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***  soumi_FcFragOnly_DestabilizedByBoundB_Rev00  ***

elNémo ID: 20102822420918941

Job options:

ID        	=	 20102822420918941
JOBID     	=	 soumi_FcFragOnly_DestabilizedByBoundB_Rev00
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -300
DQMAX     	=	 300
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER soumi_FcFragOnly_DestabilizedByBoundB_Rev00

ATOM      1  N   GLY A 237      25.242  23.386  35.215  1.00 94.47           N  
ANISOU    1  N   GLY A 237     9071   9470  17353   1290  -2227  -2220       N  
ATOM      2  CA  GLY A 237      25.136  23.158  33.784  1.00100.31           C  
ANISOU    2  CA  GLY A 237     9702  10256  18155   1212  -1945  -2352       C  
ATOM      3  C   GLY A 237      24.187  24.122  33.097  1.00105.68           C  
ANISOU    3  C   GLY A 237    10439  11087  18627   1128  -1719  -2335       C  
ATOM      4  O   GLY A 237      24.296  25.338  33.256  1.00105.72           O  
ANISOU    4  O   GLY A 237    10437  11181  18549   1090  -1696  -2337       O  
ATOM      5  N   PRO A 238      23.246  23.573  32.321  1.00111.54           N  
ANISOU    5  N   PRO A 238    11242  11854  19283   1096  -1555  -2320       N  
ATOM      6  CA  PRO A 238      22.294  24.346  31.520  1.00111.89           C  
ANISOU    6  CA  PRO A 238    11343  12032  19137   1011  -1324  -2317       C  
ATOM      7  C   PRO A 238      21.126  24.883  32.333  1.00108.32           C  
ANISOU    7  C   PRO A 238    11077  11632  18446   1041  -1414  -2135       C  
ATOM      8  O   PRO A 238      20.820  24.372  33.415  1.00108.98           O  
ANISOU    8  O   PRO A 238    11283  11635  18489   1125  -1632  -1993       O  
ATOM      9  CB  PRO A 238      21.797  23.328  30.481  1.00116.00           C  
ANISOU    9  CB  PRO A 238    11867  12528  19681    978  -1152  -2371       C  
ATOM     10  CG  PRO A 238      22.668  22.100  30.653  1.00118.04           C  
ANISOU   10  CG  PRO A 238    12035  12645  20170   1040  -1275  -2425       C  
ATOM     11  CD  PRO A 238      23.118  22.131  32.070  1.00116.12           C  
ANISOU   11  CD  PRO A 238    11829  12328  19962   1135  -1569  -2323       C  
ATOM     12  N   SER A 239      20.477  25.912  31.800  1.00100.22           N  
ANISOU   12  N   SER A 239    10083  10738  17259    967  -1240  -2140       N  
ATOM     13  CA  SER A 239      19.300  26.497  32.426  1.00 96.60           C  
ANISOU   13  CA  SER A 239     9792  10338  16574    984  -1291  -1982       C  
ATOM     14  C   SER A 239      18.107  26.479  31.473  1.00 91.98           C  
ANISOU   14  C   SER A 239     9298   9826  15825    907  -1065  -1976       C  
ATOM     15  O   SER A 239      18.270  26.387  30.255  1.00 91.25           O  
ANISOU   15  O   SER A 239     9110   9764  15796    841   -850  -2121       O  
ATOM     16  CB  SER A 239      19.598  27.929  32.868  1.00 92.85           C  
ANISOU   16  CB  SER A 239     9292   9966  16020    960  -1326  -1972       C  
ATOM     17  OG  SER A 239      20.995  28.158  32.911  1.00 99.04           O  
ANISOU   17  OG  SER A 239     9923  10723  16984    953  -1374  -2088       O  
ATOM     18  N   VAL A 240      16.903  26.560  32.024  1.00 90.27           N  
ANISOU   18  N   VAL A 240     9307   9656  15336    876  -1104  -1793       N  
ATOM     19  CA  VAL A 240      15.719  26.586  31.181  1.00 92.22           C  
ANISOU   19  CA  VAL A 240     9677   9993  15371    769   -902  -1763       C  
ATOM     20  C   VAL A 240      14.796  27.746  31.572  1.00 90.84           C  
ANISOU   20  C   VAL A 240     9665   9962  14888    690   -878  -1628       C  
ATOM     21  O   VAL A 240      14.576  28.024  32.755  1.00 87.38           O  
ANISOU   21  O   VAL A 240     9337   9517  14345    729  -1048  -1486       O  
ATOM     22  CB  VAL A 240      14.960  25.237  31.229  1.00 89.75           C  
ANISOU   22  CB  VAL A 240     9471   9573  15058    801   -933  -1691       C  
ATOM     23  CG1 VAL A 240      14.272  25.031  32.567  1.00 89.43           C  
ANISOU   23  CG1 VAL A 240     9620   9490  14869    846  -1125  -1484       C  
ATOM     24  CG2 VAL A 240      13.960  25.158  30.100  1.00 89.39           C  
ANISOU   24  CG2 VAL A 240     9496   9605  14863    693   -710  -1717       C  
ATOM     25  N   PHE A 241      14.290  28.447  30.563  1.00 92.54           N  
ANISOU   25  N   PHE A 241     9898  10302  14961    578   -667  -1678       N  
ATOM     26  CA  PHE A 241      13.395  29.571  30.798  1.00 89.35           C  
ANISOU   26  CA  PHE A 241     9637  10034  14277    500   -628  -1565       C  
ATOM     27  C   PHE A 241      12.119  29.414  29.985  1.00 82.97           C  
ANISOU   27  C   PHE A 241     8951   9287  13285    412   -469  -1531       C  
ATOM     28  O   PHE A 241      12.157  29.127  28.785  1.00 79.89           O  
ANISOU   28  O   PHE A 241     8502   8905  12947    362   -306  -1654       O  
ATOM     29  CB  PHE A 241      14.091  30.893  30.466  1.00 90.89           C  
ANISOU   29  CB  PHE A 241     9737  10331  14465    449   -551  -1653       C  
ATOM     30  CG  PHE A 241      15.290  31.173  31.330  1.00 99.32           C  
ANISOU   30  CG  PHE A 241    10685  11346  15705    530   -720  -1682       C  
ATOM     31  CD1 PHE A 241      15.154  31.309  32.703  1.00 98.47           C  
ANISOU   31  CD1 PHE A 241    10679  11212  15524    593   -933  -1537       C  
ATOM     32  CD2 PHE A 241      16.552  31.301  30.770  1.00105.75           C  
ANISOU   32  CD2 PHE A 241    11290  12135  16758    540   -666  -1859       C  
ATOM     33  CE1 PHE A 241      16.253  31.563  33.502  1.00 99.76           C  
ANISOU   33  CE1 PHE A 241    10739  11322  15844    670  -1108  -1566       C  
ATOM     34  CE2 PHE A 241      17.655  31.558  31.565  1.00106.14           C  
ANISOU   34  CE2 PHE A 241    11216  12131  16982    616   -834  -1893       C  
ATOM     35  CZ  PHE A 241      17.504  31.689  32.932  1.00103.26           C  
ANISOU   35  CZ  PHE A 241    10957  11739  16538    683  -1065  -1745       C  
ATOM     36  N   LEU A 242      10.988  29.598  30.654  1.00 75.33           N  
ANISOU   36  N   LEU A 242     8157   8360  12106    392   -519  -1369       N  
ATOM     37  CA  LEU A 242       9.687  29.380  30.040  1.00 66.88           C  
ANISOU   37  CA  LEU A 242     7205   7336  10872    317   -400  -1322       C  
ATOM     38  C   LEU A 242       8.930  30.695  29.876  1.00 64.52           C  
ANISOU   38  C   LEU A 242     6994   7184  10336    230   -316  -1269       C  
ATOM     39  O   LEU A 242       8.714  31.424  30.845  1.00 65.53           O  
ANISOU   39  O   LEU A 242     7197   7354  10346    241   -406  -1160       O  
ATOM     40  CB  LEU A 242       8.873  28.396  30.879  1.00 59.80           C  
ANISOU   40  CB  LEU A 242     6432   6350   9939    359   -508  -1183       C  
ATOM     41  CG  LEU A 242       7.596  27.859  30.242  1.00 55.90           C  
ANISOU   41  CG  LEU A 242     6035   5869   9336    293   -399  -1151       C  
ATOM     42  CD1 LEU A 242       7.907  27.248  28.885  1.00 55.21           C  
ANISOU   42  CD1 LEU A 242     5847   5755   9375    265   -266  -1310       C  
ATOM     43  CD2 LEU A 242       6.951  26.837  31.160  1.00 48.90           C  
ANISOU   43  CD2 LEU A 242     5259   4875   8445    337   -509  -1019       C  
ATOM     44  N   PHE A 243       8.525  30.992  28.648  1.00 59.61           N  
ANISOU   44  N   PHE A 243     6373   6634   9644    144   -147  -1349       N  
ATOM     45  CA  PHE A 243       7.882  32.267  28.357  1.00 59.69           C  
ANISOU   45  CA  PHE A 243     6458   6777   9445     63    -66  -1315       C  
ATOM     46  C   PHE A 243       6.436  32.080  27.916  1.00 61.87           C  
ANISOU   46  C   PHE A 243     6859   7090   9558      1      1  -1250       C  
ATOM     47  O   PHE A 243       6.136  31.194  27.116  1.00 69.30           O  
ANISOU   47  O   PHE A 243     7795   7986  10551    -18     69  -1309       O  
ATOM     48  CB  PHE A 243       8.662  33.018  27.279  1.00 60.10           C  
ANISOU   48  CB  PHE A 243     6418   6889   9530      6     71  -1463       C  
ATOM     49  CG  PHE A 243      10.106  33.235  27.623  1.00 63.76           C  
ANISOU   49  CG  PHE A 243     6736   7315  10176     58     20  -1546       C  
ATOM     50  CD1 PHE A 243      10.497  34.332  28.370  1.00 64.62           C  
ANISOU   50  CD1 PHE A 243     6840   7480  10233     65    -51  -1501       C  
ATOM     51  CD2 PHE A 243      11.073  32.336  27.202  1.00 67.73           C  
ANISOU   51  CD2 PHE A 243     7100   7722  10913    100     39  -1675       C  
ATOM     52  CE1 PHE A 243      11.825  34.532  28.690  1.00 66.81           C  
ANISOU   52  CE1 PHE A 243     6972   7718  10692    112   -107  -1584       C  
ATOM     53  CE2 PHE A 243      12.402  32.530  27.519  1.00 66.62           C  
ANISOU   53  CE2 PHE A 243     6808   7542  10964    150    -13  -1760       C  
ATOM     54  CZ  PHE A 243      12.779  33.630  28.263  1.00 67.37           C  
ANISOU   54  CZ  PHE A 243     6895   7694  11008    155    -90  -1715       C  
ATOM     55  N   PRO A 244       5.538  32.921  28.446  1.00 55.53           N  
ANISOU   55  N   PRO A 244     6165   6367   8567    -29    -20  -1134       N  
ATOM     56  CA  PRO A 244       4.122  32.902  28.078  1.00 53.52           C  
ANISOU   56  CA  PRO A 244     6018   6155   8161    -88     37  -1073       C  
ATOM     57  C   PRO A 244       3.920  33.444  26.668  1.00 48.33           C  
ANISOU   57  C   PRO A 244     5359   5572   7432   -172    177  -1174       C  
ATOM     58  O   PRO A 244       4.857  33.990  26.090  1.00 48.68           O  
ANISOU   58  O   PRO A 244     5333   5644   7520   -190    239  -1277       O  
ATOM     59  CB  PRO A 244       3.482  33.820  29.123  1.00 53.93           C  
ANISOU   59  CB  PRO A 244     6163   6271   8058    -88    -28   -938       C  
ATOM     60  CG  PRO A 244       4.556  34.787  29.456  1.00 47.59           C  
ANISOU   60  CG  PRO A 244     5302   5507   7275    -68    -60   -971       C  
ATOM     61  CD  PRO A 244       5.838  33.992  29.412  1.00 56.12           C  
ANISOU   61  CD  PRO A 244     6259   6495   8569     -9    -99  -1064       C  
ATOM     62  N   PRO A 245       2.716  33.279  26.111  1.00 45.89           N  
ANISOU   62  N   PRO A 245     5131   5288   7018   -225    226  -1148       N  
ATOM     63  CA  PRO A 245       2.417  33.901  24.818  1.00 45.63           C  
ANISOU   63  CA  PRO A 245     5126   5326   6885   -306    339  -1229       C  
ATOM     64  C   PRO A 245       2.271  35.416  24.937  1.00 42.12           C  
ANISOU   64  C   PRO A 245     4729   4987   6289   -341    350  -1189       C  
ATOM     65  O   PRO A 245       2.155  35.926  26.049  1.00 38.91           O  
ANISOU   65  O   PRO A 245     4343   4601   5839   -306    270  -1087       O  
ATOM     66  CB  PRO A 245       1.090  33.247  24.411  1.00 43.26           C  
ANISOU   66  CB  PRO A 245     4900   5010   6525   -341    350  -1194       C  
ATOM     67  CG  PRO A 245       0.511  32.719  25.686  1.00 44.72           C  
ANISOU   67  CG  PRO A 245     5112   5149   6729   -290    250  -1063       C  
ATOM     68  CD  PRO A 245       1.666  32.343  26.544  1.00 47.42           C  
ANISOU   68  CD  PRO A 245     5384   5426   7207   -214    180  -1060       C  
ATOM     69  N   LYS A 246       2.296  36.120  23.807  1.00 45.25           N  
ANISOU   69  N   LYS A 246     5152   5442   6600   -410    448  -1269       N  
ATOM     70  CA  LYS A 246       1.996  37.546  23.797  1.00 42.61           C  
ANISOU   70  CA  LYS A 246     4881   5201   6110   -450    461  -1228       C  
ATOM     71  C   LYS A 246       0.516  37.732  24.071  1.00 50.62           C  
ANISOU   71  C   LYS A 246     5988   6250   6997   -464    415  -1121       C  
ATOM     72  O   LYS A 246      -0.314  37.044  23.473  1.00 56.30           O  
ANISOU   72  O   LYS A 246     6742   6945   7705   -489    430  -1132       O  
ATOM     73  CB  LYS A 246       2.368  38.185  22.461  1.00 41.12           C  
ANISOU   73  CB  LYS A 246     4715   5051   5855   -526    579  -1340       C  
ATOM     74  CG  LYS A 246       3.731  37.775  21.952  1.00 46.43           C  
ANISOU   74  CG  LYS A 246     5291   5677   6674   -526    658  -1472       C  
ATOM     75  CD  LYS A 246       4.189  38.651  20.799  1.00 63.76           C  
ANISOU   75  CD  LYS A 246     7523   7917   8786   -608    786  -1572       C  
ATOM     76  CE  LYS A 246       5.271  39.612  21.260  1.00 76.39           C  
ANISOU   76  CE  LYS A 246     9056   9545  10424   -603    801  -1591       C  
ATOM     77  NZ  LYS A 246       6.427  38.886  21.863  1.00 80.05           N1+
ANISOU   77  NZ  LYS A 246     9369   9941  11106   -537    772  -1645       N1+
ATOM     78  N   PRO A 247       0.187  38.653  24.991  1.00 44.45           N  
ANISOU   78  N   PRO A 247     5241   5519   6130   -447    360  -1023       N  
ATOM     79  CA  PRO A 247      -1.189  38.945  25.392  1.00 40.56           C  
ANISOU   79  CA  PRO A 247     4823   5058   5529   -456    321   -921       C  
ATOM     80  C   PRO A 247      -2.126  39.064  24.198  1.00 43.58           C  
ANISOU   80  C   PRO A 247     5265   5468   5825   -518    367   -960       C  
ATOM     81  O   PRO A 247      -3.248  38.576  24.257  1.00 46.56           O  
ANISOU   81  O   PRO A 247     5672   5830   6190   -523    341   -913       O  
ATOM     82  CB  PRO A 247      -1.054  40.277  26.131  1.00 29.37           C  
ANISOU   82  CB  PRO A 247     3432   3706   4019   -447    293   -860       C  
ATOM     83  CG  PRO A 247       0.300  40.198  26.749  1.00 28.45           C  
ANISOU   83  CG  PRO A 247     3243   3562   4006   -403    266   -886       C  
ATOM     84  CD  PRO A 247       1.162  39.445  25.762  1.00 34.26           C  
ANISOU   84  CD  PRO A 247     3910   4251   4855   -417    330  -1010       C  
ATOM     85  N   LYS A 248      -1.652  39.670  23.114  1.00 39.07           N  
ANISOU   85  N   LYS A 248     4717   4930   5200   -568    435  -1048       N  
ATOM     86  CA  LYS A 248      -2.483  39.872  21.935  1.00 40.43           C  
ANISOU   86  CA  LYS A 248     4966   5123   5271   -629    466  -1086       C  
ATOM     87  C   LYS A 248      -2.810  38.553  21.232  1.00 42.65           C  
ANISOU   87  C   LYS A 248     5239   5341   5625   -642    482  -1145       C  
ATOM     88  O   LYS A 248      -3.906  38.379  20.699  1.00 33.48           O  
ANISOU   88  O   LYS A 248     4132   4180   4409   -672    460  -1137       O  
ATOM     89  CB  LYS A 248      -1.795  40.832  20.960  1.00 35.28           C  
ANISOU   89  CB  LYS A 248     4360   4511   4533   -684    541  -1166       C  
ATOM     90  CG  LYS A 248      -2.662  41.248  19.783  1.00 41.82           C  
ANISOU   90  CG  LYS A 248     5298   5363   5228   -747    555  -1193       C  
ATOM     91  CD  LYS A 248      -1.906  42.159  18.831  1.00 47.26           C  
ANISOU   91  CD  LYS A 248     6051   6079   5825   -808    640  -1270       C  
ATOM     92  CE  LYS A 248      -2.788  42.586  17.668  1.00 55.54           C  
ANISOU   92  CE  LYS A 248     7233   7142   6726   -868    636  -1291       C  
ATOM     93  NZ  LYS A 248      -2.047  43.405  16.670  1.00 63.09           N1+
ANISOU   93  NZ  LYS A 248     8277   8114   7580   -937    730  -1367       N1+
ATOM     94  N   ASP A 249      -1.859  37.624  21.239  1.00 45.33           N  
ANISOU   94  N   ASP A 249     5506   5620   6098   -618    513  -1208       N  
ATOM     95  CA  ASP A 249      -2.026  36.361  20.526  1.00 49.27           C  
ANISOU   95  CA  ASP A 249     5995   6051   6674   -631    538  -1279       C  
ATOM     96  C   ASP A 249      -3.093  35.473  21.164  1.00 46.54           C  
ANISOU   96  C   ASP A 249     5643   5662   6377   -604    466  -1198       C  
ATOM     97  O   ASP A 249      -3.788  34.730  20.469  1.00 42.96           O  
ANISOU   97  O   ASP A 249     5216   5173   5933   -634    469  -1235       O  
ATOM     98  CB  ASP A 249      -0.692  35.611  20.451  1.00 49.33           C  
ANISOU   98  CB  ASP A 249     5916   5998   6830   -604    590  -1369       C  
ATOM     99  CG  ASP A 249       0.331  36.326  19.587  1.00 48.72           C  
ANISOU   99  CG  ASP A 249     5843   5950   6719   -648    691  -1476       C  
ATOM    100  OD1 ASP A 249      -0.077  37.132  18.722  1.00 51.00           O  
ANISOU  100  OD1 ASP A 249     6226   6290   6860   -713    731  -1498       O  
ATOM    101  OD2 ASP A 249       1.542  36.079  19.770  1.00 44.69           O1-
ANISOU  101  OD2 ASP A 249     5242   5406   6334   -620    730  -1539       O1-
ATOM    102  N   THR A 250      -3.225  35.559  22.483  1.00 43.45           N  
ANISOU  102  N   THR A 250     5225   5271   6015   -552    405  -1091       N  
ATOM    103  CA  THR A 250      -4.223  34.773  23.199  1.00 39.43           C  
ANISOU  103  CA  THR A 250     4716   4717   5548   -532    351  -1007       C  
ATOM    104  C   THR A 250      -5.604  35.389  23.087  1.00 35.95           C  
ANISOU  104  C   THR A 250     4332   4327   5000   -569    327   -952       C  
ATOM    105  O   THR A 250      -6.607  34.716  23.292  1.00 39.73           O  
ANISOU  105  O   THR A 250     4813   4769   5513   -575    302   -913       O  
ATOM    106  CB  THR A 250      -3.883  34.635  24.695  1.00 41.61           C  
ANISOU  106  CB  THR A 250     4962   4966   5881   -468    298   -909       C  
ATOM    107  CG2 THR A 250      -2.471  34.145  24.874  1.00 46.55           C  
ANISOU  107  CG2 THR A 250     5523   5540   6623   -423    299   -963       C  
ATOM    108  OG1 THR A 250      -4.027  35.907  25.340  1.00 42.27           O  
ANISOU  108  OG1 THR A 250     5077   5126   5857   -463    277   -838       O  
ATOM    109  N   LEU A 251      -5.651  36.675  22.769  1.00 39.22           N  
ANISOU  109  N   LEU A 251     4788   4820   5293   -592    335   -953       N  
ATOM    110  CA  LEU A 251      -6.905  37.408  22.767  1.00 39.83           C  
ANISOU  110  CA  LEU A 251     4912   4946   5276   -615    302   -898       C  
ATOM    111  C   LEU A 251      -7.539  37.459  21.382  1.00 43.49           C  
ANISOU  111  C   LEU A 251     5427   5418   5680   -672    305   -973       C  
ATOM    112  O   LEU A 251      -8.764  37.408  21.253  1.00 36.41           O  
ANISOU  112  O   LEU A 251     4545   4521   4769   -690    263   -947       O  
ATOM    113  CB  LEU A 251      -6.684  38.825  23.293  1.00 39.15           C  
ANISOU  113  CB  LEU A 251     4851   4933   5092   -603    295   -847       C  
ATOM    114  CG  LEU A 251      -6.266  38.929  24.757  1.00 41.00           C  
ANISOU  114  CG  LEU A 251     5054   5164   5361   -549    273   -761       C  
ATOM    115  CD1 LEU A 251      -5.851  40.354  25.090  1.00 38.39           C  
ANISOU  115  CD1 LEU A 251     4751   4904   4933   -543    272   -735       C  
ATOM    116  CD2 LEU A 251      -7.391  38.471  25.663  1.00 34.73           C  
ANISOU  116  CD2 LEU A 251     4258   4343   4596   -534    243   -670       C  
ATOM    117  N   MET A 252      -6.708  37.563  20.350  1.00 40.14           N  
ANISOU  117  N   MET A 252     5032   4996   5221   -703    355  -1070       N  
ATOM    118  CA  MET A 252      -7.201  37.638  18.978  1.00 35.35           C  
ANISOU  118  CA  MET A 252     4502   4393   4537   -761    356  -1146       C  
ATOM    119  C   MET A 252      -7.200  36.258  18.322  1.00 37.80           C  
ANISOU  119  C   MET A 252     4797   4630   4935   -778    375  -1225       C  
ATOM    120  O   MET A 252      -6.165  35.594  18.258  1.00 42.28           O  
ANISOU  120  O   MET A 252     5324   5156   5583   -766    434  -1284       O  
ATOM    121  CB  MET A 252      -6.355  38.617  18.161  1.00 30.67           C  
ANISOU  121  CB  MET A 252     3978   3843   3832   -797    412  -1209       C  
ATOM    122  CG  MET A 252      -6.294  40.024  18.737  1.00 28.32           C  
ANISOU  122  CG  MET A 252     3702   3614   3446   -784    396  -1139       C  
ATOM    123  SD  MET A 252      -7.904  40.831  18.843  1.00 49.10           S  
ANISOU  123  SD  MET A 252     6384   6284   5989   -787    299  -1058       S  
ATOM    124  CE  MET A 252      -8.162  40.837  20.614  1.00 47.07           C  
ANISOU  124  CE  MET A 252     6034   6036   5814   -720    269   -940       C  
ATOM    125  N   ILE A 253      -8.365  35.837  17.838  1.00 36.58           N  
ANISOU  125  N   ILE A 253     4669   4453   4776   -805    321  -1231       N  
ATOM    126  CA  ILE A 253      -8.515  34.509  17.245  1.00 40.55           C  
ANISOU  126  CA  ILE A 253     5161   4882   5365   -825    329  -1304       C  
ATOM    127  C   ILE A 253      -7.763  34.402  15.916  1.00 35.08           C  
ANISOU  127  C   ILE A 253     4539   4175   4613   -871    393  -1430       C  
ATOM    128  O   ILE A 253      -7.388  33.312  15.489  1.00 42.18           O  
ANISOU  128  O   ILE A 253     5422   5010   5596   -879    432  -1507       O  
ATOM    129  CB  ILE A 253     -10.012  34.145  17.034  1.00 39.49           C  
ANISOU  129  CB  ILE A 253     5034   4726   5243   -848    247  -1284       C  
ATOM    130  CG1 ILE A 253     -10.170  32.651  16.729  1.00 44.27           C  
ANISOU  130  CG1 ILE A 253     5608   5244   5967   -860    253  -1342       C  
ATOM    131  CG2 ILE A 253     -10.642  35.009  15.945  1.00 29.05           C  
ANISOU  131  CG2 ILE A 253     3814   3445   3780   -895    198  -1323       C  
ATOM    132  CD1 ILE A 253      -9.596  31.744  17.797  1.00 38.36           C  
ANISOU  132  CD1 ILE A 253     4773   4441   5362   -811    288  -1299       C  
ATOM    133  N   SER A 254      -7.520  35.543  15.278  1.00 36.39           N  
ANISOU  133  N   SER A 254     4792   4398   4636   -903    411  -1452       N  
ATOM    134  CA  SER A 254      -6.798  35.576  14.012  1.00 39.75           C  
ANISOU  134  CA  SER A 254     5309   4813   4984   -958    488  -1571       C  
ATOM    135  C   SER A 254      -5.321  35.262  14.219  1.00 46.51           C  
ANISOU  135  C   SER A 254     6099   5648   5925   -939    600  -1626       C  
ATOM    136  O   SER A 254      -4.574  35.075  13.260  1.00 53.59           O  
ANISOU  136  O   SER A 254     7046   6521   6793   -981    692  -1738       O  
ATOM    137  CB  SER A 254      -6.951  36.941  13.339  1.00 40.00           C  
ANISOU  137  CB  SER A 254     5464   4904   4831  -1000    477  -1568       C  
ATOM    138  OG  SER A 254      -6.446  37.976  14.167  1.00 43.86           O  
ANISOU  138  OG  SER A 254     5917   5449   5298   -970    495  -1497       O  
ATOM    139  N   ARG A 255      -4.904  35.205  15.478  1.00 42.87           N  
ANISOU  139  N   ARG A 255     5526   5191   5571   -875    591  -1552       N  
ATOM    140  CA  ARG A 255      -3.501  35.004  15.804  1.00 42.81           C  
ANISOU  140  CA  ARG A 255     5440   5164   5661   -847    675  -1598       C  
ATOM    141  C   ARG A 255      -3.250  33.664  16.490  1.00 43.94           C  
ANISOU  141  C   ARG A 255     5477   5230   5990   -792    662  -1596       C  
ATOM    142  O   ARG A 255      -4.174  33.022  16.992  1.00 47.83           O  
ANISOU  142  O   ARG A 255     5950   5692   6530   -771    587  -1531       O  
ATOM    143  CB  ARG A 255      -3.005  36.148  16.686  1.00 43.60           C  
ANISOU  143  CB  ARG A 255     5508   5327   5730   -817    669  -1523       C  
ATOM    144  CG  ARG A 255      -3.147  37.518  16.040  1.00 50.09           C  
ANISOU  144  CG  ARG A 255     6439   6217   6375   -871    686  -1524       C  
ATOM    145  CD  ARG A 255      -2.498  38.588  16.899  1.00 58.59           C  
ANISOU  145  CD  ARG A 255     7476   7347   7438   -843    692  -1464       C  
ATOM    146  NE  ARG A 255      -1.830  39.588  16.077  1.00 65.34           N  
ANISOU  146  NE  ARG A 255     8409   8237   8182   -902    777  -1527       N  
ATOM    147  CZ  ARG A 255      -0.625  39.420  15.547  1.00 70.00           C  
ANISOU  147  CZ  ARG A 255     8974   8801   8821   -929    894  -1634       C  
ATOM    148  NH1 ARG A 255      -0.083  40.377  14.808  1.00 77.75           N1+
ANISOU  148  NH1 ARG A 255    10037   9812   9693   -992    981  -1687       N1+
ATOM    149  NH2 ARG A 255       0.035  38.290  15.756  1.00 63.50           N  
ANISOU  149  NH2 ARG A 255     8045   7919   8164   -894    927  -1692       N  
ATOM    150  N   THR A 256      -1.989  33.250  16.508  1.00 47.85           N  
ANISOU  150  N   THR A 256     5901   5686   6595   -769    736  -1670       N  
ATOM    151  CA  THR A 256      -1.614  31.948  17.037  1.00 51.68           C  
ANISOU  151  CA  THR A 256     6290   6083   7262   -715    724  -1683       C  
ATOM    152  C   THR A 256      -0.691  32.086  18.244  1.00 50.56           C  
ANISOU  152  C   THR A 256     6046   5936   7230   -642    701  -1630       C  
ATOM    153  O   THR A 256       0.493  32.371  18.085  1.00 49.08           O  
ANISOU  153  O   THR A 256     5807   5749   7092   -637    770  -1704       O  
ATOM    154  CB  THR A 256      -0.914  31.087  15.964  1.00 56.89           C  
ANISOU  154  CB  THR A 256     6945   6676   7993   -742    823  -1837       C  
ATOM    155  CG2 THR A 256      -0.640  29.685  16.494  1.00 62.66           C  
ANISOU  155  CG2 THR A 256     7583   7305   8919   -682    798  -1848       C  
ATOM    156  OG1 THR A 256      -1.737  31.007  14.796  1.00 55.44           O  
ANISOU  156  OG1 THR A 256     6876   6498   7692   -814    839  -1893       O  
ATOM    157  N   PRO A 257      -1.234  31.887  19.455  1.00 48.01           N  
ANISOU  157  N   PRO A 257     5696   5602   6944   -590    604  -1504       N  
ATOM    158  CA  PRO A 257      -0.436  31.968  20.683  1.00 40.77           C  
ANISOU  158  CA  PRO A 257     4699   4671   6121   -518    558  -1442       C  
ATOM    159  C   PRO A 257       0.527  30.798  20.857  1.00 42.35           C  
ANISOU  159  C   PRO A 257     4808   4769   6515   -464    564  -1507       C  
ATOM    160  O   PRO A 257       0.222  29.671  20.471  1.00 43.83           O  
ANISOU  160  O   PRO A 257     4994   4881   6778   -466    570  -1547       O  
ATOM    161  CB  PRO A 257      -1.499  31.975  21.792  1.00 44.00           C  
ANISOU  161  CB  PRO A 257     5138   5088   6493   -492    462  -1294       C  
ATOM    162  CG  PRO A 257      -2.667  31.278  21.192  1.00 45.50           C  
ANISOU  162  CG  PRO A 257     5377   5249   6661   -533    459  -1300       C  
ATOM    163  CD  PRO A 257      -2.661  31.652  19.735  1.00 41.72           C  
ANISOU  163  CD  PRO A 257     4949   4807   6095   -602    534  -1413       C  
ATOM    164  N   GLU A 258       1.687  31.080  21.438  1.00 44.73           N  
ANISOU  164  N   GLU A 258     5028   5063   6902   -415    555  -1519       N  
ATOM    165  CA  GLU A 258       2.705  30.067  21.667  1.00 50.87           C  
ANISOU  165  CA  GLU A 258     5704   5740   7882   -353    547  -1584       C  
ATOM    166  C   GLU A 258       3.283  30.159  23.068  1.00 53.97           C  
ANISOU  166  C   GLU A 258     6041   6108   8356   -270    438  -1494       C  
ATOM    167  O   GLU A 258       3.469  31.250  23.601  1.00 55.34           O  
ANISOU  167  O   GLU A 258     6221   6354   8450   -269    411  -1440       O  
ATOM    168  CB  GLU A 258       3.853  30.209  20.657  1.00 46.92           C  
ANISOU  168  CB  GLU A 258     5141   5237   7451   -379    667  -1747       C  
ATOM    169  CG  GLU A 258       3.462  30.228  19.189  1.00 52.06           C  
ANISOU  169  CG  GLU A 258     5865   5912   8004   -467    787  -1852       C  
ATOM    170  CD  GLU A 258       4.632  30.620  18.300  1.00 57.88           C  
ANISOU  170  CD  GLU A 258     6552   6656   8782   -503    924  -2004       C  
ATOM    171  OE1 GLU A 258       4.632  30.249  17.108  1.00 62.57           O  
ANISOU  171  OE1 GLU A 258     7188   7229   9355   -561   1034  -2122       O  
ATOM    172  OE2 GLU A 258       5.554  31.300  18.800  1.00 60.51           O1-
ANISOU  172  OE2 GLU A 258     6808   7014   9169   -477    925  -2009       O1-
ATOM    173  N   VAL A 259       3.591  29.014  23.659  1.00 52.29           N  
ANISOU  173  N   VAL A 259     5779   5786   8301   -202    368  -1480       N  
ATOM    174  CA  VAL A 259       4.436  28.996  24.843  1.00 55.35           C  
ANISOU  174  CA  VAL A 259     6105   6130   8797   -117    261  -1427       C  
ATOM    175  C   VAL A 259       5.831  28.560  24.411  1.00 55.20           C  
ANISOU  175  C   VAL A 259     5952   6044   8976    -78    297  -1572       C  
ATOM    176  O   VAL A 259       5.975  27.599  23.656  1.00 57.78           O  
ANISOU  176  O   VAL A 259     6245   6299   9411    -81    357  -1670       O  
ATOM    177  CB  VAL A 259       3.887  28.067  25.926  1.00 56.02           C  
ANISOU  177  CB  VAL A 259     6235   6126   8922    -60    142  -1302       C  
ATOM    178  CG1 VAL A 259       4.904  27.896  27.032  1.00 56.80           C  
ANISOU  178  CG1 VAL A 259     6274   6158   9151     34     19  -1268       C  
ATOM    179  CG2 VAL A 259       2.582  28.624  26.477  1.00 59.35           C  
ANISOU  179  CG2 VAL A 259     6776   6617   9157    -98    115  -1162       C  
ATOM    180  N   THR A 260       6.858  29.270  24.872  1.00 50.37           N  
ANISOU  180  N   THR A 260     5261   5455   8423    -43    265  -1593       N  
ATOM    181  CA  THR A 260       8.211  29.044  24.373  1.00 47.57           C  
ANISOU  181  CA  THR A 260     4762   5050   8264    -17    319  -1748       C  
ATOM    182  C   THR A 260       9.178  28.613  25.472  1.00 50.27           C  
ANISOU  182  C   THR A 260     5004   5299   8796     92    172  -1727       C  
ATOM    183  O   THR A 260       9.426  29.347  26.428  1.00 55.27           O  
ANISOU  183  O   THR A 260     5640   5967   9393    124     69  -1646       O  
ATOM    184  CB  THR A 260       8.760  30.310  23.682  1.00 51.38           C  
ANISOU  184  CB  THR A 260     5211   5632   8678    -85    439  -1836       C  
ATOM    185  CG2 THR A 260      10.061  30.010  22.962  1.00 59.67           C  
ANISOU  185  CG2 THR A 260     6112   6627   9931    -77    538  -2018       C  
ATOM    186  OG1 THR A 260       7.801  30.794  22.731  1.00 57.96           O  
ANISOU  186  OG1 THR A 260     6161   6549   9311   -183    552  -1838       O  
ATOM    187  N   CYS A 261       9.726  27.412  25.322  1.00 55.45           N  
ANISOU  187  N   CYS A 261     5576   5832   9659    150    155  -1805       N  
ATOM    188  CA  CYS A 261      10.688  26.877  26.276  1.00 60.20           C  
ANISOU  188  CA  CYS A 261     6078   6327  10468    261      2  -1799       C  
ATOM    189  C   CYS A 261      12.100  27.032  25.730  1.00 64.54           C  
ANISOU  189  C   CYS A 261     6444   6851  11227    280     70  -1977       C  
ATOM    190  O   CYS A 261      12.430  26.483  24.678  1.00 60.57           O  
ANISOU  190  O   CYS A 261     5871   6310  10832    255    205  -2124       O  
ATOM    191  CB  CYS A 261      10.381  25.409  26.574  1.00 61.18           C  
ANISOU  191  CB  CYS A 261     6229   6314  10703    324    -80  -1762       C  
ATOM    192  SG  CYS A 261      11.358  24.690  27.896  1.00 66.23           S  
ANISOU  192  SG  CYS A 261     6792   6806  11568    469   -309  -1717       S  
ATOM    193  N   VAL A 262      12.929  27.787  26.443  1.00 68.41           N  
ANISOU  193  N   VAL A 262     6856   7362  11777    319    -19  -1971       N  
ATOM    194  CA  VAL A 262      14.276  28.100  25.973  1.00 71.30           C  
ANISOU  194  CA  VAL A 262     7035   7713  12343    327     52  -2142       C  
ATOM    195  C   VAL A 262      15.336  27.512  26.895  1.00 69.42           C  
ANISOU  195  C   VAL A 262     6660   7351  12367    454   -133  -2161       C  
ATOM    196  O   VAL A 262      15.345  27.785  28.096  1.00 65.65           O  
ANISOU  196  O   VAL A 262     6225   6865  11856    513   -322  -2035       O  
ATOM    197  CB  VAL A 262      14.493  29.626  25.859  1.00 74.65           C  
ANISOU  197  CB  VAL A 262     7456   8269  12639    254    123  -2152       C  
ATOM    198  CG1 VAL A 262      15.883  29.934  25.315  1.00 79.07           C  
ANISOU  198  CG1 VAL A 262     7815   8809  13419    250    219  -2340       C  
ATOM    199  CG2 VAL A 262      13.424  30.249  24.975  1.00 70.23           C  
ANISOU  199  CG2 VAL A 262     7043   7825  11816    135    285  -2125       C  
ATOM    200  N   VAL A 263      16.228  26.705  26.327  1.00 71.10           N  
ANISOU  200  N   VAL A 263     6713   7462  12841    495    -81  -2322       N  
ATOM    201  CA  VAL A 263      17.309  26.099  27.097  1.00 74.67           C  
ANISOU  201  CA  VAL A 263     7021   7788  13564    614   -259  -2355       C  
ATOM    202  C   VAL A 263      18.652  26.752  26.768  1.00 80.94           C  
ANISOU  202  C   VAL A 263     7652   8618  14482    565   -203  -2483       C  
ATOM    203  O   VAL A 263      19.059  26.809  25.606  1.00 79.86           O  
ANISOU  203  O   VAL A 263     7457   8518  14369    468     -1  -2615       O  
ATOM    204  CB  VAL A 263      17.408  24.585  26.840  1.00 71.33           C  
ANISOU  204  CB  VAL A 263     6583   7244  13274    649   -285  -2380       C  
ATOM    205  CG1 VAL A 263      18.340  23.941  27.854  1.00 70.09           C  
ANISOU  205  CG1 VAL A 263     6345   6970  13315    754   -520  -2350       C  
ATOM    206  CG2 VAL A 263      16.033  23.944  26.905  1.00 65.85           C  
ANISOU  206  CG2 VAL A 263     6060   6513  12447    664   -289  -2276       C  
ATOM    207  N   VAL A 264      19.334  27.243  27.798  1.00 85.76           N  
ANISOU  207  N   VAL A 264     8205   9212  15168    627   -386  -2441       N  
ATOM    208  CA  VAL A 264      20.621  27.904  27.617  1.00 90.39           C  
ANISOU  208  CA  VAL A 264     8646   9816  15881    582   -353  -2559       C  
ATOM    209  C   VAL A 264      21.729  27.176  28.375  1.00 97.20           C  
ANISOU  209  C   VAL A 264     9402  10549  16981    670   -559  -2580       C  
ATOM    210  O   VAL A 264      21.455  26.270  29.166  1.00 97.75           O  
ANISOU  210  O   VAL A 264     9526  10526  17088    768   -748  -2482       O  
ATOM    211  CB  VAL A 264      20.564  29.375  28.074  1.00 87.97           C  
ANISOU  211  CB  VAL A 264     8360   9617  15447    555   -368  -2514       C  
ATOM    212  CG1 VAL A 264      19.566  30.159  27.225  1.00 85.72           C  
ANISOU  212  CG1 VAL A 264     8172   9464  14933    456   -149  -2510       C  
ATOM    213  CG2 VAL A 264      20.203  29.462  29.546  1.00 89.90           C  
ANISOU  213  CG2 VAL A 264     8678   9834  15646    665   -635  -2352       C  
ATOM    214  N   ASP A 265      22.975  27.579  28.119  1.00101.14           N  
ANISOU  214  N   ASP A 265     9758  11034  17635    630   -521  -2710       N  
ATOM    215  CA  ASP A 265      24.167  26.943  28.692  1.00101.89           C  
ANISOU  215  CA  ASP A 265     9732  11003  17979    700   -695  -2765       C  
ATOM    216  C   ASP A 265      24.242  25.470  28.311  1.00 99.83           C  
ANISOU  216  C   ASP A 265     9437  10637  17856    734   -697  -2804       C  
ATOM    217  O   ASP A 265      24.521  24.613  29.150  1.00 99.49           O  
ANISOU  217  O   ASP A 265     9388  10483  17932    834   -915  -2751       O  
ATOM    218  CB  ASP A 265      24.200  27.101  30.220  1.00105.09           C  
ANISOU  218  CB  ASP A 265    10192  11366  18373    809   -993  -2628       C  
ATOM    219  CG  ASP A 265      24.433  28.534  30.644  1.00104.06           C  
ANISOU  219  CG  ASP A 265    10061  11322  18156    778  -1012  -2613       C  
ATOM    220  OD1 ASP A 265      24.782  29.346  29.766  1.00104.06           O  
ANISOU  220  OD1 ASP A 265     9995  11396  18147    677   -802  -2726       O  
ATOM    221  OD2 ASP A 265      24.279  28.846  31.846  1.00101.20           O1-
ANISOU  221  OD2 ASP A 265     9774  10950  17727    851  -1234  -2488       O1-
ATOM    222  N   VAL A 266      23.996  25.186  27.038  1.00100.18           N  
ANISOU  222  N   VAL A 266     9471  10716  17875    646   -454  -2896       N  
ATOM    223  CA  VAL A 266      23.982  23.817  26.537  1.00100.24           C  
ANISOU  223  CA  VAL A 266     9454  10637  17995    666   -425  -2940       C  
ATOM    224  C   VAL A 266      25.360  23.386  26.055  1.00 97.80           C  
ANISOU  224  C   VAL A 266     8962  10246  17951    645   -383  -3110       C  
ATOM    225  O   VAL A 266      25.915  23.967  25.120  1.00 98.92           O  
ANISOU  225  O   VAL A 266     9028  10435  18122    541   -178  -3243       O  
ATOM    226  CB  VAL A 266      22.968  23.656  25.391  1.00100.08           C  
ANISOU  226  CB  VAL A 266     9529  10691  17805    581   -190  -2951       C  
ATOM    227  CG1 VAL A 266      23.119  22.295  24.730  1.00100.58           C  
ANISOU  227  CG1 VAL A 266     9547  10668  18000    587   -134  -3024       C  
ATOM    228  CG2 VAL A 266      21.548  23.861  25.904  1.00 98.41           C  
ANISOU  228  CG2 VAL A 266     9499  10535  17359    614   -247  -2785       C  
ATOM    229  N   SER A 267      25.893  22.349  26.690  1.00 98.38           N  
ANISOU  229  N   SER A 267     8973  10191  18216    742   -575  -3104       N  
ATOM    230  CA  SER A 267      27.249  21.864  26.422  1.00104.81           C  
ANISOU  230  CA  SER A 267     9604  10907  19313    743   -579  -3261       C  
ATOM    231  C   SER A 267      27.503  21.408  24.981  1.00109.09           C  
ANISOU  231  C   SER A 267    10070  11452  19927    646   -314  -3415       C  
ATOM    232  O   SER A 267      26.623  20.841  24.325  1.00105.89           O  
ANISOU  232  O   SER A 267     9754  11076  19403    619   -194  -3387       O  
ATOM    233  CB  SER A 267      27.567  20.709  27.375  1.00104.02           C  
ANISOU  233  CB  SER A 267     9480  10665  19376    871   -845  -3206       C  
ATOM    234  OG  SER A 267      28.557  19.850  26.834  1.00105.12           O  
ANISOU  234  OG  SER A 267     9461  10705  19776    869   -805  -3357       O  
ATOM    235  N   HIS A 268      28.720  21.661  24.505  1.00116.12           N  
ANISOU  235  N   HIS A 268    10800  12307  21013    592   -226  -3580       N  
ATOM    236  CA  HIS A 268      29.193  21.141  23.224  1.00116.25           C  
ANISOU  236  CA  HIS A 268    10726  12300  21144    506      3  -3740       C  
ATOM    237  C   HIS A 268      29.380  19.632  23.311  1.00113.85           C  
ANISOU  237  C   HIS A 268    10363  11874  21022    588    -99  -3759       C  
ATOM    238  O   HIS A 268      29.115  18.909  22.348  1.00110.49           O  
ANISOU  238  O   HIS A 268     9944  11445  20593    542     67  -3818       O  
ATOM    239  CB  HIS A 268      30.515  21.803  22.821  1.00122.00           C  
ANISOU  239  CB  HIS A 268    11295  13003  22057    435    105  -3911       C  
ATOM    240  CG  HIS A 268      30.366  22.919  21.833  1.00122.43           C  
ANISOU  240  CG  HIS A 268    11399  13172  21946    291    373  -3968       C  
ATOM    241  CD2 HIS A 268      31.099  23.249  20.743  1.00123.78           C  
ANISOU  241  CD2 HIS A 268    11491  13345  22196    171    612  -4131       C  
ATOM    242  ND1 HIS A 268      29.357  23.855  21.911  1.00118.66           N  
ANISOU  242  ND1 HIS A 268    11082  12821  21183    256    415  -3849       N  
ATOM    243  CE1 HIS A 268      29.476  24.713  20.914  1.00116.64           C  
ANISOU  243  CE1 HIS A 268    10847  12641  20830    121    661  -3932       C  
ATOM    244  NE2 HIS A 268      30.525  24.369  20.190  1.00119.72           N  
ANISOU  244  NE2 HIS A 268    11100  12957  21433     65    787  -4101       N  
ATOM    245  N   GLU A 269      29.833  19.164  24.473  1.00116.24           N  
ANISOU  245  N   GLU A 269    10618  12074  21476    710   -376  -3707       N  
ATOM    246  CA  GLU A 269      30.069  17.739  24.706  1.00120.38           C  
ANISOU  246  CA  GLU A 269    11089  12468  22182    800   -509  -3715       C  
ATOM    247  C   GLU A 269      28.826  16.893  24.461  1.00124.07           C  
ANISOU  247  C   GLU A 269    11705  12952  22482    821   -475  -3608       C  
ATOM    248  O   GLU A 269      28.811  16.032  23.574  1.00122.79           O  
ANISOU  248  O   GLU A 269    11509  12758  22387    791   -335  -3691       O  
ATOM    249  CB  GLU A 269      30.563  17.502  26.137  1.00119.49           C  
ANISOU  249  CB  GLU A 269    10951  12253  22196    929   -841  -3637       C  
ATOM    250  CG  GLU A 269      32.070  17.649  26.328  1.00119.75           C  
ANISOU  250  CG  GLU A 269    10785  12194  22521    939   -914  -3786       C  
ATOM    251  CD  GLU A 269      32.487  19.064  26.680  1.00114.46           C  
ANISOU  251  CD  GLU A 269    10096  11588  21805    899   -921  -3799       C  
ATOM    252  OE1 GLU A 269      31.600  19.902  26.953  1.00110.63           O  
ANISOU  252  OE1 GLU A 269     9758  11214  21062    879   -909  -3673       O  
ATOM    253  OE2 GLU A 269      33.707  19.337  26.685  1.00111.43           O1-
ANISOU  253  OE2 GLU A 269     9548  11139  21651    887   -937  -3938       O1-
ATOM    254  N   ASP A 270      27.789  17.140  25.256  1.00133.20           N  
ANISOU  254  N   ASP A 270    13030  14155  23426    871   -602  -3427       N  
ATOM    255  CA  ASP A 270      26.527  16.414  25.174  1.00129.72           C  
ANISOU  255  CA  ASP A 270    12750  13723  22817    896   -591  -3309       C  
ATOM    256  C   ASP A 270      25.400  17.382  24.809  1.00122.27           C  
ANISOU  256  C   ASP A 270    11953  12924  21579    818   -441  -3232       C  
ATOM    257  O   ASP A 270      24.737  17.941  25.693  1.00115.05           O  
ANISOU  257  O   ASP A 270    11159  12049  20507    860   -571  -3086       O  
ATOM    258  CB  ASP A 270      26.236  15.706  26.508  1.00132.95           C  
ANISOU  258  CB  ASP A 270    13245  14032  23238   1030   -890  -3151       C  
ATOM    259  CG  ASP A 270      27.301  16.008  27.570  1.00130.99           C  
ANISOU  259  CG  ASP A 270    12904  13713  23154   1101  -1126  -3155       C  
ATOM    260  OD1 ASP A 270      27.733  17.194  27.647  1.00129.36           O  
ANISOU  260  OD1 ASP A 270    12649  13579  22924   1054  -1093  -3193       O  
ATOM    261  OD2 ASP A 270      27.694  15.070  28.317  1.00132.35           O1-
ANISOU  261  OD2 ASP A 270    13059  13756  23472   1201  -1344  -3119       O1-
ATOM    262  N   PRO A 271      25.181  17.587  23.501  1.00123.32           N  
ANISOU  262  N   PRO A 271    12085  13135  21635    704   -168  -3331       N  
ATOM    263  CA  PRO A 271      24.274  18.646  23.056  1.00124.46           C  
ANISOU  263  CA  PRO A 271    12355  13422  21514    616    -13  -3284       C  
ATOM    264  C   PRO A 271      22.896  18.161  22.599  1.00124.86           C  
ANISOU  264  C   PRO A 271    12572  13509  21361    598     73  -3202       C  
ATOM    265  O   PRO A 271      22.162  18.945  21.997  1.00125.02           O  
ANISOU  265  O   PRO A 271    12691  13644  21168    512    232  -3188       O  
ATOM    266  CB  PRO A 271      25.044  19.242  21.882  1.00124.85           C  
ANISOU  266  CB  PRO A 271    12303  13526  21611    491    231  -3454       C  
ATOM    267  CG  PRO A 271      25.713  18.041  21.263  1.00124.22           C  
ANISOU  267  CG  PRO A 271    12109  13343  21745    496    284  -3577       C  
ATOM    268  CD  PRO A 271      25.992  17.064  22.382  1.00124.44           C  
ANISOU  268  CD  PRO A 271    12094  13241  21948    638     12  -3512       C  
ATOM    269  N   GLU A 272      22.542  16.911  22.881  1.00120.88           N  
ANISOU  269  N   GLU A 272    12105  12905  20918    676    -32  -3150       N  
ATOM    270  CA  GLU A 272      21.259  16.379  22.416  1.00110.73           C  
ANISOU  270  CA  GLU A 272    10976  11640  19457    655     51  -3084       C  
ATOM    271  C   GLU A 272      20.168  16.545  23.478  1.00 98.77           C  
ANISOU  271  C   GLU A 272     9623  10126  17778    721   -113  -2894       C  
ATOM    272  O   GLU A 272      20.112  15.792  24.454  1.00 98.44           O  
ANISOU  272  O   GLU A 272     9613   9978  17811    824   -322  -2797       O  
ATOM    273  CB  GLU A 272      21.406  14.910  22.019  1.00109.48           C  
ANISOU  273  CB  GLU A 272    10781  11370  19445    689     53  -3138       C  
ATOM    274  CG  GLU A 272      22.597  14.634  21.098  1.00111.70           C  
ANISOU  274  CG  GLU A 272    10889  11626  19926    637    192  -3327       C  
ATOM    275  CD  GLU A 272      22.215  14.558  19.628  1.00111.66           C  
ANISOU  275  CD  GLU A 272    10926  11688  19812    520    462  -3425       C  
ATOM    276  OE1 GLU A 272      23.113  14.705  18.770  1.00110.53           O  
ANISOU  276  OE1 GLU A 272    10665  11556  19776    447    620  -3578       O  
ATOM    277  OE2 GLU A 272      21.020  14.343  19.332  1.00112.03           O1-
ANISOU  277  OE2 GLU A 272    11130  11770  19665    498    514  -3351       O1-
ATOM    278  N   VAL A 273      19.293  17.525  23.263  1.00 85.30           N  
ANISOU  278  N   VAL A 273     8031   8536  15843    656    -15  -2843       N  
ATOM    279  CA  VAL A 273      18.312  17.938  24.265  1.00 85.67           C  
ANISOU  279  CA  VAL A 273     8224   8596  15729    704   -152  -2673       C  
ATOM    280  C   VAL A 273      16.902  17.392  23.997  1.00 86.64           C  
ANISOU  280  C   VAL A 273     8520   8712  15686    684   -101  -2592       C  
ATOM    281  O   VAL A 273      16.411  17.442  22.868  1.00 89.10           O  
ANISOU  281  O   VAL A 273     8873   9090  15891    590     97  -2662       O  
ATOM    282  CB  VAL A 273      18.247  19.480  24.345  1.00 86.72           C  
ANISOU  282  CB  VAL A 273     8371   8858  15722    651    -96  -2661       C  
ATOM    283  CG1 VAL A 273      17.375  19.922  25.509  1.00 86.17           C  
ANISOU  283  CG1 VAL A 273     8438   8789  15512    713   -259  -2487       C  
ATOM    284  CG2 VAL A 273      19.649  20.063  24.482  1.00 86.97           C  
ANISOU  284  CG2 VAL A 273     8231   8896  15917    651   -123  -2758       C  
ATOM    285  N   LYS A 274      16.254  16.884  25.046  1.00 87.56           N  
ANISOU  285  N   LYS A 274     8749   8745  15776    766   -283  -2441       N  
ATOM    286  CA  LYS A 274      14.909  16.319  24.926  1.00 89.29           C  
ANISOU  286  CA  LYS A 274     9136   8937  15854    745   -254  -2355       C  
ATOM    287  C   LYS A 274      13.849  17.078  25.734  1.00 92.56           C  
ANISOU  287  C   LYS A 274     9706   9383  16078    748   -326  -2204       C  
ATOM    288  O   LYS A 274      14.028  17.354  26.925  1.00 98.46           O  
ANISOU  288  O   LYS A 274    10479  10092  16840    825   -509  -2094       O  
ATOM    289  CB  LYS A 274      14.918  14.855  25.358  1.00 90.31           C  
ANISOU  289  CB  LYS A 274     9287   8914  16111    821   -382  -2306       C  
ATOM    290  CG  LYS A 274      13.608  14.129  25.114  1.00 93.15           C  
ANISOU  290  CG  LYS A 274     9807   9234  16353    788   -337  -2238       C  
ATOM    291  CD  LYS A 274      13.493  12.894  25.993  1.00 94.80           C  
ANISOU  291  CD  LYS A 274    10079   9285  16655    876   -516  -2130       C  
ATOM    292  CE  LYS A 274      12.213  12.128  25.696  1.00 94.10           C  
ANISOU  292  CE  LYS A 274    10141   9150  16462    830   -459  -2072       C  
ATOM    293  NZ  LYS A 274      12.013  10.970  26.611  1.00 96.53           N1+
ANISOU  293  NZ  LYS A 274    10536   9302  16838    907   -629  -1950       N1+
ATOM    294  N   PHE A 275      12.734  17.397  25.081  1.00 81.20           N  
ANISOU  294  N   PHE A 275     8381   8013  14458    661   -185  -2198       N  
ATOM    295  CA  PHE A 275      11.638  18.107  25.732  1.00 72.97           C  
ANISOU  295  CA  PHE A 275     7491   7002  13232    646   -230  -2065       C  
ATOM    296  C   PHE A 275      10.437  17.205  25.997  1.00 73.14           C  
ANISOU  296  C   PHE A 275     7673   6959  13159    629   -272  -1939       C  
ATOM    297  O   PHE A 275      10.127  16.309  25.208  1.00 70.84           O  
ANISOU  297  O   PHE A 275     7388   6607  12922    602   -184  -2015       O  
ATOM    298  CB  PHE A 275      11.178  19.296  24.884  1.00 67.56           C  
ANISOU  298  CB  PHE A 275     6839   6499  12331    523    -55  -2104       C  
ATOM    299  CG  PHE A 275      12.241  20.319  24.622  1.00 70.41           C  
ANISOU  299  CG  PHE A 275     7064   6939  12752    519      5  -2215       C  
ATOM    300  CD1 PHE A 275      13.080  20.200  23.524  1.00 68.72           C  
ANISOU  300  CD1 PHE A 275     6725   6751  12637    475    155  -2382       C  
ATOM    301  CD2 PHE A 275      12.382  21.420  25.454  1.00 69.58           C  
ANISOU  301  CD2 PHE A 275     6973   6922  12544    525    -84  -2116       C  
ATOM    302  CE1 PHE A 275      14.054  21.150  23.271  1.00 71.71           C  
ANISOU  302  CE1 PHE A 275     6984   7212  13049    447    220  -2468       C  
ATOM    303  CE2 PHE A 275      13.352  22.373  25.207  1.00 69.51           C  
ANISOU  303  CE2 PHE A 275     6836   6980  12594    514    -25  -2221       C  
ATOM    304  CZ  PHE A 275      14.191  22.237  24.113  1.00 71.52           C  
ANISOU  304  CZ  PHE A 275     6956   7236  12981    478    132  -2405       C  
ATOM    305  N   ASN A 276       9.765  17.453  27.116  1.00 73.94           N  
ANISOU  305  N   ASN A 276     7907   7076  13111    637   -401  -1747       N  
ATOM    306  CA  ASN A 276       8.443  16.890  27.367  1.00 73.19           C  
ANISOU  306  CA  ASN A 276     7978   6957  12875    589   -410  -1614       C  
ATOM    307  C   ASN A 276       7.460  17.984  27.775  1.00 75.40           C  
ANISOU  307  C   ASN A 276     8381   7387  12881    510   -392  -1478       C  
ATOM    308  O   ASN A 276       7.688  18.703  28.748  1.00 77.94           O  
ANISOU  308  O   ASN A 276     8730   7747  13135    544   -499  -1378       O  
ATOM    309  CB  ASN A 276       8.509  15.802  28.437  1.00 69.21           C  
ANISOU  309  CB  ASN A 276     7535   6275  12485    684   -588  -1504       C  
ATOM    310  CG  ASN A 276       8.801  14.443  27.850  1.00 74.56           C  
ANISOU  310  CG  ASN A 276     8155   6796  13378    725   -569  -1611       C  
ATOM    311  ND2 ASN A 276      10.067  14.187  27.551  1.00 77.84           N  
ANISOU  311  ND2 ASN A 276     8410   7175  13992    791   -585  -1739       N  
ATOM    312  OD1 ASN A 276       7.893  13.636  27.649  1.00 79.11           O  
ANISOU  312  OD1 ASN A 276     8828   7314  13917    683   -532  -1571       O  
ATOM    313  N   TRP A 277       6.376  18.113  27.015  1.00 68.90           N  
ANISOU  313  N   TRP A 277     7629   6644  11905    406   -262  -1482       N  
ATOM    314  CA  TRP A 277       5.380  19.143  27.282  1.00 66.08           C  
ANISOU  314  CA  TRP A 277     7377   6428  11302    328   -234  -1368       C  
ATOM    315  C   TRP A 277       4.154  18.567  27.969  1.00 74.63           C  
ANISOU  315  C   TRP A 277     8607   7461  12289    302   -281  -1213       C  
ATOM    316  O   TRP A 277       3.721  17.457  27.661  1.00 81.38           O  
ANISOU  316  O   TRP A 277     9489   8213  13221    294   -262  -1229       O  
ATOM    317  CB  TRP A 277       4.963  19.842  25.987  1.00 63.11           C  
ANISOU  317  CB  TRP A 277     6985   6186  10810    226    -66  -1473       C  
ATOM    318  CG  TRP A 277       6.022  20.722  25.414  1.00 68.18           C  
ANISOU  318  CG  TRP A 277     7511   6905  11488    228      0  -1601       C  
ATOM    319  CD1 TRP A 277       7.005  20.354  24.544  1.00 71.71           C  
ANISOU  319  CD1 TRP A 277     7835   7306  12105    248     77  -1775       C  
ATOM    320  CD2 TRP A 277       6.218  22.119  25.673  1.00 72.24           C  
ANISOU  320  CD2 TRP A 277     8022   7553  11874    206      4  -1568       C  
ATOM    321  CE2 TRP A 277       7.336  22.530  24.921  1.00 73.37           C  
ANISOU  321  CE2 TRP A 277     8036   7722  12118    208     87  -1727       C  
ATOM    322  CE3 TRP A 277       5.557  23.063  26.467  1.00 73.11           C  
ANISOU  322  CE3 TRP A 277     8224   7758  11797    181    -48  -1424       C  
ATOM    323  NE1 TRP A 277       7.799  21.436  24.239  1.00 76.22           N  
ANISOU  323  NE1 TRP A 277     8324   7973  12662    233    136  -1854       N  
ATOM    324  CZ2 TRP A 277       7.806  23.841  24.937  1.00 69.25           C  
ANISOU  324  CZ2 TRP A 277     7479   7317  11517    184    116  -1742       C  
ATOM    325  CZ3 TRP A 277       6.027  24.366  26.481  1.00 70.20           C  
ANISOU  325  CZ3 TRP A 277     7820   7504  11347    164    -26  -1441       C  
ATOM    326  CH2 TRP A 277       7.138  24.741  25.721  1.00 66.17           C  
ANISOU  326  CH2 TRP A 277     7184   7016  10941    164     54  -1596       C  
ATOM    327  N   TYR A 278       3.596  19.328  28.905  1.00 76.68           N  
ANISOU  327  N   TYR A 278     8961   7789  12383    286   -333  -1067       N  
ATOM    328  CA  TYR A 278       2.402  18.897  29.622  1.00 77.80           C  
ANISOU  328  CA  TYR A 278     9245   7891  12423    252   -360   -917       C  
ATOM    329  C   TYR A 278       1.382  20.022  29.763  1.00 72.99           C  
ANISOU  329  C   TYR A 278     8710   7432  11592    170   -300   -836       C  
ATOM    330  O   TYR A 278       1.722  21.153  30.117  1.00 70.82           O  
ANISOU  330  O   TYR A 278     8426   7259  11225    177   -320   -812       O  
ATOM    331  CB  TYR A 278       2.772  18.359  31.006  1.00 81.36           C  
ANISOU  331  CB  TYR A 278     9771   8215  12928    337   -518   -789       C  
ATOM    332  CG  TYR A 278       3.836  17.285  30.983  1.00 79.50           C  
ANISOU  332  CG  TYR A 278     9460   7820  12926    433   -604   -861       C  
ATOM    333  CD1 TYR A 278       5.185  17.616  31.048  1.00 78.82           C  
ANISOU  333  CD1 TYR A 278     9256   7726  12965    516   -678   -942       C  
ATOM    334  CD2 TYR A 278       3.494  15.940  30.900  1.00 76.75           C  
ANISOU  334  CD2 TYR A 278     9153   7322  12685    442   -614   -854       C  
ATOM    335  CE1 TYR A 278       6.162  16.639  31.026  1.00 83.28           C  
ANISOU  335  CE1 TYR A 278     9740   8140  13764    610   -762  -1016       C  
ATOM    336  CE2 TYR A 278       4.466  14.957  30.879  1.00 79.24           C  
ANISOU  336  CE2 TYR A 278     9399   7484  13225    535   -697   -923       C  
ATOM    337  CZ  TYR A 278       5.797  15.310  30.942  1.00 81.99           C  
ANISOU  337  CZ  TYR A 278     9623   7827  13701    622   -773  -1005       C  
ATOM    338  OH  TYR A 278       6.765  14.330  30.920  1.00 85.30           O  
ANISOU  338  OH  TYR A 278     9961   8088  14363    721   -860  -1081       O  
ATOM    339  N   VAL A 279       0.125  19.701  29.479  1.00 76.83           N  
ANISOU  339  N   VAL A 279     9265   7925  12003     92   -229   -799       N  
ATOM    340  CA  VAL A 279      -0.972  20.632  29.697  1.00 68.63           C  
ANISOU  340  CA  VAL A 279     8297   7006  10773     18   -179   -715       C  
ATOM    341  C   VAL A 279      -1.852  20.091  30.817  1.00 72.55           C  
ANISOU  341  C   VAL A 279     8920   7423  11223      7   -220   -559       C  
ATOM    342  O   VAL A 279      -2.532  19.076  30.649  1.00 74.69           O  
ANISOU  342  O   VAL A 279     9225   7602  11552    -25   -192   -548       O  
ATOM    343  CB  VAL A 279      -1.805  20.848  28.420  1.00 58.51           C  
ANISOU  343  CB  VAL A 279     6988   5810   9435    -73    -60   -806       C  
ATOM    344  CG1 VAL A 279      -2.906  21.865  28.675  1.00 56.16           C  
ANISOU  344  CG1 VAL A 279     6750   5631   8955   -140    -21   -723       C  
ATOM    345  CG2 VAL A 279      -0.910  21.300  27.272  1.00 52.13           C  
ANISOU  345  CG2 VAL A 279     6076   5066   8666    -70     -6   -965       C  
ATOM    346  N   ASP A 280      -1.819  20.771  31.961  1.00 77.81           N  
ANISOU  346  N   ASP A 280     9660   8118  11785     31   -280   -440       N  
ATOM    347  CA  ASP A 280      -2.500  20.314  33.170  1.00 78.74           C  
ANISOU  347  CA  ASP A 280     9917   8151  11848     25   -320   -285       C  
ATOM    348  C   ASP A 280      -2.127  18.872  33.510  1.00 80.49           C  
ANISOU  348  C   ASP A 280    10176   8186  12219     77   -393   -262       C  
ATOM    349  O   ASP A 280      -2.987  18.066  33.862  1.00 89.11           O  
ANISOU  349  O   ASP A 280    11359   9188  13311     37   -367   -186       O  
ATOM    350  CB  ASP A 280      -4.022  20.449  33.027  1.00 79.36           C  
ANISOU  350  CB  ASP A 280    10047   8282  11824    -77   -210   -239       C  
ATOM    351  CG  ASP A 280      -4.520  21.849  33.353  1.00 80.36           C  
ANISOU  351  CG  ASP A 280    10198   8557  11778   -114   -172   -191       C  
ATOM    352  OD1 ASP A 280      -3.809  22.586  34.071  1.00 82.94           O  
ANISOU  352  OD1 ASP A 280    10549   8921  12043    -62   -241   -148       O  
ATOM    353  OD2 ASP A 280      -5.627  22.209  32.899  1.00 76.98           O1-
ANISOU  353  OD2 ASP A 280     9763   8204  11283   -193    -78   -199       O1-
ATOM    354  N   GLY A 281      -0.842  18.550  33.396  1.00 79.92           N  
ANISOU  354  N   GLY A 281    10030   8051  12283    166   -482   -332       N  
ATOM    355  CA  GLY A 281      -0.344  17.248  33.804  1.00 82.75           C  
ANISOU  355  CA  GLY A 281    10424   8223  12794    233   -577   -309       C  
ATOM    356  C   GLY A 281      -0.365  16.196  32.711  1.00 83.14           C  
ANISOU  356  C   GLY A 281    10393   8196  13002    221   -518   -428       C  
ATOM    357  O   GLY A 281       0.334  15.187  32.805  1.00 86.76           O  
ANISOU  357  O   GLY A 281    10837   8505  13623    293   -599   -453       O  
ATOM    358  N   VAL A 282      -1.166  16.425  31.676  1.00 77.82           N  
ANISOU  358  N   VAL A 282     9671   7616  12282    132   -386   -505       N  
ATOM    359  CA  VAL A 282      -1.272  15.476  30.570  1.00 75.37           C  
ANISOU  359  CA  VAL A 282     9293   7240  12103    109   -323   -626       C  
ATOM    360  C   VAL A 282      -0.291  15.824  29.447  1.00 75.07           C  
ANISOU  360  C   VAL A 282     9109   7265  12148    137   -286   -802       C  
ATOM    361  O   VAL A 282      -0.272  16.949  28.952  1.00 82.17           O  
ANISOU  361  O   VAL A 282     9959   8317  12943    101   -227   -852       O  
ATOM    362  CB  VAL A 282      -2.707  15.427  30.002  1.00 72.18           C  
ANISOU  362  CB  VAL A 282     8923   6887  11613     -5   -208   -623       C  
ATOM    363  CG1 VAL A 282      -2.792  14.417  28.874  1.00 71.51           C  
ANISOU  363  CG1 VAL A 282     8780   6727  11663    -29   -153   -752       C  
ATOM    364  CG2 VAL A 282      -3.707  15.076  31.099  1.00 69.23           C  
ANISOU  364  CG2 VAL A 282     8688   6447  11169    -43   -219   -458       C  
ATOM    365  N   GLU A 283       0.524  14.852  29.047  1.00 68.96           N  
ANISOU  365  N   GLU A 283     8269   6368  11565    198   -316   -897       N  
ATOM    366  CA  GLU A 283       1.545  15.097  28.034  1.00 72.17           C  
ANISOU  366  CA  GLU A 283     8535   6816  12070    226   -271  -1071       C  
ATOM    367  C   GLU A 283       0.934  15.332  26.656  1.00 71.01           C  
ANISOU  367  C   GLU A 283     8353   6766  11861    131   -125  -1192       C  
ATOM    368  O   GLU A 283       0.004  14.637  26.248  1.00 70.29           O  
ANISOU  368  O   GLU A 283     8310   6631  11766     70    -77  -1194       O  
ATOM    369  CB  GLU A 283       2.541  13.935  27.973  1.00 77.34           C  
ANISOU  369  CB  GLU A 283     9125   7301  12961    319   -335  -1149       C  
ATOM    370  CG  GLU A 283       3.712  14.183  27.030  1.00 80.65           C  
ANISOU  370  CG  GLU A 283     9388   7750  13504    355   -283  -1335       C  
ATOM    371  CD  GLU A 283       4.766  13.095  27.095  1.00 92.20           C  
ANISOU  371  CD  GLU A 283    10773   9040  15220    460   -358  -1411       C  
ATOM    372  OE1 GLU A 283       5.530  12.946  26.116  1.00 93.37           O  
ANISOU  372  OE1 GLU A 283    10797   9181  15500    474   -280  -1587       O  
ATOM    373  OE2 GLU A 283       4.834  12.390  28.125  1.00 98.20           O1-
ANISOU  373  OE2 GLU A 283    11600   9663  16047    527   -494  -1296       O1-
ATOM    374  N   VAL A 284       1.461  16.332  25.953  1.00 73.27           N  
ANISOU  374  N   VAL A 284     8562   7180  12098    115    -60  -1293       N  
ATOM    375  CA  VAL A 284       1.064  16.615  24.577  1.00 70.62           C  
ANISOU  375  CA  VAL A 284     8202   6932  11699     30     71  -1421       C  
ATOM    376  C   VAL A 284       2.271  16.463  23.653  1.00 65.53           C  
ANISOU  376  C   VAL A 284     7441   6265  11192     65    131  -1603       C  
ATOM    377  O   VAL A 284       3.416  16.459  24.111  1.00 65.72           O  
ANISOU  377  O   VAL A 284     7386   6242  11343    151     73  -1626       O  
ATOM    378  CB  VAL A 284       0.463  18.026  24.437  1.00 68.28           C  
ANISOU  378  CB  VAL A 284     7939   6813  11190    -40    118  -1380       C  
ATOM    379  CG1 VAL A 284      -0.792  18.149  25.289  1.00 63.73           C  
ANISOU  379  CG1 VAL A 284     7469   6255  10490    -79     77  -1216       C  
ATOM    380  CG2 VAL A 284       1.479  19.080  24.835  1.00 62.51           C  
ANISOU  380  CG2 VAL A 284     7151   6160  10439      9     90  -1382       C  
ATOM    381  N   HIS A 285       2.023  16.340  22.353  1.00 65.74           N  
ANISOU  381  N   HIS A 285     7458   6322  11198     -4    248  -1737       N  
ATOM    382  CA  HIS A 285       3.087  15.952  21.428  1.00 70.01           C  
ANISOU  382  CA  HIS A 285     7900   6813  11886     22    325  -1921       C  
ATOM    383  C   HIS A 285       3.205  16.826  20.177  1.00 67.83           C  
ANISOU  383  C   HIS A 285     7613   6663  11497    -57    464  -2054       C  
ATOM    384  O   HIS A 285       3.895  16.455  19.228  1.00 64.26           O  
ANISOU  384  O   HIS A 285     7102   6171  11144    -60    561  -2220       O  
ATOM    385  CB  HIS A 285       2.885  14.495  21.004  1.00 76.52           C  
ANISOU  385  CB  HIS A 285     8733   7488  12855     29    336  -1988       C  
ATOM    386  CG  HIS A 285       2.795  13.541  22.154  1.00 81.97           C  
ANISOU  386  CG  HIS A 285     9448   8034  13662    102    205  -1864       C  
ATOM    387  CD2 HIS A 285       1.736  13.131  22.892  1.00 80.14           C  
ANISOU  387  CD2 HIS A 285     9319   7762  13370     80    137  -1714       C  
ATOM    388  ND1 HIS A 285       3.896  12.891  22.669  1.00 84.02           N  
ANISOU  388  ND1 HIS A 285     9628   8165  14130    212    129  -1891       N  
ATOM    389  CE1 HIS A 285       3.518  12.122  23.674  1.00 83.57           C  
ANISOU  389  CE1 HIS A 285     9639   7992  14123    254     13  -1755       C  
ATOM    390  NE2 HIS A 285       2.213  12.248  23.830  1.00 80.41           N  
ANISOU  390  NE2 HIS A 285     9351   7643  13560    172     25  -1647       N  
ATOM    391  N   ASN A 286       2.549  17.983  20.178  1.00 68.41           N  
ANISOU  391  N   ASN A 286     7750   6880  11365   -120    478  -1982       N  
ATOM    392  CA  ASN A 286       2.529  18.829  18.985  1.00 68.96           C  
ANISOU  392  CA  ASN A 286     7838   7062  11301   -202    602  -2093       C  
ATOM    393  C   ASN A 286       3.593  19.925  18.981  1.00 69.12           C  
ANISOU  393  C   ASN A 286     7789   7167  11308   -185    645  -2139       C  
ATOM    394  O   ASN A 286       3.596  20.788  18.101  1.00 70.59           O  
ANISOU  394  O   ASN A 286     8005   7454  11364   -257    746  -2212       O  
ATOM    395  CB  ASN A 286       1.148  19.466  18.817  1.00 68.68           C  
ANISOU  395  CB  ASN A 286     7916   7130  11050   -288    595  -2004       C  
ATOM    396  CG  ASN A 286       0.690  20.208  20.060  1.00 69.70           C  
ANISOU  396  CG  ASN A 286     8072   7321  11090   -265    496  -1825       C  
ATOM    397  ND2 ASN A 286       0.187  21.423  19.872  1.00 67.96           N  
ANISOU  397  ND2 ASN A 286     7902   7235  10685   -321    518  -1787       N  
ATOM    398  OD1 ASN A 286       0.788  19.694  21.175  1.00 71.00           O  
ANISOU  398  OD1 ASN A 286     8221   7409  11347   -198    402  -1724       O  
ATOM    399  N   ALA A 287       4.500  19.890  19.952  1.00 64.90           N  
ANISOU  399  N   ALA A 287     7165   6585  10910    -94    566  -2100       N  
ATOM    400  CA  ALA A 287       5.526  20.918  20.035  1.00 63.44           C  
ANISOU  400  CA  ALA A 287     6900   6472  10732    -76    597  -2143       C  
ATOM    401  C   ALA A 287       6.575  20.750  18.950  1.00 72.57           C  
ANISOU  401  C   ALA A 287     7965   7599  12007    -87    738  -2346       C  
ATOM    402  O   ALA A 287       6.972  19.633  18.613  1.00 78.41           O  
ANISOU  402  O   ALA A 287     8652   8230  12911    -53    759  -2433       O  
ATOM    403  CB  ALA A 287       6.180  20.905  21.391  1.00 59.27           C  
ANISOU  403  CB  ALA A 287     6305   5895  10321     26    456  -2046       C  
ATOM    404  N   LYS A 288       7.025  21.874  18.410  1.00 76.98           N  
ANISOU  404  N   LYS A 288     8510   8263  12474   -140    838  -2411       N  
ATOM    405  CA  LYS A 288       8.056  21.859  17.390  1.00 81.81           C  
ANISOU  405  CA  LYS A 288     9041   8894  13149   -169    980  -2560       C  
ATOM    406  C   LYS A 288       9.354  22.451  17.925  1.00 80.34           C  
ANISOU  406  C   LYS A 288     8711   8716  13097   -116    969  -2592       C  
ATOM    407  O   LYS A 288       9.399  23.597  18.378  1.00 74.17           O  
ANISOU  407  O   LYS A 288     7939   8004  12238   -123    953  -2556       O  
ATOM    408  CB  LYS A 288       7.575  22.601  16.143  1.00 83.96           C  
ANISOU  408  CB  LYS A 288     9424   9285  13190   -292   1118  -2600       C  
ATOM    409  CG  LYS A 288       6.299  21.993  15.578  1.00 89.34           C  
ANISOU  409  CG  LYS A 288    10241   9957  13746   -344   1113  -2573       C  
ATOM    410  CD  LYS A 288       5.916  22.562  14.226  1.00 93.07           C  
ANISOU  410  CD  LYS A 288    10828  10533  14002   -456   1235  -2617       C  
ATOM    411  CE  LYS A 288       4.751  21.772  13.641  1.00 94.66           C  
ANISOU  411  CE  LYS A 288    11143  10707  14116   -496   1214  -2603       C  
ATOM    412  NZ  LYS A 288       4.304  22.269  12.310  1.00 96.85           N1+
ANISOU  412  NZ  LYS A 288    11550  11073  14175   -599   1307  -2638       N1+
ATOM    413  N   THR A 289      10.404  21.637  17.889  1.00 82.22           N  
ANISOU  413  N   THR A 289     8814   8879  13545    -62    969  -2663       N  
ATOM    414  CA  THR A 289      11.713  22.030  18.383  1.00 81.47           C  
ANISOU  414  CA  THR A 289     8562   8778  13616    -10    943  -2703       C  
ATOM    415  C   THR A 289      12.562  22.580  17.245  1.00 83.76           C  
ANISOU  415  C   THR A 289     8797   9146  13882   -104   1124  -2824       C  
ATOM    416  O   THR A 289      12.674  21.963  16.185  1.00 86.37           O  
ANISOU  416  O   THR A 289     9138   9468  14211   -160   1241  -2907       O  
ATOM    417  CB  THR A 289      12.442  20.844  19.049  1.00 80.29           C  
ANISOU  417  CB  THR A 289     8289   8494  13725    100    821  -2709       C  
ATOM    418  CG2 THR A 289      13.890  21.196  19.341  1.00 79.99           C  
ANISOU  418  CG2 THR A 289     8075   8449  13867    136    804  -2776       C  
ATOM    419  OG1 THR A 289      11.788  20.507  20.278  1.00 78.63           O  
ANISOU  419  OG1 THR A 289     8135   8206  13537    190    637  -2577       O  
ATOM    420  N   LYS A 290      13.147  23.751  17.460  1.00 79.53           N  
ANISOU  420  N   LYS A 290     8213   8682  13325   -125   1148  -2833       N  
ATOM    421  CA  LYS A 290      14.002  24.352  16.451  1.00 82.68           C  
ANISOU  421  CA  LYS A 290     8564   9144  13705   -223   1319  -2940       C  
ATOM    422  C   LYS A 290      15.359  23.658  16.409  1.00 93.75           C  
ANISOU  422  C   LYS A 290     9783  10463  15374   -188   1328  -3043       C  
ATOM    423  O   LYS A 290      15.844  23.181  17.437  1.00 93.61           O  
ANISOU  423  O   LYS A 290     9653  10363  15552    -79   1173  -3019       O  
ATOM    424  CB  LYS A 290      14.173  25.847  16.717  1.00 75.37           C  
ANISOU  424  CB  LYS A 290     7651   8316  12672   -264   1340  -2913       C  
ATOM    425  CG  LYS A 290      13.309  26.705  15.815  1.00 74.88           C  
ANISOU  425  CG  LYS A 290     7764   8362  12323   -379   1461  -2889       C  
ATOM    426  CD  LYS A 290      13.356  28.167  16.196  1.00 77.69           C  
ANISOU  426  CD  LYS A 290     8146   8808  12563   -411   1463  -2846       C  
ATOM    427  CE  LYS A 290      12.491  28.980  15.251  1.00 77.41           C  
ANISOU  427  CE  LYS A 290     8297   8875  12240   -527   1570  -2815       C  
ATOM    428  NZ  LYS A 290      12.507  30.427  15.585  1.00 81.21           N1+
ANISOU  428  NZ  LYS A 290     8815   9444  12599   -562   1574  -2769       N1+
ATOM    429  N   PRO A 291      15.966  23.579  15.211  1.00 98.30           N  
ANISOU  429  N   PRO A 291    10337  11055  15958   -282   1505  -3158       N  
ATOM    430  CA  PRO A 291      17.340  23.078  15.130  1.00 93.94           C  
ANISOU  430  CA  PRO A 291     9603  10427  15664   -265   1529  -3270       C  
ATOM    431  C   PRO A 291      18.265  23.964  15.948  1.00 90.85           C  
ANISOU  431  C   PRO A 291     9086  10042  15389   -238   1459  -3275       C  
ATOM    432  O   PRO A 291      18.328  25.177  15.743  1.00 88.69           O  
ANISOU  432  O   PRO A 291     8856   9856  14987   -313   1536  -3271       O  
ATOM    433  CB  PRO A 291      17.664  23.148  13.632  1.00 93.44           C  
ANISOU  433  CB  PRO A 291     9579  10398  15527   -396   1756  -3381       C  
ATOM    434  CG  PRO A 291      16.696  24.127  13.074  1.00 97.27           C  
ANISOU  434  CG  PRO A 291    10252  10995  15709   -487   1838  -3317       C  
ATOM    435  CD  PRO A 291      15.449  23.982  13.893  1.00 99.18           C  
ANISOU  435  CD  PRO A 291    10595  11247  15842   -410   1683  -3187       C  
ATOM    436  N   ARG A 292      18.936  23.333  16.901  1.00 92.84           N  
ANISOU  436  N   ARG A 292     9196  10197  15880   -127   1298  -3276       N  
ATOM    437  CA  ARG A 292      19.863  23.970  17.825  1.00 98.10           C  
ANISOU  437  CA  ARG A 292     9734  10846  16694    -78   1185  -3279       C  
ATOM    438  C   ARG A 292      20.814  24.968  17.146  1.00 95.63           C  
ANISOU  438  C   ARG A 292     9360  10582  16392   -190   1345  -3386       C  
ATOM    439  O   ARG A 292      21.388  24.671  16.097  1.00 94.84           O  
ANISOU  439  O   ARG A 292     9223  10463  16348   -273   1511  -3503       O  
ATOM    440  CB  ARG A 292      20.634  22.861  18.538  1.00105.68           C  
ANISOU  440  CB  ARG A 292    10546  11673  17933     36   1025  -3305       C  
ATOM    441  CG  ARG A 292      21.916  23.263  19.177  1.00112.23           C  
ANISOU  441  CG  ARG A 292    11212  12458  18971     69    936  -3361       C  
ATOM    442  CD  ARG A 292      22.662  22.036  19.676  1.00118.78           C  
ANISOU  442  CD  ARG A 292    11908  13150  20073    170    792  -3399       C  
ATOM    443  NE  ARG A 292      23.257  21.273  18.583  1.00120.47           N  
ANISOU  443  NE  ARG A 292    12048  13317  20408    109    952  -3540       N  
ATOM    444  CZ  ARG A 292      23.042  19.978  18.379  1.00119.80           C  
ANISOU  444  CZ  ARG A 292    11961  13155  20404    156    931  -3551       C  
ATOM    445  NH1 ARG A 292      22.246  19.302  19.197  1.00123.17           N1+
ANISOU  445  NH1 ARG A 292    12461  13537  20800    260    755  -3425       N1+
ATOM    446  NH2 ARG A 292      23.624  19.356  17.362  1.00115.85           N  
ANISOU  446  NH2 ARG A 292    11389  12614  20013     96   1087  -3686       N  
ATOM    447  N   GLU A 293      20.960  26.155  17.735  1.00 97.02           N  
ANISOU  447  N   GLU A 293     9536  10816  16512   -196   1299  -3344       N  
ATOM    448  CA  GLU A 293      21.747  27.228  17.119  1.00103.53           C  
ANISOU  448  CA  GLU A 293    10330  11687  17318   -310   1452  -3432       C  
ATOM    449  C   GLU A 293      22.953  27.644  17.960  1.00105.19           C  
ANISOU  449  C   GLU A 293    10378  11843  17748   -261   1340  -3479       C  
ATOM    450  O   GLU A 293      22.868  27.728  19.187  1.00103.09           O  
ANISOU  450  O   GLU A 293    10080  11558  17533   -151   1133  -3393       O  
