.06           C  
ANISOU   27  C   TRP A 297     8488  10180  12511   -440   1630   1363       C  
ATOM     28  O   TRP A 297     -12.443 -31.594  -4.721  1.00 82.42           O  
ANISOU   28  O   TRP A 297     8677   9987  12651   -325   1575   1399       O  
ATOM     29  CB  TRP A 297     -11.309 -34.092  -3.427  1.00 75.08           C  
ANISOU   29  CB  TRP A 297     7421   9594  11512   -530   1145    695       C  
ATOM     30  CG  TRP A 297     -10.018 -33.631  -2.751  1.00 75.57           C  
ANISOU   30  CG  TRP A 297     7290   9465  11957   -836   1148    550       C  
ATOM     31  CD1 TRP A 297      -9.745 -32.386  -2.263  1.00 77.80           C  
ANISOU   31  CD1 TRP A 297     7599   9365  12597  -1056   1238    505       C  
ATOM     32  CD2 TRP A 297      -8.865 -34.430  -2.462  1.00 73.86           C  
ANISOU   32  CD2 TRP A 297     6780   9422  11858   -957   1024    396       C  
ATOM     33  NE1 TRP A 297      -8.493 -32.356  -1.708  1.00 78.40           N  
ANISOU   33  NE1 TRP A 297     7401   9412  12972  -1347   1143    303       N  
ATOM     34  CE2 TRP A 297      -7.939 -33.604  -1.801  1.00 76.69           C  
ANISOU   34  CE2 TRP A 297     6965   9552  12620  -1267    989    261       C  
ATOM     35  CE3 TRP A 297      -8.524 -35.769  -2.701  1.00 72.74           C  
ANISOU   35  CE3 TRP A 297     6478   9577  11581   -825    940    346       C  
ATOM     36  CZ2 TRP A 297      -6.685 -34.070  -1.374  1.00 79.05           C  
ANISOU   36  CZ2 TRP A 297     6883   9974  13177  -1434    811    111       C  
ATOM     37  CZ3 TRP A 297      -7.271 -36.229  -2.281  1.00 74.52           C  
ANISOU   37  CZ3 TRP A 297     6346   9865  12102   -947    817    231       C  
ATOM     38  CH2 TRP A 297      -6.366 -35.376  -1.631  1.00 76.58           C  
ANISOU   38  CH2 TRP A 297     6390   9957  12750  -1242    727    131       C  
ATOM     39  N   THR A 298     -10.421 -31.736  -5.704  1.00 86.29           N  
ANISOU   39  N   THR A 298     8935  10604  13247   -614   1935   1569       N  
ATOM     40  CA  THR A 298     -10.266 -30.320  -5.980  1.00 91.77           C  
ANISOU   40  CA  THR A 298     9726  10840  14302   -709   2239   1897       C  
ATOM     41  C   THR A 298     -10.690 -30.053  -7.416  1.00 95.59           C  
ANISOU   41  C   THR A 298    10415  11476  14429   -466   2467   2464       C  
ATOM     42  O   THR A 298     -10.891 -28.912  -7.798  1.00100.04           O  
ANISOU   42  O   THR A 298    11137  11664  15210   -424   2700   2886       O  
ATOM     43  CB  THR A 298      -8.802 -29.894  -5.712  1.00 94.56           C  
ANISOU   43  CB  THR A 298     9818  10952  15156  -1105   2466   1784       C  
ATOM     44  OG1 THR A 298      -8.643 -29.633  -4.316  1.00 93.70           O  
ANISOU   44  OG1 THR A 298     9612  10586  15402  -1333   2216   1323       O  
ATOM     45  CG2 THR A 298      -8.406 -28.663  -6.485  1.00100.98           C  
ANISOU   45  CG2 THR A 298    10708  11359  16298  -1224   2940   2247       C  
ATOM     46  N   ARG A 299     -10.826 -31.117  -8.201  1.00 95.33           N  
ANISOU   46  N   ARG A 299    10397  11988  13833   -306   2391   2470       N  
ATOM     47  CA  ARG A 299     -11.358 -31.030  -9.548  1.00 99.96           C  
ANISOU   47  CA  ARG A 299    11219  12873  13887    -60   2494   2944       C  
ATOM     48  C   ARG A 299     -12.887 -30.818  -9.541  1.00100.19           C  
ANISOU   48  C   ARG A 299    11398  12937  13729    272   2144   3094       C  
ATOM     49  O   ARG A 299     -13.563 -31.058  -8.530  1.00 96.21           O  
ANISOU   49  O   ARG A 299    10800  12323  13433    312   1855   2736       O  
ATOM     50  CB  ARG A 299     -10.954 -32.268 -10.357  1.00 99.78           C  
ANISOU   50  CB  ARG A 299    11161  13428  13320    -44   2543   2771       C  
ATOM     51  CG  ARG A 299      -9.623 -32.118 -11.099  1.00106.50           C  
ANISOU   51  CG  ARG A 299    11954  14309  14200   -251   3078   2949       C  
ATOM     52  CD  ARG A 299      -8.902 -33.446 -11.339  1.00109.63           C  
ANISOU   52  CD  ARG A 299    12156  15098  14399   -311   3170   2520       C  
ATOM     53  NE  ARG A 299      -9.546 -34.296 -12.351  1.00114.41           N  
ANISOU   53  NE  ARG A 299    12987  16256  14229    -99   3090   2470       N  
ATOM     54  CZ  ARG A 299      -9.346 -35.617 -12.483  1.00114.69           C  
ANISOU   54  CZ  ARG A 299    12907  16608  14062    -81   3056   1987       C  
ATOM     55  NH1 ARG A 299      -8.518 -36.289 -11.669  1.00112.14           N1+
ANISOU   55  NH1 ARG A 299    12230  16114  14264   -204   3076   1589       N1+
ATOM     56  NH2 ARG A 299      -9.987 -36.278 -13.439  1.00116.41           N  
ANISOU   56  NH2 ARG A 299    13359  17308  13563     68   2980   1895       N  
ATOM     57  N   ASN A 300     -13.409 -30.343 -10.673  1.00105.94           N  
ANISOU   57  N   ASN A 300    12347  13833  14071    513   2185   3655       N  
ATOM     58  CA  ASN A 300     -14.833 -30.054 -10.858  1.00107.97           C  
ANISOU   58  CA  ASN A 300    12680  14162  14181    876   1833   3906       C  
ATOM     59  C   ASN A 300     -15.626 -31.284 -11.282  1.00106.30           C  
ANISOU   59  C   ASN A 300    12414  14613  13359   1027   1421   3621       C  
ATOM     60  O   ASN A 300     -15.304 -31.916 -12.288  1.00107.84           O  
ANISOU   60  O   ASN A 300    12725  15317  12932   1010   1461   3656       O  
ATOM     61  CB  ASN A 300     -15.004 -28.931 -11.882  1.00115.73           C  
ANISOU   61  CB  ASN A 300    13913  15017  15040   1092   2011   4725       C  
ATOM     62  CG  ASN A 300     -16.357 -28.964 -12.583  1.00119.73           C  
ANISOU   62  CG  ASN A 300    14480  15919  15092   1516   1560   5068       C  
ATOM     63  OD1 ASN A 300     -16.416 -29.054 -13.807  1.00125.77           O  
ANISOU   63  OD1 ASN A 300    15458  17171  15155   1657   1514   5502       O  
ATOM     64  ND2 ASN A 300     -17.447 -28.888 -11.814  1.00118.27           N  
ANISOU   64  ND2 ASN A 300    14091  15557  15289   1717   1227   4868       N  
ATOM     65  N   PRO A 301     -16.688 -31.611 -10.522  1.00103.78           N  
ANISOU   65  N   PRO A 301    11919  14275  13237   1153   1064   3308       N  
ATOM     66  CA  PRO A 301     -17.371 -32.893 -10.681  1.00102.10           C  
ANISOU   66  CA  PRO A 301    11580  14592  12619   1194    705   2892       C  
ATOM     67  C   PRO A 301     -17.898 -33.215 -12.093  1.00107.71           C  
ANISOU   67  C   PRO A 301    12406  15936  12583   1382    454   3141       C  
ATOM     68  O   PRO A 301     -18.160 -34.380 -12.383  1.00107.04           O  
ANISOU   68  O   PRO A 301    12248  16306  12115   1316    236   2707       O  
ATOM     69  CB  PRO A 301     -18.503 -32.812  -9.652  1.00 99.54           C  
ANISOU   69  CB  PRO A 301    11039  14030  12749   1317    464   2675       C  
ATOM     70  CG  PRO A 301     -17.974 -31.903  -8.607  1.00 97.72           C  
ANISOU   70  CG  PRO A 301    10836  13155  13137   1195    765   2676       C  
ATOM     71  CD  PRO A 301     -17.246 -30.848  -9.389  1.00102.59           C  
ANISOU   71  CD  PRO A 301    11660  13566  13752   1215   1052   3244       C  
ATOM     72  N   ASP A 302     -18.034 -32.226 -12.969  1.00114.40           N  
ANISOU   72  N   ASP A 302    13450  16816  13201   1599    479   3822       N  
ATOM     73  CA  ASP A 302     -18.416 -32.532 -14.353  1.00120.82           C  
ANISOU   73  CA  ASP A 302    14434  18322  13147   1755    219   4076       C  
ATOM     74  C   ASP A 302     -17.278 -33.133 -15.168  1.00122.34           C  
ANISOU   74  C   ASP A 302    14874  18875  12734   1519    577   3948       C  
ATOM     75  O   ASP A 302     -17.520 -33.908 -16.090  1.00125.57           O  
ANISOU   75  O   ASP A 302    15393  19938  12379   1527    366   3764       O  
ATOM     76  CB  ASP A 302     -19.019 -31.319 -15.064  1.00128.33           C  
ANISOU   76  CB  ASP A 302    15537  19251  13971   2120     70   4938       C  
ATOM     77  CG  ASP A 302     -20.489 -31.148 -14.753  1.00130.17           C  
ANISOU   77  CG  ASP A 302    15456  19505  14496   2447   -481   4986       C  
ATOM     78  OD1 ASP A 302     -21.181 -30.388 -15.468  1.00137.75           O  
ANISOU   78  OD1 ASP A 302    16470  20604  15263   2817   -768   5670       O  
ATOM     79  OD2 ASP A 302     -20.955 -31.793 -13.787  1.00125.68           O1-
ANISOU   79  OD2 ASP A 302    14567  18816  14367   2342   -614   4363       O1-
ATOM     80  N   ASP A 303     -16.045 -32.773 -14.817  1.00121.00           N  
ANISOU   80  N   ASP A 303    14761  18277  12935   1295   1129   3996       N  
ATOM     81  CA  ASP A 303     -14.850 -33.223 -15.555  1.00123.37           C  
ANISOU   81  CA  ASP A 303    15236  18838  12800   1076   1599   3909       C  
ATOM     82  C   ASP A 303     -14.318 -34.584 -15.079  1.00118.05           C  
ANISOU   82  C   ASP A 303    14349  18268  12235    845   1662   3091       C  
ATOM     83  O   ASP A 303     -13.350 -35.106 -15.652  1.00120.10           O  
ANISOU   83  O   ASP A 303    14685  18739  12205    686   2070   2910       O  
ATOM     84  CB  ASP A 303     -13.704 -32.190 -15.473  1.00125.52           C  
ANISOU   84  CB  ASP A 303    15589  18597  13503    920   2208   4362       C  
ATOM     85  CG  ASP A 303     -14.134 -30.782 -15.842  1.00131.00           C  
ANISOU   85  CG  ASP A 303    16500  19007  14266   1142   2238   5220       C  
ATOM     86  OD1 ASP A 303     -15.301 -30.596 -16.240  1.00134.57           O  
ANISOU   86  OD1 ASP A 303    17035  19722  14372   1464   1760   5521       O  
ATOM     87  OD2 ASP A 303     -13.298 -29.860 -15.721  1.00132.67           O1-
ANISOU   87  OD2 ASP A 303    16763  18698  14944    992   2739   5599       O1-
ATOM     88  N   ILE A 304     -14.927 -35.146 -14.034  1.00111.73           N  
ANISOU   88  N   ILE A 304    13280  17286  11884    840   1314   2630       N  
ATOM     89  CA  ILE A 304     -14.496 -36.444 -13.517  1.00106.89           C  
ANISOU   89  CA  ILE A 304    12474  16697  11440    661   1350   1938       C  
ATOM     90  C   ILE A 304     -15.471 -37.547 -13.940  1.00107.44           C  
ANISOU   90  C   ILE A 304    12524  17236  11062    717    951   1495       C  
ATOM     91  O   ILE A 304     -16.689 -37.360 -13.877  1.00107.96           O  
ANISOU   91  O   ILE A 304    12527  17412  11077    870    505   1580       O  
ATOM     92  CB  ILE A 304     -14.334 -36.425 -11.981  1.00100.53           C  
ANISOU   92  CB  ILE A 304    11411  15345  11438    560   1307   1717       C  
ATOM     93  CG1 ILE A 304     -13.536 -35.203 -11.527  1.00100.71           C  
ANISOU   93  CG1 ILE A 304    11434  14893  11937    473   1614   2104       C  
ATOM     94  CG2 ILE A 304     -13.637 -37.681 -11.508  1.00 97.52           C  
ANISOU   94  CG2 ILE A 304    10853  14944  11254    403   1409   1160       C  
ATOM     95  CD1 ILE A 304     -13.445 -35.058 -10.020  1.00 95.43           C  
ANISOU   95  CD1 ILE A 304    10566  13750  11942    362   1516   1871       C  
ATOM     96  N   THR A 305     -14.930 -38.684 -14.382  1.00108.28           N  
ANISOU   96  N   THR A 305    12644  17586  10909    586   1132    997       N  
ATOM     97  CA  THR A 305     -15.743 -39.837 -14.804  1.00109.71           C  
ANISOU   97  CA  THR A 305    12801  18159  10722    566    809    451       C  
ATOM     98  C   THR A 305     -15.831 -40.901 -13.710  1.00104.59           C  
ANISOU   98  C   THR A 305    11878  17159  10701    452    741    -91       C  
ATOM     99  O   THR A 305     -15.021 -40.907 -12.787  1.00100.66           O  
ANISOU   99  O   THR A 305    11249  16217  10779    391    983    -85       O  
ATOM    100  CB  THR A 305     -15.227 -40.454 -16.127  1.00115.66           C  
ANISOU  100  CB  THR A 305    13806  19425  10713    495   1071    181       C  
ATOM    101  OG1 THR A 305     -13.798 -40.562 -16.097  1.00114.52           O  
ANISOU  101  OG1 THR A 305    13661  19050  10798    393   1689    139       O  
ATOM    102  CG2 THR A 305     -15.645 -39.592 -17.315  1.00122.54           C  
ANISOU  102  CG2 THR A 305    15000  20826  10732    632    932    701       C  
ATOM    103  N   ASN A 306     -16.817 -41.790 -13.789  1.00105.69           N  
ANISOU  103  N   ASN A 306    11920  17491  10745    412    396   -537       N  
ATOM    104  CA  ASN A 306     -16.975 -42.804 -12.739  1.00101.97           C  
ANISOU  104  CA  ASN A 306    11216  16636  10889    300    369   -975       C  
ATOM    105  C   ASN A 306     -15.770 -43.747 -12.671  1.00101.46           C  
ANISOU  105  C   ASN A 306    11147  16355  11045    202    796  -1332       C  
ATOM    106  O   ASN A 306     -15.384 -44.241 -11.604  1.00 97.38           O  
ANISOU  106  O   ASN A 306    10469  15390  11140    167    894  -1424       O  
ATOM    107  CB  ASN A 306     -18.262 -43.599 -12.921  1.00103.89           C  
ANISOU  107  CB  ASN A 306    11325  17098  11048    227    -27  -1405       C  
ATOM    108  CG  ASN A 306     -18.754 -44.204 -11.609  1.00100.91           C  
ANISOU  108  CG  ASN A 306    10700  16255  11383    145    -88  -1594       C  
ATOM    109  OD1 ASN A 306     -18.998 -43.488 -10.613  1.00 97.51           O  
ANISOU  109  OD1 ASN A 306    10178  15537  11333    221   -131  -1239       O  
ATOM    110  ND2 ASN A 306     -18.909 -45.532 -11.600  1.00102.66           N  
ANISOU  110  ND2 ASN A 306    10838  16380  11787    -22    -47  -2163       N  
ATOM    111  N   GLU A 307     -15.192 -43.978 -13.840  1.00106.27           N  
ANISOU  111  N   GLU A 307    11940  17308  11129    180   1057  -1508       N  
ATOM    112  CA  GLU A 307     -13.956 -44.700 -13.984  1.00107.43           C  
ANISOU  112  CA  GLU A 307    12065  17286  11468    136   1552  -1804       C  
ATOM    113  C   GLU A 307     -12.845 -44.008 -13.198  1.00103.65           C  
ANISOU  113  C   GLU A 307    11445  16429  11508    183   1821  -1370       C  
ATOM    114  O   GLU A 307     -12.101 -44.670 -12.479  1.00101.89           O  
ANISOU  114  O   GLU A 307    11010  15826  11877    180   1999  -1541       O  
ATOM    115  CB  GLU A 307     -13.610 -44.876 -15.473  1.00114.90           C  
ANISOU  115  CB  GLU A 307    13277  18742  11638    104   1841  -2047       C  
ATOM    116  CG  GLU A 307     -14.357 -43.911 -16.450  1.00121.34           C  
ANISOU  116  CG  GLU A 307    14374  20149  11578    154   1559  -1672       C  
ATOM    117  CD  GLU A 307     -15.872 -44.230 -16.653  1.00124.58           C  
ANISOU  117  CD  GLU A 307    14768  20883  11684    125    919  -1924       C  
ATOM    118  OE1 GLU A 307     -16.190 -45.121 -17.482  1.00130.09           O  
ANISOU  118  OE1 GLU A 307    15578  21949  11901      3    856  -2540       O  
ATOM    119  OE2 GLU A 307     -16.734 -43.566 -16.010  1.00120.79           O1-
ANISOU  119  OE2 GLU A 307    14138  20294  11460    215    495  -1540       O1-
ATOM    120  N   GLU A 308     -12.751 -42.683 -13.295  1.00103.13           N  
ANISOU  120  N   GLU A 308    11472  16439  11273    225   1820   -807       N  
ATOM    121  CA  GLU A 308     -11.779 -41.931 -12.482  1.00100.11           C  
ANISOU  121  CA  GLU A 308    10924  15679  11435    209   2017   -441       C  
ATOM    122  C   GLU A 308     -12.123 -41.909 -10.987  1.00 94.08           C  
ANISOU  122  C   GLU A 308     9972  14502  11271    204   1692   -396       C  
ATOM    123  O   GLU A 308     -11.230 -42.081 -10.150  1.00 91.86           O  
ANISOU  123  O   GLU A 308     9477  13907  11518    168   1797   -408       O  
ATOM    124  CB  GLU A 308     -11.595 -40.507 -13.002  1.00102.55           C  
ANISOU  124  CB  GLU A 308    11397  16094  11469    220   2159    133       C  
ATOM    125  CG  GLU A 308     -10.384 -40.317 -13.888  1.00109.41           C  
ANISOU  125  CG  GLU A 308    12309  17097  12163    160   2745    231       C  
ATOM    126  CD  GLU A 308     -10.530 -39.146 -14.876  1.00117.31           C  
ANISOU  126  CD  GLU A 308    13626  18366  12579    186   2902    792       C  
ATOM    127  OE1 GLU A 308      -9.889 -39.185 -15.968  1.00123.36           O  
ANISOU  127  OE1 GLU A 308    14563  19441  12864    149   3382    826       O  
ATOM    128  OE2 GLU A 308     -11.290 -38.195 -14.565  1.00116.39           O1-
ANISOU  128  OE2 GLU A 308    13598  18135  12489    260   2582   1219       O1-
ATOM    129  N   TYR A 309     -13.401 -41.689 -10.654  1.00 91.75           N  
ANISOU  129  N   TYR A 309     9742  14238  10880    244   1303   -341       N  
ATOM    130  CA  TYR A 309     -13.825 -41.668  -9.257  1.00 86.94           C  
ANISOU  130  CA  TYR A 309     9007  13279  10744    229   1062   -319       C  
ATOM    131  C   TYR A 309     -13.556 -43.032  -8.678  1.00 85.27           C  
ANISOU  131  C   TYR A 309     8660  12878  10860    190   1083   -698       C  
ATOM    132  O   TYR A 309     -12.997 -43.161  -7.598  1.00 83.03           O  
ANISOU  132  O   TYR A 309     8255  12290  11001    168   1071   -642       O  
ATOM    133  CB  TYR A 309     -15.308 -41.369  -9.120  1.00 86.54           C  
ANISOU  133  CB  TYR A 309     8996  13319  10564    287    723   -269       C  
ATOM    134  CG  TYR A 309     -15.684 -39.906  -9.072  1.00 87.33           C  
ANISOU  134  CG  TYR A 309     9172  13374  10635    374    650    185       C  
ATOM    135  CD1 TYR A 309     -15.224 -39.067  -8.047  1.00 85.52           C  
ANISOU  135  CD1 TYR A 309     8916  12768  10810    332    728    391       C  
ATOM    136  CD2 TYR A 309     -16.542 -39.366 -10.034  1.00 90.00           C  
ANISOU  136  CD2 TYR A 309     9602  14032  10560    507    477    397       C  
ATOM    137  CE1 TYR A 309     -15.595 -37.712  -8.007  1.00 86.75           C  
ANISOU  137  CE1 TYR A 309     9146  12783  11029    415    715    769       C  
ATOM    138  CE2 TYR A 309     -16.905 -38.026 -10.009  1.00 91.13           C  
ANISOU  138  CE2 TYR A 309     9805  14056  10763    639    430    867       C  
ATOM    139  CZ  TYR A 309     -16.432 -37.205  -9.001  1.00 90.01           C  
ANISOU  139  CZ  TYR A 309     9646  13455  11100    590    587   1035       C  
ATOM    140  OH  TYR A 309     -16.806 -35.881  -9.006  1.00 93.54           O  
ANISOU  140  OH  TYR A 309    10158  13698  11684    724    592   1464       O  
ATOM    141  N   GLY A 310     -13.952 -44.048  -9.427  1.00 87.30           N  
ANISOU  141  N   GLY A 310     8947  13314  10907    180   1103  -1081       N  
ATOM    142  CA  GLY A 310     -13.751 -45.418  -9.023  1.00 87.17           C  
ANISOU  142  CA  GLY A 310     8820  13048  11251    155   1176  -1449       C  
ATOM    143  C   GLY A 310     -12.297 -45.700  -8.727  1.00 87.49           C  
ANISOU  143  C   GLY A 310     8708  12854  11676    207   1456  -1409       C  
ATOM    144  O   GLY A 310     -11.974 -46.236  -7.662  1.00 86.20           O  
ANISOU  144  O   GLY A 310     8412  12350  11990    237   1390  -1367       O  
ATOM    145  N   GLU A 311     -11.423 -45.333  -9.664  1.00 89.83           N  
ANISOU  145  N   GLU A 311     9009  13352  11769    225   1770  -1390       N  
ATOM    146  CA  GLU A 311      -9.994 -45.517  -9.480  1.00 90.84           C  
ANISOU  146  CA  GLU A 311     8895  13290  12329    277   2069  -1353       C  
ATOM    147  C   GLU A 311      -9.522 -44.799  -8.215  1.00 86.74           C  
ANISOU  147  C   GLU A 311     8206  12534  12216    262   1852   -971       C  
ATOM    148  O   GLU A 311      -8.680 -45.306  -7.487  1.00 87.15           O  
ANISOU  148  O   GLU A 311     7999  12336  12775    325   1846   -958       O  
ATOM    149  CB  GLU A 311      -9.200 -45.100 -10.732  1.00 95.50           C  
ANISOU  149  CB  GLU A 311     9514  14164  12605    265   2524  -1369       C  
ATOM    150  CG  GLU A 311      -9.151 -46.211 -11.814  1.00103.80           C  
ANISOU  150  CG  GLU A 311    10649  15363  13425    295   2862  -1907       C  
ATOM    151  CD  GLU A 311      -8.613 -45.760 -13.200  1.00114.61           C  
ANISOU  151  CD  GLU A 311    12177  17136  14232    259   3347  -1942       C  
ATOM    152  OE1 GLU A 311      -8.107 -44.614 -13.342  1.00117.94           O  
ANISOU  152  OE1 GLU A 311    12594  17664  14553    216   3495  -1491       O  
ATOM    153  OE2 GLU A 311      -8.693 -46.568 -14.164  1.00120.49           O1-
ANISOU  153  OE2 GLU A 311    13073  18084  14622    254   3623  -2439       O1-
ATOM    154  N   PHE A 312     -10.089 -43.641  -7.916  1.00 83.40           N  
ANISOU  154  N   PHE A 312     7923  12180  11583    186   1644   -678       N  
ATOM    155  CA  PHE A 312      -9.668 -42.962  -6.714  1.00 80.45           C  
ANISOU  155  CA  PHE A 312     7425  11591  11550    129   1442   -424       C  
ATOM    156  C   PHE A 312     -10.095 -43.742  -5.474  1.00 77.60           C  
ANISOU  156  C   PHE A 312     7051  11011  11420    164   1137   -484       C  
ATOM    157  O   PHE A 312      -9.320 -43.933  -4.537  1.00 77.47           O  
ANISOU  157  O   PHE A 312     6849  10827  11760    175   1005   -396       O  
ATOM    158  CB  PHE A 312     -10.207 -41.528  -6.654  1.00 79.57           C  
ANISOU  158  CB  PHE A 312     7485  11521  11225     43   1348   -147       C  
ATOM    159  CG  PHE A 312      -9.819 -40.797  -5.386  1.00 77.38           C  
ANISOU  159  CG  PHE A 312     7116  11014  11270    -62   1146      2       C  
ATOM    160  CD1 PHE A 312      -8.488 -40.457  -5.145  1.00 76.24           C  
ANISOU  160  CD1 PHE A 312     6695  10780  11491   -161   1237     68       C  
ATOM    161  CD2 PHE A 312     -10.776 -40.485  -4.427  1.00 74.40           C  
ANISOU  161  CD2 PHE A 312     6902  10528  10836    -83    876     24       C  
ATOM    162  CE1 PHE A 312      -8.112 -39.808  -3.990  1.00 75.96           C  
ANISOU  162  CE1 PHE A 312     6569  10580  11712   -300    994    125       C  
ATOM    163  CE2 PHE A 312     -10.401 -39.830  -3.255  1.00 75.04           C  
ANISOU  163  CE2 PHE A 312     6946  10435  11131   -208    700     78       C  
ATOM    164  CZ  PHE A 312      -9.054 -39.488  -3.039  1.00 75.46           C  
ANISOU  164  CZ  PHE A 312     6741  10428  11503   -329    724    114       C  
ATOM    165  N   TYR A 313     -11.345 -44.180  -5.481  1.00 75.51           N  
ANISOU  165  N   TYR A 313     6976  10771  10941    174   1019   -611       N  
ATOM    166  CA  TYR A 313     -11.907 -44.920  -4.369  1.00 73.24           C  
ANISOU  166  CA  TYR A 313     6726  10271  10831    182    816   -632       C  
ATOM    167  C   TYR A 313     -11.078 -46.163  -3.993  1.00 74.74           C  
ANISOU  167  C   TYR A 313     6744  10225  11427    286    866   -696       C  
ATOM    168  O   TYR A 313     -10.843 -46.435  -2.818  1.00 73.98           O  
ANISOU  168  O   TYR A 313     6621   9945  11540    314    672   -512       O  
ATOM    169  CB  TYR A 313     -13.341 -45.302  -4.694  1.00 72.23           C  
ANISOU  169  CB  TYR A 313     6743  10211  10488    150    771   -815       C  
ATOM    170  CG  TYR A 313     -13.922 -46.243  -3.689  1.00 71.46           C  
ANISOU  170  CG  TYR A 313     6677   9857  10616    132    683   -848       C  
ATOM    171  CD1 TYR A 313     -14.535 -45.766  -2.549  1.00 68.43           C  
ANISOU  171  CD1 TYR A 313     6398   9398  10203     76    538   -659       C  
ATOM    172  CD2 TYR A 313     -13.849 -47.625  -3.876  1.00 72.75           C  
ANISOU  172  CD2 TYR A 313     6785   9815  11041    164    807  -1069       C  
ATOM    173  CE1 TYR A 313     -15.074 -46.634  -1.622  1.00 67.96           C  
ANISOU  173  CE1 TYR A 313     6404   9111  10306     43    529   -634       C  
ATOM    174  CE2 TYR A 313     -14.384 -48.499  -2.951  1.00 71.81           C  
ANISOU  174  CE2 TYR A 313     6717   9400  11168    136    781  -1026       C  
ATOM    175  CZ  TYR A 313     -14.988 -47.994  -1.821  1.00 69.84           C  
ANISOU  175  CZ  TYR A 313     6587   9124  10821     72    646   -778       C  
ATOM    176  OH  TYR A 313     -15.498 -48.853  -0.877  1.00 71.57           O  
ANISOU  176  OH  TYR A 313     6895   9059  11239     32    685   -674       O  
ATOM    177  N   LYS A 314     -10.642 -46.912  -4.997  1.00 77.19           N  
ANISOU  177  N   LYS A 314     6952  10539  11834    361   1135   -949       N  
ATOM    178  CA  LYS A 314      -9.944 -48.163  -4.757  1.00 79.83           C  
ANISOU  178  CA  LYS A 314     7106  10573  12649    508   1239  -1036       C  
ATOM    179  C   LYS A 314      -8.566 -47.864  -4.170  1.00 81.71           C  
ANISOU  179  C   LYS A 314     7045  10753  13247    606   1165   -771       C  
ATOM    180  O   LYS A 314      -8.088 -48.549  -3.250  1.00 83.19           O  
ANISOU  180  O   LYS A 314     7090  10690  13826    742    995   -590       O  
ATOM    181  CB  LYS A 314      -9.847 -48.982  -6.052  1.00 83.06           C  
ANISOU  181  CB  LYS A 314     7492  10991  13075    553   1613  -1473       C  
ATOM    182  CG  LYS A 314     -11.146 -49.689  -6.468  1.00 82.66           C  
ANISOU  182  CG  LYS A 314     7657  10914  12834    447   1620  -1822       C  
ATOM    183  CD  LYS A 314     -10.925 -50.786  -7.490  1.00 86.41           C  
ANISOU  183  CD  LYS A 314     8100  11275  13454    485   1981  -2341       C  
ATOM    184  CE  LYS A 314     -10.944 -50.267  -8.926  1.00 89.49           C  
ANISOU  184  CE  LYS A 314     8607  12136  13260    402   2189  -2643       C  
ATOM    185  NZ  LYS A 314     -10.350 -51.263  -9.881  1.00 93.17           N1+
ANISOU  185  NZ  LYS A 314     9023  12495  13880    463   2643  -3178       N1+
ATOM    186  N   SER A 315      -7.940 -46.822  -4.711  1.00 82.31           N  
ANISOU  186  N   SER A 315     7009  11065  13201    529   1279   -722       N  
ATOM    187  CA  SER A 315      -6.724 -46.245  -4.166  1.00 83.75           C  
ANISOU  187  CA  SER A 315     6861  11250  13709    532   1167   -496       C  
ATOM    188  C   SER A 315      -6.920 -45.841  -2.714  1.00 81.85           C  
ANISOU  188  C   SER A 315     6694  10962  13441    464    688   -232       C  
ATOM    189  O   SER A 315      -6.161 -46.224  -1.845  1.00 83.23           O  
ANISOU  189  O   SER A 315     6629  11036  13956    563    429    -64       O  
ATOM    190  CB  SER A 315      -6.395 -45.013  -4.973  1.00 83.95           C  
ANISOU  190  CB  SER A 315     6861  11507  13526    372   1396   -472       C  
ATOM    191  OG  SER A 315      -5.029 -44.708  -4.867  1.00 89.77           O  
ANISOU  191  OG  SER A 315     7159  12232  14718    366   1468   -379       O  
ATOM    192  N   LEU A 316      -7.989 -45.091  -2.470  1.00 79.60           N  
ANISOU  192  N   LEU A 316     6750  10767  12724    310    572   -205       N  
ATOM    193  CA  LEU A 316      -8.283 -44.524  -1.162  1.00 78.86           C  
ANISOU  193  CA  LEU A 316     6803  10668  12492    203    205    -34       C  
ATOM    194  C   LEU A 316      -8.485 -45.559  -0.081  1.00 80.11           C  
ANISOU  194  C   LEU A 316     7042  10674  12721    317    -37    100       C  
ATOM    195  O   LEU A 316      -7.987 -45.399   1.027  1.00 82.33           O  
ANISOU  195  O   LEU A 316     7279  10981  13018    297   -379    284       O  
ATOM    196  CB  LEU A 316      -9.526 -43.638  -1.237  1.00 75.77           C  
ANISOU  196  CB  LEU A 316     6747  10350  11691     67    239    -78       C  
ATOM    197  CG  LEU A 316     -10.021 -43.055   0.095  1.00 75.32           C  
ANISOU  197  CG  LEU A 316     6906  10271  11439    -50    -33      8       C  
ATOM    198  CD1 LEU A 316      -9.083 -41.957   0.633  1.00 76.87           C  
ANISOU  198  CD1 LEU A 316     6968  10512  11725   -212   -212     45       C  
ATOM    199  CD2 LEU A 316     -11.428 -42.530  -0.055  1.00 73.23           C  
ANISOU  199  CD2 LEU A 316     6920  10018  10885   -100     79    -61       C  
ATOM    200  N   THR A 317      -9.208 -46.620  -0.410  1.00 80.27           N  
ANISOU  200  N   THR A 317     7189  10537  12771    420    136     12       N  
ATOM    201  CA  THR A 317      -9.733 -47.529   0.589  1.00 81.42           C  
ANISOU  201  CA  THR A 317     7518  10487  12931    485     -3    185       C  
ATOM    202  C   THR A 317      -9.158 -48.938   0.505  1.00 85.31           C  
ANISOU  202  C   THR A 317     7828  10679  13905    721     77    253       C  
ATOM    203  O   THR A 317      -9.477 -49.762   1.354  1.00 87.48           O  
ANISOU  203  O   THR A 317     8253  10730  14255    799    -18    487       O  
ATOM    204  CB  THR A 317     -11.260 -47.633   0.460  1.00 79.05           C  
ANISOU  204  CB  THR A 317     7521  10152  12363    366    159     41       C  
ATOM    205  OG1 THR A 317     -11.589 -48.290  -0.763  1.00 79.71           O  
ANISOU  205  OG1 THR A 317     7535  10162  12588    399    445   -259       O  
ATOM    206  CG2 THR A 317     -11.896 -46.267   0.418  1.00 77.33           C  
ANISOU  206  CG2 THR A 317     7443  10170  11769    195    131    -30       C  
ATOM    207  N   ASN A 318      -8.330 -49.217  -0.506  1.00 87.62           N  
ANISOU  207  N   ASN A 318     7812  10934  14544    843    305     64       N  
ATOM    208  CA  ASN A 318      -7.735 -50.550  -0.724  1.00 92.34           C  
ANISOU  208  CA  ASN A 318     8192  11177  15714   1104    471     57       C  
ATOM    209  C   ASN A 318      -8.723 -51.658  -1.053  1.00 92.89           C  
ANISOU  209  C   ASN A 318     8488  10913  15891   1106    743   -148       C  
ATOM    210  O   ASN A 318      -8.399 -52.843  -0.885  1.00 96.78           O  
ANISOU  210  O   ASN A 318     8881  10984  16907   1322    848    -67       O  
ATOM    211  CB  ASN A 318      -6.883 -50.978   0.464  1.00 96.30           C  
ANISOU  211  CB  ASN A 318     8510  11540  16536   1320     98    519       C  
ATOM    212  CG  ASN A 318      -5.461 -50.511   0.348  1.00102.18           C  
ANISOU  212  CG  ASN A 318     8760  12453  17608   1431    -35    582       C  
ATOM    213  OD1 ASN A 318      -4.694 -50.596   1.312  1.00110.09           O  
ANISOU  213  OD1 ASN A 318     9546  13478  18805   1576   -461    952       O  
ATOM    214  ND2 ASN A 318      -5.076 -50.032  -0.840  1.00103.94           N  
ANISOU  214  ND2 ASN A 318     8778  12815  17898   1360    325    235       N  
ATOM    215  N   ASP A 319      -9.922 -51.264  -1.500  1.00 89.47           N  
ANISOU  215  N   ASP A 319     8324  10643  15028    867    845   -407       N  
ATOM    216  CA  ASP A 319     -10.976 -52.181  -1.938  1.00 90.41           C  
ANISOU  216  CA  ASP A 319     8609  10511  15230    778   1086   -710       C  
ATOM    217  C   ASP A 319     -10.549 -52.875  -3.239  1.00 93.29           C  
ANISOU  217  C   ASP A 319     8815  10753  15877    855   1454  -1192       C  
ATOM    218  O   ASP A 319      -9.628 -52.397  -3.918  1.00 94.11           O  
ANISOU  218  O   ASP A 319     8722  11077  15958    937   1563  -1294       O  
ATOM    219  CB  ASP A 319     -12.246 -51.378  -2.195  1.00 86.98           C  
ANISOU  219  CB  ASP A 319     8385  10395  14268    517   1035   -881       C  
ATOM    220  CG  ASP A 319     -13.524 -52.094  -1.760  1.00 88.83           C  
ANISOU  220  CG  ASP A 319     8795  10378  14576    369   1095   -932       C  
ATOM    221  OD1 ASP A 319     -13.676 -53.328  -1.946  1.00 93.18           O  
ANISOU  221  OD1 ASP A 319     9327  10513  15562    384   1312  -1113       O  
ATOM    222  OD2 ASP A 319     -14.419 -51.379  -1.253  1.00 88.93           O1-
ANISOU  222  OD2 ASP A 319     8945  10589  14254    218    967   -818       O1-
ATOM    223  N   TRP A 320     -11.198 -53.997  -3.584  1.00 95.34           N  
ANISOU  223  N   TRP A 320     9157  10649  16418    804   1691  -1521       N  
ATOM    224  CA  TRP A 320     -10.974 -54.632  -4.885  1.00 98.23           C  
ANISOU  224  CA  TRP A 320     9442  10932  16949    814   2071  -2125       C  
ATOM    225  C   TRP A 320     -11.973 -54.196  -5.945  1.00 97.07           C  
ANISOU  225  C   TRP A 320     9459  11205  16217    534   2101  -2620       C  
ATOM    226  O   TRP A 320     -11.733 -54.398  -7.134  1.00100.04           O  
ANISOU  226  O   TRP A 320     9820  11722  16469    510   2372  -3131       O  
ATOM    227  CB  TRP A 320     -11.042 -56.126  -4.777  1.00102.90           C  
ANISOU  227  CB  TRP A 320    10016  10846  18234    898   2338  -2310       C  
ATOM    228  CG  TRP A 320     -12.418 -56.618  -4.691  1.00103.25           C  
ANISOU  228  CG  TRP A 320    10264  10717  18249    614   2342  -2534       C  
ATOM    229  CD1 TRP A 320     -13.313 -56.812  -5.724  1.00105.42           C  
ANISOU  229  CD1 TRP A 320    10620  11144  18289    331   2468  -3206       C  
ATOM    230  CD2 TRP A 320     -13.088 -56.997  -3.510  1.00102.71           C  
ANISOU  230  CD2 TRP A 320    10319  10307  18397    554   2221  -2100       C  
ATOM    231  NE1 TRP A 320     -14.510 -57.288  -5.239  1.00104.80           N  
ANISOU  231  NE1 TRP A 320    10639  10813  18365     85   2421  -3234       N  
ATOM    232  CE2 TRP A 320     -14.396 -57.416  -3.882  1.00103.85           C  
ANISOU  232  CE2 TRP A 320    10564  10368  18527    216   2323  -2545       C  
ATOM    233  CE3 TRP A 320     -12.715 -57.032  -2.167  1.00101.97           C  
ANISOU  233  CE3 TRP A 320    10265  10001  18475    740   2035  -1373       C  
ATOM    234  CZ2 TRP A 320     -15.318 -57.857  -2.961  1.00105.49           C  
ANISOU  234  CZ2 TRP A 320    10883  10241  18955     52   2329  -2275       C  
ATOM    235  CZ3 TRP A 320     -13.623 -57.472  -1.256  1.00104.48           C  
ANISOU  235  CZ3 TRP A 320    10772  10020  18903    595   2037  -1080       C  
ATOM    236  CH2 TRP A 320     -14.917 -57.878  -1.651  1.00106.60           C  
ANISOU  236  CH2 TRP A 320    11115  10163  19223    248   2224  -1523       C  
ATOM    237  N   GLU A 321     -13.105 -53.642  -5.515  1.00 93.69           N  
ANISOU  237  N   GLU A 321     9179  10985  15434    333   1829  -2477       N  
ATOM    238  CA  GLU A 321     -14.141 -53.168  -6.437  1.00 93.42           C  
ANISOU  238  CA  GLU A 321     9242  11388  14862     99   1747  -2862       C  
ATOM    239  C   GLU A 321     -14.372 -51.680  -6.222  1.00 89.03           C  
ANISOU  239  C   GLU A 321     8738  11312  13777     82   1461  -2482       C  
ATOM    240  O   GLU A 321     -13.902 -51.130  -5.220  1.00 86.76           O  
ANISOU  240  O   GLU A 321     8437  10962  13566    184   1331  -1995       O  
ATOM    241  CB  GLU A 321     -15.446 -53.935  -6.241  1.00 94.79           C  
ANISOU  241  CB  GLU A 321     9456  11326  15234   -133   1717  -3122       C  
ATOM    242  CG  GLU A 321     -16.043 -53.841  -4.843  1.00 92.90           C  
ANISOU  242  CG  GLU A 321     9255  10860  15181   -170   1572  -2623       C  
ATOM    243  CD  GLU A 321     -17.214 -54.780  -4.666  1.00 97.11           C  
ANISOU  243  CD  GLU A 321     9774  11054  16068   -421   1669  -2893       C  
ATOM    244  OE1 GLU A 321     -17.678 -54.940  -3.512  1.00 96.68           O  
ANISOU  244  OE1 GLU A 321     9772  10726  16236   -465   1676  -2496       O  
ATOM    245  OE2 GLU A 321     -17.657 -55.366  -5.686  1.00101.17           O1-
ANISOU  245  OE2 GLU A 321    10227  11582  16628   -600   1757  -3523       O1-
ATOM    246  N   ASP A 322     -15.082 -51.023  -7.142  1.00 88.69           N  
ANISOU  246  N   ASP A 322     8756  11735  13204    -40   1348  -2698       N  
ATOM    247  CA  ASP A 322     -15.320 -49.595  -6.967  1.00 84.75           C  
ANISOU  247  CA  ASP A 322     8304  11602  12294    -23   1115  -2312       C  
ATOM    248  C   ASP A 322     -16.556 -49.288  -6.175  1.00 81.84           C  
ANISOU  248  C   ASP A 322     7939  11214  11941   -127    888  -2154       C  
ATOM    249  O   ASP A 322     -17.328 -50.181  -5.847  1.00 83.40           O  
ANISOU  249  O   ASP A 322     8093  11165  12428   -252    909  -2355       O  
ATOM    250  CB  ASP A 322     -15.246 -48.779  -8.268  1.00 86.84           C  
ANISOU  250  CB  ASP A 322     8641  12381  11973    -19   1110  -2413       C  
ATOM    251  CG  ASP A 322     -16.219 -49.231  -9.338  1.00 92.43           C  
ANISOU  251  CG  ASP A 322     9389  13382  12345   -161   1018  -2904       C  
ATOM    252  OD1 ASP A 322     -15.855 -49.035 -10.521  1.00 98.57           O  
ANISOU  252  OD1 ASP A 322    10272  14533  12647   -150   1122  -3098       O  
ATOM    253  OD2 ASP A 322     -17.324 -49.739  -9.037  1.00 94.88           O1-
ANISOU  253  OD2 ASP A 322     9623  13595  12832   -302    847  -3101       O1-
ATOM    254  N   HIS A 323     -16.709 -48.012  -5.855  1.00 78.20           N  
ANISOU  254  N   HIS A 323     7515  10968  11228    -80    727  -1801       N  
ATOM    255  CA  HIS A 323     -17.772 -47.507  -5.019  1.00 75.84           C  
ANISOU  255  CA  HIS A 323     7205  10647  10960   -136    579  -1619       C  
ATOM    256  C   HIS A 323     -19.185 -47.850  -5.563  1.00 77.89           C  
ANISOU  256  C   HIS A 323     7338  11067  11189   -270    458  -1938       C  
ATOM    257  O   HIS A 323     -19.344 -48.263  -6.728  1.00 81.03           O  
ANISOU  257  O   HIS A 323     7693  11698  11394   -325    408  -2303       O  
ATOM    258  CB  HIS A 323     -17.586 -46.012  -4.935  1.00 73.53           C  
ANISOU  258  CB  HIS A 323     6971  10559  10407    -43    477  -1282       C  
ATOM    259  CG  HIS A 323     -17.678 -45.341  -6.260  1.00 76.44           C  
ANISOU  259  CG  HIS A 323     7347  11317  10379     10    401  -1322       C  
ATOM    260  ND1 HIS A 323     -16.741 -45.526  -7.252  1.00 79.81           N  
ANISOU  260  ND1 HIS A 323     7824  11899  10601     43    539  -1431       N  
ATOM    261  CD2 HIS A 323     -18.622 -44.522  -6.782  1.00 80.19           C  
ANISOU  261  CD2 HIS A 323     7787  12073  10606     53    210  -1238       C  
ATOM    262  CE1 HIS A 323     -17.089 -44.834  -8.323  1.00 83.13           C  
ANISOU  262  CE1 HIS A 323     8300  12706  10576     85    441  -1388       C  
ATOM    263  NE2 HIS A 323     -18.228 -44.214  -8.064  1.00 84.29           N  
ANISOU  263  NE2 HIS A 323     8387  12934  10704    109    202  -1245       N  
ATOM    264  N   LEU A 324     -20.207 -47.692  -4.719  1.00 76.57           N  
ANISOU  264  N   LEU A 324     7087  10797  11207   -340    418  -1837       N  
ATOM    265  CA  LEU A 324     -21.604 -47.862  -5.161  1.00 78.25           C  
ANISOU  265  CA  LEU A 324     7067  11188  11474   -468    270  -2110       C  
ATOM    266  C   LEU A 324     -22.208 -46.514  -5.549  1.00 77.68           C  
ANISOU  266  C   LEU A 324     6905  11489  11120   -329     30  -1907       C  
ATOM    267  O   LEU A 324     -23.006 -46.430  -6.477  1.00 80.46           O  
ANISOU  267  O   LEU A 324     7065  12187  11316   -348   -226  -2106       O  
ATOM    268  CB  LEU A 324     -22.453 -48.563  -4.086  1.00 78.55           C  
ANISOU  268  CB  LEU A 324     6993  10876  11975   -638    444  -2138       C  
ATOM    269  CG  LEU A 324     -23.940 -48.818  -4.325  1.00 80.69           C  
ANISOU  269  CG  LEU A 324     6918  11259  12479   -818    343  -2427       C  
ATOM    270  CD1 LEU A 324     -24.182 -49.982  -5.260  1.00 84.68           C  
ANISOU  270  CD1 LEU A 324     7282  11772  13120  -1037    281  -2973       C  
ATOM    271  CD2 LEU A 324     -24.599 -49.079  -3.010  1.00 80.40           C  
ANISOU  271  CD2 LEU A 324     6827  10875  12846   -936    630  -2265       C  
ATOM    272  N   ALA A 325     -21.803 -45.466  -4.845  1.00 74.46           N  
ANISOU  272  N   ALA A 325     6630  10997  10662   -185     94  -1514       N  
ATOM    273  CA  ALA A 325     -22.294 -44.125  -5.114  1.00 75.23           C  
ANISOU  273  CA  ALA A 325     6664  11317  10601    -16    -67  -1266       C  
ATOM    274  C   ALA A 325     -21.215 -43.094  -4.761  1.00 72.94           C  
ANISOU  274  C   ALA A 325     6618  10914  10182    108     40   -918       C  
ATOM    275  O   ALA A 325     -20.260 -43.427  -4.055  1.00 70.93           O  
ANISOU  275  O   ALA A 325     6522  10426  10002     48    203   -880       O  
ATOM    276  CB  ALA A 325     -23.589 -43.867  -4.327  1.00 75.71           C  
ANISOU  276  CB  ALA A 325     6488  11280  10996    -28    -41  -1254       C  
ATOM    277  N   VAL A 326     -21.362 -41.859  -5.245  1.00 73.88           N  
ANISOU  277  N   VAL A 326     6741  11179  10150    277    -65   -656       N  
ATOM    278  CA  VAL A 326     -20.393 -40.807  -4.959  1.00 72.71           C  
ANISOU  278  CA  VAL A 326     6794  10872   9961    348     60   -357       C  
ATOM    279  C   VAL A 326     -21.062 -39.450  -4.783  1.00 74.68           C  
ANISOU  279  C   VAL A 326     7001  11035  10336    518     38    -92       C  
ATOM    280  O   VAL A 326     -21.995 -39.110  -5.517  1.00 78.39           O  
ANISOU  280  O   VAL A 326     7301  11720  10763    673   -156     -1       O  
ATOM    281  CB  VAL A 326     -19.262 -40.745  -6.037  1.00 73.51           C  
ANISOU  281  CB  VAL A 326     7029  11157   9744    365     85   -266       C  
ATOM    282  CG1 VAL A 326     -19.824 -40.624  -7.409  1.00 75.86           C  
ANISOU  282  CG1 VAL A 326     7283  11857   9681    471   -113   -227       C  
ATOM    283  CG2 VAL A 326     -18.278 -39.606  -5.762  1.00 72.93           C  
ANISOU  283  CG2 VAL A 326     7100  10884   9726    390    241     37       C  
ATOM    284  N   LYS A 327     -20.606 -38.676  -3.800  1.00 73.70           N  
ANISOU  284  N   LYS A 327     7015  10591  10396    496    222     11       N  
ATOM    285  CA  LYS A 327     -21.096 -37.304  -3.632  1.00 75.74           C  
ANISOU  285  CA  LYS A 327     7264  10657  10854    663    279    235       C  
ATOM    286  C   LYS A 327     -19.914 -36.361  -3.506  1.00 75.97           C  
ANISOU  286  C   LYS A 327     7511  10450  10904    614    425    417       C  
ATOM    287  O   LYS A 327     -19.135 -36.461  -2.571  1.00 74.85           O  
ANISOU  287  O   LYS A 327     7495  10129  10816    431    536    269       O  
ATOM    288  CB  LYS A 327     -22.026 -37.182  -2.416  1.00 75.53           C  
ANISOU  288  CB  LYS A 327     7155  10406  11135    658    432     62       C  
ATOM    289  CG  LYS A 327     -22.940 -35.944  -2.433  1.00 76.97           C  
ANISOU  289  CG  LYS A 327     7204  10406  11632    908    492    235       C  
ATOM    290  CD  LYS A 327     -24.117 -36.177  -3.335  1.00 77.04           C  
ANISOU  290  CD  LYS A 327     6862  10710  11697   1108    236    314       C  
ATOM    291  CE  LYS A 327     -24.956 -34.947  -3.471  1.00 79.47           C  
ANISOU  291  CE  LYS A 327     6986  10831  12374   1430    252    570       C  
ATOM    292  NZ  LYS A 327     -25.951 -35.137  -4.566  1.00 81.85           N1+
ANISOU  292  NZ  LYS A 327     6917  11522  12659   1654   -138    729       N1+
ATOM    293  N   HIS A 328     -19.778 -35.460  -4.464  1.00 78.92           N  
ANISOU  293  N   HIS A 328     7917  10835  11232    765    409    756       N  
ATOM    294  CA  HIS A 328     -18.634 -34.577  -4.527  1.00 80.04           C  
ANISOU  294  CA  HIS A 328     8228  10734  11447    680    589    952       C  
ATOM    295  C   HIS A 328     -19.217 -33.188  -4.525  1.00 84.20           C  
ANISOU  295  C   HIS A 328     8774  10922  12295    875    689   1232       C  
ATOM    296  O   HIS A 328     -19.936 -32.800  -5.449  1.00 87.65           O  
ANISOU  296  O   HIS A 328     9141  11486  12673   1140    567   1568       O  
ATOM    297  CB  HIS A 328     -17.837 -34.863  -5.803  1.00 81.00           C  
ANISOU  297  CB  HIS A 328     8404  11154  11218    669    579   1155       C  
ATOM    298  CG  HIS A 328     -16.554 -34.098  -5.925  1.00 81.98           C  
ANISOU  298  CG  HIS A 328     8641  11046  11458    527    824   1347       C  
ATOM    299  ND1 HIS A 328     -15.741 -34.195  -7.033  1.00 83.72           N  
ANISOU  299  ND1 HIS A 328     8919  11487  11400    498    946   1558       N  
ATOM    300  CD2 HIS A 328     -15.949 -33.216  -5.094  1.00 82.26           C  
ANISOU  300  CD2 HIS A 328     8724  10650  11879    374    998   1325       C  
ATOM    301  CE1 HIS A 328     -14.689 -33.413  -6.878  1.00 84.57           C  
ANISOU  301  CE1 HIS A 328     9064  11292  11777    332   1205   1694       C  
ATOM    302  NE2 HIS A 328     -14.790 -32.810  -5.708  1.00 83.62           N  
ANISOU  302  NE2 HIS A 328     8931  10769  12072    242   1209   1537       N  
ATOM    303  N   PHE A 329     -18.948 -32.448  -3.459  1.00 85.13           N  
ANISOU  303  N   PHE A 329     8982  10603  12760    757    893   1078       N  
ATOM    304  CA  PHE A 329     -19.598 -31.159  -3.264  1.00 89.90           C  
ANISOU  304  CA  PHE A 329     9594  10768  13794    949   1055   1244       C  
ATOM    305  C   PHE A 329     -18.663 -30.174  -2.604  1.00 91.72           C  
ANISOU  305  C   PHE A 329    10001  10500  14346    725   1318   1148       C  
ATOM    306  O   PHE A 329     -17.671 -30.560  -1.987  1.00 89.52           O  
ANISOU  306  O   PHE A 329     9795  10258  13959    408   1321    858       O  
ATOM    307  CB  PHE A 329     -20.898 -31.306  -2.446  1.00 90.26           C  
ANISOU  307  CB  PHE A 329     9489  10757  14045   1090   1073    980       C  
ATOM    308  CG  PHE A 329     -20.687 -31.756  -1.006  1.00 88.61           C  
ANISOU  308  CG  PHE A 329     9387  10466  13812    815   1208    471       C  
ATOM    309  CD1 PHE A 329     -20.547 -33.110  -0.691  1.00 86.31           C  
ANISOU  309  CD1 PHE A 329     9077  10547  13169    646   1063    250       C  
ATOM    310  CD2 PHE A 329     -20.650 -30.829   0.030  1.00 90.95           C  
ANISOU  310  CD2 PHE A 329     9830  10306  14418    728   1488    218       C  
ATOM    311  CE1 PHE A 329     -20.355 -33.530   0.627  1.00 84.99           C  
ANISOU  311  CE1 PHE A 329     9053  10335  12904    418   1167   -115       C  
ATOM    312  CE2 PHE A 329     -20.468 -31.240   1.348  1.00 90.10           C  
ANISOU  312  CE2 PHE A 329     9876  10205  14150    471   1585   -234       C  
ATOM    313  CZ  PHE A 329     -20.323 -32.592   1.647  1.00 87.12           C  
ANISOU  313  CZ  PHE A 329     9496  10240  13365    328   1411   -353       C  
ATOM    314  N   SER A 330     -18.981 -28.897  -2.749  1.00 96.95           N  
ANISOU  314  N   SER A 330    10706  10678  15449    893   1521   1392       N  
ATOM    315  CA  SER A 330     -18.238 -27.868  -2.057  1.00100.19           C  
ANISOU  315  CA  SER A 330    11271  10520  16274    654   1803   1213       C  
ATOM    316  C   SER A 330     -19.220 -26.973  -1.338  1.00104.21           C  
ANISOU  316  C   SER A 330    11787  10522  17284    842   2035   1043       C  
ATOM    317  O   SER A 330     -20.172 -26.467  -1.928  1.00107.32           O  
ANISOU  317  O   SER A 330    12069  10762  17946   1241   2064   1421       O  
ATOM    318  CB  SER A 330     -17.363 -27.067  -3.015  1.00103.33           C  
ANISOU  318  CB  SER A 330    11748  10666  16845    604   1958   1688       C  
ATOM    319  OG  SER A 330     -18.148 -26.199  -3.797  1.00108.39           O  
ANISOU  319  OG  SER A 330    12390  11020  17772    992   2054   2231       O  
ATOM    320  N   VAL A 331     -18.986 -26.826  -0.042  1.00105.10           N  
ANISOU  320  N   VAL A 331    12023  10413  17496    563   2187    453       N  
ATOM    321  CA  VAL A 331     -19.734 -25.914   0.790  1.00110.18           C  
ANISOU  321  CA  VAL A 331    12724  10513  18627    664   2514    142       C  
ATOM    322  C   VAL A 331     -19.044 -24.562   0.684  1.00116.10           C  
ANISOU  322  C   VAL A 331    13614  10552  19945    535   2801    207       C  
ATOM    323  O   VAL A 331     -17.844 -24.443   0.943  1.00116.27           O  
ANISOU  323  O   VAL A 331    13749  10509  19916    113   2786     -5       O  
ATOM    324  CB  VAL A 331     -19.758 -26.382   2.247  1.00108.66           C  
ANISOU  324  CB  VAL A 331    12670  10451  18165    381   2575   -563       C  
ATOM    325  CG1 VAL A 331     -20.545 -25.403   3.098  1.00114.49           C  
ANISOU  325  CG1 VAL A 331    13491  10614  19393    483   3007   -959       C  
ATOM    326  CG2 VAL A 331     -20.364 -27.765   2.340  1.00103.79           C  
ANISOU  326  CG2 VAL A 331    11924  10474  17035    466   2343   -573       C  
ATOM    327  N   GLU A 332     -19.806 -23.559   0.264  1.00121.97           N  
ANISOU  327  N   GLU A 332    14306  10744  21290    907   3053    533       N  
ATOM    328  CA  GLU A 332     -19.291 -22.214   0.078  1.00128.67           C  
ANISOU  328  CA  GLU A 332    15287  10788  22813    836   3392    679       C  
ATOM    329  C   GLU A 332     -20.030 -21.323   1.059  1.00134.21           C  
ANISOU  329  C   GLU A 332    16052  10811  24131    934   3807    175       C  
ATOM    330  O   GLU A 332     -21.178 -21.592   1.408  1.00134.21           O  
ANISOU  330  O   GLU A 332    15910  10937  24145   1260   3849     40       O  
ATOM    331  CB  GLU A 332     -19.526 -21.742  -1.366  1.00131.96           C  
ANISOU  331  CB  GLU A 332    15622  11062  23455   1246   3371   1620       C  
ATOM    332  CG  GLU A 332     -18.989 -22.696  -2.454  1.00127.68           C  
ANISOU  332  CG  GLU A 332    15029  11276  22207   1218   2997   2115       C  
ATOM    333  CD  GLU A 332     -17.637 -22.277  -3.002  1.00129.71           C  
ANISOU  333  CD  GLU A 332    15423  11330  22530    868   3151   2380       C  
ATOM    334  OE1 GLU A 332     -16.674 -23.080  -2.951  1.00125.48           O  
ANISOU  334  OE1 GLU A 332    14873  11275  21528    495   2988   2152       O  
ATOM    335  OE2 GLU A 332     -17.541 -21.133  -3.489  1.00136.55           O1-
ANISOU  335  OE2 GLU A 332    16386  11516  23978    976   3469   2842       O1-
ATOM    336  N   GLY A 333     -19.368 -20.277   1.528  1.00139.73           N  
ANISOU  336  N   GLY A 333    16943  10777  25370    626   4150   -164       N  
ATOM    337  CA  GLY A 333     -20.029 -19.315   2.400  1.00146.52           C  
ANISOU  337  CA  GLY A 333    17894  10879  26897    718   4630   -692       C  
ATOM    338  C   GLY A 333     -19.258 -18.958   3.657  1.00149.13           C  
ANISOU  338  C   GLY A 333    18490  10940  27232    114   4820  -1660       C  
ATOM    339  O   GLY A 333     -18.132 -18.435   3.587  1.00151.57           O  
ANISOU  339  O   GLY A 333    18904  10917  27767   -323   4849  -1758       O  
ATOM    340  N   GLN A 334     -19.883 -19.224   4.806  1.00149.31           N  
ANISOU  340  N   GLN A 334    18611  11118  27001     76   4961  -2387       N  
ATOM    341  CA  GLN A 334     -19.290 -18.919   6.112  1.00152.24           C  
ANISOU  341  CA  GLN A 334    19285  11333  27226   -485   5115  -3395       C  
ATOM    342  C   GLN A 334     -17.962 -19.680   6.306  1.00147.04           C  
ANISOU  342  C   GLN A 334    18686  11337  25845  -1047   4591  -3549       C  
ATOM    343  O   GLN A 334     -16.932 -19.079   6.647  1.00150.81           O  
ANISOU  343  O   GLN A 334    19281  11488  26531  -1556   4594  -3980       O  
ATOM    344  CB  GLN A 334     -20.299 -19.170   7.253  1.00153.92           C  
ANISOU  344  CB  GLN A 334    19621  11702  27157   -377   5400  -4067       C  
ATOM    345  CG  GLN A 334     -21.101 -20.480   7.144  1.00147.31           C  
ANISOU  345  CG  GLN A 334    18594  11723  25651    -64   5137  -3723       C  
ATOM    346  CD  GLN A 334     -22.353 -20.509   8.025  1.00151.03           C  
ANISOU  346  CD  GLN A 334    19087  12153  26143    177   5608  -4208       C  
ATOM    347  OE1 GLN A 334     -22.966 -21.565   8.204  1.00147.22           O  
ANISOU  347  OE1 GLN A 334    18492  12337  25107    306   5478  -4104       O  
ATOM    348  NE2 GLN A 334     -22.739 -19.353   8.569  1.00158.48           N  
ANISOU  348  NE2 GLN A 334    20161  12275  27777    229   6214  -4754       N  
ATOM    349  N   LEU A 335     -17.988 -20.987   6.049  1.00138.47           N  
ANISOU  349  N   LEU A 335    17473  11139  24000   -946   4146  -3189       N  
ATOM    350  CA  LEU A 335     -16.783 -21.797   6.088  1.00133.27           C  
ANISOU  350  CA  LEU A 335    16789  11107  22741  -1360   3639  -3198       C  
ATOM    351  C   LEU A 335     -16.700 -22.618   4.827  1.00126.40           C  
ANISOU  351  C   LEU A 335    15654  10700  21668  -1076   3335  -2342       C  
ATOM    352  O   LEU A 335     -17.473 -23.554   4.660  1.00121.79           O  
ANISOU  352  O   LEU A 335    14983  10628  20663   -759   3190  -2090       O  
ATOM    353  CB  LEU A 335     -16.804 -22.720   7.304  1.00131.19           C  
ANISOU  353  CB  LEU A 335    16707  11506  21630  -1585   3400  -3767       C  
ATOM    354  CG  LEU A 335     -15.770 -23.844   7.325  1.00126.58           C  
ANISOU  354  CG  LEU A 335    16036  11683  20376  -1857   2813  -3637       C  
ATOM    355  CD1 LEU A 335     -14.341 -23.299   7.280  1.00130.79           C  
ANISOU  355  CD1 LEU A 335    16490  12026  21175  -2345   2614  -3827       C  
ATOM    356  CD2 LEU A 335     -15.977 -24.718   8.538  1.00126.24           C  
ANISOU  356  CD2 LEU A 335    16222  12235  19506  -1991   2626  -4082       C  
ATOM    357  N   GLU A 336     -15.774 -22.278   3.937  1.00126.25           N  
ANISOU  357  N   GLU A 336    15511  10503  21952  -1213   3277  -1927       N  
ATOM    358  CA  GLU A 336     -15.630 -23.060   2.711  1.00120.71           C  
ANISOU  358  CA  GLU A 336    14604  10278  20979   -972   3030  -1169       C  
ATOM    359  C   GLU A 336     -14.704 -24.269   2.864  1.00114.52           C  
ANISOU  359  C   GLU A 336    13718  10244  19548  -1248   2582  -1258       C  
ATOM    360  O   GLU A 336     -13.640 -24.199   3.480  1.00115.67           O  
ANISOU  360  O   GLU A 336    13857  10420  19672  -1706   2436  -1674       O  
ATOM    361  CB  GLU A 336     -15.308 -22.200   1.472  1.00124.59           C  
ANISOU  361  CB  GLU A 336    15023  10271  22042   -858   3265   -504       C  
ATOM    362  CG  GLU A 336     -13.972 -21.465   1.488  1.00131.10           C  
ANISOU  362  CG  GLU A 336    15833  10673  23305  -1372   3397   -659       C  
ATOM    363  CD  GLU A 336     -13.851 -20.407   0.379  1.00139.55           C  
ANISOU  363  CD  GLU A 336    16904  11062  25056  -1239   3789     21       C  
ATOM    364  OE1 GLU A 336     -12.851 -20.449  -0.390  1.00140.82           O  
ANISOU  364  OE1 GLU A 336    16945  11308  25250  -1458   3807    404       O  
ATOM    365  OE2 GLU A 336     -14.749 -19.529   0.281  1.00144.66           O1-
ANISOU  365  OE2 GLU A 336    17665  11066  26231   -903   4114    200       O1-
ATOM    366  N   PHE A 337     -15.178 -25.386   2.330  1.00108.18           N  
ANISOU  366  N   PHE A 337    12811  10030  18261   -948   2355   -889       N  
ATOM    367  CA  PHE A 337     -14.456 -26.644   2.328  1.00102.65           C  
ANISOU  367  CA  PHE A 337    11993   9997  17011  -1091   1972   -876       C  
ATOM    368  C   PHE A 337     -14.994 -27.537   1.223  1.00 98.06           C  
ANISOU  368  C   PHE A 337    11280   9840  16136   -718   1858   -331       C  
ATOM    369  O   PHE A 337     -16.007 -27.240   0.588  1.00 98.57           O  
ANISOU  369  O   PHE A 337    11338   9772  16341   -353   1997      0       O  
ATOM    370  CB  PHE A 337     -14.502 -27.355   3.695  1.00101.12           C  
ANISOU  370  CB  PHE A 337    11926  10151  16342  -1276   1748  -1432       C  
ATOM    371  CG  PHE A 337     -15.808 -28.039   3.999  1.00 97.66           C  
ANISOU  371  CG  PHE A 337    11564   9957  15582   -963   1786  -1435       C  
ATOM    372  CD1 PHE A 337     -16.076 -29.319   3.507  1.00 91.81           C  
ANISOU  372  CD1 PHE A 337    10694   9736  14451   -766   1564  -1124       C  
ATOM    373  CD2 PHE A 337     -16.761 -27.416   4.806  1.00 99.75           C  
ANISOU  373  CD2 PHE A 337    12009   9905  15983   -891   2091  -1799       C  
ATOM    374  CE1 PHE A 337     -17.283 -29.954   3.787  1.00 89.12           C  
ANISOU  374  CE1 PHE A 337    10373   9588  13899   -530   1627  -1144       C  
ATOM    375  CE2 PHE A 337     -17.965 -28.041   5.100  1.00 96.80           C  
ANISOU  375  CE2 PHE A 337    11643   9750  15384   -628   2188  -1808       C  
ATOM    376  CZ  PHE A 337     -18.228 -29.312   4.591  1.00 92.36           C  
ANISOU  376  CZ  PHE A 337    10922   9702  14465   -464   1945  -1469       C  
ATOM    377  N   ARG A 338     -14.306 -28.643   1.015  1.00 93.97           N  
ANISOU  377  N   ARG A 338    10639   9836  15229   -809   1583   -270       N  
ATOM    378  CA  ARG A 338     -14.546 -29.474  -0.128  1.00 90.61           C  
ANISOU  378  CA  ARG A 338    10094   9800  14533   -546   1490    165       C  
ATOM    379  C   ARG A 338     -14.610 -30.952   0.315  1.00 85.53           C  
ANISOU  379  C   ARG A 338     9400   9681  13416   -541   1205    -17       C  
ATOM    380  O   ARG A 338     -13.784 -31.413   1.114  1.00 84.80           O  
ANISOU  380  O   ARG A 338     9288   9729  13201   -791   1026   -292       O  
ATOM    381  CB  ARG A 338     -13.409 -29.227  -1.121  1.00 92.29           C  
ANISOU  381  CB  ARG A 338    10189   9992  14885   -675   1582    488       C  
ATOM    382  CG  ARG A 338     -13.761 -29.538  -2.542  1.00 93.69           C  
ANISOU  382  CG  ARG A 338    10336  10420  14841   -382   1627   1006       C  
ATOM    383  CD  ARG A 338     -14.036 -28.284  -3.329  1.00100.77           C  
ANISOU  383  CD  ARG A 338    11331  10886  16069   -237   1911   1464       C  
ATOM    384  NE  ARG A 338     -12.810 -27.740  -3.917  1.00107.21           N  
ANISOU  384  NE  ARG A 338    12103  11512  17116   -486   2164   1697       N  
ATOM    385  CZ  ARG A 338     -11.978 -26.894  -3.308  1.00111.95           C  
ANISOU  385  CZ  ARG A 338    12669  11638  18228   -840   2346   1478       C  
ATOM    386  NH1 ARG A 338     -12.229 -26.470  -2.070  1.00114.22           N1+
ANISOU  386  NH1 ARG A 338    13012  11608  18777   -986   2285    978       N1+
ATOM    387  NH2 ARG A 338     -10.889 -26.471  -3.940  1.00114.99           N  
ANISOU  387  NH2 ARG A 338    12956  11872  18862  -1079   2616   1723       N  
ATOM    388  N   ALA A 339     -15.596 -31.690  -0.187  1.00 82.32           N  
ANISOU  388  N   ALA A 339     8955   9543  12777   -261   1145    146       N  
ATOM    389  CA  ALA A 339     -15.749 -33.093   0.196  1.00 78.15           C  
ANISOU  389  CA  ALA A 339     8388   9411  11893   -259    939     -3       C  
ATOM    390  C   ALA A 339     -16.061 -34.003  -0.981  1.00 75.81           C  
ANISOU  390  C   ALA A 339     7962   9457  11385    -63    850    239       C  
ATOM    391  O   ALA A 339     -16.861 -33.661  -1.863  1.00 76.77           O  
ANISOU  391  O   ALA A 339     8044   9596  11527    163    891    479       O  
ATOM    392  CB  ALA A 339     -16.811 -33.240   1.256  1.00 78.16           C  
ANISOU  392  CB  ALA A 339     8496   9370  11829   -217    988   -264       C  
ATOM    393  N   LEU A 340     -15.416 -35.166  -0.977  1.00 73.05           N  
ANISOU  393  N   LEU A 340     7543   9375  10837   -145    710    161       N  
ATOM    394  CA  LEU A 340     -15.681 -36.217  -1.943  1.00 71.14           C  
ANISOU  394  CA  LEU A 340     7200   9446  10382    -10    639    245       C  
ATOM    395  C   LEU A 340     -16.094 -37.429  -1.138  1.00 69.20           C  
ANISOU  395  C   LEU A 340     6952   9309  10029    -38    531     27       C  
ATOM    396  O   LEU A 340     -15.289 -37.970  -0.404  1.00 68.84           O  
ANISOU  396  O   LEU A 340     6920   9261   9975   -165    453    -68       O  
ATOM    397  CB  LEU A 340     -14.407 -36.534  -2.700  1.00 71.38           C  
ANISOU  397  CB  LEU A 340     7138   9603  10379    -83    674    333       C  
ATOM    398  CG  LEU A 340     -14.468 -37.148  -4.084  1.00 70.91           C  
ANISOU  398  CG  LEU A 340     7027   9837  10078     42    714    439       C  
ATOM    399  CD1 LEU A 340     -13.127 -37.786  -4.373  1.00 71.57           C  
ANISOU  399  CD1 LEU A 340     6985  10009  10197    -55    800    382       C  
ATOM    400  CD2 LEU A 340     -15.566 -38.156  -4.179  1.00 69.70           C  
ANISOU  400  CD2 LEU A 340     6854   9875   9751    149    574    277       C  
ATOM    401  N   LEU A 341     -17.348 -37.843  -1.251  1.00 68.99           N  
ANISOU  401  N   LEU A 341     6889   9367   9957     78    523    -19       N  
ATOM    402  CA  LEU A 341     -17.872 -38.912  -0.400  1.00 68.29           C  
ANISOU  402  CA  LEU A 341     6812   9303   9829     22    507   -193       C  
ATOM    403  C   LEU A 341     -18.300 -40.137  -1.190  1.00 67.92           C  
ANISOU  403  C   LEU A 341     6627   9450   9726     67    445   -259       C  
ATOM    404  O   LEU A 341     -18.916 -40.004  -2.258  1.00 69.37           O  
ANISOU  404  O   LEU A 341     6690   9799   9865    177    389   -229       O  
ATOM    405  CB  LEU A 341     -19.044 -38.408   0.423  1.00 69.34           C  
ANISOU  405  CB  LEU A 341     6984   9303  10057     49    639   -279       C  
ATOM    406  CG  LEU A 341     -18.722 -37.256   1.373  1.00 71.68           C  
ANISOU  406  CG  LEU A 341     7462   9365  10407    -30    750   -340       C  
ATOM    407  CD1 LEU A 341     -19.988 -36.946   2.212  1.00 73.38           C  
ANISOU  407  CD1 LEU A 341     7708   9455  10717     10    977   -492       C  
ATOM    408  CD2 LEU A 341     -17.471 -37.546   2.241  1.00 68.87           C  
ANISOU  408  CD2 LEU A 341     7264   9013   9889   -230    637   -408       C  
ATOM    409  N   PHE A 342     -17.975 -41.318  -0.660  1.00 66.54           N  
ANISOU  409  N   PHE A 342     6478   9246   9558    -17    438   -348       N  
ATOM    410  CA  PHE A 342     -18.268 -42.568  -1.326  1.00 66.71           C  
ANISOU  410  CA  PHE A 342     6383   9355   9608    -17    423   -482       C  
ATOM    411  C   PHE A 342     -19.084 -43.499  -0.447  1.00 67.50           C  
ANISOU  411  C   PHE A 342     6493   9318   9836   -104    516   -570       C  
ATOM    412  O   PHE A 342     -18.788 -43.645   0.742  1.00 68.30           O  
ANISOU  412  O   PHE A 342     6757   9271   9923   -165    573   -473       O  
ATOM    413  CB  PHE A 342     -16.986 -43.289  -1.640  1.00 66.18           C  
ANISOU  413  CB  PHE A 342     6311   9275   9558    -20    408   -484       C  
ATOM    414  CG  PHE A 342     -16.131 -42.622  -2.681  1.00 67.38           C  
ANISOU  414  CG  PHE A 342     6421   9575   9605     35    413   -418       C  
ATOM    415  CD1 PHE A 342     -16.448 -42.723  -4.040  1.00 68.28           C  
ANISOU  415  CD1 PHE A 342     6476   9920   9544     91    425   -511       C  
ATOM    416  CD2 PHE A 342     -14.961 -41.954  -2.313  1.00 66.29           C  
ANISOU  416  CD2 PHE A 342     6295   9366   9524      6    414   -272       C  
ATOM    417  CE1 PHE A 342     -15.647 -42.149  -4.995  1.00 68.00           C  
ANISOU  417  CE1 PHE A 342     6451  10035   9352    131    504   -406       C  
ATOM    418  CE2 PHE A 342     -14.149 -41.379  -3.268  1.00 65.95           C  
ANISOU  418  CE2 PHE A 342     6192   9427   9437     25    505   -189       C  
ATOM    419  CZ  PHE A 342     -14.488 -41.483  -4.608  1.00 68.33           C  
ANISOU  419  CZ  PHE A 342     6488   9950   9524     95    584   -230       C  
ATOM    420  N   VAL A 343     -20.103 -44.134  -1.025  1.00 68.22           N  
ANISOU  420  N   VAL A 343     6410   9472  10037   -132    529   -748       N  
ATOM    421  CA  VAL A 343     -20.689 -45.331  -0.429  1.00 68.62           C  
ANISOU  421  CA  VAL A 343     6434   9338  10298   -262    671   -847       C  
ATOM    422  C   VAL A 343     -20.063 -46.599  -1.070  1.00 69.53           C  
ANISOU  422  C   VAL A 343     6520   9366  10531   -296    662   -994       C  
ATOM    423  O   VAL A 343     -20.046 -46.744  -2.293  1.00 69.81           O  
ANISOU  423  O   VAL A 343     6432   9585  10505   -277    563  -1211       O  
ATOM    424  CB  VAL A 343     -22.206 -45.379  -0.615  1.00 70.26           C  
ANISOU  424  CB  VAL A 343     6393   9610  10691   -328    723  -1020       C  
ATOM    425  CG1 VAL A 343     -22.761 -46.623   0.045  1.00 71.82           C  
ANISOU  425  CG1 VAL A 343     6561   9552  11173   -513    948  -1102       C  
ATOM    426  CG2 VAL A 343     -22.860 -44.131  -0.079  1.00 69.38           C  
ANISOU  426  CG2 VAL A 343     6259   9543  10559   -245    786   -910       C  
ATOM    427  N   PRO A 344     -19.541 -47.513  -0.242  1.00 70.12           N  
ANISOU  427  N   PRO A 344     6727   9155  10761   -330    778   -871       N  
ATOM    428  CA  PRO A 344     -19.078 -48.803  -0.705  1.00 72.39           C  
ANISOU  428  CA  PRO A 344     6971   9230  11303   -344    846  -1016       C  
ATOM    429  C   PRO A 344     -20.231 -49.725  -1.138  1.00 76.04           C  
ANISOU  429  C   PRO A 344     7267   9572  12053   -526    968  -1344       C  
ATOM    430  O   PRO A 344     -21.393 -49.516  -0.750  1.00 77.30           O  
ANISOU  430  O   PRO A 344     7331   9759  12278   -650   1035  -1369       O  
ATOM    431  CB  PRO A 344     -18.409 -49.392   0.538  1.00 73.08           C  
ANISOU  431  CB  PRO A 344     7249   9012  11505   -302    921   -670       C  
ATOM    432  CG  PRO A 344     -18.186 -48.264   1.459  1.00 70.86           C  
ANISOU  432  CG  PRO A 344     7127   8899  10895   -266    815   -403       C  
ATOM    433  CD  PRO A 344     -19.307 -47.343   1.198  1.00 70.21           C  
ANISOU  433  CD  PRO A 344     6961   9025  10689   -337    845   -565       C  
ATOM    434  N   ARG A 345     -19.908 -50.742  -1.933  1.00 78.71           N  
ANISOU  434  N   ARG A 345     7537   9758  12612   -560   1024  -1640       N  
ATOM    435  CA  ARG A 345     -20.889 -51.711  -2.393  1.00 82.47           C  
ANISOU  435  CA  ARG A 345     7840  10074  13421   -786   1130  -2045       C  
ATOM    436  C   ARG A 345     -21.180 -52.723  -1.305  1.00 85.72           C  
ANISOU  436  C   ARG A 345     8326   9956  14285   -905   1419  -1852       C  
ATOM    437  O   ARG A 345     -22.202 -53.434  -1.354  1.00 89.31           O  
ANISOU  437  O   ARG A 345     8616  10207  15107  -1157   1574  -2112       O  
ATOM    438  CB  ARG A 345     -20.377 -52.448  -3.626  1.00 84.69           C  
ANISOU  438  CB  ARG A 345     8066  10341  13768   -798   1135  -2507       C  
ATOM    439  CG  ARG A 345     -20.111 -51.563  -4.816  1.00 83.60           C  
ANISOU  439  CG  ARG A 345     7900  10748  13114   -703    904  -2689       C  
ATOM    440  CD  ARG A 345     -19.712 -52.398  -6.003  1.00 86.87           C  
ANISOU  440  CD  ARG A 345     8300  11163  13542   -758    983  -3227       C  
ATOM    441  NE  ARG A 345     -19.378 -51.588  -7.169  1.00 87.04           N  
ANISOU  441  NE  ARG A 345     8361  11738  12971   -667    816  -3355       N  
ATOM    442  CZ  ARG A 345     -20.256 -51.150  -8.069  1.00 89.98           C  
ANISOU  442  CZ  ARG A 345     8641  12599  12946   -768    542  -3612       C  
ATOM    443  NH1 ARG A 345     -21.554 -51.414  -7.947  1.00 91.92           N1+
ANISOU  443  NH1 ARG A 345     8671  12865  13389   -976    376  -3823       N1+
ATOM    444  NH2 ARG A 345     -19.831 -50.433  -9.097  1.00 91.42           N  
ANISOU  444  NH2 ARG A 345     8930  13268  12536   -658    429  -3623       N  
ATOM    445  N   ARG A 346     -20.273 -52.803  -0.332  1.00 85.67           N  
ANISOU  445  N   ARG A 346     8557   9730  14262   -736   1483  -1379       N  
ATOM    446  CA  ARG A 346     -20.385 -53.778   0.753  1.00 89.51           C  
ANISOU  446  CA  ARG A 346     9196   9708  15105   -797   1755  -1052       C  
ATOM    447  C   ARG A 346     -20.134 -53.151   2.118  1.00 88.44           C  
ANISOU  447  C   ARG A 346     9325   9654  14622   -694   1733   -482       C  
ATOM    448  O   ARG A 346     -19.107 -52.510   2.348  1.00 86.65           O  
ANISOU  448  O   ARG A 346     9212   9636  14075   -485   1496   -251       O  
ATOM    449  CB  ARG A 346     -19.445 -54.968   0.526  1.00 92.71           C  
ANISOU  449  CB  ARG A 346     9643   9637  15945   -674   1868  -1047       C  
ATOM    450  CG  ARG A 346     -19.968 -56.002  -0.440  1.00 97.47           C  
ANISOU  450  CG  ARG A 346    10059   9929  17046   -881   2060  -1626       C  
ATOM    451  CD  ARG A 346     -18.879 -56.976  -0.853  1.00102.97           C  
ANISOU  451  CD  ARG A 346    10777  10188  18159   -693   2182  -1715       C  
ATOM    452  NE  ARG A 346     -19.462 -58.238  -1.317  1.00111.60           N  
ANISOU  452  NE  ARG A 346    11773  10731  19896   -935   2490  -2174       N  
ATOM    453  CZ  ARG A 346     -19.696 -58.556  -2.592  1.00114.74           C  
ANISOU  453  CZ  ARG A 346    12002  11205  20389  -1103   2504  -2938       C  
ATOM    454  NH1 ARG A 346     -19.393 -57.707  -3.575  1.00112.36           N1+
ANISOU  454  NH1 ARG A 346    11633  11534  19523  -1028   2241  -3265       N1+
ATOM    455  NH2 ARG A 346     -20.236 -59.735  -2.887  1.00120.14           N  
ANISOU  455  NH2 ARG A 346    12605  11322  21720  -1368   2798  -3383       N  
ATOM    456  N   ALA A 347     -21.095 -53.349   3.012  1.00 90.90           N  
ANISOU  456  N   ALA A 347     9723   9815  14999   -874   2001   -300       N  
ATOM    457  CA  ALA A 347     -21.015 -52.884   4.386  1.00 91.52           C  
ANISOU  457  CA  ALA A 347    10116   9969  14686   -829   2061    194       C  
ATOM    458  C   ALA A 347     -19.758 -53.424   5.049  1.00 93.57           C  
ANISOU  458  C   ALA A 347    10640  10026  14885   -605   1930    682       C  
ATOM    459  O   ALA A 347     -19.504 -54.631   5.028  1.00 97.56           O  
ANISOU  459  O   ALA A 347    11165  10054  15850   -571   2079    831       O  
ATOM    460  CB  ALA A 347     -22.269 -53.324   5.167  1.00 95.23           C  
ANISOU  460  CB  ALA A 347    10635  10216  15331  -1088   2512    307       C  
ATOM    461  N   PRO A 348     -18.956 -52.533   5.627  1.00 91.85           N  
ANISOU  461  N   PRO A 348    10595  10149  14153   -447   1631    923       N  
ATOM    462  CA  PRO A 348     -17.751 -52.944   6.315  1.00 94.67           C  
ANISOU  462  CA  PRO A 348    11142  10409  14419   -220   1401   1407       C  
ATOM    463  C   PRO A 348     -18.025 -53.588   7.660  1.00100.03           C  
ANISOU  463  C   PRO A 348    12198  10873  14935   -253   1598   1980       C  
ATOM    464  O   PRO A 348     -19.120 -53.470   8.205  1.00101.03           O  
ANISOU  464  O   PRO A 348    12479  11009  14897   -477   1948   1989       O  
ATOM    465  CB  PRO A 348     -17.015 -51.628   6.522  1.00 91.72           C  
ANISOU  465  CB  PRO A 348    10797  10533  13519   -136   1014   1381       C  
ATOM    466  CG  PRO A 348     -18.076 -50.625   6.559  1.00 89.33           C  
ANISOU  466  CG  PRO A 348    10520  10493  12929   -336   1179   1087       C  
ATOM    467  CD  PRO A 348     -19.064 -51.075   5.546  1.00 88.02           C  
ANISOU  467  CD  PRO A 348    10080  10143  13219   -465   1451    709       C  
ATOM    468  N   PHE A 349     -17.023 -54.290   8.166  1.00104.42           N  
ANISOU  468  N   PHE A 349    12883  11231  15560    -12   1394   2484       N  
ATOM    469  CA  PHE A 349     -17.009 -54.694   9.549  1.00110.70           C  
ANISOU  469  CA  PHE A 349    14111  11968  15981     20   1436   3157       C  
ATOM    470  C   PHE A 349     -16.470 -53.508  10.347  1.00110.32           C  
ANISOU  470  C   PHE A 349    14272  12538  15106     50   1020   3245       C  
ATOM    471  O   PHE A 349     -15.700 -52.694   9.838  1.00106.94           O  
ANISOU  471  O   PHE A 349    13601  12425  14604    137    626   2944       O  
ATOM    472  CB  PHE A 349     -16.103 -55.891   9.727  1.00115.88           C  
ANISOU  472  CB  PHE A 349    14784  12171  17073    321   1306   3705       C  
ATOM    473  CG  PHE A 349     -16.361 -56.656  10.974  1.00123.52           C  
ANISOU  473  CG  PHE A 349    16212  12895  17823    338   1503   4470       C  
ATOM    474  CD1 PHE A 349     -17.481 -57.468  11.084  1.00127.09           C  
ANISOU  474  CD1 PHE A 349    16798  12849  18639    103   2137   4562       C  
ATOM    475  CD2 PHE A 349     -15.473 -56.587  12.040  1.00128.84           C  
ANISOU  475  CD2 PHE A 349    17180  13844  17929    577   1049   5125       C  
ATOM    476  CE1 PHE A 349     -17.720 -58.202  12.251  1.00135.38           C  
ANISOU  476  CE1 PHE A 349    18319  13639  19480    109   2397   5356       C  
ATOM    477  CE2 PHE A 349     -15.699 -57.318  13.212  1.00137.13           C  
ANISOU  477  CE2 PHE A 349    18723  14700  18679    614   1225   5931       C  
ATOM    478  CZ  PHE A 349     -16.828 -58.125  13.318  1.00140.02           C  
ANISOU  478  CZ  PHE A 349    19268  14529  19402    381   1942   6073       C  
ATOM    479  N   ASN A 359     -15.034 -40.276  10.865  1.00105.21           N  
ANISOU  479  N   ASN A 359    12221  14284  13469  -1861    239   1063       N  
ATOM    480  CA  ASN A 359     -14.614 -41.624  11.346  1.00109.67           C  
ANISOU  480  CA  ASN A 359    12724  14985  13960  -1728    290   2040       C  
ATOM    481  C   ASN A 359     -13.497 -42.277  10.514  1.00108.28           C  
ANISOU  481  C   ASN A 359    12394  14425  14319  -1328    120   2613       C  
ATOM    482  O   ASN A 359     -12.414 -42.546  11.033  1.00112.50           O  
ANISOU  482  O   ASN A 359    12719  15431  14591  -1258   -141   3335       O  
ATOM    483  CB  ASN A 359     -15.822 -42.558  11.456  1.00110.99           C  
ANISOU  483  CB  ASN A 359    12993  14733  14443  -1728    782   2108       C  
ATOM    484  CG  ASN A 359     -15.590 -43.694  12.447  1.00119.04           C  
ANISOU  484  CG  ASN A 359    13942  16054  15232  -1733    957   3188       C  
ATOM    485  OD1 ASN A 359     -14.447 -44.105  12.694  1.00122.21           O  
ANISOU  485  OD1 ASN A 359    14143  16748  15541  -1539    695   4079       O  
ATOM    486  ND2 ASN A 359     -16.677 -44.200  13.028  1.00122.35           N  
ANISOU  486  ND2 ASN A 359    14471  16418  15596  -1940   1418   3198       N  
ATOM    487  N   ASN A 360     -13.783 -42.549   9.239  1.00103.64           N  
ANISOU  487  N   ASN A 360    11834  13080  14464  -1107    292   2266       N  
ATOM    488  CA  ASN A 360     -12.787 -43.049   8.272  1.00101.90           C  
ANISOU  488  CA  ASN A 360    11440  12453  14822   -824    241   2514       C  
ATOM    489  C   ASN A 360     -12.680 -42.102   7.066  1.00 95.53           C  
ANISOU  489  C   ASN A 360    10679  11499  14117   -827     60   1817       C  
ATOM    490  O   ASN A 360     -12.571 -42.517   5.916  1.00 93.77           O  
ANISOU  490  O   ASN A 360    10365  10875  14386   -725    211   1615       O  
ATOM    491  CB  ASN A 360     -13.131 -44.476   7.831  1.00104.40           C  
ANISOU  491  CB  ASN A 360    11641  12069  15956   -663    775   2757       C  
ATOM    492  CG  ASN A 360     -11.899 -45.347   7.664  1.00109.77           C  
ANISOU  492  CG  ASN A 360    12012  12439  17256   -374    850   3475       C  
ATOM    493  OD1 ASN A 360     -11.830 -46.454   8.210  1.00117.08           O  
ANISOU  493  OD1 ASN A 360    12759  13041  18684   -207   1212   4260       O  
ATOM    494  ND2 ASN A 360     -10.907 -44.849   6.921  1.00109.40           N  
ANISOU  494  ND2 ASN A 360    11851  12438  17275   -298    563   3271       N  
ATOM    495  N   ILE A 361     -12.737 -40.812   7.366  1.00 93.22           N  
ANISOU  495  N   ILE A 361    10486  11567  13364   -996   -193   1448       N  
ATOM    496  CA  ILE A 361     -12.648 -39.745   6.395  1.00 88.61           C  
ANISOU  496  CA  ILE A 361     9928  10851  12888   -986   -337    986       C  
ATOM    497  C   ILE A 361     -11.250 -39.160   6.531  1.00 88.99           C  
ANISOU  497  C   ILE A 361     9883  11161  12765  -1025   -616   1134       C  
ATOM    498  O   ILE A 361     -10.759 -38.974   7.653  1.00 92.53           O  
ANISOU  498  O   ILE A 361    10257  12125  12773  -1201   -753   1286       O  
ATOM    499  CB  ILE A 361     -13.676 -38.671   6.744  1.00 88.26           C  
ANISOU  499  CB  ILE A 361     9968  10854  12711  -1141   -276    488       C  
ATOM    500  CG1 ILE A 361     -15.099 -39.191   6.489  1.00 88.41           C  
ANISOU  500  CG1 ILE A 361     9992  10655  12944  -1097    -21    276       C  
ATOM    501  CG2 ILE A 361     -13.383 -37.379   6.026  1.00 87.13           C  
ANISOU  501  CG2 ILE A 361     9794  10560  12749  -1116   -392    230       C  
ATOM    502  CD1 ILE A 361     -15.694 -38.850   5.142  1.00 87.67           C  
ANISOU  502  CD1 ILE A 361     9780  10368  13164   -945    -54     46       C  
ATOM    503  N   LYS A 362     -10.584 -38.897   5.413  1.00 85.85           N  
ANISOU  503  N   LYS A 362     9436  10541  12640   -925   -687   1070       N  
ATOM    504  CA  LYS A 362      -9.270 -38.276   5.497  1.00 86.38           C  
ANISOU  504  CA  LYS A 362     9384  10829  12605  -1002   -900   1116       C  
ATOM    505  C   LYS A 362      -9.481 -36.757   5.537  1.00 85.58           C  
ANISOU  505  C   LYS A 362     9365  10713  12436  -1202   -885    641       C  
ATOM    506  O   LYS A 362     -10.244 -36.226   4.735  1.00 84.03           O  
ANISOU  506  O   LYS A 362     9263  10165  12500  -1119   -764    476       O  
ATOM    507  CB  LYS A 362      -8.374 -38.721   4.333  1.00 85.44           C  
ANISOU  507  CB  LYS A 362     9142  10462  12860   -860   -886   1243       C  
ATOM    508  CG  LYS A 362      -8.424 -40.231   4.015  1.00 86.87           C  
ANISOU  508  CG  LYS A 362     9188  10372  13446   -678   -661   1520       C  
ATOM    509  CD  LYS A 362      -7.314 -41.038   4.704  1.00 92.92           C  
ANISOU  509  CD  LYS A 362     9645  11249  14408   -525   -736   2100       C  
ATOM    510  CE  LYS A 362      -7.531 -42.578   4.618  1.00 96.88           C  
ANISOU  510  CE  LYS A 362     9963  11273  15574   -312   -341   2464       C  
ATOM    511  NZ  LYS A 362      -8.720 -43.119   5.407  1.00 97.80           N1+
ANISOU  511  NZ  LYS A 362    10228  11342  15586   -310   -153   2662       N1+
ATOM    512  N   LEU A 363      -8.864 -36.064   6.493  1.00 87.68           N  
ANISOU  512  N   LEU A 363     9519  11390  12405  -1487   -956    423       N  
ATOM    513  CA  LEU A 363      -9.073 -34.623   6.606  1.00 88.26           C  
ANISOU  513  CA  LEU A 363     9600  11292  12643  -1737   -751   -154       C  
ATOM    514  C   LEU A 363      -7.863 -33.823   6.160  1.00 89.40           C  
ANISOU  514  C   LEU A 363     9615  11366  12987  -1869   -754   -310       C  
ATOM    515  O   LEU A 363      -6.726 -34.034   6.630  1.00 91.85           O  
ANISOU  515  O   LEU A 363     9704  12204  12988  -2036   -956   -281       O  
ATOM    516  CB  LEU A 363      -9.492 -34.205   8.021  1.00 92.50           C  
ANISOU  516  CB  LEU A 363    10051  12314  12779  -2150   -611   -642       C  
ATOM    517  CG  LEU A 363      -9.568 -32.690   8.338  1.00 95.85           C  
ANISOU  517  CG  LEU A 363    10359  12526  13532  -2540   -220  -1459       C  
ATOM    518  CD1 LEU A 363     -10.660 -31.908   7.589  1.00 93.10           C  
ANISOU  518  CD1 LEU A 363    10102  11259  14009  -2301    137  -1588       C  
ATOM    519  CD2 LEU A 363      -9.722 -32.463   9.823  1.00101.60           C  
ANISOU  519  CD2 LEU A 363    10903  14033  13666  -3120    -64  -2084       C  
ATOM    520  N   TYR A 364      -8.125 -32.885   5.261  1.00 88.20           N  
ANISOU  520  N   TYR A 364     9542  10589  13379  -1791   -515   -412       N  
ATOM    521  CA  TYR A 364      -7.091 -32.035   4.723  1.00 89.52           C  
ANISOU  521  CA  TYR A 364     9614  10537  13862  -1928   -390   -533       C  
ATOM    522  C   TYR A 364      -7.432 -30.593   4.959  1.00 93.89           C  
ANISOU  522  C   TYR A 364    10097  10590  14984  -2162     85  -1037       C  
ATOM    523  O   TYR A 364      -8.573 -30.179   4.782  1.00 94.59           O  
ANISOU  523  O   TYR A 364    10245  10201  15494  -1982    310   -985       O  
ATOM    524  CB  TYR A 364      -7.009 -32.211   3.229  1.00 86.52           C  
ANISOU  524  CB  TYR A 364     9349   9798  13724  -1620   -426    -15       C  
ATOM    525  CG  TYR A 364      -6.346 -33.454   2.750  1.00 83.76           C  
ANISOU  525  CG  TYR A 364     8973   9763  13088  -1484   -696    302       C  
ATOM    526  CD1 TYR A 364      -6.923 -34.703   2.947  1.00 81.88           C  
ANISOU  526  CD1 TYR A 364     8768   9724  12618  -1298   -851    506       C  
ATOM    527  CD2 TYR A 364      -5.157 -33.378   2.048  1.00 84.18           C  
ANISOU  527  CD2 TYR A 364     8927   9810  13246  -1559   -684    359       C  
ATOM    528  CE1 TYR A 364      -6.302 -35.845   2.481  1.00 81.21           C  
ANISOU  528  CE1 TYR A 364     8576   9745  12533  -1181   -936    739       C  
ATOM    529  CE2 TYR A 364      -4.540 -34.497   1.577  1.00 82.52           C  
ANISOU  529  CE2 TYR A 364     8612   9782  12959  -1450   -812    557       C  
ATOM    530  CZ  TYR A 364      -5.107 -35.723   1.794  1.00 81.43           C  
ANISOU  530  CZ  TYR A 364     8468   9756  12714  -1254   -911    739       C  
ATOM    531  OH  TYR A 364      -4.470 -36.828   1.304  1.00 82.00           O  
ANISOU  531  OH  TYR A 364     8357   9841  12958  -1158   -884    871       O  
ATOM    532  N   VAL A 365      -6.417 -29.824   5.325  1.00 98.01           N  
ANISOU  532  N   VAL A 365    10416  11181  15642  -2570    298  -1548       N  
ATOM    533  CA  VAL A 365      -6.502 -28.377   5.366  1.00103.03           C  
ANISOU  533  CA  VAL A 365    10918  11121  17107  -2836    935  -2077       C  
ATOM    534  C   VAL A 365      -5.581 -27.883   4.264  1.00103.40           C  
ANISOU  534  C   VAL A 365    10974  10708  17604  -2767   1075  -1739       C  
ATOM    535  O   VAL A 365      -4.407 -28.238   4.235  1.00103.06           O  
ANISOU  535  O   VAL A 365    10831  11145  17180  -2946    846  -1817       O  
ATOM    536  CB  VAL A 365      -6.074 -27.846   6.748  1.00109.23           C  
ANISOU  536  CB  VAL A 365    11379  12430  17692  -3540   1218  -3170       C  
ATOM    537  CG1 VAL A 365      -5.814 -26.339   6.717  1.00116.21           C  
ANISOU  537  CG1 VAL A 365    12030  12500  19624  -3935   2040  -3895       C  
ATOM    538  CG2 VAL A 365      -7.137 -28.202   7.778  1.00110.06           C  
ANISOU  538  CG2 VAL A 365    11482  12955  17377  -3663   1206  -3497       C  
ATOM    539  N   ARG A 366      -6.128 -27.104   3.337  1.00105.05           N  
ANISOU  539  N   ARG A 366    11257  10037  18619  -2482   1442  -1259       N  
ATOM    540  CA  ARG A 366      -5.351 -26.518   2.239  1.00107.25           C  
ANISOU  540  CA  ARG A 366    11550   9843  19357  -2441   1678   -810       C  
ATOM    541  C   ARG A 366      -4.386 -27.516   1.598  1.00102.22           C  
ANISOU  541  C   ARG A 366    11014   9851  17972  -2392   1174   -475       C  
ATOM    542  O   ARG A 366      -3.161 -27.329   1.639  1.00103.85           O  
ANISOU  542  O   ARG A 366    11081  10198  18179  -2727   1276   -836       O  
ATOM    543  CB  ARG A 366      -4.594 -25.254   2.702  1.00115.03           C  
ANISOU  543  CB  ARG A 366    12273  10276  21157  -2964   2406  -1588       C  
ATOM    544  CG  ARG A 366      -5.468 -24.204   3.363  1.00122.27           C  
ANISOU  544  CG  ARG A 366    12987  10400  23069  -3101   3117  -2119       C  
ATOM    545  CD  ARG A 366      -5.228 -22.836   2.762  1.00132.40           C  
ANISOU  545  CD  ARG A 366    14107  10458  25741  -3155   3999  -1960       C  
ATOM    546  NE  ARG A 366      -4.600 -21.873   3.670  1.00142.81           N  
ANISOU  546  NE  ARG A 366    15061  11413  27786  -3899   4821  -3297       N  
ATOM    547  CZ  ARG A 366      -5.164 -21.379   4.777  1.00149.15           C  
ANISOU  547  CZ  ARG A 366    15574  12034  29060  -4308   5360  -4396       C  
ATOM    548  NH1 ARG A 366      -6.365 -21.790   5.169  1.00146.45           N1+
ANISOU  548  NH1 ARG A 366    15298  11831  28516  -4006   5119  -4274       N1+
ATOM    549  NH2 ARG A 366      -4.512 -20.482   5.513  1.00157.69           N  
ANISOU  549  NH2 ARG A 366    16251  12861  30801  -5110   6201  -5757       N  
ATOM    550  N   ARG A 367      -4.957 -28.582   1.037  1.00 96.84           N  
ANISOU  550  N   ARG A 367    10505   9551  16737  -2019    704    101       N  
ATOM    551  CA  ARG A 367      -4.214 -29.616   0.298  1.00 93.11           C  
ANISOU  551  CA  ARG A 367    10079   9577  15719  -1958    352    384       C  
ATOM    552  C   ARG A 367      -3.218 -30.448   1.097  1.00 91.16           C  
ANISOU  552  C   ARG A 367     9660   9916  15060  -2149     62    -59       C  
ATOM    553  O   ARG A 367      -2.439 -31.185   0.514  1.00 89.88           O  
ANISOU  553  O   ARG A 367     9434  10012  14703  -2120    -94     92       O  
ATOM    554  CB  ARG A 367      -3.492 -28.984  -0.888  1.00 96.30           C  
ANISOU  554  CB  ARG A 367    10495   9695  16399  -2040    638    753       C  
ATOM    555  CG  ARG A 367      -4.074 -29.267  -2.249  1.00 97.06           C  
ANISOU  555  CG  ARG A 367    10708   9932  16235  -1792    544   1537       C  
ATOM    556  CD  ARG A 367      -5.546 -29.482  -2.207  1.00 98.30           C  
ANISOU  556  CD  ARG A 367    10907  10145  16295  -1461    353   1860       C  
ATOM    557  NE  ARG A 367      -6.273 -28.399  -1.554  1.00103.93           N  
ANISOU  557  NE  ARG A 367    11559  10205  17721  -1359    660   1846       N  
ATOM    558  CZ  ARG A 367      -6.715 -27.308  -2.166  1.00110.74           C  
ANISOU  558  CZ  ARG A 367    12336  10513  19226  -1182   1006   2506       C  
ATOM    559  NH1 ARG A 367      -6.478 -27.115  -3.461  1.00114.60           N1+
ANISOU  559  NH1 ARG A 367    12819  11173  19549  -1119   1027   3332       N1+
ATOM    560  NH2 ARG A 367      -7.390 -26.405  -1.472  1.00114.68           N  
ANISOU  560  NH2 ARG A 367    12699  10294  20577  -1087   1386   2368       N  
ATOM    561  N   VAL A 368      -3.246 -30.341   2.420  1.00 92.36           N  
ANISOU  561  N   VAL A 368     9662  10346  15083  -2358     13   -575       N  
ATOM    562  CA  VAL A 368      -2.237 -30.973   3.274  1.00 93.09           C  
ANISOU  562  CA  VAL A 368     9450  11169  14747  -2556   -297   -859       C  
ATOM    563  C   VAL A 368      -2.910 -31.921   4.257  1.00 91.80           C  
ANISOU  563  C   VAL A 368     9274  11545  14061  -2424   -645   -738       C  
ATOM    564  O   VAL A 368      -3.781 -31.496   5.025  1.00 93.37           O  
ANISOU  564  O   VAL A 368     9534  11758  14182  -2562   -513  -1042       O  
ATOM    565  CB  VAL A 368      -1.409 -29.910   4.045  1.00 98.73           C  
ANISOU  565  CB  VAL A 368     9842  12064  15606  -3108    -27  -1640       C  
ATOM    566  CG1 VAL A 368      -0.538 -30.552   5.094  1.00100.94           C  
ANISOU  566  CG1 VAL A 368     9685  13399  15266  -3326   -453  -1861       C  
ATOM    567  CG2 VAL A 368      -0.560 -29.120   3.086  1.00101.32           C  
ANISOU  567  CG2 VAL A 368    10144  11860  16492  -3258    356  -1709       C  
ATOM    568  N   PHE A 369      -2.511 -33.195   4.234  1.00 89.88           N  
ANISOU  568  N   PHE A 369     8914  11677  13558  -2171  -1001   -288       N  
ATOM    569  CA  PHE A 369      -3.118 -34.204   5.105  1.00 89.50           C  
ANISOU  569  CA  PHE A 369     8842  12064  13101  -2003  -1268     26       C  
ATOM    570  C   PHE A 369      -2.943 -33.871   6.593  1.00 94.87           C  
ANISOU  570  C   PHE A 369     9237  13585  13222  -2393  -1411   -312       C  
ATOM    571  O   PHE A 369      -1.852 -33.492   7.015  1.00 99.06           O  
ANISOU  571  O   PHE A 369     9373  14686  13578  -2704  -1522   -600       O  
ATOM    572  CB  PHE A 369      -2.556 -35.593   4.794  1.00 88.80           C  
ANISOU  572  CB  PHE A 369     8562  12071  13105  -1655  -1487    623       C  
ATOM    573  CG  PHE A 369      -2.969 -36.647   5.782  1.00 90.41           C  
ANISOU  573  CG  PHE A 369     8647  12705  12997  -1478  -1707   1118       C  
ATOM    574  CD1 PHE A 369      -4.292 -37.086   5.843  1.00 87.89           C  
ANISOU  574  CD1 PHE A 369     8651  12099  12642  -1333  -1575   1246       C  
ATOM    575  CD2 PHE A 369      -2.042 -37.194   6.658  1.00 95.16           C  
ANISOU  575  CD2 PHE A 369     8755  14051  13348  -1456  -2037   1539       C  
ATOM    576  CE1 PHE A 369      -4.678 -38.053   6.759  1.00 89.92           C  
ANISOU  576  CE1 PHE A 369     8810  12702  12653  -1198  -1690   1767       C  
ATOM    577  CE2 PHE A 369      -2.416 -38.164   7.581  1.00 98.05           C  
ANISOU  577  CE2 PHE A 369     8978  14845  13429  -1271  -2214   2219       C  
ATOM    578  CZ  PHE A 369      -3.733 -38.596   7.631  1.00 95.67           C  
ANISOU  578  CZ  PHE A 369     9071  14149  13129  -1156  -2002   2326       C  
ATOM    579  N   ILE A 370      -4.020 -34.004   7.374  1.00 95.33           N  
ANISOU  579  N   ILE A 370     9442  13833  12944  -2446  -1385   -347       N  
ATOM    580  CA  ILE A 370      -3.964 -33.697   8.812  1.00101.78           C  
ANISOU  580  CA  ILE A 370     9968  15644  13056  -2941  -1468   -747       C  
ATOM    581  C   ILE A 370      -4.119 -34.949   9.675  1.00104.72           C  
ANISOU  581  C   ILE A 370    10194  16800  12793  -2772  -1842     14       C  
ATOM    582  O   ILE A 370      -3.292 -35.214  10.548  1.00111.03           O  
ANISOU  582  O   ILE A 370    10516  18712  12957  -2984  -2192    239       O  
ATOM    583  CB  ILE A 370      -5.018 -32.624   9.247  1.00102.89           C  
ANISOU  583  CB  ILE A 370    10285  15518  13288  -3332   -994  -1582       C  
ATOM    584  CG1 ILE A 370      -4.934 -31.344   8.398  1.00101.73           C  
ANISOU  584  CG1 ILE A 370    10233  14422  13996  -3433   -512  -2152       C  
ATOM    585  CG2 ILE A 370      -4.896 -32.310  10.736  1.00110.27           C  
ANISOU  585  CG2 ILE A 370    10848  17669  13380  -4013  -1000  -2195       C  
ATOM    586  CD1 ILE A 370      -3.633 -30.565   8.481  1.00105.02           C  
ANISOU  586  CD1 ILE A 370    10278  15136  14487  -3884   -405  -2726       C  
ATOM    587  N   MET A 371      -5.185 -35.709   9.419  1.00101.43           N  
ANISOU  587  N   MET A 371    10128  15841  12568  -2401  -1746    460       N  
ATOM    588  CA  MET A 371      -5.521 -36.926  10.173  1.00104.87           C  
ANISOU  588  CA  MET A 371    10484  16770  12589  -2210  -1941   1272       C  
ATOM    589  C   MET A 371      -6.627 -37.711   9.464  1.00100.11           C  
ANISOU  589  C   MET A 371    10280  15224  12532  -1786  -1690   1584       C  
ATOM    590  O   MET A 371      -7.319 -37.159   8.599  1.00 95.25           O  
ANISOU  590  O   MET A 371     9973  13843  12371  -1734  -1427   1091       O  
ATOM    591  CB  MET A 371      -5.962 -36.577  11.599  1.00111.02           C  
ANISOU  591  CB  MET A 371    11131  18619  12430  -2758  -1951    972       C  
ATOM    592  CG  MET A 371      -7.080 -35.554  11.679  1.00108.77           C  
ANISOU  592  CG  MET A 371    11154  17920  12252  -3119  -1489    -33       C  
ATOM    593  SD  MET A 371      -7.747 -35.358  13.336  1.00117.39           S  
ANISOU  593  SD  MET A 371    12084  20271  12247  -3831  -1362   -465       S  
ATOM    594  CE  MET A 371      -6.622 -34.176  14.086  1.00126.03           C  
ANISOU  594  CE  MET A 371    12624  22555  12706  -4666  -1393  -1472       C  
ATOM    595  N   ASP A 372      -6.799 -38.989   9.817  1.00103.41           N  
ANISOU  595  N   ASP A 372    10619  15723  12946  -1498  -1737   2431       N  
ATOM    596  CA  ASP A 372      -8.005 -39.734   9.387  1.00100.90           C  
ANISOU  596  CA  ASP A 372    10623  14650  13062  -1254  -1399   2554       C  
ATOM    597  C   ASP A 372      -8.915 -40.310  10.472  1.00105.23           C  
ANISOU  597  C   ASP A 372    11238  15587  13154  -1370  -1274   2915       C  
ATOM    598  O   ASP A 372     -10.078 -40.591  10.195  1.00102.83           O  
ANISOU  598  O   ASP A 372    11212  14725  13133  -1318   -943   2699       O  
ATOM    599  CB  ASP A 372      -7.733 -40.777   8.286  1.00 98.69           C  
ANISOU  599  CB  ASP A 372    10292  13552  13650   -811  -1229   2948       C  
ATOM    600  CG  ASP A 372      -6.360 -41.384   8.367  1.00103.56           C  
ANISOU  600  CG  ASP A 372    10458  14377  14513   -574  -1442   3643       C  
ATOM    601  OD1 ASP A 372      -5.997 -41.848   9.465  1.00111.62           O  
ANISOU  601  OD1 ASP A 372    11170  16094  15143   -539  -1660   4423       O  
ATOM    602  OD2 ASP A 372      -5.655 -41.413   7.324  1.00101.37           O1-
ANISOU  602  OD2 ASP A 372    10076  13623  14816   -427  -1380   3457       O1-
ATOM    603  N   ASN A 373      -8.420 -40.469  11.691  1.00113.09           N  
ANISOU  603  N   ASN A 373    11941  17641  13386  -1573  -1530   3457       N  
ATOM    604  CA  ASN A 373      -9.270 -40.983  12.767  1.00118.82           C  
ANISOU  604  CA  ASN A 373    12725  18878  13543  -1762  -1380   3866       C  
ATOM    605  C   ASN A 373     -10.033 -39.876  13.510  1.00120.26           C  
ANISOU  605  C   ASN A 373    13057  19671  12965  -2401  -1247   2863       C  
ATOM    606  O   ASN A 373      -9.855 -39.689  14.719  1.00128.35           O  
ANISOU  606  O   ASN A 373    13843  21968  12957  -2880  -1390   2963       O  
ATOM    607  CB  ASN A 373      -8.465 -41.875  13.738  1.00128.77           C  
ANISOU  607  CB  ASN A 373    13525  21097  14304  -1649  -1686   5209       C  
ATOM    608  CG  ASN A 373      -7.170 -41.214  14.244  1.00133.91           C  
ANISOU  608  CG  ASN A 373    13680  22984  14215  -1911  -2230   5222       C  
ATOM    609  OD1 ASN A 373      -6.671 -40.247  13.662  1.00128.94           O  
ANISOU  609  OD1 ASN A 373    13056  22196  13737  -2070  -2318   4295       O  
ATOM    610  ND2 ASN A 373      -6.624 -41.752  15.332  1.00144.27           N  
ANISOU  610  ND2 ASN A 373    14501  25596  14718  -1973  -2580   6336       N  
ATOM    611  N   CYS A 374     -10.893 -39.156  12.789  1.00113.98           N  
ANISOU  611  N   CYS A 374    12579  18029  12699  -2432   -937   1905       N  
ATOM    612  CA  CYS A 374     -11.500 -37.941  13.339  1.00115.87           C  
ANISOU  612  CA  CYS A 374    12860  18596  12567  -3001   -702    809       C  
ATOM    613  C   CYS A 374     -12.871 -38.099  13.999  1.00117.41           C  
ANISOU  613  C   CYS A 374    13231  18836  12542  -3261   -295    524       C  
ATOM    614  O   CYS A 374     -13.910 -38.133  13.316  1.00112.43           O  
ANISOU  614  O   CYS A 374    12831  17270  12617  -3015     -1    222       O  
ATOM    615  CB  CYS A 374     -11.553 -36.818  12.298  1.00110.49           C  
ANISOU  615  CB  CYS A 374    12280  17036  12664  -2913   -562    -28       C  
ATOM    616  SG  CYS A 374     -11.886 -35.195  13.097  1.00117.75           S  
ANISOU  616  SG  CYS A 374    13043  18325  13368  -3669   -158  -1409       S  
ATOM    617  N   GLU A 375     -12.859 -38.155  15.333  1.00125.38           N  
ANISOU  617  N   GLU A 375    14065  21073  12499  -3815   -281    585       N  
ATOM    618  CA  GLU A 375     -14.088 -38.249  16.135  1.00128.49           C  
ANISOU  618  CA  GLU A 375    14580  21722  12516  -4216    163    233       C  
ATOM    619  C   GLU A 375     -15.077 -37.172  15.682  1.00123.77           C  
ANISOU  619  C   GLU A 375    14099  20256  12668  -4343    625  -1060       C  
ATOM    620  O   GLU A 375     -14.775 -35.967  15.729  1.00125.61           O  
ANISOU  620  O   GLU A 375    14159  20562  13004  -4698    749  -2020       O  
ATOM    621  CB  GLU A 375     -13.812 -38.073  17.648  1.00139.84           C  
ANISOU  621  CB  GLU A 375    15720  24893  12516  -5028    144    151       C  
ATOM    622  CG  GLU A 375     -12.676 -38.906  18.258  1.00147.28           C  
ANISOU  622  CG  GLU A 375    16343  27072  12542  -4973   -408   1514       C  
ATOM    623  CD  GLU A 375     -12.497 -38.653  19.761  1.00160.70           C  
ANISOU  623  CD  GLU A 375    17664  30801  12593  -5898   -448   1379       C  
ATOM    624  OE1 GLU A 375     -13.396 -39.011  20.551  1.00166.17           O  
ANISOU  624  OE1 GLU A 375    18459  32006  12672  -6285    -92   1469       O  
ATOM    625  OE2 GLU A 375     -11.449 -38.105  20.161  1.00166.53           O1-
ANISOU  625  OE2 GLU A 375    17953  32747  12573  -6307   -819   1148       O1-
ATOM    626  N   GLU A 376     -16.243 -37.602  15.224  1.00118.35           N  
ANISOU  626  N   GLU A 376    13632  18714  12622  -4042    923  -1069       N  
ATOM    627  CA  GLU A 376     -17.331 -36.670  14.977  1.00115.69           C  
ANISOU  627  CA  GLU A 376    13283  17694  12979  -4153   1382  -2148       C  
ATOM    628  C   GLU A 376     -17.126 -35.736  13.768  1.00108.88           C  
ANISOU  628  C   GLU A 376    12368  15869  13132  -3745   1301  -2511       C  
ATOM    629  O   GLU A 376     -17.392 -34.541  13.845  1.00110.96           O  
ANISOU  629  O   GLU A 376    12450  15852  13858  -3993   1649  -3419       O  
ATOM    630  CB  GLU A 376     -17.659 -35.874  16.262  1.00124.48           C  
ANISOU  630  CB  GLU A 376    14193  19654  13447  -5014   1834  -3158       C  
ATOM    631  CG  GLU A 376     -18.003 -36.746  17.488  1.00132.48           C  
ANISOU  631  CG  GLU A 376    15240  21771  13323  -5505   1975  -2768       C  
ATOM    632  CD  GLU A 376     -19.147 -36.181  18.349  1.00140.11           C  
ANISOU  632  CD  GLU A 376    16093  22992  14150  -6198   2686  -3930       C  
ATOM    633  OE1 GLU A 376     -18.963 -35.098  18.958  1.00145.95           O  
ANISOU  633  OE1 GLU A 376    16546  24259  14649  -6887   3014  -5080       O  
ATOM    634  OE2 GLU A 376     -20.223 -36.836  18.430  1.00139.72           O1-
ANISOU  634  OE2 GLU A 376    16192  22612  14281  -6112   2996  -3781       O1-
ATOM    635  N   LEU A 377     -16.641 -36.282  12.661  1.00101.49           N  
ANISOU  635  N   LEU A 377    11547  14427  12588  -3153    918  -1783       N  
ATOM    636  CA  LEU A 377     -16.851 -35.651  11.358  1.00 95.31           C  
ANISOU  636  CA  LEU A 377    10733  12730  12750  -2701    883  -1921       C  
ATOM    637  C   LEU A 377     -18.183 -36.126  10.774  1.00 91.92           C  
ANISOU  637  C   LEU A 377    10318  11773  12835  -2392   1047  -1905       C  
ATOM    638  O   LEU A 377     -18.801 -35.427   9.974  1.00 90.57           O  
ANISOU  638  O   LEU A 377     9990  11025  13398  -2122   1123  -2143       O  
ATOM    639  CB  LEU A 377     -15.733 -35.994  10.376  1.00 91.07           C  
ANISOU  639  CB  LEU A 377    10257  12036  12309  -2317    448  -1271       C  
ATOM    640  CG  LEU A 377     -14.592 -35.014  10.136  1.00 91.87           C  
ANISOU  640  CG  LEU A 377    10254  12140  12511  -2403    317  -1449       C  
ATOM    641  CD1 LEU A 377     -13.849 -35.418   8.882  1.00 87.21           C  
ANISOU  641  CD1 LEU A 377     9725  11211  12199  -1959    -14   -851       C  
ATOM    642  CD2 LEU A 377     -15.087 -33.582  10.012  1.00 94.40           C  
ANISOU  642  CD2 LEU A 377    10417  11926  13523  -2518    701  -2183       C  
ATOM    643  N   ILE A 378     -18.581 -37.342  11.147  1.00 90.75           N  
ANISOU  643  N   ILE A 378    10293  11856  12331  -2422   1104  -1541       N  
ATOM    644  CA  ILE A 378     -19.896 -37.897  10.858  1.00 89.13           C  
ANISOU  644  CA  ILE A 378    10050  11311  12503  -2296   1360  -1682       C  
ATOM    645  C   ILE A 378     -20.281 -38.681  12.086  1.00 92.72           C  
ANISOU  645  C   ILE A 378    10620  12242  12368  -2691   1671  -1597       C  
ATOM    646  O   ILE A 378     -19.395 -39.069  12.861  1.00 95.85           O  
ANISOU  646  O   ILE A 378    11115  13236  12067  -2902   1547  -1102       O  
ATOM    647  CB  ILE A 378     -19.929 -38.905   9.670  1.00 85.20           C  
ANISOU  647  CB  ILE A 378     9561  10465  12344  -1893   1193  -1219       C  
ATOM    648  CG1 ILE A 378     -18.700 -39.806   9.671  1.00 85.35           C  
ANISOU  648  CG1 ILE A 378     9722  10638  12066  -1814    989   -498       C  
ATOM    649  CG2 ILE A 378     -20.140 -38.208   8.325  1.00 82.15           C  
ANISOU  649  CG2 ILE A 378     8967   9728  12517  -1543    974  -1362       C  
ATOM    650  CD1 ILE A 378     -17.476 -39.165   8.986  1.00 85.90           C  
ANISOU  650  CD1 ILE A 378     9769  10689  12177  -1630    593   -327       C  
ATOM    651  N   PRO A 379     -21.594 -38.927  12.274  1.00 93.10           N  
ANISOU  651  N   PRO A 379    10600  12105  12666  -2797   2072  -2002       N  
ATOM    652  CA  PRO A 379     -22.055 -39.764  13.375  1.00 97.24           C  
ANISOU  652  CA  PRO A 379    11246  13042  12658  -3188   2453  -1845       C  
ATOM    653  C   PRO A 379     -21.790 -41.227  13.076  1.00 95.95           C  
ANISOU  653  C   PRO A 379    11217  12688  12549  -2954   2452   -972       C  
ATOM    654  O   PRO A 379     -21.556 -41.594  11.926  1.00 91.56           O  
ANISOU  654  O   PRO A 379    10611  11629  12548  -2548   2258   -794       O  
ATOM    655  CB  PRO A 379     -23.563 -39.496  13.425  1.00 98.70           C  
ANISOU  655  CB  PRO A 379    11248  12925  13327  -3320   2913  -2655       C  
ATOM    656  CG  PRO A 379     -23.799 -38.340  12.516  1.00 96.11           C  
ANISOU  656  CG  PRO A 379    10643  12121  13752  -2996   2736  -3177       C  
ATOM    657  CD  PRO A 379     -22.718 -38.374  11.508  1.00 91.23           C  
ANISOU  657  CD  PRO A 379    10100  11343  13219  -2574   2201  -2585       C  
ATOM    658  N   GLU A 380     -21.832 -42.059  14.104  1.00100.92           N  
ANISOU  658  N   GLU A 380    11968  13723  12652  -3246   2744   -428       N  
ATOM    659  CA  GLU A 380     -21.511 -43.463  13.944  1.00101.92           C  
ANISOU  659  CA  GLU A 380    12163  13534  13027  -3016   2885    526       C  
ATOM    660  C   GLU A 380     -22.365 -44.138  12.863  1.00 97.92           C  
ANISOU  660  C   GLU A 380    11559  12160  13483  -2783   3206    145       C  
ATOM    661  O   GLU A 380     -21.852 -44.953  12.106  1.00 96.70           O  
ANISOU  661  O   GLU A 380    11355  11516  13871  -2482   3215    572       O  
ATOM    662  CB  GLU A 380     -21.594 -44.183  15.293  1.00110.76           C  
ANISOU  662  CB  GLU A 380    13379  15243  13462  -3383   3236   1287       C  
ATOM    663  CG  GLU A 380     -20.873 -45.530  15.378  1.00117.07           C  
ANISOU  663  CG  GLU A 380    14173  15806  14500  -3094   3345   2669       C  
ATOM    664  CD  GLU A 380     -21.833 -46.743  15.429  1.00124.22           C  
ANISOU  664  CD  GLU A 380    15112  16009  16077  -3139   4128   2919       C  
ATOM    665  OE1 GLU A 380     -21.548 -47.749  14.727  1.00125.65           O  
ANISOU  665  OE1 GLU A 380    15198  15322  17219  -2773   4385   3413       O  
ATOM    666  OE2 GLU A 380     -22.858 -46.705  16.168  1.00127.83           O1-
ANISOU  666  OE2 GLU A 380    15649  16737  16182  -3586   4579   2551       O1-
ATOM    667  N   TYR A 381     -23.643 -43.784  12.747  1.00 96.34           N  
ANISOU  667  N   TYR A 381    11246  11821  13536  -2956   3493   -746       N  
ATOM    668  CA  TYR A 381     -24.498 -44.531  11.825  1.00 94.32           C  
ANISOU  668  CA  TYR A 381    10798  10970  14069  -2852   3831  -1149       C  
ATOM    669  C   TYR A 381     -24.170 -44.320  10.365  1.00 88.52           C  
ANISOU  669  C   TYR A 381     9855   9989  13789  -2497   3429  -1415       C  
ATOM    670  O   TYR A 381     -24.560 -45.114   9.517  1.00 87.85           O  
ANISOU  670  O   TYR A 381     9562   9558  14259  -2470   3689  -1681       O  
ATOM    671  CB  TYR A 381     -25.989 -44.314  12.095  1.00 96.70           C  
ANISOU  671  CB  TYR A 381    10924  11275  14542  -3141   4255  -2004       C  
ATOM    672  CG  TYR A 381     -26.566 -43.006  11.615  1.00 93.76           C  
ANISOU  672  CG  TYR A 381    10269  11025  14329  -3027   3930  -2815       C  
ATOM    673  CD1 TYR A 381     -27.012 -42.854  10.300  1.00 89.86           C  
ANISOU  673  CD1 TYR A 381     9397  10358  14385  -2737   3689  -3234       C  
ATOM    674  CD2 TYR A 381     -26.708 -41.928  12.493  1.00 95.62           C  
ANISOU  674  CD2 TYR A 381    10526  11590  14215  -3245   3936  -3158       C  
ATOM    675  CE1 TYR A 381     -27.554 -41.659   9.871  1.00 88.17           C  
ANISOU  675  CE1 TYR A 381     8834  10240  14425  -2547   3399  -3723       C  
ATOM    676  CE2 TYR A 381     -27.249 -40.737  12.068  1.00 93.36           C  
ANISOU  676  CE2 TYR A 381     9898  11216  14357  -3085   3769  -3818       C  
ATOM    677  CZ  TYR A 381     -27.662 -40.612  10.761  1.00 90.09           C  
ANISOU  677  CZ  TYR A 381     9111  10570  14549  -2679   3475  -3975       C  
ATOM    678  OH  TYR A 381     -28.192 -39.431  10.347  1.00 91.72           O  
ANISOU  678  OH  TYR A 381     8897  10677  15273  -2436   3309  -4381       O  
ATOM    679  N   LEU A 382     -23.453 -43.243  10.076  1.00 84.92           N  
ANISOU  679  N   LEU A 382     9417   9774  13072  -2299   2854  -1394       N  
ATOM    680  CA  LEU A 382     -22.995 -42.999   8.719  1.00 80.93           C  
ANISOU  680  CA  LEU A 382     8737   9158  12852  -1994   2455  -1483       C  
ATOM    681  C   LEU A 382     -21.543 -43.366   8.575  1.00 80.15           C  
ANISOU  681  C   LEU A 382     8806   8999  12648  -1828   2227   -789       C  
ATOM    682  O   LEU A 382     -20.906 -43.003   7.591  1.00 77.14           O  
ANISOU  682  O   LEU A 382     8335   8617  12356  -1622   1867   -797       O  
ATOM    683  CB  LEU A 382     -23.208 -41.540   8.303  1.00 78.41           C  
ANISOU  683  CB  LEU A 382     8251   9023  12516  -1837   2040  -1856       C  
ATOM    684  CG  LEU A 382     -24.633 -41.083   7.968  1.00 79.50           C  
ANISOU  684  CG  LEU A 382     8003   9187  13015  -1833   2152  -2508       C  
ATOM    685  CD1 LEU A 382     -24.642 -39.688   7.421  1.00 77.86           C  
ANISOU  685  CD1 LEU A 382     7555   9022  13002  -1551   1757  -2577       C  
ATOM    686  CD2 LEU A 382     -25.319 -42.005   6.993  1.00 79.74           C  
ANISOU  686  CD2 LEU A 382     7710   9242  13344  -1854   2295  -2805       C  
ATOM    687  N   ASN A 383     -21.009 -44.100   9.541  1.00 84.38           N  
ANISOU  687  N   ASN A 383     9526   9529  13003  -1912   2445   -111       N  
ATOM    688  CA  ASN A 383     -19.569 -44.308   9.558  1.00 85.48           C  
ANISOU  688  CA  ASN A 383     9729   9707  13042  -1713   2163    637       C  
ATOM    689  C   ASN A 383     -19.020 -45.168   8.410  1.00 84.96           C  
ANISOU  689  C   ASN A 383     9492   9117  13669  -1501   2293    721       C  
ATOM    690  O   ASN A 383     -17.807 -45.236   8.206  1.00 85.04           O  
ANISOU  690  O   ASN A 383     9476   9106  13728  -1302   2045   1211       O  
ATOM    691  CB  ASN A 383     -19.055 -44.695  10.952  1.00 91.01           C  
ANISOU  691  CB  ASN A 383    10554  10786  13239  -1828   2231   1517       C  
ATOM    692  CG  ASN A 383     -18.908 -46.179  11.138  1.00 98.59           C  
ANISOU  692  CG  ASN A 383    11448  11252  14758  -1719   2737   2324       C  
ATOM    693  OD1 ASN A 383     -19.881 -46.900  11.429  1.00102.96           O  
ANISOU  693  OD1 ASN A 383    12014  11485  15621  -1894   3332   2251       O  
ATOM    694  ND2 ASN A 383     -17.666 -46.658  11.003  1.00102.54           N  
ANISOU  694  ND2 ASN A 383    11823  11622  15513  -1421   2575   3142       N  
ATOM    695  N   PHE A 384     -19.921 -45.770   7.635  1.00 86.05           N  
ANISOU  695  N   PHE A 384     9445   8907  14342  -1609   2711    103       N  
ATOM    696  CA  PHE A 384     -19.552 -46.531   6.430  1.00 86.86           C  
ANISOU  696  CA  PHE A 384     9292   8619  15089  -1577   2956   -167       C  
ATOM    697  C   PHE A 384     -19.085 -45.633   5.295  1.00 83.28           C  
ANISOU  697  C   PHE A 384     8740   8537  14365  -1487   2408   -539       C  
ATOM    698  O   PHE A 384     -18.452 -46.108   4.347  1.00 84.39           O  
ANISOU  698  O   PHE A 384     8687   8513  14863  -1495   2529   -699       O  
ATOM    699  CB  PHE A 384     -20.698 -47.422   5.933  1.00 89.39           C  
ANISOU  699  CB  PHE A 384     9345   8635  15983  -1868   3626   -917       C  
ATOM    700  CG  PHE A 384     -21.976 -46.671   5.606  1.00 86.90           C  
ANISOU  700  CG  PHE A 384     8886   8827  15303  -2032   3422  -1715       C  
ATOM    701  CD1 PHE A 384     -22.259 -46.285   4.309  1.00 83.99           C  
ANISOU  701  CD1 PHE A 384     8176   8908  14827  -2104   3154  -2394       C  
ATOM    702  CD2 PHE A 384     -22.905 -46.371   6.604  1.00 87.27           C  
ANISOU  702  CD2 PHE A 384     9063   8977  15119  -2129   3522  -1739       C  
ATOM    703  CE1 PHE A 384     -23.441 -45.605   4.012  1.00 83.71           C  
ANISOU  703  CE1 PHE A 384     7876   9400  14527  -2178   2926  -2948       C  
ATOM    704  CE2 PHE A 384     -24.085 -45.691   6.314  1.00 86.01           C  
ANISOU  704  CE2 PHE A 384     8662   9218  14799  -2226   3371  -2441       C  
ATOM    705  CZ  PHE A 384     -24.356 -45.312   5.015  1.00 84.30           C  
ANISOU  705  CZ  PHE A 384     8049   9429  14550  -2207   3046  -2982       C  
ATOM    706  N   ILE A 385     -19.400 -44.345   5.377  1.00 80.91           N  
ANISOU  706  N   ILE A 385     8530   8699  13511  -1429   1895   -677       N  
ATOM    707  CA  ILE A 385     -19.009 -43.429   4.326  1.00 79.22           C  
ANISOU  707  CA  ILE A 385     8211   8812  13077  -1322   1418   -850       C  
ATOM    708  C   ILE A 385     -17.505 -43.325   4.366  1.00 79.34           C  
ANISOU  708  C   ILE A 385     8369   8736  13040  -1169   1191   -318       C  
ATOM    709  O   ILE A 385     -16.910 -43.427   5.442  1.00 81.74           O  
ANISOU  709  O   ILE A 385     8856   8962  13239  -1104   1171    219       O  
ATOM    710  CB  ILE A 385     -19.671 -42.041   4.494  1.00 77.57           C  
ANISOU  710  CB  ILE A 385     8005   8916  12549  -1237   1044   -987       C  
ATOM    711  CG1 ILE A 385     -21.197 -42.149   4.319  1.00 79.27           C  
ANISOU  711  CG1 ILE A 385     7938   9277  12902  -1353   1243  -1533       C  
ATOM    712  CG2 ILE A 385     -19.082 -41.013   3.520  1.00 75.30           C  
ANISOU  712  CG2 ILE A 385     7633   8873  12103  -1070    584   -874       C  
ATOM    713  CD1 ILE A 385     -21.669 -42.576   2.935  1.00 78.81           C  
ANISOU  713  CD1 ILE A 385     7450   9581  12913  -1465   1254  -1980       C  
ATOM    714  N   ARG A 386     -16.886 -43.171   3.202  1.00 79.08           N  
ANISOU  714  N   ARG A 386     8191   8823  13031  -1152   1032   -458       N  
ATOM    715  CA  ARG A 386     -15.430 -43.036   3.104  1.00 79.13           C  
ANISOU  715  CA  ARG A 386     8267   8751  13047  -1026    837    -48       C  
ATOM    716  C   ARG A 386     -15.163 -41.910   2.117  1.00 77.02           C  
ANISOU  716  C   ARG A 386     7960   8852  12450  -1006    437   -178       C  
ATOM    717  O   ARG A 386     -15.944 -41.712   1.186  1.00 78.29           O  
ANISOU  717  O   ARG A 386     7921   9345  12480  -1107    407   -540       O  
ATOM    718  CB  ARG A 386     -14.782 -44.359   2.632  1.00 82.04           C  
ANISOU  718  CB  ARG A 386     8424   8711  14034  -1081   1309    -76       C  
ATOM    719  CG  ARG A 386     -14.992 -45.548   3.588  1.00 88.39           C  
ANISOU  719  CG  ARG A 386     9210   8990  15383  -1043   1820    270       C  
ATOM    720  CD  ARG A 386     -14.324 -46.838   3.127  1.00 97.83           C  
ANISOU  720  CD  ARG A 386    10101   9556  17511  -1052   2436    273       C  
ATOM    721  NE  ARG A 386     -15.079 -48.025   3.572  1.00109.23           N  
ANISOU  721  NE  ARG A 386    11425  10412  19665  -1144   3169    262       N  
ATOM    722  CZ  ARG A 386     -14.864 -49.289   3.160  1.00117.31           C  
ANISOU  722  CZ  ARG A 386    12098  10673  21799  -1236   3995     61       C  
ATOM    723  NH1 ARG A 386     -13.898 -49.575   2.276  1.00117.72           N1+
ANISOU  723  NH1 ARG A 386    11861  10498  22365  -1265   4195   -214       N1+
ATOM    724  NH2 ARG A 386     -15.624 -50.286   3.636  1.00122.76           N  
ANISOU  724  NH2 ARG A 386    12690  10752  23200  -1337   4734     81       N  
ATOM    725  N   GLY A 387     -14.080 -41.168   2.311  1.00 75.57           N  
ANISOU  725  N   GLY A 387     7908   8684  12119   -896    143    163       N  
ATOM    726  CA  GLY A 387     -13.721 -40.098   1.394  1.00 74.06           C  
ANISOU  726  CA  GLY A 387     7688   8736  11713   -880   -142    163       C  
ATOM    727  C   GLY A 387     -12.852 -39.094   2.092  1.00 73.57           C  
ANISOU  727  C   GLY A 387     7796   8606  11550   -803   -380    443       C  
ATOM    728  O   GLY A 387     -12.390 -39.337   3.197  1.00 74.39           O  
ANISOU  728  O   GLY A 387     7983   8652  11630   -803   -381    613       O  
ATOM    729  N   VAL A 388     -12.615 -37.957   1.454  1.00 74.08           N  
ANISOU  729  N   VAL A 388     7855   8743  11546   -776   -552    511       N  
ATOM    730  CA  VAL A 388     -11.721 -36.947   2.026  1.00 74.58           C  
ANISOU  730  CA  VAL A 388     8019   8694  11623   -793   -661    618       C  
ATOM    731  C   VAL A 388     -12.452 -35.605   2.209  1.00 76.67           C  
ANISOU  731  C   VAL A 388     8283   8793  12055   -744   -641    567       C  
ATOM    732  O   VAL A 388     -13.405 -35.299   1.467  1.00 77.79           O  
ANISOU  732  O   VAL A 388     8296   8957  12303   -607   -650    673       O  
ATOM    733  CB  VAL A 388     -10.381 -36.787   1.206  1.00 74.16           C  
ANISOU  733  CB  VAL A 388     7922   8668  11587   -846   -715    749       C  
ATOM    734  CG1 VAL A 388     -10.151 -37.940   0.260  1.00 73.40           C  
ANISOU  734  CG1 VAL A 388     7693   8695  11498   -895   -600    691       C  
ATOM    735  CG2 VAL A 388     -10.366 -35.511   0.420  1.00 75.97           C  
ANISOU  735  CG2 VAL A 388     8142   8832  11888   -831   -738    901       C  
ATOM    736  N   VAL A 389     -12.027 -34.827   3.208  1.00 78.74           N  
ANISOU  736  N   VAL A 389     8596   8929  12391   -879   -570    382       N  
ATOM    737  CA  VAL A 389     -12.502 -33.447   3.364  1.00 82.81           C  
ANISOU  737  CA  VAL A 389     9035   9085  13342   -876   -372    236       C  
ATOM    738  C   VAL A 389     -11.318 -32.488   3.362  1.00 85.88           C  
ANISOU  738  C   VAL A 389     9407   9281  13941  -1042   -267    162       C  
ATOM    739  O   VAL A 389     -10.434 -32.566   4.215  1.00 86.66           O  
ANISOU  739  O   VAL A 389     9512   9629  13784  -1322   -280   -142       O  
ATOM    740  CB  VAL A 389     -13.405 -33.234   4.619  1.00 84.51           C  
ANISOU  740  CB  VAL A 389     9223   9258  13628  -1025   -149   -230       C  
ATOM    741  CG1 VAL A 389     -13.733 -31.772   4.807  1.00 88.20           C  
ANISOU  741  CG1 VAL A 389     9523   9196  14793  -1066    217   -508       C  
ATOM    742  CG2 VAL A 389     -14.689 -34.026   4.490  1.00 83.16           C  
ANISOU  742  CG2 VAL A 389     9021   9184  13390   -858   -178   -177       C  
ATOM    743  N   ASP A 390     -11.309 -31.603   2.371  1.00 89.27           N  
ANISOU  743  N   ASP A 390     9758   9340  14817   -883   -157    503       N  
ATOM    744  CA  ASP A 390     -10.269 -30.611   2.216  1.00 93.20           C  
ANISOU  744  CA  ASP A 390    10221   9513  15677  -1045     64    464       C  
ATOM    745  C   ASP A 390     -10.871 -29.259   2.530  1.00100.07           C  
ANISOU  745  C   ASP A 390    10916   9683  17420  -1035    544    302       C  
ATOM    746  O   ASP A 390     -11.702 -28.714   1.782  1.00103.06           O  
ANISOU  746  O   ASP A 390    11149   9677  18330   -687    648    860       O  
ATOM    747  CB  ASP A 390      -9.704 -30.641   0.800  1.00 92.75           C  
ANISOU  747  CB  ASP A 390    10182   9519  15537   -908    -58   1075       C  
ATOM    748  CG  ASP A 390      -8.409 -29.867   0.668  1.00 95.20           C  
ANISOU  748  CG  ASP A 390    10481   9568  16120  -1146    175    985       C  
ATOM    749  OD1 ASP A 390      -8.387 -28.821  -0.008  1.00100.95           O  
ANISOU  749  OD1 ASP A 390    11134   9804  17419  -1067    476   1393       O  
ATOM    750  OD2 ASP A 390      -7.401 -30.291   1.242  1.00 93.84           O1-
ANISOU  750  OD2 ASP A 390    10321   9688  15644  -1410     83    561       O1-
ATOM    751  N   SER A 391     -10.454 -28.734   3.669  1.00104.53           N  
ANISOU  751  N   SER A 391    11411  10142  18163  -1445    871   -480       N  
ATOM    752  CA  SER A 391     -10.859 -27.423   4.134  1.00112.96           C  
ANISOU  752  CA  SER A 391    12239  10443  20235  -1586   1533   -933       C  
ATOM    753  C   SER A 391      -9.966 -26.366   3.479  1.00118.55           C  
ANISOU  753  C   SER A 391    12851  10509  21684  -1650   1935   -746       C  
ATOM    754  O   SER A 391      -8.774 -26.590   3.284  1.00117.25           O  
ANISOU  754  O   SER A 391    12783  10689  21077  -1870   1763   -791       O  
ATOM    755  CB  SER A 391     -10.732 -27.389   5.659  1.00115.11           C  
ANISOU  755  CB  SER A 391    12417  11098  20222  -2177   1772  -2048       C  
ATOM    756  OG  SER A 391     -11.259 -26.200   6.201  1.00123.51           O  
ANISOU  756  OG  SER A 391    13185  11412  22331  -2408   2547  -2733       O  
ATOM    757  N   GLU A 392     -10.532 -25.220   3.127  1.00126.80           N  
ANISOU  757  N   GLU A 392    13656  10565  23956  -1438   2518   -477       N  
ATOM    758  CA  GLU A 392      -9.735 -24.133   2.540  1.00134.29           C  
ANISOU  758  CA  GLU A 392    14484  10730  25809  -1509   3063   -233       C  
ATOM    759  C   GLU A 392      -9.175 -23.173   3.589  1.00141.65           C  
ANISOU  759  C   GLU A 392    15168  11133  27520  -2163   3889  -1503       C  
ATOM    760  O   GLU A 392      -8.261 -22.401   3.297  1.00146.45           O  
ANISOU  760  O   GLU A 392    15682  11212  28750  -2410   4382  -1602       O  
ATOM    761  CB  GLU A 392     -10.534 -23.372   1.469  1.00140.33           C  
ANISOU  761  CB  GLU A 392    15038  10658  27620   -889   3318    995       C  
ATOM    762  CG  GLU A 392     -11.004 -24.258   0.304  1.00137.09           C  
ANISOU  762  CG  GLU A 392    14767  11023  26295   -375   2512   2198       C  
ATOM    763  CD  GLU A 392      -9.848 -24.985  -0.375  1.00133.30           C  
ANISOU  763  CD  GLU A 392    14598  11313  24737   -571   2050   2396       C  
ATOM    764  OE1 GLU A 392      -9.087 -24.303  -1.108  1.00138.81           O  
ANISOU  764  OE1 GLU A 392    15278  11627  25836   -609   2357   2918       O  
ATOM    765  OE2 GLU A 392      -9.699 -26.220  -0.170  1.00124.27           O1-
ANISOU  765  OE2 GLU A 392    13675  11073  22466   -693   1469   2035       O1-
ATOM    766  N   ASP A 393      -9.733 -23.223   4.801  1.00143.96           N  
ANISOU  766  N   ASP A 393    15315  11630  27753  -2519   4101  -2550       N  
ATOM    767  CA  ASP A 393      -9.273 -22.377   5.914  1.00152.54           C  
ANISOU  767  CA  ASP A 393    16074  12478  29404  -3320   4929  -4036       C  
ATOM    768  C   ASP A 393      -9.277 -23.061   7.296  1.00151.25           C  
ANISOU  768  C   ASP A 393    15883  13544  28040  -3950   4675  -5191       C  
ATOM    769  O   ASP A 393     -10.278 -23.656   7.720  1.00148.35           O  
ANISOU  769  O   ASP A 393    15590  13538  27238  -3783   4411  -5159       O  
ATOM    770  CB  ASP A 393      -9.992 -20.996   5.946  1.00163.43           C  
ANISOU  770  CB  ASP A 393    17020  12308  32766  -3282   6092  -4319       C  
ATOM    771  CG  ASP A 393     -11.515 -21.107   6.152  1.00164.91           C  
ANISOU  771  CG  ASP A 393    17074  12186  33397  -2849   6136  -4116       C  
ATOM    772  OD1 ASP A 393     -12.004 -20.744   7.246  1.00171.25           O  
ANISOU  772  OD1 ASP A 393    17573  12866  34628  -3371   6785  -5408       O  
ATOM    773  OD2 ASP A 393     -12.233 -21.546   5.226  1.00161.23           O1-
ANISOU  773  OD2 ASP A 393    16743  11679  32837  -2050   5559  -2746       O1-
ATOM    774  N   LEU A 394      -8.119 -22.993   7.955  1.00154.17           N  
ANISOU  774  N   LEU A 394    16105  14662  27810  -4684   4730  -6122       N  
ATOM    775  CA  LEU A 394      -7.953 -23.342   9.367  1.00157.20           C  
ANISOU  775  CA  LEU A 394    16279  16333  27115  -5479   4663  -7330       C  
ATOM    776  C   LEU A 394      -6.644 -22.697   9.855  1.00164.60           C  
ANISOU  776  C   LEU A 394    16826  17709  28003  -6345   5072  -8467       C  
ATOM    777  O   LEU A 394      -5.554 -23.084   9.406  1.00161.10           O  
ANISOU  777  O   LEU A 394    16461  17762  26987  -6275   4542  -8007       O  
ATOM    778  CB  LEU A 394      -7.957 -24.858   9.575  1.00148.58           C  
ANISOU  778  CB  LEU A 394    15503  16577  24372  -5206   3554  -6592       C  
ATOM    779  CG  LEU A 394      -8.884 -25.321  10.704  1.00150.51           C  
ANISOU  779  CG  LEU A 394    15695  17591  23901  -5515   3532  -7128       C  
ATOM    780  CD1 LEU A 394      -9.425 -26.745  10.465  1.00140.62           C  
ANISOU  780  CD1 LEU A 394    14848  16877  21702  -4875   2647  -5957       C  
ATOM    781  CD2 LEU A 394      -8.208 -25.179  12.081  1.00158.80           C  
ANISOU  781  CD2 LEU A 394    16322  20035  23979  -6584   3695  -8440       C  
ATOM    782  N   PRO A 395      -6.755 -21.694  10.758  1.00175.79           N  
ANISOU  782  N   PRO A 395    17750  18938  30102  -7217   6096 -10065       N  
ATOM    783  CA  PRO A 395      -5.661 -20.757  11.134  1.00185.57           C  
ANISOU  783  CA  PRO A 395    18483  20242  31783  -8150   6849 -11432       C  
ATOM    784  C   PRO A 395      -4.343 -21.387  11.625  1.00185.15           C  
ANISOU  784  C   PRO A 395    18238  22018  30093  -8697   6085 -11749       C  
ATOM    785  O   PRO A 395      -4.280 -22.552  12.021  1.00179.51           O  
ANISOU  785  O   PRO A 395    17675  22758  27770  -8534   5043 -11141       O  
ATOM    786  CB  PRO A 395      -6.290 -19.896  12.244  1.00197.32           C  
ANISOU  786  CB  PRO A 395    19443  21593  33933  -9077   7995 -13244       C  
ATOM    787  CG  PRO A 395      -7.763 -19.985  12.003  1.00194.31           C  
ANISOU  787  CG  PRO A 395    19317  20197  34314  -8350   8127 -12543       C  
ATOM    788  CD  PRO A 395      -8.008 -21.383  11.477  1.00180.55           C  
ANISOU  788  CD  PRO A 395    18186  19212  31203  -7425   6716 -10810       C  
ATOM    789  N   GLN A 405     -10.514 -30.618  18.048  1.00154.04           N  
ANISOU  789  N   GLN A 405    15889  19577  23062  -7582  -1925  -1757       N  
ATOM    790  CA  GLN A 405     -11.548 -30.261  19.070  1.00155.39           C  
ANISOU  790  CA  GLN A 405    16569  19827  22642  -8018  -1742  -2268       C  
ATOM    791  C   GLN A 405     -11.925 -28.778  18.968  1.00156.47           C  
ANISOU  791  C   GLN A 405    16973  19628  22849  -8140  -1210  -2822       C  
ATOM    792  O   GLN A 405     -11.087 -27.892  19.220  1.00160.02           O  
ANISOU  792  O   GLN A 405    17398  20024  23377  -8562  -1281  -2909       O  
ATOM    793  CB  GLN A 405     -11.057 -30.612  20.488  1.00160.76           C  
ANISOU  793  CB  GLN A 405    17369  20928  22785  -8823  -2288  -2158       C  
ATOM    794  CG  GLN A 405      -9.641 -30.108  20.820  1.00164.46           C  
ANISOU  794  CG  GLN A 405    17613  21506  23365  -9343  -2700  -1921       C  
ATOM    795  CD  GLN A 405      -9.099 -30.666  22.118  1.00168.49           C  
ANISOU  795  CD  GLN A 405    18151  22500  23367 -10111  -3339  -1649       C  
ATOM    796  OE1 GLN A 405      -9.125 -31.872  22.352  1.00166.84           O  
ANISOU  796  OE1 GLN A 405    17770  22552  23068 -10020  -3698  -1218       O  
ATOM    797  NE2 GLN A 405      -8.589 -29.788  22.966  1.00174.21           N  
ANISOU  797  NE2 GLN A 405    19079  23349  23762 -10901  -3488  -1881       N  
ATOM    798  N   SER A 406     -13.179 -28.525  18.574  1.00152.88           N  
ANISOU  798  N   SER A 406    16740  18932  22415  -7763   -672  -3162       N  
ATOM    799  CA  SER A 406     -13.737 -27.164  18.489  1.00153.50           C  
ANISOU  799  CA  SER A 406    17062  18639  22622  -7833    -83  -3681       C  
ATOM    800  C   SER A 406     -15.218 -27.197  18.147  1.00149.61           C  
ANISOU  800  C   SER A 406    16764  17941  22139  -7403    428  -3930       C  
ATOM    801  O   SER A 406     -15.871 -28.227  18.335  1.00147.41           O  
ANISOU  801  O   SER A 406    16552  17865  21591  -7245    296  -3816       O  
ATOM    802  CB  SER A 406     -12.973 -26.306  17.471  1.00153.15           C  
ANISOU  802  CB  SER A 406    16712  18301  23177  -7550     80  -3566       C  
ATOM    803  OG  SER A 406     -11.846 -25.687  18.090  1.00157.65           O  
ANISOU  803  OG  SER A 406    17261  18943  23696  -8161   -188  -3598       O  
ATOM    804  N   LYS A 407     -15.748 -26.068  17.670  1.00148.83           N  