ATOM    451  CB  GLU A 293      20.864  28.452  16.849  1.00 99.00           C  
ANISOU  451  CB  GLU A 293     9923  11240  16453   -389   1533  -3354       C  
ATOM    452  CG  GLU A 293      20.272  29.102  18.093  1.00 97.42           C  
ANISOU  452  CG  GLU A 293     9758  11083  16176   -303   1356  -3225       C  
ATOM    453  CD  GLU A 293      19.358  30.265  17.763  1.00101.03           C  
ANISOU  453  CD  GLU A 293    10382  11663  16344   -384   1442  -3153       C  
ATOM    454  OE1 GLU A 293      19.560  31.367  18.321  1.00 98.79           O  
ANISOU  454  OE1 GLU A 293    10090  11428  16020   -388   1403  -3122       O  
ATOM    455  OE2 GLU A 293      18.443  30.085  16.932  1.00105.68           O1-
ANISOU  455  OE2 GLU A 293    11116  12297  16743   -445   1545  -3129       O1-
ATOM    456  N   GLU A 294      24.073  27.909  17.293  1.00107.47           N  
ANISOU  456  N   GLU A 294    10571  12100  18162   -345   1476  -3616       N  
ATOM    457  CA  GLU A 294      25.300  28.316  17.979  1.00107.43           C  
ANISOU  457  CA  GLU A 294    10409  12032  18377   -310   1385  -3682       C  
ATOM    458  C   GLU A 294      25.179  29.687  18.626  1.00103.63           C  
ANISOU  458  C   GLU A 294     9975  11626  17772   -315   1331  -3612       C  
ATOM    459  O   GLU A 294      24.524  30.588  18.097  1.00103.22           O  
ANISOU  459  O   GLU A 294    10061  11676  17480   -405   1457  -3570       O  
ATOM    460  CB  GLU A 294      26.484  28.326  17.011  1.00110.77           C  
ANISOU  460  CB  GLU A 294    10730  12401  18957   -412   1571  -3855       C  
ATOM    461  CG  GLU A 294      27.134  26.978  16.803  1.00116.37           C  
ANISOU  461  CG  GLU A 294    11305  12994  19914   -369   1556  -3953       C  
ATOM    462  CD  GLU A 294      28.570  27.097  16.338  1.00122.43           C  
ANISOU  462  CD  GLU A 294    11918  13682  20917   -432   1666  -4127       C  
ATOM    463  OE1 GLU A 294      29.071  28.239  16.263  1.00126.53           O  
ANISOU  463  OE1 GLU A 294    12435  14230  21410   -503   1740  -4166       O  
ATOM    464  OE2 GLU A 294      29.196  26.055  16.053  1.00123.22           O1-
ANISOU  464  OE2 GLU A 294    11900  13685  21232   -412   1681  -4227       O1-
ATOM    465  N   GLN A 295      25.830  29.849  19.770  1.00105.51           N  
ANISOU  465  N   GLN A 295    10102  11811  18174   -217   1136  -3599       N  
ATOM    466  CA  GLN A 295      25.744  31.107  20.492  1.00110.37           C  
ANISOU  466  CA  GLN A 295    10756  12494  18686   -209   1064  -3529       C  
ATOM    467  C   GLN A 295      27.045  31.885  20.530  1.00125.93           C  
ANISOU  467  C   GLN A 295    12609  14426  20814   -248   1098  -3643       C  
ATOM    468  O   GLN A 295      28.081  31.446  20.019  1.00128.33           O  
ANISOU  468  O   GLN A 295    12791  14643  21328   -282   1177  -3784       O  
ATOM    469  CB  GLN A 295      25.264  30.861  21.923  1.00105.48           C  
ANISOU  469  CB  GLN A 295    10139  11862  18077    -60    790  -3391       C  
ATOM    470  CG  GLN A 295      23.960  31.558  22.235  1.00102.47           C  
ANISOU  470  CG  GLN A 295     9918  11596  17419    -59    771  -3245       C  
ATOM    471  CD  GLN A 295      22.899  31.275  21.190  1.00 98.55           C  
ANISOU  471  CD  GLN A 295     9560  11164  16722   -137    946  -3226       C  
ATOM    472  NE2 GLN A 295      22.106  32.287  20.866  1.00 92.50           N  
ANISOU  472  NE2 GLN A 295     8928  10511  15706   -211   1047  -3168       N  
ATOM    473  OE1 GLN A 295      22.798  30.161  20.674  1.00102.43           O  
ANISOU  473  OE1 GLN A 295    10040  11600  17279   -131    985  -3263       O  
ATOM    474  N   TYR A 296      26.943  33.068  21.123  1.00135.17           N  
ANISOU  474  N   TYR A 296    13822  15662  21876   -246   1046  -3580       N  
ATOM    475  CA  TYR A 296      28.061  33.939  21.455  1.00144.62           C  
ANISOU  475  CA  TYR A 296    14917  16827  23204   -258   1031  -3658       C  
ATOM    476  C   TYR A 296      29.200  33.166  22.125  1.00142.24           C  
ANISOU  476  C   TYR A 296    14431  16390  23222   -162    865  -3737       C  
ATOM    477  O   TYR A 296      30.367  33.271  21.732  1.00136.66           O  
ANISOU  477  O   TYR A 296    13602  15611  22712   -208    950  -3884       O  
ATOM    478  CB  TYR A 296      27.538  35.061  22.366  1.00152.06           C  
ANISOU  478  CB  TYR A 296    15936  17860  23980   -221    915  -3532       C  
ATOM    479  CG  TYR A 296      28.452  35.425  23.501  1.00158.98           C  
ANISOU  479  CG  TYR A 296    16691  18679  25034   -133    717  -3540       C  
ATOM    480  CD1 TYR A 296      29.433  36.392  23.336  1.00159.28           C  
ANISOU  480  CD1 TYR A 296    16661  18705  25151   -193    800  -3640       C  
ATOM    481  CD2 TYR A 296      28.325  34.814  24.747  1.00162.96           C  
ANISOU  481  CD2 TYR A 296    17160  19136  25621     10    442  -3445       C  
ATOM    482  CE1 TYR A 296      30.269  36.725  24.369  1.00161.18           C  
ANISOU  482  CE1 TYR A 296    16792  18892  25555   -112    614  -3650       C  
ATOM    483  CE2 TYR A 296      29.158  35.137  25.781  1.00164.71           C  
ANISOU  483  CE2 TYR A 296    17286  19302  25995     87    248  -3448       C  
ATOM    484  CZ  TYR A 296      30.124  36.095  25.595  1.00163.83           C  
ANISOU  484  CZ  TYR A 296    17099  19183  25965     28    333  -3552       C  
ATOM    485  OH  TYR A 296      30.940  36.403  26.658  1.00165.44           O  
ANISOU  485  OH  TYR A 296    17209  19329  26322    109    127  -3554       O  
ATOM    486  N   ASN A 297      28.828  32.372  23.124  1.00142.45           N  
ANISOU  486  N   ASN A 297    14446  16379  23298    -30    628  -3636       N  
ATOM    487  CA  ASN A 297      29.731  31.482  23.836  1.00143.06           C  
ANISOU  487  CA  ASN A 297    14375  16325  23659     74    434  -3684       C  
ATOM    488  C   ASN A 297      30.208  30.383  22.869  1.00133.52           C  
ANISOU  488  C   ASN A 297    13080  15033  22617     33    567  -3815       C  
ATOM    489  O   ASN A 297      29.922  30.440  21.676  1.00137.21           O  
ANISOU  489  O   ASN A 297    13606  15549  22978    -82    809  -3871       O  
ATOM    490  CB  ASN A 297      29.003  30.916  25.083  1.00152.29           C  
ANISOU  490  CB  ASN A 297    15600  17482  24783    214    157  -3519       C  
ATOM    491  CG  ASN A 297      29.168  31.811  26.328  1.00148.47           C  
ANISOU  491  CG  ASN A 297    15123  17016  24272    284    -49  -3432       C  
ATOM    492  ND2 ASN A 297      28.060  32.222  27.012  1.00139.52           N  
ANISOU  492  ND2 ASN A 297    14128  15970  22912    325   -152  -3264       N  
ATOM    493  OD1 ASN A 297      30.312  32.140  26.669  1.00154.03           O  
ANISOU  493  OD1 ASN A 297    15706  17653  25165    299   -115  -3521       O  
ATOM    494  N   SER A 298      30.955  29.395  23.339  1.00124.51           N  
ANISOU  494  N   SER A 298    11806  13767  21734    120    413  -3867       N  
ATOM    495  CA  SER A 298      31.120  28.212  22.504  1.00114.24           C  
ANISOU  495  CA  SER A 298    10449  12401  20556     95    518  -3958       C  
ATOM    496  C   SER A 298      30.021  27.270  22.947  1.00115.58           C  
ANISOU  496  C   SER A 298    10718  12580  20619    184    382  -3814       C  
ATOM    497  O   SER A 298      30.273  26.152  23.392  1.00116.40           O  
ANISOU  497  O   SER A 298    10751  12582  20893    277    227  -3813       O  
ATOM    498  CB  SER A 298      32.511  27.593  22.634  1.00103.37           C  
ANISOU  498  CB  SER A 298     8872  10881  19525    132    450  -4105       C  
ATOM    499  OG  SER A 298      33.353  28.051  21.587  1.00100.09           O  
ANISOU  499  OG  SER A 298     8376  10451  19202      8    694  -4275       O  
ATOM    500  N   THR A 299      28.790  27.762  22.835  1.00113.95           N  
ANISOU  500  N   THR A 299    10678  12490  20126    155    440  -3692       N  
ATOM    501  CA  THR A 299      27.620  27.132  23.432  1.00110.13           C  
ANISOU  501  CA  THR A 299    10312  12027  19507    243    298  -3533       C  
ATOM    502  C   THR A 299      26.469  27.180  22.434  1.00103.40           C  
ANISOU  502  C   THR A 299     9605  11276  18408    155    505  -3497       C  
ATOM    503  O   THR A 299      26.462  27.997  21.511  1.00 97.10           O  
ANISOU  503  O   THR A 299     8848  10554  17491     32    723  -3558       O  
ATOM    504  CB  THR A 299      27.217  27.841  24.765  1.00105.21           C  
ANISOU  504  CB  THR A 299     9755  11440  18780    330     75  -3384       C  
ATOM    505  CG2 THR A 299      26.100  27.104  25.492  1.00 98.62           C  
ANISOU  505  CG2 THR A 299     9036  10600  17835    429    -92  -3220       C  
ATOM    506  OG1 THR A 299      28.355  27.919  25.636  1.00110.92           O  
ANISOU  506  OG1 THR A 299    10351  12072  19721    399   -113  -3426       O  
ATOM    507  N   TYR A 300      25.510  26.283  22.609  1.00113.36           N  
ANISOU  507  N   TYR A 300    10951  12528  19593    217    434  -3399       N  
ATOM    508  CA  TYR A 300      24.324  26.243  21.773  1.00116.93           C  
ANISOU  508  CA  TYR A 300    11552  13067  19811    149    599  -3354       C  
ATOM    509  C   TYR A 300      23.100  26.744  22.531  1.00110.25           C  
ANISOU  509  C   TYR A 300    10852  12297  18742    198    493  -3186       C  
ATOM    510  O   TYR A 300      23.054  26.688  23.763  1.00108.75           O  
ANISOU  510  O   TYR A 300    10657  12068  18596    309    263  -3087       O  
ATOM    511  CB  TYR A 300      24.071  24.821  21.289  1.00127.69           C  
ANISOU  511  CB  TYR A 300    12912  14359  21247    174    622  -3378       C  
ATOM    512  CG  TYR A 300      25.073  24.277  20.291  1.00140.64           C  
ANISOU  512  CG  TYR A 300    14429  15938  23070    107    777  -3549       C  
ATOM    513  CD1 TYR A 300      25.013  24.638  18.948  1.00145.52           C  
ANISOU  513  CD1 TYR A 300    15095  16620  23576    -33   1042  -3636       C  
ATOM    514  CD2 TYR A 300      26.054  23.370  20.681  1.00148.31           C  
ANISOU  514  CD2 TYR A 300    15247  16781  24323    182    655  -3619       C  
ATOM    515  CE1 TYR A 300      25.907  24.129  18.029  1.00150.67           C  
ANISOU  515  CE1 TYR A 300    15643  17212  24392    -98   1190  -3791       C  
ATOM    516  CE2 TYR A 300      26.958  22.859  19.765  1.00154.51           C  
ANISOU  516  CE2 TYR A 300    15915  17506  25285    120    803  -3781       C  
ATOM    517  CZ  TYR A 300      26.881  23.246  18.440  1.00154.84           C  
ANISOU  517  CZ  TYR A 300    16006  17616  25212    -21   1075  -3867       C  
ATOM    518  OH  TYR A 300      27.776  22.744  17.520  1.00157.48           O  
ANISOU  518  OH  TYR A 300    16229  17886  25719    -87   1231  -4028       O  
ATOM    519  N   ARG A 301      22.108  27.231  21.793  1.00102.98           N  
ANISOU  519  N   ARG A 301    10070  11480  17579    114    656  -3154       N  
ATOM    520  CA  ARG A 301      20.796  27.516  22.366  1.00 93.57           C  
ANISOU  520  CA  ARG A 301     9025  10351  16177    156    578  -3003       C  
ATOM    521  C   ARG A 301      19.752  26.701  21.618  1.00 84.72           C  
ANISOU  521  C   ARG A 301     8021   9235  14934    130    677  -2982       C  
ATOM    522  O   ARG A 301      19.801  26.590  20.391  1.00 85.14           O  
ANISOU  522  O   ARG A 301     8094   9316  14939     27    877  -3073       O  
ATOM    523  CB  ARG A 301      20.465  29.008  22.291  1.00 92.73           C  
ANISOU  523  CB  ARG A 301     8992  10368  15872     82    662  -2972       C  
ATOM    524  CG  ARG A 301      19.326  29.441  23.203  1.00 95.24           C  
ANISOU  524  CG  ARG A 301     9426  10740  16020    148    536  -2817       C  
ATOM    525  CD  ARG A 301      18.186  30.078  22.419  1.00 97.56           C  
ANISOU  525  CD  ARG A 301     9880  11146  16041     53    705  -2787       C  
ATOM    526  NE  ARG A 301      18.592  31.299  21.728  1.00 94.04           N  
ANISOU  526  NE  ARG A 301     9442  10792  15499    -67    867  -2851       N  
ATOM    527  CZ  ARG A 301      17.751  32.099  21.078  1.00 88.87           C  
ANISOU  527  CZ  ARG A 301     8929  10241  14596   -160   1004  -2824       C  
ATOM    528  NH1 ARG A 301      16.454  31.810  21.030  1.00 78.44           N1+
ANISOU  528  NH1 ARG A 301     7750   8946  13107   -147    999  -2743       N1+
ATOM    529  NH2 ARG A 301      18.205  33.190  20.475  1.00 91.34           N  
ANISOU  529  NH2 ARG A 301     9255  10623  14829   -270   1141  -2877       N  
ATOM    530  N   VAL A 302      18.814  26.118  22.354  1.00 77.45           N  
ANISOU  530  N   VAL A 302     7187   8281  13962    222    533  -2860       N  
ATOM    531  CA  VAL A 302      17.798  25.285  21.727  1.00 76.28           C  
ANISOU  531  CA  VAL A 302     7155   8121  13708    203    608  -2838       C  
ATOM    532  C   VAL A 302      16.397  25.627  22.245  1.00 73.03           C  
ANISOU  532  C   VAL A 302     6909   7752  13086    228    549  -2702       C  
ATOM    533  O   VAL A 302      16.163  25.777  23.451  1.00 71.74           O  
ANISOU  533  O   VAL A 302     6764   7558  12935    322    365  -2592       O  
ATOM    534  CB  VAL A 302      18.115  23.779  21.924  1.00 70.22           C  
ANISOU  534  CB  VAL A 302     6322   7220  13138    284    507  -2853       C  
ATOM    535  CG1 VAL A 302      18.118  23.397  23.402  1.00 65.31           C  
ANISOU  535  CG1 VAL A 302     5689   6510  12615    423    242  -2734       C  
ATOM    536  CG2 VAL A 302      17.155  22.911  21.118  1.00 75.23           C  
ANISOU  536  CG2 VAL A 302     7069   7843  13670    248    607  -2851       C  
ATOM    537  N   VAL A 303      15.468  25.768  21.307  1.00 72.99           N  
ANISOU  537  N   VAL A 303     7037   7815  12882    136    704  -2709       N  
ATOM    538  CA  VAL A 303      14.136  26.280  21.603  1.00 68.87           C  
ANISOU  538  CA  VAL A 303     6681   7344  12142    128    682  -2603       C  
ATOM    539  C   VAL A 303      13.044  25.340  21.097  1.00 73.08           C  
ANISOU  539  C   VAL A 303     7342   7839  12585    106    714  -2577       C  
ATOM    540  O   VAL A 303      13.109  24.850  19.967  1.00 71.14           O  
ANISOU  540  O   VAL A 303     7104   7603  12323     33    852  -2660       O  
ATOM    541  CB  VAL A 303      13.932  27.671  20.964  1.00 60.06           C  
ANISOU  541  CB  VAL A 303     5634   6369  10819     14    828  -2623       C  
ATOM    542  CG1 VAL A 303      12.541  28.193  21.252  1.00 53.82           C  
ANISOU  542  CG1 VAL A 303     5039   5674   9738    -33    769  -2447       C  
ATOM    543  CG2 VAL A 303      14.995  28.651  21.454  1.00 60.52           C  
ANISOU  543  CG2 VAL A 303     5565   6463  10966     28    803  -2654       C  
ATOM    544  N   SER A 304      12.048  25.076  21.936  1.00 76.28           N  
ANISOU  544  N   SER A 304     7867   8243  12873    135    564  -2399       N  
ATOM    545  CA  SER A 304      10.862  24.361  21.476  1.00 78.34           C  
ANISOU  545  CA  SER A 304     8264   8490  13013     94    593  -2354       C  
ATOM    546  C   SER A 304       9.614  25.206  21.710  1.00 71.77           C  
ANISOU  546  C   SER A 304     7595   7777  11898     27    567  -2201       C  
ATOM    547  O   SER A 304       9.461  25.849  22.751  1.00 65.49           O  
ANISOU  547  O   SER A 304     6827   7026  11029     57    446  -2068       O  
ATOM    548  CB  SER A 304      10.724  23.006  22.166  1.00 85.04           C  
ANISOU  548  CB  SER A 304     9103   9196  14011    187    454  -2297       C  
ATOM    549  OG  SER A 304      10.620  23.151  23.578  1.00 90.90           O  
ANISOU  549  OG  SER A 304     9873   9924  14742    260    261  -2133       O  
ATOM    550  N   VAL A 305       8.726  25.199  20.723  1.00 68.19           N  
ANISOU  550  N   VAL A 305     7248   7371  11289    -63    678  -2226       N  
ATOM    551  CA  VAL A 305       7.548  26.052  20.741  1.00 62.82           C  
ANISOU  551  CA  VAL A 305     6712   6806  10352   -134    672  -2108       C  
ATOM    552  C   VAL A 305       6.252  25.243  20.754  1.00 66.44           C  
ANISOU  552  C   VAL A 305     7281   7230  10732   -149    625  -2023       C  
ATOM    553  O   VAL A 305       5.977  24.477  19.829  1.00 62.27           O  
ANISOU  553  O   VAL A 305     6777   6655  10227   -185    704  -2114       O  
ATOM    554  CB  VAL A 305       7.544  26.988  19.526  1.00 61.42           C  
ANISOU  554  CB  VAL A 305     6582   6728  10029   -239    835  -2206       C  
ATOM    555  CG1 VAL A 305       6.357  27.921  19.584  1.00 56.55           C  
ANISOU  555  CG1 VAL A 305     6106   6223   9160   -302    811  -2083       C  
ATOM    556  CG2 VAL A 305       8.843  27.772  19.467  1.00 59.16           C  
ANISOU  556  CG2 VAL A 305     6181   6468   9830   -234    902  -2300       C  
ATOM    557  N   LEU A 306       5.460  25.409  21.807  1.00 62.88           N  
ANISOU  557  N   LEU A 306     6898   6799  10193   -126    501  -1854       N  
ATOM    558  CA  LEU A 306       4.179  24.725  21.897  1.00 56.47           C  
ANISOU  558  CA  LEU A 306     6187   5958   9311   -148    461  -1768       C  
ATOM    559  C   LEU A 306       3.036  25.654  21.515  1.00 59.54           C  
ANISOU  559  C   LEU A 306     6686   6466   9469   -234    498  -1709       C  
ATOM    560  O   LEU A 306       2.746  26.625  22.215  1.00 64.31           O  
ANISOU  560  O   LEU A 306     7326   7151   9957   -236    447  -1603       O  
ATOM    561  CB  LEU A 306       3.954  24.170  23.308  1.00 50.94           C  
ANISOU  561  CB  LEU A 306     5501   5184   8670    -71    312  -1621       C  
ATOM    562  CG  LEU A 306       2.654  23.386  23.518  1.00 51.74           C  
ANISOU  562  CG  LEU A 306     5698   5240   8721    -95    276  -1527       C  
ATOM    563  CD1 LEU A 306       2.701  22.046  22.793  1.00 56.12           C  
ANISOU  563  CD1 LEU A 306     6228   5678   9415    -92    316  -1628       C  
ATOM    564  CD2 LEU A 306       2.359  23.190  24.997  1.00 44.07           C  
ANISOU  564  CD2 LEU A 306     4772   4222   7751    -38    144  -1361       C  
ATOM    565  N   THR A 307       2.396  25.358  20.389  1.00 56.51           N  
ANISOU  565  N   THR A 307     6359   6090   9023   -305    579  -1783       N  
ATOM    566  CA  THR A 307       1.196  26.079  19.992  1.00 49.98           C  
ANISOU  566  CA  THR A 307     5639   5358   7995   -382    592  -1730       C  
ATOM    567  C   THR A 307       0.084  25.763  20.989  1.00 47.50           C  
ANISOU  567  C   THR A 307     5374   5025   7650   -364    488  -1575       C  
ATOM    568  O   THR A 307      -0.156  24.598  21.309  1.00 53.70           O  
ANISOU  568  O   THR A 307     6150   5707   8546   -335    447  -1554       O  
ATOM    569  CB  THR A 307       0.751  25.710  18.561  1.00 49.28           C  
ANISOU  569  CB  THR A 307     5607   5263   7855   -458    683  -1848       C  
ATOM    570  CG2 THR A 307      -0.649  26.218  18.292  1.00 51.69           C  
ANISOU  570  CG2 THR A 307     6018   5640   7982   -524    656  -1778       C  
ATOM    571  OG1 THR A 307       1.649  26.297  17.611  1.00 48.94           O  
ANISOU  571  OG1 THR A 307     5550   5260   7786   -494    798  -1980       O  
ATOM    572  N   VAL A 308      -0.580  26.799  21.495  1.00 42.15           N  
ANISOU  572  N   VAL A 308     4747   4441   6826   -385    453  -1469       N  
ATOM    573  CA  VAL A 308      -1.636  26.609  22.485  1.00 37.99           C  
ANISOU  573  CA  VAL A 308     4267   3901   6265   -375    373  -1325       C  
ATOM    574  C   VAL A 308      -2.982  27.145  22.003  1.00 43.94           C  
ANISOU  574  C   VAL A 308     5095   4728   6870   -448    386  -1293       C  
ATOM    575  O   VAL A 308      -3.048  27.995  21.113  1.00 46.94           O  
ANISOU  575  O   VAL A 308     5504   5190   7140   -498    435  -1354       O  
ATOM    576  CB  VAL A 308      -1.275  27.281  23.818  1.00 41.23           C  
ANISOU  576  CB  VAL A 308     4669   4340   6655   -319    302  -1209       C  
ATOM    577  CG1 VAL A 308       0.106  26.842  24.267  1.00 44.03           C  
ANISOU  577  CG1 VAL A 308     4944   4623   7163   -243    271  -1247       C  
ATOM    578  CG2 VAL A 308      -1.321  28.786  23.680  1.00 40.79           C  
ANISOU  578  CG2 VAL A 308     4639   4413   6448   -353    327  -1195       C  
ATOM    579  N   LEU A 309      -4.055  26.622  22.587  1.00 48.68           N  
ANISOU  579  N   LEU A 309     5727   5292   7477   -455    341  -1201       N  
ATOM    580  CA  LEU A 309      -5.397  27.103  22.293  1.00 45.58           C  
ANISOU  580  CA  LEU A 309     5388   4959   6970   -517    338  -1163       C  
ATOM    581  C   LEU A 309      -5.662  28.354  23.115  1.00 39.46           C  
ANISOU  581  C   LEU A 309     4636   4277   6081   -508    312  -1060       C  
ATOM    582  O   LEU A 309      -5.366  28.380  24.312  1.00 38.07           O  
ANISOU  582  O   LEU A 309     4453   4082   5931   -458    274   -967       O  
ATOM    583  CB  LEU A 309      -6.439  26.024  22.594  1.00 41.34           C  
ANISOU  583  CB  LEU A 309     4863   4339   6504   -534    313  -1115       C  
ATOM    584  CG  LEU A 309      -6.274  24.716  21.817  1.00 47.26           C  
ANISOU  584  CG  LEU A 309     5596   4988   7373   -545    334  -1215       C  
ATOM    585  CD1 LEU A 309      -7.265  23.674  22.307  1.00 48.29           C  
ANISOU  585  CD1 LEU A 309     5738   5028   7583   -560    307  -1152       C  
ATOM    586  CD2 LEU A 309      -6.434  24.960  20.322  1.00 41.14           C  
ANISOU  586  CD2 LEU A 309     4844   4256   6531   -605    378  -1343       C  
ATOM    587  N   HIS A 310      -6.193  29.387  22.462  1.00 37.44           N  
ANISOU  587  N   HIS A 310     4414   4114   5696   -555    327  -1079       N  
ATOM    588  CA  HIS A 310      -6.561  30.636  23.127  1.00 40.24           C  
ANISOU  588  CA  HIS A 310     4793   4557   5938   -552    306   -990       C  
ATOM    589  C   HIS A 310      -7.347  30.362  24.398  1.00 42.56           C  
ANISOU  589  C   HIS A 310     5095   4821   6256   -533    269   -864       C  
ATOM    590  O   HIS A 310      -7.020  30.862  25.473  1.00 41.54           O  
ANISOU  590  O   HIS A 310     4972   4710   6100   -493    247   -780       O  
ATOM    591  CB  HIS A 310      -7.404  31.527  22.208  1.00 43.00           C  
ANISOU  591  CB  HIS A 310     5187   4986   6164   -610    312  -1022       C  
ATOM    592  CG  HIS A 310      -6.762  31.845  20.893  1.00 43.67           C  
ANISOU  592  CG  HIS A 310     5296   5099   6198   -644    355  -1143       C  
ATOM    593  CD2 HIS A 310      -6.396  33.030  20.347  1.00 38.53           C  
ANISOU  593  CD2 HIS A 310     4685   4527   5429   -665    379  -1175       C  
ATOM    594  ND1 HIS A 310      -6.463  30.882  19.952  1.00 43.57           N  
ANISOU  594  ND1 HIS A 310     5281   5024   6250   -665    389  -1249       N  
ATOM    595  CE1 HIS A 310      -5.926  31.458  18.891  1.00 40.51           C  
ANISOU  595  CE1 HIS A 310     4933   4676   5781   -700    438  -1343       C  
ATOM    596  NE2 HIS A 310      -5.872  32.761  19.106  1.00 42.65           N  
ANISOU  596  NE2 HIS A 310     5233   5033   5941   -702    432  -1298       N  
ATOM    597  N   GLN A 311      -8.386  29.546  24.253  1.00 43.91           N  
ANISOU  597  N   GLN A 311     5269   4939   6477   -566    266   -856       N  
ATOM    598  CA  GLN A 311      -9.298  29.244  25.349  1.00 45.98           C  
ANISOU  598  CA  GLN A 311     5542   5165   6762   -565    252   -744       C  
ATOM    599  C   GLN A 311      -8.594  28.541  26.500  1.00 47.59           C  
ANISOU  599  C   GLN A 311     5753   5289   7041   -509    234   -673       C  
ATOM    600  O   GLN A 311      -8.947  28.741  27.659  1.00 43.74           O  
ANISOU  600  O   GLN A 311     5298   4796   6525   -495    225   -565       O  
ATOM    601  CB  GLN A 311     -10.469  28.389  24.857  1.00 46.25           C  
ANISOU  601  CB  GLN A 311     5568   5145   6859   -618    259   -767       C  
ATOM    602  CG  GLN A 311     -10.074  27.084  24.188  1.00 50.18           C  
ANISOU  602  CG  GLN A 311     6048   5548   7471   -622    265   -849       C  
ATOM    603  CD  GLN A 311     -10.033  27.189  22.675  1.00 51.62           C  
ANISOU  603  CD  GLN A 311     6230   5762   7623   -661    273   -979       C  
ATOM    604  NE2 GLN A 311     -10.498  26.145  21.997  1.00 46.94           N  
ANISOU  604  NE2 GLN A 311     5630   5095   7111   -697    274  -1044       N  
ATOM    605  OE1 GLN A 311      -9.596  28.199  22.122  1.00 53.11           O  
ANISOU  605  OE1 GLN A 311     6435   6035   7712   -664    279  -1021       O  
ATOM    606  N   ASP A 312      -7.595  27.726  26.186  1.00 46.48           N  
ANISOU  606  N   ASP A 312     5586   5080   6993   -477    228   -736       N  
ATOM    607  CA  ASP A 312      -6.888  26.987  27.222  1.00 43.21           C  
ANISOU  607  CA  ASP A 312     5180   4574   6662   -418    191   -673       C  
ATOM    608  C   ASP A 312      -6.056  27.905  28.110  1.00 43.38           C  
ANISOU  608  C   ASP A 312     5215   4645   6622   -366    154   -615       C  
ATOM    609  O   ASP A 312      -6.080  27.771  29.335  1.00 44.07           O  
ANISOU  609  O   ASP A 312     5350   4691   6704   -334    117   -508       O  
ATOM    610  CB  ASP A 312      -6.001  25.914  26.604  1.00 45.27           C  
ANISOU  610  CB  ASP A 312     5399   4745   7055   -391    188   -768       C  
ATOM    611  CG  ASP A 312      -6.786  24.701  26.157  1.00 50.34           C  
ANISOU  611  CG  ASP A 312     6044   5297   7785   -430    207   -794       C  
ATOM    612  OD1 ASP A 312      -7.947  24.541  26.599  1.00 52.85           O  
ANISOU  612  OD1 ASP A 312     6396   5602   8081   -469    214   -719       O  
ATOM    613  OD2 ASP A 312      -6.236  23.904  25.366  1.00 50.12           O1-
ANISOU  613  OD2 ASP A 312     5981   5208   7853   -423    219   -896       O1-
ATOM    614  N   TRP A 313      -5.321  28.831  27.495  1.00 42.87           N  
ANISOU  614  N   TRP A 313     5117   4664   6507   -361    166   -687       N  
ATOM    615  CA  TRP A 313      -4.543  29.800  28.254  1.00 35.19           C  
ANISOU  615  CA  TRP A 313     4150   3745   5476   -318    131   -644       C  
ATOM    616  C   TRP A 313      -5.460  30.644  29.120  1.00 36.05           C  
ANISOU  616  C   TRP A 313     4320   3913   5463   -335    127   -533       C  
ATOM    617  O   TRP A 313      -5.229  30.812  30.317  1.00 39.02           O  
ANISOU  617  O   TRP A 313     4739   4272   5815   -296     82   -441       O  
ATOM    618  CB  TRP A 313      -3.729  30.711  27.329  1.00 39.88           C  
ANISOU  618  CB  TRP A 313     4699   4421   6033   -328    163   -747       C  
ATOM    619  CG  TRP A 313      -2.948  31.738  28.097  1.00 39.93           C  
ANISOU  619  CG  TRP A 313     4706   4481   5986   -289    126   -707       C  
ATOM    620  CD1 TRP A 313      -3.295  33.038  28.320  1.00 32.80           C  
ANISOU  620  CD1 TRP A 313     3837   3677   4950   -310    133   -665       C  
ATOM    621  CD2 TRP A 313      -1.705  31.532  28.778  1.00 39.64           C  
ANISOU  621  CD2 TRP A 313     4631   4394   6035   -222     65   -706       C  
ATOM    622  CE2 TRP A 313      -1.353  32.754  29.386  1.00 43.37           C  
ANISOU  622  CE2 TRP A 313     5119   4942   6416   -209     39   -665       C  
ATOM    623  CE3 TRP A 313      -0.853  30.435  28.927  1.00 41.76           C  
ANISOU  623  CE3 TRP A 313     4852   4556   6457   -168     24   -740       C  
ATOM    624  NE1 TRP A 313      -2.340  33.658  29.094  1.00 38.48           N  
ANISOU  624  NE1 TRP A 313     4547   4413   5662   -264     85   -639       N  
ATOM    625  CZ2 TRP A 313      -0.186  32.908  30.128  1.00 40.99           C  
ANISOU  625  CZ2 TRP A 313     4786   4615   6172   -148    -34   -658       C  
ATOM    626  CZ3 TRP A 313       0.304  30.589  29.665  1.00 48.44           C  
ANISOU  626  CZ3 TRP A 313     5663   5374   7367   -102    -52   -733       C  
ATOM    627  CH2 TRP A 313       0.627  31.816  30.256  1.00 45.04           C  
ANISOU  627  CH2 TRP A 313     5248   5024   6843    -94    -82   -693       C  
ATOM    628  N   LEU A 314      -6.506  31.175  28.499  1.00 42.24           N  
ANISOU  628  N   LEU A 314     5113   4763   6173   -393    171   -548       N  
ATOM    629  CA  LEU A 314      -7.439  32.061  29.182  1.00 44.03           C  
ANISOU  629  CA  LEU A 314     5384   5050   6294   -412    179   -461       C  
ATOM    630  C   LEU A 314      -8.220  31.347  30.286  1.00 53.23           C  
ANISOU  630  C   LEU A 314     6597   6142   7485   -412    179   -355       C  
ATOM    631  O   LEU A 314      -8.641  31.979  31.255  1.00 54.50           O  
ANISOU  631  O   LEU A 314     6808   6332   7568   -409    183   -268       O  
ATOM    632  CB  LEU A 314      -8.403  32.686  28.171  1.00 34.59           C  
ANISOU  632  CB  LEU A 314     4177   3928   5038   -470    214   -511       C  
ATOM    633  CG  LEU A 314      -7.741  33.628  27.163  1.00 32.08           C  
ANISOU  633  CG  LEU A 314     3842   3689   4656   -479    222   -599       C  
ATOM    634  CD1 LEU A 314      -8.705  34.009  26.054  1.00 32.08           C  
ANISOU  634  CD1 LEU A 314     3846   3736   4606   -535    239   -654       C  
ATOM    635  CD2 LEU A 314      -7.220  34.869  27.866  1.00 23.57           C  
ANISOU  635  CD2 LEU A 314     2787   2683   3488   -451    207   -552       C  
ATOM    636  N   ASN A 315      -8.407  30.037  30.147  1.00 57.17           N  
ANISOU  636  N   ASN A 315     7089   6541   8091   -420    183   -365       N  
ATOM    637  CA  ASN A 315      -9.150  29.275  31.152  1.00 58.07           C  
ANISOU  637  CA  ASN A 315     7257   6572   8233   -430    195   -267       C  
ATOM    638  C   ASN A 315      -8.260  28.756  32.278  1.00 59.10           C  
ANISOU  638  C   ASN A 315     7447   6620   8389   -370    140   -192       C  
ATOM    639  O   ASN A 315      -8.720  28.013  33.145  1.00 65.06           O  
ANISOU  639  O   ASN A 315     8268   7286   9165   -376    146   -107       O  
ATOM    640  CB  ASN A 315      -9.897  28.105  30.505  1.00 49.98           C  
ANISOU  640  CB  ASN A 315     6206   5470   7313   -475    226   -307       C  
ATOM    641  CG  ASN A 315     -11.142  28.549  29.758  1.00 43.14           C  
ANISOU  641  CG  ASN A 315     5302   4666   6421   -541    270   -346       C  
ATOM    642  ND2 ASN A 315     -11.447  27.865  28.660  1.00 38.31           N  
ANISOU  642  ND2 ASN A 315     4646   4026   5886   -576    276   -435       N  
ATOM    643  OD1 ASN A 315     -11.825  29.490  30.163  1.00 43.91           O  
ANISOU  643  OD1 ASN A 315     5414   4834   6437   -558    293   -300       O  
ATOM    644  N   GLY A 316      -6.989  29.146  32.255  1.00 54.40           N  
ANISOU  644  N   GLY A 316     6830   6048   7794   -314     83   -227       N  
ATOM    645  CA  GLY A 316      -6.096  28.916  33.378  1.00 53.88           C  
ANISOU  645  CA  GLY A 316     6820   5917   7737   -250      6   -156       C  
ATOM    646  C   GLY A 316      -5.315  27.615  33.381  1.00 54.27           C  
ANISOU  646  C   GLY A 316     6857   5838   7925   -204    -50   -177       C  
ATOM    647  O   GLY A 316      -4.805  27.198  34.421  1.00 57.39           O  
ANISOU  647  O   GLY A 316     7320   6150   8333   -153   -124    -99       O  
ATOM    648  N   LYS A 317      -5.207  26.972  32.224  1.00 49.76           N  
ANISOU  648  N   LYS A 317     6206   5244   7455   -219    -22   -282       N  
ATOM    649  CA  LYS A 317      -4.500  25.701  32.146  1.00 54.28           C  
ANISOU  649  CA  LYS A 317     6759   5689   8175   -174    -69   -313       C  
ATOM    650  C   LYS A 317      -2.997  25.885  32.327  1.00 63.38           C  
ANISOU  650  C   LYS A 317     7866   6828   9388    -94   -152   -353       C  
ATOM    651  O   LYS A 317      -2.416  26.855  31.836  1.00 65.43           O  
ANISOU  651  O   LYS A 317     8062   7185   9612    -91   -141   -423       O  
ATOM    652  CB  LYS A 317      -4.791  25.008  30.817  1.00 56.39           C  
ANISOU  652  CB  LYS A 317     6956   5938   8532   -215     -9   -427       C  
ATOM    653  CG  LYS A 317      -6.259  24.680  30.620  1.00 54.30           C  
ANISOU  653  CG  LYS A 317     6723   5668   8239   -292     59   -396       C  
ATOM    654  CD  LYS A 317      -6.441  23.400  29.823  1.00 54.77           C  
ANISOU  654  CD  LYS A 317     6750   5631   8429   -312     80   -469       C  
ATOM    655  CE  LYS A 317      -7.912  23.019  29.736  1.00 57.00           C  
ANISOU  655  CE  LYS A 317     7060   5896   8701   -390    138   -435       C  
ATOM    656  NZ  LYS A 317      -8.131  21.740  29.002  1.00 58.47           N1+
ANISOU  656  NZ  LYS A 317     7220   5979   9016   -414    155   -505       N1+
ATOM    657  N   GLU A 318      -2.376  24.950  33.039  1.00 71.81           N  
ANISOU  657  N   GLU A 318     8965   7767  10553    -32   -239   -311       N  
ATOM    658  CA  GLU A 318      -0.937  24.990  33.284  1.00 73.89           C  
ANISOU  658  CA  GLU A 318     9175   7996  10904     53   -338   -351       C  
ATOM    659  C   GLU A 318      -0.139  24.335  32.162  1.00 69.08           C  
ANISOU  659  C   GLU A 318     8443   7345  10462     75   -320   -498       C  
ATOM    660  O   GLU A 318      -0.490  23.257  31.678  1.00 69.28           O  
ANISOU  660  O   GLU A 318     8461   7284  10577     61   -288   -529       O  
ATOM    661  CB  GLU A 318      -0.602  24.302  34.610  1.00 79.47           C  
ANISOU  661  CB  GLU A 318     9981   8573  11640    118   -461   -236       C  
ATOM    662  CG  GLU A 318      -1.310  24.880  35.821  1.00 85.53           C  
ANISOU  662  CG  GLU A 318    10892   9366  12239     97   -476    -90       C  
ATOM    663  CD  GLU A 318      -0.943  24.149  37.096  1.00 91.17           C  
ANISOU  663  CD  GLU A 318    11730   9940  12972    159   -603     24       C  
ATOM    664  OE1 GLU A 318      -0.187  23.159  37.010  1.00 90.89           O  
ANISOU  664  OE1 GLU A 318    11660   9783  13091    221   -684    -11       O  
ATOM    665  OE2 GLU A 318      -1.406  24.561  38.181  1.00 92.66           O1-
ANISOU  665  OE2 GLU A 318    12055  10133  13018    147   -622    145       O1-
ATOM    666  N   TYR A 319       0.945  24.986  31.759  1.00 67.15           N  
ANISOU  666  N   TYR A 319     8098   7154  10261    108   -333   -592       N  
ATOM    667  CA  TYR A 319       1.820  24.437  30.736  1.00 65.17           C  
ANISOU  667  CA  TYR A 319     7725   6862  10174    131   -304   -742       C  
ATOM    668  C   TYR A 319       3.193  24.149  31.321  1.00 68.79           C  
ANISOU  668  C   TYR A 319     8121   7234  10783    231   -425   -764       C  
ATOM    669  O   TYR A 319       3.854  25.039  31.859  1.00 70.03           O  
ANISOU  669  O   TYR A 319     8259   7444  10907    263   -486   -749       O  
ATOM    670  CB  TYR A 319       1.928  25.396  29.552  1.00 60.23           C  
ANISOU  670  CB  TYR A 319     7024   6367   9493     73   -190   -860       C  
ATOM    671  CG  TYR A 319       0.621  25.579  28.826  1.00 52.31           C  
ANISOU  671  CG  TYR A 319     6074   5434   8367    -20    -86   -856       C  
ATOM    672  CD1 TYR A 319      -0.328  26.482  29.283  1.00 48.94           C  
ANISOU  672  CD1 TYR A 319     5728   5101   7768    -65    -74   -758       C  
ATOM    673  CD2 TYR A 319       0.327  24.837  27.693  1.00 51.65           C  
ANISOU  673  CD2 TYR A 319     5960   5319   8346    -60     -8   -956       C  
ATOM    674  CE1 TYR A 319      -1.530  26.643  28.626  1.00 51.49           C  
ANISOU  674  CE1 TYR A 319     6086   5479   7997   -143      6   -759       C  
ATOM    675  CE2 TYR A 319      -0.870  24.992  27.031  1.00 48.47           C  
ANISOU  675  CE2 TYR A 319     5605   4974   7838   -141     67   -956       C  
ATOM    676  CZ  TYR A 319      -1.794  25.896  27.500  1.00 51.05           C  
ANISOU  676  CZ  TYR A 319     5999   5391   8007   -181     69   -858       C  
ATOM    677  OH  TYR A 319      -2.988  26.048  26.833  1.00 48.44           O  
ANISOU  677  OH  TYR A 319     5704   5111   7590   -257    131   -864       O  
ATOM    678  N   LYS A 320       3.617  22.894  31.226  1.00 72.25           N  
ANISOU  678  N   LYS A 320     8525   7532  11394    282   -468   -803       N  
ATOM    679  CA  LYS A 320       4.902  22.504  31.781  1.00 77.36           C  
ANISOU  679  CA  LYS A 320     9105   8078  12210    386   -600   -829       C  
ATOM    680  C   LYS A 320       5.898  22.077  30.711  1.00 74.44           C  
ANISOU  680  C   LYS A 320     8573   7671  12040    414   -548  -1010       C  
ATOM    681  O   LYS A 320       5.594  21.263  29.837  1.00 68.22           O  
ANISOU  681  O   LYS A 320     7761   6837  11323    385   -462  -1087       O  
ATOM    682  CB  LYS A 320       4.730  21.377  32.798  1.00 79.46           C  
ANISOU  682  CB  LYS A 320     9476   8184  12531    445   -727   -711       C  
ATOM    683  CG  LYS A 320       6.040  20.916  33.415  1.00 83.12           C  
ANISOU  683  CG  LYS A 320     9878   8526  13177    562   -892   -732       C  
ATOM    684  CD  LYS A 320       5.838  19.765  34.386  1.00 89.22           C  
ANISOU  684  CD  LYS A 320    10776   9129  13996    619  -1022   -610       C  
ATOM    685  CE  LYS A 320       5.112  20.212  35.644  1.00 89.35           C  
ANISOU  685  CE  LYS A 320    10980   9163  13807    599  -1088   -426       C  
ATOM    686  NZ  LYS A 320       5.059  19.125  36.659  1.00 90.15           N1+
ANISOU  686  NZ  LYS A 320    11220   9085  13948    658  -1227   -305       N1+
ATOM    687  N   CYS A 321       7.094  22.647  30.790  1.00 71.98           N  
ANISOU  687  N   CYS A 321     8148   7378  11823    466   -597  -1084       N  
ATOM    688  CA  CYS A 321       8.206  22.209  29.968  1.00 68.32           C  
ANISOU  688  CA  CYS A 321     7518   6858  11582    506   -561  -1258       C  
ATOM    689  C   CYS A 321       9.149  21.360  30.812  1.00 73.66           C  
ANISOU  689  C   CYS A 321     8149   7373  12464    629   -741  -1245       C  
ATOM    690  O   CYS A 321       9.497  21.726  31.936  1.00 71.26           O  
ANISOU  690  O   CYS A 321     7886   7053  12138    686   -895  -1148       O  
ATOM    691  CB  CYS A 321       8.945  23.405  29.368  1.00 63.70           C  
ANISOU  691  CB  CYS A 321     6818   6395  10990    475   -476  -1372       C  
ATOM    692  SG  CYS A 321      10.353  22.969  28.326  1.00 65.80           S  
ANISOU  692  SG  CYS A 321     6869   6598  11535    513   -400  -1602       S  
ATOM    693  N   LYS A 322       9.545  20.212  30.272  1.00 78.54           N  
ANISOU  693  N   LYS A 322     8691   7868  13283    670   -728  -1343       N  
ATOM    694  CA  LYS A 322      10.473  19.323  30.956  1.00 77.23           C  
ANISOU  694  CA  LYS A 322     8469   7533  13341    794   -901  -1347       C  
ATOM    695  C   LYS A 322      11.666  19.021  30.060  1.00 78.49           C  
ANISOU  695  C   LYS A 322     8419   7645  13760    837   -843  -1554       C  
ATOM    696  O   LYS A 322      11.527  18.420  28.993  1.00 76.78           O  
ANISOU  696  O   LYS A 322     8153   7406  13615    800   -701  -1670       O  
ATOM    697  CB  LYS A 322       9.763  18.034  31.379  1.00 78.27           C  
ANISOU  697  CB  LYS A 322     8730   7522  13488    818   -968  -1245       C  
ATOM    698  CG  LYS A 322      10.663  17.001  32.031  1.00 80.70           C  
ANISOU  698  CG  LYS A 322     8995   7635  14031    948  -1154  -1246       C  
ATOM    699  CD  LYS A 322       9.909  16.230  33.103  1.00 82.69           C  
ANISOU  699  CD  LYS A 322     9449   7771  14200    972  -1285  -1058       C  
ATOM    700  CE  LYS A 322      10.318  14.767  33.142  1.00 83.63           C  
ANISOU  700  CE  LYS A 322     9547   7680  14547   1060  -1378  -1088       C  
ATOM    701  NZ  LYS A 322       9.738  13.997  32.006  1.00 80.57           N1+
ANISOU  701  NZ  LYS A 322     9134   7273  14205    997  -1206  -1181       N1+
ATOM    702  N   VAL A 323      12.843  19.452  30.500  1.00 83.44           N  
ANISOU  702  N   VAL A 323     8921   8253  14531    913   -951  -1606       N  
ATOM    703  CA  VAL A 323      14.048  19.334  29.690  1.00 90.02           C  
ANISOU  703  CA  VAL A 323     9534   9052  15618    949   -884  -1813       C  
ATOM    704  C   VAL A 323      14.989  18.267  30.239  1.00 96.43           C  
ANISOU  704  C   VAL A 323    10279   9740  16620   1035  -1055  -1810       C  
ATOM    705  O   VAL A 323      15.340  18.276  31.421  1.00 97.57           O  
ANISOU  705  O   VAL A 323    10465   9825  16782   1112  -1270  -1703       O  
ATOM    706  CB  VAL A 323      14.789  20.682  29.601  1.00 89.53           C  
ANISOU  706  CB  VAL A 323     9358   9115  15545    924   -845  -1885       C  
ATOM    707  CG1 VAL A 323      16.093  20.522  28.844  1.00 87.26           C  
ANISOU  707  CG1 VAL A 323     8864   8837  15452    909   -771  -2061       C  
ATOM    708  CG2 VAL A 323      13.905  21.723  28.928  1.00 91.22           C  
ANISOU  708  CG2 VAL A 323     9658   9513  15489    787   -657  -1867       C  
ATOM    709  N   SER A 324      15.392  17.348  29.366  1.00 99.35           N  
ANISOU  709  N   SER A 324    10552  10070  17124   1018   -960  -1928       N  
ATOM    710  CA  SER A 324      16.271  16.251  29.749  1.00 95.43           C  
ANISOU  710  CA  SER A 324     9985   9451  16823   1094  -1105  -1943       C  
ATOM    711  C   SER A 324      17.563  16.263  28.929  1.00 92.15           C  
ANISOU  711  C   SER A 324     9349   9062  16601   1074  -1016  -2134       C  
ATOM    712  O   SER A 324      17.538  16.375  27.698  1.00 88.88           O  
ANISOU  712  O   SER A 324     8866   8718  16185    990   -795  -2264       O  
ATOM    713  CB  SER A 324      15.541  14.919  29.589  1.00 92.22           C  
ANISOU  713  CB  SER A 324     9681   8939  16419   1103  -1097  -1895       C  
ATOM    714  OG  SER A 324      14.231  14.996  30.126  1.00 93.18           O  
ANISOU  714  OG  SER A 324    10008   9047  16350   1089  -1124  -1736       O  
ATOM    715  N   ASN A 325      18.688  16.138  29.628  1.00 92.33           N  
ANISOU  715  N   ASN A 325     9273   9023  16786   1144  -1191  -2149       N  
ATOM    716  CA  ASN A 325      20.010  16.237  29.025  1.00 93.83           C  
ANISOU  716  CA  ASN A 325     9251   9224  17178   1125  -1132  -2325       C  
ATOM    717  C   ASN A 325      21.070  15.835  30.052  1.00 98.62           C  
ANISOU  717  C   ASN A 325     9789   9720  17960   1221  -1384  -2306       C  
ATOM    718  O   ASN A 325      20.999  16.238  31.215  1.00 93.74           O  
ANISOU  718  O   ASN A 325     9262   9085  17269   1278  -1581  -2177       O  
ATOM    719  CB  ASN A 325      20.250  17.653  28.502  1.00 91.49           C  
ANISOU  719  CB  ASN A 325     8880   9070  16812   1042   -982  -2407       C  
ATOM    720  CG  ASN A 325      21.676  17.885  28.061  1.00 94.67           C  
ANISOU  720  CG  ASN A 325     9074   9474  17423   1018   -939  -2576       C  
ATOM    721  ND2 ASN A 325      22.065  17.267  26.950  1.00 96.90           N  
ANISOU  721  ND2 ASN A 325     9255   9741  17822    967   -770  -2720       N  
ATOM    722  OD1 ASN A 325      22.421  18.619  28.707  1.00 93.95           O  
ANISOU  722  OD1 ASN A 325     8918   9393  17386   1041  -1054  -2580       O  
ATOM    723  N   LYS A 326      22.045  15.039  29.618  1.00108.59           N  
ANISOU  723  N   LYS A 326    10900  10906  19452   1237  -1380  -2435       N  
ATOM    724  CA  LYS A 326      22.943  14.333  30.539  1.00118.53           C  
ANISOU  724  CA  LYS A 326    12111  12032  20892   1336  -1629  -2416       C  
ATOM    725  C   LYS A 326      23.740  15.247  31.489  1.00122.64           C  
ANISOU  725  C   LYS A 326    12588  12564  21446   1370  -1809  -2397       C  
ATOM    726  O   LYS A 326      24.164  14.812  32.565  1.00123.07           O  
ANISOU  726  O   LYS A 326    12681  12515  21566   1458  -2061  -2320       O  
ATOM    727  CB  LYS A 326      23.903  13.436  29.746  1.00121.43           C  
ANISOU  727  CB  LYS A 326    12298  12325  21516   1334  -1561  -2587       C  
ATOM    728  CG  LYS A 326      25.383  13.743  29.960  1.00123.58           C  
ANISOU  728  CG  LYS A 326    12378  12559  22016   1354  -1654  -2711       C  
ATOM    729  CD  LYS A 326      26.263  12.535  29.668  1.00122.47           C  
ANISOU  729  CD  LYS A 326    12100  12289  22142   1397  -1694  -2826       C  
ATOM    730  CE  LYS A 326      26.079  12.033  28.240  1.00115.96           C  
ANISOU  730  CE  LYS A 326    11209  11495  21358   1321  -1421  -2955       C  
ATOM    731  NZ  LYS A 326      27.101  11.002  27.894  1.00113.99           N1+
ANISOU  731  NZ  LYS A 326    10795  11125  21392   1355  -1444  -3093       N1+
ATOM    732  N   ALA A 327      23.934  16.507  31.108  1.00123.02           N  
ANISOU  732  N   ALA A 327    12569  12734  21440   1298  -1683  -2464       N  
ATOM    733  CA  ALA A 327      24.654  17.455  31.963  1.00126.62           C  
ANISOU  733  CA  ALA A 327    12987  13206  21916   1322  -1839  -2451       C  
ATOM    734  C   ALA A 327      23.743  18.061  33.037  1.00126.06           C  
ANISOU  734  C   ALA A 327    13121  13174  21604   1355  -1980  -2253       C  
ATOM    735  O   ALA A 327      23.880  19.231  33.400  1.00125.99           O  
ANISOU  735  O   ALA A 327    13113  13245  21514   1333  -2002  -2238       O  
ATOM    736  CB  ALA A 327      25.287  18.556  31.121  1.00128.54           C  
ANISOU  736  CB  ALA A 327    13078  13555  22207   1228  -1644  -2606       C  
ATOM    737  N   LEU A 328      22.813  17.249  33.533  1.00125.27           N  
ANISOU  737  N   LEU A 328    13198  13010  21389   1403  -2067  -2104       N  
ATOM    738  CA  LEU A 328      21.911  17.625  34.618  1.00123.62           C  
ANISOU  738  CA  LEU A 328    13207  12812  20952   1436  -2208  -1904       C  
ATOM    739  C   LEU A 328      21.583  16.377  35.429  1.00125.18           C  
ANISOU  739  C   LEU A 328    13555  12867  21140   1515  -2395  -1772       C  
ATOM    740  O   LEU A 328      21.240  15.342  34.857  1.00125.64           O  
ANISOU  740  O   LEU A 328    13618  12866  21251   1515  -2312  -1793       O  
ATOM    741  CB  LEU A 328      20.624  18.261  34.080  1.00120.07           C  
ANISOU  741  CB  LEU A 328    12863  12476  20280   1366  -2010  -1849       C  
ATOM    742  CG  LEU A 328      20.706  19.671  33.490  1.00114.26           C  
ANISOU  742  CG  LEU A 328    12040  11892  19483   1289  -1845  -1934       C  
ATOM    743  CD1 LEU A 328      19.445  20.006  32.708  1.00105.42           C  
ANISOU  743  CD1 LEU A 328    11009  10864  18181   1217  -1624  -1910       C  
ATOM    744  CD2 LEU A 328      20.952  20.701  34.585  1.00113.87           C  
ANISOU  744  CD2 LEU A 328    12043  11877  19345   1317  -2019  -1848       C  
ATOM    745  N   PRO A 329      21.694  16.464  36.764  1.00124.75           N  
ANISOU  745  N   PRO A 329    13634  12756  21010   1578  -2645  -1637       N  
ATOM    746  CA  PRO A 329      21.420  15.295  37.612  1.00127.57           C  
ANISOU  746  CA  PRO A 329    14157  12972  21343   1648  -2830  -1503       C  
ATOM    747  C   PRO A 329      19.973  14.825  37.482  1.00124.83           C  
ANISOU  747  C   PRO A 329    14004  12620  20807   1621  -2723  -1373       C  
ATOM    748  O   PRO A 329      19.716  13.635  37.286  1.00121.10           O  
ANISOU  748  O   PRO A 329    13571  12048  20391   1642  -2715  -1358       O  
ATOM    749  CB  PRO A 329      21.712  15.809  39.027  1.00126.42           C  
ANISOU  749  CB  PRO A 329    14140  12800  21094   1696  -3085  -1382       C  
ATOM    750  CG  PRO A 329      21.589  17.297  38.932  1.00120.45           C  
ANISOU  750  CG  PRO A 329    13353  12189  20223   1641  -2999  -1399       C  
ATOM    751  CD  PRO A 329      22.049  17.656  37.554  1.00119.89           C  
ANISOU  751  CD  PRO A 329    13039  12202  20311   1580  -2765  -1599       C  
ATOM    752  N   ALA A 330      19.043  15.768  37.587  1.00126.60           N  
ANISOU  752  N   ALA A 330    14344  12944  20814   1572  -2640  -1285       N  
ATOM    753  CA  ALA A 330      17.632  15.502  37.340  1.00125.58           C  
ANISOU  753  CA  ALA A 330    14382  12822  20512   1528  -2507  -1182       C  
ATOM    754  C   ALA A 330      17.147  16.390  36.197  1.00121.63           C  
ANISOU  754  C   ALA A 330    13786  12462  19967   1444  -2251  -1281       C  
ATOM    755  O   ALA A 330      17.711  17.462  35.966  1.00125.30           O  
ANISOU  755  O   ALA A 330    14123  13029  20456   1422  -2210  -1369       O  
ATOM    756  CB  ALA A 330      16.812  15.743  38.599  1.00127.55           C  
ANISOU  756  CB  ALA A 330    14897  13045  20521   1540  -2646   -967       C  
ATOM    757  N   PRO A 331      16.113  15.948  35.464  1.00112.05           N  
ANISOU  757  N   PRO A 331    12636  11251  18688   1392  -2075  -1273       N  
ATOM    758  CA  PRO A 331      15.585  16.817  34.409  1.00107.15           C  
ANISOU  758  CA  PRO A 331    11949  10762  18001   1308  -1837  -1362       C  
ATOM    759  C   PRO A 331      14.844  18.012  35.001  1.00103.27           C  
ANISOU  759  C   PRO A 331    11587  10352  17297   1283  -1851  -1246       C  
ATOM    760  O   PRO A 331      14.185  17.877  36.032  1.00104.34           O  
ANISOU  760  O   PRO A 331    11926  10429  17289   1306  -1981  -1070       O  
ATOM    761  CB  PRO A 331      14.636  15.898  33.637  1.00104.19           C  
ANISOU  761  CB  PRO A 331    11639  10344  17604   1262  -1685  -1367       C  
ATOM    762  CG  PRO A 331      14.200  14.893  34.639  1.00106.62           C  
ANISOU  762  CG  PRO A 331    12131  10513  17867   1313  -1852  -1203       C  
ATOM    763  CD  PRO A 331      15.381  14.673  35.548  1.00111.01           C  
ANISOU  763  CD  PRO A 331    12641  11001  18536   1401  -2083  -1188       C  
ATOM    764  N   ILE A 332      14.954  19.167  34.357  1.00 96.12           N  
ANISOU  764  N   ILE A 332    10575   9581  16367   1232  -1713  -1344       N  
ATOM    765  CA  ILE A 332      14.376  20.387  34.904  1.00 89.25           C  
ANISOU  765  CA  ILE A 332     9818   8830  15264   1186  -1716  -1238       C  
ATOM    766  C   ILE A 332      12.937  20.611  34.426  1.00 86.83           C  
ANISOU  766  C   ILE A 332     9658   8639  14693   1059  -1521  -1162       C  
ATOM    767  O   ILE A 332      12.617  20.382  33.259  1.00 91.37           O  
ANISOU  767  O   ILE A 332    10170   9257  15291    993  -1328  -1266       O  
ATOM    768  CB  ILE A 332      15.229  21.617  34.542  1.00 81.45           C  
ANISOU  768  CB  ILE A 332     8659   7965  14324   1165  -1663  -1361       C  
ATOM    769  CG1 ILE A 332      16.702  21.362  34.862  1.00 82.21           C  
ANISOU  769  CG1 ILE A 332     8590   7985  14662   1247  -1820  -1453       C  
ATOM    770  CG2 ILE A 332      14.748  22.836  35.301  1.00 79.59           C  
ANISOU  770  CG2 ILE A 332     8556   7859  13827   1113  -1699  -1232       C  
ATOM    771  CD1 ILE A 332      17.603  22.549  34.569  1.00 80.34           C  
ANISOU  771  CD1 ILE A 332     8184   7859  14482   1217  -1772  -1574       C  
ATOM    772  N   GLU A 333      12.077  21.051  35.343  1.00 80.02           N  
ANISOU  772  N   GLU A 333     8995   7824  13585   1024  -1578   -984       N  
ATOM    773  CA  GLU A 333      10.683  21.354  35.027  1.00 75.84           C  
ANISOU  773  CA  GLU A 333     8603   7406  12808    908  -1412   -904       C  
ATOM    774  C   GLU A 333      10.324  22.818  35.290  1.00 77.53           C  
ANISOU  774  C   GLU A 333     8869   7791  12800    839  -1364   -850       C  
ATOM    775  O   GLU A 333      10.730  23.399  36.295  1.00 80.51           O  
ANISOU  775  O   GLU A 333     9293   8169  13127    883  -1513   -777       O  
ATOM    776  CB  GLU A 333       9.752  20.450  35.833  1.00 67.34           C  
ANISOU  776  CB  GLU A 333     7733   6221  11633    913  -1484   -737       C  
ATOM    777  CG  GLU A 333       9.904  18.971  35.541  1.00 70.41           C  
ANISOU  777  CG  GLU A 333     8097   6438  12217    968  -1515   -776       C  
ATOM    778  CD  GLU A 333       8.921  18.131  36.328  1.00 75.75           C  
ANISOU  778  CD  GLU A 333     8989   7010  12782    958  -1569   -606       C  
ATOM    779  OE1 GLU A 333       8.787  16.924  36.032  1.00 75.16           O  
ANISOU  779  OE1 GLU A 333     8921   6803  12833    980  -1565   -624       O  
ATOM    780  OE2 GLU A 333       8.278  18.686  37.244  1.00 81.90           O1-
ANISOU  780  OE2 GLU A 333     9936   7836  13347    924  -1608   -456       O1-
ATOM    781  N   LYS A 334       9.560  23.411  34.381  1.00 77.84           N  
ANISOU  781  N   LYS A 334     8904   7967  12704    732  -1164   -888       N  
ATOM    782  CA  LYS A 334       9.056  24.764  34.576  1.00 81.47           C  
ANISOU  782  CA  LYS A 334     9427   8585  12943    661  -1106   -832       C  
ATOM    783  C   LYS A 334       7.576  24.808  34.236  1.00 81.83           C  
ANISOU  783  C   LYS A 334     9599   8703  12790    562   -964   -757       C  
ATOM    784  O   LYS A 334       7.149  24.217  33.247  1.00 86.35           O  
ANISOU  784  O   LYS A 334    10136   9269  13406    519   -839   -828       O  
ATOM    785  CB  LYS A 334       9.829  25.771  33.719  1.00 83.82           C  
ANISOU  785  CB  LYS A 334     9560   8995  13293    631  -1009   -981       C  
ATOM    786  CG  LYS A 334      11.238  26.056  34.210  1.00 84.80           C  
ANISOU  786  CG  LYS A 334     9558   9074  13589    717  -1154  -1044       C  
ATOM    787  CD  LYS A 334      11.228  26.671  35.598  1.00 82.99           C  
ANISOU  787  CD  LYS A 334     9450   8851  13232    753  -1325   -903       C  
ATOM    788  CE  LYS A 334      12.634  26.779  36.167  1.00 82.31           C  
ANISOU  788  CE  LYS A 334     9243   8693  13340    851  -1507   -963       C  
ATOM    789  NZ  LYS A 334      13.487  27.747  35.420  1.00 80.33           N1+
ANISOU  789  NZ  LYS A 334     8806   8538  13178    820  -1415  -1117       N1+
ATOM    790  N   THR A 335       6.797  25.502  35.060  1.00 75.30           N  
ANISOU  790  N   THR A 335     8917   7941  11752    527   -984   -621       N  
ATOM    791  CA  THR A 335       5.355  25.600  34.850  1.00 70.10           C  
ANISOU  791  CA  THR A 335     8372   7349  10914    435   -858   -546       C  
ATOM    792  C   THR A 335       4.883  27.052  34.837  1.00 65.19           C  
ANISOU  792  C   THR A 335     7780   6890  10100    369   -784   -523       C  
ATOM    793  O   THR A 335       5.247  27.839  35.710  1.00 64.54           O  
ANISOU  793  O   THR A 335     7738   6839   9945    396   -875   -465       O  
ATOM    794  CB  THR A 335       4.576  24.829  35.938  1.00 72.63           C  
ANISOU  794  CB  THR A 335     8870   7567  11160    448   -936   -386       C  
ATOM    795  CG2 THR A 335       3.076  25.084  35.822  1.00 72.53           C  
ANISOU  795  CG2 THR A 335     8964   7631  10965    350   -803   -310       C  
ATOM    796  OG1 THR A 335       4.827  23.425  35.806  1.00 76.79           O  
ANISOU  796  OG1 THR A 335     9379   7939  11856    497   -983   -407       O  
ATOM    797  N   ILE A 336       4.079  27.408  33.838  1.00 59.57           N  
ANISOU  797  N   ILE A 336     7051   6274   9308    283   -626   -570       N  
ATOM    798  CA  ILE A 336       3.451  28.723  33.806  1.00 61.54           C  
ANISOU  798  CA  ILE A 336     7343   6668   9371    217   -553   -538       C  
ATOM    799  C   ILE A 336       1.968  28.624  33.475  1.00 60.45           C  
ANISOU  799  C   ILE A 336     7289   6571   9109    138   -444   -484       C  
ATOM    800  O   ILE A 336       1.498  27.622  32.933  1.00 59.99           O  
ANISOU  800  O   ILE A 336     7226   6449   9117    119   -397   -508       O  
ATOM    801  CB  ILE A 336       4.115  29.662  32.782  1.00 60.64           C  
ANISOU  801  CB  ILE A 336     7104   6658   9277    187   -471   -672       C  
ATOM    802  CG1 ILE A 336       4.050  29.055  31.380  1.00 59.25           C  
ANISOU  802  CG1 ILE A 336     6847   6474   9192    148   -351   -797       C  
ATOM    803  CG2 ILE A 336       5.553  29.967  33.176  1.00 59.08           C  
ANISOU  803  CG2 ILE A 336     6813   6434   9200    258   -574   -727       C  
ATOM    804  CD1 ILE A 336       4.493  30.001  30.293  1.00 60.62           C  
ANISOU  804  CD1 ILE A 336     6933   6752   9348     98   -242   -921       C  
ATOM    805  N   SER A 337       1.239  29.680  33.813  1.00 57.60           N  
ANISOU  805  N   SER A 337     6999   6313   8575     92   -407   -417       N  
ATOM    806  CA  SER A 337      -0.172  29.796  33.490  1.00 57.06           C  
ANISOU  806  CA  SER A 337     6992   6296   8393     15   -305   -376       C  
ATOM    807  C   SER A 337      -0.562  31.250  33.641  1.00 55.74           C  
ANISOU  807  C   SER A 337     6855   6258   8065    -22   -269   -348       C  
ATOM    808  O   SER A 337       0.198  32.041  34.199  1.00 52.08           O  
ANISOU  808  O   SER A 337     6388   5829   7571     12   -332   -338       O  
ATOM    809  CB  SER A 337      -1.026  28.912  34.399  1.00 62.31           C  
ANISOU  809  CB  SER A 337     7773   6867   9034     15   -331   -254       C  
ATOM    810  OG  SER A 337      -0.909  29.326  35.750  1.00 65.47           O  
ANISOU  810  OG  SER A 337     8276   7254   9345     49   -414   -141       O  
ATOM    811  N   LYS A 338      -1.736  31.608  33.139  1.00 57.20           N  
ANISOU  811  N   LYS A 338     7066   6511   8158    -91   -174   -339       N  
ATOM    812  CA  LYS A 338      -2.243  32.962  33.305  1.00 50.48           C  
ANISOU  812  CA  LYS A 338     6250   5773   7157   -126   -139   -307       C  
ATOM    813  C   LYS A 338      -2.430  33.254  34.787  1.00 44.96           C  
ANISOU  813  C   LYS A 338     5658   5056   6368    -99   -201   -181       C  
ATOM    814  O   LYS A 338      -2.742  32.353  35.565  1.00 51.90           O  
ANISOU  814  O   LYS A 338     6611   5841   7268    -82   -233   -101       O  
ATOM    815  CB  LYS A 338      -3.564  33.142  32.551  1.00 51.02           C  
ANISOU  815  CB  LYS A 338     6326   5896   7161   -198    -43   -317       C  
ATOM    816  CG  LYS A 338      -3.975  34.589  32.355  1.00 47.31           C  
ANISOU  816  CG  LYS A 338     5868   5547   6561   -233     -3   -318       C  
ATOM    817  CD  LYS A 338      -5.440  34.682  31.976  1.00 44.75           C  
ANISOU  817  CD  LYS A 338     5567   5255   6180   -292     66   -298       C  
ATOM    818  CE  LYS A 338      -6.325  34.344  33.163  1.00 44.92           C  
ANISOU  818  CE  LYS A 338     5670   5231   6167   -293     67   -182       C  
ATOM    819  NZ  LYS A 338      -7.762  34.246  32.783  1.00 45.48           N1+
ANISOU  819  NZ  LYS A 338     5741   5315   6222   -352    136   -173       N1+
ATOM    820  N   ALA A 339      -2.227  34.508  35.176  1.00 39.11           N  
ANISOU  820  N   ALA A 339     4938   4399   5524    -98   -213   -165       N  
ATOM    821  CA  ALA A 339      -2.366  34.904  36.572  1.00 41.94           C  
ANISOU  821  CA  ALA A 339     5409   4746   5781    -75   -268    -53       C  
ATOM    822  C   ALA A 339      -3.778  34.637  37.083  1.00 49.75           C  
ANISOU  822  C   ALA A 339     6494   5718   6691   -119   -201     38       C  
ATOM    823  O   ALA A 339      -4.759  34.891  36.383  1.00 45.41           O  
ANISOU  823  O   ALA A 339     5916   5225   6115   -174   -106     13       O  
ATOM    824  CB  ALA A 339      -2.003  36.372  36.744  1.00 37.20           C  
ANISOU  824  CB  ALA A 339     4807   4246   5081    -77   -278    -66       C  
ATOM    825  N   LYS A 340      -3.874  34.114  38.301  1.00 53.98           N  
ANISOU  825  N   LYS A 340     7147   6172   7194    -95   -250    140       N  
ATOM    826  CA  LYS A 340      -5.163  33.846  38.924  1.00 57.37           C  
ANISOU  826  CA  LYS A 340     7676   6573   7549   -140   -173    230       C  
ATOM    827  C   LYS A 340      -5.720  35.123  39.530  1.00 57.60           C  
ANISOU  827  C   LYS A 340     7768   6688   7428   -164   -130    274       C  
ATOM    828  O   LYS A 340      -4.968  36.044  39.845  1.00 59.30           O  
ANISOU  828  O   LYS A 340     7991   6956   7585   -133   -191    264       O  
ATOM    829  CB  LYS A 340      -5.021  32.762  39.994  1.00 61.10           C  
ANISOU  829  CB  LYS A 340     8269   6911   8035   -111   -235    325       C  
ATOM    830  CG  LYS A 340      -4.391  31.476  39.491  1.00 65.72           C  
ANISOU  830  CG  LYS A 340     8798   7395   8778    -78   -292    284       C  
ATOM    831  CD  LYS A 340      -3.813  30.662  40.635  1.00 70.34           C  
ANISOU  831  CD  LYS A 340     9508   7849   9370    -24   -406    374       C  
ATOM    832  CE  LYS A 340      -4.365  29.249  40.633  1.00 72.42           C  
ANISOU  832  CE  LYS A 340     9815   7989   9714    -43   -375    412       C  
ATOM    833  NZ  LYS A 340      -4.170  28.576  39.322  1.00 69.05           N1+
ANISOU  833  NZ  LYS A 340     9237   7552   9445    -44   -351    302       N1+
ATOM    834  N   GLY A 341      -7.036  35.179  39.699  1.00 49.49           N  
ANISOU  834  N   GLY A 341     6782   5673   6348   -220    -22    316       N  
ATOM    835  CA  GLY A 341      -7.676  36.354  40.263  1.00 41.43           C  
ANISOU  835  CA  GLY A 341     5817   4728   5196   -244     34    351       C  
ATOM    836  C   GLY A 341      -8.787  36.848  39.364  1.00 43.54           C  
ANISOU  836  C   GLY A 341     5997   5071   5474   -298    139    300       C  
ATOM    837  O   GLY A 341      -8.748  36.635  38.154  1.00 47.61           O  
ANISOU  837  O   GLY A 341     6401   5611   6076   -309    144    218       O  
ATOM    838  N   GLN A 342      -9.780  37.511  39.951  1.00 49.78           N  
ANISOU  838  N   GLN A 342     6842   5895   6178   -332    222    344       N  
ATOM    839  CA  GLN A 342     -10.930  37.986  39.184  1.00 49.70           C  
ANISOU  839  CA  GLN A 342     6749   5948   6189   -379    312    297       C  
ATOM    840  C   GLN A 342     -10.520  38.993  38.117  1.00 45.09           C  
ANISOU  840  C   GLN A 342     6069   5463   5600   -368    278    210       C  
ATOM    841  O   GLN A 342      -9.901  40.015  38.418  1.00 44.01           O  
ANISOU  841  O   GLN A 342     5959   5381   5381   -341    238    210       O  
ATOM    842  CB  GLN A 342     -11.977  38.615  40.103  1.00 53.39           C  
ANISOU  842  CB  GLN A 342     7287   6428   6569   -410    407    354       C  
ATOM    843  CG  GLN A 342     -13.278  38.965  39.389  1.00 66.14           C  
ANISOU  843  CG  GLN A 342     8807   8088   8233   -457    496    308       C  
ATOM    844  CD  GLN A 342     -14.352  39.461  40.339  1.00 85.58           C  
ANISOU  844  CD  GLN A 342    11330  10551  10637   -488    606    357       C  
ATOM    845  NE2 GLN A 342     -15.548  38.895  40.227  1.00 87.68           N  
ANISOU  845  NE2 GLN A 342    11551  10777  10984   -540    702    355       N  
ATOM    846  OE1 GLN A 342     -14.108  40.337  41.168  1.00 96.08           O  
ANISOU  846  OE1 GLN A 342    12742  11910  11853   -469    608    392       O  
ATOM    847  N   PRO A 343     -10.850  38.690  36.856  1.00 44.39           N  
ANISOU  847  N   PRO A 343     5880   5391   5597   -392    291    136       N  
ATOM    848  CA  PRO A 343     -10.597  39.624  35.760  1.00 39.90           C  
ANISOU  848  CA  PRO A 343     5238   4909   5015   -392    269     55       C  
ATOM    849  C   PRO A 343     -11.325  40.944  35.980  1.00 42.36           C  
ANISOU  849  C   PRO A 343     5562   5294   5240   -404    308     65       C  
ATOM    850  O   PRO A 343     -12.447  40.961  36.483  1.00 48.67           O  
ANISOU  850  O   PRO A 343     6377   6080   6035   -429    376    103       O  
ATOM    851  CB  PRO A 343     -11.146  38.886  34.533  1.00 45.74           C  
ANISOU  851  CB  PRO A 343     5895   5632   5853   -426    287    -12       C  
ATOM    852  CG  PRO A 343     -11.087  37.441  34.908  1.00 41.25           C  
ANISOU  852  CG  PRO A 343     5344   4963   5367   -426    289     21       C  
ATOM    853  CD  PRO A 343     -11.388  37.407  36.379  1.00 38.33           C  
ANISOU  853  CD  PRO A 343     5072   4552   4940   -421    319    122       C  
ATOM    854  N   ARG A 344     -10.681  42.042  35.616  1.00 44.50           N  
ANISOU  854  N   ARG A 344     5823   5634   5449   -386    270     28       N  
ATOM    855  CA AARG A 344     -11.307  43.345  35.747  0.43 38.95           C  
ANISOU  855  CA AARG A 344     5133   4999   4670   -393    299     31       C  
ATOM    856  CA BARG A 344     -11.276  43.364  35.762  0.57 38.48           C  
ANISOU  856  CA BARG A 344     5074   4939   4607   -392    297     31       C  
ATOM    857  C   ARG A 344     -11.171  44.142  34.455  1.00 39.74           C  
ANISOU  857  C   ARG A 344     5176   5162   4761   -403    273    -47       C  
ATOM    858  O   ARG A 344     -10.114  44.165  33.831  1.00 43.71           O  
ANISOU  858  O   ARG A 344     5661   5678   5268   -394    230    -94       O  
ATOM    859  CB AARG A 344     -10.707  44.111  36.924  0.43 37.21           C  
ANISOU  859  CB AARG A 344     4996   4793   4349   -363    281     83       C  
ATOM    860  CB BARG A 344     -10.596  44.134  36.896  0.57 36.51           C  
ANISOU  860  CB BARG A 344     4907   4706   4259   -361    275     80       C  
ATOM    861  CG AARG A 344     -10.960  43.453  38.271  0.43 38.64           C  
ANISOU  861  CG AARG A 344     5264   4907   4509   -359    311    168       C  
ATOM    862  CG BARG A 344     -10.787  43.522  38.275  0.57 38.62           C  
ANISOU  862  CG BARG A 344     5264   4908   4500   -354    300    166       C  
ATOM    863  CD AARG A 344     -11.150  44.501  39.345  0.43 35.96           C  
ANISOU  863  CD AARG A 344     5011   4597   4056   -349    336    214       C  
ATOM    864  CD BARG A 344     -11.814  44.292  39.082  0.57 36.47           C  
ANISOU  864  CD BARG A 344     5044   4656   4157   -368    377    206       C  
ATOM    865  NE AARG A 344     -10.116  44.431  40.369  0.43 30.81           N  
ANISOU  865  NE AARG A 344     4455   3913   3337   -316    272    262       N  
ATOM    866  NE BARG A 344     -11.927  43.784  40.445  0.57 31.85           N  
ANISOU  866  NE BARG A 344     4571   4006   3522   -368    409    289       N  
ATOM    867  CZ AARG A 344      -9.818  45.431  41.192  0.43 26.99           C  
ANISOU  867  CZ AARG A 344     4049   3460   2747   -299    257    287       C  
ATOM    868  CZ BARG A 344     -13.064  43.376  40.996  0.57 34.67           C  
ANISOU  868  CZ BARG A 344     4958   4323   3893   -402    510    328       C  
ATOM    869  NH1AARG A 344      -8.864  45.279  42.100  0.43 24.55           N1+
ANISOU  869  NH1AARG A 344     3831   3114   2384   -267    181    328       N1+
ATOM    870  NH1BARG A 344     -13.074  42.929  42.244  0.57 22.52           N1+
ANISOU  870  NH1BARG A 344     3545   2720   2291   -406    542    405       N1+
ATOM    871  NH2AARG A 344     -10.472  46.582  41.104  0.43 20.02           N  
ANISOU  871  NH2AARG A 344     3156   2638   1814   -310    308    267       N  
ATOM    872  NH2BARG A 344     -14.191  43.422  40.301  0.57 28.48           N  
ANISOU  872  NH2BARG A 344     4080   3556   3184   -435    578    288       N  
ATOM    873  N   GLU A 345     -12.264  44.780  34.051  1.00 41.31           N  
ANISOU  873  N   GLU A 345     5349   5394   4953   -422    303    -63       N  
ATOM    874  CA  GLU A 345     -12.306  45.523  32.796  1.00 38.65           C  
ANISOU  874  CA  GLU A 345     4978   5108   4601   -435    273   -131       C  
ATOM    875  C   GLU A 345     -11.490  46.816  32.835  1.00 37.36           C  
ANISOU  875  C   GLU A 345     4853   4999   4341   -418    245   -140       C  
ATOM    876  O   GLU A 345     -11.676  47.652  33.721  1.00 41.74           O  
ANISOU  876  O   GLU A 345     5449   5576   4835   -401    260    -99       O  
ATOM    877  CB  GLU A 345     -13.757  45.839  32.430  1.00 36.65           C  
ANISOU  877  CB  GLU A 345     4686   4862   4377   -455    295   -143       C  
ATOM    878  CG  GLU A 345     -13.933  46.506  31.080  1.00 41.98           C  
ANISOU  878  CG  GLU A 345     5340   5574   5036   -468    248   -210       C  
ATOM    879  CD  GLU A 345     -15.388  46.766  30.757  1.00 55.35           C  
ANISOU  879  CD  GLU A 345     6987   7265   6777   -480    249   -223       C  
ATOM    880  OE1 GLU A 345     -16.238  46.545  31.644  1.00 58.31           O  
ANISOU  880  OE1 GLU A 345     7340   7616   7199   -480    303   -184       O  
ATOM    881  OE2 GLU A 345     -15.682  47.188  29.619  1.00 63.32           O1-
ANISOU  881  OE2 GLU A 345     7986   8292   7780   -492    196   -276       O1-
ATOM    882  N   PRO A 346     -10.576  46.977  31.870  1.00 38.97           N  
ANISOU  882  N   PRO A 346     5047   5224   4535   -426    212   -199       N  
ATOM    883  CA  PRO A 346      -9.810  48.219  31.749  1.00 37.61           C  
ANISOU  883  CA  PRO A 346     4908   5102   4281   -420    193   -216       C  
ATOM    884  C   PRO A 346     -10.686  49.383  31.313  1.00 33.02           C  
ANISOU  884  C   PRO A 346     4342   4559   3644   -429    192   -225       C  
ATOM    885  O   PRO A 346     -11.418  49.259  30.333  1.00 28.92           O  
ANISOU  885  O   PRO A 346     3801   4037   3150   -451    182   -261       O  
ATOM    886  CB  PRO A 346      -8.763  47.886  30.679  1.00 30.19           C  
ANISOU  886  CB  PRO A 346     3946   4160   3363   -438    179   -287       C  
ATOM    887  CG  PRO A 346      -9.360  46.767  29.899  1.00 28.83           C  
ANISOU  887  CG  PRO A 346     3736   3952   3267   -459    186   -317       C  
ATOM    888  CD  PRO A 346     -10.152  45.965  30.886  1.00 31.74           C  
ANISOU  888  CD  PRO A 346     4093   4279   3688   -444    203   -255       C  
ATOM    889  N   GLN A 347     -10.619  50.487  32.045  1.00 33.09           N  
ANISOU  889  N   GLN A 347     4393   4597   3583   -412    193   -194       N  
ATOM    890  CA  GLN A 347     -11.242  51.726  31.606  1.00 37.30           C  
ANISOU  890  CA  GLN A 347     4947   5164   4061   -415    182   -207       C  
ATOM    891  C   GLN A 347     -10.245  52.493  30.740  1.00 38.15           C  
ANISOU  891  C   GLN A 347     5087   5299   4109   -434    158   -253       C  
ATOM    892  O   GLN A 347      -9.106  52.726  31.147  1.00 35.51           O  
ANISOU  892  O   GLN A 347     4770   4975   3748   -430    158   -254       O  
ATOM    893  CB  GLN A 347     -11.697  52.565  32.802  1.00 38.41           C  
ANISOU  893  CB  GLN A 347     5120   5316   4157   -388    204   -157       C  
ATOM    894  CG  GLN A 347     -12.605  51.808  33.764  1.00 49.30           C  
ANISOU  894  CG  GLN A 347     6481   6663   5589   -378    251   -110       C  
ATOM    895  CD  GLN A 347     -13.852  51.257  33.086  1.00 59.80           C  
ANISOU  895  CD  GLN A 347     7749   7971   7003   -394    260   -131       C  
ATOM    896  NE2 GLN A 347     -14.066  49.952  33.207  1.00 57.42           N  
ANISOU  896  NE2 GLN A 347     7412   7629   6776   -406    284   -121       N  
ATOM    897  OE1 GLN A 347     -14.609  52.000  32.454  1.00 64.73           O  
ANISOU  897  OE1 GLN A 347     8356   8610   7629   -394    239   -158       O  
ATOM    898  N   VAL A 348     -10.668  52.865  29.537  1.00 35.15           N  
ANISOU  898  N   VAL A 348     4719   4926   3712   -457    136   -294       N  
ATOM    899  CA  VAL A 348      -9.768  53.517  28.599  1.00 27.95           C  
ANISOU  899  CA  VAL A 348     3850   4031   2738   -487    127   -341       C  
ATOM    900  C   VAL A 348     -10.150  54.974  28.363  1.00 33.30           C  
ANISOU  900  C   VAL A 348     4588   4730   3335   -486    104   -336       C  
ATOM    901  O   VAL A 348     -11.222  55.273  27.842  1.00 38.72           O  
ANISOU  901  O   VAL A 348     5285   5409   4020   -484     70   -338       O  
ATOM    902  CB  VAL A 348      -9.742  52.780  27.255  1.00 30.51           C  
ANISOU  902  CB  VAL A 348     4172   4337   3085   -523    121   -399       C  
ATOM    903  CG1 VAL A 348      -8.711  53.404  26.338  1.00 25.44           C  