ANISOU  804  N   LYS A 407    16733  17433  22379  -7231   1008  -4243       N  
ATOM    805  CA  LYS A 407     -17.108 -26.032  17.117  1.00144.77           C  
ANISOU  805  CA  LYS A 407    16296  16682  22028  -6736   1503  -4369       C  
ATOM    806  C   LYS A 407     -17.143 -25.777  15.609  1.00140.08           C  
ANISOU  806  C   LYS A 407    15350  15846  22027  -6044   1728  -4084       C  
ATOM    807  O   LYS A 407     -18.217 -25.742  15.002  1.00137.39           O  
ANISOU  807  O   LYS A 407    15005  15325  21869  -5611   2097  -4094       O  
ATOM    808  CB  LYS A 407     -18.031 -25.085  17.890  1.00148.32           C  
ANISOU  808  CB  LYS A 407    17131  16853  22368  -7093   2059  -4942       C  
ATOM    809  CG  LYS A 407     -19.060 -25.842  18.725  1.00148.82           C  
ANISOU  809  CG  LYS A 407    17511  17096  21938  -7240   2079  -5117       C  
ATOM    810  CD  LYS A 407     -19.917 -24.910  19.562  1.00153.95           C  
ANISOU  810  CD  LYS A 407    18558  17449  22484  -7648   2674  -5713       C  
ATOM    811  CE  LYS A 407     -21.050 -25.671  20.244  1.00153.31           C  
ANISOU  811  CE  LYS A 407    18761  17506  21982  -7696   2760  -5856       C  
ATOM    812  NZ  LYS A 407     -21.766 -24.780  21.202  1.00157.84           N1+
ANISOU  812  NZ  LYS A 407    19756  17799  22415  -8200   3354  -6476       N1+
ATOM    813  N   ILE A 408     -15.959 -25.618  15.017  1.00138.85           N  
ANISOU  813  N   ILE A 408    14892  15705  22158  -5970   1489  -3802       N  
ATOM    814  CA  ILE A 408     -15.786 -25.673  13.565  1.00133.83           C  
ANISOU  814  CA  ILE A 408    13900  14955  21993  -5340   1573  -3438       C  
ATOM    815  C   ILE A 408     -16.341 -26.985  12.979  1.00128.59           C  
ANISOU  815  C   ILE A 408    13141  14505  21210  -4873   1414  -3136       C  
ATOM    816  O   ILE A 408     -16.996 -26.974  11.937  1.00125.30           O  
ANISOU  816  O   ILE A 408    12603  13963  21043  -4376   1685  -3004       O  
ATOM    817  CB  ILE A 408     -14.298 -25.537  13.185  1.00134.87           C  
ANISOU  817  CB  ILE A 408    13729  15133  22381  -5398   1262  -3155       C  
ATOM    818  CG1 ILE A 408     -13.774 -24.147  13.574  1.00139.07           C  
ANISOU  818  CG1 ILE A 408    14322  15409  23106  -5809   1470  -3447       C  
ATOM    819  CG2 ILE A 408     -14.092 -25.815  11.700  1.00130.90           C  
ANISOU  819  CG2 ILE A 408    12878  14573  22285  -4768   1322  -2761       C  
ATOM    820  CD1 ILE A 408     -12.255 -23.964  13.453  1.00140.16           C  
ANISOU  820  CD1 ILE A 408    14191  15610  23452  -5996   1119  -3200       C  
ATOM    821  N   LEU A 409     -16.087 -28.101  13.666  1.00127.61           N  
ANISOU  821  N   LEU A 409    13070  14708  20707  -5068    976  -3017       N  
ATOM    822  CA  LEU A 409     -16.452 -29.438  13.185  1.00123.10           C  
ANISOU  822  CA  LEU A 409    12393  14342  20038  -4677    792  -2726       C  
ATOM    823  C   LEU A 409     -17.955 -29.658  13.024  1.00120.12           C  
ANISOU  823  C   LEU A 409    12201  13904  19532  -4404   1110  -2878       C  
ATOM    824  O   LEU A 409     -18.379 -30.465  12.189  1.00116.42           O  
ANISOU  824  O   LEU A 409    11605  13506  19121  -3964   1108  -2649       O  
ATOM    825  CB  LEU A 409     -15.903 -30.524  14.107  1.00124.31           C  
ANISOU  825  CB  LEU A 409    12557  14831  19841  -4998    274  -2563       C  
ATOM    826  CG  LEU A 409     -14.417 -30.752  14.392  1.00127.45           C  
ANISOU  826  CG  LEU A 409    12712  15383  20327  -5280   -183  -2270       C  
ATOM    827  CD1 LEU A 409     -14.256 -32.240  14.663  1.00126.98           C  
ANISOU  827  CD1 LEU A 409    12531  15611  20101  -5232   -589  -1932       C  
ATOM    828  CD2 LEU A 409     -13.453 -30.298  13.280  1.00127.10           C  
ANISOU  828  CD2 LEU A 409    12322  15159  20809  -4990   -119  -2029       C  
ATOM    829  N   LYS A 410     -18.748 -28.956  13.837  1.00121.49           N  
ANISOU  829  N   LYS A 410    12677  13942  19542  -4694   1397  -3268       N  
ATOM    830  CA  LYS A 410     -20.211 -29.011  13.762  1.00118.73           C  
ANISOU  830  CA  LYS A 410    12492  13483  19136  -4468   1751  -3419       C  
ATOM    831  C   LYS A 410     -20.695 -28.628  12.368  1.00114.69           C  
ANISOU  831  C   LYS A 410    11751  12762  19063  -3922   2070  -3226       C  
ATOM    832  O   LYS A 410     -21.580 -29.282  11.820  1.00111.32           O  
ANISOU  832  O   LYS A 410    11294  12397  18606  -3569   2129  -3082       O  
ATOM    833  CB  LYS A 410     -20.844 -28.077  14.801  1.00122.82           C  
ANISOU  833  CB  LYS A 410    13340  13795  19530  -4891   2114  -3892       C  
ATOM    834  CG  LYS A 410     -22.387 -28.187  14.897  1.00123.58           C  
ANISOU  834  CG  LYS A 410    13610  13766  19578  -4702   2488  -4045       C  
ATOM    835  CD  LYS A 410     -23.027 -26.871  15.398  1.00129.98           C  
ANISOU  835  CD  LYS A 410    14622  14177  20586  -4946   3078  -4470       C  
ATOM    836  CE  LYS A 410     -23.364 -25.884  14.260  1.00129.83           C  
ANISOU  836  CE  LYS A 410    14343  13781  21205  -4531   3517  -4342       C  
ATOM    837  NZ  LYS A 410     -24.657 -26.214  13.564  1.00126.95           N1+
ANISOU  837  NZ  LYS A 410    13876  13338  21021  -4052   3749  -4142       N1+
ATOM    838  N   VAL A 411     -20.110 -27.565  11.809  1.00114.53           N  
ANISOU  838  N   VAL A 411    11565  12510  19438  -3887   2261  -3205       N  
ATOM    839  CA  VAL A 411     -20.473 -27.088  10.472  1.00111.04           C  
ANISOU  839  CA  VAL A 411    10880  11886  19422  -3420   2550  -2974       C  
ATOM    840  C   VAL A 411     -20.165 -28.142   9.422  1.00106.53           C  
ANISOU  840  C   VAL A 411    10087  11558  18829  -3037   2279  -2584       C  
ATOM    841  O   VAL A 411     -21.024 -28.464   8.607  1.00103.96           O  
ANISOU  841  O   VAL A 411     9693  11255  18550  -2685   2414  -2414       O  
ATOM    842  CB  VAL A 411     -19.791 -25.745  10.096  1.00113.41           C  
ANISOU  842  CB  VAL A 411    11025  11895  20168  -3478   2790  -3001       C  
ATOM    843  CG1 VAL A 411     -20.469 -25.129   8.871  1.00111.36           C  
ANISOU  843  CG1 VAL A 411    10544  11427  20340  -3044   3157  -2772       C  
ATOM    844  CG2 VAL A 411     -19.848 -24.777  11.259  1.00117.19           C  
ANISOU  844  CG2 VAL A 411    11748  12141  20635  -3961   3032  -3443       C  
ATOM    845  N   ILE A 412     -18.952 -28.684   9.455  1.00105.44           N  
ANISOU  845  N   ILE A 412     9834  11593  18632  -3133   1914  -2440       N  
ATOM    846  CA  ILE A 412     -18.599 -29.766   8.559  1.00101.81           C  
ANISOU  846  CA  ILE A 412     9183  11335  18164  -2816   1702  -2114       C  
ATOM    847  C   ILE A 412     -19.573 -30.918   8.763  1.00 99.51           C  
ANISOU  847  C   ILE A 412     9034  11234  17539  -2702   1612  -2115       C  
ATOM    848  O   ILE A 412     -20.191 -31.380   7.805  1.00 97.23           O  
ANISOU  848  O   ILE A 412     8671  10998  17273  -2358   1717  -1950       O  
ATOM    849  CB  ILE A 412     -17.156 -30.235   8.758  1.00102.76           C  
ANISOU  849  CB  ILE A 412     9145  11579  18319  -2975   1337  -1955       C  
ATOM    850  CG1 ILE A 412     -16.180 -29.079   8.465  1.00105.00           C  
ANISOU  850  CG1 ILE A 412     9264  11666  18965  -3069   1432  -1933       C  
ATOM    851  CG2 ILE A 412     -16.871 -31.408   7.842  1.00 99.68           C  
ANISOU  851  CG2 ILE A 412     8567  11346  17961  -2644   1205  -1652       C  
ATOM    852  CD1 ILE A 412     -14.805 -29.206   9.101  1.00105.47           C  
ANISOU  852  CD1 ILE A 412     9212  11805  19056  -3397   1072  -1850       C  
ATOM    853  N   ARG A 413     -19.741 -31.338  10.017  1.00100.42           N  
ANISOU  853  N   ARG A 413     9363  11461  17329  -3022   1426  -2303       N  
ATOM    854  CA  ARG A 413     -20.560 -32.502  10.371  1.00 98.33           C  
ANISOU  854  CA  ARG A 413     9232  11388  16738  -2959   1297  -2300       C  
ATOM    855  C   ARG A 413     -21.998 -32.410   9.877  1.00 96.42           C  
ANISOU  855  C   ARG A 413     9075  11065  16496  -2686   1615  -2347       C  
ATOM    856  O   ARG A 413     -22.539 -33.412   9.436  1.00 94.14           O  
ANISOU  856  O   ARG A 413     8765  10924  16078  -2450   1541  -2209       O  
ATOM    857  CB  ARG A 413     -20.559 -32.715  11.885  1.00100.88           C  
ANISOU  857  CB  ARG A 413     9795  11827  16706  -3413   1093  -2514       C  
ATOM    858  CG  ARG A 413     -20.607 -34.157  12.345  1.00 99.95           C  
ANISOU  858  CG  ARG A 413     9699  11981  16296  -3431    752  -2374       C  
ATOM    859  CD  ARG A 413     -20.626 -34.253  13.875  1.00104.47           C  
ANISOU  859  CD  ARG A 413    10518  12693  16480  -3939    552  -2568       C  
ATOM    860  NE  ARG A 413     -21.833 -34.927  14.360  1.00105.25           N  
ANISOU  860  NE  ARG A 413    10831  12883  16275  -3905    611  -2680       N  
ATOM    861  CZ  ARG A 413     -21.865 -36.119  14.971  1.00105.42           C  
ANISOU  861  CZ  ARG A 413    10879  13152  16021  -3999    292  -2547       C  
ATOM    862  NH1 ARG A 413     -20.745 -36.805  15.221  1.00105.47           N1+
ANISOU  862  NH1 ARG A 413    10694  13344  16034  -4145   -122  -2268       N1+
ATOM    863  NH2 ARG A 413     -23.034 -36.624  15.350  1.00104.19           N  
ANISOU  863  NH2 ARG A 413    10919  13047  15619  -3947    396  -2665       N  
ATOM    864  N   LYS A 414     -22.615 -31.225   9.965  1.00 97.87           N  
ANISOU  864  N   LYS A 414     9334  10998  16853  -2733   1975  -2526       N  
ATOM    865  CA  LYS A 414     -23.982 -30.991   9.461  1.00 96.55           C  
ANISOU  865  CA  LYS A 414     9182  10712  16787  -2476   2301  -2503       C  
ATOM    866  C   LYS A 414     -24.004 -31.059   7.943  1.00 94.40           C  
ANISOU  866  C   LYS A 414     8652  10472  16740  -2087   2355  -2168       C  
ATOM    867  O   LYS A 414     -24.907 -31.660   7.347  1.00 92.54           O  
ANISOU  867  O   LYS A 414     8394  10342  16425  -1848   2385  -2017       O  
ATOM    868  CB  LYS A 414     -24.520 -29.624   9.880  1.00 99.37           C  
ANISOU  868  CB  LYS A 414     9621  10734  17399  -2620   2722  -2734       C  
ATOM    869  CG  LYS A 414     -25.496 -29.629  11.057  1.00102.86           C  
ANISOU  869  CG  LYS A 414    10353  11098  17630  -2855   2895  -3049       C  
ATOM    870  CD  LYS A 414     -26.627 -28.567  10.929  1.00107.05           C  
ANISOU  870  CD  LYS A 414    10870  11264  18539  -2757   3435  -3127       C  
ATOM    871  CE  LYS A 414     -26.243 -27.346  10.047  1.00110.85           C  
ANISOU  871  CE  LYS A 414    11093  11475  19549  -2616   3701  -2979       C  
ATOM    872  NZ  LYS A 414     -25.090 -26.494  10.538  1.00113.84           N1+
ANISOU  872  NZ  LYS A 414    11511  11711  20030  -2945   3723  -3208       N1+
ATOM    873  N   ASN A 415     -23.009 -30.435   7.316  1.00 94.74           N  
ANISOU  873  N   ASN A 415     8508  10439  17049  -2054   2369  -2048       N  
ATOM    874  CA  ASN A 415     -22.927 -30.431   5.874  1.00 92.77           C  
ANISOU  874  CA  ASN A 415     8027  10236  16983  -1740   2433  -1733       C  
ATOM    875  C   ASN A 415     -22.771 -31.823   5.309  1.00 90.38           C  
ANISOU  875  C   ASN A 415     7693  10214  16430  -1583   2186  -1571       C  
ATOM    876  O   ASN A 415     -23.583 -32.243   4.500  1.00 88.94           O  
ANISOU  876  O   ASN A 415     7478  10140  16173  -1373   2254  -1411       O  
ATOM    877  CB  ASN A 415     -21.836 -29.501   5.413  1.00 94.17           C  
ANISOU  877  CB  ASN A 415     8021  10270  17488  -1763   2502  -1653       C  
ATOM    878  CG  ASN A 415     -22.304 -28.081   5.364  1.00 96.38           C  
ANISOU  878  CG  ASN A 415     8244  10247  18128  -1775   2866  -1691       C  
ATOM    879  OD1 ASN A 415     -23.273 -27.778   4.681  1.00 96.07           O  
ANISOU  879  OD1 ASN A 415     8115  10154  18233  -1568   3085  -1511       O  
ATOM    880  ND2 ASN A 415     -21.634 -27.195   6.097  1.00 99.32           N  
ANISOU  880  ND2 ASN A 415     8653  10409  18673  -2037   2940  -1909       N  
ATOM    881  N   LEU A 416     -21.770 -32.556   5.771  1.00 90.27           N  
ANISOU  881  N   LEU A 416     7685  10311  16301  -1710   1910  -1605       N  
ATOM    882  CA  LEU A 416     -21.618 -33.931   5.358  1.00 88.82           C  
ANISOU  882  CA  LEU A 416     7470  10341  15936  -1580   1722  -1480       C  
ATOM    883  C   LEU A 416     -22.919 -34.729   5.533  1.00 87.94           C  
ANISOU  883  C   LEU A 416     7516  10352  15544  -1503   1721  -1529       C  
ATOM    884  O   LEU A 416     -23.300 -35.530   4.665  1.00 86.53           O  
ANISOU  884  O   LEU A 416     7299  10311  15264  -1312   1731  -1397       O  
ATOM    885  CB  LEU A 416     -20.529 -34.604   6.171  1.00 89.30           C  
ANISOU  885  CB  LEU A 416     7510  10468  15950  -1773   1422  -1502       C  
ATOM    886  CG  LEU A 416     -19.101 -34.095   6.194  1.00 91.65           C  
ANISOU  886  CG  LEU A 416     7633  10677  16510  -1896   1330  -1426       C  
ATOM    887  CD1 LEU A 416     -18.260 -35.257   6.669  1.00 92.18           C  
ANISOU  887  CD1 LEU A 416     7617  10871  16536  -1986   1020  -1315       C  
ATOM    888  CD2 LEU A 416     -18.592 -33.550   4.850  1.00 90.91           C  
ANISOU  888  CD2 LEU A 416     7336  10498  16705  -1677   1535  -1248       C  
ATOM    889  N   VAL A 417     -23.602 -34.517   6.659  1.00 89.02           N  
ANISOU  889  N   VAL A 417     7840  10435  15546  -1677   1727  -1734       N  
ATOM    890  CA  VAL A 417     -24.764 -35.327   6.983  1.00 87.74           C  
ANISOU  890  CA  VAL A 417     7827  10382  15125  -1627   1704  -1786       C  
ATOM    891  C   VAL A 417     -25.951 -34.950   6.119  1.00 87.65           C  
ANISOU  891  C   VAL A 417     7779  10334  15190  -1414   1952  -1669       C  
ATOM    892  O   VAL A 417     -26.740 -35.801   5.767  1.00 86.36           O  
ANISOU  892  O   VAL A 417     7647  10314  14849  -1287   1913  -1593       O  
ATOM    893  CB  VAL A 417     -25.075 -35.284   8.475  1.00 88.82           C  
ANISOU  893  CB  VAL A 417     8185  10489  15073  -1908   1642  -2036       C  
ATOM    894  CG1 VAL A 417     -26.428 -35.903   8.775  1.00 86.91           C  
ANISOU  894  CG1 VAL A 417     8092  10312  14617  -1839   1694  -2090       C  
ATOM    895  CG2 VAL A 417     -23.980 -36.017   9.223  1.00 88.93           C  
ANISOU  895  CG2 VAL A 417     8199  10637  14951  -2118   1304  -2042       C  
ATOM    896  N   LYS A 418     -26.055 -33.680   5.751  1.00 90.16           N  
ANISOU  896  N   LYS A 418     8001  10458  15795  -1386   2199  -1622       N  
ATOM    897  CA  LYS A 418     -27.056 -33.244   4.778  1.00 91.09           C  
ANISOU  897  CA  LYS A 418     8002  10550  16057  -1187   2412  -1400       C  
ATOM    898  C   LYS A 418     -26.820 -33.923   3.427  1.00 89.92           C  
ANISOU  898  C   LYS A 418     7720  10628  15814  -1014   2315  -1142       C  
ATOM    899  O   LYS A 418     -27.693 -34.622   2.916  1.00 88.95           O  
ANISOU  899  O   LYS A 418     7615  10673  15509   -915   2284  -1022       O  
ATOM    900  CB  LYS A 418     -27.040 -31.714   4.636  1.00 93.77           C  
ANISOU  900  CB  LYS A 418     8214  10610  16803  -1198   2703  -1355       C  
ATOM    901  CG  LYS A 418     -27.832 -31.175   3.441  1.00 95.83           C  
ANISOU  901  CG  LYS A 418     8263  10861  17287   -994   2890  -1003       C  
ATOM    902  CD  LYS A 418     -27.733 -29.654   3.314  1.00100.83           C  
ANISOU  902  CD  LYS A 418     8728  11183  18400   -998   3194   -925       C  
ATOM    903  CE  LYS A 418     -29.066 -29.023   3.687  1.00104.36           C  
ANISOU  903  CE  LYS A 418     9147  11395  19110   -969   3490   -887       C  
ATOM    904  NZ  LYS A 418     -29.243 -27.649   3.136  1.00108.06           N1+
ANISOU  904  NZ  LYS A 418     9348  11584  20124   -891   3814   -639       N1+
ATOM    905  N   LYS A 419     -25.628 -33.733   2.874  1.00 90.60           N  
ANISOU  905  N   LYS A 419     7688  10720  16014  -1007   2281  -1075       N  
ATOM    906  CA  LYS A 419     -25.285 -34.276   1.573  1.00 90.45           C  
ANISOU  906  CA  LYS A 419     7560  10892  15915   -886   2255   -866       C  
ATOM    907  C   LYS A 419     -25.345 -35.796   1.504  1.00 88.81           C  
ANISOU  907  C   LYS A 419     7456  10894  15393   -869   2086   -925       C  
ATOM    908  O   LYS A 419     -25.630 -36.366   0.451  1.00 88.28           O  
ANISOU  908  O   LYS A 419     7363  11007  15171   -795   2114   -787       O  
ATOM    909  CB  LYS A 419     -23.905 -33.785   1.122  1.00 91.71           C  
ANISOU  909  CB  LYS A 419     7575  10978  16292   -895   2280   -811       C  
ATOM    910  CG  LYS A 419     -23.801 -32.287   0.903  1.00 95.07           C  
ANISOU  910  CG  LYS A 419     7858  11201  17062   -890   2479   -703       C  
ATOM    911  CD  LYS A 419     -24.968 -31.731   0.103  1.00 98.47           C  
ANISOU  911  CD  LYS A 419     8196  11663  17555   -783   2650   -446       C  
ATOM    912  CE  LYS A 419     -24.549 -30.500  -0.678  1.00102.87           C  
ANISOU  912  CE  LYS A 419     8530  12096  18458   -734   2836   -210       C  
ATOM    913  NZ  LYS A 419     -25.267 -30.496  -1.982  1.00104.77           N1+
ANISOU  913  NZ  LYS A 419     8642  12544  18620   -640   2894    157       N1+
ATOM    914  N   CYS A 420     -25.067 -36.467   2.608  1.00 88.51           N  
ANISOU  914  N   CYS A 420     7532  10838  15260   -965   1919  -1122       N  
ATOM    915  CA  CYS A 420     -25.179 -37.909   2.575  1.00 87.89           C  
ANISOU  915  CA  CYS A 420     7526  10922  14944   -939   1785  -1160       C  
ATOM    916  C   CYS A 420     -26.650 -38.280   2.424  1.00 86.66           C  
ANISOU  916  C   CYS A 420     7471  10879  14574   -884   1817  -1134       C  
ATOM    917  O   CYS A 420     -27.010 -39.066   1.544  1.00 86.34           O  
ANISOU  917  O   CYS A 420     7434  11007  14362   -823   1829  -1053       O  
ATOM    918  CB  CYS A 420     -24.566 -38.554   3.811  1.00 88.02           C  
ANISOU  918  CB  CYS A 420     7604  10907  14931  -1065   1576  -1308       C  
ATOM    919  SG  CYS A 420     -22.769 -38.630   3.759  1.00 92.60           S  
ANISOU  919  SG  CYS A 420     8006  11412  15764  -1118   1486  -1249       S  
ATOM    920  N   LEU A 421     -27.506 -37.691   3.247  1.00 86.25           N  
ANISOU  920  N   LEU A 421     7498  10727  14544   -926   1856  -1202       N  
ATOM    921  CA  LEU A 421     -28.919 -37.956   3.119  1.00 85.46           C  
ANISOU  921  CA  LEU A 421     7457  10707  14305   -868   1898  -1138       C  
ATOM    922  C   LEU A 421     -29.442 -37.484   1.761  1.00 85.98           C  
ANISOU  922  C   LEU A 421     7383  10864  14419   -776   2023   -859       C  
ATOM    923  O   LEU A 421     -30.399 -38.031   1.236  1.00 85.41           O  
ANISOU  923  O   LEU A 421     7325  10955  14171   -743   2001   -738       O  
ATOM    924  CB  LEU A 421     -29.706 -37.334   4.268  1.00 86.02           C  
ANISOU  924  CB  LEU A 421     7626  10605  14452   -936   1981  -1265       C  
ATOM    925  CG  LEU A 421     -29.352 -37.747   5.699  1.00 85.47           C  
ANISOU  925  CG  LEU A 421     7725  10486  14263  -1095   1850  -1530       C  
ATOM    926  CD1 LEU A 421     -30.351 -37.119   6.636  1.00 87.41           C  
ANISOU  926  CD1 LEU A 421     8087  10567  14556  -1172   2015  -1657       C  
ATOM    927  CD2 LEU A 421     -29.336 -39.239   5.906  1.00 83.14           C  
ANISOU  927  CD2 LEU A 421     7509  10377  13702  -1091   1631  -1570       C  
ATOM    928  N   GLU A 422     -28.796 -36.482   1.185  1.00 87.46           N  
ANISOU  928  N   GLU A 422     7427  10967  14837   -760   2139   -733       N  
ATOM    929  CA  GLU A 422     -29.170 -36.015  -0.142  1.00 88.83           C  
ANISOU  929  CA  GLU A 422     7445  11261  15044   -707   2235   -416       C  
ATOM    930  C   GLU A 422     -28.958 -37.159  -1.122  1.00 87.82           C  
ANISOU  930  C   GLU A 422     7363  11409  14595   -728   2149   -381       C  
ATOM    931  O   GLU A 422     -29.919 -37.614  -1.757  1.00 87.43           O  
ANISOU  931  O   GLU A 422     7325  11562  14329   -747   2117   -229       O  
ATOM    932  CB  GLU A 422     -28.340 -34.785  -0.530  1.00 90.77           C  
ANISOU  932  CB  GLU A 422     7524  11356  15606   -693   2373   -298       C  
ATOM    933  CG  GLU A 422     -28.885 -33.967  -1.685  1.00 95.12           C  
ANISOU  933  CG  GLU A 422     7875  11982  16284   -652   2493     92       C  
ATOM    934  CD  GLU A 422     -27.997 -32.761  -2.002  1.00102.08           C  
ANISOU  934  CD  GLU A 422     8582  12689  17512   -633   2638    203       C  
ATOM    935  OE1 GLU A 422     -28.024 -31.765  -1.226  1.00105.33           O  
ANISOU  935  OE1 GLU A 422     8939  12804  18275   -625   2775    135       O  
ATOM    936  OE2 GLU A 422     -27.273 -32.803  -3.032  1.00102.80           O1-
ANISOU  936  OE2 GLU A 422     8597  12930  17530   -641   2644    344       O1-
ATOM    937  N   LEU A 423     -27.701 -37.627  -1.197  1.00 87.42           N  
ANISOU  937  N   LEU A 423     7332  11346  14535   -745   2127   -527       N  
ATOM    938  CA  LEU A 423     -27.275 -38.744  -2.041  1.00 86.95           C  
ANISOU  938  CA  LEU A 423     7325  11474  14238   -780   2124   -564       C  
ATOM    939  C   LEU A 423     -28.206 -39.942  -1.937  1.00 86.86           C  
ANISOU  939  C   LEU A 423     7455  11617  13928   -811   2033   -651       C  
ATOM    940  O   LEU A 423     -28.604 -40.507  -2.960  1.00 88.19           O  
ANISOU  940  O   LEU A 423     7662  12006  13840   -882   2071   -573       O  
ATOM    941  CB  LEU A 423     -25.872 -39.181  -1.662  1.00 86.48           C  
ANISOU  941  CB  LEU A 423     7253  11284  14321   -777   2114   -740       C  
ATOM    942  CG  LEU A 423     -25.318 -40.470  -2.272  1.00 85.24           C  
ANISOU  942  CG  LEU A 423     7143  11220  14021   -805   2168   -840       C  
ATOM    943  CD1 LEU A 423     -25.096 -40.316  -3.748  1.00 85.72           C  
ANISOU  943  CD1 LEU A 423     7169  11431  13969   -857   2354   -709       C  
ATOM    944  CD2 LEU A 423     -24.021 -40.844  -1.589  1.00 84.63           C  
ANISOU  944  CD2 LEU A 423     6999  10955  14200   -786   2132   -959       C  
ATOM    945  N   PHE A 424     -28.556 -40.334  -0.707  1.00 85.78           N  
ANISOU  945  N   PHE A 424     7406  11377  13806   -790   1917   -814       N  
ATOM    946  CA  PHE A 424     -29.450 -41.464  -0.495  1.00 84.17           C  
ANISOU  946  CA  PHE A 424     7328  11295  13355   -809   1828   -896       C  
ATOM    947  C   PHE A 424     -30.820 -41.222  -1.130  1.00 85.31           C  
ANISOU  947  C   PHE A 424     7461  11606  13344   -832   1835   -685       C  
ATOM    948  O   PHE A 424     -31.305 -42.108  -1.819  1.00 85.94           O  
ANISOU  948  O   PHE A 424     7608  11889  13155   -904   1814   -672       O  
ATOM    949  CB  PHE A 424     -29.611 -41.808   0.988  1.00 82.71           C  
ANISOU  949  CB  PHE A 424     7230  10977  13216   -796   1703  -1074       C  
ATOM    950  CG  PHE A 424     -28.321 -42.055   1.723  1.00 80.85           C  
ANISOU  950  CG  PHE A 424     6976  10607  13136   -814   1637  -1215       C  
ATOM    951  CD1 PHE A 424     -27.218 -42.605   1.088  1.00 80.43           C  
ANISOU  951  CD1 PHE A 424     6852  10557  13149   -812   1687  -1226       C  
ATOM    952  CD2 PHE A 424     -28.231 -41.765   3.083  1.00 78.31           C  
ANISOU  952  CD2 PHE A 424     6702  10156  12896   -864   1529  -1321       C  
ATOM    953  CE1 PHE A 424     -26.028 -42.836   1.803  1.00 80.37           C  
ANISOU  953  CE1 PHE A 424     6774  10415  13346   -834   1605  -1287       C  
ATOM    954  CE2 PHE A 424     -27.066 -41.994   3.793  1.00 77.53           C  
ANISOU  954  CE2 PHE A 424     6563   9971  12924   -928   1417  -1392       C  
ATOM    955  CZ  PHE A 424     -25.967 -42.536   3.161  1.00 78.60           C  
ANISOU  955  CZ  PHE A 424     6582  10101  13180   -901   1440  -1349       C  
ATOM    956  N   THR A 425     -31.442 -40.050  -0.921  1.00 86.40           N  
ANISOU  956  N   THR A 425     7500  11651  13674   -792   1878   -506       N  
ATOM    957  CA  THR A 425     -32.742 -39.749  -1.562  1.00 87.86           C  
ANISOU  957  CA  THR A 425     7606  11984  13791   -816   1877   -210       C  
ATOM    958  C   THR A 425     -32.638 -39.886  -3.064  1.00 89.72           C  
ANISOU  958  C   THR A 425     7788  12495  13805   -927   1888      0       C  
ATOM    959  O   THR A 425     -33.557 -40.405  -3.698  1.00 90.10           O  
ANISOU  959  O   THR A 425     7855  12784  13596  -1031   1812    150       O  
ATOM    960  CB  THR A 425     -33.254 -38.316  -1.340  1.00 89.03           C  
ANISOU  960  CB  THR A 425     7582  11950  14296   -750   1989     24       C  
ATOM    961  OG1 THR A 425     -33.231 -37.992   0.048  1.00 89.34           O  
ANISOU  961  OG1 THR A 425     7690  11708  14546   -695   2042   -207       O  
ATOM    962  CG2 THR A 425     -34.696 -38.189  -1.851  1.00 90.83           C  
ANISOU  962  CG2 THR A 425     7693  12316  14500   -773   1961    372       C  
ATOM    963  N   GLU A 426     -31.524 -39.394  -3.620  1.00 91.19           N  
ANISOU  963  N   GLU A 426     7911  12655  14080   -934   1985     14       N  
ATOM    964  CA  GLU A 426     -31.252 -39.493  -5.048  1.00 93.64           C  
ANISOU  964  CA  GLU A 426     8196  13228  14155  -1075   2034    182       C  
ATOM    965  C   GLU A 426     -31.147 -40.941  -5.468  1.00 93.85           C  
ANISOU  965  C   GLU A 426     8413  13437  13808  -1203   2023    -49       C  
ATOM    966  O   GLU A 426     -31.777 -41.355  -6.434  1.00 95.20           O  
ANISOU  966  O   GLU A 426     8628  13901  13641  -1389   1996     85       O  
ATOM    967  CB  GLU A 426     -29.970 -38.770  -5.413  1.00 94.29           C  
ANISOU  967  CB  GLU A 426     8189  13202  14436  -1042   2167    190       C  
ATOM    968  CG  GLU A 426     -30.055 -37.290  -5.341  1.00 96.82           C  
ANISOU  968  CG  GLU A 426     8299  13375  15113   -959   2221    465       C  
ATOM    969  CD  GLU A 426     -28.689 -36.646  -5.297  1.00100.92           C  
ANISOU  969  CD  GLU A 426     8747  13700  15896   -895   2339    381       C  
ATOM    970  OE1 GLU A 426     -27.701 -37.252  -5.799  1.00101.64           O  
ANISOU  970  OE1 GLU A 426     8910  13854  15853   -947   2401    230       O  
ATOM    971  OE2 GLU A 426     -28.601 -35.525  -4.746  1.00103.30           O1-
ANISOU  971  OE2 GLU A 426     8914  13762  16572   -802   2396    460       O1-
ATOM    972  N   LEU A 427     -30.363 -41.708  -4.727  1.00 93.38           N  
ANISOU  972  N   LEU A 427     8454  13199  13824  -1129   2048   -384       N  
ATOM    973  CA  LEU A 427     -30.202 -43.114  -5.009  1.00 94.92           C  
ANISOU  973  CA  LEU A 427     8807  13487  13768  -1228   2090   -627       C  
ATOM    974  C   LEU A 427     -31.547 -43.848  -5.051  1.00 96.30           C  
ANISOU  974  C   LEU A 427     9080  13853  13654  -1326   1970   -602       C  
ATOM    975  O   LEU A 427     -31.664 -44.859  -5.753  1.00 97.76           O  
ANISOU  975  O   LEU A 427     9395  14209  13540  -1497   2032   -728       O  
ATOM    976  CB  LEU A 427     -29.288 -43.769  -3.971  1.00 93.32           C  
ANISOU  976  CB  LEU A 427     8635  13025  13797  -1105   2100   -909       C  
ATOM    977  CG  LEU A 427     -27.766 -43.664  -4.047  1.00 93.18           C  
ANISOU  977  CG  LEU A 427     8543  12831  14030  -1057   2241  -1002       C  
ATOM    978  CD1 LEU A 427     -27.147 -44.594  -3.009  1.00 90.69           C  
ANISOU  978  CD1 LEU A 427     8237  12310  13910   -977   2196  -1214       C  
ATOM    979  CD2 LEU A 427     -27.257 -43.987  -5.440  1.00 94.66           C  
ANISOU  979  CD2 LEU A 427     8768  13157  14041  -1203   2471  -1018       C  
ATOM    980  N   ALA A 428     -32.542 -43.333  -4.312  1.00 96.88           N  
ANISOU  980  N   ALA A 428     9091  13879  13838  -1235   1828   -450       N  
ATOM    981  CA  ALA A 428     -33.871 -43.948  -4.168  1.00 97.96           C  
ANISOU  981  CA  ALA A 428     9288  14155  13778  -1296   1698   -397       C  
ATOM    982  C   ALA A 428     -34.809 -43.749  -5.365  1.00101.67           C  
ANISOU  982  C   ALA A 428     9706  14955  13967  -1504   1637    -69       C  
ATOM    983  O   ALA A 428     -35.891 -44.346  -5.418  1.00102.23           O  
ANISOU  983  O   ALA A 428     9821  15182  13839  -1603   1518     -5       O  
ATOM    984  CB  ALA A 428     -34.531 -43.496  -2.884  1.00 96.31           C  
ANISOU  984  CB  ALA A 428     9028  13739  13827  -1126   1615   -369       C  
ATOM    985  N   GLU A 429     -34.397 -42.908  -6.314  1.00105.49           N  
ANISOU  985  N   GLU A 429    10084  15558  14437  -1591   1701    165       N  
ATOM    986  CA  GLU A 429     -34.853 -43.013  -7.702  1.00110.26           C  
ANISOU  986  CA  GLU A 429    10694  16549  14649  -1891   1665    410       C  
ATOM    987  C   GLU A 429     -34.222 -44.297  -8.212  1.00111.37           C  
ANISOU  987  C   GLU A 429    11076  16788  14451  -2072   1797     24       C  
ATOM    988  O   GLU A 429     -34.009 -45.212  -7.436  1.00109.99           O  
ANISOU  988  O   GLU A 429    11019  16425  14344  -1965   1834   -320       O  
ATOM    989  CB  GLU A 429     -34.343 -41.829  -8.519  1.00112.67           C  
ANISOU  989  CB  GLU A 429    10833  16932  15042  -1934   1731    727       C  
ATOM    990  CG  GLU A 429     -35.159 -40.565  -8.374  1.00116.59           C  
ANISOU  990  CG  GLU A 429    11053  17393  15852  -1837   1628   1212       C  
ATOM    991  CD  GLU A 429     -35.139 -40.015  -6.960  1.00117.41           C  
ANISOU  991  CD  GLU A 429    11078  17076  16454  -1517   1670   1093       C  
ATOM    992  OE1 GLU A 429     -36.049 -40.394  -6.166  1.00117.44           O  
ANISOU  992  OE1 GLU A 429    11104  16998  16517  -1443   1583   1049       O  
ATOM    993  OE2 GLU A 429     -34.209 -39.224  -6.655  1.00116.85           O1-
ANISOU  993  OE2 GLU A 429    10935  16767  16694  -1368   1799   1031       O1-
ATOM    994  N   ASP A 430     -33.894 -44.385  -9.494  1.00115.04           N  
ANISOU  994  N   ASP A 430    11610  17527  14571  -2357   1899     74       N  
ATOM    995  CA  ASP A 430     -33.135 -45.533  -9.980  1.00116.70           C  
ANISOU  995  CA  ASP A 430    12050  17755  14535  -2528   2129   -340       C  
ATOM    996  C   ASP A 430     -33.315 -46.707  -9.010  1.00114.46           C  
ANISOU  996  C   ASP A 430    11883  17261  14347  -2402   2126   -695       C  
ATOM    997  O   ASP A 430     -32.400 -47.036  -8.249  1.00112.55           O  
ANISOU  997  O   ASP A 430    11643  16696  14424  -2181   2252   -963       O  
ATOM    998  CB  ASP A 430     -31.652 -45.150 -10.094  1.00117.31           C  
ANISOU  998  CB  ASP A 430    12096  17615  14858  -2407   2375   -484       C  
ATOM    999  CG  ASP A 430     -30.841 -46.123 -10.966  1.00121.13           C  
ANISOU  999  CG  ASP A 430    12788  18150  15085  -2650   2697   -832       C  
ATOM   1000  OD1 ASP A 430     -29.591 -46.096 -10.839  1.00121.34           O  
ANISOU 1000  OD1 ASP A 430    12787  17914  15403  -2507   2928  -1015       O  
ATOM   1001  OD2 ASP A 430     -31.437 -46.896 -11.771  1.00124.47           O1-
ANISOU 1001  OD2 ASP A 430    13396  18859  15037  -3000   2739   -921       O1-
ATOM   1002  N   LYS A 431     -34.513 -47.303  -9.026  1.00115.04           N  
ANISOU 1002  N   LYS A 431    12022  17523  14163  -2551   1961   -646       N  
ATOM   1003  CA  LYS A 431     -34.909 -48.364  -8.076  1.00113.19           C  
ANISOU 1003  CA  LYS A 431    11872  17114  14018  -2434   1920   -913       C  
ATOM   1004  C   LYS A 431     -33.927 -49.544  -8.058  1.00113.13           C  
ANISOU 1004  C   LYS A 431    12020  16912  14050  -2453   2202  -1370       C  
ATOM   1005  O   LYS A 431     -33.586 -50.054  -6.984  1.00111.04           O  
ANISOU 1005  O   LYS A 431    11732  16348  14108  -2208   2215  -1560       O  
ATOM   1006  CB  LYS A 431     -36.337 -48.844  -8.356  1.00114.15           C  
ANISOU 1006  CB  LYS A 431    12045  17517  13807  -2659   1720   -772       C  
ATOM   1007  CG  LYS A 431     -37.417 -47.795  -8.099  1.00115.52           C  
ANISOU 1007  CG  LYS A 431    12008  17791  14090  -2575   1448   -292       C  
ATOM   1008  CD  LYS A 431     -37.558 -46.796  -9.248  1.00120.44           C  
ANISOU 1008  CD  LYS A 431    12512  18725  14523  -2799   1386    127       C  
ATOM   1009  CE  LYS A 431     -39.031 -46.438  -9.490  1.00123.69           C  
ANISOU 1009  CE  LYS A 431    12766  19403  14824  -2946   1102    608       C  
ATOM   1010  NZ  LYS A 431     -39.273 -45.939 -10.889  1.00128.06           N1+
ANISOU 1010  NZ  LYS A 431    13258  20394  15002  -3334   1011   1006       N1+
ATOM   1011  N   GLU A 432     -33.477 -49.956  -9.250  1.00115.65           N  
ANISOU 1011  N   GLU A 432    12485  17395  14060  -2763   2445  -1524       N  
ATOM   1012  CA  GLU A 432     -32.402 -50.944  -9.411  1.00115.96           C  
ANISOU 1012  CA  GLU A 432    12642  17206  14209  -2796   2813  -1940       C  
ATOM   1013  C   GLU A 432     -31.299 -50.761  -8.364  1.00112.69           C  
ANISOU 1013  C   GLU A 432    12068  16379  14367  -2409   2875  -2008       C  
ATOM   1014  O   GLU A 432     -30.991 -51.675  -7.598  1.00111.75           O  
ANISOU 1014  O   GLU A 432    11943  15991  14524  -2265   2955  -2229       O  
ATOM   1015  CB  GLU A 432     -31.785 -50.859 -10.822  1.00120.06           C  
ANISOU 1015  CB  GLU A 432    13291  17915  14411  -3133   3112  -2023       C  
ATOM   1016  CG  GLU A 432     -32.691 -51.359 -11.979  1.00124.81           C  
ANISOU 1016  CG  GLU A 432    14112  18940  14368  -3641   3125  -2056       C  
ATOM   1017  CD  GLU A 432     -31.910 -51.848 -13.228  1.00129.65           C  
ANISOU 1017  CD  GLU A 432    14946  19639  14675  -4028   3577  -2365       C  
ATOM   1018  OE1 GLU A 432     -30.852 -51.268 -13.572  1.00129.09           O  
ANISOU 1018  OE1 GLU A 432    14820  19462  14766  -3958   3794  -2353       O  
ATOM   1019  OE2 GLU A 432     -32.373 -52.822 -13.869  1.00133.09           O1-
ANISOU 1019  OE2 GLU A 432    15620  20243  14702  -4426   3735  -2634       O1-
ATOM   1020  N   ASN A 433     -30.727 -49.563  -8.324  1.00110.80           N  
ANISOU 1020  N   ASN A 433    11682  16103  14311  -2263   2820  -1784       N  
ATOM   1021  CA  ASN A 433     -29.570 -49.293  -7.484  1.00107.96           C  
ANISOU 1021  CA  ASN A 433    11170  15393  14454  -1967   2878  -1826       C  
ATOM   1022  C   ASN A 433     -29.853 -49.037  -6.018  1.00103.61           C  
ANISOU 1022  C   ASN A 433    10498  14663  14205  -1685   2597  -1733       C  
ATOM   1023  O   ASN A 433     -28.943 -49.126  -5.186  1.00102.36           O  
ANISOU 1023  O   ASN A 433    10231  14223  14435  -1491   2618  -1800       O  
ATOM   1024  CB  ASN A 433     -28.755 -48.140  -8.065  1.00109.33           C  
ANISOU 1024  CB  ASN A 433    11244  15586  14711  -1953   2964  -1653       C  
ATOM   1025  CG  ASN A 433     -27.726 -48.618  -9.066  1.00112.94           C  
ANISOU 1025  CG  ASN A 433    11779  15995  15137  -2120   3365  -1863       C  
ATOM   1026  OD1 ASN A 433     -28.037 -49.399  -9.976  1.00115.98           O  
ANISOU 1026  OD1 ASN A 433    12356  16553  15157  -2419   3570  -2046       O  
ATOM   1027  ND2 ASN A 433     -26.484 -48.165  -8.896  1.00113.55           N  
ANISOU 1027  ND2 ASN A 433    11712  15826  15604  -1953   3505  -1851       N  
ATOM   1028  N   TYR A 434     -31.100 -48.701  -5.692  1.00100.88           N  
ANISOU 1028  N   TYR A 434    10162  14479  13688  -1684   2339  -1559       N  
ATOM   1029  CA  TYR A 434     -31.421 -48.457  -4.298  1.00 96.52           C  
ANISOU 1029  CA  TYR A 434     9527  13758  13387  -1454   2118  -1502       C  
ATOM   1030  C   TYR A 434     -31.487 -49.785  -3.606  1.00 95.13           C  
ANISOU 1030  C   TYR A 434     9415  13448  13279  -1417   2127  -1730       C  
ATOM   1031  O   TYR A 434     -31.205 -49.885  -2.415  1.00 93.37           O  
ANISOU 1031  O   TYR A 434     9125  13025  13326  -1243   2017  -1755       O  
ATOM   1032  CB  TYR A 434     -32.704 -47.666  -4.098  1.00 95.14           C  
ANISOU 1032  CB  TYR A 434     9317  13735  13094  -1445   1898  -1242       C  
ATOM   1033  CG  TYR A 434     -32.831 -47.188  -2.672  1.00 92.15           C  
ANISOU 1033  CG  TYR A 434     8865  13145  13003  -1228   1748  -1211       C  
ATOM   1034  CD1 TYR A 434     -32.096 -46.100  -2.217  1.00 91.07           C  
ANISOU 1034  CD1 TYR A 434     8617  12844  13141  -1105   1752  -1136       C  
ATOM   1035  CD2 TYR A 434     -33.666 -47.844  -1.760  1.00 90.29           C  
ANISOU 1035  CD2 TYR A 434     8686  12871  12749  -1175   1619  -1278       C  
ATOM   1036  CE1 TYR A 434     -32.207 -45.659  -0.893  1.00 89.31           C  
ANISOU 1036  CE1 TYR A 434     8363  12437  13132   -971   1641  -1149       C  
ATOM   1037  CE2 TYR A 434     -33.777 -47.415  -0.437  1.00 87.09           C  
ANISOU 1037  CE2 TYR A 434     8245  12286  12558  -1025   1510  -1274       C  
ATOM   1038  CZ  TYR A 434     -33.043 -46.327  -0.016  1.00 87.45           C  
ANISOU 1038  CZ  TYR A 434     8204  12183  12839   -943   1527  -1223       C  
ATOM   1039  OH  TYR A 434     -33.131 -45.902   1.280  1.00 87.08           O  
ANISOU 1039  OH  TYR A 434     8157  11972  12957   -860   1446  -1258       O  
ATOM   1040  N   LYS A 435     -31.830 -50.812  -4.375  1.00 95.85           N  
ANISOU 1040  N   LYS A 435     9637  13657  13122  -1611   2268  -1891       N  
ATOM   1041  CA  LYS A 435     -31.879 -52.149  -3.842  1.00 95.16           C  
ANISOU 1041  CA  LYS A 435     9598  13423  13133  -1590   2327  -2110       C  
ATOM   1042  C   LYS A 435     -30.480 -52.543  -3.395  1.00 94.73           C  
ANISOU 1042  C   LYS A 435     9430  13057  13505  -1451   2499  -2227       C  
ATOM   1043  O   LYS A 435     -30.315 -53.047  -2.294  1.00 93.40           O  
ANISOU 1043  O   LYS A 435     9179  12701  13607  -1298   2395  -2238       O  
ATOM   1044  CB  LYS A 435     -32.446 -53.133  -4.861  1.00 97.72           C  
ANISOU 1044  CB  LYS A 435    10095  13916  13117  -1871   2500  -2295       C  
ATOM   1045  CG  LYS A 435     -32.885 -54.479  -4.270  1.00 99.11           C  
ANISOU 1045  CG  LYS A 435    10320  13968  13367  -1858   2519  -2485       C  
ATOM   1046  CD  LYS A 435     -32.353 -55.634  -5.147  1.00105.65           C  
ANISOU 1046  CD  LYS A 435    11259  14705  14175  -2070   2920  -2808       C  
ATOM   1047  CE  LYS A 435     -33.033 -56.964  -4.812  1.00107.83           C  
ANISOU 1047  CE  LYS A 435    11608  14909  14452  -2129   2959  -2996       C  
ATOM   1048  NZ  LYS A 435     -32.546 -58.075  -5.690  1.00111.62           N1+
ANISOU 1048  NZ  LYS A 435    12206  15264  14940  -2365   3415  -3347       N1+
ATOM   1049  N   LYS A 436     -29.467 -52.287  -4.219  1.00 95.95           N  
ANISOU 1049  N   LYS A 436     9557  13158  13739  -1511   2751  -2274       N  
ATOM   1050  CA  LYS A 436     -28.104 -52.611  -3.803  1.00 96.14           C  
ANISOU 1050  CA  LYS A 436     9424  12866  14238  -1373   2915  -2327       C  
ATOM   1051  C   LYS A 436     -27.703 -51.851  -2.523  1.00 93.71           C  
ANISOU 1051  C   LYS A 436     8945  12434  14223  -1154   2621  -2126       C  
ATOM   1052  O   LYS A 436     -27.213 -52.449  -1.558  1.00 93.32           O  
ANISOU 1052  O   LYS A 436     8769  12177  14508  -1039   2557  -2113       O  
ATOM   1053  CB  LYS A 436     -27.095 -52.408  -4.932  1.00 98.58           C  
ANISOU 1053  CB  LYS A 436     9727  13127  14600  -1477   3266  -2404       C  
ATOM   1054  CG  LYS A 436     -26.894 -53.651  -5.784  1.00102.58           C  
ANISOU 1054  CG  LYS A 436    10347  13545  15084  -1665   3688  -2697       C  
ATOM   1055  CD  LYS A 436     -27.338 -53.454  -7.241  1.00107.07           C  
ANISOU 1055  CD  LYS A 436    11139  14411  15129  -1985   3888  -2806       C  
ATOM   1056  CE  LYS A 436     -26.279 -52.684  -8.067  1.00108.98           C  
ANISOU 1056  CE  LYS A 436    11337  14630  15440  -2029   4133  -2765       C  
ATOM   1057  NZ  LYS A 436     -26.752 -52.351  -9.440  1.00111.06           N1+
ANISOU 1057  NZ  LYS A 436    11815  15247  15135  -2375   4266  -2805       N1+
ATOM   1058  N   PHE A 437     -27.951 -50.544  -2.508  1.00 91.88           N  
ANISOU 1058  N   PHE A 437     8708  12338  13863  -1129   2446  -1958       N  
ATOM   1059  CA  PHE A 437     -27.690 -49.736  -1.331  1.00 89.59           C  
ANISOU 1059  CA  PHE A 437     8303  11952  13785   -985   2193  -1811       C  
ATOM   1060  C   PHE A 437     -28.422 -50.220  -0.068  1.00 87.83           C  
ANISOU 1060  C   PHE A 437     8105  11708  13557   -924   1951  -1809       C  
ATOM   1061  O   PHE A 437     -27.802 -50.390   0.977  1.00 87.94           O  
ANISOU 1061  O   PHE A 437     8010  11569  13833   -854   1825  -1767       O  
ATOM   1062  CB  PHE A 437     -28.036 -48.270  -1.607  1.00 89.07           C  
ANISOU 1062  CB  PHE A 437     8241  12018  13582   -988   2102  -1652       C  
ATOM   1063  CG  PHE A 437     -28.051 -47.417  -0.380  1.00 85.81           C  
ANISOU 1063  CG  PHE A 437     7764  11517  13320   -892   1872  -1554       C  
ATOM   1064  CD1 PHE A 437     -29.226 -47.240   0.343  1.00 82.48           C  
ANISOU 1064  CD1 PHE A 437     7423  11167  12748   -878   1698  -1524       C  
ATOM   1065  CD2 PHE A 437     -26.884 -46.812   0.073  1.00 85.37           C  
ANISOU 1065  CD2 PHE A 437     7575  11298  13560   -843   1849  -1504       C  
ATOM   1066  CE1 PHE A 437     -29.252 -46.455   1.504  1.00 81.00           C  
ANISOU 1066  CE1 PHE A 437     7212  10884  12680   -835   1542  -1482       C  
ATOM   1067  CE2 PHE A 437     -26.898 -46.031   1.229  1.00 84.58           C  
ANISOU 1067  CE2 PHE A 437     7450  11128  13557   -819   1652  -1453       C  
ATOM   1068  CZ  PHE A 437     -28.097 -45.846   1.944  1.00 81.42           C  
ANISOU 1068  CZ  PHE A 437     7160  10795  12979   -824   1518  -1462       C  
ATOM   1069  N   TYR A 438     -29.731 -50.428  -0.154  1.00 86.45           N  
ANISOU 1069  N   TYR A 438     8062  11700  13082   -974   1875  -1828       N  
ATOM   1070  CA  TYR A 438     -30.518 -50.700   1.041  1.00 84.43           C  
ANISOU 1070  CA  TYR A 438     7839  11436  12801   -918   1656  -1809       C  
ATOM   1071  C   TYR A 438     -30.256 -52.092   1.565  1.00 84.33           C  
ANISOU 1071  C   TYR A 438     7794  11298  12950   -898   1674  -1904       C  
ATOM   1072  O   TYR A 438     -30.234 -52.313   2.765  1.00 83.39           O  
ANISOU 1072  O   TYR A 438     7629  11103  12951   -843   1494  -1854       O  
ATOM   1073  CB  TYR A 438     -32.003 -50.482   0.772  1.00 83.59           C  
ANISOU 1073  CB  TYR A 438     7851  11525  12382   -969   1582  -1764       C  
ATOM   1074  CG  TYR A 438     -32.879 -50.490   2.009  1.00 82.17           C  
ANISOU 1074  CG  TYR A 438     7709  11329  12183   -907   1386  -1729       C  
ATOM   1075  CD1 TYR A 438     -33.202 -49.309   2.686  1.00 81.75           C  
ANISOU 1075  CD1 TYR A 438     7646  11251  12162   -862   1287  -1625       C  
ATOM   1076  CD2 TYR A 438     -33.405 -51.679   2.489  1.00 81.18           C  
ANISOU 1076  CD2 TYR A 438     7632  11195  12017   -907   1337  -1811       C  
ATOM   1077  CE1 TYR A 438     -34.031 -49.340   3.824  1.00 80.84           C  
ANISOU 1077  CE1 TYR A 438     7589  11108  12016   -834   1163  -1624       C  
ATOM   1078  CE2 TYR A 438     -34.218 -51.716   3.600  1.00 79.97           C  
ANISOU 1078  CE2 TYR A 438     7523  11034  11829   -864   1179  -1779       C  
ATOM   1079  CZ  TYR A 438     -34.534 -50.562   4.262  1.00 80.00           C  
ANISOU 1079  CZ  TYR A 438     7536  11019  11841   -835   1101  -1694       C  
ATOM   1080  OH  TYR A 438     -35.351 -50.675   5.367  1.00 80.15           O  
ANISOU 1080  OH  TYR A 438     7620  11018  11815   -817    995  -1693       O  
ATOM   1081  N   GLU A 439     -30.030 -53.027   0.660  1.00 85.86           N  
ANISOU 1081  N   GLU A 439     8004  11461  13155   -964   1915  -2036       N  
ATOM   1082  CA  GLU A 439     -29.700 -54.394   1.044  1.00 87.38           C  
ANISOU 1082  CA  GLU A 439     8127  11479  13593   -941   2005  -2118       C  
ATOM   1083  C   GLU A 439     -28.521 -54.373   2.025  1.00 86.90           C  
ANISOU 1083  C   GLU A 439     7853  11214  13950   -838   1905  -1975       C  
ATOM   1084  O   GLU A 439     -28.509 -55.116   3.003  1.00 87.07           O  
ANISOU 1084  O   GLU A 439     7785  11143  14152   -793   1775  -1905       O  
ATOM   1085  CB  GLU A 439     -29.365 -55.221  -0.203  1.00 90.35           C  
ANISOU 1085  CB  GLU A 439     8543  11794  13991  -1054   2380  -2314       C  
ATOM   1086  CG  GLU A 439     -29.647 -56.725  -0.130  1.00 95.34           C  
ANISOU 1086  CG  GLU A 439     9182  12297  14744  -1087   2537  -2464       C  
ATOM   1087  CD  GLU A 439     -29.561 -57.427  -1.523  1.00103.54           C  
ANISOU 1087  CD  GLU A 439    10341  13314  15684  -1280   2962  -2731       C  
ATOM   1088  OE1 GLU A 439     -30.639 -57.850  -2.037  1.00105.48           O  
ANISOU 1088  OE1 GLU A 439    10777  13740  15562  -1444   2984  -2873       O  
ATOM   1089  OE2 GLU A 439     -28.433 -57.543  -2.101  1.00105.42           O1-
ANISOU 1089  OE2 GLU A 439    10492  13359  16203  -1296   3283  -2803       O1-
ATOM   1090  N   GLN A 440     -27.565 -53.479   1.769  1.00 86.59           N  
ANISOU 1090  N   GLN A 440     7723  11127  14050   -822   1941  -1899       N  
ATOM   1091  CA  GLN A 440     -26.343 -53.322   2.571  1.00 85.91           C  
ANISOU 1091  CA  GLN A 440     7412  10868  14359   -765   1833  -1728       C  
ATOM   1092  C   GLN A 440     -26.443 -52.410   3.795  1.00 84.21           C  
ANISOU 1092  C   GLN A 440     7194  10733  14067   -771   1479  -1585       C  
ATOM   1093  O   GLN A 440     -25.734 -52.638   4.776  1.00 85.07           O  
ANISOU 1093  O   GLN A 440     7137  10749  14433   -778   1301  -1425       O  
ATOM   1094  CB  GLN A 440     -25.232 -52.782   1.689  1.00 86.93           C  
ANISOU 1094  CB  GLN A 440     7440  10896  14692   -763   2056  -1717       C  
ATOM   1095  CG  GLN A 440     -24.854 -53.718   0.589  1.00 88.53           C  
ANISOU 1095  CG  GLN A 440     7624  10961  15050   -789   2465  -1869       C  
ATOM   1096  CD  GLN A 440     -24.181 -54.956   1.099  1.00 88.40           C  
ANISOU 1096  CD  GLN A 440     7388  10677  15520   -734   2565  -1802       C  
ATOM   1097  OE1 GLN A 440     -23.473 -54.921   2.097  1.00 88.87           O  
ANISOU 1097  OE1 GLN A 440     7225  10629  15912   -677   2345  -1564       O  
ATOM   1098  NE2 GLN A 440     -24.386 -56.063   0.409  1.00 89.67           N  
ANISOU 1098  NE2 GLN A 440     7597  10726  15747   -776   2906  -1995       N  
ATOM   1099  N   PHE A 441     -27.290 -51.379   3.736  1.00 81.89           N  
ANISOU 1099  N   PHE A 441     7070  10603  13442   -794   1394  -1628       N  
ATOM   1100  CA  PHE A 441     -27.207 -50.280   4.698  1.00 80.79           C  
ANISOU 1100  CA  PHE A 441     6939  10495  13261   -832   1165  -1544       C  
ATOM   1101  C   PHE A 441     -28.509 -49.942   5.404  1.00 79.87           C  
ANISOU 1101  C   PHE A 441     7000  10502  12844   -861   1024  -1588       C  
ATOM   1102  O   PHE A 441     -28.638 -48.842   5.969  1.00 80.00           O  
ANISOU 1102  O   PHE A 441     7071  10535  12787   -911    931  -1577       O  
ATOM   1103  CB  PHE A 441     -26.564 -49.035   4.046  1.00 80.48           C  
ANISOU 1103  CB  PHE A 441     6859  10436  13281   -834   1257  -1517       C  
ATOM   1104  CG  PHE A 441     -25.146 -49.266   3.627  1.00 80.96           C  
ANISOU 1104  CG  PHE A 441     6719  10345  13695   -815   1371  -1444       C  
ATOM   1105  CD1 PHE A 441     -24.167 -49.565   4.575  1.00 80.00           C  
ANISOU 1105  CD1 PHE A 441     6412  10111  13873   -850   1199  -1297       C  
ATOM   1106  CD2 PHE A 441     -24.789 -49.274   2.295  1.00 80.42           C  
ANISOU 1106  CD2 PHE A 441     6631  10249  13674   -784   1657  -1497       C  
ATOM   1107  CE1 PHE A 441     -22.869 -49.840   4.203  1.00 78.55           C  
ANISOU 1107  CE1 PHE A 441     5997   9757  14089   -822   1317  -1185       C  
ATOM   1108  CE2 PHE A 441     -23.473 -49.548   1.928  1.00 80.26           C  
ANISOU 1108  CE2 PHE A 441     6411  10050  14031   -760   1812  -1431       C  
ATOM   1109  CZ  PHE A 441     -22.524 -49.824   2.891  1.00 79.19           C  
ANISOU 1109  CZ  PHE A 441     6063   9773  14251   -763   1643  -1264       C  
ATOM   1110  N   SER A 442     -29.453 -50.890   5.399  1.00 79.39           N  
ANISOU 1110  N   SER A 442     7022  10499  12641   -838   1035  -1646       N  
ATOM   1111  CA  SER A 442     -30.762 -50.708   6.043  1.00 78.24           C  
ANISOU 1111  CA  SER A 442     7032  10452  12244   -854    932  -1678       C  
ATOM   1112  C   SER A 442     -30.565 -50.490   7.536  1.00 78.75           C  
ANISOU 1112  C   SER A 442     7106  10495  12318   -936    718  -1632       C  
ATOM   1113  O   SER A 442     -31.208 -49.616   8.135  1.00 78.35           O  
ANISOU 1113  O   SER A 442     7176  10475  12117   -988    679  -1668       O  
ATOM   1114  CB  SER A 442     -31.678 -51.913   5.809  1.00 77.53           C  
ANISOU 1114  CB  SER A 442     7001  10415  12041   -826    971  -1734       C  
ATOM   1115  OG  SER A 442     -31.821 -52.713   6.984  1.00 77.93           O  
ANISOU 1115  OG  SER A 442     7042  10442  12125   -842    811  -1699       O  
ATOM   1116  N   LYS A 443     -29.661 -51.288   8.107  1.00 80.06           N  
ANISOU 1116  N   LYS A 443     7134  10603  12681   -970    602  -1538       N  
ATOM   1117  CA  LYS A 443     -29.283 -51.235   9.515  1.00 81.80           C  
ANISOU 1117  CA  LYS A 443     7336  10845  12898  -1112    358  -1442       C  
ATOM   1118  C   LYS A 443     -28.911 -49.834   9.965  1.00 82.41           C  
ANISOU 1118  C   LYS A 443     7474  10928  12908  -1240    300  -1471       C  
ATOM   1119  O   LYS A 443     -29.397 -49.375  10.984  1.00 83.24           O  
ANISOU 1119  O   LYS A 443     7725  11093  12809  -1382    198  -1523       O  
ATOM   1120  CB  LYS A 443     -28.064 -52.108   9.741  1.00 84.10           C  
ANISOU 1120  CB  LYS A 443     7381  11056  13516  -1132    257  -1251       C  
ATOM   1121  CG  LYS A 443     -28.241 -53.184  10.780  1.00 87.49           C  
ANISOU 1121  CG  LYS A 443     7753  11525  13961  -1196     65  -1111       C  
ATOM   1122  CD  LYS A 443     -28.147 -54.560  10.113  1.00 92.06           C  
ANISOU 1122  CD  LYS A 443     8173  11983  14823  -1049    221  -1063       C  
ATOM   1123  CE  LYS A 443     -26.785 -54.727   9.433  1.00 96.28           C  
ANISOU 1123  CE  LYS A 443     8446  12345  15791   -997    343   -943       C  
ATOM   1124  NZ  LYS A 443     -26.513 -56.135   9.028  1.00100.99           N1+
ANISOU 1124  NZ  LYS A 443     8842  12764  16762   -893    517   -867       N1+
ATOM   1125  N   ASN A 444     -28.025 -49.182   9.209  1.00 82.79           N  
ANISOU 1125  N   ASN A 444     7415  10902  13137  -1207    391  -1450       N  
ATOM   1126  CA  ASN A 444     -27.550 -47.846   9.489  1.00 83.13           C  
ANISOU 1126  CA  ASN A 444     7488  10920  13176  -1323    368  -1480       C  
ATOM   1127  C   ASN A 444     -28.659 -46.821   9.418  1.00 82.65           C  
ANISOU 1127  C   ASN A 444     7622  10867  12915  -1315    514  -1632       C  
ATOM   1128  O   ASN A 444     -28.768 -45.966  10.281  1.00 83.59           O  
ANISOU 1128  O   ASN A 444     7852  10972  12933  -1477    477  -1711       O  
ATOM   1129  CB  ASN A 444     -26.459 -47.474   8.505  1.00 83.61           C  
ANISOU 1129  CB  ASN A 444     7376  10889  13503  -1250    477  -1413       C  
ATOM   1130  CG  ASN A 444     -25.258 -48.391   8.594  1.00 85.20           C  
ANISOU 1130  CG  ASN A 444     7337  11028  14006  -1258    373  -1228       C  
ATOM   1131  OD1 ASN A 444     -25.325 -49.557   8.190  1.00 85.16           O  
ANISOU 1131  OD1 ASN A 444     7250  10990  14116  -1148    448  -1187       O  
ATOM   1132  ND2 ASN A 444     -24.147 -47.871   9.114  1.00 85.07           N  
ANISOU 1132  ND2 ASN A 444     7187  10977  14157  -1399    216  -1103       N  
ATOM   1133  N   ILE A 445     -29.490 -46.896   8.389  1.00 82.06           N  
ANISOU 1133  N   ILE A 445     7576  10805  12796  -1151    695  -1661       N  
ATOM   1134  CA  ILE A 445     -30.638 -46.004   8.306  1.00 82.24           C  
ANISOU 1134  CA  ILE A 445     7727  10819  12699  -1129    835  -1731       C  
ATOM   1135  C   ILE A 445     -31.462 -46.112   9.574  1.00 82.83           C  
ANISOU 1135  C   ILE A 445     7962  10910  12598  -1239    767  -1816       C  
ATOM   1136  O   ILE A 445     -31.824 -45.095  10.174  1.00 83.89           O  
ANISOU 1136  O   ILE A 445     8202  10969  12701  -1339    856  -1909       O  
ATOM   1137  CB  ILE A 445     -31.483 -46.276   7.054  1.00 81.20           C  
ANISOU 1137  CB  ILE A 445     7581  10750  12521   -977    978  -1683       C  
ATOM   1138  CG1 ILE A 445     -30.710 -45.785   5.834  1.00 82.38           C  
ANISOU 1138  CG1 ILE A 445     7608  10887  12806   -922   1092  -1613       C  
ATOM   1139  CG2 ILE A 445     -32.838 -45.564   7.127  1.00 79.96           C  
ANISOU 1139  CG2 ILE A 445     7514  10582  12285   -954   1091  -1683       C  
ATOM   1140  CD1 ILE A 445     -30.814 -46.695   4.663  1.00 83.07           C  
ANISOU 1140  CD1 ILE A 445     7658  11069  12835   -855   1167  -1582       C  
ATOM   1141  N   LYS A 446     -31.729 -47.341   9.997  1.00 83.03           N  
ANISOU 1141  N   LYS A 446     8004  11015  12528  -1234    639  -1793       N  
ATOM   1142  CA  LYS A 446     -32.516 -47.570  11.198  1.00 84.06           C  
ANISOU 1142  CA  LYS A 446     8289  11179  12469  -1347    574  -1860       C  
ATOM   1143  C   LYS A 446     -31.786 -47.054  12.429  1.00 86.53           C  
ANISOU 1143  C   LYS A 446     8669  11494  12712  -1607    443  -1908       C  
ATOM   1144  O   LYS A 446     -32.339 -46.246  13.170  1.00 88.27           O  
ANISOU 1144  O   LYS A 446     9059  11670  12807  -1749    545  -2048       O  
ATOM   1145  CB  LYS A 446     -32.881 -49.039  11.337  1.00 83.12           C  
ANISOU 1145  CB  LYS A 446     8145  11144  12291  -1285    460  -1794       C  
ATOM   1146  CG  LYS A 446     -33.876 -49.476  10.290  1.00 83.41           C  
ANISOU 1146  CG  LYS A 446     8175  11197  12316  -1101    598  -1789       C  
ATOM   1147  CD  LYS A 446     -34.208 -50.951  10.402  1.00 85.81           C  
ANISOU 1147  CD  LYS A 446     8453  11560  12591  -1052    510  -1748       C  
ATOM   1148  CE  LYS A 446     -34.980 -51.420   9.183  1.00 85.26           C  
ANISOU 1148  CE  LYS A 446     8366  11522  12505   -920    638  -1752       C  
ATOM   1149  NZ  LYS A 446     -34.338 -52.701   8.721  1.00 88.20           N1+
ANISOU 1149  NZ  LYS A 446     8621  11884  13004   -881    620  -1729       N1+
ATOM   1150  N   LEU A 447     -30.544 -47.489  12.628  1.00 87.81           N  
ANISOU 1150  N   LEU A 447     8691  11698  12972  -1695    237  -1787       N  
ATOM   1151  CA  LEU A 447     -29.689 -47.023  13.719  1.00 90.42           C  
ANISOU 1151  CA  LEU A 447     9052  12072  13229  -1996     55  -1781       C  
ATOM   1152  C   LEU A 447     -29.709 -45.508  13.858  1.00 91.59           C  
ANISOU 1152  C   LEU A 447     9332  12121  13346  -2128    226  -1966       C  
ATOM   1153  O   LEU A 447     -29.573 -44.978  14.947  1.00 93.92           O  
ANISOU 1153  O   LEU A 447     9776  12450  13457  -2435    166  -2074       O  
ATOM   1154  CB  LEU A 447     -28.271 -47.449  13.424  1.00 91.64           C  
ANISOU 1154  CB  LEU A 447     8955  12234  13630  -2001   -128  -1572       C  
ATOM   1155  CG  LEU A 447     -27.327 -47.789  14.555  1.00 95.44           C  
ANISOU 1155  CG  LEU A 447     9355  12831  14076  -2297   -454  -1396       C  
ATOM   1156  CD1 LEU A 447     -26.515 -49.012  14.102  1.00 97.18           C  
ANISOU 1156  CD1 LEU A 447     9269  13034  14620  -2149   -581  -1109       C  
ATOM   1157  CD2 LEU A 447     -26.432 -46.600  14.888  1.00 97.62           C  
ANISOU 1157  CD2 LEU A 447     9643  13093  14355  -2547   -515  -1438       C  
ATOM   1158  N   GLY A 448     -29.881 -44.817  12.741  1.00 90.67           N  
ANISOU 1158  N   GLY A 448     9156  11882  13409  -1921    453  -1998       N  
ATOM   1159  CA  GLY A 448     -29.906 -43.370  12.725  1.00 91.95           C  
ANISOU 1159  CA  GLY A 448     9394  11905  13636  -2004    661  -2143       C  
ATOM   1160  C   GLY A 448     -31.245 -42.799  13.114  1.00 92.23           C  
ANISOU 1160  C   GLY A 448     9620  11845  13575  -2017    917  -2311       C  
ATOM   1161  O   GLY A 448     -31.310 -41.749  13.733  1.00 94.42           O  
ANISOU 1161  O   GLY A 448    10029  12002  13842  -2215   1081  -2490       O  
ATOM   1162  N   ILE A 449     -32.322 -43.467  12.734  1.00 90.88           N  
ANISOU 1162  N   ILE A 449     9456  11705  13369  -1817    982  -2256       N  
ATOM   1163  CA  ILE A 449     -33.655 -43.063  13.185  1.00 91.68           C  
ANISOU 1163  CA  ILE A 449     9711  11704  13417  -1824   1226  -2377       C  
ATOM   1164  C   ILE A 449     -33.709 -43.054  14.708  1.00 94.14           C  
ANISOU 1164  C   ILE A 449    10252  12044  13472  -2148   1193  -2566       C  
ATOM   1165  O   ILE A 449     -34.269 -42.144  15.322  1.00 95.48           O  
ANISOU 1165  O   ILE A 449    10583  12055  13637  -2298   1468  -2764       O  
ATOM   1166  CB  ILE A 449     -34.734 -43.983  12.599  1.00 89.54           C  
ANISOU 1166  CB  ILE A 449     9392  11500  13127  -1587   1231  -2251       C  
ATOM   1167  CG1 ILE A 449     -35.086 -43.498  11.205  1.00 88.59           C  
ANISOU 1167  CG1 ILE A 449     9106  11318  13233  -1353   1383  -2104       C  
ATOM   1168  CG2 ILE A 449     -35.979 -44.003  13.468  1.00 89.93           C  
ANISOU 1168  CG2 ILE A 449     9612  11490  13065  -1649   1390  -2360       C  
ATOM   1169  CD1 ILE A 449     -35.400 -44.596  10.285  1.00 88.11           C  
ANISOU 1169  CD1 ILE A 449     8943  11406  13127  -1174   1262  -1948       C  
ATOM   1170  N   HIS A 450     -33.091 -44.064  15.310  1.00 95.25           N  
ANISOU 1170  N   HIS A 450    10396  12380  13414  -2281    873  -2492       N  
ATOM   1171  CA  HIS A 450     -33.023 -44.139  16.744  1.00 98.66           C  
ANISOU 1171  CA  HIS A 450    11036  12906  13543  -2645    779  -2621       C  
ATOM   1172  C   HIS A 450     -32.265 -42.975  17.348  1.00102.17           C  
ANISOU 1172  C   HIS A 450    11594  13286  13938  -2983    840  -2803       C  
ATOM   1173  O   HIS A 450     -32.732 -42.394  18.320  1.00104.94           O  
ANISOU 1173  O   HIS A 450    12196  13582  14092  -3272   1030  -3048       O  
ATOM   1174  CB  HIS A 450     -32.392 -45.437  17.215  1.00 98.68           C  
ANISOU 1174  CB  HIS A 450    10956  13144  13393  -2732    386  -2418       C  
ATOM   1175  CG  HIS A 450     -32.547 -45.654  18.687  1.00102.78           C  
ANISOU 1175  CG  HIS A 450    11695  13809  13545  -3117    274  -2503       C  
ATOM   1176  ND1 HIS A 450     -33.537 -46.451  19.222  1.00103.67           N  
ANISOU 1176  ND1 HIS A 450    11918  13994  13476  -3098    288  -2499       N  
ATOM   1177  CD2 HIS A 450     -31.871 -45.136  19.740  1.00106.76           C  
ANISOU 1177  CD2 HIS A 450    12348  14414  13799  -3569    158  -2600       C  
ATOM   1178  CE1 HIS A 450     -33.446 -46.439  20.541  1.00106.66           C  
ANISOU 1178  CE1 HIS A 450    12504  14521  13500  -3518    187  -2580       C  
ATOM   1179  NE2 HIS A 450     -32.444 -45.646  20.880  1.00109.65           N  
ANISOU 1179  NE2 HIS A 450    12918  14931  13812  -3830    101  -2646       N  
ATOM   1180  N   GLU A 451     -31.110 -42.634  16.776  1.00102.94           N  
ANISOU 1180  N   GLU A 451    11517  13380  14215  -2968    708  -2702       N  
ATOM   1181  CA  GLU A 451     -30.210 -41.654  17.387  1.00106.60           C  
ANISOU 1181  CA  GLU A 451    12066  13817  14619  -3333    691  -2847       C  
ATOM   1182  C   GLU A 451     -30.436 -40.236  16.913  1.00107.14           C  
ANISOU 1182  C   GLU A 451    12168  13606  14931  -3284   1084  -3044       C  
ATOM   1183  O   GLU A 451     -30.378 -39.313  17.714  1.00110.79           O  
ANISOU 1183  O   GLU A 451    12834  13974  15287  -3630   1261  -3309       O  
ATOM   1184  CB  GLU A 451     -28.735 -42.009  17.147  1.00107.51           C  
ANISOU 1184  CB  GLU A 451    11951  14066  14829  -3388    323  -2606       C  
ATOM   1185  CG  GLU A 451     -28.390 -43.491  17.178  1.00109.14           C  
ANISOU 1185  CG  GLU A 451    11985  14479  15001  -3297    -32  -2303       C  
ATOM   1186  CD  GLU A 451     -28.308 -44.075  18.581  1.00115.68           C  
ANISOU 1186  CD  GLU A 451    12952  15541  15461  -3699   -307  -2264       C  
ATOM   1187  OE1 GLU A 451     -29.270 -43.952  19.375  1.00118.20           O  
ANISOU 1187  OE1 GLU A 451    13543  15878  15488  -3870   -153  -2476       O  
ATOM   1188  OE2 GLU A 451     -27.265 -44.684  18.887  1.00119.73           O1-
ANISOU 1188  OE2 GLU A 451    13279  16220  15991  -3854   -678  -1988       O1-
ATOM   1189  N   ASP A 452     -30.679 -40.056  15.620  1.00104.67           N  
ANISOU 1189  N   ASP A 452    11655  13165  14948  -2886   1231  -2910       N  
ATOM   1190  CA  ASP A 452     -30.642 -38.728  15.008  1.00105.58           C  
ANISOU 1190  CA  ASP A 452    11713  13027  15374  -2815   1548  -2996       C  
ATOM   1191  C   ASP A 452     -32.022 -38.114  14.770  1.00105.37           C  
ANISOU 1191  C   ASP A 452    11738  12765  15533  -2645   1977  -3082       C  
ATOM   1192  O   ASP A 452     -32.603 -38.274  13.685  1.00103.44           O  
ANISOU 1192  O   ASP A 452    11313  12487  15502  -2293   2051  -2873       O  
ATOM   1193  CB  ASP A 452     -29.858 -38.790  13.695  1.00104.06           C  
ANISOU 1193  CB  ASP A 452    11236  12854  15447  -2532   1427  -2744       C  
ATOM   1194  CG  ASP A 452     -29.599 -37.412  13.094  1.00106.27           C  
ANISOU 1194  CG  ASP A 452    11427  12896  16053  -2491   1704  -2789       C  
ATOM   1195  OD1 ASP A 452     -29.868 -36.394  13.787  1.00110.32           O  
ANISOU 1195  OD1 ASP A 452    12096  13212  16606  -2718   1979  -3038       O  
ATOM   1196  OD2 ASP A 452     -29.123 -37.355  11.929  1.00103.87           O1-
ANISOU 1196  OD2 ASP A 452    10898  12593  15974  -2247   1670  -2581       O1-
ATOM   1197  N   SER A 453     -32.517 -37.393  15.780  1.00107.87           N  
ANISOU 1197  N   SER A 453    12290  12914  15779  -2926   2272  -3378       N  
ATOM   1198  CA  SER A 453     -33.864 -36.800  15.779  1.00108.02           C  
ANISOU 1198  CA  SER A 453    12359  12659  16022  -2809   2736  -3471       C  
ATOM   1199  C   SER A 453     -34.021 -35.662  14.763  1.00107.89           C  
ANISOU 1199  C   SER A 453    12124  12357  16512  -2577   3058  -3364       C  
ATOM   1200  O   SER A 453     -35.064 -35.540  14.121  1.00106.91           O  
ANISOU 1200  O   SER A 453    11858  12094  16668  -2295   3281  -3189       O  
ATOM   1201  CB  SER A 453     -34.216 -36.292  17.177  1.00111.81           C  
ANISOU 1201  CB  SER A 453    13167  13006  16307  -3225   3025  -3859       C  
ATOM   1202  OG  SER A 453     -33.643 -35.010  17.422  1.00115.19           O  
ANISOU 1202  OG  SER A 453    13661  13199  16907  -3478   3296  -4100       O  
ATOM   1203  N   GLN A 454     -32.981 -34.843  14.621  1.00108.75           N  
ANISOU 1203  N   GLN A 454    12182  12385  16750  -2708   3063  -3431       N  
ATOM   1204  CA  GLN A 454     -32.959 -33.763  13.639  1.00109.00           C  
ANISOU 1204  CA  GLN A 454    11980  12163  17272  -2501   3333  -3293       C  
ATOM   1205  C   GLN A 454     -33.191 -34.252  12.207  1.00105.16           C  
ANISOU 1205  C   GLN A 454    11198  11809  16949  -2084   3166  -2875       C  
ATOM   1206  O   GLN A 454     -33.573 -33.482  11.343  1.00105.59           O  
ANISOU 1206  O   GLN A 454    11036  11675  17405  -1877   3407  -2677       O  
ATOM   1207  CB  GLN A 454     -31.621 -33.012  13.697  1.00111.15           C  
ANISOU 1207  CB  GLN A 454    12238  12392  17600  -2716   3268  -3408       C  
ATOM   1208  CG  GLN A 454     -31.515 -31.907  14.760  1.00117.49           C  
ANISOU 1208  CG  GLN A 454    13269  12916  18456  -3120   3635  -3819       C  
ATOM   1209  CD  GLN A 454     -30.208 -31.093  14.646  1.00122.65           C  
ANISOU 1209  CD  GLN A 454    13862  13511  19229  -3308   3574  -3892       C  
ATOM   1210  OE1 GLN A 454     -29.339 -31.382  13.809  1.00122.08           O  
ANISOU 1210  OE1 GLN A 454    13573  13611  19201  -3129   3248  -3624       O  
ATOM   1211  NE2 GLN A 454     -30.071 -30.071  15.492  1.00127.29           N  
ANISOU 1211  NE2 GLN A 454    14646  13840  19879  -3689   3917  -4269       N  
ATOM   1212  N   ASN A 455     -32.940 -35.526  11.952  1.00101.76           N  
ANISOU 1212  N   ASN A 455    10753  11701  16208  -1990   2766  -2732       N  
ATOM   1213  CA  ASN A 455     -33.053 -36.058  10.605  1.00 98.63           C  
ANISOU 1213  CA  ASN A 455    10121  11459  15892  -1669   2608  -2388       C  
ATOM   1214  C   ASN A 455     -34.030 -37.220  10.503  1.00 96.78           C  
ANISOU 1214  C   ASN A 455     9913  11401  15457  -1526   2482  -2273       C  
ATOM   1215  O   ASN A 455     -34.248 -37.758   9.410  1.00 95.33           O  
ANISOU 1215  O   ASN A 455     9567  11369  15285  -1307   2358  -2011       O  
ATOM   1216  CB  ASN A 455     -31.686 -36.523  10.107  1.00 97.36           C  
ANISOU 1216  CB  ASN A 455     9871  11498  15621  -1668   2281  -2305       C  
ATOM   1217  CG  ASN A 455     -30.749 -35.381   9.818  1.00 97.41           C  
ANISOU 1217  CG  ASN A 455     9774  11346  15890  -1733   2394  -2321       C  
ATOM   1218  OD1 ASN A 455     -31.085 -34.453   9.089  1.00 97.09           O  
ANISOU 1218  OD1 ASN A 455     9577  11129  16183  -1595   2649  -2186       O  
ATOM   1219  ND2 ASN A 455     -29.555 -35.452  10.377  1.00 96.40           N  
ANISOU 1219  ND2 ASN A 455     9707  11283  15637  -1950   2190  -2449       N  
ATOM   1220  N   ARG A 456     -34.616 -37.601  11.637  1.00 96.93           N  
ANISOU 1220  N   ARG A 456    10146  11406  15276  -1680   2523  -2475       N  
ATOM   1221  CA  ARG A 456     -35.482 -38.770  11.728  1.00 94.44           C  
ANISOU 1221  CA  ARG A 456     9877  11255  14748  -1579   2387  -2397       C  
ATOM   1222  C   ARG A 456     -36.520 -38.889  10.590  1.00 92.79           C  
ANISOU 1222  C   ARG A 456     9466  11053  14735  -1294   2464  -2094       C  
ATOM   1223  O   ARG A 456     -36.721 -39.971  10.057  1.00 90.83           O  
ANISOU 1223  O   ARG A 456     9172  11029  14310  -1174   2229  -1948       O  
ATOM   1224  CB  ARG A 456     -36.131 -38.836  13.116  1.00 95.95           C  
ANISOU 1224  CB  ARG A 456    10322  11362  14772  -1794   2536  -2657       C  
ATOM   1225  CG  ARG A 456     -36.852 -40.151  13.412  1.00 95.20           C  
ANISOU 1225  CG  ARG A 456    10300  11458  14413  -1733   2351  -2602       C  
ATOM   1226  CD  ARG A 456     -37.465 -40.185  14.792  1.00 98.43           C  
ANISOU 1226  CD  ARG A 456    10970  11792  14638  -1968   2517  -2856       C  
ATOM   1227  NE  ARG A 456     -36.494 -40.493  15.846  1.00101.37           N  
ANISOU 1227  NE  ARG A 456    11539  12320  14656  -2302   2293  -3053       N  
ATOM   1228  CZ  ARG A 456     -36.234 -39.710  16.889  1.00104.72           C  
ANISOU 1228  CZ  ARG A 456    12184  12628  14975  -2654   2485  -3348       C  
ATOM   1229  NH1 ARG A 456     -36.872 -38.556  17.038  1.00107.85           N1+
ANISOU 1229  NH1 ARG A 456    12638  12697  15641  -2696   2966  -3519       N1+
ATOM   1230  NH2 ARG A 456     -35.338 -40.086  17.790  1.00106.22           N  
ANISOU 1230  NH2 ARG A 456    12529  13025  14803  -2991   2208  -3460       N  
ATOM   1231  N   LYS A 457     -37.161 -37.790  10.204  1.00 94.18           N  
ANISOU 1231  N   LYS A 457     9507  10987  15289  -1210   2789  -1978       N  
ATOM   1232  CA  LYS A 457     -38.173 -37.830   9.136  1.00 93.60           C  
ANISOU 1232  CA  LYS A 457     9206  10941  15417   -984   2834  -1617       C  
ATOM   1233  C   LYS A 457     -37.568 -38.173   7.757  1.00 91.98           C  
ANISOU 1233  C   LYS A 457     8823  10984  15142   -864   2579  -1357       C  
ATOM   1234  O   LYS A 457     -38.121 -38.998   7.033  1.00 90.78           O  
ANISOU 1234  O   LYS A 457     8597  11044  14848   -766   2410  -1152       O  
ATOM   1235  CB  LYS A 457     -39.018 -36.538   9.112  1.00 96.28           C  
ANISOU 1235  CB  LYS A 457     9392  10930  16258   -931   3263  -1494       C  
ATOM   1236  CG  LYS A 457     -40.037 -36.451   7.980  1.00 97.79           C  
ANISOU 1236  CG  LYS A 457     9288  11156  16712   -729   3287  -1028       C  
ATOM   1237  CD  LYS A 457     -40.644 -35.049   7.861  1.00104.67           C  
ANISOU 1237  CD  LYS A 457     9930  11646  18192   -669   3718   -835       C  
ATOM   1238  CE  LYS A 457     -41.887 -35.016   6.911  1.00109.13           C  
ANISOU 1238  CE  LYS A 457    10168  12242  19055   -497   3735   -297       C  
ATOM   1239  NZ  LYS A 457     -43.216 -35.557   7.464  1.00110.25           N1+
ANISOU 1239  NZ  LYS A 457    10329  12313  19245   -459   3832   -247       N1+
ATOM   1240  N   LYS A 458     -36.440 -37.551   7.400  1.00 92.19           N  
ANISOU 1240  N   LYS A 458     8791  10982  15253   -899   2569  -1381       N  
ATOM   1241  CA  LYS A 458     -35.733 -37.913   6.162  1.00 90.91           C  
ANISOU 1241  CA  LYS A 458     8496  11051  14992   -819   2359  -1185       C  
ATOM   1242  C   LYS A 458     -35.276 -39.368   6.179  1.00 88.13           C  
ANISOU 1242  C   LYS A 458     8266  10961  14257   -841   2059  -1291       C  
ATOM   1243  O   LYS A 458     -35.394 -40.069   5.182  1.00 87.40           O  
ANISOU 1243  O   LYS A 458     8100  11081  14025   -771   1928  -1121       O  
ATOM   1244  CB  LYS A 458     -34.534 -36.993   5.883  1.00 92.11           C  
ANISOU 1244  CB  LYS A 458     8570  11103  15323   -859   2419  -1211       C  
ATOM   1245  CG  LYS A 458     -34.915 -35.601   5.356  1.00 96.43           C  
ANISOU 1245  CG  LYS A 458     8904  11427  16306   -791   2705   -985       C  
ATOM   1246  CD  LYS A 458     -33.774 -34.920   4.596  1.00 99.33           C  
ANISOU 1246  CD  LYS A 458     9136  11791  16814   -783   2702   -894       C  
ATOM   1247  CE  LYS A 458     -33.537 -35.617   3.225  1.00101.10           C  
ANISOU 1247  CE  LYS A 458     9248  12336  16828   -701   2489   -630       C  
ATOM   1248  NZ  LYS A 458     -32.216 -35.307   2.529  1.00101.56           N1+
ANISOU 1248  NZ  LYS A 458     9225  12445  16917   -711   2443   -599       N1+
ATOM   1249  N   LEU A 459     -34.756 -39.819   7.313  1.00 87.04           N  
ANISOU 1249  N   LEU A 459     8306  10804  13958   -966   1965  -1560       N  
ATOM   1250  CA  LEU A 459     -34.306 -41.186   7.438  1.00 85.17           C  
ANISOU 1250  CA  LEU A 459     8147  10769  13442   -985   1704  -1629       C  
ATOM   1251  C   LEU A 459     -35.458 -42.173   7.262  1.00 84.06           C  
ANISOU 1251  C   LEU A 459     8035  10758  13146   -905   1645  -1547       C  
ATOM   1252  O   LEU A 459     -35.274 -43.277   6.762  1.00 82.83           O  
ANISOU 1252  O   LEU A 459     7870  10778  12822   -868   1482  -1514       O  
ATOM   1253  CB  LEU A 459     -33.581 -41.399   8.773  1.00 85.50           C  
ANISOU 1253  CB  LEU A 459     8344  10777  13365  -1169   1594  -1864       C  
ATOM   1254  CG  LEU A 459     -32.142 -40.854   8.822  1.00 86.95           C  
ANISOU 1254  CG  LEU A 459     8477  10915  13643  -1274   1533  -1917       C  
ATOM   1255  CD1 LEU A 459     -31.639 -40.687  10.243  1.00 88.75           C  
ANISOU 1255  CD1 LEU A 459     8862  11096  13763  -1534   1460  -2127       C  
ATOM   1256  CD2 LEU A 459     -31.166 -41.708   8.017  1.00 85.77           C  
ANISOU 1256  CD2 LEU A 459     8205  10912  13471  -1196   1348  -1805       C  
ATOM   1257  N   SER A 460     -36.656 -41.760   7.650  1.00 85.19           N  
ANISOU 1257  N   SER A 460     8199  10788  13379   -884   1808  -1513       N  
ATOM   1258  CA  SER A 460     -37.807 -42.646   7.638  1.00 84.64           C  
ANISOU 1258  CA  SER A 460     8156  10819  13184   -825   1755  -1436       C  
ATOM   1259  C   SER A 460     -38.335 -42.859   6.216  1.00 84.84           C  
ANISOU 1259  C   SER A 460     8016  11007  13211   -728   1708  -1151       C  
ATOM   1260  O   SER A 460     -38.962 -43.874   5.928  1.00 84.37           O  
ANISOU 1260  O   SER A 460     7974  11107  12975   -708   1585  -1094       O  
ATOM   1261  CB  SER A 460     -38.897 -42.089   8.530  1.00 85.54           C  
ANISOU 1261  CB  SER A 460     8328  10732  13442   -842   1978  -1477       C  
ATOM   1262  OG  SER A 460     -39.546 -41.024   7.875  1.00 86.91           O  
ANISOU 1262  OG  SER A 460     8317  10764  13941   -758   2197  -1243       O  
ATOM   1263  N   GLU A 461     -38.067 -41.911   5.325  1.00 86.20           N  
ANISOU 1263  N   GLU A 461     8029  11153  13567   -698   1799   -966       N  
ATOM   1264  CA  GLU A 461     -38.477 -42.037   3.934  1.00 86.85           C  
ANISOU 1264  CA  GLU A 461     7959  11437  13603   -670   1736   -668       C  
ATOM   1265  C   GLU A 461     -37.534 -42.915   3.138  1.00 85.41           C  
ANISOU 1265  C   GLU A 461     7818  11473  13158   -717   1578   -740       C  
ATOM   1266  O   GLU A 461     -37.762 -43.165   1.955  1.00 86.37           O  
ANISOU 1266  O   GLU A 461     7862  11803  13149   -756   1523   -546       O  
ATOM   1267  CB  GLU A 461     -38.578 -40.666   3.281  1.00 89.09           C  
ANISOU 1267  CB  GLU A 461     8033  11618  14198   -637   1898   -391       C  
ATOM   1268  CG  GLU A 461     -39.915 -40.001   3.501  1.00 94.48           C  
ANISOU 1268  CG  GLU A 461     8576  12142  15180   -582   2064   -149       C  
ATOM   1269  CD  GLU A 461     -39.932 -38.534   3.086  1.00102.27           C  
ANISOU 1269  CD  GLU A 461     9327  12935  16593   -538   2281    117       C  
ATOM   1270  OE1 GLU A 461     -38.875 -38.015   2.625  1.00103.16           O  
ANISOU 1270  OE1 GLU A 461     9404  13056  16737   -554   2289     99       O  
ATOM   1271  OE2 GLU A 461     -41.015 -37.899   3.231  1.00106.43           O1-
ANISOU 1271  OE2 GLU A 461     9684  13280  17472   -482   2465    365       O1-
ATOM   1272  N   LEU A 462     -36.465 -43.377   3.774  1.00 83.77           N  
ANISOU 1272  N   LEU A 462     7726  11216  12886   -739   1521  -1004       N  
ATOM   1273  CA  LEU A 462     -35.508 -44.216   3.080  1.00 82.56           C  
ANISOU 1273  CA  LEU A 462     7590  11203  12574   -772   1435  -1079       C  
ATOM   1274  C   LEU A 462     -35.785 -45.662   3.393  1.00 81.57           C  
ANISOU 1274  C   LEU A 462     7573  11169  12250   -790   1321  -1212       C  
ATOM   1275  O   LEU A 462     -35.290 -46.543   2.691  1.00 81.72           O  
ANISOU 1275  O   LEU A 462     7604  11300  12145   -826   1297  -1266       O  
ATOM   1276  CB  LEU A 462     -34.077 -43.846   3.452  1.00 82.47           C  
ANISOU 1276  CB  LEU A 462     7571  11069  12693   -783   1446  -1214       C  
ATOM   1277  CG  LEU A 462     -33.623 -42.514   2.857  1.00 83.03           C  
ANISOU 1277  CG  LEU A 462     7515  11067  12962   -770   1570  -1076       C  
ATOM   1278  CD1 LEU A 462     -32.374 -42.054   3.558  1.00 82.01           C  
ANISOU 1278  CD1 LEU A 462     7390  10781  12989   -801   1568  -1225       C  
ATOM   1279  CD2 LEU A 462     -33.411 -42.603   1.334  1.00 82.85           C  
ANISOU 1279  CD2 LEU A 462     7404  11228  12844   -787   1602   -907       C  
ATOM   1280  N   LEU A 463     -36.590 -45.894   4.440  1.00 80.77           N  
ANISOU 1280  N   LEU A 463     7549  11000  12139   -773   1286  -1270       N  
ATOM   1281  CA  LEU A 463     -36.946 -47.240   4.908  1.00 79.20           C  
ANISOU 1281  CA  LEU A 463     7444  10864  11785   -782   1179  -1381       C  
ATOM   1282  C   LEU A 463     -37.835 -47.986   3.930  1.00 79.05           C  
ANISOU 1282  C   LEU A 463     7412  11024  11596   -807   1152  -1280       C  
ATOM   1283  O   LEU A 463     -38.732 -47.406   3.307  1.00 79.67           O  
ANISOU 1283  O   LEU A 463     7418  11176  11675   -817   1184  -1073       O  
ATOM   1284  CB  LEU A 463     -37.654 -47.175   6.253  1.00 78.80           C  
ANISOU 1284  CB  LEU A 463     7482  10703  11756   -776   1171  -1448       C  
ATOM   1285  CG  LEU A 463     -36.853 -46.786   7.497  1.00 79.66           C  
ANISOU 1285  CG  LEU A 463     7664  10676  11927   -836   1156  -1602       C  
ATOM   1286  CD1 LEU A 463     -37.810 -46.527   8.690  1.00 78.97           C  
ANISOU 1286  CD1 LEU A 463     7690  10488  11827   -872   1222  -1665       C  
ATOM   1287  CD2 LEU A 463     -35.782 -47.826   7.849  1.00 78.60           C  
ANISOU 1287  CD2 LEU A 463     7541  10586  11738   -878    999  -1696       C  
ATOM   1288  N   ARG A 464     -37.571 -49.282   3.825  1.00 78.43           N  
ANISOU 1288  N   ARG A 464     7390  11010  11399   -838   1096  -1410       N  
ATOM   1289  CA  ARG A 464     -38.287 -50.207   2.958  1.00 78.69           C  
ANISOU 1289  CA  ARG A 464     7446  11212  11238   -914   1078  -1386       C  
ATOM   1290  C   ARG A 464     -38.603 -51.440   3.796  1.00 77.61           C  
ANISOU 1290  C   ARG A 464     7383  11031  11072   -892   1009  -1522       C  
ATOM   1291  O   ARG A 464     -37.791 -51.860   4.632  1.00 77.73           O  
ANISOU 1291  O   ARG A 464     7410  10924  11197   -849    984  -1642       O  
ATOM   1292  CB  ARG A 464     -37.383 -50.616   1.782  1.00 80.06           C  
ANISOU 1292  CB  ARG A 464     7616  11473  11328  -1008   1165  -1461       C  
ATOM   1293  CG  ARG A 464     -37.568 -49.858   0.468  1.00 82.17           C  
ANISOU 1293  CG  ARG A 464     7833  11917  11468  -1117   1215  -1283       C  
ATOM   1294  CD  ARG A 464     -37.861 -48.408   0.692  1.00 83.52           C  
ANISOU 1294  CD  ARG A 464     7899  12036  11798  -1040   1204  -1060       C  
ATOM   1295  NE  ARG A 464     -37.658 -47.599  -0.493  1.00 86.22           N  
ANISOU 1295  NE  ARG A 464     8156  12515  12088  -1128   1257   -867       N  
ATOM   1296  CZ  ARG A 464     -37.643 -46.272  -0.478  1.00 87.65           C  
ANISOU 1296  CZ  ARG A 464     8211  12623  12467  -1063   1294   -663       C  
ATOM   1297  NH1 ARG A 464     -37.810 -45.621   0.667  1.00 85.02           N1+
ANISOU 1297  NH1 ARG A 464     7851  12067  12385   -928   1314   -676       N1+
ATOM   1298  NH2 ARG A 464     -37.447 -45.595  -1.607  1.00 90.89           N  
ANISOU 1298  NH2 ARG A 464     8528  13179  12827  -1156   1333   -452       N  
ATOM   1299  N   TYR A 465     -39.769 -52.032   3.586  1.00 77.08           N  
ANISOU 1299  N   TYR A 465     7344  11069  10873   -935    965  -1469       N  
ATOM   1300  CA  TYR A 465     -40.179 -53.201   4.378  1.00 75.56           C  
ANISOU 1300  CA  TYR A 465     7210  10831  10667   -910    905  -1576       C  
ATOM   1301  C   TYR A 465     -41.065 -54.187   3.589  1.00 75.99           C  
ANISOU 1301  C   TYR A 465     7295  11033  10543  -1022    889  -1580       C  
ATOM   1302  O   TYR A 465     -41.777 -53.799   2.655  1.00 77.05           O  
ANISOU 1302  O   TYR A 465     7404  11333  10537  -1127    873  -1431       O  
ATOM   1303  CB  TYR A 465     -41.002 -52.749   5.559  1.00 74.33           C  
ANISOU 1303  CB  TYR A 465     7072  10590  10580   -829    857  -1503       C  
ATOM   1304  CG  TYR A 465     -40.337 -51.961   6.669  1.00 73.08           C  
ANISOU 1304  CG  TYR A 465     6933  10282  10552   -775    870  -1548       C  
ATOM   1305  CD1 TYR A 465     -40.433 -50.563   6.718  1.00 72.37           C  
ANISOU 1305  CD1 TYR A 465     6811  10126  10559   -757    953  -1458       C  
ATOM   1306  CD2 TYR A 465     -39.722 -52.622   7.737  1.00 71.17           C  
ANISOU 1306  CD2 TYR A 465     6735   9964  10340   -772    799  -1661       C  
ATOM   1307  CE1 TYR A 465     -39.891 -49.838   7.787  1.00 72.73           C  
ANISOU 1307  CE1 TYR A 465     6905  10031  10696   -761    987  -1541       C  
ATOM   1308  CE2 TYR A 465     -39.186 -51.928   8.797  1.00 71.63           C  
ANISOU 1308  CE2 TYR A 465     6832   9928  10454   -794    785  -1699       C  
ATOM   1309  CZ  TYR A 465     -39.269 -50.533   8.832  1.00 73.84           C  
ANISOU 1309  CZ  TYR A 465     7118  10141  10796   -801    889  -1669       C  
ATOM   1310  OH  TYR A 465     -38.723 -49.859   9.921  1.00 75.61           O  
ANISOU 1310  OH  TYR A 465     7411  10270  11047   -877    895  -1752       O  
ATOM   1311  N   TYR A 466     -41.020 -55.462   3.971  1.00 75.11           N  
ANISOU 1311  N   TYR A 466     7224  10866  10446  -1023    887  -1729       N  
ATOM   1312  CA  TYR A 466     -41.974 -56.459   3.487  1.00 74.41           C  
ANISOU 1312  CA  TYR A 466     7176  10884  10211  -1134    869  -1758       C  
ATOM   1313  C   TYR A 466     -43.292 -56.225   4.225  1.00 73.01           C  
ANISOU 1313  C   TYR A 466     6985  10719  10033  -1070    755  -1593       C  
ATOM   1314  O   TYR A 466     -43.286 -56.008   5.433  1.00 71.46           O  
ANISOU 1314  O   TYR A 466     6790  10389   9970   -936    726  -1582       O  
ATOM   1315  CB  TYR A 466     -41.474 -57.873   3.787  1.00 74.23           C  
ANISOU 1315  CB  TYR A 466     7175  10739  10289  -1133    939  -1961       C  
ATOM   1316  CG  TYR A 466     -40.331 -58.350   2.940  1.00 76.73           C  
ANISOU 1316  CG  TYR A 466     7495  11007  10652  -1220   1123  -2140       C  
ATOM   1317  CD1 TYR A 466     -40.437 -58.398   1.555  1.00 80.79           C  
ANISOU 1317  CD1 TYR A 466     8075  11680  10941  -1433   1233  -2213       C  
ATOM   1318  CD2 TYR A 466     -39.141 -58.794   3.522  1.00 79.29           C  
ANISOU 1318  CD2 TYR A 466     7745  11123  11256  -1117   1202  -2222       C  
ATOM   1319  CE1 TYR A 466     -39.387 -58.852   0.767  1.00 83.63           C  
ANISOU 1319  CE1 TYR A 466     8456  11968  11349  -1535   1469  -2412       C  
ATOM   1320  CE2 TYR A 466     -38.073 -59.256   2.740  1.00 81.02           C  
ANISOU 1320  CE2 TYR A 466     7941  11247  11596  -1187   1428  -2378       C  
ATOM   1321  CZ  TYR A 466     -38.208 -59.277   1.364  1.00 84.22           C  
ANISOU 1321  CZ  TYR A 466     8442  11789  11769  -1392   1586  -2498       C  
ATOM   1322  OH  TYR A 466     -37.177 -59.731   0.567  1.00 88.58           O  
ANISOU 1322  OH  TYR A 466     8993  12227  12435  -1485   1872  -2685       O  
ATOM   1323  N   THR A 467     -44.411 -56.240   3.503  1.00 73.22           N  
ANISOU 1323  N   THR A 467     6995  10912   9912  -1189    697  -1452       N  
ATOM   1324  CA  THR A 467     -45.705 -56.048   4.128  1.00 72.62           C  
ANISOU 1324  CA  THR A 467     6874  10828   9889  -1127    614  -1266       C  
ATOM   1325  C   THR A 467     -46.694 -57.059   3.593  1.00 73.89           C  
ANISOU 1325  C   THR A 467     7046  11127   9901  -1278    540  -1246       C  
ATOM   1326  O   THR A 467     -46.465 -57.662   2.565  1.00 75.45           O  
ANISOU 1326  O   THR A 467     7293  11463   9910  -1476    556  -1354       O  
ATOM   1327  CB  THR A 467     -46.311 -54.657   3.863  1.00 72.97           C  
ANISOU 1327  CB  THR A 467     6804  10915  10004  -1109    601   -968       C  
ATOM   1328  OG1 THR A 467     -46.998 -54.677   2.616  1.00 73.93           O  
ANISOU 1328  OG1 THR A 467     6861  11277   9952  -1310    514   -772       O  
ATOM   1329  CG2 THR A 467     -45.273 -53.560   3.854  1.00 72.89           C  
ANISOU 1329  CG2 THR A 467     6775  10826  10093  -1040    688   -979       C  
ATOM   1330  N   SER A 468     -47.832 -57.195   4.268  1.00 73.95           N  
ANISOU 1330  N   SER A 468     7012  11095   9988  -1212    475  -1108       N  
ATOM   1331  CA  SER A 468     -48.840 -58.157   3.878  1.00 74.48           C  
ANISOU 1331  CA  SER A 468     7077  11281   9941  -1355    388  -1073       C  
ATOM   1332  C   SER A 468     -49.388 -57.849   2.505  1.00 76.85           C  
ANISOU 1332  C   SER A 468     7317  11849  10033  -1609    291   -871       C  
ATOM   1333  O   SER A 468     -50.169 -58.623   1.965  1.00 78.92           O  
ANISOU 1333  O   SER A 468     7584  12262  10139  -1809    198   -841       O  
ATOM   1334  CB  SER A 468     -49.959 -58.183   4.898  1.00 73.33           C  
ANISOU 1334  CB  SER A 468     6873  11028   9961  -1219    351   -919       C  
ATOM   1335  OG  SER A 468     -50.669 -56.980   4.856  1.00 73.76           O  
ANISOU 1335  OG  SER A 468     6794  11089  10142  -1173    340   -603       O  
ATOM   1336  N   ALA A 469     -48.986 -56.731   1.924  1.00 77.46           N  
ANISOU 1336  N   ALA A 469     7331  12003  10097  -1633    300   -714       N  
ATOM   1337  CA  ALA A 469     -49.507 -56.389   0.607  1.00 80.16           C  
ANISOU 1337  CA  ALA A 469     7595  12640  10220  -1911    177   -455       C  
ATOM   1338  C   ALA A 469     -48.498 -56.609  -0.508  1.00 81.48           C  
ANISOU 1338  C   ALA A 469     7884  12971  10101  -2142    243   -662       C  
ATOM   1339  O   ALA A 469     -48.881 -56.745  -1.677  1.00 83.84           O  
ANISOU 1339  O   ALA A 469     8190  13566  10098  -2476    144   -545       O  
ATOM   1340  CB  ALA A 469     -49.999 -54.972   0.586  1.00 80.96           C  
ANISOU 1340  CB  ALA A 469     7491  12743  10525  -1823    133    -35       C  
ATOM   1341  N   SER A 470     -47.227 -56.695  -0.131  1.00 80.14           N  
ANISOU 1341  N   SER A 470     7813  12614  10021  -1993    414   -964       N  
ATOM   1342  CA  SER A 470     -46.132 -56.432  -1.050  1.00 81.65           C  
ANISOU 1342  CA  SER A 470     8071  12894  10056  -2127    526  -1091       C  
ATOM   1343  C   SER A 470     -45.497 -57.627  -1.749  1.00 83.65           C  
ANISOU 1343  C   SER A 470     8498  13189  10094  -2357    679  -1464       C  
ATOM   1344  O   SER A 470     -44.737 -57.435  -2.681  1.00 85.24           O  
ANISOU 1344  O   SER A 470     8766  13498  10121  -2532    794  -1557       O  
ATOM   1345  CB  SER A 470     -45.053 -55.613  -0.347  1.00 79.83           C  
ANISOU 1345  CB  SER A 470     7807  12433  10090  -1850    634  -1145       C  
ATOM   1346  OG  SER A 470     -44.353 -56.379   0.619  1.00 77.81           O  
ANISOU 1346  OG  SER A 470     7620  11928  10014  -1672    736  -1433       O  
ATOM   1347  N   GLY A 471     -45.795 -58.844  -1.310  1.00 84.39           N  
ANISOU 1347  N   GLY A 471     8663  13176  10225  -2362    718  -1681       N  
ATOM   1348  CA  GLY A 471     -45.218 -60.043  -1.923  1.00 87.81           C  
ANISOU 1348  CA  GLY A 471     9251  13582  10530  -2580    933  -2062       C  
ATOM   1349  C   GLY A 471     -43.778 -60.318  -1.531  1.00 88.43           C  
ANISOU 1349  C   GLY A 471     9349  13374  10876  -2393   1181  -2332       C  
ATOM   1350  O   GLY A 471     -43.449 -60.423  -0.355  1.00 85.96           O  
ANISOU 1350  O   GLY A 471     8958  12814  10887  -2090   1173  -2335       O  
ATOM   1351  N   ASP A 472     -42.916 -60.438  -2.536  1.00 92.63           N  
ANISOU 1351  N   ASP A 472     9978  13946  11269  -2601   1407  -2539       N  
ATOM   1352  CA  ASP A 472     -41.473 -60.620  -2.311  1.00 94.27           C  
ANISOU 1352  CA  ASP A 472    10170  13877  11771  -2441   1667  -2753       C  
ATOM   1353  C   ASP A 472     -40.666 -59.344  -2.527  1.00 93.85           C  
ANISOU 1353  C   ASP A 472    10056  13860  11742  -2342   1657  -2600       C  
ATOM   1354  O   ASP A 472     -39.443 -59.353  -2.408  1.00 94.45           O  
ANISOU 1354  O   ASP A 472    10096  13725  12063  -2222   1854  -2730       O  
ATOM   1355  CB  ASP A 472     -40.921 -61.764  -3.175  1.00 97.76           C  
ANISOU 1355  CB  ASP A 472    10750  14235  12159  -2710   2029  -3142       C  
ATOM   1356  CG  ASP A 472     -41.371 -63.145  -2.671  1.00101.79           C  
ANISOU 1356  CG  ASP A 472    11275  14560  12839  -2712   2116  -3335       C  
ATOM   1357  OD1 ASP A 472     -41.916 -63.938  -3.493  1.00106.79           O  
ANISOU 1357  OD1 ASP A 472    12059  15309  13205  -3065   2244  -3552       O  
ATOM   1358  OD2 ASP A 472     -41.210 -63.424  -1.444  1.00102.66           O1-
ANISOU 1358  OD2 ASP A 472    11246  14425  13334  -2388   2046  -3258       O1-
ATOM   1359  N   GLU A 473     -41.352 -58.256  -2.851  1.00 93.76           N  
ANISOU 1359  N   GLU A 473    10006  14101  11516  -2397   1435  -2298       N  
ATOM   1360  CA  GLU A 473     -40.720 -56.963  -2.989  1.00 93.34           C  
ANISOU 1360  CA  GLU A 473     9871  14075  11518  -2289   1409  -2111       C  
ATOM   1361  C   GLU A 473     -40.905 -56.294  -1.647  1.00 90.10           C  
ANISOU 1361  C   GLU A 473     9327  13495  11412  -1947   1236  -1919       C  
ATOM   1362  O   GLU A 473     -41.849 -56.645  -0.934  1.00 89.05           O  
ANISOU 1362  O   GLU A 473     9174  13341  11319  -1874   1098  -1848       O  
ATOM   1363  CB  GLU A 473     -41.401 -56.150  -4.090  1.00 95.49           C  
ANISOU 1363  CB  GLU A 473    10142  14704  11434  -2555   1278  -1844       C  
ATOM   1364  CG  GLU A 473     -40.465 -55.199  -4.818  1.00 98.60           C  
ANISOU 1364  CG  GLU A 473    10514  15163  11784  -2597   1383  -1776       C  
ATOM   1365  CD  GLU A 473     -39.700 -55.869  -5.975  1.00104.86           C  
ANISOU 1365  CD  GLU A 473    11480  16036  12325  -2913   1670  -2082       C  
ATOM   1366  OE1 GLU A 473     -38.777 -55.212  -6.535  1.00106.29           O  
ANISOU 1366  OE1 GLU A 473    11654  16229  12501  -2935   1810  -2074       O  
ATOM   1367  OE2 GLU A 473     -40.025 -57.039  -6.327  1.00106.63           O1-
ANISOU 1367  OE2 GLU A 473    11851  16298  12364  -3152   1786  -2343       O1-
ATOM   1368  N   MET A 474     -40.000 -55.367  -1.301  1.00 88.63           N  
ANISOU 1368  N   MET A 474     9062  13183  11428  -1766   1266  -1855       N  
ATOM   1369  CA  MET A 474     -40.105 -54.532  -0.093  1.00 86.14           C  
ANISOU 1369  CA  MET A 474     8647  12722  11361  -1504   1135  -1692       C  
ATOM   1370  C   MET A 474     -40.559 -53.144  -0.478  1.00 86.08           C  
ANISOU 1370  C   MET A 474     8549  12845  11311  -1512   1048  -1391       C  
ATOM   1371  O   MET A 474     -40.020 -52.562  -1.424  1.00 87.58           O  
ANISOU 1371  O   MET A 474     8723  13146  11407  -1620   1117  -1332       O  
ATOM   1372  CB  MET A 474     -38.760 -54.374   0.600  1.00 85.60           C  
ANISOU 1372  CB  MET A 474     8538  12418  11566  -1331   1221  -1813       C  
ATOM   1373  CG  MET A 474     -38.151 -55.633   1.165  1.00 86.44           C  
ANISOU 1373  CG  MET A 474     8659  12340  11842  -1280   1305  -2031       C  
ATOM   1374  SD  MET A 474     -36.892 -55.168   2.374  1.00 87.23           S  
ANISOU 1374  SD  MET A 474     8655  12202  12286  -1074   1272  -2012       S  
ATOM   1375  CE  MET A 474     -35.980 -56.712   2.488  1.00 90.00           C  
ANISOU 1375  CE  MET A 474     8958  12355  12883  -1071   1434  -2201       C  
ATOM   1376  N   VAL A 475     -41.522 -52.598   0.262  1.00 84.50           N  
ANISOU 1376  N   VAL A 475     8276  12609  11220  -1397    927  -1188       N  
ATOM   1377  CA  VAL A 475     -42.120 -51.300  -0.099  1.00 84.64           C  
ANISOU 1377  CA  VAL A 475     8160  12714  11284  -1400    872   -847       C  
ATOM   1378  C   VAL A 475     -41.786 -50.164   0.887  1.00 83.18           C  
ANISOU 1378  C   VAL A 475     7898  12293  11413  -1182    925   -789       C  
ATOM   1379  O   VAL A 475     -41.314 -50.423   2.000  1.00 82.04           O  
ANISOU 1379  O   VAL A 475     7819  11950  11400  -1049    954   -993       O  
ATOM   1380  CB  VAL A 475     -43.652 -51.425  -0.382  1.00 85.83           C  
ANISOU 1380  CB  VAL A 475     8240  13035  11336  -1509    733   -576       C  
ATOM   1381  CG1 VAL A 475     -43.901 -52.260  -1.661  1.00 87.74           C  
ANISOU 1381  CG1 VAL A 475     8556  13580  11201  -1826    677   -593       C  
ATOM   1382  CG2 VAL A 475     -44.413 -52.005   0.809  1.00 83.34           C  
ANISOU 1382  CG2 VAL A 475     7950  12563  11151  -1368    694   -645       C  
ATOM   1383  N   SER A 476     -41.991 -48.912   0.467  1.00 83.52           N  
ANISOU 1383  N   SER A 476     7800  12358  11575  -1174    945   -506       N  
ATOM   1384  CA  SER A 476     -41.758 -47.751   1.348  1.00 82.23           C  
ANISOU 1384  CA  SER A 476     7564  11945  11731  -1002   1044   -463       C  
ATOM   1385  C   SER A 476     -42.983 -47.411   2.220  1.00 82.07           C  
ANISOU 1385  C   SER A 476     7478  11785  11918   -906   1064   -315       C  
ATOM   1386  O   SER A 476     -44.106 -47.883   1.965  1.00 82.59           O  
ANISOU 1386  O   SER A 476     7496  11972  11912   -965    975   -141       O  
ATOM   1387  CB  SER A 476     -41.340 -46.528   0.536  1.00 83.53           C  
ANISOU 1387  CB  SER A 476     7586  12142  12008  -1024   1108   -233       C  
ATOM   1388  OG  SER A 476     -42.428 -46.012  -0.203  1.00 84.50           O  
ANISOU 1388  OG  SER A 476     7530  12410  12164  -1102   1052    176       O  
ATOM   1389  N   LEU A 477     -42.768 -46.595   3.250  1.00 81.26           N  
ANISOU 1389  N   LEU A 477     7379  11420  12076   -782   1203   -393       N  
ATOM   1390  CA  LEU A 477     -43.879 -46.141   4.096  1.00 80.81           C  
ANISOU 1390  CA  LEU A 477     7263  11177  12263   -700   1310   -277       C  
ATOM   1391  C   LEU A 477     -44.866 -45.291   3.292  1.00 82.80           C  
ANISOU 1391  C   LEU A 477     7260  11461  12738   -708   1347    174       C  
ATOM   1392  O   LEU A 477     -46.074 -45.386   3.495  1.00 83.34           O  
ANISOU 1392  O   LEU A 477     7232  11495  12938   -686   1357    377       O  
ATOM   1393  CB  LEU A 477     -43.378 -45.392   5.343  1.00 80.20           C  
ANISOU 1393  CB  LEU A 477     7273  10807  12390   -628   1500   -500       C  
ATOM   1394  CG  LEU A 477     -42.676 -46.215   6.426  1.00 77.59           C  
ANISOU 1394  CG  LEU A 477     7166  10440  11875   -646   1443   -866       C  
ATOM   1395  CD1 LEU A 477     -42.473 -45.416   7.686  1.00 77.65           C  
ANISOU 1395  CD1 LEU A 477     7267  10191  12043   -649   1632  -1046       C  
ATOM   1396  CD2 LEU A 477     -43.482 -47.435   6.756  1.00 76.74           C  
ANISOU 1396  CD2 LEU A 477     7130  10423  11603   -648   1331   -899       C  
ATOM   1397  N   LYS A 478     -44.350 -44.479   2.366  1.00 84.16           N  
ANISOU 1397  N   LYS A 478     7297  11703  12974   -746   1360    369       N  
ATOM   1398  CA  LYS A 478     -45.206 -43.666   1.493  1.00 86.87           C  
ANISOU 1398  CA  LYS A 478     7351  12113  13542   -779   1360    882       C  
ATOM   1399  C   LYS A 478     -46.256 -44.554   0.813  1.00 87.13           C  
ANISOU 1399  C   LYS A 478     7321  12433  13349   -916   1136   1131       C  
ATOM   1400  O   LYS A 478     -47.456 -44.272   0.893  1.00 88.45           O  
ANISOU 1400  O   LYS A 478     7286  12541  13778   -892   1151   1481       O  
ATOM   1401  CB  LYS A 478     -44.378 -42.829   0.484  1.00 88.30           C  
ANISOU 1401  CB  LYS A 478     7411  12392  13744   -836   1366   1061       C  
ATOM   1402  CG  LYS A 478     -45.146 -42.384  -0.784  1.00 93.03           C  
ANISOU 1402  CG  LYS A 478     7721  13235  14388   -968   1241   1643       C  
ATOM   1403  CD  LYS A 478     -44.209 -41.893  -1.903  1.00 98.10           C  
ANISOU 1403  CD  LYS A 478     8309  14076  14887  -1081   1197   1768       C  
ATOM   1404  CE  LYS A 478     -44.128 -40.357  -2.018  1.00101.91           C  
ANISOU 1404  CE  LYS A 478     8510  14340  15871   -977   1382   2114       C  
ATOM   1405  NZ  LYS A 478     -43.451 -39.709  -0.853  1.00101.52           N1+
ANISOU 1405  NZ  LYS A 478     8553  13870  16151   -778   1656   1755       N1+
ATOM   1406  N   ASP A 479     -45.796 -45.642   0.196  1.00 85.95           N  
ANISOU 1406  N   ASP A 479     7345  12567  12743  -1072    956    934       N  
ATOM   1407  CA  ASP A 479     -46.678 -46.566  -0.505  1.00 86.66           C  
ANISOU 1407  CA  ASP A 479     7419  12956  12551  -1264    742   1104       C  
ATOM   1408  C   ASP A 479     -47.691 -47.219   0.382  1.00 85.20           C  
ANISOU 1408  C   ASP A 479     7261  12655  12455  -1186    728   1059       C  
ATOM   1409  O   ASP A 479     -48.838 -47.393  -0.039  1.00 86.92           O  
ANISOU 1409  O   ASP A 479     7318  13019  12685  -1293    594   1413       O  
ATOM   1410  CB  ASP A 479     -45.903 -47.630  -1.264  1.00 86.68           C  
ANISOU 1410  CB  ASP A 479     7638  13225  12068  -1463    634    813       C  
ATOM   1411  CG  ASP A 479     -45.899 -47.367  -2.757  1.00 92.02           C  
ANISOU 1411  CG  ASP A 479     8214  14254  12492  -1738    509   1127       C  
ATOM   1412  OD1 ASP A 479     -46.789 -47.937  -3.454  1.00 94.26           O  
ANISOU 1412  OD1 ASP A 479     8458  14826  12528  -1983    321   1346       O  
ATOM   1413  OD2 ASP A 479     -45.034 -46.553  -3.213  1.00 94.66           O1-
ANISOU 1413  OD2 ASP A 479     8503  14586  12877  -1729    593   1177       O1-
ATOM   1414  N   TYR A 480     -47.266 -47.598   1.592  1.00 82.12           N  
ANISOU 1414  N   TYR A 480     7063  12024  12115  -1025    851    653       N  
ATOM   1415  CA  TYR A 480     -48.173 -48.118   2.605  1.00 80.40           C  
ANISOU 1415  CA  TYR A 480     6881  11655  12012   -930    884    592       C  
ATOM   1416  C   TYR A 480     -49.325 -47.135   2.745  1.00 83.01           C  
ANISOU 1416  C   TYR A 480     6939  11826  12772   -852    993   1025       C  
ATOM   1417  O   TYR A 480     -50.506 -47.522   2.723  1.00 83.97           O  
ANISOU 1417  O   TYR A 480     6943  11996  12966   -884    914   1272       O  
ATOM   1418  CB  TYR A 480     -47.462 -48.286   3.949  1.00 77.78           C  
ANISOU 1418  CB  TYR A 480     6760  11071  11722   -786   1031    165       C  
ATOM   1419  CG  TYR A 480     -48.355 -48.828   5.040  1.00 75.58           C  
ANISOU 1419  CG  TYR A 480     6539  10645  11530   -706   1083     91       C  
ATOM   1420  CD1 TYR A 480     -49.221 -47.994   5.746  1.00 74.96           C  
ANISOU 1420  CD1 TYR A 480     6343  10312  11826   -600   1292    262       C  
ATOM   1421  CD2 TYR A 480     -48.362 -50.183   5.343  1.00 73.55           C  
ANISOU 1421  CD2 TYR A 480     6442  10487  11014   -744    954   -139       C  
ATOM   1422  CE1 TYR A 480     -50.069 -48.495   6.727  1.00 73.46           C  
ANISOU 1422  CE1 TYR A 480     6212   9987  11711   -540   1368    196       C  
ATOM   1423  CE2 TYR A 480     -49.205 -50.696   6.330  1.00 72.40           C  
ANISOU 1423  CE2 TYR A 480     6344  10220  10944   -676   1000   -184       C  
ATOM   1424  CZ  TYR A 480     -50.056 -49.846   7.017  1.00 71.86           C  
ANISOU 1424  CZ  TYR A 480     6174   9917  11210   -578   1204    -20       C  
ATOM   1425  OH  TYR A 480     -50.875 -50.365   7.995  1.00 69.40           O  
ANISOU 1425  OH  TYR A 480     5922   9482  10964   -523   1277    -76       O  
ATOM   1426  N   CYS A 481     -48.968 -45.857   2.856  1.00 84.33           N  
ANISOU 1426  N   CYS A 481     6985  11786  13268   -756   1192   1135       N  
ATOM   1427  CA  CYS A 481     -49.940 -44.807   3.079  1.00 87.04           C  
ANISOU 1427  CA  CYS A 481     7048  11885  14138   -657   1389   1528       C  
ATOM   1428  C   CYS A 481     -50.855 -44.591   1.909  1.00 89.83           C  
ANISOU 1428  C   CYS A 481     7073  12466  14590   -781   1205   2136       C  
ATOM   1429  O   CYS A 481     -52.024 -44.324   2.108  1.00 92.29           O  
ANISOU 1429  O   CYS A 481     7147  12643  15277   -730   1276   2498       O  
ATOM   1430  CB  CYS A 481     -49.245 -43.525   3.468  1.00 87.52           C  
ANISOU 1430  CB  CYS A 481     7068  11647  14539   -545   1677   1458       C  
ATOM   1431  SG  CYS A 481     -48.388 -43.752   5.018  1.00 87.11           S  
ANISOU 1431  SG  CYS A 481     7383  11332  14379   -461   1881    800       S  
ATOM   1432  N   THR A 482     -50.344 -44.730   0.692  1.00 90.84           N  
ANISOU 1432  N   THR A 482     7183  12948  14381   -971    969   2268       N  
ATOM   1433  CA  THR A 482     -51.189 -44.605  -0.495  1.00 94.08           C  
ANISOU 1433  CA  THR A 482     7297  13664  14786  -1173    731   2875       C  
ATOM   1434  C   THR A 482     -52.304 -45.647  -0.518  1.00 94.83           C  
ANISOU 1434  C   THR A 482     7377  13931  14720  -1293    523   2998       C  
ATOM   1435  O   THR A 482     -53.327 -45.424  -1.156  1.00 98.46           O  
ANISOU 1435  O   THR A 482     7522  14543  15342  -1423    363   3582       O  
ATOM   1436  CB  THR A 482     -50.400 -44.694  -1.816  1.00 94.74           C  
ANISOU 1436  CB  THR A 482     7427  14150  14420  -1426    515   2939       C  
ATOM   1437  OG1 THR A 482     -50.129 -46.065  -2.127  1.00 93.43           O  
ANISOU 1437  OG1 THR A 482     7558  14273  13668  -1620    324   2571       O  
ATOM   1438  CG2 THR A 482     -49.110 -43.925  -1.726  1.00 93.39           C  
ANISOU 1438  CG2 THR A 482     7344  13819  14318  -1307    708   2691       C  
ATOM   1439  N   ARG A 483     -52.120 -46.767   0.180  1.00 92.24           N  
ANISOU 1439  N   ARG A 483     7362  13578  14107  -1258    518   2490       N  
ATOM   1440  CA  ARG A 483     -53.141 -47.822   0.210  1.00 92.74           C  
ANISOU 1440  CA  ARG A 483     7429  13786  14020  -1369    334   2561       C  
ATOM   1441  C   ARG A 483     -54.014 -47.853   1.447  1.00 92.84           C  
ANISOU 1441  C   ARG A 483     7393  13449  14433  -1143    528   2544       C  
ATOM   1442  O   ARG A 483     -54.856 -48.741   1.578  1.00 92.80           O  
ANISOU 1442  O   ARG A 483     7393  13531  14336  -1209    395   2585       O  
ATOM   1443  CB  ARG A 483     -52.493 -49.184   0.084  1.00 90.29           C  
ANISOU 1443  CB  ARG A 483     7469  13687  13148  -1508    200   2052       C  
ATOM   1444  CG  ARG A 483     -52.078 -49.520  -1.306  1.00 90.86           C  
ANISOU 1444  CG  ARG A 483     7587  14179  12754  -1840    -23   2119       C  
ATOM   1445  CD  ARG A 483     -51.569 -50.918  -1.352  1.00 86.19           C  
ANISOU 1445  CD  ARG A 483     7321  13721  11706  -1972    -79   1607       C  
ATOM   1446  NE  ARG A 483     -50.363 -51.060  -0.551  1.00 80.99           N  
ANISOU 1446  NE  ARG A 483     6896  12812  11062  -1753    130   1090       N  
ATOM   1447  CZ  ARG A 483     -49.137 -51.029  -1.048  1.00 78.76           C  
ANISOU 1447  CZ  ARG A 483     6757  12600  10567  -1815    190    837       C  
ATOM   1448  NH1 ARG A 483     -48.957 -50.860  -2.344  1.00 80.99           N1+
ANISOU 1448  NH1 ARG A 483     7004  13197  10570  -2096     81   1019       N1+
ATOM   1449  NH2 ARG A 483     -48.096 -51.176  -0.248  1.00 76.04           N  
ANISOU 1449  NH2 ARG A 483     6583  12020  10286  -1620    356    424       N  
ATOM   1450  N   MET A 484     -53.804 -46.911   2.365  1.00 93.72           N  
ANISOU 1450  N   MET A 484     7474  13163  14971   -900    863   2456       N  
ATOM   1451  CA  MET A 484     -54.535 -46.905   3.627  1.00 94.42           C  
ANISOU 1451  CA  MET A 484     7567  12892  15415   -706   1121   2364       C  
ATOM   1452  C   MET A 484     -55.999 -46.730   3.344  1.00 98.37           C  
ANISOU 1452  C   MET A 484     7699  13371  16303   -727   1077   2960       C  
ATOM   1453  O   MET A 484     -56.372 -45.992   2.436  1.00101.63           O  
ANISOU 1453  O   MET A 484     7772  13883  16957   -811    988   3514       O  
ATOM   1454  CB  MET A 484     -54.022 -45.829   4.572  1.00 94.03           C  
ANISOU 1454  CB  MET A 484     7563  12426  15735   -511   1526   2152       C  
ATOM   1455  CG  MET A 484     -52.774 -46.266   5.284  1.00 92.16           C  
ANISOU 1455  CG  MET A 484     7720  12167  15127   -485   1571   1518       C  
ATOM   1456  SD  MET A 484     -51.993 -45.049   6.358  1.00 95.27           S  
ANISOU 1456  SD  MET A 484     8226  12137  15832   -350   2003   1203       S  
ATOM   1457  CE  MET A 484     -52.879 -45.326   7.889  1.00 94.07           C  
ANISOU 1457  CE  MET A 484     8201  11660  15879   -256   2303    992       C  
ATOM   1458  N   LYS A 485     -56.817 -47.429   4.123  1.00 99.20           N  
ANISOU 1458  N   LYS A 485     7853  13355  16480   -662   1129   2877       N  
ATOM   1459  CA  LYS A 485     -58.253 -47.545   3.879  1.00103.21           C  
ANISOU 1459  CA  LYS A 485     8026  13875  17311   -702   1038   3425       C  
ATOM   1460  C   LYS A 485     -59.004 -46.234   4.159  1.00106.85           C  
ANISOU 1460  C   LYS A 485     8096  13936  18563   -534   1385   3901       C  
ATOM   1461  O   LYS A 485     -58.401 -45.156   4.212  1.00107.46           O  
ANISOU 1461  O   LYS A 485     8119  13801  18908   -439   1636   3890       O  
ATOM   1462  CB  LYS A 485     -58.823 -48.698   4.728  1.00101.84           C  
ANISOU 1462  CB  LYS A 485     8044  13652  16996   -660   1033   3143       C  
ATOM   1463  CG  LYS A 485     -58.353 -50.123   4.347  1.00100.19           C  
ANISOU 1463  CG  LYS A 485     8136  13823  16108   -847    687   2783       C  
ATOM   1464  CD  LYS A 485     -59.121 -50.667   3.146  1.00105.43           C  
ANISOU 1464  CD  LYS A 485     8589  14878  16588  -1128    289   3229       C  
ATOM   1465  CE  LYS A 485     -58.762 -52.106   2.825  1.00105.08           C  
ANISOU 1465  CE  LYS A 485     8843  15147  15932  -1330     24   2838       C  
ATOM   1466  NZ  LYS A 485     -58.387 -52.273   1.366  1.00108.12           N1+
ANISOU 1466  NZ  LYS A 485     9217  15981  15881  -1676   -294   2983       N1+
ATOM   1467  N   GLU A 486     -60.317 -46.303   4.327  1.00109.73           N  
ANISOU 1467  N   GLU A 486     8165  14169  19357   -499   1427   4335       N  
ATOM   1468  CA  GLU A 486     -60.951 -45.148   4.938  1.00113.39           C  
ANISOU 1468  CA  GLU A 486     8323  14120  20640   -288   1905   4633       C  
ATOM   1469  C   GLU A 486     -61.273 -45.292   6.420  1.00112.32           C  
ANISOU 1469  C   GLU A 486     8397  13547  20730    -93   2356   4208       C  
ATOM   1470  O   GLU A 486     -61.838 -46.310   6.870  1.00110.95           O  
ANISOU 1470  O   GLU A 486     8352  13440  20363   -105   2255   4072       O  
ATOM   1471  CB  GLU A 486     -62.102 -44.537   4.126  1.00118.59           C  
ANISOU 1471  CB  GLU A 486     8377  14771  21910   -337   1814   5542       C  
ATOM   1472  CG  GLU A 486     -61.901 -43.016   3.986  1.00123.20           C  
ANISOU 1472  CG  GLU A 486     8643  15014  23154   -211   2169   5871       C  
ATOM   1473  CD  GLU A 486     -60.404 -42.611   4.090  1.00122.73           C  
ANISOU 1473  CD  GLU A 486     8952  14960  22718   -189   2277   5287       C  
ATOM   1474  OE1 GLU A 486     -59.825 -42.205   3.062  1.00124.56           O  
ANISOU 1474  OE1 GLU A 486     9066  15472  22787   -316   2028   5536       O  
ATOM   1475  OE2 GLU A 486     -59.796 -42.717   5.188  1.00120.08           O1-
ANISOU 1475  OE2 GLU A 486     9021  14373  22230    -68   2593   4595       O1-
ATOM   1476  N   ASN A 487     -60.878 -44.251   7.155  1.00112.70           N  
ANISOU 1476  N   ASN A 487     8491  13157  21172     58   2863   3988       N  
ATOM   1477  CA  ASN A 487     -60.929 -44.204   8.618  1.00111.81           C  
ANISOU 1477  CA  ASN A 487     8657  12625  21200    187   3362   3480       C  
ATOM   1478  C   ASN A 487     -59.723 -44.915   9.236  1.00106.95           C  
ANISOU 1478  C   ASN A 487     8601  12196  19839    124   3252   2722       C  
ATOM   1479  O   ASN A 487     -59.694 -45.181  10.433  1.00106.33           O  
ANISOU 1479  O   ASN A 487     8820  11907  19671    161   3537   2268       O  
ATOM   1480  CB  ASN A 487     -62.263 -44.754   9.178  1.00113.19           C  
ANISOU 1480  CB  ASN A 487     8692  12626  21689    253   3492   3685       C  
ATOM   1481  CG  ASN A 487     -63.501 -44.121   8.519  1.00118.70           C  
ANISOU 1481  CG  ASN A 487     8772  13153  23175    305   3555   4529       C  
ATOM   1482  OD1 ASN A 487     -63.400 -43.179   7.724  1.00121.46           O  
ANISOU 1482  OD1 ASN A 487     8780  13472  23897    301   3554   4978       O  
ATOM   1483  ND2 ASN A 487     -64.680 -44.651   8.853  1.00121.66           N  
ANISOU 1483  ND2 ASN A 487     8975  13417  23832    349   3603   4786       N  
ATOM   1484  N   GLN A 488     -58.723 -45.219   8.422  1.00103.76           N  
ANISOU 1484  N   GLN A 488     8324  12187  18912     11   2848   2611       N  
ATOM   1485  CA  GLN A 488     -57.544 -45.864   8.947  1.00 99.50           C  
ANISOU 1485  CA  GLN A 488     8249  11807  17748    -45   2739   1969       C  
ATOM   1486  C   GLN A 488     -56.551 -44.825   9.469  1.00 99.78           C  
ANISOU 1486  C   GLN A 488     8443  11588  17880    -16   3076   1632       C  
ATOM   1487  O   GLN A 488     -55.957 -44.060   8.693  1.00100.72           O  
ANISOU 1487  O   GLN A 488     8423  11756  18088    -33   3028   1792       O  
ATOM   1488  CB  GLN A 488     -56.905 -46.765   7.898  1.00 96.92           C  
ANISOU 1488  CB  GLN A 488     8005  11984  16836   -187   2204   1957       C  
ATOM   1489  CG  GLN A 488     -56.030 -47.830   8.531  1.00 92.45           C  
ANISOU 1489  CG  GLN A 488     7862  11573  15691   -232   2066   1376       C  
ATOM   1490  CD  GLN A 488     -55.045 -48.438   7.571  1.00 88.69           C  
ANISOU 1490  CD  GLN A 488     7499  11487  14713   -362   1683   1260       C  
ATOM   1491  OE1 GLN A 488     -55.320 -48.574   6.385  1.00 89.54           O  
ANISOU 1491  OE1 GLN A 488     7410  11860  14748   -474   1415   1607       O  
ATOM   1492  NE2 GLN A 488     -53.887 -48.818   8.085  1.00 85.21           N  
ANISOU 1492  NE2 GLN A 488     7369  11084  13922   -376   1666    780       N  
ATOM   1493  N   LYS A 489     -56.369 -44.799  10.787  1.00 99.24           N  
ANISOU 1493  N   LYS A 489     8671  11262  17774     -3   3413   1167       N  
ATOM   1494  CA  LYS A 489     -55.494 -43.806  11.422  1.00 99.58           C  
ANISOU 1494  CA  LYS A 489     8893  11042  17901    -28   3769    808       C  
ATOM   1495  C   LYS A 489     -54.094 -44.350  11.762  1.00 95.89           C  
ANISOU 1495  C   LYS A 489     8818  10827  16786   -145   3527    294       C  
ATOM   1496  O   LYS A 489     -53.171 -43.577  12.005  1.00 96.64           O  
ANISOU 1496  O   LYS A 489     9038  10807  16873   -201   3690     43       O  
ATOM   1497  CB  LYS A 489     -56.162 -43.223  12.668  1.00102.31           C  
ANISOU 1497  CB  LYS A 489     9310  10908  18653     -4   4368    627       C  
ATOM   1498  CG  LYS A 489     -57.707 -43.145  12.584  1.00107.57           C  
ANISOU 1498  CG  LYS A 489     9622  11335  19913    118   4586   1104       C  
ATOM   1499  CD  LYS A 489     -58.259 -41.810  12.001  1.00114.93           C  
ANISOU 1499  CD  LYS A 489    10097  11905  21663    224   4935   1598       C  
ATOM   1500  CE  LYS A 489     -58.004 -41.645  10.483  1.00115.59           C  
ANISOU 1500  CE  LYS A 489     9850  12316  21752    233   4478   2107       C  
ATOM   1501  NZ  LYS A 489     -58.247 -40.252  10.004  1.00119.42           N1+
ANISOU 1501  NZ  LYS A 489     9923  12451  22999    316   4824   2538       N1+
ATOM   1502  N   HIS A 490     -53.922 -45.667  11.748  1.00 92.15           N  
ANISOU 1502  N   HIS A 490     8511  10685  15815   -189   3142    168       N  
ATOM   1503  CA  HIS A 490     -52.659 -46.254  12.183  1.00 88.77           C  
ANISOU 1503  CA  HIS A 490     8415  10459  14853   -294   2937   -269       C  
ATOM   1504  C   HIS A 490     -51.854 -47.045  11.123  1.00 85.68           C  
ANISOU 1504  C   HIS A 490     8015  10462  14075   -327   2461   -228       C  
ATOM   1505  O   HIS A 490     -52.407 -47.640  10.197  1.00 85.40           O  
ANISOU 1505  O   HIS A 490     7806  10634  14008   -309   2210     64       O  
ATOM   1506  CB  HIS A 490     -52.904 -47.115  13.429  1.00 88.17           C  
ANISOU 1506  CB  HIS A 490     8606  10366  14527   -349   2990   -565       C  
ATOM   1507  CG  HIS A 490     -53.655 -46.404  14.511  1.00 91.11           C  
ANISOU 1507  CG  HIS A 490     9036  10354  15224   -360   3501   -666       C  
ATOM   1508  ND1 HIS A 490     -53.157 -45.292  15.157  1.00 91.79           N  
ANISOU 1508  ND1 HIS A 490     9254  10171  15448   -452   3885   -925       N  
ATOM   1509  CD2 HIS A 490     -54.871 -46.645  15.060  1.00 92.94           C  
ANISOU 1509  CD2 HIS A 490     9220  10408  15683   -307   3730   -562       C  
ATOM   1510  CE1 HIS A 490     -54.032 -44.880  16.055  1.00 95.21           C  
ANISOU 1510  CE1 HIS A 490     9733  10268  16174   -470   4358   -999       C  
ATOM   1511  NE2 HIS A 490     -55.082 -45.682  16.016  1.00 95.17           N  
ANISOU 1511  NE2 HIS A 490     9612  10307  16239   -370   4276   -770       N  
ATOM   1512  N   ILE A 491     -50.537 -47.038  11.276  1.00 83.22           N  
ANISOU 1512  N   ILE A 491     7895  10244  13479   -401   2363   -528       N  
ATOM   1513  CA  ILE A 491     -49.677 -47.915  10.510  1.00 80.37           C  
ANISOU 1513  CA  ILE A 491     7577  10206  12755   -443   1986   -577       C  
ATOM   1514  C   ILE A 491     -49.452 -49.138  11.386  1.00 78.55           C  
ANISOU 1514  C   ILE A 491     7572  10074  12197   -490   1848   -845       C  
ATOM   1515  O   ILE A 491     -49.025 -49.011  12.518  1.00 78.72           O  
ANISOU 1515  O   ILE A 491     7791   9986  12131   -555   1974  -1108       O  
ATOM   1516  CB  ILE A 491     -48.351 -47.201  10.126  1.00 80.11           C  
ANISOU 1516  CB  ILE A 491     7573  10195  12670   -485   1968   -696       C  
ATOM   1517  CG1 ILE A 491     -48.669 -45.955   9.291  1.00 81.68           C  
ANISOU 1517  CG1 ILE A 491     7517  10276  13241   -433   2126   -382       C  
ATOM   1518  CG2 ILE A 491     -47.408 -48.134   9.376  1.00 77.80           C  
ANISOU 1518  CG2 ILE A 491     7328  10194  12038   -531   1640   -771       C  
ATOM   1519  CD1 ILE A 491     -47.489 -45.152   8.849  1.00 81.78           C  
ANISOU 1519  CD1 ILE A 491     7522  10287  13261   -462   2137   -452       C  
ATOM   1520  N   TYR A 492     -49.786 -50.318  10.888  1.00 77.19           N  
ANISOU 1520  N   TYR A 492     7366  10109  11853   -484   1598   -762       N  
ATOM   1521  CA  TYR A 492     -49.712 -51.511  11.711  1.00 76.11           C  
ANISOU 1521  CA  TYR A 492     7396  10041  11481   -513   1484   -957       C  
ATOM   1522  C   TYR A 492     -48.471 -52.257  11.358  1.00 75.37           C  
ANISOU 1522  C   TYR A 492     7374  10129  11133   -565   1250  -1115       C  
ATOM   1523  O   TYR A 492     -48.189 -52.465  10.172  1.00 75.95           O  
ANISOU 1523  O   TYR A 492     7347  10351  11156   -576   1110  -1024       O  
ATOM   1524  CB  TYR A 492     -50.917 -52.432  11.468  1.00 76.08           C  
ANISOU 1524  CB  TYR A 492     7301  10108  11498   -476   1391   -777       C  
ATOM   1525  CG  TYR A 492     -52.268 -51.829  11.802  1.00 76.36           C  
ANISOU 1525  CG  TYR A 492     7218   9944  11848   -411   1628   -565       C  
ATOM   1526  CD1 TYR A 492     -52.734 -51.818  13.099  1.00 75.19           C  
ANISOU 1526  CD1 TYR A 492     7201   9609  11755   -402   1853   -697       C  
ATOM   1527  CD2 TYR A 492     -53.071 -51.282  10.811  1.00 76.59           C  
ANISOU 1527  CD2 TYR A 492     6990   9974  12136   -378   1635   -205       C  
ATOM   1528  CE1 TYR A 492     -53.952 -51.259  13.410  1.00 77.92           C  
ANISOU 1528  CE1 TYR A 492     7429   9728  12447   -337   2130   -509       C  
ATOM   1529  CE2 TYR A 492     -54.290 -50.743  11.103  1.00 78.63           C  
ANISOU 1529  CE2 TYR A 492     7090  10019  12764   -308   1867     38       C  
ATOM   1530  CZ  TYR A 492     -54.733 -50.728  12.413  1.00 79.68           C  
ANISOU 1530  CZ  TYR A 492     7361   9922  12992   -275   2141   -129       C  
ATOM   1531  OH  TYR A 492     -55.958 -50.175  12.738  1.00 81.69           O  
ANISOU 1531  OH  TYR A 492     7450   9912  13676   -199   2441    105       O  
ATOM   1532  N   TYR A 493     -47.723 -52.678  12.368  1.00 75.09           N  
ANISOU 1532  N   TYR A 493     7501  10086  10943   -620   1214  -1332       N  
ATOM   1533  CA  TYR A 493     -46.550 -53.520  12.120  1.00 74.20           C  
ANISOU 1533  CA  TYR A 493     7414  10111  10666   -659   1005  -1441       C  
ATOM   1534  C   TYR A 493     -46.538 -54.691  13.094  1.00 74.44           C  
ANISOU 1534  C   TYR A 493     7533  10176  10573   -690    901  -1520       C  
ATOM   1535  O   TYR A 493     -47.081 -54.601  14.198  1.00 74.97           O  
ANISOU 1535  O   TYR A 493     7703  10169  10613   -724    998  -1554       O  
ATOM   1536  CB  TYR A 493     -45.243 -52.706  12.248  1.00 74.01           C  
ANISOU 1536  CB  TYR A 493     7433  10057  10630   -720   1021  -1555       C  
ATOM   1537  CG  TYR A 493     -44.959 -52.264  13.677  1.00 73.45           C  
ANISOU 1537  CG  TYR A 493     7522   9893  10491   -830   1108  -1700       C  
ATOM   1538  CD1 TYR A 493     -45.543 -51.103  14.194  1.00 73.32           C  
ANISOU 1538  CD1 TYR A 493     7569   9706  10582   -862   1372  -1736       C  
ATOM   1539  CD2 TYR A 493     -44.147 -53.024  14.524  1.00 70.28           C  
ANISOU 1539  CD2 TYR A 493     7202   9572   9927   -932    943  -1785       C  
ATOM   1540  CE1 TYR A 493     -45.318 -50.703  15.519  1.00 73.00           C  
ANISOU 1540  CE1 TYR A 493     7719   9591  10427  -1028   1488  -1914       C  
ATOM   1541  CE2 TYR A 493     -43.933 -52.637  15.845  1.00 70.62           C  
ANISOU 1541  CE2 TYR A 493     7411   9581   9838  -1103    999  -1902       C  
ATOM   1542  CZ  TYR A 493     -44.519 -51.480  16.335  1.00 71.80           C  
ANISOU 1542  CZ  TYR A 493     7670   9575  10034  -1167   1280  -1995       C  
ATOM   1543  OH  TYR A 493     -44.312 -51.084  17.635  1.00 72.49           O  
ANISOU 1543  OH  TYR A 493     7962   9637   9944  -1398   1372  -2157       O  
ATOM   1544  N   ILE A 494     -45.907 -55.779  12.679  1.00 74.44           N  
ANISOU 1544  N   ILE A 494     7486  10276  10519   -690    733  -1543       N  
ATOM   1545  CA  ILE A 494     -45.520 -56.845  13.590  1.00 75.31           C  
ANISOU 1545  CA  ILE A 494     7637  10411  10565   -727    617  -1584       C  
ATOM   1546  C   ILE A 494     -44.001 -57.050  13.497  1.00 76.42           C  
ANISOU 1546  C   ILE A 494     7734  10582  10719   -774    505  -1630       C  
ATOM   1547  O   ILE A 494     -43.424 -56.918  12.415  1.00 76.37           O  
ANISOU 1547  O   ILE A 494     7649  10591  10776   -747    511  -1647       O  
ATOM   1548  CB  ILE A 494     -46.273 -58.148  13.265  1.00 74.56           C  
ANISOU 1548  CB  ILE A 494     7479  10353  10495   -674    554  -1531       C  
ATOM   1549  CG1 ILE A 494     -45.774 -59.320  14.123  1.00 74.55           C  
ANISOU 1549  CG1 ILE A 494     7470  10362  10491   -702    435  -1530       C  
ATOM   1550  CG2 ILE A 494     -46.190 -58.467  11.783  1.00 74.41           C  
ANISOU 1550  CG2 ILE A 494     7364  10393  10515   -658    537  -1533       C  
ATOM   1551  CD1 ILE A 494     -46.784 -60.467  14.250  1.00 75.15           C  
ANISOU 1551  CD1 ILE A 494     7514  10436  10601   -657    415  -1475       C  
ATOM   1552  N   THR A 495     -43.354 -57.352  14.623  1.00 78.13           N  
ANISOU 1552  N   THR A 495     7989  10813  10883   -864    404  -1624       N  
ATOM   1553  CA  THR A 495     -41.948 -57.752  14.609  1.00 79.56           C  
ANISOU 1553  CA  THR A 495     8069  11013  11145   -909    272  -1594       C  
ATOM   1554  C   THR A 495     -41.772 -59.220  15.023  1.00 80.60           C  
ANISOU 1554  C   THR A 495     8095  11156  11372   -899    149  -1488       C  
ATOM   1555  O   THR A 495     -42.323 -59.644  16.032  1.00 81.05           O  
ANISOU 1555  O   THR A 495     8208  11248  11337   -951     94  -1424       O  
ATOM   1556  CB  THR A 495     -41.063 -56.853  15.506  1.00 80.73           C  
ANISOU 1556  CB  THR A 495     8290  11186  11196  -1069    211  -1605       C  
ATOM   1557  OG1 THR A 495     -41.288 -57.177  16.876  1.00 83.24           O  
ANISOU 1557  OG1 THR A 495     8700  11568  11359  -1210    123  -1553       O  
ATOM   1558  CG2 THR A 495     -41.353 -55.380  15.291  1.00 80.69           C  
ANISOU 1558  CG2 THR A 495     8396  11129  11132  -1089    379  -1719       C  
ATOM   1559  N   GLY A 496     -41.006 -59.980  14.234  1.00 81.84           N  
ANISOU 1559  N   GLY A 496     8091  11262  11740   -840    139  -1466       N  
ATOM   1560  CA  GLY A 496     -40.673 -61.391  14.518  1.00 84.10           C  
ANISOU 1560  CA  GLY A 496     8219  11500  12232   -819     68  -1346       C  
ATOM   1561  C   GLY A 496     -39.436 -61.881  13.777  1.00 86.40           C  
ANISOU 1561  C   GLY A 496     8318  11687  12821   -786    107  -1320       C  
ATOM   1562  O   GLY A 496     -38.738 -61.083  13.129  1.00 86.17           O  
ANISOU 1562  O   GLY A 496     8289  11647  12802   -793    161  -1391       O  
ATOM   1563  N   GLU A 497     -39.151 -63.184  13.860  1.00 89.12           N  
ANISOU 1563  N   GLU A 497     8483  11928  13449   -749    113  -1213       N  
ATOM   1564  CA  GLU A 497     -37.874 -63.726  13.306  1.00 92.49           C  
ANISOU 1564  CA  GLU A 497     8682  12198  14260   -720    195  -1152       C  
ATOM   1565  C   GLU A 497     -37.892 -63.848  11.792  1.00 92.12           C  
ANISOU 1565  C   GLU A 497     8660  12051  14289   -668    461  -1395       C  
ATOM   1566  O   GLU A 497     -36.951 -63.438  11.128  1.00 93.25           O  
ANISOU 1566  O   GLU A 497     8742  12132  14555   -671    557  -1440       O  
ATOM   1567  CB  GLU A 497     -37.468 -65.084  13.912  1.00 94.78           C  
ANISOU 1567  CB  GLU A 497     8720  12360  14931   -699    155   -916       C  
ATOM   1568  CG  GLU A 497     -37.632 -65.230  15.434  1.00 99.30           C  
ANISOU 1568  CG  GLU A 497     9265  13068  15397   -790   -119   -638       C  
ATOM   1569  CD  GLU A 497     -37.070 -66.565  15.975  1.00106.55           C  
ANISOU 1569  CD  GLU A 497     9862  13851  16771   -773   -170   -318       C  
ATOM   1570  OE1 GLU A 497     -37.439 -67.653  15.449  1.00108.01           O  
ANISOU 1570  OE1 GLU A 497     9944  13851  17243   -667     29   -380       O  
ATOM   1571  OE2 GLU A 497     -36.259 -66.515  16.941  1.00110.73           O1-
ANISOU 1571  OE2 GLU A 497    10228  14461  17383   -889   -413     15       O1-
ATOM   1572  N   THR A 498     -38.962 -64.433  11.264  1.00 91.86           N  
ANISOU 1572  N   THR A 498     8717  12014  14168   -651    577  -1544       N  
ATOM   1573  CA  THR A 498     -39.143 -64.629   9.825  1.00 92.03           C  
ANISOU 1573  CA  THR A 498     8800  11988  14176   -677    821  -1789       C  
ATOM   1574  C   THR A 498     -40.475 -64.043   9.307  1.00 90.01           C  
ANISOU 1574  C   THR A 498     8756  11912  13529   -722    800  -1912       C  
ATOM   1575  O   THR A 498     -41.458 -63.929  10.047  1.00 88.75           O  
ANISOU 1575  O   THR A 498     8670  11843  13208   -702    662  -1831       O  
ATOM   1576  CB  THR A 498     -38.955 -66.132   9.390  1.00 94.03           C  
ANISOU 1576  CB  THR A 498     8912  12020  14793   -676   1051  -1866       C  
ATOM   1577  OG1 THR A 498     -39.906 -66.472   8.369  1.00 95.08           O  
ANISOU 1577  OG1 THR A 498     9197  12196  14733   -764   1210  -2111       O  
ATOM   1578  CG2 THR A 498     -39.149 -67.106  10.560  1.00 95.36           C  
ANISOU 1578  CG2 THR A 498     8929  12104  15197   -616    935  -1650       C  
ATOM   1579  N   LYS A 499     -40.462 -63.658   8.034  1.00 89.81           N  
ANISOU 1579  N   LYS A 499     8812  11937  13374   -799    945  -2077       N  
ATOM   1580  CA  LYS A 499     -41.634 -63.245   7.297  1.00 88.87           C  
ANISOU 1580  CA  LYS A 499     8839  11989  12936   -883    935  -2148       C  
ATOM   1581  C   LYS A 499     -42.753 -64.288   7.415  1.00 89.01           C  
ANISOU 1581  C   LYS A 499     8877  12003  12936   -916    932  -2179       C  
ATOM   1582  O   LYS A 499     -43.855 -63.962   7.872  1.00 87.85           O  
ANISOU 1582  O   LYS A 499     8789  11965  12625   -893    792  -2076       O  
ATOM   1583  CB  LYS A 499     -41.249 -63.001   5.841  1.00 89.89           C  
ANISOU 1583  CB  LYS A 499     9023  12170  12958  -1018   1112  -2311       C  
ATOM   1584  CG  LYS A 499     -42.391 -62.629   4.944  1.00 90.78           C  
ANISOU 1584  CG  LYS A 499     9257  12497  12738  -1163   1079  -2333       C  
ATOM   1585  CD  LYS A 499     -41.905 -62.286   3.561  1.00 93.01           C  
ANISOU 1585  CD  LYS A 499     9601  12871  12867  -1335   1234  -2462       C  
ATOM   1586  CE  LYS A 499     -43.103 -62.006   2.675  1.00 96.28           C  
ANISOU 1586  CE  LYS A 499    10111  13539  12932  -1532   1154  -2421       C  
ATOM   1587  NZ  LYS A 499     -42.851 -62.551   1.306  1.00101.17           N1+
ANISOU 1587  NZ  LYS A 499    10827  14232  13378  -1813   1365  -2649       N1+
ATOM   1588  N   ASP A 500     -42.472 -65.536   7.047  1.00 90.34           N  
ANISOU 1588  N   ASP A 500     8987  12021  13317   -966   1111  -2317       N  
ATOM   1589  CA  ASP A 500     -43.474 -66.602   7.194  1.00 91.26           C  
ANISOU 1589  CA  ASP A 500     9108  12105  13458  -1003   1121  -2354       C  
ATOM   1590  C   ASP A 500     -44.082 -66.657   8.599  1.00 89.33           C  
ANISOU 1590  C   ASP A 500     8820  11867  13252   -863    914  -2137       C  
ATOM   1591  O   ASP A 500     -45.280 -66.489   8.749  1.00 89.27           O  
ANISOU 1591  O   ASP A 500     8888  11979  13048   -878    806  -2083       O  
ATOM   1592  CB  ASP A 500     -42.934 -67.970   6.767  1.00 94.09           C  
ANISOU 1592  CB  ASP A 500     9381  12230  14139  -1064   1392  -2534       C  
ATOM   1593  CG  ASP A 500     -42.647 -68.051   5.245  1.00 99.20           C  
ANISOU 1593  CG  ASP A 500    10136  12891  14663  -1284   1656  -2821       C  
ATOM   1594  OD1 ASP A 500     -43.440 -68.722   4.532  1.00102.50           O  
ANISOU 1594  OD1 ASP A 500    10654  13350  14940  -1479   1762  -3006       O  
ATOM   1595  OD2 ASP A 500     -41.635 -67.451   4.760  1.00101.89           O1-
ANISOU 1595  OD2 ASP A 500    10471  13212  15030  -1293   1763  -2866       O1-
ATOM   1596  N   GLN A 501     -43.262 -66.856   9.622  1.00 88.75           N  
ANISOU 1596  N   GLN A 501     8618  11678  13424   -751    857  -1989       N  
ATOM   1597  CA  GLN A 501     -43.700 -66.813  11.020  1.00 86.92           C  
ANISOU 1597  CA  GLN A 501     8365  11484  13174   -666    660  -1774       C  
ATOM   1598  C   GLN A 501     -44.707 -65.693  11.293  1.00 84.34           C  
ANISOU 1598  C   GLN A 501     8196  11339  12508   -666    533  -1728       C  
ATOM   1599  O   GLN A 501     -45.779 -65.944  11.842  1.00 83.77           O  
ANISOU 1599  O   GLN A 501     8162  11302  12362   -645    472  -1660       O  
ATOM   1600  CB  GLN A 501     -42.476 -66.683  11.935  1.00 87.99           C  
ANISOU 1600  CB  GLN A 501     8367  11559  13505   -617    568  -1592       C  
ATOM   1601  CG  GLN A 501     -42.730 -66.381  13.427  1.00 89.61           C  
ANISOU 1601  CG  GLN A 501     8590  11862  13596   -602    348  -1370       C  
ATOM   1602  CD  GLN A 501     -41.418 -66.080  14.178  1.00 93.90           C  
ANISOU 1602  CD  GLN A 501     9010  12400  14266   -630    221  -1180       C  
ATOM   1603  OE1 GLN A 501     -40.948 -64.927  14.226  1.00 91.61           O  
ANISOU 1603  OE1 GLN A 501     8804  12201  13800   -675    159  -1198       O  
ATOM   1604  NE2 GLN A 501     -40.814 -67.130  14.752  1.00 97.14           N  
ANISOU 1604  NE2 GLN A 501     9195  12698  15014   -616    180   -969       N  
ATOM   1605  N   VAL A 502     -44.378 -64.466  10.901  1.00 82.88           N  
ANISOU 1605  N   VAL A 502     8084  11241  12164   -685    523  -1754       N  
ATOM   1606  CA  VAL A 502     -45.235 -63.308  11.242  1.00 80.71           C  
ANISOU 1606  CA  VAL A 502     7924  11082  11660   -674    451  -1685       C  
ATOM   1607  C   VAL A 502     -46.481 -63.227  10.362  1.00 80.14           C  
ANISOU 1607  C   VAL A 502     7899  11095  11452   -722    482  -1708       C  
ATOM   1608  O   VAL A 502     -47.560 -62.897  10.851  1.00 79.48           O  
ANISOU 1608  O   VAL A 502     7854  11048  11296   -692    442  -1606       O  
ATOM   1609  CB  VAL A 502     -44.470 -61.929  11.278  1.00 80.18           C  
ANISOU 1609  CB  VAL A 502     7898  11051  11513   -678    439  -1675       C  
ATOM   1610  CG1 VAL A 502     -43.395 -61.961  12.325  1.00 79.54           C  
ANISOU 1610  CG1 VAL A 502     7770  10922  11529   -676    356  -1605       C  
ATOM   1611  CG2 VAL A 502     -43.880 -61.542   9.914  1.00 79.25           C  
ANISOU 1611  CG2 VAL A 502     7765  10961  11382   -725    530  -1776       C  
ATOM   1612  N   ALA A 503     -46.321 -63.549   9.076  1.00 80.11           N  
ANISOU 1612  N   ALA A 503     7888  11128  11422   -822    561  -1829       N  
ATOM   1613  CA  ALA A 503     -47.405 -63.466   8.108  1.00 79.66           C  
ANISOU 1613  CA  ALA A 503     7865  11203  11199   -937    553  -1819       C  
ATOM   1614  C   ALA A 503     -48.502 -64.442   8.459  1.00 79.66           C  
ANISOU 1614  C   ALA A 503     7849  11183  11233   -945    516  -1787       C  
ATOM   1615  O   ALA A 503     -49.685 -64.203   8.165  1.00 80.27           O  
ANISOU 1615  O   ALA A 503     7929  11366  11204  -1001    450  -1672       O  
ATOM   1616  CB  ALA A 503     -46.894 -63.752   6.742  1.00 80.97           C  
ANISOU 1616  CB  ALA A 503     8052  11424  11285  -1105    658  -1984       C  
ATOM   1617  N   ASN A 504     -48.115 -65.545   9.089  1.00 79.25           N  
ANISOU 1617  N   ASN A 504     7752  10989  11370   -891    556  -1850       N  
ATOM   1618  CA  ASN A 504     -49.079 -66.563   9.478  1.00 79.22           C  
ANISOU 1618  CA  ASN A 504     7719  10941  11436   -890    535  -1821       C  
ATOM   1619  C   ASN A 504     -49.315 -66.605  10.983  1.00 77.63           C  
ANISOU 1619  C   ASN A 504     7493  10673  11329   -738    459  -1661       C  
ATOM   1620  O   ASN A 504     -49.792 -67.597  11.498  1.00 78.39           O  
ANISOU 1620  O   ASN A 504     7541  10695  11548   -711    455  -1629       O  
ATOM   1621  CB  ASN A 504     -48.684 -67.931   8.911  1.00 80.79           C  
ANISOU 1621  CB  ASN A 504     7875  11021  11799   -984    675  -2012       C  
ATOM   1622  CG  ASN A 504     -48.362 -67.866   7.405  1.00 84.53           C  
ANISOU 1622  CG  ASN A 504     8416  11572  12128  -1194    795  -2216       C  
ATOM   1623  OD1 ASN A 504     -49.261 -67.707   6.544  1.00 87.09           O  
ANISOU 1623  OD1 ASN A 504     8805  12066  12216  -1373    748  -2229       O  
ATOM   1624  ND2 ASN A 504     -47.069 -67.966   7.081  1.00 85.56           N  
ANISOU 1624  ND2 ASN A 504     8524  11591  12394  -1196    951  -2352       N  
ATOM   1625  N   SER A 505     -48.998 -65.516  11.684  1.00 75.86           N  
ANISOU 1625  N   SER A 505     7312  10478  11031   -667    412  -1569       N  
ATOM   1626  CA  SER A 505     -49.259 -65.420  13.115  1.00 73.81           C  
ANISOU 1626  CA  SER A 505     7073  10189  10780   -588    360  -1437       C  
ATOM   1627  C   SER A 505     -50.716 -65.113  13.323  1.00 72.95           C  
ANISOU 1627  C   SER A 505     7003  10113  10599   -569    365  -1341       C  
ATOM   1628  O   SER A 505     -51.378 -64.518  12.452  1.00 73.02           O  
ANISOU 1628  O   SER A 505     7014  10187  10544   -607    381  -1320       O  
ATOM   1629  CB  SER A 505     -48.401 -64.336  13.769  1.00 73.75           C  
ANISOU 1629  CB  SER A 505     7125  10201  10693   -580    339  -1412       C  
ATOM   1630  OG  SER A 505     -48.929 -63.034  13.565  1.00 72.58           O  
ANISOU 1630  OG  SER A 505     7056  10100  10420   -582    387  -1398       O  
ATOM   1631  N   ALA A 506     -51.223 -65.511  14.485  1.00 72.09           N  
ANISOU 1631  N   ALA A 506     6907   9962  10520   -521    354  -1246       N  
ATOM   1632  CA  ALA A 506     -52.628 -65.292  14.789  1.00 70.58           C  
ANISOU 1632  CA  ALA A 506     6735   9764  10314   -491    395  -1139       C  
ATOM   1633  C   ALA A 506     -52.895 -63.807  14.821  1.00 69.88           C  
ANISOU 1633  C   ALA A 506     6713   9684  10152   -482    481  -1101       C  
ATOM   1634  O   ALA A 506     -53.964 -63.381  14.467  1.00 70.80           O  
ANISOU 1634  O   ALA A 506     6791   9792  10316   -467    532   -997       O  
ATOM   1635  CB  ALA A 506     -53.006 -65.948  16.079  1.00 70.40           C  
ANISOU 1635  CB  ALA A 506     6730   9695  10324   -455    396  -1053       C  
ATOM   1636  N   PHE A 507     -51.906 -63.012  15.200  1.00 69.43           N  
ANISOU 1636  N   PHE A 507     6733   9631  10016   -502    503  -1167       N  
ATOM   1637  CA  PHE A 507     -52.105 -61.568  15.368  1.00 69.07           C  
ANISOU 1637  CA  PHE A 507     6755   9548   9938   -502    634  -1153       C  
ATOM   1638  C   PHE A 507     -52.495 -60.810  14.119  1.00 69.16           C  
ANISOU 1638  C   PHE A 507     6681   9582  10012   -494    661  -1089       C  
ATOM   1639  O   PHE A 507     -52.979 -59.707  14.221  1.00 70.29           O  
ANISOU 1639  O   PHE A 507     6827   9655  10225   -472    801  -1016       O  
ATOM   1640  CB  PHE A 507     -50.864 -60.893  15.904  1.00 68.57           C  
ANISOU 1640  CB  PHE A 507     6787   9494   9771   -561    638  -1256       C  
ATOM   1641  CG  PHE A 507     -50.257 -61.570  17.061  1.00 67.95           C  
ANISOU 1641  CG  PHE A 507     6769   9443   9604   -623    557  -1268       C  
ATOM   1642  CD1 PHE A 507     -50.708 -61.318  18.333  1.00 69.18           C  
ANISOU 1642  CD1 PHE A 507     7054   9577   9653   -688    652  -1256       C  
ATOM   1643  CD2 PHE A 507     -49.198 -62.424  16.888  1.00 68.08           C  
ANISOU 1643  CD2 PHE A 507     6703   9507   9657   -639    402  -1271       C  
ATOM   1644  CE1 PHE A 507     -50.124 -61.923  19.415  1.00 69.75           C  
ANISOU 1644  CE1 PHE A 507     7177   9722   9602   -794    545  -1221       C  
ATOM   1645  CE2 PHE A 507     -48.596 -63.020  17.967  1.00 69.65           C  
ANISOU 1645  CE2 PHE A 507     6910   9745   9807   -714    298  -1203       C  
ATOM   1646  CZ  PHE A 507     -49.069 -62.773  19.234  1.00 70.01           C  
ANISOU 1646  CZ  PHE A 507     7090   9817   9692   -804    345  -1166       C  
ATOM   1647  N   VAL A 508     -52.277 -61.364  12.939  1.00 69.14           N  
ANISOU 1647  N   VAL A 508     6598   9674   9996   -535    548  -1106       N  
ATOM   1648  CA  VAL A 508     -52.610 -60.614  11.718  1.00 69.72           C  
ANISOU 1648  CA  VAL A 508     6587   9819  10081   -578    542  -1004       C  
ATOM   1649  C   VAL A 508     -53.862 -61.112  10.965  1.00 70.87           C  
ANISOU 1649  C   VAL A 508     6620  10038  10266   -635    469   -839       C  
ATOM   1650  O   VAL A 508     -54.236 -60.552   9.931  1.00 71.68           O  
ANISOU 1650  O   VAL A 508     6629  10242  10365   -713    425   -690       O  
ATOM   1651  CB  VAL A 508     -51.416 -60.523  10.757  1.00 69.23           C  
ANISOU 1651  CB  VAL A 508     6534   9848   9923   -650    488  -1127       C  
ATOM   1652  CG1 VAL A 508     -50.371 -59.623  11.346  1.00 69.03           C  
ANISOU 1652  CG1 VAL A 508     6579   9756   9891   -609    556  -1210       C  
ATOM   1653  CG2 VAL A 508     -50.843 -61.908  10.461  1.00 68.67           C  
ANISOU 1653  CG2 VAL A 508     6471   9805   9814   -706    422  -1286       C  
ATOM   1654  N   GLU A 509     -54.500 -62.154  11.497  1.00 70.93           N  
ANISOU 1654  N   GLU A 509     6625  10010  10314   -615    443   -838       N  
ATOM   1655  CA  GLU A 509     -55.567 -62.842  10.810  1.00 71.70           C  
ANISOU 1655  CA  GLU A 509     6621  10185  10434   -703    347   -714       C  
ATOM   1656  C   GLU A 509     -56.631 -61.849  10.351  1.00 72.76           C  
ANISOU 1656  C   GLU A 509     6617  10345  10681   -718    353   -414       C  
ATOM   1657  O   GLU A 509     -56.890 -61.719   9.162  1.00 73.68           O  
ANISOU 1657  O   GLU A 509     6642  10623  10727   -870    232   -289       O  
ATOM   1658  CB  GLU A 509     -56.131 -63.938  11.712  1.00 71.73           C  
ANISOU 1658  CB  GLU A 509     6636  10100  10516   -644    354   -734       C  
ATOM   1659  CG  GLU A 509     -55.215 -65.196  11.828  1.00 73.80           C  
ANISOU 1659  CG  GLU A 509     6958  10349  10734   -669    319   -963       C  
ATOM   1660  CD  GLU A 509     -55.685 -66.281  12.862  1.00 74.92           C  
ANISOU 1660  CD  GLU A 509     7091  10388  10985   -596    332   -949       C  
ATOM   1661  OE1 GLU A 509     -56.807 -66.187  13.410  1.00 74.95           O  
ANISOU 1661  OE1 GLU A 509     7059  10346  11072   -541    362   -786       O  
ATOM   1662  OE2 GLU A 509     -54.909 -67.239  13.116  1.00 75.14           O1-
ANISOU 1662  OE2 GLU A 509     7129  10368  11051   -594    325  -1080       O1-
ATOM   1663  N   ARG A 510     -57.200 -61.100  11.288  1.00 73.12           N  
ANISOU 1663  N   ARG A 510     6639  10227  10912   -582    512   -285       N  
ATOM   1664  CA  ARG A 510     -58.318 -60.205  10.986  1.00 74.40           C  
ANISOU 1664  CA  ARG A 510     6616  10346  11304   -567    568     53       C  
ATOM   1665  C   ARG A 510     -57.884 -58.941  10.218  1.00 74.25           C  
ANISOU 1665  C   ARG A 510     6520  10368  11320   -597    591    173       C  
ATOM   1666  O   ARG A 510     -58.575 -58.505   9.315  1.00 75.79           O  
ANISOU 1666  O   ARG A 510     6517  10657  11623   -681    502    490       O  
ATOM   1667  CB  ARG A 510     -59.093 -59.889  12.279  1.00 75.44           C  
ANISOU 1667  CB  ARG A 510     6750  10237  11675   -417    808    125       C  
ATOM   1668  CG  ARG A 510     -60.437 -59.188  12.123  1.00 79.74           C  
ANISOU 1668  CG  ARG A 510     7057  10667  12572   -377    914    512       C  
ATOM   1669  CD  ARG A 510     -61.415 -59.697  13.194  1.00 85.31           C  
ANISOU 1669  CD  ARG A 510     7762  11198  13453   -282   1070    558       C  
ATOM   1670  NE  ARG A 510     -62.771 -59.183  12.983  1.00 91.19           N  
ANISOU 1670  NE  ARG A 510     8232  11818  14597   -244   1165    972       N  
ATOM   1671  CZ  ARG A 510     -63.218 -58.019  13.454  1.00 94.75           C  
ANISOU 1671  CZ  ARG A 510     8585  12006  15408   -138   1496   1131       C  
ATOM   1672  NH1 ARG A 510     -62.430 -57.241  14.192  1.00 94.92           N1+
ANISOU 1672  NH1 ARG A 510     8800  11876  15389    -84   1764    867       N1+
ATOM   1673  NH2 ARG A 510     -64.461 -57.631  13.187  1.00 97.46           N  
ANISOU 1673  NH2 ARG A 510     8623  12223  16182   -102   1575   1564       N  
ATOM   1674  N   LEU A 511     -56.739 -58.359  10.545  1.00 72.70           N  
ANISOU 1674  N   LEU A 511     6462  10119  11041   -549    692    -44       N  
ATOM   1675  CA  LEU A 511     -56.257 -57.230   9.739  1.00 72.94           C  
ANISOU 1675  CA  LEU A 511     6414  10196  11101   -584    705     63       C  
ATOM   1676  C   LEU A 511     -56.143 -57.635   8.265  1.00 73.45           C  
ANISOU 1676  C   LEU A 511     6402  10538  10967   -776    458    154       C  
ATOM   1677  O   LEU A 511     -56.669 -56.940   7.389  1.00 75.56           O  
ANISOU 1677  O   LEU A 511     6478  10899  11329   -858    393    482       O  
ATOM   1678  CB  LEU A 511     -54.947 -56.648  10.280  1.00 71.54           C  
ANISOU 1678  CB  LEU A 511     6405   9934  10841   -529    827   -211       C  
ATOM   1679  CG  LEU A 511     -55.053 -56.003  11.681  1.00 72.03           C  
ANISOU 1679  CG  LEU A 511     6564   9742  11062   -418   1102   -302       C  
ATOM   1680  CD1 LEU A 511     -53.721 -55.779  12.359  1.00 70.73           C  
ANISOU 1680  CD1 LEU A 511     6600   9544  10729   -427   1156   -608       C  
ATOM   1681  CD2 LEU A 511     -55.820 -54.697  11.642  1.00 73.58           C  
ANISOU 1681  CD2 LEU A 511     6594   9752  11609   -357   1334    -42       C  
ATOM   1682  N   ARG A 512     -55.514 -58.785   8.012  1.00 71.79           N  
ANISOU 1682  N   ARG A 512     6331  10450  10496   -870    338   -115       N  
ATOM   1683  CA  ARG A 512     -55.377 -59.353   6.680  1.00 71.85           C  
ANISOU 1683  CA  ARG A 512     6325  10711  10264  -1105    155   -120       C  
ATOM   1684  C   ARG A 512     -56.723 -59.585   5.989  1.00 74.11           C  
ANISOU 1684  C   ARG A 512     6436  11148  10574  -1269     -6    210       C  
ATOM   1685  O   ARG A 512     -56.870 -59.303   4.787  1.00 76.29           O  
ANISOU 1685  O   ARG A 512     6621  11659  10706  -1494   -153    404       O  
ATOM   1686  CB  ARG A 512     -54.621 -60.661   6.768  1.00 70.80           C  
ANISOU 1686  CB  ARG A 512     6359  10588   9951  -1154    142   -485       C  
ATOM   1687  CG  ARG A 512     -53.152 -60.522   7.093  1.00 69.36           C  
ANISOU 1687  CG  ARG A 512     6307  10321   9724  -1067    245   -762       C  
ATOM   1688  CD  ARG A 512     -52.350 -60.996   5.912  1.00 70.28           C  
ANISOU 1688  CD  ARG A 512     6486  10592   9625  -1267    211   -942       C  
ATOM   1689  NE  ARG A 512     -51.632 -62.255   6.123  1.00 67.94           N  
ANISOU 1689  NE  ARG A 512     6288  10214   9310  -1279    272  -1248       N  
ATOM   1690  CZ  ARG A 512     -51.559 -63.191   5.187  1.00 68.83           C  
ANISOU 1690  CZ  ARG A 512     6448  10426   9277  -1500    274  -1411       C  
ATOM   1691  NH1 ARG A 512     -52.200 -62.986   4.046  1.00 71.67           N1+
ANISOU 1691  NH1 ARG A 512     6783  11015   9432  -1751    176  -1286       N1+
ATOM   1692  NH2 ARG A 512     -50.883 -64.321   5.377  1.00 67.28           N  
ANISOU 1692  NH2 ARG A 512     6312  10102   9150  -1499    384  -1680       N  
ATOM   1693  N   LYS A 513     -57.710 -60.091   6.731  1.00 73.85           N  
ANISOU 1693  N   LYS A 513     6348  11000  10712  -1184      8    303       N  
ATOM   1694  CA  LYS A 513     -59.033 -60.351   6.152  1.00 75.64           C  
ANISOU 1694  CA  LYS A 513     6381  11358  10998  -1344   -161    651       C  
ATOM   1695  C   LYS A 513     -59.680 -59.067   5.660  1.00 77.47           C  
ANISOU 1695  C   LYS A 513     6355  11624  11455  -1360   -188   1131       C  
ATOM   1696  O   LYS A 513     -60.265 -59.038   4.593  1.00 79.74           O  
ANISOU 1696  O   LYS A 513     6481  12159  11655  -1612   -409   1444       O  
ATOM   1697  CB  LYS A 513     -59.944 -61.040   7.154  1.00 75.41           C  
ANISOU 1697  CB  LYS A 513     6325  11156  11169  -1212   -103    675       C  
ATOM   1698  CG  LYS A 513     -61.193 -61.643   6.545  1.00 78.79           C  
ANISOU 1698  CG  LYS A 513     6581  11737  11617  -1414   -310    965       C  
ATOM   1699  CD  LYS A 513     -62.019 -62.353   7.573  1.00 80.33           C  
ANISOU 1699  CD  LYS A 513     6756  11743  12023  -1266   -232    969       C  
ATOM   1700  CE  LYS A 513     -63.299 -62.833   6.951  1.00 87.01           C  
ANISOU 1700  CE  LYS A 513     7395  12735  12927  -1474   -449   1308       C  
ATOM   1701  NZ  LYS A 513     -64.292 -63.277   7.996  1.00 91.36           N1+
ANISOU 1701  NZ  LYS A 513     7864  13064  13783  -1295   -343   1417       N1+
ATOM   1702  N   HIS A 514     -59.550 -57.996   6.431  1.00 77.28           N  
ANISOU 1702  N   HIS A 514     6284  11350  11727  -1117     45   1199       N  
ATOM   1703  CA  HIS A 514     -60.156 -56.720   6.058  1.00 79.70           C  
ANISOU 1703  CA  HIS A 514     6305  11612  12362  -1095     85   1678       C  
ATOM   1704  C   HIS A 514     -59.323 -55.940   5.080  1.00 80.05           C  
ANISOU 1704  C   HIS A 514     6329  11830  12256  -1213     13   1738       C  
ATOM   1705  O   HIS A 514     -59.801 -54.959   4.494  1.00 82.89           O  
ANISOU 1705  O   HIS A 514     6414  12222  12858  -1256    -16   2201       O  
ATOM   1706  CB  HIS A 514     -60.469 -55.879   7.285  1.00 79.58           C  
ANISOU 1706  CB  HIS A 514     6239  11211  12785   -811    434   1721       C  
ATOM   1707  CG  HIS A 514     -61.579 -56.448   8.108  1.00 82.51           C  
ANISOU 1707  CG  HIS A 514     6547  11415  13388   -717    519   1813       C  
ATOM   1708  ND1 HIS A 514     -61.824 -56.062   9.406  1.00 84.29           N  
ANISOU 1708  ND1 HIS A 514     6826  11294  13906   -495    871   1710       N  
ATOM   1709  CD2 HIS A 514     -62.496 -57.402   7.815  1.00 84.23           C  
ANISOU 1709  CD2 HIS A 514     6665  11768  13569   -838    308   1982       C  
ATOM   1710  CE1 HIS A 514     -62.856 -56.743   9.870  1.00 85.77           C  
ANISOU 1710  CE1 HIS A 514     6938  11406  14245   -463    880   1831       C  
ATOM   1711  NE2 HIS A 514     -63.281 -57.561   8.924  1.00 84.99           N  
ANISOU 1711  NE2 HIS A 514     6735  11591  13965   -660    530   2005       N  
ATOM   1712  N   GLY A 515     -58.085 -56.379   4.890  1.00 77.29           N  
ANISOU 1712  N   GLY A 515     6243  11582  11541  -1267     -7   1305       N  
ATOM   1713  CA  GLY A 515     -57.225 -55.728   3.933  1.00 77.30           C  
ANISOU 1713  CA  GLY A 515     6246  11756  11365  -1392    -65   1328       C  
ATOM   1714  C   GLY A 515     -56.567 -54.503   4.503  1.00 75.97           C  
ANISOU 1714  C   GLY A 515     6070  11343  11450  -1167    180   1295       C  
ATOM   1715  O   GLY A 515     -56.237 -53.587   3.768  1.00 77.52           O  
ANISOU 1715  O   GLY A 515     6147  11624  11682  -1227    163   1507       O  
ATOM   1716  N   LEU A 516     -56.365 -54.498   5.816  1.00 74.04           N  
ANISOU 1716  N   LEU A 516     5960  10806  11364   -937    412   1027       N  
ATOM   1717  CA  LEU A 516     -55.547 -53.478   6.483  1.00 73.06           C  
ANISOU 1717  CA  LEU A 516     5908  10450  11402   -769    662    868       C  
ATOM   1718  C   LEU A 516     -54.125 -53.956   6.466  1.00 71.37           C  
ANISOU 1718  C   LEU A 516     5948  10322  10847   -802    618    437       C  
ATOM   1719  O   LEU A 516     -53.814 -55.011   7.003  1.00 69.74           O  
ANISOU 1719  O   LEU A 516     5920  10118  10458   -794    582    137       O  
ATOM   1720  CB  LEU A 516     -56.003 -53.249   7.928  1.00 72.50           C  
ANISOU 1720  CB  LEU A 516     5887  10046  11612   -576    942    771       C  
ATOM   1721  CG  LEU A 516     -57.390 -52.632   8.076  1.00 72.09           C  
ANISOU 1721  CG  LEU A 516     5557   9814  12017   -506   1086   1201       C  
ATOM   1722  CD1 LEU A 516     -57.909 -52.935   9.424  1.00 69.41           C  
ANISOU 1722  CD1 LEU A 516     5330   9219  11822   -377   1320   1031       C  
ATOM   1723  CD2 LEU A 516     -57.332 -51.150   7.850  1.00 73.56           C  
ANISOU 1723  CD2 LEU A 516     5551   9826  12572   -442   1296   1451       C  
ATOM   1724  N   GLU A 517     -53.269 -53.193   5.811  1.00 72.24           N  
ANISOU 1724  N   GLU A 517     6042  10497  10909   -842    624    445       N  
ATOM   1725  CA  GLU A 517     -51.915 -53.634   5.569  1.00 71.54           C  
ANISOU 1725  CA  GLU A 517     6147  10505  10529   -896    575     96       C  
ATOM   1726  C   GLU A 517     -51.175 -53.724   6.891  1.00 70.20           C  
ANISOU 1726  C   GLU A 517     6161  10117  10394   -747    725   -241       C  
ATOM   1727  O   GLU A 517     -51.441 -52.967   7.822  1.00 70.45           O  
ANISOU 1727  O   GLU A 517     6184   9925  10657   -628    913   -219       O  
ATOM   1728  CB  GLU A 517     -51.234 -52.649   4.634  1.00 72.74           C  
ANISOU 1728  CB  GLU A 517     6217  10749  10669   -959    576    223       C  
ATOM   1729  CG  GLU A 517     -49.975 -53.125   3.922  1.00 73.35           C  
ANISOU 1729  CG  GLU A 517     6440  10990  10439  -1076    506    -43       C  
ATOM   1730  CD  GLU A 517     -49.680 -52.276   2.676  1.00 76.69           C  
ANISOU 1730  CD  GLU A 517     6741  11593  10804  -1209    459    194       C  
ATOM   1731  OE1 GLU A 517     -50.600 -51.575   2.179  1.00 80.82           O  
ANISOU 1731  OE1 GLU A 517     7043  12185  11477  -1261    405    620       O  
ATOM   1732  OE2 GLU A 517     -48.539 -52.305   2.187  1.00 74.33           O1-
ANISOU 1732  OE2 GLU A 517     6544  11363  10332  -1268    477     -7       O1-
ATOM   1733  N   VAL A 518     -50.262 -54.678   6.968  1.00 69.77           N  
ANISOU 1733  N   VAL A 518     6265  10126  10117   -784    652   -541       N  
ATOM   1734  CA  VAL A 518     -49.432 -54.888   8.139  1.00 69.07           C  
ANISOU 1734  CA  VAL A 518     6329   9890  10025   -695    729   -815       C  
ATOM   1735  C   VAL A 518     -47.983 -54.956   7.662  1.00 69.82           C  
ANISOU 1735  C   VAL A 518     6486  10045   9994   -742    695  -1003       C  
ATOM   1736  O   VAL A 518     -47.671 -55.672   6.705  1.00 70.26           O  
ANISOU 1736  O   VAL A 518     6542  10248   9904   -845    611  -1057       O  
ATOM   1737  CB  VAL A 518     -49.839 -56.182   8.859  1.00 68.17           C  
ANISOU 1737  CB  VAL A 518     6289   9760   9849   -681    671   -927       C  
ATOM   1738  CG1 VAL A 518     -48.805 -56.579   9.895  1.00 66.67           C  
ANISOU 1738  CG1 VAL A 518     6232   9484   9614   -643    687  -1164       C  
ATOM   1739  CG2 VAL A 518     -51.227 -56.018   9.502  1.00 67.78           C  
ANISOU 1739  CG2 VAL A 518     6182   9610   9959   -618    747   -748       C  
ATOM   1740  N   ILE A 519     -47.106 -54.191   8.306  1.00 70.45           N  
ANISOU 1740  N   ILE A 519     6621  10005  10141   -688    782  -1107       N  
ATOM   1741  CA  ILE A 519     -45.695 -54.220   7.978  1.00 70.64           C  
ANISOU 1741  CA  ILE A 519     6680  10057  10099   -719    757  -1262       C  
ATOM   1742  C   ILE A 519     -45.001 -55.357   8.717  1.00 71.11           C  
ANISOU 1742  C   ILE A 519     6819  10086  10113   -716    693  -1447       C  
ATOM   1743  O   ILE A 519     -45.097 -55.479   9.940  1.00 70.75           O  
ANISOU 1743  O   ILE A 519     6839   9953  10089   -685    695  -1490       O  
ATOM   1744  CB  ILE A 519     -45.010 -52.912   8.377  1.00 70.98           C  
ANISOU 1744  CB  ILE A 519     6732   9985  10250   -689    861  -1278       C  
ATOM   1745  CG1 ILE A 519     -45.787 -51.704   7.840  1.00 70.77           C  
ANISOU 1745  CG1 ILE A 519     6589   9929  10370   -669    966  -1049       C  
ATOM   1746  CG2 ILE A 519     -43.513 -52.941   7.966  1.00 70.45           C  
ANISOU 1746  CG2 ILE A 519     6675   9948  10144   -722    826  -1407       C  
ATOM   1747  CD1 ILE A 519     -44.951 -50.457   7.699  1.00 70.36           C  
ANISOU 1747  CD1 ILE A 519     6507   9793  10432   -662   1070  -1052       C  
ATOM   1748  N   TYR A 520     -44.275 -56.165   7.957  1.00 72.89           N  
ANISOU 1748  N   TYR A 520     7028  10377  10290   -765    656  -1541       N  
ATOM   1749  CA  TYR A 520     -43.528 -57.316   8.470  1.00 74.15           C  
ANISOU 1749  CA  TYR A 520     7199  10480  10493   -759    618  -1668       C  
ATOM   1750  C   TYR A 520     -42.105 -56.957   8.907  1.00 75.28           C  
ANISOU 1750  C   TYR A 520     7326  10548  10727   -748    614  -1724       C  
ATOM   1751  O   TYR A 520     -41.187 -56.994   8.091  1.00 76.17           O  
ANISOU 1751  O   TYR A 520     7391  10663  10885   -774    663  -1780       O  
ATOM   1752  CB  TYR A 520     -43.468 -58.431   7.397  1.00 74.05           C  
ANISOU 1752  CB  TYR A 520     7162  10525  10449   -835    650  -1757       C  
ATOM   1753  CG  TYR A 520     -44.808 -59.041   7.051  1.00 74.40           C  
ANISOU 1753  CG  TYR A 520     7218  10652  10396   -890    620  -1711       C  
ATOM   1754  CD1 TYR A 520     -45.836 -59.120   8.003  1.00 73.53           C  
ANISOU 1754  CD1 TYR A 520     7118  10509  10308   -822    564  -1612       C  
ATOM   1755  CD2 TYR A 520     -45.049 -59.561   5.784  1.00 74.75           C  
ANISOU 1755  CD2 TYR A 520     7270  10814  10316  -1041    657  -1769       C  
ATOM   1756  CE1 TYR A 520     -47.067 -59.684   7.692  1.00 72.87           C  
ANISOU 1756  CE1 TYR A 520     7023  10496  10166   -874    526  -1544       C  
ATOM   1757  CE2 TYR A 520     -46.259 -60.135   5.468  1.00 74.89           C  
ANISOU 1757  CE2 TYR A 520     7293  10926  10234  -1132    604  -1716       C  
ATOM   1758  CZ  TYR A 520     -47.276 -60.189   6.425  1.00 74.47           C  
ANISOU 1758  CZ  TYR A 520     7221  10827  10246  -1033    528  -1588       C  
ATOM   1759  OH  TYR A 520     -48.494 -60.768   6.111  1.00 75.26           O  
ANISOU 1759  OH  TYR A 520     7303  11014  10274  -1125    465  -1510       O  
ATOM   1760  N   MET A 521     -41.903 -56.652  10.184  1.00 76.64           N  
ANISOU 1760  N   MET A 521     7539  10662  10919   -738    559  -1706       N  
ATOM   1761  CA  MET A 521     -40.554 -56.327  10.649  1.00 79.08           C  
ANISOU 1761  CA  MET A 521     7818  10925  11304   -771    513  -1725       C  
ATOM   1762  C   MET A 521     -39.794 -57.547  11.159  1.00 80.85           C  
ANISOU 1762  C   MET A 521     7954  11110  11652   -781    420  -1700       C  
ATOM   1763  O   MET A 521     -40.112 -58.089  12.207  1.00 81.09           O  
ANISOU 1763  O   MET A 521     8006  11145  11659   -804    329  -1642       O  
ATOM   1764  CB  MET A 521     -40.580 -55.193  11.652  1.00 79.07           C  
ANISOU 1764  CB  MET A 521     7909  10898  11234   -826    510  -1722       C  
ATOM   1765  CG  MET A 521     -41.098 -53.927  11.025  1.00 80.46           C  
ANISOU 1765  CG  MET A 521     8111  11057  11404   -802    645  -1718       C  
ATOM   1766  SD  MET A 521     -41.211 -52.555  12.179  1.00 85.60           S  
ANISOU 1766  SD  MET A 521     8884  11613  12027   -887    743  -1769       S  
ATOM   1767  CE  MET A 521     -42.042 -51.290  11.186  1.00 83.90           C  
ANISOU 1767  CE  MET A 521     8611  11333  11931   -809    943  -1687       C  
ATOM   1768  N   ILE A 522     -38.786 -57.969  10.393  1.00 83.09           N  
ANISOU 1768  N   ILE A 522     8123  11343  12101   -770    467  -1722       N  
ATOM   1769  CA  ILE A 522     -38.160 -59.279  10.585  1.00 85.61           C  
ANISOU 1769  CA  ILE A 522     8304  11575  12648   -756    450  -1675       C  
ATOM   1770  C   ILE A 522     -36.663 -59.262  10.869  1.00 88.25           C  
ANISOU 1770  C   ILE A 522     8482  11829  13217   -780    396  -1575       C  
ATOM   1771  O   ILE A 522     -36.038 -60.318  10.967  1.00 89.90           O  
ANISOU 1771  O   ILE A 522     8520  11928  13709   -759    410  -1489       O  
ATOM   1772  CB  ILE A 522     -38.449 -60.209   9.408  1.00 85.61           C  
ANISOU 1772  CB  ILE A 522     8275  11528  12723   -734    624  -1794       C  
ATOM   1773  CG1 ILE A 522     -37.880 -59.641   8.110  1.00 85.75           C  
ANISOU 1773  CG1 ILE A 522     8297  11549  12732   -762    780  -1901       C  
ATOM   1774  CG2 ILE A 522     -39.941 -60.397   9.274  1.00 85.96           C  
ANISOU 1774  CG2 ILE A 522     8437  11662  12560   -738    624  -1837       C  
ATOM   1775  CD1 ILE A 522     -38.135 -60.505   6.872  1.00 85.39           C  
ANISOU 1775  CD1 ILE A 522     8267  11482  12692   -818    986  -2062       C  
ATOM   1776  N   GLU A 523     -36.097 -58.063  10.993  1.00 89.80           N  
ANISOU 1776  N   GLU A 523     8713  12064  13341   -826    348  -1566       N  
ATOM   1777  CA  GLU A 523     -34.737 -57.871  11.472  1.00 92.30           C  
ANISOU 1777  CA  GLU A 523     8885  12335  13848   -885    240  -1431       C  
ATOM   1778  C   GLU A 523     -34.788 -57.424  12.937  1.00 93.49           C  
ANISOU 1778  C   GLU A 523     9106  12589  13826  -1025     14  -1321       C  
ATOM   1779  O   GLU A 523     -35.720 -56.699  13.327  1.00 92.96           O  
ANISOU 1779  O   GLU A 523     9239  12600  13482  -1067     23  -1422       O  
ATOM   1780  CB  GLU A 523     -34.062 -56.802  10.633  1.00 92.53           C  
ANISOU 1780  CB  GLU A 523     8917  12345  13893   -881    338  -1506       C  
ATOM   1781  CG  GLU A 523     -33.545 -57.275   9.269  1.00 96.12           C  
ANISOU 1781  CG  GLU A 523     9271  12694  14554   -804    563  -1584       C  
ATOM   1782  CD  GLU A 523     -33.510 -56.140   8.232  1.00100.19           C  
ANISOU 1782  CD  GLU A 523     9872  13253  14940   -800    693  -1695       C  
ATOM   1783  OE1 GLU A 523     -32.682 -55.181   8.388  1.00101.17           O  
ANISOU 1783  OE1 GLU A 523     9956  13366  15117   -832    642  -1643       O  
ATOM   1784  OE2 GLU A 523     -34.336 -56.210   7.273  1.00101.07           O1-
ANISOU 1784  OE2 GLU A 523    10082  13425  14892   -786    832  -1812       O1-
ATOM   1785  N   PRO A 524     -33.800 -57.858  13.766  1.00 95.90           N  
ANISOU 1785  N   PRO A 524     9241  12894  14301  -1125   -175  -1099       N  
ATOM   1786  CA  PRO A 524     -33.687 -57.414  15.168  1.00 97.12           C  
ANISOU 1786  CA  PRO A 524     9471  13190  14240  -1343   -413   -982       C  
ATOM   1787  C   PRO A 524     -33.609 -55.902  15.359  1.00 97.20           C  
ANISOU 1787  C   PRO A 524     9666  13260  14003  -1474   -404  -1130       C  
ATOM   1788  O   PRO A 524     -34.233 -55.390  16.271  1.00 97.60           O  
ANISOU 1788  O   PRO A 524     9919  13410  13755  -1630   -448  -1201       O  
ATOM   1789  CB  PRO A 524     -32.395 -58.079  15.641  1.00 99.39           C  
ANISOU 1789  CB  PRO A 524     9469  13460  14834  -1431   -615   -665       C  
ATOM   1790  CG  PRO A 524     -32.301 -59.310  14.835  1.00 99.19           C  
ANISOU 1790  CG  PRO A 524     9234  13261  15193  -1229   -459   -608       C  
ATOM   1791  CD  PRO A 524     -32.818 -58.923  13.470  1.00 97.60           C  
ANISOU 1791  CD  PRO A 524     9166  12974  14943  -1063   -166   -915       C  
ATOM   1792  N   ILE A 525     -32.883 -55.195  14.501  1.00 97.33           N  
ANISOU 1792  N   ILE A 525     9622  13200  14158  -1419   -310  -1190       N  
ATOM   1793  CA  ILE A 525     -32.737 -53.744  14.616  1.00 98.58           C  
ANISOU 1793  CA  ILE A 525     9927  13380  14148  -1536   -274  -1326       C  
ATOM   1794  C   ILE A 525     -34.089 -53.044  14.657  1.00 97.81           C  
ANISOU 1794  C   ILE A 525    10078  13288  13797  -1511    -98  -1536       C  
ATOM   1795  O   ILE A 525     -34.225 -51.946  15.196  1.00 98.64           O  
ANISOU 1795  O   ILE A 525    10342  13400  13733  -1663    -52  -1655       O  
ATOM   1796  CB  ILE A 525     -31.928 -53.142  13.446  1.00 98.42           C  
ANISOU 1796  CB  ILE A 525     9794  13255  14343  -1426   -147  -1363       C  
ATOM   1797  CG1 ILE A 525     -30.811 -54.095  12.990  1.00101.23           C  
ANISOU 1797  CG1 ILE A 525     9868  13531  15062  -1352   -196  -1170       C  
ATOM   1798  CG2 ILE A 525     -31.307 -51.797  13.858  1.00 99.03           C  
ANISOU 1798  CG2 ILE A 525     9943  13348  14335  -1608   -192  -1415       C  
ATOM   1799  CD1 ILE A 525     -31.257 -55.346  12.150  1.00101.04           C  
ANISOU 1799  CD1 ILE A 525     9758  13421  15212  -1153    -34  -1184       C  
ATOM   1800  N   ASP A 526     -35.095 -53.699  14.091  1.00 97.01           N  
ANISOU 1800  N   ASP A 526     9993  13163  13702  -1335     19  -1575       N  
ATOM   1801  CA  ASP A 526     -36.435 -53.142  14.002  1.00 96.28           C  
ANISOU 1801  CA  ASP A 526    10074  13055  13452  -1281    193  -1711       C  
ATOM   1802  C   ASP A 526     -37.074 -52.938  15.368  1.00 97.47           C  
ANISOU 1802  C   ASP A 526    10408  13255  13370  -1456    165  -1758       C  
ATOM   1803  O   ASP A 526     -37.888 -52.029  15.545  1.00 97.50           O  
ANISOU 1803  O   ASP A 526    10563  13202  13278  -1482    349  -1888       O  
ATOM   1804  CB  ASP A 526     -37.299 -54.017  13.099  1.00 94.74           C  
ANISOU 1804  CB  ASP A 526     9830  12849  13317  -1093    280  -1703       C  
ATOM   1805  CG  ASP A 526     -36.995 -53.797  11.624  1.00 95.04           C  
ANISOU 1805  CG  ASP A 526     9773  12851  13486   -973    400  -1725       C  
ATOM   1806  OD1 ASP A 526     -37.023 -52.606  11.199  1.00 95.16           O  
ANISOU 1806  OD1 ASP A 526     9826  12840  13489   -972    506  -1768       O  
ATOM   1807  OD2 ASP A 526     -36.744 -54.801  10.898  1.00 94.90           O1-
ANISOU 1807  OD2 ASP A 526     9646  12823  13586   -899    412  -1702       O1-
ATOM   1808  N   GLU A 527     -36.689 -53.781  16.326  1.00 98.86           N  
ANISOU 1808  N   GLU A 527    10554  13528  13477  -1592    -43  -1635       N  
ATOM   1809  CA  GLU A 527     -37.201 -53.702  17.687  1.00100.50           C  
ANISOU 1809  CA  GLU A 527    10949  13823  13413  -1815    -86  -1667       C  
ATOM   1810  C   GLU A 527     -36.656 -52.446  18.335  1.00102.09           C  
ANISOU 1810  C   GLU A 527    11297  14039  13451  -2083    -65  -1791       C  
ATOM   1811  O   GLU A 527     -37.363 -51.745  19.053  1.00103.55           O  
ANISOU 1811  O   GLU A 527    11711  14205  13427  -2239    100  -1965       O  
ATOM   1812  CB  GLU A 527     -36.813 -54.954  18.482  1.00101.85           C  
ANISOU 1812  CB  GLU A 527    11011  14122  13564  -1917   -351  -1438       C  
ATOM   1813  CG  GLU A 527     -37.611 -55.173  19.786  1.00105.59           C  
ANISOU 1813  CG  GLU A 527    11677  14709  13732  -2120   -380  -1446       C  
ATOM   1814  CD  GLU A 527     -39.125 -55.408  19.570  1.00106.18           C  
ANISOU 1814  CD  GLU A 527    11860  14699  13782  -1932   -153  -1563       C  
ATOM   1815  OE1 GLU A 527     -39.513 -56.456  18.981  1.00104.25           O  
ANISOU 1815  OE1 GLU A 527    11469  14418  13720  -1710   -172  -1461       O  
ATOM   1816  OE2 GLU A 527     -39.914 -54.536  20.017  1.00106.38           O1-
ANISOU 1816  OE2 GLU A 527    12110  14679  13628  -2026     61  -1755       O1-
ATOM   1817  N   TYR A 528     -35.396 -52.161  18.039  1.00102.46           N  
ANISOU 1817  N   TYR A 528    11208  14097  13623  -2141   -199  -1714       N  
ATOM   1818  CA  TYR A 528     -34.698 -50.988  18.524  1.00104.06           C  
ANISOU 1818  CA  TYR A 528    11518  14311  13709  -2407   -201  -1823       C  
ATOM   1819  C   TYR A 528     -35.183 -49.762  17.772  1.00102.50           C  
ANISOU 1819  C   TYR A 528    11407  13932  13605  -2278    120  -2043       C  
ATOM   1820  O   TYR A 528     -35.184 -48.657  18.293  1.00104.18           O  
ANISOU 1820  O   TYR A 528    11794  14092  13698  -2491    263  -2230       O  
ATOM   1821  CB  TYR A 528     -33.213 -51.199  18.268  1.00105.20           C  
ANISOU 1821  CB  TYR A 528    11425  14504  14043  -2455   -451  -1616       C  
ATOM   1822  CG  TYR A 528     -32.267 -50.160  18.822  1.00108.82           C  
ANISOU 1822  CG  TYR A 528    11946  15007  14391  -2776   -540  -1669       C  
ATOM   1823  CD1 TYR A 528     -32.033 -50.059  20.197  1.00112.47           C  
ANISOU 1823  CD1 TYR A 528    12558  15655  14520  -3205   -730  -1650       C  
ATOM   1824  CD2 TYR A 528     -31.551 -49.321  17.965  1.00108.84           C  
ANISOU 1824  CD2 TYR A 528    11853  14888  14613  -2685   -451  -1721       C  
ATOM   1825  CE1 TYR A 528     -31.130 -49.125  20.705  1.00115.69           C  
ANISOU 1825  CE1 TYR A 528    13031  16123  14803  -3556   -830  -1705       C  
ATOM   1826  CE2 TYR A 528     -30.644 -48.390  18.463  1.00111.84           C  
ANISOU 1826  CE2 TYR A 528    12276  15303  14913  -2993   -542  -1765       C  
ATOM   1827  CZ  TYR A 528     -30.439 -48.295  19.833  1.00115.40           C  
ANISOU 1827  CZ  TYR A 528    12886  15939  15021  -3438   -734  -1765       C  
ATOM   1828  OH  TYR A 528     -29.546 -47.364  20.333  1.00118.70           O  
ANISOU 1828  OH  TYR A 528    13363  16407  15329  -3798   -832  -1825       O  
ATOM   1829  N   CYS A 529     -35.608 -49.971  16.538  1.00 99.63           N  
ANISOU 1829  N   CYS A 529    10916  13473  13465  -1952    244  -2009       N  
ATOM   1830  CA  CYS A 529     -35.914 -48.868  15.649  1.00 98.25           C  
ANISOU 1830  CA  CYS A 529    10744  13146  13438  -1817    501  -2117       C  
ATOM   1831  C   CYS A 529     -37.288 -48.254  15.914  1.00 98.48           C  
ANISOU 1831  C   CYS A 529    10936  13061  13419  -1797    789  -2255       C  
ATOM   1832  O   CYS A 529     -37.401 -47.043  16.071  1.00 99.53           O  
ANISOU 1832  O   CYS A 529    11161  13056  13596  -1888   1015  -2398       O  
ATOM   1833  CB  CYS A 529     -35.787 -49.323  14.199  1.00 95.80           C  
ANISOU 1833  CB  CYS A 529    10233  12818  13347  -1536    505  -1997       C  
ATOM   1834  SG  CYS A 529     -36.233 -48.064  13.048  1.00 93.85           S  
ANISOU 1834  SG  CYS A 529     9953  12433  13273  -1383    780  -2040       S  
ATOM   1835  N   VAL A 530     -38.323 -49.096  15.955  1.00 97.71           N  
ANISOU 1835  N   VAL A 530    10853  12993  13277  -1677    804  -2202       N  
ATOM   1836  CA  VAL A 530     -39.694 -48.635  16.190  1.00 98.15           C  
ANISOU 1836  CA  VAL A 530    11022  12922  13346  -1635   1086  -2285       C  
ATOM   1837  C   VAL A 530     -39.858 -48.061  17.582  1.00100.89           C  
ANISOU 1837  C   VAL A 530    11613  13225  13494  -1930   1226  -2482       C  
ATOM   1838  O   VAL A 530     -40.848 -47.380  17.862  1.00102.10           O  
ANISOU 1838  O   VAL A 530    11872  13205  13713  -1936   1552  -2596       O  
ATOM   1839  CB  VAL A 530     -40.766 -49.738  16.000  1.00 96.62           C  
ANISOU 1839  CB  VAL A 530    10786  12779  13145  -1465   1051  -2172       C  
ATOM   1840  CG1 VAL A 530     -41.022 -49.993  14.531  1.00 94.42           C  
ANISOU 1840  CG1 VAL A 530    10313  12503  13056  -1214   1037  -2026       C  
ATOM   1841  CG2 VAL A 530     -40.417 -51.010  16.775  1.00 96.40           C  
ANISOU 1841  CG2 VAL A 530    10781  12918  12927  -1563    786  -2112       C  
ATOM   1842  N   GLN A 531     -38.894 -48.347  18.453  1.00102.38           N  
ANISOU 1842  N   GLN A 531    11881  13568  13448  -2198    995  -2507       N  
ATOM   1843  CA  GLN A 531     -38.826 -47.682  19.740  1.00105.54           C  
ANISOU 1843  CA  GLN A 531    12540  13966  13593  -2574   1113  -2721       C  
ATOM   1844  C   GLN A 531     -38.793 -46.154  19.549  1.00106.45           C  
ANISOU 1844  C   GLN A 531    12728  13848  13867  -2641   1455  -2931       C  
ATOM   1845  O   GLN A 531     -39.185 -45.419  20.451  1.00109.29           O  
ANISOU 1845  O   GLN A 531    13327  14098  14100  -2905   1740  -3177       O  
ATOM   1846  CB  GLN A 531     -37.614 -48.174  20.542  1.00107.40           C  
ANISOU 1846  CB  GLN A 531    12796  14446  13562  -2887    739  -2642       C  
ATOM   1847  CG  GLN A 531     -37.579 -47.696  22.003  1.00112.83           C  
ANISOU 1847  CG  GLN A 531    13789  15215  13864  -3373    806  -2850       C  
ATOM   1848  CD  GLN A 531     -36.158 -47.415  22.521  1.00117.24           C  
ANISOU 1848  CD  GLN A 531    14356  15952  14238  -3746    513  -2817       C  
ATOM   1849  OE1 GLN A 531     -35.250 -48.243  22.371  1.00117.72           O  
ANISOU 1849  OE1 GLN A 531    14199  16195  14334  -3723    114  -2527       O  
ATOM   1850  NE2 GLN A 531     -35.969 -46.246  23.146  1.00119.76           N  
ANISOU 1850  NE2 GLN A 531    14913  16201  14386  -4108    728  -3108       N  
ATOM   1851  N   GLN A 532     -38.362 -45.689  18.371  1.00104.41           N  
ANISOU 1851  N   GLN A 532    12267  13500  13902  -2411   1461  -2839       N  
ATOM   1852  CA  GLN A 532     -38.207 -44.248  18.100  1.00105.31           C  
ANISOU 1852  CA  GLN A 532    12398  13385  14227  -2456   1765  -2991       C  
ATOM   1853  C   GLN A 532     -39.004 -43.720  16.908  1.00103.30           C  
ANISOU 1853  C   GLN A 532    11957  12926  14365  -2112   2019  -2871       C  
ATOM   1854  O   GLN A 532     -39.307 -42.529  16.854  1.00104.99           O  
ANISOU 1854  O   GLN A 532    12189  12887  14813  -2135   2376  -2985       O  
ATOM   1855  CB  GLN A 532     -36.728 -43.854  17.951  1.00106.05           C  
ANISOU 1855  CB  GLN A 532    12429  13557  14308  -2604   1551  -2989       C  
ATOM   1856  CG  GLN A 532     -35.936 -43.831  19.249  1.00109.92           C  
ANISOU 1856  CG  GLN A 532    13123  14197  14441  -3062   1385  -3135       C  
ATOM   1857  CD  GLN A 532     -36.443 -42.781  20.228  1.00115.54           C  
ANISOU 1857  CD  GLN A 532    14130  14735  15034  -3391   1779  -3480       C  
ATOM   1858  OE1 GLN A 532     -36.305 -41.574  19.998  1.00118.04           O  
ANISOU 1858  OE1 GLN A 532    14466  14821  15563  -3438   2074  -3647       O  
ATOM   1859  NE2 GLN A 532     -37.034 -43.237  21.333  1.00117.64           N  
ANISOU 1859  NE2 GLN A 532    14628  15096  14971  -3636   1817  -3596       N  
ATOM   1860  N   LEU A 533     -39.328 -44.584  15.950  1.00100.09           N  
ANISOU 1860  N   LEU A 533    11360  12627  14041  -1822   1842  -2629       N  
ATOM   1861  CA  LEU A 533     -40.207 -44.186  14.846  1.00 98.69           C  
ANISOU 1861  CA  LEU A 533    10999  12314  14183  -1545   2036  -2458       C  
ATOM   1862  C   LEU A 533     -41.646 -44.247  15.359  1.00 99.41           C  
ANISOU 1862  C   LEU A 533    11162  12274  14334  -1510   2292  -2473       C  
ATOM   1863  O   LEU A 533     -42.330 -45.265  15.230  1.00 98.07           O  
ANISOU 1863  O   LEU A 533    10955  12222  14084  -1389   2157  -2346       O  
ATOM   1864  CB  LEU A 533     -40.000 -45.069  13.594  1.00 95.86           C  
ANISOU 1864  CB  LEU A 533    10434  12142  13844  -1318   1761  -2215       C  
ATOM   1865  CG  LEU A 533     -40.795 -44.739  12.315  1.00 93.90           C  
ANISOU 1865  CG  LEU A 533     9978  11840  13856  -1089   1875  -1979       C  
ATOM   1866  CD1 LEU A 533     -40.551 -43.338  11.786  1.00 94.18           C  
ANISOU 1866  CD1 LEU A 533     9906  11694  14183  -1068   2100  -1936       C  
ATOM   1867  CD2 LEU A 533     -40.524 -45.754  11.234  1.00 90.78           C  
ANISOU 1867  CD2 LEU A 533     9454  11666  13370   -963   1607  -1813       C  
ATOM   1868  N   LYS A 534     -42.082 -43.153  15.975  1.00101.80           N  
ANISOU 1868  N   LYS A 534    11569  12308  14800  -1630   2690  -2642       N  
ATOM   1869  CA  LYS A 534     -43.359 -43.107  16.674  1.00102.80           C  
ANISOU 1869  CA  LYS A 534    11792  12258  15006  -1646   3011  -2705       C  
ATOM   1870  C   LYS A 534     -44.519 -43.001  15.698  1.00101.96           C  
ANISOU 1870  C   LYS A 534    11424  12025  15290  -1347   3151  -2398       C  
ATOM   1871  O   LYS A 534     -45.549 -43.646  15.882  1.00101.69           O  
ANISOU 1871  O   LYS A 534    11379  11994  15261  -1261   3183  -2302       O  
ATOM   1872  CB  LYS A 534     -43.378 -41.951  17.677  1.00106.44           C  
ANISOU 1872  CB  LYS A 534    12464  12437  15539  -1914   3457  -3027       C  
ATOM   1873  CG  LYS A 534     -42.411 -42.117  18.864  1.00109.10           C  
ANISOU 1873  CG  LYS A 534    13107  12938  15408  -2309   3317  -3335       C  
ATOM   1874  CD  LYS A 534     -42.755 -43.341  19.739  1.00110.75           C  
ANISOU 1874  CD  LYS A 534    13485  13378  15217  -2424   3111  -3357       C  
ATOM   1875  CE  LYS A 534     -43.847 -43.008  20.762  1.00114.92           C  
ANISOU 1875  CE  LYS A 534    14235  13681  15747  -2588   3583  -3579       C  
ATOM   1876  NZ  LYS A 534     -44.725 -44.171  21.103  1.00113.88           N1+
ANISOU 1876  NZ  LYS A 534    14127  13682  15458  -2495   3470  -3457       N1+
ATOM   1877  N   GLU A 535     -44.341 -42.196  14.656  1.00102.05           N  
ANISOU 1877  N   GLU A 535    11208  11940  15625  -1207   3215  -2212       N  
ATOM   1878  CA  GLU A 535     -45.349 -42.026  13.605  1.00102.09           C  
ANISOU 1878  CA  GLU A 535    10915  11870  16003   -960   3291  -1836       C  
ATOM   1879  C   GLU A 535     -44.711 -41.577  12.290  1.00100.49           C  
ANISOU 1879  C   GLU A 535    10479  11757  15946   -846   3133  -1597       C  
ATOM   1880  O   GLU A 535     -43.572 -41.144  12.276  1.00101.03           O  
ANISOU 1880  O   GLU A 535    10608  11845  15931   -940   3078  -1750       O  
ATOM   1881  CB  GLU A 535     -46.458 -41.062  14.045  1.00105.40           C  
ANISOU 1881  CB  GLU A 535    11271  11888  16886   -938   3819  -1810       C  
ATOM   1882  CG  GLU A 535     -45.977 -39.706  14.480  1.00111.70           C  
ANISOU 1882  CG  GLU A 535    12132  12367  17942  -1075   4221  -2035       C  
ATOM   1883  CD  GLU A 535     -46.230 -38.630  13.432  1.00117.47           C  
ANISOU 1883  CD  GLU A 535    12513  12879  19241   -899   4424  -1696       C  
ATOM   1884  OE1 GLU A 535     -47.349 -38.043  13.498  1.00120.82           O  
ANISOU 1884  OE1 GLU A 535    12765  12972  20169   -806   4834  -1522       O  
ATOM   1885  OE2 GLU A 535     -45.318 -38.370  12.578  1.00115.72           O1-
ANISOU 1885  OE2 GLU A 535    12175  12803  18987   -861   4192  -1585       O1-
ATOM   1886  N   PHE A 536     -45.449 -41.709  11.193  1.00 98.96           N  
ANISOU 1886  N   PHE A 536    10018  11635  15946   -672   3048  -1208       N  
ATOM   1887  CA  PHE A 536     -44.995 -41.316   9.879  1.00 97.40           C  
ANISOU 1887  CA  PHE A 536     9591  11555  15860   -590   2903   -932       C  
ATOM   1888  C   PHE A 536     -46.148 -40.651   9.178  1.00 99.08           C  
ANISOU 1888  C   PHE A 536     9487  11618  16540   -463   3091   -500       C  
ATOM   1889  O   PHE A 536     -47.242 -41.181   9.160  1.00 99.03           O  
ANISOU 1889  O   PHE A 536     9398  11637  16591   -404   3071   -307       O  
ATOM   1890  CB  PHE A 536     -44.557 -42.534   9.077  1.00 94.46           C  
ANISOU 1890  CB  PHE A 536     9226  11569  15092   -575   2467   -862       C  
ATOM   1891  CG  PHE A 536     -44.021 -42.202   7.697  1.00 93.91           C  
ANISOU 1891  CG  PHE A 536     8961  11659  15060   -537   2323   -608       C  
ATOM   1892  CD1 PHE A 536     -42.650 -42.101   7.467  1.00 93.04           C  
ANISOU 1892  CD1 PHE A 536     8924  11635  14792   -591   2210   -776       C  
ATOM   1893  CD2 PHE A 536     -44.882 -42.008   6.624  1.00 93.55           C  
ANISOU 1893  CD2 PHE A 536     8649  11694  15199   -472   2289   -175       C  
ATOM   1894  CE1 PHE A 536     -42.157 -41.802   6.190  1.00 92.04           C  
ANISOU 1894  CE1 PHE A 536     8629  11657  14682   -570   2105   -548       C  
ATOM   1895  CE2 PHE A 536     -44.398 -41.713   5.354  1.00 92.15           C  
ANISOU 1895  CE2 PHE A 536     8308  11700  15002   -483   2152     69       C  
ATOM   1896  CZ  PHE A 536     -43.040 -41.606   5.137  1.00 91.78           C  
ANISOU 1896  CZ  PHE A 536     8357  11724  14789   -526   2078   -133       C  
ATOM   1897  N   GLU A 537     -45.890 -39.481   8.600  1.00101.00           N  
ANISOU 1897  N   GLU A 537     9526  11701  17148   -427   3267   -313       N  
ATOM   1898  CA  GLU A 537     -46.861 -38.743   7.783  1.00103.10           C  
ANISOU 1898  CA  GLU A 537     9412  11836  17924   -313   3417    204       C  
ATOM   1899  C   GLU A 537     -48.143 -38.481   8.551  1.00104.43           C  
ANISOU 1899  C   GLU A 537     9504  11669  18504   -259   3785    278       C  
ATOM   1900  O   GLU A 537     -49.236 -38.567   7.995  1.00105.51           O  
ANISOU 1900  O   GLU A 537     9357  11818  18911   -172   3760    733       O  
ATOM   1901  CB  GLU A 537     -47.181 -39.531   6.516  1.00102.55           C  
ANISOU 1901  CB  GLU A 537     9167  12170  17626   -291   3002    600       C  
ATOM   1902  CG  GLU A 537     -46.960 -38.794   5.206  1.00106.40           C  
ANISOU 1902  CG  GLU A 537     9349  12767  18312   -276   2917   1040       C  
ATOM   1903  CD  GLU A 537     -47.498 -39.587   4.014  1.00109.28           C  
ANISOU 1903  CD  GLU A 537     9554  13544  18422   -327   2532   1447       C  
ATOM   1904  OE1 GLU A 537     -46.769 -39.713   3.000  1.00108.53           O  
ANISOU 1904  OE1 GLU A 537     9440  13748  18045   -407   2287   1540       O  
ATOM   1905  OE2 GLU A 537     -48.656 -40.083   4.102  1.00111.67           O1-
ANISOU 1905  OE2 GLU A 537     9759  13869  18799   -313   2489   1663       O1-
ATOM   1906  N   GLY A 538     -47.995 -38.188   9.838  1.00104.57           N  
ANISOU 1906  N   GLY A 538     9781  11397  18552   -341   4126   -166       N  
ATOM   1907  CA  GLY A 538     -49.125 -37.877  10.709  1.00106.25           C  
ANISOU 1907  CA  GLY A 538     9972  11232  19163   -318   4576   -186       C  
ATOM   1908  C   GLY A 538     -49.909 -39.055  11.236  1.00104.23           C  
ANISOU 1908  C   GLY A 538     9856  11121  18626   -316   4437   -244       C  
ATOM   1909  O   GLY A 538     -50.914 -38.861  11.904  1.00106.65           O  
ANISOU 1909  O   GLY A 538    10127  11121  19273   -288   4812   -227       O  
ATOM   1910  N   LYS A 539     -49.456 -40.270  10.941  1.00100.47           N  
ANISOU 1910  N   LYS A 539     9526  11079  17566   -347   3933   -312       N  
ATOM   1911  CA  LYS A 539     -50.194 -41.493  11.281  1.00 98.68           C  
ANISOU 1911  CA  LYS A 539     9395  11026  17073   -335   3745   -315       C  
ATOM   1912  C   LYS A 539     -49.344 -42.304  12.244  1.00 96.17           C  
ANISOU 1912  C   LYS A 539     9477  10870  16193   -481   3590   -810       C  
ATOM   1913  O   LYS A 539     -48.195 -42.598  11.929  1.00 94.37           O  
ANISOU 1913  O   LYS A 539     9354  10882  15619   -541   3294   -951       O  
ATOM   1914  CB  LYS A 539     -50.449 -42.350  10.031  1.00 96.89           C  
ANISOU 1914  CB  LYS A 539     8971  11183  16659   -270   3277     65       C  
ATOM   1915  CG  LYS A 539     -50.812 -41.613   8.752  1.00 99.57           C  
ANISOU 1915  CG  LYS A 539     8913  11537  17380   -196   3241    602       C  
ATOM   1916  CD  LYS A 539     -52.308 -41.604   8.539  1.00105.05           C  
ANISOU 1916  CD  LYS A 539     9301  12116  18496   -111   3339   1067       C  
ATOM   1917  CE  LYS A 539     -52.689 -41.110   7.136  1.00108.65           C  
ANISOU 1917  CE  LYS A 539     9335  12711  19234    -89   3166   1698       C  
ATOM   1918  NZ  LYS A 539     -54.192 -41.092   6.962  1.00112.36           N1+
ANISOU 1918  NZ  LYS A 539     9456  13064  20170    -23   3243   2223       N1+
ATOM   1919  N   THR A 540     -49.882 -42.689  13.401  1.00 95.99           N  
ANISOU 1919  N   THR A 540     9660  10726  16085   -548   3782  -1044       N  
ATOM   1920  CA  THR A 540     -49.038 -43.392  14.374  1.00 94.04           C  
ANISOU 1920  CA  THR A 540     9772  10646  15310   -726   3625  -1465       C  
ATOM   1921  C   THR A 540     -48.849 -44.858  14.026  1.00 90.76           C  
ANISOU 1921  C   THR A 540     9391  10617  14476   -692   3131  -1403       C  
ATOM   1922  O   THR A 540     -49.752 -45.479  13.472  1.00 90.05           O  
ANISOU 1922  O   THR A 540     9134  10613  14468   -567   3006  -1125       O  
ATOM   1923  CB  THR A 540     -49.539 -43.253  15.792  1.00 95.73           C  
ANISOU 1923  CB  THR A 540    10234  10625  15513   -873   4008  -1766       C  
ATOM   1924  OG1 THR A 540     -50.869 -43.761  15.865  1.00 96.86           O  
ANISOU 1924  OG1 THR A 540    10264  10694  15844   -750   4107  -1554       O  
ATOM   1925  CG2 THR A 540     -49.541 -41.814  16.184  1.00 98.93           C  
ANISOU 1925  CG2 THR A 540    10650  10627  16310   -957   4541  -1917       C  
ATOM   1926  N   LEU A 541     -47.657 -45.385  14.314  1.00 88.90           N  
ANISOU 1926  N   LEU A 541     9348  10598  13832   -814   2860  -1641       N  
ATOM   1927  CA  LEU A 541     -47.358 -46.803  14.127  1.00 85.95           C  
ANISOU 1927  CA  LEU A 541     9015  10537  13103   -799   2449  -1623       C  
ATOM   1928  C   LEU A 541     -47.829 -47.580  15.350  1.00 86.60           C  
ANISOU 1928  C   LEU A 541     9300  10628  12974   -892   2481  -1785       C  
ATOM   1929  O   LEU A 541     -47.604 -47.141  16.479  1.00 88.44           O  
ANISOU 1929  O   LEU A 541     9749  10744  13107  -1073   2689  -2040       O  
ATOM   1930  CB  LEU A 541     -45.858 -47.031  13.907  1.00 84.21           C  
ANISOU 1930  CB  LEU A 541     8860  10509  12626   -881   2171  -1753       C  
ATOM   1931  CG  LEU A 541     -45.252 -47.009  12.497  1.00 81.79           C  
ANISOU 1931  CG  LEU A 541     8363  10346  12366   -781   1968  -1573       C  
ATOM   1932  CD1 LEU A 541     -45.197 -45.607  11.938  1.00 83.76           C  
ANISOU 1932  CD1 LEU A 541     8476  10415  12931   -746   2197  -1472       C  
ATOM   1933  CD2 LEU A 541     -43.866 -47.596  12.505  1.00 78.72           C  
ANISOU 1933  CD2 LEU A 541     8052  10135  11721   -861   1702  -1713       C  
ATOM   1934  N   VAL A 542     -48.499 -48.713  15.127  1.00 85.45           N  
ANISOU 1934  N   VAL A 542     9091  10624  12750   -797   2288  -1638       N  
ATOM   1935  CA  VAL A 542     -48.952 -49.577  16.225  1.00 85.85           C  
ANISOU 1935  CA  VAL A 542     9312  10708  12598   -872   2285  -1751       C  
ATOM   1936  C   VAL A 542     -48.571 -51.037  16.022  1.00 84.08           C  
ANISOU 1936  C   VAL A 542     9080  10753  12112   -849   1893  -1708       C  
ATOM   1937  O   VAL A 542     -48.664 -51.569  14.911  1.00 83.28           O  
ANISOU 1937  O   VAL A 542     8807  10772  12062   -727   1695  -1534       O  
ATOM   1938  CB  VAL A 542     -50.471 -49.433  16.550  1.00 87.09           C  
ANISOU 1938  CB  VAL A 542     9415  10657  13016   -793   2588  -1635       C  
ATOM   1939  CG1 VAL A 542     -50.790 -48.003  16.965  1.00 90.23           C  
ANISOU 1939  CG1 VAL A 542     9838  10723  13722   -842   3064  -1722       C  
ATOM   1940  CG2 VAL A 542     -51.322 -49.834  15.396  1.00 85.57           C  
ANISOU 1940  CG2 VAL A 542     8951  10521  13037   -606   2452  -1298       C  
ATOM   1941  N   SER A 543     -48.113 -51.668  17.103  1.00 84.36           N  
ANISOU 1941  N   SER A 543     9299  10880  11871   -996   1797  -1864       N  
ATOM   1942  CA  SER A 543     -47.686 -53.058  17.089  1.00 82.82           C  
ANISOU 1942  CA  SER A 543     9082  10897  11487   -986   1466  -1814       C  
ATOM   1943  C   SER A 543     -48.917 -53.929  17.114  1.00 82.41           C  
ANISOU 1943  C   SER A 543     8975  10842  11494   -878   1472  -1688       C  
ATOM   1944  O   SER A 543     -49.855 -53.631  17.838  1.00 84.34           O  
ANISOU 1944  O   SER A 543     9300  10951  11792   -901   1717  -1709       O  
ATOM   1945  CB  SER A 543     -46.826 -53.335  18.316  1.00 83.68           C  
ANISOU 1945  CB  SER A 543     9373  11105  11315  -1209   1362  -1953       C  
ATOM   1946  OG  SER A 543     -46.725 -54.724  18.559  1.00 83.66           O  
ANISOU 1946  OG  SER A 543     9332  11256  11197  -1196   1108  -1859       O  
ATOM   1947  N   VAL A 544     -48.944 -54.997  16.330  1.00 81.02           N  
ANISOU 1947  N   VAL A 544     8664  10793  11326   -775   1239  -1570       N  
ATOM   1948  CA  VAL A 544     -50.103 -55.892  16.372  1.00 80.71           C  
ANISOU 1948  CA  VAL A 544     8569  10754  11340   -693   1228  -1453       C  
ATOM   1949  C   VAL A 544     -50.002 -56.953  17.464  1.00 82.03           C  
ANISOU 1949  C   VAL A 544     8840  10997  11331   -768   1122  -1495       C  
ATOM   1950  O   VAL A 544     -50.874 -57.809  17.545  1.00 82.56           O  
ANISOU 1950  O   VAL A 544     8859  11068  11441   -702   1096  -1403       O  
ATOM   1951  CB  VAL A 544     -50.405 -56.612  15.034  1.00 78.63           C  
ANISOU 1951  CB  VAL A 544     8124  10587  11164   -589   1058  -1313       C  
ATOM   1952  CG1 VAL A 544     -50.622 -55.635  13.910  1.00 78.10           C  
ANISOU 1952  CG1 VAL A 544     7930  10491  11251   -544   1128  -1199       C  
ATOM   1953  CG2 VAL A 544     -49.335 -57.592  14.720  1.00 76.30           C  
ANISOU 1953  CG2 VAL A 544     7811  10423  10756   -616    830  -1379       C  
ATOM   1954  N   THR A 545     -48.968 -56.914  18.299  1.00 83.50           N  
ANISOU 1954  N   THR A 545     9149  11251  11327   -920   1045  -1600       N  
ATOM   1955  CA  THR A 545     -48.834 -57.933  19.326  1.00 85.02           C  
ANISOU 1955  CA  THR A 545     9404  11543  11354  -1017    911  -1571       C  
ATOM   1956  C   THR A 545     -49.008 -57.380  20.715  1.00 88.34           C  
ANISOU 1956  C   THR A 545    10050  11946  11566  -1225   1079  -1675       C  
ATOM   1957  O   THR A 545     -48.715 -58.059  21.698  1.00 89.66           O  
ANISOU 1957  O   THR A 545    10294  12239  11532  -1377    949  -1637       O  
ATOM   1958  CB  THR A 545     -47.487 -58.662  19.266  1.00 84.86           C  
ANISOU 1958  CB  THR A 545     9303  11659  11280  -1071    627  -1524       C  
ATOM   1959  OG1 THR A 545     -46.417 -57.727  19.450  1.00 85.56           O  
ANISOU 1959  OG1 THR A 545     9463  11774  11271  -1214    613  -1615       O  
ATOM   1960  CG2 THR A 545     -47.335 -59.423  17.946  1.00 82.77           C  
ANISOU 1960  CG2 THR A 545     8837  11395  11214   -897    511  -1458       C  
ATOM   1961  N   LYS A 546     -49.485 -56.143  20.799  1.00 90.98           N  
ANISOU 1961  N   LYS A 546    10487  12122  11958  -1257   1387  -1797       N  
ATOM   1962  CA  LYS A 546     -49.678 -55.472  22.087  1.00 94.76           C  
ANISOU 1962  CA  LYS A 546    11220  12548  12237  -1501   1642  -1965       C  
ATOM   1963  C   LYS A 546     -51.155 -55.163  22.302  1.00 96.26           C  
ANISOU 1963  C   LYS A 546    11441  12523  12609  -1413   2010  -1971       C  
ATOM   1964  O   LYS A 546     -51.931 -55.169  21.346  1.00 95.03           O  
ANISOU 1964  O   LYS A 546    11088  12253  12764  -1171   2061  -1830       O  
ATOM   1965  CB  LYS A 546     -48.780 -54.232  22.201  1.00 96.09           C  
ANISOU 1965  CB  LYS A 546    11508  12675  12326  -1682   1750  -2151       C  
ATOM   1966  CG  LYS A 546     -47.297 -54.585  22.079  1.00 97.14           C  
ANISOU 1966  CG  LYS A 546    11589  13020  12300  -1784   1375  -2108       C  
ATOM   1967  CD  LYS A 546     -46.340 -53.413  22.289  1.00102.30           C  
ANISOU 1967  CD  LYS A 546    12365  13655  12848  -2003   1447  -2287       C  
ATOM   1968  CE  LYS A 546     -45.936 -53.250  23.775  1.00108.03           C  
ANISOU 1968  CE  LYS A 546    13365  14513  13166  -2423   1458  -2426       C  
ATOM   1969  NZ  LYS A 546     -45.330 -54.471  24.438  1.00108.22           N1+
ANISOU 1969  NZ  LYS A 546    13358  14821  12938  -2571   1062  -2228       N1+
ATOM   1970  N   GLU A 547     -51.539 -54.923  23.556  1.00 99.78           N  
ANISOU 1970  N   GLU A 547    12127  12924  12860  -1636   2265  -2116       N  
ATOM   1971  CA  GLU A 547     -52.953 -54.840  23.935  1.00102.19           C  
ANISOU 1971  CA  GLU A 547    12462  13021  13342  -1566   2632  -2106       C  
ATOM   1972  C   GLU A 547     -53.697 -53.721  23.223  1.00102.89           C  
ANISOU 1972  C   GLU A 547    12429  12798  13867  -1397   3001  -2100       C  
ATOM   1973  O   GLU A 547     -53.073 -52.778  22.736  1.00103.40           O  
ANISOU 1973  O   GLU A 547    12471  12792  14023  -1413   3058  -2182       O  
ATOM   1974  CB  GLU A 547     -53.134 -54.742  25.471  1.00105.74           C  
ANISOU 1974  CB  GLU A 547    13232  13484  13457  -1894   2886  -2303       C  
ATOM   1975  CG  GLU A 547     -52.683 -53.427  26.147  1.00110.54           C  
ANISOU 1975  CG  GLU A 547    14112  13977  13911  -2207   3240  -2623       C  
ATOM   1976  CD  GLU A 547     -52.629 -53.525  27.687  1.00115.39           C  
ANISOU 1976  CD  GLU A 547    15083  14714  14045  -2634   3393  -2824       C  
ATOM   1977  OE1 GLU A 547     -53.267 -54.440  28.236  1.00115.43           O  
ANISOU 1977  OE1 GLU A 547    15113  14806  13939  -2632   3355  -2708       O  
ATOM   1978  OE2 GLU A 547     -51.945 -52.697  28.347  1.00118.02           O1-
ANISOU 1978  OE2 GLU A 547    15677  15074  14092  -3000   3547  -3095       O1-
ATOM   1979  N   GLY A 548     -55.021 -53.846  23.161  1.00103.61           N  
ANISOU 1979  N   GLY A 548    12409  12699  14257  -1234   3241  -1964       N  
ATOM   1980  CA  GLY A 548     -55.887 -52.818  22.600  1.00105.60           C  
ANISOU 1980  CA  GLY A 548    12498  12623  15002  -1079   3626  -1879       C  
ATOM   1981  C   GLY A 548     -55.513 -52.436  21.180  1.00104.38           C  
ANISOU 1981  C   GLY A 548    12077  12494  15089   -896   3407  -1695       C  
ATOM   1982  O   GLY A 548     -54.972 -51.359  20.934  1.00105.38           O  
ANISOU 1982  O   GLY A 548    12212  12504  15321   -943   3565  -1795       O  
ATOM   1983  N   LEU A 549     -55.783 -53.323  20.235  1.00102.57           N  
ANISOU 1983  N   LEU A 549    11618  12424  14929   -713   3050  -1434       N  
ATOM   1984  CA  LEU A 549     -55.545 -52.999  18.850  1.00101.47           C  
ANISOU 1984  CA  LEU A 549    11232  12333  14987   -577   2855  -1239       C  
ATOM   1985  C   LEU A 549     -56.739 -52.214  18.348  1.00103.79           C  
ANISOU 1985  C   LEU A 549    11279  12357  15799   -436   3157   -975       C  
ATOM   1986  O   LEU A 549     -57.855 -52.720  18.327  1.00103.88           O  
ANISOU 1986  O   LEU A 549    11153  12308  16007   -340   3194   -764       O  
ATOM   1987  CB  LEU A 549     -55.332 -54.267  18.033  1.00 98.59           C  
ANISOU 1987  CB  LEU A 549    10747  12253  14459   -501   2383  -1098       C  
ATOM   1988  CG  LEU A 549     -55.248 -54.092  16.524  1.00 96.64           C  
ANISOU 1988  CG  LEU A 549    10253  12097  14366   -402   2173   -878       C  
ATOM   1989  CD1 LEU A 549     -54.021 -53.323  16.166  1.00 96.41           C  
ANISOU 1989  CD1 LEU A 549    10277  12111  14243   -462   2133  -1013       C  
ATOM   1990  CD2 LEU A 549     -55.230 -55.437  15.864  1.00 94.89           C  
ANISOU 1990  CD2 LEU A 549     9954  12117  13981   -375   1798   -791       C  
ATOM   1991  N   GLU A 550     -56.490 -50.963  17.984  1.00106.27           N  
ANISOU 1991  N   GLU A 550    11516  12492  16366   -430   3384   -965       N  
ATOM   1992  CA  GLU A 550     -57.512 -50.084  17.426  1.00109.76           C  
ANISOU 1992  CA  GLU A 550    11661  12654  17388   -296   3676   -647       C  
ATOM   1993  C   GLU A 550     -57.687 -50.387  15.951  1.00108.76           C  
ANISOU 1993  C   GLU A 550    11219  12737  17367   -183   3283   -260       C  
ATOM   1994  O   GLU A 550     -56.702 -50.573  15.228  1.00107.22           O  
ANISOU 1994  O   GLU A 550    11045  12797  16895   -220   2945   -309       O  
ATOM   1995  CB  GLU A 550     -57.123 -48.606  17.599  1.00112.37           C  
ANISOU 1995  CB  GLU A 550    12014  12693  17988   -345   4091   -775       C  
ATOM   1996  CG  GLU A 550     -57.581 -47.944  18.922  1.00117.88           C  
ANISOU 1996  CG  GLU A 550    12915  13017  18854   -454   4706  -1045       C  
ATOM   1997  CD  GLU A 550     -56.768 -46.684  19.296  1.00122.81           C  
ANISOU 1997  CD  GLU A 550    13701  13428  19531   -602   5062  -1351       C  
ATOM   1998  OE1 GLU A 550     -55.685 -46.442  18.695  1.00122.31           O  
ANISOU 1998  OE1 GLU A 550    13642  13552  19278   -633   4776  -1399       O  
ATOM   1999  OE2 GLU A 550     -57.211 -45.941  20.206  1.00126.36           O1-
ANISOU 1999  OE2 GLU A 550    14281  13509  20219   -706   5654  -1561       O1-
ATOM   2000  N   LEU A 551     -58.941 -50.428  15.515  1.00110.59           N  
ANISOU 2000  N   LEU A 551    11156  12862  17997    -74   3339    132       N  
ATOM   2001  CA  LEU A 551     -59.285 -50.673  14.130  1.00110.69           C  
ANISOU 2001  CA  LEU A 551    10856  13088  18113    -28   2977    550       C  
ATOM   2002  C   LEU A 551     -60.281 -49.648  13.640  1.00114.43           C  
ANISOU 2002  C   LEU A 551    10947  13293  19238     63   3237   1016       C  
ATOM   2003  O   LEU A 551     -61.051 -49.110  14.442  1.00117.34           O  
ANISOU 2003  O   LEU A 551    11267  13286  20028    128   3704   1046       O  
ATOM   2004  CB  LEU A 551     -59.947 -52.032  14.007  1.00109.50           C  
ANISOU 2004  CB  LEU A 551    10675  13146  17782    -30   2672    660       C  
ATOM   2005  CG  LEU A 551     -59.090 -53.274  13.821  1.00107.26           C  
ANISOU 2005  CG  LEU A 551    10603  13214  16935   -114   2255    404       C  
ATOM   2006  CD1 LEU A 551     -58.691 -53.856  15.158  1.00106.49           C  
ANISOU 2006  CD1 LEU A 551    10827  13074  16558   -146   2368     14       C  
ATOM   2007  CD2 LEU A 551     -59.895 -54.286  13.012  1.00108.20           C  
ANISOU 2007  CD2 LEU A 551    10533  13544  17033   -134   1925    690       C  
ATOM   2008  N   PRO A 552     -60.286 -49.374  12.319  1.00115.24           N  
ANISOU 2008  N   PRO A 552    10760  13578  19448     53   2955   1407       N  
ATOM   2009  CA  PRO A 552     -61.467 -48.737  11.754  1.00118.96           C  
ANISOU 2009  CA  PRO A 552    10783  13868  20546    125   3079   2000       C  
ATOM   2010  C   PRO A 552     -62.694 -49.647  11.947  1.00120.26           C  
ANISOU 2010  C   PRO A 552    10820  14044  20827    150   2997   2233       C  
ATOM   2011  O   PRO A 552     -62.676 -50.831  11.594  1.00117.88           O  
ANISOU 2011  O   PRO A 552    10609  14086  20091     64   2576   2186       O  
ATOM   2012  CB  PRO A 552     -61.110 -48.557  10.274  1.00118.72           C  
ANISOU 2012  CB  PRO A 552    10525  14166  20416     36   2667   2351       C  
ATOM   2013  CG  PRO A 552     -59.945 -49.427  10.037  1.00114.96           C  
ANISOU 2013  CG  PRO A 552    10385  14061  19231    -76   2301   1931       C  
ATOM   2014  CD  PRO A 552     -59.210 -49.502  11.326  1.00113.36           C  
ANISOU 2014  CD  PRO A 552    10572  13687  18812    -39   2566   1352       C  
ATOM   2015  N   GLU A 553     -63.743 -49.075  12.529  1.00124.33           N  
ANISOU 2015  N   GLU A 553    11124  14151  21965    263   3441   2470       N  
ATOM   2016  CA  GLU A 553     -64.877 -49.844  13.000  1.00126.05           C  
ANISOU 2016  CA  GLU A 553    11260  14290  22343    308   3481   2620       C  
ATOM   2017  C   GLU A 553     -66.170 -49.074  12.752  1.00130.26           C  
ANISOU 2017  C   GLU A 553    11285  14484  23721    412   3763   3255       C  
ATOM   2018  O   GLU A 553     -66.406 -48.049  13.391  1.00133.03           O  
ANISOU 2018  O   GLU A 553    11562  14364  24617    515   4351   3245       O  
ATOM   2019  CB  GLU A 553     -64.689 -50.103  14.494  1.00125.64           C  
ANISOU 2019  CB  GLU A 553    11612  14015  22109    333   3870   2062       C  
ATOM   2020  CG  GLU A 553     -65.314 -51.384  15.011  1.00126.76           C  
ANISOU 2020  CG  GLU A 553    11863  14270  22028    329   3723   1994       C  
ATOM   2021  CD  GLU A 553     -65.182 -51.530  16.521  1.00129.26           C  
ANISOU 2021  CD  GLU A 553    12561  14365  22186    325   4142   1498       C  
ATOM   2022  OE1 GLU A 553     -64.509 -50.672  17.142  1.00129.99           O  
ANISOU 2022  OE1 GLU A 553    12870  14254  22265    287   4513   1160       O  
ATOM   2023  OE2 GLU A 553     -65.759 -52.500  17.082  1.00130.53           O1-
ANISOU 2023  OE2 GLU A 553    12804  14565  22223    332   4099   1453       O1-
ATOM   2024  N   ASP A 554     -67.001 -49.565  11.829  1.00131.48           N  
ANISOU 2024  N   ASP A 554    11082  14869  24005    361   3362   3815       N  
ATOM   2025  CA  ASP A 554     -68.264 -48.881  11.481  1.00136.39           C  
ANISOU 2025  CA  ASP A 554    11138  15204  25478    442   3555   4544       C  
ATOM   2026  C   ASP A 554     -69.325 -48.992  12.592  1.00138.67           C  
ANISOU 2026  C   ASP A 554    11373  15050  26262    585   4053   4552       C  
ATOM   2027  O   ASP A 554     -69.436 -50.039  13.250  1.00136.63           O  
ANISOU 2027  O   ASP A 554    11411  14896  25607    570   3979   4206       O  
ATOM   2028  CB  ASP A 554     -68.809 -49.344  10.106  1.00137.35           C  
ANISOU 2028  CB  ASP A 554    10876  15756  25552    280   2923   5190       C  
ATOM   2029  CG  ASP A 554     -69.442 -50.745  10.139  1.00135.90           C  
ANISOU 2029  CG  ASP A 554    10762  15838  25034    188   2563   5185       C  
ATOM   2030  OD1 ASP A 554     -68.821 -51.710   9.652  1.00132.62           O  
ANISOU 2030  OD1 ASP A 554    10618  15882  23888     14   2082   4903       O  
ATOM   2031  OD2 ASP A 554     -70.575 -50.880  10.635  1.00138.03           O1-
ANISOU 2031  OD2 ASP A 554    10801  15835  25809    285   2784   5473       O1-
ATOM   2032  N   GLU A 555     -70.095 -47.917  12.791  1.00143.12           N  
ANISOU 2032  N   GLU A 555    11549  15106  27723    722   4585   4960       N  
ATOM   2033  CA  GLU A 555     -71.131 -47.838  13.847  1.00145.82           C  
ANISOU 2033  CA  GLU A 555    11804  14937  28664    865   5187   4990       C  
ATOM   2034  C   GLU A 555     -71.824 -49.165  14.170  1.00144.41           C  
ANISOU 2034  C   GLU A 555    11713  14949  28205    840   4926   4970       C  
ATOM   2035  O   GLU A 555     -72.084 -49.475  15.334  1.00144.27           O  
ANISOU 2035  O   GLU A 555    11964  14669  28180    903   5347   4582       O  
ATOM   2036  CB  GLU A 555     -72.177 -46.769  13.510  1.00151.26           C  
ANISOU 2036  CB  GLU A 555    11840  15161  30471    993   5575   5751       C  
ATOM   2037  CG  GLU A 555     -71.649 -45.337  13.580  1.00154.12           C  
ANISOU 2037  CG  GLU A 555    12125  15121  31312   1064   6102   5696       C  
ATOM   2038  CD  GLU A 555     -71.052 -44.851  12.260  1.00154.05           C  
ANISOU 2038  CD  GLU A 555    11859  15457  31213    977   5607   6097       C  
ATOM   2039  OE1 GLU A 555     -71.829 -44.409  11.389  1.00157.86           O  
ANISOU 2039  OE1 GLU A 555    11719  15900  32358    995   5466   6943       O  
ATOM   2040  OE2 GLU A 555     -69.812 -44.898  12.097  1.00149.98           O1-
ANISOU 2040  OE2 GLU A 555    11747  15254  29983    879   5362   5598       O1-
ATOM   2041  N   GLU A 556     -72.107 -49.944  13.132  1.00143.57           N  
ANISOU 2041  N   GLU A 556    11392  15309  27850    719   4239   5379       N  
ATOM   2042  CA  GLU A 556     -72.761 -51.230  13.278  1.00142.53           C  
ANISOU 2042  CA  GLU A 556    11305  15388  27460    670   3931   5404       C  
ATOM   2043  C   GLU A 556     -71.858 -52.251  13.964  1.00137.85           C  
ANISOU 2043  C   GLU A 556    11334  15050  25991    611   3791   4622       C  
ATOM   2044  O   GLU A 556     -72.236 -52.827  14.979  1.00137.58           O  
ANISOU 2044  O   GLU A 556    11503  14847  25922    677   4050   4349       O  
ATOM   2045  CB  GLU A 556     -73.211 -51.735  11.909  1.00143.33           C  
ANISOU 2045  CB  GLU A 556    11032  15946  27480    488   3226   6020       C  
ATOM   2046  CG  GLU A 556     -73.746 -53.151  11.907  1.00143.58           C  
ANISOU 2046  CG  GLU A 556    11143  16267  27142    384   2825   5997       C  
ATOM   2047  CD  GLU A 556     -74.346 -53.549  10.571  1.00148.00           C  
ANISOU 2047  CD  GLU A 556    11295  17243  27694    149   2179   6659       C  
ATOM   2048  OE1 GLU A 556     -75.371 -52.939  10.153  1.00154.01           O  
ANISOU 2048  OE1 GLU A 556    11481  17827  29206    163   2223   7432       O  
ATOM   2049  OE2 GLU A 556     -73.796 -54.489   9.951  1.00145.49           O1-
ANISOU 2049  OE2 GLU A 556    11227  17424  26626    -74   1641   6411       O1-
ATOM   2050  N   GLU A 557     -70.667 -52.462  13.406  1.00134.79           N  
ANISOU 2050  N   GLU A 557    11222  15061  24931    483   3393   4298       N  
ATOM   2051  CA  GLU A 557     -69.696 -53.454  13.896  1.00130.30           C  
ANISOU 2051  CA  GLU A 557    11184  14768  23553    411   3191   3629       C  
ATOM   2052  C   GLU A 557     -69.302 -53.276  15.374  1.00129.05           C  
ANISOU 2052  C   GLU A 557    11428  14297  23305    500   3734   3055       C  
ATOM   2053  O   GLU A 557     -69.116 -54.268  16.071  1.00126.77           O  
ANISOU 2053  O   GLU A 557    11456  14130  22578    472   3657   2685       O  
ATOM   2054  CB  GLU A 557     -68.465 -53.470  12.970  1.00128.21           C  
ANISOU 2054  CB  GLU A 557    11076  14908  22727    270   2758   3447       C  
ATOM   2055  CG  GLU A 557     -67.221 -54.222  13.464  1.00125.95           C  
ANISOU 2055  CG  GLU A 557    11307  14846  21701    212   2622   2767       C  
ATOM   2056  CD  GLU A 557     -67.406 -55.735  13.571  1.00126.57           C  
ANISOU 2056  CD  GLU A 557    11534  15181  21373    141   2286   2617       C  
ATOM   2057  OE1 GLU A 557     -68.463 -56.251  13.141  1.00128.65           O  
ANISOU 2057  OE1 GLU A 557    11520  15504  21858    107   2098   3019       O  
ATOM   2058  OE2 GLU A 557     -66.483 -56.407  14.100  1.00124.87           O1-
ANISOU 2058  OE2 GLU A 557    11697  15099  20646    110   2215   2115       O1-
ATOM   2059  N   LYS A 558     -69.190 -52.022  15.834  1.00130.68           N  
ANISOU 2059  N   LYS A 558    11614  14108  23928    578   4281   2998       N  
ATOM   2060  CA  LYS A 558     -68.937 -51.684  17.254  1.00130.50           C  
ANISOU 2060  CA  LYS A 558    11960  13750  23871    601   4880   2477       C  
ATOM   2061  C   LYS A 558     -70.024 -52.251  18.187  1.00131.31           C  
ANISOU 2061  C   LYS A 558    12062  13613  24215    665   5196   2507       C  
ATOM   2062  O   LYS A 558     -69.738 -52.744  19.280  1.00129.83           O  
ANISOU 2062  O   LYS A 558    12281  13417  23631    609   5382   2030       O  
ATOM   2063  CB  LYS A 558     -68.815 -50.161  17.443  1.00133.54           C  
ANISOU 2063  CB  LYS A 558    12249  13697  24792    651   5466   2480       C  
ATOM   2064  CG  LYS A 558     -68.028 -49.454  16.331  1.00134.63           C  
ANISOU 2064  CG  LYS A 558    12232  14015  24906    621   5178   2647       C  
ATOM   2065  CD  LYS A 558     -67.507 -48.041  16.696  1.00138.90           C  
ANISOU 2065  CD  LYS A 558    12828  14164  25781    632   5748   2441       C  
ATOM   2066  CE  LYS A 558     -68.443 -46.926  16.202  1.00144.28           C  
ANISOU 2066  CE  LYS A 558    12948  14411  27460    767   6129   3062       C  
ATOM   2067  NZ  LYS A 558     -68.034 -45.562  16.655  1.00147.29           N1+
ANISOU 2067  NZ  LYS A 558    13377  14328  28257    780   6786   2837       N1+
ATOM   2068  N   LYS A 559     -71.271 -52.174  17.737  1.00133.48           N  
ANISOU 2068  N   LYS A 559    11859  13705  25149    767   5241   3108       N  
ATOM   2069  CA  LYS A 559     -72.413 -52.716  18.469  1.00134.87           C  
ANISOU 2069  CA  LYS A 559    11953  13648  25644    843   5515   3235       C  
ATOM   2070  C   LYS A 559     -72.392 -54.254  18.425  1.00130.97           C  
ANISOU 2070  C   LYS A 559    11631  13587  24543    773   4952   3124       C  
ATOM   2071  O   LYS A 559     -72.885 -54.923  19.341  1.00131.12           O  
ANISOU 2071  O   LYS A 559    11807  13503  24509    796   5152   2963       O  
ATOM   2072  CB  LYS A 559     -73.730 -52.106  17.928  1.00139.26           C  
ANISOU 2072  CB  LYS A 559    11880  13862  27167    971   5720   3985       C  
ATOM   2073  CG  LYS A 559     -74.990 -52.987  17.975  1.00141.14           C  
ANISOU 2073  CG  LYS A 559    11846  14079  27702   1024   5603   4389       C  
ATOM   2074  CD  LYS A 559     -75.781 -52.865  19.288  1.00145.71           C  
ANISOU 2074  CD  LYS A 559    12505  14143  28715   1131   6355   4238       C  
ATOM   2075  CE  LYS A 559     -76.950 -51.862  19.196  1.00151.66           C  
ANISOU 2075  CE  LYS A 559    12690  14321  30609   1285   6912   4851       C  
ATOM   2076  NZ  LYS A 559     -76.532 -50.426  19.288  1.00154.59           N1+
ANISOU 2076  NZ  LYS A 559    13022  14293  31420   1324   7481   4765       N1+
ATOM   2077  N   LYS A 560     -71.806 -54.811  17.372  1.00127.42           N  
ANISOU 2077  N   LYS A 560    11158  13607  23646    674   4285   3194       N  
ATOM   2078  CA  LYS A 560     -71.682 -56.254  17.268  1.00123.78           C  
ANISOU 2078  CA  LYS A 560    10865  13535  22631    590   3781   3050       C  
ATOM   2079  C   LYS A 560     -70.534 -56.757  18.156  1.00120.10           C  
ANISOU 2079  C   LYS A 560    10940  13213  21478    528   3800   2381       C  
ATOM   2080  O   LYS A 560     -70.613 -57.858  18.697  1.00118.30           O  
ANISOU 2080  O   LYS A 560    10896  13112  20938    505   3670   2197       O  
ATOM   2081  CB  LYS A 560     -71.518 -56.687  15.802  1.00122.89           C  
ANISOU 2081  CB  LYS A 560    10535  13849  22308    463   3115   3353       C  
ATOM   2082  CG  LYS A 560     -71.758 -58.183  15.538  1.00121.71           C  
ANISOU 2082  CG  LYS A 560    10433  14028  21781    363   2639   3335       C  
ATOM   2083  CD  LYS A 560     -71.951 -58.508  14.047  1.00122.67           C  
ANISOU 2083  CD  LYS A 560    10268  14516  21823    184   2061   3735       C  
ATOM   2084  CE  LYS A 560     -73.433 -58.519  13.649  1.00126.14           C  
ANISOU 2084  CE  LYS A 560    10218  14852  22856    178   2003   4402       C  
ATOM   2085  NZ  LYS A 560     -73.965 -57.150  13.390  1.00129.79           N1+
ANISOU 2085  NZ  LYS A 560    10281  15023  24008    267   2291   4910       N1+
ATOM   2086  N   GLN A 561     -69.484 -55.946  18.315  1.00118.92           N  
ANISOU 2086  N   GLN A 561    11019  13039  21126    490   3959   2057       N  
ATOM   2087  CA  GLN A 561     -68.347 -56.294  19.183  1.00115.98           C  
ANISOU 2087  CA  GLN A 561    11131  12803  20133    398   3977   1474       C  
ATOM   2088  C   GLN A 561     -68.717 -56.234  20.663  1.00116.90           C  
ANISOU 2088  C   GLN A 561    11493  12629  20294    396   4522   1211       C  
ATOM   2089  O   GLN A 561     -68.208 -57.010  21.461  1.00115.33           O  
ANISOU 2089  O   GLN A 561    11626  12595  19596    308   4444    869       O  
ATOM   2090  CB  GLN A 561     -67.108 -55.421  18.895  1.00115.33           C  
ANISOU 2090  CB  GLN A 561    11204  12788  19825    330   3969   1226       C  
ATOM   2091  CG  GLN A 561     -66.010 -56.086  18.039  1.00113.58           C  
ANISOU 2091  CG  GLN A 561    11079  13009  19064    243   3375   1100       C  
ATOM   2092  CD  GLN A 561     -65.300 -57.272  18.741  1.00113.85           C  
ANISOU 2092  CD  GLN A 561    11455  13283  18519    162   3157    723       C  
ATOM   2093  OE1 GLN A 561     -64.901 -57.179  19.913  1.00114.31           O  
ANISOU 2093  OE1 GLN A 561    11815  13250  18367    103   3432    392       O  
ATOM   2094  NE2 GLN A 561     -65.136 -58.386  18.012  1.00112.40           N  
ANISOU 2094  NE2 GLN A 561    11214  13406  18085    132   2670    787       N  
ATOM   2095  N   GLU A 562     -69.616 -55.325  21.019  1.00119.81           N  
ANISOU 2095  N   GLU A 562    11683  12559  21278    478   5088   1392       N  
ATOM   2096  CA  GLU A 562     -70.022 -55.150  22.413  1.00121.53           C  
ANISOU 2096  CA  GLU A 562    12146  12459  21569    443   5704   1122       C  
ATOM   2097  C   GLU A 562     -70.870 -56.308  22.935  1.00120.32           C  
ANISOU 2097  C   GLU A 562    11985  12346  21383    480   5642   1223       C  
ATOM   2098  O   GLU A 562     -70.783 -56.653  24.110  1.00120.60           O  
ANISOU 2098  O   GLU A 562    12362  12348  21112    380   5910    887       O  
ATOM   2099  CB  GLU A 562     -70.757 -53.821  22.595  1.00126.28           C  
ANISOU 2099  CB  GLU A 562    12534  12519  22927    521   6402   1286       C  
ATOM   2100  CG  GLU A 562     -70.811 -53.321  24.034  1.00130.92           C  
ANISOU 2100  CG  GLU A 562    13485  12763  23496    402   7145    845       C  
ATOM   2101  CD  GLU A 562     -71.795 -52.152  24.237  1.00138.24           C  
ANISOU 2101  CD  GLU A 562    14140  13063  25321    503   7933   1052       C  
ATOM   2102  OE1 GLU A 562     -71.532 -51.050  23.684  1.00140.36           O  
ANISOU 2102  OE1 GLU A 562    14229  13128  25973    539   8114   1149       O  
ATOM   2103  OE2 GLU A 562     -72.810 -52.334  24.966  1.00139.93           O1-
ANISOU 2103  OE2 GLU A 562    14315  12968  25883    545   8399   1119       O1-
ATOM   2104  N   GLU A 563     -71.676 -56.906  22.058  1.00118.92           N  
ANISOU 2104  N   GLU A 563    11422  12259  21502    593   5279   1693       N  
ATOM   2105  CA  GLU A 563     -72.518 -58.058  22.411  1.00117.94           C  
ANISOU 2105  CA  GLU A 563    11241  12183  21388    634   5166   1835       C  
ATOM   2106  C   GLU A 563     -71.679 -59.249  22.800  1.00113.58           C  
ANISOU 2106  C   GLU A 563    11036  12019  20097    525   4764   1484       C  
ATOM   2107  O   GLU A 563     -71.951 -59.904  23.801  1.00113.64           O  
ANISOU 2107  O   GLU A 563    11239  11997  19940    497   4933   1331       O  
ATOM   2108  CB  GLU A 563     -73.403 -58.470  21.244  1.00118.26           C  
ANISOU 2108  CB  GLU A 563    10799  12309  21824    720   4760   2404       C  
ATOM   2109  CG  GLU A 563     -74.260 -57.360  20.690  1.00124.62           C  
ANISOU 2109  CG  GLU A 563    11155  12768  23425    825   5055   2893       C  
ATOM   2110  CD  GLU A 563     -75.559 -57.879  20.111  1.00130.54           C  
ANISOU 2110  CD  GLU A 563    11437  13484  24677    895   4852   3489       C  
ATOM   2111  OE1 GLU A 563     -75.527 -58.983  19.510  1.00128.96           O  
ANISOU 2111  OE1 GLU A 563    11208  13668  24122    818   4255   3565       O  
ATOM   2112  OE2 GLU A 563     -76.607 -57.189  20.269  1.00136.01           O1-
ANISOU 2112  OE2 GLU A 563    11784  13749  26141   1012   5310   3881       O1-
ATOM   2113  N   LYS A 564     -70.664 -59.518  21.977  1.00109.82           N  
ANISOU 2113  N   LYS A 564    10612  11897  19218    461   4246   1389       N  
ATOM   2114  CA  LYS A 564     -69.693 -60.585  22.201  1.00105.66           C  
ANISOU 2114  CA  LYS A 564    10369  11726  18048    361   3849   1083       C  
ATOM   2115  C   LYS A 564     -68.918 -60.385  23.494  1.00105.37           C  
ANISOU 2115  C   LYS A 564    10758  11671  17605    236   4148    647       C  
ATOM   2116  O   LYS A 564     -68.736 -61.342  24.238  1.00104.65           O  
ANISOU 2116  O   LYS A 564    10862  11730  17170    171   4045    502       O  
ATOM   2117  CB  LYS A 564     -68.728 -60.697  21.026  1.00102.91           C  
ANISOU 2117  CB  LYS A 564     9976  11690  17432    313   3341   1062       C  
ATOM   2118  CG  LYS A 564     -69.308 -61.430  19.847  1.00102.19           C  
ANISOU 2118  CG  LYS A 564     9569  11769  17488    335   2903   1404       C  
ATOM   2119  CD  LYS A 564     -68.582 -61.035  18.577  1.00102.12           C  
ANISOU 2119  CD  LYS A 564     9465  11973  17362    271   2567   1452       C  
ATOM   2120  CE  LYS A 564     -69.292 -61.564  17.330  1.00102.79           C  
ANISOU 2120  CE  LYS A 564     9219  12224  17610    226   2173   1834       C  
ATOM   2121  NZ  LYS A 564     -68.591 -61.121  16.085  1.00101.54           N1+
ANISOU 2121  NZ  LYS A 564     8984  12290  17303    123   1873   1885       N1+
ATOM   2122  N   LYS A 565     -68.471 -59.158  23.764  1.00105.78           N  
ANISOU 2122  N   LYS A 565    10944  11549  17695    175   4511    458       N  
ATOM   2123  CA  LYS A 565     -67.836 -58.855  25.042  1.00106.39           C  
ANISOU 2123  CA  LYS A 565    11438  11599  17385     -9   4846     45       C  
ATOM   2124  C   LYS A 565     -68.672 -59.317  26.250  1.00108.25           C  
ANISOU 2124  C   LYS A 565    11812  11683  17634    -53   5219      2       C  
ATOM   2125  O   LYS A 565     -68.164 -60.036  27.112  1.00108.14           O  
ANISOU 2125  O   LYS A 565    12086  11887  17115   -209   5113   -209       O  
ATOM   2126  CB  LYS A 565     -67.480 -57.371  25.148  1.00108.53           C  
ANISOU 2126  CB  LYS A 565    11800  11620  17812    -79   5287   -137       C  
ATOM   2127  CG  LYS A 565     -65.992 -57.096  25.032  1.00108.01           C  
ANISOU 2127  CG  LYS A 565    11971  11815  17250   -232   5021   -435       C  
ATOM   2128  CD  LYS A 565     -65.656 -55.848  24.209  1.00110.47           C  
ANISOU 2128  CD  LYS A 565    12136  11973  17863   -184   5134   -398       C  
ATOM   2129  CE  LYS A 565     -65.587 -54.581  25.064  1.00115.32           C  
ANISOU 2129  CE  LYS A 565    12974  12248  18594   -331   5803   -696       C  
ATOM   2130  NZ  LYS A 565     -65.036 -53.431  24.281  1.00115.97           N1+
ANISOU 2130  NZ  LYS A 565    12935  12220  18909   -301   5857   -688       N1+
ATOM   2131  N   THR A 566     -69.948 -58.942  26.308  1.00109.95           N  
ANISOU 2131  N   THR A 566    11802  11532  18439     75   5646    240       N  
ATOM   2132  CA  THR A 566     -70.768 -59.334  27.453  1.00111.41           C  
ANISOU 2132  CA  THR A 566    12120  11546  18662     32   6057    195       C  
ATOM   2133  C   THR A 566     -71.234 -60.795  27.410  1.00108.94           C  
ANISOU 2133  C   THR A 566    11688  11450  18253    115   5644    414       C  
ATOM   2134  O   THR A 566     -71.560 -61.374  28.447  1.00110.65           O  
ANISOU 2134  O   THR A 566    12095  11662  18282     32   5842    320       O  
ATOM   2135  CB  THR A 566     -71.960 -58.354  27.725  1.00115.71           C  
ANISOU 2135  CB  THR A 566    12494  11552  19919    123   6794    335       C  
ATOM   2136  OG1 THR A 566     -72.972 -58.503  26.724  1.00115.09           O  
ANISOU 2136  OG1 THR A 566    11909  11339  20481    369   6630    853       O  
ATOM   2137  CG2 THR A 566     -71.477 -56.905  27.763  1.00117.63           C  
ANISOU 2137  CG2 THR A 566    12847  11542  20305     33   7244    101       C  
ATOM   2138  N   LYS A 567     -71.253 -61.402  26.229  1.00104.96           N  
ANISOU 2138  N   LYS A 567    10881  11139  17857    251   5085    693       N  
ATOM   2139  CA  LYS A 567     -71.657 -62.801  26.106  1.00102.20           C  
ANISOU 2139  CA  LYS A 567    10410  10981  17438    313   4692    877       C  
ATOM   2140  C   LYS A 567     -70.603 -63.713  26.722  1.00 99.62           C  
ANISOU 2140  C   LYS A 567    10396  10995  16460    165   4388    603       C  
ATOM   2141  O   LYS A 567     -70.919 -64.725  27.314  1.00 99.88           O  
ANISOU 2141  O   LYS A 567    10469  11105  16373    155   4317    647       O  
ATOM   2142  CB  LYS A 567     -71.846 -63.159  24.638  1.00100.34           C  
ANISOU 2142  CB  LYS A 567     9810  10883  17432    425   4187   1192       C  
ATOM   2143  CG  LYS A 567     -72.459 -64.512  24.393  1.00 99.45           C  
ANISOU 2143  CG  LYS A 567     9521  10901  17363    479   3839   1407       C  
ATOM   2144  CD  LYS A 567     -72.129 -65.008  23.004  1.00 98.17           C  
ANISOU 2144  CD  LYS A 567     9152  11000  17147    472   3263   1542       C  
ATOM   2145  CE  LYS A 567     -73.023 -66.184  22.642  1.00100.17           C  
ANISOU 2145  CE  LYS A 567     9167  11307  17585    510   2993   1807       C  
ATOM   2146  NZ  LYS A 567     -72.331 -67.144  21.714  1.00 99.21           N1+
ANISOU 2146  NZ  LYS A 567     9027  11508  17157    423   2443   1731       N1+
ATOM   2147  N   PHE A 568     -69.341 -63.337  26.557  1.00 97.41           N  
ANISOU 2147  N   PHE A 568    10303  10909  15798     50   4203    359       N  
ATOM   2148  CA  PHE A 568     -68.207 -64.062  27.111  1.00 94.55           C  
ANISOU 2148  CA  PHE A 568    10202  10864  14859   -107   3910    142       C  
ATOM   2149  C   PHE A 568     -67.653 -63.314  28.322  1.00 96.61           C  
ANISOU 2149  C   PHE A 568    10845  11103  14760   -344   4293   -170       C  
ATOM   2150  O   PHE A 568     -66.555 -63.605  28.784  1.00 96.39           O  
ANISOU 2150  O   PHE A 568    11040  11343  14240   -526   4067   -345       O  
ATOM   2151  CB  PHE A 568     -67.114 -64.246  26.038  1.00 91.00           C  
ANISOU 2151  CB  PHE A 568     9674  10662  14237    -94   3404    109       C  
ATOM   2152  CG  PHE A 568     -67.518 -65.157  24.924  1.00 87.39           C  
ANISOU 2152  CG  PHE A 568     8909  10287  14006     49   3006    352       C  
ATOM   2153  CD1 PHE A 568     -68.204 -64.677  23.826  1.00 87.35           C  
ANISOU 2153  CD1 PHE A 568     8623  10162  14402    164   2982    572       C  
ATOM   2154  CD2 PHE A 568     -67.227 -66.511  24.980  1.00 84.26           C  
ANISOU 2154  CD2 PHE A 568     8495  10087  13430     40   2663    378       C  
ATOM   2155  CE1 PHE A 568     -68.603 -65.544  22.797  1.00 86.23           C  
ANISOU 2155  CE1 PHE A 568     8221  10130  14412    226   2605    784       C  
ATOM   2156  CE2 PHE A 568     -67.621 -67.381  23.963  1.00 81.71           C  
ANISOU 2156  CE2 PHE A 568     7913   9824  13306    129   2336    556       C  
ATOM   2157  CZ  PHE A 568     -68.307 -66.898  22.870  1.00 82.64           C  
ANISOU 2157  CZ  PHE A 568     7787   9855  13755    200   2299    743       C  
ATOM   2158  N   GLU A 569     -68.402 -62.342  28.830  1.00 99.12           N  
ANISOU 2158  N   GLU A 569    11229  11093  15337   -368   4886   -234       N  
ATOM   2159  CA  GLU A 569     -67.981 -61.617  30.021  1.00101.66           C  
ANISOU 2159  CA  GLU A 569    11948  11373  15304   -651   5324   -574       C  
ATOM   2160  C   GLU A 569     -67.746 -62.626  31.139  1.00101.03           C  
ANISOU 2160  C   GLU A 569    12111  11553  14720   -852   5209   -632       C  
ATOM   2161  O   GLU A 569     -66.769 -62.530  31.877  1.00101.77           O  
ANISOU 2161  O   GLU A 569    12520  11882  14265  -1146   5153   -864       O  
ATOM   2162  CB  GLU A 569     -69.031 -60.570  30.413  1.00106.07           C  
ANISOU 2162  CB  GLU A 569    12511  11471  16319   -633   6066   -618       C  
ATOM   2163  CG  GLU A 569     -68.686 -59.714  31.642  1.00112.49           C  
ANISOU 2163  CG  GLU A 569    13768  12187  16786   -978   6633  -1032       C  
ATOM   2164  CD  GLU A 569     -69.048 -58.230  31.466  1.00118.70           C  
ANISOU 2164  CD  GLU A 569    14523  12523  18051   -959   7262  -1161       C  
ATOM   2165  OE1 GLU A 569     -69.983 -57.772  32.167  1.00121.02           O  
ANISOU 2165  OE1 GLU A 569    14887  12443  18650  -1004   7952  -1232       O  
ATOM   2166  OE2 GLU A 569     -68.383 -57.532  30.634  1.00119.16           O1-
ANISOU 2166  OE2 GLU A 569    14480  12588  18206   -902   7089  -1186       O1-
ATOM   2167  N   ASN A 570     -68.634 -63.609  31.225  1.00 99.43           N  
ANISOU 2167  N   ASN A 570    11734  11325  14718   -705   5142   -383       N  
ATOM   2168  CA  ASN A 570     -68.499 -64.697  32.180  1.00 98.62           C  
ANISOU 2168  CA  ASN A 570    11788  11471  14212   -857   4987   -351       C  
ATOM   2169  C   ASN A 570     -67.355 -65.662  31.935  1.00 95.05           C  
ANISOU 2169  C   ASN A 570    11307  11413  13395   -900   4337   -285       C  
ATOM   2170  O   ASN A 570     -66.618 -65.959  32.864  1.00 96.61           O  
ANISOU 2170  O   ASN A 570    11755  11870  13083  -1174   4246   -374       O  
ATOM   2171  CB  ASN A 570     -69.789 -65.481  32.276  1.00 99.09           C  
ANISOU 2171  CB  ASN A 570    11636  11366  14648   -666   5101    -83       C  
ATOM   2172  CG  ASN A 570     -70.773 -64.841  33.194  1.00102.24           C  
ANISOU 2172  CG  ASN A 570    12193  11449  15203   -754   5812   -177       C  
ATOM   2173  OD1 ASN A 570     -71.829 -65.400  33.441  1.00103.34           O  
ANISOU 2173  OD1 ASN A 570    12194  11435  15635   -631   5981     23       O  
ATOM   2174  ND2 ASN A 570     -70.439 -63.669  33.718  1.00103.63           N  
ANISOU 2174  ND2 ASN A 570    12663  11506  15205   -981   6267   -496       N  
ATOM   2175  N   LEU A 571     -67.203 -66.177  30.719  1.00 90.28           N  
ANISOU 2175  N   LEU A 571    10393  10856  13054   -661   3900   -113       N  
ATOM   2176  CA  LEU A 571     -66.092 -67.084  30.471  1.00 86.94           C  
ANISOU 2176  CA  LEU A 571     9925  10749  12357   -699   3352    -63       C  
ATOM   2177  C   LEU A 571     -64.722 -66.419  30.734  1.00 87.44           C  
ANISOU 2177  C   LEU A 571    10226  11012  11983   -939   3254   -286       C  
ATOM   2178  O   LEU A 571     -63.816 -67.029  31.314  1.00 88.59           O  
ANISOU 2178  O   LEU A 571    10470  11434  11754  -1123   2975   -259       O  
ATOM   2179  CB  LEU A 571     -66.158 -67.681  29.072  1.00 83.11           C  
ANISOU 2179  CB  LEU A 571     9099  10255  12223   -443   2972     99       C  
ATOM   2180  CG  LEU A 571     -64.882 -68.402  28.651  1.00 80.36           C  
ANISOU 2180  CG  LEU A 571     8699  10168  11665   -478   2487     99       C  
ATOM   2181  CD1 LEU A 571     -64.708 -69.682  29.423  1.00 81.24           C  
ANISOU 2181  CD1 LEU A 571     8799  10441  11626   -543   2295    252       C  
ATOM   2182  CD2 LEU A 571     -64.866 -68.675  27.180  1.00 77.63           C  
ANISOU 2182  CD2 LEU A 571     8084   9790  11621   -288   2208    162       C  
ATOM   2183  N   CYS A 572     -64.560 -65.170  30.321  1.00 87.02           N  
ANISOU 2183  N   CYS A 572    10243  10816  12005   -951   3474   -474       N  
ATOM   2184  CA  CYS A 572     -63.334 -64.443  30.626  1.00 86.98           C  
ANISOU 2184  CA  CYS A 572    10476  10974  11598  -1202   3428   -701       C  
ATOM   2185  C   CYS A 572     -63.018 -64.422  32.121  1.00 89.77           C  
ANISOU 2185  C   CYS A 572    11180  11499  11429  -1581   3600   -827       C  
ATOM   2186  O   CYS A 572     -61.862 -64.543  32.519  1.00 89.62           O  
ANISOU 2186  O   CYS A 572    11295  11769  10987  -1825   3316   -868       O  
ATOM   2187  CB  CYS A 572     -63.426 -63.028  30.081  1.00 87.51           C  
ANISOU 2187  CB  CYS A 572    10569  10796  11881  -1162   3751   -886       C  
ATOM   2188  SG  CYS A 572     -63.303 -63.006  28.305  1.00 84.11           S  
ANISOU 2188  SG  CYS A 572     9768  10314  11873   -837   3405   -732       S  
ATOM   2189  N   LYS A 573     -64.061 -64.278  32.935  1.00 92.26           N  
ANISOU 2189  N   LYS A 573    11633  11642  11778  -1652   4066   -867       N  
ATOM   2190  CA  LYS A 573     -63.920 -64.235  34.390  1.00 95.80           C  
ANISOU 2190  CA  LYS A 573    12448  12252  11697  -2063   4298  -1001       C  
ATOM   2191  C   LYS A 573     -63.384 -65.541  34.935  1.00 94.94           C  
ANISOU 2191  C   LYS A 573    12304  12513  11255  -2183   3826   -747       C  
ATOM   2192  O   LYS A 573     -62.425 -65.537  35.711  1.00 96.73           O  
ANISOU 2192  O   LYS A 573    12753  13054  10943  -2556   3655   -792       O  
ATOM   2193  CB  LYS A 573     -65.234 -63.828  35.091  1.00 98.94           C  
ANISOU 2193  CB  LYS A 573    12989  12343  12258  -2099   4963  -1102       C  
ATOM   2194  CG  LYS A 573     -65.589 -62.371  34.826  1.00102.24           C  
ANISOU 2194  CG  LYS A 573    13497  12390  12959  -2088   5523  -1381       C  
ATOM   2195  CD  LYS A 573     -66.537 -61.749  35.861  1.00109.19           C  
ANISOU 2195  CD  LYS A 573    14654  12989  13843  -2296   6295  -1599       C  
ATOM   2196  CE  LYS A 573     -66.561 -60.219  35.681  1.00111.65           C  
ANISOU 2196  CE  LYS A 573    15089  12948  14382  -2364   6852  -1924       C  
ATOM   2197  NZ  LYS A 573     -67.496 -59.561  36.618  1.00116.57           N1+
ANISOU 2197  NZ  LYS A 573    15967  13223  15099  -2560   7693  -2166       N1+
ATOM   2198  N   ILE A 574     -63.979 -66.656  34.512  1.00 92.18           N  
ANISOU 2198  N   ILE A 574    11653  12126  11246  -1884   3605   -456       N  
ATOM   2199  CA  ILE A 574     -63.601 -67.930  35.084  1.00 91.98           C  
ANISOU 2199  CA  ILE A 574    11559  12396  10992  -1981   3223   -179       C  
ATOM   2200  C   ILE A 574     -62.241 -68.337  34.537  1.00 89.70           C  
ANISOU 2200  C   ILE A 574    11115  12351  10613  -1982   2667    -69       C  
ATOM   2201  O   ILE A 574     -61.432 -68.880  35.265  1.00 91.23           O  
ANISOU 2201  O   ILE A 574    11364  12856  10440  -2242   2383     90       O  
ATOM   2202  CB  ILE A 574     -64.700 -69.064  34.987  1.00 91.17           C  
ANISOU 2202  CB  ILE A 574    11201  12166  11270  -1705   3211     95       C  
ATOM   2203  CG1 ILE A 574     -64.314 -70.155  33.999  1.00 88.87           C  
ANISOU 2203  CG1 ILE A 574    10534  11926  11303  -1423   2699    338       C  
ATOM   2204  CG2 ILE A 574     -66.142 -68.538  34.761  1.00 91.06           C  
ANISOU 2204  CG2 ILE A 574    11156  11765  11676  -1497   3717     13       C  
ATOM   2205  CD1 ILE A 574     -63.567 -71.312  34.655  1.00 92.12           C  
ANISOU 2205  CD1 ILE A 574    10878  12644  11478  -1577   2313    617       C  
ATOM   2206  N   MET A 575     -61.966 -68.027  33.277  1.00 86.63           N  
ANISOU 2206  N   MET A 575    10532  11825  10558  -1719   2526   -136       N  
ATOM   2207  CA  MET A 575     -60.660 -68.331  32.709  1.00 85.36           C  
ANISOU 2207  CA  MET A 575    10228  11853  10349  -1717   2063    -61       C  
ATOM   2208  C   MET A 575     -59.494 -67.614  33.383  1.00 87.86           C  
ANISOU 2208  C   MET A 575    10801  12415  10166  -2100   1991   -186       C  
ATOM   2209  O   MET A 575     -58.420 -68.193  33.528  1.00 88.53           O  
ANISOU 2209  O   MET A 575    10790  12751  10095  -2223   1588      3       O  
ATOM   2210  CB  MET A 575     -60.630 -68.017  31.237  1.00 81.93           C  
ANISOU 2210  CB  MET A 575     9580  11226  10321  -1407   1986   -145       C  
ATOM   2211  CG  MET A 575     -61.086 -69.133  30.402  1.00 80.38           C  
ANISOU 2211  CG  MET A 575     9060  10939  10541  -1106   1777     53       C  
ATOM   2212  SD  MET A 575     -61.070 -68.544  28.723  1.00 79.85           S  
ANISOU 2212  SD  MET A 575     8813  10692  10832   -847   1728    -78       S  
ATOM   2213  CE  MET A 575     -59.560 -69.212  28.070  1.00 76.28           C  
ANISOU 2213  CE  MET A 575     8198  10418  10367   -845   1272    -18       C  
ATOM   2214  N   LYS A 576     -59.704 -66.355  33.761  1.00 89.92           N  
ANISOU 2214  N   LYS A 576    11363  12583  10218  -2294   2392   -494       N  
ATOM   2215  CA  LYS A 576     -58.702 -65.556  34.456  1.00 92.73           C  
ANISOU 2215  CA  LYS A 576    12009  13157  10065  -2716   2384   -668       C  
ATOM   2216  C   LYS A 576     -58.436 -66.114  35.845  1.00 96.91           C  
ANISOU 2216  C   LYS A 576    12728  14024  10068  -3140   2279   -508       C  
ATOM   2217  O   LYS A 576     -57.302 -66.089  36.328  1.00 98.63           O  
ANISOU 2217  O   LYS A 576    13029  14559   9885  -3480   1973   -432       O  
ATOM   2218  CB  LYS A 576     -59.175 -64.104  34.540  1.00 94.28           C  
ANISOU 2218  CB  LYS A 576    12482  13105  10232  -2820   2936  -1063       C  
ATOM   2219  CG  LYS A 576     -58.569 -63.260  35.650  1.00 99.46           C  
ANISOU 2219  CG  LYS A 576    13554  13952  10283  -3368   3125  -1316       C  
ATOM   2220  CD  LYS A 576     -57.200 -62.722  35.301  1.00101.36           C  
ANISOU 2220  CD  LYS A 576    13807  14365  10340  -3523   2811  -1390       C  
ATOM   2221  CE  LYS A 576     -56.556 -62.034  36.500  1.00107.35           C  
ANISOU 2221  CE  LYS A 576    14982  15379  10426  -4148   2930  -1606       C  
ATOM   2222  NZ  LYS A 576     -56.050 -63.026  37.495  1.00111.60           N1+
ANISOU 2222  NZ  LYS A 576    15555  16357  10489  -4498   2535  -1288       N1+
ATOM   2223  N   ASP A 577     -59.486 -66.618  36.485  1.00 98.84           N  
ANISOU 2223  N   ASP A 577    13028  14212  10313  -3139   2523   -425       N  
ATOM   2224  CA  ASP A 577     -59.343 -67.202  37.799  1.00103.32           C  
ANISOU 2224  CA  ASP A 577    13766  15113  10377  -3547   2433   -235       C  
ATOM   2225  C   ASP A 577     -58.481 -68.448  37.739  1.00102.70           C  
ANISOU 2225  C   ASP A 577    13367  15316  10337  -3510   1814    223       C  
ATOM   2226  O   ASP A 577     -57.585 -68.622  38.574  1.00105.78           O  
ANISOU 2226  O   ASP A 577    13851  16085  10253  -3933   1527    408       O  
ATOM   2227  CB  ASP A 577     -60.706 -67.487  38.420  1.00105.24           C  
ANISOU 2227  CB  ASP A 577    14114  15201  10669  -3516   2858   -239       C  
ATOM   2228  CG  ASP A 577     -61.476 -66.209  38.742  1.00109.10           C  
ANISOU 2228  CG  ASP A 577    14956  15419  11078  -3659   3546   -684       C  
ATOM   2229  OD1 ASP A 577     -62.496 -66.298  39.479  1.00113.29           O  
ANISOU 2229  OD1 ASP A 577    15649  15844  11549  -3747   3971   -727       O  
ATOM   2230  OD2 ASP A 577     -61.056 -65.119  38.265  1.00108.51           O1-
ANISOU 2230  OD2 ASP A 577    14984  15213  11030  -3683   3690   -985       O1-
ATOM   2231  N   ILE A 578     -58.713 -69.297  36.738  1.00 99.27           N  
ANISOU 2231  N   ILE A 578    12540  14693  10482  -3033   1611    417       N  
ATOM   2232  CA  ILE A 578     -57.918 -70.509  36.643  1.00 99.19           C  
ANISOU 2232  CA  ILE A 578    12193  14877  10615  -2974   1093    848       C  
ATOM   2233  C   ILE A 578     -56.483 -70.141  36.256  1.00 99.07           C  
ANISOU 2233  C   ILE A 578    12108  15021  10510  -3093    750    863       C  
ATOM   2234  O   ILE A 578     -55.536 -70.615  36.868  1.00101.92           O  
ANISOU 2234  O   ILE A 578    12389  15697  10638  -3373    385   1186       O  
ATOM   2235  CB  ILE A 578     -58.532 -71.666  35.743  1.00 95.93           C  
ANISOU 2235  CB  ILE A 578    11380  14218  10850  -2480    990   1050       C  
ATOM   2236  CG1 ILE A 578     -57.754 -71.844  34.461  1.00 93.97           C  
ANISOU 2236  CG1 ILE A 578    10840  13852  11012  -2195    719   1052       C  
ATOM   2237  CG2 ILE A 578     -60.031 -71.545  35.474  1.00 93.87           C  
ANISOU 2237  CG2 ILE A 578    11163  13644  10856  -2220   1404    872       C  
ATOM   2238  CD1 ILE A 578     -56.557 -72.745  34.646  1.00 97.39           C  
ANISOU 2238  CD1 ILE A 578    11009  14506  11488  -2295    267   1442       C  
ATOM   2239  N   LEU A 579     -56.321 -69.267  35.273  1.00 96.79           N  
ANISOU 2239  N   LEU A 579    11841  14523  10412  -2902    868    546       N  
ATOM   2240  CA  LEU A 579     -54.991 -68.851  34.847  1.00 96.81           C  
ANISOU 2240  CA  LEU A 579    11779  14645  10360  -2995    579    538       C  
ATOM   2241  C   LEU A 579     -54.301 -67.882  35.805  1.00101.49           C  
ANISOU 2241  C   LEU A 579    12720  15511  10327  -3527    601    400       C  
ATOM   2242  O   LEU A 579     -53.191 -67.424  35.541  1.00101.90           O  
ANISOU 2242  O   LEU A 579    12746  15675  10296  -3652    373    383       O  
ATOM   2243  CB  LEU A 579     -55.064 -68.216  33.471  1.00 92.63           C  
ANISOU 2243  CB  LEU A 579    11160  13812  10222  -2634    705    253       C  
ATOM   2244  CG  LEU A 579     -55.259 -69.148  32.296  1.00 88.30           C  
ANISOU 2244  CG  LEU A 579    10236  13056  10255  -2184    559    389       C  
ATOM   2245  CD1 LEU A 579     -54.870 -68.411  31.063  1.00 84.75           C  
ANISOU 2245  CD1 LEU A 579     9730  12438  10031  -1983    581    151       C  
ATOM   2246  CD2 LEU A 579     -54.396 -70.367  32.442  1.00 89.31           C  
ANISOU 2246  CD2 LEU A 579    10064  13346  10523  -2199    150    794       C  
ATOM   2247  N   GLU A 580     -54.977 -67.559  36.900  1.00105.87           N  
ANISOU 2247  N   GLU A 580    13613  16166  10445  -3858    900    283       N  
ATOM   2248  CA  GLU A 580     -54.467 -66.667  37.947  1.00111.13           C  
ANISOU 2248  CA  GLU A 580    14677  17109  10436  -4455    985    109       C  
ATOM   2249  C   GLU A 580     -53.122 -65.976  37.678  1.00111.49           C  
ANISOU 2249  C   GLU A 580    14732  17306  10322  -4662    712     48       C  
ATOM   2250  O   GLU A 580     -53.088 -64.955  36.997  1.00109.91           O  
ANISOU 2250  O   GLU A 580    14634  16872  10254  -4537    952   -323       O  
ATOM   2251  CB  GLU A 580     -54.468 -67.389  39.299  1.00116.09           C  
ANISOU 2251  CB  GLU A 580    15413  18122  10574  -4902    828    437       C  
ATOM   2252  CG  GLU A 580     -53.840 -68.783  39.277  1.00117.32           C  
ANISOU 2252  CG  GLU A 580    15128  18484  10964  -4792    263   1046       C  
ATOM   2253  CD  GLU A 580     -54.145 -69.575  40.531  1.00122.82           C  
ANISOU 2253  CD  GLU A 580    15888  19501  11275  -5148    169   1406       C  
ATOM   2254  OE1 GLU A 580     -54.202 -68.966  41.622  1.00128.00           O  
ANISOU 2254  OE1 GLU A 580    16961  20424  11246  -5715    341   1256       O  
ATOM   2255  OE2 GLU A 580     -54.328 -70.808  40.426  1.00122.69           O1-
ANISOU 2255  OE2 GLU A 580    15510  19469  11638  -4883    -59   1833       O1-
ATOM   2256  N   LYS A 581     -52.026 -66.528  38.193  1.00114.16           N  
ANISOU 2256  N   LYS A 581    14933  18023  10417  -4973    210    448       N  
ATOM   2257  CA  LYS A 581     -50.758 -65.787  38.259  1.00116.24           C  
ANISOU 2257  CA  LYS A 581    15274  18501  10390  -5321    -35    404       C  
ATOM   2258  C   LYS A 581     -50.110 -65.538  36.904  1.00111.94           C  
ANISOU 2258  C   LYS A 581    14449  17709  10374  -4894   -165    333       C  
ATOM   2259  O   LYS A 581     -49.309 -64.617  36.775  1.00112.82           O  
ANISOU 2259  O   LYS A 581    14683  17876  10307  -5104   -204    140       O  
ATOM   2260  CB  LYS A 581     -49.749 -66.464  39.207  1.00120.80           C  
ANISOU 2260  CB  LYS A 581    15735  19573  10587  -5804   -574    935       C  
ATOM   2261  CG  LYS A 581     -50.118 -66.423  40.708  1.00127.40           C  
ANISOU 2261  CG  LYS A 581    16949  20778  10676  -6442   -481    974       C  
ATOM   2262  CD  LYS A 581     -48.907 -66.745  41.610  1.00133.25           C  
ANISOU 2262  CD  LYS A 581    17615  22071  10942  -7050  -1055   1475       C  
ATOM   2263  CE  LYS A 581     -49.243 -66.587  43.093  1.00138.93           C  
ANISOU 2263  CE  LYS A 581    18770  23203  10814  -7778   -952   1471       C  
ATOM   2264  NZ  LYS A 581     -48.398 -67.450  43.976  1.00143.64           N1+
ANISOU 2264  NZ  LYS A 581    19141  24345  11089  -8254  -1575   2192       N1+
ATOM   2265  N   LYS A 582     -50.479 -66.344  35.904  1.00107.96           N  
ANISOU 2265  N   LYS A 582    13586  16933  10498  -4326   -207    470       N  
ATOM   2266  CA  LYS A 582     -49.826 -66.361  34.577  1.00104.04           C  
ANISOU 2266  CA  LYS A 582    12779  16227  10524  -3924   -365    469       C  
ATOM   2267  C   LYS A 582     -50.303 -65.281  33.608  1.00100.84           C  
ANISOU 2267  C   LYS A 582    12512  15488  10313  -3652     14    -11       C  
ATOM   2268  O   LYS A 582     -49.606 -64.949  32.644  1.00 98.69           O  
ANISOU 2268  O   LYS A 582    12083  15104  10309  -3459    -90    -77       O  
ATOM   2269  CB  LYS A 582     -49.977 -67.740  33.926  1.00101.56           C  
ANISOU 2269  CB  LYS A 582    12033  15775  10777  -3497   -558    812       C  
ATOM   2270  CG  LYS A 582     -49.136 -68.821  34.606  1.00105.27           C  
ANISOU 2270  CG  LYS A 582    12223  16532  11243  -3702  -1008   1381       C  
ATOM   2271  CD  LYS A 582     -49.450 -70.244  34.119  1.00104.96           C  
ANISOU 2271  CD  LYS A 582    11777  16318  11785  -3307  -1111   1705       C  
ATOM   2272  CE  LYS A 582     -50.877 -70.693  34.420  1.00103.50           C  
ANISOU 2272  CE  LYS A 582    11699  16019  11604  -3169   -832   1633       C  
ATOM   2273  NZ  LYS A 582     -50.983 -72.171  34.582  1.00104.42           N1+
ANISOU 2273  NZ  LYS A 582    11452  16129  12092  -3019  -1027   2097       N1+
ATOM   2274  N   VAL A 583     -51.487 -64.738  33.870  1.00100.97           N  
ANISOU 2274  N   VAL A 583    12801  15340  10223  -3644    467   -313       N  
ATOM   2275  CA  VAL A 583     -52.111 -63.756  32.986  1.00 98.36           C  
ANISOU 2275  CA  VAL A 583    12555  14667  10151  -3371    858   -698       C  
ATOM   2276  C   VAL A 583     -52.728 -62.607  33.794  1.00101.40           C  
ANISOU 2276  C   VAL A 583    13366  14991  10168  -3692   1345  -1072       C  
ATOM   2277  O   VAL A 583     -53.359 -62.827  34.838  1.00104.20           O  
ANISOU 2277  O   VAL A 583    13931  15443  10214  -3945   1528  -1067       O  
ATOM   2278  CB  VAL A 583     -53.144 -64.455  32.033  1.00 94.71           C  
ANISOU 2278  CB  VAL A 583    11834  13920  10231  -2852    958   -630       C  
ATOM   2279  CG1 VAL A 583     -54.473 -63.712  31.950  1.00 94.39           C  
ANISOU 2279  CG1 VAL A 583    11969  13589  10304  -2727   1479   -914       C  
ATOM   2280  CG2 VAL A 583     -52.546 -64.656  30.666  1.00 91.05           C  
ANISOU 2280  CG2 VAL A 583    11062  13339  10191  -2508    729   -575       C  
ATOM   2281  N   GLU A 584     -52.526 -61.381  33.316  1.00101.04           N  
ANISOU 2281  N   GLU A 584    13448  14771  10172  -3696   1584  -1400       N  
ATOM   2282  CA  GLU A 584     -53.089 -60.212  33.976  1.00104.34           C  
ANISOU 2282  CA  GLU A 584    14253  15051  10338  -3983   2127  -1796       C  
ATOM   2283  C   GLU A 584     -54.566 -60.044  33.639  1.00102.67           C  
ANISOU 2283  C   GLU A 584    14024  14458  10525  -3649   2618  -1921       C  
ATOM   2284  O   GLU A 584     -55.369 -59.673  34.493  1.00105.83           O  
ANISOU 2284  O   GLU A 584    14704  14765  10741  -3869   3076  -2118       O  
ATOM   2285  CB  GLU A 584     -52.296 -58.944  33.638  1.00105.16           C  
ANISOU 2285  CB  GLU A 584    14482  15086  10387  -4132   2224  -2086       C  
ATOM   2286  CG  GLU A 584     -52.305 -57.893  34.773  1.00112.25           C  
ANISOU 2286  CG  GLU A 584    15849  16020  10778  -4699   2642  -2467       C  
ATOM   2287  CD  GLU A 584     -51.102 -56.937  34.715  1.00117.40           C  
ANISOU 2287  CD  GLU A 584    16623  16774  11210  -5004   2531  -2658       C  
ATOM   2288  OE1 GLU A 584     -50.765 -56.341  35.773  1.00121.95           O  
ANISOU 2288  OE1 GLU A 584    17577  17525  11231  -5596   2689  -2898       O  
ATOM   2289  OE2 GLU A 584     -50.492 -56.784  33.618  1.00114.95           O1-
ANISOU 2289  OE2 GLU A 584    16038  16374  11262  -4680   2293  -2575       O1-
ATOM   2290  N   LYS A 585     -54.926 -60.338  32.396  1.00 98.24           N  
ANISOU 2290  N   LYS A 585    13129  13684  10513  -3142   2527  -1790       N  
ATOM   2291  CA  LYS A 585     -56.288 -60.116  31.920  1.00 96.71           C  
ANISOU 2291  CA  LYS A 585    12854  13127  10764  -2814   2943  -1849       C  
ATOM   2292  C   LYS A 585     -56.629 -61.076  30.796  1.00 91.73           C  
ANISOU 2292  C   LYS A 585    11830  12434  10589  -2351   2641  -1561       C  
ATOM   2293  O   LYS A 585     -55.786 -61.366  29.948  1.00 89.31           O  
ANISOU 2293  O   LYS A 585    11315  12224  10394  -2206   2255  -1448       O  
ATOM   2294  CB  LYS A 585     -56.415 -58.662  31.446  1.00 97.47           C  
ANISOU 2294  CB  LYS A 585    13036  12920  11075  -2784   3362  -2147       C  
ATOM   2295  CG  LYS A 585     -57.795 -58.232  30.997  1.00 98.69           C  
ANISOU 2295  CG  LYS A 585    13084  12670  11742  -2485   3838  -2174       C  
ATOM   2296  CD  LYS A 585     -58.182 -56.858  31.582  1.00105.25           C  
ANISOU 2296  CD  LYS A 585    14200  13212  12575  -2719   4505  -2534       C  
ATOM   2297  CE  LYS A 585     -57.371 -55.683  31.011  1.00105.67           C  
ANISOU 2297  CE  LYS A 585    14273  13167  12708  -2766   4564  -2733       C  
ATOM   2298  NZ  LYS A 585     -57.530 -54.484  31.911  1.00111.58           N1+
ANISOU 2298  NZ  LYS A 585    15384  13696  13312  -3136   5207  -3139       N1+
ATOM   2299  N   VAL A 586     -57.851 -61.588  30.796  1.00 90.33           N  
ANISOU 2299  N   VAL A 586    11557  12093  10670  -2145   2829  -1450       N  
ATOM   2300  CA  VAL A 586     -58.360 -62.251  29.591  1.00 86.12           C  
ANISOU 2300  CA  VAL A 586    10669  11439  10612  -1726   2636  -1238       C  
ATOM   2301  C   VAL A 586     -59.581 -61.529  29.016  1.00 85.34           C  
ANISOU 2301  C   VAL A 586    10481  10985  10956  -1495   3050  -1283       C  
ATOM   2302  O   VAL A 586     -60.551 -61.197  29.722  1.00 87.29           O  
ANISOU 2302  O   VAL A 586    10860  11047  11256  -1556   3492  -1353       O  
ATOM   2303  CB  VAL A 586     -58.543 -63.803  29.703  1.00 85.04           C  
ANISOU 2303  CB  VAL A 586    10349  11454  10508  -1618   2305   -951       C  
ATOM   2304  CG1 VAL A 586     -58.787 -64.247  31.104  1.00 88.04           C  
ANISOU 2304  CG1 VAL A 586    10936  11975  10538  -1889   2408   -908       C  
ATOM   2305  CG2 VAL A 586     -59.662 -64.294  28.792  1.00 83.39           C  
ANISOU 2305  CG2 VAL A 586     9869  11033  10779  -1262   2342   -803       C  
ATOM   2306  N   VAL A 587     -59.504 -61.297  27.710  1.00 81.93           N  
ANISOU 2306  N   VAL A 587     9807  10464  10858  -1243   2903  -1216       N  
ATOM   2307  CA  VAL A 587     -60.433 -60.419  27.036  1.00 81.05           C  
ANISOU 2307  CA  VAL A 587     9568  10042  11183  -1055   3240  -1208       C  
ATOM   2308  C   VAL A 587     -61.004 -61.076  25.781  1.00 78.39           C  
ANISOU 2308  C   VAL A 587     8882   9675  11227   -752   2979   -944       C  
ATOM   2309  O   VAL A 587     -60.407 -62.010  25.250  1.00 75.91           O  
ANISOU 2309  O   VAL A 587     8450   9567  10823   -697   2549   -852       O  
ATOM   2310  CB  VAL A 587     -59.736 -59.072  26.721  1.00 81.14           C  
ANISOU 2310  CB  VAL A 587     9669   9965  11193  -1141   3400  -1411       C  
ATOM   2311  CG1 VAL A 587     -59.315 -58.400  28.003  1.00 83.17           C  
ANISOU 2311  CG1 VAL A 587    10296  10233  11071  -1495   3713  -1702       C  
ATOM   2312  CG2 VAL A 587     -58.542 -59.282  25.871  1.00 77.72           C  
ANISOU 2312  CG2 VAL A 587     9132   9748  10646  -1105   2942  -1387       C  
ATOM   2313  N   VAL A 588     -62.159 -60.606  25.316  1.00 79.17           N  
ANISOU 2313  N   VAL A 588     8807   9513  11761   -584   3249   -811       N  
ATOM   2314  CA  VAL A 588     -62.621 -61.002  23.987  1.00 78.10           C  
ANISOU 2314  CA  VAL A 588     8342   9377  11953   -364   2983   -559       C  
ATOM   2315  C   VAL A 588     -61.824 -60.288  22.884  1.00 77.52           C  
ANISOU 2315  C   VAL A 588     8178   9359  11916   -335   2810   -585       C  
ATOM   2316  O   VAL A 588     -61.738 -59.077  22.877  1.00 79.25           O  
ANISOU 2316  O   VAL A 588     8440   9414  12254   -365   3095   -669       O  
ATOM   2317  CB  VAL A 588     -64.116 -60.768  23.786  1.00 79.21           C  
ANISOU 2317  CB  VAL A 588     8270   9250  12576   -213   3267   -323       C  
ATOM   2318  CG1 VAL A 588     -64.457 -60.839  22.316  1.00 77.51           C  
ANISOU 2318  CG1 VAL A 588     7725   9063  12661    -64   2989    -58       C  
ATOM   2319  CG2 VAL A 588     -64.898 -61.812  24.531  1.00 79.25           C  
ANISOU 2319  CG2 VAL A 588     8286   9253  12572   -197   3297   -231       C  
ATOM   2320  N   SER A 589     -61.250 -61.049  21.959  1.00 75.95           N  
ANISOU 2320  N   SER A 589     7853   9373  11631   -288   2378   -521       N  
ATOM   2321  CA  SER A 589     -60.376 -60.510  20.929  1.00 75.55           C  
ANISOU 2321  CA  SER A 589     7738   9412  11554   -285   2193   -559       C  
ATOM   2322  C   SER A 589     -61.096 -59.724  19.856  1.00 76.45           C  
ANISOU 2322  C   SER A 589     7610   9398  12037   -178   2270   -346       C  
ATOM   2323  O   SER A 589     -62.306 -59.873  19.671  1.00 77.73           O  
ANISOU 2323  O   SER A 589     7587   9440  12504    -90   2359   -108       O  
ATOM   2324  CB  SER A 589     -59.681 -61.657  20.228  1.00 73.64           C  
ANISOU 2324  CB  SER A 589     7423   9404  11151   -279   1766   -551       C  
ATOM   2325  OG  SER A 589     -58.575 -61.167  19.484  1.00 74.49           O  
ANISOU 2325  OG  SER A 589     7537   9613  11150   -315   1617   -651       O  
ATOM   2326  N   ASN A 590     -60.336 -58.896  19.140  1.00 76.48           N  
ANISOU 2326  N   ASN A 590     7593   9437  12028   -197   2219   -393       N  
ATOM   2327  CA  ASN A 590     -60.804 -58.278  17.886  1.00 77.53           C  
ANISOU 2327  CA  ASN A 590     7459   9535  12461   -125   2173   -136       C  
ATOM   2328  C   ASN A 590     -59.859 -58.569  16.693  1.00 75.75           C  
ANISOU 2328  C   ASN A 590     7181   9563  12035   -168   1795   -157       C  
ATOM   2329  O   ASN A 590     -60.085 -58.113  15.580  1.00 76.26           O  
ANISOU 2329  O   ASN A 590     7045   9669  12259   -159   1700     53       O  
ATOM   2330  CB  ASN A 590     -61.029 -56.768  18.069  1.00 79.77           C  
ANISOU 2330  CB  ASN A 590     7711   9553  13045   -102   2573   -102       C  
ATOM   2331  CG  ASN A 590     -59.739 -56.014  18.420  1.00 81.49           C  
ANISOU 2331  CG  ASN A 590     8155   9784  13021   -201   2655   -409       C  
ATOM   2332  OD1 ASN A 590     -58.713 -56.611  18.811  1.00 82.97           O  
ANISOU 2332  OD1 ASN A 590     8548  10163  12811   -296   2450   -647       O  
ATOM   2333  ND2 ASN A 590     -59.785 -54.700  18.282  1.00 82.71           N  
ANISOU 2333  ND2 ASN A 590     8247   9724  13453   -186   2956   -376       N  
ATOM   2334  N   ARG A 591     -58.828 -59.372  16.924  1.00 74.23           N  
ANISOU 2334  N   ARG A 591     7153   9540  11510   -230   1589   -386       N  
ATOM   2335  CA  ARG A 591     -57.781 -59.535  15.956  1.00 73.02           C  
ANISOU 2335  CA  ARG A 591     6986   9573  11183   -279   1329   -464       C  
ATOM   2336  C   ARG A 591     -57.667 -60.940  15.358  1.00 71.99           C  
ANISOU 2336  C   ARG A 591     6805   9617  10930   -311   1037   -473       C  
ATOM   2337  O   ARG A 591     -56.830 -61.176  14.460  1.00 72.06           O  
ANISOU 2337  O   ARG A 591     6800   9767  10811   -369    855   -553       O  
ATOM   2338  CB  ARG A 591     -56.452 -59.047  16.566  1.00 72.84           C  
ANISOU 2338  CB  ARG A 591     7162   9563  10948   -341   1375   -716       C  
ATOM   2339  CG  ARG A 591     -55.685 -60.064  17.409  1.00 73.01           C  
ANISOU 2339  CG  ARG A 591     7331   9683  10724   -400   1243   -880       C  
ATOM   2340  CD  ARG A 591     -54.404 -59.452  18.016  1.00 72.70           C  
ANISOU 2340  CD  ARG A 591     7462   9671  10488   -502   1268  -1073       C  
ATOM   2341  NE  ARG A 591     -54.726 -58.694  19.213  1.00 73.36           N  
ANISOU 2341  NE  ARG A 591     7712   9624  10535   -577   1554  -1155       N  
ATOM   2342  CZ  ARG A 591     -54.149 -57.549  19.551  1.00 76.41           C  
ANISOU 2342  CZ  ARG A 591     8223   9941  10865   -673   1727  -1297       C  
ATOM   2343  NH1 ARG A 591     -53.203 -57.003  18.782  1.00 76.73           N1+
ANISOU 2343  NH1 ARG A 591     8221  10036  10897   -678   1619  -1343       N1+
ATOM   2344  NH2 ARG A 591     -54.524 -56.937  20.661  1.00 78.37           N  
ANISOU 2344  NH2 ARG A 591     8649  10058  11069   -783   2036  -1409       N  
ATOM   2345  N   LEU A 592     -58.512 -61.863  15.825  1.00 71.95           N  
ANISOU 2345  N   LEU A 592     6769   9582  10986   -283   1025   -400       N  
ATOM   2346  CA  LEU A 592     -58.448 -63.295  15.424  1.00 70.36           C  
ANISOU 2346  CA  LEU A 592     6527   9498  10706   -322    801   -437       C  
ATOM   2347  C   LEU A 592     -59.587 -63.694  14.484  1.00 71.00           C  
ANISOU 2347  C   LEU A 592     6421   9626  10928   -357    692   -227       C  
ATOM   2348  O   LEU A 592     -60.682 -63.135  14.567  1.00 72.42           O  
ANISOU 2348  O   LEU A 592     6485   9711  11319   -313    803      2       O  
ATOM   2349  CB  LEU A 592     -58.489 -64.189  16.663  1.00 69.63           C  
ANISOU 2349  CB  LEU A 592     6528   9355  10574   -290    838   -500       C  
ATOM   2350  CG  LEU A 592     -57.496 -63.794  17.748  1.00 68.60           C  
ANISOU 2350  CG  LEU A 592     6580   9210  10274   -313    925   -652       C  
ATOM   2351  CD1 LEU A 592     -57.812 -64.457  19.065  1.00 67.77           C  
ANISOU 2351  CD1 LEU A 592     6559   9066  10124   -315    993   -637       C  
ATOM   2352  CD2 LEU A 592     -56.088 -64.074  17.310  1.00 66.93           C  
ANISOU 2352  CD2 LEU A 592     6393   9108   9927   -365    756   -795       C  
ATOM   2353  N   VAL A 593     -59.323 -64.633  13.578  1.00 70.26           N  
ANISOU 2353  N   VAL A 593     6292   9670  10734   -463    493   -299       N  
ATOM   2354  CA  VAL A 593     -60.384 -65.229  12.767  1.00 71.43           C  
ANISOU 2354  CA  VAL A 593     6288   9893  10959   -562    360   -129       C  
ATOM   2355  C   VAL A 593     -60.375 -66.761  12.823  1.00 71.98           C  
ANISOU 2355  C   VAL A 593     6378   9977  10994   -616    270   -270       C  
ATOM   2356  O   VAL A 593     -61.378 -67.366  13.212  1.00 73.22           O  
ANISOU 2356  O   VAL A 593     6457  10072  11290   -591    269   -143       O  
ATOM   2357  CB  VAL A 593     -60.551 -64.637  11.300  1.00 71.92           C  
ANISOU 2357  CB  VAL A 593     6234  10129  10962   -730    218     18       C  
ATOM   2358  CG1 VAL A 593     -59.439 -63.760  10.901  1.00 70.93           C  