ANISOU  903  CG1 VAL A 348     3585   3706   2373   -562    134   -450       C  
ATOM    904  CG2 VAL A 348      -9.437  51.310  27.475  1.00 28.66           C  
ANISOU  904  CG2 VAL A 348     3876   4073   2940   -520    142   -406       C  
ATOM    905  N   TYR A 349      -9.257  55.880  28.756  1.00 36.94           N  
ANISOU  905  N   TYR A 349     5087   5211   3738   -488    114   -333       N  
ATOM    906  CA  TYR A 349      -9.486  57.305  28.575  1.00 26.45           C  
ANISOU  906  CA  TYR A 349     3822   3895   2331   -489     94   -327       C  
ATOM    907  C   TYR A 349      -8.391  57.940  27.729  1.00 32.52           C  
ANISOU  907  C   TYR A 349     4649   4670   3036   -535    107   -371       C  
ATOM    908  O   TYR A 349      -7.206  57.708  27.956  1.00 33.89           O  
ANISOU  908  O   TYR A 349     4804   4851   3224   -551    139   -391       O  
ATOM    909  CB  TYR A 349      -9.570  58.016  29.926  1.00 23.15           C  
ANISOU  909  CB  TYR A 349     3409   3491   1895   -452    102   -281       C  
ATOM    910  CG  TYR A 349     -10.559  57.404  30.891  1.00 30.52           C  
ANISOU  910  CG  TYR A 349     4295   4414   2885   -415    114   -240       C  
ATOM    911  CD1 TYR A 349     -11.929  57.505  30.673  1.00 25.63           C  
ANISOU  911  CD1 TYR A 349     3658   3782   2298   -399     99   -233       C  
ATOM    912  CD2 TYR A 349     -10.124  56.738  32.031  1.00 26.54           C  
ANISOU  912  CD2 TYR A 349     3769   3907   2408   -398    140   -209       C  
ATOM    913  CE1 TYR A 349     -12.837  56.949  31.554  1.00 24.30           C  
ANISOU  913  CE1 TYR A 349     3441   3600   2191   -373    129   -201       C  
ATOM    914  CE2 TYR A 349     -11.028  56.180  32.922  1.00 29.47           C  
ANISOU  914  CE2 TYR A 349     4114   4262   2821   -372    166   -169       C  
ATOM    915  CZ  TYR A 349     -12.382  56.290  32.675  1.00 29.06           C  
ANISOU  915  CZ  TYR A 349     4036   4200   2806   -364    170   -167       C  
ATOM    916  OH  TYR A 349     -13.289  55.739  33.550  1.00 35.66           O  
ANISOU  916  OH  TYR A 349     4840   5015   3692   -347    214   -135       O  
ATOM    917  N   THR A 350      -8.799  58.744  26.753  1.00 31.82           N  
ANISOU  917  N   THR A 350     4611   4553   2927   -534     76   -371       N  
ATOM    918  CA  THR A 350      -7.847  59.498  25.955  1.00 32.55           C  
ANISOU  918  CA  THR A 350     4738   4615   3014   -547     92   -383       C  
ATOM    919  C   THR A 350      -7.733  60.919  26.488  1.00 36.44           C  
ANISOU  919  C   THR A 350     5254   5097   3496   -513     80   -346       C  
ATOM    920  O   THR A 350      -8.734  61.538  26.847  1.00 32.31           O  
ANISOU  920  O   THR A 350     4746   4572   2958   -476     42   -316       O  
ATOM    921  CB  THR A 350      -8.244  59.547  24.472  1.00 31.27           C  
ANISOU  921  CB  THR A 350     4631   4419   2830   -568     69   -403       C  
ATOM    922  CG2 THR A 350      -8.317  58.144  23.891  1.00 36.10           C  
ANISOU  922  CG2 THR A 350     5225   5037   3455   -605     82   -448       C  
ATOM    923  OG1 THR A 350      -9.517  60.186  24.342  1.00 30.03           O  
ANISOU  923  OG1 THR A 350     4508   4252   2648   -536      2   -377       O  
ATOM    924  N   LEU A 351      -6.506  61.425  26.555  1.00 39.22           N  
ANISOU  924  N   LEU A 351     5605   5441   3855   -531    114   -356       N  
ATOM    925  CA  LEU A 351      -6.265  62.786  27.010  1.00 36.74           C  
ANISOU  925  CA  LEU A 351     5314   5114   3531   -507    106   -330       C  
ATOM    926  C   LEU A 351      -5.488  63.570  25.956  1.00 32.97           C  
ANISOU  926  C   LEU A 351     4883   4605   3040   -548    129   -347       C  
ATOM    927  O   LEU A 351      -4.466  63.100  25.460  1.00 25.84           O  
ANISOU  927  O   LEU A 351     3971   3701   2147   -601    179   -387       O  
ATOM    928  CB  LEU A 351      -5.493  62.791  28.340  1.00 38.29           C  
ANISOU  928  CB  LEU A 351     5471   5335   3744   -498    121   -326       C  
ATOM    929  CG  LEU A 351      -5.748  61.681  29.364  1.00 33.93           C  
ANISOU  929  CG  LEU A 351     4875   4817   3202   -482    119   -319       C  
ATOM    930  CD1 LEU A 351      -4.828  61.856  30.562  1.00 21.74           C  
ANISOU  930  CD1 LEU A 351     3313   3290   1659   -477    122   -317       C  
ATOM    931  CD2 LEU A 351      -7.203  61.645  29.808  1.00 34.06           C  
ANISOU  931  CD2 LEU A 351     4898   4839   3206   -441     93   -282       C  
ATOM    932  N   PRO A 352      -5.968  64.776  25.614  1.00 32.34           N  
ANISOU  932  N   PRO A 352     4856   4499   2934   -529    100   -322       N  
ATOM    933  CA  PRO A 352      -5.313  65.628  24.616  1.00 30.87           C  
ANISOU  933  CA  PRO A 352     4730   4277   2724   -574    124   -332       C  
ATOM    934  C   PRO A 352      -4.012  66.216  25.167  1.00 31.62           C  
ANISOU  934  C   PRO A 352     4809   4373   2831   -607    171   -347       C  
ATOM    935  O   PRO A 352      -3.744  66.042  26.352  1.00 37.18           O  
ANISOU  935  O   PRO A 352     5462   5106   3559   -585    168   -345       O  
ATOM    936  CB  PRO A 352      -6.358  66.719  24.360  1.00 31.09           C  
ANISOU  936  CB  PRO A 352     4813   4280   2719   -537     68   -298       C  
ATOM    937  CG  PRO A 352      -7.069  66.846  25.654  1.00 23.74           C  
ANISOU  937  CG  PRO A 352     3838   3377   1805   -477     36   -276       C  
ATOM    938  CD  PRO A 352      -7.132  65.443  26.226  1.00 22.49           C  
ANISOU  938  CD  PRO A 352     3616   3253   1675   -471     49   -287       C  
ATOM    939  N   PRO A 353      -3.211  66.882  24.319  1.00 41.73           N  
ANISOU  939  N   PRO A 353     6142   5622   4093   -668    213   -364       N  
ATOM    940  CA  PRO A 353      -1.986  67.503  24.833  1.00 32.28           C  
ANISOU  940  CA  PRO A 353     4932   4425   2907   -712    258   -387       C  
ATOM    941  C   PRO A 353      -2.273  68.531  25.916  1.00 32.07           C  
ANISOU  941  C   PRO A 353     4904   4402   2878   -663    216   -354       C  
ATOM    942  O   PRO A 353      -3.326  69.170  25.875  1.00 34.12           O  
ANISOU  942  O   PRO A 353     5198   4647   3118   -613    166   -316       O  
ATOM    943  CB  PRO A 353      -1.388  68.180  23.594  1.00 31.80           C  
ANISOU  943  CB  PRO A 353     4949   4318   2814   -787    309   -404       C  
ATOM    944  CG  PRO A 353      -1.920  67.406  22.451  1.00 32.80           C  
ANISOU  944  CG  PRO A 353     5109   4430   2922   -796    310   -408       C  
ATOM    945  CD  PRO A 353      -3.310  67.000  22.853  1.00 37.58           C  
ANISOU  945  CD  PRO A 353     5693   5056   3530   -711    228   -371       C  
ATOM    946  N   SER A 354      -1.360  68.669  26.870  1.00 24.02           N  
ANISOU  946  N   SER A 354     3846   3404   1878   -680    234   -376       N  
ATOM    947  CA  SER A 354      -1.407  69.776  27.814  1.00 18.52           C  
ANISOU  947  CA  SER A 354     3160   2704   1173   -649    204   -354       C  
ATOM    948  C   SER A 354      -1.348  71.074  27.036  1.00 29.13           C  
ANISOU  948  C   SER A 354     4581   4000   2486   -684    217   -344       C  
ATOM    949  O   SER A 354      -0.622  71.165  26.044  1.00 31.09           O  
ANISOU  949  O   SER A 354     4866   4222   2722   -761    272   -371       O  
ATOM    950  CB  SER A 354      -0.251  69.709  28.809  1.00 29.47           C  
ANISOU  950  CB  SER A 354     4504   4118   2576   -680    222   -391       C  
ATOM    951  OG  SER A 354      -0.353  70.739  29.781  1.00 36.13           O  
ANISOU  951  OG  SER A 354     5363   4957   3408   -647    187   -370       O  
ATOM    952  N   ARG A 355      -2.111  72.068  27.484  1.00 35.21           N  
ANISOU  952  N   ARG A 355     5381   4756   3241   -633    172   -308       N  
ATOM    953  CA  ARG A 355      -2.133  73.378  26.836  1.00 38.47           C  
ANISOU  953  CA  ARG A 355     5877   5119   3620   -664    175   -296       C  
ATOM    954  C   ARG A 355      -0.722  73.920  26.628  1.00 39.29           C  
ANISOU  954  C   ARG A 355     6009   5202   3718   -759    239   -332       C  
ATOM    955  O   ARG A 355      -0.417  74.500  25.586  1.00 36.13           O  
ANISOU  955  O   ARG A 355     5685   4755   3288   -824    276   -336       O  
ATOM    956  CB  ARG A 355      -2.960  74.372  27.660  1.00 38.23           C  
ANISOU  956  CB  ARG A 355     5862   5084   3581   -600    124   -265       C  
ATOM    957  CG  ARG A 355      -4.446  74.051  27.709  1.00 30.79           C  
ANISOU  957  CG  ARG A 355     4906   4155   2637   -524     70   -237       C  
ATOM    958  CD  ARG A 355      -5.282  75.189  27.162  1.00 36.99           C  
ANISOU  958  CD  ARG A 355     5772   4896   3387   -512     34   -214       C  
ATOM    959  NE  ARG A 355      -5.766  76.080  28.211  1.00 38.97           N  
ANISOU  959  NE  ARG A 355     6022   5149   3636   -467      7   -203       N  
ATOM    960  CZ  ARG A 355      -6.036  77.366  28.020  1.00 40.03           C  
ANISOU  960  CZ  ARG A 355     6233   5236   3741   -473    -13   -190       C  
ATOM    961  NH1 ARG A 355      -6.481  78.110  29.022  1.00 50.72           N1+
ANISOU  961  NH1 ARG A 355     7586   6592   5093   -432    -33   -186       N1+
ATOM    962  NH2 ARG A 355      -5.854  77.912  26.825  1.00 25.00           N  
ANISOU  962  NH2 ARG A 355     4419   3276   1804   -524    -11   -183       N  
ATOM    963  N   GLU A 356       0.135  73.707  27.621  1.00 37.07           N  
ANISOU  963  N   GLU A 356     5670   4954   3461   -774    255   -363       N  
ATOM    964  CA  GLU A 356       1.506  74.195  27.581  1.00 33.44           C  
ANISOU  964  CA  GLU A 356     5223   4483   2999   -872    318   -413       C  
ATOM    965  C   GLU A 356       2.368  73.503  26.527  1.00 27.72           C  
ANISOU  965  C   GLU A 356     4495   3753   2283   -964    402   -463       C  
ATOM    966  O   GLU A 356       3.320  74.095  26.019  1.00 39.97           O  
ANISOU  966  O   GLU A 356     6084   5275   3826  -1062    476   -504       O  
ATOM    967  CB  GLU A 356       2.164  74.035  28.953  1.00 31.23           C  
ANISOU  967  CB  GLU A 356     4877   4246   2741   -863    300   -444       C  
ATOM    968  CG  GLU A 356       1.747  75.074  29.972  1.00 28.26           C  
ANISOU  968  CG  GLU A 356     4525   3862   2350   -809    245   -414       C  
ATOM    969  CD  GLU A 356       2.605  75.030  31.220  1.00 46.47           C  
ANISOU  969  CD  GLU A 356     6786   6202   4667   -821    227   -455       C  
ATOM    970  OE1 GLU A 356       2.872  73.913  31.714  1.00 56.20           O  
ANISOU  970  OE1 GLU A 356     7954   7478   5920   -807    213   -479       O  
ATOM    971  OE2 GLU A 356       3.018  76.107  31.701  1.00 46.26           O1-
ANISOU  971  OE2 GLU A 356     6795   6157   4625   -846    221   -467       O1-
ATOM    972  N   GLU A 357       2.040  72.257  26.194  1.00 29.17           N  
ANISOU  972  N   GLU A 357     4635   3962   2485   -938    400   -467       N  
ATOM    973  CA  GLU A 357       2.845  71.504  25.233  1.00 29.58           C  
ANISOU  973  CA  GLU A 357     4677   4011   2551  -1021    486   -523       C  
ATOM    974  C   GLU A 357       2.649  72.029  23.818  1.00 33.75           C  
ANISOU  974  C   GLU A 357     5307   4478   3039  -1070    524   -506       C  
ATOM    975  O   GLU A 357       3.420  71.704  22.916  1.00 38.60           O  
ANISOU  975  O   GLU A 357     5937   5072   3656  -1158    613   -556       O  
ATOM    976  CB  GLU A 357       2.515  70.011  25.283  1.00 31.17           C  
ANISOU  976  CB  GLU A 357     4808   4253   2781   -979    471   -534       C  
ATOM    977  CG  GLU A 357       3.585  69.132  24.635  1.00 35.83           C  
ANISOU  977  CG  GLU A 357     5356   4853   3405  -1066    570   -617       C  
ATOM    978  CD  GLU A 357       3.222  67.659  24.617  1.00 38.56           C  
ANISOU  978  CD  GLU A 357     5641   5232   3778  -1026    556   -629       C  
ATOM    979  OE1 GLU A 357       4.129  66.818  24.436  1.00 30.15           O  
ANISOU  979  OE1 GLU A 357     4511   4186   2757  -1082    630   -711       O  
ATOM    980  OE2 GLU A 357       2.023  67.344  24.776  1.00 41.08           O1-
ANISOU  980  OE2 GLU A 357     5971   5556   4079   -942    477   -565       O1-
ATOM    981  N   MET A 358       1.633  72.866  23.633  1.00 37.01           N  
ANISOU  981  N   MET A 358     5793   4857   3412  -1017    458   -443       N  
ATOM    982  CA  MET A 358       1.302  73.385  22.309  1.00 42.33           C  
ANISOU  982  CA  MET A 358     6580   5468   4036  -1055    473   -421       C  
ATOM    983  C   MET A 358       2.299  74.414  21.784  1.00 45.52           C  
ANISOU  983  C   MET A 358     7066   5817   4414  -1166    556   -449       C  
ATOM    984  O   MET A 358       2.120  74.949  20.689  1.00 50.65           O  
ANISOU  984  O   MET A 358     7830   6404   5012  -1209    573   -432       O  
ATOM    985  CB  MET A 358      -0.100  73.993  22.320  1.00 44.65           C  
ANISOU  985  CB  MET A 358     6923   5743   4299   -967    375   -356       C  
ATOM    986  CG  MET A 358      -1.202  72.967  22.522  1.00 49.31           C  
ANISOU  986  CG  MET A 358     7453   6376   4908   -875    307   -334       C  
ATOM    987  SD  MET A 358      -1.213  71.715  21.226  1.00 46.02           S  
ANISOU  987  SD  MET A 358     7053   5954   4478   -911    342   -357       S  
ATOM    988  CE  MET A 358      -1.791  72.670  19.825  1.00 68.88           C  
ANISOU  988  CE  MET A 358    10105   8769   7295   -943    321   -325       C  
ATOM    989  N   THR A 359       3.346  74.691  22.554  1.00 46.97           N  
ANISOU  989  N   THR A 359     7199   6021   4629  -1218    607   -496       N  
ATOM    990  CA  THR A 359       4.410  75.582  22.098  1.00 42.45           C  
ANISOU  990  CA  THR A 359     6692   5397   4040  -1341    705   -538       C  
ATOM    991  C   THR A 359       5.539  74.793  21.449  1.00 45.15           C  
ANISOU  991  C   THR A 359     6998   5742   4416  -1446    830   -622       C  
ATOM    992  O   THR A 359       6.499  75.375  20.948  1.00 50.46           O  
ANISOU  992  O   THR A 359     7717   6369   5085  -1563    937   -674       O  
ATOM    993  CB  THR A 359       4.988  76.425  23.253  1.00 39.96           C  
ANISOU  993  CB  THR A 359     6344   5098   3742  -1357    703   -558       C  
ATOM    994  CG2 THR A 359       3.928  77.344  23.826  1.00 41.68           C  
ANISOU  994  CG2 THR A 359     6609   5301   3929  -1263    595   -483       C  
ATOM    995  OG1 THR A 359       5.476  75.559  24.285  1.00 47.85           O  
ANISOU  995  OG1 THR A 359     7211   6173   4798  -1333    698   -605       O  
ATOM    996  N   LYS A 360       5.421  73.468  21.466  1.00 39.95           N  
ANISOU  996  N   LYS A 360     6253   5132   3793  -1406    824   -642       N  
ATOM    997  CA  LYS A 360       6.443  72.597  20.891  1.00 35.79           C  
ANISOU  997  CA  LYS A 360     5676   4611   3313  -1495    944   -732       C  
ATOM    998  C   LYS A 360       6.083  72.149  19.472  1.00 43.97           C  
ANISOU  998  C   LYS A 360     6797   5599   4310  -1519    975   -719       C  
ATOM    999  O   LYS A 360       4.934  72.275  19.044  1.00 43.12           O  
ANISOU  999  O   LYS A 360     6768   5471   4145  -1450    886   -641       O  
ATOM   1000  CB  LYS A 360       6.658  71.373  21.785  1.00 34.74           C  
ANISOU 1000  CB  LYS A 360     5394   4557   3248  -1446    927   -777       C  
ATOM   1001  CG  LYS A 360       6.933  71.683  23.247  1.00 22.41           C  
ANISOU 1001  CG  LYS A 360     3752   3047   1716  -1411    878   -792       C  
ATOM   1002  CD  LYS A 360       8.293  72.319  23.456  1.00 24.91           C  
ANISOU 1002  CD  LYS A 360     4033   3356   2074  -1525    984   -889       C  
ATOM   1003  CE  LYS A 360       8.532  72.586  24.935  1.00 35.71           C  
ANISOU 1003  CE  LYS A 360     5326   4777   3464  -1485    917   -911       C  
ATOM   1004  NZ  LYS A 360       9.769  73.385  25.155  1.00 48.03           N1+
ANISOU 1004  NZ  LYS A 360     6858   6326   5065  -1594   1009  -1010       N1+
ATOM   1005  N   ASN A 361       7.069  71.619  18.752  1.00 50.19           N  
ANISOU 1005  N   ASN A 361     7568   6369   5134  -1618   1104   -804       N  
ATOM   1006  CA  ASN A 361       6.853  71.133  17.390  1.00 49.38           C  
ANISOU 1006  CA  ASN A 361     7552   6218   4991  -1652   1146   -803       C  
ATOM   1007  C   ASN A 361       6.119  69.802  17.377  1.00 48.34           C  
ANISOU 1007  C   ASN A 361     7360   6134   4872  -1565   1083   -786       C  
ATOM   1008  O   ASN A 361       5.347  69.512  16.462  1.00 45.34           O  
ANISOU 1008  O   ASN A 361     7067   5725   4434  -1543   1048   -744       O  
ATOM   1009  CB  ASN A 361       8.182  70.998  16.650  1.00 54.86           C  
ANISOU 1009  CB  ASN A 361     8245   6870   5729  -1789   1317   -911       C  
ATOM   1010  CG  ASN A 361       8.889  72.326  16.476  1.00 63.95           C  
ANISOU 1010  CG  ASN A 361     9478   7958   6861  -1890   1393   -934       C  
ATOM   1011  ND2 ASN A 361      10.216  72.302  16.512  1.00 69.14           N  
ANISOU 1011  ND2 ASN A 361    10063   8605   7602  -1996   1535  -1051       N  
ATOM   1012  OD1 ASN A 361       8.247  73.364  16.318  1.00 68.03           O  
ANISOU 1012  OD1 ASN A 361    10117   8432   7297  -1874   1327   -856       O  
ATOM   1013  N   GLN A 362       6.369  68.993  18.398  1.00 47.90           N  
ANISOU 1013  N   GLN A 362     7160   6148   4891  -1521   1068   -823       N  
ATOM   1014  CA  GLN A 362       5.661  67.735  18.561  1.00 46.78           C  
ANISOU 1014  CA  GLN A 362     6956   6052   4766  -1437   1004   -808       C  
ATOM   1015  C   GLN A 362       4.854  67.748  19.853  1.00 39.24           C  
ANISOU 1015  C   GLN A 362     5942   5152   3816  -1325    877   -748       C  
ATOM   1016  O   GLN A 362       5.264  68.351  20.845  1.00 42.40           O  
ANISOU 1016  O   GLN A 362     6296   5575   4239  -1322    866   -757       O  
ATOM   1017  CB  GLN A 362       6.641  66.561  18.552  1.00 52.98           C  
ANISOU 1017  CB  GLN A 362     7626   6863   5640  -1483   1106   -915       C  
ATOM   1018  CG  GLN A 362       7.500  66.489  17.301  1.00 57.35           C  
ANISOU 1018  CG  GLN A 362     8228   7357   6203  -1598   1247   -986       C  
ATOM   1019  CD  GLN A 362       7.746  65.062  16.850  1.00 70.21           C  
ANISOU 1019  CD  GLN A 362     9788   8998   7890  -1603   1304  -1054       C  
ATOM   1020  NE2 GLN A 362       7.075  64.657  15.775  1.00 73.69           N  
ANISOU 1020  NE2 GLN A 362    10329   9406   8264  -1599   1292  -1017       N  
ATOM   1021  OE1 GLN A 362       8.523  64.329  17.462  1.00 73.05           O  
ANISOU 1021  OE1 GLN A 362    10005   9395   8357  -1608   1357  -1143       O  
ATOM   1022  N   VAL A 363       3.698  67.095  19.834  1.00 30.65           N  
ANISOU 1022  N   VAL A 363     4858   4081   2706  -1236    786   -693       N  
ATOM   1023  CA  VAL A 363       2.854  67.030  21.019  1.00 32.75           C  
ANISOU 1023  CA  VAL A 363     5073   4392   2980  -1132    674   -639       C  
ATOM   1024  C   VAL A 363       2.534  65.591  21.389  1.00 35.99           C  
ANISOU 1024  C   VAL A 363     5398   4847   3429  -1083    650   -657       C  
ATOM   1025  O   VAL A 363       2.714  64.676  20.585  1.00 32.99           O  
ANISOU 1025  O   VAL A 363     5014   4460   3061  -1115    702   -699       O  
ATOM   1026  CB  VAL A 363       1.544  67.804  20.827  1.00 35.53           C  
ANISOU 1026  CB  VAL A 363     5510   4718   3274  -1063    576   -551       C  
ATOM   1027  CG1 VAL A 363       1.828  69.292  20.713  1.00 35.51           C  
ANISOU 1027  CG1 VAL A 363     5584   4671   3236  -1102    588   -531       C  
ATOM   1028  CG2 VAL A 363       0.803  67.288  19.602  1.00 35.31           C  
ANISOU 1028  CG2 VAL A 363     5550   4660   3205  -1060    563   -535       C  
ATOM   1029  N   SER A 364       2.056  65.399  22.613  1.00 32.17           N  
ANISOU 1029  N   SER A 364     4853   4406   2963  -1007    574   -628       N  
ATOM   1030  CA  SER A 364       1.798  64.062  23.122  1.00 30.53           C  
ANISOU 1030  CA  SER A 364     4568   4240   2792   -965    551   -647       C  
ATOM   1031  C   SER A 364       0.304  63.788  23.225  1.00 33.67           C  
ANISOU 1031  C   SER A 364     4992   4641   3162   -880    457   -574       C  
ATOM   1032  O   SER A 364      -0.438  64.562  23.826  1.00 33.03           O  
ANISOU 1032  O   SER A 364     4932   4558   3060   -822    389   -515       O  
ATOM   1033  CB  SER A 364       2.456  63.874  24.491  1.00 28.15           C  
ANISOU 1033  CB  SER A 364     4179   3987   2532   -953    542   -683       C  
ATOM   1034  OG  SER A 364       3.753  64.443  24.525  1.00 32.07           O  
ANISOU 1034  OG  SER A 364     4650   4480   3054  -1030    618   -753       O  
ATOM   1035  N   LEU A 365      -0.134  62.687  22.623  1.00 32.57           N  
ANISOU 1035  N   LEU A 365     4846   4502   3027   -875    460   -589       N  
ATOM   1036  CA  LEU A 365      -1.490  62.197  22.819  1.00 29.01           C  
ANISOU 1036  CA  LEU A 365     4399   4061   2563   -805    381   -540       C  
ATOM   1037  C   LEU A 365      -1.444  61.048  23.818  1.00 29.33           C  
ANISOU 1037  C   LEU A 365     4353   4146   2645   -780    373   -563       C  
ATOM   1038  O   LEU A 365      -0.686  60.096  23.647  1.00 32.52           O  
ANISOU 1038  O   LEU A 365     4710   4563   3085   -820    430   -630       O  
ATOM   1039  CB  LEU A 365      -2.114  61.751  21.496  1.00 27.10           C  
ANISOU 1039  CB  LEU A 365     4218   3790   2290   -819    378   -543       C  
ATOM   1040  CG  LEU A 365      -2.071  62.765  20.347  1.00 30.46           C  
ANISOU 1040  CG  LEU A 365     4744   4166   2663   -856    392   -528       C  
ATOM   1041  CD1 LEU A 365      -2.929  62.292  19.179  1.00 35.58           C  
ANISOU 1041  CD1 LEU A 365     5460   4790   3270   -855    362   -523       C  
ATOM   1042  CD2 LEU A 365      -2.495  64.153  20.805  1.00 33.30           C  
ANISOU 1042  CD2 LEU A 365     5139   4514   2998   -819    339   -473       C  
ATOM   1043  N   THR A 366      -2.253  61.142  24.867  1.00 27.17           N  
ANISOU 1043  N   THR A 366     4062   3895   2369   -717    307   -513       N  
ATOM   1044  CA  THR A 366      -2.154  60.204  25.977  1.00 20.43           C  
ANISOU 1044  CA  THR A 366     3139   3082   1542   -697    296   -527       C  
ATOM   1045  C   THR A 366      -3.354  59.268  26.073  1.00 32.62           C  
ANISOU 1045  C   THR A 366     4675   4637   3084   -661    257   -503       C  
ATOM   1046  O   THR A 366      -4.504  59.708  26.035  1.00 34.20           O  
ANISOU 1046  O   THR A 366     4910   4825   3261   -622    209   -452       O  
ATOM   1047  CB  THR A 366      -2.004  60.951  27.312  1.00 23.97           C  
ANISOU 1047  CB  THR A 366     3574   3549   1985   -661    261   -492       C  
ATOM   1048  CG2 THR A 366      -2.049  59.985  28.481  1.00 15.82           C  
ANISOU 1048  CG2 THR A 366     2491   2557    964   -637    237   -495       C  
ATOM   1049  OG1 THR A 366      -0.760  61.662  27.323  1.00 19.63           O  
ANISOU 1049  OG1 THR A 366     3020   2997   1443   -707    300   -533       O  
ATOM   1050  N   CYS A 367      -3.078  57.973  26.202  1.00 34.35           N  
ANISOU 1050  N   CYS A 367     4845   4878   3330   -680    280   -551       N  
ATOM   1051  CA  CYS A 367      -4.118  56.989  26.465  1.00 32.96           C  
ANISOU 1051  CA  CYS A 367     4654   4717   3153   -657    250   -536       C  
ATOM   1052  C   CYS A 367      -3.932  56.381  27.847  1.00 35.92           C  
ANISOU 1052  C   CYS A 367     4952   5096   3599   -605    225   -500       C  
ATOM   1053  O   CYS A 367      -2.999  55.613  28.080  1.00 26.88           O  
ANISOU 1053  O   CYS A 367     3742   3940   2533   -602    240   -530       O  
ATOM   1054  CB  CYS A 367      -4.110  55.890  25.397  1.00 26.10           C  
ANISOU 1054  CB  CYS A 367     3773   3829   2315   -689    281   -591       C  
ATOM   1055  SG  CYS A 367      -5.464  54.694  25.520  1.00 33.89           S  
ANISOU 1055  SG  CYS A 367     4720   4800   3355   -647    234   -554       S  
ATOM   1056  N   LEU A 368      -4.822  56.740  28.767  1.00 38.68           N  
ANISOU 1056  N   LEU A 368     5317   5456   3924   -561    186   -435       N  
ATOM   1057  CA  LEU A 368      -4.819  56.151  30.098  1.00 30.04           C  
ANISOU 1057  CA  LEU A 368     4177   4358   2881   -512    163   -389       C  
ATOM   1058  C   LEU A 368      -5.688  54.901  30.132  1.00 36.62           C  
ANISOU 1058  C   LEU A 368     4973   5169   3772   -491    158   -367       C  
ATOM   1059  O   LEU A 368      -6.858  54.931  29.744  1.00 39.44           O  
ANISOU 1059  O   LEU A 368     5348   5526   4113   -490    153   -351       O  
ATOM   1060  CB  LEU A 368      -5.299  57.166  31.136  1.00 21.75           C  
ANISOU 1060  CB  LEU A 368     3170   3323   1770   -482    140   -336       C  
ATOM   1061  CG  LEU A 368      -5.693  56.623  32.512  1.00 26.43           C  
ANISOU 1061  CG  LEU A 368     3750   3906   2386   -434    122   -277       C  
ATOM   1062  CD1 LEU A 368      -4.522  55.930  33.180  1.00 28.08           C  
ANISOU 1062  CD1 LEU A 368     3921   4100   2649   -421    100   -283       C  
ATOM   1063  CD2 LEU A 368      -6.226  57.741  33.395  1.00 28.79           C  
ANISOU 1063  CD2 LEU A 368     4104   4220   2613   -412    114   -236       C  
ATOM   1064  N   VAL A 369      -5.097  53.801  30.586  1.00 33.26           N  
ANISOU 1064  N   VAL A 369     4493   4720   3424   -474    155   -369       N  
ATOM   1065  CA  VAL A 369      -5.813  52.543  30.732  1.00 29.42           C  
ANISOU 1065  CA  VAL A 369     3972   4204   3000   -456    153   -345       C  
ATOM   1066  C   VAL A 369      -5.678  52.059  32.172  1.00 34.20           C  
ANISOU 1066  C   VAL A 369     4572   4791   3633   -413    130   -286       C  
ATOM   1067  O   VAL A 369      -4.586  51.697  32.607  1.00 35.52           O  
ANISOU 1067  O   VAL A 369     4715   4941   3842   -399    107   -298       O  
ATOM   1068  CB  VAL A 369      -5.280  51.466  29.774  1.00 28.86           C  
ANISOU 1068  CB  VAL A 369     3854   4107   3003   -479    172   -405       C  
ATOM   1069  CG1 VAL A 369      -6.134  50.220  29.857  1.00 27.09           C  
ANISOU 1069  CG1 VAL A 369     3600   3849   2843   -465    170   -382       C  
ATOM   1070  CG2 VAL A 369      -5.248  51.989  28.348  1.00 29.28           C  
ANISOU 1070  CG2 VAL A 369     3938   4177   3012   -528    199   -467       C  
ATOM   1071  N   LYS A 370      -6.781  52.057  32.915  1.00 26.93           N  
ANISOU 1071  N   LYS A 370     3677   3865   2690   -393    135   -227       N  
ATOM   1072  CA  LYS A 370      -6.713  51.716  34.333  1.00 31.04           C  
ANISOU 1072  CA  LYS A 370     4222   4363   3208   -358    120   -165       C  
ATOM   1073  C   LYS A 370      -7.731  50.665  34.757  1.00 29.46           C  
ANISOU 1073  C   LYS A 370     4017   4126   3052   -350    145   -120       C  
ATOM   1074  O   LYS A 370      -8.700  50.397  34.051  1.00 27.67           O  
ANISOU 1074  O   LYS A 370     3762   3897   2854   -368    173   -133       O  
ATOM   1075  CB  LYS A 370      -6.893  52.971  35.191  1.00 30.75           C  
ANISOU 1075  CB  LYS A 370     4247   4354   3081   -345    117   -132       C  
ATOM   1076  CG  LYS A 370      -8.186  53.718  34.930  1.00 32.96           C  
ANISOU 1076  CG  LYS A 370     4545   4656   3323   -352    152   -123       C  
ATOM   1077  CD  LYS A 370      -8.516  54.690  36.056  1.00 32.90           C  
ANISOU 1077  CD  LYS A 370     4600   4661   3240   -331    161    -81       C  
ATOM   1078  CE  LYS A 370      -8.968  53.956  37.309  1.00 31.86           C  
ANISOU 1078  CE  LYS A 370     4501   4494   3108   -311    185    -21       C  
ATOM   1079  NZ  LYS A 370      -9.545  54.885  38.320  1.00 29.96           N1+
ANISOU 1079  NZ  LYS A 370     4327   4263   2792   -297    216     13       N1+
ATOM   1080  N   GLY A 371      -7.486  50.070  35.919  1.00 26.18           N  
ANISOU 1080  N   GLY A 371     3634   3673   2639   -324    131    -68       N  
ATOM   1081  CA  GLY A 371      -8.428  49.158  36.533  1.00 25.66           C  
ANISOU 1081  CA  GLY A 371     3584   3565   2602   -321    166    -15       C  
ATOM   1082  C   GLY A 371      -8.532  47.793  35.882  1.00 35.54           C  
ANISOU 1082  C   GLY A 371     4780   4772   3952   -333    171    -33       C  
ATOM   1083  O   GLY A 371      -9.529  47.093  36.069  1.00 33.24           O  
ANISOU 1083  O   GLY A 371     4486   4448   3697   -344    214     -3       O  
ATOM   1084  N   PHE A 372      -7.516  47.397  35.122  1.00 35.84           N  
ANISOU 1084  N   PHE A 372     4771   4804   4041   -333    135    -87       N  
ATOM   1085  CA  PHE A 372      -7.562  46.080  34.499  1.00 29.61           C  
ANISOU 1085  CA  PHE A 372     3932   3968   3349   -343    141   -111       C  
ATOM   1086  C   PHE A 372      -6.788  45.033  35.289  1.00 30.41           C  
ANISOU 1086  C   PHE A 372     4047   4005   3504   -312    100    -79       C  
ATOM   1087  O   PHE A 372      -5.791  45.331  35.948  1.00 38.24           O  
ANISOU 1087  O   PHE A 372     5063   4993   4474   -283     47    -68       O  
ATOM   1088  CB  PHE A 372      -7.053  46.128  33.055  1.00 27.34           C  
ANISOU 1088  CB  PHE A 372     3587   3704   3098   -367    140   -200       C  
ATOM   1089  CG  PHE A 372      -5.635  46.609  32.902  1.00 33.37           C  
ANISOU 1089  CG  PHE A 372     4335   4485   3858   -357    108   -245       C  
ATOM   1090  CD1 PHE A 372      -4.581  45.710  32.898  1.00 32.55           C  
ANISOU 1090  CD1 PHE A 372     4190   4335   3842   -338     79   -275       C  
ATOM   1091  CD2 PHE A 372      -5.359  47.954  32.714  1.00 35.79           C  
ANISOU 1091  CD2 PHE A 372     4663   4847   4088   -369    110   -265       C  
ATOM   1092  CE1 PHE A 372      -3.278  46.142  32.736  1.00 33.09           C  
ANISOU 1092  CE1 PHE A 372     4226   4416   3931   -332     55   -327       C  
ATOM   1093  CE2 PHE A 372      -4.056  48.395  32.552  1.00 31.75           C  
ANISOU 1093  CE2 PHE A 372     4129   4348   3587   -368     89   -313       C  
ATOM   1094  CZ  PHE A 372      -3.013  47.487  32.565  1.00 28.94           C  
ANISOU 1094  CZ  PHE A 372     3719   3948   3328   -350     64   -347       C  
ATOM   1095  N   TYR A 373      -7.290  43.808  35.228  1.00 31.00           N  
ANISOU 1095  N   TYR A 373     4108   4021   3651   -318    118    -63       N  
ATOM   1096  CA  TYR A 373      -6.619  42.647  35.790  1.00 38.22           C  
ANISOU 1096  CA  TYR A 373     5032   4858   4631   -289     75    -37       C  
ATOM   1097  C   TYR A 373      -6.982  41.431  34.946  1.00 42.11           C  
ANISOU 1097  C   TYR A 373     5470   5303   5228   -309    100    -72       C  
ATOM   1098  O   TYR A 373      -8.133  41.280  34.549  1.00 43.49           O  
ANISOU 1098  O   TYR A 373     5632   5483   5409   -343    154    -71       O  
ATOM   1099  CB  TYR A 373      -7.016  42.430  37.250  1.00 37.49           C  
ANISOU 1099  CB  TYR A 373     5038   4721   4485   -273     72     62       C  
ATOM   1100  CG  TYR A 373      -6.193  41.370  37.946  1.00 39.59           C  
ANISOU 1100  CG  TYR A 373     5339   4901   4803   -235      3     98       C  
ATOM   1101  CD1 TYR A 373      -6.522  40.026  37.841  1.00 45.56           C  
ANISOU 1101  CD1 TYR A 373     6088   5578   5644   -241     16    114       C  
ATOM   1102  CD2 TYR A 373      -5.082  41.714  38.704  1.00 36.73           C  
ANISOU 1102  CD2 TYR A 373     5017   4529   4410   -193    -85    114       C  
ATOM   1103  CE1 TYR A 373      -5.767  39.057  38.468  1.00 40.99           C  
ANISOU 1103  CE1 TYR A 373     5547   4910   5116   -202    -57    148       C  
ATOM   1104  CE2 TYR A 373      -4.325  40.748  39.337  1.00 39.03           C  
ANISOU 1104  CE2 TYR A 373     5342   4732   4755   -152   -168    146       C  
ATOM   1105  CZ  TYR A 373      -4.672  39.422  39.214  1.00 39.25           C  
ANISOU 1105  CZ  TYR A 373     5368   4679   4865   -155   -154    165       C  
ATOM   1106  OH  TYR A 373      -3.924  38.453  39.840  1.00 41.76           O  
ANISOU 1106  OH  TYR A 373     5726   4900   5241   -110   -245    200       O  
ATOM   1107  N   PRO A 374      -6.005  40.560  34.658  1.00 45.97           N  
ANISOU 1107  N   PRO A 374     5919   5741   5806   -286     57   -110       N  
ATOM   1108  CA  PRO A 374      -4.579  40.658  34.996  1.00 39.29           C  
ANISOU 1108  CA  PRO A 374     5061   4881   4986   -244    -15   -129       C  
ATOM   1109  C   PRO A 374      -3.829  41.699  34.167  1.00 39.20           C  
ANISOU 1109  C   PRO A 374     4995   4942   4956   -255    -11   -212       C  
ATOM   1110  O   PRO A 374      -4.439  42.402  33.363  1.00 35.85           O  
ANISOU 1110  O   PRO A 374     4561   4579   4481   -295     43   -245       O  
ATOM   1111  CB  PRO A 374      -4.052  39.246  34.705  1.00 38.66           C  
ANISOU 1111  CB  PRO A 374     4937   4715   5036   -223    -43   -158       C  
ATOM   1112  CG  PRO A 374      -5.011  38.676  33.719  1.00 38.73           C  
ANISOU 1112  CG  PRO A 374     4913   4721   5083   -268     27   -193       C  
ATOM   1113  CD  PRO A 374      -6.345  39.243  34.092  1.00 45.12           C  
ANISOU 1113  CD  PRO A 374     5774   5568   5800   -300     77   -132       C  
ATOM   1114  N   SER A 375      -2.519  41.785  34.376  1.00 37.04           N  
ANISOU 1114  N   SER A 375     4689   4654   4729   -221    -71   -245       N  
ATOM   1115  CA  SER A 375      -1.691  42.807  33.744  1.00 32.00           C  
ANISOU 1115  CA  SER A 375     4003   4078   4079   -236    -63   -320       C  
ATOM   1116  C   SER A 375      -1.465  42.545  32.259  1.00 34.11           C  
ANISOU 1116  C   SER A 375     4197   4356   4409   -272      0   -424       C  
ATOM   1117  O   SER A 375      -1.018  43.430  31.529  1.00 40.61           O  
ANISOU 1117  O   SER A 375     4996   5231   5203   -303     36   -488       O  
ATOM   1118  CB  SER A 375      -0.347  42.918  34.463  1.00 32.92           C  
ANISOU 1118  CB  SER A 375     4095   4167   4247   -190   -149   -331       C  
ATOM   1119  OG  SER A 375       0.344  41.684  34.449  1.00 32.45           O  
ANISOU 1119  OG  SER A 375     3980   4026   4324   -153   -193   -358       O  
ATOM   1120  N   ASP A 376      -1.770  41.329  31.816  1.00 36.51           N  
ANISOU 1120  N   ASP A 376     4475   4603   4793   -274     17   -440       N  
ATOM   1121  CA  ASP A 376      -1.628  40.966  30.408  1.00 33.33           C  
ANISOU 1121  CA  ASP A 376     4018   4201   4443   -311     80   -541       C  
ATOM   1122  C   ASP A 376      -2.530  41.840  29.546  1.00 35.37           C  
ANISOU 1122  C   ASP A 376     4316   4531   4594   -367    139   -556       C  
ATOM   1123  O   ASP A 376      -3.755  41.802  29.672  1.00 41.82           O  
ANISOU 1123  O   ASP A 376     5176   5356   5358   -381    146   -501       O  
ATOM   1124  CB  ASP A 376      -1.955  39.486  30.196  1.00 35.98           C  
ANISOU 1124  CB  ASP A 376     4334   4459   4878   -302     82   -546       C  
ATOM   1125  CG  ASP A 376      -1.014  38.565  30.954  1.00 43.62           C  
ANISOU 1125  CG  ASP A 376     5266   5343   5965   -242     13   -537       C  
ATOM   1126  OD1 ASP A 376       0.186  38.902  31.074  1.00 48.91           O  
ANISOU 1126  OD1 ASP A 376     5885   6014   6687   -216    -18   -583       O  
ATOM   1127  OD2 ASP A 376      -1.474  37.503  31.429  1.00 44.17           O1-
ANISOU 1127  OD2 ASP A 376     5358   5340   6083   -221    -13   -484       O1-
ATOM   1128  N   ILE A 377      -1.921  42.628  28.666  1.00 34.14           N  
ANISOU 1128  N   ILE A 377     4144   4419   4408   -400    180   -633       N  
ATOM   1129  CA  ILE A 377      -2.665  43.615  27.896  1.00 33.48           C  
ANISOU 1129  CA  ILE A 377     4114   4399   4209   -450    220   -643       C  
ATOM   1130  C   ILE A 377      -1.851  44.092  26.693  1.00 32.24           C  
ANISOU 1130  C   ILE A 377     3945   4264   4042   -495    281   -747       C  
ATOM   1131  O   ILE A 377      -0.623  44.005  26.692  1.00 28.95           O  
ANISOU 1131  O   ILE A 377     3470   3830   3700   -487    295   -804       O  
ATOM   1132  CB  ILE A 377      -3.055  44.823  28.784  1.00 29.61           C  
ANISOU 1132  CB  ILE A 377     3675   3960   3617   -438    190   -566       C  
ATOM   1133  CG1 ILE A 377      -4.228  45.593  28.185  1.00 30.80           C  
ANISOU 1133  CG1 ILE A 377     3883   4156   3664   -474    211   -552       C  
ATOM   1134  CG2 ILE A 377      -1.865  45.742  29.022  1.00 31.28           C  
ANISOU 1134  CG2 ILE A 377     3871   4198   3817   -434    185   -595       C  
ATOM   1135  CD1 ILE A 377      -4.710  46.704  29.071  1.00 27.02           C  
ANISOU 1135  CD1 ILE A 377     3451   3718   3097   -459    187   -480       C  
ATOM   1136  N   ALA A 378      -2.543  44.575  25.664  1.00 26.33           N  
ANISOU 1136  N   ALA A 378     3253   3547   3204   -546    318   -774       N  
ATOM   1137  CA  ALA A 378      -1.889  45.135  24.485  1.00 26.40           C  
ANISOU 1137  CA  ALA A 378     3284   3576   3173   -601    386   -865       C  
ATOM   1138  C   ALA A 378      -2.535  46.462  24.107  1.00 33.81           C  
ANISOU 1138  C   ALA A 378     4312   4568   3967   -636    386   -839       C  
ATOM   1139  O   ALA A 378      -3.751  46.613  24.207  1.00 32.33           O  
ANISOU 1139  O   ALA A 378     4167   4393   3723   -630    344   -781       O  
ATOM   1140  CB  ALA A 378      -1.948  44.161  23.319  1.00 20.43           C  
ANISOU 1140  CB  ALA A 378     2527   2780   2455   -634    434   -947       C  
ATOM   1141  N   VAL A 379      -1.716  47.423  23.689  1.00 30.33           N  
ANISOU 1141  N   VAL A 379     3894   4153   3476   -672    434   -884       N  
ATOM   1142  CA  VAL A 379      -2.203  48.749  23.320  1.00 28.51           C  
ANISOU 1142  CA  VAL A 379     3758   3966   3109   -706    433   -861       C  
ATOM   1143  C   VAL A 379      -1.590  49.209  21.999  1.00 35.26           C  
ANISOU 1143  C   VAL A 379     4675   4821   3902   -779    517   -950       C  
ATOM   1144  O   VAL A 379      -0.386  49.077  21.785  1.00 39.21           O  
ANISOU 1144  O   VAL A 379     5126   5306   4465   -801    587  -1022       O  
ATOM   1145  CB  VAL A 379      -1.894  49.793  24.418  1.00 30.62           C  
ANISOU 1145  CB  VAL A 379     4018   4266   3352   -678    400   -802       C  
ATOM   1146  CG1 VAL A 379      -2.449  51.157  24.040  1.00 26.96           C  
ANISOU 1146  CG1 VAL A 379     3654   3838   2751   -709    396   -777       C  
ATOM   1147  CG2 VAL A 379      -2.469  49.349  25.748  1.00 29.70           C  
ANISOU 1147  CG2 VAL A 379     3861   4145   3281   -612    328   -716       C  
ATOM   1148  N   GLU A 380      -2.424  49.739  21.109  1.00 36.27           N  
ANISOU 1148  N   GLU A 380     4913   4959   3910   -818    509   -946       N  
ATOM   1149  CA  GLU A 380      -1.962  50.234  19.818  1.00 38.85           C  
ANISOU 1149  CA  GLU A 380     5334   5279   4147   -895    588  -1022       C  
ATOM   1150  C   GLU A 380      -2.636  51.554  19.468  1.00 40.31           C  
ANISOU 1150  C   GLU A 380     5626   5477   4214   -901    540   -946       C  
ATOM   1151  O   GLU A 380      -3.653  51.918  20.065  1.00 42.25           O  
ANISOU 1151  O   GLU A 380     5887   5744   4423   -864    456   -879       O  
ATOM   1152  CB  GLU A 380      -2.232  49.199  18.719  1.00 33.90           C  
ANISOU 1152  CB  GLU A 380     4741   4615   3523   -928    617  -1089       C  
ATOM   1153  CG  GLU A 380      -1.481  47.891  18.900  1.00 40.83           C  
ANISOU 1153  CG  GLU A 380     5502   5458   4552   -908    663  -1147       C  
ATOM   1154  CD  GLU A 380      -2.043  46.770  18.049  1.00 41.93           C  
ANISOU 1154  CD  GLU A 380     5668   5560   4704   -924    664  -1195       C  
ATOM   1155  OE1 GLU A 380      -1.543  45.632  18.167  1.00 47.04           O  
ANISOU 1155  OE1 GLU A 380     6224   6170   5478   -904    694  -1242       O  
ATOM   1156  OE2 GLU A 380      -2.985  47.022  17.269  1.00 33.88           O1-
ANISOU 1156  OE2 GLU A 380     4760   4541   3571   -954    625  -1187       O1-
ATOM   1157  N   TRP A 381      -2.068  52.272  18.503  1.00 37.49           N  
ANISOU 1157  N   TRP A 381     5330   5094   3819   -938    589   -946       N  
ATOM   1158  CA  TRP A 381      -2.658  53.513  18.011  1.00 35.89           C  
ANISOU 1158  CA  TRP A 381     5226   4881   3530   -932    536   -867       C  
ATOM   1159  C   TRP A 381      -2.905  53.442  16.510  1.00 42.47           C  
ANISOU 1159  C   TRP A 381     6160   5671   4306   -967    546   -878       C  
ATOM   1160  O   TRP A 381      -2.214  52.714  15.791  1.00 41.45           O  
ANISOU 1160  O   TRP A 381     6028   5519   4201  -1011    628   -948       O  
ATOM   1161  CB  TRP A 381      -1.753  54.708  18.312  1.00 33.95           C  
ANISOU 1161  CB  TRP A 381     4981   4640   3280   -949    576   -849       C  
ATOM   1162  CG  TRP A 381      -1.651  55.076  19.760  1.00 39.91           C  
ANISOU 1162  CG  TRP A 381     5664   5435   4066   -909    544   -821       C  
ATOM   1163  CD1 TRP A 381      -0.843  54.498  20.693  1.00 39.10           C  
ANISOU 1163  CD1 TRP A 381     5462   5360   4035   -908    583   -876       C  
ATOM   1164  CD2 TRP A 381      -2.359  56.124  20.436  1.00 35.14           C  
ANISOU 1164  CD2 TRP A 381     5086   4845   3420   -864    465   -738       C  
ATOM   1165  CE2 TRP A 381      -1.933  56.115  21.780  1.00 38.93           C  
ANISOU 1165  CE2 TRP A 381     5487   5363   3940   -841    462   -739       C  
ATOM   1166  CE3 TRP A 381      -3.315  57.064  20.038  1.00 29.11           C  
ANISOU 1166  CE3 TRP A 381     4403   4062   2595   -837    396   -669       C  
ATOM   1167  NE1 TRP A 381      -1.009  55.112  21.914  1.00 35.58           N  
ANISOU 1167  NE1 TRP A 381     4989   4948   3582   -868    529   -826       N  
ATOM   1168  CZ2 TRP A 381      -2.427  57.010  22.724  1.00 36.34           C  
ANISOU 1168  CZ2 TRP A 381     5165   5053   3588   -795    399   -669       C  
ATOM   1169  CZ3 TRP A 381      -3.805  57.952  20.981  1.00 33.50           C  
ANISOU 1169  CZ3 TRP A 381     4952   4636   3142   -789    337   -607       C  
ATOM   1170  CH2 TRP A 381      -3.363  57.915  22.308  1.00 31.25           C  
ANISOU 1170  CH2 TRP A 381     4593   4388   2894   -769    342   -605       C  
ATOM   1171  N   GLU A 382      -3.885  54.202  16.035  1.00 46.67           N  
ANISOU 1171  N   GLU A 382     6781   6189   4763   -946    462   -816       N  
ATOM   1172  CA  GLU A 382      -4.129  54.307  14.604  1.00 49.95           C  
ANISOU 1172  CA  GLU A 382     7309   6561   5107   -977    460   -821       C  
ATOM   1173  C   GLU A 382      -4.857  55.594  14.255  1.00 47.70           C  
ANISOU 1173  C   GLU A 382     7117   6259   4746   -955    379   -750       C  
ATOM   1174  O   GLU A 382      -5.420  56.263  15.123  1.00 37.53           O  
ANISOU 1174  O   GLU A 382     5800   4994   3467   -905    313   -698       O  
ATOM   1175  CB  GLU A 382      -4.926  53.105  14.097  1.00 52.07           C  
ANISOU 1175  CB  GLU A 382     7588   6820   5377   -971    416   -856       C  
ATOM   1176  CG  GLU A 382      -6.406  53.127  14.441  1.00 56.70           C  
ANISOU 1176  CG  GLU A 382     8180   7417   5948   -918    284   -813       C  
ATOM   1177  CD  GLU A 382      -7.133  51.899  13.922  1.00 72.17           C  
ANISOU 1177  CD  GLU A 382    10145   9360   7918   -922    242   -860       C  
ATOM   1178  OE1 GLU A 382      -8.342  52.001  13.618  1.00 74.55           O  
ANISOU 1178  OE1 GLU A 382    10489   9651   8187   -896    130   -838       O  
ATOM   1179  OE2 GLU A 382      -6.489  50.832  13.818  1.00 77.25           O1-
ANISOU 1179  OE2 GLU A 382    10744   9997   8609   -952    318   -925       O1-
ATOM   1180  N   SER A 383      -4.836  55.933  12.972  1.00 50.54           N  
ANISOU 1180  N   SER A 383     7592   6576   5033   -992    389   -753       N  
ATOM   1181  CA  SER A 383      -5.495  57.133  12.476  1.00 47.90           C  
ANISOU 1181  CA  SER A 383     7359   6215   4624   -977    314   -694       C  
ATOM   1182  C   SER A 383      -5.952  56.913  11.039  1.00 54.91           C  
ANISOU 1182  C   SER A 383     8372   7059   5431  -1006    284   -709       C  
ATOM   1183  O   SER A 383      -5.172  56.467  10.197  1.00 57.76           O  
ANISOU 1183  O   SER A 383     8782   7394   5770  -1068    376   -754       O  
ATOM   1184  CB  SER A 383      -4.556  58.334  12.567  1.00 38.64           C  
ANISOU 1184  CB  SER A 383     6213   5030   3439  -1011    382   -672       C  
ATOM   1185  OG  SER A 383      -5.200  59.520  12.145  1.00 49.84           O  
ANISOU 1185  OG  SER A 383     7729   6417   4790   -996    308   -616       O  
ATOM   1186  N   ASN A 384      -7.217  57.231  10.771  1.00 58.33           N  
ANISOU 1186  N   ASN A 384     8859   7481   5823   -961    156   -674       N  
ATOM   1187  CA  ASN A 384      -7.838  56.975   9.473  1.00 59.81           C  
ANISOU 1187  CA  ASN A 384     9165   7626   5933   -979     98   -687       C  
ATOM   1188  C   ASN A 384      -7.586  55.555   8.967  1.00 57.15           C  
ANISOU 1188  C   ASN A 384     8817   7289   5611  -1011    147   -756       C  
ATOM   1189  O   ASN A 384      -7.113  55.360   7.845  1.00 55.30           O  
ANISOU 1189  O   ASN A 384     8682   7015   5314  -1068    204   -785       O  
ATOM   1190  CB  ASN A 384      -7.354  57.989   8.434  1.00 63.55           C  
ANISOU 1190  CB  ASN A 384     9785   8046   6315  -1033    136   -664       C  
ATOM   1191  CG  ASN A 384      -8.052  59.330   8.561  1.00 74.94           C  
ANISOU 1191  CG  ASN A 384    11281   9470   7722   -997     41   -599       C  
ATOM   1192  ND2 ASN A 384      -7.318  60.348   9.004  1.00 76.03           N  
ANISOU 1192  ND2 ASN A 384    11416   9605   7868  -1013    103   -569       N  
ATOM   1193  OD1 ASN A 384      -9.239  59.451   8.258  1.00 81.01           O  
ANISOU 1193  OD1 ASN A 384    12093  10224   8462   -956    -90   -580       O  
ATOM   1194  N   GLY A 385      -7.885  54.576   9.815  1.00 53.59           N  
ANISOU 1194  N   GLY A 385     8246   6874   5241   -978    129   -783       N  
ATOM   1195  CA  GLY A 385      -7.769  53.170   9.465  1.00 55.37           C  
ANISOU 1195  CA  GLY A 385     8447   7095   5494  -1001    164   -851       C  
ATOM   1196  C   GLY A 385      -6.353  52.624   9.461  1.00 61.11           C  
ANISOU 1196  C   GLY A 385     9135   7825   6261  -1055    322   -903       C  
ATOM   1197  O   GLY A 385      -6.148  51.412   9.394  1.00 68.31           O  
ANISOU 1197  O   GLY A 385     9999   8735   7219  -1070    364   -965       O  
ATOM   1198  N   GLN A 386      -5.375  53.517   9.542  1.00 60.55           N  
ANISOU 1198  N   GLN A 386     9076   7751   6180  -1087    410   -884       N  
ATOM   1199  CA  GLN A 386      -3.973  53.133   9.419  1.00 60.77           C  
ANISOU 1199  CA  GLN A 386     9070   7774   6248  -1148    565   -941       C  
ATOM   1200  C   GLN A 386      -3.208  53.271  10.735  1.00 57.91           C  
ANISOU 1200  C   GLN A 386     8571   7451   5981  -1135    621   -943       C  
ATOM   1201  O   GLN A 386      -3.423  54.222  11.486  1.00 58.83           O  
ANISOU 1201  O   GLN A 386     8667   7587   6097  -1101    571   -885       O  
ATOM   1202  CB  GLN A 386      -3.303  53.967   8.325  1.00 69.35           C  
ANISOU 1202  CB  GLN A 386    10285   8814   7252  -1218    639   -937       C  
ATOM   1203  CG  GLN A 386      -3.673  53.535   6.912  1.00 80.45           C  
ANISOU 1203  CG  GLN A 386    11826  10175   8568  -1254    628   -962       C  
ATOM   1204  CD  GLN A 386      -3.042  52.203   6.528  1.00 89.49           C  
ANISOU 1204  CD  GLN A 386    12933  11311   9757  -1293    730  -1051       C  
ATOM   1205  NE2 GLN A 386      -1.712  52.154   6.528  1.00 91.57           N  
ANISOU 1205  NE2 GLN A 386    13154  11568  10070  -1354    884  -1100       N  
ATOM   1206  OE1 GLN A 386      -3.742  51.231   6.239  1.00 92.07           O  
ANISOU 1206  OE1 GLN A 386    13263  11636  10082  -1269    670  -1080       O  
ATOM   1207  N   PRO A 387      -2.301  52.319  11.010  1.00 51.96           N  
ANISOU 1207  N   PRO A 387     7724   6705   5312  -1161    723  -1017       N  
ATOM   1208  CA  PRO A 387      -1.551  52.296  12.272  1.00 41.11           C  
ANISOU 1208  CA  PRO A 387     6214   5368   4037  -1147    770  -1033       C  
ATOM   1209  C   PRO A 387      -0.598  53.475  12.456  1.00 42.94           C  
ANISOU 1209  C   PRO A 387     6450   5599   4268  -1182    836  -1017       C  
ATOM   1210  O   PRO A 387       0.145  53.832  11.540  1.00 39.36           O  
ANISOU 1210  O   PRO A 387     6064   5109   3783  -1250    927  -1044       O  
ATOM   1211  CB  PRO A 387      -0.766  50.983  12.185  1.00 37.42           C  
ANISOU 1211  CB  PRO A 387     5665   4893   3660  -1174    869  -1132       C  
ATOM   1212  CG  PRO A 387      -0.650  50.702  10.728  1.00 45.20           C  
ANISOU 1212  CG  PRO A 387     6759   5832   4582  -1229    923  -1166       C  
ATOM   1213  CD  PRO A 387      -1.934  51.198  10.129  1.00 47.17           C  
ANISOU 1213  CD  PRO A 387     7134   6070   4717  -1203    798  -1095       C  
ATOM   1214  N   GLU A 388      -0.636  54.070  13.643  1.00 47.18           N  
ANISOU 1214  N   GLU A 388     6918   6172   4838  -1140    792   -976       N  
ATOM   1215  CA  GLU A 388       0.355  55.049  14.073  1.00 42.20           C  
ANISOU 1215  CA  GLU A 388     6259   5544   4230  -1171    854   -975       C  
ATOM   1216  C   GLU A 388       1.389  54.341  14.937  1.00 39.89           C  
ANISOU 1216  C   GLU A 388     5822   5277   4057  -1177    931  -1053       C  
ATOM   1217  O   GLU A 388       1.032  53.680  15.910  1.00 48.56           O  
ANISOU 1217  O   GLU A 388     6835   6410   5208  -1122    880  -1056       O  
ATOM   1218  CB  GLU A 388      -0.315  56.189  14.843  1.00 40.33           C  
ANISOU 1218  CB  GLU A 388     6039   5327   3955  -1119    754   -886       C  
ATOM   1219  CG  GLU A 388      -1.335  56.970  14.035  1.00 43.98           C  
ANISOU 1219  CG  GLU A 388     6633   5761   4317  -1104    670   -818       C  
ATOM   1220  CD  GLU A 388      -0.704  58.059  13.191  1.00 56.55           C  
ANISOU 1220  CD  GLU A 388     8327   7309   5853  -1170    731   -810       C  
ATOM   1221  OE1 GLU A 388      -1.372  58.559  12.261  1.00 56.53           O  
ANISOU 1221  OE1 GLU A 388     8448   7269   5763  -1174    682   -772       O  
ATOM   1222  OE2 GLU A 388       0.461  58.423  13.463  1.00 63.34           O1-
ANISOU 1222  OE2 GLU A 388     9144   8167   6756  -1220    826   -846       O1-
ATOM   1223  N   ASN A 389       2.663  54.468  14.589  1.00 38.45           N  
ANISOU 1223  N   ASN A 389     5611   5074   3923  -1245   1056  -1123       N  
ATOM   1224  CA  ASN A 389       3.681  53.656  15.244  1.00 45.42           C  
ANISOU 1224  CA  ASN A 389     6347   5971   4940  -1249   1135  -1220       C  
ATOM   1225  C   ASN A 389       4.699  54.436  16.066  1.00 45.48           C  
ANISOU 1225  C   ASN A 389     6272   5994   5012  -1268   1179  -1249       C  
ATOM   1226  O   ASN A 389       5.575  53.842  16.692  1.00 48.62           O  
ANISOU 1226  O   ASN A 389     6534   6402   5535  -1263   1235  -1338       O  
ATOM   1227  CB  ASN A 389       4.417  52.811  14.203  1.00 58.41           C  
ANISOU 1227  CB  ASN A 389     7984   7574   6636  -1310   1256  -1315       C  
ATOM   1228  CG  ASN A 389       3.634  51.577  13.799  1.00 64.29           C  
ANISOU 1228  CG  ASN A 389     8742   8311   7373  -1277   1219  -1326       C  
ATOM   1229  ND2 ASN A 389       3.593  51.304  12.497  1.00 66.90           N  
ANISOU 1229  ND2 ASN A 389     9170   8601   7649  -1328   1272  -1345       N  
ATOM   1230  OD1 ASN A 389       3.066  50.880  14.638  1.00 60.69           O  
ANISOU 1230  OD1 ASN A 389     8219   7883   6958  -1212   1144  -1321       O  
ATOM   1231  N   ASN A 390       4.588  55.762  16.069  1.00 38.41           N  
ANISOU 1231  N   ASN A 390     5456   5098   4041  -1285   1151  -1180       N  
ATOM   1232  CA  ASN A 390       5.492  56.584  16.868  1.00 33.84           C  
ANISOU 1232  CA  ASN A 390     4808   4534   3515  -1304   1185  -1206       C  
ATOM   1233  C   ASN A 390       4.960  56.743  18.291  1.00 39.36           C  
ANISOU 1233  C   ASN A 390     5451   5287   4218  -1224   1074  -1156       C  
ATOM   1234  O   ASN A 390       4.764  57.858  18.770  1.00 36.03           O  
ANISOU 1234  O   ASN A 390     5069   4876   3744  -1213   1022  -1092       O  
ATOM   1235  CB  ASN A 390       5.700  57.959  16.220  1.00 35.06           C  
ANISOU 1235  CB  ASN A 390     5075   4653   3592  -1368   1216  -1164       C  
ATOM   1236  CG  ASN A 390       6.841  58.742  16.860  1.00 41.60           C  
ANISOU 1236  CG  ASN A 390     5829   5488   4490  -1412   1281  -1217       C  
ATOM   1237  ND2 ASN A 390       6.917  60.034  16.558  1.00 44.56           N  
ANISOU 1237  ND2 ASN A 390     6299   5835   4797  -1456   1288  -1171       N  
ATOM   1238  OD1 ASN A 390       7.642  58.188  17.614  1.00 46.90           O  
ANISOU 1238  OD1 ASN A 390     6356   6184   5282  -1404   1323  -1305       O  
ATOM   1239  N   TYR A 391       4.722  55.618  18.961  1.00 37.90           N  
ANISOU 1239  N   TYR A 391     5178   5129   4093  -1168   1038  -1188       N  
ATOM   1240  CA  TYR A 391       4.207  55.647  20.323  1.00 33.99           C  
ANISOU 1240  CA  TYR A 391     4638   4681   3596  -1096    936  -1147       C  
ATOM   1241  C   TYR A 391       5.018  54.768  21.269  1.00 39.02           C  
ANISOU 1241  C   TYR A 391     5125   5334   4365  -1068    957  -1249       C  
ATOM   1242  O   TYR A 391       5.698  53.833  20.845  1.00 45.14           O  
ANISOU 1242  O   TYR A 391     5819   6080   5253  -1080   1028  -1336       O  
ATOM   1243  CB  TYR A 391       2.736  55.215  20.356  1.00 33.65           C  
ANISOU 1243  CB  TYR A 391     4657   4647   3481  -1038    831  -1061       C  
ATOM   1244  CG  TYR A 391       2.494  53.753  20.021  1.00 33.30           C  
ANISOU 1244  CG  TYR A 391     4575   4592   3487  -1025    847  -1117       C  
ATOM   1245  CD1 TYR A 391       2.571  52.769  21.003  1.00 35.29           C  
ANISOU 1245  CD1 TYR A 391     4718   4857   3833   -973    813  -1150       C  
ATOM   1246  CD2 TYR A 391       2.170  53.358  18.728  1.00 36.80           C  
ANISOU 1246  CD2 TYR A 391     5089   4997   3894  -1057    879  -1121       C  
ATOM   1247  CE1 TYR A 391       2.347  51.436  20.706  1.00 32.98           C  
ANISOU 1247  CE1 TYR A 391     4381   4537   3612   -951    813  -1180       C  
ATOM   1248  CE2 TYR A 391       1.939  52.021  18.420  1.00 39.06           C  
ANISOU 1248  CE2 TYR A 391     5343   5269   4228  -1047    892  -1175       C  
ATOM   1249  CZ  TYR A 391       2.031  51.065  19.417  1.00 35.49           C  
ANISOU 1249  CZ  TYR A 391     4784   4832   3867  -1003    872  -1227       C  
ATOM   1250  OH  TYR A 391       1.809  49.736  19.141  1.00 42.86           O  
ANISOU 1250  OH  TYR A 391     5678   5737   4871   -985    875  -1269       O  
ATOM   1251  N   LYS A 392       4.931  55.076  22.558  1.00 31.55           N  
ANISOU 1251  N   LYS A 392     4121   4411   3456  -1001    848  -1178       N  
ATOM   1252  CA  LYS A 392       5.546  54.253  23.587  1.00 27.75           C  
ANISOU 1252  CA  LYS A 392     3487   3917   3141   -931    786  -1186       C  
ATOM   1253  C   LYS A 392       4.546  54.014  24.709  1.00 33.68           C  
ANISOU 1253  C   LYS A 392     4247   4686   3863   -844    647  -1072       C  
ATOM   1254  O   LYS A 392       3.764  54.900  25.053  1.00 34.89           O  
ANISOU 1254  O   LYS A 392     4489   4870   3898   -837    598   -995       O  
ATOM   1255  CB  LYS A 392       6.818  54.908  24.127  1.00 34.25           C  
ANISOU 1255  CB  LYS A 392     4217   4735   4061   -946    803  -1237       C  
ATOM   1256  CG  LYS A 392       7.839  55.273  23.061  1.00 41.86           C  
ANISOU 1256  CG  LYS A 392     5170   5677   5059  -1044    960  -1354       C  
ATOM   1257  CD  LYS A 392       9.109  54.447  23.185  1.00 50.31           C  
ANISOU 1257  CD  LYS A 392     6062   6708   6344  -1032   1000  -1460       C  
ATOM   1258  CE  LYS A 392       9.115  53.272  22.225  1.00 50.42           C  
ANISOU 1258  CE  LYS A 392     6059   6690   6409  -1047   1087  -1532       C  
ATOM   1259  NZ  LYS A 392      10.443  52.599  22.196  1.00 55.36           N1+
ANISOU 1259  NZ  LYS A 392     6509   7269   7254  -1047   1150  -1655       N1+
ATOM   1260  N   THR A 393       4.570  52.811  25.269  1.00 34.23           N  
ANISOU 1260  N   THR A 393     4230   4733   4045   -780    590  -1064       N  
ATOM   1261  CA  THR A 393       3.636  52.439  26.320  1.00 29.31           C  
ANISOU 1261  CA  THR A 393     3620   4118   3400   -704    475   -959       C  
ATOM   1262  C   THR A 393       4.395  52.024  27.571  1.00 38.45           C  
ANISOU 1262  C   THR A 393     4676   5253   4680   -640    391   -947       C  
ATOM   1263  O   THR A 393       5.324  51.220  27.499  1.00 43.82           O  
ANISOU 1263  O   THR A 393     5251   5894   5504   -627    402  -1017       O  
ATOM   1264  CB  THR A 393       2.714  51.289  25.868  1.00 26.30           C  
ANISOU 1264  CB  THR A 393     3257   3718   3018   -687    472   -942       C  
ATOM   1265  CG2 THR A 393       1.656  50.991  26.924  1.00 18.62           C  
ANISOU 1265  CG2 THR A 393     2308   2751   2014   -621    373   -834       C  
ATOM   1266  OG1 THR A 393       2.071  51.645  24.636  1.00 29.47           O  
ANISOU 1266  OG1 THR A 393     3757   4133   3308   -748    538   -963       O  
ATOM   1267  N   THR A 394       4.010  52.585  28.713  1.00 36.09           N  
ANISOU 1267  N   THR A 394     4413   4974   4325   -597    301   -862       N  
ATOM   1268  CA  THR A 394       4.618  52.212  29.985  1.00 32.15           C  
ANISOU 1268  CA  THR A 394     3847   4450   3918   -533    200   -837       C  
ATOM   1269  C   THR A 394       4.282  50.765  30.311  1.00 29.76           C  
ANISOU 1269  C   THR A 394     3512   4105   3691   -477    152   -807       C  
ATOM   1270  O   THR A 394       3.291  50.230  29.809  1.00 28.43           O  
ANISOU 1270  O   THR A 394     3391   3938   3474   -483    183   -779       O  
ATOM   1271  CB  THR A 394       4.136  53.126  31.145  1.00 30.71           C  
ANISOU 1271  CB  THR A 394     3738   4296   3633   -503    120   -747       C  
ATOM   1272  CG2 THR A 394       4.126  54.590  30.721  1.00 25.96           C  
ANISOU 1272  CG2 THR A 394     3197   3736   2931   -561    173   -761       C  
ATOM   1273  OG1 THR A 394       2.823  52.730  31.560  1.00 26.14           O  
ANISOU 1273  OG1 THR A 394     3234   3723   2973   -469     90   -655       O  
ATOM   1274  N   PRO A 395       5.108  50.115  31.145  1.00 32.19           N  
ANISOU 1274  N   PRO A 395     3741   4367   4121   -422     69   -815       N  
ATOM   1275  CA  PRO A 395       4.716  48.791  31.635  1.00 35.62           C  
ANISOU 1275  CA  PRO A 395     4168   4754   4614   -364      9   -768       C  
ATOM   1276  C   PRO A 395       3.487  48.911  32.528  1.00 36.88           C  
ANISOU 1276  C   PRO A 395     4438   4929   4645   -336    -43   -646       C  
ATOM   1277  O   PRO A 395       3.175  50.012  32.973  1.00 38.16           O  
ANISOU 1277  O   PRO A 395     4666   5135   4699   -347    -54   -605       O  
ATOM   1278  CB  PRO A 395       5.939  48.326  32.436  1.00 31.03           C  
ANISOU 1278  CB  PRO A 395     3493   4118   4180   -309    -90   -797       C  
ATOM   1279  CG  PRO A 395       7.068  49.180  31.962  1.00 34.27           C  
ANISOU 1279  CG  PRO A 395     3824   4545   4652   -352    -45   -897       C  
ATOM   1280  CD  PRO A 395       6.453  50.497  31.606  1.00 31.56           C  
ANISOU 1280  CD  PRO A 395     3573   4271   4147   -412     23   -873       C  
ATOM   1281  N   PRO A 396       2.788  47.799  32.778  1.00 39.10           N  
ANISOU 1281  N   PRO A 396     4740   5173   4944   -303    -65   -594       N  
ATOM   1282  CA  PRO A 396       1.670  47.873  33.723  1.00 31.93           C  
ANISOU 1282  CA  PRO A 396     3932   4272   3928   -279   -103   -483       C  
ATOM   1283  C   PRO A 396       2.164  48.216  35.122  1.00 36.14           C  
ANISOU 1283  C   PRO A 396     4499   4789   4443   -234   -207   -430       C  
ATOM   1284  O   PRO A 396       3.226  47.740  35.527  1.00 36.85           O  
ANISOU 1284  O   PRO A 396     4529   4831   4640   -197   -284   -459       O  
ATOM   1285  CB  PRO A 396       1.068  46.460  33.678  1.00 33.70           C  
ANISOU 1285  CB  PRO A 396     4154   4442   4208   -258   -102   -454       C  
ATOM   1286  CG  PRO A 396       1.552  45.870  32.389  1.00 36.46           C  
ANISOU 1286  CG  PRO A 396     4419   4777   4658   -286    -39   -553       C  
ATOM   1287  CD  PRO A 396       2.907  46.469  32.155  1.00 36.92           C  
ANISOU 1287  CD  PRO A 396     4402   4844   4782   -294    -42   -638       C  
ATOM   1288  N   VAL A 397       1.418  49.045  35.844  1.00 34.96           N  
ANISOU 1288  N   VAL A 397     4446   4675   4163   -235   -215   -358       N  
ATOM   1289  CA  VAL A 397       1.795  49.412  37.205  1.00 32.71           C  
ANISOU 1289  CA  VAL A 397     4219   4374   3836   -195   -313   -305       C  
ATOM   1290  C   VAL A 397       0.693  49.030  38.184  1.00 32.44           C  
ANISOU 1290  C   VAL A 397     4297   4319   3710   -173   -325   -200       C  
ATOM   1291  O   VAL A 397      -0.478  49.347  37.974  1.00 35.08           O  
ANISOU 1291  O   VAL A 397     4680   4687   3961   -199   -247   -166       O  
ATOM   1292  CB  VAL A 397       2.095  50.922  37.324  1.00 31.33           C  
ANISOU 1292  CB  VAL A 397     4067   4255   3584   -221   -311   -326       C  
ATOM   1293  CG1 VAL A 397       2.493  51.276  38.752  1.00 26.59           C  
ANISOU 1293  CG1 VAL A 397     3535   3633   2935   -181   -421   -275       C  
ATOM   1294  CG2 VAL A 397       3.193  51.321  36.355  1.00 28.19           C  
ANISOU 1294  CG2 VAL A 397     3561   3872   3278   -254   -282   -433       C  
ATOM   1295  N   LEU A 398       1.078  48.338  39.251  1.00 32.67           N  
ANISOU 1295  N   LEU A 398     4369   4285   3760   -125   -422   -150       N  
ATOM   1296  CA  LEU A 398       0.135  47.910  40.278  1.00 32.44           C  
ANISOU 1296  CA  LEU A 398     4463   4223   3641   -108   -428    -49       C  
ATOM   1297  C   LEU A 398      -0.451  49.110  41.017  1.00 35.41           C  
ANISOU 1297  C   LEU A 398     4941   4645   3867   -121   -408     -4       C  
ATOM   1298  O   LEU A 398       0.287  49.941  41.544  1.00 33.83           O  
ANISOU 1298  O   LEU A 398     4761   4459   3632   -110   -477    -18       O  
ATOM   1299  CB  LEU A 398       0.826  46.957  41.258  1.00 29.77           C  
ANISOU 1299  CB  LEU A 398     4164   3796   3349    -54   -552     -7       C  
ATOM   1300  CG  LEU A 398      -0.058  46.208  42.258  1.00 37.07           C  
ANISOU 1300  CG  LEU A 398     5224   4663   4196    -40   -554     99       C  
ATOM   1301  CD1 LEU A 398      -1.071  45.333  41.537  1.00 33.81           C  
ANISOU 1301  CD1 LEU A 398     4783   4240   3823    -67   -447    109       C  
ATOM   1302  CD2 LEU A 398       0.797  45.375  43.199  1.00 36.13           C  
ANISOU 1302  CD2 LEU A 398     5157   4450   4119     17   -700    136       C  
ATOM   1303  N   ASP A 399      -1.778  49.195  41.048  1.00 31.92           N  
ANISOU 1303  N   ASP A 399     4558   4224   3348   -145   -314     44       N  
ATOM   1304  CA  ASP A 399      -2.458  50.319  41.683  1.00 36.11           C  
ANISOU 1304  CA  ASP A 399     5179   4795   3746   -158   -276     79       C  
ATOM   1305  C   ASP A 399      -2.812  49.987  43.134  1.00 41.69           C  
ANISOU 1305  C   ASP A 399     6028   5450   4362   -136   -306    167       C  
ATOM   1306  O   ASP A 399      -2.570  48.871  43.601  1.00 41.31           O  
ANISOU 1306  O   ASP A 399     6012   5332   4350   -112   -359    206       O  
ATOM   1307  CB  ASP A 399      -3.725  50.697  40.905  1.00 35.77           C  
ANISOU 1307  CB  ASP A 399     5113   4799   3680   -195   -155     71       C  
ATOM   1308  CG  ASP A 399      -3.909  52.201  40.773  1.00 37.36           C  
ANISOU 1308  CG  ASP A 399     5329   5064   3803   -213   -125     46       C  
ATOM   1309  OD1 ASP A 399      -3.368  52.946  41.619  1.00 40.20           O  
ANISOU 1309  OD1 ASP A 399     5752   5428   4094   -199   -180     57       O  
ATOM   1310  OD2 ASP A 399      -4.590  52.641  39.820  1.00 36.33           O1-
ANISOU 1310  OD2 ASP A 399     5151   4973   3678   -241    -56     15       O1-
ATOM   1311  N   SER A 400      -3.386  50.960  43.836  1.00 42.82           N  
ANISOU 1311  N   SER A 400     6265   5622   4383   -145   -268    197       N  
ATOM   1312  CA  SER A 400      -3.735  50.810  45.244  1.00 38.23           C  
ANISOU 1312  CA  SER A 400     5842   4994   3690   -132   -282    276       C  
ATOM   1313  C   SER A 400      -4.701  49.651  45.470  1.00 38.84           C  
ANISOU 1313  C   SER A 400     5964   5018   3776   -143   -208    337       C  
ATOM   1314  O   SER A 400      -4.601  48.931  46.463  1.00 42.90           O  
ANISOU 1314  O   SER A 400     6596   5462   4244   -127   -251    402       O  
ATOM   1315  CB  SER A 400      -4.354  52.104  45.779  1.00 34.56           C  
ANISOU 1315  CB  SER A 400     5456   4574   3100   -148   -221    283       C  
ATOM   1316  OG  SER A 400      -3.642  53.243  45.329  1.00 46.69           O  
ANISOU 1316  OG  SER A 400     6934   6165   4641   -150   -264    219       O  
ATOM   1317  N   ASP A 401      -5.627  49.470  44.537  1.00 35.37           N  
ANISOU 1317  N   ASP A 401     5435   4606   3397   -173   -101    314       N  
ATOM   1318  CA  ASP A 401      -6.726  48.531  44.735  1.00 34.12           C  
ANISOU 1318  CA  ASP A 401     5311   4402   3249   -194     -8    365       C  
ATOM   1319  C   ASP A 401      -6.437  47.130  44.195  1.00 34.07           C  
ANISOU 1319  C   ASP A 401     5242   4341   3362   -187    -40    365       C  
ATOM   1320  O   ASP A 401      -7.332  46.291  44.121  1.00 43.68           O  
ANISOU 1320  O   ASP A 401     6461   5521   4615   -211     38    395       O  
ATOM   1321  CB  ASP A 401      -7.994  49.086  44.088  1.00 32.14           C  
ANISOU 1321  CB  ASP A 401     4998   4204   3010   -229    120    339       C  
ATOM   1322  CG  ASP A 401      -7.893  49.176  42.578  1.00 45.93           C  
ANISOU 1322  CG  ASP A 401     6592   5998   4860   -238    117    264       C  
ATOM   1323  OD1 ASP A 401      -6.775  49.014  42.039  1.00 45.11           O  
ANISOU 1323  OD1 ASP A 401     6430   5898   4811   -221     32    223       O  
ATOM   1324  OD2 ASP A 401      -8.934  49.415  41.931  1.00 47.21           O1-
ANISOU 1324  OD2 ASP A 401     6696   6190   5051   -263    201    241       O1-
ATOM   1325  N   GLY A 402      -5.190  46.880  43.809  1.00 27.97           N  
ANISOU 1325  N   GLY A 402     4408   3559   2661   -157   -152    326       N  
ATOM   1326  CA  GLY A 402      -4.802  45.566  43.333  1.00 30.38           C  
ANISOU 1326  CA  GLY A 402     4654   3805   3085   -143   -191    319       C  
ATOM   1327  C   GLY A 402      -4.923  45.426  41.828  1.00 32.35           C  
ANISOU 1327  C   GLY A 402     4750   4096   3445   -165   -143    240       C  
ATOM   1328  O   GLY A 402      -4.417  44.473  41.247  1.00 39.51           O  
ANISOU 1328  O   GLY A 402     5587   4962   4462   -153   -178    210       O  
ATOM   1329  N   SER A 403      -5.601  46.376  41.194  1.00 33.87           N  
ANISOU 1329  N   SER A 403     4899   4363   3606   -196    -65    204       N  
ATOM   1330  CA  SER A 403      -5.696  46.392  39.739  1.00 36.90           C  
ANISOU 1330  CA  SER A 403     5160   4788   4072   -219    -29    127       C  
ATOM   1331  C   SER A 403      -4.450  47.040  39.133  1.00 35.87           C  
ANISOU 1331  C   SER A 403     4963   4696   3969   -209    -90     54       C  
ATOM   1332  O   SER A 403      -3.607  47.576  39.853  1.00 31.50           O  
ANISOU 1332  O   SER A 403     4448   4143   3376   -184   -161     62       O  
ATOM   1333  CB  SER A 403      -6.957  47.129  39.279  1.00 33.04           C  
ANISOU 1333  CB  SER A 403     4658   4353   3542   -254     66    119       C  
ATOM   1334  OG  SER A 403      -6.836  48.527  39.446  1.00 34.48           O  
ANISOU 1334  OG  SER A 403     4866   4595   3639   -254     63    105       O  
ATOM   1335  N   PHE A 404      -4.337  46.989  37.810  1.00 31.51           N  
ANISOU 1335  N   PHE A 404     4315   4172   3486   -232    -60    -19       N  
ATOM   1336  CA  PHE A 404      -3.198  47.588  37.129  1.00 29.52           C  
ANISOU 1336  CA  PHE A 404     3998   3953   3267   -234    -92    -96       C  
ATOM   1337  C   PHE A 404      -3.617  48.792  36.298  1.00 30.72           C  
ANISOU 1337  C   PHE A 404     4137   4176   3359   -271    -36   -137       C  
ATOM   1338  O   PHE A 404      -4.787  48.940  35.940  1.00 34.86           O  
ANISOU 1338  O   PHE A 404     4676   4721   3850   -294     23   -121       O  
ATOM   1339  CB  PHE A 404      -2.503  46.564  36.231  1.00 26.56           C  
ANISOU 1339  CB  PHE A 404     3532   3541   3019   -233   -101   -160       C  
ATOM   1340  CG  PHE A 404      -1.760  45.500  36.984  1.00 28.72           C  
ANISOU 1340  CG  PHE A 404     3805   3737   3369   -187   -181   -136       C  
ATOM   1341  CD1 PHE A 404      -2.395  44.327  37.355  1.00 36.66           C  
ANISOU 1341  CD1 PHE A 404     4845   4679   4404   -176   -177    -80       C  
ATOM   1342  CD2 PHE A 404      -0.424  45.668  37.313  1.00 30.45           C  
ANISOU 1342  CD2 PHE A 404     3990   3940   3640   -156   -265   -170       C  
ATOM   1343  CE1 PHE A 404      -1.713  43.344  38.046  1.00 31.57           C  
ANISOU 1343  CE1 PHE A 404     4215   3954   3829   -131   -260    -53       C  
ATOM   1344  CE2 PHE A 404       0.263  44.689  38.004  1.00 30.94           C  
ANISOU 1344  CE2 PHE A 404     4053   3921   3780   -107   -357   -148       C  
ATOM   1345  CZ  PHE A 404      -0.385  43.524  38.372  1.00 28.92           C  
ANISOU 1345  CZ  PHE A 404     3845   3599   3543    -93   -358    -86       C  
ATOM   1346  N   PHE A 405      -2.654  49.655  35.997  1.00 23.78           N  
ANISOU 1346  N   PHE A 405     3232   3330   2475   -279    -57   -190       N  
ATOM   1347  CA  PHE A 405      -2.880  50.744  35.060  1.00 25.23           C  
ANISOU 1347  CA  PHE A 405     3408   3570   2608   -318     -7   -235       C  
ATOM   1348  C   PHE A 405      -1.632  50.971  34.224  1.00 27.92           C  
ANISOU 1348  C   PHE A 405     3683   3920   3007   -340     -9   -321       C  
ATOM   1349  O   PHE A 405      -0.545  50.525  34.586  1.00 25.66           O  
ANISOU 1349  O   PHE A 405     3351   3602   2798   -317    -59   -345       O  
ATOM   1350  CB  PHE A 405      -3.278  52.038  35.785  1.00 28.08           C  
ANISOU 1350  CB  PHE A 405     3842   3969   2859   -316    -10   -195       C  
ATOM   1351  CG  PHE A 405      -2.118  52.784  36.394  1.00 25.08           C  
ANISOU 1351  CG  PHE A 405     3470   3595   2463   -305    -67   -212       C  
ATOM   1352  CD1 PHE A 405      -1.691  52.492  37.679  1.00 26.55           C  
ANISOU 1352  CD1 PHE A 405     3697   3748   2643   -265   -138   -166       C  
ATOM   1353  CD2 PHE A 405      -1.468  53.791  35.688  1.00 23.62           C  
ANISOU 1353  CD2 PHE A 405     3261   3445   2268   -337    -52   -273       C  
ATOM   1354  CE1 PHE A 405      -0.631  53.175  38.244  1.00 24.31           C  
ANISOU 1354  CE1 PHE A 405     3418   3467   2352   -255   -206   -186       C  
ATOM   1355  CE2 PHE A 405      -0.404  54.474  36.246  1.00 28.22           C  
ANISOU 1355  CE2 PHE A 405     3841   4030   2849   -332   -105   -295       C  
ATOM   1356  CZ  PHE A 405       0.013  54.167  37.528  1.00 27.57           C  
ANISOU 1356  CZ  PHE A 405     3789   3917   2770   -288   -187   -253       C  
ATOM   1357  N   LEU A 406      -1.799  51.665  33.104  1.00 29.42           N  
ANISOU 1357  N   LEU A 406     3869   4146   3164   -384     47   -370       N  
ATOM   1358  CA  LEU A 406      -0.670  52.109  32.302  1.00 25.91           C  
ANISOU 1358  CA  LEU A 406     3378   3712   2754   -418     70   -454       C  
ATOM   1359  C   LEU A 406      -1.023  53.370  31.542  1.00 31.83           C  
ANISOU 1359  C   LEU A 406     4179   4506   3411   -465    117   -473       C  
ATOM   1360  O   LEU A 406      -2.181  53.782  31.499  1.00 33.78           O  
ANISOU 1360  O   LEU A 406     4485   4772   3580   -465    126   -428       O  
ATOM   1361  CB  LEU A 406      -0.210  51.018  31.323  1.00 27.31           C  
ANISOU 1361  CB  LEU A 406     3484   3857   3033   -435    106   -522       C  
ATOM   1362  CG  LEU A 406      -1.137  50.381  30.276  1.00 28.11           C  
ANISOU 1362  CG  LEU A 406     3597   3955   3129   -460    157   -536       C  
ATOM   1363  CD1 LEU A 406      -1.511  51.308  29.127  1.00 23.87           C  
ANISOU 1363  CD1 LEU A 406     3110   3454   2505   -516    212   -572       C  
ATOM   1364  CD2 LEU A 406      -0.499  49.114  29.716  1.00 34.18           C  
ANISOU 1364  CD2 LEU A 406     4292   4678   4017   -460    175   -598       C  
ATOM   1365  N   TYR A 407      -0.011  53.976  30.942  1.00 33.32           N  
ANISOU 1365  N   TYR A 407     4343   4703   3613   -504    148   -542       N  
ATOM   1366  CA  TYR A 407      -0.224  55.053  29.997  1.00 28.15           C  
ANISOU 1366  CA  TYR A 407     3746   4077   2874   -557    201   -569       C  
ATOM   1367  C   TYR A 407       0.438  54.713  28.666  1.00 33.49           C  
ANISOU 1367  C   TYR A 407     4392   4741   3594   -612    275   -658       C  
ATOM   1368  O   TYR A 407       1.509  54.108  28.636  1.00 33.13           O  
ANISOU 1368  O   TYR A 407     4263   4671   3654   -614    289   -717       O  
ATOM   1369  CB  TYR A 407       0.339  56.364  30.533  1.00 23.70           C  
ANISOU 1369  CB  TYR A 407     3209   3533   2262   -568    186   -567       C  
ATOM   1370  CG  TYR A 407      -0.457  57.016  31.639  1.00 28.86           C  
ANISOU 1370  CG  TYR A 407     3924   4203   2838   -528    133   -487       C  
ATOM   1371  CD1 TYR A 407      -0.292  56.634  32.962  1.00 17.54           C  
ANISOU 1371  CD1 TYR A 407     2476   2758   1432   -476     68   -443       C  
ATOM   1372  CD2 TYR A 407      -1.348  58.041  31.360  1.00 29.77           C  
ANISOU 1372  CD2 TYR A 407     4120   4341   2851   -542    149   -459       C  
ATOM   1373  CE1 TYR A 407      -1.003  57.248  33.973  1.00 25.39           C  
ANISOU 1373  CE1 TYR A 407     3536   3763   2346   -445     35   -376       C  
ATOM   1374  CE2 TYR A 407      -2.066  58.662  32.360  1.00 23.52           C  
ANISOU 1374  CE2 TYR A 407     3379   3560   1996   -506    113   -396       C  
ATOM   1375  CZ  TYR A 407      -1.891  58.262  33.667  1.00 25.81           C  
ANISOU 1375  CZ  TYR A 407     3657   3841   2309   -460     64   -357       C  
ATOM   1376  OH  TYR A 407      -2.598  58.869  34.673  1.00 24.73           O  
ANISOU 1376  OH  TYR A 407     3582   3713   2103   -429     42   -300       O  
ATOM   1377  N   SER A 408      -0.199  55.101  27.569  1.00 25.76           N  
ANISOU 1377  N   SER A 408     3482   3771   2533   -657    321   -672       N  
ATOM   1378  CA  SER A 408       0.439  54.999  26.267  1.00 32.73           C  
ANISOU 1378  CA  SER A 408     4368   4641   3425   -722    404   -759       C  
ATOM   1379  C   SER A 408       0.569  56.399  25.685  1.00 37.75           C  
ANISOU 1379  C   SER A 408     5094   5294   3957   -779    445   -772       C  
ATOM   1380  O   SER A 408      -0.382  57.178  25.710  1.00 41.64           O  
ANISOU 1380  O   SER A 408     5672   5802   4347   -773    410   -716       O  
ATOM   1381  CB  SER A 408      -0.342  54.089  25.318  1.00 31.17           C  
ANISOU 1381  CB  SER A 408     4197   4428   3220   -733    423   -773       C  
ATOM   1382  OG  SER A 408       0.317  53.964  24.070  1.00 28.53           O  
ANISOU 1382  OG  SER A 408     3878   4076   2884   -800    513   -862       O  
ATOM   1383  N   LYS A 409       1.756  56.721  25.180  1.00 34.65           N  
ANISOU 1383  N   LYS A 409     4678   4890   3597   -836    521   -850       N  
ATOM   1384  CA  LYS A 409       2.018  58.056  24.669  1.00 29.25           C  
ANISOU 1384  CA  LYS A 409     4078   4209   2826   -895    567   -860       C  
ATOM   1385  C   LYS A 409       2.293  58.044  23.172  1.00 37.33           C  
ANISOU 1385  C   LYS A 409     5144   5189   3851   -952    649   -890       C  
ATOM   1386  O   LYS A 409       3.299  57.501  22.723  1.00 39.75           O  
ANISOU 1386  O   LYS A 409     5393   5484   4225  -1001    740   -989       O  
ATOM   1387  CB  LYS A 409       3.199  58.690  25.408  1.00 18.58           C  
ANISOU 1387  CB  LYS A 409     2660   2862   1536   -907    578   -894       C  
ATOM   1388  CG  LYS A 409       3.485  60.128  25.009  1.00 21.88           C  
ANISOU 1388  CG  LYS A 409     3154   3269   1889   -959    615   -883       C  
ATOM   1389  CD  LYS A 409       4.494  60.769  25.949  1.00 30.48           C  
ANISOU 1389  CD  LYS A 409     4183   4373   3025   -971    609   -924       C  
ATOM   1390  CE  LYS A 409       5.879  60.156  25.794  1.00 28.93           C  
ANISOU 1390  CE  LYS A 409     3854   4154   2983  -1001    674  -1025       C  
ATOM   1391  NZ  LYS A 409       6.505  60.487  24.482  1.00 22.12           N1+
ANISOU 1391  NZ  LYS A 409     3032   3269   2103  -1104    820  -1110       N1+
ATOM   1392  N   LEU A 410       1.389  58.646  22.406  1.00 31.61           N  
ANISOU 1392  N   LEU A 410     4517   4435   3057   -943    613   -811       N  
ATOM   1393  CA  LEU A 410       1.594  58.817  20.977  1.00 31.73           C  
ANISOU 1393  CA  LEU A 410     4601   4406   3050  -1000    676   -828       C  
ATOM   1394  C   LEU A 410       2.105  60.224  20.677  1.00 44.60           C  
ANISOU 1394  C   LEU A 410     6290   6009   4647  -1043    705   -808       C  
ATOM   1395  O   LEU A 410       1.526  61.219  21.118  1.00 48.38           O  
ANISOU 1395  O   LEU A 410     6811   6487   5083  -1005    635   -735       O  
ATOM   1396  CB  LEU A 410       0.300  58.546  20.204  1.00 30.47           C  
ANISOU 1396  CB  LEU A 410     4519   4225   2833   -968    614   -772       C  
ATOM   1397  CG  LEU A 410       0.327  58.869  18.708  1.00 35.37           C  
ANISOU 1397  CG  LEU A 410     5240   4795   3403  -1021    656   -775       C  
ATOM   1398  CD1 LEU A 410       1.275  57.936  17.974  1.00 30.84           C  
ANISOU 1398  CD1 LEU A 410     4636   4206   2875  -1085    767   -868       C  
ATOM   1399  CD2 LEU A 410      -1.064  58.817  18.092  1.00 30.80           C  
ANISOU 1399  CD2 LEU A 410     4742   4201   2762   -979    568   -717       C  
ATOM   1400  N   THR A 411       3.202  60.299  19.931  1.00 38.54           N  
ANISOU 1400  N   THR A 411     5521   5215   3907  -1125    816   -879       N  
ATOM   1401  CA  THR A 411       3.793  61.579  19.582  1.00 34.61           C  
ANISOU 1401  CA  THR A 411     5082   4686   3382  -1183    861   -873       C  
ATOM   1402  C   THR A 411       3.509  61.917  18.124  1.00 39.19           C  
ANISOU 1402  C   THR A 411     5788   5209   3895  -1229    891   -851       C  
ATOM   1403  O   THR A 411       3.829  61.140  17.226  1.00 43.92           O  
ANISOU 1403  O   THR A 411     6396   5787   4507  -1274    964   -904       O  
ATOM   1404  CB  THR A 411       5.310  61.580  19.819  1.00 36.38           C  
ANISOU 1404  CB  THR A 411     5217   4916   3691  -1257    977   -981       C  
ATOM   1405  CG2 THR A 411       5.890  62.954  19.527  1.00 26.89           C  
ANISOU 1405  CG2 THR A 411     4078   3678   2459  -1325   1026   -975       C  
ATOM   1406  OG1 THR A 411       5.583  61.229  21.181  1.00 26.75           O  
ANISOU 1406  OG1 THR A 411     3883   3749   2531  -1211    940  -1013       O  
ATOM   1407  N   VAL A 412       2.893  63.075  17.898  1.00 35.82           N  
ANISOU 1407  N   VAL A 412     5461   4755   3395  -1215    833   -775       N  
ATOM   1408  CA  VAL A 412       2.583  63.530  16.547  1.00 34.02           C  
ANISOU 1408  CA  VAL A 412     5368   4468   3092  -1257    848   -751       C  
ATOM   1409  C   VAL A 412       3.068  64.963  16.319  1.00 41.15           C  
ANISOU 1409  C   VAL A 412     6350   5327   3957  -1315    883   -735       C  
ATOM   1410  O   VAL A 412       3.286  65.711  17.274  1.00 43.39           O  
ANISOU 1410  O   VAL A 412     6593   5630   4263  -1298    860   -720       O  
ATOM   1411  CB  VAL A 412       1.062  63.461  16.250  1.00 29.34           C  
ANISOU 1411  CB  VAL A 412     4840   3871   2436  -1178    726   -675       C  
ATOM   1412  CG1 VAL A 412       0.506  62.082  16.590  1.00 29.79           C  
ANISOU 1412  CG1 VAL A 412     4819   3970   2530  -1122    687   -690       C  
ATOM   1413  CG2 VAL A 412       0.310  64.541  17.014  1.00 32.51           C  
ANISOU 1413  CG2 VAL A 412     5256   4280   2816  -1111    627   -602       C  
ATOM   1414  N   ASP A 413       3.253  65.338  15.056  1.00 49.52           N  
ANISOU 1414  N   ASP A 413     7531   6326   4959  -1388    941   -741       N  
ATOM   1415  CA  ASP A 413       3.518  66.730  14.717  1.00 45.11           C  
ANISOU 1415  CA  ASP A 413     7077   5714   4350  -1442    964   -717       C  
ATOM   1416  C   ASP A 413       2.340  67.586  15.164  1.00 42.50           C  
ANISOU 1416  C   ASP A 413     6791   5385   3973  -1353    827   -626       C  
ATOM   1417  O   ASP A 413       1.182  67.206  14.968  1.00 47.26           O  
ANISOU 1417  O   ASP A 413     7416   5998   4544  -1279    730   -580       O  
ATOM   1418  CB  ASP A 413       3.767  66.897  13.216  1.00 56.77           C  
ANISOU 1418  CB  ASP A 413     8697   7116   5758  -1533   1042   -734       C  
ATOM   1419  CG  ASP A 413       5.136  66.396  12.789  1.00 71.76           C  
ANISOU 1419  CG  ASP A 413    10558   8996   7711  -1643   1206   -837       C  
ATOM   1420  OD1 ASP A 413       6.080  66.476  13.606  1.00 75.53           O  
ANISOU 1420  OD1 ASP A 413    10923   9500   8273  -1672   1270   -894       O  
ATOM   1421  OD2 ASP A 413       5.270  65.927  11.638  1.00 77.89           O1-
ANISOU 1421  OD2 ASP A 413    11416   9729   8450  -1701   1273   -866       O1-
ATOM   1422  N   LYS A 414       2.638  68.729  15.780  1.00 43.89           N  
ANISOU 1422  N   LYS A 414     6973   5552   4152  -1363    823   -608       N  
ATOM   1423  CA  LYS A 414       1.603  69.620  16.294  1.00 48.81           C  
ANISOU 1423  CA  LYS A 414     7628   6174   4743  -1280    704   -531       C  
ATOM   1424  C   LYS A 414       0.602  69.989  15.210  1.00 56.04           C  
ANISOU 1424  C   LYS A 414     8682   7036   5576  -1266    641   -481       C  
ATOM   1425  O   LYS A 414      -0.603  70.031  15.449  1.00 60.71           O  
ANISOU 1425  O   LYS A 414     9272   7642   6153  -1175    528   -431       O  
ATOM   1426  CB  LYS A 414       2.218  70.889  16.883  1.00 44.15           C  
ANISOU 1426  CB  LYS A 414     7053   5565   4159  -1317    729   -528       C  
ATOM   1427  CG  LYS A 414       1.191  71.978  17.167  1.00 45.04           C  
ANISOU 1427  CG  LYS A 414     7226   5656   4230  -1247    621   -455       C  
ATOM   1428  CD  LYS A 414       1.748  73.078  18.048  1.00 44.35           C  
ANISOU 1428  CD  LYS A 414     7125   5565   4161  -1266    635   -454       C  
ATOM   1429  CE  LYS A 414       2.812  73.888  17.328  1.00 41.77           C  
ANISOU 1429  CE  LYS A 414     6896   5170   3803  -1394    744   -490       C  
ATOM   1430  NZ  LYS A 414       3.435  74.905  18.222  1.00 47.80           N1+
ANISOU 1430  NZ  LYS A 414     7641   5932   4588  -1422    765   -500       N1+
ATOM   1431  N   SER A 415       1.116  70.244  14.012  1.00 56.12           N  
ANISOU 1431  N   SER A 415     8814   6980   5530  -1361    719   -502       N  
ATOM   1432  CA  SER A 415       0.286  70.625  12.876  1.00 54.30           C  
ANISOU 1432  CA  SER A 415     8739   6687   5208  -1363    665   -461       C  
ATOM   1433  C   SER A 415      -0.778  69.572  12.547  1.00 48.61           C  
ANISOU 1433  C   SER A 415     7999   5995   4474  -1291    582   -446       C  
ATOM   1434  O   SER A 415      -1.925  69.918  12.248  1.00 55.26           O  
ANISOU 1434  O   SER A 415     8911   6817   5269  -1234    473   -397       O  
ATOM   1435  CB  SER A 415       1.166  70.883  11.655  1.00 53.82           C  
ANISOU 1435  CB  SER A 415     8813   6548   5089  -1490    783   -497       C  
ATOM   1436  OG  SER A 415       2.052  69.801  11.427  1.00 63.14           O  
ANISOU 1436  OG  SER A 415     9926   7751   6313  -1548    894   -569       O  
ATOM   1437  N   ARG A 416      -0.393  68.297  12.599  1.00 44.20           N  
ANISOU 1437  N   ARG A 416     7351   5481   3963  -1297    633   -494       N  
ATOM   1438  CA  ARG A 416      -1.332  67.195  12.389  1.00 47.44           C  
ANISOU 1438  CA  ARG A 416     7731   5923   4371  -1234    561   -490       C  
ATOM   1439  C   ARG A 416      -2.468  67.269  13.402  1.00 54.34           C  
ANISOU 1439  C   ARG A 416     8524   6845   5278  -1119    435   -444       C  
ATOM   1440  O   ARG A 416      -3.638  67.077  13.064  1.00 56.66           O  
ANISOU 1440  O   ARG A 416     8854   7135   5538  -1064    336   -416       O  
ATOM   1441  CB  ARG A 416      -0.619  65.841  12.489  1.00 42.92           C  
ANISOU 1441  CB  ARG A 416     7058   5391   3857  -1260    644   -555       C  
ATOM   1442  CG  ARG A 416      -0.116  65.305  11.159  1.00 53.92           C  
ANISOU 1442  CG  ARG A 416     8547   6738   5202  -1347    734   -600       C  
ATOM   1443  CD  ARG A 416      -0.571  63.876  10.931  1.00 51.87           C  
ANISOU 1443  CD  ARG A 416     8238   6511   4958  -1314    714   -628       C  
ATOM   1444  NE  ARG A 416       0.158  62.933  11.771  1.00 47.59           N  
ANISOU 1444  NE  ARG A 416     7543   6023   4514  -1311    778   -684       N  
ATOM   1445  CZ  ARG A 416      -0.197  61.664  11.938  1.00 45.35           C  
ANISOU 1445  CZ  ARG A 416     7185   5778   4269  -1271    757   -710       C  
ATOM   1446  NH1 ARG A 416       0.522  60.867  12.717  1.00 44.05           N1+
ANISOU 1446  NH1 ARG A 416     6887   5656   4196  -1272    817   -764       N1+
ATOM   1447  NH2 ARG A 416      -1.277  61.191  11.330  1.00 34.79           N  
ANISOU 1447  NH2 ARG A 416     5907   4433   2878  -1232    672   -687       N  
ATOM   1448  N   TRP A 417      -2.110  67.564  14.647  1.00 46.75           N  
ANISOU 1448  N   TRP A 417     7457   5925   4381  -1089    441   -442       N  
ATOM   1449  CA  TRP A 417      -3.091  67.686  15.713  1.00 44.86           C  
ANISOU 1449  CA  TRP A 417     7140   5729   4176   -989    339   -404       C  
ATOM   1450  C   TRP A 417      -3.993  68.895  15.505  1.00 49.08           C  
ANISOU 1450  C   TRP A 417     7765   6222   4660   -955    254   -351       C  
ATOM   1451  O   TRP A 417      -5.206  68.809  15.690  1.00 47.85           O  
ANISOU 1451  O   TRP A 417     7598   6080   4502   -882    155   -324       O  
ATOM   1452  CB  TRP A 417      -2.396  67.782  17.073  1.00 40.80           C  
ANISOU 1452  CB  TRP A 417     6508   5261   3733   -974    372   -416       C  
ATOM   1453  CG  TRP A 417      -3.343  68.046  18.193  1.00 35.80           C  
ANISOU 1453  CG  TRP A 417     5810   4664   3128   -879    281   -377       C  
ATOM   1454  CD1 TRP A 417      -3.492  69.211  18.883  1.00 37.69           C  
ANISOU 1454  CD1 TRP A 417     6056   4896   3368   -851    249   -345       C  
ATOM   1455  CD2 TRP A 417      -4.292  67.126  18.747  1.00 36.58           C  
ANISOU 1455  CD2 TRP A 417     5835   4808   3257   -805    217   -370       C  
ATOM   1456  CE2 TRP A 417      -4.980  67.804  19.774  1.00 37.50           C  
ANISOU 1456  CE2 TRP A 417     5914   4942   3391   -737    154   -335       C  
ATOM   1457  CE3 TRP A 417      -4.628  65.796  18.473  1.00 36.74           C  
ANISOU 1457  CE3 TRP A 417     5819   4850   3290   -797    211   -393       C  
ATOM   1458  NE1 TRP A 417      -4.471  69.074  19.838  1.00 41.29           N  
ANISOU 1458  NE1 TRP A 417     6445   5392   3853   -764    174   -321       N  
ATOM   1459  CZ2 TRP A 417      -5.980  67.195  20.531  1.00 32.41           C  
ANISOU 1459  CZ2 TRP A 417     5202   4337   2775   -666     94   -323       C  
ATOM   1460  CZ3 TRP A 417      -5.623  65.196  19.223  1.00 38.03           C  
ANISOU 1460  CZ3 TRP A 417     5915   5051   3482   -727    145   -380       C  
ATOM   1461  CH2 TRP A 417      -6.287  65.895  20.242  1.00 34.28           C  
ANISOU 1461  CH2 TRP A 417     5408   4594   3024   -665     90   -345       C  
ATOM   1462  N   GLN A 418      -3.390  70.015  15.121  1.00 51.68           N  
ANISOU 1462  N   GLN A 418     8188   6497   4951  -1015    295   -342       N  
ATOM   1463  CA  GLN A 418      -4.114  71.264  14.909  1.00 54.90           C  
ANISOU 1463  CA  GLN A 418     8697   6854   5309   -994    222   -295       C  
ATOM   1464  C   GLN A 418      -5.203  71.141  13.844  1.00 54.90           C  
ANISOU 1464  C   GLN A 418     8804   6813   5244   -975    137   -272       C  
ATOM   1465  O   GLN A 418      -6.189  71.873  13.872  1.00 61.33           O  
ANISOU 1465  O   GLN A 418     9667   7600   6034   -925     39   -235       O  
ATOM   1466  CB  GLN A 418      -3.140  72.377  14.509  1.00 60.78           C  
ANISOU 1466  CB  GLN A 418     9544   7534   6016  -1083    297   -296       C  
ATOM   1467  CG  GLN A 418      -2.175  72.817  15.597  1.00 68.03           C  
ANISOU 1467  CG  GLN A 418    10375   8482   6992  -1101    361   -315       C  
ATOM   1468  CD  GLN A 418      -2.748  73.917  16.468  1.00 78.64           C  
ANISOU 1468  CD  GLN A 418    11711   9823   8344  -1041    288   -275       C  
ATOM   1469  NE2 GLN A 418      -1.872  74.683  17.111  1.00 76.84           N  
ANISOU 1469  NE2 GLN A 418    11468   9590   8137  -1080    343   -286       N  
ATOM   1470  OE1 GLN A 418      -3.965  74.084  16.555  1.00 82.40           O  
ANISOU 1470  OE1 GLN A 418    12199  10300   8809   -964    187   -240       O  
ATOM   1471  N   GLN A 419      -5.021  70.214  12.910  1.00 50.05           N  
ANISOU 1471  N   GLN A 419     8228   6189   4600  -1018    171   -299       N  
ATOM   1472  CA  GLN A 419      -5.914  70.106  11.762  1.00 55.64           C  
ANISOU 1472  CA  GLN A 419     9060   6848   5234  -1015     94   -283       C  
ATOM   1473  C   GLN A 419      -7.139  69.236  12.011  1.00 61.31           C  
ANISOU 1473  C   GLN A 419     9704   7613   5979   -931    -11   -281       C  
ATOM   1474  O   GLN A 419      -7.975  69.066  11.124  1.00 70.54           O  
ANISOU 1474  O   GLN A 419    10964   8744   7093   -923    -92   -272       O  
ATOM   1475  CB  GLN A 419      -5.148  69.570  10.555  1.00 64.24           C  
ANISOU 1475  CB  GLN A 419    10246   7896   6266  -1108    182   -316       C  
ATOM   1476  CG  GLN A 419      -4.249  70.596   9.909  1.00 81.18           C  
ANISOU 1476  CG  GLN A 419    12529   9963   8352  -1204    264   -312       C  
ATOM   1477  CD  GLN A 419      -3.794  70.165   8.537  1.00 96.37           C  
ANISOU 1477  CD  GLN A 419    14588  11829  10197  -1294    332   -338       C  
ATOM   1478  NE2 GLN A 419      -3.547  71.135   7.662  1.00104.36           N  
ANISOU 1478  NE2 GLN A 419    15782  12747  11123  -1366    355   -320       N  
ATOM   1479  OE1 GLN A 419      -3.667  68.972   8.261  1.00 97.10           O  
ANISOU 1479  OE1 GLN A 419    14633  11957  10304  -1301    367   -376       O  
ATOM   1480  N   GLY A 420      -7.245  68.678  13.210  1.00 55.32           N  
ANISOU 1480  N   GLY A 420     8788   6930   5303   -875    -11   -293       N  
ATOM   1481  CA  GLY A 420      -8.433  67.930  13.582  1.00 49.67           C  
ANISOU 1481  CA  GLY A 420     7999   6255   4619   -801   -107   -294       C  
ATOM   1482  C   GLY A 420      -8.429  66.469  13.178  1.00 46.80           C  
ANISOU 1482  C   GLY A 420     7597   5920   4265   -813    -88   -334       C  
ATOM   1483  O   GLY A 420      -9.484  65.835  13.145  1.00 46.65           O  
ANISOU 1483  O   GLY A 420     7554   5917   4255   -767   -176   -339       O  
ATOM   1484  N   ASN A 421      -7.255  65.931  12.866  1.00 42.52           N  
ANISOU 1484  N   ASN A 421     7052   5379   3724   -878     25   -368       N  
ATOM   1485  CA  ASN A 421      -7.136  64.501  12.597  1.00 51.43           C  
ANISOU 1485  CA  ASN A 421     8135   6536   4871   -891     56   -412       C  
ATOM   1486  C   ASN A 421      -7.576  63.680  13.804  1.00 51.51           C  
ANISOU 1486  C   ASN A 421     7997   6613   4962   -827     28   -422       C  
ATOM   1487  O   ASN A 421      -7.228  63.996  14.943  1.00 51.34           O  
ANISOU 1487  O   ASN A 421     7888   6626   4994   -803     53   -412       O  
ATOM   1488  CB  ASN A 421      -5.700  64.138  12.207  1.00 61.78           C  
ANISOU 1488  CB  ASN A 421     9454   7838   6182   -974    195   -453       C  
ATOM   1489  CG  ASN A 421      -5.350  64.571  10.797  1.00 67.36           C  
ANISOU 1489  CG  ASN A 421    10323   8473   6798  -1051    232   -455       C  
ATOM   1490  ND2 ASN A 421      -4.608  65.665  10.677  1.00 66.26           N  
ANISOU 1490  ND2 ASN A 421    10249   8293   6634  -1102    291   -440       N  
ATOM   1491  OD1 ASN A 421      -5.738  63.922   9.824  1.00 77.85           O  
ANISOU 1491  OD1 ASN A 421    11725   9778   8076  -1068    210   -472       O  
ATOM   1492  N   VAL A 422      -8.354  62.632  13.556  1.00 52.48           N  
ANISOU 1492  N   VAL A 422     8100   6750   5090   -805    -27   -444       N  
ATOM   1493  CA  VAL A 422      -8.826  61.768  14.631  1.00 46.01           C  
ANISOU 1493  CA  VAL A 422     7156   5984   4340   -757    -53   -457       C  
ATOM   1494  C   VAL A 422      -7.840  60.638  14.894  1.00 43.80           C  
ANISOU 1494  C   VAL A 422     6805   5732   4106   -792     47   -502       C  
ATOM   1495  O   VAL A 422      -7.370  59.982  13.962  1.00 49.90           O  
ANISOU 1495  O   VAL A 422     7623   6484   4853   -842     96   -539       O  
ATOM   1496  CB  VAL A 422     -10.209  61.185  14.304  1.00 39.10           C  
ANISOU 1496  CB  VAL A 422     6291   5108   3459   -722   -168   -464       C  
ATOM   1497  CG1 VAL A 422     -10.644  60.192  15.375  1.00 40.33           C  
ANISOU 1497  CG1 VAL A 422     6326   5312   3685   -689   -182   -483       C  
ATOM   1498  CG2 VAL A 422     -11.215  62.307  14.175  1.00 28.38           C  
ANISOU 1498  CG2 VAL A 422     4990   3722   2070   -683   -275   -424       C  
ATOM   1499  N   PHE A 423      -7.518  60.425  16.167  1.00 42.18           N  
ANISOU 1499  N   PHE A 423     6491   5569   3965   -769     77   -501       N  
ATOM   1500  CA  PHE A 423      -6.606  59.362  16.563  1.00 38.27           C  
ANISOU 1500  CA  PHE A 423     5920   5100   3521   -799    162   -545       C  
ATOM   1501  C   PHE A 423      -7.317  58.375  17.478  1.00 32.04           C  
ANISOU 1501  C   PHE A 423     5043   4349   2783   -760    121   -553       C  
ATOM   1502  O   PHE A 423      -8.186  58.759  18.264  1.00 40.41           O  
ANISOU 1502  O   PHE A 423     6074   5427   3853   -711     54   -518       O  
ATOM   1503  CB  PHE A 423      -5.368  59.943  17.249  1.00 35.69           C  
ANISOU 1503  CB  PHE A 423     5551   4785   3226   -821    244   -545       C  
ATOM   1504  CG  PHE A 423      -4.537  60.822  16.356  1.00 32.85           C  
ANISOU 1504  CG  PHE A 423     5275   4384   2823   -879    304   -548       C  
ATOM   1505  CD1 PHE A 423      -4.910  62.137  16.119  1.00 38.50           C  
ANISOU 1505  CD1 PHE A 423     6067   5071   3491   -867    259   -501       C  
ATOM   1506  CD2 PHE A 423      -3.393  60.334  15.743  1.00 31.18           C  
ANISOU 1506  CD2 PHE A 423     5071   4158   2619   -952    410   -603       C  
ATOM   1507  CE1 PHE A 423      -4.158  62.948  15.292  1.00 35.83           C  
ANISOU 1507  CE1 PHE A 423     5818   4688   3107   -931    317   -504       C  
ATOM   1508  CE2 PHE A 423      -2.635  61.142  14.912  1.00 41.72           C  
ANISOU 1508  CE2 PHE A 423     6492   5450   3911  -1017    475   -609       C  
ATOM   1509  CZ  PHE A 423      -3.021  62.452  14.688  1.00 36.46           C  
ANISOU 1509  CZ  PHE A 423     5909   4753   3191  -1009    428   -557       C  
ATOM   1510  N   SER A 424      -6.959  57.100  17.371  1.00 31.54           N  
ANISOU 1510  N   SER A 424     4938   4294   2750   -789    167   -604       N  
ATOM   1511  CA  SER A 424      -7.608  56.066  18.169  1.00 39.19           C  
ANISOU 1511  CA  SER A 424     5831   5295   3767   -767    135   -619       C  
ATOM   1512  C   SER A 424      -6.629  55.245  19.002  1.00 31.86           C  
ANISOU 1512  C   SER A 424     4811   4395   2899   -785    216   -657       C  
ATOM   1513  O   SER A 424      -5.575  54.819  18.527  1.00 37.33           O  
ANISOU 1513  O   SER A 424     5499   5077   3609   -828    298   -706       O  
ATOM   1514  CB  SER A 424      -8.426  55.137  17.265  1.00 40.76           C  
ANISOU 1514  CB  SER A 424     6064   5471   3951   -779     86   -654       C  
ATOM   1515  OG  SER A 424      -9.614  55.776  16.825  1.00 50.87           O  
ANISOU 1515  OG  SER A 424     7405   6733   5189   -749    -20   -622       O  
ATOM   1516  N   CYS A 425      -6.993  55.039  20.263  1.00 33.58           N  
ANISOU 1516  N   CYS A 425     4958   4649   3150   -755    192   -637       N  
ATOM   1517  CA  CYS A 425      -6.253  54.154  21.148  1.00 35.31           C  
ANISOU 1517  CA  CYS A 425     5092   4898   3426   -765    249   -676       C  
ATOM   1518  C   CYS A 425      -6.979  52.814  21.237  1.00 34.15           C  
ANISOU 1518  C   CYS A 425     4904   4754   3317   -768    226   -709       C  
ATOM   1519  O   CYS A 425      -8.113  52.745  21.713  1.00 32.58           O  
ANISOU 1519  O   CYS A 425     4678   4557   3145   -727    159   -659       O  
ATOM   1520  CB  CYS A 425      -6.100  54.785  22.533  1.00 29.04           C  
ANISOU 1520  CB  CYS A 425     4254   4139   2640   -731    240   -630       C  
ATOM   1521  SG  CYS A 425      -5.272  53.735  23.740  1.00 33.34           S  
ANISOU 1521  SG  CYS A 425     4680   4700   3288   -709    277   -645       S  
ATOM   1522  N   SER A 426      -6.334  51.756  20.755  1.00 36.44           N  
ANISOU 1522  N   SER A 426     5162   5023   3661   -793    279   -771       N  
ATOM   1523  CA  SER A 426      -6.936  50.425  20.776  1.00 36.95           C  
ANISOU 1523  CA  SER A 426     5162   5062   3816   -772    255   -777       C  
ATOM   1524  C   SER A 426      -6.356  49.604  21.913  1.00 33.48           C  
ANISOU 1524  C   SER A 426     4604   4619   3498   -730    280   -758       C  
ATOM   1525  O   SER A 426      -5.141  49.528  22.082  1.00 31.56           O  
ANISOU 1525  O   SER A 426     4327   4375   3289   -737    338   -792       O  
ATOM   1526  CB  SER A 426      -6.726  49.702  19.441  1.00 34.74           C  
ANISOU 1526  CB  SER A 426     4933   4749   3516   -826    288   -862       C  
ATOM   1527  OG  SER A 426      -7.397  50.365  18.382  1.00 51.15           O  
ANISOU 1527  OG  SER A 426     7131   6818   5484   -855    242   -865       O  
ATOM   1528  N   VAL A 427      -7.240  48.997  22.697  1.00 28.16           N  
ANISOU 1528  N   VAL A 427     3872   3936   2892   -686    233   -703       N  
ATOM   1529  CA  VAL A 427      -6.825  48.192  23.836  1.00 29.33           C  
ANISOU 1529  CA  VAL A 427     3930   4070   3144   -644    244   -672       C  
ATOM   1530  C   VAL A 427      -7.405  46.786  23.736  1.00 34.45           C  
ANISOU 1530  C   VAL A 427     4530   4675   3884   -636    233   -680       C  
ATOM   1531  O   VAL A 427      -8.595  46.604  23.466  1.00 39.06           O  
ANISOU 1531  O   VAL A 427     5124   5250   4467   -640    194   -665       O  
ATOM   1532  CB  VAL A 427      -7.253  48.824  25.177  1.00 29.80           C  
ANISOU 1532  CB  VAL A 427     3974   4153   3195   -598    213   -585       C  
ATOM   1533  CG1 VAL A 427      -6.714  48.016  26.340  1.00 24.19           C  
ANISOU 1533  CG1 VAL A 427     3198   3421   2574   -558    217   -551       C  
ATOM   1534  CG2 VAL A 427      -6.775  50.269  25.268  1.00 28.72           C  
ANISOU 1534  CG2 VAL A 427     3890   4056   2967   -607    218   -577       C  
ATOM   1535  N   MET A 428      -6.549  45.793  23.948  1.00 30.24           N  
ANISOU 1535  N   MET A 428     3940   4108   3440   -626    264   -709       N  
ATOM   1536  CA  MET A 428      -6.967  44.404  23.922  1.00 26.39           C  
ANISOU 1536  CA  MET A 428     3407   3570   3050   -618    258   -717       C  
ATOM   1537  C   MET A 428      -6.720  43.749  25.278  1.00 30.96           C  
ANISOU 1537  C   MET A 428     3926   4122   3716   -567    247   -655       C  
ATOM   1538  O   MET A 428      -5.596  43.739  25.783  1.00 28.63           O  
ANISOU 1538  O   MET A 428     3603   3822   3455   -545    258   -661       O  
ATOM   1539  CB  MET A 428      -6.239  43.661  22.803  1.00 27.20           C  
ANISOU 1539  CB  MET A 428     3508   3641   3186   -652    303   -816       C  
ATOM   1540  CG  MET A 428      -6.701  44.077  21.414  1.00 25.09           C  
ANISOU 1540  CG  MET A 428     3324   3385   2824   -707    305   -874       C  
ATOM   1541  SD  MET A 428      -5.445  43.861  20.144  1.00 49.36           S  
ANISOU 1541  SD  MET A 428     6431   6441   5882   -760    393   -996       S  
ATOM   1542  CE  MET A 428      -4.439  45.319  20.416  1.00 31.67           C  
ANISOU 1542  CE  MET A 428     4217   4251   3566   -769    434   -989       C  
ATOM   1543  N   HIS A 429      -7.788  43.217  25.866  1.00 29.77           N  
ANISOU 1543  N   HIS A 429     3761   3949   3602   -552    222   -596       N  
ATOM   1544  CA  HIS A 429      -7.741  42.628  27.201  1.00 34.84           C  
ANISOU 1544  CA  HIS A 429     4374   4557   4305   -510    212   -524       C  
ATOM   1545  C   HIS A 429      -8.914  41.657  27.385  1.00 35.34           C  
ANISOU 1545  C   HIS A 429     4419   4575   4433   -515    209   -492       C  
ATOM   1546  O   HIS A 429      -9.984  41.860  26.815  1.00 38.05           O  
ANISOU 1546  O   HIS A 429     4769   4931   4758   -542    201   -503       O  
ATOM   1547  CB  HIS A 429      -7.765  43.729  28.267  1.00 34.51           C  
ANISOU 1547  CB  HIS A 429     4362   4558   4192   -484    200   -453       C  
ATOM   1548  CG  HIS A 429      -7.614  43.224  29.667  1.00 34.35           C  
ANISOU 1548  CG  HIS A 429     4340   4503   4211   -444    187   -378       C  
ATOM   1549  CD2 HIS A 429      -6.516  43.047  30.439  1.00 28.51           C  
ANISOU 1549  CD2 HIS A 429     3595   3741   3495   -409    164   -361       C  
ATOM   1550  ND1 HIS A 429      -8.690  42.841  30.438  1.00 39.88           N  
ANISOU 1550  ND1 HIS A 429     5051   5178   4925   -439    194   -310       N  
ATOM   1551  CE1 HIS A 429      -8.262  42.443  31.622  1.00 45.00           C  
ANISOU 1551  CE1 HIS A 429     5720   5790   5590   -405    181   -249       C  
ATOM   1552  NE2 HIS A 429      -6.946  42.559  31.649  1.00 36.65           N  
ANISOU 1552  NE2 HIS A 429     4652   4733   4539   -383    152   -278       N  
ATOM   1553  N   GLU A 430      -8.711  40.605  28.176  1.00 28.23           N  
ANISOU 1553  N   GLU A 430     3497   3614   3614   -491    209   -455       N  
ATOM   1554  CA  GLU A 430      -9.704  39.536  28.277  1.00 31.65           C  
ANISOU 1554  CA  GLU A 430     3912   3991   4124   -504    217   -434       C  
ATOM   1555  C   GLU A 430     -11.007  39.994  28.927  1.00 37.66           C  
ANISOU 1555  C   GLU A 430     4684   4769   4858   -512    227   -368       C  
ATOM   1556  O   GLU A 430     -12.070  39.433  28.660  1.00 38.69           O  
ANISOU 1556  O   GLU A 430     4788   4869   5043   -538    236   -373       O  
ATOM   1557  CB  GLU A 430      -9.135  38.344  29.043  1.00 31.18           C  
ANISOU 1557  CB  GLU A 430     3842   3854   4152   -475    214   -402       C  
ATOM   1558  CG  GLU A 430      -8.877  38.603  30.512  1.00 34.66           C  
ANISOU 1558  CG  GLU A 430     4321   4287   4562   -437    203   -309       C  
ATOM   1559  CD  GLU A 430      -8.490  37.345  31.263  1.00 43.87           C  
ANISOU 1559  CD  GLU A 430     5495   5362   5812   -410    188   -268       C  
ATOM   1560  OE1 GLU A 430      -9.386  36.526  31.558  1.00 49.98           O  
ANISOU 1560  OE1 GLU A 430     6277   6081   6634   -429    212   -230       O  
ATOM   1561  OE2 GLU A 430      -7.290  37.176  31.560  1.00 46.25           O1-
ANISOU 1561  OE2 GLU A 430     5794   5640   6138   -371    150   -276       O1-
ATOM   1562  N   ALA A 431     -10.931  41.020  29.767  1.00 36.78           N  
ANISOU 1562  N   ALA A 431     4605   4701   4669   -490    228   -314       N  
ATOM   1563  CA  ALA A 431     -12.107  41.494  30.487  1.00 35.51           C  
ANISOU 1563  CA  ALA A 431     4453   4552   4488   -494    252   -256       C  
ATOM   1564  C   ALA A 431     -12.892  42.517  29.670  1.00 40.63           C  
ANISOU 1564  C   ALA A 431     5090   5255   5091   -513    238   -294       C  
ATOM   1565  O   ALA A 431     -13.854  43.108  30.157  1.00 36.57           O  
ANISOU 1565  O   ALA A 431     4573   4758   4565   -514    255   -259       O  
ATOM   1566  CB  ALA A 431     -11.707  42.081  31.820  1.00 25.83           C  
ANISOU 1566  CB  ALA A 431     3277   3339   3198   -462    262   -183       C  
ATOM   1567  N   LEU A 432     -12.477  42.726  28.426  1.00 34.63           N  
ANISOU 1567  N   LEU A 432     4331   4519   4310   -530    207   -367       N  
ATOM   1568  CA  LEU A 432     -13.224  43.582  27.520  1.00 36.31           C  
ANISOU 1568  CA  LEU A 432     4547   4768   4479   -549    175   -405       C  
ATOM   1569  C   LEU A 432     -14.132  42.732  26.645  1.00 40.27           C  
ANISOU 1569  C   LEU A 432     5010   5231   5058   -581    154   -452       C  
ATOM   1570  O   LEU A 432     -13.804  41.589  26.336  1.00 44.17           O  
ANISOU 1570  O   LEU A 432     5487   5679   5616   -594    162   -481       O  
ATOM   1571  CB  LEU A 432     -12.279  44.415  26.655  1.00 34.67           C  
ANISOU 1571  CB  LEU A 432     4388   4604   4182   -556    155   -455       C  
ATOM   1572  CG  LEU A 432     -11.579  45.602  27.318  1.00 30.78           C  
ANISOU 1572  CG  LEU A 432     3934   4159   3603   -532    163   -420       C  
ATOM   1573  CD1 LEU A 432     -10.455  46.091  26.425  1.00 35.05           C  
ANISOU 1573  CD1 LEU A 432     4513   4724   4081   -549    161   -479       C  
ATOM   1574  CD2 LEU A 432     -12.565  46.725  27.604  1.00 28.77           C  
ANISOU 1574  CD2 LEU A 432     3693   3937   3302   -522    147   -387       C  
ATOM   1575  N   HIS A 433     -15.278  43.282  26.256  1.00 38.30           N  
ANISOU 1575  N   HIS A 433     4744   4994   4812   -592    119   -463       N  
ATOM   1576  CA  HIS A 433     -16.147  42.612  25.295  1.00 36.59           C  
ANISOU 1576  CA  HIS A 433     4493   4743   4665   -623     77   -519       C  
ATOM   1577  C   HIS A 433     -15.413  42.477  23.964  1.00 43.08           C  
ANISOU 1577  C   HIS A 433     5368   5568   5432   -647     41   -594       C  
ATOM   1578  O   HIS A 433     -14.842  43.451  23.470  1.00 43.12           O  
ANISOU 1578  O   HIS A 433     5437   5615   5332   -645     22   -612       O  
ATOM   1579  CB  HIS A 433     -17.460  43.376  25.115  1.00 33.54           C  
ANISOU 1579  CB  HIS A 433     4077   4369   4296   -623     29   -522       C  
ATOM   1580  CG  HIS A 433     -18.534  42.583  24.439  1.00 41.34           C  
ANISOU 1580  CG  HIS A 433     5006   5310   5389   -653    -17   -569       C  
ATOM   1581  CD2 HIS A 433     -19.114  42.722  23.223  1.00 46.13           C  
ANISOU 1581  CD2 HIS A 433     5623   5911   5995   -672   -110   -634       C  
ATOM   1582  ND1 HIS A 433     -19.138  41.496  25.032  1.00 44.76           N  
ANISOU 1582  ND1 HIS A 433     5368   5692   5949   -668     30   -553       N  
ATOM   1583  CE1 HIS A 433     -20.045  41.000  24.209  1.00 51.31           C  
ANISOU 1583  CE1 HIS A 433     6150   6485   6860   -697    -31   -611       C  
ATOM   1584  NE2 HIS A 433     -20.050  41.725  23.105  1.00 49.74           N  
ANISOU 1584  NE2 HIS A 433     6002   6314   6585   -698   -123   -661       N  
ATOM   1585  N   ASN A 434     -15.422  41.265  23.406  1.00 41.15           N  
ANISOU 1585  N   ASN A 434     5104   5274   5259   -672     39   -641       N  
ATOM   1586  CA  ASN A 434     -14.681  40.925  22.189  1.00 40.36           C  
ANISOU 1586  CA  ASN A 434     5056   5164   5116   -699     25   -721       C  
ATOM   1587  C   ASN A 434     -13.163  41.040  22.356  1.00 46.35           C  
ANISOU 1587  C   ASN A 434     5849   5941   5822   -686     81   -725       C  
ATOM   1588  O   ASN A 434     -12.432  41.031  21.365  1.00 53.91           O  
ANISOU 1588  O   ASN A 434     6858   6900   6726   -710     88   -794       O  
ATOM   1589  CB  ASN A 434     -15.121  41.800  21.006  1.00 33.27           C  
ANISOU 1589  CB  ASN A 434     4224   4292   4126   -722    -49   -770       C  
ATOM   1590  CG  ASN A 434     -16.583  41.625  20.659  1.00 40.31           C  
ANISOU 1590  CG  ASN A 434     5074   5157   5085   -735   -126   -785       C  
ATOM   1591  ND2 ASN A 434     -17.213  42.701  20.194  1.00 45.40           N  
ANISOU 1591  ND2 ASN A 434     5756   5828   5666   -731   -202   -788       N  
ATOM   1592  OD1 ASN A 434     -17.144  40.540  20.798  1.00 50.24           O  
ANISOU 1592  OD1 ASN A 434     6266   6365   6458   -748   -122   -795       O  
ATOM   1593  N   HIS A 435     -12.707  41.147  23.605  1.00 33.95           N  
ANISOU 1593  N   HIS A 435     4252   4379   4270   -650    121   -656       N  
ATOM   1594  CA  HIS A 435     -11.293  41.350  23.923  1.00 37.22           C  
ANISOU 1594  CA  HIS A 435     4683   4809   4650   -631    161   -656       C  
ATOM   1595  C   HIS A 435     -10.745  42.616  23.267  1.00 38.92           C  
ANISOU 1595  C   HIS A 435     4961   5080   4745   -643    157   -687       C  
ATOM   1596  O   HIS A 435      -9.540  42.738  23.050  1.00 35.90           O  
ANISOU 1596  O   HIS A 435     4595   4706   4338   -646    193   -723       O  
ATOM   1597  CB  HIS A 435     -10.448  40.146  23.487  1.00 31.58           C  
ANISOU 1597  CB  HIS A 435     3950   4043   4007   -639    190   -715       C  
ATOM   1598  CG  HIS A 435     -10.793  38.865  24.182  1.00 30.86           C  
ANISOU 1598  CG  HIS A 435     3806   3886   4034   -625    197   -682       C  
ATOM   1599  CD2 HIS A 435     -11.423  38.625  25.355  1.00 38.08           C  
ANISOU 1599  CD2 HIS A 435     4694   4780   4995   -604    200   -598       C  
ATOM   1600  ND1 HIS A 435     -10.464  37.630  23.665  1.00 32.56           N  
ANISOU 1600  ND1 HIS A 435     4001   4039   4333   -637    210   -739       N  
ATOM   1601  CE1 HIS A 435     -10.883  36.685  24.487  1.00 34.03           C  
ANISOU 1601  CE1 HIS A 435     4150   4167   4613   -623    214   -687       C  
ATOM   1602  NE2 HIS A 435     -11.467  37.262  25.521  1.00 31.29           N  
ANISOU 1602  NE2 HIS A 435     3802   3844   4241   -605    212   -600       N  
ATOM   1603  N   TYR A 436     -11.626  43.555  22.943  1.00 37.82           N  
ANISOU 1603  N   TYR A 436     4857   4973   4541   -653    113   -676       N  
ATOM   1604  CA  TYR A 436     -11.221  44.722  22.178  1.00 36.62           C  
ANISOU 1604  CA  TYR A 436     4784   4862   4269   -672    103   -706       C  
ATOM   1605  C   TYR A 436     -12.131  45.920  22.413  1.00 35.90           C  
ANISOU 1605  C   TYR A 436     4716   4804   4119   -658     54   -659       C  
ATOM   1606  O   TYR A 436     -13.357  45.801  22.408  1.00 42.34           O  
ANISOU 1606  O   TYR A 436     5503   5605   4978   -653      4   -645       O  
ATOM   1607  CB  TYR A 436     -11.181  44.378  20.683  1.00 47.55           C  
ANISOU 1607  CB  TYR A 436     6228   6224   5614   -720     89   -793       C  
ATOM   1608  CG  TYR A 436     -10.896  45.556  19.775  1.00 66.82           C  
ANISOU 1608  CG  TYR A 436     8775   8695   7917   -750     77   -823       C  
ATOM   1609  CD1 TYR A 436      -9.589  45.919  19.465  1.00 77.58           C  
ANISOU 1609  CD1 TYR A 436    10182  10072   9222   -772    147   -861       C  
ATOM   1610  CD2 TYR A 436     -11.934  46.299  19.222  1.00 76.07           C  
ANISOU 1610  CD2 TYR A 436    10005   9873   9024   -758     -5   -816       C  
ATOM   1611  CE1 TYR A 436      -9.321  46.993  18.637  1.00 80.78           C  
ANISOU 1611  CE1 TYR A 436    10699  10498   9497   -808    148   -886       C  
ATOM   1612  CE2 TYR A 436     -11.678  47.376  18.395  1.00 84.71           C  
ANISOU 1612  CE2 TYR A 436    11216  10985   9984   -786    -22   -837       C  
ATOM   1613  CZ  TYR A 436     -10.368  47.719  18.104  1.00 85.18           C  
ANISOU 1613  CZ  TYR A 436    11330  11059   9977   -815     61   -870       C  
ATOM   1614  OH  TYR A 436     -10.106  48.788  17.279  1.00 86.15           O  
ANISOU 1614  OH  TYR A 436    11581  11192   9962   -852     56   -889       O  
ATOM   1615  N   THR A 437     -11.513  47.076  22.622  1.00 27.86           N  
ANISOU 1615  N   THR A 437     3745   3827   3014   -651     68   -640       N  
ATOM   1616  CA  THR A 437     -12.230  48.337  22.610  1.00 30.86           C  
ANISOU 1616  CA  THR A 437     4167   4234   3325   -641     19   -610       C  
ATOM   1617  C   THR A 437     -11.338  49.415  22.016  1.00 33.06           C  
ANISOU 1617  C   THR A 437     4538   4540   3484   -664     32   -634       C  
ATOM   1618  O   THR A 437     -10.131  49.228  21.871  1.00 31.35           O  
ANISOU 1618  O   THR A 437     4333   4326   3252   -684     93   -666       O  
ATOM   1619  CB  THR A 437     -12.695  48.751  24.012  1.00 35.71           C  
ANISOU 1619  CB  THR A 437     4727   4865   3975   -596     28   -535       C  
ATOM   1620  CG2 THR A 437     -11.515  49.193  24.862  1.00 35.12           C  
ANISOU 1620  CG2 THR A 437     4661   4818   3867   -580     80   -506       C  
ATOM   1621  OG1 THR A 437     -13.631  49.829  23.900  1.00 44.47           O  
ANISOU 1621  OG1 THR A 437     5863   5989   5044   -583    -27   -516       O  
ATOM   1622  N   GLN A 438     -11.935  50.547  21.672  1.00 35.60           N  
ANISOU 1622  N   GLN A 438     4924   4875   3729   -663    -23   -620       N  
ATOM   1623  CA  GLN A 438     -11.200  51.599  20.997  1.00 34.99           C  
ANISOU 1623  CA  GLN A 438     4953   4813   3529   -694    -12   -641       C  
ATOM   1624  C   GLN A 438     -11.759  52.967  21.367  1.00 36.09           C  
ANISOU 1624  C   GLN A 438     5129   4970   3612   -667    -60   -593       C  
ATOM   1625  O   GLN A 438     -12.965  53.186  21.303  1.00 50.87           O  
ANISOU 1625  O   GLN A 438     6992   6830   5507   -644   -137   -575       O  
ATOM   1626  CB  GLN A 438     -11.258  51.374  19.485  1.00 34.79           C  
ANISOU 1626  CB  GLN A 438     5023   4759   3435   -745    -40   -707       C  
ATOM   1627  CG  GLN A 438     -10.273  52.194  18.681  1.00 56.27           C  
ANISOU 1627  CG  GLN A 438     7857   7480   6043   -785      5   -732       C  
ATOM   1628  CD  GLN A 438     -10.459  52.007  17.187  1.00 66.69           C  
ANISOU 1628  CD  GLN A 438     9262   8752   7325   -803    -26   -760       C  
ATOM   1629  NE2 GLN A 438      -9.354  52.001  16.447  1.00 67.95           N  
ANISOU 1629  NE2 GLN A 438     9463   8894   7462   -828     57   -783       N  
ATOM   1630  OE1 GLN A 438     -11.582  51.860  16.705  1.00 67.75           O  
ANISOU 1630  OE1 GLN A 438     9424   8866   7452   -798   -124   -766       O  
ATOM   1631  N   LYS A 439     -10.881  53.881  21.767  1.00 30.33           N  
ANISOU 1631  N   LYS A 439     4435   4266   2822   -670    -15   -576       N  
ATOM   1632  CA  LYS A 439     -11.294  55.231  22.132  1.00 33.56           C  
ANISOU 1632  CA  LYS A 439     4887   4689   3176   -646    -54   -533       C  
ATOM   1633  C   LYS A 439     -10.652  56.261  21.209  1.00 41.05           C  
ANISOU 1633  C   LYS A 439     5931   5613   4053   -656    -48   -531       C  
ATOM   1634  O   LYS A 439      -9.481  56.142  20.847  1.00 36.86           O  
ANISOU 1634  O   LYS A 439     5408   5074   3525   -679     23   -550       O  
ATOM   1635  CB  LYS A 439     -10.941  55.525  23.593  1.00 34.88           C  
ANISOU 1635  CB  LYS A 439     4986   4884   3383   -607    -10   -485       C  
ATOM   1636  CG  LYS A 439     -11.645  54.624  24.590  1.00 39.72           C  
ANISOU 1636  CG  LYS A 439     5491   5495   4107   -566     -6   -452       C  
ATOM   1637  CD  LYS A 439     -13.152  54.765  24.507  1.00 44.55           C  
ANISOU 1637  CD  LYS A 439     6080   6089   4758   -539    -74   -436       C  
ATOM   1638  CE  LYS A 439     -13.827  53.948  25.591  1.00 56.42           C  
ANISOU 1638  CE  LYS A 439     7479   7586   6371   -506    -47   -403       C  
ATOM   1639  NZ  LYS A 439     -15.306  53.994  25.462  1.00 63.96           N1+
ANISOU 1639  NZ  LYS A 439     8391   8519   7392   -485   -104   -402       N1+
ATOM   1640  N   SER A 440     -11.427  57.268  20.820  1.00 45.19           N  
ANISOU 1640  N   SER A 440     6510   6115   4544   -628   -121   -502       N  
ATOM   1641  CA  SER A 440     -10.944  58.245  19.859  1.00 41.21           C  
ANISOU 1641  CA  SER A 440     6087   5575   3997   -626   -119   -488       C  
ATOM   1642  C   SER A 440     -10.583  59.563  20.525  1.00 42.08           C  
ANISOU 1642  C   SER A 440     6200   5690   4100   -596   -102   -443       C  
ATOM   1643  O   SER A 440     -11.051  59.873  21.618  1.00 33.49           O  
ANISOU 1643  O   SER A 440     5069   4628   3030   -564   -118   -418       O  
ATOM   1644  CB  SER A 440     -11.978  58.483  18.756  1.00 43.86           C  
ANISOU 1644  CB  SER A 440     6495   5874   4296   -619   -218   -493       C  
ATOM   1645  OG  SER A 440     -11.974  57.413  17.826  1.00 62.54           O  
ANISOU 1645  OG  SER A 440     8882   8222   6658   -654   -221   -539       O  
ATOM   1646  N   LEU A 441      -9.751  60.332  19.835  1.00 42.87           N  
ANISOU 1646  N   LEU A 441     6356   5763   4171   -613    -65   -436       N  
ATOM   1647  CA  LEU A 441      -9.207  61.569  20.357  1.00 39.52           C  
ANISOU 1647  CA  LEU A 441     5937   5336   3742   -598    -41   -403       C  
ATOM   1648  C   LEU A 441      -8.932  62.539  19.219  1.00 40.50           C  
ANISOU 1648  C   LEU A 441     6158   5415   3815   -622    -44   -394       C  
ATOM   1649  O   LEU A 441      -8.217  62.210  18.270  1.00 37.66           O  
ANISOU 1649  O   LEU A 441     5843   5034   3434   -672      5   -419       O  
ATOM   1650  CB  LEU A 441      -7.927  61.286  21.146  1.00 33.96           C  
ANISOU 1650  CB  LEU A 441     5170   4656   3077   -619     46   -414       C  
ATOM   1651  CG  LEU A 441      -7.130  62.463  21.703  1.00 30.18           C  
ANISOU 1651  CG  LEU A 441     4692   4174   2601   -615     78   -391       C  
ATOM   1652  CD1 LEU A 441      -7.885  63.158  22.829  1.00 26.89           C  
ANISOU 1652  CD1 LEU A 441     4250   3775   2194   -557     32   -353       C  
ATOM   1653  CD2 LEU A 441      -5.756  61.998  22.169  1.00 31.27           C  
ANISOU 1653  CD2 LEU A 441     4777   4329   2774   -653    158   -422       C  
ATOM   1654  N   SER A 442      -9.510  63.729  19.315  1.00 40.28           N  
ANISOU 1654  N   SER A 442     6170   5371   3765   -590    -97   -360       N  
ATOM   1655  CA  SER A 442      -9.284  64.779  18.332  1.00 43.69           C  
ANISOU 1655  CA  SER A 442     6704   5754   4143   -616   -103   -345       C  
ATOM   1656  C   SER A 442      -9.477  66.136  18.993  1.00 41.06           C  
ANISOU 1656  C   SER A 442     6380   5414   3809   -584   -127   -309       C  
ATOM   1657  O   SER A 442     -10.079  66.222  20.063  1.00 45.96           O  
ANISOU 1657  O   SER A 442     6937   6065   4462   -535   -158   -297       O  
ATOM   1658  CB  SER A 442     -10.229  64.616  17.143  1.00 51.20           C  
ANISOU 1658  CB  SER A 442     7738   6669   5045   -619   -184   -349       C  
ATOM   1659  OG  SER A 442     -11.579  64.663  17.565  1.00 57.14           O  
ANISOU 1659  OG  SER A 442     8467   7431   5812   -565   -286   -339       O  
ATOM   1660  N   LEU A 443      -8.969  67.189  18.358  1.00 38.39           N  
ANISOU 1660  N   LEU A 443     6128   5030   3429   -617   -109   -294       N  
ATOM   1661  CA  LEU A 443      -9.029  68.532  18.934  1.00 47.36           C  
ANISOU 1661  CA  LEU A 443     7282   6151   4562   -596   -125   -263       C  
ATOM   1662  C   LEU A 443     -10.468  68.987  19.142  1.00 44.80           C  
ANISOU 1662  C   LEU A 443     6972   5819   4231   -537   -232   -243       C  
ATOM   1663  O   LEU A 443     -11.145  69.386  18.195  1.00 45.52           O  
ANISOU 1663  O   LEU A 443     7157   5862   4277   -540   -304   -231       O  
ATOM   1664  CB  LEU A 443      -8.278  69.529  18.047  1.00 51.23           C  
ANISOU 1664  CB  LEU A 443     7883   6581   5001   -654    -90   -253       C  
ATOM   1665  CG  LEU A 443      -7.913  70.878  18.679  1.00 55.49           C  
ANISOU 1665  CG  LEU A 443     8439   7102   5541   -652    -77   -230       C  
ATOM   1666  CD1 LEU A 443      -6.596  71.386  18.124  1.00 49.60           C  
ANISOU 1666  CD1 LEU A 443     7758   6318   4770   -734     10   -239       C  
ATOM   1667  CD2 LEU A 443      -9.004  71.917  18.459  1.00 65.26           C  
ANISOU 1667  CD2 LEU A 443     9757   8295   6744   -616   -171   -198       C  
TER   
HETATM 1668  O   HOH A 601      -7.070  36.210  36.392  1.00 42.22           O  
HETATM 1669  O   HOH A 602      -3.267  28.045  18.635  1.00 59.74           O  
HETATM 1670  O   HOH A 603      11.494  40.667  24.377  1.00 54.74           O  
HETATM 1671  O   HOH A 604       0.582  71.763  31.876  1.00 51.87           O  
HETATM 1672  O   HOH A 605     -10.273  25.817  27.689  1.00 43.49           O  
HETATM 1673  O   HOH A 606       5.660  58.867  22.695  1.00 40.61           O  
HETATM 1674  O   HOH A 607       2.198  34.109  21.309  1.00 33.74           O  
HETATM 1675  O   HOH A 608       6.293  67.544  23.258  1.00 20.95           O  
HETATM 1676  O   HOH A 609     -12.122  54.465  35.501  1.00 37.79           O  
HETATM 1677  O   HOH A 610      -6.195  40.217  28.833  1.00 33.90           O  
HETATM 1678  O   HOH A 611       1.450  49.151  23.676  1.00 42.91           O  
HETATM 1679  O   HOH A 612      -6.297  50.926  38.431  1.00 31.12           O  
HETATM 1680  O   HOH A 613       5.571  48.779  36.288  1.00 37.63           O  
HETATM 1681  O   HOH A 614       7.761  50.254  26.895  1.00 38.67           O  
HETATM 1682  O   HOH A 615      -3.360  29.665  31.881  1.00 43.65           O  
HETATM 1683  O   HOH A 616       2.894  50.018  42.288  1.00 35.64           O  
HETATM 1684  O   HOH A 617      -8.848  41.039  40.722  1.00 33.54           O  
HETATM 1685  O   HOH A 618      -1.323  64.194  26.463  1.00 28.69           O  
HETATM 1686  O   HOH A 619       5.704  63.006  23.254  1.00 34.17           O  
HETATM 1687  O   HOH A 620       4.941  11.788  20.375  1.00 45.45           O  
HETATM 1688  O   HOH A 621       0.861  43.104  29.539  1.00 39.46           O  
HETATM 1689  O   HOH A 622      -8.964  57.806  12.835  1.00 50.78           O  
HETATM 1690  O   HOH A 623      -9.256  66.516  22.690  1.00 39.37           O  
HETATM 1691  O   HOH A 624     -13.608  50.079  28.820  1.00 50.40           O  
HETATM 1692  O   HOH A 625      -8.942  38.269  15.452  1.00 39.41           O  
HETATM 1693  O   HOH A 626      -9.035  51.147  39.679  1.00 48.91           O  
HETATM 1694  O   HOH A 627      -5.126  66.609  28.783  1.00 32.53           O  
HETATM 1695  O   HOH A 628       1.001  46.632  23.318  1.00 41.99           O  
HETATM 1696  O   HOH A 629       0.500  66.519  27.200  1.00 35.08           O  
HETATM 1697  O   HOH A 630      -7.163  66.559  16.227  1.00 49.59           O  
HETATM 1698  O   HOH A 631     -12.614  62.216  18.757  1.00 46.40           O  
HETATM 1699  O   HOH A 632       6.105  50.548  24.264  1.00 33.64           O  
HETATM 1700  O   HOH A 633      -7.360  43.157  40.743  1.00 39.70           O  
HETATM 1701  O   HOH A 634      -8.688  55.000  12.626  1.00 52.25           O  
HETATM 1702  O   HOH A 635       5.109  18.146  22.333  1.00 53.26           O  
HETATM 1703  O   HOH A 636       1.323  20.598  33.081  1.00 46.67           O  
HETATM 1704  O   HOH A 637       5.361  50.875  17.140  1.00 52.97           O  
HETATM 1705  O   HOH A 638       0.108  35.256  15.436  1.00 43.09           O  
HETATM 1706  O   HOH A 639       8.428  27.247  37.013  1.00 52.45           O  
HETATM 1707  O   HOH A 640     -13.800  53.011  28.963  1.00 33.63           O  
HETATM 1708  O   HOH A 641      -1.178  39.734  36.523  1.00 37.47           O  
HETATM 1709  O   HOH A 642     -20.965  37.741  24.982  1.00 39.16           O  
HETATM 1710  O   HOH A 643     -13.090  43.646  18.146  1.00 42.91           O  
ATOM   1711  N   LEU B 235      26.702  27.313  50.062  1.00 82.52           N  
ANISOU 1711  N   LEU B 235     9656   7545  14153    902  -1936     27       N  
ATOM   1712  CA  LEU B 235      26.530  26.271  49.060  1.00 88.61           C  
ANISOU 1712  CA  LEU B 235    10355   8201  15113    864  -2008   -102       C  
ATOM   1713  C   LEU B 235      27.231  26.699  47.781  1.00 95.43           C  
ANISOU 1713  C   LEU B 235    11193   9143  15923    885  -2007   -376       C  
ATOM   1714  O   LEU B 235      28.042  25.961  47.220  1.00 95.31           O  
ANISOU 1714  O   LEU B 235    11128   9081  16006    914  -2077   -521       O  
ATOM   1715  CB  LEU B 235      25.046  25.999  48.789  1.00 80.83           C  
ANISOU 1715  CB  LEU B 235     9343   7152  14216    780  -1997    -18       C  
ATOM   1716  CG  LEU B 235      24.033  25.927  49.939  1.00 70.28           C  
ANISOU 1716  CG  LEU B 235     8033   5786  12884    743  -1964    264       C  
ATOM   1717  CD1 LEU B 235      24.570  25.178  51.167  1.00 63.56           C  
ANISOU 1717  CD1 LEU B 235     7190   4870  12090    782  -2004    445       C  
ATOM   1718  CD2 LEU B 235      23.516  27.323  50.304  1.00 63.00           C  
ANISOU 1718  CD2 LEU B 235     7177   5011  11749    742  -1861    340       C  
ATOM   1719  N   GLY B 236      26.904  27.904  47.325  1.00 97.72           N  
ANISOU 1719  N   GLY B 236    11515   9562  16053    872  -1926   -439       N  
ATOM   1720  CA  GLY B 236      27.581  28.515  46.196  1.00 94.72           C  
ANISOU 1720  CA  GLY B 236    11116   9290  15583    894  -1906   -674       C  
ATOM   1721  C   GLY B 236      28.167  29.836  46.636  1.00 90.06           C  
ANISOU 1721  C   GLY B 236    10585   8844  14790    932  -1831   -668       C  
ATOM   1722  O   GLY B 236      28.476  30.706  45.820  1.00 88.66           O  
ANISOU 1722  O   GLY B 236    10404   8785  14496    938  -1784   -819       O  
ATOM   1723  N   GLY B 237      28.326  29.975  47.951  1.00 84.76           N  
ANISOU 1723  N   GLY B 237     9961   8167  14076    962  -1824   -487       N  
ATOM   1724  CA  GLY B 237      28.713  31.239  48.555  1.00 82.86           C  
ANISOU 1724  CA  GLY B 237     9777   8059  13647   1000  -1758   -450       C  
ATOM   1725  C   GLY B 237      27.523  32.177  48.624  1.00 81.53           C  
ANISOU 1725  C   GLY B 237     9649   7952  13377    958  -1683   -363       C  
ATOM   1726  O   GLY B 237      26.477  31.907  48.034  1.00 80.90           O  
ANISOU 1726  O   GLY B 237     9550   7822  13366    897  -1677   -361       O  
ATOM   1727  N   PRO B 238      27.669  33.284  49.365  1.00 81.95           N  
ANISOU 1727  N   PRO B 238     9754   8116  13267    992  -1630   -291       N  
ATOM   1728  CA  PRO B 238      26.584  34.270  49.375  1.00 78.37           C  
ANISOU 1728  CA  PRO B 238     9337   7732  12707    958  -1560   -224       C  
ATOM   1729  C   PRO B 238      26.569  35.115  48.105  1.00 75.02           C  
ANISOU 1729  C   PRO B 238     8902   7392  12213    932  -1512   -420       C  
ATOM   1730  O   PRO B 238      27.417  34.939  47.227  1.00 76.38           O  
ANISOU 1730  O   PRO B 238     9034   7580  12408    941  -1531   -601       O  
ATOM   1731  CB  PRO B 238      26.904  35.129  50.603  1.00 72.66           C  
ANISOU 1731  CB  PRO B 238     8666   7109  11835   1017  -1532    -99       C  
ATOM   1732  CG  PRO B 238      27.896  34.329  51.407  1.00 76.71           C  
ANISOU 1732  CG  PRO B 238     9170   7575  12402   1074  -1593    -46       C  
ATOM   1733  CD  PRO B 238      28.679  33.558  50.402  1.00 79.30           C  
ANISOU 1733  CD  PRO B 238     9445   7835  12851   1066  -1642   -232       C  
ATOM   1734  N   SER B 239      25.590  36.009  48.002  1.00 67.59           N  
ANISOU 1734  N   SER B 239     7990   6509  11182    900  -1451   -376       N  
ATOM   1735  CA  SER B 239      25.532  36.956  46.899  1.00 68.57           C  
ANISOU 1735  CA  SER B 239     8110   6728  11216    879  -1396   -540       C  
ATOM   1736  C   SER B 239      25.490  38.367  47.459  1.00 67.10           C  
ANISOU 1736  C   SER B 239     7974   6662  10858    905  -1336   -491       C  
ATOM   1737  O   SER B 239      24.987  38.588  48.560  1.00 70.79           O  
ANISOU 1737  O   SER B 239     8480   7135  11282    923  -1330   -314       O  
ATOM   1738  CB  SER B 239      24.311  36.693  46.025  1.00 68.34           C  
ANISOU 1738  CB  SER B 239     8061   6653  11251    812  -1381   -562       C  
ATOM   1739  OG  SER B 239      23.934  35.332  46.101  1.00 74.65           O  
ANISOU 1739  OG  SER B 239     8825   7315  12222    786  -1445   -502       O  
ATOM   1740  N   VAL B 240      26.026  39.322  46.709  1.00 65.88           N  
ANISOU 1740  N   VAL B 240     7815   6613  10603    909  -1293   -644       N  
ATOM   1741  CA  VAL B 240      26.018  40.708  47.159  1.00 60.37           C  
ANISOU 1741  CA  VAL B 240     7158   6029   9750    931  -1241   -617       C  
ATOM   1742  C   VAL B 240      25.350  41.616  46.132  1.00 57.07           C  
ANISOU 1742  C   VAL B 240     6743   5681   9260    888  -1174   -709       C  
ATOM   1743  O   VAL B 240      25.671  41.573  44.942  1.00 52.17           O  
ANISOU 1743  O   VAL B 240     6084   5088   8649    862  -1157   -865       O  
ATOM   1744  CB  VAL B 240      27.437  41.231  47.439  1.00 52.63           C  
ANISOU 1744  CB  VAL B 240     6171   5129   8698    982  -1248   -696       C  
ATOM   1745  CG1 VAL B 240      27.360  42.548  48.177  1.00 49.42           C  
ANISOU 1745  CG1 VAL B 240     5806   4825   8147   1012  -1212   -639       C  
ATOM   1746  CG2 VAL B 240      28.241  40.219  48.253  1.00 52.36           C  
ANISOU 1746  CG2 VAL B 240     6125   5025   8746   1027  -1318   -638       C  
ATOM   1747  N   PHE B 241      24.417  42.436  46.599  1.00 56.13           N  
ANISOU 1747  N   PHE B 241     6666   5599   9060    884  -1136   -608       N  
ATOM   1748  CA  PHE B 241      23.747  43.388  45.727  1.00 51.17           C  
ANISOU 1748  CA  PHE B 241     6047   5040   8355    847  -1071   -683       C  
ATOM   1749  C   PHE B 241      23.927  44.802  46.253  1.00 48.12           C  
ANISOU 1749  C   PHE B 241     5700   4790   7793    861  -1020   -659       C  
ATOM   1750  O   PHE B 241      23.753  45.066  47.445  1.00 43.63           O  
ANISOU 1750  O   PHE B 241     5167   4255   7154    885  -1027   -520       O  
ATOM   1751  CB  PHE B 241      22.266  43.038  45.590  1.00 62.88           C  
ANISOU 1751  CB  PHE B 241     7542   6471   9880    793  -1057   -588       C  
ATOM   1752  CG  PHE B 241      22.028  41.681  44.993  1.00 76.90           C  
ANISOU 1752  CG  PHE B 241     9274   8122  11823    763  -1105   -622       C  
ATOM   1753  CD1 PHE B 241      22.371  41.422  43.675  1.00 81.75           C  
ANISOU 1753  CD1 PHE B 241     9844   8755  12462    737  -1099   -801       C  
ATOM   1754  CD2 PHE B 241      21.473  40.662  45.750  1.00 79.14           C  
ANISOU 1754  CD2 PHE B 241     9555   8295  12220    753  -1153   -466       C  
ATOM   1755  CE1 PHE B 241      22.161  40.175  43.123  1.00 82.70           C  
ANISOU 1755  CE1 PHE B 241     9919   8782  12722    709  -1148   -839       C  
ATOM   1756  CE2 PHE B 241      21.261  39.411  45.203  1.00 80.04           C  
ANISOU 1756  CE2 PHE B 241     9624   8303  12485    716  -1198   -499       C  
ATOM   1757  CZ  PHE B 241      21.605  39.169  43.887  1.00 82.71           C  
ANISOU 1757  CZ  PHE B 241     9918   8657  12850    697  -1201   -694       C  
ATOM   1758  N   LEU B 242      24.294  45.704  45.352  1.00 45.58           N  
ANISOU 1758  N   LEU B 242     5367   4557   7395    842   -969   -794       N  
ATOM   1759  CA  LEU B 242      24.622  47.073  45.721  1.00 44.13           C  
ANISOU 1759  CA  LEU B 242     5211   4499   7058    847   -924   -794       C  
ATOM   1760  C   LEU B 242      23.607  48.045  45.136  1.00 42.90           C  
ANISOU 1760  C   LEU B 242     5082   4428   6789    785   -846   -790       C  
ATOM   1761  O   LEU B 242      23.413  48.097  43.921  1.00 44.97           O  
ANISOU 1761  O   LEU B 242     5320   4703   7065    747   -811   -892       O  
ATOM   1762  CB  LEU B 242      26.031  47.424  45.244  1.00 40.80           C  
ANISOU 1762  CB  LEU B 242     4747   4112   6645    878   -931   -941       C  
ATOM   1763  CG  LEU B 242      26.628  48.742  45.733  1.00 40.55           C  
ANISOU 1763  CG  LEU B 242     4730   4187   6490    891   -905   -949       C  
ATOM   1764  CD1 LEU B 242      26.574  48.814  47.249  1.00 36.94           C  
ANISOU 1764  CD1 LEU B 242     4314   3735   5986    937   -946   -816       C  
ATOM   1765  CD2 LEU B 242      28.057  48.880  45.236  1.00 41.25           C  
ANISOU 1765  CD2 LEU B 242     4762   4302   6607    910   -914  -1082       C  
ATOM   1766  N   PHE B 243      22.965  48.820  46.003  1.00 43.92           N  
ANISOU 1766  N   PHE B 243     5260   4624   6803    781   -821   -676       N  
ATOM   1767  CA  PHE B 243      21.897  49.708  45.564  1.00 47.97           C  
ANISOU 1767  CA  PHE B 243     5801   5212   7212    727   -752   -656       C  
ATOM   1768  C   PHE B 243      22.260  51.185  45.702  1.00 47.88           C  
ANISOU 1768  C   PHE B 243     5811   5310   7072    731   -714   -689       C  
ATOM   1769  O   PHE B 243      22.831  51.604  46.712  1.00 41.11           O  
ANISOU 1769  O   PHE B 243     4969   4483   6169    778   -743   -654       O  
ATOM   1770  CB  PHE B 243      20.622  49.410  46.347  1.00 40.75           C  
ANISOU 1770  CB  PHE B 243     4921   4287   6273    715   -749   -496       C  
ATOM   1771  CG  PHE B 243      20.179  47.979  46.246  1.00 48.90           C  
ANISOU 1771  CG  PHE B 243     5929   5201   7449    702   -789   -447       C  
ATOM   1772  CD1 PHE B 243      20.545  47.058  47.214  1.00 49.76           C  
ANISOU 1772  CD1 PHE B 243     6032   5235   7639    748   -852   -355       C  
ATOM   1773  CD2 PHE B 243      19.417  47.550  45.174  1.00 53.28           C  
ANISOU 1773  CD2 PHE B 243     6462   5715   8067    648   -770   -496       C  
ATOM   1774  CE1 PHE B 243      20.148  45.738  47.120  1.00 55.16           C  
ANISOU 1774  CE1 PHE B 243     6689   5794   8476    733   -894   -304       C  
ATOM   1775  CE2 PHE B 243      19.016  46.231  45.074  1.00 57.23           C  
ANISOU 1775  CE2 PHE B 243     6934   6093   8719    635   -816   -460       C  
ATOM   1776  CZ  PHE B 243      19.381  45.323  46.049  1.00 54.84           C  
ANISOU 1776  CZ  PHE B 243     6625   5703   8508    675   -879   -360       C  
ATOM   1777  N   PRO B 244      21.924  51.976  44.674  1.00 43.62           N  
ANISOU 1777  N   PRO B 244     5268   4827   6478    683   -655   -756       N  
ATOM   1778  CA  PRO B 244      22.154  53.420  44.669  1.00 36.67           C  
ANISOU 1778  CA  PRO B 244     4404   4038   5491    676   -617   -784       C  
ATOM   1779  C   PRO B 244      21.221  54.137  45.647  1.00 35.35           C  
ANISOU 1779  C   PRO B 244     4292   3923   5218    683   -606   -671       C  
ATOM   1780  O   PRO B 244      20.280  53.527  46.155  1.00 37.98           O  
ANISOU 1780  O   PRO B 244     4646   4234   5551    683   -612   -569       O  
ATOM   1781  CB  PRO B 244      21.841  53.812  43.224  1.00 30.59           C  
ANISOU 1781  CB  PRO B 244     3613   3304   4707    621   -558   -864       C  
ATOM   1782  CG  PRO B 244      20.827  52.819  42.791  1.00 31.71           C  
ANISOU 1782  CG  PRO B 244     3753   3394   4900    595   -556   -834       C  
ATOM   1783  CD  PRO B 244      21.225  51.526  43.459  1.00 40.36           C  
ANISOU 1783  CD  PRO B 244     4835   4394   6106    634   -624   -805       C  
ATOM   1784  N   PRO B 245      21.492  55.417  45.919  1.00 33.08           N  
ANISOU 1784  N   PRO B 245     4020   3704   4845    691   -591   -690       N  
ATOM   1785  CA  PRO B 245      20.579  56.220  46.736  1.00 38.19           C  
ANISOU 1785  CA  PRO B 245     4715   4412   5384    703   -579   -605       C  
ATOM   1786  C   PRO B 245      19.302  56.565  45.991  1.00 36.59           C  
ANISOU 1786  C   PRO B 245     4530   4238   5133    649   -519   -579       C  
ATOM   1787  O   PRO B 245      19.289  56.553  44.759  1.00 49.44           O  
ANISOU 1787  O   PRO B 245     6133   5857   6793    602   -484   -646       O  
ATOM   1788  CB  PRO B 245      21.394  57.482  47.039  1.00 27.67           C  
ANISOU 1788  CB  PRO B 245     3383   3127   4003    725   -590   -666       C  
ATOM   1789  CG  PRO B 245      22.436  57.529  45.976  1.00 29.00           C  
ANISOU 1789  CG  PRO B 245     3503   3273   4244    696   -578   -776       C  
ATOM   1790  CD  PRO B 245      22.755  56.117  45.638  1.00 28.31           C  
ANISOU 1790  CD  PRO B 245     3384   3118   4253    699   -598   -791       C  
ATOM   1791  N   LYS B 246      18.234  56.844  46.733  1.00 35.04           N  
ANISOU 1791  N   LYS B 246     4372   4085   4858    661   -510   -482       N  
ATOM   1792  CA  LYS B 246      17.005  57.324  46.123  1.00 31.25           C  
ANISOU 1792  CA  LYS B 246     3909   3644   4322    616   -456   -457       C  
ATOM   1793  C   LYS B 246      17.314  58.642  45.423  1.00 37.12           C  
ANISOU 1793  C   LYS B 246     4654   4429   5021    594   -426   -537       C  
ATOM   1794  O   LYS B 246      17.979  59.504  46.002  1.00 39.31           O  
ANISOU 1794  O   LYS B 246     4939   4732   5265    628   -448   -564       O  
ATOM   1795  CB  LYS B 246      15.906  57.506  47.172  1.00 32.58           C  
ANISOU 1795  CB  LYS B 246     4111   3864   4402    644   -453   -342       C  
ATOM   1796  CG  LYS B 246      15.822  56.377  48.186  1.00 42.41           C  
ANISOU 1796  CG  LYS B 246     5354   5082   5680    681   -490   -241       C  
ATOM   1797  CD  LYS B 246      14.523  56.437  48.974  1.00 57.49           C  
ANISOU 1797  CD  LYS B 246     7285   7055   7505    696   -470   -115       C  
ATOM   1798  CE  LYS B 246      13.501  55.453  48.417  1.00 72.03           C  
ANISOU 1798  CE  LYS B 246     9107   8850   9413    639   -444    -49       C  
ATOM   1799  NZ  LYS B 246      14.007  54.046  48.470  1.00 75.45           N1+
ANISOU 1799  NZ  LYS B 246     9509   9182   9975    636   -485    -22       N1+
ATOM   1800  N   PRO B 247      16.858  58.787  44.167  1.00 35.48           N  
ANISOU 1800  N   PRO B 247     4434   4228   4820    539   -378   -575       N  
ATOM   1801  CA  PRO B 247      17.112  59.970  43.337  1.00 35.41           C  
ANISOU 1801  CA  PRO B 247     4419   4257   4777    511   -343   -636       C  
ATOM   1802  C   PRO B 247      16.870  61.271  44.096  1.00 35.39           C  
ANISOU 1802  C   PRO B 247     4452   4301   4695    537   -348   -609       C  
ATOM   1803  O   PRO B 247      17.663  62.202  43.980  1.00 33.98           O  
ANISOU 1803  O   PRO B 247     4263   4129   4519    538   -354   -662       O  
ATOM   1804  CB  PRO B 247      16.110  59.809  42.192  1.00 30.85           C  
ANISOU 1804  CB  PRO B 247     3837   3698   4188    461   -294   -634       C  
ATOM   1805  CG  PRO B 247      15.968  58.337  42.047  1.00 31.30           C  
ANISOU 1805  CG  PRO B 247     3872   3700   4321    456   -312   -630       C  
ATOM   1806  CD  PRO B 247      16.063  57.775  43.448  1.00 26.38           C  
ANISOU 1806  CD  PRO B 247     3266   3045   3711    502   -359   -558       C  
ATOM   1807  N   LYS B 248      15.804  61.311  44.886  1.00 34.94           N  
ANISOU 1807  N   LYS B 248     4430   4275   4572    561   -350   -531       N  
ATOM   1808  CA  LYS B 248      15.456  62.501  45.647  1.00 32.75           C  
ANISOU 1808  CA  LYS B 248     4184   4047   4212    597   -361   -513       C  
ATOM   1809  C   LYS B 248      16.510  62.854  46.695  1.00 36.68           C  
ANISOU 1809  C   LYS B 248     4682   4541   4712    656   -419   -545       C  
ATOM   1810  O   LYS B 248      16.814  64.026  46.908  1.00 39.26           O  
ANISOU 1810  O   LYS B 248     5017   4886   5016    673   -435   -587       O  
ATOM   1811  CB  LYS B 248      14.097  62.308  46.320  1.00 26.09           C  
ANISOU 1811  CB  LYS B 248     3369   3249   3293    619   -350   -420       C  
ATOM   1812  CG  LYS B 248      13.622  63.512  47.098  1.00 31.17           C  
ANISOU 1812  CG  LYS B 248     4044   3955   3844    666   -361   -410       C  
ATOM   1813  CD  LYS B 248      12.329  63.202  47.803  1.00 29.50           C  
ANISOU 1813  CD  LYS B 248     3850   3802   3555    693   -347   -314       C  
ATOM   1814  CE  LYS B 248      11.838  64.388  48.593  1.00 28.08           C  
ANISOU 1814  CE  LYS B 248     3697   3695   3278    752   -361   -316       C  
ATOM   1815  NZ  LYS B 248      10.653  63.957  49.365  1.00 35.11           N1+
ANISOU 1815  NZ  LYS B 248     4594   4656   4089    785   -346   -215       N1+
ATOM   1816  N   ASP B 249      17.067  61.833  47.341  1.00 29.63           N  
ANISOU 1816  N   ASP B 249     3778   3623   3857    688   -455   -527       N  
ATOM   1817  CA  ASP B 249      18.024  62.040  48.424  1.00 31.99           C  
ANISOU 1817  CA  ASP B 249     4075   3927   4153    752   -517   -552       C  
ATOM   1818  C   ASP B 249      19.329  62.681  47.945  1.00 32.66           C  
ANISOU 1818  C   ASP B 249     4128   3978   4303    737   -535   -654       C  
ATOM   1819  O   ASP B 249      19.981  63.405  48.694  1.00 30.10           O  
ANISOU 1819  O   ASP B 249     3803   3667   3967    782   -584   -696       O  
ATOM   1820  CB  ASP B 249      18.319  60.716  49.133  1.00 32.47           C  
ANISOU 1820  CB  ASP B 249     4127   3965   4246    789   -551   -499       C  
ATOM   1821  CG  ASP B 249      17.107  60.154  49.851  1.00 29.86           C  
ANISOU 1821  CG  ASP B 249     3821   3675   3849    812   -540   -381       C  
ATOM   1822  OD1 ASP B 249      16.190  60.941  50.170  1.00 39.03           O  
ANISOU 1822  OD1 ASP B 249     5008   4902   4918    827   -521   -350       O  
ATOM   1823  OD2 ASP B 249      17.071  58.931  50.102  1.00 38.01           O1-
ANISOU 1823  OD2 ASP B 249     4842   4673   4928    817   -551   -315       O1-
ATOM   1824  N   THR B 250      19.702  62.419  46.698  1.00 33.65           N  
ANISOU 1824  N   THR B 250     4221   4067   4498    675   -497   -696       N  
ATOM   1825  CA  THR B 250      20.913  63.003  46.129  1.00 31.48           C  
ANISOU 1825  CA  THR B 250     3905   3770   4287    652   -503   -781       C  
ATOM   1826  C   THR B 250      20.677  64.415  45.620  1.00 33.50           C  
ANISOU 1826  C   THR B 250     4165   4045   4519    620   -477   -801       C  
ATOM   1827  O   THR B 250      21.621  65.184  45.438  1.00 39.80           O  
ANISOU 1827  O   THR B 250     4929   4827   5365    608   -492   -858       O  
ATOM   1828  CB  THR B 250      21.452  62.162  44.960  1.00 36.57           C  
ANISOU 1828  CB  THR B 250     4504   4384   5007    606   -470   -819       C  
ATOM   1829  CG2 THR B 250      21.536  60.719  45.361  1.00 38.01           C  
ANISOU 1829  CG2 THR B 250     4684   4533   5227    635   -497   -795       C  