ANISOU 2358  CG1 VAL A 593     6186  10056  10706   -739    246    -96       C  
ATOM   2359  CG2 VAL A 593     -60.737 -65.711  10.272  1.00 72.59           C  
ANISOU 2359  CG2 VAL A 593     6287  10380  10912   -951     25    -39       C  
ATOM   2360  N   THR A 594     -59.263 -67.384  12.461  1.00 71.89           N  
ANISOU 2360  N   THR A 594     6453  10015  10847   -684    224   -521       N  
ATOM   2361  CA  THR A 594     -59.180 -68.838  12.509  1.00 72.47           C  
ANISOU 2361  CA  THR A 594     6523  10051  10959   -732    191   -661       C  
ATOM   2362  C   THR A 594     -58.680 -69.352  13.876  1.00 72.26           C  
ANISOU 2362  C   THR A 594     6550   9889  11017   -573    278   -712       C  
ATOM   2363  O   THR A 594     -59.204 -70.326  14.384  1.00 73.08           O  
ANISOU 2363  O   THR A 594     6604   9916  11245   -543    282   -674       O  
ATOM   2364  CB  THR A 594     -58.349 -69.401  11.333  1.00 72.78           C  
ANISOU 2364  CB  THR A 594     6598  10175  10880   -917    148   -896       C  
ATOM   2365  OG1 THR A 594     -57.178 -68.604  11.154  1.00 73.41           O  
ANISOU 2365  OG1 THR A 594     6755  10285  10851   -891    189  -1002       O  
ATOM   2366  CG2 THR A 594     -59.133 -69.339  10.054  1.00 73.66           C  
ANISOU 2366  CG2 THR A 594     6653  10454  10879  -1156     30   -824       C  
ATOM   2367  N   SER A 595     -57.696 -68.696  14.482  1.00 72.01           N  
ANISOU 2367  N   SER A 595     6607   9840  10910   -496    333   -770       N  
ATOM   2368  CA  SER A 595     -57.190 -69.127  15.781  1.00 72.46           C  
ANISOU 2368  CA  SER A 595     6708   9821  11000   -406    374   -768       C  
ATOM   2369  C   SER A 595     -58.140 -68.821  16.929  1.00 72.98           C  
ANISOU 2369  C   SER A 595     6805   9831  11091   -325    464   -607       C  
ATOM   2370  O   SER A 595     -58.758 -67.760  16.952  1.00 72.66           O  
ANISOU 2370  O   SER A 595     6791   9780  11035   -303    553   -525       O  
ATOM   2371  CB  SER A 595     -55.847 -68.484  16.066  1.00 72.43           C  
ANISOU 2371  CB  SER A 595     6789   9846  10885   -401    380   -858       C  
ATOM   2372  OG  SER A 595     -54.926 -68.824  15.048  1.00 74.22           O  
ANISOU 2372  OG  SER A 595     6980  10095  11125   -468    339  -1008       O  
ATOM   2373  N   PRO A 596     -58.251 -69.761  17.898  1.00 73.92           N  
ANISOU 2373  N   PRO A 596     6909   9897  11277   -286    468   -548       N  
ATOM   2374  CA  PRO A 596     -59.193 -69.622  19.018  1.00 74.55           C  
ANISOU 2374  CA  PRO A 596     7030   9922  11373   -232    583   -405       C  
ATOM   2375  C   PRO A 596     -58.766 -68.591  20.037  1.00 75.18           C  
ANISOU 2375  C   PRO A 596     7276  10019  11269   -250    702   -421       C  
ATOM   2376  O   PRO A 596     -59.613 -68.062  20.746  1.00 76.65           O  
ANISOU 2376  O   PRO A 596     7528  10141  11454   -232    877   -349       O  
ATOM   2377  CB  PRO A 596     -59.218 -71.016  19.654  1.00 74.49           C  
ANISOU 2377  CB  PRO A 596     6949   9878  11474   -214    529   -337       C  
ATOM   2378  CG  PRO A 596     -57.937 -71.627  19.274  1.00 74.55           C  
ANISOU 2378  CG  PRO A 596     6907   9909  11510   -249    421   -437       C  
ATOM   2379  CD  PRO A 596     -57.528 -71.048  17.946  1.00 73.99           C  
ANISOU 2379  CD  PRO A 596     6840   9877  11395   -298    392   -593       C  
ATOM   2380  N   CYS A 597     -57.472 -68.311  20.113  1.00 75.46           N  
ANISOU 2380  N   CYS A 597     7379  10128  11163   -307    631   -522       N  
ATOM   2381  CA  CYS A 597     -56.941 -67.304  21.032  1.00 77.35           C  
ANISOU 2381  CA  CYS A 597     7795  10405  11189   -384    728   -568       C  
ATOM   2382  C   CYS A 597     -55.492 -66.942  20.674  1.00 76.94           C  
ANISOU 2382  C   CYS A 597     7765  10435  11033   -446    608   -675       C  
ATOM   2383  O   CYS A 597     -54.910 -67.504  19.749  1.00 76.41           O  
ANISOU 2383  O   CYS A 597     7576  10378  11077   -417    481   -712       O  
ATOM   2384  CB  CYS A 597     -57.041 -67.785  22.476  1.00 78.33           C  
ANISOU 2384  CB  CYS A 597     8005  10563  11193   -454    761   -474       C  
ATOM   2385  SG  CYS A 597     -56.328 -69.410  22.670  1.00 84.40           S  
ANISOU 2385  SG  CYS A 597     8609  11389  12070   -453    526   -343       S  
ATOM   2386  N   CYS A 598     -54.934 -65.976  21.391  1.00 78.03           N  
ANISOU 2386  N   CYS A 598     8064  10619  10965   -551    678   -737       N  
ATOM   2387  CA  CYS A 598     -53.545 -65.612  21.260  1.00 78.52           C  
ANISOU 2387  CA  CYS A 598     8148  10764  10922   -632    558   -808       C  
ATOM   2388  C   CYS A 598     -53.160 -64.824  22.498  1.00 80.22           C  
ANISOU 2388  C   CYS A 598     8567  11050  10862   -815    633   -844       C  
ATOM   2389  O   CYS A 598     -54.025 -64.411  23.276  1.00 81.26           O  
ANISOU 2389  O   CYS A 598     8839  11138  10896   -868    835   -862       O  
ATOM   2390  CB  CYS A 598     -53.341 -64.772  20.015  1.00 77.46           C  
ANISOU 2390  CB  CYS A 598     7981  10592  10857   -574    591   -922       C  
ATOM   2391  SG  CYS A 598     -53.883 -63.088  20.237  1.00 81.07           S  
ANISOU 2391  SG  CYS A 598     8596  10970  11234   -609    853  -1010       S  
ATOM   2392  N   ILE A 599     -51.861 -64.625  22.689  1.00 81.33           N  
ANISOU 2392  N   ILE A 599     8726  11297  10879   -938    484   -857       N  
ATOM   2393  CA  ILE A 599     -51.379 -63.834  23.816  1.00 83.64           C  
ANISOU 2393  CA  ILE A 599     9227  11690  10860  -1181    528   -909       C  
ATOM   2394  C   ILE A 599     -50.749 -62.555  23.348  1.00 83.97           C  
ANISOU 2394  C   ILE A 599     9355  11706  10844  -1231    603  -1085       C  
ATOM   2395  O   ILE A 599     -49.926 -62.550  22.441  1.00 82.76           O  
ANISOU 2395  O   ILE A 599     9069  11554  10820  -1153    469  -1091       O  
ATOM   2396  CB  ILE A 599     -50.437 -64.631  24.731  1.00 85.07           C  
ANISOU 2396  CB  ILE A 599     9365  12056  10901  -1363    270   -716       C  
ATOM   2397  CG1 ILE A 599     -51.285 -65.366  25.755  1.00 86.63           C  
ANISOU 2397  CG1 ILE A 599     9614  12302  11000  -1428    308   -579       C  
ATOM   2398  CG2 ILE A 599     -49.475 -63.718  25.478  1.00 86.07           C  
ANISOU 2398  CG2 ILE A 599     9666  12329  10708  -1656    220   -777       C  
ATOM   2399  CD1 ILE A 599     -50.792 -66.734  26.086  1.00 89.49           C  
ANISOU 2399  CD1 ILE A 599     9761  12759  11480  -1433     43   -286       C  
ATOM   2400  N   VAL A 600     -51.175 -61.461  23.963  1.00 86.32           N  
ANISOU 2400  N   VAL A 600     9873  11953  10971  -1366    860  -1238       N  
ATOM   2401  CA  VAL A 600     -50.611 -60.155  23.668  1.00 87.71           C  
ANISOU 2401  CA  VAL A 600    10146  12080  11098  -1442    976  -1415       C  
ATOM   2402  C   VAL A 600     -49.959 -59.582  24.923  1.00 91.74           C  
ANISOU 2402  C   VAL A 600    10898  12717  11239  -1796   1002  -1515       C  
ATOM   2403  O   VAL A 600     -50.252 -60.015  26.030  1.00 93.62           O  
ANISOU 2403  O   VAL A 600    11267  13059  11245  -1984   1014  -1468       O  
ATOM   2404  CB  VAL A 600     -51.656 -59.207  23.038  1.00 86.82           C  
ANISOU 2404  CB  VAL A 600    10041  11741  11203  -1289   1307  -1519       C  
ATOM   2405  CG1 VAL A 600     -52.198 -59.825  21.750  1.00 84.54           C  
ANISOU 2405  CG1 VAL A 600     9507  11396  11219  -1011   1207  -1384       C  
ATOM   2406  CG2 VAL A 600     -52.782 -58.900  23.994  1.00 87.31           C  
ANISOU 2406  CG2 VAL A 600    10275  11688  11211  -1371   1642  -1582       C  
ATOM   2407  N   THR A 601     -49.047 -58.641  24.749  1.00 93.97           N  
ANISOU 2407  N   THR A 601    11243  13013  11447  -1918    996  -1644       N  
ATOM   2408  CA  THR A 601     -48.334 -58.107  25.887  1.00 99.04           C  
ANISOU 2408  CA  THR A 601    12117  13805  11708  -2311    984  -1743       C  
ATOM   2409  C   THR A 601     -48.842 -56.714  26.208  1.00102.97           C  
ANISOU 2409  C   THR A 601    12865  14123  12135  -2451   1421  -2043       C  
ATOM   2410  O   THR A 601     -49.329 -56.010  25.327  1.00101.84           O  
ANISOU 2410  O   THR A 601    12647  13747  12299  -2220   1654  -2130       O  
ATOM   2411  CB  THR A 601     -46.818 -58.101  25.661  1.00 98.68           C  
ANISOU 2411  CB  THR A 601    11964  13918  11608  -2422    646  -1656       C  
ATOM   2412  OG1 THR A 601     -46.509 -57.275  24.539  1.00 97.36           O  
ANISOU 2412  OG1 THR A 601    11711  13596  11683  -2238    734  -1775       O  
ATOM   2413  CG2 THR A 601     -46.320 -59.500  25.392  1.00 96.26           C  
ANISOU 2413  CG2 THR A 601    11384  13735  11453  -2286    280  -1347       C  
ATOM   2414  N   SER A 602     -48.747 -56.331  27.479  1.00109.29           N  
ANISOU 2414  N   SER A 602    13957  15026  12540  -2854   1550  -2188       N  
ATOM   2415  CA  SER A 602     -49.204 -55.021  27.938  1.00114.51           C  
ANISOU 2415  CA  SER A 602    14893  15488  13127  -3052   2040  -2522       C  
ATOM   2416  C   SER A 602     -48.473 -53.917  27.182  1.00115.97           C  
ANISOU 2416  C   SER A 602    15035  15549  13476  -3019   2097  -2667       C  
ATOM   2417  O   SER A 602     -47.284 -54.057  26.874  1.00115.56           O  
ANISOU 2417  O   SER A 602    14876  15676  13354  -3070   1725  -2566       O  
ATOM   2418  CB  SER A 602     -48.943 -54.867  29.434  1.00118.76           C  
ANISOU 2418  CB  SER A 602    15778  16227  13118  -3590   2109  -2671       C  
ATOM   2419  OG  SER A 602     -47.587 -54.507  29.667  1.00120.17           O  
ANISOU 2419  OG  SER A 602    16017  16625  13016  -3909   1826  -2697       O  
ATOM   2420  N   THR A 603     -49.182 -52.825  26.894  1.00119.11           N  
ANISOU 2420  N   THR A 603    15494  15624  14136  -2931   2575  -2876       N  
ATOM   2421  CA  THR A 603     -48.611 -51.680  26.151  1.00121.19           C  
ANISOU 2421  CA  THR A 603    15702  15725  14617  -2881   2691  -3005       C  
ATOM   2422  C   THR A 603     -47.338 -51.148  26.804  1.00124.86           C  
ANISOU 2422  C   THR A 603    16368  16372  14698  -3307   2555  -3178       C  
ATOM   2423  O   THR A 603     -46.361 -50.812  26.127  1.00123.31           O  
ANISOU 2423  O   THR A 603    16040  16219  14591  -3256   2334  -3139       O  
ATOM   2424  CB  THR A 603     -49.644 -50.525  25.979  1.00122.77           C  
ANISOU 2424  CB  THR A 603    15947  15515  15186  -2782   3304  -3191       C  
ATOM   2425  OG1 THR A 603     -50.480 -50.432  27.148  1.00125.30           O  
ANISOU 2425  OG1 THR A 603    16541  15735  15331  -3028   3713  -3385       O  
ATOM   2426  CG2 THR A 603     -50.516 -50.772  24.727  1.00120.45           C  
ANISOU 2426  CG2 THR A 603    15309  15047  15407  -2295   3307  -2923       C  
ATOM   2427  N   TYR A 604     -47.377 -51.115  28.135  1.00130.68           N  
ANISOU 2427  N   TYR A 604    17427  17233  14990  -3752   2682  -3356       N  
ATOM   2428  CA  TYR A 604     -46.285 -50.633  28.977  1.00135.94           C  
ANISOU 2428  CA  TYR A 604    18338  18115  15197  -4276   2563  -3529       C  
ATOM   2429  C   TYR A 604     -45.090 -51.622  29.001  1.00136.01           C  
ANISOU 2429  C   TYR A 604    18178  18524  14974  -4361   1887  -3199       C  
ATOM   2430  O   TYR A 604     -43.939 -51.201  28.838  1.00136.59           O  
ANISOU 2430  O   TYR A 604    18215  18708  14974  -4524   1653  -3198       O  
ATOM   2431  CB  TYR A 604     -46.835 -50.315  30.387  1.00140.64           C  
ANISOU 2431  CB  TYR A 604    19351  18727  15358  -4770   2952  -3827       C  
ATOM   2432  CG  TYR A 604     -46.141 -49.177  31.112  1.00145.81           C  
ANISOU 2432  CG  TYR A 604    20339  19395  15666  -5324   3171  -4201       C  
ATOM   2433  CD1 TYR A 604     -45.452 -48.174  30.404  1.00145.92           C  
ANISOU 2433  CD1 TYR A 604    20271  19238  15932  -5265   3231  -4333       C  
ATOM   2434  CD2 TYR A 604     -46.195 -49.084  32.512  1.00151.22           C  
ANISOU 2434  CD2 TYR A 604    21436  20266  15754  -5943   3340  -4439       C  
ATOM   2435  CE1 TYR A 604     -44.805 -47.120  31.075  1.00150.68           C  
ANISOU 2435  CE1 TYR A 604    21185  19842  16223  -5803   3444  -4699       C  
ATOM   2436  CE2 TYR A 604     -45.558 -48.034  33.195  1.00156.37           C  
ANISOU 2436  CE2 TYR A 604    22425  20942  16043  -6522   3555  -4821       C  
ATOM   2437  CZ  TYR A 604     -44.866 -47.057  32.470  1.00156.11           C  
ANISOU 2437  CZ  TYR A 604    22295  20721  16297  -6443   3607  -4955       C  
ATOM   2438  OH  TYR A 604     -44.240 -46.023  33.136  1.00160.55           O  
ANISOU 2438  OH  TYR A 604    23191  21294  16516  -7032   3830  -5348       O  
ATOM   2439  N   GLY A 605     -45.377 -52.921  29.164  1.00135.97           N  
ANISOU 2439  N   GLY A 605    18038  18701  14923  -4232   1599  -2898       N  
ATOM   2440  CA  GLY A 605     -44.353 -53.988  29.202  1.00136.74           C  
ANISOU 2440  CA  GLY A 605    17916  19129  14907  -4277    998  -2523       C  
ATOM   2441  C   GLY A 605     -43.701 -54.331  27.863  1.00134.00           C  
ANISOU 2441  C   GLY A 605    17192  18717  15003  -3849    718  -2303       C  
ATOM   2442  O   GLY A 605     -43.898 -53.624  26.862  1.00132.04           O  
ANISOU 2442  O   GLY A 605    16864  18210  15093  -3558    942  -2445       O  
ATOM   2443  N   TRP A 606     -42.925 -55.420  27.836  1.00134.25           N  
ANISOU 2443  N   TRP A 606    16979  18974  15055  -3824    250  -1942       N  
ATOM   2444  CA  TRP A 606     -42.132 -55.765  26.639  1.00132.06           C  
ANISOU 2444  CA  TRP A 606    16359  18639  15179  -3487      6  -1749       C  
ATOM   2445  C   TRP A 606     -42.277 -57.210  26.117  1.00129.66           C  
ANISOU 2445  C   TRP A 606    15745  18347  15172  -3152   -219  -1428       C  
ATOM   2446  O   TRP A 606     -42.523 -58.139  26.906  1.00131.05           O  
ANISOU 2446  O   TRP A 606    15907  18682  15202  -3269   -371  -1219       O  
ATOM   2447  CB  TRP A 606     -40.669 -55.242  26.729  1.00134.26           C  
ANISOU 2447  CB  TRP A 606    16590  19060  15362  -3759   -256  -1692       C  
ATOM   2448  CG  TRP A 606     -39.708 -55.745  27.844  1.00139.60           C  
ANISOU 2448  CG  TRP A 606    17250  20089  15702  -4218   -674  -1405       C  
ATOM   2449  CD1 TRP A 606     -38.402 -56.131  27.659  1.00141.13           C  
ANISOU 2449  CD1 TRP A 606    17160  20420  16040  -4274  -1078  -1080       C  
ATOM   2450  CD2 TRP A 606     -39.948 -55.845  29.275  1.00144.87           C  
ANISOU 2450  CD2 TRP A 606    18179  21019  15845  -4711   -726  -1390       C  
ATOM   2451  NE1 TRP A 606     -37.830 -56.485  28.861  1.00145.96           N  
ANISOU 2451  NE1 TRP A 606    17805  21371  16278  -4759  -1412   -816       N  
ATOM   2452  CE2 TRP A 606     -38.748 -56.322  29.867  1.00148.02           C  
ANISOU 2452  CE2 TRP A 606    18414  21737  16089  -5054  -1217  -1006       C  
ATOM   2453  CE3 TRP A 606     -41.053 -55.593  30.107  1.00146.80           C  
ANISOU 2453  CE3 TRP A 606    18770  21261  15747  -4913   -397  -1643       C  
ATOM   2454  CZ2 TRP A 606     -38.626 -56.557  31.252  1.00152.30           C  
ANISOU 2454  CZ2 TRP A 606    19133  22637  16094  -5619  -1427   -849       C  
ATOM   2455  CZ3 TRP A 606     -40.928 -55.831  31.491  1.00151.23           C  
ANISOU 2455  CZ3 TRP A 606    19539  22161  15759  -5472   -563  -1538       C  
ATOM   2456  CH2 TRP A 606     -39.721 -56.306  32.042  1.00153.75           C  
ANISOU 2456  CH2 TRP A 606    19694  22836  15886  -5831  -1094  -1136       C  
ATOM   2457  N   THR A 607     -42.122 -57.369  24.790  1.00126.38           N  
ANISOU 2457  N   THR A 607    15091  17759  15166  -2765   -215  -1400       N  
ATOM   2458  CA  THR A 607     -42.662 -58.525  24.000  1.00123.46           C  
ANISOU 2458  CA  THR A 607    14486  17292  15128  -2392   -247  -1243       C  
ATOM   2459  C   THR A 607     -42.015 -59.916  24.149  1.00123.46           C  
ANISOU 2459  C   THR A 607    14212  17407  15287  -2366   -575   -885       C  
ATOM   2460  O   THR A 607     -41.266 -60.177  25.089  1.00126.23           O  
ANISOU 2460  O   THR A 607    14535  17963  15460  -2661   -833   -666       O  
ATOM   2461  CB  THR A 607     -42.773 -58.198  22.466  1.00120.58           C  
ANISOU 2461  CB  THR A 607    13989  16718  15106  -2041    -97  -1362       C  
ATOM   2462  OG1 THR A 607     -41.579 -57.544  22.003  1.00121.23           O  
ANISOU 2462  OG1 THR A 607    13998  16804  15257  -2095   -190  -1381       O  
ATOM   2463  CG2 THR A 607     -43.991 -57.318  22.175  1.00119.66           C  
ANISOU 2463  CG2 THR A 607    14045  16435  14985  -1934    259  -1602       C  
ATOM   2464  N   ALA A 608     -42.346 -60.809  23.219  1.00120.68           N  
ANISOU 2464  N   ALA A 608    13648  16917  15286  -2034   -550   -813       N  
ATOM   2465  CA  ALA A 608     -41.736 -62.136  23.156  1.00120.92           C  
ANISOU 2465  CA  ALA A 608    13376  16968  15598  -1956   -779   -495       C  
ATOM   2466  C   ALA A 608     -40.581 -62.144  22.163  1.00120.12           C  
ANISOU 2466  C   ALA A 608    13041  16770  15827  -1832   -846   -444       C  
ATOM   2467  O   ALA A 608     -39.669 -62.963  22.268  1.00121.41           O  
ANISOU 2467  O   ALA A 608    12934  16949  16245  -1850  -1045   -148       O  
ATOM   2468  CB  ALA A 608     -42.758 -63.172  22.762  1.00119.40           C  
ANISOU 2468  CB  ALA A 608    13097  16657  15611  -1706   -670   -474       C  
ATOM   2469  N   ASN A 609     -40.659 -61.250  21.180  1.00117.96           N  
ANISOU 2469  N   ASN A 609    12853  16379  15586  -1700   -656   -711       N  
ATOM   2470  CA  ASN A 609     -39.578 -61.001  20.245  1.00117.25           C  
ANISOU 2470  CA  ASN A 609    12599  16205  15745  -1615   -676   -713       C  
ATOM   2471  C   ASN A 609     -38.387 -60.421  21.008  1.00120.33           C  
ANISOU 2471  C   ASN A 609    12970  16736  16011  -1897   -894   -572       C  
ATOM   2472  O   ASN A 609     -37.233 -60.814  20.787  1.00121.12           O  
ANISOU 2472  O   ASN A 609    12814  16817  16388  -1898  -1048   -354       O  
ATOM   2473  CB  ASN A 609     -40.059 -60.005  19.194  1.00114.67           C  
ANISOU 2473  CB  ASN A 609    12407  15767  15392  -1469   -432  -1011       C  
ATOM   2474  CG  ASN A 609     -39.157 -59.938  17.995  1.00111.93           C  
ANISOU 2474  CG  ASN A 609    11889  15315  15323  -1334   -396  -1033       C  
ATOM   2475  OD1 ASN A 609     -38.708 -60.958  17.492  1.00110.34           O  
ANISOU 2475  OD1 ASN A 609    11469  15031  15424  -1221   -419   -912       O  
ATOM   2476  ND2 ASN A 609     -38.907 -58.731  17.514  1.00109.17           N  
ANISOU 2476  ND2 ASN A 609    11638  14944  14897  -1350   -300  -1195       N  
ATOM   2477  N   MET A 610     -38.696 -59.497  21.921  1.00122.22           N  
ANISOU 2477  N   MET A 610    13481  17108  15847  -2157   -887   -697       N  
ATOM   2478  CA  MET A 610     -37.706 -58.862  22.774  1.00125.82           C  
ANISOU 2478  CA  MET A 610    13983  17739  16084  -2511  -1096   -600       C  
ATOM   2479  C   MET A 610     -37.139 -59.833  23.804  1.00128.77           C  
ANISOU 2479  C   MET A 610    14183  18311  16433  -2741  -1433   -191       C  
ATOM   2480  O   MET A 610     -35.925 -59.932  23.937  1.00130.85           O  
ANISOU 2480  O   MET A 610    14226  18650  16838  -2881  -1686     78       O  
ATOM   2481  CB  MET A 610     -38.272 -57.605  23.445  1.00127.03           C  
ANISOU 2481  CB  MET A 610    14508  17952  15806  -2764   -925   -903       C  
ATOM   2482  CG  MET A 610     -37.251 -56.846  24.322  1.00132.63           C  
ANISOU 2482  CG  MET A 610    15309  18854  16229  -3203  -1126   -860       C  
ATOM   2483  SD  MET A 610     -36.134 -55.635  23.521  1.00137.21           S  
ANISOU 2483  SD  MET A 610    15841  19333  16959  -3208  -1098  -1001       S  
ATOM   2484  CE  MET A 610     -35.229 -56.594  22.294  1.00134.03           C  
ANISOU 2484  CE  MET A 610    14992  18798  17133  -2837  -1239   -712       C  
ATOM   2485  N   GLU A 611     -38.006 -60.553  24.516  1.00129.61           N  
ANISOU 2485  N   GLU A 611    14356  18498  16391  -2781  -1442   -104       N  
ATOM   2486  CA  GLU A 611     -37.566 -61.601  25.453  1.00132.84           C  
ANISOU 2486  CA  GLU A 611    14557  19095  16818  -2977  -1764    348       C  
ATOM   2487  C   GLU A 611     -36.543 -62.586  24.857  1.00133.74           C  
ANISOU 2487  C   GLU A 611    14211  19096  17506  -2787  -1935    723       C  
ATOM   2488  O   GLU A 611     -35.718 -63.142  25.584  1.00137.15           O  
ANISOU 2488  O   GLU A 611    14399  19689  18020  -3010  -2258   1174       O  
ATOM   2489  CB  GLU A 611     -38.760 -62.376  26.015  1.00132.37           C  
ANISOU 2489  CB  GLU A 611    14591  19071  16632  -2936  -1687    378       C  
ATOM   2490  CG  GLU A 611     -39.086 -62.077  27.468  1.00135.50           C  
ANISOU 2490  CG  GLU A 611    15258  19759  16464  -3385  -1794    420       C  
ATOM   2491  CD  GLU A 611     -40.204 -62.961  28.024  1.00136.26           C  
ANISOU 2491  CD  GLU A 611    15405  19886  16481  -3332  -1726    505       C  
ATOM   2492  OE1 GLU A 611     -40.322 -64.144  27.620  1.00134.59           O  
ANISOU 2492  OE1 GLU A 611    14895  19554  16688  -3050  -1774    747       O  
ATOM   2493  OE2 GLU A 611     -40.972 -62.468  28.879  1.00137.96           O1-
ANISOU 2493  OE2 GLU A 611    15961  20228  16226  -3585  -1595    316       O1-
ATOM   2494  N   ARG A 612     -36.591 -62.787  23.541  1.00131.54           N  
ANISOU 2494  N   ARG A 612    13808  18539  17632  -2404  -1705    552       N  
ATOM   2495  CA  ARG A 612     -35.727 -63.760  22.865  1.00132.64           C  
ANISOU 2495  CA  ARG A 612    13528  18497  18372  -2199  -1749    837       C  
ATOM   2496  C   ARG A 612     -34.449 -63.116  22.373  1.00133.55           C  
ANISOU 2496  C   ARG A 612    13498  18565  18677  -2240  -1815    884       C  
ATOM   2497  O   ARG A 612     -33.449 -63.798  22.168  1.00135.43           O  
ANISOU 2497  O   ARG A 612    13356  18700  19399  -2187  -1919   1227       O  
ATOM   2498  CB  ARG A 612     -36.459 -64.395  21.683  1.00130.04           C  
ANISOU 2498  CB  ARG A 612    13161  17892  18357  -1815  -1429    601       C  
ATOM   2499  CG  ARG A 612     -36.245 -65.905  21.511  1.00132.14           C  
ANISOU 2499  CG  ARG A 612    13055  17985  19167  -1648  -1424    910       C  
ATOM   2500  CD  ARG A 612     -37.538 -66.580  21.005  1.00131.08           C  
ANISOU 2500  CD  ARG A 612    13025  17710  19067  -1419  -1172    671       C  
ATOM   2501  NE  ARG A 612     -38.325 -65.664  20.173  1.00128.50           N  
ANISOU 2501  NE  ARG A 612    13014  17351  18458  -1313   -942    206       N  
ATOM   2502  CZ  ARG A 612     -39.116 -66.024  19.167  1.00126.95           C  
ANISOU 2502  CZ  ARG A 612    12869  16990  18376  -1098   -688    -52       C  
ATOM   2503  NH1 ARG A 612     -39.247 -67.304  18.828  1.00127.23           N1+
ANISOU 2503  NH1 ARG A 612    12690  16849  18801   -960   -588     40       N1+
ATOM   2504  NH2 ARG A 612     -39.769 -65.089  18.486  1.00124.94           N  
ANISOU 2504  NH2 ARG A 612    12868  16746  17857  -1044   -531   -390       N  
ATOM   2505  N   ILE A 613     -34.490 -61.802  22.175  1.00132.69           N  
ANISOU 2505  N   ILE A 613    13672  18505  18236  -2326  -1728    549       N  
ATOM   2506  CA  ILE A 613     -33.304 -61.037  21.777  1.00133.50           C  
ANISOU 2506  CA  ILE A 613    13672  18583  18467  -2396  -1795    572       C  
ATOM   2507  C   ILE A 613     -32.313 -60.865  22.956  1.00137.84           C  
ANISOU 2507  C   ILE A 613    14109  19393  18871  -2814  -2194    958       C  
ATOM   2508  O   ILE A 613     -31.124 -60.631  22.727  1.00139.48           O  
ANISOU 2508  O   ILE A 613    14086  19574  19337  -2876  -2329   1156       O  
ATOM   2509  CB  ILE A 613     -33.690 -59.704  21.044  1.00130.71           C  
ANISOU 2509  CB  ILE A 613    13626  18158  17879  -2320  -1536     96       C  
ATOM   2510  CG1 ILE A 613     -34.318 -60.016  19.677  1.00126.85           C  
ANISOU 2510  CG1 ILE A 613    13124  17425  17648  -1930  -1209   -151       C  
ATOM   2511  CG2 ILE A 613     -32.484 -58.798  20.852  1.00132.08           C  
ANISOU 2511  CG2 ILE A 613    13726  18343  18112  -2456  -1633    125       C  
ATOM   2512  CD1 ILE A 613     -35.092 -58.878  19.049  1.00122.69           C  
ANISOU 2512  CD1 ILE A 613    12892  16850  16872  -1845   -955   -558       C  
ATOM   2513  N   MET A 614     -32.786 -61.016  24.199  1.00140.21           N  
ANISOU 2513  N   MET A 614    14557  19952  18761  -3123  -2388   1091       N  
ATOM   2514  CA  MET A 614     -31.882 -61.056  25.363  1.00145.18           C  
ANISOU 2514  CA  MET A 614    15048  20880  19231  -3576  -2817   1539       C  
ATOM   2515  C   MET A 614     -31.111 -62.394  25.410  1.00147.60           C  
ANISOU 2515  C   MET A 614    14822  21132  20127  -3486  -3045   2152       C  
ATOM   2516  O   MET A 614     -31.661 -63.437  25.789  1.00148.05           O  
ANISOU 2516  O   MET A 614    14763  21198  20289  -3417  -3075   2376       O  
ATOM   2517  CB  MET A 614     -32.613 -60.722  26.687  1.00147.30           C  
ANISOU 2517  CB  MET A 614    15680  21474  18810  -4003  -2932   1469       C  
ATOM   2518  CG  MET A 614     -33.169 -61.914  27.509  1.00149.77           C  
ANISOU 2518  CG  MET A 614    15886  21928  19089  -4070  -3084   1822       C  
ATOM   2519  SD  MET A 614     -33.191 -61.725  29.334  1.00156.87           S  
ANISOU 2519  SD  MET A 614    17014  23343  19245  -4788  -3456   2077       S  
ATOM   2520  CE  MET A 614     -31.452 -61.515  29.758  1.00160.29           C  
ANISOU 2520  CE  MET A 614    17105  24016  19779  -5211  -3966   2622       C  
ATOM   2521  N   LYS A 615     -29.845 -62.355  24.988  1.00149.37           N  
ANISOU 2521  N   LYS A 615    14701  21261  20792  -3470  -3170   2428       N  
ATOM   2522  CA  LYS A 615     -29.019 -63.567  24.808  1.00151.77           C  
ANISOU 2522  CA  LYS A 615    14435  21400  21827  -3317  -3288   2999       C  
ATOM   2523  C   LYS A 615     -27.536 -63.307  25.104  1.00155.68           C  
ANISOU 2523  C   LYS A 615    14579  21997  22575  -3584  -3636   3484       C  
ATOM   2524  O   LYS A 615     -27.077 -63.396  26.245  1.00159.95           O  
ANISOU 2524  O   LYS A 615    14993  22869  22911  -4020  -4076   3967       O  
ATOM   2525  CB  LYS A 615     -29.163 -64.136  23.377  1.00148.66           C  
ANISOU 2525  CB  LYS A 615    13889  20560  22035  -2784  -2847   2759       C  
ATOM   2526  CG  LYS A 615     -30.537 -64.703  22.995  1.00145.26           C  
ANISOU 2526  CG  LYS A 615    13678  19994  21518  -2503  -2529   2403       C  
ATOM   2527  CD  LYS A 615     -30.776 -66.131  23.495  1.00147.87           C  
ANISOU 2527  CD  LYS A 615    13700  20280  22204  -2445  -2608   2833       C  
ATOM   2528  CE  LYS A 615     -32.162 -66.633  23.055  1.00145.52           C  
ANISOU 2528  CE  LYS A 615    13639  19842  21811  -2174  -2283   2440       C  
ATOM   2529  NZ  LYS A 615     -32.480 -68.042  23.441  1.00147.11           N1+
ANISOU 2529  NZ  LYS A 615    13548  19952  22393  -2083  -2302   2807       N1+
ATOM   2530  N   ALA A 630     -42.817 -58.940  31.921  1.00125.49           N  
ANISOU 2530  N   ALA A 630    13239  16766  17674  -3726  -1220  -4590       N  
ATOM   2531  CA  ALA A 630     -43.734 -59.176  30.758  1.00120.49           C  
ANISOU 2531  CA  ALA A 630    12873  15797  17109  -3490   -882  -3947       C  
ATOM   2532  C   ALA A 630     -45.178 -59.503  31.175  1.00116.62           C  
ANISOU 2532  C   ALA A 630    12843  15203  16262  -3149   -864  -3715       C  
ATOM   2533  O   ALA A 630     -45.505 -60.656  31.519  1.00113.94           O  
ANISOU 2533  O   ALA A 630    12597  15225  15469  -2812  -1124  -3531       O  
ATOM   2534  CB  ALA A 630     -43.174 -60.264  29.821  1.00117.62           C  
ANISOU 2534  CB  ALA A 630    12281  15749  16660  -3289   -970  -3557       C  
ATOM   2535  N   LYS A 631     -46.025 -58.471  31.127  1.00116.71           N  
ANISOU 2535  N   LYS A 631    13128  14695  16519  -3238   -520  -3715       N  
ATOM   2536  CA  LYS A 631     -47.458 -58.551  31.436  1.00112.93           C  
ANISOU 2536  CA  LYS A 631    13047  14044  15817  -2949   -412  -3503       C  
ATOM   2537  C   LYS A 631     -48.216 -59.054  30.210  1.00107.31           C  
ANISOU 2537  C   LYS A 631    12438  13207  15124  -2682   -231  -2873       C  
ATOM   2538  O   LYS A 631     -48.122 -58.445  29.146  1.00107.54           O  
ANISOU 2538  O   LYS A 631    12429  12910  15519  -2782     63  -2638       O  
ATOM   2539  CB  LYS A 631     -47.960 -57.160  31.835  1.00116.69           C  
ANISOU 2539  CB  LYS A 631    13732  13997  16607  -3144    -95  -3786       C  
ATOM   2540  CG  LYS A 631     -47.204 -56.543  33.025  1.00123.12           C  
ANISOU 2540  CG  LYS A 631    14449  14906  17426  -3460   -265  -4502       C  
ATOM   2541  CD  LYS A 631     -46.557 -55.170  32.707  1.00129.49           C  
ANISOU 2541  CD  LYS A 631    15133  15212  18855  -3920     45  -4821       C  
ATOM   2542  CE  LYS A 631     -47.478 -53.969  32.993  1.00131.90           C  
ANISOU 2542  CE  LYS A 631    15795  14885  19433  -3969    445  -4965       C  
ATOM   2543  NZ  LYS A 631     -46.836 -52.677  32.601  1.00136.28           N1+
ANISOU 2543  NZ  LYS A 631    16254  14877  20649  -4421    802  -5227       N1+
ATOM   2544  N   LYS A 632     -48.953 -60.159  30.368  1.00102.26           N  
ANISOU 2544  N   LYS A 632    11933  12832  14087  -2349   -402  -2612       N  
ATOM   2545  CA  LYS A 632     -49.640 -60.842  29.256  1.00 96.96           C  
ANISOU 2545  CA  LYS A 632    11323  12143  13373  -2099   -316  -2080       C  
ATOM   2546  C   LYS A 632     -51.159 -60.741  29.337  1.00 94.64           C  
ANISOU 2546  C   LYS A 632    11303  11640  13016  -1873   -153  -1857       C  
ATOM   2547  O   LYS A 632     -51.735 -60.771  30.420  1.00 95.47           O  
ANISOU 2547  O   LYS A 632    11564  11787  12921  -1800   -200  -2047       O  
ATOM   2548  CB  LYS A 632     -49.302 -62.336  29.233  1.00 94.15           C  
ANISOU 2548  CB  LYS A 632    10869  12239  12662  -1903   -624  -1940       C  
ATOM   2549  CG  LYS A 632     -47.852 -62.717  29.031  1.00 95.93           C  
ANISOU 2549  CG  LYS A 632    10780  12755  12914  -2026   -811  -2079       C  
ATOM   2550  CD  LYS A 632     -47.623 -64.150  29.530  1.00 95.28           C  
ANISOU 2550  CD  LYS A 632    10672  13106  12422  -1778  -1142  -2034       C  
ATOM   2551  CE  LYS A 632     -46.146 -64.535  29.532  1.00 98.50           C  
ANISOU 2551  CE  LYS A 632    10731  13857  12837  -1850  -1366  -2215       C  
ATOM   2552  NZ  LYS A 632     -45.311 -63.719  30.491  1.00104.65           N1+
ANISOU 2552  NZ  LYS A 632    11318  14747  13694  -2111  -1503  -2717       N1+
ATOM   2553  N   HIS A 633     -51.801 -60.646  28.177  1.00 92.03           N  
ANISOU 2553  N   HIS A 633    11011  11122  12833  -1743     36  -1449       N  
ATOM   2554  CA  HIS A 633     -53.245 -60.777  28.049  1.00 89.19           C  
ANISOU 2554  CA  HIS A 633    10819  10661  12405  -1487    139  -1178       C  
ATOM   2555  C   HIS A 633     -53.538 -61.980  27.184  1.00 84.81           C  
ANISOU 2555  C   HIS A 633    10201  10368  11653  -1297     -9   -834       C  
ATOM   2556  O   HIS A 633     -52.866 -62.202  26.173  1.00 84.39           O  
ANISOU 2556  O   HIS A 633    10028  10389  11648  -1329    -28   -675       O  
ATOM   2557  CB  HIS A 633     -53.810 -59.580  27.320  1.00 91.40           C  
ANISOU 2557  CB  HIS A 633    11182  10512  13032  -1459    472   -980       C  
ATOM   2558  CG  HIS A 633     -53.957 -58.364  28.165  1.00 96.92           C  
ANISOU 2558  CG  HIS A 633    12014  10848  13960  -1581    693  -1288       C  
ATOM   2559  ND1 HIS A 633     -53.050 -58.022  29.145  1.00101.24           N  
ANISOU 2559  ND1 HIS A 633    12534  11411  14522  -1851    618  -1774       N  
ATOM   2560  CD2 HIS A 633     -54.896 -57.388  28.159  1.00100.42           C  
ANISOU 2560  CD2 HIS A 633    12617  10897  14638  -1460    990  -1201       C  
ATOM   2561  CE1 HIS A 633     -53.436 -56.900  29.725  1.00105.49           C  
ANISOU 2561  CE1 HIS A 633    13233  11560  15285  -1917    868  -2008       C  
ATOM   2562  NE2 HIS A 633     -54.554 -56.495  29.145  1.00105.21           N  
ANISOU 2562  NE2 HIS A 633    13321  11251  15400  -1669   1114  -1652       N  
ATOM   2563  N   LEU A 634     -54.546 -62.753  27.556  1.00 81.47           N  
ANISOU 2563  N   LEU A 634     9858  10074  11021  -1111    -88   -735       N  
ATOM   2564  CA  LEU A 634     -55.013 -63.806  26.688  1.00 77.29           C  
ANISOU 2564  CA  LEU A 634     9278   9728  10359   -952   -196   -441       C  
ATOM   2565  C   LEU A 634     -56.274 -63.291  26.027  1.00 77.26           C  
ANISOU 2565  C   LEU A 634     9305   9549  10501   -793    -27   -180       C  
ATOM   2566  O   LEU A 634     -57.250 -62.949  26.710  1.00 78.41           O  
ANISOU 2566  O   LEU A 634     9524   9580  10685   -710     84   -215       O  
ATOM   2567  CB  LEU A 634     -55.282 -65.071  27.482  1.00 75.11           C  
ANISOU 2567  CB  LEU A 634     9045   9695   9799   -873   -377   -494       C  
ATOM   2568  CG  LEU A 634     -55.966 -66.210  26.734  1.00 71.93           C  
ANISOU 2568  CG  LEU A 634     8606   9428   9293   -738   -464   -248       C  
ATOM   2569  CD1 LEU A 634     -55.167 -66.736  25.514  1.00 68.87           C  
ANISOU 2569  CD1 LEU A 634     8112   9167   8886   -744   -571   -129       C  
ATOM   2570  CD2 LEU A 634     -56.236 -67.312  27.720  1.00 69.82           C  
ANISOU 2570  CD2 LEU A 634     8422   9305   8800   -686   -560   -308       C  
ATOM   2571  N   GLU A 635     -56.240 -63.184  24.704  1.00 76.05           N  
ANISOU 2571  N   GLU A 635     9088   9392  10415   -726      1     81       N  
ATOM   2572  CA  GLU A 635     -57.388 -62.711  23.957  1.00 75.91           C  
ANISOU 2572  CA  GLU A 635     9071   9272  10498   -525    115    361       C  
ATOM   2573  C   GLU A 635     -58.104 -63.953  23.468  1.00 73.48           C  
ANISOU 2573  C   GLU A 635     8675   9256   9986   -402    -90    488       C  
ATOM   2574  O   GLU A 635     -57.455 -64.900  23.077  1.00 72.57           O  
ANISOU 2574  O   GLU A 635     8522   9346   9705   -458   -255    464       O  
ATOM   2575  CB  GLU A 635     -56.935 -61.841  22.781  1.00 77.58           C  
ANISOU 2575  CB  GLU A 635     9289   9330  10855   -496    273    594       C  
ATOM   2576  CG  GLU A 635     -56.252 -60.551  23.196  1.00 81.41           C  
ANISOU 2576  CG  GLU A 635     9859   9450  11624   -659    530    462       C  
ATOM   2577  CD  GLU A 635     -56.471 -59.365  22.237  1.00 86.78           C  
ANISOU 2577  CD  GLU A 635    10615   9820  12535   -531    816    783       C  
ATOM   2578  OE1 GLU A 635     -56.124 -58.209  22.613  1.00 88.90           O  
ANISOU 2578  OE1 GLU A 635    10979   9691  13105   -655   1087    683       O  
ATOM   2579  OE2 GLU A 635     -56.990 -59.573  21.117  1.00 88.98           O1-
ANISOU 2579  OE2 GLU A 635    10871  10243  12691   -299    777   1133       O1-
ATOM   2580  N   ILE A 636     -59.429 -63.988  23.490  1.00 73.08           N  
ANISOU 2580  N   ILE A 636     8574   9223   9970   -244    -75    598       N  
ATOM   2581  CA  ILE A 636     -60.117 -65.185  23.012  1.00 70.89           C  
ANISOU 2581  CA  ILE A 636     8179   9214   9541   -181   -272    667       C  
ATOM   2582  C   ILE A 636     -61.114 -64.896  21.890  1.00 72.41           C  
ANISOU 2582  C   ILE A 636     8243   9499   9768     31   -304    922       C  
ATOM   2583  O   ILE A 636     -61.897 -63.945  21.965  1.00 74.63           O  
ANISOU 2583  O   ILE A 636     8496   9639  10221    190   -157   1044       O  
ATOM   2584  CB  ILE A 636     -60.796 -65.948  24.160  1.00 70.20           C  
ANISOU 2584  CB  ILE A 636     8081   9170   9421   -230   -283    515       C  
ATOM   2585  CG1 ILE A 636     -61.790 -65.040  24.909  1.00 71.26           C  
ANISOU 2585  CG1 ILE A 636     8209   9129   9735   -128    -70    517       C  
ATOM   2586  CG2 ILE A 636     -59.741 -66.560  25.097  1.00 68.55           C  
ANISOU 2586  CG2 ILE A 636     7999   8978   9067   -389   -334    302       C  
ATOM   2587  CD1 ILE A 636     -62.788 -65.774  25.768  1.00 68.95           C  
ANISOU 2587  CD1 ILE A 636     7853   8912   9430   -130    -32    450       C  
ATOM   2588  N   ASN A 637     -61.085 -65.738  20.861  1.00 71.34           N  
ANISOU 2588  N   ASN A 637     8030   9619   9456     56   -507    987       N  
ATOM   2589  CA  ASN A 637     -61.907 -65.576  19.657  1.00 72.72           C  
ANISOU 2589  CA  ASN A 637     8075   9981   9573    271   -611   1208       C  
ATOM   2590  C   ASN A 637     -63.374 -65.946  19.906  1.00 73.97           C  
ANISOU 2590  C   ASN A 637     8014  10272   9816    351   -697   1188       C  
ATOM   2591  O   ASN A 637     -63.711 -67.125  20.051  1.00 73.53           O  
ANISOU 2591  O   ASN A 637     7859  10377   9702    221   -847   1023       O  
ATOM   2592  CB  ASN A 637     -61.311 -66.428  18.531  1.00 71.66           C  
ANISOU 2592  CB  ASN A 637     7946  10102   9178    248   -806   1208       C  
ATOM   2593  CG  ASN A 637     -61.972 -66.198  17.189  1.00 74.15           C  
ANISOU 2593  CG  ASN A 637     8165  10667   9342    491   -939   1430       C  
ATOM   2594  OD1 ASN A 637     -63.110 -65.733  17.089  1.00 75.44           O  
ANISOU 2594  OD1 ASN A 637     8177  10892   9592    679   -969   1559       O  
ATOM   2595  ND2 ASN A 637     -61.252 -66.534  16.136  1.00 74.34           N  
ANISOU 2595  ND2 ASN A 637     8265  10868   9113    515  -1022   1476       N  
ATOM   2596  N   PRO A 638     -64.266 -64.947  19.951  1.00 76.42           N  
ANISOU 2596  N   PRO A 638     8233  10502  10298    568   -580   1356       N  
ATOM   2597  CA  PRO A 638     -65.656 -65.293  20.295  1.00 77.75           C  
ANISOU 2597  CA  PRO A 638     8136  10811  10593    633   -633   1315       C  
ATOM   2598  C   PRO A 638     -66.373 -66.103  19.212  1.00 79.59           C  
ANISOU 2598  C   PRO A 638     8112  11439  10688    693   -944   1330       C  
ATOM   2599  O   PRO A 638     -67.406 -66.690  19.494  1.00 81.47           O  
ANISOU 2599  O   PRO A 638     8086  11825  11041    649  -1018   1222       O  
ATOM   2600  CB  PRO A 638     -66.329 -63.935  20.458  1.00 80.09           C  
ANISOU 2600  CB  PRO A 638     8395  10929  11106    912   -425   1516       C  
ATOM   2601  CG  PRO A 638     -65.547 -63.026  19.536  1.00 81.36           C  
ANISOU 2601  CG  PRO A 638     8745  10983  11184   1066   -374   1761       C  
ATOM   2602  CD  PRO A 638     -64.115 -63.524  19.595  1.00 78.58           C  
ANISOU 2602  CD  PRO A 638     8616  10561  10678    784   -385   1606       C  
ATOM   2603  N   ASP A 639     -65.841 -66.146  17.992  1.00 80.22           N  
ANISOU 2603  N   ASP A 639     8255  11700  10521    779  -1114   1439       N  
ATOM   2604  CA  ASP A 639     -66.505 -66.848  16.903  1.00 82.27           C  
ANISOU 2604  CA  ASP A 639     8285  12375  10598    852  -1438   1412       C  
ATOM   2605  C   ASP A 639     -65.929 -68.237  16.689  1.00 79.96           C  
ANISOU 2605  C   ASP A 639     8050  12195  10134    573  -1603   1135       C  
ATOM   2606  O   ASP A 639     -66.114 -68.814  15.630  1.00 82.14           O  
ANISOU 2606  O   ASP A 639     8229  12795  10186    608  -1868   1070       O  
ATOM   2607  CB  ASP A 639     -66.408 -66.057  15.593  1.00 85.73           C  
ANISOU 2607  CB  ASP A 639     8767  13004  10801   1180  -1534   1715       C  
ATOM   2608  CG  ASP A 639     -67.130 -64.705  15.647  1.00 91.38           C  
ANISOU 2608  CG  ASP A 639     9409  13617  11695   1531  -1384   2034       C  
ATOM   2609  OD1 ASP A 639     -67.194 -64.101  16.740  1.00 93.01           O  
ANISOU 2609  OD1 ASP A 639     9672  13467  12198   1495  -1103   2031       O  
ATOM   2610  OD2 ASP A 639     -67.626 -64.233  14.587  1.00 97.77           O1-
ANISOU 2610  OD2 ASP A 639    10118  14702  12327   1874  -1542   2293       O1-
ATOM   2611  N   HIS A 640     -65.245 -68.785  17.686  1.00 76.49           N  
ANISOU 2611  N   HIS A 640     7777  11500   9786    320  -1452    963       N  
ATOM   2612  CA  HIS A 640     -64.569 -70.066  17.516  1.00 74.62           C  
ANISOU 2612  CA  HIS A 640     7639  11304   9406     99  -1564    732       C  
ATOM   2613  C   HIS A 640     -65.287 -71.232  18.213  1.00 74.61           C  
ANISOU 2613  C   HIS A 640     7495  11279   9574   -132  -1591    492       C  
ATOM   2614  O   HIS A 640     -65.679 -71.127  19.375  1.00 73.75           O  
ANISOU 2614  O   HIS A 640     7363  10977   9680   -205  -1399    487       O  
ATOM   2615  CB  HIS A 640     -63.113 -69.970  17.983  1.00 71.61           C  
ANISOU 2615  CB  HIS A 640     7554  10687   8967     15  -1397    731       C  
ATOM   2616  CG  HIS A 640     -62.217 -71.003  17.369  1.00 71.43           C  
ANISOU 2616  CG  HIS A 640     7650  10752   8737    -83  -1511    579       C  
ATOM   2617  ND1 HIS A 640     -62.207 -72.324  17.777  1.00 71.29           N  
ANISOU 2617  ND1 HIS A 640     7647  10686   8753   -274  -1561    345       N  
ATOM   2618  CD2 HIS A 640     -61.312 -70.913  16.365  1.00 71.46           C  
ANISOU 2618  CD2 HIS A 640     7772  10871   8506      0  -1549    635       C  
ATOM   2619  CE1 HIS A 640     -61.322 -72.995  17.060  1.00 71.63           C  
ANISOU 2619  CE1 HIS A 640     7814  10800   8600   -290  -1636    246       C  
ATOM   2620  NE2 HIS A 640     -60.770 -72.165  16.191  1.00 72.04           N  
ANISOU 2620  NE2 HIS A 640     7920  10974   8475   -128  -1631    411       N  
ATOM   2621  N   SER A 641     -65.440 -72.345  17.492  1.00 75.87           N  
ANISOU 2621  N   SER A 641     7578  11616   9633   -255  -1799    284       N  
ATOM   2622  CA  SER A 641     -66.087 -73.548  18.024  1.00 76.51           C  
ANISOU 2622  CA  SER A 641     7533  11629   9908   -514  -1798     45       C  
ATOM   2623  C   SER A 641     -65.507 -73.980  19.351  1.00 74.31           C  
ANISOU 2623  C   SER A 641     7482  11004   9749   -660  -1538     31       C  
ATOM   2624  O   SER A 641     -66.269 -74.261  20.264  1.00 75.53           O  
ANISOU 2624  O   SER A 641     7528  11036  10133   -780  -1386      2       O  
ATOM   2625  CB  SER A 641     -66.034 -74.702  17.032  1.00 77.97           C  
ANISOU 2625  CB  SER A 641     7691  11977   9956   -647  -2030   -220       C  
ATOM   2626  OG  SER A 641     -64.772 -74.763  16.405  1.00 77.07           O  
ANISOU 2626  OG  SER A 641     7855  11867   9560   -563  -2063   -207       O  
ATOM   2627  N   ILE A 642     -64.178 -74.006  19.487  1.00 71.87           N  
ANISOU 2627  N   ILE A 642     7469  10561   9276   -631  -1478     65       N  
ATOM   2628  CA  ILE A 642     -63.578 -74.330  20.785  1.00 70.01           C  
ANISOU 2628  CA  ILE A 642     7446  10054   9100   -711  -1267     73       C  
ATOM   2629  C   ILE A 642     -64.018 -73.355  21.865  1.00 69.79           C  
ANISOU 2629  C   ILE A 642     7394   9922   9198   -650  -1069    205       C  
ATOM   2630  O   ILE A 642     -64.347 -73.740  22.974  1.00 69.48           O  
ANISOU 2630  O   ILE A 642     7402   9730   9266   -738   -891    191       O  
ATOM   2631  CB  ILE A 642     -62.040 -74.370  20.739  1.00 68.39           C  
ANISOU 2631  CB  ILE A 642     7497   9784   8702   -654  -1265     86       C  
ATOM   2632  CG1 ILE A 642     -61.564 -75.509  19.836  1.00 69.00           C  
ANISOU 2632  CG1 ILE A 642     7635   9916   8664   -706  -1402    -73       C  
ATOM   2633  CG2 ILE A 642     -61.441 -74.540  22.163  1.00 66.08           C  
ANISOU 2633  CG2 ILE A 642     7397   9278   8428   -682  -1088    111       C  
ATOM   2634  CD1 ILE A 642     -60.070 -75.550  19.671  1.00 68.22           C  
ANISOU 2634  CD1 ILE A 642     7729   9795   8394   -620  -1393    -59       C  
ATOM   2635  N   ILE A 643     -64.030 -72.082  21.519  1.00 70.47           N  
ANISOU 2635  N   ILE A 643     7431  10077   9265   -483  -1073    341       N  
ATOM   2636  CA  ILE A 643     -64.403 -71.056  22.472  1.00 71.22           C  
ANISOU 2636  CA  ILE A 643     7528  10046   9486   -403   -868    436       C  
ATOM   2637  C   ILE A 643     -65.902 -71.054  22.764  1.00 74.16           C  
ANISOU 2637  C   ILE A 643     7626  10472  10078   -402   -794    443       C  
ATOM   2638  O   ILE A 643     -66.302 -70.979  23.918  1.00 74.58           O  
ANISOU 2638  O   ILE A 643     7707  10388  10241   -437   -569    435       O  
ATOM   2639  CB  ILE A 643     -63.860 -69.671  22.046  1.00 70.84           C  
ANISOU 2639  CB  ILE A 643     7548   9970   9395   -229   -841    579       C  
ATOM   2640  CG1 ILE A 643     -62.324 -69.727  21.952  1.00 68.68           C  
ANISOU 2640  CG1 ILE A 643     7505   9634   8955   -280   -863    543       C  
ATOM   2641  CG2 ILE A 643     -64.253 -68.590  23.038  1.00 71.08           C  
ANISOU 2641  CG2 ILE A 643     7604   9822   9580   -147   -606    631       C  
ATOM   2642  CD1 ILE A 643     -61.628 -70.137  23.254  1.00 64.69           C  
ANISOU 2642  CD1 ILE A 643     7180   8982   8417   -395   -759    421       C  
ATOM   2643  N   GLU A 644     -66.738 -71.173  21.744  1.00 77.22           N  
ANISOU 2643  N   GLU A 644     7733  11090  10517   -359   -982    444       N  
ATOM   2644  CA  GLU A 644     -68.174 -71.188  21.999  1.00 81.31           C  
ANISOU 2644  CA  GLU A 644     7913  11700  11281   -362   -924    433       C  
ATOM   2645  C   GLU A 644     -68.587 -72.452  22.799  1.00 81.64           C  
ANISOU 2645  C   GLU A 644     7920  11631  11467   -637   -790    278       C  
ATOM   2646  O   GLU A 644     -69.472 -72.377  23.660  1.00 83.13           O  
ANISOU 2646  O   GLU A 644     7956  11759  11868   -669   -560    294       O  
ATOM   2647  CB  GLU A 644     -68.978 -70.922  20.701  1.00 84.72           C  
ANISOU 2647  CB  GLU A 644     8006  12466  11716   -215  -1200    466       C  
ATOM   2648  CG  GLU A 644     -70.379 -71.569  20.580  1.00 92.78           C  
ANISOU 2648  CG  GLU A 644     8577  13697  12976   -332  -1283    330       C  
ATOM   2649  CD  GLU A 644     -71.511 -70.867  21.390  1.00100.23           C  
ANISOU 2649  CD  GLU A 644     9243  14624  14215   -214  -1049    428       C  
ATOM   2650  OE1 GLU A 644     -72.699 -70.957  20.941  1.00104.40           O  
ANISOU 2650  OE1 GLU A 644     9301  15434  14930   -185  -1186    377       O  
ATOM   2651  OE2 GLU A 644     -71.220 -70.250  22.458  1.00 98.86           O1-
ANISOU 2651  OE2 GLU A 644     9297  14181  14083   -148   -737    528       O1-
ATOM   2652  N   THR A 645     -67.907 -73.582  22.552  1.00 80.54           N  
ANISOU 2652  N   THR A 645     7948  11434  11219   -817   -885    148       N  
ATOM   2653  CA  THR A 645     -68.132 -74.832  23.305  1.00 80.95           C  
ANISOU 2653  CA  THR A 645     8050  11300  11406  -1067   -714     41       C  
ATOM   2654  C   THR A 645     -67.597 -74.702  24.710  1.00 79.24           C  
ANISOU 2654  C   THR A 645     8142  10841  11123  -1038   -420    149       C  
ATOM   2655  O   THR A 645     -68.202 -75.181  25.651  1.00 81.24           O  
ANISOU 2655  O   THR A 645     8382  10962  11524  -1151   -159    165       O  
ATOM   2656  CB  THR A 645     -67.426 -76.031  22.664  1.00 80.40           C  
ANISOU 2656  CB  THR A 645     8135  11178  11235  -1217   -870   -115       C  
ATOM   2657  OG1 THR A 645     -68.001 -76.293  21.387  1.00 84.03           O  
ANISOU 2657  OG1 THR A 645     8310  11888  11728  -1274  -1151   -279       O  
ATOM   2658  CG2 THR A 645     -67.604 -77.260  23.496  1.00 81.79           C  
ANISOU 2658  CG2 THR A 645     8418  11087  11572  -1444   -638   -175       C  
ATOM   2659  N   LEU A 646     -66.444 -74.063  24.845  1.00 76.34           N  
ANISOU 2659  N   LEU A 646     8048  10435  10522   -890   -460    216       N  
ATOM   2660  CA  LEU A 646     -65.857 -73.823  26.140  1.00 74.89           C  
ANISOU 2660  CA  LEU A 646     8147  10090  10217   -838   -245    279       C  
ATOM   2661  C   LEU A 646     -66.750 -72.958  27.014  1.00 75.48           C  
ANISOU 2661  C   LEU A 646     8123  10141  10411   -761      3    339       C  
ATOM   2662  O   LEU A 646     -66.791 -73.157  28.210  1.00 76.24           O  
ANISOU 2662  O   LEU A 646     8391  10122  10454   -776    248    365       O  
ATOM   2663  CB  LEU A 646     -64.491 -73.155  25.989  1.00 73.25           C  
ANISOU 2663  CB  LEU A 646     8160   9889   9780   -716   -371    289       C  
ATOM   2664  CG  LEU A 646     -63.345 -73.624  26.896  1.00 74.07           C  
ANISOU 2664  CG  LEU A 646     8580   9892   9671   -710   -325    277       C  
ATOM   2665  CD1 LEU A 646     -62.193 -72.602  26.873  1.00 74.65           C  
ANISOU 2665  CD1 LEU A 646     8767  10001   9593   -607   -417    255       C  
ATOM   2666  CD2 LEU A 646     -63.799 -73.900  28.340  1.00 76.43           C  
ANISOU 2666  CD2 LEU A 646     9014  10083   9942   -720    -55    319       C  
ATOM   2667  N   ARG A 647     -67.454 -71.995  26.435  1.00 75.63           N  
ANISOU 2667  N   ARG A 647     7886  10276  10571   -644    -43    373       N  
ATOM   2668  CA  ARG A 647     -68.339 -71.157  27.226  1.00 77.21           C  
ANISOU 2668  CA  ARG A 647     7978  10443  10915   -536    219    421       C  
ATOM   2669  C   ARG A 647     -69.379 -72.040  27.897  1.00 79.74           C  
ANISOU 2669  C   ARG A 647     8137  10739  11419   -688    456    409       C  
ATOM   2670  O   ARG A 647     -69.529 -72.027  29.117  1.00 80.28           O  
ANISOU 2670  O   ARG A 647     8364  10692  11446   -683    766    433       O  
ATOM   2671  CB  ARG A 647     -69.034 -70.124  26.344  1.00 78.67           C  
ANISOU 2671  CB  ARG A 647     7866  10764  11259   -349    116    490       C  
ATOM   2672  CG  ARG A 647     -69.724 -69.010  27.110  1.00 80.18           C  
ANISOU 2672  CG  ARG A 647     7997  10875  11589   -162    397    542       C  
ATOM   2673  CD  ARG A 647     -70.607 -68.170  26.213  1.00 83.41           C  
ANISOU 2673  CD  ARG A 647     8058  11434  12200     61    303    649       C  
ATOM   2674  NE  ARG A 647     -72.020 -68.419  26.491  1.00 89.47           N  
ANISOU 2674  NE  ARG A 647     8426  12325  13244     63    456    646       N  
ATOM   2675  CZ  ARG A 647     -72.784 -69.247  25.793  1.00 93.09           C  
ANISOU 2675  CZ  ARG A 647     8502  13017  13849    -61    272    602       C  
ATOM   2676  NH1 ARG A 647     -72.276 -69.905  24.753  1.00 92.99           N1+
ANISOU 2676  NH1 ARG A 647     8497  13137  13698   -178    -74    548       N1+
ATOM   2677  NH2 ARG A 647     -74.054 -69.418  26.131  1.00 97.31           N  
ANISOU 2677  NH2 ARG A 647     8632  13662  14678    -79    446    583       N  
ATOM   2678  N   GLN A 648     -70.072 -72.822  27.076  1.00 81.39           N  
ANISOU 2678  N   GLN A 648     8035  11066  11822   -836    317    356       N  
ATOM   2679  CA  GLN A 648     -71.097 -73.735  27.528  1.00 84.91           C  
ANISOU 2679  CA  GLN A 648     8260  11478  12521  -1043    540    323       C  
ATOM   2680  C   GLN A 648     -70.650 -74.654  28.664  1.00 84.99           C  
ANISOU 2680  C   GLN A 648     8626  11247  12417  -1176    823    365       C  
ATOM   2681  O   GLN A 648     -71.343 -74.778  29.679  1.00 87.49           O  
ANISOU 2681  O   GLN A 648     8922  11479  12841  -1216   1197    431       O  
ATOM   2682  CB  GLN A 648     -71.627 -74.546  26.350  1.00 86.53           C  
ANISOU 2682  CB  GLN A 648     8121  11836  12920  -1233    274    185       C  
ATOM   2683  CG  GLN A 648     -72.908 -73.992  25.772  1.00 91.28           C  
ANISOU 2683  CG  GLN A 648     8180  12704  13798  -1168    193    156       C  
ATOM   2684  CD  GLN A 648     -72.909 -73.945  24.252  1.00 94.36           C  
ANISOU 2684  CD  GLN A 648     8337  13377  14136  -1124   -268     56       C  
ATOM   2685  OE1 GLN A 648     -72.257 -74.750  23.572  1.00 94.72           O  
ANISOU 2685  OE1 GLN A 648     8531  13412  14045  -1270   -492    -70       O  
ATOM   2686  NE2 GLN A 648     -73.643 -72.984  23.709  1.00 97.51           N  
ANISOU 2686  NE2 GLN A 648     8383  14041  14622   -886   -403    121       N  
ATOM   2687  N   LYS A 649     -69.499 -75.291  28.500  1.00 83.04           N  
ANISOU 2687  N   LYS A 649     8707  10901  11943  -1213    666    351       N  
ATOM   2688  CA  LYS A 649     -69.020 -76.239  29.497  1.00 84.02           C  
ANISOU 2688  CA  LYS A 649     9183  10804  11934  -1287    902    430       C  
ATOM   2689  C   LYS A 649     -68.674 -75.558  30.834  1.00 84.25           C  
ANISOU 2689  C   LYS A 649     9513  10797  11700  -1099   1147    538       C  
ATOM   2690  O   LYS A 649     -69.016 -76.053  31.912  1.00 85.95           O  
ANISOU 2690  O   LYS A 649     9882  10892  11882  -1131   1499    646       O  
ATOM   2691  CB  LYS A 649     -67.839 -77.033  28.947  1.00 81.91           C  
ANISOU 2691  CB  LYS A 649     9169  10459  11493  -1312    656    391       C  
ATOM   2692  CG  LYS A 649     -68.106 -77.664  27.590  1.00 82.76           C  
ANISOU 2692  CG  LYS A 649     9020  10620  11802  -1483    400    230       C  
ATOM   2693  CD  LYS A 649     -68.720 -79.037  27.709  1.00 88.02           C  
ANISOU 2693  CD  LYS A 649     9641  11068  12735  -1756    599    185       C  
ATOM   2694  CE  LYS A 649     -69.109 -79.566  26.330  1.00 91.46           C  
ANISOU 2694  CE  LYS A 649     9775  11596  13377  -1950    318    -58       C  
ATOM   2695  NZ  LYS A 649     -68.875 -81.038  26.169  1.00 93.86           N1+
ANISOU 2695  NZ  LYS A 649    10245  11607  13810  -2171    392   -159       N1+
ATOM   2696  N   ALA A 650     -68.021 -74.406  30.755  1.00 82.86           N  
ANISOU 2696  N   ALA A 650     9424  10722  11334   -911    980    496       N  
ATOM   2697  CA  ALA A 650     -67.558 -73.730  31.946  1.00 83.86           C  
ANISOU 2697  CA  ALA A 650     9848  10833  11181   -749   1150    517       C  
ATOM   2698  C   ALA A 650     -68.722 -73.120  32.701  1.00 87.60           C  
ANISOU 2698  C   ALA A 650    10181  11312  11789   -697   1507    539       C  
ATOM   2699  O   ALA A 650     -68.722 -73.086  33.932  1.00 89.75           O  
ANISOU 2699  O   ALA A 650    10706  11547  11847   -622   1793    579       O  
ATOM   2700  CB  ALA A 650     -66.552 -72.685  31.594  1.00 81.29           C  
ANISOU 2700  CB  ALA A 650     9622  10575  10686   -618    890    422       C  
ATOM   2701  N   GLU A 651     -69.730 -72.649  31.977  1.00 89.40           N  
ANISOU 2701  N   GLU A 651    10002  11613  12352   -709   1498    516       N  
ATOM   2702  CA  GLU A 651     -70.867 -72.039  32.648  1.00 92.96           C  
ANISOU 2702  CA  GLU A 651    10268  12080  12970   -626   1854    535       C  
ATOM   2703  C   GLU A 651     -71.728 -73.113  33.260  1.00 96.27           C  
ANISOU 2703  C   GLU A 651    10595  12439  13542   -801   2205    625       C  
ATOM   2704  O   GLU A 651     -72.490 -72.837  34.164  1.00 99.81           O  
ANISOU 2704  O   GLU A 651    11007  12878  14035   -740   2603    666       O  
ATOM   2705  CB  GLU A 651     -71.657 -71.120  31.712  1.00 93.75           C  
ANISOU 2705  CB  GLU A 651     9940  12299  13379   -519   1730    506       C  
ATOM   2706  CG  GLU A 651     -70.871 -69.863  31.320  1.00 93.66           C  
ANISOU 2706  CG  GLU A 651    10078  12277  13231   -314   1517    458       C  
ATOM   2707  CD  GLU A 651     -71.735 -68.716  30.818  1.00 98.68           C  
ANISOU 2707  CD  GLU A 651    10387  12971  14135   -101   1546    484       C  
ATOM   2708  OE1 GLU A 651     -72.031 -68.678  29.602  1.00 99.39           O  
ANISOU 2708  OE1 GLU A 651    10170  13199  14394    -76   1267    531       O  
ATOM   2709  OE2 GLU A 651     -72.102 -67.839  31.642  1.00102.92           O1-
ANISOU 2709  OE2 GLU A 651    10990  13420  14692     70   1850    456       O1-
ATOM   2710  N   ALA A 652     -71.588 -74.344  32.777  1.00 96.49           N  
ANISOU 2710  N   ALA A 652    10601  12400  13661  -1023   2094    651       N  
ATOM   2711  CA  ALA A 652     -72.296 -75.490  33.344  1.00 99.99           C  
ANISOU 2711  CA  ALA A 652    11002  12708  14280  -1235   2462    751       C  
ATOM   2712  C   ALA A 652     -71.628 -75.974  34.642  1.00101.24           C  
ANISOU 2712  C   ALA A 652    11694  12721  14050  -1157   2745    905       C  
ATOM   2713  O   ALA A 652     -72.303 -76.458  35.546  1.00105.13           O  
ANISOU 2713  O   ALA A 652    12233  13116  14593  -1219   3209   1042       O  
ATOM   2714  CB  ALA A 652     -72.387 -76.612  32.329  1.00 99.65           C  
ANISOU 2714  CB  ALA A 652    10759  12598  14504  -1509   2253    686       C  
ATOM   2715  N   ASP A 653     -70.303 -75.837  34.723  1.00 98.97           N  
ANISOU 2715  N   ASP A 653    11793  12444  13366  -1008   2470    893       N  
ATOM   2716  CA  ASP A 653     -69.514 -76.158  35.929  1.00100.03           C  
ANISOU 2716  CA  ASP A 653    12438  12526  13041   -859   2636   1025       C  
ATOM   2717  C   ASP A 653     -68.189 -75.397  35.853  1.00 96.55           C  
ANISOU 2717  C   ASP A 653    12235  12216  12233   -666   2246    901       C  
ATOM   2718  O   ASP A 653     -67.238 -75.839  35.193  1.00 93.85           O  
ANISOU 2718  O   ASP A 653    11973  11860  11826   -682   1907    878       O  
ATOM   2719  CB  ASP A 653     -69.294 -77.684  36.071  1.00102.06           C  
ANISOU 2719  CB  ASP A 653    12903  12567  13307   -985   2764   1213       C  
ATOM   2720  CG  ASP A 653     -68.641 -78.099  37.420  1.00104.85           C  
ANISOU 2720  CG  ASP A 653    13787  12887  13162   -778   2993   1425       C  
ATOM   2721  OD1 ASP A 653     -68.979 -77.532  38.485  1.00107.08           O  
ANISOU 2721  OD1 ASP A 653    14217  13270  13196   -632   3294   1472       O  
ATOM   2722  OD2 ASP A 653     -67.809 -79.041  37.405  1.00105.06           O1-
ANISOU 2722  OD2 ASP A 653    14089  12792  13037   -738   2882   1553       O1-
ATOM   2723  N   LYS A 654     -68.150 -74.237  36.508  1.00 96.91           N  
ANISOU 2723  N   LYS A 654    12369  12379  12073   -497   2314    794       N  
ATOM   2724  CA  LYS A 654     -66.948 -73.409  36.526  1.00 94.91           C  
ANISOU 2724  CA  LYS A 654    12309  12237  11515   -356   1985    628       C  
ATOM   2725  C   LYS A 654     -65.768 -74.105  37.222  1.00 95.29           C  
ANISOU 2725  C   LYS A 654    12758  12336  11112   -250   1866    699       C  
ATOM   2726  O   LYS A 654     -64.635 -73.634  37.135  1.00 93.63           O  
ANISOU 2726  O   LYS A 654    12659  12237  10678   -169   1541    554       O  
ATOM   2727  CB  LYS A 654     -67.231 -72.026  37.143  1.00 96.16           C  
ANISOU 2727  CB  LYS A 654    12489  12461  11584   -221   2131    454       C  
ATOM   2728  CG  LYS A 654     -67.209 -71.962  38.673  1.00100.56           C  
ANISOU 2728  CG  LYS A 654    13411  13092  11703    -70   2436    453       C  
ATOM   2729  CD  LYS A 654     -67.412 -70.537  39.197  1.00103.12           C  
ANISOU 2729  CD  LYS A 654    13771  13455  11952     56   2559    205       C  
ATOM   2730  CE  LYS A 654     -68.856 -70.282  39.631  1.00107.54           C  
ANISOU 2730  CE  LYS A 654    14165  13964  12730     93   3051    263       C  
ATOM   2731  NZ  LYS A 654     -69.200 -68.829  39.642  1.00108.53           N1+
ANISOU 2731  NZ  LYS A 654    14193  14049  12992    208   3136     23       N1+
ATOM   2732  N   ASN A 655     -66.034 -75.226  37.898  1.00 97.83           N  
ANISOU 2732  N   ASN A 655    13277  12575  11318   -242   2139    933       N  
ATOM   2733  CA  ASN A 655     -64.995 -75.940  38.640  1.00 98.70           C  
ANISOU 2733  CA  ASN A 655    13784  12746  10972    -72   2055   1061       C  
ATOM   2734  C   ASN A 655     -64.572 -77.263  38.008  1.00 98.19           C  
ANISOU 2734  C   ASN A 655    13750  12511  11045   -136   1941   1241       C  
ATOM   2735  O   ASN A 655     -63.765 -77.988  38.571  1.00 99.34           O  
ANISOU 2735  O   ASN A 655    14212  12676  10854     40   1894   1401       O  
ATOM   2736  CB  ASN A 655     -65.431 -76.153  40.089  1.00102.95           C  
ANISOU 2736  CB  ASN A 655    14646  13328  11142     81   2478   1230       C  
ATOM   2737  CG  ASN A 655     -65.926 -74.884  40.739  1.00103.97           C  
ANISOU 2737  CG  ASN A 655    14761  13600  11141    152   2646   1021       C  
ATOM   2738  OD1 ASN A 655     -65.214 -73.894  40.796  1.00104.52           O  
ANISOU 2738  OD1 ASN A 655    14864  13832  11014    234   2363    750       O  
ATOM   2739  ND2 ASN A 655     -67.149 -74.907  41.237  1.00106.75           N  
ANISOU 2739  ND2 ASN A 655    15058  13875  11628    114   3136   1129       N  
ATOM   2740  N   ASP A 656     -65.111 -77.572  36.836  1.00 97.16           N  
ANISOU 2740  N   ASP A 656    13294  12224  11397   -366   1888   1202       N  
ATOM   2741  CA  ASP A 656     -64.791 -78.825  36.154  1.00 98.01           C  
ANISOU 2741  CA  ASP A 656    13424  12130  11683   -455   1805   1312       C  
ATOM   2742  C   ASP A 656     -63.283 -78.929  35.954  1.00 96.14           C  
ANISOU 2742  C   ASP A 656    13364  12007  11155   -268   1410   1271       C  
ATOM   2743  O   ASP A 656     -62.697 -78.111  35.253  1.00 93.33           O  
ANISOU 2743  O   ASP A 656    12835  11812  10812   -270   1071   1058       O  
ATOM   2744  CB  ASP A 656     -65.552 -78.908  34.816  1.00 96.84           C  
ANISOU 2744  CB  ASP A 656    12858  11880  12055   -733   1721   1171       C  
ATOM   2745  CG  ASP A 656     -65.503 -80.305  34.165  1.00 99.09           C  
ANISOU 2745  CG  ASP A 656    13163  11896  12588   -883   1733   1240       C  
ATOM   2746  OD1 ASP A 656     -65.708 -81.333  34.868  1.00103.89           O  
ANISOU 2746  OD1 ASP A 656    14016  12265  13192   -889   2070   1469       O  
ATOM   2747  OD2 ASP A 656     -65.297 -80.364  32.925  1.00 97.10           O1-
ANISOU 2747  OD2 ASP A 656    12692  11656  12545   -997   1432   1061       O1-
ATOM   2748  N   LYS A 657     -62.659 -79.917  36.592  1.00 98.74           N  
ANISOU 2748  N   LYS A 657    14030  12257  11229    -88   1478   1496       N  
ATOM   2749  CA  LYS A 657     -61.206 -80.101  36.517  1.00 98.51           C  
ANISOU 2749  CA  LYS A 657    14147  12368  10914    138   1118   1482       C  
ATOM   2750  C   LYS A 657     -60.763 -80.141  35.060  1.00 95.48           C  
ANISOU 2750  C   LYS A 657    13494  11942  10840      1    806   1294       C  
ATOM   2751  O   LYS A 657     -59.609 -79.835  34.720  1.00 93.62           O  
ANISOU 2751  O   LYS A 657    13227  11892  10453    129    464   1177       O  
ATOM   2752  CB  LYS A 657     -60.803 -81.414  37.176  1.00102.16           C  
ANISOU 2752  CB  LYS A 657    14973  12661  11179    354   1283   1809       C  
ATOM   2753  CG  LYS A 657     -59.681 -81.289  38.195  1.00105.48           C  
ANISOU 2753  CG  LYS A 657    15674  13379  11021    731   1096   1898       C  
ATOM   2754  CD  LYS A 657     -60.212 -81.545  39.629  1.00111.71           C  
ANISOU 2754  CD  LYS A 657    16823  14182  11440    910   1481   2184       C  
ATOM   2755  CE  LYS A 657     -60.261 -83.046  39.938  1.00115.63           C  
ANISOU 2755  CE  LYS A 657    17644  14339  11951   1055   1788   2604       C  
ATOM   2756  NZ  LYS A 657     -61.205 -83.357  41.034  1.00121.02           N1+
ANISOU 2756  NZ  LYS A 657    18609  14902  12470   1094   2319   2907       N1+
ATOM   2757  N   SER A 658     -61.709 -80.514  34.201  1.00 95.40           N  
ANISOU 2757  N   SER A 658    13271  11712  11261   -263    936   1253       N  
ATOM   2758  CA  SER A 658     -61.458 -80.697  32.774  1.00 93.14           C  
ANISOU 2758  CA  SER A 658    12756  11380  11251   -400    684   1077       C  
ATOM   2759  C   SER A 658     -61.481 -79.361  32.031  1.00 89.77           C  
ANISOU 2759  C   SER A 658    12029  11193  10887   -478    438    844       C  
ATOM   2760  O   SER A 658     -60.620 -79.107  31.181  1.00 87.77           O  
ANISOU 2760  O   SER A 658    11683  11051  10612   -440    146    718       O  
ATOM   2761  CB  SER A 658     -62.491 -81.653  32.212  1.00 94.86           C  
ANISOU 2761  CB  SER A 658    12870  11295  11877   -658    907   1088       C  
ATOM   2762  OG  SER A 658     -63.210 -82.222  33.291  1.00 99.13           O  
ANISOU 2762  OG  SER A 658    13602  11641  12419   -672   1322   1320       O  
ATOM   2763  N   VAL A 659     -62.451 -78.509  32.364  1.00 89.53           N  
ANISOU 2763  N   VAL A 659    11856  11224  10935   -563    593    811       N  
ATOM   2764  CA  VAL A 659     -62.439 -77.134  31.891  1.00 86.89           C  
ANISOU 2764  CA  VAL A 659    11306  11082  10626   -572    415    641       C  
ATOM   2765  C   VAL A 659     -61.082 -76.531  32.235  1.00 86.06           C  
ANISOU 2765  C   VAL A 659    11345  11152  10201   -395    186    571       C  
ATOM   2766  O   VAL A 659     -60.461 -75.875  31.406  1.00 84.07           O  
ANISOU 2766  O   VAL A 659    10949  11001   9990   -406    -52    441       O  
ATOM   2767  CB  VAL A 659     -63.549 -76.281  32.531  1.00 87.92           C  
ANISOU 2767  CB  VAL A 659    11337  11241  10827   -602    664    637       C  
ATOM   2768  CG1 VAL A 659     -63.575 -74.907  31.904  1.00 85.48           C  
ANISOU 2768  CG1 VAL A 659    10811  11059  10606   -595    502    485       C  
ATOM   2769  CG2 VAL A 659     -64.896 -76.942  32.382  1.00 89.48           C  
ANISOU 2769  CG2 VAL A 659    11355  11292  11351   -782    927    709       C  
ATOM   2770  N   LYS A 660     -60.622 -76.779  33.459  1.00 88.20           N  
ANISOU 2770  N   LYS A 660    11890  11471  10148   -232    267    660       N  
ATOM   2771  CA  LYS A 660     -59.350 -76.258  33.917  1.00 88.46           C  
ANISOU 2771  CA  LYS A 660    12027  11719   9864    -71     29    559       C  
ATOM   2772  C   LYS A 660     -58.238 -76.783  33.031  1.00 86.70           C  
ANISOU 2772  C   LYS A 660    11741  11527   9674    -28   -244    535       C  
ATOM   2773  O   LYS A 660     -57.495 -75.998  32.448  1.00 84.64           O  
ANISOU 2773  O   LYS A 660    11319  11399   9440    -55   -466    368       O  
ATOM   2774  CB  LYS A 660     -59.111 -76.606  35.394  1.00 92.06           C  
ANISOU 2774  CB  LYS A 660    12798  12269   9910    134    143    677       C  
ATOM   2775  CG  LYS A 660     -57.821 -76.031  35.967  1.00 95.29           C  
ANISOU 2775  CG  LYS A 660    13275  12969   9962    298   -144    520       C  
ATOM   2776  CD  LYS A 660     -57.665 -76.308  37.466  1.00104.83           C  
ANISOU 2776  CD  LYS A 660    14805  14339  10685    536    -55    625       C  
ATOM   2777  CE  LYS A 660     -58.154 -75.125  38.342  1.00109.14           C  
ANISOU 2777  CE  LYS A 660    15409  15014  11045    508     66    422       C  
ATOM   2778  NZ  LYS A 660     -57.187 -73.956  38.356  1.00110.40           N1+
ANISOU 2778  NZ  LYS A 660    15437  15408  11101    475   -253     60       N1+
ATOM   2779  N   ASP A 661     -58.148 -78.104  32.897  1.00 87.89           N  
ANISOU 2779  N   ASP A 661    12015  11525   9854     33   -188    702       N  
ATOM   2780  CA  ASP A 661     -57.126 -78.709  32.042  1.00 87.44           C  
ANISOU 2780  CA  ASP A 661    11909  11474   9841    104   -405    677       C  
ATOM   2781  C   ASP A 661     -57.156 -78.130  30.632  1.00 84.11           C  
ANISOU 2781  C   ASP A 661    11206  11072   9677    -71   -545    503       C  
ATOM   2782  O   ASP A 661     -56.109 -77.831  30.055  1.00 83.21           O  
ANISOU 2782  O   ASP A 661    10985  11102   9527    -17   -759    401       O  
ATOM   2783  CB  ASP A 661     -57.286 -80.226  31.981  1.00 90.28           C  
ANISOU 2783  CB  ASP A 661    12450  11565  10286    164   -252    866       C  
ATOM   2784  CG  ASP A 661     -56.013 -80.942  31.469  1.00 93.32           C  
ANISOU 2784  CG  ASP A 661    12863  11973  10621    356   -451    869       C  
ATOM   2785  OD1 ASP A 661     -54.911 -80.737  32.064  1.00 95.09           O  
ANISOU 2785  OD1 ASP A 661    13130  12437  10562    595   -635    882       O  
ATOM   2786  OD2 ASP A 661     -56.128 -81.717  30.474  1.00 95.88           O1-
ANISOU 2786  OD2 ASP A 661    13151  12089  11190    273   -422    834       O1-
ATOM   2787  N   LEU A 662     -58.361 -77.954  30.093  1.00 82.56           N  
ANISOU 2787  N   LEU A 662    10879  10759   9730   -267   -415    480       N  
ATOM   2788  CA  LEU A 662     -58.546 -77.299  28.808  1.00 79.69           C  
ANISOU 2788  CA  LEU A 662    10266  10455   9558   -397   -541    350       C  
ATOM   2789  C   LEU A 662     -57.957 -75.865  28.726  1.00 78.07           C  
ANISOU 2789  C   LEU A 662     9947  10433   9282   -377   -669    244       C  
ATOM   2790  O   LEU A 662     -57.063 -75.575  27.914  1.00 76.96           O  
ANISOU 2790  O   LEU A 662     9710  10390   9139   -360   -833    172       O  
ATOM   2791  CB  LEU A 662     -60.018 -77.284  28.468  1.00 79.80           C  
ANISOU 2791  CB  LEU A 662    10134  10367   9816   -569   -393    353       C  
ATOM   2792  CG  LEU A 662     -60.258 -76.908  27.011  1.00 79.55           C  
ANISOU 2792  CG  LEU A 662     9863  10417   9944   -661   -551    248       C  
ATOM   2793  CD1 LEU A 662     -59.518 -77.877  26.096  1.00 79.45           C  
ANISOU 2793  CD1 LEU A 662     9892  10375   9918   -647   -686    186       C  
ATOM   2794  CD2 LEU A 662     -61.759 -76.831  26.686  1.00 80.31           C  
ANISOU 2794  CD2 LEU A 662     9748  10484  10280   -809   -452    234       C  
ATOM   2795  N   VAL A 663     -58.470 -74.974  29.570  1.00 77.98           N  
ANISOU 2795  N   VAL A 663     9954  10442   9233   -388   -555    228       N  
ATOM   2796  CA  VAL A 663     -57.967 -73.601  29.666  1.00 76.16           C  
ANISOU 2796  CA  VAL A 663     9654  10313   8969   -391   -624    102       C  
ATOM   2797  C   VAL A 663     -56.433 -73.515  29.714  1.00 75.96           C  
ANISOU 2797  C   VAL A 663     9638  10433   8787   -323   -825      7       C  
ATOM   2798  O   VAL A 663     -55.846 -72.740  28.948  1.00 75.21           O  
ANISOU 2798  O   VAL A 663     9398  10384   8794   -383   -914    -76       O  
ATOM   2799  CB  VAL A 663     -58.615 -72.840  30.840  1.00 77.19           C  
ANISOU 2799  CB  VAL A 663     9875  10427   9026   -379   -447     60       C  
ATOM   2800  CG1 VAL A 663     -57.930 -71.517  31.051  1.00 76.23           C  
ANISOU 2800  CG1 VAL A 663     9723  10367   8871   -397   -515   -122       C  
ATOM   2801  CG2 VAL A 663     -60.106 -72.641  30.570  1.00 76.26           C  
ANISOU 2801  CG2 VAL A 663     9641  10192   9141   -446   -248    134       C  
ATOM   2802  N   ILE A 664     -55.790 -74.318  30.572  1.00 76.59           N  
ANISOU 2802  N   ILE A 664     9872  10593   8633   -187   -884     39       N  
ATOM   2803  CA  ILE A 664     -54.320 -74.289  30.679  1.00 76.51           C  
ANISOU 2803  CA  ILE A 664     9813  10777   8479    -96  -1102    -59       C  
ATOM   2804  C   ILE A 664     -53.687 -74.796  29.378  1.00 75.12           C  
ANISOU 2804  C   ILE A 664     9495  10597   8448    -96  -1199    -35       C  
ATOM   2805  O   ILE A 664     -52.659 -74.282  28.939  1.00 74.55           O  
ANISOU 2805  O   ILE A 664     9258  10659   8408   -116  -1325   -148       O  
ATOM   2806  CB  ILE A 664     -53.777 -75.090  31.899  1.00 78.74           C  
ANISOU 2806  CB  ILE A 664    10287  11192   8438    121  -1171      3       C  
ATOM   2807  CG1 ILE A 664     -54.424 -74.642  33.197  1.00 80.17           C  
ANISOU 2807  CG1 ILE A 664    10648  11406   8407    145  -1049    -19       C  
ATOM   2808  CG2 ILE A 664     -52.298 -74.890  32.074  1.00 79.60           C  
ANISOU 2808  CG2 ILE A 664    10268  11566   8407    219  -1430   -138       C  
ATOM   2809  CD1 ILE A 664     -54.360 -75.692  34.303  1.00 82.48           C  
ANISOU 2809  CD1 ILE A 664    11210  11761   8368    388  -1013    166       C  
ATOM   2810  N   LEU A 665     -54.311 -75.796  28.754  1.00 74.69           N  
ANISOU 2810  N   LEU A 665     9498  10386   8493    -90  -1118     88       N  
ATOM   2811  CA  LEU A 665     -53.817 -76.264  27.469  1.00 73.91           C  
ANISOU 2811  CA  LEU A 665     9292  10283   8507    -89  -1186     75       C  
ATOM   2812  C   LEU A 665     -53.870 -75.094  26.508  1.00 72.66           C  
ANISOU 2812  C   LEU A 665     8946  10174   8487   -231  -1195      0       C  
ATOM   2813  O   LEU A 665     -52.842 -74.720  25.964  1.00 73.02           O  
ANISOU 2813  O   LEU A 665     8861  10339   8540   -220  -1274    -65       O  
ATOM   2814  CB  LEU A 665     -54.599 -77.470  26.922  1.00 73.96           C  
ANISOU 2814  CB  LEU A 665     9394  10092   8614   -102  -1093    154       C  
ATOM   2815  CG  LEU A 665     -53.782 -78.532  26.144  1.00 74.37           C  
ANISOU 2815  CG  LEU A 665     9465  10117   8674     15  -1153    139       C  
ATOM   2816  CD1 LEU A 665     -54.670 -79.447  25.303  1.00 72.50           C  
ANISOU 2816  CD1 LEU A 665     9278   9675   8590    -84  -1066    118       C  
ATOM   2817  CD2 LEU A 665     -52.679 -77.953  25.267  1.00 72.10           C  
ANISOU 2817  CD2 LEU A 665     8991  10023   8379     44  -1270     42       C  
ATOM   2818  N   LEU A 666     -55.043 -74.482  26.347  1.00 72.17           N  
ANISOU 2818  N   LEU A 666     8862  10021   8537   -344  -1093     26       N  
ATOM   2819  CA  LEU A 666     -55.178 -73.347  25.440  1.00 71.89           C  
ANISOU 2819  CA  LEU A 666     8682  10007   8625   -429  -1077     12       C  
ATOM   2820  C   LEU A 666     -54.159 -72.256  25.735  1.00 72.51           C  
ANISOU 2820  C   LEU A 666     8688  10156   8704   -462  -1099    -80       C  
ATOM   2821  O   LEU A 666     -53.518 -71.725  24.823  1.00 72.83           O  
ANISOU 2821  O   LEU A 666     8612  10241   8816   -497  -1103    -84       O  
ATOM   2822  CB  LEU A 666     -56.590 -72.774  25.466  1.00 72.05           C  
ANISOU 2822  CB  LEU A 666     8679   9932   8765   -489   -965     68       C  
ATOM   2823  CG  LEU A 666     -57.699 -73.559  24.753  1.00 72.77           C  
ANISOU 2823  CG  LEU A 666     8725   9988   8935   -516   -959    124       C  
ATOM   2824  CD1 LEU A 666     -58.997 -72.795  24.851  1.00 73.93           C  
ANISOU 2824  CD1 LEU A 666     8777  10091   9219   -547   -857    175       C  
ATOM   2825  CD2 LEU A 666     -57.365 -73.806  23.312  1.00 72.62           C  
ANISOU 2825  CD2 LEU A 666     8626  10061   8903   -504  -1066    119       C  
ATOM   2826  N   TYR A 667     -53.992 -71.941  27.008  1.00 73.45           N  
ANISOU 2826  N   TYR A 667     8877  10292   8737   -459  -1101   -170       N  
ATOM   2827  CA  TYR A 667     -53.019 -70.941  27.412  1.00 75.17           C  
ANISOU 2827  CA  TYR A 667     9009  10582   8969   -531  -1141   -333       C  
ATOM   2828  C   TYR A 667     -51.588 -71.299  26.971  1.00 76.00           C  
ANISOU 2828  C   TYR A 667     8967  10855   9052   -502  -1274   -392       C  
ATOM   2829  O   TYR A 667     -50.910 -70.477  26.352  1.00 76.52           O  
ANISOU 2829  O   TYR A 667     8876  10932   9266   -613  -1240   -453       O  
ATOM   2830  CB  TYR A 667     -53.115 -70.674  28.924  1.00 76.65           C  
ANISOU 2830  CB  TYR A 667     9315  10807   8999   -515  -1153   -467       C  
ATOM   2831  CG  TYR A 667     -51.934 -69.942  29.477  1.00 79.60           C  
ANISOU 2831  CG  TYR A 667     9583  11320   9340   -590  -1269   -708       C  
ATOM   2832  CD1 TYR A 667     -51.737 -68.581  29.216  1.00 82.12           C  
ANISOU 2832  CD1 TYR A 667     9799  11522   9880   -776  -1175   -854       C  
ATOM   2833  CD2 TYR A 667     -50.982 -70.612  30.242  1.00 82.43           C  
ANISOU 2833  CD2 TYR A 667     9926  11926   9467   -473  -1473   -797       C  
ATOM   2834  CE1 TYR A 667     -50.608 -67.901  29.729  1.00 85.07           C  
ANISOU 2834  CE1 TYR A 667    10034  12015  10271   -902  -1282  -1137       C  
ATOM   2835  CE2 TYR A 667     -49.860 -69.949  30.748  1.00 85.13           C  
ANISOU 2835  CE2 TYR A 667    10104  12454   9785   -558  -1624  -1068       C  
ATOM   2836  CZ  TYR A 667     -49.685 -68.608  30.491  1.00 86.43           C  
ANISOU 2836  CZ  TYR A 667    10147  12492  10199   -800  -1527  -1259       C  
ATOM   2837  OH  TYR A 667     -48.582 -67.989  31.001  1.00 91.77           O  
ANISOU 2837  OH  TYR A 667    10632  13346  10891   -930  -1676  -1573       O  
ATOM   2838  N   GLU A 668     -51.145 -72.518  27.279  1.00 76.64           N  
ANISOU 2838  N   GLU A 668     9097  11050   8972   -341  -1391   -355       N  
ATOM   2839  CA  GLU A 668     -49.831 -72.997  26.868  1.00 78.07           C  
ANISOU 2839  CA  GLU A 668     9119  11404   9137   -257  -1507   -396       C  
ATOM   2840  C   GLU A 668     -49.615 -72.927  25.368  1.00 77.14           C  
ANISOU 2840  C   GLU A 668     8885  11254   9171   -306  -1418   -334       C  
ATOM   2841  O   GLU A 668     -48.556 -72.480  24.914  1.00 78.05           O  
ANISOU 2841  O   GLU A 668     8791  11485   9376   -356  -1421   -410       O  
ATOM   2842  CB  GLU A 668     -49.607 -74.430  27.329  1.00 79.18           C  
ANISOU 2842  CB  GLU A 668     9379  11603   9100    -19  -1601   -308       C  
ATOM   2843  CG  GLU A 668     -49.158 -74.531  28.772  1.00 83.50           C  
ANISOU 2843  CG  GLU A 668     9977  12323   9426    106  -1748   -374       C  
ATOM   2844  CD  GLU A 668     -49.224 -75.946  29.325  1.00 87.19           C  
ANISOU 2844  CD  GLU A 668    10650  12773   9702    379  -1779   -200       C  
ATOM   2845  OE1 GLU A 668     -49.541 -76.895  28.567  1.00 85.07           O  
ANISOU 2845  OE1 GLU A 668    10471  12329   9521    445  -1682    -67       O  
ATOM   2846  OE2 GLU A 668     -48.953 -76.096  30.542  1.00 92.30           O1-
ANISOU 2846  OE2 GLU A 668    11387  13580  10101    534  -1893   -203       O1-
ATOM   2847  N   THR A 669     -50.619 -73.363  24.606  1.00 75.82           N  
ANISOU 2847  N   THR A 669     8837  10949   9021   -296  -1334   -207       N  
ATOM   2848  CA  THR A 669     -50.526 -73.432  23.145  1.00 75.65           C  
ANISOU 2848  CA  THR A 669     8752  10935   9056   -301  -1265   -147       C  
ATOM   2849  C   THR A 669     -50.426 -72.047  22.513  1.00 76.25           C  
ANISOU 2849  C   THR A 669     8715  10991   9263   -442  -1145   -124       C  
ATOM   2850  O   THR A 669     -49.698 -71.831  21.543  1.00 76.77           O  
ANISOU 2850  O   THR A 669     8670  11133   9366   -448  -1069    -97       O  
ATOM   2851  CB  THR A 669     -51.719 -74.144  22.581  1.00 74.49           C  
ANISOU 2851  CB  THR A 669     8743  10679   8878   -276  -1243    -69       C  
ATOM   2852  OG1 THR A 669     -51.864 -75.389  23.256  1.00 75.11           O  
ANISOU 2852  OG1 THR A 669     8954  10698   8884   -173  -1296    -76       O  
ATOM   2853  CG2 THR A 669     -51.498 -74.432  21.124  1.00 76.00           C  
ANISOU 2853  CG2 THR A 669     8897  10938   9041   -238  -1211    -50       C  
ATOM   2854  N   ALA A 670     -51.170 -71.114  23.094  1.00 76.71           N  
ANISOU 2854  N   ALA A 670     8821  10926   9400   -541  -1091   -121       N  
ATOM   2855  CA  ALA A 670     -51.148 -69.719  22.706  1.00 77.62           C  
ANISOU 2855  CA  ALA A 670     8871  10940   9679   -665   -942    -86       C  
ATOM   2856  C   ALA A 670     -49.817 -69.082  23.069  1.00 79.61           C  
ANISOU 2856  C   ALA A 670     8954  11248  10046   -788   -923   -241       C  
ATOM   2857  O   ALA A 670     -49.302 -68.240  22.345  1.00 81.12           O  
ANISOU 2857  O   ALA A 670     9044  11386  10392   -891   -763   -197       O  
ATOM   2858  CB  ALA A 670     -52.265 -69.015  23.405  1.00 77.61           C  
ANISOU 2858  CB  ALA A 670     8973  10771   9742   -704   -883    -78       C  
ATOM   2859  N   LEU A 671     -49.267 -69.489  24.202  1.00 80.20           N  
ANISOU 2859  N   LEU A 671     8989  11442  10041   -777  -1081   -419       N  
ATOM   2860  CA  LEU A 671     -47.981 -69.007  24.633  1.00 82.76           C  
ANISOU 2860  CA  LEU A 671     9092  11889  10462   -895  -1127   -622       C  
ATOM   2861  C   LEU A 671     -46.927 -69.423  23.622  1.00 84.11           C  
ANISOU 2861  C   LEU A 671     9065  12209  10682   -857  -1089   -573       C  
ATOM   2862  O   LEU A 671     -46.111 -68.605  23.191  1.00 86.21           O  
ANISOU 2862  O   LEU A 671     9129  12471  11155  -1025   -953   -630       O  
ATOM   2863  CB  LEU A 671     -47.670 -69.588  26.007  1.00 83.65           C  
ANISOU 2863  CB  LEU A 671     9213  12182  10387   -808  -1362   -795       C  
ATOM   2864  CG  LEU A 671     -46.785 -68.889  27.032  1.00 85.70           C  
ANISOU 2864  CG  LEU A 671     9296  12582  10684   -948  -1485  -1098       C  
ATOM   2865  CD1 LEU A 671     -47.386 -67.588  27.506  1.00 85.33           C  
ANISOU 2865  CD1 LEU A 671     9341  12304  10773  -1160  -1355  -1236       C  
ATOM   2866  CD2 LEU A 671     -46.652 -69.838  28.187  1.00 87.00           C  
ANISOU 2866  CD2 LEU A 671     9534  12979  10539   -734  -1739  -1159       C  
ATOM   2867  N   LEU A 672     -46.947 -70.691  23.227  1.00 83.72           N  
ANISOU 2867  N   LEU A 672     9078  12266  10465   -644  -1169   -474       N  
ATOM   2868  CA  LEU A 672     -45.995 -71.171  22.227  1.00 85.83           C  
ANISOU 2868  CA  LEU A 672     9179  12675  10754   -566  -1103   -435       C  
ATOM   2869  C   LEU A 672     -46.144 -70.425  20.915  1.00 86.90           C  
ANISOU 2869  C   LEU A 672     9317  12708  10992   -663   -848   -284       C  
ATOM   2870  O   LEU A 672     -45.155 -69.939  20.356  1.00 89.70           O  
ANISOU 2870  O   LEU A 672     9455  13134  11493   -755   -694   -298       O  
ATOM   2871  CB  LEU A 672     -46.170 -72.656  21.962  1.00 84.83           C  
ANISOU 2871  CB  LEU A 672     9184  12606  10439   -312  -1194   -366       C  
ATOM   2872  CG  LEU A 672     -45.477 -73.612  22.921  1.00 86.37           C  
ANISOU 2872  CG  LEU A 672     9317  12961  10538   -122  -1395   -458       C  
ATOM   2873  CD1 LEU A 672     -46.082 -75.010  22.750  1.00 84.87           C  
ANISOU 2873  CD1 LEU A 672     9373  12676  10195     99  -1428   -358       C  
ATOM   2874  CD2 LEU A 672     -43.952 -73.605  22.725  1.00 89.36           C  
ANISOU 2874  CD2 LEU A 672     9348  13585  11019    -78  -1404   -562       C  
ATOM   2875  N   SER A 673     -47.385 -70.331  20.439  1.00 85.72           N  
ANISOU 2875  N   SER A 673     9399  12408  10762   -632   -797   -129       N  
ATOM   2876  CA  SER A 673     -47.696 -69.652  19.196  1.00 86.89           C  
ANISOU 2876  CA  SER A 673     9598  12482  10932   -657   -582     63       C  
ATOM   2877  C   SER A 673     -47.245 -68.213  19.139  1.00 89.38           C  
ANISOU 2877  C   SER A 673     9805  12658  11498   -861   -359     95       C  
ATOM   2878  O   SER A 673     -47.052 -67.678  18.057  1.00 91.24           O  
ANISOU 2878  O   SER A 673    10039  12862  11764   -870   -124    277       O  
ATOM   2879  CB  SER A 673     -49.187 -69.689  18.959  1.00 85.38           C  
ANISOU 2879  CB  SER A 673     9627  12184  10627   -581   -625    196       C  
ATOM   2880  OG  SER A 673     -49.546 -70.977  18.551  1.00 85.40           O  
ANISOU 2880  OG  SER A 673     9721  12298  10427   -426   -756    180       O  
ATOM   2881  N   SER A 674     -47.086 -67.582  20.295  1.00 90.49           N  
ANISOU 2881  N   SER A 674     9872  12699  11808  -1024   -411    -84       N  
ATOM   2882  CA  SER A 674     -46.777 -66.166  20.339  1.00 93.37           C  
ANISOU 2882  CA  SER A 674    10163  12850  12464  -1256   -182    -98       C  
ATOM   2883  C   SER A 674     -45.303 -65.889  20.553  1.00 96.75           C  
ANISOU 2883  C   SER A 674    10270  13383  13106  -1453   -126   -302       C  
ATOM   2884  O   SER A 674     -44.920 -64.764  20.848  1.00 99.63           O  
ANISOU 2884  O   SER A 674    10531  13558  13764  -1710     37   -415       O  
ATOM   2885  CB  SER A 674     -47.620 -65.483  21.402  1.00 92.86           C  
ANISOU 2885  CB  SER A 674    10232  12571  12479  -1338   -233   -208       C  
ATOM   2886  OG  SER A 674     -48.990 -65.592  21.054  1.00 91.58           O  
ANISOU 2886  OG  SER A 674    10305  12310  12179  -1164   -232      8       O  
ATOM   2887  N   GLY A 675     -44.468 -66.906  20.390  1.00 97.28           N  
ANISOU 2887  N   GLY A 675    10160  13742  13059  -1337   -248   -366       N  
ATOM   2888  CA  GLY A 675     -43.027 -66.687  20.432  1.00101.32           C  
ANISOU 2888  CA  GLY A 675    10294  14408  13794  -1501   -179   -543       C  
ATOM   2889  C   GLY A 675     -42.431 -66.851  21.814  1.00102.97           C  
ANISOU 2889  C   GLY A 675    10285  14800  14038  -1574   -483   -889       C  
ATOM   2890  O   GLY A 675     -41.214 -66.803  21.981  1.00105.93           O  
ANISOU 2890  O   GLY A 675    10281  15382  14585  -1687   -507  -1083       O  
ATOM   2891  N   PHE A 676     -43.291 -67.057  22.807  1.00101.60           N  
ANISOU 2891  N   PHE A 676    10336  14585  13683  -1494   -716   -964       N  
ATOM   2892  CA  PHE A 676     -42.836 -67.250  24.172  1.00103.39           C  
ANISOU 2892  CA  PHE A 676    10419  15023  13841  -1508  -1028  -1272       C  
ATOM   2893  C   PHE A 676     -42.335 -68.665  24.312  1.00104.06           C  
ANISOU 2893  C   PHE A 676    10418  15435  13685  -1197  -1267  -1245       C  
ATOM   2894  O   PHE A 676     -42.723 -69.537  23.548  1.00102.41           O  
ANISOU 2894  O   PHE A 676    10376  15206  13329   -972  -1209  -1009       O  
ATOM   2895  CB  PHE A 676     -43.960 -66.980  25.167  1.00101.04           C  
ANISOU 2895  CB  PHE A 676    10427  14566  13396  -1503  -1137  -1334       C  
ATOM   2896  CG  PHE A 676     -44.339 -65.531  25.272  1.00100.92           C  
ANISOU 2896  CG  PHE A 676    10476  14221  13646  -1795   -918  -1433       C  
ATOM   2897  CD1 PHE A 676     -43.581 -64.652  26.034  1.00104.34           C  
ANISOU 2897  CD1 PHE A 676    10682  14670  14290  -2082   -961  -1806       C  
ATOM   2898  CD2 PHE A 676     -45.459 -65.042  24.614  1.00 98.13           C  
ANISOU 2898  CD2 PHE A 676    10404  13536  13344  -1773   -674  -1171       C  
ATOM   2899  CE1 PHE A 676     -43.932 -63.309  26.139  1.00105.62           C  
ANISOU 2899  CE1 PHE A 676    10934  14459  14737  -2358   -721  -1921       C  
ATOM   2900  CE2 PHE A 676     -45.819 -63.699  24.711  1.00 99.30           C  
ANISOU 2900  CE2 PHE A 676    10636  13332  13760  -1997   -440  -1236       C  
ATOM   2901  CZ  PHE A 676     -45.056 -62.836  25.479  1.00102.97           C  
ANISOU 2901  CZ  PHE A 676    10911  13751  14461  -2297   -445  -1615       C  
ATOM   2902  N   SER A 677     -41.446 -68.884  25.267  1.00108.12           N  
ANISOU 2902  N   SER A 677    10663  16251  14163  -1173  -1537  -1499       N  
ATOM   2903  CA  SER A 677     -41.020 -70.222  25.602  1.00109.50           C  
ANISOU 2903  CA  SER A 677    10790  16722  14093   -817  -1785  -1455       C  
ATOM   2904  C   SER A 677     -41.780 -70.681  26.841  1.00109.13           C  
ANISOU 2904  C   SER A 677    11038  16702  13724   -644  -2036  -1473       C  
ATOM   2905  O   SER A 677     -42.246 -69.860  27.636  1.00109.85           O  
ANISOU 2905  O   SER A 677    11231  16708  13798   -829  -2079  -1639       O  
ATOM   2906  CB  SER A 677     -39.525 -70.233  25.861  1.00113.95           C  
ANISOU 2906  CB  SER A 677    10839  17662  14793   -831  -1941  -1688       C  
ATOM   2907  OG  SER A 677     -38.951 -71.371  25.246  1.00115.69           O  
ANISOU 2907  OG  SER A 677    10949  18054  14951   -511  -1939  -1528       O  
ATOM   2908  N   LEU A 678     -41.917 -71.988  27.015  1.00108.84           N  
ANISOU 2908  N   LEU A 678    11159  16758  13434   -283  -2163  -1298       N  
ATOM   2909  CA  LEU A 678     -42.672 -72.486  28.161  1.00108.74           C  
ANISOU 2909  CA  LEU A 678    11462  16747  13106   -103  -2338  -1254       C  
ATOM   2910  C   LEU A 678     -41.847 -72.548  29.445  1.00113.01           C  
ANISOU 2910  C   LEU A 678    11810  17679  13448     22  -2679  -1470       C  
ATOM   2911  O   LEU A 678     -40.611 -72.505  29.435  1.00115.96           O  
ANISOU 2911  O   LEU A 678    11765  18370  13922     42  -2832  -1636       O  
ATOM   2912  CB  LEU A 678     -43.315 -73.845  27.862  1.00106.60           C  
ANISOU 2912  CB  LEU A 678    11503  16334  12667    207  -2283   -956       C  
ATOM   2913  CG  LEU A 678     -44.375 -73.884  26.761  1.00103.22           C  
ANISOU 2913  CG  LEU A 678    11313  15555  12349    104  -2010   -773       C  
ATOM   2914  CD1 LEU A 678     -44.445 -75.269  26.157  1.00103.34           C  
ANISOU 2914  CD1 LEU A 678    11470  15497  12296    380  -1962   -582       C  
ATOM   2915  CD2 LEU A 678     -45.730 -73.473  27.306  1.00102.42           C  
ANISOU 2915  CD2 LEU A 678    11519  15227  12167    -13  -1944   -728       C  
ATOM   2916  N   GLU A 679     -42.575 -72.623  30.552  1.00113.59           N  
ANISOU 2916  N   GLU A 679    12181  17750  13225    108  -2792  -1471       N  
ATOM   2917  CA  GLU A 679     -42.017 -72.764  31.887  1.00117.83           C  
ANISOU 2917  CA  GLU A 679    12644  18679  13444    290  -3134  -1641       C  
ATOM   2918  C   GLU A 679     -41.342 -74.125  32.025  1.00119.11           C  
ANISOU 2918  C   GLU A 679    12755  19091  13410    754  -3314  -1430       C  
ATOM   2919  O   GLU A 679     -40.183 -74.208  32.429  1.00123.14           O  
ANISOU 2919  O   GLU A 679    12898  20027  13863    896  -3600  -1594       O  
ATOM   2920  CB  GLU A 679     -43.136 -72.597  32.941  1.00117.88           C  
ANISOU 2920  CB  GLU A 679    13072  18577  13140    306  -3125  -1626       C  
ATOM   2921  CG  GLU A 679     -44.337 -73.605  32.844  1.00116.56           C  
ANISOU 2921  CG  GLU A 679    13364  18097  12827    525  -2914  -1227       C  
ATOM   2922  CD  GLU A 679     -45.067 -73.605  31.482  1.00115.44           C  
ANISOU 2922  CD  GLU A 679    13298  17541  13020    351  -2592  -1048       C  
ATOM   2923  OE1 GLU A 679     -45.455 -74.707  31.014  1.00114.72           O  
ANISOU 2923  OE1 GLU A 679    13390  17285  12910    554  -2484   -768       O  
ATOM   2924  OE2 GLU A 679     -45.253 -72.512  30.882  1.00114.97           O1-
ANISOU 2924  OE2 GLU A 679    13126  17322  13234     22  -2446  -1191       O1-
ATOM   2925  N   ASP A 680     -42.081 -75.180  31.672  1.00115.93           N  
ANISOU 2925  N   ASP A 680    12706  18408  12933    988  -3136  -1077       N  
ATOM   2926  CA  ASP A 680     -41.645 -76.567  31.832  1.00117.05           C  
ANISOU 2926  CA  ASP A 680    12915  18659  12896   1465  -3234   -822       C  
ATOM   2927  C   ASP A 680     -42.243 -77.395  30.709  1.00112.48           C  
ANISOU 2927  C   ASP A 680    12561  17667  12506   1515  -2928   -561       C  
ATOM   2928  O   ASP A 680     -43.392 -77.836  30.812  1.00110.06           O  
ANISOU 2928  O   ASP A 680    12665  17035  12118   1522  -2751   -365       O  
ATOM   2929  CB  ASP A 680     -42.084 -77.122  33.195  1.00119.77           C  
ANISOU 2929  CB  ASP A 680    13605  19109  12791   1769  -3379   -670       C  
ATOM   2930  CG  ASP A 680     -41.657 -78.578  33.415  1.00124.06           C  
ANISOU 2930  CG  ASP A 680    14271  19713  13152   2309  -3447   -350       C  
ATOM   2931  OD1 ASP A 680     -40.430 -78.880  33.397  1.00128.49           O  
ANISOU 2931  OD1 ASP A 680    14469  20629  13719   2571  -3678   -401       O  
ATOM   2932  OD2 ASP A 680     -42.566 -79.415  33.632  1.00124.74           O1-
ANISOU 2932  OD2 ASP A 680    14811  19475  13108   2476  -3250    -41       O1-
ATOM   2933  N   PRO A 681     -41.460 -77.619  29.636  1.00111.48           N  
ANISOU 2933  N   PRO A 681    12154  17568  12634   1543  -2856   -582       N  
ATOM   2934  CA  PRO A 681     -41.966 -78.278  28.437  1.00107.73           C  
ANISOU 2934  CA  PRO A 681    11863  16732  12334   1545  -2571   -419       C  
ATOM   2935  C   PRO A 681     -42.339 -79.740  28.671  1.00107.39           C  
ANISOU 2935  C   PRO A 681    12178  16478  12147   1927  -2515   -145       C  
ATOM   2936  O   PRO A 681     -42.975 -80.344  27.816  1.00105.35           O  
ANISOU 2936  O   PRO A 681    12143  15875  12010   1899  -2283    -43       O  
ATOM   2937  CB  PRO A 681     -40.799 -78.156  27.445  1.00109.11           C  
ANISOU 2937  CB  PRO A 681    11614  17090  12751   1547  -2534   -536       C  
ATOM   2938  CG  PRO A 681     -39.867 -77.135  28.038  1.00112.22           C  
ANISOU 2938  CG  PRO A 681    11571  17883  13185   1397  -2759   -794       C  
ATOM   2939  CD  PRO A 681     -40.031 -77.283  29.505  1.00114.77           C  
ANISOU 2939  CD  PRO A 681    12040  18386  13180   1578  -3035   -785       C  
ATOM   2940  N   GLN A 682     -41.957 -80.291  29.819  1.00109.68           N  
ANISOU 2940  N   GLN A 682    12529  16968  12175   2278  -2720    -33       N  
ATOM   2941  CA  GLN A 682     -42.327 -81.652  30.184  1.00110.22           C  
ANISOU 2941  CA  GLN A 682    12982  16789  12106   2657  -2629    272       C  
ATOM   2942  C   GLN A 682     -43.794 -81.699  30.595  1.00107.16           C  
ANISOU 2942  C   GLN A 682    13038  16048  11630   2470  -2444    404       C  
ATOM   2943  O   GLN A 682     -44.531 -82.566  30.137  1.00105.91           O  
ANISOU 2943  O   GLN A 682    13182  15475  11583   2492  -2198    565       O  
ATOM   2944  CB  GLN A 682     -41.468 -82.184  31.334  1.00115.28           C  
ANISOU 2944  CB  GLN A 682    13570  17781  12450   3142  -2903    404       C  
ATOM   2945  CG  GLN A 682     -40.162 -81.425  31.573  1.00119.05           C  
ANISOU 2945  CG  GLN A 682    13495  18831  12906   3174  -3237    147       C  
ATOM   2946  CD  GLN A 682     -38.926 -82.230  31.226  1.00123.53           C  
ANISOU 2946  CD  GLN A 682    13764  19604  13566   3614  -3329    213       C  
ATOM   2947  OE1 GLN A 682     -37.862 -82.042  31.824  1.00126.56           O  
ANISOU 2947  OE1 GLN A 682    13757  20502  13827   3843  -3658    111       O  
ATOM   2948  NE2 GLN A 682     -39.062 -83.144  30.266  1.00123.26           N  
ANISOU 2948  NE2 GLN A 682    13898  19184  13749   3746  -3043    361       N  
ATOM   2949  N   THR A 683     -44.221 -80.778  31.461  1.00106.06           N  
ANISOU 2949  N   THR A 683    12923  16068  11305   2278  -2547    310       N  
ATOM   2950  CA  THR A 683     -45.606 -80.794  31.949  1.00103.91           C  
ANISOU 2950  CA  THR A 683    13039  15497  10943   2124  -2348    439       C  
ATOM   2951  C   THR A 683     -46.564 -80.525  30.808  1.00 98.96           C  
ANISOU 2951  C   THR A 683    12450  14517  10631   1749  -2099    372       C  
ATOM   2952  O   THR A 683     -47.619 -81.152  30.735  1.00 98.31           O  
ANISOU 2952  O   THR A 683    12666  14079  10606   1700  -1870    531       O  
ATOM   2953  CB  THR A 683     -45.892 -79.761  33.044  1.00104.63           C  
ANISOU 2953  CB  THR A 683    13144  15832  10778   1986  -2477    305       C  
ATOM   2954  OG1 THR A 683     -45.594 -78.461  32.533  1.00104.11           O  
ANISOU 2954  OG1 THR A 683    12740  15916  10900   1633  -2560    -19       O  
ATOM   2955  CG2 THR A 683     -45.072 -80.037  34.320  1.00109.51           C  
ANISOU 2955  CG2 THR A 683    13768  16858  10979   2382  -2760    368       C  
ATOM   2956  N   HIS A 684     -46.196 -79.598  29.923  1.00 95.81           N  
ANISOU 2956  N   HIS A 684    11738  14227  10435   1490  -2137    142       N  
ATOM   2957  CA  HIS A 684     -46.987 -79.350  28.735  1.00 91.33           C  
ANISOU 2957  CA  HIS A 684    11186  13392  10122   1197  -1935     95       C  
ATOM   2958  C   HIS A 684     -47.072 -80.611  27.869  1.00 90.94           C  
ANISOU 2958  C   HIS A 684    11275  13077  10198   1343  -1789    207       C  
ATOM   2959  O   HIS A 684     -48.142 -80.965  27.365  1.00 89.32           O  
ANISOU 2959  O   HIS A 684    11263  12568  10105   1190  -1610    249       O  
ATOM   2960  CB  HIS A 684     -46.445 -78.192  27.908  1.00 89.86           C  
ANISOU 2960  CB  HIS A 684    10666  13369  10108    952  -1971   -115       C  
ATOM   2961  CG  HIS A 684     -47.051 -78.136  26.544  1.00 87.89           C  
ANISOU 2961  CG  HIS A 684    10433  12900  10058    761  -1785   -121       C  
ATOM   2962  ND1 HIS A 684     -48.336 -77.694  26.323  1.00 86.20           N  
ANISOU 2962  ND1 HIS A 684    10365  12482   9905    530  -1660    -99       N  
ATOM   2963  CD2 HIS A 684     -46.585 -78.551  25.343  1.00 87.97           C  
ANISOU 2963  CD2 HIS A 684    10348  12888  10187    805  -1709   -143       C  
ATOM   2964  CE1 HIS A 684     -48.622 -77.804  25.039  1.00 84.73           C  
ANISOU 2964  CE1 HIS A 684    10158  12187   9846    439  -1552   -111       C  
ATOM   2965  NE2 HIS A 684     -47.577 -78.323  24.421  1.00 85.38           N  
ANISOU 2965  NE2 HIS A 684    10117  12372   9950    597  -1568   -143       N  
ATOM   2966  N   ALA A 685     -45.942 -81.285  27.694  1.00 92.56           N  
ANISOU 2966  N   ALA A 685    11364  13406  10398   1640  -1866    228       N  
ATOM   2967  CA  ALA A 685     -45.922 -82.548  26.968  1.00 92.87           C  
ANISOU 2967  CA  ALA A 685    11563  13170  10552   1827  -1712    310       C  
ATOM   2968  C   ALA A 685     -46.830 -83.583  27.646  1.00 93.85           C  
ANISOU 2968  C   ALA A 685    12094  12937  10627   1939  -1565    527       C  
ATOM   2969  O   ALA A 685     -47.656 -84.194  26.985  1.00 92.91           O  
ANISOU 2969  O   ALA A 685    12167  12463  10671   1804  -1368    520       O  
ATOM   2970  CB  ALA A 685     -44.501 -83.065  26.822  1.00 95.48           C  
ANISOU 2970  CB  ALA A 685    11683  13710  10883   2188  -1810    309       C  
ATOM   2971  N   ASN A 686     -46.695 -83.748  28.965  1.00 96.04           N  
ANISOU 2971  N   ASN A 686    12498  13318  10673   2169  -1652    709       N  
ATOM   2972  CA  ASN A 686     -47.528 -84.675  29.742  1.00 97.45           C  
ANISOU 2972  CA  ASN A 686    13082  13158  10783   2288  -1464    971       C  
ATOM   2973  C   ASN A 686     -49.007 -84.413  29.581  1.00 94.76           C  
ANISOU 2973  C   ASN A 686    12893  12539  10571   1890  -1260    939       C  
ATOM   2974  O   ASN A 686     -49.798 -85.348  29.578  1.00 95.78           O  
ANISOU 2974  O   ASN A 686    13303  12261  10828   1867  -1015   1073       O  
ATOM   2975  CB  ASN A 686     -47.195 -84.597  31.229  1.00100.46           C  
ANISOU 2975  CB  ASN A 686    13563  13798  10808   2576  -1607   1165       C  
ATOM   2976  CG  ASN A 686     -45.829 -85.140  31.554  1.00104.08           C  
ANISOU 2976  CG  ASN A 686    13910  14514  11119   3065  -1806   1269       C  
ATOM   2977  OD1 ASN A 686     -45.319 -86.039  30.885  1.00105.27           O  
ANISOU 2977  OD1 ASN A 686    14072  14479  11447   3289  -1723   1320       O  
ATOM   2978  ND2 ASN A 686     -45.227 -84.601  32.601  1.00106.45           N  
ANISOU 2978  ND2 ASN A 686    14093  15265  11087   3254  -2079   1282       N  
ATOM   2979  N   ARG A 687     -49.371 -83.139  29.469  1.00 91.68           N  
ANISOU 2979  N   ARG A 687    12302  12358  10174   1581  -1349    759       N  
ATOM   2980  CA  ARG A 687     -50.745 -82.751  29.220  1.00 89.66           C  
ANISOU 2980  CA  ARG A 687    12107  11898  10058   1223  -1183    709       C  
ATOM   2981  C   ARG A 687     -51.173 -83.311  27.893  1.00 88.74           C  
ANISOU 2981  C   ARG A 687    11980  11517  10219   1059  -1064    597       C  
ATOM   2982  O   ARG A 687     -52.085 -84.120  27.837  1.00 89.74           O  
ANISOU 2982  O   ARG A 687    12306  11298  10491    964   -860    662       O  
ATOM   2983  CB  ARG A 687     -50.874 -81.245  29.188  1.00 87.40           C  
ANISOU 2983  CB  ARG A 687    11585  11880   9741    981  -1305    531       C  
ATOM   2984  CG  ARG A 687     -52.200 -80.733  29.662  1.00 86.97           C  
ANISOU 2984  CG  ARG A 687    11626  11711   9706    750  -1156    556       C  
ATOM   2985  CD  ARG A 687     -52.158 -79.220  29.832  1.00 88.17           C  
ANISOU 2985  CD  ARG A 687    11581  12113   9807    586  -1270    390       C  
ATOM   2986  NE  ARG A 687     -50.958 -78.711  30.522  1.00 89.75           N  
ANISOU 2986  NE  ARG A 687    11673  12639   9788    747  -1490    311       N  
ATOM   2987  CZ  ARG A 687     -50.858 -78.519  31.833  1.00 92.35           C  
ANISOU 2987  CZ  ARG A 687    12123  13130   9833    878  -1548    345       C  
ATOM   2988  NH1 ARG A 687     -51.870 -78.811  32.634  1.00 94.22           N1+
ANISOU 2988  NH1 ARG A 687    12622  13216   9961    886  -1356    497       N1+
ATOM   2989  NH2 ARG A 687     -49.739 -78.039  32.350  1.00 95.08           N  
ANISOU 2989  NH2 ARG A 687    12315  13816   9993    998  -1795    212       N  
ATOM   2990  N   ILE A 688     -50.490 -82.904  26.828  1.00 87.79           N  
ANISOU 2990  N   ILE A 688    11625  11565  10165   1023  -1181    415       N  
ATOM   2991  CA  ILE A 688     -50.711 -83.483  25.507  1.00 88.06           C  
ANISOU 2991  CA  ILE A 688    11659  11411  10387    924  -1095    276       C  
ATOM   2992  C   ILE A 688     -50.907 -84.997  25.589  1.00 91.78           C  
ANISOU 2992  C   ILE A 688    12415  11487  10967   1069   -916    365       C  
ATOM   2993  O   ILE A 688     -51.862 -85.509  25.046  1.00 92.47           O  
ANISOU 2993  O   ILE A 688    12606  11294  11234    856   -777    274       O  
ATOM   2994  CB  ILE A 688     -49.547 -83.199  24.517  1.00 87.45           C  
ANISOU 2994  CB  ILE A 688    11352  11570  10302   1023  -1200    131       C  
ATOM   2995  CG1 ILE A 688     -49.064 -81.757  24.604  1.00 84.91           C  
ANISOU 2995  CG1 ILE A 688    10753  11607   9899    921  -1345     76       C  
ATOM   2996  CG2 ILE A 688     -49.953 -83.525  23.106  1.00 86.43           C  
ANISOU 2996  CG2 ILE A 688    11227  11316  10295    875  -1120    -49       C  
ATOM   2997  CD1 ILE A 688     -50.052 -80.784  24.180  1.00 81.12           C  
ANISOU 2997  CD1 ILE A 688    10212  11138   9472    609  -1324     10       C  
ATOM   2998  N   TYR A 689     -50.014 -85.705  26.273  1.00 95.61           N  
ANISOU 2998  N   TYR A 689    13020  11944  11360   1436   -916    537       N  
ATOM   2999  CA  TYR A 689     -50.065 -87.171  26.311  1.00100.29           C  
ANISOU 2999  CA  TYR A 689    13913  12106  12087   1626   -708    645       C  
ATOM   3000  C   TYR A 689     -51.345 -87.681  26.940  1.00102.77           C  
ANISOU 3000  C   TYR A 689    14493  12043  12510   1439   -475    784       C  
ATOM   3001  O   TYR A 689     -51.937 -88.637  26.444  1.00104.58           O  
ANISOU 3001  O   TYR A 689    14900  11846  12988   1319   -262    715       O  
ATOM   3002  CB  TYR A 689     -48.865 -87.780  27.060  1.00103.36           C  
ANISOU 3002  CB  TYR A 689    14382  12559  12330   2130   -756    872       C  
ATOM   3003  CG  TYR A 689     -47.500 -87.565  26.429  1.00102.75           C  
ANISOU 3003  CG  TYR A 689    14024  12804  12211   2367   -932    744       C  
ATOM   3004  CD1 TYR A 689     -47.307 -87.685  25.051  1.00101.06           C  
ANISOU 3004  CD1 TYR A 689    13696  12542  12158   2259   -883    481       C  
ATOM   3005  CD2 TYR A 689     -46.400 -87.265  27.223  1.00103.62           C  
ANISOU 3005  CD2 TYR A 689    13968  13293  12110   2709  -1140    876       C  
ATOM   3006  CE1 TYR A 689     -46.065 -87.483  24.493  1.00102.05           C  
ANISOU 3006  CE1 TYR A 689    13552  12967  12255   2476   -989    380       C  
ATOM   3007  CE2 TYR A 689     -45.158 -87.070  26.677  1.00104.14           C  
ANISOU 3007  CE2 TYR A 689    13719  13668  12180   2910  -1280    754       C  
ATOM   3008  CZ  TYR A 689     -44.991 -87.182  25.318  1.00103.68           C  
ANISOU 3008  CZ  TYR A 689    13556  13532  12305   2794  -1178    521       C  
ATOM   3009  OH  TYR A 689     -43.738 -86.993  24.787  1.00106.32           O  
ANISOU 3009  OH  TYR A 689    13562  14180  12654   3001  -1266    415       O  
ATOM   3010  N   ARG A 690     -51.754 -87.039  28.039  1.00104.10           N  
ANISOU 3010  N   ARG A 690    14681  12369  12503   1406   -495    957       N  
ATOM   3011  CA  ARG A 690     -52.935 -87.438  28.804  1.00107.13           C  
ANISOU 3011  CA  ARG A 690    15301  12440  12962   1251   -232   1134       C  
ATOM   3012  C   ARG A 690     -54.137 -87.359  27.865  1.00106.54           C  
ANISOU 3012  C   ARG A 690    15114  12179  13187    796   -132    884       C  
ATOM   3013  O   ARG A 690     -54.969 -88.277  27.786  1.00109.06           O  
ANISOU 3013  O   ARG A 690    15606  12065  13766    628    131    896       O  
ATOM   3014  CB  ARG A 690     -53.114 -86.532  30.027  1.00106.34           C  
ANISOU 3014  CB  ARG A 690    15193  12640  12570   1288   -295   1296       C  
ATOM   3015  CG  ARG A 690     -53.144 -87.307  31.341  1.00111.77           C  
ANISOU 3015  CG  ARG A 690    16239  13148  13080   1579    -91   1675       C  
ATOM   3016  CD  ARG A 690     -53.487 -86.437  32.567  1.00113.92           C  
ANISOU 3016  CD  ARG A 690    16543  13713  13025   1593   -113   1803       C  
ATOM   3017  NE  ARG A 690     -52.422 -85.499  32.936  1.00113.69           N  
ANISOU 3017  NE  ARG A 690    16321  14212  12661   1799   -475   1713       N  
ATOM   3018  CZ  ARG A 690     -52.500 -84.172  32.813  1.00110.36           C  
ANISOU 3018  CZ  ARG A 690    15628  14120  12181   1573   -664   1464       C  
ATOM   3019  NH1 ARG A 690     -53.607 -83.597  32.334  1.00106.54           N1+
ANISOU 3019  NH1 ARG A 690    15032  13522  11923   1185   -539   1314       N1+
ATOM   3020  NH2 ARG A 690     -51.463 -83.418  33.178  1.00109.89           N  
ANISOU 3020  NH2 ARG A 690    15394  14501  11858   1743   -976   1359       N  
ATOM   3021  N   MET A 691     -54.175 -86.260  27.124  1.00104.22           N  
ANISOU 3021  N   MET A 691    14515  12221  12860    607   -349    653       N  
ATOM   3022  CA  MET A 691     -55.146 -86.037  26.079  1.00104.27           C  
ANISOU 3022  CA  MET A 691    14353  12181  13081    241   -348    396       C  
ATOM   3023  C   MET A 691     -55.094 -87.092  24.964  1.00106.19           C  
ANISOU 3023  C   MET A 691    14665  12145  13535    187   -287    181       C  
ATOM   3024  O   MET A 691     -56.091 -87.748  24.689  1.00108.21           O  
ANISOU 3024  O   MET A 691    14977  12091  14046    -72   -125     68       O  
ATOM   3025  CB  MET A 691     -54.949 -84.644  25.504  1.00101.09           C  
ANISOU 3025  CB  MET A 691    13651  12208  12551    156   -592    254       C  
ATOM   3026  CG  MET A 691     -55.851 -84.363  24.349  1.00103.89           C  
ANISOU 3026  CG  MET A 691    13822  12589  13060   -142   -639     15       C  
ATOM   3027  SD  MET A 691     -56.209 -82.609  24.246  1.00108.43           S  
ANISOU 3027  SD  MET A 691    14116  13556  13525   -264   -801      0       S  
ATOM   3028  CE  MET A 691     -56.853 -82.338  25.921  1.00109.14           C  
ANISOU 3028  CE  MET A 691    14314  13571  13583   -266   -635    232       C  
ATOM   3029  N   ILE A 692     -53.942 -87.268  24.329  1.00106.50           N  
ANISOU 3029  N   ILE A 692    14689  12292  13484    422   -402     94       N  
ATOM   3030  CA  ILE A 692     -53.869 -88.182  23.196  1.00108.71           C  
ANISOU 3030  CA  ILE A 692    15038  12336  13929    380   -343   -165       C  
ATOM   3031  C   ILE A 692     -54.032 -89.637  23.642  1.00113.58           C  
ANISOU 3031  C   ILE A 692    15988  12395  14772    458    -57    -75       C  
ATOM   3032  O   ILE A 692     -54.034 -90.556  22.823  1.00116.49           O  
ANISOU 3032  O   ILE A 692    16473  12461  15325    413     44   -311       O  
ATOM   3033  CB  ILE A 692     -52.625 -87.929  22.288  1.00107.60           C  
ANISOU 3033  CB  ILE A 692    14772  12478  13632    606   -499   -303       C  
ATOM   3034  CG1 ILE A 692     -51.488 -88.883  22.576  1.00110.13           C  
ANISOU 3034  CG1 ILE A 692    15277  12610  13955   1011   -399   -185       C  
ATOM   3035  CG2 ILE A 692     -52.133 -86.517  22.407  1.00103.51           C  
ANISOU 3035  CG2 ILE A 692    13988  12450  12891    638   -708   -228       C  
ATOM   3036  CD1 ILE A 692     -50.356 -88.679  21.632  1.00110.18           C  
ANISOU 3036  CD1 ILE A 692    15126  12887  13850   1208   -504   -344       C  
ATOM   3037  N   LYS A 693     -54.204 -89.818  24.949  1.00115.57           N  
ANISOU 3037  N   LYS A 693    16412  12497  15002    571     92    266       N  
ATOM   3038  CA  LYS A 693     -54.479 -91.119  25.574  1.00120.68           C  
ANISOU 3038  CA  LYS A 693    17413  12572  15866    646    429    453       C  
ATOM   3039  C   LYS A 693     -55.982 -91.227  25.867  1.00122.38           C  
ANISOU 3039  C   LYS A 693    17635  12532  16331    213    642    435       C  
ATOM   3040  O   LYS A 693     -56.536 -92.331  25.929  1.00126.37           O  
ANISOU 3040  O   LYS A 693    18367  12491  17156     76    956    434       O  
ATOM   3041  CB  LYS A 693     -53.664 -91.243  26.863  1.00121.71           C  
ANISOU 3041  CB  LYS A 693    17741  12746  15754   1103    470    891       C  
ATOM   3042  CG  LYS A 693     -53.481 -92.632  27.418  1.00126.14           C  
ANISOU 3042  CG  LYS A 693    18711  12742  16472   1370    802   1159       C  
ATOM   3043  CD  LYS A 693     -52.371 -92.580  28.446  1.00126.31           C  
ANISOU 3043  CD  LYS A 693    18844  13000  16148   1926    704   1548       C  
ATOM   3044  CE  LYS A 693     -52.731 -93.291  29.730  1.00130.35           C  
ANISOU 3044  CE  LYS A 693    19742  13157  16625   2119   1025   2011       C  
ATOM   3045  NZ  LYS A 693     -52.070 -92.621  30.886  1.00129.45           N1+
ANISOU 3045  NZ  LYS A 693    19611  13538  16033   2501    813   2329       N1+
ATOM   3046  N   LEU A 694     -56.615 -90.064  26.061  1.00119.98           N  
ANISOU 3046  N   LEU A 694    17067  12611  15905      5    494    422       N  
ATOM   3047  CA  LEU A 694     -58.077 -89.921  26.099  1.00121.18           C  
ANISOU 3047  CA  LEU A 694    17083  12658  16299   -431    632    326       C  
ATOM   3048  C   LEU A 694     -58.650 -90.414  24.772  1.00122.61           C  
ANISOU 3048  C   LEU A 694    17128  12681  16775   -768    593   -113       C  
ATOM   3049  O   LEU A 694     -59.213 -91.512  24.715  1.00126.98           O  
ANISOU 3049  O   LEU A 694    17837  12734  17674   -971    867   -201       O  
ATOM   3050  CB  LEU A 694     -58.477 -88.448  26.344  1.00117.51           C  
ANISOU 3050  CB  LEU A 694    16323  12696  15628   -520    428    347       C  
ATOM   3051  CG  LEU A 694     -59.888 -87.913  26.016  1.00117.70           C  
ANISOU 3051  CG  LEU A 694    16048  12812  15860   -934    434    164       C  
ATOM   3052  CD1 LEU A 694     -60.605 -87.479  27.292  1.00118.95           C  
ANISOU 3052  CD1 LEU A 694    16224  12981  15987   -969    652    445       C  
ATOM   3053  CD2 LEU A 694     -59.858 -86.749  25.000  1.00113.84           C  
ANISOU 3053  CD2 LEU A 694    15222  12798  15231   -997     76    -76       C  
ATOM   3054  N   GLY A 695     -58.473 -89.614  23.712  1.00119.70           N  
ANISOU 3054  N   GLY A 695    16487  12734  16257   -820    263   -390       N  
ATOM   3055  CA  GLY A 695     -59.024 -89.901  22.382  1.00121.02           C  
ANISOU 3055  CA  GLY A 695    16493  12894  16595  -1116    148   -839       C  
ATOM   3056  C   GLY A 695     -58.427 -91.137  21.736  1.00124.45           C  
ANISOU 3056  C   GLY A 695    17177  12942  17164  -1037    257  -1057       C  
ATOM   3057  O   GLY A 695     -57.927 -91.066  20.612  1.00124.06           O  
ANISOU 3057  O   GLY A 695    17063  13095  16979   -981     58  -1350       O  
ATOM   3058  N   LEU A 696     -58.508 -92.261  22.455  1.00128.25           N  
ANISOU 3058  N   LEU A 696    17963  12851  17914  -1021    607   -904       N  
ATOM   3059  CA  LEU A 696     -57.866 -93.540  22.110  1.00132.49           C  
ANISOU 3059  CA  LEU A 696    18822  12892  18623   -871    803  -1024       C  
ATOM   3060  C   LEU A 696     -58.281 -94.692  23.049  1.00137.51           C  
ANISOU 3060  C   LEU A 696    19790  12832  19623   -926   1259   -789       C  
ATOM   3061  O   LEU A 696     -58.157 -95.867  22.689  1.00141.94           O  
ANISOU 3061  O   LEU A 696    20611  12844  20476   -949   1494   -969       O  
ATOM   3062  CB  LEU A 696     -56.328 -93.419  22.135  1.00130.85           C  
ANISOU 3062  CB  LEU A 696    18742  12873  18101   -332    694   -837       C  
ATOM   3063  CG  LEU A 696     -55.526 -93.576  20.837  1.00130.49           C  
ANISOU 3063  CG  LEU A 696    18668  12967  17942   -200    531  -1205       C  
ATOM   3064  CD1 LEU A 696     -55.244 -92.226  20.207  1.00125.37           C  
ANISOU 3064  CD1 LEU A 696    17680  13016  16936   -183    168  -1288       C  
ATOM   3065  CD2 LEU A 696     -54.223 -94.306  21.107  1.00131.72           C  
ANISOU 3065  CD2 LEU A 696    19099  12888  18059    306    677  -1009       C  
ATOM   3066  N   GLY A 697     -58.757 -94.349  24.247  1.00137.07           N  
ANISOU 3066  N   GLY A 697    19750  12783  19545   -933   1415   -383       N  
ATOM   3067  CA  GLY A 697     -59.042 -95.333  25.295  1.00141.82           C  
ANISOU 3067  CA  GLY A 697    20707  12765  20411   -903   1889    -32       C  
ATOM   3068  C   GLY A 697     -58.104 -95.156  26.480  1.00141.18           C  
ANISOU 3068  C   GLY A 697    20875  12794  19970   -352   1937    533       C  
ATOM   3069  O   GLY A 697     -58.194 -94.185  27.243  1.00138.06           O  
ANISOU 3069  O   GLY A 697    20349  12834  19271   -268   1814    787       O  
TER   
ATOM   3070  N   LYS B 294      15.648 -61.562  52.380  1.00 88.83           N  
ANISOU 3070  N   LYS B 294     7332  12219  14201  -1369  -2104   -151       N  
ATOM   3071  CA  LYS B 294      14.782 -60.395  52.678  1.00 88.51           C  
ANISOU 3071  CA  LYS B 294     7600  11751  14277  -1620  -2177   -391       C  
ATOM   3072  C   LYS B 294      13.385 -60.515  52.059  1.00 83.45           C  
ANISOU 3072  C   LYS B 294     7473  10774  13459  -1492  -1854   -160       C  
ATOM   3073  O   LYS B 294      12.407 -60.593  52.810  1.00 82.38           O  
ANISOU 3073  O   LYS B 294     7699  10592  13009  -1298  -1937   -335       O  
ATOM   3074  CB  LYS B 294      15.460 -59.082  52.305  1.00 92.97           C  
ANISOU 3074  CB  LYS B 294     7833  12033  15457  -2151  -2218   -517       C  
ATOM   3075  CG  LYS B 294      16.629 -58.712  53.206  1.00 99.64           C  
ANISOU 3075  CG  LYS B 294     8181  13171  16505  -2348  -2653   -924       C  
ATOM   3076  CD  LYS B 294      17.052 -57.251  52.994  1.00104.12           C  
ANISOU 3076  CD  LYS B 294     8521  13301  17739  -2950  -2712  -1134       C  
ATOM   3077  CE  LYS B 294      18.387 -56.951  53.651  1.00110.41           C  
ANISOU 3077  CE  LYS B 294     8678  14439  18832  -3229  -3112  -1515       C  
ATOM   3078  NZ  LYS B 294      18.904 -55.605  53.264  1.00115.81           N1+
ANISOU 3078  NZ  LYS B 294     9083  14649  20271  -3901  -3091  -1647       N1+
ATOM   3079  N   PRO B 295      13.262 -60.565  50.709  1.00 81.32           N  
ANISOU 3079  N   PRO B 295     7220  10332  13345  -1587  -1488    220       N  
ATOM   3080  CA  PRO B 295      11.887 -60.538  50.191  1.00 77.12           C  
ANISOU 3080  CA  PRO B 295     7139   9501  12659  -1481  -1277    378       C  
ATOM   3081  C   PRO B 295      11.099 -61.805  50.582  1.00 73.41           C  
ANISOU 3081  C   PRO B 295     6959   9245  11689  -1079  -1220    413       C  
ATOM   3082  O   PRO B 295      11.669 -62.890  50.719  1.00 73.10           O  
ANISOU 3082  O   PRO B 295     6807   9521  11444   -862  -1209    499       O  
ATOM   3083  CB  PRO B 295      12.083 -60.441  48.672  1.00 76.53           C  
ANISOU 3083  CB  PRO B 295     6996   9322  12759  -1649   -937    787       C  
ATOM   3084  CG  PRO B 295      13.356 -61.138  48.415  1.00 78.17           C  
ANISOU 3084  CG  PRO B 295     6791   9919  12988  -1638   -854    876       C  
ATOM   3085  CD  PRO B 295      14.224 -60.943  49.655  1.00 82.48           C  
ANISOU 3085  CD  PRO B 295     7014  10663  13658  -1681  -1232    520       C  
ATOM   3086  N   ILE B 296       9.795 -61.655  50.760  1.00 71.53           N  
ANISOU 3086  N   ILE B 296     7071   8806  11300   -982  -1176    353       N  
ATOM   3087  CA  ILE B 296       8.969 -62.696  51.363  1.00 69.33           C  
ANISOU 3087  CA  ILE B 296     7056   8695  10589   -684  -1128    338       C  
ATOM   3088  C   ILE B 296       9.058 -64.021  50.626  1.00 67.52           C  
ANISOU 3088  C   ILE B 296     6862   8611  10179   -512   -900    636       C  
ATOM   3089  O   ILE B 296       9.049 -65.068  51.262  1.00 67.83           O  
ANISOU 3089  O   ILE B 296     7003   8837   9930   -280   -915    661       O  
ATOM   3090  CB  ILE B 296       7.513 -62.253  51.465  1.00 67.42           C  
ANISOU 3090  CB  ILE B 296     7095   8224  10296   -648  -1054    235       C  
ATOM   3091  CG1 ILE B 296       6.783 -63.087  52.508  1.00 66.36           C  
ANISOU 3091  CG1 ILE B 296     7172   8305   9734   -418  -1036    126       C  
ATOM   3092  CG2 ILE B 296       6.845 -62.325  50.107  1.00 65.25           C  
ANISOU 3092  CG2 ILE B 296     6908   7766  10119   -679   -821    521       C  
ATOM   3093  CD1 ILE B 296       5.259 -62.960  52.420  1.00 65.15           C  
ANISOU 3093  CD1 ILE B 296     7224   8006   9523   -359   -867     77       C  
ATOM   3094  N   TRP B 297       9.160 -63.983  49.298  1.00 66.97           N  
ANISOU 3094  N   TRP B 297     6734   8447  10264   -617   -686    861       N  
ATOM   3095  CA  TRP B 297       9.278 -65.217  48.511  1.00 65.73           C  
ANISOU 3095  CA  TRP B 297     6613   8415   9944   -454   -457   1057       C  
ATOM   3096  C   TRP B 297      10.640 -65.928  48.686  1.00 68.44           C  
ANISOU 3096  C   TRP B 297     6668   9018  10317   -315   -488   1082       C  
ATOM   3097  O   TRP B 297      10.791 -67.073  48.237  1.00 68.68           O  
ANISOU 3097  O   TRP B 297     6742   9124  10228   -103   -317   1182       O  
ATOM   3098  CB  TRP B 297       8.970 -64.990  47.018  1.00 64.45           C  
ANISOU 3098  CB  TRP B 297     6492   8158   9837   -586   -220   1254       C  
ATOM   3099  CG  TRP B 297       9.898 -64.013  46.360  1.00 66.71           C  
ANISOU 3099  CG  TRP B 297     6508   8437  10401   -843   -178   1374       C  
ATOM   3100  CD1 TRP B 297      11.114 -64.278  45.811  1.00 67.59           C  
ANISOU 3100  CD1 TRP B 297     6309   8771  10599   -884    -29   1471       C  
ATOM   3101  CD2 TRP B 297       9.681 -62.611  46.197  1.00 67.85           C  
ANISOU 3101  CD2 TRP B 297     6656   8312  10812  -1107   -258   1424       C  
ATOM   3102  NE1 TRP B 297      11.671 -63.130  45.321  1.00 69.91           N  
ANISOU 3102  NE1 TRP B 297     6400   8980  11181  -1212     14   1602       N  
ATOM   3103  CE2 TRP B 297      10.812 -62.089  45.538  1.00 70.42           C  
ANISOU 3103  CE2 TRP B 297     6683   8698  11375  -1356   -136   1594       C  
ATOM   3104  CE3 TRP B 297       8.625 -61.746  46.528  1.00 67.89           C  
ANISOU 3104  CE3 TRP B 297     6879   8006  10910  -1142   -402   1344       C  
ATOM   3105  CZ2 TRP B 297      10.932 -60.735  45.201  1.00 74.47           C  
ANISOU 3105  CZ2 TRP B 297     7152   8912  12229  -1683   -155   1733       C  
ATOM   3106  CZ3 TRP B 297       8.745 -60.393  46.202  1.00 72.40           C  
ANISOU 3106  CZ3 TRP B 297     7413   8256  11838  -1401   -453   1447       C  
ATOM   3107  CH2 TRP B 297       9.901 -59.901  45.545  1.00 74.49           C  
ANISOU 3107  CH2 TRP B 297     7420   8531  12349  -1690   -331   1663       C  
ATOM   3108  N   THR B 298      11.622 -65.273  49.314  1.00 71.37           N  
ANISOU 3108  N   THR B 298     6722   9515  10877   -419   -716    960       N  
ATOM   3109  CA  THR B 298      12.890 -65.954  49.595  1.00 74.30           C  
ANISOU 3109  CA  THR B 298     6752  10187  11292   -233   -807    963       C  
ATOM   3110  C   THR B 298      12.944 -66.538  50.997  1.00 75.70           C  
ANISOU 3110  C   THR B 298     7018  10526  11218     41  -1113    864       C  
ATOM   3111  O   THR B 298      13.879 -67.235  51.331  1.00 78.52           O  
ANISOU 3111  O   THR B 298     7134  11128  11571    289  -1241    900       O  
ATOM   3112  CB  THR B 298      14.161 -65.101  49.312  1.00 78.00           C  
ANISOU 3112  CB  THR B 298     6691  10804  12139   -501   -865    913       C  
ATOM   3113  OG1 THR B 298      14.188 -63.965  50.171  1.00 79.61           O  
ANISOU 3113  OG1 THR B 298     6826  10932  12491   -754  -1177    676       O  
ATOM   3114  CG2 THR B 298      14.202 -64.652  47.868  1.00 77.82           C  
ANISOU 3114  CG2 THR B 298     6598  10674  12294   -756   -501   1110       C  
ATOM   3115  N   ARG B 299      11.934 -66.276  51.811  1.00 74.83           N  
ANISOU 3115  N   ARG B 299     7249  10307  10875     26  -1220    756       N  
ATOM   3116  CA  ARG B 299      11.907 -66.844  53.141  1.00 77.52           C  
ANISOU 3116  CA  ARG B 299     7736  10847  10869    281  -1469    713       C  
ATOM   3117  C   ARG B 299      11.350 -68.266  53.181  1.00 76.29           C  
ANISOU 3117  C   ARG B 299     7918  10624  10444    588  -1283    974       C  
ATOM   3118  O   ARG B 299      10.623 -68.722  52.276  1.00 73.60           O  
ANISOU 3118  O   ARG B 299     7774  10040  10151    557   -963   1095       O  
ATOM   3119  CB  ARG B 299      11.127 -65.941  54.064  1.00 78.16           C  
ANISOU 3119  CB  ARG B 299     8017  10900  10779    135  -1625    448       C  
ATOM   3120  CG  ARG B 299      11.921 -64.758  54.536  1.00 85.77           C  
ANISOU 3120  CG  ARG B 299     8658  11976  11951    -88  -1952    121       C  
ATOM   3121  CD  ARG B 299      11.007 -63.584  54.809  1.00 92.12           C  
ANISOU 3121  CD  ARG B 299     9650  12538  12811   -316  -1958   -177       C  
ATOM   3122  NE  ARG B 299      10.092 -63.815  55.931  1.00 96.93           N  
ANISOU 3122  NE  ARG B 299    10610  13279  12939   -140  -1999   -319       N  
ATOM   3123  CZ  ARG B 299       9.097 -62.987  56.249  1.00 99.80           C  
ANISOU 3123  CZ  ARG B 299    11171  13462  13284   -237  -1942   -597       C  
ATOM   3124  NH1 ARG B 299       8.890 -61.878  55.532  1.00 99.54           N1+
ANISOU 3124  NH1 ARG B 299    11053  13046  13721   -483  -1886   -731       N1+
ATOM   3125  NH2 ARG B 299       8.306 -63.270  57.278  1.00101.68           N  
ANISOU 3125  NH2 ARG B 299    11691  13899  13040    -70  -1919   -722       N  
ATOM   3126  N   ASN B 300      11.704 -68.976  54.238  1.00 79.06           N  
ANISOU 3126  N   ASN B 300     8343  11183  10512    877  -1506   1066       N  
ATOM   3127  CA  ASN B 300      11.250 -70.330  54.406  1.00 79.07           C  
ANISOU 3127  CA  ASN B 300     8690  11055  10296   1157  -1348   1359       C  
ATOM   3128  C   ASN B 300       9.781 -70.348  54.810  1.00 77.08           C  
ANISOU 3128  C   ASN B 300     8869  10647   9769   1023  -1151   1372       C  
ATOM   3129  O   ASN B 300       9.423 -69.721  55.792  1.00 78.17           O  
ANISOU 3129  O   ASN B 300     9098  10972   9630    952  -1305   1220       O  
ATOM   3130  CB  ASN B 300      12.110 -70.999  55.467  1.00 83.95           C  
ANISOU 3130  CB  ASN B 300     9266  11948  10680   1527  -1682   1521       C  
ATOM   3131  CG  ASN B 300      11.835 -72.466  55.592  1.00 85.00           C  
ANISOU 3131  CG  ASN B 300     9753  11862  10680   1851  -1529   1897       C  
ATOM   3132  OD1 ASN B 300      10.753 -72.861  56.010  1.00 84.85           O  
ANISOU 3132  OD1 ASN B 300    10166  11679  10394   1792  -1343   2041       O  
ATOM   3133  ND2 ASN B 300      12.817 -73.292  55.239  1.00 87.33           N  
ANISOU 3133  ND2 ASN B 300     9852  12130  11199   2197  -1588   2056       N  
ATOM   3134  N   PRO B 301       8.924 -71.073  54.060  1.00 74.98           N  
ANISOU 3134  N   PRO B 301     8841  10068   9579    981   -806   1510       N  
ATOM   3135  CA  PRO B 301       7.475 -71.090  54.315  1.00 73.83           C  