ATOM   1830  OG1 THR B 250      20.574  62.286  43.835  1.00 41.74           O  
ANISOU 1830  OG1 THR B 250     5163   5058   5638    551   -406   -803       O  
ATOM   1831  N   LEU B 251      19.416  64.744  45.376  1.00 29.02           N  
ANISOU 1831  N   LEU B 251     3633   3508   3886    603   -439   -750       N  
ATOM   1832  CA  LEU B 251      19.066  66.009  44.746  1.00 33.71           C  
ANISOU 1832  CA  LEU B 251     4231   4115   4462    569   -410   -758       C  
ATOM   1833  C   LEU B 251      18.734  67.090  45.766  1.00 27.47           C  
ANISOU 1833  C   LEU B 251     3473   3341   3623    618   -454   -758       C  
ATOM   1834  O   LEU B 251      19.077  68.254  45.576  1.00 27.11           O  
ANISOU 1834  O   LEU B 251     3416   3279   3604    605   -465   -793       O  
ATOM   1835  CB  LEU B 251      17.892  65.804  43.787  1.00 29.00           C  
ANISOU 1835  CB  LEU B 251     3649   3544   3825    524   -346   -712       C  
ATOM   1836  CG  LEU B 251      18.167  64.911  42.576  1.00 32.81           C  
ANISOU 1836  CG  LEU B 251     4094   4018   4353    476   -302   -731       C  
ATOM   1837  CD1 LEU B 251      16.873  64.576  41.844  1.00 28.97           C  
ANISOU 1837  CD1 LEU B 251     3626   3562   3819    446   -253   -687       C  
ATOM   1838  CD2 LEU B 251      19.165  65.575  41.643  1.00 23.22           C  
ANISOU 1838  CD2 LEU B 251     2832   2800   3191    436   -279   -780       C  
ATOM   1839  N   MET B 252      18.066  66.701  46.847  1.00 29.03           N  
ANISOU 1839  N   MET B 252     3706   3574   3751    678   -481   -718       N  
ATOM   1840  CA  MET B 252      17.676  67.640  47.891  1.00 31.67           C  
ANISOU 1840  CA  MET B 252     4069   3942   4023    741   -526   -725       C  
ATOM   1841  C   MET B 252      18.693  67.664  49.029  1.00 35.75           C  
ANISOU 1841  C   MET B 252     4574   4455   4554    808   -603   -776       C  
ATOM   1842  O   MET B 252      18.969  66.639  49.654  1.00 32.06           O  
ANISOU 1842  O   MET B 252     4104   4000   4077    844   -624   -751       O  
ATOM   1843  CB  MET B 252      16.290  67.282  48.435  1.00 28.52           C  
ANISOU 1843  CB  MET B 252     3709   3605   3522    776   -507   -648       C  
ATOM   1844  CG  MET B 252      15.196  67.218  47.376  1.00 30.19           C  
ANISOU 1844  CG  MET B 252     3931   3826   3715    715   -437   -600       C  
ATOM   1845  SD  MET B 252      14.960  68.775  46.489  1.00 48.71           S  
ANISOU 1845  SD  MET B 252     6278   6156   6072    677   -417   -636       S  
ATOM   1846  CE  MET B 252      15.595  68.356  44.872  1.00 37.52           C  
ANISOU 1846  CE  MET B 252     4822   4695   4741    584   -361   -649       C  
ATOM   1847  N   ILE B 253      19.242  68.845  49.296  1.00 38.18           N  
ANISOU 1847  N   ILE B 253     4871   4744   4892    826   -651   -847       N  
ATOM   1848  CA  ILE B 253      20.254  68.998  50.332  1.00 39.32           C  
ANISOU 1848  CA  ILE B 253     4997   4885   5057    891   -733   -912       C  
ATOM   1849  C   ILE B 253      19.669  68.710  51.718  1.00 44.64           C  
ANISOU 1849  C   ILE B 253     5705   5639   5618    991   -776   -886       C  
ATOM   1850  O   ILE B 253      20.394  68.345  52.642  1.00 43.93           O  
ANISOU 1850  O   ILE B 253     5603   5566   5521   1054   -836   -913       O  
ATOM   1851  CB  ILE B 253      20.877  70.415  50.302  1.00 38.46           C  
ANISOU 1851  CB  ILE B 253     4865   4732   5016    886   -782   -999       C  
ATOM   1852  CG1 ILE B 253      22.107  70.488  51.210  1.00 40.20           C  
ANISOU 1852  CG1 ILE B 253     5054   4940   5283    942   -869  -1080       C  
ATOM   1853  CG2 ILE B 253      19.855  71.472  50.686  1.00 18.26           C  
ANISOU 1853  CG2 ILE B 253     2343   2203   2393    925   -798  -1005       C  
ATOM   1854  CD1 ILE B 253      23.217  69.556  50.800  1.00 40.68           C  
ANISOU 1854  CD1 ILE B 253     5071   4966   5421    906   -859  -1086       C  
ATOM   1855  N   SER B 254      18.352  68.846  51.849  1.00 39.92           N  
ANISOU 1855  N   SER B 254     5144   5097   4927   1008   -742   -827       N  
ATOM   1856  CA  SER B 254      17.682  68.594  53.121  1.00 39.21           C  
ANISOU 1856  CA  SER B 254     5080   5102   4716   1104   -771   -788       C  
ATOM   1857  C   SER B 254      17.572  67.100  53.415  1.00 37.36           C  
ANISOU 1857  C   SER B 254     4846   4895   4455   1111   -746   -693       C  
ATOM   1858  O   SER B 254      17.195  66.706  54.517  1.00 41.41           O  
ANISOU 1858  O   SER B 254     5371   5491   4873   1191   -770   -643       O  
ATOM   1859  CB  SER B 254      16.293  69.230  53.129  1.00 35.81           C  
ANISOU 1859  CB  SER B 254     4679   4728   4197   1118   -739   -754       C  
ATOM   1860  OG  SER B 254      15.503  68.732  52.063  1.00 37.12           O  
ANISOU 1860  OG  SER B 254     4854   4874   4377   1036   -656   -678       O  
ATOM   1861  N   ARG B 255      17.902  66.276  52.425  1.00 34.45           N  
ANISOU 1861  N   ARG B 255     4460   4456   4172   1030   -701   -667       N  
ATOM   1862  CA  ARG B 255      17.869  64.825  52.584  1.00 35.62           C  
ANISOU 1862  CA  ARG B 255     4604   4604   4327   1028   -685   -583       C  
ATOM   1863  C   ARG B 255      19.279  64.241  52.677  1.00 32.81           C  
ANISOU 1863  C   ARG B 255     4215   4194   4056   1034   -729   -629       C  
ATOM   1864  O   ARG B 255      20.256  64.893  52.306  1.00 30.95           O  
ANISOU 1864  O   ARG B 255     3956   3913   3891   1015   -755   -725       O  
ATOM   1865  CB  ARG B 255      17.109  64.176  51.424  1.00 41.41           C  
ANISOU 1865  CB  ARG B 255     5337   5300   5096    941   -608   -524       C  
ATOM   1866  CG  ARG B 255      15.676  64.663  51.246  1.00 45.43           C  
ANISOU 1866  CG  ARG B 255     5872   5861   5526    929   -561   -473       C  
ATOM   1867  CD  ARG B 255      14.737  64.052  52.273  1.00 51.93           C  
ANISOU 1867  CD  ARG B 255     6711   6766   6255    987   -558   -367       C  
ATOM   1868  NE  ARG B 255      14.708  62.595  52.181  1.00 65.06           N  
ANISOU 1868  NE  ARG B 255     8358   8394   7967    959   -540   -283       N  
ATOM   1869  CZ  ARG B 255      13.973  61.809  52.960  1.00 72.19           C  
ANISOU 1869  CZ  ARG B 255     9263   9351   8815    993   -532   -166       C  
ATOM   1870  NH1 ARG B 255      14.014  60.493  52.806  1.00 71.61           N1+
ANISOU 1870  NH1 ARG B 255     9171   9224   8813    961   -523    -92       N1+
ATOM   1871  NH2 ARG B 255      13.195  62.332  53.897  1.00 74.36           N  
ANISOU 1871  NH2 ARG B 255     9552   9733   8967   1061   -534   -121       N  
ATOM   1872  N   THR B 256      19.371  63.008  53.169  1.00 34.00           N  
ANISOU 1872  N   THR B 256     4363   4349   4208   1060   -738   -557       N  
ATOM   1873  CA  THR B 256      20.653  62.321  53.316  1.00 30.74           C  
ANISOU 1873  CA  THR B 256     3919   3886   3875   1075   -784   -593       C  
ATOM   1874  C   THR B 256      20.706  61.054  52.458  1.00 33.50           C  
ANISOU 1874  C   THR B 256     4250   4163   4315   1012   -745   -549       C  
ATOM   1875  O   THR B 256      20.087  60.044  52.787  1.00 40.18           O  
ANISOU 1875  O   THR B 256     5106   5015   5147   1023   -733   -446       O  
ATOM   1876  CB  THR B 256      20.932  61.946  54.787  1.00 39.18           C  
ANISOU 1876  CB  THR B 256     4993   5020   4875   1180   -849   -553       C  
ATOM   1877  CG2 THR B 256      22.250  61.194  54.909  1.00 43.53           C  
ANISOU 1877  CG2 THR B 256     5509   5516   5512   1197   -898   -587       C  
ATOM   1878  OG1 THR B 256      20.996  63.135  55.580  1.00 42.74           O  
ANISOU 1878  OG1 THR B 256     5453   5540   5245   1248   -897   -619       O  
ATOM   1879  N   PRO B 257      21.452  61.111  51.349  1.00 29.32           N  
ANISOU 1879  N   PRO B 257     3689   3566   3883    949   -727   -629       N  
ATOM   1880  CA  PRO B 257      21.557  59.965  50.442  1.00 33.09           C  
ANISOU 1880  CA  PRO B 257     4145   3978   4451    896   -696   -615       C  
ATOM   1881  C   PRO B 257      22.412  58.821  50.999  1.00 38.43           C  
ANISOU 1881  C   PRO B 257     4798   4614   5187    940   -748   -600       C  
ATOM   1882  O   PRO B 257      23.424  59.065  51.654  1.00 44.82           O  
ANISOU 1882  O   PRO B 257     5591   5432   6005    992   -805   -650       O  
ATOM   1883  CB  PRO B 257      22.196  60.576  49.188  1.00 37.56           C  
ANISOU 1883  CB  PRO B 257     4678   4511   5084    831   -665   -715       C  
ATOM   1884  CG  PRO B 257      22.973  61.741  49.697  1.00 29.55           C  
ANISOU 1884  CG  PRO B 257     3654   3519   4055    862   -707   -785       C  
ATOM   1885  CD  PRO B 257      22.171  62.292  50.840  1.00 26.04           C  
ANISOU 1885  CD  PRO B 257     3254   3139   3502    923   -733   -735       C  
ATOM   1886  N   GLU B 258      21.994  57.587  50.731  1.00 40.13           N  
ANISOU 1886  N   GLU B 258     5011   4784   5454    920   -732   -534       N  
ATOM   1887  CA  GLU B 258      22.711  56.397  51.175  1.00 36.85           C  
ANISOU 1887  CA  GLU B 258     4573   4317   5113    958   -782   -509       C  
ATOM   1888  C   GLU B 258      22.965  55.410  50.040  1.00 40.09           C  
ANISOU 1888  C   GLU B 258     4949   4638   5645    905   -764   -548       C  
ATOM   1889  O   GLU B 258      22.116  55.220  49.175  1.00 33.33           O  
ANISOU 1889  O   GLU B 258     4096   3764   4803    846   -713   -535       O  
ATOM   1890  CB  GLU B 258      21.926  55.677  52.269  1.00 39.45           C  
ANISOU 1890  CB  GLU B 258     4928   4671   5392   1006   -800   -365       C  
ATOM   1891  CG  GLU B 258      21.469  56.517  53.436  1.00 44.98           C  
ANISOU 1891  CG  GLU B 258     5660   5477   5952   1069   -814   -315       C  
ATOM   1892  CD  GLU B 258      20.519  55.739  54.321  1.00 46.49           C  
ANISOU 1892  CD  GLU B 258     5868   5704   6092   1103   -812   -153       C  
ATOM   1893  OE1 GLU B 258      20.439  56.032  55.534  1.00 50.90           O  
ANISOU 1893  OE1 GLU B 258     6441   6354   6544   1183   -843    -98       O  
ATOM   1894  OE2 GLU B 258      19.859  54.818  53.791  1.00 44.21           O1-
ANISOU 1894  OE2 GLU B 258     5572   5354   5872   1050   -780    -82       O1-
ATOM   1895  N   VAL B 259      24.124  54.763  50.063  1.00 33.27           N  
ANISOU 1895  N   VAL B 259     4049   3723   4869    933   -810   -600       N  
ATOM   1896  CA  VAL B 259      24.351  53.599  49.218  1.00 32.48           C  
ANISOU 1896  CA  VAL B 259     3915   3536   4890    905   -810   -629       C  
ATOM   1897  C   VAL B 259      24.217  52.360  50.096  1.00 34.23           C  
ANISOU 1897  C   VAL B 259     4141   3704   5159    951   -861   -521       C  
ATOM   1898  O   VAL B 259      24.720  52.335  51.219  1.00 38.57           O  
ANISOU 1898  O   VAL B 259     4698   4277   5678   1019   -913   -477       O  
ATOM   1899  CB  VAL B 259      25.725  53.639  48.526  1.00 39.27           C  
ANISOU 1899  CB  VAL B 259     4722   4371   5828    905   -825   -765       C  
ATOM   1900  CG1 VAL B 259      26.023  52.314  47.851  1.00 42.70           C  
ANISOU 1900  CG1 VAL B 259     5118   4717   6388    899   -842   -798       C  
ATOM   1901  CG2 VAL B 259      25.763  54.763  47.507  1.00 34.81           C  
ANISOU 1901  CG2 VAL B 259     4144   3855   5227    849   -766   -851       C  
ATOM   1902  N   THR B 260      23.524  51.340  49.598  1.00 34.24           N  
ANISOU 1902  N   THR B 260     4136   3633   5239    915   -850   -474       N  
ATOM   1903  CA  THR B 260      23.188  50.190  50.431  1.00 36.43           C  
ANISOU 1903  CA  THR B 260     4419   3854   5569    948   -892   -343       C  
ATOM   1904  C   THR B 260      23.756  48.882  49.883  1.00 45.42           C  
ANISOU 1904  C   THR B 260     5515   4869   6873    948   -935   -384       C  
ATOM   1905  O   THR B 260      23.443  48.478  48.760  1.00 44.73           O  
ANISOU 1905  O   THR B 260     5406   4727   6863    894   -911   -450       O  
ATOM   1906  CB  THR B 260      21.662  50.046  50.582  1.00 34.95           C  
ANISOU 1906  CB  THR B 260     4258   3682   5340    910   -851   -213       C  
ATOM   1907  CG2 THR B 260      21.331  49.006  51.629  1.00 34.49           C  
ANISOU 1907  CG2 THR B 260     4202   3583   5321    948   -893    -49       C  
ATOM   1908  OG1 THR B 260      21.099  51.306  50.972  1.00 35.65           O  
ANISOU 1908  OG1 THR B 260     4382   3886   5275    912   -810   -192       O  
ATOM   1909  N   CYS B 261      24.588  48.224  50.689  1.00 46.69           N  
ANISOU 1909  N   CYS B 261     5662   4989   7087   1013  -1003   -350       N  
ATOM   1910  CA  CYS B 261      25.190  46.942  50.322  1.00 35.05           C  
ANISOU 1910  CA  CYS B 261     4147   3391   5779   1027  -1057   -384       C  
ATOM   1911  C   CYS B 261      24.472  45.796  51.028  1.00 36.51           C  
ANISOU 1911  C   CYS B 261     4338   3495   6038   1037  -1092   -214       C  
ATOM   1912  O   CYS B 261      24.458  45.724  52.257  1.00 40.53           O  
ANISOU 1912  O   CYS B 261     4868   4039   6492   1090  -1120    -81       O  
ATOM   1913  CB  CYS B 261      26.678  46.936  50.673  1.00 28.84           C  
ANISOU 1913  CB  CYS B 261     3334   2604   5021   1095  -1114   -466       C  
ATOM   1914  SG  CYS B 261      27.616  45.532  50.042  1.00 47.16           S  
ANISOU 1914  SG  CYS B 261     5598   4794   7527   1105  -1169   -552       S  
ATOM   1915  N   VAL B 262      23.880  44.898  50.245  1.00 34.41           N  
ANISOU 1915  N   VAL B 262     4051   3124   5901    987  -1092   -217       N  
ATOM   1916  CA  VAL B 262      23.051  43.831  50.798  1.00 38.38           C  
ANISOU 1916  CA  VAL B 262     4552   3537   6492    979  -1120    -47       C  
ATOM   1917  C   VAL B 262      23.610  42.454  50.476  1.00 45.65           C  
ANISOU 1917  C   VAL B 262     5429   4295   7620    996  -1195    -78       C  
ATOM   1918  O   VAL B 262      23.773  42.093  49.308  1.00 51.28           O  
ANISOU 1918  O   VAL B 262     6111   4953   8420    954  -1190   -224       O  
ATOM   1919  CB  VAL B 262      21.605  43.916  50.269  1.00 39.60           C  
ANISOU 1919  CB  VAL B 262     4717   3696   6634    899  -1061      4       C  
ATOM   1920  CG1 VAL B 262      20.750  42.813  50.872  1.00 39.78           C  
ANISOU 1920  CG1 VAL B 262     4728   3624   6761    884  -1089    193       C  
ATOM   1921  CG2 VAL B 262      21.006  45.277  50.569  1.00 33.99           C  
ANISOU 1921  CG2 VAL B 262     4048   3142   5724    886   -989     32       C  
ATOM   1922  N   VAL B 263      23.895  41.683  51.519  1.00 46.20           N  
ANISOU 1922  N   VAL B 263     5499   4330   7724   1034  -1241     58       N  
ATOM   1923  CA  VAL B 263      24.438  40.341  51.340  1.00 50.63           C  
ANISOU 1923  CA  VAL B 263     6028   4774   8437   1024  -1289     40       C  
ATOM   1924  C   VAL B 263      23.372  39.282  51.618  1.00 48.96           C  
ANISOU 1924  C   VAL B 263     5806   4459   8337    979  -1302    208       C  
ATOM   1925  O   VAL B 263      22.804  39.230  52.709  1.00 50.09           O  
ANISOU 1925  O   VAL B 263     5969   4632   8431    997  -1298    409       O  
ATOM   1926  CB  VAL B 263      25.653  40.088  52.257  1.00 57.76           C  
ANISOU 1926  CB  VAL B 263     6932   5699   9317   1096  -1335     63       C  
ATOM   1927  CG1 VAL B 263      26.364  38.813  51.832  1.00 54.98           C  
ANISOU 1927  CG1 VAL B 263     6540   5229   9122   1085  -1387     -4       C  
ATOM   1928  CG2 VAL B 263      26.617  41.276  52.220  1.00 50.77           C  
ANISOU 1928  CG2 VAL B 263     6054   4932   8303   1139  -1320    -71       C  
ATOM   1929  N   VAL B 264      23.105  38.444  50.622  1.00 45.93           N  
ANISOU 1929  N   VAL B 264     5386   3966   8100    919  -1318    124       N  
ATOM   1930  CA  VAL B 264      22.129  37.370  50.761  1.00 62.21           C  
ANISOU 1930  CA  VAL B 264     7427   5916  10295    865  -1336    262       C  
ATOM   1931  C   VAL B 264      22.806  36.016  50.603  1.00 67.85           C  
ANISOU 1931  C   VAL B 264     8100   6508  11173    863  -1404    222       C  
ATOM   1932  O   VAL B 264      23.959  35.940  50.183  1.00 63.97           O  
ANISOU 1932  O   VAL B 264     7595   6021  10691    897  -1432     65       O  
ATOM   1933  CB  VAL B 264      20.997  37.495  49.728  1.00 70.38           C  
ANISOU 1933  CB  VAL B 264     8445   6919  11375    790  -1304    206       C  
ATOM   1934  CG1 VAL B 264      20.226  38.790  49.943  1.00 72.76           C  
ANISOU 1934  CG1 VAL B 264     8786   7336  11523    792  -1240    266       C  
ATOM   1935  CG2 VAL B 264      21.562  37.421  48.316  1.00 68.98           C  
ANISOU 1935  CG2 VAL B 264     8236   6723  11249    772  -1314    -44       C  
ATOM   1936  N   ASP B 265      22.070  34.957  50.932  1.00 70.81           N  
ANISOU 1936  N   ASP B 265     8450   6776  11676    820  -1431    367       N  
ATOM   1937  CA  ASP B 265      22.598  33.593  50.962  1.00 70.87           C  
ANISOU 1937  CA  ASP B 265     8418   6658  11852    819  -1504    365       C  
ATOM   1938  C   ASP B 265      23.769  33.478  51.935  1.00 77.38           C  
ANISOU 1938  C   ASP B 265     9262   7512  12627    900  -1533    414       C  
ATOM   1939  O   ASP B 265      24.725  32.734  51.703  1.00 84.11           O  
ANISOU 1939  O   ASP B 265    10086   8298  13573    924  -1591    318       O  
ATOM   1940  CB  ASP B 265      23.012  33.118  49.563  1.00 68.66           C  
ANISOU 1940  CB  ASP B 265     8090   6314  11683    793  -1541    127       C  
ATOM   1941  CG  ASP B 265      21.819  32.870  48.660  1.00 68.33           C  
ANISOU 1941  CG  ASP B 265     8016   6218  11730    714  -1532     92       C  
ATOM   1942  OD1 ASP B 265      20.679  32.817  49.177  1.00 62.87           O  
ANISOU 1942  OD1 ASP B 265     7330   5505  11054    670  -1508    271       O  
ATOM   1943  OD2 ASP B 265      22.021  32.719  47.435  1.00 72.64           O1-
ANISOU 1943  OD2 ASP B 265     8525   6751  12325    697  -1550   -112       O1-
ATOM   1944  N   VAL B 266      23.681  34.233  53.025  1.00 77.30           N  
ANISOU 1944  N   VAL B 266     9297   7613  12462    946  -1496    562       N  
ATOM   1945  CA  VAL B 266      24.557  34.035  54.168  1.00 69.92           C  
ANISOU 1945  CA  VAL B 266     8378   6712  11475   1024  -1524    660       C  
ATOM   1946  C   VAL B 266      24.049  32.834  54.955  1.00 78.80           C  
ANISOU 1946  C   VAL B 266     9485   7743  12713   1006  -1554    871       C  
ATOM   1947  O   VAL B 266      22.899  32.815  55.394  1.00 80.73           O  
ANISOU 1947  O   VAL B 266     9732   8000  12941    965  -1517   1045       O  
ATOM   1948  CB  VAL B 266      24.602  35.270  55.083  1.00 59.85           C  
ANISOU 1948  CB  VAL B 266     7152   5606   9983   1088  -1479    740       C  
ATOM   1949  CG1 VAL B 266      25.519  35.015  56.260  1.00 51.52           C  
ANISOU 1949  CG1 VAL B 266     6110   4593   8872   1175  -1513    834       C  
ATOM   1950  CG2 VAL B 266      25.067  36.486  54.310  1.00 65.34           C  
ANISOU 1950  CG2 VAL B 266     7859   6390  10576   1099  -1450    537       C  
ATOM   1951  N   SER B 267      24.895  31.824  55.120  1.00 84.08           N  
ANISOU 1951  N   SER B 267    10130   8318  13498   1033  -1619    857       N  
ATOM   1952  CA  SER B 267      24.480  30.629  55.840  1.00 86.85           C  
ANISOU 1952  CA  SER B 267    10457   8570  13971   1014  -1652   1054       C  
ATOM   1953  C   SER B 267      24.638  30.832  57.342  1.00 90.02           C  
ANISOU 1953  C   SER B 267    10896   9078  14230   1088  -1635   1264       C  
ATOM   1954  O   SER B 267      25.429  31.666  57.790  1.00 92.49           O  
ANISOU 1954  O   SER B 267    11243   9513  14384   1169  -1624   1220       O  
ATOM   1955  CB  SER B 267      25.271  29.406  55.371  1.00 90.62           C  
ANISOU 1955  CB  SER B 267    10890   8898  14645   1013  -1736    954       C  
ATOM   1956  OG  SER B 267      25.236  28.366  56.336  1.00 97.18           O  
ANISOU 1956  OG  SER B 267    11706   9654  15562   1025  -1774   1153       O  
ATOM   1957  N   HIS B 268      23.875  30.064  58.111  1.00 91.72           N  
ANISOU 1957  N   HIS B 268    11097   9252  14502   1061  -1633   1491       N  
ATOM   1958  CA  HIS B 268      23.884  30.151  59.562  1.00 91.03           C  
ANISOU 1958  CA  HIS B 268    11039   9276  14275   1129  -1614   1709       C  
ATOM   1959  C   HIS B 268      25.229  29.765  60.167  1.00 86.67           C  
ANISOU 1959  C   HIS B 268    10496   8721  13713   1225  -1672   1692       C  
ATOM   1960  O   HIS B 268      25.488  30.051  61.331  1.00 86.64           O  
ANISOU 1960  O   HIS B 268    10523   8840  13555   1307  -1660   1825       O  
ATOM   1961  CB  HIS B 268      22.798  29.247  60.148  1.00 97.78           C  
ANISOU 1961  CB  HIS B 268    11862  10072  15220   1067  -1602   1949       C  
ATOM   1962  CG  HIS B 268      23.107  27.787  60.026  1.00105.72           C  
ANISOU 1962  CG  HIS B 268    12817  10891  16459   1039  -1677   1975       C  
ATOM   1963  CD2 HIS B 268      23.617  26.906  60.919  1.00109.85           C  
ANISOU 1963  CD2 HIS B 268    13332  11373  17032   1086  -1721   2114       C  
ATOM   1964  ND1 HIS B 268      22.904  27.076  58.862  1.00106.50           N  
ANISOU 1964  ND1 HIS B 268    12865  10822  16776    957  -1721   1842       N  
ATOM   1965  CE1 HIS B 268      23.270  25.820  59.045  1.00108.75           C  
ANISOU 1965  CE1 HIS B 268    13110  10967  17242    953  -1791   1896       C  
ATOM   1966  NE2 HIS B 268      23.704  25.690  60.286  1.00111.50           N  
ANISOU 1966  NE2 HIS B 268    13485  11384  17495   1029  -1791   2066       N  
ATOM   1967  N   GLU B 269      26.073  29.114  59.370  1.00 89.77           N  
ANISOU 1967  N   GLU B 269    10859   8982  14266   1219  -1735   1522       N  
ATOM   1968  CA  GLU B 269      27.314  28.521  59.865  1.00 97.59           C  
ANISOU 1968  CA  GLU B 269    11847   9941  15290   1300  -1799   1509       C  
ATOM   1969  C   GLU B 269      28.546  29.411  59.682  1.00 98.72           C  
ANISOU 1969  C   GLU B 269    12013  10183  15313   1378  -1805   1318       C  
ATOM   1970  O   GLU B 269      29.589  29.175  60.294  1.00 94.54           O  
ANISOU 1970  O   GLU B 269    11488   9674  14759   1462  -1847   1323       O  
ATOM   1971  CB  GLU B 269      27.543  27.171  59.190  1.00100.06           C  
ANISOU 1971  CB  GLU B 269    12107  10052  15859   1251  -1872   1446       C  
ATOM   1972  CG  GLU B 269      26.960  26.007  59.978  1.00103.05           C  
ANISOU 1972  CG  GLU B 269    12461  10336  16357   1226  -1897   1685       C  
ATOM   1973  CD  GLU B 269      26.656  24.798  59.119  1.00106.53           C  
ANISOU 1973  CD  GLU B 269    12838  10573  17065   1142  -1958   1630       C  
ATOM   1974  OE1 GLU B 269      26.757  24.907  57.880  1.00106.39           O  
ANISOU 1974  OE1 GLU B 269    12797  10501  17125   1100  -1975   1406       O  
ATOM   1975  OE2 GLU B 269      26.311  23.738  59.688  1.00107.56           O1-
ANISOU 1975  OE2 GLU B 269    12937  10604  17327   1119  -1992   1809       O1-
ATOM   1976  N   ASP B 270      28.421  30.440  58.851  1.00107.89           N  
ANISOU 1976  N   ASP B 270    13183  11409  16400   1350  -1764   1154       N  
ATOM   1977  CA  ASP B 270      29.513  31.390  58.647  1.00118.15           C  
ANISOU 1977  CA  ASP B 270    14496  12812  17584   1411  -1764    974       C  
ATOM   1978  C   ASP B 270      29.229  32.834  59.093  1.00133.33           C  
ANISOU 1978  C   ASP B 270    16458  14918  19283   1445  -1702    994       C  
ATOM   1979  O   ASP B 270      30.033  33.730  58.820  1.00136.31           O  
ANISOU 1979  O   ASP B 270    16841  15381  19571   1481  -1698    833       O  
ATOM   1980  CB  ASP B 270      29.890  31.403  57.160  1.00113.62           C  
ANISOU 1980  CB  ASP B 270    13890  12164  17116   1356  -1777    719       C  
ATOM   1981  CG  ASP B 270      28.673  31.309  56.256  1.00107.18           C  
ANISOU 1981  CG  ASP B 270    13060  11280  16382   1256  -1746    701       C  
ATOM   1982  OD1 ASP B 270      27.728  30.574  56.637  1.00109.48           O  
ANISOU 1982  OD1 ASP B 270    13344  11498  16755   1214  -1748    877       O  
ATOM   1983  OD2 ASP B 270      28.656  31.952  55.185  1.00 94.94           O1-
ANISOU 1983  OD2 ASP B 270    11503   9755  14816   1219  -1721    517       O1-
ATOM   1984  N   PRO B 271      28.112  33.065  59.821  1.00148.13           N  
ANISOU 1984  N   PRO B 271    18357  16860  21065   1436  -1657   1191       N  
ATOM   1985  CA  PRO B 271      27.541  34.417  59.755  1.00140.26           C  
ANISOU 1985  CA  PRO B 271    17388  16004  19901   1432  -1596   1163       C  
ATOM   1986  C   PRO B 271      28.358  35.487  60.475  1.00129.33           C  
ANISOU 1986  C   PRO B 271    16027  14789  18324   1530  -1594   1121       C  
ATOM   1987  O   PRO B 271      27.956  35.937  61.541  1.00131.52           O  
ANISOU 1987  O   PRO B 271    16330  15200  18441   1586  -1572   1272       O  
ATOM   1988  CB  PRO B 271      26.189  34.237  60.444  1.00144.72           C  
ANISOU 1988  CB  PRO B 271    17966  16601  20421   1402  -1553   1396       C  
ATOM   1989  CG  PRO B 271      26.451  33.209  61.491  1.00148.57           C  
ANISOU 1989  CG  PRO B 271    18449  17059  20942   1450  -1591   1574       C  
ATOM   1990  CD  PRO B 271      27.577  32.325  60.986  1.00149.59           C  
ANISOU 1990  CD  PRO B 271    18549  17048  21240   1459  -1660   1447       C  
ATOM   1991  N   GLU B 272      29.484  35.897  59.896  1.00115.30           N  
ANISOU 1991  N   GLU B 272    14237  13015  16558   1549  -1619    914       N  
ATOM   1992  CA  GLU B 272      30.237  37.034  60.424  1.00100.54           C  
ANISOU 1992  CA  GLU B 272    12380  11303  14519   1625  -1618    844       C  
ATOM   1993  C   GLU B 272      30.807  37.856  59.276  1.00 81.59           C  
ANISOU 1993  C   GLU B 272     9967   8904  12130   1585  -1608    594       C  
ATOM   1994  O   GLU B 272      32.002  37.798  58.977  1.00 76.91           O  
ANISOU 1994  O   GLU B 272     9350   8294  11578   1606  -1643    448       O  
ATOM   1995  CB  GLU B 272      31.344  36.573  61.368  1.00106.47           C  
ANISOU 1995  CB  GLU B 272    13122  12083  15250   1718  -1672    888       C  
ATOM   1996  CG  GLU B 272      30.964  36.717  62.835  1.00112.43           C  
ANISOU 1996  CG  GLU B 272    13900  12974  15843   1803  -1664   1102       C  
ATOM   1997  CD  GLU B 272      31.886  35.960  63.772  1.00120.49           C  
ANISOU 1997  CD  GLU B 272    14910  14000  16869   1894  -1719   1184       C  
ATOM   1998  OE1 GLU B 272      32.967  35.517  63.329  1.00122.66           O  
ANISOU 1998  OE1 GLU B 272    15159  14190  17257   1897  -1765   1053       O  
ATOM   1999  OE2 GLU B 272      31.523  35.804  64.957  1.00123.07           O1-
ANISOU 1999  OE2 GLU B 272    15257  14424  17080   1966  -1716   1377       O1-
ATOM   2000  N   VAL B 273      29.930  38.639  58.660  1.00 69.04           N  
ANISOU 2000  N   VAL B 273     8391   7345  10496   1528  -1557    554       N  
ATOM   2001  CA  VAL B 273      30.226  39.363  57.431  1.00 62.13           C  
ANISOU 2001  CA  VAL B 273     7503   6464   9638   1476  -1535    334       C  
ATOM   2002  C   VAL B 273      30.950  40.688  57.681  1.00 54.75           C  
ANISOU 2002  C   VAL B 273     6576   5670   8556   1520  -1529    222       C  
ATOM   2003  O   VAL B 273      30.572  41.454  58.566  1.00 56.02           O  
ANISOU 2003  O   VAL B 273     6763   5952   8570   1564  -1516    311       O  
ATOM   2004  CB  VAL B 273      28.925  39.637  56.650  1.00 60.67           C  
ANISOU 2004  CB  VAL B 273     7329   6252   9471   1397  -1483    343       C  
ATOM   2005  CG1 VAL B 273      29.239  40.164  55.267  1.00 56.47           C  
ANISOU 2005  CG1 VAL B 273     6778   5702   8976   1343  -1459    119       C  
ATOM   2006  CG2 VAL B 273      28.085  38.364  56.560  1.00 57.35           C  
ANISOU 2006  CG2 VAL B 273     6899   5701   9192   1349  -1490    475       C  
ATOM   2007  N   LYS B 274      31.988  40.955  56.893  1.00 53.71           N  
ANISOU 2007  N   LYS B 274     6416   5527   8463   1506  -1538     23       N  
ATOM   2008  CA  LYS B 274      32.760  42.181  57.047  1.00 55.15           C  
ANISOU 2008  CA  LYS B 274     6599   5830   8528   1535  -1534    -96       C  
ATOM   2009  C   LYS B 274      32.751  43.017  55.772  1.00 54.66           C  
ANISOU 2009  C   LYS B 274     6523   5778   8468   1468  -1488   -273       C  
ATOM   2010  O   LYS B 274      32.968  42.499  54.669  1.00 57.85           O  
ANISOU 2010  O   LYS B 274     6897   6101   8984   1417  -1480   -379       O  
ATOM   2011  CB  LYS B 274      34.198  41.862  57.448  1.00 63.31           C  
ANISOU 2011  CB  LYS B 274     7603   6868   9584   1589  -1589   -162       C  
ATOM   2012  CG  LYS B 274      34.841  42.947  58.290  1.00 71.11           C  
ANISOU 2012  CG  LYS B 274     8597   7993  10430   1645  -1603   -196       C  
ATOM   2013  CD  LYS B 274      36.205  43.341  57.756  1.00 79.89           C  
ANISOU 2013  CD  LYS B 274     9669   9118  11568   1639  -1622   -390       C  
ATOM   2014  CE  LYS B 274      36.778  44.506  58.551  1.00 85.17           C  
ANISOU 2014  CE  LYS B 274    10342   9916  12102   1684  -1638   -435       C  
ATOM   2015  NZ  LYS B 274      38.122  44.919  58.060  1.00 88.36           N1+
ANISOU 2015  NZ  LYS B 274    10700  10333  12538   1674  -1657   -616       N1+
ATOM   2016  N   PHE B 275      32.507  44.317  55.931  1.00 45.74           N  
ANISOU 2016  N   PHE B 275     5412   4757   7210   1471  -1458   -306       N  
ATOM   2017  CA  PHE B 275      32.405  45.241  54.800  1.00 46.40           C  
ANISOU 2017  CA  PHE B 275     5486   4865   7280   1409  -1407   -452       C  
ATOM   2018  C   PHE B 275      33.583  46.204  54.705  1.00 49.61           C  
ANISOU 2018  C   PHE B 275     5866   5349   7635   1419  -1413   -600       C  
ATOM   2019  O   PHE B 275      34.064  46.728  55.712  1.00 48.08           O  
ANISOU 2019  O   PHE B 275     5681   5233   7353   1475  -1446   -580       O  
ATOM   2020  CB  PHE B 275      31.110  46.056  54.887  1.00 45.27           C  
ANISOU 2020  CB  PHE B 275     5382   4776   7043   1392  -1363   -381       C  
ATOM   2021  CG  PHE B 275      29.860  45.229  54.903  1.00 44.56           C  
ANISOU 2021  CG  PHE B 275     5313   4615   7004   1371  -1352   -234       C  
ATOM   2022  CD1 PHE B 275      29.331  44.776  56.098  1.00 49.24           C  
ANISOU 2022  CD1 PHE B 275     5931   5226   7553   1421  -1376    -46       C  
ATOM   2023  CD2 PHE B 275      29.200  44.918  53.722  1.00 52.52           C  
ANISOU 2023  CD2 PHE B 275     6310   5543   8101   1299  -1314   -281       C  
ATOM   2024  CE1 PHE B 275      28.174  44.017  56.120  1.00 57.35           C  
ANISOU 2024  CE1 PHE B 275     6969   6186   8635   1392  -1363    103       C  
ATOM   2025  CE2 PHE B 275      28.040  44.161  53.737  1.00 56.96           C  
ANISOU 2025  CE2 PHE B 275     6885   6033   8722   1271  -1307   -147       C  
ATOM   2026  CZ  PHE B 275      27.528  43.710  54.940  1.00 58.17           C  
ANISOU 2026  CZ  PHE B 275     7062   6199   8842   1314  -1331     49       C  
ATOM   2027  N   ASN B 276      34.039  46.442  53.482  1.00 50.14           N  
ANISOU 2027  N   ASN B 276     5895   5401   7755   1362  -1381   -748       N  
ATOM   2028  CA  ASN B 276      34.992  47.509  53.219  1.00 51.30           C  
ANISOU 2028  CA  ASN B 276     6010   5623   7857   1352  -1372   -882       C  
ATOM   2029  C   ASN B 276      34.472  48.416  52.114  1.00 46.60           C  
ANISOU 2029  C   ASN B 276     5408   5058   7239   1283  -1302   -960       C  
ATOM   2030  O   ASN B 276      34.138  47.949  51.025  1.00 42.90           O  
ANISOU 2030  O   ASN B 276     4922   4542   6837   1232  -1265  -1000       O  
ATOM   2031  CB  ASN B 276      36.360  46.940  52.840  1.00 60.13           C  
ANISOU 2031  CB  ASN B 276     7073   6716   9058   1355  -1404   -986       C  
ATOM   2032  CG  ASN B 276      37.093  46.362  54.032  1.00 56.21           C  
ANISOU 2032  CG  ASN B 276     6580   6215   8564   1430  -1475   -928       C  
ATOM   2033  ND2 ASN B 276      38.034  47.125  54.575  1.00 42.54           N  
ANISOU 2033  ND2 ASN B 276     4831   4556   6778   1459  -1503   -989       N  
ATOM   2034  OD1 ASN B 276      36.819  45.240  54.460  1.00 60.19           O  
ANISOU 2034  OD1 ASN B 276     7100   6650   9121   1459  -1506   -826       O  
ATOM   2035  N   TRP B 277      34.399  49.711  52.404  1.00 41.66           N  
ANISOU 2035  N   TRP B 277     4795   4515   6520   1284  -1287   -982       N  
ATOM   2036  CA  TRP B 277      33.831  50.681  51.472  1.00 39.07           C  
ANISOU 2036  CA  TRP B 277     4465   4220   6161   1223  -1219  -1038       C  
ATOM   2037  C   TRP B 277      34.890  51.554  50.826  1.00 42.82           C  
ANISOU 2037  C   TRP B 277     4884   4743   6644   1187  -1201  -1170       C  
ATOM   2038  O   TRP B 277      35.843  51.976  51.479  1.00 50.54           O  
ANISOU 2038  O   TRP B 277     5841   5757   7605   1218  -1245  -1207       O  
ATOM   2039  CB  TRP B 277      32.806  51.566  52.185  1.00 40.69           C  
ANISOU 2039  CB  TRP B 277     4725   4478   6259   1245  -1211   -960       C  
ATOM   2040  CG  TRP B 277      31.557  50.845  52.552  1.00 41.80           C  
ANISOU 2040  CG  TRP B 277     4912   4580   6391   1263  -1210   -824       C  
ATOM   2041  CD1 TRP B 277      31.322  50.145  53.698  1.00 37.15           C  
ANISOU 2041  CD1 TRP B 277     4352   3983   5779   1324  -1258   -698       C  
ATOM   2042  CD2 TRP B 277      30.363  50.743  51.765  1.00 44.04           C  
ANISOU 2042  CD2 TRP B 277     5214   4828   6689   1216  -1157   -793       C  
ATOM   2043  CE2 TRP B 277      29.444  49.972  52.503  1.00 40.51           C  
ANISOU 2043  CE2 TRP B 277     4808   4356   6230   1239  -1173   -640       C  
ATOM   2044  CE3 TRP B 277      29.982  51.230  50.509  1.00 40.17           C  
ANISOU 2044  CE3 TRP B 277     4714   4344   6205   1138  -1084   -867       C  
ATOM   2045  NE1 TRP B 277      30.052  49.620  53.679  1.00 41.01           N  
ANISOU 2045  NE1 TRP B 277     4872   4434   6274   1315  -1239   -581       N  
ATOM   2046  CZ2 TRP B 277      28.169  49.679  52.031  1.00 41.34           C  
ANISOU 2046  CZ2 TRP B 277     4940   4434   6333   1180  -1119   -566       C  
ATOM   2047  CZ3 TRP B 277      28.712  50.937  50.043  1.00 35.15           C  
ANISOU 2047  CZ3 TRP B 277     4110   3686   5558   1085  -1034   -799       C  
ATOM   2048  CH2 TRP B 277      27.823  50.168  50.802  1.00 33.04           C  
ANISOU 2048  CH2 TRP B 277     3880   3388   5287   1104  -1053   -653       C  
ATOM   2049  N   TYR B 278      34.711  51.831  49.540  1.00 39.29           N  
ANISOU 2049  N   TYR B 278     4407   4300   6220   1121  -1135  -1235       N  
ATOM   2050  CA  TYR B 278      35.663  52.649  48.806  1.00 36.87           C  
ANISOU 2050  CA  TYR B 278     4037   4044   5928   1081  -1108  -1343       C  
ATOM   2051  C   TYR B 278      34.953  53.678  47.942  1.00 40.06           C  
ANISOU 2051  C   TYR B 278     4444   4487   6292   1022  -1032  -1361       C  
ATOM   2052  O   TYR B 278      33.976  53.363  47.262  1.00 47.31           O  
ANISOU 2052  O   TYR B 278     5385   5385   7205    992   -984  -1334       O  
ATOM   2053  CB  TYR B 278      36.569  51.772  47.938  1.00 39.43           C  
ANISOU 2053  CB  TYR B 278     4296   4350   6335   1064  -1105  -1419       C  
ATOM   2054  CG  TYR B 278      37.252  50.658  48.696  1.00 40.59           C  
ANISOU 2054  CG  TYR B 278     4441   4449   6532   1121  -1178  -1403       C  
ATOM   2055  CD1 TYR B 278      36.636  49.422  48.862  1.00 45.18           C  
ANISOU 2055  CD1 TYR B 278     5056   4955   7153   1143  -1200  -1335       C  
ATOM   2056  CD2 TYR B 278      38.513  50.841  49.248  1.00 50.27           C  
ANISOU 2056  CD2 TYR B 278     5628   5700   7773   1152  -1228  -1453       C  
ATOM   2057  CE1 TYR B 278      37.258  48.403  49.558  1.00 53.58           C  
ANISOU 2057  CE1 TYR B 278     6117   5970   8269   1195  -1267  -1311       C  
ATOM   2058  CE2 TYR B 278      39.140  49.826  49.943  1.00 52.67           C  
ANISOU 2058  CE2 TYR B 278     5931   5961   8120   1206  -1295  -1436       C  
ATOM   2059  CZ  TYR B 278      38.509  48.612  50.096  1.00 53.67           C  
ANISOU 2059  CZ  TYR B 278     6094   6013   8285   1228  -1313  -1361       C  
ATOM   2060  OH  TYR B 278      39.135  47.603  50.789  1.00 57.54           O  
ANISOU 2060  OH  TYR B 278     6582   6457   8824   1283  -1379  -1336       O  
ATOM   2061  N   VAL B 279      35.445  54.911  47.985  1.00 37.05           N  
ANISOU 2061  N   VAL B 279     4035   4155   5886   1005  -1025  -1406       N  
ATOM   2062  CA  VAL B 279      34.950  55.976  47.124  1.00 38.80           C  
ANISOU 2062  CA  VAL B 279     4249   4413   6081    947   -953  -1427       C  
ATOM   2063  C   VAL B 279      36.050  56.360  46.146  1.00 49.55           C  
ANISOU 2063  C   VAL B 279     5518   5810   7498    905   -919  -1519       C  
ATOM   2064  O   VAL B 279      37.065  56.938  46.541  1.00 57.76           O  
ANISOU 2064  O   VAL B 279     6511   6869   8567    914   -954  -1565       O  
ATOM   2065  CB  VAL B 279      34.508  57.213  47.930  1.00 37.56           C  
ANISOU 2065  CB  VAL B 279     4132   4280   5861    959   -970  -1399       C  
ATOM   2066  CG1 VAL B 279      34.000  58.301  46.995  1.00 32.20           C  
ANISOU 2066  CG1 VAL B 279     3444   3626   5164    896   -896  -1418       C  
ATOM   2067  CG2 VAL B 279      33.440  56.835  48.944  1.00 35.33           C  
ANISOU 2067  CG2 VAL B 279     3932   3979   5513   1013  -1003  -1306       C  
ATOM   2068  N   ASP B 280      35.844  56.026  44.873  1.00 46.93           N  
ANISOU 2068  N   ASP B 280     5156   5493   7182    863   -851  -1546       N  
ATOM   2069  CA  ASP B 280      36.870  56.179  43.842  1.00 47.07           C  
ANISOU 2069  CA  ASP B 280     5079   5557   7250    833   -812  -1630       C  
ATOM   2070  C   ASP B 280      38.186  55.520  44.257  1.00 47.24           C  
ANISOU 2070  C   ASP B 280     5047   5570   7332    870   -874  -1680       C  
ATOM   2071  O   ASP B 280      39.258  56.091  44.068  1.00 51.43           O  
ANISOU 2071  O   ASP B 280     5501   6136   7904    860   -872  -1742       O  
ATOM   2072  CB  ASP B 280      37.103  57.657  43.511  1.00 44.49           C  
ANISOU 2072  CB  ASP B 280     4709   5272   6923    795   -770  -1655       C  
ATOM   2073  CG  ASP B 280      36.132  58.179  42.470  1.00 47.10           C  
ANISOU 2073  CG  ASP B 280     5052   5632   7212    748   -681  -1639       C  
ATOM   2074  OD1 ASP B 280      35.536  57.356  41.745  1.00 46.87           O  
ANISOU 2074  OD1 ASP B 280     5039   5608   7160    740   -646  -1634       O  
ATOM   2075  OD2 ASP B 280      35.970  59.413  42.373  1.00 50.21           O1-
ANISOU 2075  OD2 ASP B 280     5445   6051   7583    702   -650  -1614       O1-
ATOM   2076  N   GLY B 281      38.094  54.323  44.830  1.00 43.41           N  
ANISOU 2076  N   GLY B 281     4600   5034   6858    912   -928  -1652       N  
ATOM   2077  CA  GLY B 281      39.272  53.555  45.192  1.00 38.86           C  
ANISOU 2077  CA  GLY B 281     3982   4445   6340    950   -988  -1698       C  
ATOM   2078  C   GLY B 281      39.830  53.836  46.575  1.00 47.39           C  
ANISOU 2078  C   GLY B 281     5080   5509   7416    996  -1067  -1679       C  
ATOM   2079  O   GLY B 281      40.610  53.045  47.105  1.00 58.11           O  
ANISOU 2079  O   GLY B 281     6425   6842   8811   1039  -1127  -1697       O  
ATOM   2080  N   VAL B 282      39.444  54.962  47.162  1.00 50.89           N  
ANISOU 2080  N   VAL B 282     5553   5969   7813    991  -1071  -1650       N  
ATOM   2081  CA  VAL B 282      39.923  55.326  48.491  1.00 51.87           C  
ANISOU 2081  CA  VAL B 282     5696   6091   7921   1038  -1150  -1641       C  
ATOM   2082  C   VAL B 282      38.972  54.824  49.567  1.00 53.77           C  
ANISOU 2082  C   VAL B 282     6030   6300   8100   1091  -1191  -1545       C  
ATOM   2083  O   VAL B 282      37.771  55.072  49.504  1.00 58.18           O  
ANISOU 2083  O   VAL B 282     6645   6855   8607   1079  -1155  -1484       O  
ATOM   2084  CB  VAL B 282      40.084  56.846  48.632  1.00 50.91           C  
ANISOU 2084  CB  VAL B 282     5550   6004   7788   1011  -1145  -1671       C  
ATOM   2085  CG1 VAL B 282      40.604  57.195  50.016  1.00 49.59           C  
ANISOU 2085  CG1 VAL B 282     5400   5841   7601   1065  -1236  -1677       C  
ATOM   2086  CG2 VAL B 282      41.016  57.371  47.561  1.00 46.59           C  
ANISOU 2086  CG2 VAL B 282     4901   5488   7314    959  -1099  -1754       C  
ATOM   2087  N   GLU B 283      39.509  54.123  50.560  1.00 48.20           N  
ANISOU 2087  N   GLU B 283     5338   5576   7399   1153  -1264  -1528       N  
ATOM   2088  CA  GLU B 283      38.673  53.537  51.603  1.00 47.66           C  
ANISOU 2088  CA  GLU B 283     5349   5484   7275   1211  -1301  -1424       C  
ATOM   2089  C   GLU B 283      38.097  54.595  52.543  1.00 54.48           C  
ANISOU 2089  C   GLU B 283     6260   6392   8047   1237  -1322  -1387       C  
ATOM   2090  O   GLU B 283      38.791  55.523  52.958  1.00 56.22           O  
ANISOU 2090  O   GLU B 283     6454   6651   8256   1242  -1356  -1449       O  
ATOM   2091  CB  GLU B 283      39.459  52.498  52.408  1.00 44.57           C  
ANISOU 2091  CB  GLU B 283     4954   5066   6913   1274  -1371  -1410       C  
ATOM   2092  CG  GLU B 283      38.616  51.736  53.427  1.00 46.64           C  
ANISOU 2092  CG  GLU B 283     5289   5304   7129   1335  -1404  -1282       C  
ATOM   2093  CD  GLU B 283      39.362  50.585  54.079  1.00 52.94           C  
ANISOU 2093  CD  GLU B 283     6079   6066   7970   1393  -1466  -1256       C  
ATOM   2094  OE1 GLU B 283      38.874  50.057  55.100  1.00 55.44           O  
ANISOU 2094  OE1 GLU B 283     6444   6376   8243   1452  -1501  -1145       O  
ATOM   2095  OE2 GLU B 283      40.438  50.207  53.569  1.00 61.20           O1-
ANISOU 2095  OE2 GLU B 283     7067   7095   9092   1381  -1478  -1343       O1-
ATOM   2096  N   VAL B 284      36.814  54.444  52.865  1.00 52.28           N  
ANISOU 2096  N   VAL B 284     6049   6108   7706   1254  -1305  -1290       N  
ATOM   2097  CA  VAL B 284      36.147  55.295  53.845  1.00 44.39           C  
ANISOU 2097  CA  VAL B 284     5102   5161   6605   1292  -1328  -1244       C  
ATOM   2098  C   VAL B 284      35.612  54.427  54.985  1.00 43.44           C  
ANISOU 2098  C   VAL B 284     5036   5044   6426   1368  -1369  -1126       C  
ATOM   2099  O   VAL B 284      35.490  53.210  54.834  1.00 46.48           O  
ANISOU 2099  O   VAL B 284     5425   5373   6862   1376  -1367  -1066       O  
ATOM   2100  CB  VAL B 284      35.004  56.107  53.207  1.00 43.67           C  
ANISOU 2100  CB  VAL B 284     5036   5080   6475   1246  -1264  -1229       C  
ATOM   2101  CG1 VAL B 284      35.543  56.997  52.093  1.00 35.79           C  
ANISOU 2101  CG1 VAL B 284     3979   4084   5535   1171  -1219  -1330       C  
ATOM   2102  CG2 VAL B 284      33.925  55.176  52.677  1.00 41.65           C  
ANISOU 2102  CG2 VAL B 284     4815   4779   6232   1231  -1217  -1145       C  
ATOM   2103  N   HIS B 285      35.290  55.043  56.120  1.00 39.62           N  
ANISOU 2103  N   HIS B 285     4590   4627   5835   1423  -1405  -1088       N  
ATOM   2104  CA  HIS B 285      35.038  54.267  57.334  1.00 43.11           C  
ANISOU 2104  CA  HIS B 285     5071   5096   6212   1502  -1448   -975       C  
ATOM   2105  C   HIS B 285      33.731  54.581  58.066  1.00 49.42           C  
ANISOU 2105  C   HIS B 285     5931   5960   6888   1539  -1435   -865       C  
ATOM   2106  O   HIS B 285      33.501  54.064  59.162  1.00 52.10           O  
ANISOU 2106  O   HIS B 285     6298   6344   7153   1607  -1466   -761       O  
ATOM   2107  CB  HIS B 285      36.202  54.464  58.311  1.00 42.32           C  
ANISOU 2107  CB  HIS B 285     4952   5041   6087   1559  -1519  -1029       C  
ATOM   2108  CG  HIS B 285      37.533  54.076  57.752  1.00 48.26           C  
ANISOU 2108  CG  HIS B 285     5643   5742   6953   1534  -1539  -1126       C  
ATOM   2109  CD2 HIS B 285      38.442  54.784  57.041  1.00 49.30           C  
ANISOU 2109  CD2 HIS B 285     5718   5864   7150   1482  -1537  -1258       C  
ATOM   2110  ND1 HIS B 285      38.064  52.814  57.907  1.00 51.18           N  
ANISOU 2110  ND1 HIS B 285     5999   6064   7381   1563  -1565  -1083       N  
ATOM   2111  CE1 HIS B 285      39.242  52.761  57.312  1.00 56.36           C  
ANISOU 2111  CE1 HIS B 285     6596   6690   8128   1533  -1577  -1194       C  
ATOM   2112  NE2 HIS B 285      39.495  53.943  56.779  1.00 58.80           N  
ANISOU 2112  NE2 HIS B 285     6875   7024   8442   1483  -1559  -1297       N  
ATOM   2113  N   ASN B 286      32.880  55.415  57.474  1.00 46.55           N  
ANISOU 2113  N   ASN B 286     5584   5608   6496   1497  -1388   -883       N  
ATOM   2114  CA  ASN B 286      31.679  55.882  58.166  1.00 43.82           C  
ANISOU 2114  CA  ASN B 286     5291   5339   6022   1532  -1376   -797       C  
ATOM   2115  C   ASN B 286      30.464  54.982  57.997  1.00 45.27           C  
ANISOU 2115  C   ASN B 286     5505   5495   6200   1528  -1336   -653       C  
ATOM   2116  O   ASN B 286      29.366  55.335  58.422  1.00 50.77           O  
ANISOU 2116  O   ASN B 286     6242   6257   6793   1548  -1315   -574       O  
ATOM   2117  CB  ASN B 286      31.325  57.295  57.704  1.00 47.33           C  
ANISOU 2117  CB  ASN B 286     5737   5811   6433   1495  -1351   -885       C  
ATOM   2118  CG  ASN B 286      31.292  57.424  56.194  1.00 53.96           C  
ANISOU 2118  CG  ASN B 286     6547   6572   7382   1408  -1294   -946       C  
ATOM   2119  ND2 ASN B 286      30.242  58.051  55.674  1.00 55.22           N  
ANISOU 2119  ND2 ASN B 286     6735   6744   7501   1362  -1235   -927       N  
ATOM   2120  OD1 ASN B 286      32.198  56.963  55.504  1.00 54.69           O  
ANISOU 2120  OD1 ASN B 286     6593   6604   7582   1370  -1291  -1006       O  
ATOM   2121  N   ALA B 287      30.654  53.822  57.379  1.00 40.90           N  
ANISOU 2121  N   ALA B 287     4931   4846   5761   1501  -1327   -622       N  
ATOM   2122  CA  ALA B 287      29.538  52.920  57.119  1.00 41.71           C  
ANISOU 2122  CA  ALA B 287     5057   4901   5889   1487  -1296   -493       C  
ATOM   2123  C   ALA B 287      29.017  52.276  58.398  1.00 44.61           C  
ANISOU 2123  C   ALA B 287     5453   5323   6172   1556  -1321   -326       C  
ATOM   2124  O   ALA B 287      29.785  51.968  59.310  1.00 46.22           O  
ANISOU 2124  O   ALA B 287     5649   5561   6351   1611  -1367   -306       O  
ATOM   2125  CB  ALA B 287      29.946  51.854  56.134  1.00 32.78           C  
ANISOU 2125  CB  ALA B 287     3893   3648   4915   1439  -1286   -520       C  
ATOM   2126  N   LYS B 288      27.705  52.074  58.452  1.00 47.22           N  
ANISOU 2126  N   LYS B 288     5816   5669   6456   1544  -1280   -201       N  
ATOM   2127  CA  LYS B 288      27.065  51.427  59.591  1.00 46.22           C  
ANISOU 2127  CA  LYS B 288     5710   5599   6251   1607  -1296    -18       C  
ATOM   2128  C   LYS B 288      26.398  50.121  59.158  1.00 46.35           C  
ANISOU 2128  C   LYS B 288     5722   5507   6380   1557  -1270    112       C  
ATOM   2129  O   LYS B 288      25.821  50.035  58.072  1.00 50.32           O  
ANISOU 2129  O   LYS B 288     6226   5937   6955   1463  -1211     82       O  
ATOM   2130  CB  LYS B 288      26.046  52.370  60.230  1.00 50.39           C  
ANISOU 2130  CB  LYS B 288     6273   6266   6607   1633  -1263     34       C  
ATOM   2131  CG  LYS B 288      26.617  53.721  60.619  1.00 51.36           C  
ANISOU 2131  CG  LYS B 288     6399   6485   6629   1659  -1279   -106       C  
ATOM   2132  CD  LYS B 288      27.689  53.578  61.685  1.00 54.36           C  
ANISOU 2132  CD  LYS B 288     6765   6917   6973   1723  -1335   -119       C  
ATOM   2133  CE  LYS B 288      28.475  54.869  61.852  1.00 53.46           C  
ANISOU 2133  CE  LYS B 288     6646   6858   6810   1735  -1363   -293       C  
ATOM   2134  NZ  LYS B 288      29.540  54.745  62.886  1.00 55.43           N1+
ANISOU 2134  NZ  LYS B 288     6879   7157   7024   1800  -1422   -317       N1+
ATOM   2135  N   THR B 289      26.486  49.103  60.007  1.00 49.29           N  
ANISOU 2135  N   THR B 289     6088   5868   6771   1615  -1313    258       N  
ATOM   2136  CA  THR B 289      26.010  47.771  59.651  1.00 54.75           C  
ANISOU 2136  CA  THR B 289     6767   6433   7602   1574  -1307    381       C  
ATOM   2137  C   THR B 289      24.791  47.383  60.473  1.00 58.36           C  
ANISOU 2137  C   THR B 289     7241   6953   7979   1587  -1277    602       C  
ATOM   2138  O   THR B 289      24.783  47.533  61.695  1.00 60.96           O  
ANISOU 2138  O   THR B 289     7578   7407   8175   1671  -1298    705       O  
ATOM   2139  CB  THR B 289      27.115  46.708  59.850  1.00 54.10           C  
ANISOU 2139  CB  THR B 289     6654   6264   7639   1599  -1360    386       C  
ATOM   2140  CG2 THR B 289      26.543  45.307  59.691  1.00 55.05           C  
ANISOU 2140  CG2 THR B 289     6761   6258   7898   1565  -1360    537       C  
ATOM   2141  OG1 THR B 289      28.152  46.898  58.878  1.00 53.69           O  
ANISOU 2141  OG1 THR B 289     6577   6142   7682   1563  -1370    186       O  
ATOM   2142  N   LYS B 290      23.759  46.892  59.795  1.00 65.50           N  
ANISOU 2142  N   LYS B 290     8145   7781   8960   1498  -1222    673       N  
ATOM   2143  CA  LYS B 290      22.546  46.433  60.462  1.00 78.96           C  
ANISOU 2143  CA  LYS B 290     9855   9533  10615   1496  -1187    894       C  
ATOM   2144  C   LYS B 290      22.743  45.038  61.049  1.00 90.56           C  
ANISOU 2144  C   LYS B 290    11297  10913  12197   1530  -1240   1069       C  
ATOM   2145  O   LYS B 290      23.448  44.212  60.467  1.00 87.76           O  
ANISOU 2145  O   LYS B 290    10920  10405  12019   1510  -1285   1012       O  
ATOM   2146  CB  LYS B 290      21.364  46.429  59.490  1.00 76.63           C  
ANISOU 2146  CB  LYS B 290     9561   9183  10372   1384  -1112    900       C  
ATOM   2147  CG  LYS B 290      20.473  47.658  59.589  1.00 77.77           C  
ANISOU 2147  CG  LYS B 290     9734   9476  10340   1373  -1045    881       C  
ATOM   2148  CD  LYS B 290      19.437  47.691  58.474  1.00 77.69           C  
ANISOU 2148  CD  LYS B 290     9722   9403  10393   1262   -977    857       C  
ATOM   2149  CE  LYS B 290      18.417  48.795  58.711  1.00 74.61           C  
ANISOU 2149  CE  LYS B 290     9358   9163   9829   1259   -912    873       C  
ATOM   2150  NZ  LYS B 290      17.417  48.875  57.612  1.00 74.10           N1+
ANISOU 2150  NZ  LYS B 290     9291   9045   9821   1155   -849    844       N1+
ATOM   2151  N   PRO B 291      22.121  44.774  62.209  1.00 97.65           N  
ANISOU 2151  N   PRO B 291    12195  11914  12993   1585  -1234   1285       N  
ATOM   2152  CA  PRO B 291      22.203  43.448  62.834  1.00101.85           C  
ANISOU 2152  CA  PRO B 291    12719  12386  13594   1597  -1248   1443       C  
ATOM   2153  C   PRO B 291      21.620  42.353  61.942  1.00105.50           C  
ANISOU 2153  C   PRO B 291    13158  12662  14266   1484  -1225   1491       C  
ATOM   2154  O   PRO B 291      20.523  42.529  61.404  1.00108.82           O  
ANISOU 2154  O   PRO B 291    13573  13069  14705   1407  -1172   1527       O  
ATOM   2155  CB  PRO B 291      21.378  43.611  64.116  1.00100.11           C  
ANISOU 2155  CB  PRO B 291    12522  12332  13184   1632  -1219   1609       C  
ATOM   2156  CG  PRO B 291      20.497  44.792  63.863  1.00 94.97           C  
ANISOU 2156  CG  PRO B 291    11879  11797  12409   1604  -1158   1568       C  
ATOM   2157  CD  PRO B 291      21.289  45.706  62.990  1.00 94.66           C  
ANISOU 2157  CD  PRO B 291    11837  11736  12393   1624  -1183   1355       C  
ATOM   2158  N   ARG B 292      22.348  41.250  61.793  1.00101.50           N  
ANISOU 2158  N   ARG B 292    12634  12016  13914   1478  -1267   1484       N  
ATOM   2159  CA  ARG B 292      21.936  40.141  60.929  1.00101.73           C  
ANISOU 2159  CA  ARG B 292    12636  11855  14161   1377  -1263   1502       C  
ATOM   2160  C   ARG B 292      20.479  39.731  61.154  1.00102.61           C  
ANISOU 2160  C   ARG B 292    12738  11973  14275   1307  -1206   1692       C  
ATOM   2161  O   ARG B 292      20.020  39.654  62.294  1.00106.27           O  
ANISOU 2161  O   ARG B 292    13213  12554  14612   1344  -1183   1865       O  
ATOM   2162  CB  ARG B 292      22.842  38.925  61.157  1.00105.76           C  
ANISOU 2162  CB  ARG B 292    13130  12249  14803   1399  -1319   1521       C  
ATOM   2163  CG  ARG B 292      24.229  39.232  61.704  1.00108.38           C  
ANISOU 2163  CG  ARG B 292    13472  12649  15059   1504  -1370   1434       C  
ATOM   2164  CD  ARG B 292      24.769  38.007  62.437  1.00110.30           C  
ANISOU 2164  CD  ARG B 292    13706  12830  15374   1544  -1413   1551       C  
ATOM   2165  NE  ARG B 292      26.151  38.160  62.883  1.00109.10           N  
ANISOU 2165  NE  ARG B 292    13554  12725  15176   1640  -1465   1463       N  
ATOM   2166  CZ  ARG B 292      26.760  37.323  63.721  1.00106.24           C  
ANISOU 2166  CZ  ARG B 292    13189  12351  14827   1705  -1507   1562       C  
ATOM   2167  NH1 ARG B 292      26.111  36.272  64.209  1.00106.79           N1+
ANISOU 2167  NH1 ARG B 292    13258  12358  14958   1680  -1505   1752       N1+
ATOM   2168  NH2 ARG B 292      28.022  37.530  64.067  1.00 99.22           N  
ANISOU 2168  NH2 ARG B 292    12293  11511  13896   1789  -1551   1472       N  
ATOM   2169  N   GLU B 293      19.753  39.472  60.071  1.00 97.64           N  
ANISOU 2169  N   GLU B 293    12086  11223  13788   1205  -1184   1652       N  
ATOM   2170  CA  GLU B 293      18.346  39.100  60.191  1.00 95.08           C  
ANISOU 2170  CA  GLU B 293    11743  10901  13483   1129  -1128   1821       C  
ATOM   2171  C   GLU B 293      18.055  37.763  59.504  1.00 92.32           C  
ANISOU 2171  C   GLU B 293    11350  10345  13382   1036  -1150   1844       C  
ATOM   2172  O   GLU B 293      18.562  37.478  58.416  1.00 90.72           O  
ANISOU 2172  O   GLU B 293    11134  10003  13334   1002  -1190   1672       O  
ATOM   2173  CB  GLU B 293      17.444  40.207  59.630  1.00 91.36           C  
ANISOU 2173  CB  GLU B 293    11279  10512  12920   1092  -1071   1773       C  
ATOM   2174  CG  GLU B 293      17.395  40.296  58.108  1.00 92.04           C  
ANISOU 2174  CG  GLU B 293    11351  10460  13160   1020  -1082   1591       C  
ATOM   2175  CD  GLU B 293      16.760  41.586  57.616  1.00 90.33           C  
ANISOU 2175  CD  GLU B 293    11152  10349  12819   1005  -1030   1514       C  
ATOM   2176  OE1 GLU B 293      15.637  41.530  57.070  1.00 89.32           O  
ANISOU 2176  OE1 GLU B 293    11008  10199  12731    922   -982   1546       O  
ATOM   2177  OE2 GLU B 293      17.391  42.655  57.768  1.00 86.43           O1-
ANISOU 2177  OE2 GLU B 293    10696   9981  12163   1060  -1020   1385       O1-
ATOM   2178  N   GLU B 294      17.244  36.939  60.161  1.00 87.64           N  
ANISOU 2178  N   GLU B 294    10731   9743  12827    996  -1127   2050       N  
ATOM   2179  CA  GLU B 294      16.919  35.617  59.642  1.00 86.28           C  
ANISOU 2179  CA  GLU B 294    10507   9378  12897    907  -1156   2089       C  
ATOM   2180  C   GLU B 294      15.834  35.698  58.578  1.00 81.10           C  
ANISOU 2180  C   GLU B 294     9821   8652  12342    804  -1125   2043       C  
ATOM   2181  O   GLU B 294      14.877  36.463  58.707  1.00 71.69           O  
ANISOU 2181  O   GLU B 294     8635   7580  11025    785  -1060   2109       O  
ATOM   2182  CB  GLU B 294      16.484  34.685  60.776  1.00 92.60           C  
ANISOU 2182  CB  GLU B 294    11281  10193  13712    901  -1146   2334       C  
ATOM   2183  CG  GLU B 294      16.279  33.239  60.336  1.00 98.35           C  
ANISOU 2183  CG  GLU B 294    11948  10713  14706    817  -1190   2377       C  
ATOM   2184  CD  GLU B 294      15.799  32.341  61.461  1.00106.07           C  
ANISOU 2184  CD  GLU B 294    12891  11707  15705    805  -1177   2631       C  
ATOM   2185  OE1 GLU B 294      15.247  31.260  61.162  1.00108.10           O  
ANISOU 2185  OE1 GLU B 294    13085  11816  16172    719  -1198   2705       O  
ATOM   2186  OE2 GLU B 294      15.979  32.713  62.642  1.00108.12           O1-
ANISOU 2186  OE2 GLU B 294    13179  12129  15771    884  -1150   2752       O1-
ATOM   2187  N   GLN B 295      15.986  34.898  57.529  1.00 86.03           N  
ANISOU 2187  N   GLN B 295    10411   9090  13188    741  -1175   1922       N  
ATOM   2188  CA  GLN B 295      15.063  34.937  56.404  1.00 89.69           C  
ANISOU 2188  CA  GLN B 295    10844   9476  13758    649  -1159   1843       C  
ATOM   2189  C   GLN B 295      14.074  33.776  56.373  1.00102.31           C  
ANISOU 2189  C   GLN B 295    12374  10959  15540    554  -1165   1980       C  
ATOM   2190  O   GLN B 295      14.167  32.820  57.149  1.00103.49           O  
ANISOU 2190  O   GLN B 295    12496  11065  15762    553  -1188   2131       O  
ATOM   2191  CB  GLN B 295      15.839  34.958  55.083  1.00 83.71           C  
ANISOU 2191  CB  GLN B 295    10089   8607  13112    645  -1211   1573       C  
ATOM   2192  CG  GLN B 295      16.662  36.214  54.857  1.00 78.49           C  
ANISOU 2192  CG  GLN B 295     9481   8054  12288    720  -1199   1412       C  
ATOM   2193  CD  GLN B 295      15.816  37.471  54.834  1.00 76.46           C  
ANISOU 2193  CD  GLN B 295     9249   7935  11866    716  -1130   1438       C  
ATOM   2194  NE2 GLN B 295      15.755  38.162  55.965  1.00 79.91           N  
ANISOU 2194  NE2 GLN B 295     9718   8538  12107    778  -1092   1574       N  
ATOM   2195  OE1 GLN B 295      15.227  37.820  53.812  1.00 75.46           O  
ANISOU 2195  OE1 GLN B 295     9113   7775  11783    663  -1113   1331       O  
ATOM   2196  N   TYR B 296      13.115  33.916  55.464  1.00115.04           N  
ANISOU 2196  N   TYR B 296    13958  12527  17224    475  -1145   1925       N  
ATOM   2197  CA  TYR B 296      12.206  32.866  55.017  1.00121.88           C  
ANISOU 2197  CA  TYR B 296    14749  13256  18303    374  -1167   1978       C  
ATOM   2198  C   TYR B 296      12.866  31.485  54.961  1.00113.89           C  
ANISOU 2198  C   TYR B 296    13694  12075  17503    363  -1253   1960       C  
ATOM   2199  O   TYR B 296      12.518  30.581  55.721  1.00116.36           O  
ANISOU 2199  O   TYR B 296    13961  12349  17901    335  -1262   2150       O  
ATOM   2200  CB  TYR B 296      11.686  33.249  53.628  1.00134.79           C  
ANISOU 2200  CB  TYR B 296    16372  14836  20005    318  -1169   1790       C  
ATOM   2201  CG  TYR B 296      10.399  32.600  53.167  1.00144.66           C  
ANISOU 2201  CG  TYR B 296    17548  16001  21415    213  -1169   1851       C  
ATOM   2202  CD1 TYR B 296       9.164  33.154  53.490  1.00145.98           C  
ANISOU 2202  CD1 TYR B 296    17702  16275  21488    172  -1093   1998       C  
ATOM   2203  CD2 TYR B 296      10.418  31.465  52.361  1.00149.45           C  
ANISOU 2203  CD2 TYR B 296    18092  16430  22263    160  -1248   1747       C  
ATOM   2204  CE1 TYR B 296       7.985  32.581  53.050  1.00147.21           C  
ANISOU 2204  CE1 TYR B 296    17783  16357  21792     76  -1094   2047       C  
ATOM   2205  CE2 TYR B 296       9.242  30.885  51.917  1.00150.92           C  
ANISOU 2205  CE2 TYR B 296    18202  16541  22599     68  -1255   1790       C  
ATOM   2206  CZ  TYR B 296       8.029  31.446  52.264  1.00148.69           C  
ANISOU 2206  CZ  TYR B 296    17907  16361  22226     24  -1178   1942       C  
ATOM   2207  OH  TYR B 296       6.859  30.869  51.822  1.00147.51           O  
ANISOU 2207  OH  TYR B 296    17676  16139  22231    -66  -1188   1983       O  
ATOM   2208  N   ASN B 297      13.841  31.356  54.066  1.00103.08           N  
ANISOU 2208  N   ASN B 297    12338  10618  16212    390  -1314   1728       N  
ATOM   2209  CA  ASN B 297      14.446  30.070  53.722  1.00 94.30           C  
ANISOU 2209  CA  ASN B 297    11177   9337  15315    376  -1404   1657       C  
ATOM   2210  C   ASN B 297      15.578  29.609  54.648  1.00 89.61           C  
ANISOU 2210  C   ASN B 297    10606   8740  14703    452  -1440   1726       C  
ATOM   2211  O   ASN B 297      16.539  28.993  54.181  1.00 88.74           O  
ANISOU 2211  O   ASN B 297    10485   8527  14706    477  -1512   1580       O  
ATOM   2212  CB  ASN B 297      14.965  30.143  52.282  1.00 92.43           C  
ANISOU 2212  CB  ASN B 297    10936   9027  15155    375  -1451   1362       C  
ATOM   2213  CG  ASN B 297      15.590  31.492  51.954  1.00 94.05           C  
ANISOU 2213  CG  ASN B 297    11212   9360  15163    438  -1409   1211       C  
ATOM   2214  ND2 ASN B 297      15.701  31.815  50.668  1.00 89.73           N  
ANISOU 2214  ND2 ASN B 297    10660   8793  14641    425  -1421    975       N  
ATOM   2215  OD1 ASN B 297      15.971  32.235  52.859  1.00 97.55           O  
ANISOU 2215  OD1 ASN B 297    11709   9926  15428    502  -1367   1305       O  
ATOM   2216  N   SER B 298      15.450  29.876  55.949  1.00 91.25           N  
ANISOU 2216  N   SER B 298    10841   9065  14766    490  -1391   1945       N  
ATOM   2217  CA  SER B 298      16.497  29.566  56.933  1.00 93.99           C  
ANISOU 2217  CA  SER B 298    11215   9435  15061    573  -1418   2021       C  
ATOM   2218  C   SER B 298      17.851  30.078  56.463  1.00100.48           C  
ANISOU 2218  C   SER B 298    12085  10271  15821    652  -1452   1797       C  
ATOM   2219  O   SER B 298      18.855  29.364  56.496  1.00101.47           O  
ANISOU 2219  O   SER B 298    12203  10310  16039    691  -1518   1738       O  
ATOM   2220  CB  SER B 298      16.564  28.063  57.218  1.00 92.21           C  
ANISOU 2220  CB  SER B 298    10928   9055  15054    539  -1484   2126       C  
ATOM   2221  OG  SER B 298      15.770  27.724  58.344  1.00 91.69           O  
ANISOU 2221  OG  SER B 298    10836   9044  14957    518  -1442   2402       O  
ATOM   2222  N   THR B 299      17.847  31.325  56.006  1.00103.92           N  
ANISOU 2222  N   THR B 299    12565  10817  16105    674  -1407   1673       N  
ATOM   2223  CA  THR B 299      19.039  32.012  55.537  1.00100.86           C  
ANISOU 2223  CA  THR B 299    12217  10469  15637    744  -1426   1460       C  
ATOM   2224  C   THR B 299      19.208  33.249  56.410  1.00 97.84           C  
ANISOU 2224  C   THR B 299    11893  10279  15002    821  -1370   1528       C  
ATOM   2225  O   THR B 299      18.309  33.600  57.173  1.00100.61           O  
ANISOU 2225  O   THR B 299    12253  10732  15243    812  -1314   1712       O  
ATOM   2226  CB  THR B 299      18.911  32.408  54.037  1.00 96.50           C  
ANISOU 2226  CB  THR B 299    11652   9871  15140    699  -1428   1220       C  
ATOM   2227  CG2 THR B 299      20.226  32.914  53.473  1.00 96.65           C  
ANISOU 2227  CG2 THR B 299    11696   9919  15108    763  -1452    991       C  
ATOM   2228  OG1 THR B 299      18.486  31.274  53.270  1.00 99.29           O  
ANISOU 2228  OG1 THR B 299    11943  10065  15719    623  -1478   1173       O  
ATOM   2229  N   TYR B 300      20.359  33.902  56.327  1.00 94.35           N  
ANISOU 2229  N   TYR B 300    11486   9897  14467    898  -1386   1379       N  
ATOM   2230  CA  TYR B 300      20.501  35.199  56.960  1.00 97.27           C  
ANISOU 2230  CA  TYR B 300    11904  10450  14605    968  -1341   1400       C  
ATOM   2231  C   TYR B 300      20.747  36.289  55.943  1.00 95.45           C  
ANISOU 2231  C   TYR B 300    11690  10261  14316    967  -1324   1181       C  
ATOM   2232  O   TYR B 300      21.225  36.040  54.835  1.00 94.23           O  
ANISOU 2232  O   TYR B 300    11515  10010  14278    939  -1353    987       O  
ATOM   2233  CB  TYR B 300      21.615  35.183  57.994  1.00101.26           C  
ANISOU 2233  CB  TYR B 300    12433  11024  15017   1070  -1373   1442       C  
ATOM   2234  CG  TYR B 300      21.255  34.343  59.174  1.00110.53           C  
ANISOU 2234  CG  TYR B 300    13598  12203  16194   1082  -1375   1685       C  
ATOM   2235  CD1 TYR B 300      20.519  34.870  60.225  1.00112.79           C  
ANISOU 2235  CD1 TYR B 300    13906  12646  16302   1109  -1321   1871       C  
ATOM   2236  CD2 TYR B 300      21.624  33.013  59.224  1.00119.42           C  
ANISOU 2236  CD2 TYR B 300    14692  13182  17501   1066  -1431   1727       C  
ATOM   2237  CE1 TYR B 300      20.178  34.094  61.303  1.00119.75           C  
ANISOU 2237  CE1 TYR B 300    14776  13544  17179   1119  -1317   2093       C  
ATOM   2238  CE2 TYR B 300      21.291  32.233  60.288  1.00126.28           C  
ANISOU 2238  CE2 TYR B 300    15549  14052  18378   1074  -1432   1954       C  
ATOM   2239  CZ  TYR B 300      20.572  32.772  61.324  1.00127.22           C  
ANISOU 2239  CZ  TYR B 300    15689  14334  18314   1099  -1373   2137       C  
ATOM   2240  OH  TYR B 300      20.251  31.969  62.383  1.00131.24           O  
ANISOU 2240  OH  TYR B 300    16181  14853  18829   1106  -1372   2363       O  
ATOM   2241  N   ARG B 301      20.406  37.502  56.349  1.00 89.30           N  
ANISOU 2241  N   ARG B 301    10945   9636  13348   1001  -1275   1215       N  
ATOM   2242  CA  ARG B 301      20.480  38.669  55.499  1.00 79.65           C  
ANISOU 2242  CA  ARG B 301     9740   8472  12053    999  -1251   1035       C  
ATOM   2243  C   ARG B 301      21.154  39.780  56.284  1.00 71.80           C  
ANISOU 2243  C   ARG B 301     8782   7639  10861   1092  -1246   1022       C  
ATOM   2244  O   ARG B 301      20.762  40.064  57.415  1.00 74.56           O  
ANISOU 2244  O   ARG B 301     9150   8108  11074   1135  -1225   1192       O  
ATOM   2245  CB  ARG B 301      19.077  39.078  55.051  1.00 83.14           C  
ANISOU 2245  CB  ARG B 301    10178   8931  12482    929  -1196   1089       C  
ATOM   2246  CG  ARG B 301      19.017  40.325  54.203  1.00 78.36           C  
ANISOU 2246  CG  ARG B 301     9590   8390  11792    926  -1166    921       C  
ATOM   2247  CD  ARG B 301      17.577  40.609  53.807  1.00 69.84           C  
ANISOU 2247  CD  ARG B 301     8510   7347  10680    842  -1096    976       C  
ATOM   2248  NE  ARG B 301      17.505  41.477  52.640  1.00 52.92           N  
ANISOU 2248  NE  ARG B 301     6382   5250   8477    799  -1050    767       N  
ATOM   2249  CZ  ARG B 301      17.523  42.802  52.707  1.00 54.18           C  
ANISOU 2249  CZ  ARG B 301     6581   5571   8435    816   -993    699       C  
ATOM   2250  NH1 ARG B 301      17.613  43.401  53.888  1.00 59.78           N1+
ANISOU 2250  NH1 ARG B 301     7318   6412   8982    879   -979    808       N1+
ATOM   2251  NH2 ARG B 301      17.452  43.525  51.597  1.00 53.86           N  
ANISOU 2251  NH2 ARG B 301     6548   5560   8356    774   -953    523       N  
ATOM   2252  N   VAL B 302      22.178  40.393  55.704  1.00 67.67           N  
ANISOU 2252  N   VAL B 302     8264   7130  10317   1123  -1265    815       N  
ATOM   2253  CA  VAL B 302      22.926  41.417  56.421  1.00 67.05           C  
ANISOU 2253  CA  VAL B 302     8212   7195  10068   1208  -1272    779       C  
ATOM   2254  C   VAL B 302      23.204  42.611  55.517  1.00 60.51           C  
ANISOU 2254  C   VAL B 302     7395   6420   9178   1197  -1249    571       C  
ATOM   2255  O   VAL B 302      23.552  42.459  54.342  1.00 57.53           O  
ANISOU 2255  O   VAL B 302     6995   5955   8907   1154  -1251    404       O  
ATOM   2256  CB  VAL B 302      24.245  40.847  57.004  1.00 65.85           C  
ANISOU 2256  CB  VAL B 302     8052   7027   9940   1274  -1326    758       C  
ATOM   2257  CG1 VAL B 302      25.184  40.388  55.897  1.00 68.99           C  
ANISOU 2257  CG1 VAL B 302     8422   7311  10479   1245  -1354    555       C  
ATOM   2258  CG2 VAL B 302      24.922  41.864  57.916  1.00 61.40           C  
ANISOU 2258  CG2 VAL B 302     7512   6623   9194   1366  -1337    742       C  
ATOM   2259  N   VAL B 303      23.034  43.805  56.078  1.00 52.92           N  
ANISOU 2259  N   VAL B 303     6468   5626   8015   1223  -1206    574       N  
ATOM   2260  CA  VAL B 303      23.040  45.034  55.293  1.00 46.54           C  
ANISOU 2260  CA  VAL B 303     5677   4897   7110   1185  -1151    403       C  
ATOM   2261  C   VAL B 303      24.025  46.074  55.825  1.00 46.19           C  
ANISOU 2261  C   VAL B 303     5647   4969   6933   1255  -1169    308       C  
ATOM   2262  O   VAL B 303      24.105  46.307  57.034  1.00 48.98           O  
ANISOU 2262  O   VAL B 303     6016   5419   7174   1329  -1191    410       O  
ATOM   2263  CB  VAL B 303      21.628  45.652  55.260  1.00 35.01           C  
ANISOU 2263  CB  VAL B 303     4242   3521   5541   1131  -1073    481       C  
ATOM   2264  CG1 VAL B 303      21.622  46.904  54.421  1.00 28.17           C  
ANISOU 2264  CG1 VAL B 303     3392   2725   4585   1092  -1020    314       C  
ATOM   2265  CG2 VAL B 303      20.619  44.651  54.721  1.00 32.07           C  
ANISOU 2265  CG2 VAL B 303     3847   3032   5306   1056  -1058    572       C  
ATOM   2266  N   SER B 304      24.775  46.696  54.921  1.00 40.61           N  
ANISOU 2266  N   SER B 304     4929   4257   6243   1233  -1160    113       N  
ATOM   2267  CA  SER B 304      25.671  47.790  55.290  1.00 43.67           C  
ANISOU 2267  CA  SER B 304     5324   4748   6522   1284  -1175      7       C  
ATOM   2268  C   SER B 304      25.288  49.068  54.544  1.00 45.98           C  
ANISOU 2268  C   SER B 304     5633   5112   6727   1227  -1107   -103       C  
ATOM   2269  O   SER B 304      25.066  49.047  53.332  1.00 39.13           O  
ANISOU 2269  O   SER B 304     4752   4189   5927   1153  -1065   -188       O  
ATOM   2270  CB  SER B 304      27.126  47.425  54.995  1.00 40.57           C  
ANISOU 2270  CB  SER B 304     4892   4289   6235   1320  -1235   -120       C  
ATOM   2271  OG  SER B 304      27.995  48.509  55.274  1.00 35.74           O  
ANISOU 2271  OG  SER B 304     4278   3769   5534   1360  -1249   -230       O  
ATOM   2272  N   VAL B 305      25.215  50.177  55.274  1.00 40.54           N  
ANISOU 2272  N   VAL B 305     4970   4546   5886   1265  -1100   -102       N  
ATOM   2273  CA  VAL B 305      24.771  51.444  54.703  1.00 33.48           C  
ANISOU 2273  CA  VAL B 305     4095   3720   4908   1216  -1041   -186       C  
ATOM   2274  C   VAL B 305      25.850  52.523  54.768  1.00 36.49           C  
ANISOU 2274  C   VAL B 305     4464   4154   5247   1247  -1067   -328       C  
ATOM   2275  O   VAL B 305      26.353  52.847  55.843  1.00 40.31           O  
ANISOU 2275  O   VAL B 305     4952   4705   5658   1327  -1120   -316       O  
ATOM   2276  CB  VAL B 305      23.508  51.963  55.416  1.00 41.44           C  
ANISOU 2276  CB  VAL B 305     5142   4828   5775   1226  -1003    -67       C  
ATOM   2277  CG1 VAL B 305      23.037  53.273  54.789  1.00 33.33           C  
ANISOU 2277  CG1 VAL B 305     4133   3860   4671   1177   -947   -157       C  
ATOM   2278  CG2 VAL B 305      22.407  50.907  55.374  1.00 36.15           C  
ANISOU 2278  CG2 VAL B 305     4475   4108   5154   1189   -976     85       C  
ATOM   2279  N   LEU B 306      26.199  53.078  53.610  1.00 34.91           N  
ANISOU 2279  N   LEU B 306     4243   3926   5094   1184  -1031   -460       N  
ATOM   2280  CA  LEU B 306      27.181  54.149  53.540  1.00 31.50           C  
ANISOU 2280  CA  LEU B 306     3791   3535   4642   1196  -1050   -591       C  
ATOM   2281  C   LEU B 306      26.525  55.484  53.178  1.00 37.27           C  
ANISOU 2281  C   LEU B 306     4546   4329   5287   1152   -996   -628       C  
ATOM   2282  O   LEU B 306      25.957  55.641  52.096  1.00 38.52           O  
ANISOU 2282  O   LEU B 306     4704   4464   5468   1075   -932   -649       O  
ATOM   2283  CB  LEU B 306      28.272  53.809  52.521  1.00 35.23           C  
ANISOU 2283  CB  LEU B 306     4209   3936   5241   1165  -1054   -712       C  
ATOM   2284  CG  LEU B 306      29.363  54.868  52.342  1.00 35.70           C  
ANISOU 2284  CG  LEU B 306     4231   4028   5303   1167  -1069   -843       C  
ATOM   2285  CD1 LEU B 306      30.299  54.892  53.545  1.00 33.66           C  
ANISOU 2285  CD1 LEU B 306     3961   3801   5029   1258  -1155   -853       C  
ATOM   2286  CD2 LEU B 306      30.139  54.680  51.042  1.00 27.23           C  
ANISOU 2286  CD2 LEU B 306     3102   2906   4340   1113  -1041   -955       C  
ATOM   2287  N   THR B 307      26.595  56.440  54.097  1.00 37.71           N  
ANISOU 2287  N   THR B 307     4618   4465   5244   1205  -1028   -637       N  
ATOM   2288  CA  THR B 307      26.116  57.785  53.828  1.00 32.40           C  
ANISOU 2288  CA  THR B 307     3964   3844   4504   1173   -992   -686       C  
ATOM   2289  C   THR B 307      27.071  58.469  52.861  1.00 40.23           C  
ANISOU 2289  C   THR B 307     4912   4799   5575   1120   -982   -819       C  
ATOM   2290  O   THR B 307      28.287  58.397  53.033  1.00 42.02           O  
ANISOU 2290  O   THR B 307     5096   5006   5862   1150  -1033   -892       O  
ATOM   2291  CB  THR B 307      25.987  58.609  55.119  1.00 39.23           C  
ANISOU 2291  CB  THR B 307     4854   4804   5249   1255  -1041   -676       C  
ATOM   2292  CG2 THR B 307      25.850  60.094  54.807  1.00 42.75           C  
ANISOU 2292  CG2 THR B 307     5304   5280   5659   1227  -1026   -763       C  
ATOM   2293  OG1 THR B 307      24.833  58.173  55.849  1.00 42.25           O  
ANISOU 2293  OG1 THR B 307     5276   5243   5535   1291  -1026   -541       O  
ATOM   2294  N   VAL B 308      26.524  59.119  51.836  1.00 37.66           N  
ANISOU 2294  N   VAL B 308     4590   4468   5251   1044   -916   -845       N  
ATOM   2295  CA  VAL B 308      27.346  59.750  50.809  1.00 39.51           C  
ANISOU 2295  CA  VAL B 308     4777   4675   5561    986   -893   -950       C  
ATOM   2296  C   VAL B 308      27.048  61.235  50.655  1.00 36.94           C  
ANISOU 2296  C   VAL B 308     4462   4384   5190    958   -875   -986       C  
ATOM   2297  O   VAL B 308      26.012  61.718  51.102  1.00 36.85           O  
ANISOU 2297  O   VAL B 308     4498   4413   5088    972   -864   -934       O  
ATOM   2298  CB  VAL B 308      27.137  59.063  49.451  1.00 41.12           C  
ANISOU 2298  CB  VAL B 308     4960   4834   5828    914   -827   -954       C  
ATOM   2299  CG1 VAL B 308      27.342  57.568  49.586  1.00 39.66           C  
ANISOU 2299  CG1 VAL B 308     4766   4601   5703    943   -852   -920       C  
ATOM   2300  CG2 VAL B 308      25.743  59.357  48.929  1.00 36.82           C  
ANISOU 2300  CG2 VAL B 308     4458   4310   5221    865   -761   -894       C  
ATOM   2301  N   LEU B 309      27.966  61.956  50.022  1.00 40.32           N  
ANISOU 2301  N   LEU B 309     4839   4793   5687    919   -872  -1074       N  
ATOM   2302  CA  LEU B 309      27.755  63.367  49.724  1.00 37.78           C  
ANISOU 2302  CA  LEU B 309     4518   4485   5351    882   -854  -1106       C  
ATOM   2303  C   LEU B 309      26.982  63.506  48.419  1.00 32.65           C  
ANISOU 2303  C   LEU B 309     3875   3831   4700    799   -764  -1076       C  
ATOM   2304  O   LEU B 309      27.309  62.837  47.438  1.00 32.33           O  
ANISOU 2304  O   LEU B 309     3799   3770   4714    757   -721  -1089       O  
ATOM   2305  CB  LEU B 309      29.093  64.106  49.634  1.00 33.51           C  
ANISOU 2305  CB  LEU B 309     3912   3924   4898    871   -892  -1201       C  
ATOM   2306  CG  LEU B 309      29.975  64.101  50.886  1.00 38.83           C  
ANISOU 2306  CG  LEU B 309     4569   4605   5581    954   -991  -1250       C  
ATOM   2307  CD1 LEU B 309      31.314  64.760  50.597  1.00 30.45           C  
ANISOU 2307  CD1 LEU B 309     3428   3515   4627    928  -1021  -1345       C  
ATOM   2308  CD2 LEU B 309      29.268  64.808  52.028  1.00 29.29           C  
ANISOU 2308  CD2 LEU B 309     3413   3441   4277   1019  -1041  -1237       C  
ATOM   2309  N   HIS B 310      25.958  64.361  48.422  1.00 30.54           N  
ANISOU 2309  N   HIS B 310     3650   3588   4366    785   -740  -1041       N  
ATOM   2310  CA  HIS B 310      25.152  64.627  47.231  1.00 35.73           C  
ANISOU 2310  CA  HIS B 310     4316   4249   5011    713   -659  -1010       C  
ATOM   2311  C   HIS B 310      26.027  64.886  46.012  1.00 34.04           C  
ANISOU 2311  C   HIS B 310     4037   4015   4880    647   -618  -1060       C  
ATOM   2312  O   HIS B 310      25.849  64.274  44.958  1.00 29.24           O  
ANISOU 2312  O   HIS B 310     3412   3412   4285    604   -558  -1050       O  
ATOM   2313  CB  HIS B 310      24.234  65.837  47.439  1.00 34.31           C  
ANISOU 2313  CB  HIS B 310     4177   4091   4768    711   -654   -988       C  
ATOM   2314  CG  HIS B 310      23.341  65.732  48.637  1.00 35.47           C  
ANISOU 2314  CG  HIS B 310     4381   4277   4819    781   -689   -942       C  
ATOM   2315  CD2 HIS B 310      21.993  65.698  48.742  1.00 38.46           C  
ANISOU 2315  CD2 HIS B 310     4808   4692   5111    787   -657   -873       C  
ATOM   2316  ND1 HIS B 310      23.826  65.675  49.926  1.00 43.84           N  
ANISOU 2316  ND1 HIS B 310     5445   5355   5858    862   -767   -965       N  
ATOM   2317  CE1 HIS B 310      22.817  65.600  50.774  1.00 44.54           C  
ANISOU 2317  CE1 HIS B 310     5583   5496   5845    916   -777   -907       C  
ATOM   2318  NE2 HIS B 310      21.693  65.608  50.081  1.00 46.68           N  
ANISOU 2318  NE2 HIS B 310     5881   5778   6079    870   -710   -850       N  
ATOM   2319  N   GLN B 311      26.980  65.794  46.184  1.00 28.61           N  
ANISOU 2319  N   GLN B 311     3307   3312   4251    643   -653  -1116       N  
ATOM   2320  CA  GLN B 311      27.829  66.247  45.092  1.00 29.87           C  
ANISOU 2320  CA  GLN B 311     3395   3463   4490    578   -613  -1151       C  
ATOM   2321  C   GLN B 311      28.698  65.124  44.548  1.00 32.34           C  
ANISOU 2321  C   GLN B 311     3654   3778   4858    575   -596  -1185       C  
ATOM   2322  O   GLN B 311      28.987  65.080  43.356  1.00 37.14           O  
ANISOU 2322  O   GLN B 311     4213   4404   5495    521   -533  -1194       O  
ATOM   2323  CB  GLN B 311      28.707  67.418  45.539  1.00 32.33           C  
ANISOU 2323  CB  GLN B 311     3665   3748   4871    577   -667  -1201       C  
ATOM   2324  CG  GLN B 311      29.579  67.141  46.755  1.00 36.78           C  
ANISOU 2324  CG  GLN B 311     4214   4296   5463    648   -759  -1259       C  
ATOM   2325  CD  GLN B 311      28.934  67.580  48.055  1.00 36.54           C  
ANISOU 2325  CD  GLN B 311     4247   4274   5364    718   -828  -1256       C  
ATOM   2326  NE2 GLN B 311      29.741  68.126  48.959  1.00 37.83           N  
ANISOU 2326  NE2 GLN B 311     4383   4421   5569    762   -914  -1324       N  
ATOM   2327  OE1 GLN B 311      27.727  67.436  48.244  1.00 35.70           O  
ANISOU 2327  OE1 GLN B 311     4207   4193   5163    735   -805  -1198       O  
ATOM   2328  N   ASP B 312      29.114  64.213  45.419  1.00 35.40           N  
ANISOU 2328  N   ASP B 312     4047   4150   5253    637   -654  -1205       N  
ATOM   2329  CA  ASP B 312      29.950  63.102  44.985  1.00 35.84           C  
ANISOU 2329  CA  ASP B 312     4051   4199   5367    644   -649  -1245       C  
ATOM   2330  C   ASP B 312      29.195  62.166  44.050  1.00 38.89           C  
ANISOU 2330  C   ASP B 312     4453   4596   5727    620   -587  -1216       C  
ATOM   2331  O   ASP B 312      29.712  61.780  43.004  1.00 43.31           O  
ANISOU 2331  O   ASP B 312     4956   5172   6329    590   -544  -1256       O  
ATOM   2332  CB  ASP B 312      30.479  62.322  46.184  1.00 38.61           C  
ANISOU 2332  CB  ASP B 312     4411   4528   5733    722   -732  -1262       C  
ATOM   2333  CG  ASP B 312      31.607  63.033  46.894  1.00 42.70           C  
ANISOU 2333  CG  ASP B 312     4884   5038   6303    749   -798  -1323       C  
ATOM   2334  OD1 ASP B 312      32.258  63.905  46.278  1.00 39.67           O  
ANISOU 2334  OD1 ASP B 312     4440   4655   5976    698   -777  -1362       O  
ATOM   2335  OD2 ASP B 312      31.847  62.703  48.071  1.00 40.41           O1-
ANISOU 2335  OD2 ASP B 312     4613   4741   5999    821   -875  -1328       O1-
ATOM   2336  N   TRP B 313      27.977  61.796  44.432  1.00 30.87           N  
ANISOU 2336  N   TRP B 313     3509   3578   4644    635   -585  -1151       N  
ATOM   2337  CA  TRP B 313      27.148  60.947  43.585  1.00 36.40           C  
ANISOU 2337  CA  TRP B 313     4224   4282   5325    610   -534  -1126       C  
ATOM   2338  C   TRP B 313      26.869  61.621  42.249  1.00 39.32           C  
ANISOU 2338  C   TRP B 313     4569   4694   5678    544   -456  -1133       C  
ATOM   2339  O   TRP B 313      26.985  61.001  41.193  1.00 41.40           O  
ANISOU 2339  O   TRP B 313     4794   4975   5961    522   -414  -1166       O  
ATOM   2340  CB  TRP B 313      25.819  60.603  44.265  1.00 34.93           C  
ANISOU 2340  CB  TRP B 313     4113   4089   5070    631   -543  -1044       C  
ATOM   2341  CG  TRP B 313      24.950  59.766  43.388  1.00 36.96           C  
ANISOU 2341  CG  TRP B 313     4379   4344   5321    602   -497  -1024       C  
ATOM   2342  CD1 TRP B 313      23.907  60.190  42.617  1.00 30.98           C  
ANISOU 2342  CD1 TRP B 313     3643   3619   4509    556   -439   -993       C  
ATOM   2343  CD2 TRP B 313      25.069  58.359  43.161  1.00 40.05           C  
ANISOU 2343  CD2 TRP B 313     4751   4694   5771    617   -511  -1040       C  
ATOM   2344  CE2 TRP B 313      24.058  57.994  42.249  1.00 36.57           C  
ANISOU 2344  CE2 TRP B 313     4321   4264   5311    579   -463  -1025       C  
ATOM   2345  CE3 TRP B 313      25.929  57.370  43.646  1.00 40.89           C  
ANISOU 2345  CE3 TRP B 313     4832   4754   5952    664   -566  -1069       C  
ATOM   2346  NE1 TRP B 313      23.361  59.131  41.932  1.00 34.20           N  
ANISOU 2346  NE1 TRP B 313     4046   4013   4936    543   -418   -995       N  
ATOM   2347  CZ2 TRP B 313      23.888  56.682  41.813  1.00 38.89           C  
ANISOU 2347  CZ2 TRP B 313     4598   4515   5663    584   -472  -1046       C  
ATOM   2348  CZ3 TRP B 313      25.755  56.071  43.213  1.00 48.02           C  
ANISOU 2348  CZ3 TRP B 313     5720   5610   6914    669   -574  -1082       C  
ATOM   2349  CH2 TRP B 313      24.745  55.738  42.305  1.00 43.84           C  
ANISOU 2349  CH2 TRP B 313     5200   5087   6372    629   -529  -1074       C  
ATOM   2350  N   LEU B 314      26.490  62.892  42.310  1.00 41.16           N  
ANISOU 2350  N   LEU B 314     4822   4945   5872    518   -441  -1102       N  
ATOM   2351  CA  LEU B 314      26.136  63.647  41.117  1.00 38.26           C  
ANISOU 2351  CA  LEU B 314     4436   4618   5481    457   -369  -1089       C  
ATOM   2352  C   LEU B 314      27.341  63.900  40.210  1.00 42.69           C  
ANISOU 2352  C   LEU B 314     4910   5207   6104    425   -337  -1140       C  
ATOM   2353  O   LEU B 314      27.185  64.046  38.999  1.00 35.14           O  
ANISOU 2353  O   LEU B 314     3921   4301   5129    383   -269  -1135       O  
ATOM   2354  CB  LEU B 314      25.484  64.973  41.513  1.00 29.85           C  
ANISOU 2354  CB  LEU B 314     3414   3554   4375    444   -373  -1041       C  
ATOM   2355  CG  LEU B 314      24.146  64.835  42.245  1.00 29.67           C  
ANISOU 2355  CG  LEU B 314     3472   3528   4274    473   -389   -985       C  
ATOM   2356  CD1 LEU B 314      23.682  66.177  42.789  1.00 22.33           C  
ANISOU 2356  CD1 LEU B 314     2577   2596   3312    475   -407   -958       C  
ATOM   2357  CD2 LEU B 314      23.084  64.227  41.334  1.00 31.46           C  
ANISOU 2357  CD2 LEU B 314     3718   3783   4452    445   -330   -951       C  
ATOM   2358  N   ASN B 315      28.535  63.943  40.793  1.00 41.06           N  
ANISOU 2358  N   ASN B 315     4658   4975   5967    447   -385  -1187       N  
ATOM   2359  CA  ASN B 315      29.744  64.186  40.010  1.00 37.34           C  
ANISOU 2359  CA  ASN B 315     4093   4535   5561    418   -355  -1232       C  
ATOM   2360  C   ASN B 315      30.378  62.901  39.485  1.00 42.48           C  
ANISOU 2360  C   ASN B 315     4692   5204   6242    442   -346  -1295       C  
ATOM   2361  O   ASN B 315      31.442  62.935  38.871  1.00 43.63           O  
ANISOU 2361  O   ASN B 315     4752   5386   6439    429   -322  -1340       O  
ATOM   2362  CB  ASN B 315      30.769  64.974  40.829  1.00 37.26           C  
ANISOU 2362  CB  ASN B 315     4047   4490   5622    425   -413  -1258       C  
ATOM   2363  CG  ASN B 315      30.379  66.431  40.998  1.00 43.08           C  
ANISOU 2363  CG  ASN B 315     4803   5210   6354    388   -414  -1212       C  
ATOM   2364  ND2 ASN B 315      30.758  67.016  42.130  1.00 46.01           N  
ANISOU 2364  ND2 ASN B 315     5183   5534   6763    417   -491  -1234       N  
ATOM   2365  OD1 ASN B 315      29.748  67.025  40.125  1.00 46.33           O  
ANISOU 2365  OD1 ASN B 315     5219   5652   6731    340   -350  -1161       O  
ATOM   2366  N   GLY B 316      29.726  61.769  39.736  1.00 42.11           N  
ANISOU 2366  N   GLY B 316     4695   5133   6171    480   -367  -1296       N  
ATOM   2367  CA  GLY B 316      30.092  60.521  39.088  1.00 43.19           C  
ANISOU 2367  CA  GLY B 316     4790   5283   6339    503   -357  -1358       C  
ATOM   2368  C   GLY B 316      31.081  59.627  39.812  1.00 44.99           C  
ANISOU 2368  C   GLY B 316     4988   5464   6641    560   -425  -1415       C  
ATOM   2369  O   GLY B 316      31.663  58.730  39.204  1.00 48.44           O  
ANISOU 2369  O   GLY B 316     5370   5915   7121    581   -419  -1484       O  
ATOM   2370  N   LYS B 317      31.273  59.854  41.108  1.00 41.40           N  
ANISOU 2370  N   LYS B 317     4569   4960   6201    592   -493  -1392       N  
ATOM   2371  CA  LYS B 317      32.222  59.052  41.873  1.00 42.50           C  
ANISOU 2371  CA  LYS B 317     4682   5058   6409    652   -564  -1439       C  
ATOM   2372  C   LYS B 317      31.742  57.617  42.023  1.00 45.92           C  
ANISOU 2372  C   LYS B 317     5147   5443   6856    694   -593  -1436       C  
ATOM   2373  O   LYS B 317      30.546  57.363  42.151  1.00 43.36           O  
ANISOU 2373  O   LYS B 317     4890   5100   6483    687   -584  -1373       O  
ATOM   2374  CB  LYS B 317      32.467  59.671  43.250  1.00 40.78           C  
ANISOU 2374  CB  LYS B 317     4495   4809   6189    684   -634  -1413       C  
ATOM   2375  CG  LYS B 317      33.075  61.056  43.191  1.00 41.58           C  
ANISOU 2375  CG  LYS B 317     4555   4938   6307    645   -624  -1428       C  
ATOM   2376  CD  LYS B 317      33.933  61.345  44.410  1.00 46.38           C  
ANISOU 2376  CD  LYS B 317     5149   5518   6955    693   -710  -1457       C  
ATOM   2377  CE  LYS B 317      34.657  62.674  44.257  1.00 56.34           C  
ANISOU 2377  CE  LYS B 317     6351   6794   8261    649   -706  -1483       C  
ATOM   2378  NZ  LYS B 317      35.559  62.956  45.407  1.00 58.14           N1+
ANISOU 2378  NZ  LYS B 317     6556   6997   8538    698   -798  -1529       N1+
ATOM   2379  N   GLU B 318      32.684  56.681  42.004  1.00 49.24           N  
ANISOU 2379  N   GLU B 318     5516   5843   7351    735   -629  -1500       N  
ATOM   2380  CA  GLU B 318      32.362  55.265  42.133  1.00 45.61           C  
ANISOU 2380  CA  GLU B 318     5081   5334   6916    762   -664  -1483       C  
ATOM   2381  C   GLU B 318      32.332  54.828  43.588  1.00 48.70           C  
ANISOU 2381  C   GLU B 318     5522   5664   7318    815   -745  -1423       C  
ATOM   2382  O   GLU B 318      33.203  55.190  44.379  1.00 53.11           O  
ANISOU 2382  O   GLU B 318     6063   6226   7889    843   -791  -1433       O  
ATOM   2383  CB  GLU B 318      33.370  54.408  41.364  1.00 43.77           C  
ANISOU 2383  CB  GLU B 318     4771   5120   6741    766   -666  -1562       C  
ATOM   2384  CG  GLU B 318      33.474  54.721  39.883  1.00 47.18           C  
ANISOU 2384  CG  GLU B 318     5141   5629   7154    727   -587  -1626       C  
ATOM   2385  CD  GLU B 318      34.476  53.828  39.168  1.00 53.67           C  
ANISOU 2385  CD  GLU B 318     5886   6480   8027    742   -595  -1709       C  
ATOM   2386  OE1 GLU B 318      35.104  52.975  39.839  1.00 47.70           O  
ANISOU 2386  OE1 GLU B 318     5126   5672   7326    779   -664  -1716       O  
ATOM   2387  OE2 GLU B 318      34.636  53.979  37.938  1.00 55.63           O1-
ANISOU 2387  OE2 GLU B 318     6077   6806   8254    721   -533  -1767       O1-
ATOM   2388  N   TYR B 319      31.327  54.034  43.933  1.00 46.67           N  
ANISOU 2388  N   TYR B 319     5322   5352   7059    832   -763  -1360       N  
ATOM   2389  CA  TYR B 319      31.218  53.500  45.281  1.00 40.11           C  
ANISOU 2389  CA  TYR B 319     4535   4467   6238    891   -835  -1290       C  
ATOM   2390  C   TYR B 319      31.344  51.991  45.266  1.00 39.30           C  
ANISOU 2390  C   TYR B 319     4422   4297   6212    912   -875  -1282       C  
ATOM   2391  O   TYR B 319      30.581  51.302  44.591  1.00 38.48           O  
ANISOU 2391  O   TYR B 319     4326   4160   6136    889   -853  -1276       O  
ATOM   2392  CB  TYR B 319      29.899  53.920  45.921  1.00 37.78           C  
ANISOU 2392  CB  TYR B 319     4317   4172   5866    889   -826  -1187       C  
ATOM   2393  CG  TYR B 319      29.814  55.405  46.140  1.00 40.47           C  
ANISOU 2393  CG  TYR B 319     4674   4581   6121    864   -799  -1180       C  
ATOM   2394  CD1 TYR B 319      29.406  56.253  45.120  1.00 42.09           C  
ANISOU 2394  CD1 TYR B 319     4873   4833   6288    798   -726  -1204       C  
ATOM   2395  CD2 TYR B 319      30.159  55.963  47.359  1.00 40.38           C  
ANISOU 2395  CD2 TYR B 319     4683   4588   6072    910   -852  -1153       C  
ATOM   2396  CE1 TYR B 319      29.335  57.613  45.312  1.00 46.49           C  
ANISOU 2396  CE1 TYR B 319     5443   5437   6784    775   -708  -1196       C  
ATOM   2397  CE2 TYR B 319      30.091  57.323  47.560  1.00 41.58           C  
ANISOU 2397  CE2 TYR B 319     4847   4792   6161    890   -838  -1159       C  
ATOM   2398  CZ  TYR B 319      29.676  58.141  46.535  1.00 46.91           C  
ANISOU 2398  CZ  TYR B 319     5514   5496   6812    820   -767  -1178       C  
ATOM   2399  OH  TYR B 319      29.604  59.493  46.731  1.00 48.54           O  
ANISOU 2399  OH  TYR B 319     5731   5740   6972    801   -759  -1182       O  
ATOM   2400  N   LYS B 320      32.317  51.480  46.010  1.00 41.89           N  
ANISOU 2400  N   LYS B 320     4731   4603   6581    957   -939  -1285       N  
ATOM   2401  CA  LYS B 320      32.536  50.046  46.047  1.00 41.85           C  
ANISOU 2401  CA  LYS B 320     4715   4527   6660    979   -984  -1278       C  
ATOM   2402  C   LYS B 320      32.238  49.447  47.411  1.00 42.97           C  
ANISOU 2402  C   LYS B 320     4905   4609   6812   1038  -1050  -1168       C  
ATOM   2403  O   LYS B 320      32.686  49.947  48.445  1.00 48.78           O  
ANISOU 2403  O   LYS B 320     5655   5375   7504   1081  -1087  -1136       O  
ATOM   2404  CB  LYS B 320      33.968  49.709  45.638  1.00 40.03           C  
ANISOU 2404  CB  LYS B 320     4413   4316   6480    984  -1003  -1375       C  
ATOM   2405  CG  LYS B 320      34.277  48.222  45.688  1.00 43.70           C  
ANISOU 2405  CG  LYS B 320     4863   4704   7037   1011  -1057  -1376       C  
ATOM   2406  CD  LYS B 320      35.720  47.951  45.332  1.00 46.81           C  
ANISOU 2406  CD  LYS B 320     5185   5125   7475   1023  -1079  -1476       C  
ATOM   2407  CE  LYS B 320      35.985  48.216  43.865  1.00 47.40           C  
ANISOU 2407  CE  LYS B 320     5197   5267   7544    978  -1018  -1579       C  
ATOM   2408  NZ  LYS B 320      37.365  47.804  43.492  1.00 49.54           N1+
ANISOU 2408  NZ  LYS B 320     5394   5565   7866    996  -1042  -1675       N1+
ATOM   2409  N   CYS B 321      31.462  48.371  47.401  1.00 42.07           N  
ANISOU 2409  N   CYS B 321     4812   4415   6757   1040  -1066  -1104       N  
ATOM   2410  CA  CYS B 321      31.285  47.554  48.586  1.00 40.86           C  
ANISOU 2410  CA  CYS B 321     4690   4199   6635   1094  -1129   -987       C  
ATOM   2411  C   CYS B 321      32.124  46.291  48.429  1.00 46.12           C  
ANISOU 2411  C   CYS B 321     5318   4798   7408   1107  -1177  -1024       C  
ATOM   2412  O   CYS B 321      32.117  45.653  47.372  1.00 46.61           O  
ANISOU 2412  O   CYS B 321     5346   4826   7538   1070  -1162  -1097       O  
ATOM   2413  CB  CYS B 321      29.812  47.208  48.797  1.00 40.03           C  
ANISOU 2413  CB  CYS B 321     4631   4042   6535   1086  -1120   -868       C  
ATOM   2414  SG  CYS B 321      29.487  46.278  50.308  1.00 47.95           S  
ANISOU 2414  SG  CYS B 321     5670   4986   7564   1149  -1190   -686       S  
ATOM   2415  N   LYS B 322      32.870  45.950  49.472  1.00 50.45           N  
ANISOU 2415  N   LYS B 322     5869   5336   7964   1164  -1236   -979       N  
ATOM   2416  CA  LYS B 322      33.674  44.736  49.481  1.00 46.35           C  
ANISOU 2416  CA  LYS B 322     5317   4748   7547   1186  -1290  -1002       C  
ATOM   2417  C   LYS B 322      33.247  43.874  50.660  1.00 46.68           C  
ANISOU 2417  C   LYS B 322     5396   4719   7621   1233  -1343   -844       C  
ATOM   2418  O   LYS B 322      33.285  44.311  51.812  1.00 50.19           O  
ANISOU 2418  O   LYS B 322     5871   5209   7990   1283  -1365   -755       O  
ATOM   2419  CB  LYS B 322      35.165  45.079  49.547  1.00 55.42           C  
ANISOU 2419  CB  LYS B 322     6421   5953   8684   1210  -1312  -1104       C  
ATOM   2420  CG  LYS B 322      36.108  43.884  49.567  1.00 59.48           C  
ANISOU 2420  CG  LYS B 322     6898   6404   9299   1239  -1371  -1139       C  
ATOM   2421  CD  LYS B 322      37.393  44.205  48.817  1.00 59.68           C  
ANISOU 2421  CD  LYS B 322     6856   6490   9331   1228  -1364  -1291       C  
ATOM   2422  CE  LYS B 322      38.612  43.634  49.515  1.00 61.50           C  
ANISOU 2422  CE  LYS B 322     7062   6702   9605   1285  -1432  -1306       C  
ATOM   2423  NZ  LYS B 322      38.978  44.436  50.712  1.00 60.56           N1+
ANISOU 2423  NZ  LYS B 322     6969   6638   9405   1328  -1456  -1255       N1+
ATOM   2424  N   VAL B 323      32.820  42.651  50.363  1.00 51.21           N  
ANISOU 2424  N   VAL B 323     5963   5189   8307   1218  -1364   -806       N  
ATOM   2425  CA  VAL B 323      32.267  41.762  51.379  1.00 55.20           C  
ANISOU 2425  CA  VAL B 323     6499   5618   8857   1250  -1407   -636       C  
ATOM   2426  C   VAL B 323      33.196  40.581  51.644  1.00 57.67           C  
ANISOU 2426  C   VAL B 323     6782   5856   9274   1285  -1472   -641       C  
ATOM   2427  O   VAL B 323      33.618  39.889  50.715  1.00 53.00           O  
ANISOU 2427  O   VAL B 323     6148   5209   8780   1259  -1486   -752       O  
ATOM   2428  CB  VAL B 323      30.879  41.255  50.959  1.00 48.45           C  
ANISOU 2428  CB  VAL B 323     5660   4688   8062   1200  -1385   -558       C  
ATOM   2429  CG1 VAL B 323      30.387  40.194  51.917  1.00 42.69           C  
ANISOU 2429  CG1 VAL B 323     4948   3872   7401   1224  -1429   -376       C  
ATOM   2430  CG2 VAL B 323      29.898  42.417  50.893  1.00 47.68           C  
ANISOU 2430  CG2 VAL B 323     5597   4666   7854   1176  -1326   -528       C  
ATOM   2431  N   SER B 324      33.511  40.351  52.916  1.00 66.91           N  
ANISOU 2431  N   SER B 324     7973   7032  10418   1349  -1515   -520       N  
ATOM   2432  CA  SER B 324      34.523  39.361  53.276  1.00 69.93           C  
ANISOU 2432  CA  SER B 324     8329   7357  10886   1393  -1578   -526       C  
ATOM   2433  C   SER B 324      34.076  38.386  54.361  1.00 67.57           C  
ANISOU 2433  C   SER B 324     8054   6987  10633   1431  -1619   -327       C  
ATOM   2434  O   SER B 324      33.277  38.720  55.236  1.00 69.91           O  
ANISOU 2434  O   SER B 324     8389   7327  10848   1451  -1603   -171       O  
ATOM   2435  CB  SER B 324      35.801  40.071  53.728  1.00 78.04           C  
ANISOU 2435  CB  SER B 324     9341   8479  11833   1443  -1597   -606       C  
ATOM   2436  OG  SER B 324      36.182  41.081  52.809  1.00 86.45           O  
ANISOU 2436  OG  SER B 324    10381   9618  12846   1404  -1553   -768       O  
ATOM   2437  N   ASN B 325      34.605  37.170  54.281  1.00 72.83           N  
ANISOU 2437  N   ASN B 325     8692   7551  11429   1443  -1673   -334       N  
ATOM   2438  CA  ASN B 325      34.433  36.167  55.325  1.00 79.19           C  
ANISOU 2438  CA  ASN B 325     9511   8288  12290   1486  -1718   -150       C  
ATOM   2439  C   ASN B 325      35.708  35.363  55.490  1.00 77.19           C  
ANISOU 2439  C   ASN B 325     9224   7987  12117   1536  -1783   -208       C  
ATOM   2440  O   ASN B 325      36.507  35.255  54.557  1.00 81.79           O  
ANISOU 2440  O   ASN B 325     9767   8553  12758   1518  -1797   -390       O  
ATOM   2441  CB  ASN B 325      33.259  35.235  55.010  1.00 82.61           C  
ANISOU 2441  CB  ASN B 325     9947   8600  12842   1429  -1716    -50       C  
ATOM   2442  CG  ASN B 325      32.030  35.546  55.844  1.00 90.96           C  
ANISOU 2442  CG  ASN B 325    11047   9696  13818   1426  -1680    156       C  
ATOM   2443  ND2 ASN B 325      31.049  34.651  55.815  1.00 94.08           N  
ANISOU 2443  ND2 ASN B 325    11440   9985  14320   1381  -1684    279       N  
ATOM   2444  OD1 ASN B 325      31.965  36.580  56.507  1.00 97.44           O  
ANISOU 2444  OD1 ASN B 325    11896  10644  14483   1464  -1650    201       O  
ATOM   2445  N   LYS B 326      35.906  34.805  56.680  1.00 72.21           N  
ANISOU 2445  N   LYS B 326     8608   7345  11484   1601  -1823    -50       N  
ATOM   2446  CA  LYS B 326      37.004  33.875  56.908  1.00 69.67           C  
ANISOU 2446  CA  LYS B 326     8256   6960  11256   1651  -1891    -78       C  
ATOM   2447  C   LYS B 326      36.838  32.660  56.003  1.00 76.00           C  
ANISOU 2447  C   LYS B 326     9025   7607  12245   1601  -1925   -133       C  
ATOM   2448  O   LYS B 326      37.810  31.979  55.674  1.00 77.02           O  
ANISOU 2448  O   LYS B 326     9116   7680  12469   1622  -1978   -238       O  
ATOM   2449  CB  LYS B 326      37.047  33.445  58.374  1.00 67.42           C  
ANISOU 2449  CB  LYS B 326     7994   6691  10931   1729  -1923    131       C  
ATOM   2450  CG  LYS B 326      37.567  34.515  59.319  1.00 69.34           C  
ANISOU 2450  CG  LYS B 326     8254   7095  10996   1799  -1914    152       C  
ATOM   2451  CD  LYS B 326      36.827  34.496  60.650  1.00 68.08           C  
ANISOU 2451  CD  LYS B 326     8131   6998  10737   1853  -1904    396       C  
ATOM   2452  CE  LYS B 326      36.648  33.082  61.180  1.00 70.84           C  
ANISOU 2452  CE  LYS B 326     8479   7234  11203   1878  -1946    565       C  
ATOM   2453  NZ  LYS B 326      36.262  33.080  62.620  1.00 73.43           N1+
ANISOU 2453  NZ  LYS B 326     8834   7658  11407   1956  -1943    797       N1+
ATOM   2454  N   ALA B 327      35.594  32.404  55.598  1.00 77.70           N  
ANISOU 2454  N   ALA B 327     9251   7758  12513   1534  -1896    -67       N  
ATOM   2455  CA  ALA B 327      35.279  31.297  54.703  1.00 80.11           C  
ANISOU 2455  CA  ALA B 327     9521   7919  12997   1479  -1930   -123       C  
ATOM   2456  C   ALA B 327      34.547  31.763  53.440  1.00 81.87           C  
ANISOU 2456  C   ALA B 327     9732   8151  13224   1399  -1882   -251       C  
ATOM   2457  O   ALA B 327      33.492  31.232  53.086  1.00 83.20           O  
ANISOU 2457  O   ALA B 327     9897   8233  13481   1340  -1878   -193       O  
ATOM   2458  CB  ALA B 327      34.457  30.251  55.433  1.00 83.26           C  
ANISOU 2458  CB  ALA B 327     9932   8208  13497   1472  -1958     92       C  
ATOM   2459  N   LEU B 328      35.099  32.778  52.787  1.00 82.09           N  
ANISOU 2459  N   LEU B 328     9751   8288  13152   1396  -1844   -417       N  
ATOM   2460  CA  LEU B 328      34.794  33.079  51.396  1.00 78.51           C  
ANISOU 2460  CA  LEU B 328     9269   7848  12713   1333  -1810   -585       C  
ATOM   2461  C   LEU B 328      36.081  32.785  50.639  1.00 81.68           C  
ANISOU 2461  C   LEU B 328     9615   8260  13160   1355  -1847   -780       C  
ATOM   2462  O   LEU B 328      37.153  33.184  51.093  1.00 77.65           O  
ANISOU 2462  O   LEU B 328     9101   7818  12585   1407  -1857   -817       O  
ATOM   2463  CB  LEU B 328      34.363  34.538  51.214  1.00 74.32           C  
ANISOU 2463  CB  LEU B 328     8768   7447  12022   1310  -1730   -610       C  
ATOM   2464  CG  LEU B 328      32.905  34.885  50.895  1.00 71.42           C  
ANISOU 2464  CG  LEU B 328     8427   7074  11636   1248  -1678   -543       C  
ATOM   2465  CD1 LEU B 328      32.717  36.396  50.885  1.00 67.80           C  
ANISOU 2465  CD1 LEU B 328     7999   6753  11010   1243  -1607   -568       C  
ATOM   2466  CD2 LEU B 328      32.463  34.290  49.567  1.00 75.25           C  
ANISOU 2466  CD2 LEU B 328     8869   7493  12228   1188  -1682   -665       C  
ATOM   2467  N   PRO B 329      35.997  32.072  49.503  1.00 85.22           N  
ANISOU 2467  N   PRO B 329    10014   8647  13718   1319  -1871   -907       N  
ATOM   2468  CA  PRO B 329      37.239  31.779  48.774  1.00 81.81           C  
ANISOU 2468  CA  PRO B 329     9523   8238  13322   1346  -1906  -1092       C  
ATOM   2469  C   PRO B 329      37.961  33.067  48.389  1.00 79.39           C  
ANISOU 2469  C   PRO B 329     9208   8089  12867   1352  -1847  -1210       C  
ATOM   2470  O   PRO B 329      39.171  33.192  48.590  1.00 79.39           O  
ANISOU 2470  O   PRO B 329     9184   8138  12844   1398  -1870  -1278       O  
ATOM   2471  CB  PRO B 329      36.757  31.015  47.536  1.00 84.39           C  
ANISOU 2471  CB  PRO B 329     9800   8503  13762   1302  -1928  -1205       C  
ATOM   2472  CG  PRO B 329      35.315  31.365  47.391  1.00 89.44           C  
ANISOU 2472  CG  PRO B 329    10473   9132  14378   1242  -1877  -1119       C  
ATOM   2473  CD  PRO B 329      34.802  31.593  48.785  1.00 89.18           C  
ANISOU 2473  CD  PRO B 329    10506   9074  14304   1255  -1865   -900       C  
ATOM   2474  N   ALA B 330      37.204  34.017  47.856  1.00 77.80           N  
ANISOU 2474  N   ALA B 330     9024   7966  12573   1303  -1774  -1229       N  
ATOM   2475  CA  ALA B 330      37.687  35.370  47.632  1.00 73.06           C  
ANISOU 2475  CA  ALA B 330     8422   7511  11827   1300  -1710  -1303       C  
ATOM   2476  C   ALA B 330      36.607  36.337  48.091  1.00 73.62           C  
ANISOU 2476  C   ALA B 330     8553   7622  11796   1272  -1648  -1186       C  
ATOM   2477  O   ALA B 330      35.421  36.007  48.054  1.00 75.21           O  
ANISOU 2477  O   ALA B 330     8781   7758  12038   1237  -1639  -1101       O  
ATOM   2478  CB  ALA B 330      38.029  35.593  46.166  1.00 65.62           C  
ANISOU 2478  CB  ALA B 330     7418   6643  10871   1271  -1680  -1488       C  
ATOM   2479  N   PRO B 331      37.006  37.533  48.542  1.00 74.10           N  
ANISOU 2479  N   PRO B 331     8634   7790  11729   1286  -1610  -1182       N  
ATOM   2480  CA  PRO B 331      35.975  38.507  48.909  1.00 75.47           C  
ANISOU 2480  CA  PRO B 331     8861   8011  11803   1262  -1553  -1086       C  
ATOM   2481  C   PRO B 331      35.280  39.067  47.668  1.00 72.16           C  
ANISOU 2481  C   PRO B 331     8428   7639  11349   1199  -1487  -1174       C  
ATOM   2482  O   PRO B 331      35.912  39.190  46.618  1.00 71.43           O  
ANISOU 2482  O   PRO B 331     8282   7601  11256   1183  -1470  -1323       O  
ATOM   2483  CB  PRO B 331      36.766  39.589  49.649  1.00 77.75           C  
ANISOU 2483  CB  PRO B 331     9161   8403  11976   1299  -1542  -1087       C  
ATOM   2484  CG  PRO B 331      38.138  39.502  49.073  1.00 74.02           C  
ANISOU 2484  CG  PRO B 331     8626   7969  11528   1313  -1561  -1239       C  
ATOM   2485  CD  PRO B 331      38.367  38.045  48.777  1.00 75.84           C  
ANISOU 2485  CD  PRO B 331     8826   8092  11898   1326  -1621  -1262       C  
ATOM   2486  N   ILE B 332      33.998  39.388  47.792  1.00 64.98           N  
ANISOU 2486  N   ILE B 332     7563   6716  10408   1167  -1450  -1078       N  
ATOM   2487  CA  ILE B 332      33.207  39.868  46.663  1.00 60.95           C  
ANISOU 2487  CA  ILE B 332     7046   6246   9868   1109  -1390  -1147       C  
ATOM   2488  C   ILE B 332      33.178  41.396  46.612  1.00 56.60           C  
ANISOU 2488  C   ILE B 332     6513   5818   9175   1096  -1321  -1169       C  
ATOM   2489  O   ILE B 332      33.000  42.055  47.633  1.00 56.62           O  
ANISOU 2489  O   ILE B 332     6561   5848   9106   1121  -1317  -1069       O  
ATOM   2490  CB  ILE B 332      31.764  39.328  46.729  1.00 59.01           C  
ANISOU 2490  CB  ILE B 332     6831   5910   9679   1075  -1389  -1037       C  
ATOM   2491  CG1 ILE B 332      31.783  37.799  46.792  1.00 53.98           C  
ANISOU 2491  CG1 ILE B 332     6170   5142   9199   1082  -1462  -1011       C  
ATOM   2492  CG2 ILE B 332      30.943  39.799  45.533  1.00 54.72           C  
ANISOU 2492  CG2 ILE B 332     6278   5411   9103   1018  -1329  -1116       C  
ATOM   2493  CD1 ILE B 332      30.425  37.180  47.011  1.00 49.72           C  
ANISOU 2493  CD1 ILE B 332     5655   4501   8735   1047  -1471   -883       C  
ATOM   2494  N   GLU B 333      33.361  41.951  45.417  1.00 46.79           N  
ANISOU 2494  N   GLU B 333     5232   4656   7891   1060  -1270  -1296       N  
ATOM   2495  CA  GLU B 333      33.353  43.395  45.229  1.00 43.19           C  
ANISOU 2495  CA  GLU B 333     4785   4312   7313   1041  -1203  -1322       C  
ATOM   2496  C   GLU B 333      32.244  43.845  44.265  1.00 46.67           C  
ANISOU 2496  C   GLU B 333     5234   4783   7714    986  -1138  -1342       C  
ATOM   2497  O   GLU B 333      32.015  43.217  43.229  1.00 49.39           O  
ANISOU 2497  O   GLU B 333     5543   5114   8108    962  -1133  -1414       O  
ATOM   2498  CB  GLU B 333      34.716  43.869  44.718  1.00 38.03           C  
ANISOU 2498  CB  GLU B 333     4071   3748   6631   1048  -1192  -1445       C  
ATOM   2499  CG  GLU B 333      35.888  43.454  45.599  1.00 40.88           C  
ANISOU 2499  CG  GLU B 333     4418   4085   7030   1101  -1258  -1442       C  
ATOM   2500  CD  GLU B 333      37.193  44.060  45.130  1.00 48.55           C  
ANISOU 2500  CD  GLU B 333     5326   5149   7970   1104  -1243  -1558       C  
ATOM   2501  OE1 GLU B 333      38.084  43.309  44.690  1.00 55.89           O  
ANISOU 2501  OE1 GLU B 333     6200   6070   8965   1122  -1276  -1642       O  
ATOM   2502  OE2 GLU B 333      37.332  45.296  45.204  1.00 49.89           O1-
ANISOU 2502  OE2 GLU B 333     5498   5401   8057   1088  -1200  -1564       O1-
ATOM   2503  N   LYS B 334      31.558  44.930  44.620  1.00 43.04           N  
ANISOU 2503  N   LYS B 334     4821   4370   7163    973  -1092  -1280       N  
ATOM   2504  CA  LYS B 334      30.536  45.527  43.764  1.00 41.80           C  
ANISOU 2504  CA  LYS B 334     4676   4253   6954    924  -1026  -1296       C  
ATOM   2505  C   LYS B 334      30.761  47.031  43.637  1.00 42.92           C  
ANISOU 2505  C   LYS B 334     4821   4505   6981    909   -966  -1323       C  
ATOM   2506  O   LYS B 334      31.037  47.709  44.626  1.00 48.24           O  
ANISOU 2506  O   LYS B 334     5523   5199   7609    937   -979  -1270       O  
ATOM   2507  CB  LYS B 334      29.135  45.253  44.317  1.00 45.39           C  
ANISOU 2507  CB  LYS B 334     5188   4631   7428    917  -1033  -1174       C  
ATOM   2508  CG  LYS B 334      28.748  43.783  44.339  1.00 48.46           C  
ANISOU 2508  CG  LYS B 334     5568   4901   7945    917  -1089  -1138       C  
ATOM   2509  CD  LYS B 334      28.630  43.231  42.928  1.00 56.76           C  
ANISOU 2509  CD  LYS B 334     6568   5956   9042    880  -1076  -1257       C  
ATOM   2510  CE  LYS B 334      28.427  41.721  42.928  1.00 64.62           C  
ANISOU 2510  CE  LYS B 334     7543   6829  10182    883  -1145  -1241       C  
ATOM   2511  NZ  LYS B 334      28.473  41.151  41.548  1.00 70.98           N1+
ANISOU 2511  NZ  LYS B 334     8288   7652  11030    861  -1145  -1377       N1+
ATOM   2512  N   THR B 335      30.643  47.552  42.421  1.00 38.05           N  
ANISOU 2512  N   THR B 335     4173   3962   6320    867   -902  -1404       N  
ATOM   2513  CA  THR B 335      30.860  48.973  42.176  1.00 40.32           C  
ANISOU 2513  CA  THR B 335     4457   4349   6512    845   -842  -1428       C  
ATOM   2514  C   THR B 335      29.680  49.597  41.440  1.00 44.67           C  
ANISOU 2514  C   THR B 335     5035   4938   7002    800   -775  -1419       C  
ATOM   2515  O   THR B 335      29.192  49.035  40.461  1.00 47.22           O  
ANISOU 2515  O   THR B 335     5336   5260   7343    777   -756  -1462       O  
ATOM   2516  CB  THR B 335      32.138  49.209  41.352  1.00 40.37           C  
ANISOU 2516  CB  THR B 335     4385   4435   6517    840   -821  -1536       C  
ATOM   2517  CG2 THR B 335      32.259  50.671  40.946  1.00 44.63           C  
ANISOU 2517  CG2 THR B 335     4913   5070   6973    808   -752  -1555       C  
ATOM   2518  OG1 THR B 335      33.283  48.832  42.125  1.00 45.08           O  
ANISOU 2518  OG1 THR B 335     4959   5007   7161    882   -882  -1546       O  
ATOM   2519  N   ILE B 336      29.218  50.753  41.914  1.00 43.83           N  
ANISOU 2519  N   ILE B 336     4970   4864   6818    792   -744  -1367       N  
ATOM   2520  CA  ILE B 336      28.184  51.509  41.207  1.00 47.86           C  
ANISOU 2520  CA  ILE B 336     5503   5420   7260    749   -677  -1363       C  
ATOM   2521  C   ILE B 336      28.505  52.999  41.127  1.00 43.84           C  
ANISOU 2521  C   ILE B 336     4992   4994   6673    730   -628  -1375       C  
ATOM   2522  O   ILE B 336      29.337  53.512  41.873  1.00 41.31           O  
ANISOU 2522  O   ILE B 336     4664   4683   6351    754   -654  -1370       O  
ATOM   2523  CB  ILE B 336      26.799  51.362  41.866  1.00 45.06           C  
ANISOU 2523  CB  ILE B 336     5220   5009   6892    747   -687  -1260       C  
ATOM   2524  CG1 ILE B 336      26.838  51.848  43.313  1.00 39.26           C  
ANISOU 2524  CG1 ILE B 336     4533   4272   6112    774   -720  -1156       C  
ATOM   2525  CG2 ILE B 336      26.308  49.925  41.798  1.00 22.35           C  
ANISOU 2525  CG2 ILE B 336     2340   2033   4118    761   -732  -1251       C  
ATOM   2526  CD1 ILE B 336      25.476  51.891  43.954  1.00 39.93           C  
ANISOU 2526  CD1 ILE B 336     4682   4348   6140    755   -712  -1028       C  
ATOM   2527  N   SER B 337      27.826  53.682  40.211  1.00 43.12           N  
ANISOU 2527  N   SER B 337     4903   4963   6516    684   -560  -1385       N  
ATOM   2528  CA  SER B 337      27.954  55.123  40.042  1.00 43.78           C  
ANISOU 2528  CA  SER B 337     4988   5127   6521    646   -508  -1369       C  
ATOM   2529  C   SER B 337      26.776  55.618  39.212  1.00 46.31           C  
ANISOU 2529  C   SER B 337     5335   5496   6764    595   -443  -1338       C  
ATOM   2530  O   SER B 337      26.081  54.818  38.589  1.00 44.64           O  
ANISOU 2530  O   SER B 337     5124   5270   6566    589   -436  -1357       O  
ATOM   2531  CB  SER B 337      29.288  55.489  39.381  1.00 45.06           C  
ANISOU 2531  CB  SER B 337     5067   5344   6711    648   -486  -1460       C  
ATOM   2532  OG  SER B 337      29.423  54.894  38.107  1.00 53.60           O  
ANISOU 2532  OG  SER B 337     6092   6468   7805    641   -451  -1538       O  
ATOM   2533  N   LYS B 338      26.546  56.928  39.213  1.00 46.76           N  
ANISOU 2533  N   LYS B 338     5411   5607   6747    559   -403  -1292       N  
ATOM   2534  CA  LYS B 338      25.450  57.508  38.445  1.00 48.18           C  
ANISOU 2534  CA  LYS B 338     5617   5839   6850    512   -343  -1257       C  
ATOM   2535  C   LYS B 338      25.623  57.251  36.952  1.00 45.95           C  
ANISOU 2535  C   LYS B 338     5273   5622   6563    496   -291  -1335       C  
ATOM   2536  O   LYS B 338      26.748  57.200  36.451  1.00 45.88           O  
ANISOU 2536  O   LYS B 338     5195   5648   6589    507   -281  -1407       O  
ATOM   2537  CB  LYS B 338      25.347  59.015  38.704  1.00 49.92           C  
ANISOU 2537  CB  LYS B 338     5860   6098   7008    482   -315  -1201       C  
ATOM   2538  CG  LYS B 338      24.046  59.638  38.225  1.00 50.16           C  
ANISOU 2538  CG  LYS B 338     5934   6167   6957    443   -267  -1142       C  
ATOM   2539  CD  LYS B 338      24.150  61.149  38.162  1.00 44.31           C  
ANISOU 2539  CD  LYS B 338     5195   5466   6173    411   -236  -1106       C  
ATOM   2540  CE  LYS B 338      25.009  61.585  36.988  1.00 39.78           C  
ANISOU 2540  CE  LYS B 338     4546   4959   5611    383   -183  -1152       C  
ATOM   2541  NZ  LYS B 338      25.284  63.049  37.021  1.00 44.69           N1+
ANISOU 2541  NZ  LYS B 338     5160   5601   6220    350   -162  -1110       N1+
ATOM   2542  N   ALA B 339      24.503  57.081  36.253  1.00 47.15           N  
ANISOU 2542  N   ALA B 339     5448   5799   6670    473   -260  -1323       N  
ATOM   2543  CA  ALA B 339      24.518  56.864  34.813  1.00 43.18           C  
ANISOU 2543  CA  ALA B 339     4889   5375   6142    464   -212  -1398       C  
ATOM   2544  C   ALA B 339      25.252  57.998  34.114  1.00 44.18           C  
ANISOU 2544  C   ALA B 339     4966   5599   6221    439   -150  -1402       C  
ATOM   2545  O   ALA B 339      25.017  59.167  34.412  1.00 48.56           O  
ANISOU 2545  O   ALA B 339     5552   6169   6730    407   -126  -1323       O  
ATOM   2546  CB  ALA B 339      23.097  56.739  34.278  1.00 29.64           C  
ANISOU 2546  CB  ALA B 339     3212   3678   4373    441   -190  -1371       C  
ATOM   2547  N   LYS B 340      26.148  57.652  33.195  1.00 43.07           N  
ANISOU 2547  N   LYS B 340     4744   5525   6096    457   -126  -1491       N  
ATOM   2548  CA  LYS B 340      26.878  58.654  32.432  1.00 43.90           C  
ANISOU 2548  CA  LYS B 340     4787   5735   6159    432    -60  -1486       C  
ATOM   2549  C   LYS B 340      26.037  59.156  31.260  1.00 47.02           C  
ANISOU 2549  C   LYS B 340     5179   6233   6455    403      9  -1462       C  
ATOM   2550  O   LYS B 340      25.147  58.455  30.781  1.00 43.42           O  
ANISOU 2550  O   LYS B 340     4742   5786   5971    416      4  -1496       O  
ATOM   2551  CB  LYS B 340      28.203  58.079  31.930  1.00 44.91           C  
ANISOU 2551  CB  LYS B 340     4819   5909   6335    468    -57  -1588       C  
ATOM   2552  CG  LYS B 340      29.008  57.328  32.985  1.00 49.82           C  
ANISOU 2552  CG  LYS B 340     5439   6430   7060    509   -133  -1629       C  
ATOM   2553  CD  LYS B 340      30.347  56.856  32.431  1.00 45.61           C  
ANISOU 2553  CD  LYS B 340     4802   5954   6572    546   -126  -1732       C  
ATOM   2554  CE  LYS B 340      30.934  55.739  33.278  1.00 42.16           C  
ANISOU 2554  CE  LYS B 340     4371   5416   6233    592   -213  -1778       C  
ATOM   2555  NZ  LYS B 340      31.154  56.159  34.688  1.00 47.38           N1+
ANISOU 2555  NZ  LYS B 340     5078   5982   6944    596   -263  -1721       N1+
ATOM   2556  N   GLY B 341      26.315  60.371  30.801  1.00 49.07           N  
ANISOU 2556  N   GLY B 341     5409   6569   6665    365     69  -1400       N  
ATOM   2557  CA  GLY B 341      25.582  60.928  29.681  1.00 46.38           C  
ANISOU 2557  CA  GLY B 341     5062   6336   6226    340    136  -1364       C  
ATOM   2558  C   GLY B 341      25.132  62.354  29.924  1.00 43.97           C  
ANISOU 2558  C   GLY B 341     4797   6025   5884    289    164  -1241       C  
ATOM   2559  O   GLY B 341      24.934  62.765  31.065  1.00 44.81           O  
ANISOU 2559  O   GLY B 341     4965   6031   6032    277    120  -1190       O  
ATOM   2560  N   GLN B 342      24.970  63.105  28.841  1.00 42.95           N  
ANISOU 2560  N   GLN B 342     4632   6009   5679    264    235  -1195       N  
ATOM   2561  CA  GLN B 342      24.557  64.495  28.932  1.00 45.08           C  
ANISOU 2561  CA  GLN B 342     4932   6275   5922    216    263  -1076       C  
ATOM   2562  C   GLN B 342      23.167  64.621  29.555  1.00 43.48           C  
ANISOU 2562  C   GLN B 342     4830   5998   5691    211    229  -1030       C  
ATOM   2563  O   GLN B 342      22.200  64.055  29.042  1.00 45.82           O  
ANISOU 2563  O   GLN B 342     5151   6331   5927    226    235  -1053       O  
ATOM   2564  CB  GLN B 342      24.581  65.145  27.549  1.00 48.35           C  
ANISOU 2564  CB  GLN B 342     5283   6834   6253    196    348  -1028       C  
ATOM   2565  CG  GLN B 342      24.120  66.587  27.535  1.00 55.71           C  
ANISOU 2565  CG  GLN B 342     6243   7760   7165    146    376   -897       C  
ATOM   2566  CD  GLN B 342      24.947  67.466  28.451  1.00 64.95           C  
ANISOU 2566  CD  GLN B 342     7405   8835   8437    113    349   -847       C  
ATOM   2567  NE2 GLN B 342      26.253  67.213  28.505  1.00 66.09           N  
ANISOU 2567  NE2 GLN B 342     7473   8991   8647    117    351   -893       N  
ATOM   2568  OE1 GLN B 342      24.417  68.362  29.107  1.00 70.21           O  
ANISOU 2568  OE1 GLN B 342     8131   9420   9126     88    323   -775       O  
ATOM   2569  N   PRO B 343      23.073  65.351  30.682  1.00 39.64           N  
ANISOU 2569  N   PRO B 343     4398   5413   5252    194    189   -971       N  
ATOM   2570  CA  PRO B 343      21.797  65.586  31.362  1.00 35.45           C  
ANISOU 2570  CA  PRO B 343     3957   4820   4692    193    158   -923       C  
ATOM   2571  C   PRO B 343      20.817  66.318  30.468  1.00 33.49           C  
ANISOU 2571  C   PRO B 343     3724   4644   4358    170    209   -856       C  
ATOM   2572  O   PRO B 343      21.215  67.229  29.746  1.00 36.73           O  
ANISOU 2572  O   PRO B 343     4089   5115   4752    141    258   -802       O  
ATOM   2573  CB  PRO B 343      22.190  66.454  32.561  1.00 31.75           C  
ANISOU 2573  CB  PRO B 343     3518   4259   4287    184    114   -881       C  
ATOM   2574  CG  PRO B 343      23.616  66.132  32.800  1.00 36.49           C  
ANISOU 2574  CG  PRO B 343     4055   4843   4965    193     97   -936       C  
ATOM   2575  CD  PRO B 343      24.199  65.929  31.431  1.00 33.88           C  
ANISOU 2575  CD  PRO B 343     3641   4625   4608    182    164   -961       C  
ATOM   2576  N   ARG B 344      19.550  65.919  30.512  1.00 33.17           N  
ANISOU 2576  N   ARG B 344     3740   4597   4265    182    196   -852       N  
ATOM   2577  CA  ARG B 344      18.523  66.595  29.736  1.00 39.43           C  
ANISOU 2577  CA  ARG B 344     4552   5456   4974    165    236   -790       C  
ATOM   2578  C   ARG B 344      17.366  67.027  30.624  1.00 39.54           C  
ANISOU 2578  C   ARG B 344     4648   5400   4975    166    201   -736       C  
ATOM   2579  O   ARG B 344      16.860  66.249  31.430  1.00 37.80           O  
ANISOU 2579  O   ARG B 344     4469   5120   4772    187    157   -766       O  
ATOM   2580  CB  ARG B 344      18.032  65.697  28.602  1.00 41.57           C  
ANISOU 2580  CB  ARG B 344     4794   5823   5177    183    264   -848       C  
ATOM   2581  CG  ARG B 344      19.087  65.440  27.541  1.00 48.48           C  
ANISOU 2581  CG  ARG B 344     5580   6801   6039    190    310   -897       C  
ATOM   2582  CD  ARG B 344      18.487  65.484  26.151  1.00 58.97           C  
ANISOU 2582  CD  ARG B 344     6877   8269   7260    197    363   -895       C  
ATOM   2583  NE  ARG B 344      18.563  64.188  25.485  1.00 66.92           N  
ANISOU 2583  NE  ARG B 344     7842   9338   8248    237    356  -1017       N  
ATOM   2584  CZ  ARG B 344      17.674  63.752  24.602  1.00 63.30           C  
ANISOU 2584  CZ  ARG B 344     7378   8963   7709    258    366  -1057       C  
ATOM   2585  NH1 ARG B 344      17.824  62.558  24.044  1.00 51.14           N1+
ANISOU 2585  NH1 ARG B 344     5795   7469   6168    299    349  -1183       N1+
ATOM   2586  NH2 ARG B 344      16.634  64.510  24.280  1.00 54.55           N  
ANISOU 2586  NH2 ARG B 344     6307   7892   6528    242    387   -977       N  
ATOM   2587  N   GLU B 345      16.958  68.280  30.473  1.00 40.85           N  
ANISOU 2587  N   GLU B 345     4833   5576   5114    145    221   -653       N  
ATOM   2588  CA  GLU B 345      15.913  68.861  31.302  1.00 37.62           C  
ANISOU 2588  CA  GLU B 345     4495   5108   4691    151    189   -603       C  
ATOM   2589  C   GLU B 345      14.529  68.337  30.937  1.00 38.45           C  
ANISOU 2589  C   GLU B 345     4634   5254   4721    162    195   -604       C  
ATOM   2590  O   GLU B 345      14.123  68.401  29.778  1.00 36.85           O  
ANISOU 2590  O   GLU B 345     4407   5140   4454    155    239   -593       O  
ATOM   2591  CB  GLU B 345      15.946  70.383  31.188  1.00 40.95           C  
ANISOU 2591  CB  GLU B 345     4920   5520   5120    127    203   -520       C  
ATOM   2592  CG  GLU B 345      14.961  71.105  32.083  1.00 53.06           C  
ANISOU 2592  CG  GLU B 345     6522   6992   6645    142    164   -478       C  
ATOM   2593  CD  GLU B 345      14.954  72.599  31.831  1.00 57.04           C  
ANISOU 2593  CD  GLU B 345     7024   7481   7167    120    173   -399       C  
ATOM   2594  OE1 GLU B 345      15.396  73.019  30.742  1.00 41.22           O  
ANISOU 2594  OE1 GLU B 345     4969   5536   5156     90    224   -356       O  
ATOM   2595  OE2 GLU B 345      14.511  73.355  32.723  1.00 70.96           O1-
ANISOU 2595  OE2 GLU B 345     8833   9175   8953    136    129   -379       O1-
ATOM   2596  N   PRO B 346      13.797  67.818  31.933  1.00 35.22           N  
ANISOU 2596  N   PRO B 346     4276   4788   4320    183    152   -614       N  
ATOM   2597  CA  PRO B 346      12.433  67.332  31.705  1.00 28.78           C  
ANISOU 2597  CA  PRO B 346     3488   4002   3446    190    154   -609       C  
ATOM   2598  C   PRO B 346      11.445  68.457  31.419  1.00 28.64           C  
ANISOU 2598  C   PRO B 346     3500   4017   3366    185    172   -537       C  
ATOM   2599  O   PRO B 346      11.636  69.590  31.863  1.00 28.55           O  
ANISOU 2599  O   PRO B 346     3507   3970   3371    183    164   -487       O  
ATOM   2600  CB  PRO B 346      12.083  66.634  33.023  1.00 26.94           C  
ANISOU 2600  CB  PRO B 346     3294   3693   3249    212    103   -618       C  
ATOM   2601  CG  PRO B 346      12.949  67.289  34.039  1.00 28.53           C  
ANISOU 2601  CG  PRO B 346     3508   3832   3500    222     74   -604       C  
ATOM   2602  CD  PRO B 346      14.233  67.611  33.325  1.00 32.39           C  
ANISOU 2602  CD  PRO B 346     3944   4340   4023    203     99   -627       C  
ATOM   2603  N   GLN B 347      10.404  68.137  30.658  1.00 29.64           N  
ANISOU 2603  N   GLN B 347     3626   4207   3429    185    191   -537       N  
ATOM   2604  CA  GLN B 347       9.247  69.009  30.529  1.00 28.12           C  
ANISOU 2604  CA  GLN B 347     3467   4040   3177    188    199   -474       C  
ATOM   2605  C   GLN B 347       8.127  68.400  31.356  1.00 26.82           C  
ANISOU 2605  C   GLN B 347     3340   3846   3006    205    167   -477       C  
ATOM   2606  O   GLN B 347       7.851  67.208  31.249  1.00 31.96           O  
ANISOU 2606  O   GLN B 347     3975   4502   3667    204    158   -525       O  
ATOM   2607  CB  GLN B 347       8.830  69.168  29.064  1.00 29.26           C  
ANISOU 2607  CB  GLN B 347     3580   4291   3248    181    243   -465       C  
ATOM   2608  CG  GLN B 347       9.800  69.981  28.222  1.00 39.46           C  
ANISOU 2608  CG  GLN B 347     4831   5628   4533    165    283   -430       C  
ATOM   2609  CD  GLN B 347       9.654  71.477  28.442  1.00 45.47           C  
ANISOU 2609  CD  GLN B 347     5619   6358   5299    158    285   -337       C  
ATOM   2610  NE2 GLN B 347      10.736  72.215  28.233  1.00 40.31           N  
ANISOU 2610  NE2 GLN B 347     4933   5692   4688    137    303   -299       N  
ATOM   2611  OE1 GLN B 347       8.578  71.960  28.801  1.00 42.84           O  
ANISOU 2611  OE1 GLN B 347     5330   6009   4939    171    267   -300       O  
ATOM   2612  N   VAL B 348       7.499  69.214  32.196  1.00 30.85           N  
ANISOU 2612  N   VAL B 348     3894   4324   3504    220    148   -425       N  
ATOM   2613  CA  VAL B 348       6.436  68.724  33.060  1.00 20.32           C  
ANISOU 2613  CA  VAL B 348     2590   2973   2158    239    123   -415       C  
ATOM   2614  C   VAL B 348       5.074  69.266  32.647  1.00 25.08           C  
ANISOU 2614  C   VAL B 348     3207   3629   2691    246    136   -374       C  
ATOM   2615  O   VAL B 348       4.861  70.473  32.613  1.00 34.91           O  
ANISOU 2615  O   VAL B 348     4473   4879   3911    256    140   -330       O  
ATOM   2616  CB  VAL B 348       6.701  69.085  34.530  1.00 24.45           C  
ANISOU 2616  CB  VAL B 348     3147   3431   2712    266     86   -398       C  
ATOM   2617  CG1 VAL B 348       5.640  68.463  35.412  1.00 17.62           C  
ANISOU 2617  CG1 VAL B 348     2303   2566   1828    287     67   -378       C  
ATOM   2618  CG2 VAL B 348       8.077  68.604  34.946  1.00 19.51           C  
ANISOU 2618  CG2 VAL B 348     2505   2753   2154    263     69   -438       C  
ATOM   2619  N   TYR B 349       4.155  68.358  32.331  1.00 27.56           N  
ANISOU 2619  N   TYR B 349     3508   3979   2985    240    139   -391       N  
ATOM   2620  CA  TYR B 349       2.806  68.739  31.933  1.00 22.82           C  
ANISOU 2620  CA  TYR B 349     2915   3434   2321    247    148   -358       C  
ATOM   2621  C   TYR B 349       1.754  68.053  32.796  1.00 32.51           C  
ANISOU 2621  C   TYR B 349     4150   4651   3552    256    128   -344       C  
ATOM   2622  O   TYR B 349       1.812  66.843  33.008  1.00 32.49           O  
ANISOU 2622  O   TYR B 349     4126   4623   3596    241    115   -374       O  
ATOM   2623  CB  TYR B 349       2.558  68.396  30.461  1.00 20.44           C  
ANISOU 2623  CB  TYR B 349     2576   3210   1981    230    172   -391       C  
ATOM   2624  CG  TYR B 349       3.560  68.977  29.491  1.00 24.93           C  
ANISOU 2624  CG  TYR B 349     3124   3812   2535    222    201   -395       C  
ATOM   2625  CD1 TYR B 349       3.581  70.336  29.211  1.00 17.02           C  
ANISOU 2625  CD1 TYR B 349     2139   2828   1499    229    217   -331       C  
ATOM   2626  CD2 TYR B 349       4.467  68.162  28.834  1.00 25.40           C  
ANISOU 2626  CD2 TYR B 349     3143   3891   2618    209    211   -458       C  
ATOM   2627  CE1 TYR B 349       4.491  70.867  28.317  1.00 26.85           C  
ANISOU 2627  CE1 TYR B 349     3357   4109   2735    217    248   -317       C  
ATOM   2628  CE2 TYR B 349       5.380  68.683  27.935  1.00 34.07           C  
ANISOU 2628  CE2 TYR B 349     4213   5037   3695    203    244   -454       C  
ATOM   2629  CZ  TYR B 349       5.385  70.035  27.679  1.00 36.43           C  
ANISOU 2629  CZ  TYR B 349     4526   5354   3961    204    265   -376       C  
ATOM   2630  OH  TYR B 349       6.293  70.556  26.788  1.00 42.01           O  
ANISOU 2630  OH  TYR B 349     5198   6113   4652    194    301   -355       O  
ATOM   2631  N   THR B 350       0.787  68.828  33.281  1.00 33.76           N  
ANISOU 2631  N   THR B 350     4333   4828   3664    281    125   -295       N  
ATOM   2632  CA  THR B 350      -0.347  68.265  33.998  1.00 29.44           C  
ANISOU 2632  CA  THR B 350     3784   4292   3108    289    114   -270       C  
ATOM   2633  C   THR B 350      -1.551  68.139  33.069  1.00 33.04           C  
ANISOU 2633  C   THR B 350     4216   4816   3522    278    127   -270       C  
ATOM   2634  O   THR B 350      -1.800  69.017  32.244  1.00 39.54           O  
ANISOU 2634  O   THR B 350     5044   5685   4294    286    141   -262       O  
ATOM   2635  CB  THR B 350      -0.736  69.115  35.224  1.00 26.34           C  
ANISOU 2635  CB  THR B 350     3427   3894   2687    334    101   -223       C  
ATOM   2636  CG2 THR B 350       0.415  69.183  36.213  1.00 24.89           C  
ANISOU 2636  CG2 THR B 350     3263   3649   2544    351     80   -231       C  
ATOM   2637  OG1 THR B 350      -1.081  70.439  34.803  1.00 30.93           O  
ANISOU 2637  OG1 THR B 350     4028   4503   3220    356    106   -205       O  
ATOM   2638  N   LEU B 351      -2.286  67.038  33.196  1.00 29.08           N  
ANISOU 2638  N   LEU B 351     3683   4319   3047    260    119   -275       N  
ATOM   2639  CA  LEU B 351      -3.480  66.814  32.391  1.00 23.23           C  
ANISOU 2639  CA  LEU B 351     2911   3640   2276    249    124   -282       C  
ATOM   2640  C   LEU B 351      -4.667  66.505  33.293  1.00 20.79           C  
ANISOU 2640  C   LEU B 351     2590   3342   1967    255    118   -230       C  
ATOM   2641  O   LEU B 351      -4.565  65.661  34.183  1.00 24.99           O  
ANISOU 2641  O   LEU B 351     3111   3828   2554    244    107   -210       O  
ATOM   2642  CB  LEU B 351      -3.270  65.662  31.399  1.00 24.27           C  
ANISOU 2642  CB  LEU B 351     2997   3772   2453    214    115   -354       C  
ATOM   2643  CG  LEU B 351      -1.890  65.428  30.783  1.00 31.18           C  
ANISOU 2643  CG  LEU B 351     3868   4623   3354    205    118   -414       C  
ATOM   2644  CD1 LEU B 351      -1.917  64.181  29.919  1.00 36.32           C  
ANISOU 2644  CD1 LEU B 351     4467   5280   4054    181    101   -496       C  
ATOM   2645  CD2 LEU B 351      -1.458  66.618  29.966  1.00 33.30           C  
ANISOU 2645  CD2 LEU B 351     4154   4945   3552    222    143   -407       C  
ATOM   2646  N   PRO B 352      -5.802  67.182  33.062  1.00 27.60           N  
ANISOU 2646  N   PRO B 352     3450   4269   2767    274    125   -203       N  
ATOM   2647  CA  PRO B 352      -7.025  66.995  33.851  1.00 23.32           C  
ANISOU 2647  CA  PRO B 352     2889   3758   2215    283    125   -151       C  
ATOM   2648  C   PRO B 352      -7.709  65.670  33.522  1.00 25.09           C  
ANISOU 2648  C   PRO B 352     3052   3980   2501    237    115   -166       C  
ATOM   2649  O   PRO B 352      -7.297  65.012  32.572  1.00 26.22           O  
ANISOU 2649  O   PRO B 352     3172   4105   2685    206    103   -231       O  
ATOM   2650  CB  PRO B 352      -7.889  68.187  33.429  1.00 23.11           C  
ANISOU 2650  CB  PRO B 352     2874   3801   2105    319    133   -134       C  
ATOM   2651  CG  PRO B 352      -7.486  68.440  32.025  1.00 20.97           C  
ANISOU 2651  CG  PRO B 352     2604   3550   1816    306    135   -184       C  
ATOM   2652  CD  PRO B 352      -6.001  68.152  31.969  1.00 25.49           C  
ANISOU 2652  CD  PRO B 352     3192   4058   2433    289    135   -217       C  
ATOM   2653  N   PRO B 353      -8.728  65.278  34.301  1.00 35.03           N  
ANISOU 2653  N   PRO B 353     4279   5258   3771    234    117   -108       N  
ATOM   2654  CA  PRO B 353      -9.436  64.036  33.975  1.00 32.22           C  
ANISOU 2654  CA  PRO B 353     3857   4891   3493    184    102   -117       C  
ATOM   2655  C   PRO B 353     -10.094  64.084  32.602  1.00 31.75           C  
ANISOU 2655  C   PRO B 353     3767   4883   3414    172     91   -181       C  
ATOM   2656  O   PRO B 353     -10.514  65.155  32.159  1.00 34.67           O  
ANISOU 2656  O   PRO B 353     4158   5321   3694    207    103   -181       O  
ATOM   2657  CB  PRO B 353     -10.501  63.937  35.079  1.00 28.41           C  
ANISOU 2657  CB  PRO B 353     3346   4443   3005    192    115    -25       C  
ATOM   2658  CG  PRO B 353      -9.979  64.759  36.196  1.00 32.91           C  
ANISOU 2658  CG  PRO B 353     3969   5020   3514    244    131     24       C  
ATOM   2659  CD  PRO B 353      -9.215  65.879  35.557  1.00 35.14           C  
ANISOU 2659  CD  PRO B 353     4310   5305   3737    277    131    -32       C  
ATOM   2660  N   SER B 354     -10.169  62.938  31.937  1.00 27.56           N  
ANISOU 2660  N   SER B 354     3184   4319   2967    127     64   -239       N  
ATOM   2661  CA  SER B 354     -10.970  62.813  30.730  1.00 31.31           C  
ANISOU 2661  CA  SER B 354     3615   4851   3430    117     46   -304       C  
ATOM   2662  C   SER B 354     -12.416  63.122  31.082  1.00 35.68           C  
ANISOU 2662  C   SER B 354     4135   5468   3953    122     54   -242       C  
ATOM   2663  O   SER B 354     -12.854  62.842  32.196  1.00 35.92           O  
ANISOU 2663  O   SER B 354     4149   5480   4018    113     65   -161       O  
ATOM   2664  CB  SER B 354     -10.848  61.407  30.134  1.00 31.75           C  
ANISOU 2664  CB  SER B 354     3612   4849   3602     69      5   -383       C  
ATOM   2665  OG  SER B 354     -12.049  61.013  29.489  1.00 41.86           O  
ANISOU 2665  OG  SER B 354     4826   6173   4904     50    -21   -417       O  
ATOM   2666  N   ARG B 355     -13.149  63.716  30.145  1.00 46.56           N  
ANISOU 2666  N   ARG B 355     5502   6929   5261    143     49   -277       N  
ATOM   2667  CA  ARG B 355     -14.564  64.005  30.363  1.00 44.65           C  
ANISOU 2667  CA  ARG B 355     5221   6755   4990    151     54   -230       C  
ATOM   2668  C   ARG B 355     -15.328  62.722  30.674  1.00 40.66           C  
ANISOU 2668  C   ARG B 355     4632   6213   4603     94     32   -217       C  
ATOM   2669  O   ARG B 355     -16.241  62.716  31.500  1.00 39.31           O  
ANISOU 2669  O   ARG B 355     4427   6068   4440     90     47   -136       O  
ATOM   2670  CB  ARG B 355     -15.174  64.707  29.150  1.00 59.09           C  
ANISOU 2670  CB  ARG B 355     7043   8676   6734    181     43   -281       C  
ATOM   2671  CG  ARG B 355     -14.734  64.143  27.808  1.00 78.77           C  
ANISOU 2671  CG  ARG B 355     9513  11173   9243    165     12   -391       C  
ATOM   2672  CD  ARG B 355     -15.705  64.517  26.699  1.00 89.04           C  
ANISOU 2672  CD  ARG B 355    10778  12575  10476    188     -8   -437       C  
ATOM   2673  NE  ARG B 355     -16.983  63.821  26.835  1.00 96.16           N  
ANISOU 2673  NE  ARG B 355    11601  13491  11445    157    -34   -437       N  
ATOM   2674  CZ  ARG B 355     -18.141  64.425  27.082  1.00102.22           C  
ANISOU 2674  CZ  ARG B 355    12348  14327  12164    178    -25   -384       C  
ATOM   2675  NH1 ARG B 355     -19.255  63.712  27.191  1.00104.05           N1+
ANISOU 2675  NH1 ARG B 355    12497  14569  12469    143    -48   -384       N1+
ATOM   2676  NH2 ARG B 355     -18.188  65.743  27.213  1.00101.13           N  
ANISOU 2676  NH2 ARG B 355    12266  14243  11914    236      5   -331       N  
ATOM   2677  N   GLU B 356     -14.931  61.635  30.018  1.00 39.62           N  
ANISOU 2677  N   GLU B 356     4464   6021   4569     51     -6   -297       N  
ATOM   2678  CA  GLU B 356     -15.556  60.331  30.214  1.00 39.03           C  
ANISOU 2678  CA  GLU B 356     4305   5888   4636    -10    -39   -295       C  
ATOM   2679  C   GLU B 356     -15.404  59.811  31.638  1.00 35.87           C  
ANISOU 2679  C   GLU B 356     3900   5419   4311    -36    -18   -181       C  
ATOM   2680  O   GLU B 356     -16.252  59.062  32.121  1.00 41.93           O  
ANISOU 2680  O   GLU B 356     4594   6165   5172    -81    -26   -122       O  
ATOM   2681  CB  GLU B 356     -14.974  59.311  29.236  1.00 50.48           C  
ANISOU 2681  CB  GLU B 356     5724   7275   6181    -40    -91   -419       C  
ATOM   2682  CG  GLU B 356     -15.473  59.444  27.807  1.00 66.06           C  
ANISOU 2682  CG  GLU B 356     7665   9326   8108    -24   -126   -535       C  
ATOM   2683  CD  GLU B 356     -14.990  58.305  26.923  1.00 89.07           C  
ANISOU 2683  CD  GLU B 356    10534  12180  11127    -49   -186   -668       C  
ATOM   2684  OE1 GLU B 356     -13.804  57.922  27.039  1.00 93.72           O  
ANISOU 2684  OE1 GLU B 356    11157  12698  11755    -50   -188   -697       O  
ATOM   2685  OE2 GLU B 356     -15.800  57.789  26.120  1.00 97.44           O1-
ANISOU 2685  OE2 GLU B 356    11523  13266  12233    -64   -236   -751       O1-
ATOM   2686  N   GLU B 357     -14.328  60.208  32.311  1.00 30.64           N  
ANISOU 2686  N   GLU B 357     3309   4726   3608     -9      9   -146       N  
ATOM   2687  CA  GLU B 357     -14.062  59.705  33.656  1.00 30.99           C  
ANISOU 2687  CA  GLU B 357     3351   4711   3711    -24     26    -40       C  
ATOM   2688  C   GLU B 357     -14.874  60.455  34.714  1.00 34.21           C  
ANISOU 2688  C   GLU B 357     3760   5202   4035      9     70     76       C  
ATOM   2689  O   GLU B 357     -14.988  59.999  35.851  1.00 36.81           O  
ANISOU 2689  O   GLU B 357     4067   5513   4405     -3     88    181       O  
ATOM   2690  CB  GLU B 357     -12.569  59.795  33.988  1.00 28.10           C  
ANISOU 2690  CB  GLU B 357     3056   4283   3337     -3     31    -55       C  
ATOM   2691  CG  GLU B 357     -12.154  58.931  35.178  1.00 29.94           C  
ANISOU 2691  CG  GLU B 357     3277   4437   3662    -27     32     35       C  
ATOM   2692  CD  GLU B 357     -10.727  59.175  35.626  1.00 35.50           C  
ANISOU 2692  CD  GLU B 357     4053   5096   4341      4     39     27       C  
ATOM   2693  OE1 GLU B 357     -10.193  58.343  36.388  1.00 34.54           O  
ANISOU 2693  OE1 GLU B 357     3922   4896   4306    -16     29     79       O  
ATOM   2694  OE2 GLU B 357     -10.139  60.200  35.222  1.00 37.24           O1-
ANISOU 2694  OE2 GLU B 357     4334   5355   4459     47     52    -27       O1-
ATOM   2695  N   MET B 358     -15.462  61.588  34.333  1.00 35.79           N  
ANISOU 2695  N   MET B 358     3982   5500   4117     55     87     59       N  
ATOM   2696  CA  MET B 358     -16.199  62.426  35.278  1.00 40.51           C  
ANISOU 2696  CA  MET B 358     4584   6186   4622    103    125    149       C  
ATOM   2697  C   MET B 358     -17.504  61.794  35.775  1.00 42.09           C  
ANISOU 2697  C   MET B 358     4690   6426   4878     68    135    232       C  
ATOM   2698  O   MET B 358     -18.214  62.391  36.584  1.00 48.41           O  
ANISOU 2698  O   MET B 358     5478   7312   5602    108    169    310       O  
ATOM   2699  CB  MET B 358     -16.496  63.787  34.649  1.00 47.36           C  
ANISOU 2699  CB  MET B 358     5495   7137   5364    163    132    102       C  
ATOM   2700  CG  MET B 358     -15.260  64.637  34.397  1.00 54.18           C  
ANISOU 2700  CG  MET B 358     6450   7974   6163    204    133     52       C  
ATOM   2701  SD  MET B 358     -14.362  65.048  35.910  1.00 46.79           S  
ANISOU 2701  SD  MET B 358     5574   7013   5193    248    157    122       S  
ATOM   2702  CE  MET B 358     -15.556  66.072  36.771  1.00 44.42           C  
ANISOU 2702  CE  MET B 358     5262   6829   4787    316    184    191       C  
ATOM   2703  N   THR B 359     -17.819  60.593  35.296  1.00 39.02           N  
ANISOU 2703  N   THR B 359     4228   5974   4625     -5    102    214       N  
ATOM   2704  CA  THR B 359     -18.997  59.869  35.768  1.00 44.98           C  
ANISOU 2704  CA  THR B 359     4881   6749   5459    -52    108    301       C  
ATOM   2705  C   THR B 359     -18.667  58.968  36.958  1.00 46.26           C  
ANISOU 2705  C   THR B 359     5017   6849   5711    -86    124    421       C  
ATOM   2706  O   THR B 359     -19.562  58.381  37.565  1.00 52.85           O  
ANISOU 2706  O   THR B 359     5766   7705   6612   -124    139    526       O  
ATOM   2707  CB  THR B 359     -19.624  59.014  34.646  1.00 52.64           C  
ANISOU 2707  CB  THR B 359     5773   7679   6550   -116     56    221       C  
ATOM   2708  CG2 THR B 359     -20.059  59.897  33.489  1.00 42.90           C  
ANISOU 2708  CG2 THR B 359     4557   6525   5217    -77     41    115       C  
ATOM   2709  OG1 THR B 359     -18.670  58.051  34.178  1.00 52.45           O  
ANISOU 2709  OG1 THR B 359     5755   7529   6645   -160     12    151       O  
ATOM   2710  N   LYS B 360     -17.383  58.864  37.287  1.00 38.40           N  
ANISOU 2710  N   LYS B 360     4090   5782   4718    -71    121    411       N  
ATOM   2711  CA  LYS B 360     -16.943  58.029  38.397  1.00 34.10           C  
ANISOU 2711  CA  LYS B 360     3528   5177   4253    -96    132    524       C  
ATOM   2712  C   LYS B 360     -16.870  58.835  39.691  1.00 42.44           C  
ANISOU 2712  C   LYS B 360     4623   6328   5174    -25    185    626       C  
ATOM   2713  O   LYS B 360     -16.909  60.061  39.664  1.00 44.37           O  
ANISOU 2713  O   LYS B 360     4923   6660   5275     45    204    586       O  
ATOM   2714  CB  LYS B 360     -15.581  57.403  38.091  1.00 39.42           C  
ANISOU 2714  CB  LYS B 360     4248   5721   5008   -115     94    455       C  
ATOM   2715  CG  LYS B 360     -15.490  56.699  36.747  1.00 54.65           C  
ANISOU 2715  CG  LYS B 360     6148   7565   7052   -167     36    324       C  
ATOM   2716  CD  LYS B 360     -16.221  55.368  36.745  1.00 61.46           C  
ANISOU 2716  CD  LYS B 360     6904   8350   8100   -249      3    372       C  
ATOM   2717  CE  LYS B 360     -16.098  54.686  35.389  1.00 62.98           C  
ANISOU 2717  CE  LYS B 360     7065   8460   8404   -289    -66    218       C  
ATOM   2718  NZ  LYS B 360     -16.869  53.412  35.326  1.00 58.63           N1+
ANISOU 2718  NZ  LYS B 360     6402   7822   8052   -371   -110    251       N1+
ATOM   2719  N   ASN B 361     -16.760  58.141  40.820  1.00 48.07           N  
ANISOU 2719  N   ASN B 361     5304   7025   5935    -39    204    757       N  
ATOM   2720  CA  ASN B 361     -16.635  58.803  42.112  1.00 49.85           C  
ANISOU 2720  CA  ASN B 361     5560   7349   6031     36    250    852       C  
ATOM   2721  C   ASN B 361     -15.221  59.306  42.349  1.00 48.82           C  
ANISOU 2721  C   ASN B 361     5533   7180   5837     90    239    792       C  
ATOM   2722  O   ASN B 361     -15.006  60.255  43.103  1.00 50.59           O  
ANISOU 2722  O   ASN B 361     5806   7491   5925    172    264    807       O  
ATOM   2723  CB  ASN B 361     -17.044  57.859  43.238  1.00 51.18           C  
ANISOU 2723  CB  ASN B 361     5651   7531   6266      5    276   1027       C  
ATOM   2724  CG  ASN B 361     -18.482  57.412  43.123  1.00 66.98           C  
ANISOU 2724  CG  ASN B 361     7538   9581   8330    -49    293   1103       C  
ATOM   2725  ND2 ASN B 361     -18.761  56.194  43.573  1.00 76.15           N  
ANISOU 2725  ND2 ASN B 361     8615  10684   9636   -120    293   1231       N  
ATOM   2726  OD1 ASN B 361     -19.334  58.152  42.636  1.00 68.06           O  
ANISOU 2726  OD1 ASN B 361     7661   9806   8394    -27    304   1051       O  
ATOM   2727  N   GLN B 362     -14.257  58.654  41.709  1.00 45.14           N  
ANISOU 2727  N   GLN B 362     5093   6582   5475     47    197    719       N  
ATOM   2728  CA  GLN B 362     -12.862  59.075  41.781  1.00 35.24           C  
ANISOU 2728  CA  GLN B 362     3929   5281   4178     90    182    650       C  
ATOM   2729  C   GLN B 362     -12.327  59.377  40.389  1.00 36.66           C  
ANISOU 2729  C   GLN B 362     4152   5404   4375     76    150    495       C  
ATOM   2730  O   GLN B 362     -12.662  58.691  39.422  1.00 42.65           O  
ANISOU 2730  O   GLN B 362     4866   6107   5234     16    122    440       O  
ATOM   2731  CB  GLN B 362     -12.006  58.005  42.455  1.00 36.17           C  
ANISOU 2731  CB  GLN B 362     4041   5304   4398     64    166    716       C  
ATOM   2732  CG  GLN B 362     -12.471  57.635  43.855  1.00 42.75           C  
ANISOU 2732  CG  GLN B 362     4829   6203   5213     80    200    888       C  
ATOM   2733  CD  GLN B 362     -11.312  57.346  44.792  1.00 60.29           C  
ANISOU 2733  CD  GLN B 362     7091   8385   7431    114    193    937       C  
ATOM   2734  NE2 GLN B 362     -11.007  58.302  45.662  1.00 68.24           N  
ANISOU 2734  NE2 GLN B 362     8148   9493   8286    202    216    952       N  