ANISOU 3135  CA  PRO B 301     9008   9792   9250    810   -582   1502       C  
ATOM   3136  C   PRO B 301       7.131 -71.297  55.758  1.00 77.36           C  
ANISOU 3136  C   PRO B 301     9699  10440   9250    908   -666   1598       C  
ATOM   3137  O   PRO B 301       6.182 -70.707  56.240  1.00 77.48           O  
ANISOU 3137  O   PRO B 301     9819  10535   9085    743   -573   1439       O  
ATOM   3138  CB  PRO B 301       6.991 -72.290  53.516  1.00 72.58           C  
ANISOU 3138  CB  PRO B 301     9047   9302   9226    840   -285   1694       C  
ATOM   3139  CG  PRO B 301       7.885 -72.299  52.362  1.00 71.94           C  
ANISOU 3139  CG  PRO B 301     8705   9166   9459    894   -284   1635       C  
ATOM   3140  CD  PRO B 301       9.254 -71.920  52.908  1.00 74.41           C  
ANISOU 3140  CD  PRO B 301     8723   9769   9779   1082   -603   1624       C  
ATOM   3141  N   ASP B 302       7.904 -72.123  56.445  1.00 81.75           N  
ANISOU 3141  N   ASP B 302    10342  11107   9609   1204   -838   1865       N  
ATOM   3142  CA  ASP B 302       7.624 -72.426  57.821  1.00 86.27           C  
ANISOU 3142  CA  ASP B 302    11201  11916   9660   1323   -914   2044       C  
ATOM   3143  C   ASP B 302       7.754 -71.186  58.663  1.00 88.10           C  
ANISOU 3143  C   ASP B 302    11297  12561   9616   1240  -1184   1687       C  
ATOM   3144  O   ASP B 302       7.284 -71.167  59.788  1.00 91.86           O  
ANISOU 3144  O   ASP B 302    12015  13306   9581   1271  -1192   1716       O  
ATOM   3145  CB  ASP B 302       8.578 -73.481  58.347  1.00 91.14           C  
ANISOU 3145  CB  ASP B 302    11914  12582  10129   1718  -1131   2437       C  
ATOM   3146  CG  ASP B 302       8.223 -73.924  59.744  1.00 97.78           C  
ANISOU 3146  CG  ASP B 302    13134  13666  10350   1851  -1177   2740       C  
ATOM   3147  OD1 ASP B 302       7.090 -74.431  59.899  1.00 99.66           O  
ANISOU 3147  OD1 ASP B 302    13711  13705  10450   1686   -793   2936       O  
ATOM   3148  OD2 ASP B 302       9.054 -73.762  60.683  1.00104.31           O1-
ANISOU 3148  OD2 ASP B 302    13908  14916  10805   2099  -1591   2785       O1-
ATOM   3149  N   ASP B 303       8.392 -70.148  58.131  1.00 87.07           N  
ANISOU 3149  N   ASP B 303    10792  12475   9815   1119  -1386   1338       N  
ATOM   3150  CA  ASP B 303       8.657 -68.934  58.908  1.00 89.88           C  
ANISOU 3150  CA  ASP B 303    10997  13157   9996   1024  -1693    924       C  
ATOM   3151  C   ASP B 303       7.584 -67.895  58.700  1.00 87.09           C  
ANISOU 3151  C   ASP B 303    10673  12656   9759    744  -1484    570       C  
ATOM   3152  O   ASP B 303       7.060 -67.330  59.652  1.00 89.97           O  
ANISOU 3152  O   ASP B 303    11169  13247   9767    714  -1520    302       O  
ATOM   3153  CB  ASP B 303      10.013 -68.343  58.547  1.00 91.41           C  
ANISOU 3153  CB  ASP B 303    10738  13454  10538   1010  -2050    735       C  
ATOM   3154  CG  ASP B 303      11.162 -69.174  59.067  1.00 97.89           C  
ANISOU 3154  CG  ASP B 303    11446  14561  11183   1353  -2380    989       C  
ATOM   3155  OD1 ASP B 303      11.088 -69.624  60.244  1.00103.68           O  
ANISOU 3155  OD1 ASP B 303    12440  15605  11349   1572  -2556   1132       O  
ATOM   3156  OD2 ASP B 303      12.140 -69.364  58.300  1.00100.10           O1-
ANISOU 3156  OD2 ASP B 303    11365  14786  11879   1423  -2459   1054       O1-
ATOM   3157  N   ILE B 304       7.260 -67.655  57.443  1.00 82.68           N  
ANISOU 3157  N   ILE B 304     9992  11737   9686    573  -1269    564       N  
ATOM   3158  CA  ILE B 304       6.229 -66.713  57.075  1.00 79.96           C  
ANISOU 3158  CA  ILE B 304     9650  11196   9532    364  -1089    292       C  
ATOM   3159  C   ILE B 304       4.843 -67.161  57.591  1.00 79.75           C  
ANISOU 3159  C   ILE B 304     9907  11206   9186    376   -767    346       C  
ATOM   3160  O   ILE B 304       4.496 -68.320  57.451  1.00 79.19           O  
ANISOU 3160  O   ILE B 304    10010  11069   9009    431   -546    696       O  
ATOM   3161  CB  ILE B 304       6.275 -66.407  55.534  1.00 76.27           C  
ANISOU 3161  CB  ILE B 304     8995  10380   9605    207   -970    355       C  
ATOM   3162  CG1 ILE B 304       4.886 -66.306  54.994  1.00 74.75           C  
ANISOU 3162  CG1 ILE B 304     8920   9976   9506    111   -676    342       C  
ATOM   3163  CG2 ILE B 304       7.058 -67.427  54.698  1.00 73.22           C  
ANISOU 3163  CG2 ILE B 304     8531   9927   9361    302   -916    684       C  
ATOM   3164  CD1 ILE B 304       4.377 -64.943  55.079  1.00 79.67           C  
ANISOU 3164  CD1 ILE B 304     9465  10494  10311      4   -739     -5       C  
ATOM   3165  N   THR B 305       4.097 -66.246  58.227  1.00 81.52           N  
ANISOU 3165  N   THR B 305    10158  11532   9282    320   -733    -22       N  
ATOM   3166  CA  THR B 305       2.729 -66.501  58.780  1.00 82.61           C  
ANISOU 3166  CA  THR B 305    10477  11779   9130    314   -382    -46       C  
ATOM   3167  C   THR B 305       1.624 -66.160  57.767  1.00 80.12           C  
ANISOU 3167  C   THR B 305    10038  11158   9244    187   -132   -117       C  
ATOM   3168  O   THR B 305       1.897 -65.548  56.717  1.00 77.50           O  
ANISOU 3168  O   THR B 305     9529  10539   9378    116   -256   -171       O  
ATOM   3169  CB  THR B 305       2.406 -65.662  60.054  1.00 86.67           C  
ANISOU 3169  CB  THR B 305    11057  12631   9243    371   -431   -491       C  
ATOM   3170  OG1 THR B 305       2.001 -64.340  59.673  1.00 85.50           O  
ANISOU 3170  OG1 THR B 305    10724  12257   9504    302   -474   -951       O  
ATOM   3171  CG2 THR B 305       3.586 -65.573  61.000  1.00 90.70           C  
ANISOU 3171  CG2 THR B 305    11617  13482   9363    485   -822   -587       C  
ATOM   3172  N   ASN B 306       0.372 -66.519  58.082  1.00 81.32           N  
ANISOU 3172  N   ASN B 306    10259  11404   9234    154    215   -107       N  
ATOM   3173  CA  ASN B 306      -0.728 -66.245  57.147  1.00 78.95           C  
ANISOU 3173  CA  ASN B 306     9783  10878   9336     59    407   -182       C  
ATOM   3174  C   ASN B 306      -1.034 -64.760  56.997  1.00 79.57           C  
ANISOU 3174  C   ASN B 306     9676  10837   9718    112    274   -620       C  
ATOM   3175  O   ASN B 306      -1.346 -64.303  55.894  1.00 77.07           O  
ANISOU 3175  O   ASN B 306     9200  10235   9846     78    222   -614       O  
ATOM   3176  CB  ASN B 306      -1.989 -67.016  57.494  1.00 80.29           C  
ANISOU 3176  CB  ASN B 306     9983  11197   9325    -22    817    -77       C  
ATOM   3177  CG  ASN B 306      -2.955 -67.095  56.319  1.00 79.06           C  
ANISOU 3177  CG  ASN B 306     9611  10819   9609   -140    946    -59       C  
ATOM   3178  OD1 ASN B 306      -2.625 -67.621  55.242  1.00 76.64           O  
ANISOU 3178  OD1 ASN B 306     9300  10270   9547   -218    858    166       O  
ATOM   3179  ND2 ASN B 306      -4.151 -66.555  56.512  1.00 81.73           N  
ANISOU 3179  ND2 ASN B 306     9742  11276  10035   -131   1142   -332       N  
ATOM   3180  N   GLU B 307      -0.946 -64.024  58.114  1.00 83.49           N  
ANISOU 3180  N   GLU B 307    10218  11544   9958    211    208  -1000       N  
ATOM   3181  CA  GLU B 307      -1.070 -62.570  58.116  1.00 85.08           C  
ANISOU 3181  CA  GLU B 307    10290  11555  10479    284     46  -1476       C  
ATOM   3182  C   GLU B 307       0.010 -62.031  57.179  1.00 82.51           C  
ANISOU 3182  C   GLU B 307     9895  10862  10593    195   -291  -1374       C  
ATOM   3183  O   GLU B 307      -0.303 -61.322  56.227  1.00 81.62           O  
ANISOU 3183  O   GLU B 307     9655  10387  10967    181   -341  -1382       O  
ATOM   3184  CB  GLU B 307      -0.983 -62.013  59.543  1.00 90.39           C  
ANISOU 3184  CB  GLU B 307    11067  12549  10727    393     13  -1952       C  
ATOM   3185  CG  GLU B 307      -0.898 -60.476  59.711  1.00 95.84           C  
ANISOU 3185  CG  GLU B 307    11673  12981  11761    469   -206  -2546       C  
ATOM   3186  CD  GLU B 307       0.032 -60.039  60.903  1.00104.85           C  
ANISOU 3186  CD  GLU B 307    12947  14391  12499    484   -480  -2968       C  
ATOM   3187  OE1 GLU B 307       1.195 -60.517  60.989  1.00105.81           O  
ANISOU 3187  OE1 GLU B 307    13122  14640  12438    389   -745  -2733       O  
ATOM   3188  OE2 GLU B 307      -0.382 -59.210  61.754  1.00109.78           O1-
ANISOU 3188  OE2 GLU B 307    13600  15121  12989    608   -452  -3576       O1-
ATOM   3189  N   GLU B 308       1.265 -62.431  57.378  1.00 81.88           N  
ANISOU 3189  N   GLU B 308     9875  10890  10343    137   -505  -1219       N  
ATOM   3190  CA  GLU B 308       2.339 -61.964  56.490  1.00 79.89           C  
ANISOU 3190  CA  GLU B 308     9497  10344  10510     14   -765  -1108       C  
ATOM   3191  C   GLU B 308       2.042 -62.179  55.004  1.00 75.28           C  
ANISOU 3191  C   GLU B 308     8834   9471  10297    -56   -650   -748       C  
ATOM   3192  O   GLU B 308       2.162 -61.254  54.222  1.00 75.24           O  
ANISOU 3192  O   GLU B 308     8732   9132  10723   -131   -757   -770       O  
ATOM   3193  CB  GLU B 308       3.694 -62.538  56.889  1.00 80.68           C  
ANISOU 3193  CB  GLU B 308     9594  10681  10380     -6   -987   -969       C  
ATOM   3194  CG  GLU B 308       4.449 -61.683  57.900  1.00 87.44           C  
ANISOU 3194  CG  GLU B 308    10407  11677  11137    -28  -1309  -1418       C  
ATOM   3195  CD  GLU B 308       5.400 -62.484  58.809  1.00 93.09           C  
ANISOU 3195  CD  GLU B 308    11162  12849  11356     63  -1518  -1326       C  
ATOM   3196  OE1 GLU B 308       5.357 -63.738  58.801  1.00 92.11           O  
ANISOU 3196  OE1 GLU B 308    11158  12903  10937    183  -1369   -897       O  
ATOM   3197  OE2 GLU B 308       6.191 -61.850  59.553  1.00 99.02           O1-
ANISOU 3197  OE2 GLU B 308    11827  13770  12023     24  -1860  -1695       O1-
ATOM   3198  N   TYR B 309       1.620 -63.387  54.631  1.00 72.61           N  
ANISOU 3198  N   TYR B 309     8559   9252   9776    -39   -435   -425       N  
ATOM   3199  CA  TYR B 309       1.307 -63.727  53.226  1.00 68.91           C  
ANISOU 3199  CA  TYR B 309     8033   8588   9560   -105   -340   -133       C  
ATOM   3200  C   TYR B 309       0.182 -62.852  52.722  1.00 68.99           C  
ANISOU 3200  C   TYR B 309     7952   8402   9859    -72   -306   -272       C  
ATOM   3201  O   TYR B 309       0.349 -62.109  51.769  1.00 69.10           O  
ANISOU 3201  O   TYR B 309     7896   8153  10204   -112   -428   -182       O  
ATOM   3202  CB  TYR B 309       0.876 -65.184  53.072  1.00 66.96           C  
ANISOU 3202  CB  TYR B 309     7885   8477   9079   -108   -112    122       C  
ATOM   3203  CG  TYR B 309       1.976 -66.235  52.931  1.00 65.83           C  
ANISOU 3203  CG  TYR B 309     7818   8390   8804    -98   -137    391       C  
ATOM   3204  CD1 TYR B 309       2.965 -66.149  51.950  1.00 62.58           C  
ANISOU 3204  CD1 TYR B 309     7305   7867   8603   -136   -244    530       C  
ATOM   3205  CD2 TYR B 309       1.982 -67.354  53.764  1.00 67.05           C  
ANISOU 3205  CD2 TYR B 309     8144   8703   8628    -31    -20    532       C  
ATOM   3206  CE1 TYR B 309       3.926 -67.140  51.820  1.00 61.21           C  
ANISOU 3206  CE1 TYR B 309     7157   7755   8345    -68   -241    732       C  
ATOM   3207  CE2 TYR B 309       2.931 -68.335  53.641  1.00 65.24           C  
ANISOU 3207  CE2 TYR B 309     7985   8471   8331     46    -53    782       C  
ATOM   3208  CZ  TYR B 309       3.892 -68.230  52.673  1.00 64.32           C  
ANISOU 3208  CZ  TYR B 309     7724   8255   8456     47   -165    849       C  
ATOM   3209  OH  TYR B 309       4.830 -69.240  52.612  1.00 68.05           O  
ANISOU 3209  OH  TYR B 309     8233   8739   8883    187   -183   1058       O  
ATOM   3210  N   GLY B 310      -0.966 -62.944  53.380  1.00 69.98           N  
ANISOU 3210  N   GLY B 310     8064   8671   9852     14   -132   -466       N  
ATOM   3211  CA  GLY B 310      -2.099 -62.086  53.088  1.00 70.53           C  
ANISOU 3211  CA  GLY B 310     7989   8598  10210    122   -111   -658       C  
ATOM   3212  C   GLY B 310      -1.699 -60.659  52.805  1.00 71.72           C  
ANISOU 3212  C   GLY B 310     8108   8383  10756    174   -356   -806       C  
ATOM   3213  O   GLY B 310      -2.131 -60.111  51.798  1.00 71.52           O  
ANISOU 3213  O   GLY B 310     8004   8106  11065    221   -441   -668       O  
ATOM   3214  N   GLU B 311      -0.866 -60.066  53.670  1.00 73.47           N  
ANISOU 3214  N   GLU B 311     8403   8564  10946    154   -490  -1071       N  
ATOM   3215  CA  GLU B 311      -0.439 -58.670  53.476  1.00 76.11           C  
ANISOU 3215  CA  GLU B 311     8722   8461  11732    146   -719  -1249       C  
ATOM   3216  C   GLU B 311       0.387 -58.556  52.206  1.00 73.17           C  
ANISOU 3216  C   GLU B 311     8340   7835  11626    -32   -841   -813       C  
ATOM   3217  O   GLU B 311       0.155 -57.671  51.379  1.00 74.54           O  
ANISOU 3217  O   GLU B 311     8497   7614  12210    -12   -933   -685       O  
ATOM   3218  CB  GLU B 311       0.331 -58.078  54.670  1.00 79.66           C  
ANISOU 3218  CB  GLU B 311     9231   8931  12102    106   -870  -1696       C  
ATOM   3219  CG  GLU B 311      -0.444 -58.005  56.003  1.00 87.82           C  
ANISOU 3219  CG  GLU B 311    10303  10252  12811    298   -736  -2204       C  
ATOM   3220  CD  GLU B 311      -1.692 -57.054  56.021  1.00 96.88           C  
ANISOU 3220  CD  GLU B 311    11368  11136  14304    548   -647  -2552       C  
ATOM   3221  OE1 GLU B 311      -1.513 -55.810  56.152  1.00102.88           O  
ANISOU 3221  OE1 GLU B 311    12148  11456  15485    597   -830  -2914       O  
ATOM   3222  OE2 GLU B 311      -2.850 -57.560  55.963  1.00 96.99           O1-
ANISOU 3222  OE2 GLU B 311    11276  11379  14194    699   -391  -2497       O1-
ATOM   3223  N   PHE B 312       1.338 -59.461  52.027  1.00 69.44           N  
ANISOU 3223  N   PHE B 312     7877   7596  10911   -182   -824   -560       N  
ATOM   3224  CA  PHE B 312       2.100 -59.417  50.801  1.00 66.97           C  
ANISOU 3224  CA  PHE B 312     7526   7124  10793   -346   -865   -162       C  
ATOM   3225  C   PHE B 312       1.127 -59.464  49.637  1.00 65.42           C  
ANISOU 3225  C   PHE B 312     7339   6831  10683   -261   -790    116       C  
ATOM   3226  O   PHE B 312       1.209 -58.645  48.726  1.00 67.33           O  
ANISOU 3226  O   PHE B 312     7587   6763  11229   -310   -875    342       O  
ATOM   3227  CB  PHE B 312       3.145 -60.527  50.695  1.00 64.12           C  
ANISOU 3227  CB  PHE B 312     7134   7068  10158   -447   -812     49       C  
ATOM   3228  CG  PHE B 312       3.852 -60.538  49.393  1.00 61.51           C  
ANISOU 3228  CG  PHE B 312     6741   6652   9978   -595   -777    427       C  
ATOM   3229  CD1 PHE B 312       4.644 -59.458  49.012  1.00 62.76           C  
ANISOU 3229  CD1 PHE B 312     6815   6524  10507   -792   -883    498       C  
ATOM   3230  CD2 PHE B 312       3.695 -61.602  48.517  1.00 59.74           C  
ANISOU 3230  CD2 PHE B 312     6549   6622   9528   -560   -613    699       C  
ATOM   3231  CE1 PHE B 312       5.313 -59.440  47.779  1.00 63.15           C  
ANISOU 3231  CE1 PHE B 312     6800   6542  10650   -955   -786    889       C  
ATOM   3232  CE2 PHE B 312       4.347 -61.610  47.269  1.00 60.89           C  
ANISOU 3232  CE2 PHE B 312     6646   6756   9734   -684   -539   1022       C  
ATOM   3233  CZ  PHE B 312       5.173 -60.517  46.905  1.00 63.43           C  
ANISOU 3233  CZ  PHE B 312     6871   6850  10378   -882   -607   1143       C  
ATOM   3234  N   TYR B 313       0.183 -60.392  49.688  1.00 62.70           N  
ANISOU 3234  N   TYR B 313     6994   6755  10074   -147   -645    108       N  
ATOM   3235  CA  TYR B 313      -0.767 -60.556  48.599  1.00 61.55           C  
ANISOU 3235  CA  TYR B 313     6810   6607   9967    -76   -621    323       C  
ATOM   3236  C   TYR B 313      -1.557 -59.276  48.278  1.00 64.20           C  
ANISOU 3236  C   TYR B 313     7096   6613  10682     88   -771    285       C  
ATOM   3237  O   TYR B 313      -1.555 -58.815  47.135  1.00 64.69           O  
ANISOU 3237  O   TYR B 313     7185   6498  10895     86   -882    614       O  
ATOM   3238  CB  TYR B 313      -1.687 -61.719  48.880  1.00 59.70           C  
ANISOU 3238  CB  TYR B 313     6532   6693   9455    -32   -446    238       C  
ATOM   3239  CG  TYR B 313      -2.872 -61.771  47.973  1.00 61.30           C  
ANISOU 3239  CG  TYR B 313     6619   6937   9734     51   -474    326       C  
ATOM   3240  CD1 TYR B 313      -2.814 -62.438  46.739  1.00 61.29           C  
ANISOU 3240  CD1 TYR B 313     6644   7044   9598    -39   -493    596       C  
ATOM   3241  CD2 TYR B 313      -4.065 -61.192  48.345  1.00 63.63           C  
ANISOU 3241  CD2 TYR B 313     6747   7211  10215    241   -492     96       C  
ATOM   3242  CE1 TYR B 313      -3.917 -62.507  45.899  1.00 60.93           C  
ANISOU 3242  CE1 TYR B 313     6467   7102   9580     34   -584    643       C  
ATOM   3243  CE2 TYR B 313      -5.160 -61.244  47.503  1.00 66.17           C  
ANISOU 3243  CE2 TYR B 313     6894   7623  10625    339   -573    168       C  
ATOM   3244  CZ  TYR B 313      -5.078 -61.896  46.288  1.00 64.25           C  
ANISOU 3244  CZ  TYR B 313     6685   7504  10221    224   -644    445       C  
ATOM   3245  OH  TYR B 313      -6.192 -61.916  45.486  1.00 67.69           O  
ANISOU 3245  OH  TYR B 313     6920   8083  10716    328   -787    475       O  
ATOM   3246  N   LYS B 314      -2.200 -58.688  49.283  1.00 66.29           N  
ANISOU 3246  N   LYS B 314     7304   6793  11089    257   -771   -104       N  
ATOM   3247  CA  LYS B 314      -3.030 -57.505  49.053  1.00 69.82           C  
ANISOU 3247  CA  LYS B 314     7686   6888  11952    495   -911   -187       C  
ATOM   3248  C   LYS B 314      -2.184 -56.470  48.360  1.00 72.06           C  
ANISOU 3248  C   LYS B 314     8101   6690  12587    397  -1095     86       C  
ATOM   3249  O   LYS B 314      -2.618 -55.834  47.421  1.00 74.36           O  
ANISOU 3249  O   LYS B 314     8406   6715  13131    523  -1234    381       O  
ATOM   3250  CB  LYS B 314      -3.617 -56.931  50.352  1.00 72.60           C  
ANISOU 3250  CB  LYS B 314     7968   7190  12424    698   -854   -742       C  
ATOM   3251  CG  LYS B 314      -4.470 -57.891  51.156  1.00 71.66           C  
ANISOU 3251  CG  LYS B 314     7712   7570  11946    763   -600   -998       C  
ATOM   3252  CD  LYS B 314      -5.686 -57.244  51.774  1.00 77.10           C  
ANISOU 3252  CD  LYS B 314     8202   8243  12846   1084   -524  -1423       C  
ATOM   3253  CE  LYS B 314      -5.365 -56.306  52.935  1.00 83.43           C  
ANISOU 3253  CE  LYS B 314     9097   8839  13761   1192   -530  -1946       C  
ATOM   3254  NZ  LYS B 314      -4.693 -56.977  54.094  1.00 83.26           N1+
ANISOU 3254  NZ  LYS B 314     9210   9198  13224   1006   -375  -2166       N1+
ATOM   3255  N   SER B 315      -0.957 -56.337  48.838  1.00 72.72           N  
ANISOU 3255  N   SER B 315     8267   6686  12674    157  -1098     10       N  
ATOM   3256  CA  SER B 315       0.046 -55.412  48.319  1.00 75.86           C  
ANISOU 3256  CA  SER B 315     8755   6638  13427    -50  -1220    249       C  
ATOM   3257  C   SER B 315       0.495 -55.722  46.869  1.00 74.80           C  
ANISOU 3257  C   SER B 315     8666   6569  13183   -208  -1187    868       C  
ATOM   3258  O   SER B 315       0.813 -54.830  46.102  1.00 77.87           O  
ANISOU 3258  O   SER B 315     9144   6554  13888   -298  -1267   1215       O  
ATOM   3259  CB  SER B 315       1.230 -55.417  49.289  1.00 75.92           C  
ANISOU 3259  CB  SER B 315     8747   6693  13405   -293  -1231    -55       C  
ATOM   3260  OG  SER B 315       2.347 -54.743  48.764  1.00 79.92           O  
ANISOU 3260  OG  SER B 315     9268   6866  14232   -593  -1301    192       O  
ATOM   3261  N   LEU B 316       0.482 -56.986  46.491  1.00 71.55           N  
ANISOU 3261  N   LEU B 316     8214   6656  12313   -238  -1053   1003       N  
ATOM   3262  CA  LEU B 316       0.866 -57.389  45.154  1.00 71.51           C  
ANISOU 3262  CA  LEU B 316     8255   6805  12108   -359   -992   1493       C  
ATOM   3263  C   LEU B 316      -0.256 -57.157  44.151  1.00 73.78           C  
ANISOU 3263  C   LEU B 316     8586   7069  12377   -145  -1106   1767       C  
ATOM   3264  O   LEU B 316      -0.016 -56.991  42.965  1.00 75.73           O  
ANISOU 3264  O   LEU B 316     8926   7318  12527   -214  -1121   2224       O  
ATOM   3265  CB  LEU B 316       1.244 -58.880  45.175  1.00 67.40           C  
ANISOU 3265  CB  LEU B 316     7686   6791  11130   -436   -816   1442       C  
ATOM   3266  CG  LEU B 316       1.725 -59.573  43.898  1.00 66.36           C  
ANISOU 3266  CG  LEU B 316     7591   6927  10693   -547   -695   1809       C  
ATOM   3267  CD1 LEU B 316       2.979 -58.932  43.315  1.00 67.89           C  
ANISOU 3267  CD1 LEU B 316     7786   6975  11032   -789   -629   2128       C  
ATOM   3268  CD2 LEU B 316       1.965 -61.016  44.179  1.00 63.86           C  
ANISOU 3268  CD2 LEU B 316     7238   6989  10036   -554   -539   1635       C  
ATOM   3269  N   THR B 317      -1.490 -57.160  44.629  1.00 74.96           N  
ANISOU 3269  N   THR B 317     8643   7250  12588    124  -1187   1487       N  
ATOM   3270  CA  THR B 317      -2.644 -57.181  43.744  1.00 77.32           C  
ANISOU 3270  CA  THR B 317     8891   7669  12818    355  -1331   1680       C  
ATOM   3271  C   THR B 317      -3.615 -56.006  43.941  1.00 82.71           C  
ANISOU 3271  C   THR B 317     9515   7952  13958    691  -1541   1606       C  
ATOM   3272  O   THR B 317      -4.624 -55.917  43.248  1.00 85.38           O  
ANISOU 3272  O   THR B 317     9760   8389  14290    942  -1721   1764       O  
ATOM   3273  CB  THR B 317      -3.432 -58.476  43.944  1.00 73.81           C  
ANISOU 3273  CB  THR B 317     8284   7726  12032    389  -1233   1417       C  
ATOM   3274  OG1 THR B 317      -3.929 -58.502  45.276  1.00 73.53           O  
ANISOU 3274  OG1 THR B 317     8116   7687  12134    489  -1140    948       O  
ATOM   3275  CG2 THR B 317      -2.553 -59.680  43.777  1.00 70.74           C  
ANISOU 3275  CG2 THR B 317     7968   7657  11251    124  -1034   1456       C  
ATOM   3276  N   ASN B 318      -3.337 -55.115  44.886  1.00 85.74           N  
ANISOU 3276  N   ASN B 318     9933   7895  14748    725  -1542   1328       N  
ATOM   3277  CA  ASN B 318      -4.302 -54.081  45.258  1.00 91.47           C  
ANISOU 3277  CA  ASN B 318    10582   8226  15946   1102  -1703   1119       C  
ATOM   3278  C   ASN B 318      -5.693 -54.668  45.500  1.00 91.10           C  
ANISOU 3278  C   ASN B 318    10239   8599  15776   1398  -1696    826       C  
ATOM   3279  O   ASN B 318      -6.705 -53.964  45.405  1.00 95.47           O  
ANISOU 3279  O   ASN B 318    10645   8955  16671   1789  -1866    768       O  
ATOM   3280  CB  ASN B 318      -4.363 -53.002  44.188  1.00 97.25           C  
ANISOU 3280  CB  ASN B 318    11475   8459  17014   1247  -1946   1661       C  
ATOM   3281  CG  ASN B 318      -2.996 -52.636  43.678  1.00100.53           C  
ANISOU 3281  CG  ASN B 318    12147   8585  17465    860  -1890   2084       C  
ATOM   3282  OD1 ASN B 318      -2.281 -51.837  44.288  1.00104.88           O  
ANISOU 3282  OD1 ASN B 318    12801   8624  18423    705  -1868   1925       O  
ATOM   3283  ND2 ASN B 318      -2.606 -53.240  42.558  1.00102.28           N  
ANISOU 3283  ND2 ASN B 318    12447   9161  17251    676  -1851   2585       N  
ATOM   3284  N   ASP B 319      -5.727 -55.966  45.795  1.00 86.70           N  
ANISOU 3284  N   ASP B 319     9574   8602  14766   1206  -1493    658       N  
ATOM   3285  CA  ASP B 319      -6.938 -56.638  46.248  1.00 86.80           C  
ANISOU 3285  CA  ASP B 319     9275   9033  14672   1367  -1396    320       C  
ATOM   3286  C   ASP B 319      -7.246 -56.150  47.672  1.00 88.60           C  
ANISOU 3286  C   ASP B 319     9402   9141  15118   1531  -1238   -239       C  
ATOM   3287  O   ASP B 319      -6.317 -55.939  48.473  1.00 87.91           O  
ANISOU 3287  O   ASP B 319     9510   8883  15008   1367  -1138   -428       O  
ATOM   3288  CB  ASP B 319      -6.732 -58.154  46.219  1.00 82.22           C  
ANISOU 3288  CB  ASP B 319     8678   8968  13594   1053  -1190    327       C  
ATOM   3289  CG  ASP B 319      -8.020 -58.942  46.406  1.00 83.44           C  
ANISOU 3289  CG  ASP B 319     8491   9554  13658   1125  -1094     84       C  
ATOM   3290  OD1 ASP B 319      -7.958 -60.191  46.262  1.00 81.49           O  
ANISOU 3290  OD1 ASP B 319     8240   9651  13071    859   -946    111       O  
ATOM   3291  OD2 ASP B 319      -9.082 -58.335  46.695  1.00 87.42           O1-
ANISOU 3291  OD2 ASP B 319     8710  10039  14465   1439  -1151   -146       O1-
ATOM   3292  N   TRP B 320      -8.536 -55.943  47.968  1.00 91.38           N  
ANISOU 3292  N   TRP B 320     9428   9619  15673   1862  -1227   -529       N  
ATOM   3293  CA  TRP B 320      -8.974 -55.497  49.304  1.00 93.64           C  
ANISOU 3293  CA  TRP B 320     9581   9878  16118   2065  -1025  -1122       C  
ATOM   3294  C   TRP B 320      -9.002 -56.618  50.357  1.00 91.09           C  
ANISOU 3294  C   TRP B 320     9191  10092  15324   1822   -648  -1424       C  
ATOM   3295  O   TRP B 320      -8.950 -56.350  51.558  1.00 93.13           O  
ANISOU 3295  O   TRP B 320     9473  10380  15531   1882   -447  -1879       O  
ATOM   3296  CB  TRP B 320     -10.324 -54.777  49.247  1.00 98.65           C  
ANISOU 3296  CB  TRP B 320     9844  10445  17191   2562  -1119  -1344       C  
ATOM   3297  CG  TRP B 320     -11.388 -55.510  48.489  1.00 97.84           C  
ANISOU 3297  CG  TRP B 320     9357  10814  17003   2624  -1182  -1170       C  
ATOM   3298  CD1 TRP B 320     -11.611 -55.471  47.144  1.00 98.37           C  
ANISOU 3298  CD1 TRP B 320     9390  10855  17128   2701  -1532   -690       C  
ATOM   3299  CD2 TRP B 320     -12.381 -56.380  49.030  1.00 97.49           C  
ANISOU 3299  CD2 TRP B 320     8890  11361  16791   2587   -896  -1487       C  
ATOM   3300  NE1 TRP B 320     -12.683 -56.262  46.812  1.00 98.16           N  
ANISOU 3300  NE1 TRP B 320     8923  11375  16995   2718  -1531   -746       N  
ATOM   3301  CE2 TRP B 320     -13.171 -56.838  47.951  1.00 98.06           C  
ANISOU 3301  CE2 TRP B 320     8650  11724  16882   2622  -1124  -1223       C  
ATOM   3302  CE3 TRP B 320     -12.678 -56.826  50.320  1.00 98.71           C  
ANISOU 3302  CE3 TRP B 320     8897  11854  16753   2501   -457  -1954       C  
ATOM   3303  CZ2 TRP B 320     -14.241 -57.718  48.122  1.00100.62           C  
ANISOU 3303  CZ2 TRP B 320     8480  12622  17126   2536   -932  -1442       C  
ATOM   3304  CZ3 TRP B 320     -13.756 -57.708  50.492  1.00101.78           C  
ANISOU 3304  CZ3 TRP B 320     8817  12815  17036   2418   -211  -2108       C  
ATOM   3305  CH2 TRP B 320     -14.525 -58.138  49.394  1.00101.61           C  
ANISOU 3305  CH2 TRP B 320     8451  13030  17126   2419   -453  -1866       C  
ATOM   3306  N   GLU B 321      -9.076 -57.868  49.913  1.00 87.35           N  
ANISOU 3306  N   GLU B 321     8663  10029  14494   1547   -552  -1170       N  
ATOM   3307  CA  GLU B 321      -9.073 -58.992  50.840  1.00 85.34           C  
ANISOU 3307  CA  GLU B 321     8399  10212  13813   1295   -194  -1341       C  
ATOM   3308  C   GLU B 321      -7.865 -59.883  50.614  1.00 80.89           C  
ANISOU 3308  C   GLU B 321     8164   9681  12888    934   -185  -1017       C  
ATOM   3309  O   GLU B 321      -7.216 -59.784  49.572  1.00 79.55           O  
ANISOU 3309  O   GLU B 321     8147   9304  12774    856   -417   -665       O  
ATOM   3310  CB  GLU B 321     -10.367 -59.799  50.737  1.00 86.68           C  
ANISOU 3310  CB  GLU B 321     8164  10822  13948   1278    -12  -1411       C  
ATOM   3311  CG  GLU B 321     -10.904 -60.080  49.353  1.00 85.20           C  
ANISOU 3311  CG  GLU B 321     7783  10693  13895   1272   -277  -1111       C  
ATOM   3312  CD  GLU B 321     -12.226 -60.804  49.439  1.00 88.38           C  
ANISOU 3312  CD  GLU B 321     7705  11547  14329   1224    -90  -1293       C  
ATOM   3313  OE1 GLU B 321     -12.747 -61.244  48.404  1.00 90.60           O  
ANISOU 3313  OE1 GLU B 321     7778  11984  14660   1156   -297  -1123       O  
ATOM   3314  OE2 GLU B 321     -12.762 -60.941  50.555  1.00 91.58           O1-
ANISOU 3314  OE2 GLU B 321     7915  12191  14690   1234    275  -1626       O1-
ATOM   3315  N   ASP B 322      -7.550 -60.743  51.576  1.00 79.21           N  
ANISOU 3315  N   ASP B 322     8060   9741  12295    740     89  -1116       N  
ATOM   3316  CA  ASP B 322      -6.388 -61.606  51.415  1.00 75.77           C  
ANISOU 3316  CA  ASP B 322     7910   9319  11557    468     86   -822       C  
ATOM   3317  C   ASP B 322      -6.668 -62.797  50.491  1.00 72.83           C  
ANISOU 3317  C   ASP B 322     7489   9106  11074    267    128   -534       C  
ATOM   3318  O   ASP B 322      -7.803 -62.987  50.035  1.00 74.23           O  
ANISOU 3318  O   ASP B 322     7387   9428  11386    296    150   -580       O  
ATOM   3319  CB  ASP B 322      -5.869 -62.082  52.767  1.00 76.51           C  
ANISOU 3319  CB  ASP B 322     8177   9620  11271    380    303   -974       C  
ATOM   3320  CG  ASP B 322      -6.890 -62.882  53.527  1.00 81.29           C  
ANISOU 3320  CG  ASP B 322     8635  10600  11649    327    665  -1098       C  
ATOM   3321  OD1 ASP B 322      -6.551 -63.372  54.617  1.00 86.60           O  
ANISOU 3321  OD1 ASP B 322     9478  11491  11933    255    866  -1146       O  
ATOM   3322  OD2 ASP B 322      -8.039 -63.020  53.052  1.00 85.94           O1-
ANISOU 3322  OD2 ASP B 322     8921  11294  12438    348    749  -1133       O1-
ATOM   3323  N   HIS B 323      -5.619 -63.579  50.225  1.00 68.85           N  
ANISOU 3323  N   HIS B 323     7232   8576  10352     75    123   -285       N  
ATOM   3324  CA  HIS B 323      -5.687 -64.757  49.381  1.00 66.33           C  
ANISOU 3324  CA  HIS B 323     6933   8346   9919   -117    167    -74       C  
ATOM   3325  C   HIS B 323      -6.632 -65.823  49.926  1.00 67.52           C  
ANISOU 3325  C   HIS B 323     6963   8728   9962   -273    458   -166       C  
ATOM   3326  O   HIS B 323      -6.988 -65.821  51.102  1.00 69.28           O  
ANISOU 3326  O   HIS B 323     7151   9092  10079   -254    687   -324       O  
ATOM   3327  CB  HIS B 323      -4.300 -65.344  49.215  1.00 63.79           C  
ANISOU 3327  CB  HIS B 323     6891   7936   9411   -226    149    144       C  
ATOM   3328  CG  HIS B 323      -3.640 -65.713  50.502  1.00 63.89           C  
ANISOU 3328  CG  HIS B 323     7069   8011   9195   -240    295    106       C  
ATOM   3329  ND1 HIS B 323      -3.182 -64.777  51.401  1.00 66.52           N  
ANISOU 3329  ND1 HIS B 323     7436   8318   9518   -120    220    -61       N  
ATOM   3330  CD2 HIS B 323      -3.358 -66.921  51.043  1.00 65.25           C  
ANISOU 3330  CD2 HIS B 323     7399   8267   9125   -346    483    222       C  
ATOM   3331  CE1 HIS B 323      -2.661 -65.389  52.450  1.00 68.24           C  
ANISOU 3331  CE1 HIS B 323     7812   8681   9434   -144    335    -51       C  
ATOM   3332  NE2 HIS B 323      -2.748 -66.693  52.254  1.00 68.28           N  
ANISOU 3332  NE2 HIS B 323     7905   8735   9300   -266    499    162       N  
ATOM   3333  N   LEU B 324      -7.052 -66.728  49.053  1.00 66.99           N  
ANISOU 3333  N   LEU B 324     6831   8708   9914   -451    461    -81       N  
ATOM   3334  CA  LEU B 324      -7.833 -67.872  49.479  1.00 68.44           C  
ANISOU 3334  CA  LEU B 324     6922   9032  10050   -693    752   -130       C  
ATOM   3335  C   LEU B 324      -6.912 -69.057  49.812  1.00 67.62           C  
ANISOU 3335  C   LEU B 324     7174   8793   9723   -860    917     76       C  
ATOM   3336  O   LEU B 324      -7.220 -69.850  50.697  1.00 69.40           O  
ANISOU 3336  O   LEU B 324     7458   9068   9841  -1019   1219    119       O  
ATOM   3337  CB  LEU B 324      -8.867 -68.246  48.413  1.00 69.42           C  
ANISOU 3337  CB  LEU B 324     6748   9261  10365   -830    646   -221       C  
ATOM   3338  CG  LEU B 324      -9.497 -69.631  48.506  1.00 69.43           C  
ANISOU 3338  CG  LEU B 324     6686   9307  10385  -1192    904   -253       C  
ATOM   3339  CD1 LEU B 324     -10.325 -69.764  49.746  1.00 70.07           C  
ANISOU 3339  CD1 LEU B 324     6568   9568  10486  -1293   1279   -345       C  
ATOM   3340  CD2 LEU B 324     -10.343 -69.871  47.291  1.00 71.89           C  
ANISOU 3340  CD2 LEU B 324     6701   9735  10879  -1320    681   -401       C  
ATOM   3341  N   ALA B 325      -5.791 -69.168  49.097  1.00 65.56           N  
ANISOU 3341  N   ALA B 325     7141   8364   9404   -808    735    225       N  
ATOM   3342  CA  ALA B 325      -4.829 -70.241  49.315  1.00 65.44           C  
ANISOU 3342  CA  ALA B 325     7434   8192   9234   -877    847    411       C  
ATOM   3343  C   ALA B 325      -3.445 -69.780  48.888  1.00 63.98           C  
ANISOU 3343  C   ALA B 325     7401   7917   8992   -704    642    525       C  
ATOM   3344  O   ALA B 325      -3.331 -68.925  47.999  1.00 63.89           O  
ANISOU 3344  O   ALA B 325     7285   7919   9071   -629    434    499       O  
ATOM   3345  CB  ALA B 325      -5.229 -71.453  48.531  1.00 66.29           C  
ANISOU 3345  CB  ALA B 325     7571   8186   9429  -1105    927    399       C  
ATOM   3346  N   VAL B 326      -2.400 -70.325  49.514  1.00 63.94           N  
ANISOU 3346  N   VAL B 326     7617   7835   8843   -640    698    678       N  
ATOM   3347  CA  VAL B 326      -1.028 -70.027  49.111  1.00 62.85           C  
ANISOU 3347  CA  VAL B 326     7548   7647   8686   -501    534    774       C  
ATOM   3348  C   VAL B 326      -0.298 -71.309  48.752  1.00 63.41           C  
ANISOU 3348  C   VAL B 326     7797   7567   8728   -489    623    899       C  
ATOM   3349  O   VAL B 326      -0.514 -72.346  49.373  1.00 65.48           O  
ANISOU 3349  O   VAL B 326     8219   7717   8942   -532    789    987       O  
ATOM   3350  CB  VAL B 326      -0.246 -69.291  50.229  1.00 63.31           C  
ANISOU 3350  CB  VAL B 326     7625   7792   8638   -362    436    786       C  
ATOM   3351  CG1 VAL B 326      -0.229 -70.096  51.497  1.00 65.46           C  
ANISOU 3351  CG1 VAL B 326     8071   8117   8683   -333    579    886       C  
ATOM   3352  CG2 VAL B 326       1.189 -69.016  49.812  1.00 63.33           C  
ANISOU 3352  CG2 VAL B 326     7612   7769   8681   -265    276    874       C  
ATOM   3353  N   LYS B 327       0.551 -71.243  47.735  1.00 62.69           N  
ANISOU 3353  N   LYS B 327     7683   7457   8677   -424    537    914       N  
ATOM   3354  CA  LYS B 327       1.496 -72.322  47.455  1.00 63.86           C  
ANISOU 3354  CA  LYS B 327     7968   7473   8823   -320    615    989       C  
ATOM   3355  C   LYS B 327       2.855 -71.679  47.176  1.00 63.53           C  
ANISOU 3355  C   LYS B 327     7804   7548   8787   -168    499   1053       C  
ATOM   3356  O   LYS B 327       2.975 -70.815  46.280  1.00 63.68           O  
ANISOU 3356  O   LYS B 327     7687   7677   8829   -224    430   1023       O  
ATOM   3357  CB  LYS B 327       1.023 -73.192  46.280  1.00 64.82           C  
ANISOU 3357  CB  LYS B 327     8155   7476   8995   -430    713    847       C  
ATOM   3358  CG  LYS B 327       1.798 -74.477  46.046  1.00 66.91           C  
ANISOU 3358  CG  LYS B 327     8596   7512   9314   -304    837    851       C  
ATOM   3359  CD  LYS B 327       1.875 -75.286  47.303  1.00 70.79           C  
ANISOU 3359  CD  LYS B 327     9273   7783   9840   -230    924   1041       C  
ATOM   3360  CE  LYS B 327       2.562 -76.616  47.073  1.00 74.77           C  
ANISOU 3360  CE  LYS B 327     9978   7956  10475    -60   1036   1058       C  
ATOM   3361  NZ  LYS B 327       1.615 -77.710  47.400  1.00 79.24           N1+
ANISOU 3361  NZ  LYS B 327    10779   8155  11174   -258   1206   1075       N1+
ATOM   3362  N   HIS B 328       3.863 -72.105  47.941  1.00 63.85           N  
ANISOU 3362  N   HIS B 328     7875   7573   8810     16    474   1168       N  
ATOM   3363  CA  HIS B 328       5.154 -71.429  48.012  1.00 63.36           C  
ANISOU 3363  CA  HIS B 328     7613   7671   8790    134    338   1214       C  
ATOM   3364  C   HIS B 328       6.237 -72.490  48.013  1.00 64.86           C  
ANISOU 3364  C   HIS B 328     7812   7807   9023    384    385   1294       C  
ATOM   3365  O   HIS B 328       6.293 -73.290  48.930  1.00 67.25           O  
ANISOU 3365  O   HIS B 328     8275   8004   9272    536    370   1413       O  
ATOM   3366  CB  HIS B 328       5.188 -70.642  49.308  1.00 63.85           C  
ANISOU 3366  CB  HIS B 328     7632   7850   8776    140    162   1221       C  
ATOM   3367  CG  HIS B 328       6.409 -69.806  49.493  1.00 66.43           C  
ANISOU 3367  CG  HIS B 328     7709   8341   9188    185    -25   1208       C  
ATOM   3368  ND1 HIS B 328       6.796 -69.334  50.728  1.00 68.76           N  
ANISOU 3368  ND1 HIS B 328     7955   8779   9391    240   -236   1166       N  
ATOM   3369  CD2 HIS B 328       7.331 -69.351  48.609  1.00 68.78           C  
ANISOU 3369  CD2 HIS B 328     7769   8712   9652    149    -27   1215       C  
ATOM   3370  CE1 HIS B 328       7.906 -68.627  50.597  1.00 71.89           C  
ANISOU 3370  CE1 HIS B 328     8068   9299   9946    217   -392   1119       C  
ATOM   3371  NE2 HIS B 328       8.255 -68.625  49.321  1.00 70.63           N  
ANISOU 3371  NE2 HIS B 328     7779   9094   9960    152   -242   1174       N  
ATOM   3372  N   PHE B 329       7.088 -72.512  46.991  1.00 64.28           N  
ANISOU 3372  N   PHE B 329     7570   7813   9041    449    457   1246       N  
ATOM   3373  CA  PHE B 329       8.001 -73.624  46.769  1.00 65.83           C  
ANISOU 3373  CA  PHE B 329     7756   7930   9325    732    554   1254       C  
ATOM   3374  C   PHE B 329       9.226 -73.175  45.970  1.00 67.60           C  
ANISOU 3374  C   PHE B 329     7632   8408   9642    803    605   1209       C  
ATOM   3375  O   PHE B 329       9.319 -72.017  45.563  1.00 66.55           O  
ANISOU 3375  O   PHE B 329     7312   8470   9503    582    576   1215       O  
ATOM   3376  CB  PHE B 329       7.287 -74.729  45.997  1.00 65.83           C  
ANISOU 3376  CB  PHE B 329     8019   7658   9334    720    762   1125       C  
ATOM   3377  CG  PHE B 329       6.945 -74.354  44.565  1.00 64.27           C  
ANISOU 3377  CG  PHE B 329     7772   7591   9054    534    889    939       C  
ATOM   3378  CD1 PHE B 329       5.797 -73.622  44.274  1.00 61.15           C  
ANISOU 3378  CD1 PHE B 329     7429   7256   8548    248    831    907       C  
ATOM   3379  CD2 PHE B 329       7.780 -74.726  43.512  1.00 65.56           C  
ANISOU 3379  CD2 PHE B 329     7827   7862   9221    678   1062    798       C  
ATOM   3380  CE1 PHE B 329       5.485 -73.277  42.980  1.00 61.48           C  
ANISOU 3380  CE1 PHE B 329     7447   7459   8452    112    894    789       C  
ATOM   3381  CE2 PHE B 329       7.475 -74.388  42.208  1.00 65.47           C  
ANISOU 3381  CE2 PHE B 329     7806   8040   9026    516   1178    653       C  
ATOM   3382  CZ  PHE B 329       6.317 -73.667  41.936  1.00 64.07           C  
ANISOU 3382  CZ  PHE B 329     7715   7922   8706    232   1069    671       C  
ATOM   3383  N   SER B 330      10.140 -74.118  45.725  1.00 70.77           N  
ANISOU 3383  N   SER B 330     7948   8782  10158   1113    710   1172       N  
ATOM   3384  CA  SER B 330      11.363 -73.894  44.983  1.00 73.18           C  
ANISOU 3384  CA  SER B 330     7870   9365  10569   1222    830   1108       C  
ATOM   3385  C   SER B 330      11.720 -75.160  44.239  1.00 77.18           C  
ANISOU 3385  C   SER B 330     8445   9732  11145   1527   1075    936       C  
ATOM   3386  O   SER B 330      11.410 -76.244  44.716  1.00 78.50           O  
ANISOU 3386  O   SER B 330     8894   9544  11385   1746   1053    939       O  
ATOM   3387  CB  SER B 330      12.510 -73.534  45.929  1.00 75.59           C  
ANISOU 3387  CB  SER B 330     7805   9885  11030   1388    598   1219       C  
ATOM   3388  OG  SER B 330      12.916 -74.635  46.708  1.00 75.96           O  
ANISOU 3388  OG  SER B 330     7923   9773  11164   1800    486   1289       O  
ATOM   3389  N   VAL B 331      12.374 -75.014  43.080  1.00 80.03           N  
ANISOU 3389  N   VAL B 331     8563  10359  11487   1537   1333    786       N  
ATOM   3390  CA  VAL B 331      12.825 -76.134  42.255  1.00 84.63           C  
ANISOU 3390  CA  VAL B 331     9163  10868  12123   1854   1613    526       C  
ATOM   3391  C   VAL B 331      14.322 -76.040  42.106  1.00 90.03           C  
ANISOU 3391  C   VAL B 331     9311  11900  12994   2122   1729    504       C  
ATOM   3392  O   VAL B 331      14.865 -74.943  42.054  1.00 90.27           O  
ANISOU 3392  O   VAL B 331     8970  12305  13023   1895   1714    636       O  
ATOM   3393  CB  VAL B 331      12.168 -76.128  40.884  1.00 84.14           C  
ANISOU 3393  CB  VAL B 331     9298  10895  11776   1635   1870    291       C  
ATOM   3394  CG1 VAL B 331      12.585 -77.321  40.101  1.00 88.33           C  
ANISOU 3394  CG1 VAL B 331     9886  11326  12349   1974   2154    -68       C  
ATOM   3395  CG2 VAL B 331      10.671 -76.159  41.041  1.00 81.45           C  
ANISOU 3395  CG2 VAL B 331     9387  10266  11292   1352   1718    297       C  
ATOM   3396  N   GLU B 332      14.968 -77.202  42.023  1.00 96.09           N  
ANISOU 3396  N   GLU B 332    10026  12515  13966   2602   1854    323       N  
ATOM   3397  CA  GLU B 332      16.413 -77.387  42.142  1.00102.50           C  
ANISOU 3397  CA  GLU B 332    10284  13600  15058   3003   1909    291       C  
ATOM   3398  C   GLU B 332      17.014 -77.986  40.871  1.00108.29           C  
ANISOU 3398  C   GLU B 332    10845  14508  15790   3254   2371    -81       C  
ATOM   3399  O   GLU B 332      16.315 -78.604  40.076  1.00108.66           O  
ANISOU 3399  O   GLU B 332    11300  14328  15656   3235   2584   -354       O  
ATOM   3400  CB  GLU B 332      16.672 -78.358  43.298  1.00105.28           C  
ANISOU 3400  CB  GLU B 332    10733  13573  15696   3490   1617    420       C  
ATOM   3401  CG  GLU B 332      15.905 -79.758  43.211  1.00108.94           C  
ANISOU 3401  CG  GLU B 332    11794  13367  16229   3743   1700    278       C  
ATOM   3402  CD  GLU B 332      14.365 -79.691  43.505  1.00105.85           C  
ANISOU 3402  CD  GLU B 332    11999  12610  15609   3301   1586    393       C  
ATOM   3403  OE1 GLU B 332      13.623 -80.620  43.117  1.00105.98           O  
ANISOU 3403  OE1 GLU B 332    12455  12153  15658   3316   1726    198       O  
ATOM   3404  OE2 GLU B 332      13.890 -78.712  44.128  1.00102.94           O1-
ANISOU 3404  OE2 GLU B 332    11630  12422  15059   2933   1363    641       O1-
ATOM   3405  N   GLY B 333      18.320 -77.817  40.687  1.00114.29           N  
ANISOU 3405  N   GLY B 333    10970  15703  16751   3489   2528   -135       N  
ATOM   3406  CA  GLY B 333      19.059 -78.485  39.602  1.00121.43           C  
ANISOU 3406  CA  GLY B 333    11625  16818  17692   3841   3003   -529       C  
ATOM   3407  C   GLY B 333      18.981 -77.888  38.200  1.00123.02           C  
ANISOU 3407  C   GLY B 333    11776  17488  17475   3477   3471   -701       C  
ATOM   3408  O   GLY B 333      19.858 -77.100  37.810  1.00125.48           O  
ANISOU 3408  O   GLY B 333    11519  18373  17782   3321   3710   -619       O  
ATOM   3409  N   GLN B 334      17.942 -78.276  37.443  1.00122.25           N  
ANISOU 3409  N   GLN B 334    12261  17169  17019   3330   3599   -929       N  
ATOM   3410  CA  GLN B 334      17.810 -77.931  36.002  1.00125.04           C  
ANISOU 3410  CA  GLN B 334    12662  17981  16863   3075   4043  -1142       C  
ATOM   3411  C   GLN B 334      17.871 -76.421  35.827  1.00122.20           C  
ANISOU 3411  C   GLN B 334    12064  18090  16276   2519   4057   -710       C  
ATOM   3412  O   GLN B 334      18.784 -75.881  35.192  1.00126.25           O  
ANISOU 3412  O   GLN B 334    12096  19168  16705   2437   4438   -668       O  
ATOM   3413  CB  GLN B 334      16.493 -78.464  35.398  1.00123.65           C  
ANISOU 3413  CB  GLN B 334    13181  17483  16317   2927   4010  -1416       C  
ATOM   3414  CG  GLN B 334      16.295 -79.983  35.447  1.00128.44           C  
ANISOU 3414  CG  GLN B 334    14117  17516  17167   3393   4022  -1893       C  
ATOM   3415  CD  GLN B 334      15.747 -80.466  36.791  1.00126.78           C  
ANISOU 3415  CD  GLN B 334    14185  16599  17384   3481   3560  -1652       C  
ATOM   3416  OE1 GLN B 334      14.860 -79.827  37.392  1.00121.09           O  
ANISOU 3416  OE1 GLN B 334    13689  15748  16571   3072   3231  -1296       O  
ATOM   3417  NE2 GLN B 334      16.272 -81.602  37.269  1.00130.44           N  
ANISOU 3417  NE2 GLN B 334    14643  16606  18311   4038   3552  -1831       N  
ATOM   3418  N   LEU B 335      16.863 -75.766  36.391  1.00115.58           N  
ANISOU 3418  N   LEU B 335    11572  16979  15363   2137   3662   -393       N  
ATOM   3419  CA  LEU B 335      16.940 -74.369  36.731  1.00112.47           C  
ANISOU 3419  CA  LEU B 335    10955  16787  14989   1684   3512     57       C  
ATOM   3420  C   LEU B 335      16.698 -74.324  38.232  1.00107.57           C  
ANISOU 3420  C   LEU B 335    10376  15745  14748   1730   2997    246       C  
ATOM   3421  O   LEU B 335      16.059 -75.222  38.778  1.00105.64           O  
ANISOU 3421  O   LEU B 335    10507  15051  14579   1966   2782    116       O  
ATOM   3422  CB  LEU B 335      15.868 -73.582  35.982  1.00109.92           C  
ANISOU 3422  CB  LEU B 335    11044  16530  14187   1229   3509    234       C  
ATOM   3423  CG  LEU B 335      16.323 -72.193  35.515  1.00112.80           C  
ANISOU 3423  CG  LEU B 335    11112  17305  14439    793   3686    630       C  
ATOM   3424  CD1 LEU B 335      17.266 -72.281  34.298  1.00120.99           C  
ANISOU 3424  CD1 LEU B 335    11829  18936  15203    840   4288    517       C  
ATOM   3425  CD2 LEU B 335      15.131 -71.287  35.203  1.00110.38           C  
ANISOU 3425  CD2 LEU B 335    11245  16887  13804    387   3482    928       C  
ATOM   3426  N   GLU B 336      17.244 -73.319  38.908  1.00106.11           N  
ANISOU 3426  N   GLU B 336     9804  15710  14799   1501   2816    534       N  
ATOM   3427  CA  GLU B 336      16.826 -73.017  40.280  1.00101.18           C  
ANISOU 3427  CA  GLU B 336     9296  14759  14387   1439   2310    716       C  
ATOM   3428  C   GLU B 336      15.852 -71.844  40.277  1.00 95.47           C  
ANISOU 3428  C   GLU B 336     8858  13936  13478    932   2149    958       C  
ATOM   3429  O   GLU B 336      16.101 -70.814  39.655  1.00 96.57           O  
ANISOU 3429  O   GLU B 336     8811  14326  13554    574   2318   1135       O  
ATOM   3430  CB  GLU B 336      18.029 -72.702  41.182  1.00104.50           C  
ANISOU 3430  CB  GLU B 336     9108  15386  15209   1545   2118    795       C  
ATOM   3431  CG  GLU B 336      18.704 -73.923  41.803  1.00109.74           C  
ANISOU 3431  CG  GLU B 336     9597  15966  16132   2156   2006    635       C  
ATOM   3432  CD  GLU B 336      20.225 -73.767  41.926  1.00118.18           C  
ANISOU 3432  CD  GLU B 336     9854  17490  17557   2334   2064    594       C  
ATOM   3433  OE1 GLU B 336      20.684 -72.779  42.553  1.00119.40           O  
ANISOU 3433  OE1 GLU B 336     9622  17850  17893   2033   1812    745       O  
ATOM   3434  OE2 GLU B 336      20.961 -74.639  41.396  1.00123.22           O1-
ANISOU 3434  OE2 GLU B 336    10213  18281  18323   2780   2358    371       O1-
ATOM   3435  N   PHE B 337      14.733 -72.001  40.954  1.00 89.78           N  
ANISOU 3435  N   PHE B 337     8587  12835  12688    911   1845    981       N  
ATOM   3436  CA  PHE B 337      13.844 -70.876  41.151  1.00 85.39           C  
ANISOU 3436  CA  PHE B 337     8241  12160  12044    512   1644   1182       C  
ATOM   3437  C   PHE B 337      12.942 -71.079  42.358  1.00 81.42           C  
ANISOU 3437  C   PHE B 337     8050  11302  11583    566   1280   1184       C  
ATOM   3438  O   PHE B 337      12.720 -72.206  42.787  1.00 80.96           O  
ANISOU 3438  O   PHE B 337     8189  11041  11531    861   1235   1067       O  
ATOM   3439  CB  PHE B 337      13.034 -70.568  39.882  1.00 85.02           C  
ANISOU 3439  CB  PHE B 337     8484  12183  11638    288   1853   1221       C  
ATOM   3440  CG  PHE B 337      11.990 -71.599  39.533  1.00 82.67           C  
ANISOU 3440  CG  PHE B 337     8627  11684  11098    441   1861    999       C  
ATOM   3441  CD1 PHE B 337      10.714 -71.531  40.088  1.00 78.04           C  
ANISOU 3441  CD1 PHE B 337     8382  10793  10475    335   1586   1020       C  
ATOM   3442  CD2 PHE B 337      12.271 -72.607  38.615  1.00 85.15           C  
ANISOU 3442  CD2 PHE B 337     8987  12127  11236    666   2162    727       C  
ATOM   3443  CE1 PHE B 337       9.743 -72.473  39.770  1.00 77.63           C  
ANISOU 3443  CE1 PHE B 337     8680  10556  10258    407   1591    798       C  
ATOM   3444  CE2 PHE B 337      11.308 -73.555  38.279  1.00 84.58           C  
ANISOU 3444  CE2 PHE B 337     9315  11832  10987    754   2149    461       C  
ATOM   3445  CZ  PHE B 337      10.037 -73.484  38.863  1.00 81.72           C  
ANISOU 3445  CZ  PHE B 337     9262  11158  10630    597   1854    511       C  
ATOM   3446  N   ARG B 338      12.457 -69.975  42.918  1.00 78.82           N  
ANISOU 3446  N   ARG B 338     7762  10886  11298    281   1047   1322       N  
ATOM   3447  CA  ARG B 338      11.505 -70.007  44.008  1.00 75.44           C  
ANISOU 3447  CA  ARG B 338     7622  10191  10848    290    760   1313       C  
ATOM   3448  C   ARG B 338      10.267 -69.419  43.415  1.00 72.48           C  
ANISOU 3448  C   ARG B 338     7535   9698  10306     45    776   1360       C  
ATOM   3449  O   ARG B 338      10.355 -68.596  42.503  1.00 73.48           O  
ANISOU 3449  O   ARG B 338     7584   9941  10394   -167    893   1478       O  
ATOM   3450  CB  ARG B 338      11.980 -69.160  45.181  1.00 75.97           C  
ANISOU 3450  CB  ARG B 338     7467  10293  11105    201    463   1350       C  
ATOM   3451  CG  ARG B 338      13.296 -69.642  45.782  1.00 82.83           C  
ANISOU 3451  CG  ARG B 338     7962  11362  12146    454    369   1312       C  
ATOM   3452  CD  ARG B 338      13.616 -68.957  47.087  1.00 90.14           C  
ANISOU 3452  CD  ARG B 338     8726  12345  13177    390     -6   1281       C  
ATOM   3453  NE  ARG B 338      12.622 -69.296  48.104  1.00 93.93           N  
ANISOU 3453  NE  ARG B 338     9609  12635  13441    495   -200   1270       N  
ATOM   3454  CZ  ARG B 338      12.805 -70.177  49.089  1.00 99.67           C  
ANISOU 3454  CZ  ARG B 338    10422  13386  14062    817   -380   1302       C  
ATOM   3455  NH1 ARG B 338      13.973 -70.822  49.218  1.00104.99           N1+
ANISOU 3455  NH1 ARG B 338    10781  14246  14862   1124   -449   1327       N1+
ATOM   3456  NH2 ARG B 338      11.816 -70.410  49.956  1.00 99.31           N  
ANISOU 3456  NH2 ARG B 338    10764  13192  13778    848   -483   1333       N  
ATOM   3457  N   ALA B 339       9.110 -69.859  43.885  1.00 69.62           N  
ANISOU 3457  N   ALA B 339     7490   9120   9842     80    671   1294       N  
ATOM   3458  CA  ALA B 339       7.866 -69.275  43.427  1.00 67.75           C  
ANISOU 3458  CA  ALA B 339     7457   8797   9485   -115    631   1319       C  
ATOM   3459  C   ALA B 339       6.897 -69.126  44.592  1.00 65.71           C  
ANISOU 3459  C   ALA B 339     7350   8353   9261   -132    432   1275       C  
ATOM   3460  O   ALA B 339       6.885 -69.967  45.509  1.00 66.26           O  
ANISOU 3460  O   ALA B 339     7509   8340   9326     18    401   1224       O  
ATOM   3461  CB  ALA B 339       7.259 -70.119  42.325  1.00 68.02           C  
ANISOU 3461  CB  ALA B 339     7687   8854   9301    -86    800   1209       C  
ATOM   3462  N   LEU B 340       6.089 -68.064  44.546  1.00 63.82           N  
ANISOU 3462  N   LEU B 340     7143   8055   9049   -295    318   1314       N  
ATOM   3463  CA  LEU B 340       5.030 -67.837  45.515  1.00 61.26           C  
ANISOU 3463  CA  LEU B 340     6931   7603   8741   -307    185   1226       C  
ATOM   3464  C   LEU B 340       3.725 -67.614  44.777  1.00 60.89           C  
ANISOU 3464  C   LEU B 340     6983   7519   8631   -388    178   1210       C  
ATOM   3465  O   LEU B 340       3.515 -66.570  44.174  1.00 61.54           O  
ANISOU 3465  O   LEU B 340     7019   7587   8774   -468     97   1313       O  
ATOM   3466  CB  LEU B 340       5.338 -66.607  46.340  1.00 61.13           C  
ANISOU 3466  CB  LEU B 340     6793   7538   8894   -371      7   1213       C  
ATOM   3467  CG  LEU B 340       4.952 -66.691  47.797  1.00 60.25           C  
ANISOU 3467  CG  LEU B 340     6748   7408   8736   -295    -97   1066       C  
ATOM   3468  CD1 LEU B 340       4.855 -65.302  48.302  1.00 61.75           C  
ANISOU 3468  CD1 LEU B 340     6860   7504   9098   -384   -267    959       C  
ATOM   3469  CD2 LEU B 340       3.623 -67.383  47.945  1.00 60.91           C  
ANISOU 3469  CD2 LEU B 340     7005   7452   8683   -269      2   1008       C  
ATOM   3470  N   LEU B 341       2.830 -68.584  44.831  1.00 60.50           N  
ANISOU 3470  N   LEU B 341     7057   7443   8485   -372    244   1095       N  
ATOM   3471  CA  LEU B 341       1.589 -68.469  44.080  1.00 60.73           C  
ANISOU 3471  CA  LEU B 341     7111   7502   8462   -452    199   1039       C  
ATOM   3472  C   LEU B 341       0.385 -68.287  45.003  1.00 60.37           C  
ANISOU 3472  C   LEU B 341     7038   7398   8503   -473    147    925       C  
ATOM   3473  O   LEU B 341       0.355 -68.891  46.088  1.00 61.50           O  
ANISOU 3473  O   LEU B 341     7237   7487   8641   -455    238    870       O  
ATOM   3474  CB  LEU B 341       1.433 -69.687  43.166  1.00 61.57           C  
ANISOU 3474  CB  LEU B 341     7321   7658   8415   -477    318    928       C  
ATOM   3475  CG  LEU B 341       2.658 -69.915  42.261  1.00 62.41           C  
ANISOU 3475  CG  LEU B 341     7434   7875   8402   -418    434    987       C  
ATOM   3476  CD1 LEU B 341       2.575 -71.218  41.491  1.00 62.17           C  
ANISOU 3476  CD1 LEU B 341     7533   7855   8233   -405    571    775       C  
ATOM   3477  CD2 LEU B 341       2.891 -68.721  41.323  1.00 62.66           C  
ANISOU 3477  CD2 LEU B 341     7390   8071   8347   -471    365   1185       C  
ATOM   3478  N   PHE B 342      -0.583 -67.461  44.583  1.00 59.67           N  
ANISOU 3478  N   PHE B 342     6852   7342   8478   -486     12    910       N  
ATOM   3479  CA  PHE B 342      -1.792 -67.190  45.352  1.00 58.97           C  
ANISOU 3479  CA  PHE B 342     6656   7247   8500   -477    -13    765       C  
ATOM   3480  C   PHE B 342      -3.073 -67.478  44.550  1.00 60.10           C  
ANISOU 3480  C   PHE B 342     6682   7514   8639   -536    -81    665       C  
ATOM   3481  O   PHE B 342      -3.145 -67.259  43.328  1.00 61.20           O  
ANISOU 3481  O   PHE B 342     6814   7747   8691   -529   -227    745       O  
ATOM   3482  CB  PHE B 342      -1.816 -65.735  45.802  1.00 59.38           C  
ANISOU 3482  CB  PHE B 342     6623   7203   8735   -369   -155    779       C  
ATOM   3483  CG  PHE B 342      -0.770 -65.371  46.822  1.00 60.52           C  
ANISOU 3483  CG  PHE B 342     6825   7258   8910   -342   -134    768       C  
ATOM   3484  CD1 PHE B 342      -0.979 -65.607  48.186  1.00 62.41           C  
ANISOU 3484  CD1 PHE B 342     7080   7541   9090   -310    -42    599       C  
ATOM   3485  CD2 PHE B 342       0.415 -64.741  46.437  1.00 61.83           C  
ANISOU 3485  CD2 PHE B 342     7008   7335   9146   -366   -213    920       C  
ATOM   3486  CE1 PHE B 342       0.002 -65.239  49.157  1.00 63.75           C  
ANISOU 3486  CE1 PHE B 342     7296   7693   9230   -275    -90    548       C  
ATOM   3487  CE2 PHE B 342       1.405 -64.380  47.398  1.00 62.80           C  
ANISOU 3487  CE2 PHE B 342     7124   7411   9325   -368   -248    857       C  
ATOM   3488  CZ  PHE B 342       1.199 -64.633  48.756  1.00 62.14           C  
ANISOU 3488  CZ  PHE B 342     7069   7396   9143   -308   -219    654       C  
ATOM   3489  N   VAL B 343      -4.098 -67.951  45.248  1.00 60.32           N  
ANISOU 3489  N   VAL B 343     6594   7584   8741   -605     19    492       N  
ATOM   3490  CA  VAL B 343      -5.439 -68.070  44.681  1.00 61.81           C  
ANISOU 3490  CA  VAL B 343     6553   7927   9002   -670    -76    346       C  
ATOM   3491  C   VAL B 343      -6.329 -67.019  45.343  1.00 63.07           C  
ANISOU 3491  C   VAL B 343     6462   8131   9369   -520   -137    258       C  
ATOM   3492  O   VAL B 343      -6.474 -67.018  46.571  1.00 63.10           O  
ANISOU 3492  O   VAL B 343     6440   8116   9419   -515     61    163       O  
ATOM   3493  CB  VAL B 343      -6.042 -69.463  44.959  1.00 62.98           C  
ANISOU 3493  CB  VAL B 343     6682   8089   9157   -915    131    183       C  
ATOM   3494  CG1 VAL B 343      -7.473 -69.562  44.402  1.00 65.55           C  
ANISOU 3494  CG1 VAL B 343     6676   8621   9609  -1026      8    -20       C  
ATOM   3495  CG2 VAL B 343      -5.161 -70.529  44.384  1.00 61.52           C  
ANISOU 3495  CG2 VAL B 343     6764   7783   8827  -1014    208    213       C  
ATOM   3496  N   PRO B 344      -6.914 -66.111  44.543  1.00 64.60           N  
ANISOU 3496  N   PRO B 344     6482   8394   9669   -362   -412    291       N  
ATOM   3497  CA  PRO B 344      -7.819 -65.067  45.011  1.00 66.46           C  
ANISOU 3497  CA  PRO B 344     6445   8640  10165   -142   -505    183       C  
ATOM   3498  C   PRO B 344      -9.125 -65.655  45.538  1.00 68.95           C  
ANISOU 3498  C   PRO B 344     6411   9183  10602   -239   -354    -89       C  
ATOM   3499  O   PRO B 344      -9.479 -66.783  45.209  1.00 69.48           O  
ANISOU 3499  O   PRO B 344     6423   9388  10587   -500   -274   -166       O  
ATOM   3500  CB  PRO B 344      -8.121 -64.277  43.742  1.00 68.19           C  
ANISOU 3500  CB  PRO B 344     6590   8893  10426     40   -874    358       C  
ATOM   3501  CG  PRO B 344      -7.087 -64.594  42.802  1.00 66.67           C  
ANISOU 3501  CG  PRO B 344     6696   8677   9955    -70   -927    598       C  
ATOM   3502  CD  PRO B 344      -6.709 -66.016  43.093  1.00 65.79           C  
ANISOU 3502  CD  PRO B 344     6704   8627   9665   -344   -660    456       C  
ATOM   3503  N   ARG B 345      -9.839 -64.891  46.350  1.00 71.04           N  
ANISOU 3503  N   ARG B 345     6423   9479  11089    -44   -293   -263       N  
ATOM   3504  CA  ARG B 345     -11.106 -65.344  46.864  1.00 73.94           C  
ANISOU 3504  CA  ARG B 345     6380  10116  11598   -133   -103   -523       C  
ATOM   3505  C   ARG B 345     -12.183 -65.339  45.811  1.00 77.75           C  
ANISOU 3505  C   ARG B 345     6459  10833  12247    -94   -398   -594       C  
ATOM   3506  O   ARG B 345     -13.089 -66.182  45.831  1.00 80.34           O  
ANISOU 3506  O   ARG B 345     6457  11416  12651   -343   -276   -781       O  
ATOM   3507  CB  ARG B 345     -11.524 -64.472  48.020  1.00 75.66           C  
ANISOU 3507  CB  ARG B 345     6421  10343  11981    112     74   -737       C  
ATOM   3508  CG  ARG B 345     -11.062 -65.037  49.292  1.00 74.33           C  
ANISOU 3508  CG  ARG B 345     6469  10189  11581    -64    478   -787       C  
ATOM   3509  CD  ARG B 345     -10.884 -64.000  50.349  1.00 75.15           C  
ANISOU 3509  CD  ARG B 345     6616  10224  11711    211    577   -979       C  
ATOM   3510  NE  ARG B 345      -9.999 -64.484  51.410  1.00 73.71           N  
ANISOU 3510  NE  ARG B 345     6795  10033  11176     64    837   -935       N  
ATOM   3511  CZ  ARG B 345     -10.296 -65.473  52.255  1.00 75.06           C  
ANISOU 3511  CZ  ARG B 345     6972  10436  11108   -176   1225   -937       C  
ATOM   3512  NH1 ARG B 345     -11.456 -66.129  52.170  1.00 78.43           N1+
ANISOU 3512  NH1 ARG B 345     7036  11107  11655   -364   1445  -1007       N1+
ATOM   3513  NH2 ARG B 345      -9.426 -65.814  53.187  1.00 72.96           N  
ANISOU 3513  NH2 ARG B 345     7066  10167  10486   -242   1386   -845       N  
ATOM   3514  N   ARG B 346     -12.084 -64.383  44.897  1.00 79.10           N  
ANISOU 3514  N   ARG B 346     6651  10924  12478    202   -799   -429       N  
ATOM   3515  CA  ARG B 346     -13.086 -64.201  43.866  1.00 83.91           C  
ANISOU 3515  CA  ARG B 346     6879  11794  13207    334  -1179   -456       C  
ATOM   3516  C   ARG B 346     -12.447 -64.326  42.477  1.00 83.59           C  
ANISOU 3516  C   ARG B 346     7144  11756  12860    295  -1518   -173       C  
ATOM   3517  O   ARG B 346     -11.332 -63.854  42.242  1.00 81.53           O  
ANISOU 3517  O   ARG B 346     7313  11225  12439    368  -1545    114       O  
ATOM   3518  CB  ARG B 346     -13.793 -62.855  44.051  1.00 87.41           C  
ANISOU 3518  CB  ARG B 346     7009  12189  14012    820  -1377   -498       C  
ATOM   3519  CG  ARG B 346     -15.326 -62.944  44.156  1.00 94.88           C  
ANISOU 3519  CG  ARG B 346     7254  13527  15266    915  -1426   -814       C  
ATOM   3520  CD  ARG B 346     -16.040 -63.118  42.767  1.00 99.67           C  
ANISOU 3520  CD  ARG B 346     7561  14468  15838    959  -1944   -748       C  
ATOM   3521  NE  ARG B 346     -17.496 -63.013  42.801  1.00104.78           N  
ANISOU 3521  NE  ARG B 346     7452  15510  16846   1124  -2081  -1043       N  
ATOM   3522  CZ  ARG B 346     -18.192 -62.056  43.428  1.00110.61           C  
ANISOU 3522  CZ  ARG B 346     7795  16231  18000   1571  -2054  -1195       C  
ATOM   3523  NH1 ARG B 346     -17.574 -61.114  44.134  1.00107.85           N1+
ANISOU 3523  NH1 ARG B 346     7775  15445  17756   1872  -1887  -1118       N1+
ATOM   3524  NH2 ARG B 346     -19.532 -62.047  43.370  1.00117.47           N  
ANISOU 3524  NH2 ARG B 346     7890  17531  19211   1720  -2189  -1480       N  
ATOM   3525  N   ALA B 347     -13.145 -64.997  41.569  1.00 87.01           N  
ANISOU 3525  N   ALA B 347     7337  12529  13190    148  -1755   -284       N  
ATOM   3526  CA  ALA B 347     -12.679 -65.174  40.204  1.00 88.25           C  
ANISOU 3526  CA  ALA B 347     7756  12804  12971    115  -2078    -83       C  
ATOM   3527  C   ALA B 347     -12.533 -63.808  39.546  1.00 91.20           C  
ANISOU 3527  C   ALA B 347     8231  13085  13335    552  -2449    302       C  
ATOM   3528  O   ALA B 347     -13.412 -62.959  39.705  1.00 95.29           O  
ANISOU 3528  O   ALA B 347     8390  13635  14179    895  -2664    292       O  
ATOM   3529  CB  ALA B 347     -13.661 -66.045  39.428  1.00 91.79           C  
ANISOU 3529  CB  ALA B 347     7845  13687  13341    -97  -2326   -372       C  
ATOM   3530  N   PRO B 348     -11.418 -63.571  38.832  1.00 90.23           N  
ANISOU 3530  N   PRO B 348     8587  12823  12871    553  -2496    660       N  
ATOM   3531  CA  PRO B 348     -11.243 -62.316  38.083  1.00 93.87           C  
ANISOU 3531  CA  PRO B 348     9203  13170  13291    915  -2836   1123       C  
ATOM   3532  C   PRO B 348     -12.206 -62.255  36.907  1.00100.60           C  
ANISOU 3532  C   PRO B 348     9809  14473  13940   1096  -3358   1190       C  
ATOM   3533  O   PRO B 348     -12.730 -63.292  36.496  1.00102.02           O  
ANISOU 3533  O   PRO B 348     9786  15067  13909    855  -3445    861       O  
ATOM   3534  CB  PRO B 348      -9.813 -62.410  37.572  1.00 91.14           C  
ANISOU 3534  CB  PRO B 348     9384  12682  12559    738  -2664   1438       C  
ATOM   3535  CG  PRO B 348      -9.133 -63.404  38.522  1.00 85.93           C  
ANISOU 3535  CG  PRO B 348     8829  11892  11928    399  -2191   1130       C  
ATOM   3536  CD  PRO B 348     -10.201 -64.393  38.831  1.00 85.97           C  
ANISOU 3536  CD  PRO B 348     8463  12172  12028    235  -2174    677       C  
ATOM   3537  N   PHE B 349     -12.466 -61.060  36.383  1.00105.76           N  
ANISOU 3537  N   PHE B 349    10473  15035  14675   1520  -3732   1602       N  
ATOM   3538  CA  PHE B 349     -13.266 -60.947  35.168  1.00112.86           C  
ANISOU 3538  CA  PHE B 349    11195  16405  15280   1739  -4299   1759       C  
ATOM   3539  C   PHE B 349     -12.369 -60.812  33.937  1.00114.67           C  
ANISOU 3539  C   PHE B 349    11952  16753  14863   1699  -4430   2259       C  
ATOM   3540  O   PHE B 349     -12.810 -60.778  32.777  1.00120.75           O  
ANISOU 3540  O   PHE B 349    12709  17983  15185   1848  -4897   2456       O  
ATOM   3541  CB  PHE B 349     -14.258 -59.794  35.243  1.00118.64           C  
ANISOU 3541  CB  PHE B 349    11571  17039  16467   2295  -4699   1933       C  
ATOM   3542  CG  PHE B 349     -14.948 -59.527  33.940  1.00127.60           C  
ANISOU 3542  CG  PHE B 349    12587  18645  17250   2598  -5353   2227       C  
ATOM   3543  CD1 PHE B 349     -14.766 -58.318  33.277  1.00133.31           C  
ANISOU 3543  CD1 PHE B 349    13603  19129  17919   3038  -5691   2912       C  
ATOM   3544  CD2 PHE B 349     -15.741 -60.512  33.343  1.00131.75           C  
ANISOU 3544  CD2 PHE B 349    12737  19855  17467   2417  -5647   1833       C  
ATOM   3545  CE1 PHE B 349     -15.391 -58.073  32.055  1.00141.80           C  
ANISOU 3545  CE1 PHE B 349    14605  20687  18585   3352  -6336   3250       C  
ATOM   3546  CE2 PHE B 349     -16.368 -60.282  32.119  1.00140.27           C  
ANISOU 3546  CE2 PHE B 349    13702  21454  18140   2704  -6314   2082       C  
ATOM   3547  CZ  PHE B 349     -16.195 -59.057  31.474  1.00145.33           C  
ANISOU 3547  CZ  PHE B 349    14648  21900  18670   3198  -6669   2817       C  
ATOM   3548  N   ASN B 359      -2.246 -63.026  31.716  1.00114.32           N  
ANISOU 3548  N   ASN B 359    12464  16378  14593  -1099  -3258   4351       N  
ATOM   3549  CA  ASN B 359      -1.187 -63.534  32.637  1.00106.69           C  
ANISOU 3549  CA  ASN B 359    11803  15249  13484   -814  -2376   3630       C  
ATOM   3550  C   ASN B 359      -0.662 -62.418  33.534  1.00104.51           C  
ANISOU 3550  C   ASN B 359    11449  14250  14008   -399  -2372   3765       C  
ATOM   3551  O   ASN B 359      -0.434 -61.312  33.047  1.00109.60           O  
ANISOU 3551  O   ASN B 359    12035  14685  14922   -538  -2897   4494       O  
ATOM   3552  CB  ASN B 359      -0.034 -64.136  31.827  1.00107.23           C  
ANISOU 3552  CB  ASN B 359    12264  15979  12497  -1378  -1972   3518       C  
ATOM   3553  CG  ASN B 359       1.146 -64.604  32.706  1.00102.58           C  
ANISOU 3553  CG  ASN B 359    11846  15137  11990  -1073  -1229   2939       C  
ATOM   3554  OD1 ASN B 359       1.268 -65.793  33.003  1.00100.83           O  
ANISOU 3554  OD1 ASN B 359    11655  14986  11668  -1005   -693   2301       O  
ATOM   3555  ND2 ASN B 359       2.026 -63.667  33.101  1.00102.89           N  
ANISOU 3555  ND2 ASN B 359    11949  14844  12298   -930  -1263   3228       N  
ATOM   3556  N   ASN B 360      -0.465 -62.712  34.825  1.00 98.08           N  
ANISOU 3556  N   ASN B 360    10643  13093  13529    -14  -1803   3097       N  
ATOM   3557  CA  ASN B 360       0.104 -61.733  35.775  1.00 96.53           C  
ANISOU 3557  CA  ASN B 360    10387  12335  13955    227  -1665   3032       C  
ATOM   3558  C   ASN B 360       0.861 -62.313  36.988  1.00 90.47           C  
ANISOU 3558  C   ASN B 360     9831  11580  12961    309  -1030   2440       C  
ATOM   3559  O   ASN B 360       0.583 -62.016  38.160  1.00 89.97           O  
ANISOU 3559  O   ASN B 360     9616  11201  13366    416   -781   1986       O  
ATOM   3560  CB  ASN B 360      -0.933 -60.687  36.204  1.00101.32           C  
ANISOU 3560  CB  ASN B 360    10454  12245  15796    499  -1977   3019       C  
ATOM   3561  CG  ASN B 360      -2.299 -61.281  36.420  1.00102.80           C  
ANISOU 3561  CG  ASN B 360    10286  12434  16339    627  -1969   2578       C  
ATOM   3562  OD1 ASN B 360      -2.441 -62.442  36.839  1.00 98.16           O  
ANISOU 3562  OD1 ASN B 360     9905  12235  15155    563  -1515   2049       O  
ATOM   3563  ND2 ASN B 360      -3.326 -60.495  36.119  1.00110.06           N  
ANISOU 3563  ND2 ASN B 360    10602  12855  18359    793  -2514   2836       N  
ATOM   3564  N   ILE B 361       1.827 -63.160  36.675  1.00 86.93           N  
ANISOU 3564  N   ILE B 361     9679  11526  11823    153   -786   2443       N  
ATOM   3565  CA  ILE B 361       2.826 -63.565  37.616  1.00 82.80           C  
ANISOU 3565  CA  ILE B 361     9299  10985  11174    176   -422   2207       C  
ATOM   3566  C   ILE B 361       3.965 -62.575  37.399  1.00 83.18           C  
ANISOU 3566  C   ILE B 361     9408  10960  11234     92   -497   2533       C  
ATOM   3567  O   ILE B 361       4.310 -62.278  36.257  1.00 85.86           O  
ANISOU 3567  O   ILE B 361     9812  11499  11308   -107   -662   2890       O  
ATOM   3568  CB  ILE B 361       3.278 -64.993  37.294  1.00 81.71           C  
ANISOU 3568  CB  ILE B 361     9267  11130  10648     99   -156   2037       C  
ATOM   3569  CG1 ILE B 361       2.074 -65.965  37.275  1.00 81.75           C  
ANISOU 3569  CG1 ILE B 361     9223  11209  10626    111    -93   1743       C  
ATOM   3570  CG2 ILE B 361       4.387 -65.454  38.242  1.00 80.63           C  
ANISOU 3570  CG2 ILE B 361     9163  10886  10586    128     38   1993       C  
ATOM   3571  CD1 ILE B 361       1.131 -65.891  38.477  1.00 81.43           C  
ANISOU 3571  CD1 ILE B 361     9105  10959  10873    181    -59   1486       C  
ATOM   3572  N   LYS B 362       4.523 -62.033  38.478  1.00 81.45           N  
ANISOU 3572  N   LYS B 362     9175  10529  11241    109   -371   2401       N  
ATOM   3573  CA  LYS B 362       5.624 -61.074  38.362  1.00 81.66           C  
ANISOU 3573  CA  LYS B 362     9239  10471  11317     -1   -406   2652       C  
ATOM   3574  C   LYS B 362       6.921 -61.861  38.274  1.00 79.26           C  
ANISOU 3574  C   LYS B 362     9006  10472  10635    -91   -208   2661       C  
ATOM   3575  O   LYS B 362       7.200 -62.704  39.130  1.00 77.71           O  
ANISOU 3575  O   LYS B 362     8778  10333  10414    -57    -92   2487       O  
ATOM   3576  CB  LYS B 362       5.661 -60.088  39.548  1.00 82.79           C  
ANISOU 3576  CB  LYS B 362     9271  10279  11904    -49   -310   2387       C  
ATOM   3577  CG  LYS B 362       4.352 -59.325  39.829  1.00 87.11           C  
ANISOU 3577  CG  LYS B 362     9543  10360  13192     53   -363   2115       C  
ATOM   3578  CD  LYS B 362       4.331 -57.923  39.210  1.00 94.73           C  
ANISOU 3578  CD  LYS B 362    10322  10772  14898     98   -650   2479       C  
ATOM   3579  CE  LYS B 362       2.911 -57.274  39.186  1.00100.20           C  
ANISOU 3579  CE  LYS B 362    10542  10828  16700    308   -843   2326       C  
ATOM   3580  NZ  LYS B 362       1.912 -58.004  38.324  1.00 99.91           N1+
ANISOU 3580  NZ  LYS B 362    10438  10987  16535    458  -1210   2639       N1+
ATOM   3581  N   LEU B 363       7.706 -61.605  37.234  1.00 80.03           N  
ANISOU 3581  N   LEU B 363     9141  10751  10513   -276   -192   2886       N  
ATOM   3582  CA  LEU B 363       8.956 -62.330  37.051  1.00 79.34           C  
ANISOU 3582  CA  LEU B 363     8953  10888  10305   -367     83   2740       C  
ATOM   3583  C   LEU B 363      10.192 -61.553  37.514  1.00 79.91           C  
ANISOU 3583  C   LEU B 363     8948  10903  10509   -473    112   2835       C  
ATOM   3584  O   LEU B 363      10.384 -60.376  37.161  1.00 81.57           O  
ANISOU 3584  O   LEU B 363     9260  11047  10686   -666     16   3078       O  
ATOM   3585  CB  LEU B 363       9.112 -62.823  35.606  1.00 82.13           C  
ANISOU 3585  CB  LEU B 363     9310  11623  10272   -677    293   2643       C  
ATOM   3586  CG  LEU B 363      10.366 -63.610  35.190  1.00 83.70           C  
ANISOU 3586  CG  LEU B 363     9239  12010  10553   -842    752   2239       C  
ATOM   3587  CD1 LEU B 363      10.674 -64.756  36.126  1.00 81.71           C  
ANISOU 3587  CD1 LEU B 363     8683  11440  10921   -462    840   1994       C  
ATOM   3588  CD2 LEU B 363      10.237 -64.112  33.755  1.00 87.94           C  
ANISOU 3588  CD2 LEU B 363     9784  13035  10592  -1354   1095   1912       C  
ATOM   3589  N   TYR B 364      11.014 -62.251  38.304  1.00 78.83           N  
ANISOU 3589  N   TYR B 364     8591  10760  10600   -380    180   2709       N  
ATOM   3590  CA  TYR B 364      12.276 -61.754  38.831  1.00 79.44           C  
ANISOU 3590  CA  TYR B 364     8490  10855  10839   -503    167   2776       C  
ATOM   3591  C   TYR B 364      13.416 -62.705  38.503  1.00 82.03           C  
ANISOU 3591  C   TYR B 364     8395  11244  11526   -472    357   2615       C  
ATOM   3592  O   TYR B 364      13.198 -63.925  38.406  1.00 82.55           O  
ANISOU 3592  O   TYR B 364     8270  11200  11894   -286    428   2463       O  
ATOM   3593  CB  TYR B 364      12.183 -61.704  40.333  1.00 78.24           C  
ANISOU 3593  CB  TYR B 364     8333  10647  10748   -523    -82   2855       C  
ATOM   3594  CG  TYR B 364      11.379 -60.576  40.873  1.00 78.04           C  
ANISOU 3594  CG  TYR B 364     8539  10509  10603   -661   -113   2767       C  
ATOM   3595  CD1 TYR B 364       9.985 -60.611  40.875  1.00 76.42           C  
ANISOU 3595  CD1 TYR B 364     8481  10157  10397   -545   -105   2625       C  
ATOM   3596  CD2 TYR B 364      12.008 -59.477  41.433  1.00 80.22           C  
ANISOU 3596  CD2 TYR B 364     8790  10774  10913   -937   -104   2719       C  
ATOM   3597  CE1 TYR B 364       9.260 -59.566  41.396  1.00 75.92           C  
ANISOU 3597  CE1 TYR B 364     8453   9862  10531   -663    -54   2384       C  
ATOM   3598  CE2 TYR B 364      11.280 -58.438  41.961  1.00 79.90           C  
ANISOU 3598  CE2 TYR B 364     8841  10508  11008  -1096    -18   2453       C  
ATOM   3599  CZ  TYR B 364       9.919 -58.494  41.939  1.00 78.06           C  
ANISOU 3599  CZ  TYR B 364     8671  10056  10932   -940     20   2262       C  
ATOM   3600  OH  TYR B 364       9.231 -57.448  42.463  1.00 82.64           O  
ANISOU 3600  OH  TYR B 364     9174  10292  11933  -1091    185   1850       O  
ATOM   3601  N   VAL B 365      14.623 -62.142  38.366  1.00 84.12           N  
ANISOU 3601  N   VAL B 365     8438  11606  11916   -662    463   2592       N  
ATOM   3602  CA  VAL B 365      15.883 -62.894  38.289  1.00 87.93           C  
ANISOU 3602  CA  VAL B 365     8314  12052  13041   -624    618   2381       C  
ATOM   3603  C   VAL B 365      16.849 -62.346  39.329  1.00 89.69           C  
ANISOU 3603  C   VAL B 365     8301  12287  13487   -707    287   2651       C  
ATOM   3604  O   VAL B 365      17.029 -61.140  39.405  1.00 89.61           O  
ANISOU 3604  O   VAL B 365     8542  12423  13080   -969    293   2726       O  
ATOM   3605  CB  VAL B 365      16.549 -62.757  36.891  1.00 91.65           C  
ANISOU 3605  CB  VAL B 365     8617  12770  13436   -960   1204   1915       C  
ATOM   3606  CG1 VAL B 365      18.016 -63.187  36.926  1.00 95.79           C  
ANISOU 3606  CG1 VAL B 365     8375  13215  14806   -969   1423   1582       C  
ATOM   3607  CG2 VAL B 365      15.772 -63.543  35.839  1.00 92.27           C  
ANISOU 3607  CG2 VAL B 365     8796  12965  13296  -1050   1575   1530       C  
ATOM   3608  N   ARG B 366      17.496 -63.220  40.101  1.00 93.04           N  
ANISOU 3608  N   ARG B 366     8196  12538  14616   -543    -46   2841       N  
ATOM   3609  CA  ARG B 366      18.424 -62.813  41.190  1.00 95.95           C  
ANISOU 3609  CA  ARG B 366     8276  13024  15156   -735   -522   3214       C  
ATOM   3610  C   ARG B 366      17.895 -61.618  41.975  1.00 92.76           C  
ANISOU 3610  C   ARG B 366     8450  12902  13891  -1087   -684   3364       C  
ATOM   3611  O   ARG B 366      18.632 -60.677  42.272  1.00 94.25           O  
ANISOU 3611  O   ARG B 366     8580  13294  13936  -1402   -706   3348       O  
ATOM   3612  CB  ARG B 366      19.860 -62.565  40.697  1.00100.79           C  
ANISOU 3612  CB  ARG B 366     8267  13678  16350   -827   -295   2953       C  
ATOM   3613  CG  ARG B 366      20.756 -63.820  40.698  1.00108.84           C  
ANISOU 3613  CG  ARG B 366     8324  14308  18722   -531   -444   2936       C  
ATOM   3614  CD  ARG B 366      22.215 -63.555  41.166  1.00116.90           C  
ANISOU 3614  CD  ARG B 366     8579  15387  20449   -672   -755   3081       C  
ATOM   3615  NE  ARG B 366      22.862 -62.457  40.437  1.00118.77           N  
ANISOU 3615  NE  ARG B 366     8882  15965  20278  -1008   -166   2562       N  
ATOM   3616  CZ  ARG B 366      24.129 -62.055  40.603  1.00124.77           C  
ANISOU 3616  CZ  ARG B 366     9007  16851  21545  -1207   -232   2487       C  
ATOM   3617  NH1 ARG B 366      24.930 -62.661  41.475  1.00131.81           N1+
ANISOU 3617  NH1 ARG B 366     9065  17552  23463  -1074   -952   2954       N1+
ATOM   3618  NH2 ARG B 366      24.602 -61.036  39.887  1.00123.62           N  
ANISOU 3618  NH2 ARG B 366     9033  17025  20913  -1600    362   2019       N  
ATOM   3619  N   ARG B 367      16.595 -61.684  42.272  1.00 89.09           N  
ANISOU 3619  N   ARG B 367     8475  12409  12967  -1059   -715   3389       N  
ATOM   3620  CA  ARG B 367      15.846 -60.693  43.052  1.00 87.35           C  
ANISOU 3620  CA  ARG B 367     8707  12346  12133  -1400   -737   3312       C  
ATOM   3621  C   ARG B 367      15.747 -59.346  42.333  1.00 85.92           C  
ANISOU 3621  C   ARG B 367     8774  12053  11817  -1474   -354   3022       C  
ATOM   3622  O   ARG B 367      15.622 -58.288  42.938  1.00 87.05           O  
ANISOU 3622  O   ARG B 367     9077  12220  11778  -1809   -300   2850       O  
ATOM   3623  CB  ARG B 367      16.381 -60.589  44.486  1.00 91.26           C  
ANISOU 3623  CB  ARG B 367     9072  13210  12393  -1927  -1182   3566       C  
ATOM   3624  CG  ARG B 367      16.314 -61.891  45.266  1.00 95.28           C  
ANISOU 3624  CG  ARG B 367     9398  13801  13002  -1991  -1734   4098       C  
ATOM   3625  CD  ARG B 367      17.076 -61.746  46.580  1.00107.40           C  
ANISOU 3625  CD  ARG B 367    10745  15842  14218  -2702  -2323   4530       C  
ATOM   3626  NE  ARG B 367      17.713 -62.963  47.131  1.00117.30           N  
ANISOU 3626  NE  ARG B 367    11518  17081  15966  -2756  -3124   5379       N  
ATOM   3627  CZ  ARG B 367      17.748 -64.169  46.554  1.00120.12           C  
ANISOU 3627  CZ  ARG B 367    11519  16876  17244  -2153  -3274   5674       C  
ATOM   3628  NH1 ARG B 367      17.174 -64.382  45.358  1.00114.93           N1+
ANISOU 3628  NH1 ARG B 367    10980  15773  16913  -1518  -2617   5114       N1+
ATOM   3629  NH2 ARG B 367      18.358 -65.175  47.188  1.00127.34           N  
ANISOU 3629  NH2 ARG B 367    11907  17657  18818  -2264  -4125   6559       N  
ATOM   3630  N   VAL B 368      15.772 -59.400  41.012  1.00 84.94           N  
ANISOU 3630  N   VAL B 368     8665  11794  11811  -1255    -84   2966       N  
ATOM   3631  CA  VAL B 368      15.620 -58.196  40.205  1.00 84.90           C  
ANISOU 3631  CA  VAL B 368     8918  11649  11690  -1407    138   2929       C  
ATOM   3632  C   VAL B 368      14.431 -58.337  39.232  1.00 82.95           C  
ANISOU 3632  C   VAL B 368     8955  11247  11314  -1227    193   3000       C  
ATOM   3633  O   VAL B 368      14.296 -59.328  38.510  1.00 82.03           O  
ANISOU 3633  O   VAL B 368     8773  11268  11125  -1089    294   2952       O  
ATOM   3634  CB  VAL B 368      16.987 -57.802  39.563  1.00 88.14           C  
ANISOU 3634  CB  VAL B 368     9090  12218  12180  -1661    341   2905       C  
ATOM   3635  CG1 VAL B 368      16.837 -57.242  38.170  1.00 90.66           C  
ANISOU 3635  CG1 VAL B 368     9655  12519  12271  -1872    577   3002       C  
ATOM   3636  CG2 VAL B 368      17.721 -56.832  40.461  1.00 89.66           C  
ANISOU 3636  CG2 VAL B 368     9196  12442  12426  -1982    264   2867       C  
ATOM   3637  N   PHE B 369      13.540 -57.353  39.278  1.00 83.39           N  
ANISOU 3637  N   PHE B 369     9246  10979  11456  -1260    110   3076       N  
ATOM   3638  CA  PHE B 369      12.310 -57.366  38.486  1.00 83.15           C  
ANISOU 3638  CA  PHE B 369     9401  10764  11425  -1112     -6   3257       C  
ATOM   3639  C   PHE B 369      12.635 -57.388  37.002  1.00 86.13           C  
ANISOU 3639  C   PHE B 369     9882  11382  11459  -1369     31   3561       C  
ATOM   3640  O   PHE B 369      13.555 -56.721  36.570  1.00 88.93           O  
ANISOU 3640  O   PHE B 369    10249  11816  11724  -1723    130   3703       O  
ATOM   3641  CB  PHE B 369      11.404 -56.182  38.850  1.00 84.30           C  
ANISOU 3641  CB  PHE B 369     9586  10348  12093  -1094   -146   3284       C  
ATOM   3642  CG  PHE B 369      10.156 -56.102  38.019  1.00 85.86           C  
ANISOU 3642  CG  PHE B 369     9845  10288  12489   -942   -421   3605       C  
ATOM   3643  CD1 PHE B 369       9.148 -57.051  38.145  1.00 83.43           C  
ANISOU 3643  CD1 PHE B 369     9512  10097  12090   -675   -457   3419       C  
ATOM   3644  CD2 PHE B 369       9.983 -55.082  37.090  1.00 90.52           C  
ANISOU 3644  CD2 PHE B 369    10490  10521  13381  -1134   -729   4193       C  
ATOM   3645  CE1 PHE B 369       7.990 -56.972  37.355  1.00 83.98           C  
ANISOU 3645  CE1 PHE B 369     9565   9977  12367   -574   -786   3745       C  
ATOM   3646  CE2 PHE B 369       8.836 -55.014  36.307  1.00 91.30           C  
ANISOU 3646  CE2 PHE B 369    10572  10412  13704  -1061  -1162   4660       C  
ATOM   3647  CZ  PHE B 369       7.848 -55.960  36.445  1.00 87.77           C  
ANISOU 3647  CZ  PHE B 369    10054  10134  13159   -767  -1181   4397       C  
ATOM   3648  N   ILE B 370      11.895 -58.185  36.242  1.00 86.93           N  
ANISOU 3648  N   ILE B 370    10058  11690  11281  -1321     -5   3603       N  
ATOM   3649  CA  ILE B 370      12.082 -58.274  34.805  1.00 92.33           C  
ANISOU 3649  CA  ILE B 370    10867  12790  11422  -1804     65   3814       C  
ATOM   3650  C   ILE B 370      10.832 -57.779  34.103  1.00 96.48           C  
ANISOU 3650  C   ILE B 370    11599  13192  11865  -1928   -410   4379       C  
ATOM   3651  O   ILE B 370      10.876 -56.809  33.349  1.00102.10           O  
ANISOU 3651  O   ILE B 370    12475  13866  12453  -2390   -710   5002       O  
ATOM   3652  CB  ILE B 370      12.397 -59.723  34.338  1.00 91.88           C  
ANISOU 3652  CB  ILE B 370    10635  13199  11076  -1854    487   3280       C  
ATOM   3653  CG1 ILE B 370      13.562 -60.326  35.138  1.00 91.29           C  
ANISOU 3653  CG1 ILE B 370    10175  13070  11440  -1615    801   2819       C  
ATOM   3654  CG2 ILE B 370      12.657 -59.786  32.820  1.00 97.07           C  
ANISOU 3654  CG2 ILE B 370    11408  14469  11003  -2630    722   3288       C  
ATOM   3655  CD1 ILE B 370      14.936 -59.595  34.996  1.00 94.91           C  
ANISOU 3655  CD1 ILE B 370    10486  13654  11921  -1980   1018   2787       C  
ATOM   3656  N   MET B 371       9.714 -58.446  34.362  1.00 95.57           N  
ANISOU 3656  N   MET B 371    11436  12990  11884  -1557   -547   4238       N  
ATOM   3657  CA  MET B 371       8.482 -58.201  33.629  1.00100.69           C  
ANISOU 3657  CA  MET B 371    12159  13597  12500  -1673  -1052   4753       C  
ATOM   3658  C   MET B 371       7.328 -58.904  34.314  1.00 98.08           C  
ANISOU 3658  C   MET B 371    11677  13060  12527  -1146  -1094   4398       C  
ATOM   3659  O   MET B 371       7.507 -59.538  35.346  1.00 93.29           O  
ANISOU 3659  O   MET B 371    10980  12367  12099   -787   -750   3835       O  
ATOM   3660  CB  MET B 371       8.609 -58.715  32.191  1.00105.34           C  
ANISOU 3660  CB  MET B 371    12923  14971  12128  -2398  -1024   4935       C  
ATOM   3661  CG  MET B 371       8.990 -60.191  32.091  1.00102.74           C  
ANISOU 3661  CG  MET B 371    12502  15147  11384  -2412   -380   4093       C  
ATOM   3662  SD  MET B 371       8.597 -60.899  30.487  1.00111.07           S  
ANISOU 3662  SD  MET B 371    13699  17147  11355  -3341   -301   4055       S  
ATOM   3663  CE  MET B 371       9.695 -60.018  29.357  1.00119.64           C  
ANISOU 3663  CE  MET B 371    15010  18841  11606  -4470   -219   4464       C  
ATOM   3664  N   ASP B 372       6.143 -58.788  33.723  1.00103.30           N  
ANISOU 3664  N   ASP B 372    12292  13679  13277  -1193  -1576   4801       N  
ATOM   3665  CA  ASP B 372       4.979 -59.570  34.142  1.00102.48           C  
ANISOU 3665  CA  ASP B 372    12027  13513  13395   -819  -1587   4433       C  
ATOM   3666  C   ASP B 372       3.961 -59.786  33.008  1.00108.08           C  
ANISOU 3666  C   ASP B 372    12713  14569  13782  -1139  -2093   4899       C  
ATOM   3667  O   ASP B 372       2.887 -60.374  33.226  1.00107.39           O  
ANISOU 3667  O   ASP B 372    12447  14447  13906   -883  -2166   4641       O  
ATOM   3668  CB  ASP B 372       4.319 -58.981  35.410  1.00101.48           C  
ANISOU 3668  CB  ASP B 372    11622  12656  14280   -311  -1600   4140       C  
ATOM   3669  CG  ASP B 372       4.060 -57.484  35.309  1.00108.75           C  
ANISOU 3669  CG  ASP B 372    12319  12874  16126   -295  -2069   4676       C  
ATOM   3670  OD1 ASP B 372       4.749 -56.710  36.018  1.00109.07           O  
ANISOU 3670  OD1 ASP B 372    12328  12515  16597   -248  -1842   4492       O  
ATOM   3671  OD2 ASP B 372       3.163 -57.085  34.528  1.00117.28           O1-
ANISOU 3671  OD2 ASP B 372    13202  13759  17598   -362  -2709   5307       O1-
ATOM   3672  N   ASN B 373       4.301 -59.332  31.802  1.00114.88           N  
ANISOU 3672  N   ASN B 373    13755  15850  14043  -1820  -2457   5599       N  
ATOM   3673  CA  ASN B 373       3.505 -59.702  30.632  1.00121.75           C  
ANISOU 3673  CA  ASN B 373    14659  17345  14253  -2400  -2930   6044       C  
ATOM   3674  C   ASN B 373       3.708 -61.174  30.215  1.00119.55           C  
ANISOU 3674  C   ASN B 373    14522  17888  13013  -2736  -2262   5222       C  
ATOM   3675  O   ASN B 373       3.026 -61.661  29.316  1.00124.97           O  
ANISOU 3675  O   ASN B 373    15230  19210  13043  -3294  -2512   5356       O  
ATOM   3676  CB  ASN B 373       3.614 -58.692  29.433  1.00132.44           C  
ANISOU 3676  CB  ASN B 373    16161  18974  15183  -3263  -3722   7261       C  
ATOM   3677  CG  ASN B 373       5.074 -58.303  29.042  1.00134.86           C  
ANISOU 3677  CG  ASN B 373    16805  19633  14801  -3880  -3323   7324       C  
ATOM   3678  OD1 ASN B 373       6.048 -58.640  29.727  1.00130.47           O  
ANISOU 3678  OD1 ASN B 373    16281  18982  14306  -3543  -2521   6501       O  
ATOM   3679  ND2 ASN B 373       5.205 -57.575  27.930  1.00143.34           N  
ANISOU 3679  ND2 ASN B 373    18092  21133  15236  -4868  -3958   8385       N  
ATOM   3680  N   CYS B 374       4.590 -61.882  30.920  1.00113.09           N  
ANISOU 3680  N   CYS B 374    13720  16980  12268  -2397  -1458   4371       N  
ATOM   3681  CA  CYS B 374       5.109 -63.171  30.468  1.00112.88           C  
ANISOU 3681  CA  CYS B 374    13721  17544  11623  -2758   -728   3545       C  
ATOM   3682  C   CYS B 374       4.062 -64.256  30.363  1.00112.01           C  
ANISOU 3682  C   CYS B 374    13510  17630  11420  -2703   -650   3106       C  
ATOM   3683  O   CYS B 374       3.883 -65.066  31.281  1.00106.74           O  
ANISOU 3683  O   CYS B 374    12707  16540  11308  -2091   -308   2551       O  
ATOM   3684  CB  CYS B 374       6.266 -63.645  31.354  1.00107.83           C  
ANISOU 3684  CB  CYS B 374    12964  16542  11463  -2300    -59   2892       C  
ATOM   3685  SG  CYS B 374       7.526 -64.529  30.381  1.00113.96           S  
ANISOU 3685  SG  CYS B 374    13640  17976  11683  -3052    826   2053       S  
ATOM   3686  N   GLU B 375       3.375 -64.278  29.230  1.00118.53           N  
ANISOU 3686  N   GLU B 375    14407  19147  11482  -3457  -1014   3416       N  
ATOM   3687  CA  GLU B 375       2.391 -65.318  28.978  1.00118.98           C  
ANISOU 3687  CA  GLU B 375    14359  19520  11328  -3571   -919   2949       C  
ATOM   3688  C   GLU B 375       3.144 -66.473  28.333  1.00120.66           C  
ANISOU 3688  C   GLU B 375    14577  20318  10947  -4205     20   1917       C  
ATOM   3689  O   GLU B 375       3.333 -66.531  27.111  1.00129.00           O  
ANISOU 3689  O   GLU B 375    15750  22311  10951  -5329    141   1826       O  
ATOM   3690  CB  GLU B 375       1.193 -64.810  28.142  1.00126.62           C  
ANISOU 3690  CB  GLU B 375    15300  20954  11855  -4105  -1858   3790       C  
ATOM   3691  CG  GLU B 375      -0.163 -65.491  28.518  1.00126.46           C  
ANISOU 3691  CG  GLU B 375    15024  20767  12255  -3684  -2032   3519       C  
ATOM   3692  CD  GLU B 375      -1.412 -64.619  28.252  1.00133.61           C  
ANISOU 3692  CD  GLU B 375    15667  21588  13509  -3688  -3190   4549       C  
ATOM   3693  OE1 GLU B 375      -1.652 -64.237  27.080  1.00142.95           O  
ANISOU 3693  OE1 GLU B 375    16908  23527  13879  -4640  -3885   5330       O  
ATOM   3694  OE2 GLU B 375      -2.163 -64.336  29.222  1.00129.76           O1-
ANISOU 3694  OE2 GLU B 375    14855  20288  14160  -2816  -3414   4564       O1-
ATOM   3695  N   GLU B 376       3.613 -67.349  29.211  1.00113.33           N  
ANISOU 3695  N   GLU B 376    13473  18788  10796  -3536    681   1147       N  
ATOM   3696  CA  GLU B 376       4.410 -68.522  28.894  1.00114.48           C  
ANISOU 3696  CA  GLU B 376    13417  19063  11018  -3844   1654     36       C  
ATOM   3697  C   GLU B 376       4.662 -69.202  30.223  1.00106.36           C  
ANISOU 3697  C   GLU B 376    12170  17050  11191  -2838   1894   -247       C  
ATOM   3698  O   GLU B 376       4.969 -70.393  30.279  1.00107.99           O  
ANISOU 3698  O   GLU B 376    12090  16987  11952  -2795   2548  -1081       O  
ATOM   3699  CB  GLU B 376       5.736 -68.146  28.232  1.00119.57           C  
ANISOU 3699  CB  GLU B 376    14040  20109  11281  -4488   2124   -216       C  
ATOM   3700  CG  GLU B 376       5.801 -68.549  26.783  1.00130.67           C  
ANISOU 3700  CG  GLU B 376    15462  22612  11573  -5852   2642   -881       C  
ATOM   3701  CD  GLU B 376       6.375 -67.459  25.904  1.00139.39           C  
ANISOU 3701  CD  GLU B 376    16840  24511  11609  -6847   2422   -317       C  
ATOM   3702  OE1 GLU B 376       7.593 -67.166  25.995  1.00140.93           O  
ANISOU 3702  OE1 GLU B 376    16918  24565  12062  -6877   2888   -584       O  
ATOM   3703  OE2 GLU B 376       5.603 -66.895  25.103  1.00145.89           O1-
ANISOU 3703  OE2 GLU B 376    17971  26116  11342  -7676   1725    461       O1-
ATOM   3704  N   LEU B 377       4.523 -68.422  31.290  1.00 98.31           N  
ANISOU 3704  N   LEU B 377    11255  15488  10609  -2130   1340    470       N  
ATOM   3705  CA  LEU B 377       4.687 -68.924  32.634  1.00 91.55           C  
ANISOU 3705  CA  LEU B 377    10269  13855  10658  -1375   1395    419       C  
ATOM   3706  C   LEU B 377       3.550 -69.855  33.102  1.00 88.82           C  
ANISOU 3706  C   LEU B 377     9899  13278  10570  -1147   1381    204       C  
ATOM   3707  O   LEU B 377       3.833 -70.880  33.703  1.00 88.68           O  
ANISOU 3707  O   LEU B 377     9703  12766  11225   -890   1691   -124       O  
ATOM   3708  CB  LEU B 377       4.902 -67.768  33.611  1.00 87.24           C  
ANISOU 3708  CB  LEU B 377     9847  12964  10335   -933    913   1098       C  
ATOM   3709  CG  LEU B 377       6.296 -67.140  33.664  1.00 88.05           C  
ANISOU 3709  CG  LEU B 377     9891  13011  10552   -965   1029   1220       C  
ATOM   3710  CD1 LEU B 377       6.650 -66.845  35.123  1.00 83.57           C  
ANISOU 3710  CD1 LEU B 377     9294  11906  10550   -441    803   1522       C  
ATOM   3711  CD2 LEU B 377       7.355 -68.043  33.059  1.00 91.17           C  
ANISOU 3711  CD2 LEU B 377     9978  13490  11172  -1238   1688    537       C  
ATOM   3712  N   ILE B 378       2.285 -69.511  32.847  1.00 86.93           N  
ANISOU 3712  N   ILE B 378     9780  13335   9913  -1260    980    441       N  
ATOM   3713  CA  ILE B 378       1.170 -70.432  33.098  1.00 84.76           C  
ANISOU 3713  CA  ILE B 378     9450  12967   9786  -1191   1044    123       C  
ATOM   3714  C   ILE B 378       0.193 -70.399  31.938  1.00 87.70           C  
ANISOU 3714  C   ILE B 378     9823  14041   9457  -1760    848     59       C  
ATOM   3715  O   ILE B 378       0.176 -69.409  31.206  1.00 90.62           O  
ANISOU 3715  O   ILE B 378    10265  14869   9295  -2102    406    565       O  
ATOM   3716  CB  ILE B 378       0.391 -70.145  34.425  1.00 80.62           C  
ANISOU 3716  CB  ILE B 378     8959  11985   9686   -684    713    436       C  
ATOM   3717  CG1 ILE B 378       0.435 -68.666  34.787  1.00 79.41           C  
ANISOU 3717  CG1 ILE B 378     8846  11759   9567   -480    243   1004       C  
ATOM   3718  CG2 ILE B 378       0.823 -71.102  35.576  1.00 78.25           C  
ANISOU 3718  CG2 ILE B 378     8645  11107   9978   -409    999    284       C  
ATOM   3719  CD1 ILE B 378      -0.820 -67.942  34.363  1.00 84.16           C  
ANISOU 3719  CD1 ILE B 378     9317  12557  10100   -547   -256   1261       C  
ATOM   3720  N   PRO B 379      -0.624 -71.476  31.772  1.00 87.49           N  
ANISOU 3720  N   PRO B 379     9704  14105   9431  -1937   1107   -480       N  
ATOM   3721  CA  PRO B 379      -1.603 -71.603  30.706  1.00 91.58           C  
ANISOU 3721  CA  PRO B 379    10176  15371   9245  -2580    909   -597       C  
ATOM   3722  C   PRO B 379      -2.778 -70.679  30.904  1.00 90.46           C  
ANISOU 3722  C   PRO B 379     9953  15291   9126  -2370     77    101       C  
ATOM   3723  O   PRO B 379      -3.036 -70.266  32.023  1.00 85.52           O  
ANISOU 3723  O   PRO B 379     9275  14049   9167  -1716    -97    339       O  
ATOM   3724  CB  PRO B 379      -2.071 -73.040  30.845  1.00 92.18           C  
ANISOU 3724  CB  PRO B 379    10137  15264   9622  -2651   1484  -1417       C  
ATOM   3725  CG  PRO B 379      -1.052 -73.703  31.615  1.00 89.81           C  
ANISOU 3725  CG  PRO B 379     9797  14190  10134  -2225   2022  -1723       C  
ATOM   3726  CD  PRO B 379      -0.585 -72.707  32.570  1.00 85.10           C  
ANISOU 3726  CD  PRO B 379     9315  13187   9831  -1633   1594   -983       C  
ATOM   3727  N   GLU B 380      -3.473 -70.357  29.818  1.00 96.61           N  
ANISOU 3727  N   GLU B 380    10654  16823   9229  -3014   -434    402       N  
ATOM   3728  CA  GLU B 380      -4.655 -69.517  29.865  1.00 98.69           C  
ANISOU 3728  CA  GLU B 380    10651  17080   9765  -2843  -1330   1098       C  
ATOM   3729  C   GLU B 380      -5.489 -69.822  31.111  1.00 93.21           C  
ANISOU 3729  C   GLU B 380     9741  15697   9976  -2120  -1186    762       C  
ATOM   3730  O   GLU B 380      -5.802 -68.922  31.883  1.00 91.47           O  
ANISOU 3730  O   GLU B 380     9317  14928  10507  -1570  -1543   1128       O  
ATOM   3731  CB  GLU B 380      -5.549 -69.749  28.636  1.00108.00           C  
ANISOU 3731  CB  GLU B 380    11681  19202  10152  -3722  -1806   1231       C  
ATOM   3732  CG  GLU B 380      -5.114 -69.162  27.273  1.00118.43           C  
ANISOU 3732  CG  GLU B 380    13161  21463  10371  -4760  -2307   1877       C  
ATOM   3733  CD  GLU B 380      -6.043 -69.633  26.112  1.00130.55           C  
ANISOU 3733  CD  GLU B 380    14560  24113  10931  -5851  -2723   1886       C  
ATOM   3734  OE1 GLU B 380      -6.901 -70.516  26.350  1.00129.44           O  
ANISOU 3734  OE1 GLU B 380    14210  23962  11010  -5741  -2457   1220       O  
ATOM   3735  OE2 GLU B 380      -5.921 -69.133  24.963  1.00140.86           O1-
ANISOU 3735  OE2 GLU B 380    15974  26371  11172  -6937  -3333   2580       O1-
ATOM   3736  N   TYR B 381      -5.837 -71.094  31.313  1.00 91.47           N  
ANISOU 3736  N   TYR B 381     9543  15497   9714  -2217   -596     -9       N  
ATOM   3737  CA  TYR B 381      -6.865 -71.461  32.295  1.00 88.44           C  
ANISOU 3737  CA  TYR B 381     8943  14692   9967  -1823   -503   -328       C  
ATOM   3738  C   TYR B 381      -6.509 -71.307  33.753  1.00 81.93           C  
ANISOU 3738  C   TYR B 381     8218  13117   9793  -1231   -192   -395       C  
ATOM   3739  O   TYR B 381      -7.382 -71.465  34.597  1.00 81.48           O  
ANISOU 3739  O   TYR B 381     7977  12805  10177  -1056   -101   -668       O  
ATOM   3740  CB  TYR B 381      -7.376 -72.886  32.073  1.00 90.29           C  
ANISOU 3740  CB  TYR B 381     9188  15149   9967  -2206     21  -1087       C  
ATOM   3741  CG  TYR B 381      -6.428 -73.994  32.489  1.00 87.83           C  
ANISOU 3741  CG  TYR B 381     9163  14414   9795  -2170    835  -1622       C  
ATOM   3742  CD1 TYR B 381      -6.537 -74.611  33.752  1.00 83.58           C  
ANISOU 3742  CD1 TYR B 381     8701  13203   9853  -1813   1184  -1811       C  
ATOM   3743  CD2 TYR B 381      -5.441 -74.453  31.600  1.00 90.53           C  
ANISOU 3743  CD2 TYR B 381     9627  15017   9754  -2597   1246  -1945       C  
ATOM   3744  CE1 TYR B 381      -5.673 -75.643  34.120  1.00 82.95           C  
ANISOU 3744  CE1 TYR B 381     8786  12603  10125  -1789   1749  -2098       C  
ATOM   3745  CE2 TYR B 381      -4.580 -75.474  31.950  1.00 89.57           C  
ANISOU 3745  CE2 TYR B 381     9576  14328  10126  -2510   1952  -2454       C  
ATOM   3746  CZ  TYR B 381      -4.698 -76.069  33.203  1.00 87.11           C  
ANISOU 3746  CZ  TYR B 381     9311  13235  10552  -2061   2121  -2433       C  
ATOM   3747  OH  TYR B 381      -3.820 -77.083  33.519  1.00 89.59           O  
ANISOU 3747  OH  TYR B 381     9604  12866  11569  -1981   2657  -2750       O  
ATOM   3748  N   LEU B 382      -5.243 -71.035  34.052  1.00 78.05           N  
ANISOU 3748  N   LEU B 382     7997  12360   9295  -1050     -8   -192       N  
ATOM   3749  CA  LEU B 382      -4.803 -70.814  35.418  1.00 72.93           C  
ANISOU 3749  CA  LEU B 382     7461  11146   9101   -658    195   -162       C  
ATOM   3750  C   LEU B 382      -4.462 -69.335  35.624  1.00 72.73           C  
ANISOU 3750  C   LEU B 382     7348  10947   9339   -396   -206    324       C  
ATOM   3751  O   LEU B 382      -3.729 -68.969  36.563  1.00 70.01           O  
ANISOU 3751  O   LEU B 382     7144  10262   9194   -197    -47    397       O  
ATOM   3752  CB  LEU B 382      -3.572 -71.670  35.701  1.00 70.53           C  
ANISOU 3752  CB  LEU B 382     7438  10595   8764   -662    651   -267       C  
ATOM   3753  CG  LEU B 382      -3.700 -73.183  35.792  1.00 71.33           C  
ANISOU 3753  CG  LEU B 382     7587  10532   8982   -848   1110   -727       C  
ATOM   3754  CD1 LEU B 382      -2.339 -73.814  35.846  1.00 71.99           C  
ANISOU 3754  CD1 LEU B 382     7750  10242   9359   -793   1425   -731       C  
ATOM   3755  CD2 LEU B 382      -4.478 -73.585  37.015  1.00 71.67           C  
ANISOU 3755  CD2 LEU B 382     7662  10289   9279   -827   1191   -806       C  
ATOM   3756  N   ASN B 383      -4.983 -68.472  34.753  1.00 76.41           N  
ANISOU 3756  N   ASN B 383     7552  11626   9853   -460   -780    713       N  
ATOM   3757  CA  ASN B 383      -4.527 -67.093  34.753  1.00 77.43           C  
ANISOU 3757  CA  ASN B 383     7594  11493  10333   -265  -1191   1262       C  
ATOM   3758  C   ASN B 383      -4.996 -66.330  35.973  1.00 76.10           C  
ANISOU 3758  C   ASN B 383     7124  10742  11046    101  -1129   1037       C  
ATOM   3759  O   ASN B 383      -4.436 -65.278  36.283  1.00 76.89           O  
ANISOU 3759  O   ASN B 383     7184  10484  11544    276  -1252   1295       O  
ATOM   3760  CB  ASN B 383      -4.882 -66.355  33.466  1.00 84.36           C  
ANISOU 3760  CB  ASN B 383     8262  12688  11101   -536  -1963   1960       C  
ATOM   3761  CG  ASN B 383      -6.307 -65.894  33.457  1.00 92.28           C  
ANISOU 3761  CG  ASN B 383     8657  13496  12907   -390  -2516   2073       C  
ATOM   3762  OD1 ASN B 383      -6.696 -65.032  34.253  1.00 96.66           O  
ANISOU 3762  OD1 ASN B 383     8808  13391  14525     30  -2606   2009       O  
ATOM   3763  ND2 ASN B 383      -7.118 -66.478  32.575  1.00 98.85           N  
ANISOU 3763  ND2 ASN B 383     9331  14891  13334   -784  -2847   2139       N  
ATOM   3764  N   PHE B 384      -6.005 -66.860  36.661  1.00 75.55           N  
ANISOU 3764  N   PHE B 384     6827  10604  11274    116   -856    454       N  
ATOM   3765  CA  PHE B 384      -6.441 -66.333  37.961  1.00 75.41           C  
ANISOU 3765  CA  PHE B 384     6531  10162  11959    241   -529    -70       C  
ATOM   3766  C   PHE B 384      -5.355 -66.423  39.044  1.00 71.87           C  
ANISOU 3766  C   PHE B 384     6528   9636  11143    140    -50   -211       C  
ATOM   3767  O   PHE B 384      -5.418 -65.693  40.034  1.00 73.56           O  
ANISOU 3767  O   PHE B 384     6557   9582  11809     99    202   -593       O  
ATOM   3768  CB  PHE B 384      -7.697 -67.034  38.442  1.00 76.48           C  
ANISOU 3768  CB  PHE B 384     6374  10385  12298     89   -230   -741       C  
ATOM   3769  CG  PHE B 384      -7.507 -68.494  38.729  1.00 70.99           C  
ANISOU 3769  CG  PHE B 384     6173  10012  10786   -213    210   -959       C  
ATOM   3770  CD1 PHE B 384      -7.095 -68.920  39.979  1.00 66.60           C  
ANISOU 3770  CD1 PHE B 384     5949   9407   9948   -472    714  -1235       C  
ATOM   3771  CD2 PHE B 384      -7.758 -69.446  37.744  1.00 69.97           C  
ANISOU 3771  CD2 PHE B 384     6144  10224  10217   -341     88   -862       C  
ATOM   3772  CE1 PHE B 384      -6.920 -70.261  40.242  1.00 65.05           C  
ANISOU 3772  CE1 PHE B 384     6152   9351   9211   -762    989  -1255       C  
ATOM   3773  CE2 PHE B 384      -7.582 -70.794  37.989  1.00 67.48           C  
ANISOU 3773  CE2 PHE B 384     6202  10019   9418   -601    510  -1086       C  
ATOM   3774  CZ  PHE B 384      -7.165 -71.208  39.242  1.00 65.99           C  
ANISOU 3774  CZ  PHE B 384     6316   9631   9123   -767    914  -1209       C  
ATOM   3775  N   ILE B 385      -4.364 -67.302  38.862  1.00 68.77           N  
ANISOU 3775  N   ILE B 385     6636   9469  10021     35     70     52       N  
ATOM   3776  CA  ILE B 385      -3.232 -67.399  39.803  1.00 66.84           C  
ANISOU 3776  CA  ILE B 385     6743   9158   9494    -75    326    127       C  
ATOM   3777  C   ILE B 385      -2.409 -66.119  39.763  1.00 67.68           C  
ANISOU 3777  C   ILE B 385     6809   9069   9834     84    138    418       C  
ATOM   3778  O   ILE B 385      -2.234 -65.534  38.692  1.00 69.16           O  
ANISOU 3778  O   ILE B 385     6906   9235  10134    256   -224    815       O  
ATOM   3779  CB  ILE B 385      -2.320 -68.611  39.493  1.00 64.40           C  
ANISOU 3779  CB  ILE B 385     6784   8959   8724   -140    417    381       C  
ATOM   3780  CG1 ILE B 385      -3.053 -69.920  39.735  1.00 64.69           C  
ANISOU 3780  CG1 ILE B 385     6879   9050   8650   -356    650     98       C  
ATOM   3781  CG2 ILE B 385      -1.060 -68.592  40.343  1.00 63.17           C  
ANISOU 3781  CG2 ILE B 385     6859   8693   8448   -218    471    654       C  
ATOM   3782  CD1 ILE B 385      -3.363 -70.193  41.196  1.00 66.21           C  
ANISOU 3782  CD1 ILE B 385     7184   9213   8758   -723    875    -76       C  
ATOM   3783  N   ARG B 386      -1.918 -65.687  40.924  1.00 68.41           N  
ANISOU 3783  N   ARG B 386     6981   9076   9934    -98    370    239       N  
ATOM   3784  CA  ARG B 386      -1.130 -64.448  41.046  1.00 69.74           C  
ANISOU 3784  CA  ARG B 386     7096   9029  10373    -20    278    396       C  
ATOM   3785  C   ARG B 386       0.035 -64.719  41.956  1.00 68.16           C  
ANISOU 3785  C   ARG B 386     7223   9005   9666   -308    430    517       C  
ATOM   3786  O   ARG B 386      -0.135 -65.377  42.968  1.00 69.20           O  
ANISOU 3786  O   ARG B 386     7491   9351   9451   -714    646    300       O  
ATOM   3787  CB  ARG B 386      -1.957 -63.311  41.670  1.00 74.28           C  
ANISOU 3787  CB  ARG B 386     7210   9259  11753    -70    457   -193       C  
ATOM   3788  CG  ARG B 386      -3.346 -63.111  41.111  1.00 79.12           C  
ANISOU 3788  CG  ARG B 386     7301   9620  13139    160    300   -426       C  
ATOM   3789  CD  ARG B 386      -3.374 -61.990  40.099  1.00 86.76           C  
ANISOU 3789  CD  ARG B 386     7921  10122  14921    530   -253     97       C  
ATOM   3790  NE  ARG B 386      -4.741 -61.499  39.910  1.00 97.42           N  
ANISOU 3790  NE  ARG B 386     8535  11032  17448    725   -437   -202       N  
ATOM   3791  CZ  ARG B 386      -5.524 -61.752  38.852  1.00101.70           C  
ANISOU 3791  CZ  ARG B 386     8820  11628  18192    897  -1014    263       C  
ATOM   3792  NH1 ARG B 386      -5.092 -62.477  37.818  1.00 98.31           N1+
ANISOU 3792  NH1 ARG B 386     8859  11740  16752    810  -1381    962       N1+
ATOM   3793  NH2 ARG B 386      -6.752 -61.249  38.818  1.00109.78           N  
ANISOU 3793  NH2 ARG B 386     9029  12168  20515   1087  -1216    -30       N  
ATOM   3794  N   GLY B 387       1.208 -64.200  41.626  1.00 67.50           N  
ANISOU 3794  N   GLY B 387     7243   8870   9532   -193    267    917       N  
ATOM   3795  CA  GLY B 387       2.348 -64.302  42.530  1.00 67.94           C  
ANISOU 3795  CA  GLY B 387     7497   9092   9225   -489    310   1075       C  
ATOM   3796  C   GLY B 387       3.676 -63.940  41.885  1.00 67.58           C  
ANISOU 3796  C   GLY B 387     7504   9002   9171   -298    124   1528       C  
ATOM   3797  O   GLY B 387       3.708 -63.252  40.861  1.00 68.02           O  
ANISOU 3797  O   GLY B 387     7480   8903   9462    -55      8   1676       O  
ATOM   3798  N   VAL B 388       4.783 -64.381  42.481  1.00 67.74           N  
ANISOU 3798  N   VAL B 388     7620   9174   8944   -488     47   1804       N  
ATOM   3799  CA  VAL B 388       6.063 -64.071  41.910  1.00 67.43           C  
ANISOU 3799  CA  VAL B 388     7537   9103   8977   -343    -61   2123       C  
ATOM   3800  C   VAL B 388       6.849 -65.323  41.594  1.00 68.11           C  
ANISOU 3800  C   VAL B 388     7551   9182   9145   -222   -144   2409       C  
ATOM   3801  O   VAL B 388       6.760 -66.325  42.314  1.00 68.99           O  
ANISOU 3801  O   VAL B 388     7667   9283   9260   -364   -258   2564       O  
ATOM   3802  CB  VAL B 388       6.906 -63.083  42.777  1.00 69.30           C  
ANISOU 3802  CB  VAL B 388     7759   9426   9146   -652    -89   2131       C  
ATOM   3803  CG1 VAL B 388       6.030 -62.159  43.596  1.00 71.23           C  
ANISOU 3803  CG1 VAL B 388     7986   9647   9429   -962    128   1611       C  
ATOM   3804  CG2 VAL B 388       7.847 -63.802  43.658  1.00 71.13           C  
ANISOU 3804  CG2 VAL B 388     7974   9878   9172   -942   -313   2476       C  
ATOM   3805  N   VAL B 389       7.603 -65.256  40.493  1.00 69.00           N  
ANISOU 3805  N   VAL B 389     7546   9260   9410    -33    -64   2452       N  
ATOM   3806  CA  VAL B 389       8.650 -66.230  40.212  1.00 71.89           C  
ANISOU 3806  CA  VAL B 389     7648   9515  10150     60    -34   2549       C  
ATOM   3807  C   VAL B 389      10.048 -65.595  40.251  1.00 74.35           C  
ANISOU 3807  C   VAL B 389     7761   9865  10621      3    -83   2699       C  
ATOM   3808  O   VAL B 389      10.358 -64.677  39.481  1.00 74.68           O  
ANISOU 3808  O   VAL B 389     7853  10036  10484    -50     71   2599       O  
ATOM   3809  CB  VAL B 389       8.414 -66.938  38.884  1.00 72.40           C  
ANISOU 3809  CB  VAL B 389     7618   9573  10317    163    285   2213       C  
ATOM   3810  CG1 VAL B 389       9.624 -67.803  38.505  1.00 76.71           C  
ANISOU 3810  CG1 VAL B 389     7719   9904  11521    233    485   2069       C  
ATOM   3811  CG2 VAL B 389       7.199 -67.806  38.995  1.00 71.13           C  
ANISOU 3811  CG2 VAL B 389     7568   9338  10120    199    309   2076       C  
ATOM   3812  N   ASP B 390      10.884 -66.089  41.157  1.00 77.58           N  
ANISOU 3812  N   ASP B 390     7921  10169  11383    -51   -369   3021       N  
ATOM   3813  CA  ASP B 390      12.237 -65.590  41.296  1.00 80.88           C  
ANISOU 3813  CA  ASP B 390     8049  10634  12046   -123   -474   3172       C  
ATOM   3814  C   ASP B 390      13.201 -66.654  40.825  1.00 86.60           C  
ANISOU 3814  C   ASP B 390     8187  11027  13689     99   -417   3136       C  
ATOM   3815  O   ASP B 390      13.514 -67.608  41.561  1.00 90.34           O  
ANISOU 3815  O   ASP B 390     8332  11193  14801    151   -821   3549       O  
ATOM   3816  CB  ASP B 390      12.525 -65.242  42.752  1.00 82.54           C  
ANISOU 3816  CB  ASP B 390     8307  11038  12014   -482   -943   3602       C  
ATOM   3817  CG  ASP B 390      13.667 -64.267  42.909  1.00 83.90           C  
ANISOU 3817  CG  ASP B 390     8308  11397  12173   -665  -1005   3650       C  
ATOM   3818  OD1 ASP B 390      14.138 -64.063  44.045  1.00 87.96           O  
ANISOU 3818  OD1 ASP B 390     8762  12155  12502  -1068  -1418   4001       O  
ATOM   3819  OD2 ASP B 390      14.102 -63.698  41.900  1.00 83.54           O1-
ANISOU 3819  OD2 ASP B 390     8195  11322  12221   -524   -649   3349       O1-
ATOM   3820  N   SER B 391      13.661 -66.500  39.583  1.00 89.32           N  
ANISOU 3820  N   SER B 391     8348  11410  14180    148     90   2632       N  
ATOM   3821  CA  SER B 391      14.664 -67.401  39.002  1.00 96.34           C  
ANISOU 3821  CA  SER B 391     8527  11966  16113    289    371   2283       C  
ATOM   3822  C   SER B 391      16.038 -67.015  39.486  1.00101.10           C  
ANISOU 3822  C   SER B 391     8633  12528  17250    258    124   2513       C  
ATOM   3823  O   SER B 391      16.366 -65.839  39.553  1.00 98.51           O  
ANISOU 3823  O   SER B 391     8555  12581  16291     29    110   2588       O  
ATOM   3824  CB  SER B 391      14.623 -67.384  37.476  1.00 97.30           C  
ANISOU 3824  CB  SER B 391     8630  12316  16023    102   1131   1493       C  
ATOM   3825  OG  SER B 391      15.701 -68.135  36.949  1.00105.19           O  
ANISOU 3825  OG  SER B 391     8826  13008  18130    131   1569    916       O  
ATOM   3826  N   GLU B 392      16.820 -68.026  39.844  1.00109.78           N  
ANISOU 3826  N   GLU B 392     8965  13092  19652    484   -119   2660       N  
ATOM   3827  CA  GLU B 392      18.224 -67.860  40.225  1.00117.87           C  
ANISOU 3827  CA  GLU B 392     9274  13991  21520    491   -403   2859       C  
ATOM   3828  C   GLU B 392      19.104 -67.833  38.955  1.00123.10           C  
ANISOU 3828  C   GLU B 392     9348  14625  22796    456    452   1875       C  
ATOM   3829  O   GLU B 392      20.189 -68.401  38.904  1.00131.25           O  
ANISOU 3829  O   GLU B 392     9388  15192  25286    622    488   1653       O  
ATOM   3830  CB  GLU B 392      18.637 -68.964  41.221  1.00125.19           C  
ANISOU 3830  CB  GLU B 392     9529  14272  23764    713  -1218   3626       C  
ATOM   3831  CG  GLU B 392      19.954 -68.728  41.987  1.00134.17           C  
ANISOU 3831  CG  GLU B 392     9959  15362  25657    640  -1903   4215       C  
ATOM   3832  CD  GLU B 392      19.863 -67.689  43.112  1.00133.28           C  
ANISOU 3832  CD  GLU B 392    10472  15976  24189    146  -2552   4948       C  
ATOM   3833  OE1 GLU B 392      20.344 -67.996  44.229  1.00139.90           O  
ANISOU 3833  OE1 GLU B 392    10957  16773  25425    -65  -3537   5919       O  
ATOM   3834  OE2 GLU B 392      19.337 -66.569  42.881  1.00127.08           O1-
ANISOU 3834  OE2 GLU B 392    10467  15787  22030   -106  -2100   4558       O1-
ATOM   3835  N   ASP B 393      18.581 -67.156  37.934  1.00120.35           N  
ANISOU 3835  N   ASP B 393     9596  14801  21330    146   1120   1304       N  
ATOM   3836  CA  ASP B 393      19.222 -66.913  36.634  1.00125.77           C  
ANISOU 3836  CA  ASP B 393     9994  15774  22018   -222   2019    355       C  
ATOM   3837  C   ASP B 393      18.689 -67.737  35.466  1.00129.12           C  
ANISOU 3837  C   ASP B 393    10346  16205  22506   -415   2821   -556       C  
ATOM   3838  O   ASP B 393      18.883 -68.952  35.396  1.00135.30           O  
ANISOU 3838  O   ASP B 393    10394  16367  24645   -153   3061  -1036       O  
ATOM   3839  CB  ASP B 393      20.759 -66.919  36.694  1.00133.74           C  
ANISOU 3839  CB  ASP B 393    10020  16579  24214   -222   2150     49       C  
ATOM   3840  CG  ASP B 393      21.341 -65.512  36.794  1.00133.14           C  
ANISOU 3840  CG  ASP B 393    10273  17065  23248   -593   2064    295       C  
ATOM   3841  OD1 ASP B 393      21.106 -64.700  35.866  1.00132.53           O  
ANISOU 3841  OD1 ASP B 393    10765  17556  22034  -1119   2597    -40       O  
ATOM   3842  OD2 ASP B 393      22.037 -65.218  37.797  1.00136.00           O1-
ANISOU 3842  OD2 ASP B 393    10316  17308  24047   -442   1421    877       O1-
ATOM   3843  N   LEU B 394      17.974 -67.047  34.583  1.00126.37           N  
ANISOU 3843  N   LEU B 394    10755  16544  20716   -931   3163   -728       N  
ATOM   3844  CA  LEU B 394      17.700 -67.504  33.227  1.00131.62           C  
ANISOU 3844  CA  LEU B 394    11390  17592  21024  -1514   4044  -1709       C  
ATOM   3845  C   LEU B 394      18.509 -66.587  32.292  1.00136.35           C  
ANISOU 3845  C   LEU B 394    12012  18899  20894  -2324   4621  -2157       C  
ATOM   3846  O   LEU B 394      18.737 -65.421  32.630  1.00132.53           O  
ANISOU 3846  O   LEU B 394    11945  18649  19760  -2396   4183  -1455       O  
ATOM   3847  CB  LEU B 394      16.191 -67.448  32.922  1.00126.19           C  
ANISOU 3847  CB  LEU B 394    11546  17248  19149  -1649   3829  -1383       C  
ATOM   3848  CG  LEU B 394      15.411 -66.128  33.012  1.00119.72           C  
ANISOU 3848  CG  LEU B 394    11641  16891  16956  -1811   3232   -470       C  
ATOM   3849  CD1 LEU B 394      15.399 -65.354  31.687  1.00123.60           C  
ANISOU 3849  CD1 LEU B 394    12514  18218  16230  -2771   3616   -661       C  
ATOM   3850  CD2 LEU B 394      13.991 -66.407  33.456  1.00114.55           C  
ANISOU 3850  CD2 LEU B 394    11457  16078  15989  -1450   2735      2       C  
ATOM   3851  N   PRO B 395      18.980 -67.115  31.136  1.00145.84           N  
ANISOU 3851  N   PRO B 395    12729  20441  22241  -3036   5667  -3402       N  
ATOM   3852  CA  PRO B 395      19.726 -66.269  30.183  1.00151.80           C  
ANISOU 3852  CA  PRO B 395    13550  22011  22116  -4050   6291  -3868       C  
ATOM   3853  C   PRO B 395      18.905 -65.083  29.646  1.00147.95           C  
ANISOU 3853  C   PRO B 395    14202  22338  19673  -4726   5871  -2991       C  
ATOM   3854  O   PRO B 395      19.367 -63.937  29.635  1.00147.44           O  
ANISOU 3854  O   PRO B 395    14459  22570  18990  -5064   5647  -2445       O  
ATOM   3855  CB  PRO B 395      20.089 -67.246  29.053  1.00163.31           C  
ANISOU 3855  CB  PRO B 395    14315  23749  23985  -4829   7572  -5519       C  
ATOM   3856  CG  PRO B 395      20.113 -68.590  29.707  1.00164.52           C  
ANISOU 3856  CG  PRO B 395    13603  22811  26095  -3891   7599  -5964       C  
ATOM   3857  CD  PRO B 395      19.020 -68.539  30.747  1.00153.18           C  
ANISOU 3857  CD  PRO B 395    12871  20937  24391  -2995   6406  -4563       C  
ATOM   3858  N   GLN B 405      16.781 -68.618  21.455  1.00184.32           N  
ANISOU 3858  N   GLN B 405    14003  39102  16925 -10581   3430   -317       N  
ATOM   3859  CA  GLN B 405      15.973 -69.767  21.956  1.00178.55           C  
ANISOU 3859  CA  GLN B 405    13463  37698  16678  -9663   3487   -891       C  
ATOM   3860  C   GLN B 405      14.820 -69.289  22.842  1.00171.55           C  
ANISOU 3860  C   GLN B 405    13353  35485  16344  -9271   3097   -306       C  
ATOM   3861  O   GLN B 405      13.720 -69.026  22.337  1.00170.77           O  
ANISOU 3861  O   GLN B 405    13609  35182  16091  -9423   2948    132       O  
ATOM   3862  CB  GLN B 405      16.872 -70.803  22.674  1.00177.69           C  
ANISOU 3862  CB  GLN B 405    12934  37593  16987  -9011   3701  -1809       C  
ATOM   3863  CG  GLN B 405      16.184 -71.757  23.698  1.00171.35           C  
ANISOU 3863  CG  GLN B 405    12459  35738  16908  -8029   3605  -2212       C  
ATOM   3864  CD  GLN B 405      15.198 -72.753  23.076  1.00171.00           C  
ANISOU 3864  CD  GLN B 405    12429  35762  16779  -7704   3727  -2600       C  
ATOM   3865  OE1 GLN B 405      14.157 -72.373  22.531  1.00170.45           O  
ANISOU 3865  OE1 GLN B 405    12720  35579  16464  -7947   3622  -2099       O  
ATOM   3866  NE2 GLN B 405      15.512 -74.039  23.193  1.00170.93           N  
ANISOU 3866  NE2 GLN B 405    12034  35880  17028  -7131   3908  -3499       N  
ATOM   3867  N   SER B 406      15.090 -69.162  24.147  1.00166.82           N  
ANISOU 3867  N   SER B 406    12982  34035  16366  -8793   2931   -321       N  
ATOM   3868  CA  SER B 406      14.078 -68.896  25.171  1.00159.76           C  
ANISOU 3868  CA  SER B 406    12744  31901  16053  -8292   2608     31       C  
ATOM   3869  C   SER B 406      12.948 -69.928  25.136  1.00155.42           C  
ANISOU 3869  C   SER B 406    12384  30994  15673  -7704   2679   -321       C  
ATOM   3870  O   SER B 406      12.019 -69.830  24.325  1.00155.95           O  
ANISOU 3870  O   SER B 406    12622  31182  15449  -7927   2643    -44       O  
ATOM   3871  CB  SER B 406      13.528 -67.472  25.058  1.00160.31           C  
ANISOU 3871  CB  SER B 406    13267  31580  16063  -8827   2228    975       C  
ATOM   3872  OG  SER B 406      12.766 -67.135  26.199  1.00154.38           O  
ANISOU 3872  OG  SER B 406    13069  29667  15922  -8334   1920   1224       O  
ATOM   3873  N   LYS B 407      13.064 -70.924  26.015  1.00151.27           N  
ANISOU 3873  N   LYS B 407    11814  30040  15622  -6977   2756   -919       N  
ATOM   3874  CA  LYS B 407      12.098 -72.021  26.155  1.00146.63           C  
ANISOU 3874  CA  LYS B 407    11381  29047  15281  -6360   2802  -1307       C  
ATOM   3875  C   LYS B 407      12.276 -72.689  27.519  1.00141.24           C  
ANISOU 3875  C   LYS B 407    10807  27617  15239  -5644   2722  -1675       C  
ATOM   3876  O   LYS B 407      11.463 -73.516  27.915  1.00137.83           O  
ANISOU 3876  O   LYS B 407    10583  26672  15114  -5110   2685  -1904       O  
ATOM   3877  CB  LYS B 407      12.258 -73.048  25.025  1.00150.73           C  
ANISOU 3877  CB  LYS B 407    11391  30466  15413  -6403   3122  -1940       C  
ATOM   3878  CG  LYS B 407      10.943 -73.646  24.489  1.00150.00           C  
ANISOU 3878  CG  LYS B 407    11527  30211  15255  -6194   3129  -1979       C  
ATOM   3879  CD  LYS B 407      10.772 -75.125  24.868  1.00149.10           C  
ANISOU 3879  CD  LYS B 407    11267  29842  15542  -5462   3224  -2745       C  
ATOM   3880  CE  LYS B 407      10.113 -75.930  23.743  1.00151.29           C  
ANISOU 3880  CE  LYS B 407    11356  30631  15494  -5470   3398  -3106       C  
ATOM   3881  NZ  LYS B 407      10.786 -77.256  23.543  1.00153.56           N1+
ANISOU 3881  NZ  LYS B 407    11076  31360  15910  -5090   3603  -4070       N1+
ATOM   3882  N   ILE B 408      13.341 -72.327  28.234  1.00140.67           N  
ANISOU 3882  N   ILE B 408    10592  27500  15355  -5667   2676  -1705       N  
ATOM   3883  CA  ILE B 408      13.503 -72.684  29.636  1.00135.13           C  
ANISOU 3883  CA  ILE B 408    10073  26028  15242  -5089   2524  -1877       C  
ATOM   3884  C   ILE B 408      12.207 -72.357  30.350  1.00129.01           C  
ANISOU 3884  C   ILE B 408     9930  24337  14748  -4825   2280  -1433       C  
ATOM   3885  O   ILE B 408      11.766 -73.102  31.218  1.00125.36           O  
ANISOU 3885  O   ILE B 408     9656  23284  14688  -4264   2201  -1660       O  
ATOM   3886  CB  ILE B 408      14.676 -71.907  30.269  1.00137.03           C  
ANISOU 3886  CB  ILE B 408    10190  26292  15583  -5305   2442  -1731       C  
ATOM   3887  CG1 ILE B 408      16.023 -72.620  30.007  1.00141.44           C  
ANISOU 3887  CG1 ILE B 408    10083  27571  16085  -5288   2667  -2399       C  
ATOM   3888  CG2 ILE B 408      14.430 -71.618  31.759  1.00131.86           C  
ANISOU 3888  CG2 ILE B 408     9982  24664  15452  -4905   2167  -1509       C  
ATOM   3889  CD1 ILE B 408      16.094 -74.106  30.446  1.00140.26           C  
ANISOU 3889  CD1 ILE B 408     9729  27221  16341  -4598   2711  -3137       C  
ATOM   3890  N   LEU B 409      11.589 -71.249  29.949  1.00128.07           N  
ANISOU 3890  N   LEU B 409    10115  24132  14413  -5254   2142   -804       N  
ATOM   3891  CA  LEU B 409      10.224 -70.884  30.355  1.00122.63           C  
ANISOU 3891  CA  LEU B 409     9975  22693  13926  -5068   1921   -403       C  
ATOM   3892  C   LEU B 409       9.214 -72.034  30.357  1.00118.69           C  
ANISOU 3892  C   LEU B 409     9588  21948  13559  -4572   1998   -734       C  
ATOM   3893  O   LEU B 409       8.329 -72.070  31.204  1.00114.44           O  
ANISOU 3893  O   LEU B 409     9442  20689  13350  -4206   1836   -611       O  
ATOM   3894  CB  LEU B 409       9.699 -69.771  29.456  1.00124.83           C  
ANISOU 3894  CB  LEU B 409    10424  23136  13868  -5655   1789    211       C  
ATOM   3895  CG  LEU B 409      10.471 -68.461  29.531  1.00127.45           C  
ANISOU 3895  CG  LEU B 409    10754  23535  14135  -6179   1605    687       C  
ATOM   3896  CD1 LEU B 409      10.500 -67.760  28.178  1.00132.42           C  
ANISOU 3896  CD1 LEU B 409    11255  24823  14234  -6920   1591   1116       C  
ATOM   3897  CD2 LEU B 409       9.863 -67.580  30.596  1.00123.74           C  
ANISOU 3897  CD2 LEU B 409    10768  22137  14107  -5998   1255   1081       C  
ATOM   3898  N   LYS B 410       9.331 -72.960  29.408  1.00120.12           N  
ANISOU 3898  N   LYS B 410     9413  22747  13479  -4577   2237  -1166       N  
ATOM   3899  CA  LYS B 410       8.470 -74.140  29.409  1.00116.94           C  
ANISOU 3899  CA  LYS B 410     9076  22117  13239  -4100   2294  -1529       C  
ATOM   3900  C   LYS B 410       8.667 -74.948  30.682  1.00112.48           C  
ANISOU 3900  C   LYS B 410     8565  20981  13189  -3513   2211  -1867       C  
ATOM   3901  O   LYS B 410       7.706 -75.457  31.254  1.00108.11           O  
ANISOU 3901  O   LYS B 410     8317  19854  12904  -3124   2107  -1864       O  
ATOM   3902  CB  LYS B 410       8.712 -75.043  28.183  1.00121.33           C  
ANISOU 3902  CB  LYS B 410     9169  23475  13456  -4191   2556  -2038       C  
ATOM   3903  CG  LYS B 410       7.761 -76.279  28.145  1.00121.04           C  
ANISOU 3903  CG  LYS B 410     9208  23160  13619  -3701   2577  -2409       C  
ATOM   3904  CD  LYS B 410       7.840 -77.124  26.854  1.00127.68           C  
ANISOU 3904  CD  LYS B 410     9611  24783  14117  -3797   2814  -2924       C  
ATOM   3905  CE  LYS B 410       6.988 -78.401  27.016  1.00125.98           C  
ANISOU 3905  CE  LYS B 410     9477  24168  14222  -3250   2779  -3318       C  
ATOM   3906  NZ  LYS B 410       6.317 -78.928  25.783  1.00128.51           N1+
ANISOU 3906  NZ  LYS B 410     9652  24972  14201  -3361   2920  -3539       N1+
ATOM   3907  N   VAL B 411       9.924 -75.052  31.113  1.00113.05           N  
ANISOU 3907  N   VAL B 411     8328  21239  13385  -3483   2241  -2139       N  
ATOM   3908  CA  VAL B 411      10.283 -75.889  32.253  1.00109.56           C  
ANISOU 3908  CA  VAL B 411     7869  20336  13420  -2966   2137  -2484       C  
ATOM   3909  C   VAL B 411       9.782 -75.273  33.560  1.00104.20           C  
ANISOU 3909  C   VAL B 411     7684  18868  13038  -2801   1897  -2056       C  
ATOM   3910  O   VAL B 411       9.303 -75.996  34.429  1.00101.56           O  
ANISOU 3910  O   VAL B 411     7541  18007  13037  -2371   1774  -2172       O  
ATOM   3911  CB  VAL B 411      11.805 -76.256  32.253  1.00113.37           C  
ANISOU 3911  CB  VAL B 411     7819  21292  13964  -2971   2227  -2962       C  
ATOM   3912  CG1 VAL B 411      12.556 -75.624  33.412  1.00112.14           C  