ATOM   2735  OE1 GLN B 362     -10.694  56.282  44.733  1.00 66.27           O  
ANISOU 2735  OE1 GLN B 362     7833   9022   8324     65    161    955       O  
ATOM   2736  N   VAL B 363     -11.496  60.408  40.285  1.00 28.74           N  
ANISOU 2736  N   VAL B 363     3229   4418   3273    133    151    423       N  
ATOM   2737  CA  VAL B 363     -10.935  60.796  38.995  1.00 25.70           C  
ANISOU 2737  CA  VAL B 363     2882   3995   2886    126    128    291       C  
ATOM   2738  C   VAL B 363      -9.416  60.820  39.017  1.00 28.20           C  
ANISOU 2738  C   VAL B 363     3260   4239   3216    141    111    237       C  
ATOM   2739  O   VAL B 363      -8.791  60.930  40.073  1.00 28.89           O  
ANISOU 2739  O   VAL B 363     3377   4323   3277    176    118    290       O  
ATOM   2740  CB  VAL B 363     -11.445  62.178  38.548  1.00 30.85           C  
ANISOU 2740  CB  VAL B 363     3567   4741   3412    176    145    248       C  
ATOM   2741  CG1 VAL B 363     -12.930  62.109  38.212  1.00 24.52           C  
ANISOU 2741  CG1 VAL B 363     2700   4007   2608    156    154    275       C  
ATOM   2742  CG2 VAL B 363     -11.166  63.232  39.616  1.00 21.12           C  
ANISOU 2742  CG2 VAL B 363     2388   3568   2068    252    166    288       C  
ATOM   2743  N   SER B 364      -8.822  60.722  37.836  1.00 30.58           N  
ANISOU 2743  N   SER B 364     3574   4491   3553    118     88    128       N  
ATOM   2744  CA  SER B 364      -7.375  60.651  37.719  1.00 24.05           C  
ANISOU 2744  CA  SER B 364     2792   3594   2750    126     72     69       C  
ATOM   2745  C   SER B 364      -6.794  61.982  37.275  1.00 28.60           C  
ANISOU 2745  C   SER B 364     3431   4213   3224    171     84      8       C  
ATOM   2746  O   SER B 364      -7.182  62.526  36.241  1.00 31.49           O  
ANISOU 2746  O   SER B 364     3797   4621   3548    170     87    -48       O  
ATOM   2747  CB  SER B 364      -6.972  59.556  36.730  1.00 23.50           C  
ANISOU 2747  CB  SER B 364     2688   3443   2798     74     37    -13       C  
ATOM   2748  OG  SER B 364      -7.702  58.361  36.955  1.00 27.39           O  
ANISOU 2748  OG  SER B 364     3112   3889   3404     25     19     38       O  
ATOM   2749  N   LEU B 365      -5.865  62.506  38.071  1.00 33.82           N  
ANISOU 2749  N   LEU B 365     4140   4860   3848    212     87     23       N  
ATOM   2750  CA  LEU B 365      -5.062  63.650  37.654  1.00 27.82           C  
ANISOU 2750  CA  LEU B 365     3435   4112   3024    245     90    -36       C  
ATOM   2751  C   LEU B 365      -3.713  63.143  37.153  1.00 30.26           C  
ANISOU 2751  C   LEU B 365     3753   4345   3399    224     72   -104       C  
ATOM   2752  O   LEU B 365      -3.047  62.352  37.825  1.00 28.75           O  
ANISOU 2752  O   LEU B 365     3557   4094   3272    218     57    -85       O  
ATOM   2753  CB  LEU B 365      -4.884  64.649  38.794  1.00 25.31           C  
ANISOU 2753  CB  LEU B 365     3160   3828   2630    307     96      8       C  
ATOM   2754  CG  LEU B 365      -6.165  65.150  39.470  1.00 31.35           C  
ANISOU 2754  CG  LEU B 365     3912   4678   3321    342    114     74       C  
ATOM   2755  CD1 LEU B 365      -5.867  66.295  40.420  1.00 33.62           C  
ANISOU 2755  CD1 LEU B 365     4245   5000   3527    416    111     84       C  
ATOM   2756  CD2 LEU B 365      -7.199  65.567  38.446  1.00 27.61           C  
ANISOU 2756  CD2 LEU B 365     3420   4255   2816    329    125     52       C  
ATOM   2757  N   THR B 366      -3.312  63.596  35.971  1.00 28.32           N  
ANISOU 2757  N   THR B 366     3516   4110   3136    216     75   -178       N  
ATOM   2758  CA  THR B 366      -2.141  63.037  35.311  1.00 18.65           C  
ANISOU 2758  CA  THR B 366     2285   2830   1970    196     62   -251       C  
ATOM   2759  C   THR B 366      -0.997  64.043  35.213  1.00 24.45           C  
ANISOU 2759  C   THR B 366     3062   3564   2665    222     71   -278       C  
ATOM   2760  O   THR B 366      -1.208  65.212  34.903  1.00 27.94           O  
ANISOU 2760  O   THR B 366     3528   4054   3035    243     87   -271       O  
ATOM   2761  CB  THR B 366      -2.504  62.535  33.900  1.00 21.76           C  
ANISOU 2761  CB  THR B 366     2639   3247   2384    165     58   -324       C  
ATOM   2762  CG2 THR B 366      -1.275  62.009  33.173  1.00 20.13           C  
ANISOU 2762  CG2 THR B 366     2421   3000   2226    154     46   -410       C  
ATOM   2763  OG1 THR B 366      -3.474  61.488  34.006  1.00 26.32           O  
ANISOU 2763  OG1 THR B 366     3168   3807   3025    134     40   -307       O  
ATOM   2764  N   CYS B 367       0.217  63.579  35.494  1.00 21.02           N  
ANISOU 2764  N   CYS B 367     2631   3068   2287    220     57   -306       N  
ATOM   2765  CA  CYS B 367       1.405  64.398  35.312  1.00 20.36           C  
ANISOU 2765  CA  CYS B 367     2574   2977   2186    236     62   -337       C  
ATOM   2766  C   CYS B 367       2.376  63.736  34.338  1.00 30.69           C  
ANISOU 2766  C   CYS B 367     3853   4263   3546    213     60   -417       C  
ATOM   2767  O   CYS B 367       2.992  62.723  34.654  1.00 31.13           O  
ANISOU 2767  O   CYS B 367     3891   4260   3676    205     38   -441       O  
ATOM   2768  CB  CYS B 367       2.095  64.657  36.650  1.00 21.98           C  
ANISOU 2768  CB  CYS B 367     2809   3141   2400    267     46   -303       C  
ATOM   2769  SG  CYS B 367       3.512  65.764  36.557  1.00 28.68           S  
ANISOU 2769  SG  CYS B 367     3683   3971   3242    285     46   -337       S  
ATOM   2770  N   LEU B 368       2.500  64.316  33.147  1.00 28.65           N  
ANISOU 2770  N   LEU B 368     3585   4058   3242    207     82   -455       N  
ATOM   2771  CA  LEU B 368       3.432  63.816  32.146  1.00 23.94           C  
ANISOU 2771  CA  LEU B 368     2955   3466   2674    195     86   -533       C  
ATOM   2772  C   LEU B 368       4.786  64.503  32.266  1.00 25.47           C  
ANISOU 2772  C   LEU B 368     3162   3644   2872    205     96   -538       C  
ATOM   2773  O   LEU B 368       4.878  65.727  32.214  1.00 28.81           O  
ANISOU 2773  O   LEU B 368     3609   4093   3245    214    115   -499       O  
ATOM   2774  CB  LEU B 368       2.858  64.011  30.738  1.00 23.89           C  
ANISOU 2774  CB  LEU B 368     2922   3546   2608    189    106   -569       C  
ATOM   2775  CG  LEU B 368       3.819  63.863  29.557  1.00 25.39           C  
ANISOU 2775  CG  LEU B 368     3076   3780   2789    189    122   -643       C  
ATOM   2776  CD1 LEU B 368       4.402  62.463  29.503  1.00 21.70           C  
ANISOU 2776  CD1 LEU B 368     2572   3265   2409    183     92   -727       C  
ATOM   2777  CD2 LEU B 368       3.114  64.202  28.253  1.00 29.07           C  
ANISOU 2777  CD2 LEU B 368     3520   4352   3173    193    143   -663       C  
ATOM   2778  N   VAL B 369       5.832  63.701  32.436  1.00 20.35           N  
ANISOU 2778  N   VAL B 369     2494   2945   2292    203     79   -587       N  
ATOM   2779  CA  VAL B 369       7.191  64.215  32.510  1.00 24.86           C  
ANISOU 2779  CA  VAL B 369     3065   3500   2879    209     87   -601       C  
ATOM   2780  C   VAL B 369       8.031  63.565  31.418  1.00 26.60           C  
ANISOU 2780  C   VAL B 369     3234   3749   3122    203     97   -685       C  
ATOM   2781  O   VAL B 369       8.290  62.365  31.467  1.00 35.07           O  
ANISOU 2781  O   VAL B 369     4282   4783   4261    203     70   -742       O  
ATOM   2782  CB  VAL B 369       7.833  63.949  33.886  1.00 25.20           C  
ANISOU 2782  CB  VAL B 369     3130   3463   2982    224     54   -582       C  
ATOM   2783  CG1 VAL B 369       9.190  64.616  33.979  1.00 14.17           C  
ANISOU 2783  CG1 VAL B 369     1730   2051   1604    230     58   -596       C  
ATOM   2784  CG2 VAL B 369       6.929  64.447  34.994  1.00 16.07           C  
ANISOU 2784  CG2 VAL B 369     2016   2294   1794    241     41   -507       C  
ATOM   2785  N   LYS B 370       8.447  64.352  30.430  1.00 24.72           N  
ANISOU 2785  N   LYS B 370     2978   3583   2831    200    135   -690       N  
ATOM   2786  CA  LYS B 370       9.161  63.794  29.290  1.00 28.30           C  
ANISOU 2786  CA  LYS B 370     3375   4093   3283    202    151   -771       C  
ATOM   2787  C   LYS B 370      10.472  64.514  28.980  1.00 30.99           C  
ANISOU 2787  C   LYS B 370     3692   4460   3621    200    182   -766       C  
ATOM   2788  O   LYS B 370      10.653  65.679  29.336  1.00 35.24           O  
ANISOU 2788  O   LYS B 370     4256   4988   4145    192    196   -693       O  
ATOM   2789  CB  LYS B 370       8.276  63.814  28.046  1.00 25.25           C  
ANISOU 2789  CB  LYS B 370     2966   3808   2819    203    173   -792       C  
ATOM   2790  CG  LYS B 370       7.831  65.203  27.639  1.00 26.73           C  
ANISOU 2790  CG  LYS B 370     3174   4060   2921    199    211   -709       C  
ATOM   2791  CD  LYS B 370       7.205  65.214  26.254  1.00 27.99           C  
ANISOU 2791  CD  LYS B 370     3299   4340   2994    209    236   -735       C  
ATOM   2792  CE  LYS B 370       8.262  65.080  25.170  1.00 30.26           C  
ANISOU 2792  CE  LYS B 370     3528   4716   3252    220    268   -789       C  
ATOM   2793  NZ  LYS B 370       7.704  65.268  23.803  1.00 24.61           N1+
ANISOU 2793  NZ  LYS B 370     2779   4141   2431    238    297   -803       N1+
ATOM   2794  N   GLY B 371      11.381  63.796  28.324  1.00 26.89           N  
ANISOU 2794  N   GLY B 371     3119   3973   3124    209    188   -847       N  
ATOM   2795  CA  GLY B 371      12.612  64.368  27.812  1.00 16.48           C  
ANISOU 2795  CA  GLY B 371     1760   2704   1799    207    225   -847       C  
ATOM   2796  C   GLY B 371      13.758  64.477  28.796  1.00 28.61           C  
ANISOU 2796  C   GLY B 371     3300   4155   3416    204    205   -841       C  
ATOM   2797  O   GLY B 371      14.714  65.210  28.556  1.00 31.21           O  
ANISOU 2797  O   GLY B 371     3599   4512   3748    194    235   -817       O  
ATOM   2798  N   PHE B 372      13.679  63.750  29.903  1.00 25.91           N  
ANISOU 2798  N   PHE B 372     2988   3713   3142    213    155   -858       N  
ATOM   2799  CA  PHE B 372      14.727  63.857  30.908  1.00 30.65           C  
ANISOU 2799  CA  PHE B 372     3594   4238   3815    217    129   -853       C  
ATOM   2800  C   PHE B 372      15.768  62.756  30.780  1.00 33.61           C  
ANISOU 2800  C   PHE B 372     3919   4597   4254    235    111   -944       C  
ATOM   2801  O   PHE B 372      15.468  61.636  30.362  1.00 41.89           O  
ANISOU 2801  O   PHE B 372     4947   5650   5318    249     94  -1014       O  
ATOM   2802  CB  PHE B 372      14.143  63.866  32.325  1.00 28.31           C  
ANISOU 2802  CB  PHE B 372     3360   3851   3547    224     84   -804       C  
ATOM   2803  CG  PHE B 372      13.348  62.640  32.687  1.00 32.73           C  
ANISOU 2803  CG  PHE B 372     3935   4370   4134    235     49   -826       C  
ATOM   2804  CD1 PHE B 372      13.966  61.537  33.259  1.00 32.50           C  
ANISOU 2804  CD1 PHE B 372     3891   4272   4185    252      8   -872       C  
ATOM   2805  CD2 PHE B 372      11.974  62.607  32.499  1.00 32.60           C  
ANISOU 2805  CD2 PHE B 372     3942   4375   4069    227     54   -795       C  
ATOM   2806  CE1 PHE B 372      13.231  60.415  33.613  1.00 32.65           C  
ANISOU 2806  CE1 PHE B 372     3918   4242   4245    257    -27   -879       C  
ATOM   2807  CE2 PHE B 372      11.236  61.486  32.848  1.00 30.63           C  
ANISOU 2807  CE2 PHE B 372     3697   4081   3860    230     21   -806       C  
ATOM   2808  CZ  PHE B 372      11.864  60.392  33.405  1.00 30.37           C  
ANISOU 2808  CZ  PHE B 372     3649   3975   3915    243    -20   -844       C  
ATOM   2809  N   TYR B 373      16.999  63.109  31.124  1.00 29.19           N  
ANISOU 2809  N   TYR B 373     3335   4017   3739    236    110   -948       N  
ATOM   2810  CA  TYR B 373      18.101  62.163  31.210  1.00 38.90           C  
ANISOU 2810  CA  TYR B 373     4519   5220   5039    258     87  -1030       C  
ATOM   2811  C   TYR B 373      19.072  62.644  32.286  1.00 40.40           C  
ANISOU 2811  C   TYR B 373     4717   5343   5291    260     60  -1005       C  
ATOM   2812  O   TYR B 373      19.352  63.840  32.371  1.00 36.50           O  
ANISOU 2812  O   TYR B 373     4225   4861   4781    239     81   -948       O  
ATOM   2813  CB  TYR B 373      18.813  62.022  29.860  1.00 36.68           C  
ANISOU 2813  CB  TYR B 373     4160   5047   4730    263    133  -1095       C  
ATOM   2814  CG  TYR B 373      19.813  60.891  29.831  1.00 39.24           C  
ANISOU 2814  CG  TYR B 373     4432   5352   5125    296    105  -1198       C  
ATOM   2815  CD1 TYR B 373      21.101  61.060  30.319  1.00 41.81           C  
ANISOU 2815  CD1 TYR B 373     4726   5650   5511    301     97  -1209       C  
ATOM   2816  CD2 TYR B 373      19.466  59.647  29.324  1.00 45.36           C  
ANISOU 2816  CD2 TYR B 373     5187   6133   5916    324     81  -1291       C  
ATOM   2817  CE1 TYR B 373      22.011  60.021  30.304  1.00 45.93           C  
ANISOU 2817  CE1 TYR B 373     5198   6153   6099    336     68  -1306       C  
ATOM   2818  CE2 TYR B 373      20.372  58.606  29.301  1.00 44.46           C  
ANISOU 2818  CE2 TYR B 373     5024   5993   5875    359     49  -1391       C  
ATOM   2819  CZ  TYR B 373      21.641  58.797  29.793  1.00 43.10           C  
ANISOU 2819  CZ  TYR B 373     4823   5799   5756    366     44  -1396       C  
ATOM   2820  OH  TYR B 373      22.546  57.761  29.773  1.00 51.26           O  
ANISOU 2820  OH  TYR B 373     5805   6807   6864    407      9  -1499       O  
ATOM   2821  N   PRO B 374      19.588  61.726  33.117  1.00 39.49           N  
ANISOU 2821  N   PRO B 374     4603   5152   5250    287      7  -1046       N  
ATOM   2822  CA  PRO B 374      19.288  60.289  33.167  1.00 37.15           C  
ANISOU 2822  CA  PRO B 374     4305   4814   4997    311    -30  -1105       C  
ATOM   2823  C   PRO B 374      17.908  59.987  33.740  1.00 37.24           C  
ANISOU 2823  C   PRO B 374     4377   4780   4993    307    -54  -1050       C  
ATOM   2824  O   PRO B 374      17.144  60.904  34.040  1.00 40.10           O  
ANISOU 2824  O   PRO B 374     4784   5155   5297    290    -38   -974       O  
ATOM   2825  CB  PRO B 374      20.389  59.731  34.078  1.00 36.88           C  
ANISOU 2825  CB  PRO B 374     4256   4706   5050    339    -80  -1137       C  
ATOM   2826  CG  PRO B 374      20.849  60.896  34.884  1.00 38.08           C  
ANISOU 2826  CG  PRO B 374     4431   4843   5196    330    -82  -1076       C  
ATOM   2827  CD  PRO B 374      20.730  62.079  33.978  1.00 38.73           C  
ANISOU 2827  CD  PRO B 374     4496   5007   5213    296    -20  -1044       C  
ATOM   2828  N   SER B 375      17.600  58.701  33.883  1.00 30.62           N  
ANISOU 2828  N   SER B 375     3536   3888   4213    323    -94  -1089       N  
ATOM   2829  CA  SER B 375      16.273  58.263  34.296  1.00 25.01           C  
ANISOU 2829  CA  SER B 375     2867   3137   3498    315   -114  -1037       C  
ATOM   2830  C   SER B 375      16.018  58.464  35.789  1.00 32.17           C  
ANISOU 2830  C   SER B 375     3828   3980   4416    324   -146   -946       C  
ATOM   2831  O   SER B 375      14.876  58.371  36.244  1.00 31.30           O  
ANISOU 2831  O   SER B 375     3753   3854   4285    315   -152   -880       O  
ATOM   2832  CB  SER B 375      16.075  56.793  33.930  1.00 28.14           C  
ANISOU 2832  CB  SER B 375     3232   3487   3975    326   -152  -1108       C  
ATOM   2833  OG  SER B 375      17.038  55.984  34.575  1.00 33.32           O  
ANISOU 2833  OG  SER B 375     3870   4065   4724    355   -199  -1139       O  
ATOM   2834  N   ASP B 376      17.079  58.727  36.548  1.00 29.59           N  
ANISOU 2834  N   ASP B 376     3501   3624   4117    345   -167   -943       N  
ATOM   2835  CA  ASP B 376      16.945  58.999  37.978  1.00 35.32           C  
ANISOU 2835  CA  ASP B 376     4273   4307   4839    365   -200   -865       C  
ATOM   2836  C   ASP B 376      16.088  60.236  38.213  1.00 35.57           C  
ANISOU 2836  C   ASP B 376     4349   4385   4781    352   -172   -796       C  
ATOM   2837  O   ASP B 376      16.445  61.340  37.795  1.00 35.84           O  
ANISOU 2837  O   ASP B 376     4378   4463   4777    339   -143   -805       O  
ATOM   2838  CB  ASP B 376      18.318  59.171  38.628  1.00 36.39           C  
ANISOU 2838  CB  ASP B 376     4394   4416   5016    393   -230   -891       C  
ATOM   2839  CG  ASP B 376      19.205  57.957  38.444  1.00 40.07           C  
ANISOU 2839  CG  ASP B 376     4815   4835   5574    414   -263   -962       C  
ATOM   2840  OD1 ASP B 376      18.674  56.833  38.338  1.00 40.58           O  
ANISOU 2840  OD1 ASP B 376     4875   4857   5687    416   -284   -967       O  
ATOM   2841  OD2 ASP B 376      20.437  58.125  38.392  1.00 43.28           O1-
ANISOU 2841  OD2 ASP B 376     5185   5245   6014    428   -270  -1016       O1-
ATOM   2842  N   ILE B 377      14.955  60.043  38.882  1.00 25.19           N  
ANISOU 2842  N   ILE B 377     3072   3059   3438    356   -182   -724       N  
ATOM   2843  CA  ILE B 377      13.976  61.107  39.048  1.00 24.80           C  
ANISOU 2843  CA  ILE B 377     3062   3058   3304    349   -157   -665       C  
ATOM   2844  C   ILE B 377      13.015  60.809  40.200  1.00 23.80           C  
ANISOU 2844  C   ILE B 377     2970   2918   3154    371   -179   -580       C  
ATOM   2845  O   ILE B 377      12.830  59.656  40.592  1.00 27.21           O  
ANISOU 2845  O   ILE B 377     3394   3307   3639    376   -204   -557       O  
ATOM   2846  CB  ILE B 377      13.173  61.329  37.732  1.00 34.25           C  
ANISOU 2846  CB  ILE B 377     4246   4308   4460    312   -110   -681       C  
ATOM   2847  CG1 ILE B 377      12.509  62.706  37.705  1.00 28.65           C  
ANISOU 2847  CG1 ILE B 377     3568   3649   3668    307    -82   -635       C  
ATOM   2848  CG2 ILE B 377      12.142  60.225  37.510  1.00 15.16           C  
ANISOU 2848  CG2 ILE B 377     1821   1875   2065    299   -116   -669       C  
ATOM   2849  CD1 ILE B 377      11.884  63.027  36.374  1.00 28.35           C  
ANISOU 2849  CD1 ILE B 377     3515   3671   3586    276    -38   -650       C  
ATOM   2850  N   ALA B 378      12.421  61.859  40.754  1.00 19.03           N  
ANISOU 2850  N   ALA B 378     2402   2353   2474    386   -171   -532       N  
ATOM   2851  CA  ALA B 378      11.417  61.706  41.792  1.00 24.81           C  
ANISOU 2851  CA  ALA B 378     3163   3100   3164    411   -182   -448       C  
ATOM   2852  C   ALA B 378      10.207  62.583  41.473  1.00 29.75           C  
ANISOU 2852  C   ALA B 378     3810   3785   3710    399   -148   -415       C  
ATOM   2853  O   ALA B 378      10.354  63.730  41.045  1.00 28.83           O  
ANISOU 2853  O   ALA B 378     3703   3694   3556    396   -132   -442       O  
ATOM   2854  CB  ALA B 378      11.993  62.051  43.156  1.00 18.73           C  
ANISOU 2854  CB  ALA B 378     2414   2328   2374    466   -222   -425       C  
ATOM   2855  N   VAL B 379       9.013  62.030  41.659  1.00 27.64           N  
ANISOU 2855  N   VAL B 379     3544   3534   3424    392   -137   -353       N  
ATOM   2856  CA  VAL B 379       7.782  62.768  41.409  1.00 25.88           C  
ANISOU 2856  CA  VAL B 379     3337   3371   3127    386   -107   -320       C  
ATOM   2857  C   VAL B 379       6.852  62.670  42.612  1.00 31.38           C  
ANISOU 2857  C   VAL B 379     4048   4102   3772    421   -114   -231       C  
ATOM   2858  O   VAL B 379       6.623  61.582  43.143  1.00 27.12           O  
ANISOU 2858  O   VAL B 379     3492   3541   3272    420   -126   -177       O  
ATOM   2859  CB  VAL B 379       7.052  62.253  40.150  1.00 29.77           C  
ANISOU 2859  CB  VAL B 379     3803   3870   3640    335    -79   -339       C  
ATOM   2860  CG1 VAL B 379       5.785  63.060  39.900  1.00 29.22           C  
ANISOU 2860  CG1 VAL B 379     3747   3864   3490    333    -51   -304       C  
ATOM   2861  CG2 VAL B 379       7.961  62.321  38.939  1.00 24.31           C  
ANISOU 2861  CG2 VAL B 379     3089   3164   2983    309    -68   -425       C  
ATOM   2862  N   GLU B 380       6.324  63.814  43.041  1.00 26.19           N  
ANISOU 2862  N   GLU B 380     3418   3503   3031    455   -107   -214       N  
ATOM   2863  CA  GLU B 380       5.394  63.863  44.164  1.00 28.34           C  
ANISOU 2863  CA  GLU B 380     3699   3833   3234    499   -109   -134       C  
ATOM   2864  C   GLU B 380       4.168  64.721  43.867  1.00 32.84           C  
ANISOU 2864  C   GLU B 380     4278   4468   3730    503    -80   -117       C  
ATOM   2865  O   GLU B 380       4.182  65.555  42.962  1.00 40.36           O  
ANISOU 2865  O   GLU B 380     5240   5420   4674    484    -68   -167       O  
ATOM   2866  CB  GLU B 380       6.105  64.393  45.413  1.00 22.85           C  
ANISOU 2866  CB  GLU B 380     3026   3155   2499    569   -146   -137       C  
ATOM   2867  CG  GLU B 380       7.229  63.506  45.908  1.00 28.41           C  
ANISOU 2867  CG  GLU B 380     3720   3806   3268    578   -179   -141       C  
ATOM   2868  CD  GLU B 380       8.037  64.152  47.015  1.00 41.20           C  
ANISOU 2868  CD  GLU B 380     5360   5445   4848    649   -222   -165       C  
ATOM   2869  OE1 GLU B 380       9.010  63.521  47.482  1.00 43.93           O  
ANISOU 2869  OE1 GLU B 380     5697   5753   5240    665   -254   -172       O  
ATOM   2870  OE2 GLU B 380       7.703  65.286  47.417  1.00 40.46           O1-
ANISOU 2870  OE2 GLU B 380     5287   5404   4680    694   -229   -184       O1-
ATOM   2871  N   TRP B 381       3.105  64.506  44.634  1.00 30.05           N  
ANISOU 2871  N   TRP B 381     3919   4177   3323    528    -70    -38       N  
ATOM   2872  CA  TRP B 381       1.904  65.326  44.537  1.00 26.72           C  
ANISOU 2872  CA  TRP B 381     3502   3827   2823    545    -46    -19       C  
ATOM   2873  C   TRP B 381       1.613  66.000  45.863  1.00 34.58           C  
ANISOU 2873  C   TRP B 381     4515   4899   3727    628    -61     12       C  
ATOM   2874  O   TRP B 381       1.959  65.480  46.925  1.00 33.48           O  
ANISOU 2874  O   TRP B 381     4370   4776   3575    666    -79     54       O  
ATOM   2875  CB  TRP B 381       0.692  64.488  44.118  1.00 27.41           C  
ANISOU 2875  CB  TRP B 381     3553   3936   2925    499    -15     43       C  
ATOM   2876  CG  TRP B 381       0.733  63.977  42.710  1.00 34.70           C  
ANISOU 2876  CG  TRP B 381     4458   4805   3923    427     -3     -3       C  
ATOM   2877  CD1 TRP B 381       1.341  62.836  42.271  1.00 30.88           C  
ANISOU 2877  CD1 TRP B 381     3951   4248   3536    382    -14    -20       C  
ATOM   2878  CD2 TRP B 381       0.116  64.571  41.559  1.00 29.87           C  
ANISOU 2878  CD2 TRP B 381     3844   4215   3290    400     18    -41       C  
ATOM   2879  CE2 TRP B 381       0.396  63.735  40.459  1.00 28.96           C  
ANISOU 2879  CE2 TRP B 381     3702   4047   3252    341     20    -85       C  
ATOM   2880  CE3 TRP B 381      -0.643  65.727  41.352  1.00 24.17           C  
ANISOU 2880  CE3 TRP B 381     3139   3555   2491    425     32    -45       C  
ATOM   2881  NE1 TRP B 381       1.146  62.684  40.919  1.00 23.56           N  
ANISOU 2881  NE1 TRP B 381     3005   3303   2644    332     -1    -76       N  
ATOM   2882  CZ2 TRP B 381      -0.054  64.018  39.174  1.00 26.20           C  
ANISOU 2882  CZ2 TRP B 381     3343   3718   2895    310     37   -129       C  
ATOM   2883  CZ3 TRP B 381      -1.087  66.007  40.071  1.00 27.44           C  
ANISOU 2883  CZ3 TRP B 381     3544   3977   2903    390     50    -80       C  
ATOM   2884  CH2 TRP B 381      -0.788  65.157  38.999  1.00 30.61           C  
ANISOU 2884  CH2 TRP B 381     3919   4338   3373    333     53   -121       C  
ATOM   2885  N   GLU B 382       0.969  67.158  45.800  1.00 34.30           N  
ANISOU 2885  N   GLU B 382     4495   4915   3623    662    -57    -11       N  
ATOM   2886  CA  GLU B 382       0.544  67.846  47.007  1.00 34.69           C  
ANISOU 2886  CA  GLU B 382     4554   5051   3576    751    -72      5       C  
ATOM   2887  C   GLU B 382      -0.608  68.790  46.716  1.00 34.82           C  
ANISOU 2887  C   GLU B 382     4574   5129   3528    773    -55     -1       C  
ATOM   2888  O   GLU B 382      -0.887  69.108  45.562  1.00 31.55           O  
ANISOU 2888  O   GLU B 382     4162   4681   3146    723    -38    -27       O  
ATOM   2889  CB  GLU B 382       1.712  68.610  47.635  1.00 30.78           C  
ANISOU 2889  CB  GLU B 382     4089   4530   3077    808   -123    -69       C  
ATOM   2890  CG  GLU B 382       2.111  69.863  46.892  1.00 36.42           C  
ANISOU 2890  CG  GLU B 382     4827   5193   3817    802   -142   -155       C  
ATOM   2891  CD  GLU B 382       3.463  70.378  47.329  1.00 46.92           C  
ANISOU 2891  CD  GLU B 382     6174   6469   5184    833   -195   -228       C  
ATOM   2892  OE1 GLU B 382       3.568  71.578  47.663  1.00 50.78           O  
ANISOU 2892  OE1 GLU B 382     6680   6961   5651    888   -233   -289       O  
ATOM   2893  OE2 GLU B 382       4.424  69.580  47.321  1.00 56.12           O1-
ANISOU 2893  OE2 GLU B 382     7332   7583   6410    803   -202   -230       O1-
ATOM   2894  N   SER B 383      -1.280  69.226  47.776  1.00 36.57           N  
ANISOU 2894  N   SER B 383     4791   5449   3654    855    -60     24       N  
ATOM   2895  CA  SER B 383      -2.417  70.133  47.659  1.00 31.52           C  
ANISOU 2895  CA  SER B 383     4150   4879   2946    892    -48     17       C  
ATOM   2896  C   SER B 383      -2.564  70.952  48.929  1.00 38.17           C  
ANISOU 2896  C   SER B 383     4997   5803   3704   1000    -78     -9       C  
ATOM   2897  O   SER B 383      -2.559  70.399  50.027  1.00 40.70           O  
ANISOU 2897  O   SER B 383     5292   6179   3992   1038    -76     39       O  
ATOM   2898  CB  SER B 383      -3.700  69.350  47.371  1.00 21.89           C  
ANISOU 2898  CB  SER B 383     2887   3717   1711    851      3    105       C  
ATOM   2899  OG  SER B 383      -4.811  70.220  47.263  1.00 26.24           O  
ANISOU 2899  OG  SER B 383     3431   4336   2202    887     14     96       O  
ATOM   2900  N   ASN B 384      -2.694  72.266  48.766  1.00 39.78           N  
ANISOU 2900  N   ASN B 384     5214   5982   3919   1033   -105    -85       N  
ATOM   2901  CA  ASN B 384      -2.747  73.191  49.895  1.00 45.90           C  
ANISOU 2901  CA  ASN B 384     5979   6791   4670   1123   -140   -136       C  
ATOM   2902  C   ASN B 384      -1.580  72.975  50.855  1.00 55.96           C  
ANISOU 2902  C   ASN B 384     7265   8062   5936   1170   -181   -167       C  
ATOM   2903  O   ASN B 384      -1.769  72.861  52.066  1.00 57.83           O  
ANISOU 2903  O   ASN B 384     7472   8371   6131   1233   -182   -151       O  
ATOM   2904  CB  ASN B 384      -4.080  73.055  50.633  1.00 45.30           C  
ANISOU 2904  CB  ASN B 384     5847   6815   4548   1155   -102    -77       C  
ATOM   2905  CG  ASN B 384      -5.272  73.222  49.712  1.00 53.09           C  
ANISOU 2905  CG  ASN B 384     6817   7810   5545   1110    -67    -47       C  
ATOM   2906  ND2 ASN B 384      -5.153  74.130  48.745  1.00 46.21           N  
ANISOU 2906  ND2 ASN B 384     5979   6872   4708   1096    -89   -106       N  
ATOM   2907  OD1 ASN B 384      -6.279  72.531  49.853  1.00 62.29           O  
ANISOU 2907  OD1 ASN B 384     7938   9042   6688   1090    -21     30       O  
ATOM   2908  N   GLY B 385      -0.376  72.895  50.295  1.00 55.45           N  
ANISOU 2908  N   GLY B 385     7241   7917   5911   1141   -214   -212       N  
ATOM   2909  CA  GLY B 385       0.843  72.792  51.077  1.00 58.29           C  
ANISOU 2909  CA  GLY B 385     7614   8260   6273   1184   -265   -257       C  
ATOM   2910  C   GLY B 385       1.127  71.408  51.625  1.00 62.15           C  
ANISOU 2910  C   GLY B 385     8088   8790   6735   1175   -246   -173       C  
ATOM   2911  O   GLY B 385       2.196  71.167  52.183  1.00 69.08           O  
ANISOU 2911  O   GLY B 385     8975   9646   7628   1200   -286   -202       O  
ATOM   2912  N   GLN B 386       0.184  70.490  51.457  1.00 57.34           N  
ANISOU 2912  N   GLN B 386     7451   8231   6104   1133   -186    -67       N  
ATOM   2913  CA  GLN B 386       0.297  69.178  52.083  1.00 53.17           C  
ANISOU 2913  CA  GLN B 386     6900   7743   5558   1128   -167     34       C  
ATOM   2914  C   GLN B 386       0.312  68.026  51.089  1.00 48.46           C  
ANISOU 2914  C   GLN B 386     6288   7059   5066   1011   -126     98       C  
ATOM   2915  O   GLN B 386      -0.417  68.041  50.100  1.00 50.26           O  
ANISOU 2915  O   GLN B 386     6508   7263   5326    949    -91    108       O  
ATOM   2916  CB  GLN B 386      -0.840  68.987  53.080  1.00 51.75           C  
ANISOU 2916  CB  GLN B 386     6669   7672   5323   1164   -123    110       C  
ATOM   2917  CG  GLN B 386      -0.608  69.731  54.372  1.00 56.90           C  
ANISOU 2917  CG  GLN B 386     7308   8379   5933   1259   -152     51       C  
ATOM   2918  CD  GLN B 386       0.458  69.077  55.220  1.00 69.78           C  
ANISOU 2918  CD  GLN B 386     8943  10017   7551   1293   -182     67       C  
ATOM   2919  NE2 GLN B 386       0.167  67.879  55.717  1.00 66.84           N  
ANISOU 2919  NE2 GLN B 386     8539   9699   7158   1277   -145    194       N  
ATOM   2920  OE1 GLN B 386       1.535  69.635  55.422  1.00 80.63           O  
ANISOU 2920  OE1 GLN B 386    10346  11347   8942   1332   -241    -30       O  
ATOM   2921  N   PRO B 387       1.144  67.010  51.368  1.00 44.53           N  
ANISOU 2921  N   PRO B 387     5783   6515   4621    988   -136    137       N  
ATOM   2922  CA  PRO B 387       1.323  65.873  50.460  1.00 42.63           C  
ANISOU 2922  CA  PRO B 387     5525   6178   4494    885   -111    179       C  
ATOM   2923  C   PRO B 387       0.055  65.059  50.210  1.00 42.69           C  
ANISOU 2923  C   PRO B 387     5493   6223   4505    836    -59    286       C  
ATOM   2924  O   PRO B 387      -0.637  64.676  51.154  1.00 43.68           O  
ANISOU 2924  O   PRO B 387     5590   6447   4562    878    -40    386       O  
ATOM   2925  CB  PRO B 387       2.377  65.017  51.179  1.00 34.56           C  
ANISOU 2925  CB  PRO B 387     4500   5124   3507    901   -141    208       C  
ATOM   2926  CG  PRO B 387       2.298  65.427  52.612  1.00 37.67           C  
ANISOU 2926  CG  PRO B 387     4895   5639   3778   1012   -163    232       C  
ATOM   2927  CD  PRO B 387       1.977  66.885  52.577  1.00 36.89           C  
ANISOU 2927  CD  PRO B 387     4820   5586   3610   1066   -178    136       C  
ATOM   2928  N   GLU B 388      -0.243  64.819  48.941  1.00 39.99           N  
ANISOU 2928  N   GLU B 388     5144   5810   4243    751    -36    266       N  
ATOM   2929  CA  GLU B 388      -1.218  63.814  48.545  1.00 35.67           C  
ANISOU 2929  CA  GLU B 388     4551   5261   3741    686      1    355       C  
ATOM   2930  C   GLU B 388      -0.452  62.516  48.362  1.00 43.52           C  
ANISOU 2930  C   GLU B 388     5529   6155   4852    630    -12    383       C  
ATOM   2931  O   GLU B 388       0.664  62.528  47.843  1.00 47.97           O  
ANISOU 2931  O   GLU B 388     6117   6632   5479    610    -39    300       O  
ATOM   2932  CB  GLU B 388      -1.936  64.220  47.256  1.00 40.37           C  
ANISOU 2932  CB  GLU B 388     5143   5837   4359    631     24    306       C  
ATOM   2933  CG  GLU B 388      -2.660  65.555  47.336  1.00 46.84           C  
ANISOU 2933  CG  GLU B 388     5980   6742   5075    687     32    270       C  
ATOM   2934  CD  GLU B 388      -4.007  65.441  48.011  1.00 47.19           C  
ANISOU 2934  CD  GLU B 388     5984   6903   5043    718     65    365       C  
ATOM   2935  OE1 GLU B 388      -4.506  66.461  48.535  1.00 54.76           O  
ANISOU 2935  OE1 GLU B 388     6953   7953   5898    793     64    346       O  
ATOM   2936  OE2 GLU B 388      -4.567  64.323  48.012  1.00 46.40           O1-
ANISOU 2936  OE2 GLU B 388     5837   6801   4993    666     89    457       O1-
ATOM   2937  N   ASN B 389      -1.025  61.399  48.789  1.00 39.13           N  
ANISOU 2937  N   ASN B 389     4927   5607   4332    604      4    502       N  
ATOM   2938  CA  ASN B 389      -0.265  60.155  48.775  1.00 51.69           C  
ANISOU 2938  CA  ASN B 389     6501   7097   6040    563    -18    535       C  
ATOM   2939  C   ASN B 389      -0.968  59.009  48.062  1.00 49.85           C  
ANISOU 2939  C   ASN B 389     6218   6797   5926    475     -4    590       C  
ATOM   2940  O   ASN B 389      -0.426  57.908  47.969  1.00 47.04           O  
ANISOU 2940  O   ASN B 389     5842   6343   5687    436    -27    614       O  
ATOM   2941  CB  ASN B 389       0.083  59.736  50.206  1.00 64.72           C  
ANISOU 2941  CB  ASN B 389     8145   8799   7647    626    -31    637       C  
ATOM   2942  CG  ASN B 389       1.156  60.617  50.828  1.00 69.23           C  
ANISOU 2942  CG  ASN B 389     8765   9400   8141    708    -66    557       C  
ATOM   2943  ND2 ASN B 389       1.011  60.901  52.118  1.00 66.55           N  
ANISOU 2943  ND2 ASN B 389     8424   9176   7686    795    -68    622       N  
ATOM   2944  OD1 ASN B 389       2.103  61.039  50.161  1.00 73.70           O  
ANISOU 2944  OD1 ASN B 389     9363   9890   8749    694    -92    437       O  
ATOM   2945  N   ASN B 390      -2.169  59.271  47.556  1.00 38.53           N  
ANISOU 2945  N   ASN B 390     4759   5410   4469    446     29    602       N  
ATOM   2946  CA  ASN B 390      -2.880  58.277  46.759  1.00 32.04           C  
ANISOU 2946  CA  ASN B 390     3885   4523   3767    361     35    632       C  
ATOM   2947  C   ASN B 390      -2.514  58.410  45.288  1.00 36.14           C  
ANISOU 2947  C   ASN B 390     4420   4962   4349    312     20    492       C  
ATOM   2948  O   ASN B 390      -3.381  58.545  44.426  1.00 28.00           O  
ANISOU 2948  O   ASN B 390     3367   3945   3327    273     35    462       O  
ATOM   2949  CB  ASN B 390      -4.396  58.402  46.944  1.00 27.70           C  
ANISOU 2949  CB  ASN B 390     3289   4069   3167    353     75    720       C  
ATOM   2950  CG  ASN B 390      -5.156  57.235  46.329  1.00 32.11           C  
ANISOU 2950  CG  ASN B 390     3781   4556   3865    264     75    770       C  
ATOM   2951  ND2 ASN B 390      -6.472  57.375  46.231  1.00 36.28           N  
ANISOU 2951  ND2 ASN B 390     4263   5157   4364    246    108    823       N  
ATOM   2952  OD1 ASN B 390      -4.568  56.220  45.952  1.00 39.96           O  
ANISOU 2952  OD1 ASN B 390     4759   5428   4995    216     42    757       O  
ATOM   2953  N   TYR B 391      -1.217  58.383  45.008  1.00 33.35           N  
ANISOU 2953  N   TYR B 391     4100   4536   4035    319    -11    406       N  
ATOM   2954  CA  TYR B 391      -0.757  58.431  43.633  1.00 31.58           C  
ANISOU 2954  CA  TYR B 391     3884   4247   3868    278    -23    278       C  
ATOM   2955  C   TYR B 391       0.168  57.261  43.323  1.00 33.64           C  
ANISOU 2955  C   TYR B 391     4126   4389   4265    244    -61    246       C  
ATOM   2956  O   TYR B 391       0.733  56.644  44.228  1.00 31.72           O  
ANISOU 2956  O   TYR B 391     3881   4110   4060    264    -81    310       O  
ATOM   2957  CB  TYR B 391      -0.049  59.762  43.338  1.00 28.98           C  
ANISOU 2957  CB  TYR B 391     3609   3954   3448    319    -20    183       C  
ATOM   2958  CG  TYR B 391       1.262  59.968  44.069  1.00 26.51           C  
ANISOU 2958  CG  TYR B 391     3331   3617   3124    366    -45    163       C  
ATOM   2959  CD1 TYR B 391       2.462  59.499  43.544  1.00 26.57           C  
ANISOU 2959  CD1 TYR B 391     3341   3539   3216    347    -72     87       C  
ATOM   2960  CD2 TYR B 391       1.302  60.660  45.271  1.00 28.23           C  
ANISOU 2960  CD2 TYR B 391     3574   3906   3245    434    -45    211       C  
ATOM   2961  CE1 TYR B 391       3.659  59.698  44.212  1.00 28.96           C  
ANISOU 2961  CE1 TYR B 391     3670   3823   3512    390    -97     66       C  
ATOM   2962  CE2 TYR B 391       2.492  60.866  45.942  1.00 24.19           C  
ANISOU 2962  CE2 TYR B 391     3090   3376   2724    480    -75    185       C  
ATOM   2963  CZ  TYR B 391       3.665  60.387  45.412  1.00 27.67           C  
ANISOU 2963  CZ  TYR B 391     3532   3727   3255    456   -100    115       C  
ATOM   2964  OH  TYR B 391       4.840  60.602  46.097  1.00 34.38           O  
ANISOU 2964  OH  TYR B 391     4404   4562   4097    503   -133     88       O  
ATOM   2965  N   LYS B 392       0.307  56.955  42.036  1.00 34.59           N  
ANISOU 2965  N   LYS B 392     4232   4456   4455    200    -72    143       N  
ATOM   2966  CA  LYS B 392       1.273  55.969  41.570  1.00 33.23           C  
ANISOU 2966  CA  LYS B 392     4042   4176   4407    177   -111     78       C  
ATOM   2967  C   LYS B 392       2.017  56.525  40.365  1.00 34.07           C  
ANISOU 2967  C   LYS B 392     4168   4284   4494    176   -111    -65       C  
ATOM   2968  O   LYS B 392       1.452  57.268  39.561  1.00 32.26           O  
ANISOU 2968  O   LYS B 392     3943   4117   4198    168    -86   -111       O  
ATOM   2969  CB  LYS B 392       0.579  54.650  41.217  1.00 38.81           C  
ANISOU 2969  CB  LYS B 392     4688   4806   5254    121   -136    105       C  
ATOM   2970  CG  LYS B 392      -0.259  54.063  42.345  1.00 41.15           C  
ANISOU 2970  CG  LYS B 392     4953   5104   5579    112   -130    267       C  
ATOM   2971  CD  LYS B 392       0.335  52.776  42.891  1.00 41.68           C  
ANISOU 2971  CD  LYS B 392     4992   5057   5787    101   -174    324       C  
ATOM   2972  CE  LYS B 392       1.067  52.995  44.201  1.00 42.97           C  
ANISOU 2972  CE  LYS B 392     5190   5248   5887    160   -172    411       C  
ATOM   2973  NZ  LYS B 392       1.413  51.698  44.848  1.00 39.30           N1+
ANISOU 2973  NZ  LYS B 392     4692   4680   5560    148   -211    504       N1+
ATOM   2974  N   THR B 393       3.289  56.175  40.246  1.00 29.91           N  
ANISOU 2974  N   THR B 393     3646   3696   4022    188   -138   -130       N  
ATOM   2975  CA  THR B 393       4.111  56.693  39.166  1.00 30.31           C  
ANISOU 2975  CA  THR B 393     3707   3758   4051    191   -133   -256       C  
ATOM   2976  C   THR B 393       4.706  55.544  38.369  1.00 32.29           C  
ANISOU 2976  C   THR B 393     3917   3926   4426    169   -169   -346       C  
ATOM   2977  O   THR B 393       5.324  54.645  38.937  1.00 38.65           O  
ANISOU 2977  O   THR B 393     4709   4649   5325    175   -206   -328       O  
ATOM   2978  CB  THR B 393       5.239  57.597  39.700  1.00 28.18           C  
ANISOU 2978  CB  THR B 393     3479   3510   3717    235   -128   -270       C  
ATOM   2979  CG2 THR B 393       6.056  58.181  38.556  1.00 26.74           C  
ANISOU 2979  CG2 THR B 393     3299   3349   3514    232   -115   -384       C  
ATOM   2980  OG1 THR B 393       4.670  58.665  40.467  1.00 29.25           O  
ANISOU 2980  OG1 THR B 393     3650   3720   3743    263   -103   -199       O  
ATOM   2981  N   THR B 394       4.505  55.567  37.055  1.00 30.02           N  
ANISOU 2981  N   THR B 394     3606   3663   4137    148   -163   -446       N  
ATOM   2982  CA  THR B 394       5.100  54.564  36.182  1.00 27.09           C  
ANISOU 2982  CA  THR B 394     3192   3230   3871    139   -200   -557       C  
ATOM   2983  C   THR B 394       6.620  54.645  36.244  1.00 30.27           C  
ANISOU 2983  C   THR B 394     3606   3611   4284    171   -209   -616       C  
ATOM   2984  O   THR B 394       7.172  55.699  36.554  1.00 31.89           O  
ANISOU 2984  O   THR B 394     3850   3870   4398    194   -179   -598       O  
ATOM   2985  CB  THR B 394       4.650  54.740  34.717  1.00 30.83           C  
ANISOU 2985  CB  THR B 394     3639   3765   4311    124   -188   -662       C  
ATOM   2986  CG2 THR B 394       3.164  55.069  34.637  1.00 31.23           C  
ANISOU 2986  CG2 THR B 394     3687   3867   4314     99   -169   -602       C  
ATOM   2987  OG1 THR B 394       5.418  55.782  34.104  1.00 33.19           O  
ANISOU 2987  OG1 THR B 394     3959   4144   4507    148   -151   -719       O  
ATOM   2988  N   PRO B 395       7.303  53.527  35.959  1.00 32.20           N  
ANISOU 2988  N   PRO B 395     3814   3774   4648    174   -254   -690       N  
ATOM   2989  CA  PRO B 395       8.761  53.593  35.859  1.00 31.34           C  
ANISOU 2989  CA  PRO B 395     3706   3655   4548    206   -261   -762       C  
ATOM   2990  C   PRO B 395       9.153  54.492  34.696  1.00 34.15           C  
ANISOU 2990  C   PRO B 395     4057   4112   4807    213   -220   -855       C  
ATOM   2991  O   PRO B 395       8.308  54.763  33.844  1.00 27.37           O  
ANISOU 2991  O   PRO B 395     3188   3315   3898    195   -199   -882       O  
ATOM   2992  CB  PRO B 395       9.172  52.137  35.600  1.00 30.25           C  
ANISOU 2992  CB  PRO B 395     3519   3411   4564    208   -322   -836       C  
ATOM   2993  CG  PRO B 395       8.017  51.319  36.064  1.00 21.87           C  
ANISOU 2993  CG  PRO B 395     2442   2278   3588    176   -352   -754       C  
ATOM   2994  CD  PRO B 395       6.797  52.151  35.817  1.00 24.42           C  
ANISOU 2994  CD  PRO B 395     2781   2691   3805    150   -306   -706       C  
ATOM   2995  N   PRO B 396      10.408  54.961  34.665  1.00 33.34           N  
ANISOU 2995  N   PRO B 396     3959   4031   4679    238   -207   -896       N  
ATOM   2996  CA  PRO B 396      10.847  55.717  33.487  1.00 25.98           C  
ANISOU 2996  CA  PRO B 396     3010   3196   3665    243   -166   -976       C  
ATOM   2997  C   PRO B 396      10.838  54.833  32.242  1.00 31.97           C  
ANISOU 2997  C   PRO B 396     3711   3967   4469    247   -185  -1104       C  
ATOM   2998  O   PRO B 396      11.179  53.652  32.327  1.00 41.68           O  
ANISOU 2998  O   PRO B 396     4910   5112   5815    258   -237  -1160       O  
ATOM   2999  CB  PRO B 396      12.270  56.151  33.850  1.00 24.42           C  
ANISOU 2999  CB  PRO B 396     2816   2998   3465    268   -160   -990       C  
ATOM   3000  CG  PRO B 396      12.347  56.037  35.344  1.00 25.74           C  
ANISOU 3000  CG  PRO B 396     3021   3090   3671    277   -189   -895       C  
ATOM   3001  CD  PRO B 396      11.441  54.908  35.714  1.00 22.82           C  
ANISOU 3001  CD  PRO B 396     2644   2644   3383    264   -228   -861       C  
ATOM   3002  N   VAL B 397      10.435  55.387  31.106  1.00 31.23           N  
ANISOU 3002  N   VAL B 397     3602   3979   4287    243   -148  -1150       N  
ATOM   3003  CA  VAL B 397      10.397  54.619  29.868  1.00 36.79           C  
ANISOU 3003  CA  VAL B 397     4248   4717   5015    257   -168  -1283       C  
ATOM   3004  C   VAL B 397      11.250  55.288  28.799  1.00 41.17           C  
ANISOU 3004  C   VAL B 397     4773   5394   5475    281   -120  -1354       C  
ATOM   3005  O   VAL B 397      11.144  56.492  28.566  1.00 39.01           O  
ANISOU 3005  O   VAL B 397     4523   5210   5090    272    -65  -1292       O  
ATOM   3006  CB  VAL B 397       8.956  54.449  29.345  1.00 36.38           C  
ANISOU 3006  CB  VAL B 397     4188   4691   4944    236   -176  -1285       C  
ATOM   3007  CG1 VAL B 397       8.955  53.651  28.051  1.00 31.40           C  
ANISOU 3007  CG1 VAL B 397     3493   4102   4336    259   -204  -1441       C  
ATOM   3008  CG2 VAL B 397       8.089  53.766  30.385  1.00 33.83           C  
ANISOU 3008  CG2 VAL B 397     3883   4251   4720    207   -218  -1203       C  
ATOM   3009  N   LEU B 398      12.105  54.496  28.161  1.00 42.67           N  
ANISOU 3009  N   LEU B 398     4907   5590   5715    315   -144  -1480       N  
ATOM   3010  CA  LEU B 398      12.989  54.999  27.122  1.00 33.15           C  
ANISOU 3010  CA  LEU B 398     3659   4513   4422    343    -98  -1551       C  
ATOM   3011  C   LEU B 398      12.185  55.462  25.911  1.00 37.92           C  
ANISOU 3011  C   LEU B 398     4244   5253   4910    347    -64  -1580       C  
ATOM   3012  O   LEU B 398      11.375  54.709  25.376  1.00 46.15           O  
ANISOU 3012  O   LEU B 398     5262   6294   5978    354   -103  -1656       O  
ATOM   3013  CB  LEU B 398      13.998  53.920  26.721  1.00 32.49           C  
ANISOU 3013  CB  LEU B 398     3514   4409   4422    388   -138  -1692       C  
ATOM   3014  CG  LEU B 398      15.192  54.331  25.858  1.00 36.89           C  
ANISOU 3014  CG  LEU B 398     4019   5091   4906    415    -93  -1731       C  
ATOM   3015  CD1 LEU B 398      15.984  55.428  26.544  1.00 28.86           C  
ANISOU 3015  CD1 LEU B 398     3031   4082   3853    402    -41  -1648       C  
ATOM   3016  CD2 LEU B 398      16.078  53.128  25.581  1.00 29.47           C  
ANISOU 3016  CD2 LEU B 398     3021   4117   4061    448   -149  -1823       C  
ATOM   3017  N   ASP B 399      12.405  56.707  25.495  1.00 32.20           N  
ANISOU 3017  N   ASP B 399     3528   4641   4064    341      5  -1515       N  
ATOM   3018  CA  ASP B 399      11.699  57.268  24.348  1.00 39.07           C  
ANISOU 3018  CA  ASP B 399     4381   5653   4811    348     43  -1525       C  
ATOM   3019  C   ASP B 399      12.519  57.104  23.066  1.00 46.16           C  
ANISOU 3019  C   ASP B 399     5207   6679   5651    385     62  -1603       C  
ATOM   3020  O   ASP B 399      13.644  56.604  23.103  1.00 47.01           O  
ANISOU 3020  O   ASP B 399     5279   6767   5815    404     49  -1653       O  
ATOM   3021  CB  ASP B 399      11.375  58.748  24.587  1.00 31.39           C  
ANISOU 3021  CB  ASP B 399     3458   4723   3745    317    102  -1378       C  
ATOM   3022  CG  ASP B 399       9.964  59.108  24.164  1.00 35.67           C  
ANISOU 3022  CG  ASP B 399     4021   5318   4215    305    106  -1342       C  
ATOM   3023  OD1 ASP B 399       9.458  58.490  23.206  1.00 35.11           O  
ANISOU 3023  OD1 ASP B 399     3908   5317   4116    330     87  -1440       O  
ATOM   3024  OD2 ASP B 399       9.351  59.996  24.794  1.00 36.66           O1-
ANISOU 3024  OD2 ASP B 399     4202   5415   4313    276    124  -1222       O1-
ATOM   3025  N   SER B 400      11.944  57.525  21.943  1.00 45.57           N  
ANISOU 3025  N   SER B 400     5113   6735   5468    392     86  -1589       N  
ATOM   3026  CA  SER B 400      12.586  57.399  20.641  1.00 43.03           C  
ANISOU 3026  CA  SER B 400     4723   6546   5080    426     98  -1636       C  
ATOM   3027  C   SER B 400      13.949  58.086  20.604  1.00 46.38           C  
ANISOU 3027  C   SER B 400     5126   7026   5469    429    156  -1595       C  
ATOM   3028  O   SER B 400      14.895  57.576  20.007  1.00 48.59           O  
ANISOU 3028  O   SER B 400     5347   7360   5755    459    148  -1662       O  
ATOM   3029  CB  SER B 400      11.689  57.989  19.549  1.00 42.89           C  
ANISOU 3029  CB  SER B 400     4698   6660   4938    432    121  -1597       C  
ATOM   3030  OG  SER B 400      10.323  57.935  19.924  1.00 49.85           O  
ANISOU 3030  OG  SER B 400     5621   7486   5834    412     94  -1581       O  
ATOM   3031  N   ASP B 401      14.046  59.236  21.261  1.00 39.25           N  
ANISOU 3031  N   ASP B 401     4265   6111   4535    398    211  -1488       N  
ATOM   3032  CA  ASP B 401      15.231  60.073  21.137  1.00 30.75           C  
ANISOU 3032  CA  ASP B 401     3160   5102   3422    395    275  -1434       C  
ATOM   3033  C   ASP B 401      16.284  59.809  22.216  1.00 35.50           C  
ANISOU 3033  C   ASP B 401     3761   5596   4131    392    264  -1463       C  
ATOM   3034  O   ASP B 401      17.200  60.607  22.399  1.00 41.81           O  
ANISOU 3034  O   ASP B 401     4540   6427   4920    382    317  -1412       O  
ATOM   3035  CB  ASP B 401      14.819  61.548  21.148  1.00 31.52           C  
ANISOU 3035  CB  ASP B 401     3290   5255   3433    365    341  -1300       C  
ATOM   3036  CG  ASP B 401      14.190  61.980  22.463  1.00 43.63           C  
ANISOU 3036  CG  ASP B 401     4901   6651   5025    329    323  -1229       C  
ATOM   3037  OD1 ASP B 401      13.983  61.117  23.347  1.00 39.43           O  
ANISOU 3037  OD1 ASP B 401     4400   5988   4592    326    263  -1276       O  
ATOM   3038  OD2 ASP B 401      13.895  63.184  22.610  1.00 43.56           O1-
ANISOU 3038  OD2 ASP B 401     4928   6650   4974    298    358  -1102       O1-
ATOM   3039  N   GLY B 402      16.154  58.694  22.929  1.00 33.67           N  
ANISOU 3039  N   GLY B 402     3547   5236   4010    401    194  -1539       N  
ATOM   3040  CA  GLY B 402      17.122  58.331  23.951  1.00 31.02           C  
ANISOU 3040  CA  GLY B 402     3212   4790   3784    404    170  -1566       C  
ATOM   3041  C   GLY B 402      16.881  58.986  25.300  1.00 36.58           C  
ANISOU 3041  C   GLY B 402     3993   5368   4539    360    161  -1445       C  
ATOM   3042  O   GLY B 402      17.536  58.648  26.288  1.00 42.29           O  
ANISOU 3042  O   GLY B 402     4729   5980   5357    358    125  -1444       O  
ATOM   3043  N   SER B 403      15.953  59.933  25.346  1.00 39.12           N  
ANISOU 3043  N   SER B 403     4363   5708   4792    328    187  -1340       N  
ATOM   3044  CA  SER B 403      15.545  60.522  26.616  1.00 39.59           C  
ANISOU 3044  CA  SER B 403     4498   5654   4893    293    169  -1230       C  
ATOM   3045  C   SER B 403      14.466  59.654  27.249  1.00 37.98           C  
ANISOU 3045  C   SER B 403     4336   5352   4742    291    111  -1243       C  
ATOM   3046  O   SER B 403      13.917  58.762  26.603  1.00 37.43           O  
ANISOU 3046  O   SER B 403     4240   5304   4676    309     87  -1328       O  
ATOM   3047  CB  SER B 403      15.033  61.949  26.422  1.00 33.50           C  
ANISOU 3047  CB  SER B 403     3756   4939   4033    265    218  -1114       C  
ATOM   3048  OG  SER B 403      13.720  61.943  25.896  1.00 35.33           O  
ANISOU 3048  OG  SER B 403     4007   5216   4199    264    220  -1105       O  
ATOM   3049  N   PHE B 404      14.155  59.920  28.511  1.00 29.47           N  
ANISOU 3049  N   PHE B 404     3319   4171   3708    271     86  -1159       N  
ATOM   3050  CA  PHE B 404      13.133  59.149  29.207  1.00 27.41           C  
ANISOU 3050  CA  PHE B 404     3094   3821   3500    266     37  -1148       C  
ATOM   3051  C   PHE B 404      11.862  59.954  29.420  1.00 30.30           C  
ANISOU 3051  C   PHE B 404     3510   4204   3799    243     54  -1053       C  
ATOM   3052  O   PHE B 404      11.878  61.185  29.384  1.00 32.43           O  
ANISOU 3052  O   PHE B 404     3801   4521   4002    232     94   -982       O  
ATOM   3053  CB  PHE B 404      13.654  58.648  30.555  1.00 33.09           C  
ANISOU 3053  CB  PHE B 404     3839   4418   4318    270     -8  -1123       C  
ATOM   3054  CG  PHE B 404      14.700  57.579  30.442  1.00 36.62           C  
ANISOU 3054  CG  PHE B 404     4237   4826   4852    297    -42  -1222       C  
ATOM   3055  CD1 PHE B 404      16.041  57.911  30.328  1.00 33.63           C  
ANISOU 3055  CD1 PHE B 404     3826   4475   4477    312    -23  -1252       C  
ATOM   3056  CD2 PHE B 404      14.345  56.240  30.465  1.00 29.51           C  
ANISOU 3056  CD2 PHE B 404     3318   3854   4038    309    -96  -1285       C  
ATOM   3057  CE1 PHE B 404      17.007  56.927  30.233  1.00 30.64           C  
ANISOU 3057  CE1 PHE B 404     3400   4063   4179    343    -56  -1348       C  
ATOM   3058  CE2 PHE B 404      15.308  55.251  30.372  1.00 30.61           C  
ANISOU 3058  CE2 PHE B 404     3413   3950   4268    340   -133  -1381       C  
ATOM   3059  CZ  PHE B 404      16.640  55.596  30.253  1.00 26.97           C  
ANISOU 3059  CZ  PHE B 404     2921   3526   3800    359   -112  -1416       C  
ATOM   3060  N   PHE B 405      10.761  59.245  29.634  1.00 32.49           N  
ANISOU 3060  N   PHE B 405     3800   4439   4105    236     22  -1053       N  
ATOM   3061  CA  PHE B 405       9.521  59.876  30.048  1.00 26.49           C  
ANISOU 3061  CA  PHE B 405     3085   3683   3296    218     30   -961       C  
ATOM   3062  C   PHE B 405       8.819  58.997  31.076  1.00 26.99           C  
ANISOU 3062  C   PHE B 405     3169   3647   3440    209    -16   -928       C  
ATOM   3063  O   PHE B 405       9.146  57.819  31.229  1.00 22.64           O  
ANISOU 3063  O   PHE B 405     2591   3026   2984    215    -58   -983       O  
ATOM   3064  CB  PHE B 405       8.604  60.142  28.850  1.00 28.29           C  
ANISOU 3064  CB  PHE B 405     3295   4012   3442    214     55   -985       C  
ATOM   3065  CG  PHE B 405       7.863  58.927  28.366  1.00 29.68           C  
ANISOU 3065  CG  PHE B 405     3436   4175   3666    215     15  -1064       C  
ATOM   3066  CD1 PHE B 405       6.596  58.633  28.847  1.00 28.52           C  
ANISOU 3066  CD1 PHE B 405     3308   3986   3542    196     -8  -1017       C  
ATOM   3067  CD2 PHE B 405       8.428  58.082  27.426  1.00 27.84           C  
ANISOU 3067  CD2 PHE B 405     3146   3973   3461    237     -1  -1189       C  
ATOM   3068  CE1 PHE B 405       5.912  57.519  28.405  1.00 32.96           C  
ANISOU 3068  CE1 PHE B 405     3831   4525   4167    191    -51  -1090       C  
ATOM   3069  CE2 PHE B 405       7.748  56.965  26.980  1.00 21.23           C  
ANISOU 3069  CE2 PHE B 405     2273   3113   2682    240    -48  -1274       C  
ATOM   3070  CZ  PHE B 405       6.488  56.683  27.469  1.00 27.03           C  
ANISOU 3070  CZ  PHE B 405     3025   3794   3452    213    -75  -1223       C  
ATOM   3071  N   LEU B 406       7.868  59.580  31.792  1.00 27.32           N  
ANISOU 3071  N   LEU B 406     3253   3683   3444    198    -10   -832       N  
ATOM   3072  CA  LEU B 406       6.992  58.799  32.649  1.00 29.55           C  
ANISOU 3072  CA  LEU B 406     3545   3896   3787    187    -44   -784       C  
ATOM   3073  C   LEU B 406       5.653  59.491  32.807  1.00 31.82           C  
ANISOU 3073  C   LEU B 406     3858   4228   4003    176    -24   -708       C  
ATOM   3074  O   LEU B 406       5.465  60.622  32.355  1.00 31.43           O  
ANISOU 3074  O   LEU B 406     3827   4253   3861    181     12   -689       O  
ATOM   3075  CB  LEU B 406       7.628  58.549  34.025  1.00 23.97           C  
ANISOU 3075  CB  LEU B 406     2863   3106   3139    200    -69   -729       C  
ATOM   3076  CG  LEU B 406       8.143  59.671  34.933  1.00 23.39           C  
ANISOU 3076  CG  LEU B 406     2833   3041   3010    219    -53   -664       C  
ATOM   3077  CD1 LEU B 406       7.033  60.542  35.507  1.00 14.80           C  
ANISOU 3077  CD1 LEU B 406     1785   1992   1848    220    -35   -574       C  
ATOM   3078  CD2 LEU B 406       8.955  59.062  36.064  1.00 16.71           C  
ANISOU 3078  CD2 LEU B 406     1995   2117   2238    238    -90   -643       C  
ATOM   3079  N   TYR B 407       4.724  58.791  33.441  1.00 22.15           N  
ANISOU 3079  N   TYR B 407     2630   2958   2827    162    -48   -659       N  
ATOM   3080  CA  TYR B 407       3.476  59.387  33.875  1.00 26.49           C  
ANISOU 3080  CA  TYR B 407     3203   3546   3317    157    -31   -574       C  
ATOM   3081  C   TYR B 407       3.289  59.153  35.370  1.00 28.58           C  
ANISOU 3081  C   TYR B 407     3489   3757   3613    164    -45   -476       C  
ATOM   3082  O   TYR B 407       3.622  58.088  35.892  1.00 21.93           O  
ANISOU 3082  O   TYR B 407     2628   2837   2867    158    -78   -469       O  
ATOM   3083  CB  TYR B 407       2.288  58.801  33.110  1.00 28.44           C  
ANISOU 3083  CB  TYR B 407     3411   3814   3581    132    -40   -601       C  
ATOM   3084  CG  TYR B 407       2.145  59.249  31.670  1.00 33.86           C  
ANISOU 3084  CG  TYR B 407     4078   4587   4199    134    -22   -680       C  
ATOM   3085  CD1 TYR B 407       2.891  58.661  30.656  1.00 33.27           C  
ANISOU 3085  CD1 TYR B 407     3966   4519   4155    139    -35   -793       C  
ATOM   3086  CD2 TYR B 407       1.236  60.241  31.319  1.00 34.47           C  
ANISOU 3086  CD2 TYR B 407     4172   4748   4177    137      8   -642       C  
ATOM   3087  CE1 TYR B 407       2.743  59.061  29.335  1.00 33.23           C  
ANISOU 3087  CE1 TYR B 407     3940   4613   4075    148    -16   -860       C  
ATOM   3088  CE2 TYR B 407       1.084  60.645  30.004  1.00 30.68           C  
ANISOU 3088  CE2 TYR B 407     3672   4355   3628    144     25   -703       C  
ATOM   3089  CZ  TYR B 407       1.838  60.054  29.017  1.00 33.46           C  
ANISOU 3089  CZ  TYR B 407     3987   4723   4002    150     14   -809       C  
ATOM   3090  OH  TYR B 407       1.679  60.462  27.712  1.00 28.78           O  
ANISOU 3090  OH  TYR B 407     3371   4237   3326    164     33   -865       O  
ATOM   3091  N   SER B 408       2.755  60.150  36.060  1.00 23.27           N  
ANISOU 3091  N   SER B 408     2852   3130   2857    182    -23   -399       N  
ATOM   3092  CA  SER B 408       2.333  59.954  37.436  1.00 26.98           C  
ANISOU 3092  CA  SER B 408     3336   3581   3335    196    -31   -301       C  
ATOM   3093  C   SER B 408       0.829  60.168  37.531  1.00 22.87           C  
ANISOU 3093  C   SER B 408     2806   3114   2768    186    -14   -238       C  
ATOM   3094  O   SER B 408       0.295  61.131  36.986  1.00 26.51           O  
ANISOU 3094  O   SER B 408     3281   3643   3148    193     10   -250       O  
ATOM   3095  CB  SER B 408       3.076  60.894  38.382  1.00 21.83           C  
ANISOU 3095  CB  SER B 408     2729   2941   2626    239    -28   -271       C  
ATOM   3096  OG  SER B 408       2.728  60.621  39.726  1.00 20.25           O  
ANISOU 3096  OG  SER B 408     2536   2734   2422    262    -38   -179       O  
ATOM   3097  N   LYS B 409       0.143  59.257  38.208  1.00 25.36           N  
ANISOU 3097  N   LYS B 409     3094   3401   3141    170    -26   -167       N  
ATOM   3098  CA  LYS B 409      -1.308  59.338  38.298  1.00 21.92           C  
ANISOU 3098  CA  LYS B 409     2637   3019   2675    157    -10   -104       C  
ATOM   3099  C   LYS B 409      -1.773  59.570  39.728  1.00 29.32           C  
ANISOU 3099  C   LYS B 409     3585   3990   3563    189      3     13       C  
ATOM   3100  O   LYS B 409      -1.533  58.750  40.608  1.00 16.34           O  
ANISOU 3100  O   LYS B 409     1928   2301   1979    188    -12     80       O  
ATOM   3101  CB  LYS B 409      -1.953  58.068  37.735  1.00 21.05           C  
ANISOU 3101  CB  LYS B 409     2465   2856   2676    105    -33   -117       C  
ATOM   3102  CG  LYS B 409      -3.474  58.083  37.755  1.00 21.58           C  
ANISOU 3102  CG  LYS B 409     2498   2977   2724     85    -18    -55       C  
ATOM   3103  CD  LYS B 409      -4.049  56.910  36.978  1.00 26.52           C  
ANISOU 3103  CD  LYS B 409     3059   3547   3472     30    -49    -95       C  
ATOM   3104  CE  LYS B 409      -3.800  55.590  37.689  1.00 24.62           C  
ANISOU 3104  CE  LYS B 409     2782   3201   3373      2    -82    -36       C  
ATOM   3105  NZ  LYS B 409      -4.628  55.442  38.916  1.00 19.13           N1+
ANISOU 3105  NZ  LYS B 409     2067   2528   2674     -1    -62    119       N1+
ATOM   3106  N   LEU B 410      -2.439  60.699  39.948  1.00 25.32           N  
ANISOU 3106  N   LEU B 410     3102   3571   2947    222     30     39       N  
ATOM   3107  CA  LEU B 410      -3.038  60.991  41.239  1.00 28.94           C  
ANISOU 3107  CA  LEU B 410     3565   4090   3342    261     44    142       C  
ATOM   3108  C   LEU B 410      -4.538  60.738  41.201  1.00 34.46           C  
ANISOU 3108  C   LEU B 410     4216   4841   4034    238     64    206       C  
ATOM   3109  O   LEU B 410      -5.232  61.198  40.290  1.00 31.44           O  
ANISOU 3109  O   LEU B 410     3826   4496   3624    223     75    162       O  
ATOM   3110  CB  LEU B 410      -2.756  62.436  41.652  1.00 29.14           C  
ANISOU 3110  CB  LEU B 410     3643   4177   3252    325     53    122       C  
ATOM   3111  CG  LEU B 410      -3.487  62.887  42.918  1.00 25.17           C  
ANISOU 3111  CG  LEU B 410     3141   3760   2662    381     68    209       C  
ATOM   3112  CD1 LEU B 410      -2.992  62.118  44.138  1.00 19.78           C  
ANISOU 3112  CD1 LEU B 410     2451   3062   2003    402     56    285       C  
ATOM   3113  CD2 LEU B 410      -3.353  64.386  43.126  1.00 26.00           C  
ANISOU 3113  CD2 LEU B 410     3294   3920   2665    445     68    166       C  
ATOM   3114  N   THR B 411      -5.035  59.996  42.187  1.00 36.00           N  
ANISOU 3114  N   THR B 411     4375   5045   4258    234     69    317       N  
ATOM   3115  CA  THR B 411      -6.463  59.722  42.281  1.00 33.63           C  
ANISOU 3115  CA  THR B 411     4020   4801   3958    211     91    395       C  
ATOM   3116  C   THR B 411      -7.089  60.543  43.405  1.00 36.26           C  
ANISOU 3116  C   THR B 411     4361   5252   4165    276    122    477       C  
ATOM   3117  O   THR B 411      -6.662  60.469  44.558  1.00 45.53           O  
ANISOU 3117  O   THR B 411     5545   6448   5305    320    124    545       O  
ATOM   3118  CB  THR B 411      -6.747  58.224  42.523  1.00 28.82           C  
ANISOU 3118  CB  THR B 411     3345   4120   3486    151     77    477       C  
ATOM   3119  CG2 THR B 411      -8.247  57.961  42.515  1.00 22.95           C  
ANISOU 3119  CG2 THR B 411     2533   3431   2755    118    100    554       C  
ATOM   3120  OG1 THR B 411      -6.133  57.444  41.491  1.00 29.33           O  
ANISOU 3120  OG1 THR B 411     3400   4072   3673    100     40    384       O  
ATOM   3121  N   VAL B 412      -8.097  61.338  43.065  1.00 34.94           N  
ANISOU 3121  N   VAL B 412     4186   5168   3923    291    144    465       N  
ATOM   3122  CA  VAL B 412      -8.812  62.126  44.058  1.00 35.22           C  
ANISOU 3122  CA  VAL B 412     4220   5327   3837    359    172    531       C  
ATOM   3123  C   VAL B 412     -10.312  61.892  43.936  1.00 37.63           C  
ANISOU 3123  C   VAL B 412     4456   5702   4141    332    200    597       C  
ATOM   3124  O   VAL B 412     -10.794  61.437  42.899  1.00 36.66           O  
ANISOU 3124  O   VAL B 412     4298   5534   4095    268    192    561       O  
ATOM   3125  CB  VAL B 412      -8.523  63.636  43.914  1.00 27.54           C  
ANISOU 3125  CB  VAL B 412     3311   4400   2754    427    168    443       C  
ATOM   3126  CG1 VAL B 412      -7.023  63.900  43.910  1.00 26.74           C  
ANISOU 3126  CG1 VAL B 412     3271   4223   2668    445    139    371       C  
ATOM   3127  CG2 VAL B 412      -9.165  64.181  42.650  1.00 17.41           C  
ANISOU 3127  CG2 VAL B 412     2026   3122   1466    402    170    372       C  
ATOM   3128  N   ASP B 413     -11.046  62.188  45.003  1.00 40.55           N  
ANISOU 3128  N   ASP B 413     4798   6186   4422    385    230    689       N  
ATOM   3129  CA  ASP B 413     -12.499  62.186  44.936  1.00 37.04           C  
ANISOU 3129  CA  ASP B 413     4286   5830   3957    372    261    747       C  
ATOM   3130  C   ASP B 413     -12.933  63.240  43.934  1.00 30.38           C  
ANISOU 3130  C   ASP B 413     3470   5012   3061    388    255    640       C  
ATOM   3131  O   ASP B 413     -12.366  64.334  43.900  1.00 33.71           O  
ANISOU 3131  O   ASP B 413     3960   5446   3403    449    243    562       O  
ATOM   3132  CB  ASP B 413     -13.121  62.461  46.306  1.00 34.30           C  
ANISOU 3132  CB  ASP B 413     3908   5624   3501    443    298    857       C  
ATOM   3133  CG  ASP B 413     -12.995  61.283  47.251  1.00 46.32           C  
ANISOU 3133  CG  ASP B 413     5380   7139   5081    418    312    999       C  
ATOM   3134  OD1 ASP B 413     -12.977  60.131  46.765  1.00 53.92           O  
ANISOU 3134  OD1 ASP B 413     6301   7996   6191    327    299   1034       O  
ATOM   3135  OD2 ASP B 413     -12.920  61.508  48.479  1.00 49.37           O1-
ANISOU 3135  OD2 ASP B 413     5765   7627   5368    492    332   1074       O1-
ATOM   3136  N   LYS B 414     -13.923  62.909  43.110  1.00 29.92           N  
ANISOU 3136  N   LYS B 414     3356   4958   3054    333    259    638       N  
ATOM   3137  CA  LYS B 414     -14.435  63.848  42.117  1.00 28.24           C  
ANISOU 3137  CA  LYS B 414     3162   4777   2791    349    253    548       C  
ATOM   3138  C   LYS B 414     -14.859  65.159  42.765  1.00 31.67           C  
ANISOU 3138  C   LYS B 414     3623   5327   3083    446    270    547       C  
ATOM   3139  O   LYS B 414     -14.603  66.235  42.229  1.00 28.75           O  
ANISOU 3139  O   LYS B 414     3310   4956   2658    487    254    460       O  
ATOM   3140  CB  LYS B 414     -15.613  63.238  41.352  1.00 31.33           C  
ANISOU 3140  CB  LYS B 414     3474   5181   3250    284    256    562       C  
ATOM   3141  CG  LYS B 414     -16.331  64.229  40.446  1.00 30.91           C  
ANISOU 3141  CG  LYS B 414     3429   5185   3130    310    252    487       C  
ATOM   3142  CD  LYS B 414     -17.220  63.524  39.436  1.00 39.80           C  
ANISOU 3142  CD  LYS B 414     4484   6297   4343    238    239    469       C  
ATOM   3143  CE  LYS B 414     -18.401  62.842  40.108  1.00 37.60           C  
ANISOU 3143  CE  LYS B 414     4105   6081   4099    210    265    582       C  
ATOM   3144  NZ  LYS B 414     -19.264  62.129  39.122  1.00 43.49           N1+
ANISOU 3144  NZ  LYS B 414     4774   6806   4945    136    244    556       N1+
ATOM   3145  N   SER B 415     -15.494  65.054  43.929  1.00 32.10           N  
ANISOU 3145  N   SER B 415     3631   5482   3082    486    302    647       N  
ATOM   3146  CA  SER B 415     -15.975  66.219  44.664  1.00 36.73           C  
ANISOU 3146  CA  SER B 415     4231   6193   3531    589    316    644       C  
ATOM   3147  C   SER B 415     -14.855  67.217  44.951  1.00 38.38           C  
ANISOU 3147  C   SER B 415     4529   6343   3709    653    279    550       C  
ATOM   3148  O   SER B 415     -15.034  68.423  44.780  1.00 31.62           O  
ANISOU 3148  O   SER B 415     3703   5471   2839    700    253    463       O  
ATOM   3149  CB  SER B 415     -16.634  65.789  45.979  1.00 31.75           C  
ANISOU 3149  CB  SER B 415     3532   5659   2872    618    349    760       C  
ATOM   3150  OG  SER B 415     -15.674  65.307  46.901  1.00 34.14           O  
ANISOU 3150  OG  SER B 415     3857   5939   3178    633    347    808       O  
ATOM   3151  N   ARG B 416     -13.703  66.710  45.386  1.00 38.87           N  
ANISOU 3151  N   ARG B 416     4626   6362   3781    649    273    569       N  
ATOM   3152  CA  ARG B 416     -12.552  67.566  45.675  1.00 35.40           C  
ANISOU 3152  CA  ARG B 416     4262   5855   3334    700    234    478       C  
ATOM   3153  C   ARG B 416     -12.103  68.319  44.433  1.00 29.81           C  
ANISOU 3153  C   ARG B 416     3609   5072   2644    683    208    374       C  
ATOM   3154  O   ARG B 416     -11.680  69.472  44.508  1.00 26.41           O  
ANISOU 3154  O   ARG B 416     3224   4599   2212    729    176    295       O  
ATOM   3155  CB  ARG B 416     -11.390  66.746  46.243  1.00 35.05           C  
ANISOU 3155  CB  ARG B 416     4239   5773   3305    691    229    520       C  
ATOM   3156  CG  ARG B 416     -11.490  66.494  47.735  1.00 31.91           C  
ANISOU 3156  CG  ARG B 416     3810   5443   2873    743    240    594       C  
ATOM   3157  CD  ARG B 416     -10.153  66.697  48.419  1.00 35.02           C  
ANISOU 3157  CD  ARG B 416     4257   5791   3256    787    207    553       C  
ATOM   3158  NE  ARG B 416      -9.198  65.649  48.077  1.00 36.44           N  
ANISOU 3158  NE  ARG B 416     4454   5888   3505    727    200    586       N  
ATOM   3159  CZ  ARG B 416      -7.879  65.794  48.133  1.00 36.83           C  
ANISOU 3159  CZ  ARG B 416     4557   5857   3580    739    163    521       C  
ATOM   3160  NH1 ARG B 416      -7.086  64.786  47.805  1.00 33.71           N1+
ANISOU 3160  NH1 ARG B 416     4162   5354   3292    671    152    534       N1+
ATOM   3161  NH2 ARG B 416      -7.352  66.949  48.510  1.00 37.42           N  
ANISOU 3161  NH2 ARG B 416     4682   5955   3582    819    135    438       N  
ATOM   3162  N   TRP B 417     -12.208  67.655  43.288  1.00 25.58           N  
ANISOU 3162  N   TRP B 417     3057   4489   2172    603    214    369       N  
ATOM   3163  CA  TRP B 417     -11.871  68.272  42.013  1.00 27.61           C  
ANISOU 3163  CA  TRP B 417     3355   4684   2453    581    193    280       C  
ATOM   3164  C   TRP B 417     -12.901  69.328  41.633  1.00 30.56           C  
ANISOU 3164  C   TRP B 417     3724   5121   2768    623    194    255       C  
ATOM   3165  O   TRP B 417     -12.545  70.430  41.221  1.00 30.03           O  
ANISOU 3165  O   TRP B 417     3701   5000   2710    647    166    188       O  
ATOM   3166  CB  TRP B 417     -11.772  67.212  40.917  1.00 22.01           C  
ANISOU 3166  CB  TRP B 417     2618   3901   1844    485    192    267       C  
ATOM   3167  CG  TRP B 417     -11.544  67.771  39.545  1.00 20.53           C  
ANISOU 3167  CG  TRP B 417     2459   3675   1666    465    176    186       C  
ATOM   3168  CD1 TRP B 417     -12.456  67.860  38.537  1.00 18.48           C  
ANISOU 3168  CD1 TRP B 417     2170   3449   1404    442    179    166       C  
ATOM   3169  CD2 TRP B 417     -10.324  68.315  39.031  1.00 20.19           C  
ANISOU 3169  CD2 TRP B 417     2475   3562   1633    468    157    120       C  
ATOM   3170  CE2 TRP B 417     -10.572  68.714  37.703  1.00 26.68           C  
ANISOU 3170  CE2 TRP B 417     3299   4385   2452    447    153     72       C  
ATOM   3171  CE3 TRP B 417      -9.047  68.506  39.566  1.00 20.61           C  
ANISOU 3171  CE3 TRP B 417     2575   3558   1699    487    143    100       C  
ATOM   3172  NE1 TRP B 417     -11.882  68.424  37.423  1.00 23.08           N  
ANISOU 3172  NE1 TRP B 417     2790   3993   1985    434    164     97       N  
ATOM   3173  CZ2 TRP B 417      -9.588  69.292  36.902  1.00 19.16           C  
ANISOU 3173  CZ2 TRP B 417     2391   3382   1507    443    142     16       C  
ATOM   3174  CZ3 TRP B 417      -8.072  69.081  38.770  1.00 25.88           C  
ANISOU 3174  CZ3 TRP B 417     3284   4167   2383    479    129     38       C  
ATOM   3175  CH2 TRP B 417      -8.349  69.468  37.454  1.00 19.99           C  
ANISOU 3175  CH2 TRP B 417     2536   3427   1631    456    131      2       C  
ATOM   3176  N   GLN B 418     -14.176  68.982  41.785  1.00 28.13           N  
ANISOU 3176  N   GLN B 418     3350   4893   2446    617    217    309       N  
ATOM   3177  CA  GLN B 418     -15.275  69.879  41.446  1.00 29.20           C  
ANISOU 3177  CA  GLN B 418     3465   5059   2569    645    208    283       C  
ATOM   3178  C   GLN B 418     -15.259  71.160  42.272  1.00 36.12           C  
ANISOU 3178  C   GLN B 418     4369   5924   3432    724    183    246       C  
ATOM   3179  O   GLN B 418     -15.750  72.196  41.826  1.00 31.51           O  
ANISOU 3179  O   GLN B 418     3794   5333   2845    755    164    203       O  
ATOM   3180  CB  GLN B 418     -16.617  69.172  41.635  1.00 30.59           C  
ANISOU 3180  CB  GLN B 418     3556   5337   2730    627    241    358       C  
ATOM   3181  CG  GLN B 418     -16.837  67.950  40.759  1.00 46.29           C  
ANISOU 3181  CG  GLN B 418     5498   7321   4770    538    257    385       C  
ATOM   3182  CD  GLN B 418     -17.297  68.299  39.355  1.00 66.92           C  
ANISOU 3182  CD  GLN B 418     8109   9922   7394    513    239    319       C  
ATOM   3183  NE2 GLN B 418     -18.015  67.375  38.727  1.00 75.78           N  
ANISOU 3183  NE2 GLN B 418     9162  11044   8586    443    240    333       N  
ATOM   3184  OE1 GLN B 418     -17.017  69.383  38.842  1.00 71.33           O  
ANISOU 3184  OE1 GLN B 418     8725  10473   7906    557    221    257       O  
ATOM   3185  N   GLN B 419     -14.701  71.085  43.476  1.00 35.74           N  
ANISOU 3185  N   GLN B 419     4328   5879   3371    761    182    264       N  
ATOM   3186  CA  GLN B 419     -14.724  72.209  44.408  1.00 30.07           C  
ANISOU 3186  CA  GLN B 419     3622   5171   2632    846    158    226       C  
ATOM   3187  C   GLN B 419     -13.562  73.178  44.203  1.00 34.95           C  