ANISOU 3912  CG1 VAL B 411     7768  20775  14062  -2948   2062  -2762       C  
ATOM   3913  CG2 VAL B 411      11.971 -77.757  32.293  1.00114.54           C  
ANISOU 3913  CG2 VAL B 411     7672  21433  14413  -2494   2237  -3629       C  
ATOM   3914  N   ILE B 412       9.861 -73.944  33.662  1.00102.57           N  
ANISOU 3914  N   ILE B 412     7667  18603  12700  -3166   1814  -1568       N  
ATOM   3915  CA  ILE B 412       9.208 -73.179  34.725  1.00 97.52           C  
ANISOU 3915  CA  ILE B 412     7496  17269  12287  -3068   1588  -1159       C  
ATOM   3916  C   ILE B 412       7.680 -73.360  34.722  1.00 93.64           C  
ANISOU 3916  C   ILE B 412     7373  16372  11833  -2879   1529   -993       C  
ATOM   3917  O   ILE B 412       7.091 -73.592  35.768  1.00 89.95           O  
ANISOU 3917  O   ILE B 412     7179  15354  11641  -2544   1400   -975       O  
ATOM   3918  CB  ILE B 412       9.533 -71.684  34.601  1.00 99.09           C  
ANISOU 3918  CB  ILE B 412     7790  17516  12343  -3538   1480   -686       C  
ATOM   3919  CG1 ILE B 412      11.020 -71.455  34.835  1.00101.27           C  
ANISOU 3919  CG1 ILE B 412     7738  18107  12632  -3702   1509   -824       C  
ATOM   3920  CG2 ILE B 412       8.709 -70.858  35.579  1.00 95.43           C  
ANISOU 3920  CG2 ILE B 412     7791  16343  12123  -3428   1231   -320       C  
ATOM   3921  CD1 ILE B 412      11.596 -70.303  34.055  1.00103.74           C  
ANISOU 3921  CD1 ILE B 412     7922  18853  12638  -4313   1503   -468       C  
ATOM   3922  N   ARG B 413       7.054 -73.243  33.551  1.00 94.22           N  
ANISOU 3922  N   ARG B 413     7434  16756  11606  -3122   1620   -869       N  
ATOM   3923  CA  ARG B 413       5.620 -73.462  33.393  1.00 91.22           C  
ANISOU 3923  CA  ARG B 413     7354  16064  11242  -2964   1577   -742       C  
ATOM   3924  C   ARG B 413       5.209 -74.813  33.956  1.00 88.75           C  
ANISOU 3924  C   ARG B 413     7053  15489  11178  -2465   1606  -1122       C  
ATOM   3925  O   ARG B 413       4.306 -74.883  34.798  1.00 85.49           O  
ANISOU 3925  O   ARG B 413     6963  14538  10981  -2206   1480  -1004       O  
ATOM   3926  CB  ARG B 413       5.222 -73.358  31.924  1.00 93.87           C  
ANISOU 3926  CB  ARG B 413     7578  16902  11186  -3307   1692   -643       C  
ATOM   3927  CG  ARG B 413       3.723 -73.418  31.578  1.00 91.98           C  
ANISOU 3927  CG  ARG B 413     7636  16390  10921  -3223   1632   -454       C  
ATOM   3928  CD  ARG B 413       3.590 -73.532  30.046  1.00 99.36           C  
ANISOU 3928  CD  ARG B 413     8362  17968  11421  -3576   1776   -454       C  
ATOM   3929  NE  ARG B 413       2.238 -73.362  29.475  1.00101.83           N  
ANISOU 3929  NE  ARG B 413     8933  18118  11638  -3626   1696   -190       N  
ATOM   3930  CZ  ARG B 413       1.825 -72.309  28.749  1.00104.52           C  
ANISOU 3930  CZ  ARG B 413     9406  18550  11754  -4062   1556    294       C  
ATOM   3931  NH1 ARG B 413       2.635 -71.283  28.509  1.00108.40           N1+
ANISOU 3931  NH1 ARG B 413     9817  19283  12087  -4520   1468    611       N1+
ATOM   3932  NH2 ARG B 413       0.588 -72.271  28.262  1.00102.92           N  
ANISOU 3932  NH2 ARG B 413     9419  18180  11505  -4059   1468    485       N  
ATOM   3933  N   LYS B 414       5.874 -75.884  33.517  1.00 90.42           N  
ANISOU 3933  N   LYS B 414     6898  16081  11376  -2341   1747  -1590       N  
ATOM   3934  CA  LYS B 414       5.476 -77.233  33.938  1.00 88.56           C  
ANISOU 3934  CA  LYS B 414     6656  15581  11411  -1892   1719  -1943       C  
ATOM   3935  C   LYS B 414       5.503 -77.360  35.460  1.00 85.33           C  
ANISOU 3935  C   LYS B 414     6472  14583  11365  -1596   1526  -1878       C  
ATOM   3936  O   LYS B 414       4.503 -77.784  36.056  1.00 82.23           O  
ANISOU 3936  O   LYS B 414     6357  13755  11131  -1355   1425  -1796       O  
ATOM   3937  CB  LYS B 414       6.272 -78.342  33.235  1.00 91.74           C  
ANISOU 3937  CB  LYS B 414     6582  16460  11813  -1789   1849  -2517       C  
ATOM   3938  CG  LYS B 414       6.219 -78.189  31.726  1.00 97.50           C  
ANISOU 3938  CG  LYS B 414     7072  17860  12113  -2126   2057  -2596       C  
ATOM   3939  CD  LYS B 414       5.763 -79.415  30.926  1.00102.43           C  
ANISOU 3939  CD  LYS B 414     7490  18700  12726  -1923   2147  -3049       C  
ATOM   3940  CE  LYS B 414       5.365 -78.955  29.480  1.00107.59           C  
ANISOU 3940  CE  LYS B 414     8048  19968  12861  -2344   2330  -2938       C  
ATOM   3941  NZ  LYS B 414       4.467 -79.824  28.612  1.00107.82           N1+
ANISOU 3941  NZ  LYS B 414     8030  20147  12789  -2230   2402  -3193       N1+
ATOM   3942  N   ASN B 415       6.614 -76.954  36.084  1.00 85.46           N  
ANISOU 3942  N   ASN B 415     6369  14621  11482  -1648   1471  -1894       N  
ATOM   3943  CA  ASN B 415       6.671 -76.875  37.545  1.00 82.48           C  
ANISOU 3943  CA  ASN B 415     6219  13732  11386  -1441   1278  -1777       C  
ATOM   3944  C   ASN B 415       5.481 -76.099  38.165  1.00 79.11           C  
ANISOU 3944  C   ASN B 415     6238  12870  10948  -1454   1179  -1375       C  
ATOM   3945  O   ASN B 415       4.882 -76.568  39.117  1.00 77.52           O  
ANISOU 3945  O   ASN B 415     6247  12275  10929  -1205   1060  -1357       O  
ATOM   3946  CB  ASN B 415       8.000 -76.287  38.022  1.00 83.99           C  
ANISOU 3946  CB  ASN B 415     6235  14042  11634  -1570   1235  -1791       C  
ATOM   3947  CG  ASN B 415       9.187 -77.238  37.819  1.00 87.41           C  
ANISOU 3947  CG  ASN B 415     6220  14782  12206  -1438   1268  -2266       C  
ATOM   3948  OD1 ASN B 415       9.248 -78.304  38.411  1.00 87.68           O  
ANISOU 3948  OD1 ASN B 415     6211  14566  12537  -1105   1136  -2513       O  
ATOM   3949  ND2 ASN B 415      10.157 -76.820  37.012  1.00 91.14           N  
ANISOU 3949  ND2 ASN B 415     6344  15801  12483  -1718   1415  -2391       N  
ATOM   3950  N   LEU B 416       5.125 -74.932  37.624  1.00 78.46           N  
ANISOU 3950  N   LEU B 416     6279  12867  10664  -1754   1205  -1064       N  
ATOM   3951  CA  LEU B 416       4.077 -74.104  38.219  1.00 75.01           C  
ANISOU 3951  CA  LEU B 416     6212  12014  10272  -1753   1079   -747       C  
ATOM   3952  C   LEU B 416       2.731 -74.798  38.134  1.00 72.79           C  
ANISOU 3952  C   LEU B 416     6110  11539  10006  -1544   1096   -769       C  
ATOM   3953  O   LEU B 416       1.874 -74.660  39.002  1.00 70.40           O  
ANISOU 3953  O   LEU B 416     6066  10863   9819  -1393    995   -665       O  
ATOM   3954  CB  LEU B 416       3.976 -72.752  37.519  1.00 76.04           C  
ANISOU 3954  CB  LEU B 416     6408  12245  10237  -2126   1042   -415       C  
ATOM   3955  CG  LEU B 416       5.126 -71.754  37.570  1.00 78.81           C  
ANISOU 3955  CG  LEU B 416     6638  12741  10562  -2421    979   -275       C  
ATOM   3956  CD1 LEU B 416       4.687 -70.470  36.899  1.00 79.98           C  
ANISOU 3956  CD1 LEU B 416     6922  12868  10597  -2782    862    120       C  
ATOM   3957  CD2 LEU B 416       5.606 -71.485  38.999  1.00 78.81           C  
ANISOU 3957  CD2 LEU B 416     6736  12396  10810  -2254    839   -309       C  
ATOM   3958  N   VAL B 417       2.531 -75.540  37.063  1.00 73.52           N  
ANISOU 3958  N   VAL B 417     6044  11923   9966  -1551   1227   -925       N  
ATOM   3959  CA  VAL B 417       1.274 -76.198  36.894  1.00 71.45           C  
ANISOU 3959  CA  VAL B 417     5935  11496   9715  -1377   1240   -943       C  
ATOM   3960  C   VAL B 417       1.252 -77.368  37.878  1.00 70.61           C  
ANISOU 3960  C   VAL B 417     5843  11133   9851  -1043   1166  -1157       C  
ATOM   3961  O   VAL B 417       0.243 -77.609  38.546  1.00 68.68           O  
ANISOU 3961  O   VAL B 417     5832  10568   9694   -889   1091  -1066       O  
ATOM   3962  CB  VAL B 417       1.069 -76.594  35.423  1.00 72.91           C  
ANISOU 3962  CB  VAL B 417     5941  12090   9672  -1508   1387  -1050       C  
ATOM   3963  CG1 VAL B 417      -0.259 -77.314  35.231  1.00 71.07           C  
ANISOU 3963  CG1 VAL B 417     5863  11674   9464  -1322   1390  -1076       C  
ATOM   3964  CG2 VAL B 417       1.116 -75.358  34.557  1.00 73.38           C  
ANISOU 3964  CG2 VAL B 417     6008  12392   9477  -1903   1403   -751       C  
ATOM   3965  N   LYS B 418       2.391 -78.051  38.004  1.00 72.95           N  
ANISOU 3965  N   LYS B 418     5877  11573  10265   -956   1159  -1428       N  
ATOM   3966  CA  LYS B 418       2.524 -79.207  38.888  1.00 73.22           C  
ANISOU 3966  CA  LYS B 418     5895  11354  10570   -669   1021  -1613       C  
ATOM   3967  C   LYS B 418       2.056 -78.805  40.288  1.00 71.84           C  
ANISOU 3967  C   LYS B 418     6023  10788  10483   -610    875  -1365       C  
ATOM   3968  O   LYS B 418       1.159 -79.439  40.894  1.00 70.66           O  
ANISOU 3968  O   LYS B 418     6053  10377  10417   -461    785  -1310       O  
ATOM   3969  CB  LYS B 418       3.970 -79.696  38.925  1.00 75.24           C  
ANISOU 3969  CB  LYS B 418     5814  11794  10978   -611    985  -1915       C  
ATOM   3970  CG  LYS B 418       4.115 -81.161  39.240  1.00 77.55           C  
ANISOU 3970  CG  LYS B 418     5976  11913  11576   -321    826  -2204       C  
ATOM   3971  CD  LYS B 418       5.319 -81.425  40.104  1.00 83.44           C  
ANISOU 3971  CD  LYS B 418     6564  12563  12576   -221    650  -2335       C  
ATOM   3972  CE  LYS B 418       5.891 -82.846  39.874  1.00 90.54           C  
ANISOU 3972  CE  LYS B 418     7143  13447  13810     33    497  -2770       C  
ATOM   3973  NZ  LYS B 418       7.335 -83.025  40.404  1.00 93.78           N1+
ANISOU 3973  NZ  LYS B 418     7274  13879  14476    112    342  -2993       N1+
ATOM   3974  N   LYS B 419       2.636 -77.708  40.756  1.00 72.31           N  
ANISOU 3974  N   LYS B 419     6126  10850  10499   -758    855  -1219       N  
ATOM   3975  CA  LYS B 419       2.400 -77.215  42.068  1.00 71.56           C  
ANISOU 3975  CA  LYS B 419     6257  10466  10464   -727    727  -1051       C  
ATOM   3976  C   LYS B 419       0.990 -76.673  42.261  1.00 70.69           C  
ANISOU 3976  C   LYS B 419     6422  10174  10261   -741    737   -859       C  
ATOM   3977  O   LYS B 419       0.370 -76.948  43.287  1.00 70.12           O  
ANISOU 3977  O   LYS B 419     6515   9894  10233   -635    647   -814       O  
ATOM   3978  CB  LYS B 419       3.478 -76.203  42.411  1.00 72.89           C  
ANISOU 3978  CB  LYS B 419     6358  10702  10634   -880    693   -996       C  
ATOM   3979  CG  LYS B 419       4.828 -76.849  42.742  1.00 74.77           C  
ANISOU 3979  CG  LYS B 419     6349  11031  11029   -804    620  -1200       C  
ATOM   3980  CD  LYS B 419       4.614 -78.123  43.536  1.00 76.17           C  
ANISOU 3980  CD  LYS B 419     6564  10988  11389   -565    466  -1295       C  
ATOM   3981  CE  LYS B 419       5.867 -78.646  44.171  1.00 79.58           C  
ANISOU 3981  CE  LYS B 419     6803  11400  12032   -478    304  -1447       C  
ATOM   3982  NZ  LYS B 419       6.068 -78.032  45.520  1.00 82.69           N1+
ANISOU 3982  NZ  LYS B 419     7377  11608  12434   -522    159  -1271       N1+
ATOM   3983  N   CYS B 420       0.464 -75.930  41.291  1.00 71.60           N  
ANISOU 3983  N   CYS B 420     6571  10387  10245   -886    829   -752       N  
ATOM   3984  CA  CYS B 420      -0.929 -75.482  41.365  1.00 71.29           C  
ANISOU 3984  CA  CYS B 420     6756  10170  10161   -873    819   -614       C  
ATOM   3985  C   CYS B 420      -1.879 -76.660  41.456  1.00 70.53           C  
ANISOU 3985  C   CYS B 420     6719   9996  10082   -695    839   -689       C  
ATOM   3986  O   CYS B 420      -2.869 -76.641  42.211  1.00 69.43           O  
ANISOU 3986  O   CYS B 420     6750   9678   9949   -620    795   -634       O  
ATOM   3987  CB  CYS B 420      -1.313 -74.646  40.159  1.00 71.86           C  
ANISOU 3987  CB  CYS B 420     6831  10355  10116  -1065    869   -473       C  
ATOM   3988  SG  CYS B 420      -0.716 -72.956  40.268  1.00 77.46           S  
ANISOU 3988  SG  CYS B 420     7575  11002  10851  -1309    748   -275       S  
ATOM   3989  N   LEU B 421      -1.595 -77.700  40.686  1.00 71.74           N  
ANISOU 3989  N   LEU B 421     6710  10304  10245   -635    898   -838       N  
ATOM   3990  CA  LEU B 421      -2.466 -78.861  40.726  1.00 71.50           C  
ANISOU 3990  CA  LEU B 421     6728  10172  10266   -478    881   -904       C  
ATOM   3991  C   LEU B 421      -2.337 -79.550  42.085  1.00 71.42           C  
ANISOU 3991  C   LEU B 421     6783   9960  10391   -360    727   -904       C  
ATOM   3992  O   LEU B 421      -3.308 -80.088  42.621  1.00 70.52           O  
ANISOU 3992  O   LEU B 421     6806   9704  10284   -297    673   -837       O  
ATOM   3993  CB  LEU B 421      -2.126 -79.808  39.594  1.00 72.89           C  
ANISOU 3993  CB  LEU B 421     6686  10548  10460   -431    946  -1117       C  
ATOM   3994  CG  LEU B 421      -2.518 -79.348  38.200  1.00 74.03           C  
ANISOU 3994  CG  LEU B 421     6776  10938  10411   -574   1093  -1100       C  
ATOM   3995  CD1 LEU B 421      -2.265 -80.505  37.232  1.00 77.19           C  
ANISOU 3995  CD1 LEU B 421     6941  11551  10837   -490   1148  -1392       C  
ATOM   3996  CD2 LEU B 421      -3.967 -78.923  38.166  1.00 71.48           C  
ANISOU 3996  CD2 LEU B 421     6688  10458  10011   -590   1099   -905       C  
ATOM   3997  N   GLU B 422      -1.123 -79.506  42.631  1.00 72.49           N  
ANISOU 3997  N   GLU B 422     6813  10110  10620   -362    645   -961       N  
ATOM   3998  CA  GLU B 422      -0.833 -80.055  43.939  1.00 72.68           C  
ANISOU 3998  CA  GLU B 422     6891   9964  10758   -295    461   -925       C  
ATOM   3999  C   GLU B 422      -1.603 -79.261  44.981  1.00 70.79           C  
ANISOU 3999  C   GLU B 422     6873   9634  10387   -367    447   -754       C  
ATOM   4000  O   GLU B 422      -2.332 -79.861  45.777  1.00 70.67           O  
ANISOU 4000  O   GLU B 422     6976   9523  10353   -345    358   -673       O  
ATOM   4001  CB  GLU B 422       0.671 -80.023  44.192  1.00 74.78           C  
ANISOU 4001  CB  GLU B 422     6976  10285  11151   -294    376  -1032       C  
ATOM   4002  CG  GLU B 422       1.151 -80.663  45.484  1.00 78.78           C  
ANISOU 4002  CG  GLU B 422     7511  10620  11800   -238    136   -987       C  
ATOM   4003  CD  GLU B 422       2.673 -80.636  45.584  1.00 86.53           C  
ANISOU 4003  CD  GLU B 422     8275  11664  12937   -221     48  -1126       C  
ATOM   4004  OE1 GLU B 422       3.331 -81.316  44.748  1.00 90.78           O  
ANISOU 4004  OE1 GLU B 422     8561  12291  13638   -126     45  -1361       O  
ATOM   4005  OE2 GLU B 422       3.215 -79.923  46.476  1.00 87.77           O1-
ANISOU 4005  OE2 GLU B 422     8488  11802  13056   -300    -14  -1037       O1-
ATOM   4006  N   LEU B 423      -1.473 -77.930  44.954  1.00 69.31           N  
ANISOU 4006  N   LEU B 423     6724   9493  10116   -468    520   -715       N  
ATOM   4007  CA  LEU B 423      -2.308 -77.075  45.783  1.00 67.77           C  
ANISOU 4007  CA  LEU B 423     6698   9228   9823   -513    513   -640       C  
ATOM   4008  C   LEU B 423      -3.794 -77.444  45.721  1.00 67.81           C  
ANISOU 4008  C   LEU B 423     6815   9199   9747   -472    565   -607       C  
ATOM   4009  O   LEU B 423      -4.411 -77.635  46.767  1.00 67.62           O  
ANISOU 4009  O   LEU B 423     6882   9161   9648   -477    514   -582       O  
ATOM   4010  CB  LEU B 423      -2.154 -75.617  45.404  1.00 67.11           C  
ANISOU 4010  CB  LEU B 423     6624   9147   9727   -611    553   -619       C  
ATOM   4011  CG  LEU B 423      -3.112 -74.662  46.129  1.00 63.45           C  
ANISOU 4011  CG  LEU B 423     6295   8589   9222   -622    525   -623       C  
ATOM   4012  CD1 LEU B 423      -2.866 -74.698  47.630  1.00 60.30           C  
ANISOU 4012  CD1 LEU B 423     5936   8193   8782   -618    432   -674       C  
ATOM   4013  CD2 LEU B 423      -3.000 -73.237  45.584  1.00 59.14           C  
ANISOU 4013  CD2 LEU B 423     5752   7971   8744   -718    495   -589       C  
ATOM   4014  N   PHE B 424      -4.354 -77.564  44.512  1.00 68.13           N  
ANISOU 4014  N   PHE B 424     6834   9268   9783   -454    665   -610       N  
ATOM   4015  CA  PHE B 424      -5.793 -77.781  44.364  1.00 68.25           C  
ANISOU 4015  CA  PHE B 424     6944   9253   9733   -421    716   -585       C  
ATOM   4016  C   PHE B 424      -6.201 -79.108  44.965  1.00 69.81           C  
ANISOU 4016  C   PHE B 424     7167   9425   9930   -372    649   -562       C  
ATOM   4017  O   PHE B 424      -7.229 -79.201  45.642  1.00 69.96           O  
ANISOU 4017  O   PHE B 424     7275   9448   9856   -393    648   -525       O  
ATOM   4018  CB  PHE B 424      -6.269 -77.686  42.910  1.00 67.48           C  
ANISOU 4018  CB  PHE B 424     6815   9199   9625   -426    813   -580       C  
ATOM   4019  CG  PHE B 424      -5.955 -76.361  42.216  1.00 67.08           C  
ANISOU 4019  CG  PHE B 424     6749   9170   9568   -535    830   -530       C  
ATOM   4020  CD1 PHE B 424      -5.649 -75.208  42.934  1.00 66.09           C  
ANISOU 4020  CD1 PHE B 424     6667   8962   9482   -590    755   -510       C  
ATOM   4021  CD2 PHE B 424      -6.008 -76.274  40.831  1.00 66.14           C  
ANISOU 4021  CD2 PHE B 424     6569   9158   9402   -607    894   -491       C  
ATOM   4022  CE1 PHE B 424      -5.376 -74.016  42.295  1.00 64.99           C  
ANISOU 4022  CE1 PHE B 424     6519   8796   9377   -716    710   -425       C  
ATOM   4023  CE2 PHE B 424      -5.737 -75.085  40.187  1.00 66.71           C  
ANISOU 4023  CE2 PHE B 424     6634   9254   9459   -764    864   -379       C  
ATOM   4024  CZ  PHE B 424      -5.423 -73.949  40.921  1.00 66.17           C  
ANISOU 4024  CZ  PHE B 424     6619   9049   9471   -820    755   -331       C  
ATOM   4025  N   THR B 425      -5.391 -80.140  44.746  1.00 72.30           N  
ANISOU 4025  N   THR B 425     7385   9719  10363   -323    569   -591       N  
ATOM   4026  CA  THR B 425      -5.657 -81.437  45.384  1.00 74.67           C  
ANISOU 4026  CA  THR B 425     7711   9935  10722   -301    419   -529       C  
ATOM   4027  C   THR B 425      -5.778 -81.299  46.903  1.00 75.74           C  
ANISOU 4027  C   THR B 425     7946  10082  10746   -403    314   -412       C  
ATOM   4028  O   THR B 425      -6.724 -81.815  47.485  1.00 76.22           O  
ANISOU 4028  O   THR B 425     8089  10160  10709   -470    271   -308       O  
ATOM   4029  CB  THR B 425      -4.577 -82.485  45.080  1.00 75.79           C  
ANISOU 4029  CB  THR B 425     7706   9999  11090   -215    270   -614       C  
ATOM   4030  OG1 THR B 425      -4.405 -82.582  43.666  1.00 77.76           O  
ANISOU 4030  OG1 THR B 425     7820  10323  11399   -140    389   -781       O  
ATOM   4031  CG2 THR B 425      -5.009 -83.845  45.605  1.00 77.58           C  
ANISOU 4031  CG2 THR B 425     7971  10074  11430   -205     53   -515       C  
ATOM   4032  N   GLU B 426      -4.817 -80.604  47.517  1.00 76.86           N  
ANISOU 4032  N   GLU B 426     8068  10253  10882   -438    275   -432       N  
ATOM   4033  CA  GLU B 426      -4.794 -80.381  48.953  1.00 78.41           C  
ANISOU 4033  CA  GLU B 426     8336  10513  10940   -552    177   -352       C  
ATOM   4034  C   GLU B 426      -6.041 -79.642  49.401  1.00 77.97           C  
ANISOU 4034  C   GLU B 426     8363  10589  10671   -619    305   -379       C  
ATOM   4035  O   GLU B 426      -6.603 -79.967  50.441  1.00 78.66           O  
ANISOU 4035  O   GLU B 426     8501  10798  10585   -742    246   -302       O  
ATOM   4036  CB  GLU B 426      -3.531 -79.616  49.358  1.00 79.29           C  
ANISOU 4036  CB  GLU B 426     8396  10633  11097   -563    130   -408       C  
ATOM   4037  CG  GLU B 426      -2.242 -80.426  49.152  1.00 83.93           C  
ANISOU 4037  CG  GLU B 426     8863  11118  11907   -500    -31   -412       C  
ATOM   4038  CD  GLU B 426      -0.936 -79.606  49.285  1.00 89.15           C  
ANISOU 4038  CD  GLU B 426     9435  11804  12634   -505    -46   -493       C  
ATOM   4039  OE1 GLU B 426      -0.990 -78.393  49.638  1.00 88.47           O  
ANISOU 4039  OE1 GLU B 426     9400  11786  12427   -569     40   -525       O  
ATOM   4040  OE2 GLU B 426       0.152 -80.202  49.035  1.00 91.38           O1-
ANISOU 4040  OE2 GLU B 426     9575  12026  13116   -439   -166   -548       O1-
ATOM   4041  N   LEU B 427      -6.489 -78.669  48.605  1.00 77.24           N  
ANISOU 4041  N   LEU B 427     8264  10488  10593   -556    461   -494       N  
ATOM   4042  CA  LEU B 427      -7.705 -77.928  48.921  1.00 77.69           C  
ANISOU 4042  CA  LEU B 427     8359  10641  10517   -579    559   -584       C  
ATOM   4043  C   LEU B 427      -8.878 -78.861  48.973  1.00 78.82           C  
ANISOU 4043  C   LEU B 427     8531  10856  10559   -615    584   -514       C  
ATOM   4044  O   LEU B 427      -9.789 -78.668  49.771  1.00 79.89           O  
ANISOU 4044  O   LEU B 427     8672  11165  10517   -695    623   -570       O  
ATOM   4045  CB  LEU B 427      -8.006 -76.830  47.906  1.00 76.18           C  
ANISOU 4045  CB  LEU B 427     8153  10360  10429   -502    652   -683       C  
ATOM   4046  CG  LEU B 427      -7.196 -75.537  48.000  1.00 76.17           C  
ANISOU 4046  CG  LEU B 427     8130  10295  10515   -508    612   -763       C  
ATOM   4047  CD1 LEU B 427      -7.752 -74.491  47.070  1.00 74.87           C  
ANISOU 4047  CD1 LEU B 427     7965  10016  10464   -471    638   -812       C  
ATOM   4048  CD2 LEU B 427      -7.116 -75.006  49.403  1.00 76.13           C  
ANISOU 4048  CD2 LEU B 427     8123  10390  10409   -560    556   -882       C  
ATOM   4049  N   ALA B 428      -8.849 -79.871  48.113  1.00 79.78           N  
ANISOU 4049  N   ALA B 428     8649  10867  10795   -564    558   -418       N  
ATOM   4050  CA  ALA B 428      -9.928 -80.838  48.003  1.00 81.01           C  
ANISOU 4050  CA  ALA B 428     8830  11048  10898   -600    557   -333       C  
ATOM   4051  C   ALA B 428     -10.006 -81.740  49.214  1.00 83.72           C  
ANISOU 4051  C   ALA B 428     9206  11486  11114   -768    404   -168       C  
ATOM   4052  O   ALA B 428     -11.103 -82.111  49.638  1.00 84.55           O  
ANISOU 4052  O   ALA B 428     9330  11736  11058   -886    426   -106       O  
ATOM   4053  CB  ALA B 428      -9.754 -81.656  46.752  1.00 80.38           C  
ANISOU 4053  CB  ALA B 428     8720  10812  11005   -494    539   -313       C  
ATOM   4054  N   GLU B 429      -8.852 -82.086  49.778  1.00 86.36           N  
ANISOU 4054  N   GLU B 429     9538  11759  11514   -806    231    -80       N  
ATOM   4055  CA  GLU B 429      -8.821 -83.022  50.894  1.00 90.44           C  
ANISOU 4055  CA  GLU B 429    10095  12338  11929  -1004     15    141       C  
ATOM   4056  C   GLU B 429      -9.395 -82.411  52.186  1.00 92.10           C  
ANISOU 4056  C   GLU B 429    10321  12882  11790  -1210     75    137       C  
ATOM   4057  O   GLU B 429      -9.815 -83.120  53.101  1.00 94.31           O  
ANISOU 4057  O   GLU B 429    10630  13330  11874  -1450    -55    340       O  
ATOM   4058  CB  GLU B 429      -7.443 -83.700  51.047  1.00 91.86           C  
ANISOU 4058  CB  GLU B 429    10252  12314  12334   -975   -243    243       C  
ATOM   4059  CG  GLU B 429      -6.327 -82.896  51.731  1.00 96.30           C  
ANISOU 4059  CG  GLU B 429    10794  12933  12862   -986   -276    181       C  
ATOM   4060  CD  GLU B 429      -4.908 -83.474  51.451  1.00102.30           C  
ANISOU 4060  CD  GLU B 429    11479  13452  13936   -873   -494    192       C  
ATOM   4061  OE1 GLU B 429      -3.898 -82.939  52.001  1.00104.17           O  
ANISOU 4061  OE1 GLU B 429    11686  13713  14177   -884   -555    158       O  
ATOM   4062  OE2 GLU B 429      -4.802 -84.459  50.669  1.00103.69           O1-
ANISOU 4062  OE2 GLU B 429    11602  13419  14374   -764   -612    198       O1-
ATOM   4063  N   ASP B 430      -9.445 -81.084  52.202  1.00 92.17           N  
ANISOU 4063  N   ASP B 430    10293  12996  11728  -1128    261   -108       N  
ATOM   4064  CA  ASP B 430     -10.248 -80.289  53.123  1.00 94.31           C  
ANISOU 4064  CA  ASP B 430    10523  13601  11707  -1250    384   -267       C  
ATOM   4065  C   ASP B 430     -11.698 -80.242  52.607  1.00 94.16           C  
ANISOU 4065  C   ASP B 430    10467  13677  11632  -1221    551   -370       C  
ATOM   4066  O   ASP B 430     -12.082 -79.294  51.938  1.00 93.19           O  
ANISOU 4066  O   ASP B 430    10303  13483  11621  -1049    690   -599       O  
ATOM   4067  CB  ASP B 430      -9.650 -78.881  53.137  1.00 94.27           C  
ANISOU 4067  CB  ASP B 430    10477  13564  11774  -1118    462   -527       C  
ATOM   4068  CG  ASP B 430     -10.281 -77.967  54.167  1.00 98.01           C  
ANISOU 4068  CG  ASP B 430    10871  14374  11994  -1211    554   -783       C  
ATOM   4069  OD1 ASP B 430     -11.409 -78.245  54.623  1.00101.32           O  
ANISOU 4069  OD1 ASP B 430    11236  15082  12178  -1344    632   -824       O  
ATOM   4070  OD2 ASP B 430      -9.643 -76.944  54.513  1.00100.31           O1-
ANISOU 4070  OD2 ASP B 430    11129  14656  12328  -1154    546   -975       O1-
ATOM   4071  N   LYS B 431     -12.505 -81.253  52.927  1.00 96.09           N  
ANISOU 4071  N   LYS B 431    10719  14073  11716  -1406    507   -185       N  
ATOM   4072  CA  LYS B 431     -13.819 -81.474  52.268  1.00 95.70           C  
ANISOU 4072  CA  LYS B 431    10635  14062  11661  -1376    636   -233       C  
ATOM   4073  C   LYS B 431     -14.942 -80.442  52.532  1.00 96.12           C  
ANISOU 4073  C   LYS B 431    10563  14404  11552  -1358    843   -561       C  
ATOM   4074  O   LYS B 431     -15.757 -80.206  51.654  1.00 95.38           O  
ANISOU 4074  O   LYS B 431    10436  14216  11585  -1213    950   -682       O  
ATOM   4075  CB  LYS B 431     -14.311 -82.921  52.472  1.00 97.25           C  
ANISOU 4075  CB  LYS B 431    10874  14301  11774  -1596    493     87       C  
ATOM   4076  CG  LYS B 431     -13.656 -83.961  51.521  1.00 97.17           C  
ANISOU 4076  CG  LYS B 431    10947  13871  12099  -1475    308    293       C  
ATOM   4077  CD  LYS B 431     -13.842 -85.401  52.049  1.00101.20           C  
ANISOU 4077  CD  LYS B 431    11507  14376  12567  -1738     45    654       C  
ATOM   4078  CE  LYS B 431     -14.082 -86.436  50.939  1.00100.96           C  
ANISOU 4078  CE  LYS B 431    11506  14012  12841  -1622    -66    753       C  
ATOM   4079  NZ  LYS B 431     -14.255 -87.808  51.508  1.00103.23           N1+
ANISOU 4079  NZ  LYS B 431    11842  14243  13136  -1897   -388   1123       N1+
ATOM   4080  N   GLU B 432     -15.009 -79.839  53.715  1.00 98.00           N  
ANISOU 4080  N   GLU B 432    10710  15000  11523  -1500    885   -734       N  
ATOM   4081  CA  GLU B 432     -15.746 -78.574  53.847  1.00 98.40           C  
ANISOU 4081  CA  GLU B 432    10608  15229  11549  -1382   1047  -1169       C  
ATOM   4082  C   GLU B 432     -14.795 -77.492  53.284  1.00 96.79           C  
ANISOU 4082  C   GLU B 432    10447  14672  11656  -1125   1009  -1321       C  
ATOM   4083  O   GLU B 432     -13.568 -77.605  53.413  1.00 96.48           O  
ANISOU 4083  O   GLU B 432    10501  14476  11679  -1135    895  -1160       O  
ATOM   4084  CB  GLU B 432     -16.076 -78.260  55.313  1.00101.85           C  
ANISOU 4084  CB  GLU B 432    10894  16210  11592  -1618   1102  -1376       C  
ATOM   4085  CG  GLU B 432     -17.088 -79.183  56.019  1.00104.75           C  
ANISOU 4085  CG  GLU B 432    11174  17055  11569  -1953   1151  -1246       C  
ATOM   4086  CD  GLU B 432     -17.194 -78.895  57.531  1.00109.19           C  
ANISOU 4086  CD  GLU B 432    11577  18238  11672  -2248   1195  -1430       C  
ATOM   4087  OE1 GLU B 432     -16.796 -79.755  58.355  1.00110.06           O  
ANISOU 4087  OE1 GLU B 432    11753  18582  11481  -2590   1066  -1080       O  
ATOM   4088  OE2 GLU B 432     -17.667 -77.796  57.903  1.00110.98           O1-
ANISOU 4088  OE2 GLU B 432    11599  18724  11843  -2145   1336  -1941       O1-
ATOM   4089  N   ASN B 433     -15.339 -76.455  52.653  1.00 95.51           N  
ANISOU 4089  N   ASN B 433    10209  14374  11706   -914   1073  -1612       N  
ATOM   4090  CA  ASN B 433     -14.529 -75.329  52.087  1.00 93.32           C  
ANISOU 4090  CA  ASN B 433     9965  13756  11735   -713   1000  -1731       C  
ATOM   4091  C   ASN B 433     -13.549 -75.578  50.909  1.00 89.28           C  
ANISOU 4091  C   ASN B 433     9601  12849  11471   -617    925  -1446       C  
ATOM   4092  O   ASN B 433     -12.700 -74.734  50.602  1.00 89.08           O  
ANISOU 4092  O   ASN B 433     9600  12608  11638   -529    852  -1487       O  
ATOM   4093  CB  ASN B 433     -13.959 -74.376  53.180  1.00 95.93           C  
ANISOU 4093  CB  ASN B 433    10213  14236  11998   -738    955  -2001       C  
ATOM   4094  CG  ASN B 433     -12.890 -75.016  54.064  1.00 97.76           C  
ANISOU 4094  CG  ASN B 433    10519  14611  12011   -925    889  -1783       C  
ATOM   4095  OD1 ASN B 433     -13.072 -75.149  55.274  1.00100.79           O  
ANISOU 4095  OD1 ASN B 433    10820  15397  12076  -1112    911  -1886       O  
ATOM   4096  ND2 ASN B 433     -11.757 -75.378  53.467  1.00 97.93           N  
ANISOU 4096  ND2 ASN B 433    10675  14330  12201   -887    795  -1500       N  
ATOM   4097  N   TYR B 434     -13.695 -76.719  50.240  1.00 86.06           N  
ANISOU 4097  N   TYR B 434     9268  12374  11057   -647    939  -1185       N  
ATOM   4098  CA  TYR B 434     -13.254 -76.848  48.854  1.00 82.19           C  
ANISOU 4098  CA  TYR B 434     8850  11578  10797   -529    916  -1034       C  
ATOM   4099  C   TYR B 434     -14.314 -76.165  48.017  1.00 81.53           C  
ANISOU 4099  C   TYR B 434     8724  11403  10848   -412    963  -1174       C  
ATOM   4100  O   TYR B 434     -14.022 -75.659  46.961  1.00 80.68           O  
ANISOU 4100  O   TYR B 434     8650  11071  10932   -326    925  -1129       O  
ATOM   4101  CB  TYR B 434     -13.117 -78.314  48.437  1.00 80.78           C  
ANISOU 4101  CB  TYR B 434     8734  11363  10594   -583    893   -777       C  
ATOM   4102  CG  TYR B 434     -12.678 -78.546  46.999  1.00 76.89           C  
ANISOU 4102  CG  TYR B 434     8276  10638  10298   -474    887   -681       C  
ATOM   4103  CD1 TYR B 434     -11.390 -78.229  46.589  1.00 75.20           C  
ANISOU 4103  CD1 TYR B 434     8068  10299  10205   -437    838   -648       C  
ATOM   4104  CD2 TYR B 434     -13.555 -79.093  46.049  1.00 74.62           C  
ANISOU 4104  CD2 TYR B 434     7994  10305  10053   -430    935   -639       C  
ATOM   4105  CE1 TYR B 434     -10.982 -78.440  45.289  1.00 73.70           C  
ANISOU 4105  CE1 TYR B 434     7869   9993  10138   -376    852   -593       C  
ATOM   4106  CE2 TYR B 434     -13.160 -79.307  44.728  1.00 71.69           C  
ANISOU 4106  CE2 TYR B 434     7631   9790   9815   -355    938   -583       C  
ATOM   4107  CZ  TYR B 434     -11.869 -78.978  44.370  1.00 73.35           C  
ANISOU 4107  CZ  TYR B 434     7830   9930  10111   -338    904   -568       C  
ATOM   4108  OH  TYR B 434     -11.425 -79.178  43.100  1.00 74.26           O  
ANISOU 4108  OH  TYR B 434     7915   9994  10306   -300    923   -544       O  
ATOM   4109  N   LYS B 435     -15.553 -76.180  48.503  1.00 82.33           N  
ANISOU 4109  N   LYS B 435     8738  11708  10836   -433   1031  -1337       N  
ATOM   4110  CA  LYS B 435     -16.647 -75.349  48.003  1.00 82.55           C  
ANISOU 4110  CA  LYS B 435     8678  11673  11012   -309   1042  -1558       C  
ATOM   4111  C   LYS B 435     -16.184 -73.958  47.628  1.00 81.87           C  
ANISOU 4111  C   LYS B 435     8584  11330  11193   -188    921  -1691       C  
ATOM   4112  O   LYS B 435     -16.549 -73.424  46.588  1.00 81.04           O  
ANISOU 4112  O   LYS B 435     8491  10991  11308    -93    847  -1673       O  
ATOM   4113  CB  LYS B 435     -17.684 -75.158  49.110  1.00 85.23           C  
ANISOU 4113  CB  LYS B 435     8850  12353  11178   -358   1118  -1860       C  
ATOM   4114  CG  LYS B 435     -18.612 -76.334  49.352  1.00 89.02           C  
ANISOU 4114  CG  LYS B 435     9295  13110  11419   -498   1225  -1760       C  
ATOM   4115  CD  LYS B 435     -19.527 -76.106  50.574  1.00 96.21           C  
ANISOU 4115  CD  LYS B 435     9996  14474  12085   -604   1320  -2085       C  
ATOM   4116  CE  LYS B 435     -19.554 -74.629  51.024  1.00100.71           C  
ANISOU 4116  CE  LYS B 435    10411  15045  12807   -454   1278  -2535       C  
ATOM   4117  NZ  LYS B 435     -18.457 -74.279  52.014  1.00102.40           N1+
ANISOU 4117  NZ  LYS B 435    10643  15366  12897   -537   1236  -2585       N1+
ATOM   4118  N   LYS B 436     -15.402 -73.368  48.521  1.00 81.92           N  
ANISOU 4118  N   LYS B 436     8566  11382  11178   -214    871  -1815       N  
ATOM   4119  CA  LYS B 436     -14.989 -71.998  48.392  1.00 82.26           C  
ANISOU 4119  CA  LYS B 436     8581  11185  11486   -120    719  -1972       C  
ATOM   4120  C   LYS B 436     -14.064 -71.761  47.207  1.00 79.92           C  
ANISOU 4120  C   LYS B 436     8409  10582  11373   -125    621  -1683       C  
ATOM   4121  O   LYS B 436     -14.102 -70.714  46.607  1.00 81.64           O  
ANISOU 4121  O   LYS B 436     8620  10540  11856    -67    461  -1718       O  
ATOM   4122  CB  LYS B 436     -14.312 -71.545  49.671  1.00 84.24           C  
ANISOU 4122  CB  LYS B 436     8775  11586  11643   -167    693  -2169       C  
ATOM   4123  CG  LYS B 436     -15.252 -71.285  50.813  1.00 88.66           C  
ANISOU 4123  CG  LYS B 436     9151  12470  12064   -160    753  -2576       C  
ATOM   4124  CD  LYS B 436     -14.479 -70.572  51.900  1.00 95.00           C  
ANISOU 4124  CD  LYS B 436     9893  13369  12832   -188    684  -2806       C  
ATOM   4125  CE  LYS B 436     -15.019 -70.874  53.293  1.00100.55           C  
ANISOU 4125  CE  LYS B 436    10435  14593  13175   -306    811  -3096       C  
ATOM   4126  NZ  LYS B 436     -13.962 -70.536  54.314  1.00104.84           N1+
ANISOU 4126  NZ  LYS B 436    10976  15260  13595   -395    754  -3181       N1+
ATOM   4127  N   PHE B 437     -13.207 -72.709  46.885  1.00 76.95           N  
ANISOU 4127  N   PHE B 437     8126  10247  10864   -211    691  -1407       N  
ATOM   4128  CA  PHE B 437     -12.388 -72.605  45.693  1.00 74.37           C  
ANISOU 4128  CA  PHE B 437     7871   9733  10651   -244    637  -1164       C  
ATOM   4129  C   PHE B 437     -13.229 -73.033  44.483  1.00 73.10           C  
ANISOU 4129  C   PHE B 437     7734   9523  10516   -220    673  -1044       C  
ATOM   4130  O   PHE B 437     -13.377 -72.292  43.518  1.00 73.70           O  
ANISOU 4130  O   PHE B 437     7824   9421  10755   -223    564   -968       O  
ATOM   4131  CB  PHE B 437     -11.142 -73.479  45.864  1.00 73.31           C  
ANISOU 4131  CB  PHE B 437     7774   9693  10386   -324    693  -1000       C  
ATOM   4132  CG  PHE B 437     -10.433 -73.784  44.595  1.00 71.12           C  
ANISOU 4132  CG  PHE B 437     7521   9352  10147   -369    701   -793       C  
ATOM   4133  CD1 PHE B 437     -10.726 -74.930  43.882  1.00 70.65           C  
ANISOU 4133  CD1 PHE B 437     7469   9365  10008   -360    792   -695       C  
ATOM   4134  CD2 PHE B 437      -9.476 -72.928  44.102  1.00 71.17           C  
ANISOU 4134  CD2 PHE B 437     7521   9257  10261   -440    613   -712       C  
ATOM   4135  CE1 PHE B 437     -10.069 -75.209  42.661  1.00 69.87           C  
ANISOU 4135  CE1 PHE B 437     7351   9275   9919   -409    814   -568       C  
ATOM   4136  CE2 PHE B 437      -8.833 -73.199  42.910  1.00 71.35           C  
ANISOU 4136  CE2 PHE B 437     7528   9315  10266   -523    642   -544       C  
ATOM   4137  CZ  PHE B 437      -9.124 -74.347  42.193  1.00 69.17           C  
ANISOU 4137  CZ  PHE B 437     7238   9151   9892   -500    753   -497       C  
ATOM   4138  N   TYR B 438     -13.806 -74.220  44.554  1.00 71.48           N  
ANISOU 4138  N   TYR B 438     7531   9473  10151   -218    799  -1013       N  
ATOM   4139  CA  TYR B 438     -14.555 -74.784  43.450  1.00 70.48           C  
ANISOU 4139  CA  TYR B 438     7425   9324  10029   -199    840   -908       C  
ATOM   4140  C   TYR B 438     -15.696 -73.959  42.881  1.00 71.32           C  
ANISOU 4140  C   TYR B 438     7500   9305  10292   -131    759   -993       C  
ATOM   4141  O   TYR B 438     -15.925 -74.002  41.699  1.00 71.03           O  
ANISOU 4141  O   TYR B 438     7497   9187  10303   -146    728   -852       O  
ATOM   4142  CB  TYR B 438     -15.076 -76.173  43.807  1.00 70.05           C  
ANISOU 4142  CB  TYR B 438     7370   9438   9806   -215    951   -881       C  
ATOM   4143  CG  TYR B 438     -15.476 -76.952  42.590  1.00 69.31           C  
ANISOU 4143  CG  TYR B 438     7302   9314   9715   -206    987   -755       C  
ATOM   4144  CD1 TYR B 438     -14.530 -77.644  41.835  1.00 70.23           C  
ANISOU 4144  CD1 TYR B 438     7440   9422   9821   -235    999   -627       C  
ATOM   4145  CD2 TYR B 438     -16.782 -76.970  42.172  1.00 68.65           C  
ANISOU 4145  CD2 TYR B 438     7197   9231   9657   -163   1004   -803       C  
ATOM   4146  CE1 TYR B 438     -14.905 -78.342  40.695  1.00 70.65           C  
ANISOU 4146  CE1 TYR B 438     7493   9481   9869   -225   1030   -566       C  
ATOM   4147  CE2 TYR B 438     -17.148 -77.653  41.062  1.00 69.98           C  
ANISOU 4147  CE2 TYR B 438     7386   9381   9821   -159   1027   -702       C  
ATOM   4148  CZ  TYR B 438     -16.224 -78.333  40.328  1.00 69.88           C  
ANISOU 4148  CZ  TYR B 438     7396   9373   9781   -192   1042   -591       C  
ATOM   4149  OH  TYR B 438     -16.652 -79.006  39.222  1.00 73.24           O  
ANISOU 4149  OH  TYR B 438     7820   9812  10193   -187   1065   -542       O  
ATOM   4150  N   GLU B 439     -16.444 -73.233  43.692  1.00 73.42           N  
ANISOU 4150  N   GLU B 439     7683   9570  10642    -57    710  -1244       N  
ATOM   4151  CA  GLU B 439     -17.507 -72.427  43.096  1.00 75.53           C  
ANISOU 4151  CA  GLU B 439     7898   9671  11129     30    580  -1345       C  
ATOM   4152  C   GLU B 439     -16.961 -71.210  42.356  1.00 75.79           C  
ANISOU 4152  C   GLU B 439     7972   9407  11417      9    347  -1236       C  
ATOM   4153  O   GLU B 439     -17.604 -70.689  41.462  1.00 77.00           O  
ANISOU 4153  O   GLU B 439     8127   9375  11755     30    190  -1171       O  
ATOM   4154  CB  GLU B 439     -18.673 -72.107  44.064  1.00 77.93           C  
ANISOU 4154  CB  GLU B 439     8044  10091  11474    137    593  -1713       C  
ATOM   4155  CG  GLU B 439     -18.394 -71.187  45.248  1.00 85.48           C  
ANISOU 4155  CG  GLU B 439     8895  11072  12510    185    523  -2026       C  
ATOM   4156  CD  GLU B 439     -19.579 -71.128  46.276  1.00 95.24           C  
ANISOU 4156  CD  GLU B 439     9920  12576  13689    260    602  -2450       C  
ATOM   4157  OE1 GLU B 439     -20.727 -71.569  45.967  1.00 96.79           O  
ANISOU 4157  OE1 GLU B 439    10040  12872  13861    296    669  -2509       O  
ATOM   4158  OE2 GLU B 439     -19.353 -70.620  47.410  1.00100.37           O1-
ANISOU 4158  OE2 GLU B 439    10456  13374  14303    272    601  -2751       O1-
ATOM   4159  N   GLN B 440     -15.752 -70.791  42.706  1.00 75.15           N  
ANISOU 4159  N   GLN B 440     7927   9284  11343    -59    301  -1180       N  
ATOM   4160  CA  GLN B 440     -15.073 -69.727  41.985  1.00 75.14           C  
ANISOU 4160  CA  GLN B 440     7972   9027  11550   -145     71  -1005       C  
ATOM   4161  C   GLN B 440     -14.378 -70.198  40.706  1.00 73.65           C  
ANISOU 4161  C   GLN B 440     7868   8891  11221   -314    113   -648       C  
ATOM   4162  O   GLN B 440     -14.383 -69.497  39.715  1.00 74.90           O  
ANISOU 4162  O   GLN B 440     8060   8888  11511   -422    -79   -446       O  
ATOM   4163  CB  GLN B 440     -14.041 -69.069  42.895  1.00 75.85           C  
ANISOU 4163  CB  GLN B 440     8048   9070  11701   -170      2  -1101       C  
ATOM   4164  CG  GLN B 440     -14.627 -68.265  44.023  1.00 76.49           C  
ANISOU 4164  CG  GLN B 440     8015   9075  11972    -22   -107  -1493       C  
ATOM   4165  CD  GLN B 440     -15.493 -67.161  43.530  1.00 76.87           C  
ANISOU 4165  CD  GLN B 440     8009   8800  12399     62   -403  -1592       C  
ATOM   4166  OE1 GLN B 440     -15.071 -66.345  42.749  1.00 79.02           O  
ANISOU 4166  OE1 GLN B 440     8341   8787  12894    -34   -659  -1366       O  
ATOM   4167  NE2 GLN B 440     -16.720 -67.141  43.968  1.00 79.03           N  
ANISOU 4167  NE2 GLN B 440     8153   9119  12754    227   -391  -1923       N  
ATOM   4168  N   PHE B 441     -13.767 -71.373  40.725  1.00 71.35           N  
ANISOU 4168  N   PHE B 441     7594   8843  10673   -353    339   -582       N  
ATOM   4169  CA  PHE B 441     -12.821 -71.712  39.669  1.00 70.78           C  
ANISOU 4169  CA  PHE B 441     7546   8875  10469   -516    382   -334       C  
ATOM   4170  C   PHE B 441     -13.058 -73.000  38.895  1.00 69.29           C  
ANISOU 4170  C   PHE B 441     7353   8889  10085   -521    558   -274       C  
ATOM   4171  O   PHE B 441     -12.171 -73.479  38.210  1.00 68.77           O  
ANISOU 4171  O   PHE B 441     7259   8985   9883   -631    636   -168       O  
ATOM   4172  CB  PHE B 441     -11.401 -71.668  40.236  1.00 70.58           C  
ANISOU 4172  CB  PHE B 441     7502   8921  10393   -586    417   -324       C  
ATOM   4173  CG  PHE B 441     -11.006 -70.308  40.719  1.00 72.04           C  
ANISOU 4173  CG  PHE B 441     7691   8895  10785   -627    207   -339       C  
ATOM   4174  CD1 PHE B 441     -10.754 -69.280  39.813  1.00 72.13           C  
ANISOU 4174  CD1 PHE B 441     7722   8754  10928   -799     -7   -120       C  
ATOM   4175  CD2 PHE B 441     -10.912 -70.037  42.077  1.00 70.84           C  
ANISOU 4175  CD2 PHE B 441     7517   8699  10701   -517    195   -569       C  
ATOM   4176  CE1 PHE B 441     -10.395 -68.014  40.256  1.00 72.00           C  
ANISOU 4176  CE1 PHE B 441     7709   8490  11157   -843   -254   -128       C  
ATOM   4177  CE2 PHE B 441     -10.552 -68.778  42.516  1.00 71.37           C  
ANISOU 4177  CE2 PHE B 441     7573   8552  10991   -542    -21   -625       C  
ATOM   4178  CZ  PHE B 441     -10.293 -67.763  41.595  1.00 72.36           C  
ANISOU 4178  CZ  PHE B 441     7724   8470  11298   -697   -259   -402       C  
ATOM   4179  N   SER B 442     -14.256 -73.550  38.964  1.00 68.74           N  
ANISOU 4179  N   SER B 442     7286   8822  10007   -407    612   -369       N  
ATOM   4180  CA  SER B 442     -14.487 -74.807  38.293  1.00 68.28           C  
ANISOU 4180  CA  SER B 442     7220   8929   9794   -403    754   -337       C  
ATOM   4181  C   SER B 442     -14.539 -74.596  36.802  1.00 69.22           C  
ANISOU 4181  C   SER B 442     7343   9091   9864   -533    700   -162       C  
ATOM   4182  O   SER B 442     -14.178 -75.491  36.060  1.00 69.08           O  
ANISOU 4182  O   SER B 442     7288   9262   9694   -582    811   -139       O  
ATOM   4183  CB  SER B 442     -15.764 -75.473  38.767  1.00 67.30           C  
ANISOU 4183  CB  SER B 442     7091   8810   9667   -278    817   -464       C  
ATOM   4184  OG  SER B 442     -16.853 -74.618  38.503  1.00 70.59           O  
ANISOU 4184  OG  SER B 442     7506   9086  10227   -238    692   -489       O  
ATOM   4185  N   LYS B 443     -14.992 -73.424  36.361  1.00 71.18           N  
ANISOU 4185  N   LYS B 443     7622   9171  10249   -599    503    -49       N  
ATOM   4186  CA  LYS B 443     -14.921 -73.084  34.945  1.00 73.21           C  
ANISOU 4186  CA  LYS B 443     7889   9495  10429   -797    406    183       C  
ATOM   4187  C   LYS B 443     -13.484 -73.290  34.456  1.00 73.80           C  
ANISOU 4187  C   LYS B 443     7910   9819  10309   -983    499    279       C  
ATOM   4188  O   LYS B 443     -13.260 -73.916  33.423  1.00 75.04           O  
ANISOU 4188  O   LYS B 443     8013  10240  10256  -1102    597    331       O  
ATOM   4189  CB  LYS B 443     -15.375 -71.644  34.688  1.00 75.73           C  
ANISOU 4189  CB  LYS B 443     8254   9538  10980   -878     95    339       C  
ATOM   4190  CG  LYS B 443     -16.760 -71.525  34.091  1.00 79.27           C  
ANISOU 4190  CG  LYS B 443     8723   9861  11533   -826    -37    370       C  
ATOM   4191  CD  LYS B 443     -17.802 -71.057  35.132  1.00 86.03           C  
ANISOU 4191  CD  LYS B 443     9553  10448  12684   -582   -141    120       C  
ATOM   4192  CE  LYS B 443     -18.313 -69.613  34.866  1.00 90.95           C  
ANISOU 4192  CE  LYS B 443    10187  10710  13659   -614   -544    219       C  
ATOM   4193  NZ  LYS B 443     -17.395 -68.807  33.991  1.00 93.86           N1+
ANISOU 4193  NZ  LYS B 443    10616  11029  14015   -914   -767    585       N1+
ATOM   4194  N   ASN B 444     -12.513 -72.801  35.219  1.00 73.44           N  
ANISOU 4194  N   ASN B 444     7852   9722  10328  -1005    477    261       N  
ATOM   4195  CA  ASN B 444     -11.126 -72.980  34.886  1.00 73.73           C  
ANISOU 4195  CA  ASN B 444     7805  10006  10202  -1169    569    311       C  
ATOM   4196  C   ASN B 444     -10.653 -74.410  34.885  1.00 72.86           C  
ANISOU 4196  C   ASN B 444     7598  10145   9939  -1070    803    116       C  
ATOM   4197  O   ASN B 444      -9.881 -74.792  34.017  1.00 74.40           O  
ANISOU 4197  O   ASN B 444     7676  10640   9951  -1216    894    122       O  
ATOM   4198  CB  ASN B 444     -10.286 -72.178  35.829  1.00 74.06           C  
ANISOU 4198  CB  ASN B 444     7854   9904  10379  -1184    481    309       C  
ATOM   4199  CG  ASN B 444     -10.521 -70.740  35.669  1.00 75.45           C  
ANISOU 4199  CG  ASN B 444     8097   9830  10740  -1320    200    506       C  
ATOM   4200  OD1 ASN B 444     -11.428 -70.181  36.268  1.00 75.90           O  
ANISOU 4200  OD1 ASN B 444     8217   9591  11030  -1170     51    428       O  
ATOM   4201  ND2 ASN B 444      -9.730 -70.116  34.828  1.00 76.47           N  
ANISOU 4201  ND2 ASN B 444     8193  10081  10778  -1621     99    759       N  
ATOM   4202  N   ILE B 445     -11.098 -75.202  35.856  1.00 71.50           N  
ANISOU 4202  N   ILE B 445     7454   9863   9848   -839    876    -66       N  
ATOM   4203  CA  ILE B 445     -10.790 -76.624  35.863  1.00 70.74           C  
ANISOU 4203  CA  ILE B 445     7274   9922   9680   -733   1023   -238       C  
ATOM   4204  C   ILE B 445     -11.233 -77.173  34.535  1.00 71.76           C  
ANISOU 4204  C   ILE B 445     7349  10243   9671   -796   1080   -237       C  
ATOM   4205  O   ILE B 445     -10.433 -77.691  33.759  1.00 73.21           O  
ANISOU 4205  O   ILE B 445     7391  10700   9724   -879   1166   -322       O  
ATOM   4206  CB  ILE B 445     -11.562 -77.393  36.933  1.00 68.84           C  
ANISOU 4206  CB  ILE B 445     7096   9525   9533   -534   1040   -353       C  
ATOM   4207  CG1 ILE B 445     -11.407 -76.735  38.311  1.00 69.40           C  
ANISOU 4207  CG1 ILE B 445     7227   9436   9705   -487    977   -366       C  
ATOM   4208  CG2 ILE B 445     -11.142 -78.869  36.934  1.00 67.64           C  
ANISOU 4208  CG2 ILE B 445     6858   9472   9370   -443   1114   -500       C  
ATOM   4209  CD1 ILE B 445     -10.132 -77.052  39.030  1.00 71.13           C  
ANISOU 4209  CD1 ILE B 445     7390   9701   9934   -482    990   -424       C  
ATOM   4210  N   LYS B 446     -12.520 -77.021  34.276  1.00 71.91           N  
ANISOU 4210  N   LYS B 446     7459  10143   9720   -761   1026   -171       N  
ATOM   4211  CA  LYS B 446     -13.154 -77.594  33.111  1.00 73.14           C  
ANISOU 4211  CA  LYS B 446     7581  10456   9753   -802   1065   -178       C  
ATOM   4212  C   LYS B 446     -12.492 -77.130  31.834  1.00 75.98           C  
ANISOU 4212  C   LYS B 446     7853  11111   9905  -1062   1064    -62       C  
ATOM   4213  O   LYS B 446     -12.257 -77.940  30.935  1.00 77.77           O  
ANISOU 4213  O   LYS B 446     7954  11631   9963  -1111   1170   -189       O  
ATOM   4214  CB  LYS B 446     -14.648 -77.296  33.117  1.00 72.38           C  
ANISOU 4214  CB  LYS B 446     7593  10158   9748   -734    974   -104       C  
ATOM   4215  CG  LYS B 446     -15.375 -78.131  34.139  1.00 70.71           C  
ANISOU 4215  CG  LYS B 446     7415   9798   9651   -522   1024   -253       C  
ATOM   4216  CD  LYS B 446     -16.795 -77.774  34.195  1.00 73.12           C  
ANISOU 4216  CD  LYS B 446     7787   9948  10048   -461    947   -218       C  
ATOM   4217  CE  LYS B 446     -17.381 -78.172  35.524  1.00 75.32           C  
ANISOU 4217  CE  LYS B 446     8084  10110  10425   -312    981   -340       C  
ATOM   4218  NZ  LYS B 446     -18.715 -77.494  35.682  1.00 77.34           N1+
ANISOU 4218  NZ  LYS B 446     8360  10229  10794   -256    893   -351       N1+
ATOM   4219  N   LEU B 447     -12.153 -75.846  31.768  1.00 77.45           N  
ANISOU 4219  N   LEU B 447     8085  11242  10099  -1250    932    165       N  
ATOM   4220  CA  LEU B 447     -11.425 -75.308  30.633  1.00 80.39           C  
ANISOU 4220  CA  LEU B 447     8368  11935  10240  -1575    910    337       C  
ATOM   4221  C   LEU B 447     -10.055 -75.976  30.504  1.00 81.55           C  
ANISOU 4221  C   LEU B 447     8316  12436  10233  -1624   1092    134       C  
ATOM   4222  O   LEU B 447      -9.578 -76.225  29.406  1.00 83.57           O  
ANISOU 4222  O   LEU B 447     8414  13117  10220  -1834   1180    102       O  
ATOM   4223  CB  LEU B 447     -11.255 -73.811  30.803  1.00 81.75           C  
ANISOU 4223  CB  LEU B 447     8635  11906  10518  -1765    682    637       C  
ATOM   4224  CG  LEU B 447     -10.942 -73.125  29.490  1.00 85.84           C  
ANISOU 4224  CG  LEU B 447     9106  12715  10791  -2172    574    935       C  
ATOM   4225  CD1 LEU B 447     -12.243 -72.762  28.832  1.00 87.79           C  
ANISOU 4225  CD1 LEU B 447     9470  12807  11076  -2222    381   1133       C  
ATOM   4226  CD2 LEU B 447     -10.106 -71.876  29.730  1.00 89.44           C  
ANISOU 4226  CD2 LEU B 447     9585  13078  11320  -2412    388   1191       C  
ATOM   4227  N   GLY B 448      -9.427 -76.254  31.641  1.00 80.67           N  
ANISOU 4227  N   GLY B 448     8190  12169  10289  -1437   1137    -22       N  
ATOM   4228  CA  GLY B 448      -8.180 -76.992  31.669  1.00 82.01           C  
ANISOU 4228  CA  GLY B 448     8155  12609  10395  -1417   1279   -266       C  
ATOM   4229  C   GLY B 448      -8.324 -78.392  31.102  1.00 82.81           C  
ANISOU 4229  C   GLY B 448     8110  12915  10436  -1279   1406   -574       C  
ATOM   4230  O   GLY B 448      -7.437 -78.849  30.392  1.00 84.90           O  
ANISOU 4230  O   GLY B 448     8137  13574  10545  -1373   1518   -781       O  
ATOM   4231  N   ILE B 449      -9.428 -79.079  31.418  1.00 81.42           N  
ANISOU 4231  N   ILE B 449     8051  12487  10396  -1061   1381   -633       N  
ATOM   4232  CA  ILE B 449      -9.648 -80.445  30.928  1.00 81.91           C  
ANISOU 4232  CA  ILE B 449     7986  12673  10461   -915   1453   -929       C  
ATOM   4233  C   ILE B 449      -9.732 -80.436  29.423  1.00 84.96           C  
ANISOU 4233  C   ILE B 449     8239  13481  10558  -1126   1526   -966       C  
ATOM   4234  O   ILE B 449      -9.192 -81.331  28.771  1.00 86.81           O  
ANISOU 4234  O   ILE B 449     8238  14029  10714  -1101   1622  -1295       O  
ATOM   4235  CB  ILE B 449     -10.902 -81.121  31.527  1.00 79.60           C  
ANISOU 4235  CB  ILE B 449     7853  12035  10357   -693   1390   -931       C  
ATOM   4236  CG1 ILE B 449     -10.541 -81.792  32.845  1.00 78.49           C  
ANISOU 4236  CG1 ILE B 449     7732  11627  10461   -486   1338  -1034       C  
ATOM   4237  CG2 ILE B 449     -11.430 -82.218  30.613  1.00 79.31           C  
ANISOU 4237  CG2 ILE B 449     7714  12145  10276   -628   1428  -1150       C  
ATOM   4238  CD1 ILE B 449     -11.652 -81.820  33.852  1.00 76.96           C  
ANISOU 4238  CD1 ILE B 449     7739  11097  10403   -373   1261   -892       C  
ATOM   4239  N   HIS B 450     -10.393 -79.419  28.868  1.00 86.20           N  
ANISOU 4239  N   HIS B 450     8528  13658  10565  -1343   1457   -646       N  
ATOM   4240  CA  HIS B 450     -10.510 -79.320  27.420  1.00 89.45           C  
ANISOU 4240  CA  HIS B 450     8828  14506  10651  -1609   1499   -615       C  
ATOM   4241  C   HIS B 450      -9.122 -79.265  26.795  1.00 92.49           C  
ANISOU 4241  C   HIS B 450     8942  15416  10784  -1840   1623   -762       C  
ATOM   4242  O   HIS B 450      -8.791 -80.078  25.946  1.00 94.70           O  
ANISOU 4242  O   HIS B 450     8980  16123  10878  -1873   1752  -1086       O  
ATOM   4243  CB  HIS B 450     -11.359 -78.121  26.981  1.00 90.10           C  
ANISOU 4243  CB  HIS B 450     9102  14484  10645  -1841   1334   -184       C  
ATOM   4244  CG  HIS B 450     -11.774 -78.178  25.540  1.00 94.57           C  
ANISOU 4244  CG  HIS B 450     9593  15456  10883  -2098   1341   -126       C  
ATOM   4245  ND1 HIS B 450     -10.939 -77.801  24.507  1.00 97.89           N  
ANISOU 4245  ND1 HIS B 450     9833  16436  10925  -2484   1394    -61       N  
ATOM   4246  CD2 HIS B 450     -12.928 -78.601  24.960  1.00 95.40           C  
ANISOU 4246  CD2 HIS B 450     9761  15531  10953  -2046   1302   -133       C  
ATOM   4247  CE1 HIS B 450     -11.565 -77.984  23.356  1.00100.94           C  
ANISOU 4247  CE1 HIS B 450    10179  17132  11038  -2668   1386    -24       C  
ATOM   4248  NE2 HIS B 450     -12.774 -78.464  23.603  1.00 98.27           N  
ANISOU 4248  NE2 HIS B 450     9995  16424  10919  -2394   1324    -68       N  
ATOM   4249  N   GLU B 451      -8.287 -78.351  27.266  1.00 93.32           N  
ANISOU 4249  N   GLU B 451     9060  15499  10898  -1988   1584   -570       N  
ATOM   4250  CA  GLU B 451      -7.106 -77.985  26.509  1.00 97.10           C  
ANISOU 4250  CA  GLU B 451     9292  16536  11066  -2326   1679   -594       C  
ATOM   4251  C   GLU B 451      -5.738 -78.431  27.074  1.00 97.27           C  
ANISOU 4251  C   GLU B 451     9078  16699  11182  -2215   1796   -921       C  
ATOM   4252  O   GLU B 451      -4.721 -78.292  26.389  1.00100.82           O  
ANISOU 4252  O   GLU B 451     9254  17697  11356  -2485   1910  -1032       O  
ATOM   4253  CB  GLU B 451      -7.146 -76.489  26.226  1.00 98.73           C  
ANISOU 4253  CB  GLU B 451     9644  16739  11130  -2714   1514    -73       C  
ATOM   4254  CG  GLU B 451      -7.019 -75.649  27.475  1.00 99.57           C  
ANISOU 4254  CG  GLU B 451     9953  16319  11559  -2604   1360    148       C  
ATOM   4255  CD  GLU B 451      -6.965 -74.164  27.168  1.00105.62           C  
ANISOU 4255  CD  GLU B 451    10838  17049  12243  -2996   1141    644       C  
ATOM   4256  OE1 GLU B 451      -7.903 -73.728  26.443  1.00109.11           O  
ANISOU 4256  OE1 GLU B 451    11404  17457  12592  -3167    987    920       O  
ATOM   4257  OE2 GLU B 451      -6.015 -73.458  27.645  1.00103.88           O1-
ANISOU 4257  OE2 GLU B 451    10585  16810  12074  -3133   1091    761       O1-
ATOM   4258  N   ASP B 452      -5.703 -78.962  28.295  1.00 94.02           N  
ANISOU 4258  N   ASP B 452     8750  15832  11139  -1847   1757  -1071       N  
ATOM   4259  CA  ASP B 452      -4.450 -79.479  28.866  1.00 94.18           C  
ANISOU 4259  CA  ASP B 452     8546  15936  11300  -1709   1823  -1391       C  
ATOM   4260  C   ASP B 452      -4.450 -81.020  29.021  1.00 94.02           C  
ANISOU 4260  C   ASP B 452     8366  15848  11506  -1352   1853  -1874       C  
ATOM   4261  O   ASP B 452      -4.409 -81.566  30.135  1.00 91.72           O  
ANISOU 4261  O   ASP B 452     8159  15132  11556  -1059   1754  -1955       O  
ATOM   4262  CB  ASP B 452      -4.105 -78.747  30.171  1.00 92.15           C  
ANISOU 4262  CB  ASP B 452     8474  15258  11278  -1641   1708  -1158       C  
ATOM   4263  CG  ASP B 452      -2.766 -79.183  30.772  1.00 92.56           C  
ANISOU 4263  CG  ASP B 452     8298  15391  11476  -1526   1747  -1448       C  
ATOM   4264  OD1 ASP B 452      -1.950 -79.798  30.043  1.00 96.60           O  
ANISOU 4264  OD1 ASP B 452     8467  16366  11869  -1569   1871  -1811       O  
ATOM   4265  OD2 ASP B 452      -2.533 -78.904  31.976  1.00 87.48           O1-
ANISOU 4265  OD2 ASP B 452     7798  14368  11069  -1392   1644  -1337       O1-
ATOM   4266  N   SER B 453      -4.472 -81.696  27.869  1.00 96.64           N  
ANISOU 4266  N   SER B 453     8453  16621  11641  -1406   1962  -2190       N  
ATOM   4267  CA  SER B 453      -4.456 -83.165  27.760  1.00 97.50           C  
ANISOU 4267  CA  SER B 453     8356  16717  11970  -1095   1960  -2706       C  
ATOM   4268  C   SER B 453      -3.443 -83.888  28.656  1.00 98.00           C  
ANISOU 4268  C   SER B 453     8245  16589  12401   -820   1885  -3033       C  
ATOM   4269  O   SER B 453      -3.679 -85.014  29.084  1.00 97.48           O  
ANISOU 4269  O   SER B 453     8158  16196  12681   -504   1756  -3292       O  
ATOM   4270  CB  SER B 453      -4.238 -83.591  26.301  1.00101.05           C  
ANISOU 4270  CB  SER B 453     8462  17835  12094  -1260   2115  -3084       C  
ATOM   4271  OG  SER B 453      -2.942 -83.242  25.855  1.00103.92           O  
ANISOU 4271  OG  SER B 453     8487  18768  12229  -1485   2254  -3284       O  
ATOM   4272  N   GLN B 454      -2.315 -83.251  28.936  1.00 99.34           N  
ANISOU 4272  N   GLN B 454     8285  16944  12515   -955   1932  -3006       N  
ATOM   4273  CA  GLN B 454      -1.307 -83.881  29.768  1.00100.16           C  
ANISOU 4273  CA  GLN B 454     8208  16874  12971   -707   1838  -3307       C  
ATOM   4274  C   GLN B 454      -1.772 -84.042  31.207  1.00 96.30           C  
ANISOU 4274  C   GLN B 454     8052  15692  12845   -469   1628  -3040       C  
ATOM   4275  O   GLN B 454      -1.424 -85.020  31.843  1.00 96.96           O  
ANISOU 4275  O   GLN B 454     8042  15498  13298   -191   1467  -3297       O  
ATOM   4276  CB  GLN B 454      -0.011 -83.091  29.740  1.00102.75           C  
ANISOU 4276  CB  GLN B 454     8320  17580  13137   -933   1939  -3316       C  
ATOM   4277  CG  GLN B 454       0.373 -82.542  28.387  1.00108.41           C  
ANISOU 4277  CG  GLN B 454     8771  19049  13368  -1318   2158  -3395       C  
ATOM   4278  CD  GLN B 454       1.332 -81.375  28.530  1.00114.00           C  
ANISOU 4278  CD  GLN B 454     9425  20012  13876  -1641   2220  -3137       C  
ATOM   4279  OE1 GLN B 454       1.081 -80.433  29.310  1.00112.36           O  
ANISOU 4279  OE1 GLN B 454     9557  19413  13721  -1720   2117  -2641       O  
ATOM   4280  NE2 GLN B 454       2.450 -81.429  27.790  1.00118.58           N  
ANISOU 4280  NE2 GLN B 454     9552  21267  14233  -1834   2382  -3502       N  
ATOM   4281  N   ASN B 455      -2.558 -83.085  31.708  1.00 92.98           N  
ANISOU 4281  N   ASN B 455     7996  15009  12319   -591   1609  -2538       N  
ATOM   4282  CA  ASN B 455      -2.981 -83.057  33.106  1.00 89.40           C  
ANISOU 4282  CA  ASN B 455     7840  14003  12125   -430   1443  -2276       C  
ATOM   4283  C   ASN B 455      -4.462 -83.328  33.291  1.00 87.33           C  
ANISOU 4283  C   ASN B 455     7856  13419  11903   -343   1379  -2079       C  
ATOM   4284  O   ASN B 455      -4.973 -83.290  34.418  1.00 85.17           O  
ANISOU 4284  O   ASN B 455     7823  12752  11785   -248   1259  -1857       O  
ATOM   4285  CB  ASN B 455      -2.654 -81.705  33.710  1.00 88.16           C  
ANISOU 4285  CB  ASN B 455     7844  13794  11856   -618   1454  -1922       C  
ATOM   4286  CG  ASN B 455      -1.177 -81.476  33.841  1.00 89.20           C  
ANISOU 4286  CG  ASN B 455     7728  14156  12008   -683   1480  -2081       C  
ATOM   4287  OD1 ASN B 455      -0.532 -81.963  34.761  1.00 87.02           O  
ANISOU 4287  OD1 ASN B 455     7401  13663  11996   -503   1358  -2202       O  
ATOM   4288  ND2 ASN B 455      -0.629 -80.722  32.917  1.00 92.24           N  
ANISOU 4288  ND2 ASN B 455     7947  14997  12100   -969   1623  -2063       N  
ATOM   4289  N   ARG B 456      -5.140 -83.576  32.170  1.00 88.11           N  
ANISOU 4289  N   ARG B 456     7904  13738  11835   -400   1465  -2170       N  
ATOM   4290  CA  ARG B 456      -6.548 -83.954  32.110  1.00 86.11           C  
ANISOU 4290  CA  ARG B 456     7856  13249  11611   -323   1417  -2046       C  
ATOM   4291  C   ARG B 456      -6.988 -84.921  33.217  1.00 84.69           C  
ANISOU 4291  C   ARG B 456     7800  12609  11767    -80   1232  -2051       C  
ATOM   4292  O   ARG B 456      -7.978 -84.667  33.897  1.00 82.91           O  
ANISOU 4292  O   ARG B 456     7833  12106  11559    -75   1180  -1767       O  
ATOM   4293  CB  ARG B 456      -6.850 -84.531  30.731  1.00 87.90           C  
ANISOU 4293  CB  ARG B 456     7897  13817  11684   -358   1506  -2315       C  
ATOM   4294  CG  ARG B 456      -8.233 -85.124  30.589  1.00 88.04           C  
ANISOU 4294  CG  ARG B 456     8079  13605  11767   -257   1443  -2257       C  
ATOM   4295  CD  ARG B 456      -8.630 -85.363  29.131  1.00 92.20           C  
ANISOU 4295  CD  ARG B 456     8456  14522  12050   -361   1548  -2449       C  
ATOM   4296  NE  ARG B 456      -8.589 -84.147  28.315  1.00 93.64           N  
ANISOU 4296  NE  ARG B 456     8654  15082  11842   -681   1677  -2215       N  
ATOM   4297  CZ  ARG B 456      -7.878 -84.012  27.197  1.00 97.96           C  
ANISOU 4297  CZ  ARG B 456     8931  16196  12091   -888   1811  -2422       C  
ATOM   4298  NH1 ARG B 456      -7.149 -85.024  26.732  1.00100.66           N1+
ANISOU 4298  NH1 ARG B 456     8936  16816  12494   -769   1858  -2947       N1+
ATOM   4299  NH2 ARG B 456      -7.898 -82.861  26.538  1.00 99.61           N  
ANISOU 4299  NH2 ARG B 456     9189  16710  11947  -1231   1876  -2112       N  
ATOM   4300  N   LYS B 457      -6.261 -86.015  33.411  1.00 86.21           N  
ANISOU 4300  N   LYS B 457     7792  12729  12232    100   1109  -2371       N  
ATOM   4301  CA  LYS B 457      -6.575 -86.955  34.491  1.00 85.93           C  
ANISOU 4301  CA  LYS B 457     7870  12248  12531    279    870  -2321       C  
ATOM   4302  C   LYS B 457      -6.612 -86.312  35.904  1.00 84.48           C  
ANISOU 4302  C   LYS B 457     7929  11807  12363    229    799  -1957       C  
ATOM   4303  O   LYS B 457      -7.600 -86.458  36.634  1.00 82.81           O  
ANISOU 4303  O   LYS B 457     7940  11340  12180    229    715  -1713       O  
ATOM   4304  CB  LYS B 457      -5.622 -88.155  34.453  1.00 88.42           C  
ANISOU 4304  CB  LYS B 457     7901  12500  13194    477    685  -2733       C  
ATOM   4305  CG  LYS B 457      -6.160 -89.382  35.138  1.00 89.68           C  
ANISOU 4305  CG  LYS B 457     8143  12211  13717    638    383  -2713       C  
ATOM   4306  CD  LYS B 457      -5.298 -90.600  34.884  1.00 96.32           C  
ANISOU 4306  CD  LYS B 457     8668  12961  14967    855    149  -3180       C  
ATOM   4307  CE  LYS B 457      -4.569 -91.076  36.172  1.00 99.97           C  
ANISOU 4307  CE  LYS B 457     9149  13041  15792    947   -174  -3081       C  
ATOM   4308  NZ  LYS B 457      -3.815 -90.001  36.916  1.00100.20           N1+
ANISOU 4308  NZ  LYS B 457     9252  13178  15639    827    -62  -2856       N1+
ATOM   4309  N   LYS B 458      -5.538 -85.607  36.276  1.00 85.39           N  
ANISOU 4309  N   LYS B 458     7977  12027  12439    171    836  -1945       N  
ATOM   4310  CA  LYS B 458      -5.470 -84.900  37.544  1.00 84.16           C  
ANISOU 4310  CA  LYS B 458     8020  11688  12268    111    783  -1651       C  
ATOM   4311  C   LYS B 458      -6.544 -83.831  37.646  1.00 81.90           C  
ANISOU 4311  C   LYS B 458     7972  11398  11745    -21    904  -1358       C  
ATOM   4312  O   LYS B 458      -7.170 -83.673  38.696  1.00 80.77           O  
ANISOU 4312  O   LYS B 458     8022  11052  11613    -29    833  -1150       O  
ATOM   4313  CB  LYS B 458      -4.101 -84.266  37.733  1.00 85.57           C  
ANISOU 4313  CB  LYS B 458     8057  12018  12437     59    814  -1720       C  
ATOM   4314  CG  LYS B 458      -3.248 -84.964  38.783  1.00 89.71           C  
ANISOU 4314  CG  LYS B 458     8519  12320  13246    180    584  -1782       C  
ATOM   4315  CD  LYS B 458      -3.814 -84.763  40.218  1.00 91.90           C  
ANISOU 4315  CD  LYS B 458     9072  12318  13524    140    457  -1450       C  
ATOM   4316  CE  LYS B 458      -2.915 -85.439  41.285  1.00 95.32           C  
ANISOU 4316  CE  LYS B 458     9451  12542  14222    218    187  -1462       C  
ATOM   4317  NZ  LYS B 458      -1.792 -84.568  41.796  1.00 94.83           N1+
ANISOU 4317  NZ  LYS B 458     9335  12578  14116    155    213  -1446       N1+
ATOM   4318  N   LEU B 459      -6.756 -83.094  36.557  1.00 81.47           N  
ANISOU 4318  N   LEU B 459     7886  11588  11480   -139   1066  -1353       N  
ATOM   4319  CA  LEU B 459      -7.780 -82.060  36.538  1.00 79.41           C  
ANISOU 4319  CA  LEU B 459     7825  11290  11055   -250   1129  -1101       C  
ATOM   4320  C   LEU B 459      -9.157 -82.661  36.752  1.00 78.45           C  
ANISOU 4320  C   LEU B 459     7844  10984  10977   -170   1085  -1034       C  
ATOM   4321  O   LEU B 459     -10.027 -82.040  37.394  1.00 77.64           O  
ANISOU 4321  O   LEU B 459     7912  10750  10834   -199   1077   -852       O  
ATOM   4322  CB  LEU B 459      -7.753 -81.259  35.237  1.00 79.91           C  
ANISOU 4322  CB  LEU B 459     7821  11639  10901   -423   1250  -1072       C  
ATOM   4323  CG  LEU B 459      -6.646 -80.210  35.103  1.00 80.95           C  
ANISOU 4323  CG  LEU B 459     7871  11955  10929   -597   1289  -1008       C  
ATOM   4324  CD1 LEU B 459      -6.599 -79.602  33.696  1.00 81.55           C  
ANISOU 4324  CD1 LEU B 459     7853  12375  10755   -831   1381   -955       C  
ATOM   4325  CD2 LEU B 459      -6.792 -79.136  36.158  1.00 78.65           C  
ANISOU 4325  CD2 LEU B 459     7768  11426  10689   -633   1213   -778       C  
ATOM   4326  N   SER B 460      -9.362 -83.874  36.237  1.00 78.88           N  
ANISOU 4326  N   SER B 460     7803  11035  11130    -70   1045  -1209       N  
ATOM   4327  CA  SER B 460     -10.672 -84.513  36.344  1.00 77.35           C  
ANISOU 4327  CA  SER B 460     7725  10682  10980    -19    994  -1142       C  
ATOM   4328  C   SER B 460     -10.963 -85.011  37.743  1.00 76.23           C  
ANISOU 4328  C   SER B 460     7700  10291  10970     18    850  -1010       C  
ATOM   4329  O   SER B 460     -12.119 -85.159  38.092  1.00 76.25           O  
ANISOU 4329  O   SER B 460     7824  10201  10944     -1    834   -881       O  
ATOM   4330  CB  SER B 460     -10.822 -85.635  35.343  1.00 78.43           C  
ANISOU 4330  CB  SER B 460     7721  10877  11198     64    968  -1377       C  
ATOM   4331  OG  SER B 460     -10.133 -86.765  35.794  1.00 80.60           O  
ANISOU 4331  OG  SER B 460     7885  10999  11737    190    795  -1544       O  
ATOM   4332  N   GLU B 461      -9.932 -85.247  38.548  1.00 76.14           N  
ANISOU 4332  N   GLU B 461     7643  10204  11082     46    740  -1030       N  
ATOM   4333  CA  GLU B 461     -10.138 -85.626  39.941  1.00 75.58           C  
ANISOU 4333  CA  GLU B 461     7686   9945  11082     21    585   -857       C  
ATOM   4334  C   GLU B 461     -10.646 -84.456  40.787  1.00 73.06           C  
ANISOU 4334  C   GLU B 461     7514   9676  10568    -84    680   -675       C  
ATOM   4335  O   GLU B 461     -11.026 -84.627  41.945  1.00 72.94           O  
ANISOU 4335  O   GLU B 461     7591   9598  10523   -150    593   -531       O  
ATOM   4336  CB  GLU B 461      -8.858 -86.187  40.549  1.00 77.60           C  
ANISOU 4336  CB  GLU B 461     7846  10101  11538     72    401   -921       C  
ATOM   4337  CG  GLU B 461      -8.390 -87.515  40.008  1.00 83.85           C  
ANISOU 4337  CG  GLU B 461     8470  10769  12618    205    216  -1137       C  
ATOM   4338  CD  GLU B 461      -6.936 -87.849  40.435  1.00 94.43           C  
ANISOU 4338  CD  GLU B 461     9659  12035  14185    281     40  -1267       C  
ATOM   4339  OE1 GLU B 461      -6.221 -86.957  40.985  1.00 97.51           O  
ANISOU 4339  OE1 GLU B 461    10067  12517  14465    221    109  -1197       O  
ATOM   4340  OE2 GLU B 461      -6.489 -89.013  40.221  1.00 99.48           O1-
ANISOU 4340  OE2 GLU B 461    10144  12505  15148    412   -194  -1462       O1-
ATOM   4341  N   LEU B 462     -10.654 -83.264  40.211  1.00 71.41           N  
ANISOU 4341  N   LEU B 462     7309   9593  10228   -116    836   -692       N  
ATOM   4342  CA  LEU B 462     -11.031 -82.077  40.963  1.00 70.15           C  
ANISOU 4342  CA  LEU B 462     7252   9450   9950   -186    889   -590       C  
ATOM   4343  C   LEU B 462     -12.483 -81.695  40.702  1.00 69.67           C  
ANISOU 4343  C   LEU B 462     7265   9400   9807   -200    960   -549       C  
ATOM   4344  O   LEU B 462     -13.072 -80.912  41.457  1.00 70.10           O  
ANISOU 4344  O   LEU B 462     7379   9459   9797   -234    979   -519       O  
ATOM   4345  CB  LEU B 462     -10.108 -80.900  40.632  1.00 70.03           C  
ANISOU 4345  CB  LEU B 462     7197   9508   9903   -228    945   -611       C  
ATOM   4346  CG  LEU B 462      -8.610 -81.005  40.928  1.00 69.78           C  
ANISOU 4346  CG  LEU B 462     7069   9499   9942   -227    890   -667       C  
ATOM   4347  CD1 LEU B 462      -7.868 -79.870  40.272  1.00 67.18           C  
ANISOU 4347  CD1 LEU B 462     6683   9282   9558   -310    959   -670       C  
ATOM   4348  CD2 LEU B 462      -8.378 -80.996  42.416  1.00 70.36           C  
ANISOU 4348  CD2 LEU B 462     7211   9493  10029   -243    791   -601       C  
ATOM   4349  N   LEU B 463     -13.063 -82.249  39.639  1.00 69.20           N  
ANISOU 4349  N   LEU B 463     7177   9353   9760   -167    990   -584       N  
ATOM   4350  CA  LEU B 463     -14.433 -81.953  39.264  1.00 67.79           C  
ANISOU 4350  CA  LEU B 463     7051   9181   9526   -173   1041   -554       C  
ATOM   4351  C   LEU B 463     -15.378 -82.396  40.347  1.00 67.67           C  
ANISOU 4351  C   LEU B 463     7085   9140   9485   -196   1010   -503       C  
ATOM   4352  O   LEU B 463     -15.108 -83.380  41.055  1.00 68.06           O  
ANISOU 4352  O   LEU B 463     7136   9152   9570   -222    920   -457       O  
ATOM   4353  CB  LEU B 463     -14.778 -82.701  38.002  1.00 67.86           C  
ANISOU 4353  CB  LEU B 463     7009   9220   9551   -140   1058   -610       C  
ATOM   4354  CG  LEU B 463     -14.084 -82.212  36.744  1.00 69.24           C  
ANISOU 4354  CG  LEU B 463     7110   9525   9672   -173   1113   -662       C  
ATOM   4355  CD1 LEU B 463     -14.219 -83.273  35.664  1.00 70.54           C  
ANISOU 4355  CD1 LEU B 463     7186   9767   9850   -134   1119   -790       C  
ATOM   4356  CD2 LEU B 463     -14.677 -80.861  36.290  1.00 69.67           C  
ANISOU 4356  CD2 LEU B 463     7224   9599   9648   -247   1136   -556       C  
ATOM   4357  N   ARG B 464     -16.478 -81.661  40.482  1.00 67.13           N  
ANISOU 4357  N   ARG B 464     7039   9103   9361   -206   1062   -513       N  
ATOM   4358  CA  ARG B 464     -17.574 -82.048  41.374  1.00 67.53           C  
ANISOU 4358  CA  ARG B 464     7095   9217   9344   -258   1066   -497       C  
ATOM   4359  C   ARG B 464     -18.919 -81.851  40.661  1.00 67.35           C  
ANISOU 4359  C   ARG B 464     7054   9209   9326   -225   1113   -539       C  
ATOM   4360  O   ARG B 464     -19.142 -80.794  40.061  1.00 67.56           O  
ANISOU 4360  O   ARG B 464     7073   9199   9395   -173   1128   -593       O  
ATOM   4361  CB  ARG B 464     -17.528 -81.240  42.676  1.00 67.88           C  
ANISOU 4361  CB  ARG B 464     7129   9359   9301   -309   1081   -548       C  
ATOM   4362  CG  ARG B 464     -16.266 -81.423  43.498  1.00 67.90           C  
ANISOU 4362  CG  ARG B 464     7151   9361   9285   -358   1017   -494       C  
ATOM   4363  CD  ARG B 464     -15.992 -82.853  43.805  1.00 69.19           C  
ANISOU 4363  CD  ARG B 464     7333   9493   9460   -428    910   -358       C  
ATOM   4364  NE  ARG B 464     -14.905 -83.027  44.764  1.00 71.69           N  
ANISOU 4364  NE  ARG B 464     7663   9812   9762   -493    809   -291       N  
ATOM   4365  CZ  ARG B 464     -13.668 -83.392  44.440  1.00 72.97           C  
ANISOU 4365  CZ  ARG B 464     7813   9845  10065   -433    718   -279       C  
ATOM   4366  NH1 ARG B 464     -13.347 -83.596  43.170  1.00 73.38           N1+
ANISOU 4366  NH1 ARG B 464     7824   9803  10251   -318    740   -355       N1+
ATOM   4367  NH2 ARG B 464     -12.741 -83.537  45.379  1.00 73.64           N  
ANISOU 4367  NH2 ARG B 464     7905   9926  10146   -495    602   -213       N  
ATOM   4368  N   TYR B 465     -19.803 -82.848  40.701  1.00 67.05           N  
ANISOU 4368  N   TYR B 465     7006   9203   9266   -268   1104   -497       N  
ATOM   4369  CA  TYR B 465     -21.092 -82.687  40.047  1.00 67.43           C  
ANISOU 4369  CA  TYR B 465     7022   9271   9325   -237   1142   -544       C  
ATOM   4370  C   TYR B 465     -22.310 -83.086  40.880  1.00 68.78           C  
ANISOU 4370  C   TYR B 465     7137   9588   9407   -329   1171   -553       C  
ATOM   4371  O   TYR B 465     -22.217 -83.861  41.835  1.00 69.73           O  
ANISOU 4371  O   TYR B 465     7258   9796   9438   -460   1139   -460       O  
ATOM   4372  CB  TYR B 465     -21.149 -83.473  38.766  1.00 66.81           C  
ANISOU 4372  CB  TYR B 465     6959   9109   9315   -197   1112   -512       C  
ATOM   4373  CG  TYR B 465     -20.176 -83.097  37.666  1.00 68.50           C  
ANISOU 4373  CG  TYR B 465     7184   9276   9565   -142   1109   -532       C  
ATOM   4374  CD1 TYR B 465     -19.050 -83.901  37.400  1.00 69.49           C  
ANISOU 4374  CD1 TYR B 465     7295   9376   9732   -130   1070   -545       C  
ATOM   4375  CD2 TYR B 465     -20.410 -81.996  36.836  1.00 68.40           C  
ANISOU 4375  CD2 TYR B 465     7173   9263   9551   -122   1119   -541       C  
ATOM   4376  CE1 TYR B 465     -18.173 -83.601  36.362  1.00 69.33           C  
ANISOU 4376  CE1 TYR B 465     7238   9402   9701   -112   1092   -599       C  
ATOM   4377  CE2 TYR B 465     -19.537 -81.690  35.797  1.00 69.12           C  
ANISOU 4377  CE2 TYR B 465     7261   9382   9619   -140   1113   -524       C  
ATOM   4378  CZ  TYR B 465     -18.425 -82.506  35.563  1.00 69.71           C  
ANISOU 4378  CZ  TYR B 465     7297   9503   9685   -141   1124   -569       C  
ATOM   4379  OH  TYR B 465     -17.553 -82.218  34.537  1.00 71.01           O  
ANISOU 4379  OH  TYR B 465     7412   9782   9783   -189   1144   -589       O  
ATOM   4380  N   TYR B 466     -23.461 -82.528  40.508  1.00 69.17           N  
ANISOU 4380  N   TYR B 466     7121   9680   9480   -281   1213   -658       N  
ATOM   4381  CA  TYR B 466     -24.738 -83.054  40.936  1.00 69.82           C  
ANISOU 4381  CA  TYR B 466     7118   9922   9486   -370   1249   -679       C  
ATOM   4382  C   TYR B 466     -24.982 -84.356  40.210  1.00 69.17           C  
ANISOU 4382  C   TYR B 466     7084   9751   9446   -412   1190   -538       C  
ATOM   4383  O   TYR B 466     -24.650 -84.493  39.032  1.00 68.99           O  
ANISOU 4383  O   TYR B 466     7115   9568   9527   -314   1151   -523       O  
ATOM   4384  CB  TYR B 466     -25.841 -82.056  40.616  1.00 70.83           C  
ANISOU 4384  CB  TYR B 466     7139  10089   9684   -272   1283   -870       C  
ATOM   4385  CG  TYR B 466     -25.818 -80.864  41.551  1.00 74.02           C  
ANISOU 4385  CG  TYR B 466     7444  10603  10077   -235   1315  -1082       C  
ATOM   4386  CD1 TYR B 466     -25.953 -81.045  42.934  1.00 77.64           C  
ANISOU 4386  CD1 TYR B 466     7809  11348  10343   -376   1390  -1156       C  
ATOM   4387  CD2 TYR B 466     -25.641 -79.572  41.069  1.00 75.36           C  
ANISOU 4387  CD2 TYR B 466     7606  10601  10426    -83   1243  -1206       C  
ATOM   4388  CE1 TYR B 466     -25.916 -79.992  43.798  1.00 79.43           C  
ANISOU 4388  CE1 TYR B 466     7919  11709  10550   -339   1420  -1407       C  
ATOM   4389  CE2 TYR B 466     -25.599 -78.502  41.926  1.00 77.51           C  
ANISOU 4389  CE2 TYR B 466     7773  10938  10738    -32   1236  -1440       C  
ATOM   4390  CZ  TYR B 466     -25.736 -78.719  43.289  1.00 80.33           C  
ANISOU 4390  CZ  TYR B 466     8021  11603  10896   -146   1338  -1570       C  
ATOM   4391  OH  TYR B 466     -25.711 -77.667  44.167  1.00 83.95           O  
ANISOU 4391  OH  TYR B 466     8345  12167  11383    -91   1335  -1867       O  
ATOM   4392  N   THR B 467     -25.521 -85.340  40.913  1.00 69.86           N  
ANISOU 4392  N   THR B 467     7141   9955   9445   -581   1165   -433       N  
ATOM   4393  CA  THR B 467     -25.873 -86.614  40.280  1.00 68.99           C  
ANISOU 4393  CA  THR B 467     7063   9731   9416   -630   1067   -308       C  
ATOM   4394  C   THR B 467     -27.228 -87.047  40.789  1.00 69.89           C  
ANISOU 4394  C   THR B 467     7080  10048   9427   -798   1094   -273       C  
ATOM   4395  O   THR B 467     -27.673 -86.572  41.831  1.00 71.47           O  
ANISOU 4395  O   THR B 467     7181  10517   9455   -917   1182   -328       O  
ATOM   4396  CB  THR B 467     -24.833 -87.752  40.560  1.00 69.61           C  
ANISOU 4396  CB  THR B 467     7226   9654   9569   -706    902   -136       C  
ATOM   4397  OG1 THR B 467     -25.039 -88.294  41.868  1.00 70.46           O  
ANISOU 4397  OG1 THR B 467     7316   9914   9540   -952    838     34       O  
ATOM   4398  CG2 THR B 467     -23.372 -87.276  40.407  1.00 68.02           C  
ANISOU 4398  CG2 THR B 467     7080   9332   9431   -577    891   -188       C  
ATOM   4399  N   SER B 468     -27.874 -87.959  40.072  1.00 69.50           N  
ANISOU 4399  N   SER B 468     7035   9901   9471   -824   1017   -204       N  
ATOM   4400  CA  SER B 468     -29.141 -88.528  40.501  1.00 70.46           C  
ANISOU 4400  CA  SER B 468     7057  10213   9500  -1021   1021   -137       C  
ATOM   4401  C   SER B 468     -29.037 -89.218  41.858  1.00 72.90           C  
ANISOU 4401  C   SER B 468     7352  10703   9641  -1325    950     77       C  
ATOM   4402  O   SER B 468     -30.039 -89.572  42.439  1.00 75.71           O  
ANISOU 4402  O   SER B 468     7599  11317   9848  -1557    973    147       O  
ATOM   4403  CB  SER B 468     -29.665 -89.494  39.454  1.00 69.99           C  
ANISOU 4403  CB  SER B 468     7025   9964   9603   -999    908    -80       C  
ATOM   4404  OG  SER B 468     -28.729 -90.513  39.175  1.00 68.67           O  
ANISOU 4404  OG  SER B 468     6968   9526   9596   -996    716     46       O  
ATOM   4405  N   ALA B 469     -27.830 -89.386  42.375  1.00 73.12           N  
ANISOU 4405  N   ALA B 469     7478  10626   9677  -1351    853    191       N  
ATOM   4406  CA  ALA B 469     -27.635 -90.036  43.665  1.00 75.91           C  
ANISOU 4406  CA  ALA B 469     7835  11141   9865  -1670    736    444       C  
ATOM   4407  C   ALA B 469     -27.258 -89.081  44.772  1.00 76.96           C  
ANISOU 4407  C   ALA B 469     7913  11576   9750  -1738    873    356       C  
ATOM   4408  O   ALA B 469     -27.282 -89.459  45.931  1.00 79.69           O  
ANISOU 4408  O   ALA B 469     8229  12178   9871  -2051    813    546       O  
ATOM   4409  CB  ALA B 469     -26.555 -91.083  43.560  1.00 76.35           C  
ANISOU 4409  CB  ALA B 469     8028  10842  10138  -1685    454    662       C  
ATOM   4410  N   SER B 470     -26.894 -87.855  44.415  1.00 75.60           N  
ANISOU 4410  N   SER B 470     7726  11376   9620  -1468   1029     81       N  
ATOM   4411  CA  SER B 470     -26.156 -86.980  45.315  1.00 75.91           C  
ANISOU 4411  CA  SER B 470     7749  11576   9515  -1470   1102    -15       C  
ATOM   4412  C   SER B 470     -27.045 -86.032  46.103  1.00 78.37           C  
ANISOU 4412  C   SER B 470     7864  12322   9590  -1542   1299   -270       C  
ATOM   4413  O   SER B 470     -26.568 -85.365  47.033  1.00 79.44           O  
ANISOU 4413  O   SER B 470     7952  12667   9562  -1593   1357   -378       O  
ATOM   4414  CB  SER B 470     -25.147 -86.165  44.519  1.00 73.08           C  
ANISOU 4414  CB  SER B 470     7479  10926   9362  -1159   1121   -163       C  
ATOM   4415  OG  SER B 470     -25.799 -85.179  43.744  1.00 70.32           O  
ANISOU 4415  OG  SER B 470     7057  10561   9099   -950   1247   -415       O  
ATOM   4416  N   GLY B 471     -28.326 -85.967  45.734  1.00 79.63           N  
ANISOU 4416  N   GLY B 471     7885  12624   9743  -1538   1392   -406       N  
ATOM   4417  CA  GLY B 471     -29.236 -84.982  46.309  1.00 82.28           C  
ANISOU 4417  CA  GLY B 471     7981  13354   9927  -1538   1574   -756       C  
ATOM   4418  C   GLY B 471     -28.758 -83.599  45.935  1.00 81.56           C  
ANISOU 4418  C   GLY B 471     7883  13078  10025  -1210   1619  -1061       C  
ATOM   4419  O   GLY B 471     -28.412 -83.354  44.781  1.00 79.47           O  
ANISOU 4419  O   GLY B 471     7745  12419  10029   -966   1552  -1043       O  
ATOM   4420  N   ASP B 472     -28.712 -82.700  46.908  1.00 84.27           N  
ANISOU 4420  N   ASP B 472     8075  13719  10225  -1227   1712  -1338       N  
ATOM   4421  CA  ASP B 472     -28.180 -81.360  46.671  1.00 84.92           C  
ANISOU 4421  CA  ASP B 472     8152  13596  10517   -939   1704  -1616       C  
ATOM   4422  C   ASP B 472     -26.701 -81.213  47.081  1.00 83.99           C  
ANISOU 4422  C   ASP B 472     8203  13333  10374   -943   1638  -1477       C  
ATOM   4423  O   ASP B 472     -26.310 -80.178  47.590  1.00 85.14           O  
ANISOU 4423  O   ASP B 472     8277  13531  10539   -847   1656  -1734       O  
ATOM   4424  CB  ASP B 472     -29.036 -80.325  47.406  1.00 88.24           C  
ANISOU 4424  CB  ASP B 472     8267  14380  10878   -894   1814  -2102       C  
ATOM   4425  CG  ASP B 472     -29.252 -80.684  48.875  1.00 94.67           C  
ANISOU 4425  CG  ASP B 472     8908  15792  11267  -1225   1935  -2168       C  
ATOM   4426  OD1 ASP B 472     -30.410 -80.603  49.364  1.00101.95           O  
ANISOU 4426  OD1 ASP B 472     9542  17166  12027  -1335   2059  -2452       O  
ATOM   4427  OD2 ASP B 472     -28.269 -81.067  49.549  1.00 97.57           O1-
ANISOU 4427  OD2 ASP B 472     9412  16215  11445  -1400   1898  -1935       O1-
ATOM   4428  N   GLU B 473     -25.893 -82.255  46.902  1.00 82.79           N  
ANISOU 4428  N   GLU B 473     8253  13001  10200  -1054   1542  -1098       N  
ATOM   4429  CA  GLU B 473     -24.454 -82.169  47.129  1.00 81.62           C  
ANISOU 4429  CA  GLU B 473     8258  12671  10082  -1030   1457   -965       C  
ATOM   4430  C   GLU B 473     -23.809 -82.400  45.787  1.00 79.15           C  
ANISOU 4430  C   GLU B 473     8115  11913  10044   -838   1365   -812       C  
ATOM   4431  O   GLU B 473     -24.340 -83.125  44.939  1.00 79.23           O  
ANISOU 4431  O   GLU B 473     8160  11798  10145   -823   1336   -697       O  
ATOM   4432  CB  GLU B 473     -23.955 -83.239  48.086  1.00 82.46           C  
ANISOU 4432  CB  GLU B 473     8429  12943   9958  -1328   1376   -668       C  
ATOM   4433  CG  GLU B 473     -24.831 -83.460  49.277  1.00 88.49           C  
ANISOU 4433  CG  GLU B 473     9020  14234  10369  -1635   1458   -711       C  
ATOM   4434  CD  GLU B 473     -24.518 -82.525  50.453  1.00 94.74           C  
ANISOU 4434  CD  GLU B 473     9685  15374  10936  -1699   1543   -970       C  
ATOM   4435  OE1 GLU B 473     -23.390 -81.928  50.459  1.00 94.16           O  
ANISOU 4435  OE1 GLU B 473     9712  15075  10987  -1545   1488  -1008       O  
ATOM   4436  OE2 GLU B 473     -25.398 -82.419  51.375  1.00 96.76           O1-
ANISOU 4436  OE2 GLU B 473     9721  16164  10877  -1923   1665  -1149       O1-
ATOM   4437  N   MET B 474     -22.661 -81.780  45.582  1.00 77.42           N  
ANISOU 4437  N   MET B 474     7983  11488   9944   -707   1321   -827       N  
ATOM   4438  CA  MET B 474     -21.883 -82.041  44.415  1.00 74.27           C  
ANISOU 4438  CA  MET B 474     7714  10762   9744   -576   1246   -694       C  
ATOM   4439  C   MET B 474     -20.857 -83.073  44.817  1.00 73.32           C  
ANISOU 4439  C   MET B 474     7687  10580   9591   -689   1139   -466       C  
ATOM   4440  O   MET B 474     -20.208 -82.968  45.856  1.00 74.06           O  
ANISOU 4440  O   MET B 474     7785  10787   9568   -791   1109   -436       O  
ATOM   4441  CB  MET B 474     -21.252 -80.744  43.955  1.00 74.28           C  
ANISOU 4441  CB  MET B 474     7728  10605   9887   -407   1244   -833       C  
ATOM   4442  CG  MET B 474     -22.315 -79.705  43.579  1.00 76.50           C  
ANISOU 4442  CG  MET B 474     7906  10889  10269   -290   1275  -1056       C  
ATOM   4443  SD  MET B 474     -21.700 -78.426  42.488  1.00 76.69           S  
ANISOU 4443  SD  MET B 474     7986  10615  10536   -125   1179  -1088       S  
ATOM   4444  CE  MET B 474     -20.957 -77.326  43.699  1.00 82.15           C  
ANISOU 4444  CE  MET B 474     8628  11359  11225   -118   1154  -1271       C  
ATOM   4445  N   VAL B 475     -20.740 -84.102  44.007  1.00 71.61           N  
ANISOU 4445  N   VAL B 475     7531  10181   9495   -671   1054   -323       N  
ATOM   4446  CA  VAL B 475     -19.848 -85.191  44.319  1.00 71.37           C  
ANISOU 4446  CA  VAL B 475     7564  10037   9515   -756    890   -131       C  
ATOM   4447  C   VAL B 475     -18.780 -85.393  43.245  1.00 69.88           C  
ANISOU 4447  C   VAL B 475     7413   9593   9543   -583    827   -160       C  
ATOM   4448  O   VAL B 475     -18.914 -84.910  42.109  1.00 69.20           O  
ANISOU 4448  O   VAL B 475     7314   9446   9532   -442    912   -279       O  
ATOM   4449  CB  VAL B 475     -20.644 -86.466  44.558  1.00 72.76           C  
ANISOU 4449  CB  VAL B 475     7740  10239   9665   -933    778     53       C  
ATOM   4450  CG1 VAL B 475     -21.631 -86.236  45.696  1.00 74.73           C  
ANISOU 4450  CG1 VAL B 475     7914  10842   9637  -1157    861     72       C  
ATOM   4451  CG2 VAL B 475     -21.385 -86.881  43.298  1.00 71.74           C  
ANISOU 4451  CG2 VAL B 475     7602   9976   9679   -822    794      3       C  
ATOM   4452  N   SER B 476     -17.713 -86.098  43.618  1.00 69.73           N  
ANISOU 4452  N   SER B 476     7420   9457   9617   -613    665    -60       N  
ATOM   4453  CA  SER B 476     -16.566 -86.334  42.742  1.00 68.12           C  
ANISOU 4453  CA  SER B 476     7199   9068   9614   -458    602   -144       C  
ATOM   4454  C   SER B 476     -16.761 -87.579  41.841  1.00 68.31           C  
ANISOU 4454  C   SER B 476     7195   8921   9838   -400    473   -157       C  
ATOM   4455  O   SER B 476     -17.541 -88.456  42.151  1.00 69.18           O  
ANISOU 4455  O   SER B 476     7326   8989   9969   -511    356    -25       O  
ATOM   4456  CB  SER B 476     -15.330 -86.502  43.611  1.00 68.68           C  
ANISOU 4456  CB  SER B 476     7277   9085   9732   -498    460    -75       C  
ATOM   4457  OG  SER B 476     -15.439 -87.677  44.396  1.00 70.03           O  
ANISOU 4457  OG  SER B 476     7476   9174   9958   -647    224    127       O  
ATOM   4458  N   LEU B 477     -16.037 -87.660  40.735  1.00 67.80           N  
ANISOU 4458  N   LEU B 477     7064   8780   9914   -244    484   -332       N  
ATOM   4459  CA  LEU B 477     -16.103 -88.824  39.874  1.00 68.34           C  
ANISOU 4459  CA  LEU B 477     7071   8699  10193   -165    350   -426       C  
ATOM   4460  C   LEU B 477     -15.603 -90.065  40.605  1.00 71.17           C  
ANISOU 4460  C   LEU B 477     7422   8832  10786   -208     37   -322       C  
ATOM   4461  O   LEU B 477     -16.138 -91.170  40.418  1.00 72.34           O  
ANISOU 4461  O   LEU B 477     7562   8814  11110   -229   -153   -284       O  
ATOM   4462  CB  LEU B 477     -15.341 -88.583  38.569  1.00 67.67           C  
ANISOU 4462  CB  LEU B 477     6874   8671  10164    -12    445   -688       C  
ATOM   4463  CG  LEU B 477     -15.916 -87.525  37.599  1.00 65.84           C  
ANISOU 4463  CG  LEU B 477     6649   8633   9731     -4    682   -749       C  
ATOM   4464  CD1 LEU B 477     -15.027 -87.259  36.384  1.00 64.81           C  
ANISOU 4464  CD1 LEU B 477     6393   8641   9589     69    768   -969       C  
ATOM   4465  CD2 LEU B 477     -17.313 -87.898  37.131  1.00 63.48           C  
ANISOU 4465  CD2 LEU B 477     6386   8325   9405    -27    696   -714       C  
ATOM   4466  N   LYS B 478     -14.613 -89.898  41.479  1.00 73.08           N  
ANISOU 4466  N   LYS B 478     7670   9045  11051   -239    -57   -253       N  
ATOM   4467  CA  LYS B 478     -14.141 -91.042  42.249  1.00 76.70           C  
ANISOU 4467  CA  LYS B 478     8130   9262  11751   -306   -415   -106       C  
ATOM   4468  C   LYS B 478     -15.265 -91.683  43.056  1.00 78.46           C  
ANISOU 4468  C   LYS B 478     8453   9458  11898   -545   -563    204       C  
ATOM   4469  O   LYS B 478     -15.391 -92.917  43.098  1.00 80.72           O  
ANISOU 4469  O   LYS B 478     8731   9486  12450   -593   -888    309       O  
ATOM   4470  CB  LYS B 478     -13.013 -90.674  43.179  1.00 77.46           C  
ANISOU 4470  CB  LYS B 478     8231   9360  11840   -339   -498    -37       C  
ATOM   4471  CG  LYS B 478     -12.200 -91.892  43.562  1.00 82.19           C  
ANISOU 4471  CG  LYS B 478     8776   9641  12808   -324   -921     18       C  
ATOM   4472  CD  LYS B 478     -11.248 -91.620  44.691  1.00 85.93           C  
ANISOU 4472  CD  LYS B 478     9279  10113  13255   -413  -1055    168       C  
ATOM   4473  CE  LYS B 478     -11.958 -91.745  46.013  1.00 89.91           C  
ANISOU 4473  CE  LYS B 478     9930  10704  13527   -730  -1174    567       C  
ATOM   4474  NZ  LYS B 478     -10.973 -91.642  47.129  1.00 95.40           N1+
ANISOU 4474  NZ  LYS B 478    10649  11381  14216   -837  -1372    729       N1+
ATOM   4475  N   ASP B 479     -16.078 -90.837  43.687  1.00 77.88           N  
ANISOU 4475  N   ASP B 479     8452   9662  11475   -704   -341    333       N  
ATOM   4476  CA  ASP B 479     -17.229 -91.302  44.455  1.00 79.24           C  
ANISOU 4476  CA  ASP B 479     8684   9931  11492   -973   -418    604       C  
ATOM   4477  C   ASP B 479     -18.300 -91.929  43.569  1.00 78.39           C  
ANISOU 4477  C   ASP B 479     8557   9747  11480   -948   -418    566       C  
ATOM   4478  O   ASP B 479     -18.880 -92.967  43.930  1.00 80.43           O  
ANISOU 4478  O   ASP B 479     8840   9894  11823  -1141   -666    798       O  
ATOM   4479  CB  ASP B 479     -17.799 -90.165  45.298  1.00 79.29           C  
ANISOU 4479  CB  ASP B 479     8712  10311  11101  -1119   -154    643       C  
ATOM   4480  CG  ASP B 479     -17.089 -90.016  46.648  1.00 84.00           C  
ANISOU 4480  CG  ASP B 479     9344  11017  11555  -1306   -273    824       C  
ATOM   4481  OD1 ASP B 479     -15.981 -90.602  46.837  1.00 87.89           O  
ANISOU 4481  OD1 ASP B 479     9849  11267  12275  -1275   -540    901       O  
ATOM   4482  OD2 ASP B 479     -17.647 -89.306  47.524  1.00 87.93           O1-
ANISOU 4482  OD2 ASP B 479     9836  11858  11714  -1484   -108    861       O1-
ATOM   4483  N   TYR B 480     -18.551 -91.316  42.411  1.00 75.14           N  
ANISOU 4483  N   TYR B 480     8102   9393  11056   -738   -170    299       N  
ATOM   4484  CA  TYR B 480     -19.459 -91.892  41.448  1.00 74.42           C  
ANISOU 4484  CA  TYR B 480     7983   9224  11068   -688   -175    226       C  
ATOM   4485  C   TYR B 480     -19.027 -93.315  41.161  1.00 76.59           C  
ANISOU 4485  C   TYR B 480     8226   9153  11721   -651   -537    237       C  
ATOM   4486  O   TYR B 480     -19.846 -94.244  41.202  1.00 78.33           O  
ANISOU 4486  O   TYR B 480     8463   9251  12048   -783   -728    387       O  
ATOM   4487  CB  TYR B 480     -19.481 -91.101  40.158  1.00 72.05           C  
ANISOU 4487  CB  TYR B 480     7633   9011  10730   -468     79    -60       C  
ATOM   4488  CG  TYR B 480     -20.409 -91.669  39.083  1.00 73.33           C  
ANISOU 4488  CG  TYR B 480     7762   9117  10983   -412     76   -158       C  
ATOM   4489  CD1 TYR B 480     -20.027 -92.767  38.308  1.00 74.34           C  
ANISOU 4489  CD1 TYR B 480     7823   9011  11412   -298   -136   -304       C  
ATOM   4490  CD2 TYR B 480     -21.660 -91.094  38.832  1.00 71.86           C  
ANISOU 4490  CD2 TYR B 480     7588   9111  10603   -461    268   -142       C  
ATOM   4491  CE1 TYR B 480     -20.847 -93.262  37.334  1.00 73.66           C  
ANISOU 4491  CE1 TYR B 480     7700   8889  11399   -249   -142   -417       C  
ATOM   4492  CE2 TYR B 480     -22.478 -91.585  37.855  1.00 71.08           C  
ANISOU 4492  CE2 TYR B 480     7459   8967  10581   -415    257   -228       C  
ATOM   4493  CZ  TYR B 480     -22.070 -92.672  37.105  1.00 72.74           C  
ANISOU 4493  CZ  TYR B 480     7618   8959  11061   -316     57   -360       C  
ATOM   4494  OH  TYR B 480     -22.890 -93.178  36.111  1.00 72.81           O  
ANISOU 4494  OH  TYR B 480     7588   8932  11143   -271     38   -471       O  
ATOM   4495  N   CYS B 481     -17.738 -93.492  40.882  1.00 76.68           N  
ANISOU 4495  N   CYS B 481     8173   8999  11961   -475   -657     60       N  
ATOM   4496  CA  CYS B 481     -17.230 -94.822  40.588  1.00 78.50           C  
ANISOU 4496  CA  CYS B 481     8331   8866  12627   -392  -1043    -11       C  
ATOM   4497  C   CYS B 481     -17.414 -95.814  41.704  1.00 80.65           C  
ANISOU 4497  C   CYS B 481     8679   8910  13054   -642  -1447    365       C  
ATOM   4498  O   CYS B 481     -17.759 -96.933  41.428  1.00 82.83           O  
ANISOU 4498  O   CYS B 481     8931   8900  13638   -661  -1759    397       O  
ATOM   4499  CB  CYS B 481     -15.781 -94.780  40.146  1.00 78.93           C  
ANISOU 4499  CB  CYS B 481     8257   8829  12903   -154  -1094   -318       C  
ATOM   4500  SG  CYS B 481     -15.616 -94.059  38.511  1.00 78.28           S  
ANISOU 4500  SG  CYS B 481     8039   8993  12710     93   -727   -774       S  
ATOM   4501  N   THR B 482     -17.224 -95.432  42.962  1.00 81.08           N  
ANISOU 4501  N   THR B 482     8821   9093  12891   -863  -1470    664       N  
ATOM   4502  CA  THR B 482     -17.299 -96.450  44.018  1.00 84.58           C  
ANISOU 4502  CA  THR B 482     9332   9324  13478  -1153  -1917   1070       C  
ATOM   4503  C   THR B 482     -18.733 -96.904  44.254  1.00 86.39           C  
ANISOU 4503  C   THR B 482     9622   9649  13551  -1443  -1949   1352       C  
ATOM   4504  O   THR B 482     -18.984 -97.848  44.972  1.00 89.97           O  
ANISOU 4504  O   THR B 482    10128   9931  14125  -1732  -2343   1723       O  
ATOM   4505  CB  THR B 482     -16.669 -96.035  45.361  1.00 84.82           C  
ANISOU 4505  CB  THR B 482     9432   9495  13299  -1363  -1986   1344       C  
ATOM   4506  OG1 THR B 482     -17.706 -95.706  46.270  1.00 84.27           O  
ANISOU 4506  OG1 THR B 482     9442   9785  12791  -1721  -1847   1659       O  
ATOM   4507  CG2 THR B 482     -15.722 -94.858  45.225  1.00 82.79           C  
ANISOU 4507  CG2 THR B 482     9134   9422  12900  -1137  -1670   1064       C  
ATOM   4508  N   ARG B 483     -19.684 -96.227  43.636  1.00 85.30           N  
ANISOU 4508  N   ARG B 483     9468   9789  13152  -1385  -1555   1190       N  
ATOM   4509  CA  ARG B 483     -21.077 -96.575  43.796  1.00 86.64           C  
ANISOU 4509  CA  ARG B 483     9662  10097  13160  -1645  -1542   1408       C  
ATOM   4510  C   ARG B 483     -21.587 -97.369  42.613  1.00 87.15           C  
ANISOU 4510  C   ARG B 483     9677   9891  13542  -1487  -1659   1232       C  
ATOM   4511  O   ARG B 483     -22.685 -97.918  42.667  1.00 89.13           O  
ANISOU 4511  O   ARG B 483     9940  10163  13760  -1704  -1743   1426       O  
ATOM   4512  CB  ARG B 483     -21.904 -95.310  43.977  1.00 84.68           C  
ANISOU 4512  CB  ARG B 483     9403  10339  12432  -1698  -1063   1334       C  
ATOM   4513  CG  ARG B 483     -21.865 -94.753  45.393  1.00 86.48           C  
ANISOU 4513  CG  ARG B 483     9660  10913  12285  -1991   -994   1574       C  
ATOM   4514  CD  ARG B 483     -22.933 -93.697  45.567  1.00 87.23           C  
ANISOU 4514  CD  ARG B 483     9694  11479  11968  -2059   -580   1460       C  
ATOM   4515  NE  ARG B 483     -22.733 -92.594  44.636  1.00 85.46           N  
ANISOU 4515  NE  ARG B 483     9436  11282  11750  -1695   -256   1071       N  
ATOM   4516  CZ  ARG B 483     -22.236 -91.411  44.986  1.00 85.35           C  
ANISOU 4516  CZ  ARG B 483     9411  11468  11550  -1599    -28    913       C  
ATOM   4517  NH1 ARG B 483     -21.915 -91.178  46.254  1.00 87.57           N1+
ANISOU 4517  NH1 ARG B 483     9700  11970  11600  -1823    -58   1071       N1+
ATOM   4518  NH2 ARG B 483     -22.071 -90.455  44.075  1.00 82.07           N  
ANISOU 4518  NH2 ARG B 483     8971  11038  11171  -1304    206    611       N  
ATOM   4519  N   MET B 484     -20.788 -97.450  41.558  1.00 86.51           N  
ANISOU 4519  N   MET B 484     9521   9588  13757  -1130  -1669    852       N  
ATOM   4520  CA  MET B 484     -21.170 -98.179  40.364  1.00 87.87           C  
ANISOU 4520  CA  MET B 484     9621   9536  14230   -953  -1773    605       C  
ATOM   4521  C   MET B 484     -21.673 -99.602  40.646  1.00 92.81           C  
ANISOU 4521  C   MET B 484    10267   9799  15197  -1162  -2268    873       C  
ATOM   4522  O   MET B 484     -21.282-100.230  41.638  1.00 95.62           O  
ANISOU 4522  O   MET B 484    10676   9948  15706  -1382  -2654   1210       O  
ATOM   4523  CB  MET B 484     -20.042 -98.157  39.341  1.00 86.83           C  
ANISOU 4523  CB  MET B 484     9365   9262  14364   -578  -1761    139       C  
ATOM   4524  CG  MET B 484     -19.889 -96.794  38.703  1.00 84.22           C  
ANISOU 4524  CG  MET B 484     9008   9308  13683   -408  -1263   -119       C  
ATOM   4525  SD  MET B 484     -18.594 -96.527  37.474  1.00 84.45           S  
ANISOU 4525  SD  MET B 484     8863   9356  13869    -46  -1149   -657       S  
ATOM   4526  CE  MET B 484     -19.056 -97.718  36.235  1.00 88.82           C  
ANISOU 4526  CE  MET B 484     9287   9685  14776    101  -1364   -974       C  
ATOM   4527  N   LYS B 485     -22.555-100.091  39.769  1.00 94.45           N  
ANISOU 4527  N   LYS B 485    10434   9928  15523  -1115  -2281    745       N  
ATOM   4528  CA  LYS B 485     -23.217-101.382  39.929  1.00 99.42           C  
ANISOU 4528  CA  LYS B 485    11081  10224  16469  -1332  -2736    999       C  
ATOM   4529  C   LYS B 485     -22.317-102.550  39.540  1.00103.97           C  
ANISOU 4529  C   LYS B 485    11573  10238  17690  -1138  -3266    808       C  
ATOM   4530  O   LYS B 485     -21.079-102.444  39.632  1.00104.36           O  
ANISOU 4530  O   LYS B 485    11569  10162  17920   -939  -3357    624       O  
ATOM   4531  CB  LYS B 485     -24.507-101.393  39.120  1.00 98.47           C  
ANISOU 4531  CB  LYS B 485    10937  10247  16229  -1343  -2536    904       C  
ATOM   4532  CG  LYS B 485     -25.467-100.276  39.515  1.00 96.62           C  
ANISOU 4532  CG  LYS B 485    10746  10543  15420  -1521  -2059   1055       C  
ATOM   4533  CD  LYS B 485     -25.909-100.368  40.982  1.00 98.13           C  
ANISOU 4533  CD  LYS B 485    11011  10915  15358  -1979  -2167   1577       C  
ATOM   4534  CE  LYS B 485     -25.721 -99.029  41.665  1.00 96.32           C  
ANISOU 4534  CE  LYS B 485    10796  11145  14653  -2005  -1748   1576       C  
ATOM   4535  NZ  LYS B 485     -26.874 -98.740  42.530  1.00 99.09           N1+
ANISOU 4535  NZ  LYS B 485    11138  11921  14590  -2388  -1585   1867       N1+
ATOM   4536  N   GLU B 486     -22.898-103.678  39.122  1.00108.31           N  
ANISOU 4536  N   GLU B 486    12092  10431  18628  -1186  -3648    823       N  
ATOM   4537  CA  GLU B 486     -22.000-104.768  38.712  1.00113.26           C  
ANISOU 4537  CA  GLU B 486    12601  10494  19939   -952  -4186    550       C  
ATOM   4538  C   GLU B 486     -21.607-104.855  37.231  1.00112.55           C  
ANISOU 4538  C   GLU B 486    12315  10351  20097   -496  -4066   -161       C  
ATOM   4539  O   GLU B 486     -20.420-104.651  36.893  1.00112.83           O  
ANISOU 4539  O   GLU B 486    12216  10361  20292   -193  -4037   -566       O  
ATOM   4540  CB  GLU B 486     -22.265-106.133  39.376  1.00118.80           C  
ANISOU 4540  CB  GLU B 486    13354  10657  21127  -1245  -4907    974       C  
ATOM   4541  CG  GLU B 486     -20.909-106.739  39.842  1.00124.76           C  
ANISOU 4541  CG  GLU B 486    14049  10938  22416  -1124  -5443    939       C  
ATOM   4542  CD  GLU B 486     -19.803-105.643  39.968  1.00125.56           C  
ANISOU 4542  CD  GLU B 486    14111  11367  22227   -893  -5033    694       C  
ATOM   4543  OE1 GLU B 486     -19.889-104.774  40.877  1.00124.02           O  
ANISOU 4543  OE1 GLU B 486    14053  11566  21502  -1142  -4728   1066       O  
ATOM   4544  OE2 GLU B 486     -18.860-105.631  39.135  1.00127.36           O1-
ANISOU 4544  OE2 GLU B 486    14151  11496  22744   -470  -5004    100       O1-
ATOM   4545  N   ASN B 487     -22.558-105.137  36.353  1.00111.52           N  
ANISOU 4545  N   ASN B 487    12147  10248  19976   -462  -3989   -332       N  
ATOM   4546  CA  ASN B 487     -22.207-105.110  34.957  1.00110.62           C  
ANISOU 4546  CA  ASN B 487    11839  10201  19989    -71  -3821  -1009       C  
ATOM   4547  C   ASN B 487     -21.956-103.670  34.480  1.00105.17           C  
ANISOU 4547  C   ASN B 487    11139  10099  18721     65  -3156  -1225       C  
ATOM   4548  O   ASN B 487     -21.851-103.441  33.282  1.00104.92           O  
ANISOU 4548  O   ASN B 487    10964  10273  18627    309  -2918  -1721       O  
ATOM   4549  CB  ASN B 487     -23.288-105.800  34.103  1.00112.64           C  
ANISOU 4549  CB  ASN B 487    12052  10340  20403    -75  -3931  -1151       C  
ATOM   4550  CG  ASN B 487     -23.306-107.342  34.262  1.00119.78           C  
ANISOU 4550  CG  ASN B 487    12902  10574  22035   -115  -4674  -1113       C  
ATOM   4551  OD1 ASN B 487     -24.246-108.028  33.788  1.00121.52           O  
ANISOU 4551  OD1 ASN B 487    13113  10621  22436   -187  -4861  -1122       O  
ATOM   4552  ND2 ASN B 487     -22.270-107.888  34.915  1.00123.33           N  
ANISOU 4552  ND2 ASN B 487    13309  10618  22932    -69  -5134  -1071       N  
ATOM   4553  N   GLN B 488     -21.860-102.701  35.394  1.00101.11           N  
ANISOU 4553  N   GLN B 488    10767   9864  17786   -107  -2878   -861       N  
ATOM   4554  CA  GLN B 488     -21.771-101.282  34.983  1.00 95.88           C  
ANISOU 4554  CA  GLN B 488    10114   9724  16592    -17  -2287  -1003       C  
ATOM   4555  C   GLN B 488     -20.391-100.835  34.541  1.00 95.13           C  
ANISOU 4555  C   GLN B 488     9874   9738  16532    252  -2160  -1413       C  
ATOM   4556  O   GLN B 488     -19.432-100.818  35.318  1.00 95.90           O  
ANISOU 4556  O   GLN B 488     9972   9711  16754    257  -2309  -1322       O  
ATOM   4557  CB  GLN B 488     -22.316-100.318  36.035  1.00 93.25           C  
ANISOU 4557  CB  GLN B 488     9959   9684  15786   -290  -2010   -528       C  
ATOM   4558  CG  GLN B 488     -22.541 -98.911  35.471  1.00 88.21           C  
ANISOU 4558  CG  GLN B 488     9331   9519  14663   -207  -1462   -670       C  
ATOM   4559  CD  GLN B 488     -22.867 -97.895  36.533  1.00 84.49           C  
ANISOU 4559  CD  GLN B 488     8989   9323  13788   -416  -1212   -312       C  
ATOM   4560  OE1 GLN B 488     -22.937 -98.227  37.711  1.00 86.48           O  
ANISOU 4560  OE1 GLN B 488     9320   9481  14055   -650  -1410     46       O  
ATOM   4561  NE2 GLN B 488     -23.079 -96.651  36.126  1.00 78.80           N  
ANISOU 4561  NE2 GLN B 488     8279   8952  12708   -351   -802   -413       N  
ATOM   4562  N   LYS B 489     -20.336-100.410  33.289  1.00 93.54           N  
ANISOU 4562  N   LYS B 489     9546   9822  16174    444  -1865  -1844       N  
ATOM   4563  CA  LYS B 489     -19.092-100.264  32.541  1.00 93.96           C  
ANISOU 4563  CA  LYS B 489     9380  10005  16312    703  -1787  -2357       C  
ATOM   4564  C   LYS B 489     -18.852 -98.796  32.161  1.00 89.87           C  
ANISOU 4564  C   LYS B 489     8886  10006  15255    696  -1268  -2385       C  
ATOM   4565  O   LYS B 489     -17.793 -98.446  31.638  1.00 90.71           O  
ANISOU 4565  O   LYS B 489     8821  10322  15322    844  -1137  -2738       O  
ATOM   4566  CB  LYS B 489     -19.184-101.167  31.285  1.00 96.64           C  
ANISOU 4566  CB  LYS B 489     9500  10271  16947    902  -1944  -2896       C  
ATOM   4567  CG  LYS B 489     -17.915-101.388  30.489  1.00100.90           C  
ANISOU 4567  CG  LYS B 489     9731  10916  17689   1176  -1968  -3537       C  
ATOM   4568  CD  LYS B 489     -17.077-102.585  30.982  1.00108.79           C  
ANISOU 4568  CD  LYS B 489    10577  11388  19370   1334  -2525  -3737       C  
ATOM   4569  CE  LYS B 489     -15.562-102.217  31.073  1.00110.04           C  
ANISOU 4569  CE  LYS B 489    10536  11691  19583   1502  -2464  -4051       C  
ATOM   4570  NZ  LYS B 489     -14.660-103.408  30.920  1.00115.37           N1+
ANISOU 4570  NZ  LYS B 489    10907  11970  20956   1772  -2962  -4577       N1+
ATOM   4571  N   HIS B 490     -19.830 -97.945  32.464  1.00 85.77           N  
ANISOU 4571  N   HIS B 490     8561   9683  14343    509  -1005  -2010       N  
ATOM   4572  CA  HIS B 490     -19.952 -96.636  31.853  1.00 82.37           C  
ANISOU 4572  CA  HIS B 490     8155   9692  13450    491   -575  -2038       C  
ATOM   4573  C   HIS B 490     -20.371 -95.596  32.873  1.00 79.56           C  
ANISOU 4573  C   HIS B 490     7996   9440  12792    314   -387  -1597       C  
ATOM   4574  O   HIS B 490     -21.080 -95.908  33.820  1.00 79.84           O  
ANISOU 4574  O   HIS B 490     8154   9305  12873    162   -519  -1266       O  
ATOM   4575  CB  HIS B 490     -21.035 -96.664  30.775  1.00 82.15           C  
ANISOU 4575  CB  HIS B 490     8114   9818  13279    480   -460  -2148       C  
ATOM   4576  CG  HIS B 490     -20.672 -97.444  29.552  1.00 85.41           C  
ANISOU 4576  CG  HIS B 490     8304  10269  13878    650   -558  -2662       C  
ATOM   4577  ND1 HIS B 490     -19.666 -97.060  28.694  1.00 85.98           N  
ANISOU 4577  ND1 HIS B 490     8185  10664  13817    759   -391  -3053       N  
ATOM   4578  CD2 HIS B 490     -21.200 -98.578  29.028  1.00 88.37           C  
ANISOU 4578  CD2 HIS B 490     8593  10434  14547    716   -807  -2877       C  
ATOM   4579  CE1 HIS B 490     -19.579 -97.932  27.704  1.00 88.95           C  
ANISOU 4579  CE1 HIS B 490     8349  11062  14384    893   -517  -3524       C  
ATOM   4580  NE2 HIS B 490     -20.499 -98.862  27.881  1.00 88.98           N  
ANISOU 4580  NE2 HIS B 490     8419  10718  14671    884   -781  -3434       N  
ATOM   4581  N   ILE B 491     -19.957 -94.349  32.659  1.00 77.29           N  
ANISOU 4581  N   ILE B 491     7720   9456  12189    315    -88  -1608       N  
ATOM   4582  CA  ILE B 491     -20.361 -93.224  33.495  1.00 74.10           C  
ANISOU 4582  CA  ILE B 491     7471   9175  11507    179    100  -1277       C  
ATOM   4583  C   ILE B 491     -21.353 -92.434  32.679  1.00 72.54           C  
ANISOU 4583  C   ILE B 491     7309   9205  11047    143    321  -1263       C  
ATOM   4584  O   ILE B 491     -21.021 -91.917  31.621  1.00 71.93           O  
ANISOU 4584  O   ILE B 491     7157   9345  10825    195    463  -1454       O  
ATOM   4585  CB  ILE B 491     -19.133 -92.339  33.920  1.00 73.68           C  
ANISOU 4585  CB  ILE B 491     7407   9240  11348    204    217  -1284       C  
ATOM   4586  CG1 ILE B 491     -18.152 -93.170  34.791  1.00 74.65           C  
ANISOU 4586  CG1 ILE B 491     7489   9108  11764    240    -47  -1284       C  
ATOM   4587  CG2 ILE B 491     -19.590 -91.001  34.553  1.00 69.22           C  
ANISOU 4587  CG2 ILE B 491     6973   8833  10492     90    429  -1027       C  
ATOM   4588  CD1 ILE B 491     -16.863 -92.444  35.205  1.00 73.55           C  
ANISOU 4588  CD1 ILE B 491     7314   9065  11563    274     33  -1319       C  
ATOM   4589  N   TYR B 492     -22.583 -92.373  33.172  1.00 71.98           N  
ANISOU 4589  N   TYR B 492     7335   9100  10914     31    328  -1032       N  
ATOM   4590  CA  TYR B 492     -23.680 -91.738  32.455  1.00 71.12           C  
ANISOU 4590  CA  TYR B 492     7248   9153  10618      3    479  -1013       C  
ATOM   4591  C   TYR B 492     -23.795 -90.308  32.831  1.00 69.63           C  
ANISOU 4591  C   TYR B 492     7124   9125  10206    -40    667   -877       C  
ATOM   4592  O   TYR B 492     -23.766 -89.977  34.011  1.00 69.98           O  
ANISOU 4592  O   TYR B 492     7222   9144  10223   -107    679   -716       O  
ATOM   4593  CB  TYR B 492     -24.998 -92.424  32.795  1.00 71.64           C  
ANISOU 4593  CB  TYR B 492     7348   9113  10760    -93    377   -870       C  
ATOM   4594  CG  TYR B 492     -25.035 -93.862  32.348  1.00 73.48           C  
ANISOU 4594  CG  TYR B 492     7517   9137  11262    -56    140  -1001       C  
ATOM   4595  CD1 TYR B 492     -24.983 -94.179  31.005  1.00 74.33           C  
ANISOU 4595  CD1 TYR B 492     7534   9304  11404     55    137  -1288       C  
ATOM   4596  CD2 TYR B 492     -25.120 -94.893  33.263  1.00 74.50           C  
ANISOU 4596  CD2 TYR B 492     7670   9020  11615   -153   -107   -841       C  
ATOM   4597  CE1 TYR B 492     -25.015 -95.464  30.587  1.00 77.53           C  
ANISOU 4597  CE1 TYR B 492     7859   9507  12089    110    -98  -1467       C  
ATOM   4598  CE2 TYR B 492     -25.143 -96.192  32.850  1.00 77.84           C  
ANISOU 4598  CE2 TYR B 492     8031   9195  12349   -114   -381   -968       C  
ATOM   4599  CZ  TYR B 492     -25.091 -96.470  31.504  1.00 78.94           C  
ANISOU 4599  CZ  TYR B 492     8066   9377  12549     38   -372  -1311       C  
ATOM   4600  OH  TYR B 492     -25.109 -97.758  31.048  1.00 81.91           O  
ANISOU 4600  OH  TYR B 492     8355   9498  13269    103   -664  -1506       O  
ATOM   4601  N   TYR B 493     -23.961 -89.449  31.844  1.00 69.14           N  
ANISOU 4601  N   TYR B 493     7051   9229   9989    -19    787   -939       N  
ATOM   4602  CA  TYR B 493     -24.186 -88.049  32.150  1.00 68.12           C  
ANISOU 4602  CA  TYR B 493     6976   9192   9711    -55    904   -811       C  
ATOM   4603  C   TYR B 493     -25.264 -87.488  31.285  1.00 68.36           C  
ANISOU 4603  C   TYR B 493     7009   9304   9659    -71    932   -792       C  
ATOM   4604  O   TYR B 493     -25.603 -88.060  30.249  1.00 69.47           O  
ANISOU 4604  O   TYR B 493     7110   9489   9793    -62    895   -888       O  
ATOM   4605  CB  TYR B 493     -22.910 -87.235  31.966  1.00 67.67           C  
ANISOU 4605  CB  TYR B 493     6912   9231   9569    -45    969   -844       C  
ATOM   4606  CG  TYR B 493     -22.489 -87.028  30.529  1.00 67.91           C  
ANISOU 4606  CG  TYR B 493     6879   9443   9477    -57   1004   -962       C  
ATOM   4607  CD1 TYR B 493     -21.649 -87.934  29.886  1.00 68.71           C  
ANISOU 4607  CD1 TYR B 493     6869   9622   9613    -15    980  -1188       C  
ATOM   4608  CD2 TYR B 493     -22.919 -85.919  29.820  1.00 66.66           C  
ANISOU 4608  CD2 TYR B 493     6753   9401   9172   -129   1036   -860       C  
ATOM   4609  CE1 TYR B 493     -21.258 -87.737  28.583  1.00 69.57           C  
ANISOU 4609  CE1 TYR B 493     6887   9996   9550    -66   1034  -1325       C  
ATOM   4610  CE2 TYR B 493     -22.546 -85.717  28.524  1.00 67.07           C  
ANISOU 4610  CE2 TYR B 493     6746   9679   9057   -206   1055   -923       C  
ATOM   4611  CZ  TYR B 493     -21.708 -86.615  27.908  1.00 69.64           C  
ANISOU 4611  CZ  TYR B 493     6947  10157   9354   -186   1078  -1163       C  
ATOM   4612  OH  TYR B 493     -21.339 -86.385  26.595  1.00 73.27           O  
ANISOU 4612  OH  TYR B 493     7315  10938   9583   -303   1118  -1250       O  
ATOM   4613  N   ILE B 494     -25.769 -86.340  31.708  1.00 68.37           N  
ANISOU 4613  N   ILE B 494     7044   9320   9614    -89    974   -689       N  
ATOM   4614  CA  ILE B 494     -26.737 -85.550  30.942  1.00 68.95           C  
ANISOU 4614  CA  ILE B 494     7115   9434   9648    -97    955   -652       C  
ATOM   4615  C   ILE B 494     -26.345 -84.051  31.040  1.00 69.90           C  
ANISOU 4615  C   ILE B 494     7266   9555   9736   -106    952   -574       C  
ATOM   4616  O   ILE B 494     -25.893 -83.598  32.089  1.00 69.64           O  
ANISOU 4616  O   ILE B 494     7244   9478   9735    -90    986   -563       O  
ATOM   4617  CB  ILE B 494     -28.170 -85.817  31.449  1.00 68.25           C  
ANISOU 4617  CB  ILE B 494     6991   9304   9635    -95    938   -642       C  
ATOM   4618  CG1 ILE B 494     -29.186 -85.061  30.613  1.00 67.66           C  
ANISOU 4618  CG1 ILE B 494     6895   9243   9566    -83    879   -624       C  
ATOM   4619  CG2 ILE B 494     -28.291 -85.450  32.916  1.00 67.77           C  
ANISOU 4619  CG2 ILE B 494     6912   9236   9602   -105    988   -621       C  
ATOM   4620  CD1 ILE B 494     -30.464 -85.806  30.388  1.00 66.47           C  
ANISOU 4620  CD1 ILE B 494     6690   9095   9469    -90    845   -656       C  
ATOM   4621  N   THR B 495     -26.460 -83.302  29.947  1.00 71.72           N  
ANISOU 4621  N   THR B 495     7510   9834   9906   -153    883   -509       N  
ATOM   4622  CA  THR B 495     -26.224 -81.852  30.000  1.00 73.53           C  
ANISOU 4622  CA  THR B 495     7770  10005  10163   -183    806   -400       C  
ATOM   4623  C   THR B 495     -27.536 -81.129  29.725  1.00 75.15           C  
ANISOU 4623  C   THR B 495     7956  10108  10488   -156    668   -357       C  
ATOM   4624  O   THR B 495     -28.233 -81.475  28.768  1.00 76.14           O  
ANISOU 4624  O   THR B 495     8072  10284  10573   -189    609   -333       O  
ATOM   4625  CB  THR B 495     -25.149 -81.353  28.977  1.00 74.37           C  
ANISOU 4625  CB  THR B 495     7903  10243  10111   -319    771   -294       C  
ATOM   4626  OG1 THR B 495     -25.369 -81.962  27.703  1.00 75.66           O  
ANISOU 4626  OG1 THR B 495     8041  10581  10125   -399    760   -305       O  
ATOM   4627  CG2 THR B 495     -23.741 -81.694  29.430  1.00 74.61           C  
ANISOU 4627  CG2 THR B 495     7921  10354  10072   -329    886   -357       C  
ATOM   4628  N   GLY B 496     -27.876 -80.156  30.570  1.00 76.05           N  
ANISOU 4628  N   GLY B 496     8044  10082  10769    -86    602   -384       N  
ATOM   4629  CA  GLY B 496     -28.995 -79.261  30.327  1.00 78.67           C  
ANISOU 4629  CA  GLY B 496     8327  10277  11286    -36    416   -379       C  
ATOM   4630  C   GLY B 496     -28.861 -77.982  31.132  1.00 81.00           C  
ANISOU 4630  C   GLY B 496     8589  10403  11783     31    302   -430       C  
ATOM   4631  O   GLY B 496     -27.812 -77.710  31.718  1.00 80.77           O  
ANISOU 4631  O   GLY B 496     8600  10375  11714     10    363   -423       O  
ATOM   4632  N   GLU B 497     -29.939 -77.203  31.192  1.00 83.78           N  
ANISOU 4632  N   GLU B 497     8847  10601  12381    128    119   -519       N  
ATOM   4633  CA  GLU B 497     -29.920 -75.908  31.880  1.00 85.96           C  
ANISOU 4633  CA  GLU B 497     9058  10676  12925    221    -52   -629       C  
ATOM   4634  C   GLU B 497     -30.178 -75.964  33.381  1.00 85.36           C  
ANISOU 4634  C   GLU B 497     8842  10685  12906    349    110   -945       C  
ATOM   4635  O   GLU B 497     -29.726 -75.080  34.069  1.00 86.57           O  
ANISOU 4635  O   GLU B 497     8961  10730  13200    404     34  -1052       O  
ATOM   4636  CB  GLU B 497     -30.877 -74.899  31.217  1.00 88.89           C  
ANISOU 4636  CB  GLU B 497     9366  10797  13609    277   -402   -607       C  
ATOM   4637  CG  GLU B 497     -30.829 -74.856  29.668  1.00 93.41           C  
ANISOU 4637  CG  GLU B 497    10065  11333  14091    103   -597   -265       C  
ATOM   4638  CD  GLU B 497     -32.186 -74.495  29.024  1.00101.08           C  
ANISOU 4638  CD  GLU B 497    10948  12145  15310    169   -874   -276       C  
ATOM   4639  OE1 GLU B 497     -32.975 -75.430  28.709  1.00102.45           O  
ANISOU 4639  OE1 GLU B 497    11080  12477  15368    187   -744   -336       O  
ATOM   4640  OE2 GLU B 497     -32.477 -73.282  28.844  1.00105.20           O1-
ANISOU 4640  OE2 GLU B 497    11435  12359  16175    205  -1250   -229       O1-
ATOM   4641  N   THR B 498     -30.889 -76.976  33.892  1.00 84.71           N  
ANISOU 4641  N   THR B 498     8669  10815  12701    369    317  -1090       N  
ATOM   4642  CA  THR B 498     -31.269 -77.039  35.334  1.00 85.25           C  
ANISOU 4642  CA  THR B 498     8568  11054  12766    434    472  -1390       C  
ATOM   4643  C   THR B 498     -31.258 -78.441  35.919  1.00 83.61           C  
ANISOU 4643  C   THR B 498     8369  11123  12276    324    734  -1365       C  
ATOM   4644  O   THR B 498     -31.629 -79.405  35.257  1.00 82.75           O  
ANISOU 4644  O   THR B 498     8308  11063  12069    260    777  -1234       O  
ATOM   4645  CB  THR B 498     -32.705 -76.537  35.594  1.00 87.49           C  
ANISOU 4645  CB  THR B 498     8609  11347  13284    568    377  -1694       C  
ATOM   4646  OG1 THR B 498     -32.937 -75.331  34.877  1.00 90.60           O  
ANISOU 4646  OG1 THR B 498     8987  11422  14013    675     50  -1694       O  
ATOM   4647  CG2 THR B 498     -32.935 -76.275  37.079  1.00 89.85           C  
ANISOU 4647  CG2 THR B 498     8695  11865  13576    621    511  -2059       C  
ATOM   4648  N   LYS B 499     -30.876 -78.535  37.187  1.00 83.67           N  
ANISOU 4648  N   LYS B 499     8317  11305  12167    289    877  -1493       N  
ATOM   4649  CA  LYS B 499     -30.969 -79.775  37.943  1.00 83.13           C  
ANISOU 4649  CA  LYS B 499     8229  11502  11852    148   1072  -1458       C  
ATOM   4650  C   LYS B 499     -32.342 -80.427  37.805  1.00 83.92           C  
ANISOU 4650  C   LYS B 499     8191  11754  11939    112   1112  -1528       C  
ATOM   4651  O   LYS B 499     -32.425 -81.617  37.560  1.00 83.12           O  
ANISOU 4651  O   LYS B 499     8162  11712  11707     -6   1169  -1350       O  
ATOM   4652  CB  LYS B 499     -30.659 -79.500  39.403  1.00 84.25           C  
ANISOU 4652  CB  LYS B 499     8268  11860  11882    102   1179  -1637       C  
ATOM   4653  CG  LYS B 499     -30.302 -80.696  40.237  1.00 84.87           C  
ANISOU 4653  CG  LYS B 499     8387  12172  11684    -99   1322  -1494       C  
ATOM   4654  CD  LYS B 499     -29.927 -80.205  41.644  1.00 89.54           C  
ANISOU 4654  CD  LYS B 499     8875  12998  12148   -156   1404  -1676       C  
ATOM   4655  CE  LYS B 499     -29.910 -81.337  42.659  1.00 92.78           C  
ANISOU 4655  CE  LYS B 499     9267  13724  12258   -414   1518  -1546       C  
ATOM   4656  NZ  LYS B 499     -31.245 -82.007  42.867  1.00 95.86           N1+
ANISOU 4656  NZ  LYS B 499     9485  14400  12535   -555   1592  -1596       N1+
ATOM   4657  N   ASP B 500     -33.416 -79.658  37.946  1.00 86.18           N  
ANISOU 4657  N   ASP B 500     8262  12088  12391    221   1058  -1805       N  
ATOM   4658  CA  ASP B 500     -34.762 -80.237  37.852  1.00 87.67           C  
ANISOU 4658  CA  ASP B 500     8283  12454  12571    181   1101  -1899       C  
ATOM   4659  C   ASP B 500     -35.142 -80.579  36.429  1.00 86.15           C  
ANISOU 4659  C   ASP B 500     8201  12042  12486    219    973  -1710       C  
ATOM   4660  O   ASP B 500     -35.870 -81.537  36.199  1.00 86.26           O  
ANISOU 4660  O   ASP B 500     8181  12174  12418    124   1027  -1645       O  
ATOM   4661  CB  ASP B 500     -35.843 -79.327  38.462  1.00 91.33           C  
ANISOU 4661  CB  ASP B 500     8425  13077  13199    299   1082  -2325       C  
ATOM   4662  CG  ASP B 500     -35.819 -79.320  39.989  1.00 95.04           C  
ANISOU 4662  CG  ASP B 500     8703  13948  13458    190   1271  -2571       C  
ATOM   4663  OD1 ASP B 500     -34.722 -79.490  40.594  1.00 97.41           O  
ANISOU 4663  OD1 ASP B 500     9149  14286  13576     92   1346  -2433       O  
ATOM   4664  OD2 ASP B 500     -36.901 -79.118  40.579  1.00 97.66           O1-
ANISOU 4664  OD2 ASP B 500     8720  14587  13799    195   1339  -2921       O1-
ATOM   4665  N   GLN B 501     -34.659 -79.794  35.478  1.00 85.04           N  
ANISOU 4665  N   GLN B 501     8190  11605  12516    329    789  -1610       N  
ATOM   4666  CA  GLN B 501     -34.984 -80.022  34.090  1.00 84.32           C  
ANISOU 4666  CA  GLN B 501     8198  11348  12490    337    651  -1429       C  
ATOM   4667  C   GLN B 501     -34.380 -81.347  33.606  1.00 81.86           C  
ANISOU 4667  C   GLN B 501     8065  11084  11951    198    756  -1183       C  
ATOM   4668  O   GLN B 501     -34.936 -82.000  32.732  1.00 82.12           O  
ANISOU 4668  O   GLN B 501     8123  11105  11971    167    715  -1098       O  
ATOM   4669  CB  GLN B 501     -34.485 -78.852  33.250  1.00 85.27           C  
ANISOU 4669  CB  GLN B 501     8416  11183  12798    418    409  -1332       C  
ATOM   4670  CG  GLN B 501     -35.005 -78.807  31.800  1.00 88.48           C  
ANISOU 4670  CG  GLN B 501     8886  11442  13287    412    207  -1162       C  
ATOM   4671  CD  GLN B 501     -33.865 -78.762  30.755  1.00 90.47           C  
ANISOU 4671  CD  GLN B 501     9367  11601  13405    300    130   -857       C  
ATOM   4672  OE1 GLN B 501     -33.961 -79.388  29.683  1.00 91.99           O  
ANISOU 4672  OE1 GLN B 501     9644  11835  13472    213    104   -697       O  
ATOM   4673  NE2 GLN B 501     -32.781 -78.040  31.076  1.00 88.93           N  
ANISOU 4673  NE2 GLN B 501     9250  11321  13218    287    101   -799       N  
ATOM   4674  N   VAL B 502     -33.247 -81.757  34.170  1.00 80.02           N  
ANISOU 4674  N   VAL B 502     7942  10895  11565    125    869  -1095       N  
ATOM   4675  CA  VAL B 502     -32.602 -82.989  33.725  1.00 77.65           C  
ANISOU 4675  CA  VAL B 502     7782  10602  11118     25    923   -916       C  
ATOM   4676  C   VAL B 502     -33.088 -84.176  34.513  1.00 77.99           C  
ANISOU 4676  C   VAL B 502     7762  10806  11063    -94   1026   -914       C  
ATOM   4677  O   VAL B 502     -33.347 -85.222  33.934  1.00 77.47           O  
ANISOU 4677  O   VAL B 502     7735  10721  10977   -154   1002   -828       O  
ATOM   4678  CB  VAL B 502     -31.060 -82.911  33.724  1.00 76.36           C  
ANISOU 4678  CB  VAL B 502     7764  10372  10877      9    943   -810       C  
ATOM   4679  CG1 VAL B 502     -30.585 -82.148  32.497  1.00 75.49           C  
ANISOU 4679  CG1 VAL B 502     7739  10138  10805     44    820   -722       C  
ATOM   4680  CG2 VAL B 502     -30.523 -82.291  35.009  1.00 74.93           C  
ANISOU 4680  CG2 VAL B 502     7546  10241  10680     16   1009   -890       C  
ATOM   4681  N   ALA B 503     -33.221 -84.003  35.828  1.00 79.07           N  
ANISOU 4681  N   ALA B 503     7791  11115  11136   -151   1121  -1010       N  
ATOM   4682  CA  ALA B 503     -33.780 -85.029  36.720  1.00 80.41           C  
ANISOU 4682  CA  ALA B 503     7874  11501  11176   -336   1202   -975       C  
ATOM   4683  C   ALA B 503     -35.099 -85.581  36.218  1.00 81.62           C  
ANISOU 4683  C   ALA B 503     7920  11717  11374   -378   1177   -997       C  
ATOM   4684  O   ALA B 503     -35.351 -86.778  36.296  1.00 82.82           O  
ANISOU 4684  O   ALA B 503     8090  11912  11464   -538   1165   -855       O  
ATOM   4685  CB  ALA B 503     -33.967 -84.479  38.112  1.00 81.76           C  
ANISOU 4685  CB  ALA B 503     7885  11941  11238   -404   1311  -1134       C  
ATOM   4686  N   ASN B 504     -35.945 -84.710  35.696  1.00 82.32           N  
ANISOU 4686  N   ASN B 504     7891  11786  11601   -238   1134  -1169       N  
ATOM   4687  CA  ASN B 504     -37.259 -85.126  35.253  1.00 83.58           C  
ANISOU 4687  CA  ASN B 504     7919  12020  11818   -267   1106  -1219       C  
ATOM   4688  C   ASN B 504     -37.355 -85.310  33.747  1.00 82.30           C  
ANISOU 4688  C   ASN B 504     7880  11622  11769   -176    967  -1119       C  
ATOM   4689  O   ASN B 504     -38.409 -85.116  33.154  1.00 84.01           O  
ANISOU 4689  O   ASN B 504     7985  11834  12098   -120    893  -1204       O  
ATOM   4690  CB  ASN B 504     -38.306 -84.130  35.768  1.00 85.83           C  
ANISOU 4690  CB  ASN B 504     7929  12482  12197   -182   1132  -1524       C  
ATOM   4691  CG  ASN B 504     -38.167 -83.870  37.270  1.00 88.26           C  
ANISOU 4691  CG  ASN B 504     8084  13100  12350   -282   1285  -1682       C  
ATOM   4692  OD1 ASN B 504     -37.934 -82.735  37.697  1.00 90.04           O  
ANISOU 4692  OD1 ASN B 504     8221  13326  12662   -142   1280  -1908       O  
ATOM   4693  ND2 ASN B 504     -38.289 -84.932  38.076  1.00 89.40           N  
ANISOU 4693  ND2 ASN B 504     8195  13510  12262   -547   1395  -1554       N  
ATOM   4694  N   SER B 505     -36.257 -85.678  33.118  1.00 80.10           N  
ANISOU 4694  N   SER B 505     7807  11176  11449   -170    926   -960       N  
ATOM   4695  CA  SER B 505     -36.253 -85.745  31.671  1.00 79.38           C  
ANISOU 4695  CA  SER B 505     7814  10934  11412   -106    805   -896       C  
ATOM   4696  C   SER B 505     -36.560 -87.169  31.257  1.00 78.99           C  
ANISOU 4696  C   SER B 505     7793  10885  11331   -209    785   -822       C  
ATOM   4697  O   SER B 505     -36.304 -88.113  32.009  1.00 79.13           O  
ANISOU 4697  O   SER B 505     7823  10943  11297   -330    831   -757       O  
ATOM   4698  CB  SER B 505     -34.899 -85.295  31.106  1.00 78.57           C  
ANISOU 4698  CB  SER B 505     7875  10713  11264    -57    772   -813       C  
ATOM   4699  OG  SER B 505     -33.948 -86.360  31.101  1.00 78.34           O  
ANISOU 4699  OG  SER B 505     7951  10669  11146   -125    814   -739       O  
ATOM   4700  N   ALA B 506     -37.101 -87.339  30.060  1.00 78.57           N  
ANISOU 4700  N   ALA B 506     7752  10776  11324   -176    682   -823       N  
ATOM   4701  CA  ALA B 506     -37.446 -88.677  29.632  1.00 78.23           C  
ANISOU 4701  CA  ALA B 506     7721  10715  11285   -263    637   -790       C  
ATOM   4702  C   ALA B 506     -36.198 -89.565  29.593  1.00 77.13           C  
ANISOU 4702  C   ALA B 506     7708  10489  11107   -294    631   -743       C  
ATOM   4703  O   ALA B 506     -36.263 -90.727  29.995  1.00 78.30           O  
ANISOU 4703  O   ALA B 506     7851  10596  11301   -396    593   -700       O  
ATOM   4704  CB  ALA B 506     -38.153 -88.649  28.301  1.00 78.99           C  
ANISOU 4704  CB  ALA B 506     7809  10784  11419   -219    521   -821       C  
ATOM   4705  N   PHE B 507     -35.069 -89.006  29.145  1.00 75.17           N  
ANISOU 4705  N   PHE B 507     7554  10212  10795   -219    645   -753       N  
ATOM   4706  CA  PHE B 507     -33.799 -89.743  28.970  1.00 73.34           C  
ANISOU 4706  CA  PHE B 507     7402   9918  10544   -217    633   -774       C  
ATOM   4707  C   PHE B 507     -33.276 -90.462  30.221  1.00 72.67           C  
ANISOU 4707  C   PHE B 507     7329   9769  10511   -286    644   -710       C  
ATOM   4708  O   PHE B 507     -32.490 -91.407  30.115  1.00 72.70           O  
ANISOU 4708  O   PHE B 507     7367   9668  10586   -287    567   -744       O  
ATOM   4709  CB  PHE B 507     -32.686 -88.804  28.487  1.00 72.34           C  
ANISOU 4709  CB  PHE B 507     7339   9834  10311   -156    674   -786       C  
ATOM   4710  CG  PHE B 507     -33.106 -87.838  27.425  1.00 71.52           C  
ANISOU 4710  CG  PHE B 507     7237   9800  10136   -140    628   -769       C  
ATOM   4711  CD1 PHE B 507     -33.117 -88.210  26.095  1.00 71.43           C  
ANISOU 4711  CD1 PHE B 507     7228   9869  10040   -163    561   -828       C  
ATOM   4712  CD2 PHE B 507     -33.460 -86.544  27.752  1.00 71.05           C  
ANISOU 4712  CD2 PHE B 507     7166   9726  10101   -112    618   -699       C  
ATOM   4713  CE1 PHE B 507     -33.481 -87.319  25.115  1.00 70.63           C  
ANISOU 4713  CE1 PHE B 507     7138   9848   9848   -195    481   -759       C  
ATOM   4714  CE2 PHE B 507     -33.831 -85.641  26.765  1.00 70.66           C  
ANISOU 4714  CE2 PHE B 507     7126   9693  10027   -118    503   -638       C  
ATOM   4715  CZ  PHE B 507     -33.841 -86.032  25.450  1.00 70.40           C  
ANISOU 4715  CZ  PHE B 507     7116   9756   9877   -177    432   -638       C  
ATOM   4716  N   VAL B 508     -33.672 -90.012  31.405  1.00 72.00           N  
ANISOU 4716  N   VAL B 508     7201   9758  10397   -351    719   -634       N  
ATOM   4717  CA  VAL B 508     -33.108 -90.625  32.607  1.00 72.12           C  
ANISOU 4717  CA  VAL B 508     7236   9749  10416   -461    710   -532       C  
ATOM   4718  C   VAL B 508     -34.037 -91.537  33.383  1.00 73.90           C  
ANISOU 4718  C   VAL B 508     7393  10019  10667   -655    653   -414       C  
ATOM   4719  O   VAL B 508     -33.613 -92.142  34.361  1.00 74.62           O  
ANISOU 4719  O   VAL B 508     7506  10092  10753   -799    597   -275       O  
ATOM   4720  CB  VAL B 508     -32.447 -89.604  33.562  1.00 71.38           C  
ANISOU 4720  CB  VAL B 508     7153   9743  10222   -445    824   -517       C  
ATOM   4721  CG1 VAL B 508     -31.140 -89.045  32.928  1.00 70.00           C  
ANISOU 4721  CG1 VAL B 508     7067   9490  10037   -310    837   -576       C  
ATOM   4722  CG2 VAL B 508     -33.405 -88.518  33.965  1.00 69.47           C  
ANISOU 4722  CG2 VAL B 508     6802   9669   9924   -432    925   -587       C  
ATOM   4723  N   GLU B 509     -35.282 -91.656  32.919  1.00 74.69           N  
ANISOU 4723  N   GLU B 509     7407  10182  10790   -685    643   -447       N  
ATOM   4724  CA  GLU B 509     -36.311 -92.425  33.595  1.00 76.45           C  
ANISOU 4724  CA  GLU B 509     7532  10503  11011   -905    600   -331       C  
ATOM   4725  C   GLU B 509     -35.876 -93.841  33.977  1.00 77.61           C  
ANISOU 4725  C   GLU B 509     7746  10474  11266  -1076    404   -151       C  
ATOM   4726  O   GLU B 509     -36.088 -94.263  35.110  1.00 79.35           O  
ANISOU 4726  O   GLU B 509     7926  10806  11414  -1323    374     37       O  
ATOM   4727  CB  GLU B 509     -37.551 -92.488  32.724  1.00 77.42           C  
ANISOU 4727  CB  GLU B 509     7566  10658  11192   -879    578   -415       C  
ATOM   4728  CG  GLU B 509     -38.321 -91.165  32.597  1.00 79.92           C  
ANISOU 4728  CG  GLU B 509     7762  11153  11449   -763    711   -567       C  
ATOM   4729  CD  GLU B 509     -39.405 -91.164  31.495  1.00 82.23           C  
ANISOU 4729  CD  GLU B 509     7985  11426  11829   -695    646   -656       C  
ATOM   4730  OE1 GLU B 509     -39.631 -92.207  30.830  1.00 83.36           O  
ANISOU 4730  OE1 GLU B 509     8168  11449  12055   -748    520   -613       O  
ATOM   4731  OE2 GLU B 509     -40.028 -90.098  31.293  1.00 82.87           O1-
ANISOU 4731  OE2 GLU B 509     7965  11598  11922   -583    694   -783       O1-
ATOM   4732  N   ARG B 510     -35.258 -94.573  33.051  1.00 77.20           N  
ANISOU 4732  N   ARG B 510     7779  10159  11394   -961    245   -216       N  
ATOM   4733  CA  ARG B 510     -35.001 -96.001  33.287  1.00 78.48           C  
ANISOU 4733  CA  ARG B 510     7980  10081  11759  -1103    -21    -79       C  
ATOM   4734  C   ARG B 510     -33.727 -96.250  34.072  1.00 77.94           C  
ANISOU 4734  C   ARG B 510     7991   9881  11740  -1129   -117     22       C  
ATOM   4735  O   ARG B 510     -33.700 -97.158  34.904  1.00 79.79           O  
ANISOU 4735  O   ARG B 510     8241  10005  12069  -1358   -328    259       O  
ATOM   4736  CB  ARG B 510     -35.002 -96.816  31.983  1.00 79.45           C  
ANISOU 4736  CB  ARG B 510     8111   9971  12105   -969   -194   -256       C  
ATOM   4737  CG  ARG B 510     -35.211 -98.343  32.160  1.00 82.46           C  
ANISOU 4737  CG  ARG B 510     8492  10076  12763  -1139   -528   -124       C  
ATOM   4738  CD  ARG B 510     -35.735 -99.007  30.858  1.00 84.37           C  
ANISOU 4738  CD  ARG B 510     8694  10174  13188  -1032   -663   -337       C  
ATOM   4739  NE  ARG B 510     -35.710-100.477  30.897  1.00 87.88           N  
ANISOU 4739  NE  ARG B 510     9138  10270  13982  -1141  -1042   -274       N  
ATOM   4740  CZ  ARG B 510     -34.847-101.255  30.234  1.00 89.84           C  
ANISOU 4740  CZ  ARG B 510     9385  10222  14526   -967  -1277   -517       C  
ATOM   4741  NH1 ARG B 510     -33.914-100.734  29.450  1.00 89.40           N1+
ANISOU 4741  NH1 ARG B 510     9318  10236  14411   -698  -1138   -841       N1+
ATOM   4742  NH2 ARG B 510     -34.913-102.572  30.354  1.00 93.07           N  
ANISOU 4742  NH2 ARG B 510     9782  10270  15308  -1075  -1674   -451       N  
ATOM   4743  N   LEU B 511     -32.683 -95.462  33.800  1.00 75.34           N  
ANISOU 4743  N   LEU B 511     7708   9562  11355   -921      7   -132       N  
ATOM   4744  CA  LEU B 511     -31.444 -95.521  34.579  1.00 74.69           C  
ANISOU 4744  CA  LEU B 511     7687   9388  11301   -929    -57    -54       C  
ATOM   4745  C   LEU B 511     -31.788 -95.297  36.044  1.00 75.31           C  
ANISOU 4745  C   LEU B 511     7754   9664  11193  -1189     -7    206       C  
ATOM   4746  O   LEU B 511     -31.303 -96.015  36.930  1.00 76.78           O  
ANISOU 4746  O   LEU B 511     7981   9739  11450  -1369   -207    424       O  
ATOM   4747  CB  LEU B 511     -30.420 -94.473  34.109  1.00 72.47           C  
ANISOU 4747  CB  LEU B 511     7434   9170  10928   -697    121   -252       C  
ATOM   4748  CG  LEU B 511     -29.816 -94.585  32.689  1.00 73.13           C  
ANISOU 4748  CG  LEU B 511     7506   9162  11118   -472    101   -531       C  
ATOM   4749  CD1 LEU B 511     -29.020 -93.363  32.281  1.00 71.04           C  
ANISOU 4749  CD1 LEU B 511     7255   9052  10684   -327    304   -659       C  
ATOM   4750  CD2 LEU B 511     -28.943 -95.820  32.476  1.00 75.19           C  
ANISOU 4750  CD2 LEU B 511     7752   9144  11673   -415   -165   -635       C  
ATOM   4751  N   ARG B 512     -32.671 -94.322  36.278  1.00 74.37           N  
ANISOU 4751  N   ARG B 512     7559   9854  10843  -1222    234    169       N  
ATOM   4752  CA  ARG B 512     -33.049 -93.882  37.615  1.00 74.81           C  
ANISOU 4752  CA  ARG B 512     7549  10214  10658  -1450    348    312       C  
ATOM   4753  C   ARG B 512     -33.915 -94.886  38.350  1.00 77.44           C  
ANISOU 4753  C   ARG B 512     7822  10643  10956  -1810    201    578       C  
ATOM   4754  O   ARG B 512     -33.792 -95.018  39.565  1.00 78.93           O  
ANISOU 4754  O   ARG B 512     7994  11019  10976  -2082    174    790       O  
ATOM   4755  CB  ARG B 512     -33.771 -92.563  37.528  1.00 73.53           C  
ANISOU 4755  CB  ARG B 512     7277  10335  10325  -1340    618    107       C  
ATOM   4756  CG  ARG B 512     -32.910 -91.450  37.054  1.00 72.75           C  
ANISOU 4756  CG  ARG B 512     7235  10174  10230  -1064    737    -82       C  
ATOM   4757  CD  ARG B 512     -32.773 -90.391  38.108  1.00 75.46           C  
ANISOU 4757  CD  ARG B 512     7513  10773  10382  -1097    902   -138       C  
ATOM   4758  NE  ARG B 512     -34.000 -89.613  38.234  1.00 77.76           N  
ANISOU 4758  NE  ARG B 512     7630  11329  10585  -1096   1048   -302       N  
ATOM   4759  CZ  ARG B 512     -34.415 -89.072  39.368  1.00 79.84           C  
ANISOU 4759  CZ  ARG B 512     7745  11929  10660  -1230   1175   -373       C  
ATOM   4760  NH1 ARG B 512     -33.696 -89.235  40.479  1.00 81.73           N1+
ANISOU 4760  NH1 ARG B 512     8016  12292  10744  -1402   1175   -247       N1+
ATOM   4761  NH2 ARG B 512     -35.547 -88.386  39.388  1.00 80.65           N  
ANISOU 4761  NH2 ARG B 512     7648  12263  10732  -1194   1289   -592       N  
ATOM   4762  N   LYS B 513     -34.787 -95.572  37.606  1.00 78.08           N  
ANISOU 4762  N   LYS B 513     7867  10622  11178  -1837     99    577       N  
ATOM   4763  CA  LYS B 513     -35.596 -96.690  38.106  1.00 81.00           C  
ANISOU 4763  CA  LYS B 513     8188  11015  11572  -2196   -103    858       C  
ATOM   4764  C   LYS B 513     -34.755 -97.905  38.547  1.00 83.23           C  
ANISOU 4764  C   LYS B 513     8590  10961  12069  -2370   -477   1144       C  
ATOM   4765  O   LYS B 513     -35.181 -98.691  39.406  1.00 86.49           O  
ANISOU 4765  O   LYS B 513     8981  11447  12435  -2768   -672   1486       O  
ATOM   4766  CB  LYS B 513     -36.584 -97.117  37.021  1.00 80.94           C  
ANISOU 4766  CB  LYS B 513     8126  10902  11722  -2126   -152    748       C  
ATOM   4767  CG  LYS B 513     -37.558 -98.218  37.400  1.00 84.18           C  
ANISOU 4767  CG  LYS B 513     8469  11340  12172  -2501   -359   1025       C  
ATOM   4768  CD  LYS B 513     -37.888 -99.036  36.162  1.00 85.51           C  
ANISOU 4768  CD  LYS B 513     8669  11161  12660  -2365   -565    925       C  
ATOM   4769  CE  LYS B 513     -39.237 -99.779  36.225  1.00 88.83           C  
ANISOU 4769  CE  LYS B 513     8974  11682  13093  -2675   -678   1100       C  
ATOM   4770  NZ  LYS B 513     -39.510-100.491  34.925  1.00 87.44           N1+
ANISOU 4770  NZ  LYS B 513     8828  11157  13238  -2495   -872    941       N1+
ATOM   4771  N   HIS B 514     -33.571 -98.062  37.955  1.00 82.01           N  
ANISOU 4771  N   HIS B 514     8546  10450  12161  -2091   -603   1004       N  
ATOM   4772  CA  HIS B 514     -32.707 -99.203  38.251  1.00 84.10           C  
ANISOU 4772  CA  HIS B 514     8902  10325  12726  -2186  -1009   1204       C  
ATOM   4773  C   HIS B 514     -31.500 -98.891  39.123  1.00 83.91           C  
ANISOU 4773  C   HIS B 514     8949  10294  12638  -2194  -1037   1301       C  
ATOM   4774  O   HIS B 514     -30.736 -99.787  39.505  1.00 86.38           O  
ANISOU 4774  O   HIS B 514     9329  10279  13210  -2286  -1408   1490       O  
ATOM   4775  CB  HIS B 514     -32.320 -99.917  36.966  1.00 84.00           C  
ANISOU 4775  CB  HIS B 514     8911   9888  13115  -1898  -1221    948       C  
ATOM   4776  CG  HIS B 514     -33.422-100.763  36.443  1.00 87.27           C  
ANISOU 4776  CG  HIS B 514     9276  10192  13688  -2024  -1392    998       C  
ATOM   4777  ND1 HIS B 514     -34.480-100.237  35.734  1.00 87.86           N  
ANISOU 4777  ND1 HIS B 514     9274  10503  13603  -1950  -1132    827       N  
ATOM   4778  CD2 HIS B 514     -33.693-102.078  36.612  1.00 91.63           C  
ANISOU 4778  CD2 HIS B 514     9841  10427  14547  -2254  -1821   1235       C  
ATOM   4779  CE1 HIS B 514     -35.338-101.201  35.454  1.00 89.41           C  
ANISOU 4779  CE1 HIS B 514     9435  10549  13987  -2116  -1367    934       C  
ATOM   4780  NE2 HIS B 514     -34.885-102.327  35.975  1.00 92.94           N  
ANISOU 4780  NE2 HIS B 514     9936  10653  14722  -2308  -1790   1185       N  
ATOM   4781  N   GLY B 515     -31.340 -97.619  39.452  1.00 81.47           N  
ANISOU 4781  N   GLY B 515     8616  10325  12012  -2100   -679   1170       N  
ATOM   4782  CA  GLY B 515     -30.383 -97.233  40.465  1.00 80.90           C  
ANISOU 4782  CA  GLY B 515     8594  10338  11806  -2173   -674   1291       C  
ATOM   4783  C   GLY B 515     -29.068 -96.940  39.832  1.00 78.47           C  
ANISOU 4783  C   GLY B 515     8348   9771  11696  -1813   -678   1040       C  
ATOM   4784  O   GLY B 515     -28.051 -96.917  40.513  1.00 79.23           O  
ANISOU 4784  O   GLY B 515     8497   9797  11807  -1837   -782   1137       O  
ATOM   4785  N   LEU B 516     -29.104 -96.718  38.521  1.00 76.18           N  
ANISOU 4785  N   LEU B 516     8035   9374  11536  -1503   -568    719       N  
ATOM   4786  CA  LEU B 516     -27.923 -96.392  37.747  1.00 74.20           C  
ANISOU 4786  CA  LEU B 516     7802   8960  11428  -1177   -532    436       C  
ATOM   4787  C   LEU B 516     -27.771 -94.905  37.807  1.00 72.03           C  
ANISOU 4787  C   LEU B 516     7521   8988  10857  -1059   -170    301       C  
ATOM   4788  O   LEU B 516     -28.721 -94.183  37.537  1.00 71.49           O  
ANISOU 4788  O   LEU B 516     7408   9148  10605  -1051     53    231       O  
ATOM   4789  CB  LEU B 516     -28.083 -96.846  36.300  1.00 73.83           C  
ANISOU 4789  CB  LEU B 516     7713   8736  11603   -955   -583    155       C  
ATOM   4790  CG  LEU B 516     -28.074 -98.346  35.986  1.00 75.10           C  
ANISOU 4790  CG  LEU B 516     7857   8516  12161   -987   -988    171       C  
ATOM   4791  CD1 LEU B 516     -28.405 -98.518  34.540  1.00 73.97           C  
ANISOU 4791  CD1 LEU B 516     7647   8327  12129   -771   -945   -162       C  
ATOM   4792  CD2 LEU B 516     -26.734 -99.017  36.299  1.00 75.34           C  
ANISOU 4792  CD2 LEU B 516     7893   8227  12503   -911  -1295    147       C  
ATOM   4793  N   GLU B 517     -26.584 -94.442  38.180  1.00 71.60           N  
ANISOU 4793  N   GLU B 517     7502   8916  10787   -970   -144    264       N  
ATOM   4794  CA  GLU B 517     -26.410 -93.059  38.581  1.00 70.18           C  
ANISOU 4794  CA  GLU B 517     7321   9004  10338   -925    139    203       C  
ATOM   4795  C   GLU B 517     -26.062 -92.161  37.400  1.00 68.95           C  
ANISOU 4795  C   GLU B 517     7150   8874  10171   -658    328    -72       C  
ATOM   4796  O   GLU B 517     -25.271 -92.523  36.527  1.00 69.10           O  
ANISOU 4796  O   GLU B 517     7161   8733  10358   -496    250   -234       O  
ATOM   4797  CB  GLU B 517     -25.383 -93.001  39.687  1.00 70.35           C  
ANISOU 4797  CB  GLU B 517     7387   9016  10324  -1013     56    341       C  
ATOM   4798  CG  GLU B 517     -24.981 -91.634  40.147  1.00 70.70           C  
ANISOU 4798  CG  GLU B 517     7431   9290  10141   -953    302    255       C  
ATOM   4799  CD  GLU B 517     -23.984 -91.683  41.313  1.00 74.76           C  
ANISOU 4799  CD  GLU B 517     7988   9803  10614  -1069    192    408       C  
ATOM   4800  OE1 GLU B 517     -23.569 -92.807  41.721  1.00 77.66           O  
ANISOU 4800  OE1 GLU B 517     8389   9963  11152  -1193   -103    601       O  
ATOM   4801  OE2 GLU B 517     -23.636 -90.596  41.837  1.00 73.51           O1-
ANISOU 4801  OE2 GLU B 517     7826   9834  10271  -1043    369    341       O1-
ATOM   4802  N   VAL B 518     -26.679 -90.986  37.358  1.00 68.82           N  
ANISOU 4802  N   VAL B 518     7109   9078   9958   -629    556   -137       N  
ATOM   4803  CA  VAL B 518     -26.491 -90.073  36.232  1.00 68.10           C  
ANISOU 4803  CA  VAL B 518     7011   9018   9843   -436    693   -329       C  
ATOM   4804  C   VAL B 518     -25.878 -88.757  36.682  1.00 67.71           C  
ANISOU 4804  C   VAL B 518     6977   9081   9667   -386    833   -364       C  
ATOM   4805  O   VAL B 518     -26.419 -88.097  37.564  1.00 67.67           O  
ANISOU 4805  O   VAL B 518     6943   9225   9541   -461    920   -330       O  
ATOM   4806  CB  VAL B 518     -27.830 -89.731  35.529  1.00 67.80           C  
ANISOU 4806  CB  VAL B 518     6927   9074   9760   -420    772   -386       C  
ATOM   4807  CG1 VAL B 518     -27.574 -88.834  34.325  1.00 67.58           C  
ANISOU 4807  CG1 VAL B 518     6905   9068   9704   -268    852   -525       C  
ATOM   4808  CG2 VAL B 518     -28.570 -90.971  35.105  1.00 68.27           C  
ANISOU 4808  CG2 VAL B 518     6964   9034   9940   -484    634   -353       C  
ATOM   4809  N   ILE B 519     -24.771 -88.359  36.060  1.00 68.00           N  
ANISOU 4809  N   ILE B 519     7036   9069   9731   -268    852   -457       N  
ATOM   4810  CA  ILE B 519     -24.224 -87.032  36.321  1.00 68.15           C  
ANISOU 4810  CA  ILE B 519     7069   9169   9654   -226    962   -484       C  
ATOM   4811  C   ILE B 519     -25.060 -85.977  35.622  1.00 68.44           C  
ANISOU 4811  C   ILE B 519     7086   9274   9642   -176   1038   -538       C  
ATOM   4812  O   ILE B 519     -25.294 -86.057  34.416  1.00 68.80           O  
ANISOU 4812  O   ILE B 519     7126   9309   9703   -132   1022   -582       O  
ATOM   4813  CB  ILE B 519     -22.791 -86.895  35.864  1.00 67.77           C  
ANISOU 4813  CB  ILE B 519     7032   9080   9637   -153    952   -547       C  
ATOM   4814  CG1 ILE B 519     -21.887 -87.837  36.647  1.00 68.32           C  
ANISOU 4814  CG1 ILE B 519     7106   9047   9804   -182    835   -507       C  
ATOM   4815  CG2 ILE B 519     -22.326 -85.474  36.085  1.00 68.10           C  
ANISOU 4815  CG2 ILE B 519     7091   9188   9593   -136   1040   -549       C  
ATOM   4816  CD1 ILE B 519     -20.635 -88.143  35.916  1.00 68.36           C  
ANISOU 4816  CD1 ILE B 519     7063   9008   9899    -89    793   -645       C  
ATOM   4817  N   TYR B 520     -25.515 -85.003  36.403  1.00 69.19           N  
ANISOU 4817  N   TYR B 520     7156   9443   9690   -188   1096   -551       N  
ATOM   4818  CA  TYR B 520     -26.317 -83.906  35.918  1.00 69.89           C  
ANISOU 4818  CA  TYR B 520     7206   9547   9801   -127   1109   -616       C  
ATOM   4819  C   TYR B 520     -25.386 -82.749  35.593  1.00 70.57           C  
ANISOU 4819  C   TYR B 520     7334   9577   9903    -77   1092   -617       C  
ATOM   4820  O   TYR B 520     -25.041 -81.987  36.480  1.00 71.50           O  
ANISOU 4820  O   TYR B 520     7439   9703  10024    -69   1109   -657       O  
ATOM   4821  CB  TYR B 520     -27.260 -83.445  37.032  1.00 70.15           C  
ANISOU 4821  CB  TYR B 520     7141   9697   9815   -154   1157   -701       C  
ATOM   4822  CG  TYR B 520     -28.375 -84.383  37.399  1.00 71.21           C  
ANISOU 4822  CG  TYR B 520     7201   9948   9908   -250   1177   -690       C  
ATOM   4823  CD1 TYR B 520     -28.927 -85.256  36.469  1.00 71.97           C  
ANISOU 4823  CD1 TYR B 520     7313   9983  10050   -258   1127   -636       C  
ATOM   4824  CD2 TYR B 520     -28.916 -84.376  38.678  1.00 72.90           C  
ANISOU 4824  CD2 TYR B 520     7309  10371  10019   -358   1244   -744       C  
ATOM   4825  CE1 TYR B 520     -29.959 -86.095  36.810  1.00 71.14           C  
ANISOU 4825  CE1 TYR B 520     7134   9977   9918   -371   1128   -607       C  
ATOM   4826  CE2 TYR B 520     -29.957 -85.213  39.018  1.00 72.53           C  
ANISOU 4826  CE2 TYR B 520     7174  10477   9905   -498   1261   -710       C  
ATOM   4827  CZ  TYR B 520     -30.460 -86.059  38.080  1.00 73.07           C  
ANISOU 4827  CZ  TYR B 520     7275  10438  10050   -501   1195   -629       C  
ATOM   4828  OH  TYR B 520     -31.480 -86.895  38.416  1.00 79.91           O  
ANISOU 4828  OH  TYR B 520     8053  11447  10861   -663   1194   -573       O  
ATOM   4829  N   MET B 521     -24.967 -82.593  34.346  1.00 71.58           N  
ANISOU 4829  N   MET B 521     7499   9672  10023    -70   1050   -573       N  
ATOM   4830  CA  MET B 521     -24.114 -81.450  33.989  1.00 72.45           C  
ANISOU 4830  CA  MET B 521     7644   9750  10133    -80   1009   -526       C  
ATOM   4831  C   MET B 521     -24.968 -80.250  33.556  1.00 74.64           C  
ANISOU 4831  C   MET B 521     7906   9944  10509    -59    893   -506       C  
ATOM   4832  O   MET B 521     -25.610 -80.257  32.497  1.00 75.52           O  
ANISOU 4832  O   MET B 521     8018  10054  10619    -79    820   -453       O  
ATOM   4833  CB  MET B 521     -23.100 -81.837  32.928  1.00 71.61           C  
ANISOU 4833  CB  MET B 521     7557   9721   9929   -137   1017   -484       C  
ATOM   4834  CG  MET B 521     -22.227 -82.943  33.384  1.00 70.19           C  
ANISOU 4834  CG  MET B 521     7362   9573   9732   -124   1078   -549       C  
ATOM   4835  SD  MET B 521     -21.023 -83.421  32.140  1.00 69.54           S  
ANISOU 4835  SD  MET B 521     7227   9644   9549   -169   1099   -615       S  
ATOM   4836  CE  MET B 521     -20.113 -84.707  33.007  1.00 67.13           C  
ANISOU 4836  CE  MET B 521     6879   9279   9346   -101   1099   -731       C  
ATOM   4837  N   ILE B 522     -24.959 -79.205  34.376  1.00 76.36           N  
ANISOU 4837  N   ILE B 522     8100  10078  10835    -16    844   -561       N  
ATOM   4838  CA  ILE B 522     -25.952 -78.148  34.237  1.00 78.51           C  
ANISOU 4838  CA  ILE B 522     8316  10223  11289     46    691   -613       C  
ATOM   4839  C   ILE B 522     -25.390 -76.748  33.988  1.00 80.69           C  
ANISOU 4839  C   ILE B 522     8625  10327  11704     26    502   -532       C  
ATOM   4840  O   ILE B 522     -26.084 -75.763  34.188  1.00 82.59           O  
ANISOU 4840  O   ILE B 522     8798  10406  12174    107    332   -626       O  
ATOM   4841  CB  ILE B 522     -26.960 -78.168  35.424  1.00 78.83           C  
ANISOU 4841  CB  ILE B 522     8226  10316  11407    139    751   -843       C  
ATOM   4842  CG1 ILE B 522     -26.240 -78.328  36.766  1.00 77.79           C  
ANISOU 4842  CG1 ILE B 522     8079  10292  11183    124    879   -934       C  
ATOM   4843  CG2 ILE B 522     -27.912 -79.318  35.254  1.00 78.02           C  
ANISOU 4843  CG2 ILE B 522     8081  10339  11224    123    842   -862       C  
ATOM   4844  CD1 ILE B 522     -26.941 -77.683  37.925  1.00 78.33           C  
ANISOU 4844  CD1 ILE B 522     7993  10429  11339    196    887  -1199       C  
ATOM   4845  N   GLU B 523     -24.139 -76.664  33.543  1.00 82.01           N  
ANISOU 4845  N   GLU B 523     8877  10527  11756    -88    509   -371       N  
ATOM   4846  CA  GLU B 523     -23.532 -75.391  33.121  1.00 84.89           C  
ANISOU 4846  CA  GLU B 523     9284  10741  12227   -176    300   -217       C  
ATOM   4847  C   GLU B 523     -23.053 -75.534  31.676  1.00 86.27           C  
ANISOU 4847  C   GLU B 523     9522  11035  12221   -371    252     31       C  
ATOM   4848  O   GLU B 523     -22.640 -76.630  31.276  1.00 85.41           O  
ANISOU 4848  O   GLU B 523     9413  11151  11887   -416    437     19       O  
ATOM   4849  CB  GLU B 523     -22.347 -75.005  33.998  1.00 84.36           C  
ANISOU 4849  CB  GLU B 523     9232  10663  12156   -190    350   -249       C  
ATOM   4850  CG  GLU B 523     -22.328 -75.565  35.389  1.00 86.51           C  
ANISOU 4850  CG  GLU B 523     9454  11013  12401    -73    531   -473       C  
ATOM   4851  CD  GLU B 523     -21.355 -74.812  36.287  1.00 92.88           C  
ANISOU 4851  CD  GLU B 523    10265  11754  13271    -75    502   -521       C  
ATOM   4852  OE1 GLU B 523     -20.119 -75.147  36.309  1.00 94.50           O  
ANISOU 4852  OE1 GLU B 523    10516  12055  13334   -161    592   -429       O  
ATOM   4853  OE2 GLU B 523     -21.837 -73.861  36.960  1.00 95.92           O1-
ANISOU 4853  OE2 GLU B 523    10585  11991  13869     19    372   -684       O1-
ATOM   4854  N   PRO B 524     -23.085 -74.434  30.884  1.00 89.28           N  
ANISOU 4854  N   PRO B 524     9940  11281  12700   -505    -20    250       N  
ATOM   4855  CA  PRO B 524     -22.782 -74.637  29.466  1.00 90.69           C  
ANISOU 4855  CA  PRO B 524    10157  11663  12638   -738    -59    489       C  
ATOM   4856  C   PRO B 524     -21.345 -75.082  29.186  1.00 90.69           C  
ANISOU 4856  C   PRO B 524    10153  11952  12352   -901    124    540       C  
ATOM   4857  O   PRO B 524     -21.131 -75.842  28.240  1.00 91.04           O  
ANISOU 4857  O   PRO B 524    10170  12290  12131  -1023    235    564       O  
ATOM   4858  CB  PRO B 524     -23.122 -73.281  28.822  1.00 93.47           C  
ANISOU 4858  CB  PRO B 524    10552  11783  13179   -883   -448    757       C  
ATOM   4859  CG  PRO B 524     -24.062 -72.628  29.791  1.00 93.48           C  
ANISOU 4859  CG  PRO B 524    10506  11432  13578   -636   -606    561       C  
ATOM   4860  CD  PRO B 524     -23.521 -73.046  31.138  1.00 91.40           C  
ANISOU 4860  CD  PRO B 524    10201  11219  13304   -468   -340    287       C  
ATOM   4861  N   ILE B 525     -20.384 -74.659  30.007  1.00 90.66           N  
ANISOU 4861  N   ILE B 525    10151  11890  12405   -892    158    512       N  
ATOM   4862  CA  ILE B 525     -18.996 -75.124  29.844  1.00 91.44           C  
ANISOU 4862  CA  ILE B 525    10211  12271  12262  -1020    340    509       C  
ATOM   4863  C   ILE B 525     -18.917 -76.655  29.814  1.00 90.38           C  
ANISOU 4863  C   ILE B 525    10010  12363  11964   -907    604    278       C  
ATOM   4864  O   ILE B 525     -18.049 -77.233  29.158  1.00 90.89           O  
ANISOU 4864  O   ILE B 525     9999  12731  11802  -1027    729    242       O  
ATOM   4865  CB  ILE B 525     -18.035 -74.591  30.939  1.00 91.02           C  
ANISOU 4865  CB  ILE B 525    10159  12099  12323   -979    355    463       C  
ATOM   4866  CG1 ILE B 525     -18.495 -73.226  31.463  1.00 94.13           C  
ANISOU 4866  CG1 ILE B 525    10606  12133  13023   -948     78    549       C  
ATOM   4867  CG2 ILE B 525     -16.602 -74.442  30.376  1.00 90.74           C  
ANISOU 4867  CG2 ILE B 525    10077  12332  12067  -1226    406    590       C  
ATOM   4868  CD1 ILE B 525     -19.736 -73.202  32.394  1.00 94.00           C  
ANISOU 4868  CD1 ILE B 525    10578  11871  13265   -676     44    323       C  
ATOM   4869  N   ASP B 526     -19.842 -77.304  30.512  1.00 89.68           N  
ANISOU 4869  N   ASP B 526     9929  12135  12008   -689    665    109       N  
ATOM   4870  CA  ASP B 526     -19.883 -78.754  30.576  1.00 89.36           C  
ANISOU 4870  CA  ASP B 526     9838  12228  11887   -582    845    -85       C  
ATOM   4871  C   ASP B 526     -19.947 -79.385  29.195  1.00 90.98           C  
ANISOU 4871  C   ASP B 526     9989  12690  11887   -696    877    -89       C  
ATOM   4872  O   ASP B 526     -19.285 -80.385  28.931  1.00 90.95           O  
ANISOU 4872  O   ASP B 526     9898  12883  11774   -684   1007   -257       O  
ATOM   4873  CB  ASP B 526     -21.047 -79.213  31.448  1.00 87.82           C  
ANISOU 4873  CB  ASP B 526     9659  11856  11850   -398    860   -199       C  
ATOM   4874  CG  ASP B 526     -20.778 -78.992  32.922  1.00 87.97           C  
ANISOU 4874  CG  ASP B 526     9688  11745  11991   -297    894   -277       C  
ATOM   4875  OD1 ASP B 526     -19.676 -79.358  33.411  1.00 87.47           O  
ANISOU 4875  OD1 ASP B 526     9610  11743  11881   -301    975   -322       O  
ATOM   4876  OD2 ASP B 526     -21.674 -78.456  33.600  1.00 89.31           O1-
ANISOU 4876  OD2 ASP B 526     9859  11774  12299   -216    833   -319       O1-
ATOM   4877  N   GLU B 527     -20.730 -78.781  28.313  1.00 93.12           N  
ANISOU 4877  N   GLU B 527    10296  12962  12121   -809    734     76       N  
ATOM   4878  CA  GLU B 527     -20.852 -79.261  26.959  1.00 95.54           C  
ANISOU 4878  CA  GLU B 527    10550  13554  12194   -955    747     86       C  
ATOM   4879  C   GLU B 527     -19.472 -79.353  26.308  1.00 97.48           C  
ANISOU 4879  C   GLU B 527    10695  14166  12177  -1150    847     61       C  
ATOM   4880  O   GLU B 527     -19.136 -80.349  25.675  1.00 98.25           O  
ANISOU 4880  O   GLU B 527    10672  14552  12104  -1161    979   -152       O  
ATOM   4881  CB  GLU B 527     -21.766 -78.329  26.173  1.00 97.34           C  
ANISOU 4881  CB  GLU B 527    10846  13712  12427  -1097    516    345       C  
ATOM   4882  CG  GLU B 527     -22.398 -78.979  24.965  1.00100.40           C  
ANISOU 4882  CG  GLU B 527    11194  14334  12618  -1188    513    325       C  
ATOM   4883  CD  GLU B 527     -23.292 -80.126  25.353  1.00100.79           C  
ANISOU 4883  CD  GLU B 527    11223  14275  12795   -944    615     82       C  
ATOM   4884  OE1 GLU B 527     -24.354 -79.849  25.940  1.00102.82           O  
ANISOU 4884  OE1 GLU B 527    11533  14244  13288   -803    519    110       O  
ATOM   4885  OE2 GLU B 527     -22.936 -81.297  25.094  1.00101.23           O1-
ANISOU 4885  OE2 GLU B 527    11193  14532  12737   -898    773   -151       O1-
ATOM   4886  N   TYR B 528     -18.669 -78.313  26.498  1.00 99.12           N  
ANISOU 4886  N   TYR B 528    10925  14364  12370  -1301    777    247       N  
ATOM   4887  CA  TYR B 528     -17.311 -78.253  25.963  1.00101.78           C  
ANISOU 4887  CA  TYR B 528    11142  15077  12451  -1520    872    238       C  
ATOM   4888  C   TYR B 528     -16.327 -79.111  26.759  1.00 99.63           C  
ANISOU 4888  C   TYR B 528    10765  14844  12243  -1338   1065    -64       C  
ATOM   4889  O   TYR B 528     -15.304 -79.546  26.260  1.00101.26           O  
ANISOU 4889  O   TYR B 528    10806  15413  12255  -1441   1193   -229       O  
ATOM   4890  CB  TYR B 528     -16.852 -76.783  25.860  1.00104.42           C  
ANISOU 4890  CB  TYR B 528    11542  15366  12766  -1785    684    592       C  
ATOM   4891  CG  TYR B 528     -17.551 -76.047  24.707  1.00111.21           C  
ANISOU 4891  CG  TYR B 528    12460  16311  13484  -2069    455    920       C  
ATOM   4892  CD1 TYR B 528     -18.763 -75.336  24.906  1.00113.56           C  
ANISOU 4892  CD1 TYR B 528    12899  16190  14055  -1987    194   1111       C  
ATOM   4893  CD2 TYR B 528     -17.027 -76.100  23.396  1.00117.11           C  
ANISOU 4893  CD2 TYR B 528    13094  17586  13814  -2430    486   1019       C  
ATOM   4894  CE1 TYR B 528     -19.418 -74.682  23.828  1.00117.42           C  
ANISOU 4894  CE1 TYR B 528    13442  16724  14446  -2253    -71   1436       C  
ATOM   4895  CE2 TYR B 528     -17.675 -75.452  22.319  1.00121.11           C  
ANISOU 4895  CE2 TYR B 528    13660  18195  14158  -2737    244   1365       C  
ATOM   4896  CZ  TYR B 528     -18.859 -74.746  22.540  1.00121.33           C  
ANISOU 4896  CZ  TYR B 528    13853  17743  14502  -2643    -52   1591       C  
ATOM   4897  OH  TYR B 528     -19.460 -74.114  21.466  1.00125.17           O  
ANISOU 4897  OH  TYR B 528    14396  18309  14852  -2958   -340   1956       O  
ATOM   4898  N   CYS B 529     -16.657 -79.366  28.004  1.00 96.53           N  
ANISOU 4898  N   CYS B 529    10453  14096  12127  -1078   1069   -148       N  
ATOM   4899  CA  CYS B 529     -15.799 -80.152  28.833  1.00 94.83           C  
ANISOU 4899  CA  CYS B 529    10160  13863  12006   -917   1189   -382       C  
ATOM   4900  C   CYS B 529     -15.912 -81.640  28.486  1.00 93.89           C  
ANISOU 4900  C   CYS B 529     9926  13862  11885   -779   1280   -685       C  
ATOM   4901  O   CYS B 529     -14.907 -82.293  28.259  1.00 94.78           O  
ANISOU 4901  O   CYS B 529     9872  14195  11945   -770   1366   -920       O  
ATOM   4902  CB  CYS B 529     -16.139 -79.890  30.293  1.00 93.05           C  
ANISOU 4902  CB  CYS B 529    10057  13261  12036   -738   1139   -340       C  
ATOM   4903  SG  CYS B 529     -15.039 -80.716  31.405  1.00 93.84           S  
ANISOU 4903  SG  CYS B 529    10085  13313  12255   -585   1223   -547       S  
ATOM   4904  N   VAL B 530     -17.128 -82.179  28.443  1.00 92.18           N  
ANISOU 4904  N   VAL B 530     9777  13491  11754   -668   1240   -703       N  
ATOM   4905  CA  VAL B 530     -17.306 -83.601  28.129  1.00 91.48           C  
ANISOU 4905  CA  VAL B 530     9585  13458  11713   -537   1279   -985       C  
ATOM   4906  C   VAL B 530     -16.780 -83.947  26.756  1.00 93.30           C  
ANISOU 4906  C   VAL B 530     9632  14116  11700   -670   1348  -1179       C  
ATOM   4907  O   VAL B 530     -16.556 -85.115  26.470  1.00 93.86           O  
ANISOU 4907  O   VAL B 530     9556  14275  11830   -554   1376  -1505       O  
ATOM   4908  CB  VAL B 530     -18.784 -84.112  28.199  1.00 90.34           C  
ANISOU 4908  CB  VAL B 530     9535  13103  11685   -433   1215   -954       C  
ATOM   4909  CG1 VAL B 530     -19.213 -84.330  29.613  1.00 87.74           C  
ANISOU 4909  CG1 VAL B 530     9307  12439  11589   -287   1175   -896       C  
ATOM   4910  CG2 VAL B 530     -19.741 -83.201  27.441  1.00 90.97           C  
ANISOU 4910  CG2 VAL B 530     9699  13230  11635   -571   1151   -731       C  
ATOM   4911  N   GLN B 531     -16.603 -82.937  25.910  1.00 94.29           N  
ANISOU 4911  N   GLN B 531     9753  14517  11556   -928   1352   -988       N  
ATOM   4912  CA  GLN B 531     -16.018 -83.147  24.584  1.00 97.23           C  
ANISOU 4912  CA  GLN B 531     9922  15414  11607  -1129   1436  -1162       C  
ATOM   4913  C   GLN B 531     -14.652 -83.829  24.621  1.00 97.75           C  
ANISOU 4913  C   GLN B 531     9741  15733  11665  -1073   1557  -1535       C  
ATOM   4914  O   GLN B 531     -14.258 -84.483  23.659  1.00100.09           O  
ANISOU 4914  O   GLN B 531     9803  16450  11775  -1132   1642  -1866       O  
ATOM   4915  CB  GLN B 531     -15.892 -81.835  23.826  1.00 99.34           C  
ANISOU 4915  CB  GLN B 531    10229  15941  11572  -1485   1387   -813       C  
ATOM   4916  CG  GLN B 531     -17.182 -81.380  23.196  1.00102.46           C  
ANISOU 4916  CG  GLN B 531    10770  16263  11895  -1595   1246   -545       C  
ATOM   4917  CD  GLN B 531     -16.972 -80.377  22.069  1.00109.25           C  
ANISOU 4917  CD  GLN B 531    11610  17513  12386  -2017   1165   -242       C  
ATOM   4918  OE1 GLN B 531     -17.815 -80.262  21.167  1.00112.84           O  
ANISOU 4918  OE1 GLN B 531    12104  18094  12676  -2169   1064   -102       O  
ATOM   4919  NE2 GLN B 531     -15.851 -79.646  22.109  1.00111.55           N  
ANISOU 4919  NE2 GLN B 531    11838  18006  12539  -2237   1187   -113       N  
ATOM   4920  N   GLN B 532     -13.941 -83.671  25.735  1.00 95.60           N  
ANISOU 4920  N   GLN B 532     9501  15218  11603   -956   1553  -1511       N  
ATOM   4921  CA  GLN B 532     -12.588 -84.184  25.864  1.00 96.14           C  
ANISOU 4921  CA  GLN B 532     9331  15490  11705   -900   1635  -1841       C  
ATOM   4922  C   GLN B 532     -12.425 -85.141  27.043  1.00 93.76           C  
ANISOU 4922  C   GLN B 532     9044  14771  11808   -579   1559  -2026       C  
ATOM   4923  O   GLN B 532     -11.487 -85.945  27.075  1.00 95.53           O  
ANISOU 4923  O   GLN B 532     9039  15100  12157   -457   1572  -2397       O  
ATOM   4924  CB  GLN B 532     -11.589 -83.025  25.934  1.00 97.03           C  
ANISOU 4924  CB  GLN B 532     9416  15809  11639  -1137   1683  -1634       C  
ATOM   4925  CG  GLN B 532     -11.480 -82.233  24.641  1.00100.59           C  
ANISOU 4925  CG  GLN B 532     9785  16778  11655  -1524   1735  -1478       C  
ATOM   4926  CD  GLN B 532     -10.943 -83.071  23.484  1.00105.65           C  
ANISOU 4926  CD  GLN B 532    10088  18013  12039  -1606   1875  -1928       C  
ATOM   4927  OE1 GLN B 532     -11.596 -83.216  22.441  1.00107.35           O  
ANISOU 4927  OE1 GLN B 532    10267  18515  12003  -1750   1887  -1949       O  
ATOM   4928  NE2 GLN B 532      -9.754 -83.643  23.672  1.00108.11           N  
ANISOU 4928  NE2 GLN B 532    10128  18525  12423  -1505   1970  -2327       N  
ATOM   4929  N   LEU B 533     -13.334 -85.067  28.005  1.00 90.00           N  
ANISOU 4929  N   LEU B 533     8815  13842  11539   -459   1460  -1777       N  
ATOM   4930  CA  LEU B 533     -13.315 -86.006  29.112  1.00 88.24           C  
ANISOU 4930  CA  LEU B 533     8623  13242  11661   -218   1353  -1882       C  
ATOM   4931  C   LEU B 533     -13.967 -87.347  28.707  1.00 88.98           C  
ANISOU 4931  C   LEU B 533     8644  13248  11916    -67   1270  -2142       C  
ATOM   4932  O   LEU B 533     -15.150 -87.586  28.954  1.00 87.67           O  
ANISOU 4932  O   LEU B 533     8638  12841  11830    -25   1201  -1986       O  
ATOM   4933  CB  LEU B 533     -13.997 -85.394  30.334  1.00 85.52           C  
ANISOU 4933  CB  LEU B 533     8537  12533  11424   -196   1290  -1532       C  
ATOM   4934  CG  LEU B 533     -13.852 -86.151  31.646  1.00 83.72           C  
ANISOU 4934  CG  LEU B 533     8357  11966  11484    -32   1169  -1545       C  
ATOM   4935  CD1 LEU B 533     -12.382 -86.284  32.019  1.00 85.16           C  
ANISOU 4935  CD1 LEU B 533     8392  12205  11760      8   1155  -1708       C  
ATOM   4936  CD2 LEU B 533     -14.610 -85.433  32.708  1.00 80.71           C  
ANISOU 4936  CD2 LEU B 533     8193  11357  11115    -60   1146  -1236       C  
ATOM   4937  N   LYS B 534     -13.180 -88.216  28.075  1.00 91.09           N  
ANISOU 4937  N   LYS B 534     8642  13721  12245     12   1267  -2569       N  
ATOM   4938  CA  LYS B 534     -13.679 -89.476  27.528  1.00 91.86           C  
ANISOU 4938  CA  LYS B 534     8624  13764  12513    154   1166  -2890       C  
ATOM   4939  C   LYS B 534     -13.894 -90.531  28.603  1.00 90.74           C  
ANISOU 4939  C   LYS B 534     8552  13113  12810    361    931  -2898       C  
ATOM   4940  O   LYS B 534     -14.767 -91.388  28.489  1.00 90.62           O  
ANISOU 4940  O   LYS B 534     8573  12892  12966    442    800  -2954       O  
ATOM   4941  CB  LYS B 534     -12.685 -90.013  26.499  1.00 95.60           C  
ANISOU 4941  CB  LYS B 534     8734  14660  12926    179   1227  -3422       C  
ATOM   4942  CG  LYS B 534     -12.223 -88.986  25.477  1.00 97.95           C  
ANISOU 4942  CG  LYS B 534     8918  15552  12746    -92   1453  -3408       C  
ATOM   4943  CD  LYS B 534     -13.339 -88.567  24.522  1.00 99.57           C  
ANISOU 4943  CD  LYS B 534     9235  15962  12632   -277   1518  -3221       C  
ATOM   4944  CE  LYS B 534     -12.910 -87.382  23.668  1.00102.25           C  
ANISOU 4944  CE  LYS B 534     9518  16842  12489   -619   1685  -3053       C  
ATOM   4945  NZ  LYS B 534     -11.776 -87.671  22.731  1.00106.03           N1+
ANISOU 4945  NZ  LYS B 534     9605  17942  12738   -722   1820  -3528       N1+
ATOM   4946  N   GLU B 535     -13.086 -90.460  29.652  1.00 90.09           N  
ANISOU 4946  N   GLU B 535     8489  12835  12904    417    855  -2818       N  
ATOM   4947  CA  GLU B 535     -13.034 -91.521  30.645  1.00 90.10           C  
ANISOU 4947  CA  GLU B 535     8516  12390  13327    576    581  -2834       C  
ATOM   4948  C   GLU B 535     -12.525 -91.073  32.026  1.00 87.43           C  
ANISOU 4948  C   GLU B 535     8319  11830  13070    552    518  -2535       C  
ATOM   4949  O   GLU B 535     -11.869 -90.045  32.158  1.00 86.64           O  
ANISOU 4949  O   GLU B 535     8226  11931  12761    463    679  -2438       O  
ATOM   4950  CB  GLU B 535     -12.166 -92.657  30.122  1.00 93.76           C  
ANISOU 4950  CB  GLU B 535     8662  12865  14096    763    422  -3370       C  
ATOM   4951  CG  GLU B 535     -10.724 -92.255  30.019  1.00 97.99           C  
ANISOU 4951  CG  GLU B 535     8970  13673  14586    779    516  -3615       C  
ATOM   4952  CD  GLU B 535      -9.850 -93.198  30.797  1.00104.00           C  
ANISOU 4952  CD  GLU B 535     9593  14089  15831    977    212  -3821       C  
ATOM   4953  OE1 GLU B 535      -9.708 -94.366  30.340  1.00109.53           O  
ANISOU 4953  OE1 GLU B 535    10064  14670  16879   1164     -3  -4261       O  
ATOM   4954  OE2 GLU B 535      -9.337 -92.780  31.866  1.00101.55           O1-
ANISOU 4954  OE2 GLU B 535     9401  13606  15576    947    158  -3548       O1-
ATOM   4955  N   PHE B 536     -12.865 -91.869  33.037  1.00 86.23           N  
ANISOU 4955  N   PHE B 536     8277  11274  13211    606    263  -2375       N  
ATOM   4956  CA  PHE B 536     -12.398 -91.722  34.402  1.00 84.46           C  
ANISOU 4956  CA  PHE B 536     8167  10826  13095    576    137  -2116       C  
ATOM   4957  C   PHE B 536     -12.273 -93.128  34.966  1.00 87.04           C  
ANISOU 4957  C   PHE B 536     8446  10754  13871    680   -250  -2176       C  
ATOM   4958  O   PHE B 536     -13.227 -93.921  34.901  1.00 87.58           O  
ANISOU 4958  O   PHE B 536     8578  10620  14077    672   -407  -2112       O  
ATOM   4959  CB  PHE B 536     -13.383 -90.906  35.231  1.00 81.13           C  
ANISOU 4959  CB  PHE B 536     8015  10375  12434    412    242  -1676       C  
ATOM   4960  CG  PHE B 536     -12.878 -90.546  36.605  1.00 78.11           C  
ANISOU 4960  CG  PHE B 536     7739   9870  12067    346    165  -1426       C  
ATOM   4961  CD1 PHE B 536     -12.242 -89.327  36.830  1.00 74.51           C  
ANISOU 4961  CD1 PHE B 536     7306   9607  11397    291    353  -1365       C  
ATOM   4962  CD2 PHE B 536     -13.046 -91.415  37.673  1.00 77.17           C  
ANISOU 4962  CD2 PHE B 536     7699   9454  12167    309   -119  -1234       C  
ATOM   4963  CE1 PHE B 536     -11.768 -88.985  38.079  1.00 72.19           C  
ANISOU 4963  CE1 PHE B 536     7099   9223  11104    229    281  -1166       C  
ATOM   4964  CE2 PHE B 536     -12.586 -91.073  38.939  1.00 76.35           C  
ANISOU 4964  CE2 PHE B 536     7689   9289  12031    216   -194   -998       C  
ATOM   4965  CZ  PHE B 536     -11.940 -89.851  39.139  1.00 74.24           C  
ANISOU 4965  CZ  PHE B 536     7434   9229  11546    190     18   -987       C  
ATOM   4966  N   GLU B 537     -11.093 -93.429  35.509  1.00 88.86           N  
ANISOU 4966  N   GLU B 537     8558  10853  14350    766   -435  -2287       N  
ATOM   4967  CA  GLU B 537     -10.741 -94.768  35.989  1.00 92.09           C  
ANISOU 4967  CA  GLU B 537     8880  10843  15266    881   -881  -2378       C  
ATOM   4968  C   GLU B 537     -11.064 -95.845  34.981  1.00 94.11           C  
ANISOU 4968  C   GLU B 537     8956  10994  15808   1034  -1044  -2763       C  
ATOM   4969  O   GLU B 537     -11.548 -96.912  35.336  1.00 96.01           O  
ANISOU 4969  O   GLU B 537     9240  10837  16400   1048  -1409  -2673       O  
ATOM   4970  CB  GLU B 537     -11.415 -95.078  37.315  1.00 91.86           C  
ANISOU 4970  CB  GLU B 537     9107  10496  15297    710  -1122  -1870       C  
ATOM   4971  CG  GLU B 537     -10.636 -94.556  38.497  1.00 94.94           C  
ANISOU 4971  CG  GLU B 537     9579  10857  15634    623  -1173  -1619       C  
ATOM   4972  CD  GLU B 537     -11.465 -94.486  39.769  1.00 98.01           C  
ANISOU 4972  CD  GLU B 537    10234  11135  15869    371  -1270  -1087       C  
ATOM   4973  OE1 GLU B 537     -12.383 -95.331  39.951  1.00100.06           O  
ANISOU 4973  OE1 GLU B 537    10578  11180  16260    275  -1493   -901       O  
ATOM   4974  OE2 GLU B 537     -11.184 -93.579  40.589  1.00 98.28           O1-
ANISOU 4974  OE2 GLU B 537    10375  11327  15640    253  -1124   -871       O1-
ATOM   4975  N   GLY B 538     -10.804 -95.550  33.714  1.00 94.29           N  
ANISOU 4975  N   GLY B 538     8768  11393  15665   1122   -783  -3185       N  
ATOM   4976  CA  GLY B 538     -10.990 -96.516  32.647  1.00 96.57           C  
ANISOU 4976  CA  GLY B 538     8830  11664  16195   1282   -907  -3657       C  
ATOM   4977  C   GLY B 538     -12.429 -96.810  32.288  1.00 95.46           C  
ANISOU 4977  C   GLY B 538     8856  11448  15965   1198   -898  -3484       C  
ATOM   4978  O   GLY B 538     -12.679 -97.678  31.455  1.00 98.07           O  
ANISOU 4978  O   GLY B 538     9015  11725  16521   1326  -1036  -3864       O  
ATOM   4979  N   LYS B 539     -13.370 -96.103  32.915  1.00 91.93           N  
ANISOU 4979  N   LYS B 539     8716  11005  15206    992   -746  -2953       N  
ATOM   4980  CA  LYS B 539     -14.787 -96.234  32.594  1.00 90.49           C  
ANISOU 4980  CA  LYS B 539     8686  10801  14892    893   -697  -2769       C  
ATOM   4981  C   LYS B 539     -15.135 -95.107  31.630  1.00 88.19           C  
ANISOU 4981  C   LYS B 539     8404  10991  14110    816   -275  -2812       C  
ATOM   4982  O   LYS B 539     -14.846 -93.946  31.915  1.00 86.33           O  
ANISOU 4982  O   LYS B 539     8259  10979  13564    715    -33  -2610       O  
ATOM   4983  CB  LYS B 539     -15.637 -96.116  33.859  1.00 88.92           C  
ANISOU 4983  CB  LYS B 539     8774  10371  14639    699   -786  -2200       C  
ATOM   4984  CG  LYS B 539     -15.173 -96.952  35.036  1.00 91.62           C  
ANISOU 4984  CG  LYS B 539     9151  10294  15366    681  -1198  -2011       C  
ATOM   4985  CD  LYS B 539     -15.574 -98.405  34.855  1.00 96.99           C  
ANISOU 4985  CD  LYS B 539     9762  10571  16517    743  -1625  -2121       C  
ATOM   4986  CE  LYS B 539     -15.558 -99.178  36.169  1.00100.09           C  
ANISOU 4986  CE  LYS B 539    10277  10528  17225    602  -2074  -1722       C  
ATOM   4987  NZ  LYS B 539     -16.527-100.323  36.108  1.00102.50           N1+
ANISOU 4987  NZ  LYS B 539    10621  10489  17833    526  -2425  -1608       N1+
ATOM   4988  N   THR B 540     -15.743 -95.430  30.491  1.00 88.40           N  
ANISOU 4988  N   THR B 540     8338  11170  14077    850   -216  -3065       N  
ATOM   4989  CA  THR B 540     -15.995 -94.400  29.470  1.00 86.63           C  
ANISOU 4989  CA  THR B 540     8102  11420  13390    750    134  -3105       C  
ATOM   4990  C   THR B 540     -17.303 -93.660  29.721  1.00 83.26           C  
ANISOU 4990  C   THR B 540     7943  10992  12699    586    268  -2656       C  
ATOM   4991  O   THR B 540     -18.311 -94.274  30.021  1.00 82.95           O  
ANISOU 4991  O   THR B 540     8012  10697  12806    570    120  -2502       O  
ATOM   4992  CB  THR B 540     -15.941 -94.962  28.015  1.00 89.21           C  
ANISOU 4992  CB  THR B 540     8170  12025  13698    834    164  -3623       C  
ATOM   4993  OG1 THR B 540     -16.707 -96.168  27.930  1.00 91.89           O  
ANISOU 4993  OG1 THR B 540     8501  12036  14377    929   -105  -3739       O  
ATOM   4994  CG2 THR B 540     -14.513 -95.268  27.590  1.00 91.08           C  
ANISOU 4994  CG2 THR B 540     8078  12469  14057    968    150  -4137       C  
ATOM   4995  N   LEU B 541     -17.274 -92.337  29.603  1.00 81.14           N  
ANISOU 4995  N   LEU B 541     7760  11001  12066    460    524  -2457       N  
ATOM   4996  CA  LEU B 541     -18.450 -91.498  29.868  1.00 78.38           C  
ANISOU 4996  CA  LEU B 541     7631  10648  11502    329    634  -2075       C  
ATOM   4997  C   LEU B 541     -19.442 -91.530  28.716  1.00 79.01           C  
ANISOU 4997  C   LEU B 541     7697  10896  11425    287    695  -2148       C  
ATOM   4998  O   LEU B 541     -19.072 -91.313  27.575  1.00 80.66           O  
ANISOU 4998  O   LEU B 541     7770  11435  11441    258    802  -2374       O  
ATOM   4999  CB  LEU B 541     -18.025 -90.049  30.152  1.00 76.27           C  
ANISOU 4999  CB  LEU B 541     7447  10560  10971    222    820  -1857       C  
ATOM   5000  CG  LEU B 541     -17.611 -89.680  31.577  1.00 73.83           C  
ANISOU 5000  CG  LEU B 541     7248  10056  10745    211    782  -1627       C  
ATOM   5001  CD1 LEU B 541     -16.319 -90.335  31.979  1.00 75.40           C  
ANISOU 5001  CD1 LEU B 541     7317  10168  11163    310    663  -1820       C  
ATOM   5002  CD2 LEU B 541     -17.457 -88.217  31.672  1.00 71.51           C  
ANISOU 5002  CD2 LEU B 541     7036   9926  10206    106    946  -1436       C  
ATOM   5003  N   VAL B 542     -20.705 -91.801  29.001  1.00 78.36           N  
ANISOU 5003  N   VAL B 542     7741  10625  11404    259    625  -1956       N  
ATOM   5004  CA  VAL B 542     -21.682 -91.837  27.932  1.00 79.11           C  
ANISOU 5004  CA  VAL B 542     7824  10865  11366    220    663  -2015       C  
ATOM   5005  C   VAL B 542     -22.838 -90.884  28.167  1.00 77.60           C  
ANISOU 5005  C   VAL B 542     7799  10676  11007    114    748  -1680       C  
ATOM   5006  O   VAL B 542     -23.365 -90.797  29.270  1.00 76.84           O  
ANISOU 5006  O   VAL B 542     7815  10378  11002     93    712  -1447       O  
ATOM   5007  CB  VAL B 542     -22.134 -93.278  27.579  1.00 80.92           C  
ANISOU 5007  CB  VAL B 542     7965  10916  11865    311    466  -2252       C  
ATOM   5008  CG1 VAL B 542     -21.787 -94.240  28.661  1.00 81.87           C  
ANISOU 5008  CG1 VAL B 542     8091  10664  12349    384    237  -2229       C  
ATOM   5009  CG2 VAL B 542     -23.623 -93.351  27.236  1.00 81.01           C  
ANISOU 5009  CG2 VAL B 542     8064  10892  11822    246    451  -2110       C  
ATOM   5010  N   SER B 543     -23.201 -90.154  27.115  1.00 78.14           N  
ANISOU 5010  N   SER B 543     7861  11001  10827     33    845  -1672       N  
ATOM   5011  CA  SER B 543     -24.314 -89.217  27.146  1.00 77.14           C  
ANISOU 5011  CA  SER B 543     7857  10868  10583    -47    881  -1402       C  
ATOM   5012  C   SER B 543     -25.648 -89.948  26.989  1.00 77.33           C  
ANISOU 5012  C   SER B 543     7898  10767  10716    -29    791  -1398       C  
ATOM   5013  O   SER B 543     -25.817 -90.821  26.127  1.00 78.53           O  
ANISOU 5013  O   SER B 543     7962  10978  10896     -3    730  -1614       O  
ATOM   5014  CB  SER B 543     -24.155 -88.189  26.029  1.00 77.96           C  
ANISOU 5014  CB  SER B 543     7946  11272  10403   -170    952  -1358       C  
ATOM   5015  OG  SER B 543     -25.379 -87.511  25.805  1.00 78.86           O  
ANISOU 5015  OG  SER B 543     8147  11348  10466   -228    913  -1152       O  
ATOM   5016  N   VAL B 544     -26.607 -89.578  27.819  1.00 76.29           N  
ANISOU 5016  N   VAL B 544     7855  10486  10642    -49    783  -1180       N  
ATOM   5017  CA  VAL B 544     -27.883 -90.269  27.808  1.00 76.39           C  
ANISOU 5017  CA  VAL B 544     7869  10392  10763    -55    702  -1159       C  
ATOM   5018  C   VAL B 544     -28.873 -89.642  26.815  1.00 77.40           C  
ANISOU 5018  C   VAL B 544     8000  10650  10756    -99    708  -1115       C  
ATOM   5019  O   VAL B 544     -30.020 -90.091  26.697  1.00 77.67           O  
ANISOU 5019  O   VAL B 544     8023  10621  10864   -109    645  -1099       O  
ATOM   5020  CB  VAL B 544     -28.474 -90.384  29.217  1.00 75.05           C  
ANISOU 5020  CB  VAL B 544     7745  10056  10714    -85    685   -984       C  
ATOM   5021  CG1 VAL B 544     -27.474 -91.053  30.137  1.00 75.06           C  
ANISOU 5021  CG1 VAL B 544     7750   9925  10843    -73    629   -990       C  
ATOM   5022  CG2 VAL B 544     -28.836 -89.049  29.740  1.00 73.18           C  
ANISOU 5022  CG2 VAL B 544     7548   9879  10376   -108    780   -837       C  
ATOM   5023  N   THR B 545     -28.423 -88.623  26.089  1.00 78.13           N  
ANISOU 5023  N   THR B 545     8104  10924  10657   -148    755  -1077       N  
ATOM   5024  CA  THR B 545     -29.273 -88.005  25.092  1.00 79.50           C  
ANISOU 5024  CA  THR B 545     8285  11213  10705   -217    706  -1000       C  
ATOM   5025  C   THR B 545     -28.777 -88.308  23.695  1.00 82.24           C  
ANISOU 5025  C   THR B 545     8565  11835  10848   -292    701  -1157       C  
ATOM   5026  O   THR B 545     -29.243 -87.704  22.718  1.00 83.83           O  
ANISOU 5026  O   THR B 545     8775  12199  10877   -401    645  -1065       O  
ATOM   5027  CB  THR B 545     -29.394 -86.470  25.266  1.00 79.15           C  
ANISOU 5027  CB  THR B 545     8306  11157  10608   -268    689   -775       C  
ATOM   5028  OG1 THR B 545     -28.102 -85.857  25.160  1.00 78.46           O  
ANISOU 5028  OG1 THR B 545     8231  11191  10386   -330    742   -744       O  
ATOM   5029  CG2 THR B 545     -30.084 -86.112  26.585  1.00 76.43           C  
ANISOU 5029  CG2 THR B 545     7983  10602  10454   -190    695   -692       C  
ATOM   5030  N   LYS B 546     -27.823 -89.231  23.598  1.00 83.81           N  
ANISOU 5030  N   LYS B 546     8675  12103  11064   -243    740  -1410       N  
ATOM   5031  CA  LYS B 546     -27.316 -89.676  22.297  1.00 86.25           C  
ANISOU 5031  CA  LYS B 546     8859  12737  11173   -305    752  -1667       C  
ATOM   5032  C   LYS B 546     -27.860 -91.069  21.916  1.00 87.50           C  
ANISOU 5032  C   LYS B 546     8929  12825  11489   -214    664  -1946       C  
ATOM   5033  O   LYS B 546     -28.296 -91.848  22.774  1.00 85.97           O  
ANISOU 5033  O   LYS B 546     8765  12310  11589   -106    587  -1947       O  
ATOM   5034  CB  LYS B 546     -25.780 -89.611  22.253  1.00 86.94           C  
ANISOU 5034  CB  LYS B 546     8848  13029  11154   -321    850  -1834       C  
ATOM   5035  CG  LYS B 546     -25.215 -88.195  22.161  1.00 87.87           C  
ANISOU 5035  CG  LYS B 546     9026  13326  11035   -482    915  -1575       C  
ATOM   5036  CD  LYS B 546     -23.672 -88.191  22.075  1.00 92.42           C  
ANISOU 5036  CD  LYS B 546     9471  14153  11491   -517   1023  -1765       C  
ATOM   5037  CE  LYS B 546     -23.023 -86.886  22.642  1.00 93.42           C  
ANISOU 5037  CE  LYS B 546     9691  14265  11540   -621   1064  -1464       C  
ATOM   5038  NZ  LYS B 546     -22.220 -86.033  21.672  1.00 94.76           N1+
ANISOU 5038  NZ  LYS B 546     9785  14882  11337   -886   1116  -1392       N1+
ATOM   5039  N   GLU B 547     -27.855 -91.351  20.617  1.00 90.43           N  
ANISOU 5039  N   GLU B 547     9189  13519  11652   -288    657  -2171       N  
ATOM   5040  CA  GLU B 547     -28.222 -92.661  20.083  1.00 93.34           C  
ANISOU 5040  CA  GLU B 547     9439  13865  12160   -202    560  -2515       C  
ATOM   5041  C   GLU B 547     -27.487 -93.798  20.802  1.00 94.10           C  
ANISOU 5041  C   GLU B 547     9444  13706  12601    -23    491  -2792       C  
ATOM   5042  O   GLU B 547     -26.335 -93.642  21.224  1.00 94.40           O  
ANISOU 5042  O   GLU B 547     9432  13780  12653     14    557  -2866       O  
ATOM   5043  CB  GLU B 547     -27.969 -92.733  18.550  1.00 96.66           C  
ANISOU 5043  CB  GLU B 547     9702  14786  12238   -324    594  -2802       C  
ATOM   5044  CG  GLU B 547     -26.467 -92.868  18.101  1.00101.01           C  
ANISOU 5044  CG  GLU B 547    10047  15713  12618   -341    706  -3166       C  
ATOM   5045  CD  GLU B 547     -26.255 -93.081  16.576  1.00107.91           C  
ANISOU 5045  CD  GLU B 547    10711  17174  13116   -487    750  -3528       C  
ATOM   5046  OE1 GLU B 547     -27.035 -93.822  15.926  1.00110.52           O  
ANISOU 5046  OE1 GLU B 547    10981  17527  13482   -458    651  -3743       O  
ATOM   5047  OE2 GLU B 547     -25.273 -92.526  16.022  1.00111.37           O1-
ANISOU 5047  OE2 GLU B 547    11021  18090  13201   -653    886  -3617       O1-
ATOM   5048  N   GLY B 548     -28.160 -94.936  20.942  1.00 95.18           N  
ANISOU 5048  N   GLY B 548     9557  13564  13041     73    324  -2928       N  
ATOM   5049  CA  GLY B 548     -27.499 -96.165  21.368  1.00 97.03           C  
ANISOU 5049  CA  GLY B 548     9674  13543  13648    232    168  -3240       C  
ATOM   5050  C   GLY B 548     -26.911 -96.109  22.764  1.00 95.61           C  
ANISOU 5050  C   GLY B 548     9583  13051  13692    283    140  -3021       C  
ATOM   5051  O   GLY B 548     -25.756 -96.515  22.989  1.00 96.65           O  
ANISOU 5051  O   GLY B 548     9597  13145  13977    386     95  -3266       O  
ATOM   5052  N   LEU B 549     -27.708 -95.591  23.696  1.00 93.31           N  
ANISOU 5052  N   LEU B 549     9476  12564  13410    205    161  -2584       N  
ATOM   5053  CA  LEU B 549     -27.419 -95.747  25.101  1.00 92.25           C  
ANISOU 5053  CA  LEU B 549     9428  12120  13500    219     91  -2359       C  
ATOM   5054  C   LEU B 549     -27.176 -97.232  25.315  1.00 95.36           C  
ANISOU 5054  C   LEU B 549     9730  12190  14312    315   -192  -2585       C  
ATOM   5055  O   LEU B 549     -28.028 -98.064  24.993  1.00 96.51           O  
ANISOU 5055  O   LEU B 549     9853  12185  14631    309   -360  -2651       O  
ATOM   5056  CB  LEU B 549     -28.594 -95.270  25.943  1.00 89.65           C  
ANISOU 5056  CB  LEU B 549     9253  11673  13137    106    121  -1950       C  
ATOM   5057  CG  LEU B 549     -28.444 -95.345  27.455  1.00 87.30           C  
ANISOU 5057  CG  LEU B 549     9042  11139  12988     58     67  -1679       C  
ATOM   5058  CD1 LEU B 549     -27.489 -94.287  27.944  1.00 86.53           C  
ANISOU 5058  CD1 LEU B 549     8985  11171  12719     67    236  -1591       C  
ATOM   5059  CD2 LEU B 549     -29.768 -95.164  28.111  1.00 84.08           C  
ANISOU 5059  CD2 LEU B 549     8713  10679  12554    -69     77  -1382       C  
ATOM   5060  N   GLU B 550     -25.984 -97.558  25.791  1.00 97.40           N  
ANISOU 5060  N   GLU B 550     9919  12331  14755    407   -275  -2724       N  
ATOM   5061  CA  GLU B 550     -25.665 -98.919  26.175  1.00101.52           C  
ANISOU 5061  CA  GLU B 550    10359  12461  15752    500   -617  -2894       C  
ATOM   5062  C   GLU B 550     -25.701 -99.023  27.703  1.00100.80           C  
ANISOU 5062  C   GLU B 550    10420  12048  15831    397   -753  -2462       C  
ATOM   5063  O   GLU B 550     -25.184 -98.152  28.396  1.00 99.05           O  
ANISOU 5063  O   GLU B 550    10277  11934  15421    354   -583  -2252       O  
ATOM   5064  CB  GLU B 550     -24.328 -99.362  25.568  1.00104.30           C  
ANISOU 5064  CB  GLU B 550    10478  12892  16256    687   -683  -3418       C  
ATOM   5065  CG  GLU B 550     -23.085 -98.569  26.008  1.00107.75           C  
ANISOU 5065  CG  GLU B 550    10895  13496  16548    713   -514  -3401       C  
ATOM   5066  CD  GLU B 550     -22.930 -97.162  25.362  1.00110.56           C  
ANISOU 5066  CD  GLU B 550    11272  14368  16368    620   -129  -3345       C  
ATOM   5067  OE1 GLU B 550     -21.856 -96.933  24.729  1.00113.01           O  
ANISOU 5067  OE1 GLU B 550    11395  14991  16551    679    -14  -3690       O  
ATOM   5068  OE2 GLU B 550     -23.849 -96.298  25.501  1.00108.06           O1-
ANISOU 5068  OE2 GLU B 550    11138  14140  15778    477     28  -2963       O1-
ATOM   5069  N   LEU B 551     -26.365-100.056  28.221  1.00102.95           N  
ANISOU 5069  N   LEU B 551    10731  11954  16430    324  -1062  -2308       N  
ATOM   5070  CA  LEU B 551     -26.526-100.229  29.667  1.00103.26           C  
ANISOU 5070  CA  LEU B 551    10908  11742  16583    151  -1216  -1853       C  
ATOM   5071  C   LEU B 551     -26.361-101.677  30.097  1.00107.80           C  
ANISOU 5071  C   LEU B 551    11440  11829  17688    140  -1708  -1856       C  
ATOM   5072  O   LEU B 551     -26.662-102.566  29.310  1.00110.27           O  
ANISOU 5072  O   LEU B 551    11649  11971  18277    227  -1927  -2139       O  
ATOM   5073  CB  LEU B 551     -27.860 -99.652  30.141  1.00100.97           C  
ANISOU 5073  CB  LEU B 551    10753  11600  16011    -67  -1043  -1453       C  
ATOM   5074  CG  LEU B 551     -29.133 -99.804  29.333  1.00 99.69           C  
ANISOU 5074  CG  LEU B 551    10575  11522  15780   -109  -1005  -1496       C  
ATOM   5075  CD1 LEU B 551     -29.827-101.063  29.737  1.00103.31           C  
ANISOU 5075  CD1 LEU B 551    11039  11631  16581   -251  -1369  -1337       C  
ATOM   5076  CD2 LEU B 551     -30.019 -98.643  29.635  1.00 95.93           C  
ANISOU 5076  CD2 LEU B 551    10185  11345  14920   -234   -694  -1229       C  
ATOM   5077  N   PRO B 552     -25.891-101.927  31.346  1.00109.83           N  
ANISOU 5077  N   PRO B 552    11776  11846  18105     19  -1920  -1534       N  
ATOM   5078  CA  PRO B 552     -25.488-103.288  31.706  1.00115.06           C  
ANISOU 5078  CA  PRO B 552    12384  11994  19339     26  -2465  -1554       C  
ATOM   5079  C   PRO B 552     -26.560-104.326  31.357  1.00119.11           C  
ANISOU 5079  C   PRO B 552    12886  12238  20132    -71  -2770  -1519       C  
ATOM   5080  O   PRO B 552     -27.714-104.250  31.820  1.00118.37           O  
ANISOU 5080  O   PRO B 552    12912  12216  19847   -342  -2719  -1110       O  
ATOM   5081  CB  PRO B 552     -25.239-103.212  33.218  1.00114.80           C  
ANISOU 5081  CB  PRO B 552    12492  11836  19287   -213  -2604  -1035       C  
ATOM   5082  CG  PRO B 552     -25.841-101.966  33.669  1.00110.44           C  
ANISOU 5082  CG  PRO B 552    12063  11729  18169   -376  -2145   -743       C  
ATOM   5083  CD  PRO B 552     -25.840-101.029  32.513  1.00107.66           C  
ANISOU 5083  CD  PRO B 552    11644  11749  17512   -162  -1719  -1113       C  
ATOM   5084  N   GLU B 553     -26.168-105.271  30.507  1.00124.13           N  
ANISOU 5084  N   GLU B 553    13349  12594  21219    154  -3078  -1995       N  
ATOM   5085  CA  GLU B 553     -27.099-106.255  29.967  1.00128.39           C  
ANISOU 5085  CA  GLU B 553    13847  12874  22059    111  -3374  -2073       C  
ATOM   5086  C   GLU B 553     -27.049-107.571  30.738  1.00133.28           C  
ANISOU 5086  C   GLU B 553    14484  12862  23295    -24  -4038  -1831       C  
ATOM   5087  O   GLU B 553     -25.968-108.070  31.095  1.00135.60           O  
ANISOU 5087  O   GLU B 553    14700  12818  24001    102  -4384  -1960       O  
ATOM   5088  CB  GLU B 553     -26.860-106.477  28.461  1.00129.88           C  
ANISOU 5088  CB  GLU B 553    13817  13183  22348    426  -3310  -2787       C  
ATOM   5089  CG  GLU B 553     -27.259-105.284  27.566  1.00127.79           C  
ANISOU 5089  CG  GLU B 553    13555  13536  21461    468  -2722  -2935       C  
ATOM   5090  CD  GLU B 553     -28.776-105.094  27.452  1.00128.11           C  
ANISOU 5090  CD  GLU B 553    13721  13707  21247    252  -2587  -2614       C  
ATOM   5091  OE1 GLU B 553     -29.395-105.770  26.596  1.00130.31           O  
ANISOU 5091  OE1 GLU B 553    13910  13897  21704    303  -2742  -2881       O  
ATOM   5092  OE2 GLU B 553     -29.342-104.260  28.205  1.00125.34           O1-
ANISOU 5092  OE2 GLU B 553    13535  13561  20527     41  -2329  -2135       O1-
ATOM   5093  N   ASP B 554     -28.245-108.085  31.016  1.00135.17           N  
ANISOU 5093  N   ASP B 554    14820  12952  23583   -309  -4225  -1448       N  
ATOM   5094  CA  ASP B 554     -28.441-109.401  31.585  1.00140.81           C  
ANISOU 5094  CA  ASP B 554    15554  13059  24887   -500  -4901  -1177       C  
ATOM   5095  C   ASP B 554     -28.562-110.388  30.424  1.00144.66           C  
ANISOU 5095  C   ASP B 554    15857  13217  25887   -251  -5235  -1741       C  
ATOM   5096  O   ASP B 554     -28.942-109.995  29.318  1.00143.09           O  
ANISOU 5096  O   ASP B 554    15570  13361  25434    -68  -4876  -2161       O  
ATOM   5097  CB  ASP B 554     -29.720-109.398  32.432  1.00140.57           C  
ANISOU 5097  CB  ASP B 554    15697  13123  24590   -978  -4897   -482       C  
ATOM   5098  CG  ASP B 554     -30.057-110.770  33.011  1.00146.54           C  
ANISOU 5098  CG  ASP B 554    16484  13269  25922  -1266  -5627   -109       C  
ATOM   5099  OD1 ASP B 554     -29.140-111.468  33.500  1.00150.35           O  
ANISOU 5099  OD1 ASP B 554    16948  13268  26910  -1234  -6147    -68       O  
ATOM   5100  OD2 ASP B 554     -31.248-111.149  32.981  1.00148.10           O1-
ANISOU 5100  OD2 ASP B 554    16721  13462  26086  -1540  -5711    158       O1-
ATOM   5101  N   GLU B 555     -28.236-111.658  30.673  1.00150.48           N  
ANISOU 5101  N   GLU B 555    16532  13288  27355   -253  -5948  -1756       N  
ATOM   5102  CA  GLU B 555     -28.425-112.746  29.689  1.00155.14           C  
ANISOU 5102  CA  GLU B 555    16937  13473  28536    -43  -6377  -2280       C  
ATOM   5103  C   GLU B 555     -29.875-112.798  29.167  1.00154.52           C  
ANISOU 5103  C   GLU B 555    16915  13573  28220   -231  -6219  -2151       C  
ATOM   5104  O   GLU B 555     -30.149-113.350  28.095  1.00156.49           O  
ANISOU 5104  O   GLU B 555    17005  13713  28739    -22  -6350  -2682       O  
ATOM   5105  CB  GLU B 555     -28.038-114.120  30.286  1.00161.20           C  
ANISOU 5105  CB  GLU B 555    17668  13405  30172   -112  -7270  -2140       C  
ATOM   5106  CG  GLU B 555     -27.038-114.085  31.465  1.00162.48           C  
ANISOU 5106  CG  GLU B 555    17909  13333  30492   -206  -7529  -1766       C  
ATOM   5107  CD  GLU B 555     -25.581-114.262  31.050  1.00164.41           C  
ANISOU 5107  CD  GLU B 555    17908  13380  31179    263  -7703  -2465       C  
ATOM   5108  OE1 GLU B 555     -24.792-113.300  31.186  1.00159.98           O  
ANISOU 5108  OE1 GLU B 555    17339  13249  30196    399  -7234  -2572       O  
ATOM   5109  OE2 GLU B 555     -25.225-115.373  30.599  1.00170.11           O1-
ANISOU 5109  OE2 GLU B 555    18425  13511  32695    496  -8330  -2928       O1-
ATOM   5110  N   GLU B 556     -30.790-112.200  29.927  1.00152.15           N  
ANISOU 5110  N   GLU B 556    16820  13581  27409   -624  -5931  -1481       N  
ATOM   5111  CA  GLU B 556     -32.212-112.239  29.614  1.00151.98           C  
ANISOU 5111  CA  GLU B 556    16850  13729  27165   -853  -5804  -1276       C  
ATOM   5112  C   GLU B 556     -32.777-110.906  29.075  1.00146.75           C  
ANISOU 5112  C   GLU B 556    16216  13797  25744   -796  -5035  -1368       C  
ATOM   5113  O   GLU B 556     -33.740-110.913  28.294  1.00146.32           O  
ANISOU 5113  O   GLU B 556    16125  13907  25563   -801  -4896  -1509       O  
ATOM   5114  CB  GLU B 556     -33.001-112.715  30.838  1.00154.01           C  
ANISOU 5114  CB  GLU B 556    17267  13779  27469  -1388  -6132   -465       C  
ATOM   5115  CG  GLU B 556     -34.389-113.236  30.519  1.00156.80           C  
ANISOU 5115  CG  GLU B 556    17625  14091  27862  -1640  -6254   -287       C  
ATOM   5116  CD  GLU B 556     -35.376-112.980  31.641  1.00157.95           C  
ANISOU 5116  CD  GLU B 556    17911  14501  27600  -2194  -6148    495       C  
ATOM   5117  OE1 GLU B 556     -35.263-113.654  32.689  1.00162.01           O  
ANISOU 5117  OE1 GLU B 556    18505  14676  28374  -2561  -6635   1039       O  
ATOM   5118  OE2 GLU B 556     -36.263-112.108  31.470  1.00154.63           O1-
ANISOU 5118  OE2 GLU B 556    17501  14645  26603  -2274  -5596    556       O1-
ATOM   5119  N   GLU B 557     -32.202-109.769  29.473  1.00142.97           N  
ANISOU 5119  N   GLU B 557    15799  13731  24791   -745  -4572  -1287       N  
ATOM   5120  CA  GLU B 557     -32.713-108.498  28.950  1.00138.54           C  
ANISOU 5120  CA  GLU B 557    15261  13798  23581   -688  -3918  -1369       C  
ATOM   5121  C   GLU B 557     -32.376-108.366  27.468  1.00137.70           C  
ANISOU 5121  C   GLU B 557    14994  13860  23464   -314  -3746  -2071       C  
ATOM   5122  O   GLU B 557     -33.219-107.934  26.678  1.00135.96           O  
ANISOU 5122  O   GLU B 557    14758  13961  22937   -304  -3462  -2186       O  
ATOM   5123  CB  GLU B 557     -32.234-107.266  29.744  1.00135.26           C  
ANISOU 5123  CB  GLU B 557    14946  13770  22675   -740  -3489  -1106       C  
ATOM   5124  CG  GLU B 557     -33.223-106.064  29.655  1.00133.11           C  
ANISOU 5124  CG  GLU B 557    14733  14049  21790   -850  -2944   -933       C  
ATOM   5125  CD  GLU B 557     -32.547-104.679  29.481  1.00132.27           C  
ANISOU 5125  CD  GLU B 557    14641  14377  21236   -659  -2446  -1093       C  
ATOM   5126  OE1 GLU B 557     -31.832-104.201  30.406  1.00132.07           O  
ANISOU 5126  OE1 GLU B 557    14683  14402  21095   -710  -2367   -882       O  
ATOM   5127  OE2 GLU B 557     -32.761-104.050  28.414  1.00131.10           O1-
ANISOU 5127  OE2 GLU B 557    14440  14526  20844   -484  -2150  -1407       O1-
ATOM   5128  N   LYS B 558     -31.153-108.758  27.099  1.00139.07           N  
ANISOU 5128  N   LYS B 558    15030  13841  23969    -25  -3936  -2546       N  
ATOM   5129  CA  LYS B 558     -30.700-108.660  25.709  1.00139.01           C  
ANISOU 5129  CA  LYS B 558    14825  14072  23919    306  -3772  -3265       C  
ATOM   5130  C   LYS B 558     -31.639-109.435  24.798  1.00141.03           C  
ANISOU 5130  C   LYS B 558    14993  14206  24385    318  -3977  -3524       C  
ATOM   5131  O   LYS B 558     -31.894-109.033  23.663  1.00140.30           O  
ANISOU 5131  O   LYS B 558    14805  14509  23991    446  -3686  -3913       O  
ATOM   5132  CB  LYS B 558     -29.234-109.101  25.544  1.00141.53           C  
ANISOU 5132  CB  LYS B 558    14954  14191  24626    602  -3998  -3779       C  
ATOM   5133  CG  LYS B 558     -28.983-110.609  25.436  1.00147.38           C  
ANISOU 5133  CG  LYS B 558    15537  14285  26174    726  -4681  -4104       C  
ATOM   5134  CD  LYS B 558     -27.475-110.935  25.476  1.00150.54           C  
ANISOU 5134  CD  LYS B 558    15737  14488  26974   1020  -4908  -4579       C  
ATOM   5135  CE  LYS B 558     -27.182-112.433  25.267  1.00155.71           C  
ANISOU 5135  CE  LYS B 558    16185  14464  28512   1199  -5638  -5013       C  
ATOM   5136  NZ  LYS B 558     -25.753-112.765  25.505  1.00156.69           N1+
ANISOU 5136  NZ  LYS B 558    16111  14332  29090   1467  -5921  -5410       N1+
ATOM   5137  N   LYS B 559     -32.170-110.535  25.318  1.00143.73           N  
ANISOU 5137  N   LYS B 559    15371  14006  25232    149  -4498  -3271       N  
ATOM   5138  CA  LYS B 559     -33.159-111.310  24.603  1.00145.60           C  
ANISOU 5138  CA  LYS B 559    15545  14073  25701    112  -4738  -3433       C  
ATOM   5139  C   LYS B 559     -34.503-110.590  24.660  1.00142.04           C  
ANISOU 5139  C   LYS B 559    15242  14002  24725   -156  -4365  -2983       C  
ATOM   5140  O   LYS B 559     -35.198-110.493  23.646  1.00141.82           O  
ANISOU 5140  O   LYS B 559    15147  14214  24524    -93  -4209  -3260       O  
ATOM   5141  CB  LYS B 559     -33.245-112.733  25.162  1.00150.56           C  
ANISOU 5141  CB  LYS B 559    16160  13956  27088     -3  -5476  -3283       C  
ATOM   5142  CG  LYS B 559     -31.991-113.575  24.878  1.00155.10           C  
ANISOU 5142  CG  LYS B 559    16525  14098  28309    329  -5930  -3883       C  
ATOM   5143  CD  LYS B 559     -32.140-115.049  25.297  1.00161.20           C  
ANISOU 5143  CD  LYS B 559    17266  14050  29930    229  -6760  -3776       C  
ATOM   5144  CE  LYS B 559     -33.001-115.862  24.316  1.00163.70           C  
ANISOU 5144  CE  LYS B 559    17460  14182  30554    280  -7024  -4151       C  
ATOM   5145  NZ  LYS B 559     -33.144-117.289  24.731  1.00168.56           N1+
ANISOU 5145  NZ  LYS B 559    18048  13951  32045    167  -7886  -4025       N1+
ATOM   5146  N   LYS B 560     -34.858-110.060  25.831  1.00139.33           N  
ANISOU 5146  N   LYS B 560    15075  13746  24119   -451  -4221  -2327       N  
ATOM   5147  CA  LYS B 560     -36.121-109.331  25.975  1.00136.08           C  
ANISOU 5147  CA  LYS B 560    14760  13715  23227   -696  -3867  -1936       C  
ATOM   5148  C   LYS B 560     -36.177-108.116  25.060  1.00132.05           C  
ANISOU 5148  C   LYS B 560    14222  13778  22171   -505  -3312  -2223       C  
ATOM   5149  O   LYS B 560     -37.244-107.742  24.580  1.00130.62           O  
ANISOU 5149  O   LYS B 560    14046  13856  21724   -587  -3112  -2166       O  
ATOM   5150  CB  LYS B 560     -36.375-108.912  27.424  1.00134.84           C  
ANISOU 5150  CB  LYS B 560    14750  13630  22853  -1035  -3782  -1264       C  
ATOM   5151  CG  LYS B 560     -37.027-109.992  28.263  1.00138.95           C  
ANISOU 5151  CG  LYS B 560    15313  13744  23737  -1405  -4271   -794       C  
ATOM   5152  CD  LYS B 560     -38.060-109.433  29.242  1.00138.13           C  
ANISOU 5152  CD  LYS B 560    15291  13984  23208  -1813  -4027   -197       C  
ATOM   5153  CE  LYS B 560     -38.830-110.581  29.909  1.00142.77           C  
ANISOU 5153  CE  LYS B 560    15894  14219  24131  -2240  -4530    266       C  
ATOM   5154  NZ  LYS B 560     -39.849-110.129  30.896  1.00142.06           N1+
ANISOU 5154  NZ  LYS B 560    15834  14527  23612  -2687  -4306    824       N1+
ATOM   5155  N   GLN B 561     -35.021-107.509  24.814  1.00130.36           N  
ANISOU 5155  N   GLN B 561    13972  13753  21803   -269  -3096  -2515       N  
ATOM   5156  CA  GLN B 561     -34.949-106.349  23.939  1.00127.12           C  
ANISOU 5156  CA  GLN B 561    13538  13879  20882   -125  -2620  -2752       C  
ATOM   5157  C   GLN B 561     -35.209-106.713  22.482  1.00128.41           C  
ANISOU 5157  C   GLN B 561    13554  14164  21069     37  -2655  -3284       C  
ATOM   5158  O   GLN B 561     -36.196-106.248  21.903  1.00127.19           O  
ANISOU 5158  O   GLN B 561    13420  14286  20617    -37  -2460  -3225       O  
ATOM   5159  CB  GLN B 561     -33.623-105.604  24.113  1.00125.69           C  
ANISOU 5159  CB  GLN B 561    13350  13888  20518     32  -2394  -2882       C  
ATOM   5160  CG  GLN B 561     -33.698-104.457  25.132  1.00123.09           C  
ANISOU 5160  CG  GLN B 561    13177  13781  19808   -123  -2073  -2385       C  
ATOM   5161  CD  GLN B 561     -34.573-103.285  24.662  1.00120.52           C  
ANISOU 5161  CD  GLN B 561    12900  13902  18989   -179  -1678  -2268       C  
ATOM   5162  OE1 GLN B 561     -34.477-102.843  23.517  1.00120.21           O  
ANISOU 5162  OE1 GLN B 561    12792  14153  18728    -47  -1505  -2593       O  
ATOM   5163  NE2 GLN B 561     -35.419-102.778  25.554  1.00118.78           N  
ANISOU 5163  NE2 GLN B 561    12779  13751  18599   -389  -1556  -1814       N  
ATOM   5164  N   GLU B 562     -34.357-107.567  21.904  1.00130.90           N  
ANISOU 5164  N   GLU B 562    13702  14280  21753    254  -2926  -3823       N  
ATOM   5165  CA  GLU B 562     -34.510-107.994  20.500  1.00132.52           C  
ANISOU 5165  CA  GLU B 562    13726  14639  21985    414  -2978  -4421       C  
ATOM   5166  C   GLU B 562     -35.922-108.502  20.204  1.00132.42           C  
ANISOU 5166  C   GLU B 562    13745  14500  22068    260  -3140  -4278       C  
ATOM   5167  O   GLU B 562     -36.385-108.477  19.061  1.00132.99           O  
ANISOU 5167  O   GLU B 562    13721  14845  21961    319  -3056  -4622       O  
ATOM   5168  CB  GLU B 562     -33.461-109.047  20.119  1.00136.93           C  
ANISOU 5168  CB  GLU B 562    14060  14909  23059    667  -3341  -5051       C  
ATOM   5169  CG  GLU B 562     -31.994-108.603  20.321  1.00138.48           C  
ANISOU 5169  CG  GLU B 562    14171  15256  23186    839  -3192  -5278       C  
ATOM   5170  CD  GLU B 562     -31.643-107.271  19.632  1.00137.44           C  
ANISOU 5170  CD  GLU B 562    14028  15837  22357    857  -2638  -5380       C  
ATOM   5171  OE1 GLU B 562     -31.127-106.358  20.321  1.00134.15           O  
ANISOU 5171  OE1 GLU B 562    13732  15571  21667    801  -2377  -5039       O  
ATOM   5172  OE2 GLU B 562     -31.882-107.137  18.407  1.00139.37           O1-
ANISOU 5172  OE2 GLU B 562    14139  16488  22324    903  -2489  -5784       O1-
ATOM   5173  N   GLU B 563     -36.597-108.945  21.258  1.00131.41           N  
ANISOU 5173  N   GLU B 563    13745  13990  22192     34  -3372  -3753       N  
ATOM   5174  CA  GLU B 563     -37.960-109.427  21.169  1.00131.35           C  
ANISOU 5174  CA  GLU B 563    13769  13850  22287   -162  -3536  -3533       C  
ATOM   5175  C   GLU B 563     -38.956-108.278  21.049  1.00126.52           C  
ANISOU 5175  C   GLU B 563    13250  13711  21107   -305  -3100  -3215       C  
ATOM   5176  O   GLU B 563     -39.938-108.385  20.318  1.00126.96           O  
ANISOU 5176  O   GLU B 563    13267  13879  21090   -351  -3102  -3297       O  
ATOM   5177  CB  GLU B 563     -38.286-110.296  22.381  1.00133.67           C  
ANISOU 5177  CB  GLU B 563    14147  13619  23022   -412  -3949  -3051       C  
ATOM   5178  CG  GLU B 563     -39.419-111.288  22.154  1.00137.66           C  
ANISOU 5178  CG  GLU B 563    14619  13819  23864   -581  -4318  -2983       C  
ATOM   5179  CD  GLU B 563     -39.393-112.430  23.154  1.00142.71           C  
ANISOU 5179  CD  GLU B 563    15298  13839  25085   -798  -4884  -2638       C  
ATOM   5180  OE1 GLU B 563     -40.065-113.462  22.897  1.00146.98           O  
ANISOU 5180  OE1 GLU B 563    15785  14010  26051   -902  -5314  -2672       O  
ATOM   5181  OE2 GLU B 563     -38.696-112.294  24.190  1.00142.02           O1-
ANISOU 5181  OE2 GLU B 563    15296  13630  25034   -882  -4926  -2316       O1-
ATOM   5182  N   LYS B 564     -38.707-107.189  21.768  1.00121.67           N  
ANISOU 5182  N   LYS B 564    12746  13354  20127   -366  -2757  -2873       N  
ATOM   5183  CA  LYS B 564     -39.507-105.978  21.614  1.00117.10           C  
ANISOU 5183  CA  LYS B 564    12228  13215  19047   -448  -2359  -2644       C  
ATOM   5184  C   LYS B 564     -39.128-105.253  20.325  1.00115.74           C  
ANISOU 5184  C   LYS B 564    11993  13454  18526   -254  -2107  -3050       C  
ATOM   5185  O   LYS B 564     -39.974-104.606  19.705  1.00114.23           O  
ANISOU 5185  O   LYS B 564    11807  13559  18033   -299  -1928  -3002       O  
ATOM   5186  CB  LYS B 564     -39.328-105.048  22.806  1.00114.05           C  
ANISOU 5186  CB  LYS B 564    11956  12955  18420   -564  -2109  -2201       C  
ATOM   5187  CG  LYS B 564     -39.965-105.532  24.091  1.00113.94           C  
ANISOU 5187  CG  LYS B 564    11997  12708  18588   -848  -2281  -1720       C  
ATOM   5188  CD  LYS B 564     -39.499-104.666  25.245  1.00110.79           C  
ANISOU 5188  CD  LYS B 564    11683  12459  17951   -929  -2045  -1390       C  
ATOM   5189  CE  LYS B 564     -39.822-105.261  26.600  1.00111.37           C  
ANISOU 5189  CE  LYS B 564    11797  12326  18192  -1242  -2253   -932       C  
ATOM   5190  NZ  LYS B 564     -38.938-104.657  27.636  1.00109.64           N1+
ANISOU 5190  NZ  LYS B 564    11652  12183  17820  -1268  -2108   -728       N1+
ATOM   5191  N   LYS B 565     -37.856-105.376  19.930  1.00116.15           N  
ANISOU 5191  N   LYS B 565    11969  13540  18620    -60  -2114  -3443       N  
ATOM   5192  CA  LYS B 565     -37.333-104.779  18.687  1.00115.71           C  
ANISOU 5192  CA  LYS B 565    11821  13936  18207     78  -1893  -3857       C  
ATOM   5193  C   LYS B 565     -38.056-105.224  17.410  1.00117.28           C  
ANISOU 5193  C   LYS B 565    11907  14284  18367     95  -1990  -4207       C  
ATOM   5194  O   LYS B 565     -38.429-104.389  16.577  1.00116.20           O  
ANISOU 5194  O   LYS B 565    11775  14579  17797     56  -1764  -4221       O  
ATOM   5195  CB  LYS B 565     -35.834-105.045  18.541  1.00117.16           C  
ANISOU 5195  CB  LYS B 565    11884  14127  18501    267  -1925  -4279       C  
ATOM   5196  CG  LYS B 565     -34.956-103.849  18.860  1.00115.95           C  
ANISOU 5196  CG  LYS B 565    11796  14281  17975    279  -1589  -4122       C  
ATOM   5197  CD  LYS B 565     -33.527-104.036  18.325  1.00120.32           C  
ANISOU 5197  CD  LYS B 565    12168  15006  18542    462  -1573  -4659       C  
ATOM   5198  CE  LYS B 565     -33.489-104.133  16.785  1.00123.48           C  
ANISOU 5198  CE  LYS B 565    12375  15849  18693    517  -1513  -5209       C  
ATOM   5199  NZ  LYS B 565     -32.084-104.079  16.267  1.00126.21           N1+
ANISOU 5199  NZ  LYS B 565    12510  16515  18926    654  -1411  -5724       N1+
ATOM   5200  N   THR B 566     -38.238-106.536  17.260  1.00119.75           N  
ANISOU 5200  N   THR B 566    12119  14231  19149    144  -2361  -4483       N  
ATOM   5201  CA  THR B 566     -38.895-107.085  16.076  1.00121.67           C  
ANISOU 5201  CA  THR B 566    12237  14583  19406    169  -2495  -4868       C  
ATOM   5202  C   THR B 566     -40.418-107.033  16.218  1.00119.88           C  
ANISOU 5202  C   THR B 566    12110  14280  19158    -25  -2533  -4460       C  
ATOM   5203  O   THR B 566     -41.148-107.063  15.225  1.00121.04           O  
ANISOU 5203  O   THR B 566    12195  14643  19149    -47  -2539  -4647       O  
ATOM   5204  CB  THR B 566     -38.394-108.518  15.706  1.00126.49           C  
ANISOU 5204  CB  THR B 566    12654  14842  20563    336  -2908  -5453       C  
ATOM   5205  OG1 THR B 566     -38.754-109.446  16.735  1.00128.07           O  
ANISOU 5205  OG1 THR B 566    12923  14414  21325    254  -3286  -5155       O  
ATOM   5206  CG2 THR B 566     -36.865-108.536  15.493  1.00127.69           C  
ANISOU 5206  CG2 THR B 566    12651  15131  20731    551  -2858  -5944       C  
ATOM   5207  N   LYS B 567     -40.893-106.946  17.454  1.00116.93           N  
ANISOU 5207  N   LYS B 567    11869  13639  18918   -181  -2554  -3914       N  
ATOM   5208  CA  LYS B 567     -42.303-106.708  17.695  1.00114.80           C  
ANISOU 5208  CA  LYS B 567    11664  13387  18565   -380  -2523  -3512       C  
ATOM   5209  C   LYS B 567     -42.699-105.366  17.071  1.00111.72           C  
ANISOU 5209  C   LYS B 567    11310  13501  17638   -386  -2167  -3424       C  
ATOM   5210  O   LYS B 567     -43.626-105.304  16.268  1.00112.81           O  
ANISOU 5210  O   LYS B 567    11407  13799  17654   -431  -2183  -3487       O  
ATOM   5211  CB  LYS B 567     -42.600-106.727  19.195  1.00113.61           C  
ANISOU 5211  CB  LYS B 567    11615  12979  18570   -572  -2555  -2966       C  
ATOM   5212  CG  LYS B 567     -44.011-107.132  19.552  1.00114.34           C  
ANISOU 5212  CG  LYS B 567    11704  12944  18795   -809  -2695  -2645       C  
ATOM   5213  CD  LYS B 567     -44.354-106.732  20.972  1.00113.26           C  
ANISOU 5213  CD  LYS B 567    11642  12794  18597  -1035  -2583  -2100       C  
ATOM   5214  CE  LYS B 567     -45.803-107.075  21.289  1.00115.47           C  
ANISOU 5214  CE  LYS B 567    11873  13045  18952  -1302  -2686  -1803       C  
ATOM   5215  NZ  LYS B 567     -46.322-106.275  22.435  1.00114.02           N1+
ANISOU 5215  NZ  LYS B 567    11708  13089  18525  -1507  -2435  -1359       N1+
ATOM   5216  N   PHE B 568     -41.980-104.300  17.411  1.00108.29           N  
ANISOU 5216  N   PHE B 568    10949  13293  16904   -345  -1884  -3280       N  
ATOM   5217  CA  PHE B 568     -42.322-102.969  16.914  1.00105.25           C  
ANISOU 5217  CA  PHE B 568    10607  13321  16060   -369  -1606  -3139       C  
ATOM   5218  C   PHE B 568     -41.570-102.563  15.649  1.00105.91           C  
ANISOU 5218  C   PHE B 568    10632  13794  15813   -275  -1501  -3510       C  
ATOM   5219  O   PHE B 568     -41.706-101.428  15.186  1.00104.51           O  
ANISOU 5219  O   PHE B 568    10500  13956  15252   -320  -1314  -3368       O  
ATOM   5220  CB  PHE B 568     -42.120-101.922  18.000  1.00101.88           C  
ANISOU 5220  CB  PHE B 568    10287  12931  15490   -411  -1378  -2736       C  
ATOM   5221  CG  PHE B 568     -43.114-102.005  19.098  1.00100.21           C  
ANISOU 5221  CG  PHE B 568    10100  12528  15444   -559  -1410  -2354       C  
ATOM   5222  CD1 PHE B 568     -42.890-102.831  20.195  1.00100.69           C  
ANISOU 5222  CD1 PHE B 568    10177  12266  15814   -639  -1557  -2208       C  
ATOM   5223  CD2 PHE B 568     -44.277-101.250  19.053  1.00 98.54           C  
ANISOU 5223  CD2 PHE B 568     9876  12485  15076   -642  -1312  -2140       C  
ATOM   5224  CE1 PHE B 568     -43.822-102.912  21.233  1.00100.31           C  
ANISOU 5224  CE1 PHE B 568    10127  12128  15858   -838  -1575  -1841       C  
ATOM   5225  CE2 PHE B 568     -45.218-101.315  20.092  1.00 97.92           C  
ANISOU 5225  CE2 PHE B 568     9770  12310  15122   -798  -1316  -1831       C  
ATOM   5226  CZ  PHE B 568     -44.992-102.149  21.181  1.00 98.17           C  
ANISOU 5226  CZ  PHE B 568     9814  12084  15403   -916  -1432  -1677       C  
ATOM   5227  N   GLU B 569     -40.793-103.487  15.090  1.00108.13           N  
ANISOU 5227  N   GLU B 569    10794  14040  16249   -163  -1646  -3991       N  
ATOM   5228  CA  GLU B 569     -40.075-103.246  13.844  1.00109.69           C  
ANISOU 5228  CA  GLU B 569    10880  14688  16107   -108  -1549  -4419       C  
ATOM   5229  C   GLU B 569     -41.018-102.670  12.779  1.00109.67           C  
ANISOU 5229  C   GLU B 569    10878  15050  15738   -227  -1502  -4370       C  
ATOM   5230  O   GLU B 569     -40.682-101.684  12.119  1.00109.35           O  
ANISOU 5230  O   GLU B 569    10852  15455  15241   -297  -1319  -4334       O  
ATOM   5231  CB  GLU B 569     -39.442-104.543  13.362  1.00113.47           C  
ANISOU 5231  CB  GLU B 569    11171  15044  16896     34  -1779  -5029       C  
ATOM   5232  CG  GLU B 569     -38.277-104.396  12.400  1.00117.30           C  
ANISOU 5232  CG  GLU B 569    11486  16003  17078    113  -1651  -5552       C  
ATOM   5233  CD  GLU B 569     -37.778-105.763  11.894  1.00124.62           C  
ANISOU 5233  CD  GLU B 569    12173  16794  18383    285  -1921  -6257       C  
ATOM   5234  OE1 GLU B 569     -36.544-106.016  11.931  1.00127.36           O  
ANISOU 5234  OE1 GLU B 569    12371  17196  18821    428  -1908  -6651       O  
ATOM   5235  OE2 GLU B 569     -38.621-106.597  11.472  1.00126.95           O1-
ANISOU 5235  OE2 GLU B 569    12407  16906  18919    288  -2168  -6443       O1-
ATOM   5236  N   ASN B 570     -42.201-103.269  12.641  1.00109.95           N  
ANISOU 5236  N   ASN B 570    10903  14891  15982   -276  -1693  -4331       N  
ATOM   5237  CA  ASN B 570     -43.231-102.773  11.728  1.00109.96           C  
ANISOU 5237  CA  ASN B 570    10908  15176  15695   -392  -1694  -4242       C  
ATOM   5238  C   ASN B 570     -43.681-101.339  11.976  1.00106.79           C  
ANISOU 5238  C   ASN B 570    10639  14941  14996   -493  -1513  -3741       C  
ATOM   5239  O   ASN B 570     -43.536-100.485  11.104  1.00107.30           O  
ANISOU 5239  O   ASN B 570    10711  15417  14640   -574  -1425  -3724       O  
ATOM   5240  CB  ASN B 570     -44.450-103.682  11.753  1.00111.47           C  
ANISOU 5240  CB  ASN B 570    11063  15062  16227   -427  -1938  -4241       C  
ATOM   5241  CG  ASN B 570     -44.336-104.827  10.786  1.00115.66           C  
ANISOU 5241  CG  ASN B 570    11434  15624  16888   -365  -2155  -4816       C  
ATOM   5242  OD1 ASN B 570     -43.582-104.767   9.809  1.00117.84           O  
ANISOU 5242  OD1 ASN B 570    11604  16300  16869   -329  -2092  -5231       O  
ATOM   5243  ND2 ASN B 570     -45.096-105.883  11.043  1.00117.81           N  
ANISOU 5243  ND2 ASN B 570    11666  15496  17599   -370  -2422  -4862       N  
ATOM   5244  N   LEU B 571     -44.235-101.075  13.158  1.00103.83           N  
ANISOU 5244  N   LEU B 571    10348  14257  14843   -507  -1483  -3343       N  
ATOM   5245  CA  LEU B 571     -44.650 -99.722  13.517  1.00100.80           C  
ANISOU 5245  CA  LEU B 571    10057  13979  14262   -565  -1339  -2924       C  
ATOM   5246  C   LEU B 571     -43.518 -98.712  13.338  1.00 99.74           C  
ANISOU 5246  C   LEU B 571     9982  14118  13794   -559  -1159  -2882       C  
ATOM   5247  O   LEU B 571     -43.754 -97.595  12.884  1.00 99.40           O  
ANISOU 5247  O   LEU B 571     9988  14305  13474   -637  -1118  -2667       O  
ATOM   5248  CB  LEU B 571     -45.172 -99.674  14.949  1.00 98.64           C  
ANISOU 5248  CB  LEU B 571     9821  13383  14274   -571  -1304  -2599       C  
ATOM   5249  CG  LEU B 571     -45.296 -98.280  15.550  1.00 95.63           C  
ANISOU 5249  CG  LEU B 571     9506  13079  13747   -583  -1141  -2253       C  
ATOM   5250  CD1 LEU B 571     -46.424 -97.525  14.889  1.00 95.86           C  
ANISOU 5250  CD1 LEU B 571     9510  13256  13657   -638  -1212  -2115       C  
ATOM   5251  CD2 LEU B 571     -45.516 -98.390  17.026  1.00 94.01           C  
ANISOU 5251  CD2 LEU B 571     9305  12626  13788   -595  -1077  -2035       C  
ATOM   5252  N   CYS B 572     -42.295 -99.110  13.694  1.00 99.54           N  
ANISOU 5252  N   CYS B 572     9944  14053  13821   -478  -1083  -3078       N  
ATOM   5253  CA  CYS B 572     -41.107 -98.268  13.503  1.00 98.73           C  
ANISOU 5253  CA  CYS B 572     9873  14234  13406   -486   -911  -3081       C  
ATOM   5254  C   CYS B 572     -40.923 -97.836  12.060  1.00100.93           C  
ANISOU 5254  C   CYS B 572    10099  15007  13241   -606   -908  -3238       C  
ATOM   5255  O   CYS B 572     -40.608 -96.670  11.805  1.00100.22           O  
ANISOU 5255  O   CYS B 572    10075  15172  12829   -714   -817  -2997       O  
ATOM   5256  CB  CYS B 572     -39.844 -98.952  14.030  1.00 98.60           C  
ANISOU 5256  CB  CYS B 572     9808  14098  13557   -369   -865  -3344       C  
ATOM   5257  SG  CYS B 572     -39.521 -98.596  15.795  1.00 96.05           S  
ANISOU 5257  SG  CYS B 572     9605  13396  13492   -311   -764  -2972       S  
ATOM   5258  N   LYS B 573     -41.145 -98.773  11.131  1.00103.86           N  
ANISOU 5258  N   LYS B 573    10345  15517  13598   -611  -1033  -3631       N  
ATOM   5259  CA  LYS B 573     -41.043 -98.504   9.693  1.00106.76           C  
ANISOU 5259  CA  LYS B 573    10633  16426  13502   -764  -1046  -3824       C  
ATOM   5260  C   LYS B 573     -42.132 -97.582   9.144  1.00106.37           C  
ANISOU 5260  C   LYS B 573    10672  16514  13227   -931  -1135  -3438       C  
ATOM   5261  O   LYS B 573     -41.840 -96.726   8.305  1.00107.69           O  
ANISOU 5261  O   LYS B 573    10854  17120  12944  -1121  -1112  -3322       O  
ATOM   5262  CB  LYS B 573     -40.932 -99.796   8.874  1.00110.43           C  
ANISOU 5262  CB  LYS B 573    10909  17026  14023   -710  -1160  -4426       C  
ATOM   5263  CG  LYS B 573     -39.492-100.095   8.454  1.00114.52           C  
ANISOU 5263  CG  LYS B 573    11263  17901  14348   -677  -1039  -4909       C  
ATOM   5264  CD  LYS B 573     -39.225-101.554   8.044  1.00119.94           C  
ANISOU 5264  CD  LYS B 573    11725  18543  15301   -524  -1180  -5599       C  
ATOM   5265  CE  LYS B 573     -37.774-101.923   8.435  1.00121.98           C  
ANISOU 5265  CE  LYS B 573    11848  18815  15683   -373  -1082  -5979       C  
ATOM   5266  NZ  LYS B 573     -37.231-103.075   7.672  1.00127.42           N1+
ANISOU 5266  NZ  LYS B 573    12243  19696  16472   -253  -1191  -6778       N1+
ATOM   5267  N   ILE B 574     -43.369 -97.734   9.616  1.00104.85           N  
ANISOU 5267  N   ILE B 574    10528  15962  13348   -882  -1259  -3227       N  
ATOM   5268  CA  ILE B 574     -44.437 -96.835   9.166  1.00105.04           C  
ANISOU 5268  CA  ILE B 574    10615  16065  13230  -1011  -1379  -2871       C  
ATOM   5269  C   ILE B 574     -44.236 -95.424   9.727  1.00102.93           C  
ANISOU 5269  C   ILE B 574    10470  15754  12883  -1050  -1308  -2421       C  
ATOM   5270  O   ILE B 574     -44.530 -94.440   9.045  1.00104.16           O  
ANISOU 5270  O   ILE B 574    10674  16126  12775  -1208  -1414  -2158       O  
ATOM   5271  CB  ILE B 574     -45.896 -97.369   9.430  1.00104.84           C  
ANISOU 5271  CB  ILE B 574    10562  15715  13557   -958  -1542  -2806       C  
ATOM   5272  CG1 ILE B 574     -46.630 -96.546  10.494  1.00103.62           C  
ANISOU 5272  CG1 ILE B 574    10475  15245  13648   -908  -1529  -2387       C  
ATOM   5273  CG2 ILE B 574     -45.920 -98.852   9.774  1.00105.13           C  
ANISOU 5273  CG2 ILE B 574    10510  15495  13939   -841  -1584  -3161       C  
ATOM   5274  CD1 ILE B 574     -47.462 -95.365   9.949  1.00105.37           C  
ANISOU 5274  CD1 ILE B 574    10731  15582  13720  -1013  -1674  -2061       C  
ATOM   5275  N   MET B 575     -43.721 -95.334  10.956  1.00100.26           N  
ANISOU 5275  N   MET B 575    10177  15131  12785   -917  -1161  -2335       N  
ATOM   5276  CA  MET B 575     -43.478 -94.048  11.619  1.00 98.15           C  
ANISOU 5276  CA  MET B 575    10012  14781  12500   -924  -1096  -1963       C  
ATOM   5277  C   MET B 575     -42.388 -93.255  10.932  1.00 99.09           C  
ANISOU 5277  C   MET B 575    10171  15276  12201  -1077  -1041  -1901       C  
ATOM   5278  O   MET B 575     -42.568 -92.078  10.644  1.00 99.56           O  
ANISOU 5278  O   MET B 575    10303  15418  12107  -1203  -1142  -1564       O  
ATOM   5279  CB  MET B 575     -43.137 -94.239  13.097  1.00 95.55           C  
ANISOU 5279  CB  MET B 575     9706  14104  12494   -764   -947  -1927       C  
ATOM   5280  CG  MET B 575     -44.350 -94.515  13.981  1.00 94.98           C  
ANISOU 5280  CG  MET B 575     9600  13696  12790   -683  -1001  -1817       C  
ATOM   5281  SD  MET B 575     -43.943 -94.371  15.730  1.00 92.98           S  
ANISOU 5281  SD  MET B 575     9378  13148  12801   -572   -826  -1684       S  
ATOM   5282  CE  MET B 575     -43.682 -92.614  15.893  1.00 90.64           C  
ANISOU 5282  CE  MET B 575     9156  12917  12363   -585   -795  -1383       C  
ATOM   5283  N   LYS B 576     -41.262 -93.910  10.676  1.00 99.99           N  
ANISOU 5283  N   LYS B 576    10219  15617  12154  -1077   -906  -2234       N  
ATOM   5284  CA  LYS B 576     -40.160 -93.335   9.911  1.00101.99           C  
ANISOU 5284  CA  LYS B 576    10459  16338  11953  -1263   -831  -2252       C  
ATOM   5285  C   LYS B 576     -40.621 -92.891   8.512  1.00105.41           C  
ANISOU 5285  C   LYS B 576    10876  17205  11966  -1532   -997  -2151       C  
ATOM   5286  O   LYS B 576     -40.122 -91.903   7.964  1.00106.42           O  
ANISOU 5286  O   LYS B 576    11050  17662  11722  -1771  -1025  -1895       O  
ATOM   5287  CB  LYS B 576     -39.032 -94.376   9.821  1.00103.15           C  
ANISOU 5287  CB  LYS B 576    10467  16668  12057  -1182   -676  -2760       C  
ATOM   5288  CG  LYS B 576     -38.033 -94.197   8.677  1.00106.27           C  
ANISOU 5288  CG  LYS B 576    10748  17715  11915  -1406   -599  -2977       C  
ATOM   5289  CD  LYS B 576     -36.834 -93.370   9.092  1.00104.94           C  
ANISOU 5289  CD  LYS B 576    10615  17676  11581  -1474   -439  -2812       C  
ATOM   5290  CE  LYS B 576     -36.357 -92.516   7.933  1.00107.99           C  
ANISOU 5290  CE  LYS B 576    10968  18704  11358  -1840   -447  -2669       C  
ATOM   5291  NZ  LYS B 576     -37.399 -91.517   7.564  1.00108.18           N1+
ANISOU 5291  NZ  LYS B 576    11148  18667  11288  -2028   -676  -2137       N1+
ATOM   5292  N   ASP B 577     -41.580 -93.629   7.955  1.00107.17           N  
ANISOU 5292  N   ASP B 577    11038  17427  12254  -1518  -1132  -2328       N  
ATOM   5293  CA  ASP B 577     -42.172 -93.313   6.655  1.00111.04           C  
ANISOU 5293  CA  ASP B 577    11512  18306  12372  -1773  -1324  -2232       C  
ATOM   5294  C   ASP B 577     -42.855 -91.940   6.561  1.00111.07           C  
ANISOU 5294  C   ASP B 577    11653  18213  12335  -1926  -1540  -1651       C  
ATOM   5295  O   ASP B 577     -42.534 -91.163   5.655  1.00113.94           O  
ANISOU 5295  O   ASP B 577    12044  18992  12253  -2231  -1648  -1424       O  
ATOM   5296  CB  ASP B 577     -43.147 -94.413   6.218  1.00112.65           C  
ANISOU 5296  CB  ASP B 577    11621  18448  12730  -1693  -1440  -2541       C  
ATOM   5297  CG  ASP B 577     -42.678 -95.169   4.967  1.00117.62           C  
ANISOU 5297  CG  ASP B 577    12088  19657  12942  -1845  -1424  -3015       C  
ATOM   5298  OD1 ASP B 577     -43.535 -95.844   4.352  1.00120.41           O  
ANISOU 5298  OD1 ASP B 577    12374  20051  13325  -1852  -1572  -3213       O  
ATOM   5299  OD2 ASP B 577     -41.476 -95.094   4.596  1.00119.81           O1-
ANISOU 5299  OD2 ASP B 577    12285  20376  12861  -1962  -1266  -3218       O1-
ATOM   5300  N   ILE B 578     -43.785 -91.643   7.475  1.00108.31           N  
ANISOU 5300  N   ILE B 578    11366  17337  12447  -1734  -1626  -1423       N  
ATOM   5301  CA  ILE B 578     -44.474 -90.347   7.448  1.00108.56           C  
ANISOU 5301  CA  ILE B 578    11495  17208  12545  -1827  -1877   -932       C  
ATOM   5302  C   ILE B 578     -43.674 -89.201   8.030  1.00107.15           C  
ANISOU 5302  C   ILE B 578    11414  16935  12362  -1864  -1843   -620       C  
ATOM   5303  O   ILE B 578     -43.697 -88.090   7.509  1.00109.03           O  
ANISOU 5303  O   ILE B 578    11727  17267  12430  -2083  -2078   -232       O  
ATOM   5304  CB  ILE B 578     -45.890 -90.393   8.053  1.00107.56           C  
ANISOU 5304  CB  ILE B 578    11343  16626  12898  -1627  -2021   -854       C  
ATOM   5305  CG1 ILE B 578     -45.896 -91.104   9.415  1.00103.45           C  
ANISOU 5305  CG1 ILE B 578    10779  15733  12791  -1340  -1785  -1069       C  
ATOM   5306  CG2 ILE B 578     -46.875 -91.010   7.007  1.00111.40           C  
ANISOU 5306  CG2 ILE B 578    11759  17286  13280  -1725  -2216   -971       C  
ATOM   5307  CD1 ILE B 578     -47.257 -91.666   9.829  1.00100.66           C  
ANISOU 5307  CD1 ILE B 578    10339  15086  12821  -1193  -1869  -1143       C  
ATOM   5308  N   LEU B 579     -42.932 -89.472   9.085  1.00104.35           N  
ANISOU 5308  N   LEU B 579    11059  16393  12194  -1671  -1582   -775       N  
ATOM   5309  CA  LEU B 579     -42.032 -88.464   9.621  1.00103.67           C  
ANISOU 5309  CA  LEU B 579    11057  16253  12079  -1711  -1527   -528       C  
ATOM   5310  C   LEU B 579     -40.973 -88.021   8.620  1.00107.05           C  
ANISOU 5310  C   LEU B 579    11503  17204  11965  -2042  -1532   -428       C  
ATOM   5311  O   LEU B 579     -40.106 -87.200   8.950  1.00106.89           O  
ANISOU 5311  O   LEU B 579    11547  17197  11870  -2125  -1491   -217       O  
ATOM   5312  CB  LEU B 579     -41.375 -88.962  10.902  1.00100.05           C  
ANISOU 5312  CB  LEU B 579    10584  15545  11883  -1461  -1241   -744       C  
ATOM   5313  CG  LEU B 579     -42.290 -88.932  12.110  1.00 95.94           C  
ANISOU 5313  CG  LEU B 579    10058  14532  11861  -1206  -1247   -701       C  
ATOM   5314  CD1 LEU B 579     -41.477 -89.269  13.305  1.00 92.31           C  
ANISOU 5314  CD1 LEU B 579     9602  13902  11569  -1038   -991   -842       C  
ATOM   5315  CD2 LEU B 579     -42.903 -87.558  12.254  1.00 96.32           C  
ANISOU 5315  CD2 LEU B 579    10158  14368  12070  -1230  -1491   -329       C  
ATOM   5316  N   GLU B 580     -41.047 -88.589   7.413  1.00110.62           N  
ANISOU 5316  N   GLU B 580    11881  18118  12031  -2247  -1578   -597       N  
ATOM   5317  CA  GLU B 580     -40.189 -88.242   6.273  1.00114.81           C  
ANISOU 5317  CA  GLU B 580    12385  19286  11951  -2637  -1596   -524       C  
ATOM   5318  C   GLU B 580     -38.739 -87.916   6.632  1.00114.23           C  
ANISOU 5318  C   GLU B 580    12304  19409  11689  -2709  -1369   -544       C  
ATOM   5319  O   GLU B 580     -38.064 -88.688   7.310  1.00111.83           O  
ANISOU 5319  O   GLU B 580    11923  19030  11535  -2473  -1088   -930       O  
ATOM   5320  CB  GLU B 580     -40.801 -87.077   5.500  1.00118.10           C  
ANISOU 5320  CB  GLU B 580    12904  19777  12189  -2956  -1984     22       C  
ATOM   5321  CG  GLU B 580     -41.988 -87.444   4.650  1.00121.71           C  
ANISOU 5321  CG  GLU B 580    13330  20314  12597  -3028  -2222     11       C  
ATOM   5322  CD  GLU B 580     -42.458 -86.284   3.790  1.00128.12           C  
ANISOU 5322  CD  GLU B 580    14241  21247  13191  -3399  -2653    582       C  
ATOM   5323  OE1 GLU B 580     -41.651 -85.349   3.537  1.00129.99           O  
ANISOU 5323  OE1 GLU B 580    14546  21707  13137  -3708  -2743    942       O  
ATOM   5324  OE2 GLU B 580     -43.640 -86.314   3.361  1.00131.02           O1-
ANISOU 5324  OE2 GLU B 580    14612  21475  13692  -3396  -2932    687       O1-
ATOM   5325  N   LYS B 581     -38.281 -86.755   6.176  1.00116.71           N  
ANISOU 5325  N   LYS B 581    12694  19955  11693  -3051  -1526   -102       N  
ATOM   5326  CA  LYS B 581     -36.925 -86.314   6.431  1.00117.28           C  
ANISOU 5326  CA  LYS B 581    12756  20250  11553  -3179  -1344    -60       C  
ATOM   5327  C   LYS B 581     -36.849 -85.381   7.646  1.00114.37           C  
ANISOU 5327  C   LYS B 581    12531  19285  11639  -2992  -1400    269       C  
ATOM   5328  O   LYS B 581     -36.173 -84.358   7.608  1.00115.64           O  
ANISOU 5328  O   LYS B 581    12760  19536  11639  -3236  -1493    632       O  
ATOM   5329  CB  LYS B 581     -36.329 -85.650   5.180  1.00122.35           C  
ANISOU 5329  CB  LYS B 581    13371  21591  11524  -3731  -1470    218       C  
ATOM   5330  CG  LYS B 581     -35.757 -86.621   4.125  1.00126.43           C  
ANISOU 5330  CG  LYS B 581    13666  22903  11468  -3937  -1256   -275       C  
ATOM   5331  CD  LYS B 581     -34.275 -86.302   3.820  1.00130.25           C  
ANISOU 5331  CD  LYS B 581    14033  24007  11449  -4257  -1053   -313       C  
ATOM   5332  CE  LYS B 581     -33.367 -86.658   5.035  1.00126.68           C  
ANISOU 5332  CE  LYS B 581    13539  23227  11367  -3880   -738   -632       C  
ATOM   5333  NZ  LYS B 581     -32.130 -85.833   5.186  1.00126.93           N1+
ANISOU 5333  NZ  LYS B 581    13560  23522  11142  -4136   -644   -403       N1+
ATOM   5334  N   LYS B 582     -37.544 -85.734   8.723  1.00111.01           N  
ANISOU 5334  N   LYS B 582    12134  18275  11767  -2583  -1352    133       N  
ATOM   5335  CA  LYS B 582     -37.456 -84.982   9.973  1.00108.62           C  
ANISOU 5335  CA  LYS B 582    11926  17448  11894  -2372  -1359    332       C  
ATOM   5336  C   LYS B 582     -36.557 -85.732  10.965  1.00105.78           C  
ANISOU 5336  C   LYS B 582    11509  17008  11673  -2115   -995    -39       C  
ATOM   5337  O   LYS B 582     -36.010 -85.154  11.913  1.00104.03           O  
ANISOU 5337  O   LYS B 582    11344  16526  11654  -2011   -927     74       O  
ATOM   5338  CB  LYS B 582     -38.850 -84.767  10.584  1.00107.11           C  
ANISOU 5338  CB  LYS B 582    11774  16707  12213  -2118  -1559    435       C  
ATOM   5339  CG  LYS B 582     -39.764 -83.785   9.834  1.00110.92           C  
ANISOU 5339  CG  LYS B 582    12321  17115  12709  -2321  -1999    860       C  
ATOM   5340  CD  LYS B 582     -41.194 -83.763  10.445  1.00111.55           C  
ANISOU 5340  CD  LYS B 582    12373  16689  13319  -2025  -2162    836       C  
ATOM   5341  CE  LYS B 582     -42.284 -83.354   9.420  1.00115.16           C  
ANISOU 5341  CE  LYS B 582    12839  17165  13749  -2203  -2578   1098       C  
ATOM   5342  NZ  LYS B 582     -43.683 -83.602   9.895  1.00112.74           N1+
ANISOU 5342  NZ  LYS B 582    12452  16472  13911  -1915  -2685    967       N1+
ATOM   5343  N   VAL B 583     -36.409 -87.026  10.721  1.00105.82           N  
ANISOU 5343  N   VAL B 583    11394  17226  11586  -2019   -796   -491       N  
ATOM   5344  CA  VAL B 583     -35.766 -87.948  11.638  1.00103.34           C  
ANISOU 5344  CA  VAL B 583    11013  16762  11487  -1748   -523   -870       C  
ATOM   5345  C   VAL B 583     -34.922 -88.878  10.770  1.00105.93           C  
ANISOU 5345  C   VAL B 583    11175  17623  11448  -1856   -364  -1300       C  
ATOM   5346  O   VAL B 583     -35.286 -89.157   9.638  1.00108.87           O  
ANISOU 5346  O   VAL B 583    11475  18371  11516  -2040   -451  -1396       O  
ATOM   5347  CB  VAL B 583     -36.849 -88.753  12.418  1.00100.86           C  
ANISOU 5347  CB  VAL B 583    10698  15989  11633  -1443   -532  -1024       C  
ATOM   5348  CG1 VAL B 583     -36.242 -89.794  13.287  1.00 99.02           C  
ANISOU 5348  CG1 VAL B 583    10400  15596  11624  -1210   -319  -1376       C  
ATOM   5349  CG2 VAL B 583     -37.678 -87.840  13.281  1.00 98.98           C  
ANISOU 5349  CG2 VAL B 583    10564  15300  11741  -1334   -668   -684       C  
ATOM   5350  N   GLU B 584     -33.786 -89.340  11.274  1.00105.65           N  
ANISOU 5350  N   GLU B 584    11055  17648  11437  -1746   -143  -1587       N  
ATOM   5351  CA  GLU B 584     -33.009 -90.315  10.534  1.00108.68           C  
ANISOU 5351  CA  GLU B 584    11227  18507  11556  -1787     -1  -2105       C  
ATOM   5352  C   GLU B 584     -33.589 -91.711  10.739  1.00107.75           C  
ANISOU 5352  C   GLU B 584    11025  18130  11781  -1507     -7  -2533       C  
ATOM   5353  O   GLU B 584     -33.902 -92.402   9.776  1.00110.95           O  
ANISOU 5353  O   GLU B 584    11302  18844  12006  -1573    -54  -2844       O  
ATOM   5354  CB  GLU B 584     -31.524 -90.263  10.899  1.00109.01           C  
ANISOU 5354  CB  GLU B 584    11173  18745  11501  -1786    205  -2283       C  
ATOM   5355  CG  GLU B 584     -30.636 -90.501   9.668  1.00116.38           C  
ANISOU 5355  CG  GLU B 584    11871  20459  11889  -2052    313  -2633       C  
ATOM   5356  CD  GLU B 584     -29.167 -90.864   9.985  1.00120.84           C  
ANISOU 5356  CD  GLU B 584    12245  21244  12422  -1977    536  -3026       C  
ATOM   5357  OE1 GLU B 584     -28.622 -90.484  11.063  1.00118.69           O  
ANISOU 5357  OE1 GLU B 584    12069  20611  12417  -1836    600  -2851       O  
ATOM   5358  OE2 GLU B 584     -28.555 -91.532   9.114  1.00125.43           O1-
ANISOU 5358  OE2 GLU B 584    12555  22402  12700  -2064    640  -3547       O1-
ATOM   5359  N   LYS B 585     -33.748 -92.114  11.992  1.00104.23           N  
ANISOU 5359  N   LYS B 585    10650  17127  11825  -1222     16  -2534       N  
ATOM   5360  CA  LYS B 585     -34.266 -93.438  12.333  1.00103.27           C  
ANISOU 5360  CA  LYS B 585    10462  16690  12083   -982    -31  -2872       C  
ATOM   5361  C   LYS B 585     -35.444 -93.325  13.283  1.00 99.39           C  
ANISOU 5361  C   LYS B 585    10125  15658  11981   -853   -134  -2547       C  
ATOM   5362  O   LYS B 585     -35.584 -92.335  13.988  1.00 97.17           O  
ANISOU 5362  O   LYS B 585     9976  15180  11763   -864   -123  -2158       O  
ATOM   5363  CB  LYS B 585     -33.177 -94.283  13.023  1.00103.35           C  
ANISOU 5363  CB  LYS B 585    10361  16567  12337   -782     74  -3244       C  
ATOM   5364  CG  LYS B 585     -32.282 -95.113  12.095  1.00108.79           C  
ANISOU 5364  CG  LYS B 585    10794  17707  12833   -792    127  -3844       C  
ATOM   5365  CD  LYS B 585     -32.374 -96.609  12.469  1.00112.73           C  
ANISOU 5365  CD  LYS B 585    11176  17842  13812   -524     13  -4296       C  
ATOM   5366  CE  LYS B 585     -31.336 -97.471  11.762  1.00118.08           C  
ANISOU 5366  CE  LYS B 585    11555  18888  14421   -460     47  -4985       C  
ATOM   5367  NZ  LYS B 585     -29.966 -97.278  12.352  1.00120.22           N1+
ANISOU 5367  NZ  LYS B 585    11748  19200  14727   -389    183  -5093       N1+
ATOM   5368  N   VAL B 586     -36.282 -94.349  13.321  1.00 98.51           N  
ANISOU 5368  N   VAL B 586     9971  15318  12138   -736   -239  -2734       N  
ATOM   5369  CA  VAL B 586     -37.232 -94.483  14.415  1.00 95.10           C  
ANISOU 5369  CA  VAL B 586     9634  14395  12104   -610   -302  -2504       C  
ATOM   5370  C   VAL B 586     -36.942 -95.825  15.053  1.00 94.54           C  
ANISOU 5370  C   VAL B 586     9488  14039  12391   -442   -327  -2809       C  
ATOM   5371  O   VAL B 586     -37.222 -96.854  14.455  1.00 96.81           O  
ANISOU 5371  O   VAL B 586     9671  14343  12769   -409   -440  -3135       O  
ATOM   5372  CB  VAL B 586     -38.698 -94.414  13.935  1.00 95.64           C  
ANISOU 5372  CB  VAL B 586     9723  14415  12198   -669   -458  -2357       C  
ATOM   5373  CG1 VAL B 586     -39.649 -94.863  15.046  1.00 94.37           C  
ANISOU 5373  CG1 VAL B 586     9593  13809  12454   -551   -509  -2231       C  
ATOM   5374  CG2 VAL B 586     -39.053 -93.005  13.466  1.00 95.30           C  
ANISOU 5374  CG2 VAL B 586     9766  14549  11895   -826   -506  -1989       C  
ATOM   5375  N   VAL B 587     -36.347 -95.823  16.243  1.00 91.99           N  
ANISOU 5375  N   VAL B 587     9215  13451  12284   -347   -255  -2709       N  
ATOM   5376  CA  VAL B 587     -35.966 -97.080  16.908  1.00 91.61           C  
ANISOU 5376  CA  VAL B 587     9105  13094  12606   -212   -337  -2950       C  
ATOM   5377  C   VAL B 587     -36.848 -97.367  18.133  1.00 89.63           C  
ANISOU 5377  C   VAL B 587     8939  12424  12691   -195   -412  -2660       C  
ATOM   5378  O   VAL B 587     -37.597 -96.506  18.588  1.00 88.16           O  
ANISOU 5378  O   VAL B 587     8839  12211  12445   -255   -353  -2320       O  
ATOM   5379  CB  VAL B 587     -34.447 -97.128  17.277  1.00 91.54           C  
ANISOU 5379  CB  VAL B 587     9047  13129  12603   -133   -242  -3129       C  
ATOM   5380  CG1 VAL B 587     -33.571 -96.836  16.053  1.00 93.49           C  
ANISOU 5380  CG1 VAL B 587     9166  13885  12468   -193   -143  -3438       C  
ATOM   5381  CG2 VAL B 587     -34.120 -96.166  18.397  1.00 88.51           C  
ANISOU 5381  CG2 VAL B 587     8797  12622  12209   -146   -112  -2749       C  
ATOM   5382  N   VAL B 588     -36.785 -98.585  18.650  1.00 90.03           N  
ANISOU 5382  N   VAL B 588     8944  12163  13099   -130   -568  -2806       N  
ATOM   5383  CA  VAL B 588     -37.428 -98.885  19.930  1.00 88.20           C  
ANISOU 5383  CA  VAL B 588     8781  11586  13143   -173   -638  -2500       C  
ATOM   5384  C   VAL B 588     -36.472 -98.434  21.052  1.00 86.30           C  
ANISOU 5384  C   VAL B 588     8609  11260  12920   -150   -526  -2328       C  
ATOM   5385  O   VAL B 588     -35.258 -98.668  20.985  1.00 86.19           O  
ANISOU 5385  O   VAL B 588     8555  11257  12936    -60   -523  -2547       O  
ATOM   5386  CB  VAL B 588     -37.804-100.387  20.048  1.00 90.33           C  
ANISOU 5386  CB  VAL B 588     8985  11527  13807   -170   -915  -2653       C  
ATOM   5387  CG1 VAL B 588     -38.605-100.651  21.317  1.00 88.70           C  
ANISOU 5387  CG1 VAL B 588     8840  11048  13814   -299   -990  -2276       C  
ATOM   5388  CG2 VAL B 588     -38.580-100.831  18.816  1.00 91.50           C  
ANISOU 5388  CG2 VAL B 588     9051  11792  13923   -175  -1025  -2899       C  
ATOM   5389  N   SER B 589     -37.016 -97.761  22.060  1.00 84.28           N  
ANISOU 5389  N   SER B 589     8432  10952  12638   -229   -432  -1971       N  
ATOM   5390  CA  SER B 589     -36.173 -97.167  23.080  1.00 82.84           C  
ANISOU 5390  CA  SER B 589     8315  10743  12418   -218   -308  -1807       C  
ATOM   5391  C   SER B 589     -35.713 -98.188  24.091  1.00 83.60           C  
ANISOU 5391  C   SER B 589     8415  10536  12813   -238   -463  -1766       C  
ATOM   5392  O   SER B 589     -36.353 -99.236  24.267  1.00 85.40           O  
ANISOU 5392  O   SER B 589     8612  10544  13290   -309   -672  -1746       O  
ATOM   5393  CB  SER B 589     -36.894 -96.042  23.808  1.00 81.10           C  
ANISOU 5393  CB  SER B 589     8144  10607  12061   -289   -158  -1500       C  
ATOM   5394  OG  SER B 589     -35.978 -95.320  24.627  1.00 80.05           O  
ANISOU 5394  OG  SER B 589     8068  10496  11849   -266    -27  -1391       O  
ATOM   5395  N   ASN B 590     -34.596 -97.879  24.749  1.00 82.19           N  
ANISOU 5395  N   ASN B 590     8274  10336  12619   -194   -394  -1732       N  
ATOM   5396  CA  ASN B 590     -34.186 -98.646  25.916  1.00 82.28           C  
ANISOU 5396  CA  ASN B 590     8310  10064  12887   -251   -552  -1593       C  
ATOM   5397  C   ASN B 590     -33.972 -97.775  27.171  1.00 80.24           C  
ANISOU 5397  C   ASN B 590     8131   9870  12485   -333   -390  -1289       C  
ATOM   5398  O   ASN B 590     -33.474 -98.257  28.187  1.00 80.51           O  
ANISOU 5398  O   ASN B 590     8196   9722  12672   -402   -507  -1144       O  
ATOM   5399  CB  ASN B 590     -32.964 -99.491  25.591  1.00 83.86           C  
ANISOU 5399  CB  ASN B 590     8445  10096  13321   -113   -728  -1903       C  
ATOM   5400  CG  ASN B 590     -31.685 -98.705  25.656  1.00 82.80           C  
ANISOU 5400  CG  ASN B 590     8315  10123  13020    -11   -551  -1992       C  
ATOM   5401  OD1 ASN B 590     -31.571 -97.615  25.096  1.00 82.33           O  
ANISOU 5401  OD1 ASN B 590     8267  10374  12640     12   -312  -2017       O  
ATOM   5402  ND2 ASN B 590     -30.708 -99.254  26.341  1.00 83.94           N  
ANISOU 5402  ND2 ASN B 590     8447  10045  13399     32   -700  -2022       N  
ATOM   5403  N   ARG B 591     -34.392 -96.509  27.099  1.00 78.30           N  
ANISOU 5403  N   ARG B 591     7908   9875  11965   -335   -155  -1197       N  
ATOM   5404  CA  ARG B 591     -34.217 -95.563  28.201  1.00 76.90           C  
ANISOU 5404  CA  ARG B 591     7780   9791  11648   -388      5   -982       C  
ATOM   5405  C   ARG B 591     -35.492 -94.944  28.824  1.00 77.21           C  
ANISOU 5405  C   ARG B 591     7787   9965  11581   -507    109   -793       C  
ATOM   5406  O   ARG B 591     -35.378 -94.060  29.694  1.00 76.23           O  
ANISOU 5406  O   ARG B 591     7673   9957  11334   -534    251   -682       O  
ATOM   5407  CB  ARG B 591     -33.285 -94.449  27.762  1.00 75.06           C  
ANISOU 5407  CB  ARG B 591     7577   9718  11224   -266    172  -1077       C  
ATOM   5408  CG  ARG B 591     -33.905 -93.475  26.806  1.00 74.44           C  
ANISOU 5408  CG  ARG B 591     7488   9833  10962   -231    272  -1113       C  
ATOM   5409  CD  ARG B 591     -32.866 -92.560  26.182  1.00 71.71           C  
ANISOU 5409  CD  ARG B 591     7169   9639  10435   -160    375  -1193       C  
ATOM   5410  NE  ARG B 591     -32.264 -93.117  24.978  1.00 70.26           N  
ANISOU 5410  NE  ARG B 591     6936   9545  10214   -113    323  -1442       N  
ATOM   5411  CZ  ARG B 591     -30.972 -93.010  24.698  1.00 71.54           C  
ANISOU 5411  CZ  ARG B 591     7075   9806  10298    -68    372  -1586       C  
ATOM   5412  NH1 ARG B 591     -30.163 -92.389  25.544  1.00 71.47           N1+
ANISOU 5412  NH1 ARG B 591     7114   9775  10264    -59    459  -1472       N1+
ATOM   5413  NH2 ARG B 591     -30.477 -93.523  23.584  1.00 73.31           N  
ANISOU 5413  NH2 ARG B 591     7207  10184  10463    -37    339  -1873       N  
ATOM   5414  N   LEU B 592     -36.680 -95.414  28.408  1.00 78.67           N  
ANISOU 5414  N   LEU B 592     7911  10150  11828   -574     32   -791       N  
ATOM   5415  CA  LEU B 592     -37.968 -94.802  28.810  1.00 78.77           C  
ANISOU 5415  CA  LEU B 592     7842  10333  11752   -664    131   -688       C  
ATOM   5416  C   LEU B 592     -38.812 -95.689  29.728  1.00 80.85           C  
ANISOU 5416  C   LEU B 592     8036  10582  12099   -898     41   -512       C  
ATOM   5417  O   LEU B 592     -38.889 -96.888  29.509  1.00 83.01           O  
ANISOU 5417  O   LEU B 592     8320  10666  12552   -979   -163   -487       O  
ATOM   5418  CB  LEU B 592     -38.786 -94.473  27.561  1.00 78.43           C  
ANISOU 5418  CB  LEU B 592     7757  10358  11684   -579    119   -815       C  
ATOM   5419  CG  LEU B 592     -38.126 -93.650  26.459  1.00 76.55           C  
ANISOU 5419  CG  LEU B 592     7575  10182  11325   -419    166   -948       C  
ATOM   5420  CD1 LEU B 592     -38.998 -93.658  25.227  1.00 76.67           C  
ANISOU 5420  CD1 LEU B 592     7549  10255  11325   -395     87  -1038       C  
ATOM   5421  CD2 LEU B 592     -37.898 -92.242  26.919  1.00 74.86           C  
ANISOU 5421  CD2 LEU B 592     7374  10079  10990   -366    307   -884       C  
ATOM   5422  N   VAL B 593     -39.449 -95.125  30.748  1.00 81.26           N  
ANISOU 5422  N   VAL B 593     7997  10848  12027  -1028    173   -400       N  
ATOM   5423  CA  VAL B 593     -40.463 -95.900  31.471  1.00 84.20           C  
ANISOU 5423  CA  VAL B 593     8263  11307  12423  -1303    103   -234       C  
ATOM   5424  C   VAL B 593     -41.869 -95.318  31.359  1.00 84.96           C  
ANISOU 5424  C   VAL B 593     8180  11652  12447  -1332    217   -311       C  
ATOM   5425  O   VAL B 593     -42.780 -96.012  30.926  1.00 87.09           O  
ANISOU 5425  O   VAL B 593     8382  11896  12812  -1430    106   -292       O  
ATOM   5426  CB  VAL B 593     -40.109 -96.224  32.950  1.00 85.30           C  
ANISOU 5426  CB  VAL B 593     8397  11539  12474  -1559    100     -1       C  
ATOM   5427  CG1 VAL B 593     -38.942 -97.159  33.006  1.00 86.86           C  
ANISOU 5427  CG1 VAL B 593     8746  11417  12839  -1570   -119    103       C  
ATOM   5428  CG2 VAL B 593     -39.793 -94.979  33.743  1.00 85.85           C  
ANISOU 5428  CG2 VAL B 593     8423  11862  12331  -1504    338    -58       C  
ATOM   5429  N   THR B 594     -42.047 -94.053  31.718  1.00 84.06           N  
ANISOU 5429  N   THR B 594     7977  11759  12203  -1233    410   -424       N  
ATOM   5430  CA  THR B 594     -43.365 -93.449  31.696  1.00 85.17           C  
ANISOU 5430  CA  THR B 594     7904  12134  12319  -1237    496   -548       C  
ATOM   5431  C   THR B 594     -43.589 -92.600  30.450  1.00 84.75           C  
ANISOU 5431  C   THR B 594     7867  11983  12351   -965    471   -728       C  
ATOM   5432  O   THR B 594     -44.734 -92.422  30.005  1.00 85.96           O  
ANISOU 5432  O   THR B 594     7870  12220  12568   -947    444   -823       O  
ATOM   5433  CB  THR B 594     -43.610 -92.591  32.940  1.00 85.50           C  
ANISOU 5433  CB  THR B 594     7770  12509  12207  -1310    688   -618       C  
ATOM   5434  OG1 THR B 594     -42.626 -91.567  33.000  1.00 84.45           O  
ANISOU 5434  OG1 THR B 594     7734  12307  12044  -1100    763   -711       O  
ATOM   5435  CG2 THR B 594     -43.497 -93.417  34.192  1.00 87.00           C  
ANISOU 5435  CG2 THR B 594     7925  12876  12253  -1649    702   -404       C  
ATOM   5436  N   SER B 595     -42.501 -92.060  29.901  1.00 83.58           N  
ANISOU 5436  N   SER B 595     7887  11673  12194   -777    464   -759       N  
ATOM   5437  CA  SER B 595     -42.586 -91.174  28.747  1.00 83.46           C  
ANISOU 5437  CA  SER B 595     7903  11585  12221   -572    410   -869       C  
ATOM   5438  C   SER B 595     -42.736 -92.037  27.516  1.00 83.77           C  
ANISOU 5438  C   SER B 595     8021  11493  12315   -571    262   -866       C  
ATOM   5439  O   SER B 595     -41.988 -92.987  27.348  1.00 84.11           O  
ANISOU 5439  O   SER B 595     8178  11412  12366   -615    205   -825       O  
ATOM   5440  CB  SER B 595     -41.341 -90.306  28.642  1.00 82.00           C  
ANISOU 5440  CB  SER B 595     7859  11324  11974   -436    451   -872       C  
ATOM   5441  OG  SER B 595     -41.681 -88.969  28.317  1.00 83.88           O  
ANISOU 5441  OG  SER B 595     8036  11578  12255   -295    428   -955       O  
ATOM   5442  N   PRO B 596     -43.704 -91.720  26.652  1.00 84.55           N  
ANISOU 5442  N   PRO B 596     8040  11614  12469   -514    177   -934       N  
ATOM   5443  CA  PRO B 596     -44.039 -92.587  25.530  1.00 85.38           C  
ANISOU 5443  CA  PRO B 596     8184  11639  12615   -537     33   -957       C  
ATOM   5444  C   PRO B 596     -42.959 -92.663  24.465  1.00 85.08           C  
ANISOU 5444  C   PRO B 596     8313  11520  12491   -454    -25   -997       C  
ATOM   5445  O   PRO B 596     -42.797 -93.692  23.842  1.00 85.82           O  
ANISOU 5445  O   PRO B 596     8449  11545  12612   -488   -119  -1057       O  
ATOM   5446  CB  PRO B 596     -45.291 -91.935  24.948  1.00 86.25           C  
ANISOU 5446  CB  PRO B 596     8159  11821  12791   -485    -43  -1018       C  
ATOM   5447  CG  PRO B 596     -45.151 -90.546  25.280  1.00 86.03           C  
ANISOU 5447  CG  PRO B 596     8095  11830  12760   -366      6  -1041       C  
ATOM   5448  CD  PRO B 596     -44.481 -90.477  26.623  1.00 85.17           C  
ANISOU 5448  CD  PRO B 596     7983  11774  12601   -409    175  -1016       C  
ATOM   5449  N   CYS B 597     -42.243 -91.571  24.247  1.00 85.13           N  
ANISOU 5449  N   CYS B 597     8391  11555  12398   -358     16   -983       N  
ATOM   5450  CA  CYS B 597     -41.153 -91.527  23.277  1.00 85.64           C  
ANISOU 5450  CA  CYS B 597     8583  11630  12323   -320    -12  -1021       C  
ATOM   5451  C   CYS B 597     -40.212 -90.404  23.663  1.00 84.35           C  
ANISOU 5451  C   CYS B 597     8488  11486  12074   -266     74   -952       C  
ATOM   5452  O   CYS B 597     -40.465 -89.697  24.637  1.00 83.88           O  
ANISOU 5452  O   CYS B 597     8376  11410  12085   -238    139   -903       O  
ATOM   5453  CB  CYS B 597     -41.684 -91.346  21.849  1.00 86.72           C  
ANISOU 5453  CB  CYS B 597     8718  11846  12383   -325   -153  -1055       C  
ATOM   5454  SG  CYS B 597     -42.773 -89.928  21.616  1.00 91.83           S  
ANISOU 5454  SG  CYS B 597     9292  12507  13089   -284   -264   -950       S  
ATOM   5455  N   CYS B 598     -39.116 -90.271  22.925  1.00 84.82           N  
ANISOU 5455  N   CYS B 598     8642  11606  11977   -263     75   -973       N  
ATOM   5456  CA  CYS B 598     -38.179 -89.155  23.087  1.00 85.03           C  
ANISOU 5456  CA  CYS B 598     8737  11661  11905   -241    128   -886       C  
ATOM   5457  C   CYS B 598     -37.307 -89.003  21.843  1.00 85.90           C  
ANISOU 5457  C   CYS B 598     8912  11934  11790   -300     89   -905       C  
ATOM   5458  O   CYS B 598     -37.262 -89.894  20.987  1.00 86.45           O  
ANISOU 5458  O   CYS B 598     8962  12108  11777   -337     55  -1045       O  
ATOM   5459  CB  CYS B 598     -37.297 -89.328  24.337  1.00 83.79           C  
ANISOU 5459  CB  CYS B 598     8607  11436  11793   -213    267   -888       C  
ATOM   5460  SG  CYS B 598     -35.889 -90.468  24.140  1.00 85.99           S  
ANISOU 5460  SG  CYS B 598     8934  11729  12007   -220    314  -1024       S  
ATOM   5461  N   ILE B 599     -36.625 -87.866  21.752  1.00 86.34           N  
ANISOU 5461  N   ILE B 599     9025  12037  11740   -328     86   -777       N  
ATOM   5462  CA  ILE B 599     -35.696 -87.635  20.666  1.00 88.11           C  
ANISOU 5462  CA  ILE B 599     9292  12487  11697   -442     68   -767       C  
ATOM   5463  C   ILE B 599     -34.277 -87.708  21.176  1.00 88.23           C  
ANISOU 5463  C   ILE B 599     9332  12547  11642   -430    216   -827       C  
ATOM   5464  O   ILE B 599     -33.938 -87.072  22.171  1.00 87.25           O  
ANISOU 5464  O   ILE B 599     9243  12284  11622   -376    270   -732       O  
ATOM   5465  CB  ILE B 599     -35.965 -86.304  19.924  1.00 89.25           C  
ANISOU 5465  CB  ILE B 599     9480  12687  11743   -554   -108   -526       C  
ATOM   5466  CG1 ILE B 599     -37.214 -86.463  19.053  1.00 89.93           C  