ANISOU 3187  C   GLN B 419     4312   5699   3269    871    120    149       C  
ATOM   3188  O   GLN B 419     -13.412  74.138  44.957  1.00 30.99           O  
ANISOU 3188  O   GLN B 419     3824   5201   2751    945     93    108       O  
ATOM   3189  CB  GLN B 419     -14.731  71.687  45.848  1.00 30.02           C  
ANISOU 3189  CB  GLN B 419     3580   5230   2595    884    174    280       C  
ATOM   3190  CG  GLN B 419     -16.029  71.005  46.226  1.00 37.18           C  
ANISOU 3190  CG  GLN B 419     4404   6242   3479    878    211    363       C  
ATOM   3191  CD  GLN B 419     -15.905  70.131  47.457  1.00 37.26           C  
ANISOU 3191  CD  GLN B 419     4375   6314   3467    890    236    445       C  
ATOM   3192  NE2 GLN B 419     -16.914  69.301  47.696  1.00 28.42           N  
ANISOU 3192  NE2 GLN B 419     3178   5281   2338    865    274    541       N  
ATOM   3193  OE1 GLN B 419     -14.913  70.197  48.184  1.00 35.53           O  
ANISOU 3193  OE1 GLN B 419     4191   6068   3241    922    220    427       O  
ATOM   3194  N   GLY B 420     -12.747  72.923  43.188  1.00 24.40           N  
ANISOU 3194  N   GLY B 420     3016   4292   1963    813    115    129       N  
ATOM   3195  CA  GLY B 420     -11.702  73.852  42.822  1.00 24.54           C  
ANISOU 3195  CA  GLY B 420     3095   4229   2000    829     82     66       C  
ATOM   3196  C   GLY B 420     -10.404  73.704  43.591  1.00 26.10           C  
ANISOU 3196  C   GLY B 420     3327   4388   2201    847     65     48       C  
ATOM   3197  O   GLY B 420      -9.568  74.604  43.581  1.00 29.48           O  
ANISOU 3197  O   GLY B 420     3800   4762   2641    879     31     -7       O  
ATOM   3198  N   ASN B 421     -10.229  72.573  44.262  1.00 25.94           N  
ANISOU 3198  N   ASN B 421     3285   4400   2171    830     86     97       N  
ATOM   3199  CA  ASN B 421      -8.968  72.303  44.942  1.00 27.56           C  
ANISOU 3199  CA  ASN B 421     3521   4572   2378    846     69     84       C  
ATOM   3200  C   ASN B 421      -7.796  72.229  43.959  1.00 30.90           C  
ANISOU 3200  C   ASN B 421     3993   4915   2834    801     57     44       C  
ATOM   3201  O   ASN B 421      -7.886  71.589  42.911  1.00 24.26           O  
ANISOU 3201  O   ASN B 421     3147   4064   2009    738     79     59       O  
ATOM   3202  CB  ASN B 421      -9.061  71.006  45.757  1.00 24.01           C  
ANISOU 3202  CB  ASN B 421     3035   4177   1908    834     97    163       C  
ATOM   3203  CG  ASN B 421      -9.864  71.182  47.038  1.00 28.71           C  
ANISOU 3203  CG  ASN B 421     3585   4858   2465    898    104    196       C  
ATOM   3204  ND2 ASN B 421     -11.084  70.656  47.054  1.00 22.70           N  
ANISOU 3204  ND2 ASN B 421     2766   4169   1691    879    139    263       N  
ATOM   3205  OD1 ASN B 421      -9.387  71.781  48.005  1.00 34.71           O  
ANISOU 3205  OD1 ASN B 421     4357   5626   3205    967     78    159       O  
ATOM   3206  N   VAL B 422      -6.704  72.903  44.304  1.00 28.92           N  
ANISOU 3206  N   VAL B 422     3784   4613   2591    838     20    -11       N  
ATOM   3207  CA  VAL B 422      -5.526  72.935  43.451  1.00 25.78           C  
ANISOU 3207  CA  VAL B 422     3430   4143   2222    803      8    -53       C  
ATOM   3208  C   VAL B 422      -4.570  71.796  43.782  1.00 29.05           C  
ANISOU 3208  C   VAL B 422     3839   4518   2681    764     11    -36       C  
ATOM   3209  O   VAL B 422      -4.260  71.547  44.942  1.00 34.73           O  
ANISOU 3209  O   VAL B 422     4558   5267   3372    811     -3    -23       O  
ATOM   3210  CB  VAL B 422      -4.796  74.281  43.574  1.00 27.39           C  
ANISOU 3210  CB  VAL B 422     3675   4295   2437    855    -40   -123       C  
ATOM   3211  CG1 VAL B 422      -3.502  74.268  42.778  1.00 27.29           C  
ANISOU 3211  CG1 VAL B 422     3682   4177   2509    793    -50   -154       C  
ATOM   3212  CG2 VAL B 422      -5.702  75.394  43.091  1.00 28.22           C  
ANISOU 3212  CG2 VAL B 422     3778   4407   2539    877    -47   -134       C  
ATOM   3213  N   PHE B 423      -4.113  71.099  42.747  1.00 23.70           N  
ANISOU 3213  N   PHE B 423     3154   3776   2074    682     27    -37       N  
ATOM   3214  CA  PHE B 423      -3.198  69.979  42.922  1.00 22.25           C  
ANISOU 3214  CA  PHE B 423     2962   3542   1950    640     27    -27       C  
ATOM   3215  C   PHE B 423      -1.893  70.244  42.196  1.00 23.65           C  
ANISOU 3215  C   PHE B 423     3162   3630   2193    606     10    -87       C  
ATOM   3216  O   PHE B 423      -1.889  70.771  41.086  1.00 31.74           O  
ANISOU 3216  O   PHE B 423     4193   4632   3235    575     18   -114       O  
ATOM   3217  CB  PHE B 423      -3.840  68.683  42.432  1.00 17.45           C  
ANISOU 3217  CB  PHE B 423     2311   2942   1377    575     58     23       C  
ATOM   3218  CG  PHE B 423      -5.095  68.319  43.166  1.00 20.34           C  
ANISOU 3218  CG  PHE B 423     2642   3396   1689    600     79     97       C  
ATOM   3219  CD1 PHE B 423      -5.050  67.483  44.268  1.00 20.47           C  
ANISOU 3219  CD1 PHE B 423     2638   3437   1703    616     81    162       C  
ATOM   3220  CD2 PHE B 423      -6.322  68.822  42.762  1.00 27.90           C  
ANISOU 3220  CD2 PHE B 423     3583   4418   2599    609     97    108       C  
ATOM   3221  CE1 PHE B 423      -6.205  67.146  44.948  1.00 26.67           C  
ANISOU 3221  CE1 PHE B 423     3382   4314   2438    636    106    244       C  
ATOM   3222  CE2 PHE B 423      -7.480  68.490  43.438  1.00 17.37           C  
ANISOU 3222  CE2 PHE B 423     2208   3173   1217    631    119    179       C  
ATOM   3223  CZ  PHE B 423      -7.424  67.653  44.531  1.00 23.71           C  
ANISOU 3223  CZ  PHE B 423     2986   4005   2017    643    126    250       C  
ATOM   3224  N   SER B 424      -0.782  69.870  42.827  1.00 21.03           N  
ANISOU 3224  N   SER B 424     2839   3254   1897    613    -12   -103       N  
ATOM   3225  CA  SER B 424       0.530  70.152  42.265  1.00 21.02           C  
ANISOU 3225  CA  SER B 424     2853   3174   1961    586    -29   -159       C  
ATOM   3226  C   SER B 424       1.363  68.902  42.015  1.00 29.69           C  
ANISOU 3226  C   SER B 424     3932   4222   3128    534    -24   -161       C  
ATOM   3227  O   SER B 424       1.434  68.004  42.852  1.00 25.22           O  
ANISOU 3227  O   SER B 424     3354   3661   2568    546    -31   -127       O  
ATOM   3228  CB  SER B 424       1.303  71.106  43.176  1.00 20.63           C  
ANISOU 3228  CB  SER B 424     2830   3105   1904    648    -74   -200       C  
ATOM   3229  OG  SER B 424       0.754  72.409  43.124  1.00 38.72           O  
ANISOU 3229  OG  SER B 424     5139   5415   4157    689    -87   -220       O  
ATOM   3230  N   CYS B 425       1.995  68.859  40.848  1.00 29.19           N  
ANISOU 3230  N   CYS B 425     3861   4113   3116    482    -13   -199       N  
ATOM   3231  CA  CYS B 425       2.938  67.800  40.523  1.00 20.11           C  
ANISOU 3231  CA  CYS B 425     2691   2911   2037    441    -13   -222       C  
ATOM   3232  C   CYS B 425       4.360  68.327  40.667  1.00 21.58           C  
ANISOU 3232  C   CYS B 425     2890   3046   2265    451    -38   -270       C  
ATOM   3233  O   CYS B 425       4.797  69.175  39.895  1.00 30.10           O  
ANISOU 3233  O   CYS B 425     3972   4110   3356    435    -32   -300       O  
ATOM   3234  CB  CYS B 425       2.683  67.276  39.104  1.00 20.88           C  
ANISOU 3234  CB  CYS B 425     2762   3011   2162    382     16   -240       C  
ATOM   3235  SG  CYS B 425       3.870  66.042  38.533  1.00 29.40           S  
ANISOU 3235  SG  CYS B 425     3811   4030   3330    339     12   -290       S  
ATOM   3236  N   SER B 426       5.074  67.831  41.674  1.00 20.22           N  
ANISOU 3236  N   SER B 426     2719   2848   2115    477    -67   -272       N  
ATOM   3237  CA  SER B 426       6.444  68.260  41.914  1.00 23.25           C  
ANISOU 3237  CA  SER B 426     3107   3182   2544    489    -97   -322       C  
ATOM   3238  C   SER B 426       7.431  67.253  41.330  1.00 24.04           C  
ANISOU 3238  C   SER B 426     3179   3235   2719    446    -92   -352       C  
ATOM   3239  O   SER B 426       7.318  66.048  41.558  1.00 27.22           O  
ANISOU 3239  O   SER B 426     3568   3629   3146    437    -93   -331       O  
ATOM   3240  CB  SER B 426       6.697  68.448  43.411  1.00 22.03           C  
ANISOU 3240  CB  SER B 426     2970   3037   2362    557   -140   -317       C  
ATOM   3241  OG  SER B 426       5.790  69.385  43.963  1.00 29.58           O  
ANISOU 3241  OG  SER B 426     3948   4045   3245    607   -148   -301       O  
ATOM   3242  N   VAL B 427       8.394  67.754  40.567  1.00 26.21           N  
ANISOU 3242  N   VAL B 427     3442   3480   3036    420    -88   -399       N  
ATOM   3243  CA  VAL B 427       9.377  66.895  39.933  1.00 25.76           C  
ANISOU 3243  CA  VAL B 427     3353   3390   3045    385    -82   -439       C  
ATOM   3244  C   VAL B 427      10.788  67.284  40.352  1.00 29.43           C  
ANISOU 3244  C   VAL B 427     3810   3812   3561    399   -113   -481       C  
ATOM   3245  O   VAL B 427      11.138  68.464  40.375  1.00 37.97           O  
ANISOU 3245  O   VAL B 427     4898   4885   4643    406   -122   -493       O  
ATOM   3246  CB  VAL B 427       9.253  66.946  38.399  1.00 16.52           C  
ANISOU 3246  CB  VAL B 427     2158   2244   1876    337    -38   -458       C  
ATOM   3247  CG1 VAL B 427      10.195  65.942  37.763  1.00 17.71           C  
ANISOU 3247  CG1 VAL B 427     2268   2372   2088    311    -33   -509       C  
ATOM   3248  CG2 VAL B 427       7.827  66.662  37.973  1.00 16.69           C  
ANISOU 3248  CG2 VAL B 427     2184   2311   1848    326    -14   -423       C  
ATOM   3249  N   MET B 428      11.592  66.282  40.695  1.00 30.04           N  
ANISOU 3249  N   MET B 428     3868   3856   3690    404   -133   -504       N  
ATOM   3250  CA  MET B 428      12.976  66.511  41.088  1.00 26.66           C  
ANISOU 3250  CA  MET B 428     3425   3388   3316    417   -165   -549       C  
ATOM   3251  C   MET B 428      13.955  65.756  40.188  1.00 17.16           C  
ANISOU 3251  C   MET B 428     2176   2165   2179    382   -149   -598       C  
ATOM   3252  O   MET B 428      13.876  64.538  40.040  1.00 18.12           O  
ANISOU 3252  O   MET B 428     2284   2276   2326    377   -148   -604       O  
ATOM   3253  CB  MET B 428      13.167  66.123  42.554  1.00 23.93           C  
ANISOU 3253  CB  MET B 428     3098   3029   2966    473   -216   -536       C  
ATOM   3254  CG  MET B 428      12.514  67.104  43.514  1.00 25.82           C  
ANISOU 3254  CG  MET B 428     3373   3298   3138    522   -240   -511       C  
ATOM   3255  SD  MET B 428      12.068  66.371  45.091  1.00 35.40           S  
ANISOU 3255  SD  MET B 428     4608   4542   4300    591   -277   -460       S  
ATOM   3256  CE  MET B 428      10.579  65.484  44.632  1.00 22.73           C  
ANISOU 3256  CE  MET B 428     3005   2971   2661    559   -227   -384       C  
ATOM   3257  N   HIS B 429      14.875  66.496  39.579  1.00 17.93           N  
ANISOU 3257  N   HIS B 429     2247   2258   2310    361   -138   -633       N  
ATOM   3258  CA  HIS B 429      15.806  65.936  38.603  1.00 20.29           C  
ANISOU 3258  CA  HIS B 429     2493   2557   2659    331   -115   -681       C  
ATOM   3259  C   HIS B 429      17.020  66.853  38.491  1.00 26.55           C  
ANISOU 3259  C   HIS B 429     3254   3336   3499    320   -120   -708       C  
ATOM   3260  O   HIS B 429      16.895  68.065  38.654  1.00 31.27           O  
ANISOU 3260  O   HIS B 429     3866   3929   4087    317   -125   -683       O  
ATOM   3261  CB  HIS B 429      15.120  65.765  37.245  1.00 20.06           C  
ANISOU 3261  CB  HIS B 429     2448   2581   2593    294    -60   -677       C  
ATOM   3262  CG  HIS B 429      15.981  65.130  36.197  1.00 24.60           C  
ANISOU 3262  CG  HIS B 429     2965   3177   3204    274    -34   -735       C  
ATOM   3263  CD2 HIS B 429      16.102  63.840  35.801  1.00 19.59           C  
ANISOU 3263  CD2 HIS B 429     2303   2541   2598    277    -36   -784       C  
ATOM   3264  ND1 HIS B 429      16.853  65.853  35.413  1.00 29.35           N  
ANISOU 3264  ND1 HIS B 429     3523   3809   3819    251     -3   -749       N  
ATOM   3265  CE1 HIS B 429      17.477  65.037  34.583  1.00 28.46           C  
ANISOU 3265  CE1 HIS B 429     3358   3727   3728    245     17   -806       C  
ATOM   3266  NE2 HIS B 429      17.038  63.810  34.796  1.00 27.72           N  
ANISOU 3266  NE2 HIS B 429     3275   3611   3647    263     -6   -836       N  
ATOM   3267  N   GLU B 430      18.189  66.281  38.214  1.00 29.99           N  
ANISOU 3267  N   GLU B 430     3641   3761   3995    314   -122   -759       N  
ATOM   3268  CA  GLU B 430      19.428  67.051  38.272  1.00 29.47           C  
ANISOU 3268  CA  GLU B 430     3535   3675   3988    305   -134   -783       C  
ATOM   3269  C   GLU B 430      19.527  68.117  37.182  1.00 32.29           C  
ANISOU 3269  C   GLU B 430     3860   4067   4340    259    -83   -756       C  
ATOM   3270  O   GLU B 430      20.217  69.124  37.354  1.00 34.24           O  
ANISOU 3270  O   GLU B 430     4085   4288   4636    245    -97   -750       O  
ATOM   3271  CB  GLU B 430      20.642  66.123  38.208  1.00 27.79           C  
ANISOU 3271  CB  GLU B 430     3270   3450   3839    313   -146   -845       C  
ATOM   3272  CG  GLU B 430      20.838  65.411  36.883  1.00 48.02           C  
ANISOU 3272  CG  GLU B 430     5783   6065   6399    288    -93   -876       C  
ATOM   3273  CD  GLU B 430      22.163  64.663  36.814  1.00 54.80           C  
ANISOU 3273  CD  GLU B 430     6580   6913   7327    300   -107   -945       C  
ATOM   3274  OE1 GLU B 430      23.206  65.315  36.584  1.00 60.10           O  
ANISOU 3274  OE1 GLU B 430     7200   7594   8042    283    -98   -959       O  
ATOM   3275  OE2 GLU B 430      22.162  63.427  36.989  1.00 47.14           O1-
ANISOU 3275  OE2 GLU B 430     5612   5923   6376    328   -130   -983       O1-
ATOM   3276  N   ALA B 431      18.826  67.914  36.072  1.00 30.57           N  
ANISOU 3276  N   ALA B 431     3638   3910   4069    235    -28   -736       N  
ATOM   3277  CA  ALA B 431      18.899  68.849  34.948  1.00 33.30           C  
ANISOU 3277  CA  ALA B 431     3949   4304   4400    194     25   -697       C  
ATOM   3278  C   ALA B 431      17.921  70.015  35.110  1.00 34.37           C  
ANISOU 3278  C   ALA B 431     4132   4428   4500    189     23   -631       C  
ATOM   3279  O   ALA B 431      17.793  70.856  34.215  1.00 36.89           O  
ANISOU 3279  O   ALA B 431     4430   4782   4804    157     65   -581       O  
ATOM   3280  CB  ALA B 431      18.642  68.126  33.641  1.00 20.52           C  
ANISOU 3280  CB  ALA B 431     2297   2770   2730    180     83   -712       C  
ATOM   3281  N   LEU B 432      17.236  70.059  36.251  1.00 30.53           N  
ANISOU 3281  N   LEU B 432     3704   3897   3999    225    -26   -628       N  
ATOM   3282  CA  LEU B 432      16.336  71.164  36.567  1.00 25.41           C  
ANISOU 3282  CA  LEU B 432     3101   3233   3322    232    -39   -579       C  
ATOM   3283  C   LEU B 432      17.018  72.178  37.470  1.00 26.05           C  
ANISOU 3283  C   LEU B 432     3182   3244   3473    245    -95   -590       C  
ATOM   3284  O   LEU B 432      17.836  71.815  38.310  1.00 25.23           O  
ANISOU 3284  O   LEU B 432     3069   3103   3416    268   -139   -638       O  
ATOM   3285  CB  LEU B 432      15.064  70.649  37.238  1.00 21.36           C  
ANISOU 3285  CB  LEU B 432     2646   2729   2740    269    -57   -570       C  
ATOM   3286  CG  LEU B 432      14.041  69.916  36.370  1.00 30.02           C  
ANISOU 3286  CG  LEU B 432     3749   3889   3769    256    -11   -552       C  
ATOM   3287  CD1 LEU B 432      13.036  69.182  37.246  1.00 31.68           C  
ANISOU 3287  CD1 LEU B 432     4003   4097   3936    291    -36   -546       C  
ATOM   3288  CD2 LEU B 432      13.331  70.880  35.441  1.00 24.80           C  
ANISOU 3288  CD2 LEU B 432     3092   3267   3066    233     27   -500       C  
ATOM   3289  N   HIS B 433      16.680  73.449  37.286  1.00 32.24           N  
ANISOU 3289  N   HIS B 433     3974   4007   4270    233    -97   -547       N  
ATOM   3290  CA  HIS B 433      17.136  74.500  38.185  1.00 26.84           C  
ANISOU 3290  CA  HIS B 433     3293   3247   3657    251   -162   -565       C  
ATOM   3291  C   HIS B 433      16.671  74.164  39.596  1.00 34.17           C  
ANISOU 3291  C   HIS B 433     4273   4160   4548    319   -224   -609       C  
ATOM   3292  O   HIS B 433      15.515  73.785  39.800  1.00 32.71           O  
ANISOU 3292  O   HIS B 433     4134   4015   4278    347   -214   -590       O  
ATOM   3293  CB  HIS B 433      16.600  75.862  37.741  1.00 27.76           C  
ANISOU 3293  CB  HIS B 433     3417   3338   3791    233   -159   -509       C  
ATOM   3294  CG  HIS B 433      17.253  77.029  38.418  1.00 43.23           C  
ANISOU 3294  CG  HIS B 433     5362   5207   5857    239   -227   -531       C  
ATOM   3295  CD2 HIS B 433      16.832  77.822  39.432  1.00 43.13           C  
ANISOU 3295  CD2 HIS B 433     5386   5140   5861    289   -299   -563       C  
ATOM   3296  ND1 HIS B 433      18.482  77.521  38.034  1.00 48.26           N  
ANISOU 3296  ND1 HIS B 433     5932   5801   6605    191   -227   -525       N  
ATOM   3297  CE1 HIS B 433      18.797  78.557  38.792  1.00 46.56           C  
ANISOU 3297  CE1 HIS B 433     5714   5496   6482    207   -302   -554       C  
ATOM   3298  NE2 HIS B 433      17.811  78.761  39.648  1.00 46.33           N  
ANISOU 3298  NE2 HIS B 433     5748   5460   6394    270   -349   -583       N  
ATOM   3299  N   ASN B 434      17.585  74.281  40.558  1.00 30.39           N  
ANISOU 3299  N   ASN B 434     3781   3633   4131    347   -287   -666       N  
ATOM   3300  CA  ASN B 434      17.334  73.909  41.949  1.00 30.93           C  
ANISOU 3300  CA  ASN B 434     3889   3702   4160    419   -348   -709       C  
ATOM   3301  C   ASN B 434      16.961  72.437  42.122  1.00 29.03           C  
ANISOU 3301  C   ASN B 434     3667   3514   3849    437   -323   -701       C  
ATOM   3302  O   ASN B 434      16.468  72.048  43.182  1.00 35.32           O  
ANISOU 3302  O   ASN B 434     4501   4330   4590    497   -358   -709       O  
ATOM   3303  CB  ASN B 434      16.219  74.769  42.557  1.00 23.85           C  
ANISOU 3303  CB  ASN B 434     3043   2807   3213    467   -380   -700       C  
ATOM   3304  CG  ASN B 434      16.525  76.248  42.510  1.00 28.97           C  
ANISOU 3304  CG  ASN B 434     3675   3387   3945    458   -421   -714       C  
ATOM   3305  ND2 ASN B 434      15.477  77.061  42.421  1.00 28.18           N  
ANISOU 3305  ND2 ASN B 434     3607   3288   3811    474   -423   -686       N  
ATOM   3306  OD1 ASN B 434      17.680  76.663  42.555  1.00 36.76           O  
ANISOU 3306  OD1 ASN B 434     4616   4315   5034    436   -454   -749       O  
ATOM   3307  N   HIS B 435      17.191  71.632  41.082  1.00 22.97           N  
ANISOU 3307  N   HIS B 435     2870   2770   3086    389   -263   -685       N  
ATOM   3308  CA  HIS B 435      16.767  70.225  41.043  1.00 18.13           C  
ANISOU 3308  CA  HIS B 435     2268   2194   2424    397   -239   -676       C  
ATOM   3309  C   HIS B 435      15.263  70.069  41.265  1.00 25.65           C  
ANISOU 3309  C   HIS B 435     3270   3186   3288    419   -225   -630       C  
ATOM   3310  O   HIS B 435      14.805  68.997  41.650  1.00 31.68           O  
ANISOU 3310  O   HIS B 435     4049   3970   4018    439   -224   -616       O  
ATOM   3311  CB  HIS B 435      17.514  69.391  42.091  1.00 22.55           C  
ANISOU 3311  CB  HIS B 435     2824   2734   3009    440   -289   -714       C  
ATOM   3312  CG  HIS B 435      18.997  69.322  41.886  1.00 27.42           C  
ANISOU 3312  CG  HIS B 435     3386   3319   3714    421   -302   -764       C  
ATOM   3313  CD2 HIS B 435      19.759  69.484  40.778  1.00 30.64           C  
ANISOU 3313  CD2 HIS B 435     3740   3727   4176    367   -262   -775       C  
ATOM   3314  ND1 HIS B 435      19.871  69.033  42.912  1.00 27.73           N  
ANISOU 3314  ND1 HIS B 435     3416   3330   3790    464   -363   -808       N  
ATOM   3315  CE1 HIS B 435      21.107  69.029  42.447  1.00 30.23           C  
ANISOU 3315  CE1 HIS B 435     3675   3625   4187    435   -361   -848       C  
ATOM   3316  NE2 HIS B 435      21.067  69.300  41.155  1.00 33.52           N  
ANISOU 3316  NE2 HIS B 435     4061   4061   4614    375   -298   -827       N  
ATOM   3317  N   TYR B 436      14.499  71.130  41.026  1.00 18.86           N  
ANISOU 3317  N   TYR B 436     2431   2335   2399    416   -216   -602       N  
ATOM   3318  CA  TYR B 436      13.089  71.125  41.392  1.00 20.48           C  
ANISOU 3318  CA  TYR B 436     2681   2581   2521    447   -211   -563       C  
ATOM   3319  C   TYR B 436      12.245  72.023  40.488  1.00 33.51           C  
ANISOU 3319  C   TYR B 436     4339   4250   4143    420   -176   -526       C  
ATOM   3320  O   TYR B 436      12.611  73.166  40.199  1.00 44.18           O  
ANISOU 3320  O   TYR B 436     5681   5568   5537    407   -186   -528       O  
ATOM   3321  CB  TYR B 436      12.930  71.554  42.862  1.00 21.73           C  
ANISOU 3321  CB  TYR B 436     2868   2735   2652    519   -274   -581       C  
ATOM   3322  CG  TYR B 436      11.514  71.490  43.401  1.00 24.04           C  
ANISOU 3322  CG  TYR B 436     3198   3083   2851    561   -269   -541       C  
ATOM   3323  CD1 TYR B 436      10.659  72.585  43.303  1.00 20.17           C  
ANISOU 3323  CD1 TYR B 436     2729   2607   2327    577   -271   -529       C  
ATOM   3324  CD2 TYR B 436      11.037  70.341  44.022  1.00 28.62           C  
ANISOU 3324  CD2 TYR B 436     3787   3703   3384    585   -264   -510       C  
ATOM   3325  CE1 TYR B 436       9.362  72.532  43.801  1.00 21.82           C  
ANISOU 3325  CE1 TYR B 436     2966   2876   2449    619   -264   -495       C  
ATOM   3326  CE2 TYR B 436       9.744  70.279  44.522  1.00 27.54           C  
ANISOU 3326  CE2 TYR B 436     3674   3625   3163    621   -255   -465       C  
ATOM   3327  CZ  TYR B 436       8.912  71.375  44.409  1.00 27.44           C  
ANISOU 3327  CZ  TYR B 436     3681   3635   3111    639   -254   -461       C  
ATOM   3328  OH  TYR B 436       7.631  71.306  44.909  1.00 31.04           O  
ANISOU 3328  OH  TYR B 436     4153   4159   3481    678   -243   -418       O  
ATOM   3329  N   THR B 437      11.117  71.485  40.036  1.00 25.34           N  
ANISOU 3329  N   THR B 437     3318   3265   3043    412   -137   -488       N  
ATOM   3330  CA  THR B 437      10.094  72.290  39.393  1.00 23.84           C  
ANISOU 3330  CA  THR B 437     3143   3104   2811    403   -111   -450       C  
ATOM   3331  C   THR B 437       8.731  71.768  39.799  1.00 20.76           C  
ANISOU 3331  C   THR B 437     2781   2766   2343    431   -103   -419       C  
ATOM   3332  O   THR B 437       8.614  70.660  40.312  1.00 28.21           O  
ANISOU 3332  O   THR B 437     3723   3723   3273    441   -105   -418       O  
ATOM   3333  CB  THR B 437      10.225  72.291  37.859  1.00 29.63           C  
ANISOU 3333  CB  THR B 437     3845   3859   3553    344    -56   -431       C  
ATOM   3334  CG2 THR B 437       9.787  70.960  37.278  1.00 18.75           C  
ANISOU 3334  CG2 THR B 437     2454   2528   2141    323    -20   -432       C  
ATOM   3335  OG1 THR B 437       9.418  73.340  37.305  1.00 35.70           O  
ANISOU 3335  OG1 THR B 437     4628   4645   4292    341    -42   -389       O  
ATOM   3336  N   GLN B 438       7.700  72.569  39.572  1.00 23.33           N  
ANISOU 3336  N   GLN B 438     3125   3118   2621    443    -94   -390       N  
ATOM   3337  CA  GLN B 438       6.354  72.195  39.976  1.00 21.77           C  
ANISOU 3337  CA  GLN B 438     2946   2976   2349    472    -86   -358       C  
ATOM   3338  C   GLN B 438       5.309  72.711  38.992  1.00 23.40           C  
ANISOU 3338  C   GLN B 438     3155   3221   2514    454    -52   -324       C  
ATOM   3339  O   GLN B 438       5.437  73.808  38.454  1.00 24.84           O  
ANISOU 3339  O   GLN B 438     3340   3383   2714    448    -54   -319       O  
ATOM   3340  CB  GLN B 438       6.072  72.720  41.391  1.00 29.44           C  
ANISOU 3340  CB  GLN B 438     3944   3954   3289    545   -133   -368       C  
ATOM   3341  CG  GLN B 438       4.854  72.109  42.055  1.00 30.48           C  
ANISOU 3341  CG  GLN B 438     4084   4154   3344    580   -124   -330       C  
ATOM   3342  CD  GLN B 438       4.469  72.840  43.321  1.00 32.02           C  
ANISOU 3342  CD  GLN B 438     4300   4377   3488    663   -167   -343       C  
ATOM   3343  NE2 GLN B 438       3.717  73.921  43.172  1.00 24.52           N  
ANISOU 3343  NE2 GLN B 438     3365   3444   2509    690   -173   -346       N  
ATOM   3344  OE1 GLN B 438       4.846  72.440  44.423  1.00 39.91           O  
ANISOU 3344  OE1 GLN B 438     5302   5389   4473    707   -196   -353       O  
ATOM   3345  N   LYS B 439       4.281  71.907  38.753  1.00 25.61           N  
ANISOU 3345  N   LYS B 439     3429   3554   2746    445    -24   -297       N  
ATOM   3346  CA  LYS B 439       3.159  72.318  37.920  1.00 32.16           C  
ANISOU 3346  CA  LYS B 439     4260   4433   3528    436      3   -267       C  
ATOM   3347  C   LYS B 439       1.866  72.121  38.692  1.00 34.29           C  
ANISOU 3347  C   LYS B 439     4540   4754   3736    476     -1   -239       C  
ATOM   3348  O   LYS B 439       1.725  71.154  39.440  1.00 33.43           O  
ANISOU 3348  O   LYS B 439     4423   4656   3621    484     -4   -230       O  
ATOM   3349  CB  LYS B 439       3.131  71.530  36.605  1.00 29.59           C  
ANISOU 3349  CB  LYS B 439     3904   4133   3206    381     43   -268       C  
ATOM   3350  CG  LYS B 439       4.285  71.815  35.664  1.00 35.74           C  
ANISOU 3350  CG  LYS B 439     4663   4887   4028    344     58   -287       C  
ATOM   3351  CD  LYS B 439       4.233  73.227  35.108  1.00 34.65           C  
ANISOU 3351  CD  LYS B 439     4535   4747   3885    348     61   -257       C  
ATOM   3352  CE  LYS B 439       5.288  73.413  34.032  1.00 34.52           C  
ANISOU 3352  CE  LYS B 439     4487   4725   3903    306     88   -258       C  
ATOM   3353  NZ  LYS B 439       5.348  74.821  33.568  1.00 39.31           N1+
ANISOU 3353  NZ  LYS B 439     5098   5316   4521    306     88   -212       N1+
ATOM   3354  N   SER B 440       0.925  73.042  38.516  1.00 33.79           N  
ANISOU 3354  N   SER B 440     4489   4722   3627    502      0   -220       N  
ATOM   3355  CA  SER B 440      -0.347  72.945  39.219  1.00 28.30           C  
ANISOU 3355  CA  SER B 440     3797   4089   2868    544     -1   -193       C  
ATOM   3356  C   SER B 440      -1.491  72.613  38.272  1.00 21.61           C  
ANISOU 3356  C   SER B 440     2928   3298   1985    516     34   -164       C  
ATOM   3357  O   SER B 440      -1.364  72.729  37.052  1.00 31.75           O  
ANISOU 3357  O   SER B 440     4203   4579   3281    476     53   -168       O  
ATOM   3358  CB  SER B 440      -0.642  74.236  39.978  1.00 24.12           C  
ANISOU 3358  CB  SER B 440     3293   3562   2311    615    -37   -204       C  
ATOM   3359  OG  SER B 440       0.114  74.294  41.174  1.00 36.21           O  
ANISOU 3359  OG  SER B 440     4835   5066   3855    658    -74   -234       O  
ATOM   3360  N   LEU B 441      -2.613  72.203  38.855  1.00 23.43           N  
ANISOU 3360  N   LEU B 441     3146   3587   2167    539     41   -134       N  
ATOM   3361  CA  LEU B 441      -3.739  71.678  38.101  1.00 32.92           C  
ANISOU 3361  CA  LEU B 441     4320   4845   3344    510     69   -110       C  
ATOM   3362  C   LEU B 441      -5.034  71.823  38.899  1.00 28.65           C  
ANISOU 3362  C   LEU B 441     3769   4376   2742    558     70    -74       C  
ATOM   3363  O   LEU B 441      -5.108  71.405  40.056  1.00 32.62           O  
ANISOU 3363  O   LEU B 441     4267   4898   3230    588     65    -52       O  
ATOM   3364  CB  LEU B 441      -3.478  70.208  37.751  1.00 37.92           C  
ANISOU 3364  CB  LEU B 441     4921   5462   4025    451     84   -112       C  
ATOM   3365  CG  LEU B 441      -4.551  69.392  37.040  1.00 34.24           C  
ANISOU 3365  CG  LEU B 441     4414   5040   3555    414    104    -97       C  
ATOM   3366  CD1 LEU B 441      -4.670  69.818  35.591  1.00 35.39           C  
ANISOU 3366  CD1 LEU B 441     4554   5204   3687    390    114   -125       C  
ATOM   3367  CD2 LEU B 441      -4.224  67.912  37.143  1.00 43.63           C  
ANISOU 3367  CD2 LEU B 441     5571   6194   4811    369    104    -99       C  
ATOM   3368  N   SER B 442      -6.044  72.431  38.286  1.00 26.46           N  
ANISOU 3368  N   SER B 442     3485   4145   2423    570     78    -64       N  
ATOM   3369  CA  SER B 442      -7.344  72.603  38.927  1.00 35.99           C  
ANISOU 3369  CA  SER B 442     4673   5431   3568    617     83    -32       C  
ATOM   3370  C   SER B 442      -8.434  72.803  37.891  1.00 32.45           C  
ANISOU 3370  C   SER B 442     4204   5032   3096    601     97    -23       C  
ATOM   3371  O   SER B 442      -8.153  73.139  36.743  1.00 29.47           O  
ANISOU 3371  O   SER B 442     3835   4631   2731    574     99    -41       O  
ATOM   3372  CB  SER B 442      -7.329  73.788  39.898  1.00 31.10           C  
ANISOU 3372  CB  SER B 442     4082   4814   2920    696     53    -47       C  
ATOM   3373  OG  SER B 442      -7.266  75.020  39.209  1.00 27.29           O  
ANISOU 3373  OG  SER B 442     3626   4301   2440    716     34    -72       O  
ATOM   3374  N   LEU B 443      -9.676  72.584  38.303  1.00 38.21           N  
ANISOU 3374  N   LEU B 443     4894   5817   3809    612    106     10       N  
ATOM   3375  CA  LEU B 443     -10.821  72.814  37.440  1.00 40.85           C  
ANISOU 3375  CA  LEU B 443     5198   6188   4135    600    112     18       C  
ATOM   3376  C   LEU B 443     -10.817  74.271  36.990  1.00 40.34           C  
ANISOU 3376  C   LEU B 443     5165   6094   4069    636     90     -2       C  
ATOM   3377  O   LEU B 443     -10.883  75.188  37.810  1.00 49.36           O  
ANISOU 3377  O   LEU B 443     6324   7227   5204    696     69     -8       O  
ATOM   3378  CB  LEU B 443     -12.118  72.462  38.168  1.00 33.40           C  
ANISOU 3378  CB  LEU B 443     4205   5315   3172    618    124     57       C  
ATOM   3379  CG  LEU B 443     -13.422  72.536  37.379  1.00 39.77           C  
ANISOU 3379  CG  LEU B 443     4970   6175   3966    608    130     66       C  
ATOM   3380  CD1 LEU B 443     -13.301  71.731  36.099  1.00 42.19           C  
ANISOU 3380  CD1 LEU B 443     5261   6491   4279    547    140     48       C  
ATOM   3381  CD2 LEU B 443     -14.580  72.032  38.227  1.00 47.56           C  
ANISOU 3381  CD2 LEU B 443     5899   7240   4933    624    147    112       C  
ATOM   3382  N   SER B 444     -10.716  74.479  35.681  1.00 35.94           N  
ANISOU 3382  N   SER B 444     4613   5528   3514    606     93    -11       N  
ATOM   3383  CA  SER B 444     -10.472  75.811  35.138  1.00 42.29           C  
ANISOU 3383  CA  SER B 444     5451   6304   4312    638     74    -16       C  
ATOM   3384  C   SER B 444     -11.002  75.956  33.707  1.00 32.26           C  
ANISOU 3384  C   SER B 444     4164   5063   3030    611     81     -7       C  
ATOM   3385  O   SER B 444     -11.283  74.955  33.047  1.00 27.12           O  
ANISOU 3385  O   SER B 444     3479   4444   2381    563     98    -13       O  
ATOM   3386  CB  SER B 444      -8.971  76.109  35.181  1.00 46.64           C  
ANISOU 3386  CB  SER B 444     6047   6799   4873    638     66    -34       C  
ATOM   3387  OG  SER B 444      -8.248  75.151  34.425  1.00 44.09           O  
ANISOU 3387  OG  SER B 444     5716   6474   4563    578     90    -45       O  
ATOM   3388  N   PRO B 445     -11.154  77.210  33.234  1.00 36.66           N  
ANISOU 3388  N   PRO B 445     4744   5614   3572    650     65      6       N  
ATOM   3389  CA  PRO B 445     -11.575  77.493  31.856  1.00 40.40           C  
ANISOU 3389  CA  PRO B 445     5205   6119   4028    635     69     24       C  
ATOM   3390  C   PRO B 445     -10.760  76.749  30.815  1.00 39.06           C  
ANISOU 3390  C   PRO B 445     5027   5953   3861    575     91     16       C  
ATOM   3391  O   PRO B 445      -9.532  76.836  30.820  1.00 44.80           O  
ANISOU 3391  O   PRO B 445     5782   6645   4595    565     97     13       O  
ATOM   3392  CB  PRO B 445     -11.336  78.996  31.719  1.00 40.07           C  
ANISOU 3392  CB  PRO B 445     5205   6054   3967    693     46     49       C  
ATOM   3393  CG  PRO B 445     -11.487  79.523  33.072  1.00 37.32           C  
ANISOU 3393  CG  PRO B 445     4875   5681   3623    755     21     31       C  
ATOM   3394  CD  PRO B 445     -11.067  78.445  34.037  1.00 31.71           C  
ANISOU 3394  CD  PRO B 445     4153   4959   2936    725     35      5       C  
ATOM   3395  N   GLY B 446     -11.438  76.034  29.925  1.00 44.76           N  
ANISOU 3395  N   GLY B 446     5707   6725   4574    542    100      5       N  
ATOM   3396  CA  GLY B 446     -10.764  75.341  28.846  1.00 42.79           C  
ANISOU 3396  CA  GLY B 446     5444   6495   4322    496    116    -15       C  
ATOM   3397  C   GLY B 446     -10.340  76.307  27.759  1.00 35.71           C  
ANISOU 3397  C   GLY B 446     4562   5609   3399    506    119     20       C  
ATOM   3398  O   GLY B 446      -9.251  76.186  27.199  1.00 42.73           O  
ANISOU 3398  O   GLY B 446     5456   6494   4285    483    136     18       O  
TER   
HETATM 3399  O   HOH B 601      37.606  59.004  47.410  1.00 52.28           O  
HETATM 3400  O   HOH B 602      30.991  57.928  37.076  1.00 38.51           O  
HETATM 3401  O   HOH B 603      14.029  57.206  38.268  1.00 34.65           O  
HETATM 3402  O   HOH B 604       2.051  75.244  44.491  1.00 51.17           O  
HETATM 3403  O   HOH B 605       0.000  76.126  42.910  0.50 69.19           O  
HETATM 3404  O   HOH B 606      24.267  61.466  33.678  1.00 56.27           O  
HETATM 3405  O   HOH B 607      -8.908  76.941  39.281  1.00 46.19           O  
HETATM 3406  O   HOH B 608       7.729  68.802  25.629  1.00 33.69           O  
HETATM 3407  O   HOH B 609      -3.223  56.914  41.120  1.00 29.95           O  
HETATM 3408  O   HOH B 610       6.606  59.188  42.239  1.00 27.66           O  
HETATM 3409  O   HOH B 611      20.597  61.811  38.267  1.00 32.39           O  
HETATM 3410  O   HOH B 612      -7.166  56.773  38.949  1.00 30.53           O  
HETATM 3411  O   HOH B 613      22.224  56.270  37.953  1.00 42.31           O  
HETATM 3412  O   HOH B 614      22.870  69.193  39.262  1.00 45.57           O  
HETATM 3413  O   HOH B 615       7.209  72.114  31.060  1.00 52.62           O  
HETATM 3414  O   HOH B 616      16.898  52.000  50.978  1.00 46.01           O  
HETATM 3415  O   HOH B 617      27.989  58.432  40.888  1.00 32.48           O  
HETATM 3416  O   HOH B 618       3.627  63.891  48.298  1.00 45.48           O  
HETATM 3417  O   HOH B 619      30.319  60.646  49.045  1.00 25.12           O  
HETATM 3418  O   HOH B 620      18.242  63.176  38.586  1.00 32.45           O  
HETATM 3419  O   HOH B 621      35.831  50.436  54.561  1.00 39.67           O  
HETATM 3420  O   HOH B 622     -11.706  56.456  37.564  1.00 36.55           O  
HETATM 3421  O   HOH B 623      -8.684  60.848  32.787  1.00 30.25           O  
HETATM 3422  O   HOH B 624      30.382  52.371  38.226  1.00 44.29           O  
HETATM 3423  O   HOH B 625      -5.953  62.532  33.706  1.00 21.13           O  
HETATM 3424  O   HOH B 626      16.271  70.573  50.231  1.00 31.91           O  
HETATM 3425  O   HOH B 627     -15.127  76.134  45.623  1.00 26.23           O  
HETATM 3426  O   HOH B 628      28.359  59.394  36.366  1.00 49.39           O  
HETATM 3427  O   HOH B 629      35.404  53.336  44.793  1.00 46.15           O  
HETATM 3428  O   HOH B 630      -7.077  65.484  29.895  1.00 28.28           O  
HETATM 3429  O   HOH B 631      32.041  65.778  44.209  1.00 32.09           O  
HETATM 3430  O   HOH B 632      20.241  52.818  48.821  1.00 54.66           O  
HETATM 3431  O   HOH B 633      34.275  32.813  64.518  1.00 58.24           O  
HETATM 3432  O   HOH B 634      -7.873  71.827  34.329  1.00 40.75           O  
HETATM 3433  O   HOH B 635      10.810  61.961  26.088  1.00 26.75           O  
HETATM 3434  O   HOH B 636     -10.147  71.794  40.971  1.00 27.02           O  
HETATM 3435  O   HOH B 637      12.960  75.612  41.455  1.00 32.17           O  
HETATM 3436  O   HOH B 638       2.810  74.770  40.688  1.00 23.31           O  
HETATM 3437  O   HOH B 639      33.786  46.108  41.922  1.00 40.00           O  
HETATM 3438  O   HOH B 640       0.229  73.420  34.866  1.00 36.09           O  
HETATM 3439  O   HOH B 641     -16.603  62.544  44.510  1.00 37.63           O  
HETATM 3440  O   HOH B 642       8.793  56.182  38.807  1.00 29.29           O  
HETATM 3441  O   HOH B 643       7.130  73.842  46.057  1.00 36.97           O  
HETATM 3442  O   HOH B 644       1.214  75.343  36.859  1.00 31.04           O  
HETATM 3443  O   HOH B 645      -7.319  69.918  48.745  1.00 43.60           O  
HETATM 3444  O   HOH B 646      -9.027  62.703  47.339  1.00 40.26           O  
HETATM 3445  O   HOH B 647     -12.294  69.050  34.632  1.00 41.05           O  
HETATM 3446  O   HOH B 648       9.900  51.078  31.912  1.00 37.62           O  
HETATM 3447  O   HOH B 649      -0.298  72.852  45.845  1.00 37.47           O  
HETATM 3448  O   HOH B 650      21.179  60.357  40.175  1.00 39.76           O  
HETATM 3449  O   HOH B 651      30.952  58.775  51.819  1.00 48.61           O  
HETATM 3450  O   HOH B 652      26.253  54.785  32.461  1.00 42.38           O  
HETATM 3451  O   HOH B 653      19.766  56.582  33.588  1.00 46.70           O  
HETATM 3452  O   HOH B 654       4.731  54.553  42.276  1.00 32.39           O  
HETATM 3453  O   HOH B 655      13.295  74.635  37.683  1.00 43.71           O  
HETATM 3454  O   HOH B 656     -16.855  55.150  40.916  1.00 49.01           O  
HETATM 3455  O   HOH B 657      20.435  58.393  41.443  1.00 53.04           O  
HETATM 3456  O   HOH B 658      13.504  59.295  45.156  1.00 33.91           O  
HETATM 3457  O   HOH B 659      12.219  51.421  28.363  1.00 43.49           O  
HETATM 3458  O   HOH B 660      28.057  54.749  35.107  1.00 56.26           O  
HETATM 3459  O   HOH B 661       9.407  59.380  43.216  1.00 46.10           O  
HETATM 3460  O   HOH B 662      17.779  69.952  27.990  1.00 36.53           O  
HETATM 3461  O   HOH B 663      -5.688  75.326  36.359  1.00 59.66           O  
HETATM 3462  O   HOH B 664     -14.697  75.875  30.055  1.00 50.35           O  
HETATM 3463  O   HOH B 665      34.143  65.708  42.293  1.00 44.91           O  
HETATM 3464  O   HOH B 666      18.602  54.371  50.164  1.00 29.14           O  
HETATM 3465  O   HOH B 667      -7.038  53.896  42.609  1.00 39.64           O  
HETATM 3466  O   HOH B 668       4.824  52.081  41.861  1.00 39.29           O  
HETATM 3467  C1  NAG E   1      26.613  32.047  26.958  1.00121.41           C  
ANISOU 3467  C1  NAG E   1    11989  13762  20380    329   -130  -3130       C  
HETATM 3468  C2  NAG E   1      26.125  32.134  28.414  1.00114.85           C  
ANISOU 3468  C2  NAG E   1    11226  12932  19481    446   -410  -2964       C  
HETATM 3469  N2  NAG E   1      26.704  31.066  29.211  1.00118.09           N  
ANISOU 3469  N2  NAG E   1    11571  13206  20092    557   -641  -2954       N  
HETATM 3470  C3  NAG E   1      24.593  32.089  28.492  1.00105.26           C  
ANISOU 3470  C3  NAG E   1    10171  11805  18018    455   -400  -2816       C  
HETATM 3471  O3  NAG E   1      24.185  32.301  29.838  1.00102.89           O  
ANISOU 3471  O3  NAG E   1     9943  11508  17644    550   -650  -2664       O  
HETATM 3472  C4  NAG E   1      23.949  33.122  27.575  1.00100.43           C  
ANISOU 3472  C4  NAG E   1     9634  11331  17194    333   -155  -2830       C  
HETATM 3473  O4  NAG E   1      22.522  32.994  27.581  1.00 97.19           O  
ANISOU 3473  O4  NAG E   1     9363  10993  16573    341   -139  -2708       O  
HETATM 3474  C5  NAG E   1      24.503  32.919  26.162  1.00108.32           C  
ANISOU 3474  C5  NAG E   1    10575  12315  18268    225    101  -2993       C  
HETATM 3475  O5  NAG E   1      25.935  33.049  26.158  1.00115.05           O  
ANISOU 3475  O5  NAG E   1    11281  13087  19346    216     91  -3123       O  
HETATM 3476  C6  NAG E   1      23.979  33.898  25.137  1.00111.89           C  
ANISOU 3476  C6  NAG E   1    11117  12887  18508     91    351  -3018       C  
HETATM 3477  O6  NAG E   1      23.134  34.889  25.705  1.00120.92           O  
ANISOU 3477  O6  NAG E   1    12362  14139  19441     93    302  -2894       O  
HETATM 3478  C7  NAG E   1      27.005  31.186  30.510  1.00117.15           C  
ANISOU 3478  C7  NAG E   1    11459  13039  20014    652   -908  -2871       C  
HETATM 3479  O7  NAG E   1      26.804  32.224  31.135  1.00116.56           O  
ANISOU 3479  O7  NAG E   1    11442  13036  19810    652   -976  -2796       O  
HETATM 3480  C8  NAG E   1      27.596  29.967  31.161  1.00113.67           C  
ANISOU 3480  C8  NAG E   1    10963  12450  19777    755  -1126  -2872       C  
HETATM 3481  C1  NAG E   2      21.745  33.815  28.537  1.00108.27           C  
ANISOU 3481  C1  NAG E   2    10856  12479  17802    377   -270  -2560       C  
HETATM 3482  C2  NAG E   2      20.306  34.001  28.062  1.00109.99           C  
ANISOU 3482  C2  NAG E   2    11205  12800  17785    331   -144  -2483       C  
HETATM 3483  N2  NAG E   2      20.222  34.438  26.680  1.00111.43           N  
ANISOU 3483  N2  NAG E   2    11410  13051  17876    199    137  -2585       N  
HETATM 3484  C3  NAG E   2      19.575  34.950  28.992  1.00110.01           C  
ANISOU 3484  C3  NAG E   2    11354  12893  17552    327   -267  -2315       C  
HETATM 3485  O3  NAG E   2      18.242  35.134  28.544  1.00104.06           O  
ANISOU 3485  O3  NAG E   2    10807  12227  16505    250   -157  -2210       O  
HETATM 3486  C4  NAG E   2      19.581  34.407  30.419  1.00114.09           C  
ANISOU 3486  C4  NAG E   2    11908  13328  18114    452   -561  -2188       C  
HETATM 3487  O4  NAG E   2      19.160  35.413  31.347  1.00115.94           O  
ANISOU 3487  O4  NAG E   2    12270  13638  18143    440   -677  -2051       O  
HETATM 3488  C5  NAG E   2      20.991  33.978  30.874  1.00116.13           C  
ANISOU 3488  C5  NAG E   2    11965  13466  18693    542   -706  -2296       C  
HETATM 3489  O5  NAG E   2      21.733  33.243  29.873  1.00116.90           O  
ANISOU 3489  O5  NAG E   2    11964  13492  18960    508   -559  -2447       O  
HETATM 3490  C6  NAG E   2      20.947  33.091  32.101  1.00114.66           C  
ANISOU 3490  C6  NAG E   2    11827  13168  18570    675   -989  -2182       C  
HETATM 3491  O6  NAG E   2      22.061  33.296  32.956  1.00115.78           O  
ANISOU 3491  O6  NAG E   2    11907  13242  18842    723  -1178  -2198       O  
HETATM 3492  C7  NAG E   2      19.160  34.178  25.907  1.00109.84           C  
ANISOU 3492  C7  NAG E   2    11321  12899  17514    150    281  -2565       C  
HETATM 3493  O7  NAG E   2      18.191  33.549  26.322  1.00111.80           O  
ANISOU 3493  O7  NAG E   2    11711  13133  17634    190    180  -2430       O  
HETATM 3494  C8  NAG E   2      19.219  34.706  24.504  1.00109.15           C  
ANISOU 3494  C8  NAG E   2    11272  12874  17327      7    552  -2672       C  
HETATM 3495  C1  MAN E   3      17.752  35.795  31.559  1.00106.98           C  
ANISOU 3495  C1  MAN E   3    11375  12593  16680    389   -655  -1882       C  
HETATM 3496  C2  MAN E   3      17.324  35.436  33.058  1.00 90.79           C  
ANISOU 3496  C2  MAN E   3     9461  10488  14546    483   -916  -1706       C  
HETATM 3497  O2  MAN E   3      17.865  36.351  34.015  1.00 92.37           O  
ANISOU 3497  O2  MAN E   3     9651  10709  14738    507  -1068  -1674       O  
HETATM 3498  C3  MAN E   3      15.784  35.486  33.252  1.00 98.69           C  
ANISOU 3498  C3  MAN E   3    10700  11554  15243    441   -882  -1537       C  
HETATM 3499  O3  MAN E   3      15.454  36.050  34.548  1.00 98.56           O  
ANISOU 3499  O3  MAN E   3    10819  11557  15073    471  -1054  -1392       O  
HETATM 3500  C4  MAN E   3      15.079  36.287  32.124  1.00 81.72           C  
ANISOU 3500  C4  MAN E   3     8602   9531  12915    316   -640  -1567       C  
HETATM 3501  O4  MAN E   3      13.653  36.207  32.229  1.00 80.72           O  
ANISOU 3501  O4  MAN E   3     8671   9452  12546    283   -609  -1428       O  
HETATM 3502  C5  MAN E   3      15.485  35.829  30.699  1.00 94.83           C  
ANISOU 3502  C5  MAN E   3    10134  11178  14718    269   -442  -1732       C  
HETATM 3503  O5  MAN E   3      16.815  35.215  30.651  1.00 99.70           O  
ANISOU 3503  O5  MAN E   3    10544  11691  15646    337   -493  -1871       O  
HETATM 3504  C6  MAN E   3      15.496  37.004  29.775  1.00 89.30           C  
ANISOU 3504  C6  MAN E   3     9426  10589  13915    157   -249  -1805       C  
HETATM 3505  O6  MAN E   3      15.537  36.527  28.454  1.00 90.96           O  
ANISOU 3505  O6  MAN E   3     9584  10791  14184    102    -54  -1927       O  
HETATM 3506  C1  MAN E   4      14.503  37.194  27.710  1.00 87.89           C  
ANISOU 3506  C1  MAN E   4     9343  10507  13545      0     96  -1884       C  
HETATM 3507  C2  MAN E   4      14.480  36.544  26.330  1.00 88.62           C  
ANISOU 3507  C2  MAN E   4     9405  10578  13687    -55    288  -2007       C  
HETATM 3508  O2  MAN E   4      13.501  37.152  25.497  1.00 94.29           O  
ANISOU 3508  O2  MAN E   4    10270  11389  14166   -155    428  -1976       O  
HETATM 3509  C3  MAN E   4      15.827  36.816  25.646  1.00 85.26           C  
ANISOU 3509  C3  MAN E   4     8798  10131  13466    -86    412  -2195       C  
HETATM 3510  O3  MAN E   4      15.878  36.272  24.331  1.00 80.98           O  
ANISOU 3510  O3  MAN E   4     8234   9568  12965   -144    609  -2323       O  
HETATM 3511  C4  MAN E   4      16.167  38.326  25.608  1.00 85.55           C  
ANISOU 3511  C4  MAN E   4     8837  10258  13412   -161    474  -2208       C  
HETATM 3512  O4  MAN E   4      17.508  38.489  25.175  1.00 88.74           O  
ANISOU 3512  O4  MAN E   4     9049  10624  14044   -178    568  -2381       O  
HETATM 3513  C5  MAN E   4      16.017  38.981  26.999  1.00 86.61           C  
ANISOU 3513  C5  MAN E   4     9017  10421  13472   -106    268  -2069       C  
HETATM 3514  O5  MAN E   4      14.758  38.586  27.627  1.00 88.48           O  
ANISOU 3514  O5  MAN E   4     9422  10668  13527    -68    155  -1899       O  
HETATM 3515  C6  MAN E   4      16.038  40.501  26.946  1.00 81.01           C  
ANISOU 3515  C6  MAN E   4     8355   9808  12616   -188    330  -2055       C  
HETATM 3516  O6  MAN E   4      14.791  40.975  27.452  1.00 76.54           O  
ANISOU 3516  O6  MAN E   4     7981   9312  11790   -196    261  -1888       O  
HETATM 3517  C1  NAG E   5      12.240  36.455  25.513  1.00 93.54           C  
ANISOU 3517  C1  NAG E   5    10314  11291  13937   -146    395  -1870       C  
HETATM 3518  C2  NAG E   5      11.157  37.531  25.226  1.00105.74           C  
ANISOU 3518  C2  NAG E   5    12023  12949  15205   -229    454  -1782       C  
HETATM 3519  N2  NAG E   5      10.854  38.244  26.458  1.00107.13           N  
ANISOU 3519  N2  NAG E   5    12255  13164  15285   -192    309  -1647       N  
HETATM 3520  C3  NAG E   5       9.853  36.963  24.611  1.00 91.63           C  
ANISOU 3520  C3  NAG E   5    10370  11174  13273   -264    503  -1731       C  
HETATM 3521  O3  NAG E   5       9.340  37.910  23.678  1.00 84.66           O  
ANISOU 3521  O3  NAG E   5     9585  10376  12205   -364    631  -1748       O  
HETATM 3522  C4  NAG E   5       9.979  35.605  23.921  1.00 99.08           C  
ANISOU 3522  C4  NAG E   5    11263  12030  14354   -248    558  -1822       C  
HETATM 3523  O4  NAG E   5       8.725  34.931  24.004  1.00110.45           O  
ANISOU 3523  O4  NAG E   5    12817  13460  15689   -242    512  -1724       O  
HETATM 3524  C5  NAG E   5      11.048  34.763  24.585  1.00 95.05           C  
ANISOU 3524  C5  NAG E   5    10600  11417  14098   -153    463  -1871       C  
HETATM 3525  O5  NAG E   5      12.245  35.528  24.543  1.00 95.05           O  
ANISOU 3525  O5  NAG E   5    10478  11431  14205   -164    504  -1968       O  
HETATM 3526  C6  NAG E   5      11.336  33.452  23.886  1.00 89.34           C  
ANISOU 3526  C6  NAG E   5     9808  10598  13539   -132    525  -1980       C  
HETATM 3527  O6  NAG E   5      11.382  33.606  22.475  1.00 85.31           O  
ANISOU 3527  O6  NAG E   5     9312  10116  12985   -225    724  -2107       O  
HETATM 3528  C7  NAG E   5      11.599  39.236  26.958  1.00110.87           C  
ANISOU 3528  C7  NAG E   5    12674  13670  15781   -193    272  -1658       C  
HETATM 3529  O7  NAG E   5      12.598  39.650  26.386  1.00114.86           O  
ANISOU 3529  O7  NAG E   5    13071  14176  16395   -230    368  -1785       O  
HETATM 3530  C8  NAG E   5      11.121  39.821  28.254  1.00108.92           C  
ANISOU 3530  C8  NAG E   5    12513  13456  15417   -152    117  -1510       C  
HETATM 3531  C1  GAL E   6       8.283  34.437  22.716  1.00117.12           C  
ANISOU 3531  C1  GAL E   6    13709  14299  16493   -306    645  -1807       C  
HETATM 3532  C2  GAL E   6       6.738  34.150  22.790  1.00128.61           C  
ANISOU 3532  C2  GAL E   6    15306  15776  17784   -322    597  -1687       C  
HETATM 3533  O2  GAL E   6       6.433  33.059  23.659  1.00128.24           O  
ANISOU 3533  O2  GAL E   6    15247  15649  17830   -245    477  -1609       O  
HETATM 3534  C3  GAL E   6       6.158  33.804  21.418  1.00125.28           C  
ANISOU 3534  C3  GAL E   6    14955  15359  17287   -398    721  -1767       C  
HETATM 3535  O3  GAL E   6       4.731  33.762  21.451  1.00116.77           O  
ANISOU 3535  O3  GAL E   6    14000  14313  16055   -421    675  -1662       O  
HETATM 3536  C4  GAL E   6       6.561  34.879  20.415  1.00128.56           C  
ANISOU 3536  C4  GAL E   6    15399  15844  17603   -484    858  -1858       C  
HETATM 3537  O4  GAL E   6       6.079  36.125  20.848  1.00129.29           O  
ANISOU 3537  O4  GAL E   6    15566  16026  17533   -507    817  -1758       O  
HETATM 3538  C5  GAL E   6       8.070  34.951  20.366  1.00125.64           C  
ANISOU 3538  C5  GAL E   6    14887  15439  17411   -467    922  -1978       C  
HETATM 3539  O5  GAL E   6       8.593  35.353  21.645  1.00121.59           O  
ANISOU 3539  O5  GAL E   6    14295  14929  16974   -397    799  -1904       O  
HETATM 3540  C6  GAL E   6       8.603  35.964  19.363  1.00122.26           C  
ANISOU 3540  C6  GAL E   6    14483  15066  16904   -560   1081  -2081       C  
HETATM 3541  O6  GAL E   6       9.986  35.769  19.155  1.00121.05           O  
ANISOU 3541  O6  GAL E   6    14181  14862  16950   -551   1167  -2221       O  
HETATM 3542  C1  MAN E   7      14.234  35.506  35.118  1.00102.18           C  
ANISOU 3542  C1  MAN E   7    11479  12003  15344    484  -1101  -1230       C  
HETATM 3543  C2  MAN E   7      13.630  36.571  36.074  1.00100.61           C  
ANISOU 3543  C2  MAN E   7    11441  11882  14906    460  -1170  -1097       C  
HETATM 3544  O2  MAN E   7      12.417  36.104  36.681  1.00102.41           O  
ANISOU 3544  O2  MAN E   7    11867  12098  14948    465  -1202   -941       O  
HETATM 3545  C3  MAN E   7      14.592  36.818  37.226  1.00 97.75           C  
ANISOU 3545  C3  MAN E   7    11046  11459  14635    539  -1397  -1085       C  
HETATM 3546  O3  MAN E   7      14.055  37.739  38.171  1.00 90.43           O  
ANISOU 3546  O3  MAN E   7    10279  10593  13486    522  -1468   -964       O  
HETATM 3547  C4  MAN E   7      14.961  35.498  37.929  1.00102.34           C  
ANISOU 3547  C4  MAN E   7    11631  11888  15365    649  -1588  -1049       C  
HETATM 3548  O4  MAN E   7      15.996  35.734  38.876  1.00103.86           O  
ANISOU 3548  O4  MAN E   7    11771  12019  15674    726  -1809  -1061       O  
HETATM 3549  C5  MAN E   7      15.441  34.436  36.914  1.00107.29           C  
ANISOU 3549  C5  MAN E   7    12095  12442  16228    671  -1504  -1176       C  
HETATM 3550  O5  MAN E   7      14.498  34.316  35.821  1.00107.24           O  
ANISOU 3550  O5  MAN E   7    12127  12507  16113    584  -1273  -1188       O  
HETATM 3551  C6  MAN E   7      15.582  33.063  37.544  1.00111.70           C  
ANISOU 3551  C6  MAN E   7    12686  12847  16909    774  -1676  -1124       C  
HETATM 3552  O6  MAN E   7      16.436  32.280  36.718  1.00113.11           O  
ANISOU 3552  O6  MAN E   7    12662  12947  17366    811  -1635  -1278       O  
HETATM 3553  C1  FUC E   8      23.884  36.118  25.822  1.00133.71           C  
ANISOU 3553  C1  FUC E   8    13942  15797  21066     42    332  -2938       C  
HETATM 3554  C2  FUC E   8      23.130  37.275  25.079  1.00125.15           C  
ANISOU 3554  C2  FUC E   8    12983  14847  19720    -79    532  -2915       C  
HETATM 3555  O2  FUC E   8      21.716  37.236  25.287  1.00120.49           O  
ANISOU 3555  O2  FUC E   8    12519  14340  18923    -63    502  -2781       O  
HETATM 3556  C3  FUC E   8      23.713  38.691  25.391  1.00134.36           C  
ANISOU 3556  C3  FUC E   8    14131  16064  20854   -124    538  -2926       C  
HETATM 3557  O3  FUC E   8      24.288  39.285  24.223  1.00132.32           O  
ANISOU 3557  O3  FUC E   8    13880  15816  20582   -252    779  -3049       O  
HETATM 3558  C4  FUC E   8      24.786  38.658  26.501  1.00139.92           C  
ANISOU 3558  C4  FUC E   8    14704  16684  21776    -26    321  -2942       C  
HETATM 3559  O4  FUC E   8      26.057  38.248  25.985  1.00144.94           O  
ANISOU 3559  O4  FUC E   8    15211  17213  22647    -44    392  -3100       O  
HETATM 3560  C5  FUC E   8      24.319  37.734  27.637  1.00139.91           C  
ANISOU 3560  C5  FUC E   8    14703  16635  21819    110     60  -2825       C  
HETATM 3561  O5  FUC E   8      24.087  36.379  27.206  1.00140.88           O  
ANISOU 3561  O5  FUC E   8    14817  16687  22024    144     79  -2849       O  
HETATM 3562  C6  FUC E   8      25.319  37.636  28.783  1.00138.70           C  
ANISOU 3562  C6  FUC E   8    14448  16390  21862    210   -182  -2828       C  
HETATM 3563  C1  NAG F   1      16.286  33.095  50.310  1.00 85.76           C  
ANISOU 3563  C1  NAG F   1    10216   8409  13960    481  -1379    830       C  
HETATM 3564  C2  NAG F   1      16.694  33.168  48.837  1.00 83.19           C  
ANISOU 3564  C2  NAG F   1     9872   8053  13684    475  -1406    548       C  
HETATM 3565  N2  NAG F   1      17.685  32.157  48.531  1.00 87.74           N  
ANISOU 3565  N2  NAG F   1    10412   8536  14390    498  -1484    435       N  
HETATM 3566  C3  NAG F   1      17.253  34.554  48.508  1.00 74.54           C  
ANISOU 3566  C3  NAG F   1     8832   7091  12399    528  -1355    415       C  
HETATM 3567  O3  NAG F   1      17.465  34.635  47.094  1.00 73.76           O  
ANISOU 3567  O3  NAG F   1     8709   6984  12332    514  -1367    167       O  
HETATM 3568  C4  NAG F   1      16.310  35.670  48.975  1.00 71.28           C  
ANISOU 3568  C4  NAG F   1     8460   6785  11839    519  -1279    546       C  
HETATM 3569  O4  NAG F   1      16.933  36.955  48.813  1.00 62.39           O  
ANISOU 3569  O4  NAG F   1     7383   5781  10540    577  -1239    434       O  
HETATM 3570  C5  NAG F   1      15.959  35.433  50.445  1.00 77.91           C  
ANISOU 3570  C5  NAG F   1     9311   7651  12642    529  -1265    820       C  
HETATM 3571  O5  NAG F   1      15.382  34.134  50.598  1.00 84.70           O  
ANISOU 3571  O5  NAG F   1    10114   8387  13683    468  -1304    931       O  
HETATM 3572  C6  NAG F   1      14.961  36.402  51.042  1.00 82.68           C  
ANISOU 3572  C6  NAG F   1     9943   8375  13096    523  -1192    979       C  
HETATM 3573  O6  NAG F   1      14.583  37.469  50.194  1.00 89.66           O  
ANISOU 3573  O6  NAG F   1    10848   9321  13897    514  -1151    849       O  
HETATM 3574  C7  NAG F   1      17.380  30.977  47.987  1.00 88.71           C  
ANISOU 3574  C7  NAG F   1    10466   8530  14708    451  -1549    393       C  
HETATM 3575  O7  NAG F   1      16.225  30.672  47.691  1.00 91.91           O  
ANISOU 3575  O7  NAG F   1    10834   8888  15201    382  -1547    446       O  
HETATM 3576  C8  NAG F   1      18.535  30.045  47.749  1.00 84.91           C  
ANISOU 3576  C8  NAG F   1     9953   7972  14338    490  -1629    275       C  
HETATM 3577  C1  NAG F   2      16.796  37.512  47.470  1.00 55.91           C  
ANISOU 3577  C1  NAG F   2     6557   4981   9704    554  -1219    222       C  
HETATM 3578  C2  NAG F   2      16.911  39.044  47.486  1.00 56.77           C  
ANISOU 3578  C2  NAG F   2     6718   5241   9611    592  -1153    178       C  
HETATM 3579  N2  NAG F   2      15.939  39.642  48.384  1.00 65.38           N  
ANISOU 3579  N2  NAG F   2     7839   6441  10563    568  -1089    372       N  
HETATM 3580  C3  NAG F   2      16.745  39.592  46.067  1.00 49.65           C  
ANISOU 3580  C3  NAG F   2     5810   4388   8669    557  -1117    -37       C  
HETATM 3581  O3  NAG F   2      16.989  40.998  46.098  1.00 53.43           O  
ANISOU 3581  O3  NAG F   2     6335   5047   8920    573  -1041    -84       O  
HETATM 3582  C4  NAG F   2      17.714  38.917  45.098  1.00 56.39           C  
ANISOU 3582  C4  NAG F   2     6622   5173   9629    574  -1170   -243       C  
HETATM 3583  O4  NAG F   2      17.368  39.201  43.734  1.00 59.35           O  
ANISOU 3583  O4  NAG F   2     6977   5581   9992    540  -1146   -423       O  
HETATM 3584  C5  NAG F   2      17.657  37.396  45.238  1.00 62.49           C  
ANISOU 3584  C5  NAG F   2     7345   5810  10586    546  -1241   -190       C  
HETATM 3585  O5  NAG F   2      17.796  36.976  46.603  1.00 58.88           O  
ANISOU 3585  O5  NAG F   2     6904   5318  10151    569  -1263     16       O  
HETATM 3586  C6  NAG F   2      18.750  36.681  44.466  1.00 61.51           C  
ANISOU 3586  C6  NAG F   2     7179   5660  10531    567  -1292   -377       C  
HETATM 3587  O6  NAG F   2      18.754  35.285  44.741  1.00 62.66           O  
ANISOU 3587  O6  NAG F   2     7279   5676  10851    550  -1365   -315       O  
HETATM 3588  C7  NAG F   2      16.271  40.563  49.292  1.00 68.43           C  
ANISOU 3588  C7  NAG F   2     8271   6972  10758    616  -1048    443       C  
HETATM 3589  O7  NAG F   2      17.424  40.963  49.427  1.00 70.16           O  
ANISOU 3589  O7  NAG F   2     8508   7234  10914    678  -1063    352       O  
HETATM 3590  C8  NAG F   2      15.147  41.078  50.142  1.00 64.63           C  
ANISOU 3590  C8  NAG F   2     7809   6602  10144    594   -985    636       C  
HETATM 3591  C1  MAN F   3      17.337  40.544  43.138  1.00 57.77           C  
ANISOU 3591  C1  MAN F   3     6808   5525   9616    543  -1070   -524       C  
HETATM 3592  C2  MAN F   3      18.273  40.486  41.851  1.00 66.55           C  
ANISOU 3592  C2  MAN F   3     7883   6680  10722    561  -1077   -763       C  
HETATM 3593  O2  MAN F   3      17.721  39.689  40.746  1.00 77.08           O  
ANISOU 3593  O2  MAN F   3     9163   7976  12149    518  -1104   -868       O  
HETATM 3594  C3  MAN F   3      18.562  41.902  41.287  1.00 65.49           C  
ANISOU 3594  C3  MAN F   3     7777   6694  10412    576  -1002   -869       C  
HETATM 3595  O3  MAN F   3      18.546  41.979  39.839  1.00 72.72           O  
ANISOU 3595  O3  MAN F   3     8655   7684  11291    553   -979  -1043       O  
HETATM 3596  C4  MAN F   3      17.555  42.904  41.835  1.00 59.89           C  
ANISOU 3596  C4  MAN F   3     7119   6090   9546    532   -928   -725       C  
HETATM 3597  O4  MAN F   3      17.804  44.178  41.261  1.00 61.11           O  
ANISOU 3597  O4  MAN F   3     7295   6396   9528    530   -855   -811       O  
HETATM 3598  C5  MAN F   3      17.655  43.004  43.357  1.00 62.52           C  
ANISOU 3598  C5  MAN F   3     7491   6423   9843    555   -933   -534       C  
HETATM 3599  O5  MAN F   3      17.708  41.656  43.996  1.00 61.47           O  
ANISOU 3599  O5  MAN F   3     7330   6129   9896    569  -1014   -441       O  
HETATM 3600  C6  MAN F   3      16.466  43.755  43.867  1.00 61.82           C  
ANISOU 3600  C6  MAN F   3     7439   6422   9627    513   -870   -392       C  
HETATM 3601  O6  MAN F   3      16.439  43.775  45.283  1.00 64.94           O  
ANISOU 3601  O6  MAN F   3     7863   6827   9983    539   -876   -211       O  
HETATM 3602  C1  MAN F   4      15.611  44.911  45.635  1.00 74.37           C  
ANISOU 3602  C1  MAN F   4     9098   8157  11000    518   -802   -131       C  
HETATM 3603  C2  MAN F   4      15.549  45.046  47.187  1.00 88.37           C  
ANISOU 3603  C2  MAN F   4    10901   9974  12701    557   -803     60       C  
HETATM 3604  O2  MAN F   4      14.865  46.240  47.551  1.00 86.09           O  
ANISOU 3604  O2  MAN F   4    10651   9829  12230    551   -735    115       O  
HETATM 3605  C3  MAN F   4      14.717  43.927  47.803  1.00 86.17           C  
ANISOU 3605  C3  MAN F   4    10596   9598  12546    532   -833    235       C  
HETATM 3606  O3  MAN F   4      14.550  44.117  49.211  1.00 84.75           O  
ANISOU 3606  O3  MAN F   4    10440   9488  12274    571   -823    422       O  
HETATM 3607  C4  MAN F   4      13.342  43.810  47.121  1.00 85.17           C  
ANISOU 3607  C4  MAN F   4    10448   9459  12454    455   -800    253       C  
HETATM 3608  O4  MAN F   4      12.662  42.668  47.612  1.00 77.40           O  
ANISOU 3608  O4  MAN F   4     9426   8363  11618    426   -837    411       O  
HETATM 3609  C5  MAN F   4      13.514  43.668  45.601  1.00 86.71           C  
ANISOU 3609  C5  MAN F   4    10617   9603  12726    424   -812     44       C  
HETATM 3610  O5  MAN F   4      14.304  44.769  45.085  1.00 79.99           O  
ANISOU 3610  O5  MAN F   4     9795   8860  11737    453   -775   -103       O  
HETATM 3611  C6  MAN F   4      12.208  43.681  44.841  1.00 86.05           C  
ANISOU 3611  C6  MAN F   4    10512   9524  12657    354   -781     37       C  
HETATM 3612  O6  MAN F   4      12.406  44.466  43.665  1.00 83.55           O  
ANISOU 3612  O6  MAN F   4    10205   9283  12258    347   -747   -147       O  
HETATM 3613  C1  NAG F   5      15.772  47.346  47.513  1.00 81.83           C  
ANISOU 3613  C1  NAG F   5    10141   9384  11566    590   -716      9       C  
HETATM 3614  C2  NAG F   5      14.966  48.624  47.234  1.00 80.23           C  
ANISOU 3614  C2  NAG F   5     9969   9307  11207    563   -644     -5       C  
HETATM 3615  N2  NAG F   5      14.389  48.572  45.900  1.00 77.68           N  
ANISOU 3615  N2  NAG F   5     9625   8961  10928    502   -619   -103       N  
HETATM 3616  C3  NAG F   5      15.840  49.871  47.381  1.00 73.16           C  
ANISOU 3616  C3  NAG F   5     9104   8509  10184    604   -627    -88       C  
HETATM 3617  O3  NAG F   5      15.003  51.026  47.371  1.00 70.81           O  
ANISOU 3617  O3  NAG F   5     8837   8321   9746    588   -569    -70       O  
HETATM 3618  C4  NAG F   5      16.656  49.840  48.667  1.00 71.56           C  
ANISOU 3618  C4  NAG F   5     8916   8324   9950    677   -669    -21       C  
HETATM 3619  O4  NAG F   5      17.607  50.901  48.665  1.00 67.39           O  
ANISOU 3619  O4  NAG F   5     8404   7864   9337    710   -665   -125       O  
HETATM 3620  C5  NAG F   5      17.392  48.515  48.768  1.00 73.03           C  
ANISOU 3620  C5  NAG F   5     9069   8387  10293    696   -734    -14       C  
HETATM 3621  O5  NAG F   5      16.430  47.456  48.753  1.00 80.04           O  
ANISOU 3621  O5  NAG F   5     9934   9192  11285    657   -742     93       O  
HETATM 3622  C6  NAG F   5      18.175  48.361  50.048  1.00 67.54           C  
ANISOU 3622  C6  NAG F   5     8382   7705   9573    772   -781     64       C  
HETATM 3623  O6  NAG F   5      17.314  48.239  51.173  1.00 69.92           O  
ANISOU 3623  O6  NAG F   5     8699   8057   9810    791   -773    247       O  
HETATM 3624  C7  NAG F   5      13.136  48.180  45.647  1.00 73.89           C  
ANISOU 3624  C7  NAG F   5     9130   8460  10484    451   -602    -37       C  
HETATM 3625  O7  NAG F   5      12.369  47.833  46.539  1.00 70.55           O  
ANISOU 3625  O7  NAG F   5     8706   8035  10062    447   -601    123       O  
HETATM 3626  C8  NAG F   5      12.728  48.193  44.206  1.00 70.18           C  
ANISOU 3626  C8  NAG F   5     8638   7978  10051    400   -584   -167       C  
HETATM 3627  C1  MAN F   6      19.694  41.354  39.226  1.00 80.55           C  
ANISOU 3627  C1  MAN F   6     9595   8699  12311    580  -1012  -1170       C  
HETATM 3628  C2  MAN F   6      20.612  42.416  38.565  1.00 92.28           C  
ANISOU 3628  C2  MAN F   6    11079  10342  13642    603   -949  -1285       C  
HETATM 3629  O2  MAN F   6      21.700  42.762  39.428  1.00 94.72           O  
ANISOU 3629  O2  MAN F   6    11408  10666  13917    644   -952  -1245       O  
HETATM 3630  C3  MAN F   6      21.265  41.824  37.313  1.00 87.64           C  
ANISOU 3630  C3  MAN F   6    10420   9810  13071    615   -967  -1444       C  
HETATM 3631  O3  MAN F   6      22.455  42.524  36.934  1.00 79.73           O  
ANISOU 3631  O3  MAN F   6     9401   8929  11961    644   -928  -1524       O  
HETATM 3632  C4  MAN F   6      21.567  40.338  37.534  1.00 91.05           C  
ANISOU 3632  C4  MAN F   6    10809  10117  13670    630  -1059  -1446       C  
HETATM 3633  O4  MAN F   6      22.342  39.834  36.457  1.00 95.10           O  
ANISOU 3633  O4  MAN F   6    11252  10689  14192    657  -1081  -1598       O  
HETATM 3634  C5  MAN F   6      20.224  39.573  37.626  1.00 87.44           C  
ANISOU 3634  C5  MAN F   6    10349   9542  13334    589  -1098  -1379       C  
HETATM 3635  O5  MAN F   6      19.228  40.403  38.274  1.00 83.99           O  
ANISOU 3635  O5  MAN F   6     9973   9096  12841    557  -1051  -1255       O  
HETATM 3636  C6  MAN F   6      20.291  38.244  38.381  1.00 84.14           C  
ANISOU 3636  C6  MAN F   6     9910   8966  13096    592  -1187  -1301       C  
HETATM 3637  O6  MAN F   6      20.566  38.487  39.762  1.00 77.50           O  
ANISOU 3637  O6  MAN F   6     9121   8074  12250    606  -1186  -1148       O  
HETATM 3638  C1  FUC F   7      13.296  37.282  49.528  1.00 93.68           C  
ANISOU 3638  C1  FUC F   7    11323   9780  14492    430  -1133    865       C  
HETATM 3639  C2  FUC F   7      12.270  36.217  50.155  1.00 87.02           C  
ANISOU 3639  C2  FUC F   7    10427   8866  13771    359  -1138   1086       C  
HETATM 3640  O2  FUC F   7      12.179  36.104  51.569  1.00 86.12           O  
ANISOU 3640  O2  FUC F   7    10322   8825  13576    385  -1113   1327       O  
HETATM 3641  C3  FUC F   7      10.836  36.471  49.567  1.00 80.15           C  
ANISOU 3641  C3  FUC F   7     9530   7996  12928    280  -1099   1113       C  
HETATM 3642  O3  FUC F   7      10.086  35.256  49.314  1.00 78.30           O  
ANISOU 3642  O3  FUC F   7     9221   7634  12895    197  -1137   1164       O  
HETATM 3643  C4  FUC F   7      10.861  37.293  48.242  1.00105.77           C  
ANISOU 3643  C4  FUC F   7    12795  11276  16117    275  -1081    863       C  
HETATM 3644  O4  FUC F   7      11.459  36.519  47.183  1.00104.27           O  
ANISOU 3644  O4  FUC F   7    12572  10954  16092    268  -1154    654       O  
HETATM 3645  C5  FUC F   7      11.632  38.624  48.455  1.00 95.68           C  
ANISOU 3645  C5  FUC F   7    11588  10188  14576    342  -1021    778       C  
HETATM 3646  O5  FUC F   7      12.626  38.537  49.503  1.00 95.25           O  
ANISOU 3646  O5  FUC F   7    11559  10149  14483    418  -1046    868       O  
HETATM 3647  C6  FUC F   7      12.411  39.090  47.251  1.00 92.28           C  
ANISOU 3647  C6  FUC F   7    11173   9774  14113    361  -1027    504       C  
CONECT  492 3467
CONECT 2214 3563
CONECT 3467  492 3468 3475
CONECT 3468 3467 3469 3470
CONECT 3469 3468 3478
CONECT 3470 3468 3471 3472
CONECT 3471 3470
CONECT 3472 3470 3473 3474
CONECT 3473 3472 3481
CONECT 3474 3472 3475 3476
CONECT 3475 3467 3474
CONECT 3476 3474 3477
CONECT 3477 3476 3553
CONECT 3478 3469 3479 3480
CONECT 3479 3478
CONECT 3480 3478
CONECT 3481 3473 3482 3489
CONECT 3482 3481 3483 3484
CONECT 3483 3482 3492
CONECT 3484 3482 3485 3486
CONECT 3485 3484
CONECT 3486 3484 3487 3488
CONECT 3487 3486 3495
CONECT 3488 3486 3489 3490
CONECT 3489 3481 3488
CONECT 3490 3488 3491
CONECT 3491 3490
CONECT 3492 3483 3493 3494
CONECT 3493 3492
CONECT 3494 3492
CONECT 3495 3487 3496 3503
CONECT 3496 3495 3497 3498
CONECT 3497 3496
CONECT 3498 3496 3499 3500
CONECT 3499 3498 3542
CONECT 3500 3498 3501 3502
CONECT 3501 3500
CONECT 3502 3500 3503 3504
CONECT 3503 3495 3502
CONECT 3504 3502 3505
CONECT 3505 3504 3506
CONECT 3506 3505 3507 3514
CONECT 3507 3506 3508 3509
CONECT 3508 3507 3517
CONECT 3509 3507 3510 3511
CONECT 3510 3509
CONECT 3511 3509 3512 3513
CONECT 3512 3511
CONECT 3513 3511 3514 3515
CONECT 3514 3506 3513
CONECT 3515 3513 3516
CONECT 3516 3515
CONECT 3517 3508 3518 3525
CONECT 3518 3517 3519 3520
CONECT 3519 3518 3528
CONECT 3520 3518 3521 3522
CONECT 3521 3520
CONECT 3522 3520 3523 3524
CONECT 3523 3522 3531
CONECT 3524 3522 3525 3526
CONECT 3525 3517 3524
CONECT 3526 3524 3527
CONECT 3527 3526
CONECT 3528 3519 3529 3530
CONECT 3529 3528
CONECT 3530 3528
CONECT 3531 3523 3532 3539
CONECT 3532 3531 3533 3534
CONECT 3533 3532
CONECT 3534 3532 3535 3536
CONECT 3535 3534
CONECT 3536 3534 3537 3538
CONECT 3537 3536
CONECT 3538 3536 3539 3540
CONECT 3539 3531 3538
CONECT 3540 3538 3541
CONECT 3541 3540
CONECT 3542 3499 3543 3550
CONECT 3543 3542 3544 3545
CONECT 3544 3543
CONECT 3545 3543 3546 3547
CONECT 3546 3545
CONECT 3547 3545 3548 3549
CONECT 3548 3547
CONECT 3549 3547 3550 3551
CONECT 3550 3542 3549
CONECT 3551 3549 3552
CONECT 3552 3551
CONECT 3553 3477 3554 3561
CONECT 3554 3553 3555 3556
CONECT 3555 3554
CONECT 3556 3554 3557 3558
CONECT 3557 3556
CONECT 3558 3556 3559 3560
CONECT 3559 3558
CONECT 3560 3558 3561 3562
CONECT 3561 3553 3560
CONECT 3562 3560
CONECT 3563 2214 3564 3571
CONECT 3564 3563 3565 3566
CONECT 3565 3564 3574
CONECT 3566 3564 3567 3568
CONECT 3567 3566
CONECT 3568 3566 3569 3570
CONECT 3569 3568 3577
CONECT 3570 3568 3571 3572
CONECT 3571 3563 3570
CONECT 3572 3570 3573
CONECT 3573 3572 3638
CONECT 3574 3565 3575 3576
CONECT 3575 3574
CONECT 3576 3574
CONECT 3577 3569 3578 3585
CONECT 3578 3577 3579 3580
CONECT 3579 3578 3588
CONECT 3580 3578 3581 3582
CONECT 3581 3580
CONECT 3582 3580 3583 3584
CONECT 3583 3582 3591
CONECT 3584 3582 3585 3586
CONECT 3585 3577 3584
CONECT 3586 3584 3587
CONECT 3587 3586
CONECT 3588 3579 3589 3590
CONECT 3589 3588
CONECT 3590 3588
CONECT 3591 3583 3592 3599
CONECT 3592 3591 3593 3594
CONECT 3593 3592
CONECT 3594 3592 3595 3596
CONECT 3595 3594 3627
CONECT 3596 3594 3597 3598
CONECT 3597 3596
CONECT 3598 3596 3599 3600
CONECT 3599 3591 3598
CONECT 3600 3598 3601
CONECT 3601 3600 3602
CONECT 3602 3601 3603 3610
CONECT 3603 3602 3604 3605
CONECT 3604 3603 3613
CONECT 3605 3603 3606 3607
CONECT 3606 3605
CONECT 3607 3605 3608 3609
CONECT 3608 3607
CONECT 3609 3607 3610 3611
CONECT 3610 3602 3609
CONECT 3611 3609 3612
CONECT 3612 3611
CONECT 3613 3604 3614 3621
CONECT 3614 3613 3615 3616
CONECT 3615 3614 3624
CONECT 3616 3614 3617 3618
CONECT 3617 3616
CONECT 3618 3616 3619 3620
CONECT 3619 3618
CONECT 3620 3618 3621 3622
CONECT 3621 3613 3620
CONECT 3622 3620 3623
CONECT 3623 3622
CONECT 3624 3615 3625 3626
CONECT 3625 3624
CONECT 3626 3624
CONECT 3627 3595 3628 3635
CONECT 3628 3627 3629 3630
CONECT 3629 3628
CONECT 3630 3628 3631 3632
CONECT 3631 3630
CONECT 3632 3630 3633 3634
CONECT 3633 3632
CONECT 3634 3632 3635 3636
CONECT 3635 3627 3634
CONECT 3636 3634 3637
CONECT 3637 3636
CONECT 3638 3573 3639 3646
CONECT 3639 3638 3640 3641
CONECT 3640 3639
CONECT 3641 3639 3642 3643
CONECT 3642 3641
CONECT 3643 3641 3644 3645
CONECT 3644 3643
CONECT 3645 3643 3646 3647
CONECT 3646 3638 3645
CONECT 3647 3645
END



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