ANISOU 5466  CG1 ILE B 599     9529  12800  11839   -595   -281   -503       C  
ATOM   5467  CG2 ILE B 599     -34.752 -85.898  19.073  1.00 90.16           C  
ANISOU 5467  CG2 ILE B 599     9635  13080  11538   -732    -97   -459       C  
ATOM   5468  CD1 ILE B 599     -37.417 -85.396  18.037  1.00 90.65           C  
ANISOU 5468  CD1 ILE B 599     9664  12986  11792   -759   -514   -257       C  
ATOM   5469  N   VAL B 600     -33.458 -88.502  20.491  1.00 90.34           N  
ANISOU 5469  N   VAL B 600     9558  13021  11744   -473    275  -1024       N  
ATOM   5470  CA  VAL B 600     -32.025 -88.565  20.763  1.00 91.40           C  
ANISOU 5470  CA  VAL B 600     9683  13251  11793   -472    399  -1120       C  
ATOM   5471  C   VAL B 600     -31.265 -88.114  19.520  1.00 94.68           C  
ANISOU 5471  C   VAL B 600    10064  14051  11857   -654    400  -1132       C  
ATOM   5472  O   VAL B 600     -31.815 -88.123  18.418  1.00 96.64           O  
ANISOU 5472  O   VAL B 600    10286  14506  11925   -774    309  -1130       O  
ATOM   5473  CB  VAL B 600     -31.579 -89.976  21.181  1.00 90.71           C  
ANISOU 5473  CB  VAL B 600     9524  13078  11863   -354    454  -1406       C  
ATOM   5474  CG1 VAL B 600     -32.441 -90.488  22.299  1.00 89.65           C  
ANISOU 5474  CG1 VAL B 600     9416  12622  12022   -254    422  -1343       C  
ATOM   5475  CG2 VAL B 600     -31.660 -90.928  20.025  1.00 92.95           C  
ANISOU 5475  CG2 VAL B 600     9703  13565  12048   -379    406  -1689       C  
ATOM   5476  N   THR B 601     -30.013 -87.712  19.712  1.00 96.33           N  
ANISOU 5476  N   THR B 601    10263  14386  11949   -701    499  -1133       N  
ATOM   5477  CA  THR B 601     -29.157 -87.231  18.635  1.00100.19           C  
ANISOU 5477  CA  THR B 601    10695  15306  12064   -925    522  -1129       C  
ATOM   5478  C   THR B 601     -27.946 -88.131  18.485  1.00102.75           C  
ANISOU 5478  C   THR B 601    10864  15871  12302   -886    671  -1511       C  
ATOM   5479  O   THR B 601     -27.480 -88.726  19.462  1.00101.00           O  
ANISOU 5479  O   THR B 601    10626  15407  12339   -695    736  -1662       O  
ATOM   5480  CB  THR B 601     -28.670 -85.779  18.880  1.00 99.93           C  
ANISOU 5480  CB  THR B 601    10758  15264  11947  -1069    482   -776       C  
ATOM   5481  OG1 THR B 601     -28.295 -85.602  20.258  1.00 98.25           O  
ANISOU 5481  OG1 THR B 601    10600  14723  12006   -894    552   -745       O  
ATOM   5482  CG2 THR B 601     -29.749 -84.783  18.533  1.00 99.95           C  
ANISOU 5482  CG2 THR B 601    10864  15141  11968  -1174    264   -430       C  
ATOM   5483  N   SER B 602     -27.438 -88.196  17.253  1.00108.08           N  
ANISOU 5483  N   SER B 602    11408  17047  12607  -1084    705  -1670       N  
ATOM   5484  CA  SER B 602     -26.336 -89.079  16.831  1.00112.27           C  
ANISOU 5484  CA  SER B 602    11717  17921  13017  -1062    836  -2139       C  
ATOM   5485  C   SER B 602     -25.011 -88.839  17.563  1.00113.64           C  
ANISOU 5485  C   SER B 602    11842  18095  13238  -1019    959  -2189       C  
ATOM   5486  O   SER B 602     -24.702 -87.700  17.935  1.00113.05           O  
ANISOU 5486  O   SER B 602    11883  17982  13086  -1144    964  -1827       O  
ATOM   5487  CB  SER B 602     -26.120 -88.932  15.327  1.00115.62           C  
ANISOU 5487  CB  SER B 602    11995  18991  12944  -1356    858  -2256       C  
ATOM   5488  OG  SER B 602     -25.782 -87.591  15.009  1.00115.99           O  
ANISOU 5488  OG  SER B 602    12120  19277  12671  -1663    839  -1838       O  
ATOM   5489  N   THR B 603     -24.244 -89.924  17.746  1.00117.03           N  
ANISOU 5489  N   THR B 603    12088  18548  13828   -838   1025  -2654       N  
ATOM   5490  CA  THR B 603     -22.946 -89.950  18.480  1.00119.11           C  
ANISOU 5490  CA  THR B 603    12265  18782  14206   -747   1120  -2791       C  
ATOM   5491  C   THR B 603     -22.032 -88.767  18.161  1.00121.61           C  
ANISOU 5491  C   THR B 603    12557  19494  14153  -1017   1228  -2582       C  
ATOM   5492  O   THR B 603     -21.488 -88.113  19.063  1.00119.68           O  
ANISOU 5492  O   THR B 603    12411  19040  14020   -997   1255  -2349       O  
ATOM   5493  CB  THR B 603     -22.157 -91.282  18.230  1.00121.54           C  
ANISOU 5493  CB  THR B 603    12289  19229  14662   -568   1141  -3427       C  
ATOM   5494  OG1 THR B 603     -22.406 -91.764  16.895  1.00124.03           O  
ANISOU 5494  OG1 THR B 603    12414  20005  14704   -674   1151  -3772       O  
ATOM   5495  CG2 THR B 603     -22.559 -92.349  19.256  1.00120.63           C  
ANISOU 5495  CG2 THR B 603    12234  18507  15089   -262    990  -3532       C  
ATOM   5496  N   TYR B 604     -21.865 -88.535  16.861  1.00126.91           N  
ANISOU 5496  N   TYR B 604    13085  20762  14371  -1294   1279  -2672       N  
ATOM   5497  CA  TYR B 604     -21.290 -87.314  16.320  1.00130.63           C  
ANISOU 5497  CA  TYR B 604    13557  21660  14414  -1662   1326  -2355       C  
ATOM   5498  C   TYR B 604     -22.465 -86.406  15.958  1.00131.04           C  
ANISOU 5498  C   TYR B 604    13845  21594  14350  -1857   1156  -1833       C  
ATOM   5499  O   TYR B 604     -23.452 -86.859  15.364  1.00131.81           O  
ANISOU 5499  O   TYR B 604    13958  21702  14419  -1844   1071  -1893       O  
ATOM   5500  CB  TYR B 604     -20.425 -87.632  15.079  1.00135.48           C  
ANISOU 5500  CB  TYR B 604    13844  23078  14555  -1907   1467  -2763       C  
ATOM   5501  CG  TYR B 604     -21.190 -88.103  13.828  1.00140.03           C  
ANISOU 5501  CG  TYR B 604    14321  24050  14833  -2051   1428  -2948       C  
ATOM   5502  CD1 TYR B 604     -20.780 -87.701  12.550  1.00145.74           C  
ANISOU 5502  CD1 TYR B 604    14857  25578  14938  -2482   1499  -2979       C  
ATOM   5503  CD2 TYR B 604     -22.319 -88.951  13.925  1.00139.20           C  
ANISOU 5503  CD2 TYR B 604    14300  23549  15041  -1789   1313  -3083       C  
ATOM   5504  CE1 TYR B 604     -21.465 -88.128  11.402  1.00149.78           C  
ANISOU 5504  CE1 TYR B 604    15269  26498  15141  -2636   1459  -3158       C  
ATOM   5505  CE2 TYR B 604     -23.017 -89.372  12.790  1.00142.62           C  
ANISOU 5505  CE2 TYR B 604    14641  24340  15205  -1921   1266  -3260       C  
ATOM   5506  CZ  TYR B 604     -22.584 -88.961  11.531  1.00148.51           C  
ANISOU 5506  CZ  TYR B 604    15203  25893  15328  -2337   1341  -3307       C  
ATOM   5507  OH  TYR B 604     -23.263 -89.376  10.400  1.00152.01           O  
ANISOU 5507  OH  TYR B 604    15549  26735  15471  -2488   1291  -3491       O  
ATOM   5508  N   GLY B 605     -22.384 -85.137  16.328  1.00131.21           N  
ANISOU 5508  N   GLY B 605    14041  21467  14346  -2023   1072  -1336       N  
ATOM   5509  CA  GLY B 605     -23.412 -84.196  15.913  1.00133.15           C  
ANISOU 5509  CA  GLY B 605    14479  21601  14511  -2224    853   -850       C  
ATOM   5510  C   GLY B 605     -23.628 -83.117  16.935  1.00131.90           C  
ANISOU 5510  C   GLY B 605    14541  20917  14658  -2160    715   -423       C  
ATOM   5511  O   GLY B 605     -22.774 -82.881  17.780  1.00130.77           O  
ANISOU 5511  O   GLY B 605    14398  20637  14652  -2073    805   -437       O  
ATOM   5512  N   TRP B 606     -24.782 -82.466  16.852  1.00132.84           N  
ANISOU 5512  N   TRP B 606    14828  20744  14900  -2193    481    -76       N  
ATOM   5513  CA  TRP B 606     -25.127 -81.364  17.739  1.00132.46           C  
ANISOU 5513  CA  TRP B 606    14960  20194  15173  -2127    302    288       C  
ATOM   5514  C   TRP B 606     -26.275 -81.803  18.648  1.00129.80           C  
ANISOU 5514  C   TRP B 606    14705  19340  15271  -1759    272    182       C  
ATOM   5515  O   TRP B 606     -27.227 -82.417  18.163  1.00130.30           O  
ANISOU 5515  O   TRP B 606    14754  19414  15339  -1701    229     82       O  
ATOM   5516  CB  TRP B 606     -25.568 -80.161  16.898  1.00135.60           C  
ANISOU 5516  CB  TRP B 606    15456  20656  15410  -2477     -9    773       C  
ATOM   5517  CG  TRP B 606     -24.598 -79.734  15.811  1.00141.31           C  
ANISOU 5517  CG  TRP B 606    16090  21987  15615  -2946    -15    945       C  
ATOM   5518  CD1 TRP B 606     -23.643 -78.759  15.910  1.00144.44           C  
ANISOU 5518  CD1 TRP B 606    16504  22471  15904  -3206    -80   1233       C  
ATOM   5519  CD2 TRP B 606     -24.505 -80.248  14.462  1.00146.12           C  
ANISOU 5519  CD2 TRP B 606    16557  23243  15716  -3248     39    842       C  
ATOM   5520  NE1 TRP B 606     -22.959 -78.638  14.718  1.00149.25           N  
ANISOU 5520  NE1 TRP B 606    16989  23765  15953  -3675    -61   1338       N  
ATOM   5521  CE2 TRP B 606     -23.467 -79.537  13.814  1.00150.34           C  
ANISOU 5521  CE2 TRP B 606    17019  24280  15821  -3710     20   1086       C  
ATOM   5522  CE3 TRP B 606     -25.185 -81.243  13.748  1.00147.17           C  
ANISOU 5522  CE3 TRP B 606    16602  23608  15706  -3189    102    550       C  
ATOM   5523  CZ2 TRP B 606     -23.099 -79.787  12.476  1.00154.85           C  
ANISOU 5523  CZ2 TRP B 606    17417  25632  15783  -4131     79   1038       C  
ATOM   5524  CZ3 TRP B 606     -24.822 -81.489  12.417  1.00151.79           C  
ANISOU 5524  CZ3 TRP B 606    17023  24933  15714  -3575    151    477       C  
ATOM   5525  CH2 TRP B 606     -23.786 -80.764  11.799  1.00155.36           C  
ANISOU 5525  CH2 TRP B 606    17390  25930  15707  -4049    150    713       C  
ATOM   5526  N   THR B 607     -26.202 -81.498  19.947  1.00127.75           N  
ANISOU 5526  N   THR B 607    14515  18672  15351  -1534    296    195       N  
ATOM   5527  CA  THR B 607     -27.352 -81.744  20.854  1.00126.02           C  
ANISOU 5527  CA  THR B 607    14352  18018  15510  -1243    255    130       C  
ATOM   5528  C   THR B 607     -28.383 -80.617  20.838  1.00126.93           C  
ANISOU 5528  C   THR B 607    14559  17845  15822  -1272    -31    429       C  
ATOM   5529  O   THR B 607     -28.201 -79.621  20.148  1.00129.41           O  
ANISOU 5529  O   THR B 607    14919  18236  16013  -1523   -241    733       O  
ATOM   5530  CB  THR B 607     -26.937 -82.005  22.328  1.00123.52           C  
ANISOU 5530  CB  THR B 607    14042  17433  15455   -996    407    -26       C  
ATOM   5531  OG1 THR B 607     -25.636 -81.453  22.586  1.00123.85           O  
ANISOU 5531  OG1 THR B 607    14082  17574  15401  -1097    469     36       O  
ATOM   5532  CG2 THR B 607     -26.962 -83.506  22.640  1.00122.52           C  
ANISOU 5532  CG2 THR B 607    13838  17329  15382   -814    584   -361       C  
ATOM   5533  N   ALA B 608     -29.463 -80.783  21.600  1.00125.77           N  
ANISOU 5533  N   ALA B 608    14418  17374  15992  -1030    -62    337       N  
ATOM   5534  CA  ALA B 608     -30.476 -79.733  21.776  1.00127.01           C  
ANISOU 5534  CA  ALA B 608    14613  17212  16430   -987   -341    524       C  
ATOM   5535  C   ALA B 608     -29.902 -78.548  22.525  1.00127.47           C  
ANISOU 5535  C   ALA B 608    14716  17042  16672   -982   -450    663       C  
ATOM   5536  O   ALA B 608     -30.217 -77.401  22.227  1.00129.37           O  
ANISOU 5536  O   ALA B 608    14997  17095  17060  -1079   -766    912       O  
ATOM   5537  CB  ALA B 608     -31.678 -80.273  22.528  1.00125.60           C  
ANISOU 5537  CB  ALA B 608    14378  16816  16528   -728   -296    316       C  
ATOM   5538  N   ASN B 609     -29.073 -78.856  23.515  1.00126.16           N  
ANISOU 5538  N   ASN B 609    14537  16869  16525   -868   -217    497       N  
ATOM   5539  CA  ASN B 609     -28.371 -77.869  24.305  1.00126.89           C  
ANISOU 5539  CA  ASN B 609    14664  16780  16768   -857   -277    578       C  
ATOM   5540  C   ASN B 609     -27.402 -77.051  23.432  1.00129.96           C  
ANISOU 5540  C   ASN B 609    15108  17324  16945  -1168   -427    882       C  
ATOM   5541  O   ASN B 609     -27.302 -75.829  23.593  1.00131.52           O  
ANISOU 5541  O   ASN B 609    15352  17286  17333  -1238   -688   1093       O  
ATOM   5542  CB  ASN B 609     -27.627 -78.587  25.434  1.00124.28           C  
ANISOU 5542  CB  ASN B 609    14304  16481  16434   -702     20    337       C  
ATOM   5543  CG  ASN B 609     -27.560 -77.784  26.719  1.00123.39           C  
ANISOU 5543  CG  ASN B 609    14190  16094  16597   -556    -19    284       C  
ATOM   5544  OD1 ASN B 609     -28.365 -76.885  26.971  1.00124.51           O  
ANISOU 5544  OD1 ASN B 609    14315  15982  17011   -479   -239    313       O  
ATOM   5545  ND2 ASN B 609     -26.598 -78.129  27.557  1.00121.87           N  
ANISOU 5545  ND2 ASN B 609    13994  15957  16351   -507    181    170       N  
ATOM   5546  N   MET B 610     -26.709 -77.727  22.505  1.00131.51           N  
ANISOU 5546  N   MET B 610    15279  17934  16755  -1369   -281    888       N  
ATOM   5547  CA  MET B 610     -25.746 -77.079  21.593  1.00135.05           C  
ANISOU 5547  CA  MET B 610    15743  18663  16903  -1733   -383   1167       C  
ATOM   5548  C   MET B 610     -26.402 -76.184  20.536  1.00138.50           C  
ANISOU 5548  C   MET B 610    16241  19078  17303  -2003   -763   1549       C  
ATOM   5549  O   MET B 610     -25.913 -75.091  20.280  1.00140.84           O  
ANISOU 5549  O   MET B 610    16592  19327  17591  -2259  -1012   1888       O  
ATOM   5550  CB  MET B 610     -24.802 -78.097  20.932  1.00135.58           C  
ANISOU 5550  CB  MET B 610    15707  19254  16550  -1870    -96    981       C  
ATOM   5551  CG  MET B 610     -23.445 -78.282  21.650  1.00136.48           C  
ANISOU 5551  CG  MET B 610    15766  19470  16620  -1828    136    820       C  
ATOM   5552  SD  MET B 610     -22.122 -77.046  21.347  1.00142.68           S  
ANISOU 5552  SD  MET B 610    16558  20446  17206  -2207     22   1158       S  
ATOM   5553  CE  MET B 610     -21.473 -77.603  19.754  1.00145.02           C  
ANISOU 5553  CE  MET B 610    16700  21497  16902  -2600    145   1135       C  
ATOM   5554  N   GLU B 611     -27.497 -76.651  19.930  1.00139.39           N  
ANISOU 5554  N   GLU B 611    16344  19211  17405  -1964   -838   1515       N  
ATOM   5555  CA  GLU B 611     -28.308 -75.831  19.012  1.00142.87           C  
ANISOU 5555  CA  GLU B 611    16844  19560  17879  -2184  -1252   1878       C  
ATOM   5556  C   GLU B 611     -28.893 -74.595  19.721  1.00143.89           C  
ANISOU 5556  C   GLU B 611    17031  19110  18528  -2048  -1619   2044       C  
ATOM   5557  O   GLU B 611     -29.103 -73.555  19.097  1.00147.12           O  
ANISOU 5557  O   GLU B 611    17504  19372  19021  -2293  -2050   2437       O  
ATOM   5558  CB  GLU B 611     -29.424 -76.662  18.358  1.00142.76           C  
ANISOU 5558  CB  GLU B 611    16794  19652  17795  -2114  -1244   1751       C  
ATOM   5559  CG  GLU B 611     -28.972 -77.590  17.219  1.00143.93           C  
ANISOU 5559  CG  GLU B 611    16876  20403  17405  -2361  -1043   1673       C  
ATOM   5560  CD  GLU B 611     -30.132 -78.346  16.553  1.00144.97           C  
ANISOU 5560  CD  GLU B 611    16976  20610  17494  -2299  -1079   1555       C  
ATOM   5561  OE1 GLU B 611     -31.309 -78.022  16.832  1.00144.69           O  
ANISOU 5561  OE1 GLU B 611    16975  20175  17824  -2118  -1305   1609       O  
ATOM   5562  OE2 GLU B 611     -29.870 -79.270  15.745  1.00145.92           O1-
ANISOU 5562  OE2 GLU B 611    17015  21201  17224  -2425   -888   1374       O1-
ATOM   5563  N   ARG B 612     -29.143 -74.729  21.024  1.00141.75           N  
ANISOU 5563  N   ARG B 612    16721  18528  18607  -1671  -1468   1729       N  
ATOM   5564  CA  ARG B 612     -29.543 -73.619  21.896  1.00143.04           C  
ANISOU 5564  CA  ARG B 612    16888  18184  19276  -1492  -1753   1748       C  
ATOM   5565  C   ARG B 612     -28.406 -72.603  22.085  1.00145.16           C  
ANISOU 5565  C   ARG B 612    17218  18364  19569  -1687  -1905   1991       C  
ATOM   5566  O   ARG B 612     -28.662 -71.400  22.101  1.00148.03           O  
ANISOU 5566  O   ARG B 612    17615  18347  20283  -1739  -2345   2216       O  
ATOM   5567  CB  ARG B 612     -30.007 -74.164  23.250  1.00139.87           C  
ANISOU 5567  CB  ARG B 612    16396  17616  19132  -1084  -1482   1303       C  
ATOM   5568  CG  ARG B 612     -30.591 -73.147  24.214  1.00140.45           C  
ANISOU 5568  CG  ARG B 612    16409  17226  19729   -848  -1735   1184       C  
ATOM   5569  CD  ARG B 612     -31.089 -73.833  25.489  1.00137.64           C  
ANISOU 5569  CD  ARG B 612    15934  16850  19512   -509  -1418    734       C  
ATOM   5570  NE  ARG B 612     -32.215 -74.740  25.228  1.00136.91           N  
ANISOU 5570  NE  ARG B 612    15768  16866  19383   -402  -1313    578       N  
ATOM   5571  CZ  ARG B 612     -32.246 -76.044  25.518  1.00134.11           C  
ANISOU 5571  CZ  ARG B 612    15386  16772  18797   -332   -936    375       C  
ATOM   5572  NH1 ARG B 612     -31.224 -76.651  26.110  1.00132.69           N1+
ANISOU 5572  NH1 ARG B 612    15239  16767  18408   -337   -627    285       N1+
ATOM   5573  NH2 ARG B 612     -33.322 -76.750  25.224  1.00133.73           N  
ANISOU 5573  NH2 ARG B 612    15270  16784  18756   -259   -903    266       N  
ATOM   5574  N   ILE B 613     -27.168 -73.095  22.231  1.00144.33           N  
ANISOU 5574  N   ILE B 613    17115  18591  19130  -1791  -1570   1932       N  
ATOM   5575  CA  ILE B 613     -25.950 -72.256  22.264  1.00146.31           C  
ANISOU 5575  CA  ILE B 613    17413  18865  19313  -2041  -1672   2183       C  
ATOM   5576  C   ILE B 613     -25.628 -71.611  20.882  1.00150.87           C  
ANISOU 5576  C   ILE B 613    18051  19665  19606  -2545  -1992   2691       C  
ATOM   5577  O   ILE B 613     -24.942 -70.593  20.819  1.00153.14           O  
ANISOU 5577  O   ILE B 613    18390  19843  19951  -2800  -2258   3014       O  
ATOM   5578  CB  ILE B 613     -24.703 -73.056  22.823  1.00143.77           C  
ANISOU 5578  CB  ILE B 613    17043  18869  18713  -1998  -1207   1935       C  
ATOM   5579  CG1 ILE B 613     -25.046 -73.852  24.100  1.00140.03           C  
ANISOU 5579  CG1 ILE B 613    16515  18242  18445  -1566   -902   1485       C  
ATOM   5580  CG2 ILE B 613     -23.475 -72.147  23.042  1.00145.03           C  
ANISOU 5580  CG2 ILE B 613    17234  19013  18858  -2218  -1306   2155       C  
ATOM   5581  CD1 ILE B 613     -24.793 -73.140  25.426  1.00138.85           C  
ANISOU 5581  CD1 ILE B 613    16368  17737  18652  -1362   -948   1364       C  
ATOM   5582  N   MET B 614     -26.140 -72.196  19.792  1.00152.73           N  
ANISOU 5582  N   MET B 614    18276  20223  19530  -2714  -1987   2773       N  
ATOM   5583  CA  MET B 614     -25.915 -71.695  18.411  1.00157.83           C  
ANISOU 5583  CA  MET B 614    18965  21183  19819  -3244  -2279   3262       C  
ATOM   5584  C   MET B 614     -26.798 -70.488  18.045  1.00161.47           C  
ANISOU 5584  C   MET B 614    19519  21170  20663  -3373  -2918   3686       C  
ATOM   5585  O   MET B 614     -27.553 -70.533  17.064  1.00163.75           O  
ANISOU 5585  O   MET B 614    19829  21565  20823  -3561  -3153   3904       O  
ATOM   5586  CB  MET B 614     -26.126 -72.810  17.355  1.00158.32           C  
ANISOU 5586  CB  MET B 614    18960  21820  19371  -3390  -2035   3154       C  
ATOM   5587  CG  MET B 614     -25.242 -74.073  17.470  1.00157.35           C  
ANISOU 5587  CG  MET B 614    18714  22209  18863  -3305  -1468   2725       C  
ATOM   5588  SD  MET B 614     -23.458 -73.871  17.161  1.00162.59           S  
ANISOU 5588  SD  MET B 614    19295  23425  19055  -3716  -1277   2842       S  
ATOM   5589  CE  MET B 614     -22.857 -75.547  17.424  1.00158.57           C  
ANISOU 5589  CE  MET B 614    18607  23344  18298  -3432   -673   2187       C  
ATOM   5590  N   LYS B 615     -26.696 -69.410  18.822  1.00162.38           N  
ANISOU 5590  N   LYS B 615    19677  20751  21268  -3273  -3231   3790       N  
ATOM   5591  CA  LYS B 615     -27.526 -68.223  18.590  1.00166.25           C  
ANISOU 5591  CA  LYS B 615    20231  20688  22246  -3340  -3902   4139       C  
ATOM   5592  C   LYS B 615     -26.696 -66.941  18.459  1.00170.07           C  
ANISOU 5592  C   LYS B 615    20797  20967  22851  -3721  -4349   4630       C  
ATOM   5593  O   LYS B 615     -25.856 -66.637  19.305  1.00168.76           O  
ANISOU 5593  O   LYS B 615    20623  20687  22811  -3631  -4216   4507       O  
ATOM   5594  CB  LYS B 615     -28.593 -68.090  19.685  1.00164.27           C  
ANISOU 5594  CB  LYS B 615    19911  19853  22647  -2771  -3978   3713       C  
ATOM   5595  CG  LYS B 615     -29.732 -69.111  19.574  1.00162.44           C  
ANISOU 5595  CG  LYS B 615    19605  19735  22377  -2486  -3746   3378       C  
ATOM   5596  CD  LYS B 615     -30.629 -69.102  20.820  1.00161.05           C  
ANISOU 5596  CD  LYS B 615    19312  19117  22761  -1936  -3698   2877       C  
ATOM   5597  CE  LYS B 615     -31.719 -70.191  20.793  1.00158.62           C  
ANISOU 5597  CE  LYS B 615    18914  18960  22392  -1673  -3427   2535       C  
ATOM   5598  NZ  LYS B 615     -33.001 -69.750  20.162  1.00161.35           N1+
ANISOU 5598  NZ  LYS B 615    19228  19014  23061  -1653  -3906   2673       N1+
ATOM   5599  N   ALA B 630     -27.434 -82.552  14.717  1.00121.55           N  
ANISOU 5599  N   ALA B 630    10622  17366  18194   -533   3375    632       N  
ATOM   5600  CA  ALA B 630     -28.721 -82.177  14.052  1.00120.12           C  
ANISOU 5600  CA  ALA B 630    10897  17392  17351   -431   3462    960       C  
ATOM   5601  C   ALA B 630     -29.471 -83.432  13.588  1.00116.91           C  
ANISOU 5601  C   ALA B 630    10890  17457  16071   -109   3325    601       C  
ATOM   5602  O   ALA B 630     -30.664 -83.367  13.231  1.00115.20           O  
ANISOU 5602  O   ALA B 630    11077  17394  15298     -1   3223    696       O  
ATOM   5603  CB  ALA B 630     -28.467 -81.210  12.869  1.00126.54           C  
ANISOU 5603  CB  ALA B 630    11517  18413  18146   -446   4115   1702       C  
ATOM   5604  N   LYS B 631     -28.760 -84.564  13.600  1.00116.26           N  
ANISOU 5604  N   LYS B 631    10668  17569  15936     47   3285    166       N  
ATOM   5605  CA  LYS B 631     -29.315 -85.859  13.211  1.00113.30           C  
ANISOU 5605  CA  LYS B 631    10619  17552  14876    350   3093   -259       C  
ATOM   5606  C   LYS B 631     -30.135 -86.449  14.358  1.00106.29           C  
ANISOU 5606  C   LYS B 631    10054  16310  14018    264   2460   -674       C  
ATOM   5607  O   LYS B 631     -29.593 -86.859  15.380  1.00104.26           O  
ANISOU 5607  O   LYS B 631     9682  15731  14200    175   2155   -994       O  
ATOM   5608  CB  LYS B 631     -28.200 -86.816  12.765  1.00116.94           C  
ANISOU 5608  CB  LYS B 631    10792  18322  15316    588   3295   -565       C  
ATOM   5609  CG  LYS B 631     -27.148 -86.169  11.852  1.00124.12           C  
ANISOU 5609  CG  LYS B 631    11242  19546  16369    634   3989   -112       C  
ATOM   5610  CD  LYS B 631     -26.028 -87.141  11.484  1.00128.65           C  
ANISOU 5610  CD  LYS B 631    11487  20449  16942    909   4186   -466       C  
ATOM   5611  CE  LYS B 631     -24.785 -86.404  10.988  1.00135.57           C  
ANISOU 5611  CE  LYS B 631    11742  21490  18277    840   4851     -6       C  
ATOM   5612  NZ  LYS B 631     -23.916 -85.944  12.109  1.00135.49           N1+
ANISOU 5612  NZ  LYS B 631    11270  20908  19302    472   4657    -54       N1+
ATOM   5613  N   LYS B 632     -31.451 -86.474  14.176  1.00102.77           N  
ANISOU 5613  N   LYS B 632    10000  15947  13100    310   2278   -637       N  
ATOM   5614  CA  LYS B 632     -32.370 -86.929  15.212  1.00 96.77           C  
ANISOU 5614  CA  LYS B 632     9524  14890  12352    217   1762   -915       C  
ATOM   5615  C   LYS B 632     -32.748 -88.399  15.031  1.00 95.21           C  
ANISOU 5615  C   LYS B 632     9530  14851  11794    409   1491  -1365       C  
ATOM   5616  O   LYS B 632     -32.837 -88.892  13.914  1.00 97.82           O  
ANISOU 5616  O   LYS B 632     9918  15581  11667    653   1640  -1448       O  
ATOM   5617  CB  LYS B 632     -33.652 -86.086  15.198  1.00 95.04           C  
ANISOU 5617  CB  LYS B 632     9553  14632  11925    139   1698   -616       C  
ATOM   5618  CG  LYS B 632     -33.490 -84.623  15.535  1.00 95.22           C  
ANISOU 5618  CG  LYS B 632     9440  14375  12364    -52   1846   -210       C  
ATOM   5619  CD  LYS B 632     -34.486 -83.808  14.725  1.00 97.65           C  
ANISOU 5619  CD  LYS B 632     9935  14869  12297     11   2004    191       C  
ATOM   5620  CE  LYS B 632     -34.535 -82.354  15.165  1.00100.13           C  
ANISOU 5620  CE  LYS B 632    10172  14806  13065   -171   2054    568       C  
ATOM   5621  NZ  LYS B 632     -33.180 -81.705  15.180  1.00106.35           N1+
ANISOU 5621  NZ  LYS B 632    10570  15375  14463   -327   2339    782       N1+
ATOM   5622  N   HIS B 633     -32.955 -89.088  16.147  1.00 91.36           N  
ANISOU 5622  N   HIS B 633     9154  14032  11523    320   1080  -1651       N  
ATOM   5623  CA  HIS B 633     -33.603 -90.385  16.170  1.00 89.70           C  
ANISOU 5623  CA  HIS B 633     9172  13825  11082    423    747  -2002       C  
ATOM   5624  C   HIS B 633     -34.757 -90.207  17.137  1.00 85.59           C  
ANISOU 5624  C   HIS B 633     8865  13041  10611    235    462  -1901       C  
ATOM   5625  O   HIS B 633     -34.560 -89.641  18.206  1.00 83.79           O  
ANISOU 5625  O   HIS B 633     8602  12536  10699     95    388  -1794       O  
ATOM   5626  CB  HIS B 633     -32.667 -91.455  16.729  1.00 90.26           C  
ANISOU 5626  CB  HIS B 633     9153  13701  11438    500    545  -2376       C  
ATOM   5627  CG  HIS B 633     -31.514 -91.812  15.836  1.00 95.42           C  
ANISOU 5627  CG  HIS B 633     9562  14633  12056    736    808  -2553       C  
ATOM   5628  ND1 HIS B 633     -30.653 -90.874  15.301  1.00 98.94           N  
ANISOU 5628  ND1 HIS B 633     9701  15293  12599    745   1259  -2285       N  
ATOM   5629  CD2 HIS B 633     -31.047 -93.017  15.433  1.00 97.61           C  
ANISOU 5629  CD2 HIS B 633     9832  14999  12256    988    689  -2970       C  
ATOM   5630  CE1 HIS B 633     -29.730 -91.482  14.581  1.00101.82           C  
ANISOU 5630  CE1 HIS B 633     9864  15930  12893   1004   1455  -2513       C  
ATOM   5631  NE2 HIS B 633     -29.948 -92.783  14.645  1.00102.16           N  
ANISOU 5631  NE2 HIS B 633    10097  15904  12814   1177   1095  -2964       N  
ATOM   5632  N   LEU B 634     -35.954 -90.650  16.752  1.00 84.65           N  
ANISOU 5632  N   LEU B 634     8943  13032  10187    258    302  -1946       N  
ATOM   5633  CA  LEU B 634     -37.102 -90.711  17.646  1.00 81.54           C  
ANISOU 5633  CA  LEU B 634     8704  12425   9849    100     50  -1870       C  
ATOM   5634  C   LEU B 634     -37.189 -92.110  18.205  1.00 81.73           C  
ANISOU 5634  C   LEU B 634     8816  12218  10020     87   -269  -2154       C  
ATOM   5635  O   LEU B 634     -37.364 -93.062  17.465  1.00 83.91           O  
ANISOU 5635  O   LEU B 634     9129  12576  10174    194   -405  -2418       O  
ATOM   5636  CB  LEU B 634     -38.402 -90.397  16.905  1.00 81.50           C  
ANISOU 5636  CB  LEU B 634     8796  12654   9515    116     40  -1743       C  
ATOM   5637  CG  LEU B 634     -39.718 -90.643  17.662  1.00 78.89           C  
ANISOU 5637  CG  LEU B 634     8560  12167   9244    -30   -203  -1689       C  
ATOM   5638  CD1 LEU B 634     -40.002 -89.569  18.740  1.00 75.10           C  
ANISOU 5638  CD1 LEU B 634     8085  11536   8912   -144   -129  -1400       C  
ATOM   5639  CD2 LEU B 634     -40.864 -90.724  16.690  1.00 78.12           C  
ANISOU 5639  CD2 LEU B 634     8499  12323   8858     34   -297  -1713       C  
ATOM   5640  N   GLU B 635     -37.068 -92.238  19.515  1.00 80.51           N  
ANISOU 5640  N   GLU B 635     8705  11758  10126    -15   -411  -2102       N  
ATOM   5641  CA  GLU B 635     -37.182 -93.540  20.153  1.00 81.29           C  
ANISOU 5641  CA  GLU B 635     8908  11585  10391    -34   -701  -2267       C  
ATOM   5642  C   GLU B 635     -38.600 -93.734  20.699  1.00 80.07           C  
ANISOU 5642  C   GLU B 635     8864  11339  10219   -193   -825  -2072       C  
ATOM   5643  O   GLU B 635     -39.096 -92.885  21.420  1.00 78.93           O  
ANISOU 5643  O   GLU B 635     8743  11209  10036   -264   -734  -1811       O  
ATOM   5644  CB  GLU B 635     -36.165 -93.655  21.289  1.00 81.06           C  
ANISOU 5644  CB  GLU B 635     8876  11301  10619      2   -789  -2297       C  
ATOM   5645  CG  GLU B 635     -34.716 -93.470  20.866  1.00 84.51           C  
ANISOU 5645  CG  GLU B 635     9119  11807  11181    143   -672  -2489       C  
ATOM   5646  CD  GLU B 635     -33.711 -94.182  21.786  1.00 88.10           C  
ANISOU 5646  CD  GLU B 635     9570  11981  11921    245   -902  -2669       C  
ATOM   5647  OE1 GLU B 635     -32.644 -94.607  21.274  1.00 90.07           O  
ANISOU 5647  OE1 GLU B 635     9653  12271  12297    399   -882  -2929       O  
ATOM   5648  OE2 GLU B 635     -33.984 -94.320  23.007  1.00 88.78           O1-
ANISOU 5648  OE2 GLU B 635     9816  11838  12077    211  -1096  -2547       O1-
ATOM   5649  N   ILE B 636     -39.251 -94.839  20.367  1.00 81.09           N  
ANISOU 5649  N   ILE B 636     9030  11363  10415   -238  -1037  -2208       N  
ATOM   5650  CA  ILE B 636     -40.541 -95.135  20.969  1.00 80.70           C  
ANISOU 5650  CA  ILE B 636     9011  11189  10460   -422  -1137  -1988       C  
ATOM   5651  C   ILE B 636     -40.392 -96.093  22.160  1.00 81.80           C  
ANISOU 5651  C   ILE B 636     9251  10951  10876   -487  -1293  -1885       C  
ATOM   5652  O   ILE B 636     -39.478 -96.919  22.180  1.00 83.37           O  
ANISOU 5652  O   ILE B 636     9501  10938  11237   -389  -1447  -2101       O  
ATOM   5653  CB  ILE B 636     -41.554 -95.660  19.934  1.00 82.53           C  
ANISOU 5653  CB  ILE B 636     9172  11502  10683   -476  -1301  -2145       C  
ATOM   5654  CG1 ILE B 636     -41.039 -96.924  19.242  1.00 85.57           C  
ANISOU 5654  CG1 ILE B 636     9578  11711  11222   -377  -1571  -2561       C  
ATOM   5655  CG2 ILE B 636     -41.850 -94.586  18.909  1.00 82.27           C  
ANISOU 5655  CG2 ILE B 636     9082  11875  10300   -375  -1138  -2144       C  
ATOM   5656  CD1 ILE B 636     -42.045 -97.618  18.340  1.00 86.65           C  
ANISOU 5656  CD1 ILE B 636     9645  11837  11439   -419  -1855  -2802       C  
ATOM   5657  N   ASN B 637     -41.286 -95.962  23.145  1.00 81.56           N  
ANISOU 5657  N   ASN B 637     9247  10863  10879   -616  -1233  -1531       N  
ATOM   5658  CA  ASN B 637     -41.320 -96.788  24.359  1.00 83.05           C  
ANISOU 5658  CA  ASN B 637     9552  10741  11261   -662  -1317  -1296       C  
ATOM   5659  C   ASN B 637     -42.138 -98.057  24.157  1.00 86.74           C  
ANISOU 5659  C   ASN B 637     9961  10917  12079   -859  -1508  -1253       C  
ATOM   5660  O   ASN B 637     -43.377 -97.988  24.024  1.00 87.96           O  
ANISOU 5660  O   ASN B 637     9967  11146  12307  -1042  -1454  -1071       O  
ATOM   5661  CB  ASN B 637     -41.930 -95.985  25.509  1.00 82.13           C  
ANISOU 5661  CB  ASN B 637     9479  10771  10953   -659  -1105   -905       C  
ATOM   5662  CG  ASN B 637     -41.983 -96.751  26.819  1.00 84.65           C  
ANISOU 5662  CG  ASN B 637     9950  10852  11361   -646  -1131   -581       C  
ATOM   5663  OD1 ASN B 637     -41.661 -97.938  26.891  1.00 87.68           O  
ANISOU 5663  OD1 ASN B 637    10401  10895  12018   -686  -1322   -595       O  
ATOM   5664  ND2 ASN B 637     -42.385 -96.059  27.877  1.00 84.37           N  
ANISOU 5664  ND2 ASN B 637     9986  10999  11070   -550   -940   -276       N  
ATOM   5665  N   PRO B 638     -41.469 -99.228  24.173  1.00 89.14           N  
ANISOU 5665  N   PRO B 638    10354  10849  12666   -823  -1754  -1418       N  
ATOM   5666  CA  PRO B 638     -42.179-100.468  23.872  1.00 93.16           C  
ANISOU 5666  CA  PRO B 638    10789  10986  13620  -1019  -2001  -1436       C  
ATOM   5667  C   PRO B 638     -43.358-100.717  24.799  1.00 95.45           C  
ANISOU 5667  C   PRO B 638    11009  11138  14119  -1268  -1877   -890       C  
ATOM   5668  O   PRO B 638     -44.350-101.257  24.357  1.00 98.86           O  
ANISOU 5668  O   PRO B 638    11245  11412  14903  -1502  -1999   -870       O  
ATOM   5669  CB  PRO B 638     -41.114-101.547  24.077  1.00 95.22           C  
ANISOU 5669  CB  PRO B 638    11208  10833  14135   -882  -2260  -1621       C  
ATOM   5670  CG  PRO B 638     -40.096-100.932  24.937  1.00 92.33           C  
ANISOU 5670  CG  PRO B 638    10999  10605  13476   -662  -2111  -1512       C  
ATOM   5671  CD  PRO B 638     -40.077 -99.485  24.573  1.00 88.83           C  
ANISOU 5671  CD  PRO B 638    10466  10665  12617   -599  -1847  -1576       C  
ATOM   5672  N   ASP B 639     -43.260-100.297  26.056  1.00 94.84           N  
ANISOU 5672  N   ASP B 639    11065  11149  13820  -1194  -1636   -464       N  
ATOM   5673  CA  ASP B 639     -44.261-100.615  27.067  1.00 97.97           C  
ANISOU 5673  CA  ASP B 639    11413  11446  14365  -1371  -1449    127       C  
ATOM   5674  C   ASP B 639     -45.264 -99.509  27.351  1.00 96.35           C  
ANISOU 5674  C   ASP B 639    11051  11692  13863  -1407  -1113    391       C  
ATOM   5675  O   ASP B 639     -46.003 -99.581  28.329  1.00 98.98           O  
ANISOU 5675  O   ASP B 639    11346  12064  14196  -1472   -864    912       O  
ATOM   5676  CB  ASP B 639     -43.569-100.990  28.373  1.00 99.87           C  
ANISOU 5676  CB  ASP B 639    11937  11515  14493  -1191  -1400    472       C  
ATOM   5677  CG  ASP B 639     -42.863-102.329  28.297  1.00105.24           C  
ANISOU 5677  CG  ASP B 639    12747  11640  15597  -1192  -1734    367       C  
ATOM   5678  OD1 ASP B 639     -41.609-102.340  28.182  1.00104.39           O  
ANISOU 5678  OD1 ASP B 639    12812  11487  15362   -934  -1922      7       O  
ATOM   5679  OD2 ASP B 639     -43.569-103.374  28.347  1.00113.20           O1-
ANISOU 5679  OD2 ASP B 639    13656  12229  17123  -1453  -1821    645       O1-
ATOM   5680  N   HIS B 640     -45.306 -98.472  26.535  1.00 92.79           N  
ANISOU 5680  N   HIS B 640    10509  11597  13148  -1334  -1079     69       N  
ATOM   5681  CA  HIS B 640     -46.257 -97.417  26.840  1.00 91.98           C  
ANISOU 5681  CA  HIS B 640    10266  11892  12790  -1327   -789    306       C  
ATOM   5682  C   HIS B 640     -47.552 -97.768  26.152  1.00 94.68           C  
ANISOU 5682  C   HIS B 640    10265  12215  13494  -1607   -837    350       C  
ATOM   5683  O   HIS B 640     -47.548 -98.108  24.972  1.00 95.05           O  
ANISOU 5683  O   HIS B 640    10210  12161  13741  -1689  -1116    -43       O  
ATOM   5684  CB  HIS B 640     -45.743 -96.044  26.388  1.00 87.85           C  
ANISOU 5684  CB  HIS B 640     9808  11723  11847  -1105   -727     12       C  
ATOM   5685  CG  HIS B 640     -46.380 -94.887  27.104  1.00 86.25           C  
ANISOU 5685  CG  HIS B 640     9575  11873  11322   -977   -443    257       C  
ATOM   5686  ND1 HIS B 640     -47.563 -94.312  26.692  1.00 86.19           N  
ANISOU 5686  ND1 HIS B 640     9315  12116  11315  -1058   -327    333       N  
ATOM   5687  CD2 HIS B 640     -45.985 -94.190  28.195  1.00 85.16           C  
ANISOU 5687  CD2 HIS B 640     9626  11880  10848   -727   -292    390       C  
ATOM   5688  CE1 HIS B 640     -47.875 -93.315  27.501  1.00 85.19           C  
ANISOU 5688  CE1 HIS B 640     9223  12268  10874   -861    -91    512       C  
ATOM   5689  NE2 HIS B 640     -46.931 -93.218  28.421  1.00 85.57           N  
ANISOU 5689  NE2 HIS B 640     9548  12259  10703   -652    -75    532       N  
ATOM   5690  N   SER B 641     -48.657 -97.696  26.890  1.00 97.39           N  
ANISOU 5690  N   SER B 641    10410  12674  13918  -1725   -574    810       N  
ATOM   5691  CA  SER B 641     -49.977 -97.976  26.325  1.00100.47           C  
ANISOU 5691  CA  SER B 641    10388  13060  14724  -2004   -614    876       C  
ATOM   5692  C   SER B 641     -50.185 -97.241  24.997  1.00 98.18           C  
ANISOU 5692  C   SER B 641     9979  13022  14302  -1944   -813    395       C  
ATOM   5693  O   SER B 641     -50.544 -97.879  24.007  1.00100.58           O  
ANISOU 5693  O   SER B 641    10096  13141  14978  -2110  -1141    103       O  
ATOM   5694  CB  SER B 641     -51.095 -97.654  27.322  1.00103.07           C  
ANISOU 5694  CB  SER B 641    10481  13637  15043  -2057   -206   1436       C  
ATOM   5695  OG  SER B 641     -51.165 -96.265  27.586  1.00100.04           O  
ANISOU 5695  OG  SER B 641    10169  13740  14101  -1765     29   1408       O  
ATOM   5696  N   ILE B 642     -49.933 -95.926  24.968  1.00 94.23           N  
ANISOU 5696  N   ILE B 642     9605  12915  13283  -1681   -648    306       N  
ATOM   5697  CA  ILE B 642     -50.065 -95.119  23.738  1.00 92.30           C  
ANISOU 5697  CA  ILE B 642     9299  12928  12840  -1573   -796    -64       C  
ATOM   5698  C   ILE B 642     -49.340 -95.745  22.543  1.00 92.76           C  
ANISOU 5698  C   ILE B 642     9458  12805  12979  -1566  -1153   -536       C  
ATOM   5699  O   ILE B 642     -49.942 -95.976  21.494  1.00 94.69           O  
ANISOU 5699  O   ILE B 642     9517  13086  13376  -1625  -1416   -803       O  
ATOM   5700  CB  ILE B 642     -49.546 -93.671  23.923  1.00 88.24           C  
ANISOU 5700  CB  ILE B 642     8987  12734  11806  -1281   -589    -81       C  
ATOM   5701  CG1 ILE B 642     -50.495 -92.853  24.781  1.00 87.77           C  
ANISOU 5701  CG1 ILE B 642     8781  12947  11618  -1207   -296    251       C  
ATOM   5702  CG2 ILE B 642     -49.370 -92.968  22.582  1.00 86.52           C  
ANISOU 5702  CG2 ILE B 642     8786  12708  11377  -1152   -742   -421       C  
ATOM   5703  CD1 ILE B 642     -49.933 -91.521  25.151  1.00 82.71           C  
ANISOU 5703  CD1 ILE B 642     8359  12512  10553   -912   -142    219       C  
ATOM   5704  N   ILE B 643     -48.051 -96.018  22.709  1.00 91.53           N  
ANISOU 5704  N   ILE B 643     9585  12483  12707  -1453  -1179   -666       N  
ATOM   5705  CA  ILE B 643     -47.256 -96.564  21.621  1.00 92.53           C  
ANISOU 5705  CA  ILE B 643     9812  12495  12847  -1372  -1465  -1128       C  
ATOM   5706  C   ILE B 643     -47.802 -97.931  21.274  1.00 97.68           C  
ANISOU 5706  C   ILE B 643    10302  12778  14032  -1589  -1804  -1273       C  
ATOM   5707  O   ILE B 643     -48.093 -98.218  20.115  1.00 99.94           O  
ANISOU 5707  O   ILE B 643    10489  13098  14386  -1561  -2108  -1669       O  
ATOM   5708  CB  ILE B 643     -45.750 -96.637  21.995  1.00 90.26           C  
ANISOU 5708  CB  ILE B 643     9803  12090  12402  -1202  -1411  -1220       C  
ATOM   5709  CG1 ILE B 643     -45.164 -95.228  22.147  1.00 86.17           C  
ANISOU 5709  CG1 ILE B 643     9396  11894  11449  -1001  -1145  -1156       C  
ATOM   5710  CG2 ILE B 643     -44.951 -97.445  20.980  1.00 91.34           C  
ANISOU 5710  CG2 ILE B 643    10008  12080  12616  -1104  -1696  -1693       C  
ATOM   5711  CD1 ILE B 643     -45.352 -94.310  20.949  1.00 84.74           C  
ANISOU 5711  CD1 ILE B 643     9155  12057  10983   -881  -1121  -1333       C  
ATOM   5712  N   GLU B 644     -47.964 -98.748  22.310  1.00100.88           N  
ANISOU 5712  N   GLU B 644    10684  12825  14819  -1785  -1759   -936       N  
ATOM   5713  CA  GLU B 644     -48.492-100.109  22.213  1.00106.70           C  
ANISOU 5713  CA  GLU B 644    11245  13080  16215  -2050  -2065   -964       C  
ATOM   5714  C   GLU B 644     -49.791-100.179  21.404  1.00109.80           C  
ANISOU 5714  C   GLU B 644    11263  13533  16920  -2229  -2288  -1114       C  
ATOM   5715  O   GLU B 644     -49.910-101.038  20.533  1.00113.30           O  
ANISOU 5715  O   GLU B 644    11613  13698  17737  -2289  -2734  -1542       O  
ATOM   5716  CB  GLU B 644     -48.666-100.703  23.622  1.00109.16           C  
ANISOU 5716  CB  GLU B 644    11560  13079  16834  -2239  -1844   -367       C  
ATOM   5717  CG  GLU B 644     -49.636-101.870  23.729  1.00118.14           C  
ANISOU 5717  CG  GLU B 644    12387  13741  18758  -2613  -2029   -160       C  
ATOM   5718  CD  GLU B 644     -49.048-103.170  23.201  1.00125.16           C  
ANISOU 5718  CD  GLU B 644    13369  14044  20140  -2664  -2502   -536       C  
ATOM   5719  OE1 GLU B 644     -49.785-103.922  22.513  1.00130.03           O  
ANISOU 5719  OE1 GLU B 644    13699  14334  21371  -2894  -2881   -775       O  
ATOM   5720  OE2 GLU B 644     -47.847-103.433  23.480  1.00125.43           O1-
ANISOU 5720  OE2 GLU B 644    13748  13932  19978  -2453  -2529   -628       O1-
ATOM   5721  N   THR B 645     -50.746 -99.281  21.672  1.00109.04           N  
ANISOU 5721  N   THR B 645    10948  13799  16682  -2274  -2026   -819       N  
ATOM   5722  CA  THR B 645     -52.013 -99.316  20.940  1.00112.61           C  
ANISOU 5722  CA  THR B 645    10996  14327  17463  -2427  -2264   -965       C  
ATOM   5723  C   THR B 645     -51.849 -98.744  19.538  1.00111.35           C  
ANISOU 5723  C   THR B 645    10920  14501  16886  -2146  -2547  -1530       C  
ATOM   5724  O   THR B 645     -52.457 -99.225  18.595  1.00115.40           O  
ANISOU 5724  O   THR B 645    11219  14936  17691  -2190  -2985  -1921       O  
ATOM   5725  CB  THR B 645     -53.241 -98.674  21.693  1.00113.58           C  
ANISOU 5725  CB  THR B 645    10765  14710  17678  -2571  -1910   -456       C  
ATOM   5726  OG1 THR B 645     -53.421 -97.308  21.307  1.00110.22           O  
ANISOU 5726  OG1 THR B 645    10379  14823  16676  -2300  -1764   -540       O  
ATOM   5727  CG2 THR B 645     -53.128 -98.800  23.218  1.00113.53           C  
ANISOU 5727  CG2 THR B 645    10825  14606  17705  -2667  -1445    181       C  
ATOM   5728  N   LEU B 646     -51.010 -97.729  19.403  1.00106.68           N  
ANISOU 5728  N   LEU B 646    10639  14270  15625  -1841  -2308  -1564       N  
ATOM   5729  CA  LEU B 646     -50.704 -97.159  18.100  1.00106.10           C  
ANISOU 5729  CA  LEU B 646    10697  14536  15080  -1536  -2492  -2001       C  
ATOM   5730  C   LEU B 646     -49.983 -98.159  17.183  1.00109.08           C  
ANISOU 5730  C   LEU B 646    11219  14698  15527  -1417  -2895  -2551       C  
ATOM   5731  O   LEU B 646     -49.985 -97.987  15.973  1.00110.79           O  
ANISOU 5731  O   LEU B 646    11481  15179  15432  -1163  -3148  -2972       O  
ATOM   5732  CB  LEU B 646     -49.923 -95.857  18.294  1.00101.24           C  
ANISOU 5732  CB  LEU B 646    10346  14277  13843  -1287  -2091  -1812       C  
ATOM   5733  CG  LEU B 646     -49.113 -94.974  17.331  1.00 98.17           C  
ANISOU 5733  CG  LEU B 646    10198  14247  12852   -946  -2022  -2020       C  
ATOM   5734  CD1 LEU B 646     -47.686 -95.417  17.335  1.00 96.78           C  
ANISOU 5734  CD1 LEU B 646    10273  13920  12576   -840  -1972  -2187       C  
ATOM   5735  CD2 LEU B 646     -49.656 -94.800  15.910  1.00 99.78           C  
ANISOU 5735  CD2 LEU B 646    10346  14752  12811   -737  -2324  -2365       C  
ATOM   5736  N   ARG B 647     -49.395 -99.212  17.748  1.00110.69           N  
ANISOU 5736  N   ARG B 647    11502  14434  16119  -1557  -2972  -2555       N  
ATOM   5737  CA  ARG B 647     -48.887-100.328  16.941  1.00114.90           C  
ANISOU 5737  CA  ARG B 647    12119  14676  16861  -1454  -3428  -3119       C  
ATOM   5738  C   ARG B 647     -50.037-101.176  16.384  1.00121.42           C  
ANISOU 5738  C   ARG B 647    12620  15225  18287  -1644  -3952  -3420       C  
ATOM   5739  O   ARG B 647     -49.901-101.802  15.331  1.00125.24           O  
ANISOU 5739  O   ARG B 647    13142  15639  18805  -1450  -4432  -4044       O  
ATOM   5740  CB  ARG B 647     -47.947-101.228  17.751  1.00114.82           C  
ANISOU 5740  CB  ARG B 647    12283  14186  17157  -1533  -3396  -3025       C  
ATOM   5741  CG  ARG B 647     -47.147-102.240  16.902  1.00118.56           C  
ANISOU 5741  CG  ARG B 647    12906  14408  17731  -1310  -3824  -3663       C  
ATOM   5742  CD  ARG B 647     -46.684-103.464  17.708  1.00121.69           C  
ANISOU 5742  CD  ARG B 647    13365  14132  18736  -1482  -3971  -3571       C  
ATOM   5743  NE  ARG B 647     -47.291-104.728  17.281  1.00129.71           N  
ANISOU 5743  NE  ARG B 647    14207  14591  20484  -1644  -4546  -3934       N  
ATOM   5744  CZ  ARG B 647     -48.503-105.162  17.636  1.00133.79           C  
ANISOU 5744  CZ  ARG B 647    14396  14760  21678  -2049  -4699  -3673       C  
ATOM   5745  NH1 ARG B 647     -49.284-104.437  18.428  1.00132.21           N1+
ANISOU 5745  NH1 ARG B 647    14007  14772  21454  -2302  -4282  -3039       N1+
ATOM   5746  NH2 ARG B 647     -48.945-106.330  17.188  1.00139.93           N  
ANISOU 5746  NH2 ARG B 647    15003  14963  23200  -2191  -5280  -4065       N  
ATOM   5747  N   GLN B 648     -51.155-101.221  17.106  1.00123.67           N  
ANISOU 5747  N   GLN B 648    12564  15348  19076  -2009  -3873  -2997       N  
ATOM   5748  CA  GLN B 648     -52.342-101.920  16.623  1.00130.33           C  
ANISOU 5748  CA  GLN B 648    12999  15927  20592  -2238  -4364  -3242       C  
ATOM   5749  C   GLN B 648     -52.936-101.103  15.491  1.00130.97           C  
ANISOU 5749  C   GLN B 648    12993  16549  20218  -1964  -4576  -3607       C  
ATOM   5750  O   GLN B 648     -52.898-101.530  14.339  1.00134.51           O  
ANISOU 5750  O   GLN B 648    13484  17015  20606  -1728  -5105  -4265       O  
ATOM   5751  CB  GLN B 648     -53.364-102.122  17.740  1.00132.54           C  
ANISOU 5751  CB  GLN B 648    12876  15940  21539  -2701  -4129  -2608       C  
ATOM   5752  CG  GLN B 648     -52.991-103.201  18.754  1.00135.77           C  
ANISOU 5752  CG  GLN B 648    13320  15709  22557  -2999  -4042  -2245       C  
ATOM   5753  CD  GLN B 648     -53.713-103.040  20.097  1.00137.96           C  
ANISOU 5753  CD  GLN B 648    13332  15942  23144  -3336  -3525  -1410       C  
ATOM   5754  OE1 GLN B 648     -54.729-102.333  20.207  1.00138.05           O  
ANISOU 5754  OE1 GLN B 648    13002  16307  23144  -3422  -3328  -1169       O  
ATOM   5755  NE2 GLN B 648     -53.185-103.701  21.127  1.00138.91           N  
ANISOU 5755  NE2 GLN B 648    13613  15654  23510  -3482  -3297   -957       N  
ATOM   5756  N   LYS B 649     -53.445 -99.917  15.823  1.00128.14           N  
ANISOU 5756  N   LYS B 649    12545  16643  19496  -1942  -4175  -3191       N  
ATOM   5757  CA  LYS B 649     -53.990 -98.980  14.837  1.00128.89           C  
ANISOU 5757  CA  LYS B 649    12595  17281  19093  -1643  -4318  -3428       C  
ATOM   5758  C   LYS B 649     -53.196 -98.912  13.527  1.00129.86           C  
ANISOU 5758  C   LYS B 649    13077  17691  18573  -1170  -4602  -4018       C  
ATOM   5759  O   LYS B 649     -53.787 -99.013  12.444  1.00134.38           O  
ANISOU 5759  O   LYS B 649    13541  18440  19075   -962  -5104  -4507       O  
ATOM   5760  CB  LYS B 649     -54.124 -97.583  15.437  1.00123.80           C  
ANISOU 5760  CB  LYS B 649    11997  17073  17967  -1568  -3749  -2889       C  
ATOM   5761  CG  LYS B 649     -55.510 -97.256  15.968  1.00125.75           C  
ANISOU 5761  CG  LYS B 649    11762  17383  18634  -1810  -3671  -2549       C  
ATOM   5762  CD  LYS B 649     -55.458 -96.113  16.992  1.00121.65           C  
ANISOU 5762  CD  LYS B 649    11320  17137  17762  -1779  -3037  -1960       C  
ATOM   5763  CE  LYS B 649     -54.990 -94.773  16.407  1.00117.06           C  
ANISOU 5763  CE  LYS B 649    11066  17039  16370  -1364  -2874  -1995       C  
ATOM   5764  NZ  LYS B 649     -56.072 -94.057  15.674  1.00119.13           N1+
ANISOU 5764  NZ  LYS B 649    11081  17660  16521  -1190  -3093  -2101       N1+
ATOM   5765  N   ALA B 650     -51.871 -98.760  13.628  1.00126.43           N  
ANISOU 5765  N   ALA B 650    13042  17320  17674   -976  -4288  -3979       N  
ATOM   5766  CA  ALA B 650     -51.018 -98.568  12.449  1.00127.25           C  
ANISOU 5766  CA  ALA B 650    13479  17788  17080   -491  -4402  -4430       C  
ATOM   5767  C   ALA B 650     -50.878 -99.804  11.560  1.00133.33           C  
ANISOU 5767  C   ALA B 650    14273  18321  18063   -327  -5027  -5166       C  
ATOM   5768  O   ALA B 650     -50.911 -99.687  10.336  1.00136.56           O  
ANISOU 5768  O   ALA B 650    14798  19111  17975     95  -5343  -5652       O  
ATOM   5769  CB  ALA B 650     -49.654 -98.046  12.851  1.00122.16           C  
ANISOU 5769  CB  ALA B 650    13166  17273  15977   -358  -3866  -4158       C  
ATOM   5770  N   GLU B 651     -50.718-100.976  12.170  1.00135.63           N  
ANISOU 5770  N   GLU B 651    14475  17985  19072   -620  -5221  -5252       N  
ATOM   5771  CA  GLU B 651     -50.627-102.230  11.413  1.00142.57           C  
ANISOU 5771  CA  GLU B 651    15356  18517  20295   -483  -5883  -5991       C  
ATOM   5772  C   GLU B 651     -51.987-102.695  10.893  1.00149.24           C  
ANISOU 5772  C   GLU B 651    15820  19185  21697   -617  -6536  -6364       C  
ATOM   5773  O   GLU B 651     -52.070-103.620  10.075  1.00155.47           O  
ANISOU 5773  O   GLU B 651    16591  19743  22735   -434  -7207  -7098       O  
ATOM   5774  CB  GLU B 651     -49.965-103.326  12.245  1.00142.99           C  
ANISOU 5774  CB  GLU B 651    15454  17888  20984   -738  -5897  -5936       C  
ATOM   5775  CG  GLU B 651     -48.449-103.337  12.131  1.00141.14           C  
ANISOU 5775  CG  GLU B 651    15612  17800  20214   -385  -5628  -6070       C  
ATOM   5776  CD  GLU B 651     -47.793-104.271  13.130  1.00141.74           C  
ANISOU 5776  CD  GLU B 651    15740  17220  20893   -634  -5580  -5888       C  
ATOM   5777  OE1 GLU B 651     -47.784-103.930  14.333  1.00138.55           O  
ANISOU 5777  OE1 GLU B 651    15298  16683  20661   -961  -5125  -5194       O  
ATOM   5778  OE2 GLU B 651     -47.276-105.334  12.715  1.00145.59           O1-
ANISOU 5778  OE2 GLU B 651    16327  17337  21650   -457  -6012  -6449       O1-
ATOM   5779  N   ALA B 652     -53.044-102.050  11.387  1.00148.49           N  
ANISOU 5779  N   ALA B 652    15396  19194  21827   -918  -6358  -5887       N  
ATOM   5780  CA  ALA B 652     -54.398-102.247  10.889  1.00154.45           C  
ANISOU 5780  CA  ALA B 652    15719  19894  23068  -1029  -6924  -6181       C  
ATOM   5781  C   ALA B 652     -54.639-101.353   9.672  1.00155.61           C  
ANISOU 5781  C   ALA B 652    16009  20767  22346   -491  -7116  -6533       C  
ATOM   5782  O   ALA B 652     -55.180-101.808   8.671  1.00162.13           O  
ANISOU 5782  O   ALA B 652    16722  21621  23257   -256  -7831  -7220       O  
ATOM   5783  CB  ALA B 652     -55.421-101.959  11.988  1.00153.39           C  
ANISOU 5783  CB  ALA B 652    15123  19584  23574  -1562  -6605  -5489       C  
ATOM   5784  N   ASP B 653     -54.221-100.089   9.757  1.00150.16           N  
ANISOU 5784  N   ASP B 653    15579  20641  20831   -274  -6508  -6067       N  
ATOM   5785  CA  ASP B 653     -54.391 -99.138   8.653  1.00151.41           C  
ANISOU 5785  CA  ASP B 653    15921  21498  20110    253  -6599  -6254       C  
ATOM   5786  C   ASP B 653     -53.180 -98.200   8.466  1.00146.53           C  
ANISOU 5786  C   ASP B 653    15791  21365  18519    619  -5978  -5951       C  
ATOM   5787  O   ASP B 653     -53.135 -97.105   9.037  1.00141.58           O  
ANISOU 5787  O   ASP B 653    15204  20957  17631    535  -5408  -5320       O  
ATOM   5788  CB  ASP B 653     -55.682 -98.338   8.848  1.00151.68           C  
ANISOU 5788  CB  ASP B 653    15582  21730  20318    105  -6604  -5926       C  
ATOM   5789  CG  ASP B 653     -56.333 -97.939   7.530  1.00157.20           C  
ANISOU 5789  CG  ASP B 653    16295  22935  20497    608  -7144  -6403       C  
ATOM   5790  OD1 ASP B 653     -57.459 -97.394   7.573  1.00158.62           O  
ANISOU 5790  OD1 ASP B 653    16126  23262  20879    532  -7278  -6246       O  
ATOM   5791  OD2 ASP B 653     -55.731 -98.172   6.454  1.00160.70           O1-
ANISOU 5791  OD2 ASP B 653    17093  23656  20307   1120  -7441  -6939       O1-
ATOM   5792  N   LYS B 654     -52.220 -98.646   7.651  1.00148.85           N  
ANISOU 5792  N   LYS B 654    16421  21810  18323   1035  -6108  -6426       N  
ATOM   5793  CA  LYS B 654     -50.938 -97.956   7.387  1.00145.43           C  
ANISOU 5793  CA  LYS B 654    16399  21799  17056   1383  -5532  -6195       C  
ATOM   5794  C   LYS B 654     -51.054 -96.483   6.932  1.00143.92           C  
ANISOU 5794  C   LYS B 654    16363  22239  16079   1677  -5148  -5751       C  
ATOM   5795  O   LYS B 654     -50.378 -95.596   7.479  1.00138.28           O  
ANISOU 5795  O   LYS B 654    15781  21631  15127   1594  -4495  -5158       O  
ATOM   5796  CB  LYS B 654     -50.123 -98.784   6.374  1.00150.00           C  
ANISOU 5796  CB  LYS B 654    17240  22513  17237   1872  -5852  -6904       C  
ATOM   5797  CG  LYS B 654     -49.084 -98.017   5.581  1.00149.24           C  
ANISOU 5797  CG  LYS B 654    17520  23076  16108   2414  -5388  -6794       C  
ATOM   5798  CD  LYS B 654     -48.499 -98.854   4.461  1.00155.40           C  
ANISOU 5798  CD  LYS B 654    18523  24089  16432   2992  -5770  -7575       C  
ATOM   5799  CE  LYS B 654     -47.285 -98.167   3.833  1.00155.81           C  
ANISOU 5799  CE  LYS B 654    18900  24772  15526   3484  -5154  -7358       C  
ATOM   5800  NZ  LYS B 654     -46.140 -97.981   4.801  1.00149.75           N1+
ANISOU 5800  NZ  LYS B 654    18133  23763  15003   3164  -4476  -6854       N1+
ATOM   5801  N   ASN B 655     -51.910 -96.243   5.934  1.00149.26           N  
ANISOU 5801  N   ASN B 655    17019  23293  16398   2031  -5602  -6052       N  
ATOM   5802  CA  ASN B 655     -52.059 -94.927   5.290  1.00149.53           C  
ANISOU 5802  CA  ASN B 655    17245  23938  15631   2414  -5343  -5686       C  
ATOM   5803  C   ASN B 655     -53.174 -94.044   5.874  1.00147.35           C  
ANISOU 5803  C   ASN B 655    16694  23630  15661   2143  -5276  -5208       C  
ATOM   5804  O   ASN B 655     -53.514 -93.001   5.312  1.00148.14           O  
ANISOU 5804  O   ASN B 655    16916  24176  15192   2469  -5192  -4946       O  
ATOM   5805  CB  ASN B 655     -52.240 -95.103   3.780  1.00156.73           C  
ANISOU 5805  CB  ASN B 655    18370  25377  15802   3092  -5859  -6275       C  
ATOM   5806  CG  ASN B 655     -53.375 -96.051   3.434  1.00163.58           C  
ANISOU 5806  CG  ASN B 655    18939  26022  17192   3074  -6766  -6991       C  
ATOM   5807  OD1 ASN B 655     -53.796 -96.141   2.271  1.00172.12           O  
ANISOU 5807  OD1 ASN B 655    20136  27520  17739   3625  -7320  -7514       O  
ATOM   5808  ND2 ASN B 655     -53.882 -96.765   4.436  1.00161.69           N  
ANISOU 5808  ND2 ASN B 655    18299  25123  18011   2456  -6937  -7013       N  
ATOM   5809  N   ASP B 656     -53.709 -94.466   7.017  1.00145.12           N  
ANISOU 5809  N   ASP B 656    16046  22826  16267   1573  -5285  -5066       N  
ATOM   5810  CA  ASP B 656     -54.807 -93.786   7.710  1.00143.96           C  
ANISOU 5810  CA  ASP B 656    15560  22616  16520   1291  -5212  -4656       C  
ATOM   5811  C   ASP B 656     -54.460 -92.363   8.181  1.00139.10           C  
ANISOU 5811  C   ASP B 656    15125  22217  15509   1326  -4544  -3950       C  
ATOM   5812  O   ASP B 656     -53.464 -92.157   8.890  1.00134.35           O  
ANISOU 5812  O   ASP B 656    14699  21456  14891   1158  -4011  -3609       O  
ATOM   5813  CB  ASP B 656     -55.247 -94.644   8.901  1.00142.72           C  
ANISOU 5813  CB  ASP B 656    14999  21863  17362    686  -5244  -4597       C  
ATOM   5814  CG  ASP B 656     -56.521 -94.146   9.549  1.00143.06           C  
ANISOU 5814  CG  ASP B 656    14600  21871  17886    421  -5234  -4272       C  
ATOM   5815  OD1 ASP B 656     -56.597 -94.211  10.794  1.00139.90           O  
ANISOU 5815  OD1 ASP B 656    13998  21151  18007     -9  -4852  -3854       O  
ATOM   5816  OD2 ASP B 656     -57.440 -93.700   8.821  1.00147.06           O1-
ANISOU 5816  OD2 ASP B 656    14954  22693  18228    680  -5607  -4437       O1-
ATOM   5817  N   LYS B 657     -55.304 -91.396   7.814  1.00140.74           N  
ANISOU 5817  N   LYS B 657    15268  22745  15461   1549  -4625  -3760       N  
ATOM   5818  CA  LYS B 657     -55.016 -89.971   8.035  1.00137.51           C  
ANISOU 5818  CA  LYS B 657    15065  22541  14640   1678  -4089  -3145       C  
ATOM   5819  C   LYS B 657     -54.880 -89.526   9.509  1.00131.64           C  
ANISOU 5819  C   LYS B 657    14186  21457  14374   1246  -3569  -2648       C  
ATOM   5820  O   LYS B 657     -54.235 -88.507   9.797  1.00128.40           O  
ANISOU 5820  O   LYS B 657    14006  21096  13682   1313  -3090  -2199       O  
ATOM   5821  CB  LYS B 657     -56.059 -89.108   7.326  1.00141.28           C  
ANISOU 5821  CB  LYS B 657    15483  23389  14808   2035  -4373  -3084       C  
ATOM   5822  CG  LYS B 657     -55.473 -88.017   6.438  1.00143.42           C  
ANISOU 5822  CG  LYS B 657    16198  24077  14218   2530  -4121  -2761       C  
ATOM   5823  CD  LYS B 657     -56.578 -87.336   5.608  1.00150.66           C  
ANISOU 5823  CD  LYS B 657    17073  25367  14804   2956  -4537  -2777       C  
ATOM   5824  CE  LYS B 657     -56.181 -87.163   4.130  1.00156.92           C  
ANISOU 5824  CE  LYS B 657    18290  26678  14651   3595  -4710  -2899       C  
ATOM   5825  NZ  LYS B 657     -54.950 -86.323   3.954  1.00155.41           N1+
ANISOU 5825  NZ  LYS B 657    18528  26614  13905   3752  -4038  -2330       N1+
ATOM   5826  N   SER B 658     -55.479 -90.275  10.435  1.00130.93           N  
ANISOU 5826  N   SER B 658    13720  21022  15003    827  -3669  -2720       N  
ATOM   5827  CA  SER B 658     -55.434 -89.911  11.857  1.00126.09           C  
ANISOU 5827  CA  SER B 658    12984  20149  14774    486  -3199  -2274       C  
ATOM   5828  C   SER B 658     -54.196 -90.463  12.566  1.00122.08           C  
ANISOU 5828  C   SER B 658    12680  19336  14369    259  -2871  -2205       C  
ATOM   5829  O   SER B 658     -53.658 -89.817  13.480  1.00118.11           O  
ANISOU 5829  O   SER B 658    12288  18730  13855    162  -2418  -1825       O  
ATOM   5830  CB  SER B 658     -56.716 -90.325  12.581  1.00128.10           C  
ANISOU 5830  CB  SER B 658    12718  20245  15709    180  -3364  -2261       C  
ATOM   5831  OG  SER B 658     -56.959 -91.711  12.434  1.00132.02           O  
ANISOU 5831  OG  SER B 658    12982  20481  16698    -55  -3763  -2655       O  
ATOM   5832  N   VAL B 659     -53.744 -91.648  12.146  1.00123.35           N  
ANISOU 5832  N   VAL B 659    12886  19339  14640    211  -3144  -2611       N  
ATOM   5833  CA  VAL B 659     -52.445 -92.172  12.589  1.00119.67           C  
ANISOU 5833  CA  VAL B 659    12653  18629  14185     99  -2888  -2608       C  
ATOM   5834  C   VAL B 659     -51.331 -91.212  12.183  1.00116.73           C  
ANISOU 5834  C   VAL B 659    12643  18509  13196    385  -2513  -2407       C  
ATOM   5835  O   VAL B 659     -50.510 -90.850  13.003  1.00113.07           O  
ANISOU 5835  O   VAL B 659    12293  17890  12776    261  -2113  -2116       O  
ATOM   5836  CB  VAL B 659     -52.168 -93.589  12.053  1.00123.02           C  
ANISOU 5836  CB  VAL B 659    13075  18849  14814     81  -3307  -3143       C  
ATOM   5837  CG1 VAL B 659     -50.728 -93.990  12.302  1.00120.22           C  
ANISOU 5837  CG1 VAL B 659    12994  18329  14352     86  -3049  -3169       C  
ATOM   5838  CG2 VAL B 659     -53.099 -94.585  12.711  1.00125.59           C  
ANISOU 5838  CG2 VAL B 659    13013  18772  15932   -312  -3595  -3229       C  
ATOM   5839  N   LYS B 660     -51.334 -90.777  10.928  1.00119.10           N  
ANISOU 5839  N   LYS B 660    13106  19202  12942    777  -2647  -2538       N  
ATOM   5840  CA  LYS B 660     -50.369 -89.798  10.445  1.00117.82           C  
ANISOU 5840  CA  LYS B 660    13246  19298  12219   1049  -2255  -2256       C  
ATOM   5841  C   LYS B 660     -50.242 -88.574  11.357  1.00113.43           C  
ANISOU 5841  C   LYS B 660    12701  18632  11766    913  -1817  -1710       C  
ATOM   5842  O   LYS B 660     -49.155 -88.286  11.882  1.00110.31           O  
ANISOU 5842  O   LYS B 660    12426  18083  11402    819  -1442  -1502       O  
ATOM   5843  CB  LYS B 660     -50.693 -89.383   9.007  1.00122.68           C  
ANISOU 5843  CB  LYS B 660    14017  20397  12198   1523  -2463  -2367       C  
ATOM   5844  CG  LYS B 660     -50.305 -90.440   7.951  1.00128.29           C  
ANISOU 5844  CG  LYS B 660    14851  21302  12590   1808  -2792  -2929       C  
ATOM   5845  CD  LYS B 660     -50.473 -89.960   6.503  1.00134.97           C  
ANISOU 5845  CD  LYS B 660    15924  22715  12642   2378  -2941  -3001       C  
ATOM   5846  CE  LYS B 660     -49.590 -88.752   6.193  1.00135.55           C  
ANISOU 5846  CE  LYS B 660    16260  23049  12193   2591  -2343  -2416       C  
ATOM   5847  NZ  LYS B 660     -49.942 -87.552   7.031  1.00131.88           N1+
ANISOU 5847  NZ  LYS B 660    15710  22379  12017   2348  -2043  -1827       N1+
ATOM   5848  N   ASP B 661     -51.350 -87.872  11.575  1.00113.44           N  
ANISOU 5848  N   ASP B 661    12549  18690  11860    919  -1902  -1523       N  
ATOM   5849  CA  ASP B 661     -51.315 -86.658  12.405  1.00110.16           C  
ANISOU 5849  CA  ASP B 661    12150  18163  11539    856  -1548  -1068       C  
ATOM   5850  C   ASP B 661     -50.979 -86.927  13.867  1.00105.04           C  
ANISOU 5850  C   ASP B 661    11406  17154  11350    514  -1330   -977       C  
ATOM   5851  O   ASP B 661     -50.416 -86.067  14.540  1.00102.31           O  
ANISOU 5851  O   ASP B 661    11159  16673  11040    488  -1019   -693       O  
ATOM   5852  CB  ASP B 661     -52.587 -85.805  12.257  1.00112.55           C  
ANISOU 5852  CB  ASP B 661    12315  18635  11813   1015  -1702   -916       C  
ATOM   5853  CG  ASP B 661     -52.467 -84.753  11.125  1.00117.51           C  
ANISOU 5853  CG  ASP B 661    13191  19558  11899   1415  -1663   -687       C  
ATOM   5854  OD1 ASP B 661     -52.595 -85.123   9.916  1.00122.76           O  
ANISOU 5854  OD1 ASP B 661    13954  20536  12152   1694  -1931   -904       O  
ATOM   5855  OD2 ASP B 661     -52.247 -83.552  11.456  1.00117.54           O1-
ANISOU 5855  OD2 ASP B 661    13300  19467  11892   1473  -1379   -286       O1-
ATOM   5856  N   LEU B 662     -51.299 -88.132  14.334  1.00103.97           N  
ANISOU 5856  N   LEU B 662    11086  16847  11569    275  -1520  -1221       N  
ATOM   5857  CA  LEU B 662     -50.870 -88.586  15.651  1.00 99.94           C  
ANISOU 5857  CA  LEU B 662    10534  16016  11422     -6  -1327  -1131       C  
ATOM   5858  C   LEU B 662     -49.357 -88.840  15.709  1.00 97.08           C  
ANISOU 5858  C   LEU B 662    10409  15512  10964    -14  -1141  -1178       C  
ATOM   5859  O   LEU B 662     -48.688 -88.456  16.679  1.00 94.51           O  
ANISOU 5859  O   LEU B 662    10159  15003  10747    -99   -884   -989       O  
ATOM   5860  CB  LEU B 662     -51.620 -89.850  16.071  1.00101.82           C  
ANISOU 5860  CB  LEU B 662    10507  16076  12105   -264  -1569  -1306       C  
ATOM   5861  CG  LEU B 662     -51.142 -90.382  17.430  1.00100.07           C  
ANISOU 5861  CG  LEU B 662    10286  15535  12199   -515  -1356  -1151       C  
ATOM   5862  CD1 LEU B 662     -51.705 -89.521  18.569  1.00 99.23           C  
ANISOU 5862  CD1 LEU B 662    10079  15463  12158   -535  -1081   -800       C  
ATOM   5863  CD2 LEU B 662     -51.456 -91.866  17.644  1.00101.76           C  
ANISOU 5863  CD2 LEU B 662    10320  15478  12867   -777  -1593  -1321       C  
ATOM   5864  N   VAL B 663     -48.820 -89.486  14.677  1.00 97.42           N  
ANISOU 5864  N   VAL B 663    10553  15657  10805    110  -1292  -1465       N  
ATOM   5865  CA  VAL B 663     -47.387 -89.727  14.617  1.00 94.74           C  
ANISOU 5865  CA  VAL B 663    10386  15236  10372    146  -1105  -1531       C  
ATOM   5866  C   VAL B 663     -46.595 -88.404  14.674  1.00 92.43           C  
ANISOU 5866  C   VAL B 663    10221  15010   9887    250   -730  -1190       C  
ATOM   5867  O   VAL B 663     -45.610 -88.288  15.417  1.00 89.94           O  
ANISOU 5867  O   VAL B 663     9946  14483   9742    148   -520  -1102       O  
ATOM   5868  CB  VAL B 663     -46.993 -90.588  13.396  1.00 97.90           C  
ANISOU 5868  CB  VAL B 663    10867  15811  10519    349  -1319  -1929       C  
ATOM   5869  CG1 VAL B 663     -45.471 -90.648  13.246  1.00 96.27           C  
ANISOU 5869  CG1 VAL B 663    10800  15602  10174    445  -1050  -1956       C  
ATOM   5870  CG2 VAL B 663     -47.568 -91.990  13.540  1.00 98.48           C  
ANISOU 5870  CG2 VAL B 663    10803  15654  10959    190  -1723  -2299       C  
ATOM   5871  N   ILE B 664     -47.048 -87.400  13.928  1.00 92.80           N  
ANISOU 5871  N   ILE B 664    10315  15312   9632    452   -678   -990       N  
ATOM   5872  CA  ILE B 664     -46.367 -86.115  13.951  1.00 90.95           C  
ANISOU 5872  CA  ILE B 664    10177  15065   9313    526   -344   -624       C  
ATOM   5873  C   ILE B 664     -46.508 -85.480  15.326  1.00 87.58           C  
ANISOU 5873  C   ILE B 664     9688  14337   9251    346   -247   -439       C  
ATOM   5874  O   ILE B 664     -45.546 -84.921  15.861  1.00 86.13           O  
ANISOU 5874  O   ILE B 664     9544  13950   9230    285    -29   -298       O  
ATOM   5875  CB  ILE B 664     -46.891 -85.165  12.883  1.00 93.66           C  
ANISOU 5875  CB  ILE B 664    10606  15706   9274    799   -325   -390       C  
ATOM   5876  CG1 ILE B 664     -46.689 -85.773  11.491  1.00 97.65           C  
ANISOU 5876  CG1 ILE B 664    11214  16584   9303   1068   -417   -591       C  
ATOM   5877  CG2 ILE B 664     -46.145 -83.868  12.973  1.00 93.38           C  
ANISOU 5877  CG2 ILE B 664    10648  15552   9278    826     22     32       C  
ATOM   5878  CD1 ILE B 664     -47.603 -85.231  10.418  1.00100.01           C  
ANISOU 5878  CD1 ILE B 664    11596  17240   9162   1390   -580   -488       C  
ATOM   5879  N   LEU B 665     -47.706 -85.589  15.897  1.00 86.47           N  
ANISOU 5879  N   LEU B 665     9425  14182   9247    283   -422   -466       N  
ATOM   5880  CA  LEU B 665     -48.007 -84.978  17.183  1.00 83.90           C  
ANISOU 5880  CA  LEU B 665     9046  13656   9174    200   -334   -316       C  
ATOM   5881  C   LEU B 665     -47.156 -85.565  18.328  1.00 81.42           C  
ANISOU 5881  C   LEU B 665     8755  13075   9104     25   -256   -404       C  
ATOM   5882  O   LEU B 665     -46.612 -84.817  19.167  1.00 79.58           O  
ANISOU 5882  O   LEU B 665     8581  12656   8999     34   -127   -299       O  
ATOM   5883  CB  LEU B 665     -49.505 -85.076  17.464  1.00 84.78           C  
ANISOU 5883  CB  LEU B 665     8969  13885   9356    201   -497   -321       C  
ATOM   5884  CG  LEU B 665     -50.170 -84.058  18.401  1.00 84.27           C  
ANISOU 5884  CG  LEU B 665     8841  13773   9403    278   -405   -137       C  
ATOM   5885  CD1 LEU B 665     -50.447 -84.683  19.722  1.00 83.22           C  
ANISOU 5885  CD1 LEU B 665     8595  13535   9488    131   -355   -169       C  
ATOM   5886  CD2 LEU B 665     -49.381 -82.747  18.582  1.00 84.46           C  
ANISOU 5886  CD2 LEU B 665     9042  13628   9421    405   -238     38       C  
ATOM   5887  N   LEU B 666     -47.033 -86.895  18.343  1.00 80.99           N  
ANISOU 5887  N   LEU B 666     8662  12981   9128   -103   -381   -615       N  
ATOM   5888  CA  LEU B 666     -45.988 -87.557  19.129  1.00 79.34           C  
ANISOU 5888  CA  LEU B 666     8517  12532   9094   -215   -336   -711       C  
ATOM   5889  C   LEU B 666     -44.591 -86.973  18.845  1.00 78.37           C  
ANISOU 5889  C   LEU B 666     8491  12344   8939   -145   -170   -695       C  
ATOM   5890  O   LEU B 666     -43.898 -86.531  19.764  1.00 76.95           O  
ANISOU 5890  O   LEU B 666     8347  11963   8927   -166    -89   -647       O  
ATOM   5891  CB  LEU B 666     -45.986 -89.068  18.886  1.00 80.25           C  
ANISOU 5891  CB  LEU B 666     8594  12586   9310   -326   -528   -952       C  
ATOM   5892  CG  LEU B 666     -47.170 -89.815  19.507  1.00 81.69           C  
ANISOU 5892  CG  LEU B 666     8626  12703   9710   -483   -665   -918       C  
ATOM   5893  CD1 LEU B 666     -47.067 -91.302  19.235  1.00 83.49           C  
ANISOU 5893  CD1 LEU B 666     8817  12764  10142   -609   -894  -1160       C  
ATOM   5894  CD2 LEU B 666     -47.230 -89.577  20.993  1.00 80.73           C  
ANISOU 5894  CD2 LEU B 666     8517  12446   9710   -535   -513   -699       C  
ATOM   5895  N   TYR B 667     -44.201 -86.947  17.577  1.00 79.31           N  
ANISOU 5895  N   TYR B 667     8634  12651   8850    -40   -121   -734       N  
ATOM   5896  CA  TYR B 667     -42.912 -86.414  17.226  1.00 79.75           C  
ANISOU 5896  CA  TYR B 667     8712  12676   8912     11     96   -661       C  
ATOM   5897  C   TYR B 667     -42.749 -84.992  17.757  1.00 79.16           C  
ANISOU 5897  C   TYR B 667     8635  12441   9001     11    242   -388       C  
ATOM   5898  O   TYR B 667     -41.765 -84.656  18.411  1.00 77.98           O  
ANISOU 5898  O   TYR B 667     8453  12056   9120    -50    319   -385       O  
ATOM   5899  CB  TYR B 667     -42.700 -86.467  15.717  1.00 82.36           C  
ANISOU 5899  CB  TYR B 667     9070  13325   8896    187    188   -662       C  
ATOM   5900  CG  TYR B 667     -41.583 -85.570  15.246  1.00 85.18           C  
ANISOU 5900  CG  TYR B 667     9403  13702   9257    248    514   -417       C  
ATOM   5901  CD1 TYR B 667     -40.244 -85.960  15.355  1.00 87.83           C  
ANISOU 5901  CD1 TYR B 667     9651  13948   9770    209    658   -528       C  
ATOM   5902  CD2 TYR B 667     -41.856 -84.318  14.708  1.00 88.13           C  
ANISOU 5902  CD2 TYR B 667     9811  14158   9517    340    684    -43       C  
ATOM   5903  CE1 TYR B 667     -39.199 -85.112  14.924  1.00 90.63           C  
ANISOU 5903  CE1 TYR B 667     9902  14311  10223    231    998   -258       C  
ATOM   5904  CE2 TYR B 667     -40.832 -83.466  14.281  1.00 91.83           C  
ANISOU 5904  CE2 TYR B 667    10218  14593  10079    357   1019    264       C  
ATOM   5905  CZ  TYR B 667     -39.509 -83.867  14.389  1.00 92.93           C  
ANISOU 5905  CZ  TYR B 667    10220  14657  10429    286   1190    161       C  
ATOM   5906  OH  TYR B 667     -38.514 -83.019  13.960  1.00 96.16           O  
ANISOU 5906  OH  TYR B 667    10495  15028  11011    272   1551    505       O  
ATOM   5907  N   GLU B 668     -43.738 -84.164  17.476  1.00 80.49           N  
ANISOU 5907  N   GLU B 668     8826  12711   9043     98    231   -194       N  
ATOM   5908  CA  GLU B 668     -43.690 -82.760  17.830  1.00 81.24           C  
ANISOU 5908  CA  GLU B 668     8932  12622   9311    136    328     52       C  
ATOM   5909  C   GLU B 668     -43.563 -82.608  19.360  1.00 79.34           C  
ANISOU 5909  C   GLU B 668     8683  12094   9368     68    233    -67       C  
ATOM   5910  O   GLU B 668     -42.825 -81.767  19.866  1.00 79.56           O  
ANISOU 5910  O   GLU B 668     8700  11852   9676     58    275    -19       O  
ATOM   5911  CB  GLU B 668     -44.950 -82.090  17.297  1.00 82.65           C  
ANISOU 5911  CB  GLU B 668     9141  12976   9284    285    267    231       C  
ATOM   5912  CG  GLU B 668     -44.688 -80.965  16.307  1.00 87.25           C  
ANISOU 5912  CG  GLU B 668     9781  13584   9786    412    441    580       C  
ATOM   5913  CD  GLU B 668     -45.852 -80.709  15.301  1.00 91.63           C  
ANISOU 5913  CD  GLU B 668    10394  14451   9969    627    346    724       C  
ATOM   5914  OE1 GLU B 668     -47.058 -80.856  15.683  1.00 90.08           O  
ANISOU 5914  OE1 GLU B 668    10146  14339   9741    675    131    600       O  
ATOM   5915  OE2 GLU B 668     -45.536 -80.338  14.130  1.00 93.26           O1-
ANISOU 5915  OE2 GLU B 668    10683  14836   9914    771    499    981       O1-
ATOM   5916  N   THR B 669     -44.268 -83.452  20.099  1.00 78.06           N  
ANISOU 5916  N   THR B 669     8518  11989   9153     35     96   -226       N  
ATOM   5917  CA  THR B 669     -44.220 -83.392  21.552  1.00 76.93           C  
ANISOU 5917  CA  THR B 669     8402  11660   9167     43     23   -320       C  
ATOM   5918  C   THR B 669     -42.843 -83.778  22.108  1.00 76.14           C  
ANISOU 5918  C   THR B 669     8321  11340   9266    -22      2   -479       C  
ATOM   5919  O   THR B 669     -42.317 -83.106  22.990  1.00 76.04           O  
ANISOU 5919  O   THR B 669     8335  11109   9446     38    -56   -541       O  
ATOM   5920  CB  THR B 669     -45.354 -84.234  22.155  1.00 76.43           C  
ANISOU 5920  CB  THR B 669     8306  11747   8985     27    -49   -353       C  
ATOM   5921  OG1 THR B 669     -46.584 -83.555  21.920  1.00 78.41           O  
ANISOU 5921  OG1 THR B 669     8491  12163   9136    134    -44   -225       O  
ATOM   5922  CG2 THR B 669     -45.202 -84.356  23.618  1.00 76.04           C  
ANISOU 5922  CG2 THR B 669     8318  11576   8995     80    -83   -420       C  
ATOM   5923  N   ALA B 670     -42.278 -84.858  21.572  1.00 76.12           N  
ANISOU 5923  N   ALA B 670     8294  11396   9229   -114     10   -584       N  
ATOM   5924  CA  ALA B 670     -40.941 -85.329  21.920  1.00 75.78           C  
ANISOU 5924  CA  ALA B 670     8232  11177   9383   -155    -18   -749       C  
ATOM   5925  C   ALA B 670     -39.891 -84.280  21.625  1.00 77.08           C  
ANISOU 5925  C   ALA B 670     8298  11186   9801   -157     91   -688       C  
ATOM   5926  O   ALA B 670     -38.998 -84.052  22.432  1.00 77.39           O  
ANISOU 5926  O   ALA B 670     8296  10988  10119   -154     -2   -817       O  
ATOM   5927  CB  ALA B 670     -40.630 -86.591  21.173  1.00 76.19           C  
ANISOU 5927  CB  ALA B 670     8262  11343   9343   -206    -24   -882       C  
ATOM   5928  N   LEU B 671     -40.019 -83.629  20.477  1.00 78.65           N  
ANISOU 5928  N   LEU B 671     8448  11511   9924   -153    277   -473       N  
ATOM   5929  CA  LEU B 671     -39.156 -82.506  20.108  1.00 81.06           C  
ANISOU 5929  CA  LEU B 671     8629  11641  10527   -184    436   -293       C  
ATOM   5930  C   LEU B 671     -39.063 -81.462  21.219  1.00 81.82           C  
ANISOU 5930  C   LEU B 671     8724  11385  10979   -169    275   -331       C  
ATOM   5931  O   LEU B 671     -37.981 -81.089  21.629  1.00 83.13           O  
ANISOU 5931  O   LEU B 671     8751  11277  11557   -230    233   -418       O  
ATOM   5932  CB  LEU B 671     -39.675 -81.862  18.817  1.00 82.64           C  
ANISOU 5932  CB  LEU B 671     8846  12046  10507   -130    650     40       C  
ATOM   5933  CG  LEU B 671     -38.738 -81.180  17.827  1.00 84.52           C  
ANISOU 5933  CG  LEU B 671     8942  12273  10899   -162    959    341       C  
ATOM   5934  CD1 LEU B 671     -37.538 -82.035  17.541  1.00 84.16           C  
ANISOU 5934  CD1 LEU B 671     8737  12317  10919   -208   1095    189       C  
ATOM   5935  CD2 LEU B 671     -39.494 -80.941  16.555  1.00 85.86           C  
ANISOU 5935  CD2 LEU B 671     9217  12773  10632    -24   1125    639       C  
ATOM   5936  N   LEU B 672     -40.208 -81.015  21.714  1.00 82.13           N  
ANISOU 5936  N   LEU B 672     8893  11439  10871    -62    158   -307       N  
ATOM   5937  CA  LEU B 672     -40.262 -80.018  22.774  1.00 84.17           C  
ANISOU 5937  CA  LEU B 672     9184  11397  11398     33    -31   -408       C  
ATOM   5938  C   LEU B 672     -39.698 -80.472  24.107  1.00 84.06           C  
ANISOU 5938  C   LEU B 672     9205  11243  11489     93   -269   -746       C  
ATOM   5939  O   LEU B 672     -38.972 -79.736  24.777  1.00 85.63           O  
ANISOU 5939  O   LEU B 672     9349  11115  12069    134   -450   -911       O  
ATOM   5940  CB  LEU B 672     -41.701 -79.609  23.001  1.00 84.10           C  
ANISOU 5940  CB  LEU B 672     9299  11528  11126    195    -82   -341       C  
ATOM   5941  CG  LEU B 672     -42.175 -78.447  22.147  1.00 87.77           C  
ANISOU 5941  CG  LEU B 672     9753  11923  11671    240     11    -48       C  
ATOM   5942  CD1 LEU B 672     -43.606 -78.093  22.565  1.00 88.79           C  
ANISOU 5942  CD1 LEU B 672     9972  12195  11566    449    -83    -58       C  
ATOM   5943  CD2 LEU B 672     -41.219 -77.230  22.283  1.00 91.72           C  
ANISOU 5943  CD2 LEU B 672    10168  11947  12734    199    -41     -4       C  
ATOM   5944  N   SER B 673     -40.060 -81.683  24.501  1.00 82.86           N  
ANISOU 5944  N   SER B 673     9147  11320  11013    116   -299   -846       N  
ATOM   5945  CA  SER B 673     -39.687 -82.174  25.804  1.00 83.66           C  
ANISOU 5945  CA  SER B 673     9339  11343  11103    234   -519  -1104       C  
ATOM   5946  C   SER B 673     -38.269 -82.720  25.796  1.00 84.70           C  
ANISOU 5946  C   SER B 673     9356  11321  11505    143   -592  -1269       C  
ATOM   5947  O   SER B 673     -37.741 -83.078  26.860  1.00 85.88           O  
ANISOU 5947  O   SER B 673     9574  11370  11686    268   -826  -1505       O  
ATOM   5948  CB  SER B 673     -40.671 -83.238  26.267  1.00 82.21           C  
ANISOU 5948  CB  SER B 673     9293  11431  10513    290   -494  -1058       C  
ATOM   5949  OG  SER B 673     -40.793 -84.237  25.272  1.00 82.54           O  
ANISOU 5949  OG  SER B 673     9275  11631  10452    113   -352   -948       O  
ATOM   5950  N   SER B 674     -37.654 -82.791  24.609  1.00 85.29           N  
ANISOU 5950  N   SER B 674     9252  11409  11742    -29   -391  -1147       N  
ATOM   5951  CA  SER B 674     -36.227 -83.158  24.494  1.00 86.47           C  
ANISOU 5951  CA  SER B 674     9208  11422  12224   -105   -418  -1298       C  
ATOM   5952  C   SER B 674     -35.340 -81.969  24.187  1.00 88.96           C  
ANISOU 5952  C   SER B 674     9270  11457  13074   -202   -374  -1243       C  
ATOM   5953  O   SER B 674     -34.269 -82.144  23.638  1.00 90.99           O  
ANISOU 5953  O   SER B 674     9275  11673  13624   -311   -249  -1242       O  
ATOM   5954  CB  SER B 674     -35.990 -84.228  23.424  1.00 85.91           C  
ANISOU 5954  CB  SER B 674     9071  11591  11978   -191   -204  -1237       C  
ATOM   5955  OG  SER B 674     -36.769 -85.391  23.648  1.00 85.94           O  
ANISOU 5955  OG  SER B 674     9271  11773  11607   -142   -276  -1288       O  
ATOM   5956  N   GLY B 675     -35.782 -80.763  24.513  1.00 89.93           N  
ANISOU 5956  N   GLY B 675     9429  11371  13367   -160   -465  -1187       N  
ATOM   5957  CA  GLY B 675     -34.917 -79.594  24.399  1.00 93.42           C  
ANISOU 5957  CA  GLY B 675     9612  11425  14458   -270   -496  -1152       C  
ATOM   5958  C   GLY B 675     -34.927 -78.852  23.077  1.00 95.47           C  
ANISOU 5958  C   GLY B 675     9717  11673  14883   -438   -122   -701       C  
ATOM   5959  O   GLY B 675     -34.268 -77.833  22.931  1.00 99.01           O  
ANISOU 5959  O   GLY B 675     9929  11752  15937   -564   -110   -581       O  
ATOM   5960  N   PHE B 676     -35.681 -79.349  22.111  1.00 94.04           N  
ANISOU 5960  N   PHE B 676     9667  11882  14183   -427    165   -437       N  
ATOM   5961  CA  PHE B 676     -35.695 -78.740  20.794  1.00 96.62           C  
ANISOU 5961  CA  PHE B 676     9892  12281  14536   -518    538     25       C  
ATOM   5962  C   PHE B 676     -36.811 -77.724  20.582  1.00 97.77           C  
ANISOU 5962  C   PHE B 676    10216  12353  14580   -436    532    287       C  
ATOM   5963  O   PHE B 676     -37.638 -77.486  21.455  1.00 96.45           O  
ANISOU 5963  O   PHE B 676    10233  12103  14311   -297    253     82       O  
ATOM   5964  CB  PHE B 676     -35.746 -79.818  19.723  1.00 95.47           C  
ANISOU 5964  CB  PHE B 676     9774  12622  13877   -494    829    133       C  
ATOM   5965  CG  PHE B 676     -34.499 -80.627  19.632  1.00 95.59           C  
ANISOU 5965  CG  PHE B 676     9553  12696  14071   -558    920    -40       C  
ATOM   5966  CD1 PHE B 676     -33.415 -80.172  18.884  1.00 99.06           C  
ANISOU 5966  CD1 PHE B 676     9660  13080  14896   -679   1251    223       C  
ATOM   5967  CD2 PHE B 676     -34.396 -81.843  20.295  1.00 92.89           C  
ANISOU 5967  CD2 PHE B 676     9295  12456  13542   -488    691   -438       C  
ATOM   5968  CE1 PHE B 676     -32.257 -80.908  18.797  1.00 99.80           C  
ANISOU 5968  CE1 PHE B 676     9484  13257  15179   -708   1348     45       C  
ATOM   5969  CE2 PHE B 676     -33.225 -82.608  20.213  1.00 93.36           C  
ANISOU 5969  CE2 PHE B 676     9127  12558  13786   -507    744   -627       C  
ATOM   5970  CZ  PHE B 676     -32.159 -82.135  19.465  1.00 97.76           C  
ANISOU 5970  CZ  PHE B 676     9328  13096  14720   -607   1070   -411       C  
ATOM   5971  N   SER B 677     -36.842 -77.176  19.377  1.00101.24           N  
ANISOU 5971  N   SER B 677    10603  12869  14994   -481    864    758       N  
ATOM   5972  CA  SER B 677     -37.554 -75.962  19.057  1.00104.04           C  
ANISOU 5972  CA  SER B 677    11053  13022  15455   -424    881   1099       C  
ATOM   5973  C   SER B 677     -38.304 -76.157  17.739  1.00105.03           C  
ANISOU 5973  C   SER B 677    11327  13603  14974   -307   1171   1485       C  
ATOM   5974  O   SER B 677     -37.677 -76.425  16.713  1.00107.45           O  
ANISOU 5974  O   SER B 677    11524  14147  15154   -352   1527   1772       O  
ATOM   5975  CB  SER B 677     -36.494 -74.877  18.895  1.00108.98           C  
ANISOU 5975  CB  SER B 677    11395  13144  16866   -621   1000   1384       C  
ATOM   5976  OG  SER B 677     -37.059 -73.593  18.833  1.00112.82           O  
ANISOU 5976  OG  SER B 677    11964  13259  17642   -576    922   1664       O  
ATOM   5977  N   LEU B 678     -39.631 -76.021  17.754  1.00104.24           N  
ANISOU 5977  N   LEU B 678    11462  13657  14487   -120   1014   1479       N  
ATOM   5978  CA  LEU B 678     -40.451 -76.302  16.556  1.00105.85           C  
ANISOU 5978  CA  LEU B 678    11817  14330  14068     42   1184   1752       C  
ATOM   5979  C   LEU B 678     -40.068 -75.496  15.318  1.00111.61           C  
ANISOU 5979  C   LEU B 678    12519  15062  14824     60   1538   2362       C  
ATOM   5980  O   LEU B 678     -39.898 -74.275  15.400  1.00115.24           O  
ANISOU 5980  O   LEU B 678    12933  15071  15780      8   1560   2681       O  
ATOM   5981  CB  LEU B 678     -41.931 -76.062  16.830  1.00104.25           C  
ANISOU 5981  CB  LEU B 678    11802  14218  13590    241    926   1668       C  
ATOM   5982  CG  LEU B 678     -42.778 -77.075  17.603  1.00101.15           C  
ANISOU 5982  CG  LEU B 678    11468  14071  12891    298    677   1216       C  
ATOM   5983  CD1 LEU B 678     -42.342 -78.504  17.348  1.00 99.77           C  
ANISOU 5983  CD1 LEU B 678    11253  14218  12433    212    745    991       C  
ATOM   5984  CD2 LEU B 678     -42.739 -76.772  19.082  1.00100.59           C  
ANISOU 5984  CD2 LEU B 678    11377  13656  13186    281    438    900       C  
ATOM   5985  N   GLU B 679     -39.948 -76.173  14.173  1.00113.42           N  
ANISOU 5985  N   GLU B 679    12785  15792  14515    162   1809   2530       N  
ATOM   5986  CA  GLU B 679     -39.733 -75.498  12.882  1.00119.24           C  
ANISOU 5986  CA  GLU B 679    13552  16673  15078    270   2191   3172       C  
ATOM   5987  C   GLU B 679     -40.839 -74.470  12.643  1.00120.66           C  
ANISOU 5987  C   GLU B 679    13940  16724  15178    455   2047   3497       C  
ATOM   5988  O   GLU B 679     -40.554 -73.334  12.262  1.00125.54           O  
ANISOU 5988  O   GLU B 679    14537  17020  16141    431   2244   4054       O  
ATOM   5989  CB  GLU B 679     -39.629 -76.499  11.707  1.00121.16           C  
ANISOU 5989  CB  GLU B 679    13867  17590  14576    473   2434   3193       C  
ATOM   5990  CG  GLU B 679     -40.603 -77.720  11.748  1.00119.83           C  
ANISOU 5990  CG  GLU B 679    13866  17841  13822    641   2091   2642       C  
ATOM   5991  CD  GLU B 679     -40.127 -78.871  12.674  1.00118.67           C  
ANISOU 5991  CD  GLU B 679    13586  17636  13865    460   1915   2046       C  
ATOM   5992  OE1 GLU B 679     -38.947 -79.298  12.544  1.00119.83           O  
ANISOU 5992  OE1 GLU B 679    13556  17821  14153    369   2161   2010       O  
ATOM   5993  OE2 GLU B 679     -40.939 -79.346  13.522  1.00115.40           O1-
ANISOU 5993  OE2 GLU B 679    13234  17149  13461    427   1546   1647       O1-
ATOM   5994  N   ASP B 680     -42.090 -74.873  12.905  1.00116.71           N  
ANISOU 5994  N   ASP B 680    13610  16442  14291    632   1697   3155       N  
ATOM   5995  CA  ASP B 680     -43.269 -73.999  12.807  1.00117.22           C  
ANISOU 5995  CA  ASP B 680    13845  16413  14279    850   1486   3349       C  
ATOM   5996  C   ASP B 680     -44.163 -74.217  14.046  1.00111.67           C  
ANISOU 5996  C   ASP B 680    13135  15585  13707    852   1075   2809       C  
ATOM   5997  O   ASP B 680     -44.763 -75.293  14.197  1.00108.73           O  
ANISOU 5997  O   ASP B 680    12769  15589  12952    895    914   2411       O  
ATOM   5998  CB  ASP B 680     -44.033 -74.315  11.511  1.00119.94           C  
ANISOU 5998  CB  ASP B 680    14383  17340  13847   1174   1525   3560       C  
ATOM   5999  CG  ASP B 680     -44.882 -73.147  11.004  1.00125.14           C  
ANISOU 5999  CG  ASP B 680    15216  17883  14447   1436   1442   4022       C  
ATOM   6000  OD1 ASP B 680     -44.915 -72.070  11.649  1.00127.59           O  
ANISOU 6000  OD1 ASP B 680    15500  17625  15351   1364   1353   4177       O  
ATOM   6001  OD2 ASP B 680     -45.520 -73.316   9.937  1.00128.20           O1-
ANISOU 6001  OD2 ASP B 680    15778  18745  14186   1752   1428   4206       O1-
ATOM   6002  N   PRO B 681     -44.241 -73.221  14.958  1.00110.76           N  
ANISOU 6002  N   PRO B 681    12991  14937  14153    817    906   2785       N  
ATOM   6003  CA  PRO B 681     -45.023 -73.491  16.165  1.00105.84           C  
ANISOU 6003  CA  PRO B 681    12354  14281  13576    868    580   2271       C  
ATOM   6004  C   PRO B 681     -46.529 -73.360  15.980  1.00104.92           C  
ANISOU 6004  C   PRO B 681    12331  14432  13101   1157    372   2244       C  
ATOM   6005  O   PRO B 681     -47.259 -73.966  16.750  1.00101.84           O  
ANISOU 6005  O   PRO B 681    11887  14225  12583   1198    190   1845       O  
ATOM   6006  CB  PRO B 681     -44.504 -72.458  17.165  1.00106.95           C  
ANISOU 6006  CB  PRO B 681    12438  13782  14415    794    450   2199       C  
ATOM   6007  CG  PRO B 681     -44.043 -71.339  16.338  1.00112.67           C  
ANISOU 6007  CG  PRO B 681    13183  14158  15468    779    623   2772       C  
ATOM   6008  CD  PRO B 681     -43.577 -71.908  15.020  1.00114.82           C  
ANISOU 6008  CD  PRO B 681    13463  14849  15314    730    990   3166       C  
ATOM   6009  N   GLN B 682     -46.993 -72.598  14.983  1.00107.81           N  
ANISOU 6009  N   GLN B 682    12814  14832  13314   1366    406   2683       N  
ATOM   6010  CA  GLN B 682     -48.445 -72.467  14.749  1.00107.68           C  
ANISOU 6010  CA  GLN B 682    12851  15089  12971   1675    168   2642       C  
ATOM   6011  C   GLN B 682     -49.091 -73.690  14.113  1.00105.43           C  
ANISOU 6011  C   GLN B 682    12540  15429  12090   1740    110   2449       C  
ATOM   6012  O   GLN B 682     -50.249 -73.991  14.393  1.00104.37           O  
ANISOU 6012  O   GLN B 682    12320  15528  11808   1882   -126   2186       O  
ATOM   6013  CB  GLN B 682     -48.864 -71.187  13.996  1.00112.87           C  
ANISOU 6013  CB  GLN B 682    13658  15543  13682   1945    134   3147       C  
ATOM   6014  CG  GLN B 682     -47.949 -70.739  12.881  1.00117.78           C  
ANISOU 6014  CG  GLN B 682    14400  16078  14273   1904    448   3760       C  
ATOM   6015  CD  GLN B 682     -47.061 -69.570  13.302  1.00121.89           C  
ANISOU 6015  CD  GLN B 682    14898  15867  15544   1739    552   4063       C  
ATOM   6016  OE1 GLN B 682     -46.784 -68.671  12.506  1.00127.23           O  
ANISOU 6016  OE1 GLN B 682    15684  16302  16354   1813    718   4687       O  
ATOM   6017  NE2 GLN B 682     -46.621 -69.571  14.563  1.00119.06           N  
ANISOU 6017  NE2 GLN B 682    14397  15137  15701   1532    432   3627       N  
ATOM   6018  N   THR B 683     -48.362 -74.395  13.259  1.00105.03           N  
ANISOU 6018  N   THR B 683    12532  15643  11729   1651    312   2555       N  
ATOM   6019  CA  THR B 683     -48.900 -75.629  12.693  1.00103.46           C  
ANISOU 6019  CA  THR B 683    12304  15981  11022   1715    191   2275       C  
ATOM   6020  C   THR B 683     -49.017 -76.666  13.801  1.00 98.17           C  
ANISOU 6020  C   THR B 683    11456  15314  10527   1481     76   1759       C  
ATOM   6021  O   THR B 683     -49.893 -77.540  13.768  1.00 97.33           O  
ANISOU 6021  O   THR B 683    11247  15517  10214   1516   -136   1460       O  
ATOM   6022  CB  THR B 683     -48.022 -76.177  11.582  1.00105.47           C  
ANISOU 6022  CB  THR B 683    12657  16528  10889   1725    428   2438       C  
ATOM   6023  OG1 THR B 683     -46.675 -76.205  12.047  1.00104.60           O  
ANISOU 6023  OG1 THR B 683    12482  16124  11137   1443    716   2482       O  
ATOM   6024  CG2 THR B 683     -48.117 -75.300  10.316  1.00111.47           C  
ANISOU 6024  CG2 THR B 683    13621  17437  11295   2042    545   2999       C  
ATOM   6025  N   HIS B 684     -48.135 -76.552  14.788  1.00 94.85           N  
ANISOU 6025  N   HIS B 684    10989  14529  10520   1251    202   1675       N  
ATOM   6026  CA  HIS B 684     -48.214 -77.393  15.960  1.00 90.26           C  
ANISOU 6026  CA  HIS B 684    10279  13913  10101   1074    110   1262       C  
ATOM   6027  C   HIS B 684     -49.402 -76.981  16.786  1.00 89.23           C  
ANISOU 6027  C   HIS B 684    10066  13756  10082   1212    -79   1136       C  
ATOM   6028  O   HIS B 684     -50.120 -77.818  17.339  1.00 87.47           O  
ANISOU 6028  O   HIS B 684     9704  13731   9800   1168   -184    870       O  
ATOM   6029  CB  HIS B 684     -46.942 -77.313  16.821  1.00 89.08           C  
ANISOU 6029  CB  HIS B 684    10117  13393  10336    857    244   1187       C  
ATOM   6030  CG  HIS B 684     -47.079 -78.028  18.123  1.00 85.31           C  
ANISOU 6030  CG  HIS B 684     9555  12873   9983    749    136    818       C  
ATOM   6031  ND1 HIS B 684     -47.289 -79.389  18.198  1.00 82.69           N  
ANISOU 6031  ND1 HIS B 684     9158  12800   9458    639     90    582       N  
ATOM   6032  CD2 HIS B 684     -47.114 -77.567  19.394  1.00 85.09           C  
ANISOU 6032  CD2 HIS B 684     9514  12589  10224    779     53    660       C  
ATOM   6033  CE1 HIS B 684     -47.421 -79.739  19.464  1.00 82.48           C  
ANISOU 6033  CE1 HIS B 684     9082  12680   9575    584     30    368       C  
ATOM   6034  NE2 HIS B 684     -47.314 -78.654  20.212  1.00 83.71           N  
ANISOU 6034  NE2 HIS B 684     9279  12563   9964    692      8    392       N  
ATOM   6035  N   ALA B 685     -49.597 -75.677  16.885  1.00 90.70           N  
ANISOU 6035  N   ALA B 685    10317  13677  10465   1388   -108   1343       N  
ATOM   6036  CA  ALA B 685     -50.730 -75.163  17.612  1.00 90.59           C  
ANISOU 6036  CA  ALA B 685    10218  13657  10543   1596   -278   1216       C  
ATOM   6037  C   ALA B 685     -52.009 -75.688  16.953  1.00 91.47           C  
ANISOU 6037  C   ALA B 685    10205  14219  10330   1742   -429   1177       C  
ATOM   6038  O   ALA B 685     -52.849 -76.292  17.630  1.00 90.63           O  
ANISOU 6038  O   ALA B 685     9896  14315  10223   1735   -506    928       O  
ATOM   6039  CB  ALA B 685     -50.698 -73.671  17.628  1.00 93.47           C  
ANISOU 6039  CB  ALA B 685    10695  13631  11188   1798   -325   1445       C  
ATOM   6040  N   ASN B 686     -52.130 -75.490  15.636  1.00 93.41           N  
ANISOU 6040  N   ASN B 686    10553  14631  10305   1880   -471   1432       N  
ATOM   6041  CA  ASN B 686     -53.253 -76.000  14.864  1.00 94.56           C  
ANISOU 6041  CA  ASN B 686    10584  15207  10137   2044   -689   1356       C  
ATOM   6042  C   ASN B 686     -53.495 -77.488  15.123  1.00 92.09           C  
ANISOU 6042  C   ASN B 686    10066  15156   9765   1814   -750    997       C  
ATOM   6043  O   ASN B 686     -54.628 -77.909  15.352  1.00 92.46           O  
ANISOU 6043  O   ASN B 686     9858  15422   9850   1859   -932    805       O  
ATOM   6044  CB  ASN B 686     -53.036 -75.739  13.372  1.00 98.25           C  
ANISOU 6044  CB  ASN B 686    11259  15847  10221   2236   -706   1666       C  
ATOM   6045  CG  ASN B 686     -53.107 -74.247  13.003  1.00102.12           C  
ANISOU 6045  CG  ASN B 686    11931  16086  10783   2514   -696   2100       C  
ATOM   6046  OD1 ASN B 686     -53.708 -73.436  13.713  1.00102.71           O  
ANISOU 6046  OD1 ASN B 686    11937  15932  11156   2648   -799   2083       O  
ATOM   6047  ND2 ASN B 686     -52.499 -73.891  11.869  1.00105.14           N  
ANISOU 6047  ND2 ASN B 686    12550  16515  10883   2629   -565   2507       N  
ATOM   6048  N   ARG B 687     -52.422 -78.275  15.114  1.00 89.97           N  
ANISOU 6048  N   ARG B 687     9880  14834   9468   1564   -597    919       N  
ATOM   6049  CA  ARG B 687     -52.501 -79.702  15.411  1.00 87.94           C  
ANISOU 6049  CA  ARG B 687     9462  14722   9230   1327   -658    599       C  
ATOM   6050  C   ARG B 687     -53.151 -79.980  16.753  1.00 86.41           C  
ANISOU 6050  C   ARG B 687     9037  14462   9330   1212   -652    440       C  
ATOM   6051  O   ARG B 687     -53.995 -80.875  16.850  1.00 87.44           O  
ANISOU 6051  O   ARG B 687     8919  14784   9518   1123   -792    260       O  
ATOM   6052  CB  ARG B 687     -51.123 -80.312  15.416  1.00 85.85           C  
ANISOU 6052  CB  ARG B 687     9334  14322   8961   1112   -473    553       C  
ATOM   6053  CG  ARG B 687     -51.129 -81.822  15.405  1.00 85.59           C  
ANISOU 6053  CG  ARG B 687     9185  14417   8915    916   -583    239       C  
ATOM   6054  CD  ARG B 687     -50.560 -82.358  14.098  1.00 88.27           C  
ANISOU 6054  CD  ARG B 687     9661  14966   8910    998   -626    176       C  
ATOM   6055  NE  ARG B 687     -49.350 -81.640  13.721  1.00 88.03           N  
ANISOU 6055  NE  ARG B 687     9839  14834   8774   1052   -342    443       N  
ATOM   6056  CZ  ARG B 687     -48.920 -81.520  12.474  1.00 92.69           C  
ANISOU 6056  CZ  ARG B 687    10583  15659   8974   1252   -274    576       C  
ATOM   6057  NH1 ARG B 687     -49.600 -82.082  11.478  1.00 96.95           N1+
ANISOU 6057  NH1 ARG B 687    11134  16562   9138   1460   -534    396       N1+
ATOM   6058  NH2 ARG B 687     -47.813 -80.834  12.217  1.00 93.70           N  
ANISOU 6058  NH2 ARG B 687    10838  15672   9090   1264     48    891       N  
ATOM   6059  N   ILE B 688     -52.747 -79.234  17.788  1.00 84.95           N  
ANISOU 6059  N   ILE B 688     8923  14010   9343   1225   -494    505       N  
ATOM   6060  CA  ILE B 688     -53.385 -79.321  19.118  1.00 83.89           C  
ANISOU 6060  CA  ILE B 688     8604  13873   9394   1222   -446    388       C  
ATOM   6061  C   ILE B 688     -54.846 -78.924  19.005  1.00 86.52           C  
ANISOU 6061  C   ILE B 688     8693  14446   9731   1449   -580    400       C  
ATOM   6062  O   ILE B 688     -55.716 -79.637  19.492  1.00 87.57           O  
ANISOU 6062  O   ILE B 688     8531  14783   9957   1375   -586    299       O  
ATOM   6063  CB  ILE B 688     -52.726 -78.401  20.200  1.00 83.06           C  
ANISOU 6063  CB  ILE B 688     8654  13455   9447   1313   -322    396       C  
ATOM   6064  CG1 ILE B 688     -51.197 -78.548  20.263  1.00 81.45           C  
ANISOU 6064  CG1 ILE B 688     8662  12970   9312   1122   -225    390       C  
ATOM   6065  CG2 ILE B 688     -53.327 -78.647  21.550  1.00 81.64           C  
ANISOU 6065  CG2 ILE B 688     8316  13368   9333   1363   -245    263       C  
ATOM   6066  CD1 ILE B 688     -50.720 -79.707  21.056  1.00 78.90           C  
ANISOU 6066  CD1 ILE B 688     8309  12656   9012    903   -155    225       C  
ATOM   6067  N   TYR B 689     -55.118 -77.795  18.351  1.00 88.45           N  
ANISOU 6067  N   TYR B 689     9036  14657   9913   1726   -683    549       N  
ATOM   6068  CA  TYR B 689     -56.489 -77.300  18.235  1.00 91.42           C  
ANISOU 6068  CA  TYR B 689     9173  15249  10310   2003   -842    548       C  
ATOM   6069  C   TYR B 689     -57.424 -78.359  17.654  1.00 93.62           C  
ANISOU 6069  C   TYR B 689     9135  15880  10555   1906  -1026    419       C  
ATOM   6070  O   TYR B 689     -58.437 -78.666  18.271  1.00 94.66           O  
ANISOU 6070  O   TYR B 689     8902  16199  10863   1914  -1027    321       O  
ATOM   6071  CB  TYR B 689     -56.560 -75.975  17.455  1.00 93.76           C  
ANISOU 6071  CB  TYR B 689     9669  15419  10535   2332   -969    767       C  
ATOM   6072  CG  TYR B 689     -55.817 -74.822  18.111  1.00 91.86           C  
ANISOU 6072  CG  TYR B 689     9669  14752  10479   2440   -851    867       C  
ATOM   6073  CD1 TYR B 689     -55.784 -74.686  19.501  1.00 89.46           C  
ANISOU 6073  CD1 TYR B 689     9299  14326  10363   2455   -735    674       C  
ATOM   6074  CD2 TYR B 689     -55.170 -73.856  17.344  1.00 91.97           C  
ANISOU 6074  CD2 TYR B 689     9968  14477  10497   2551   -872   1157       C  
ATOM   6075  CE1 TYR B 689     -55.107 -73.654  20.111  1.00 88.80           C  
ANISOU 6075  CE1 TYR B 689     9426  13826  10488   2577   -713    676       C  
ATOM   6076  CE2 TYR B 689     -54.494 -72.804  17.953  1.00 92.50           C  
ANISOU 6076  CE2 TYR B 689    10211  14072  10859   2618   -816   1224       C  
ATOM   6077  CZ  TYR B 689     -54.469 -72.719  19.339  1.00 90.83           C  
ANISOU 6077  CZ  TYR B 689     9926  13730  10855   2634   -772    936       C  
ATOM   6078  OH  TYR B 689     -53.814 -71.692  19.964  1.00 92.99           O  
ANISOU 6078  OH  TYR B 689    10363  13514  11452   2729   -799    911       O  
ATOM   6079  N   ARG B 690     -57.064 -78.938  16.501  1.00 95.03           N  
ANISOU 6079  N   ARG B 690     9428  16147  10528   1822  -1178    402       N  
ATOM   6080  CA  ARG B 690     -57.832 -80.040  15.894  1.00 97.92           C  
ANISOU 6080  CA  ARG B 690     9508  16790  10908   1718  -1437    193       C  
ATOM   6081  C   ARG B 690     -58.115 -81.145  16.900  1.00 97.65           C  
ANISOU 6081  C   ARG B 690     9157  16749  11196   1389  -1324     46       C  
ATOM   6082  O   ARG B 690     -59.241 -81.637  16.986  1.00100.21           O  
ANISOU 6082  O   ARG B 690     9057  17260  11755   1346  -1471    -60       O  
ATOM   6083  CB  ARG B 690     -57.097 -80.651  14.700  1.00 98.01           C  
ANISOU 6083  CB  ARG B 690     9758  16860  10618   1673  -1579    122       C  
ATOM   6084  CG  ARG B 690     -57.091 -79.807  13.450  1.00101.49           C  
ANISOU 6084  CG  ARG B 690    10450  17439  10671   2037  -1742    289       C  
ATOM   6085  CD  ARG B 690     -56.715 -80.621  12.202  1.00103.39           C  
ANISOU 6085  CD  ARG B 690    10837  17897  10549   2076  -1951    127       C  
ATOM   6086  NE  ARG B 690     -55.279 -80.895  12.072  1.00101.62           N  
ANISOU 6086  NE  ARG B 690    10920  17533  10157   1929  -1672    200       N  
ATOM   6087  CZ  ARG B 690     -54.357 -79.997  11.719  1.00101.66           C  
ANISOU 6087  CZ  ARG B 690    11251  17435   9939   2060  -1411    549       C  
ATOM   6088  NH1 ARG B 690     -54.701 -78.735  11.475  1.00103.69           N1+
ANISOU 6088  NH1 ARG B 690    11618  17660  10117   2340  -1404    880       N1+
ATOM   6089  NH2 ARG B 690     -53.080 -80.359  11.619  1.00 99.70           N  
ANISOU 6089  NH2 ARG B 690    11190  17089   9599   1907  -1154    583       N  
ATOM   6090  N   MET B 691     -57.086 -81.525  17.660  1.00 95.50           N  
ANISOU 6090  N   MET B 691     9073  16250  10961   1162  -1064     71       N  
ATOM   6091  CA  MET B 691     -57.202 -82.591  18.640  1.00 96.10           C  
ANISOU 6091  CA  MET B 691     8923  16284  11304    862   -924     12       C  
ATOM   6092  C   MET B 691     -58.188 -82.240  19.746  1.00 97.17           C  
ANISOU 6092  C   MET B 691     8740  16545  11635    954   -746    104       C  
ATOM   6093  O   MET B 691     -59.073 -83.033  20.065  1.00 99.62           O  
ANISOU 6093  O   MET B 691     8637  16990  12221    789   -746     91       O  
ATOM   6094  CB  MET B 691     -55.835 -82.963  19.213  1.00 93.54           C  
ANISOU 6094  CB  MET B 691     8911  15698  10932    676   -713     28       C  
ATOM   6095  CG  MET B 691     -55.882 -84.019  20.348  1.00 98.00           C  
ANISOU 6095  CG  MET B 691     9305  16194  11736    407   -542     40       C  
ATOM   6096  SD  MET B 691     -54.386 -84.101  21.411  1.00104.90           S  
ANISOU 6096  SD  MET B 691    10544  16782  12528    326   -288     82       S  
ATOM   6097  CE  MET B 691     -54.305 -82.432  22.091  1.00102.00           C  
ANISOU 6097  CE  MET B 691    10344  16394  12018    685   -150    159       C  
ATOM   6098  N   ILE B 692     -58.073 -81.047  20.311  1.00 96.32           N  
ANISOU 6098  N   ILE B 692     8791  16391  11413   1233   -597    193       N  
ATOM   6099  CA  ILE B 692     -59.004 -80.678  21.372  1.00 98.05           C  
ANISOU 6099  CA  ILE B 692     8716  16785  11752   1405   -409    244       C  
ATOM   6100  C   ILE B 692     -60.421 -80.437  20.840  1.00101.85           C  
ANISOU 6100  C   ILE B 692     8766  17554  12376   1580   -595    219       C  
ATOM   6101  O   ILE B 692     -61.385 -80.569  21.575  1.00104.59           O  
ANISOU 6101  O   ILE B 692     8700  18129  12911   1628   -435    258       O  
ATOM   6102  CB  ILE B 692     -58.460 -79.540  22.307  1.00 96.95           C  
ANISOU 6102  CB  ILE B 692     8868  16497  11471   1695   -227    260       C  
ATOM   6103  CG1 ILE B 692     -59.198 -78.226  22.131  1.00 99.97           C  
ANISOU 6103  CG1 ILE B 692     9193  16949  11839   2119   -334    249       C  
ATOM   6104  CG2 ILE B 692     -56.946 -79.358  22.161  1.00 92.93           C  
ANISOU 6104  CG2 ILE B 692     8829  15636  10842   1593   -235    247       C  
ATOM   6105  CD1 ILE B 692     -58.505 -77.093  22.863  1.00101.52           C  
ANISOU 6105  CD1 ILE B 692     9728  16885  11957   2395   -261    201       C  
ATOM   6106  N   LYS B 693     -60.539 -80.132  19.550  1.00103.09           N  
ANISOU 6106  N   LYS B 693     9001  17731  12438   1690   -929    163       N  
ATOM   6107  CA  LYS B 693     -61.849 -79.943  18.899  1.00107.47           C  
ANISOU 6107  CA  LYS B 693     9151  18559  13123   1883  -1204     99       C  
ATOM   6108  C   LYS B 693     -62.579 -81.279  18.854  1.00109.63           C  
ANISOU 6108  C   LYS B 693     8925  18984  13744   1547  -1297     -1       C  
ATOM   6109  O   LYS B 693     -63.783 -81.355  19.058  1.00113.27           O  
ANISOU 6109  O   LYS B 693     8849  19682  14504   1601  -1333    -20       O  
ATOM   6110  CB  LYS B 693     -61.686 -79.370  17.480  1.00108.46           C  
ANISOU 6110  CB  LYS B 693     9550  18676  12981   2113  -1567     80       C  
ATOM   6111  CG  LYS B 693     -62.654 -78.226  17.149  1.00112.26           C  
ANISOU 6111  CG  LYS B 693     9893  19311  13448   2570  -1763    115       C  
ATOM   6112  CD  LYS B 693     -62.674 -77.845  15.660  1.00115.28           C  
ANISOU 6112  CD  LYS B 693    10500  19758  13541   2819  -2165    130       C  
ATOM   6113  CE  LYS B 693     -61.347 -77.253  15.172  1.00114.02           C  
ANISOU 6113  CE  LYS B 693    10963  19324  13032   2869  -2061    341       C  
ATOM   6114  NZ  LYS B 693     -61.428 -76.753  13.762  1.00117.64           N1+
ANISOU 6114  NZ  LYS B 693    11661  19894  13140   3195  -2390    452       N1+
ATOM   6115  N   LEU B 694     -61.809 -82.323  18.574  1.00107.77           N  
ANISOU 6115  N   LEU B 694     8854  18579  13516   1203  -1344    -69       N  
ATOM   6116  CA  LEU B 694     -62.204 -83.703  18.765  1.00109.61           C  
ANISOU 6116  CA  LEU B 694     8691  18798  14154    806  -1378   -134       C  
ATOM   6117  C   LEU B 694     -62.576 -83.939  20.236  1.00110.06           C  
ANISOU 6117  C   LEU B 694     8452  18900  14463    674   -921     91       C  
ATOM   6118  O   LEU B 694     -63.722 -84.263  20.547  1.00114.08           O  
ANISOU 6118  O   LEU B 694     8374  19601  15368    601   -880    146       O  
ATOM   6119  CB  LEU B 694     -61.019 -84.579  18.385  1.00106.87           C  
ANISOU 6119  CB  LEU B 694     8720  18190  13695    539  -1447   -233       C  
ATOM   6120  CG  LEU B 694     -61.166 -85.891  17.628  1.00110.18           C  
ANISOU 6120  CG  LEU B 694     8940  18525  14397    250  -1811   -482       C  
ATOM   6121  CD1 LEU B 694     -61.696 -85.658  16.196  1.00113.57           C  
ANISOU 6121  CD1 LEU B 694     9319  19148  14683    501  -2338   -756       C  
ATOM   6122  CD2 LEU B 694     -59.788 -86.599  17.639  1.00106.35           C  
ANISOU 6122  CD2 LEU B 694     8894  17756  13756     46  -1729   -530       C  
ATOM   6123  N   GLY B 695     -61.606 -83.755  21.135  1.00106.37           N  
ANISOU 6123  N   GLY B 695     8376  18281  13757    674   -577    228       N  
ATOM   6124  CA  GLY B 695     -61.836 -83.865  22.581  1.00107.15           C  
ANISOU 6124  CA  GLY B 695     8305  18473  13932    659   -119    457       C  
ATOM   6125  C   GLY B 695     -63.206 -83.366  23.009  1.00111.69           C  
ANISOU 6125  C   GLY B 695     8342  19402  14692    886     23    542       C  
ATOM   6126  O   GLY B 695     -63.947 -84.073  23.669  1.00115.34           O  
ANISOU 6126  O   GLY B 695     8321  20014  15486    699    274    731       O  
ATOM   6127  N   LEU B 696     -63.561 -82.153  22.605  1.00112.17           N  
ANISOU 6127  N   LEU B 696     8455  19590  14573   1297   -128    426       N  
ATOM   6128  CA  LEU B 696     -64.836 -81.575  22.985  1.00116.65           C  
ANISOU 6128  CA  LEU B 696     8513  20508  15299   1591    -11    464       C  
ATOM   6129  C   LEU B 696     -66.004 -82.148  22.188  1.00121.57           C  
ANISOU 6129  C   LEU B 696     8499  21302  16391   1430   -305    393       C  
ATOM   6130  O   LEU B 696     -67.161 -81.781  22.414  1.00126.10           O  
ANISOU 6130  O   LEU B 696     8530  22189  17191   1643   -236    414       O  
ATOM   6131  CB  LEU B 696     -64.778 -80.059  22.851  1.00115.94           C  
ANISOU 6131  CB  LEU B 696     8723  20432  14893   2119   -114    350       C  
ATOM   6132  CG  LEU B 696     -64.031 -79.358  23.982  1.00113.46           C  
ANISOU 6132  CG  LEU B 696     8826  20032  14248   2375    210    382       C  
ATOM   6133  CD1 LEU B 696     -63.421 -78.069  23.500  1.00110.99           C  
ANISOU 6133  CD1 LEU B 696     9009  19468  13691   2720    -35    251       C  
ATOM   6134  CD2 LEU B 696     -64.965 -79.103  25.154  1.00118.07           C  
ANISOU 6134  CD2 LEU B 696     8997  20999  14864   2669    601    457       C  
ATOM   6135  N   GLY B 697     -65.698 -83.052  21.261  1.00121.27           N  
ANISOU 6135  N   GLY B 697     8501  21058  16516   1080   -660    268       N  
ATOM   6136  CA  GLY B 697     -66.720 -83.695  20.439  1.00126.59           C  
ANISOU 6136  CA  GLY B 697     8584  21835  17679    908  -1051    117       C  
ATOM   6137  C   GLY B 697     -67.249 -82.793  19.347  1.00128.82           C  
ANISOU 6137  C   GLY B 697     8855  22273  17815   1310  -1525   -113       C  
ATOM   6138  O   GLY B 697     -68.447 -82.545  19.260  1.00133.70           O  
ANISOU 6138  O   GLY B 697     8886  23161  18754   1473  -1646   -164       O  
ATOM   6139  N   ILE B 698     -66.337 -82.283  18.529  1.00125.93           N  
ANISOU 6139  N   ILE B 698     9135  21747  16963   1492  -1772   -220       N  
ATOM   6140  CA  ILE B 698     -66.686 -81.548  17.316  1.00128.66           C  
ANISOU 6140  CA  ILE B 698     9579  22209  17094   1870  -2267   -396       C  
ATOM   6141  C   ILE B 698     -65.859 -82.136  16.176  1.00127.75           C  
ANISOU 6141  C   ILE B 698     9885  21932  16720   1741  -2637   -575       C  
ATOM   6142  O   ILE B 698     -64.679 -82.452  16.359  1.00123.78           O  
ANISOU 6142  O   ILE B 698     9851  21192  15986   1542  -2422   -504       O  
ATOM   6143  CB  ILE B 698     -66.410 -80.022  17.426  1.00126.84           C  
ANISOU 6143  CB  ILE B 698     9773  21976  16441   2365  -2150   -264       C  
ATOM   6144  CG1 ILE B 698     -66.783 -79.479  18.810  1.00126.21           C  
ANISOU 6144  CG1 ILE B 698     9475  21993  16487   2501  -1667   -109       C  
ATOM   6145  CG2 ILE B 698     -67.167 -79.265  16.327  1.00131.35           C  
ANISOU 6145  CG2 ILE B 698    10266  22730  16910   2803  -2648   -381       C  
ATOM   6146  CD1 ILE B 698     -66.069 -78.193  19.178  1.00121.87           C  
ANISOU 6146  CD1 ILE B 698     9480  21267  15555   2866  -1492     -8       C  
ATOM   6147  N   ASP B 699     -66.487 -82.278  15.010  1.00132.57           N  
ANISOU 6147  N   ASP B 699    10315  22700  17354   1898  -3203   -831       N  
ATOM   6148  CA  ASP B 699     -65.914 -82.953  13.842  1.00133.60           C  
ANISOU 6148  CA  ASP B 699    10753  22768  17237   1845  -3628  -1086       C  
ATOM   6149  C   ASP B 699     -66.708 -84.232  13.548  1.00138.47           C  
ANISOU 6149  C   ASP B 699    10769  23398  18444   1531  -4038  -1422       C  
ATOM   6150  O   ASP B 699     -67.428 -84.330  12.544  1.00143.55           O  
ANISOU 6150  O   ASP B 699    11184  24226  19133   1744  -4640  -1738       O  
ATOM   6151  CB  ASP B 699     -64.425 -83.276  14.038  1.00128.24           C  
ANISOU 6151  CB  ASP B 699    10672  21819  16233   1628  -3304   -976       C  
ATOM   6152  CG  ASP B 699     -63.846 -84.083  12.893  1.00130.50           C  
ANISOU 6152  CG  ASP B 699    11229  22077  16275   1593  -3705  -1276       C  
ATOM   6153  OD1 ASP B 699     -64.139 -83.761  11.714  1.00135.20           O  
ANISOU 6153  OD1 ASP B 699    11940  22897  16532   1965  -4164  -1454       O  
ATOM   6154  OD2 ASP B 699     -63.096 -85.043  13.176  1.00129.90           O1-
ANISOU 6154  OD2 ASP B 699    11265  21770  16318   1237  -3570  -1345       O1-
TER   
HETATM 6155  S   SO4 A   1     -65.346 -60.298  10.247  1.00128.96           S  
HETATM 6156  O1  SO4 A   1     -65.423 -59.949   8.825  1.00127.93           O  
HETATM 6157  O2  SO4 A   1     -66.683 -60.619  10.740  1.00129.33           O  
HETATM 6158  O3  SO4 A   1     -64.457 -61.454  10.432  1.00128.23           O1-
HETATM 6159  O4  SO4 A   1     -64.868 -59.162  11.031  1.00128.05           O  
HETATM 6160  S   SO4 B   2     -37.816-102.546  33.019  1.00122.03           S  
HETATM 6161  O1  SO4 B   2     -36.790-103.282  32.276  1.00120.96           O  
HETATM 6162  O2  SO4 B   2     -39.114-103.018  32.568  1.00123.80           O  
HETATM 6163  O3  SO4 B   2     -37.684-102.819  34.450  1.00121.49           O1-
HETATM 6164  O4  SO4 B   2     -37.797-101.105  32.752  1.00121.50           O  
HETATM 6165  O   HOH A  18     -24.812 -27.932  -5.405  1.00 99.80           O  
HETATM 6166  O   HOH A  19     -18.520 -40.797 -16.659  1.00 93.58           O  
ANISOU 6166  O   HOH A  19    10817  17432   7304    665   -386    -62       O  
HETATM 6167  O   HOH A  20     -22.597 -50.535 -11.463  1.00103.03           O  
ANISOU 6167  O   HOH A  20    10020  15942  13182  -1077   -500  -4657       O  
HETATM 6168  O   HOH A  21     -21.833 -40.048  16.697  1.00 90.72           O  
ANISOU 6168  O   HOH A  21    10556  14369   9544  -4600   3006  -1622       O  
HETATM 6169  O   HOH A  23     -18.633 -52.933 -10.539  1.00 90.39           O  
ANISOU 6169  O   HOH A  23     8940  12715  12687   -848   1024  -4868       O  
HETATM 6170  O   HOH A  24     -35.560 -38.231  20.361  1.00100.11           O  
ANISOU 6170  O   HOH A  24    12425  11941  13669  -3956   2903  -4287       O  
HETATM 6171  O   HOH A  25     -29.644 -56.789  18.137  1.00 77.36           O  
HETATM 6172  O   HOH A  26     -19.274 -52.718  12.787  1.00 82.92           O  
ANISOU 6172  O   HOH A  26    11769   9427  10308   -600   2140   3448       O  
HETATM 6173  O   HOH A  33     -76.924 -70.519  26.072  1.00 94.53           O  
ANISOU 6173  O   HOH A  33     7087  13751  15075   -320    590    435       O  
HETATM 6174  O   HOH A  34     -54.838 -56.728   0.561  1.00 77.61           O  
HETATM 6175  O   HOH A  37     -66.056 -81.118  29.598  1.00 93.49           O  
ANISOU 6175  O   HOH A  37    11519  11150  12851  -1505    919    559       O  
HETATM 6176  O   HOH A  38     -45.260 -64.233  15.628  1.00 63.60           O  
ANISOU 6176  O   HOH A  38     5745   8900   9518   -664    141  -1269       O  
HETATM 6177  O   HOH A  39     -47.145 -65.269   0.485  1.00 84.44           O  
ANISOU 6177  O   HOH A  39     8887  12507  10687  -2477   1108  -2726       O  
HETATM 6178  O   HOH A  40     -48.457 -65.608   2.704  1.00 78.74           O  
ANISOU 6178  O   HOH A  40     7984  11586  10345  -2027    830  -2405       O  
HETATM 6179  O   HOH A  41     -51.283 -42.297  21.009  1.00111.96           O  
HETATM 6180  O   HOH A  42     -41.258 -39.841  -2.832  1.00102.43           O  
ANISOU 6180  O   HOH A  42     8789  14476  15652  -1019   1475   1671       O  
HETATM 6181  O   HOH A  44     -34.463 -64.036  34.482  1.00 98.57           O  
HETATM 6182  O   HOH A  49     -62.322 -60.145  33.228  1.00 85.78           O  
HETATM 6183  O   HOH A  50     -68.031 -66.536  37.471  1.00 94.37           O  
ANISOU 6183  O   HOH A  50    12420  11762  11672  -2126   5421   -541       O  
HETATM 6184  O   HOH A  68     -78.409 -51.010  21.939  1.00127.00           O  
ANISOU 6184  O   HOH A  68     9775   9892  28587   1457   8900   4403       O  
HETATM 6185  O   HOH A  74     -55.918 -89.712  18.164  1.00104.25           O  
ANISOU 6185  O   HOH A  74    14304  11567  13738   -538   -497  -1724       O  
HETATM 6186  O   HOH A  80      -0.880 -32.520 -17.380  1.00 97.98           O  
HETATM 6187  O   HOH A  81     -41.683 -44.120  -2.501  1.00101.70           O  
ANISOU 6187  O   HOH A  81     9393  14876  14372  -1294   1081    783       O  
HETATM 6188  O   HOH A  82     -38.720 -42.524  -4.426  1.00 82.62           O  
ANISOU 6188  O   HOH A  82     6904  12578  11908  -1405   1300    818       O  
HETATM 6189  O   HOH A  83     -23.203 -34.677  -6.619  1.00103.20           O  
ANISOU 6189  O   HOH A  83    10386  14499  14325   1557   -268   1349       O  
HETATM 6190  O   HOH A  89     -52.560 -74.614  40.167  1.00 93.06           O  
HETATM 6191  O   HOH A  94     -30.843 -54.775  18.848  1.00 83.43           O  
HETATM 6192  O   HOH A  95     -44.594 -42.062  23.433  1.00108.64           O  
ANISOU 6192  O   HOH A  95    14136  12594  14546  -3373   4430  -4322       O  
HETATM 6193  O   HOH A  98     -42.940 -65.103  -0.803  1.00105.47           O  
ANISOU 6193  O   HOH A  98    11629  14743  13699  -2475   1935  -3338       O  
HETATM 6194  O   HOH A  99     -34.203 -61.999  -2.810  1.00 87.21           O  
HETATM 6195  O   HOH A 100     -31.169 -58.624  -7.566  1.00105.58           O  
ANISOU 6195  O   HOH A 100    11618  14373  14122  -2761   4210  -3792       O  
HETATM 6196  O   HOH A 107     -40.589 -45.190 -13.372  1.00103.61           O  
ANISOU 6196  O   HOH A 107     9971  18292  11104  -4211    613   2007       O  
HETATM 6197  O   HOH A 108     -14.374 -45.151  14.954  1.00107.82           O  
ANISOU 6197  O   HOH A 108    12126  16280  12560  -1824    809   5895       O  
HETATM 6198  O   HOH A 112     -57.008 -95.620  29.363  1.00108.39           O  
ANISOU 6198  O   HOH A 112    17427   8452  15301    612   2362   1782       O  
HETATM 6199  O   HOH A 113     -28.637 -62.330  28.339  1.00133.24           O  
ANISOU 6199  O   HOH A 113    12522  20222  17878  -4832  -4337   3564       O  
HETATM 6200  O   HOH A 115     -27.988 -60.980  22.982  1.00103.77           O  
ANISOU 6200  O   HOH A 115     8693  15076  15656  -3171  -2918   2165       O  
HETATM 6201  O   HOH A 116      -3.817 -25.751  14.403  1.00100.90           O  
HETATM 6202  O   HOH A 120     -39.510 -66.916   5.543  1.00 89.19           O  
ANISOU 6202  O   HOH A 120     8610  11362  13916  -1053   1798  -2663       O  
HETATM 6203  O   HOH A 121     -31.922 -27.231   2.996  1.00108.76           O  
ANISOU 6203  O   HOH A 121     9208  11445  20671   -695   4213   -204       O  
HETATM 6204  O   HOH A 124     -19.161 -39.279  15.650  1.00101.68           O  
ANISOU 6204  O   HOH A 124    11848  15890  10895  -4028   1862   -942       O  
HETATM 6205  O   HOH A 125     -39.045 -31.472   8.294  1.00117.63           O  
ANISOU 6205  O   HOH A 125    11402  12392  20897   -845   4611  -1125       O  
HETATM 6206  O   HOH A 127     -51.107 -42.309  33.288  1.00106.65           O  
HETATM 6207  O   HOH A 739     -35.974 -55.188  -7.936  1.00 76.18           O  
HETATM 6208  O   HOH A 740     -35.672 -52.754  -1.969  1.00 69.36           O  
HETATM 6209  O   HOH B   3     -32.064-101.395  33.454  1.00 83.28           O  
ANISOU 6209  O   HOH B   3     8729   9096  13815  -1210  -1567     75       O  
HETATM 6210  O   HOH B   4       3.206 -75.450  50.526  1.00 90.03           O  
ANISOU 6210  O   HOH B   4    11928  10295  11983    207    790   1661       O  
HETATM 6211  O   HOH B   5      -3.051 -72.110  51.765  1.00 68.31           O  
ANISOU 6211  O   HOH B   5     8476   8378   9098   -804   1205    924       O  
HETATM 6212  O   HOH B   6     -22.083 -68.372  30.196  1.00 92.52           O  
HETATM 6213  O   HOH B   7     -33.723 -82.065  29.014  1.00 72.38           O  
ANISOU 6213  O   HOH B   7     7262   9650  10587     58    407   -626       O  
HETATM 6214  O   HOH B   8     -18.609 -78.425  45.661  1.00 72.62           O  
ANISOU 6214  O   HOH B   8     7534  10362   9694   -360   1170  -1048       O  
HETATM 6215  O   HOH B   9     -24.297 -88.567  48.343  1.00 60.47           O  
HETATM 6216  O   HOH B  10      -1.918 -76.465  27.762  1.00 84.88           O  
ANISOU 6216  O   HOH B  10     7067  15760   9420  -2845   1866   -750       O  
HETATM 6217  O   HOH B  11      -0.063 -69.086  60.587  1.00 68.95           O  
ANISOU 6217  O   HOH B  11     9359  10520   6319    233    736    656       O  
HETATM 6218  O   HOH B  12       6.010 -56.059  45.549  1.00 79.14           O  
HETATM 6219  O   HOH B  27      -6.048 -84.199  23.325  1.00102.75           O  
ANISOU 6219  O   HOH B  27     8513  18959  11568  -1616   2288  -3324       O  
HETATM 6220  O   HOH B  28      15.383 -58.983  58.310  1.00 99.91           O  
HETATM 6221  O   HOH B  29      -8.289 -51.528  47.640  1.00 81.02           O  
ANISOU 6221  O   HOH B  29     8527   6148  16106   2743  -1901   -462       O  
HETATM 6222  O   HOH B  31       1.336 -49.276  43.465  1.00 88.85           O  
HETATM 6223  O   HOH B  32     -50.981-108.928  17.605  1.00118.45           O  
ANISOU 6223  O   HOH B  32    11485  10493  23025  -3170  -6258  -3959       O  
HETATM 6224  O   HOH B  35     -60.488 -77.288  10.021  1.00103.97           O  
HETATM 6225  O   HOH B  36     -58.423 -75.176  14.609  1.00 75.74           O  
ANISOU 6225  O   HOH B  36     7340  13674   7761   3017  -1633   1031       O  
HETATM 6226  O   HOH B  43     -27.981 -74.500  10.195  1.00 91.54           O  
HETATM 6227  O   HOH B  51     -48.767 -96.187  30.007  1.00 76.87           O  
ANISOU 6227  O   HOH B  51     8157  10739  10310  -1152    239   1696       O  
HETATM 6228  O   HOH B  52     -30.796 -95.387  19.353  1.00 82.06           O  
ANISOU 6228  O   HOH B  52     7921  11996  11261    -49    163  -2905       O  
HETATM 6229  O   HOH B  53     -16.430 -99.012  25.907  1.00 94.37           O  
ANISOU 6229  O   HOH B  53     8157  12243  15456   1362   -613  -5127       O  
HETATM 6230  O   HOH B  55     -28.833 -64.360  16.913  1.00128.79           O  
ANISOU 6230  O   HOH B  55    15732  14524  18676  -4172  -6281   5757       O  
HETATM 6231  O   HOH B  62      20.596 -62.515  25.799  1.00101.42           O  
HETATM 6232  O   HOH B  63     -26.581 -63.010  16.993  1.00138.35           O  
ANISOU 6232  O   HOH B  63    17063  15797  19703  -4879  -6542   6429       O  
HETATM 6233  O   HOH B  64     -19.605 -84.876  23.325  1.00108.42           O  
ANISOU 6233  O   HOH B  64    11486  16566  13142   -904   1264  -1285       O  
HETATM 6234  O   HOH B  65     -31.158 -84.150   2.879  1.00111.66           O  
ANISOU 6234  O   HOH B  65    11545  23094   7784  -5463   -936    398       O  
HETATM 6235  O   HOH B  66     -28.265 -73.665   7.388  1.00 89.06           O  
HETATM 6236  O   HOH B  67     -34.144-121.029  30.992  1.00 90.49           O  
HETATM 6237  O   HOH B  69     -20.054 -72.639  39.981  1.00 91.79           O  
ANISOU 6237  O   HOH B  69     9981  11471  13423     92    410  -1077       O  
HETATM 6238  O   HOH B  70     -17.474 -85.993  46.769  1.00 72.72           O  
ANISOU 6238  O   HOH B  70     7822  10226   9583  -1052    545    206       O  
HETATM 6239  O   HOH B  71       3.004 -77.376  30.857  1.00 95.20           O  
ANISOU 6239  O   HOH B  71     7584  17091  11493  -2309   1978  -1763       O  
HETATM 6240  O   HOH B  72      15.957 -71.388  44.250  1.00 73.46           O  
ANISOU 6240  O   HOH B  72     5939  10723  11250   1092    940   1161       O  
HETATM 6241  O   HOH B  73     -54.574 -84.937  15.792  1.00 80.54           O  
HETATM 6242  O   HOH B  75     -41.674-110.706   1.772  1.00 89.95           O  
HETATM 6243  O   HOH B  76     -40.281-112.957   7.402  1.00108.70           O  
HETATM 6244  O   HOH B  84      -9.102 -96.889  47.757  1.00114.57           O  
ANISOU 6244  O   HOH B  84    12901  12079  18549   -841  -3565   1194       O  
HETATM 6245  O   HOH B  85     -13.304 -88.099  46.361  1.00 85.37           O  
ANISOU 6245  O   HOH B  85     9448  11010  11978   -805   -166    366       O  
HETATM 6246  O   HOH B  86      -4.986 -87.127  45.334  1.00106.11           O  
ANISOU 6246  O   HOH B  86    11445  13221  15649    -46   -529   -532       O  
HETATM 6247  O   HOH B  87     -58.333 -91.989   6.207  1.00 96.41           O  
ANISOU 6247  O   HOH B  87     8910  17474  10244   1937  -6285  -4767       O  
HETATM 6248  O   HOH B  88     -11.362 -95.016  45.757  1.00113.67           O  
ANISOU 6248  O   HOH B  88    12824  12773  17592   -671  -2264    706       O  
HETATM 6249  O   HOH B  96     -59.893 -81.689  25.209  1.00 82.50           O  
ANISOU 6249  O   HOH B  96    10543  10163  10637   -834   -514     53       O  
HETATM 6250  O   HOH B  97     -21.643 -90.614  24.223  1.00 84.83           O  
ANISOU 6250  O   HOH B  97     8298  12657  11273    -38    966  -2384       O  
HETATM 6251  O   HOH B 101     -30.314 -75.778  38.589  1.00 90.93           O  
ANISOU 6251  O   HOH B 101     9034  12031  13484    523    653  -1986       O  
HETATM 6252  O   HOH B 106     -30.571-103.201  33.647  1.00 93.31           O  
ANISOU 6252  O   HOH B 106     9995   9629  15826  -1139  -2293     20       O  
HETATM 6253  O   HOH B 109       9.179 -79.578  24.939  1.00121.27           O  
ANISOU 6253  O   HOH B 109     7446  25620  13010  -3601   3308  -4741       O  
HETATM 6254  O   HOH B 111      20.035 -71.416  37.478  1.00109.82           O  
ANISOU 6254  O   HOH B 111     8751  17480  15492    954   3690    816       O  
HETATM 6255  O   HOH B 117     -44.729 -83.324   3.727  1.00120.87           O  
ANISOU 6255  O   HOH B 117    13581  19279  13062  -3556  -3887   1923       O  
HETATM 6256  O   HOH B 118      18.904 -61.333  27.802  1.00120.26           O  
ANISOU 6256  O   HOH B 118    12698  20808  12186  -7371   5255   -983       O  
HETATM 6257  O   HOH B 123     -57.111-101.076  18.569  1.00129.63           O  
ANISOU 6257  O   HOH B 123    11082  16001  22168  -3363  -3800  -1688       O  
HETATM 6258  O   HOH B 126      -7.313 -49.857  45.641  1.00103.15           O  
ANISOU 6258  O   HOH B 126    11893   7774  19522   2742  -2412    735       O  
HETATM 6259  O   HOH B 129     -20.298 -84.393  50.378  1.00 78.40           O  
HETATM 6260  O   HOH B 130      17.147 -63.896  21.793  1.00106.31           O  
HETATM 6261  O   HOH B 133     -46.274 -81.742  -1.375  1.00 99.88           O  
CONECT 6155 6156 6157 6158 6159
CONECT 6156 6155
CONECT 6157 6155
CONECT 6158 6155
CONECT 6159 6155
CONECT 6160 6161 6162 6163 6164
CONECT 6161 6160
CONECT 6162 6160
CONECT 6163 6160
CONECT 6164 6160
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.