CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 24081600143719985

Job options:

ID        	=	 24081600143719985
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 -1
CUTOFF    	=	 10
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   SER A  96      12.070 -18.414  32.222  1.00 29.94           N  
ANISOU    1  N   SER A  96     3771   3012   4595   1574   -245   1007       N  
ATOM      2  CA  SER A  96      12.232 -17.060  32.737  1.00 29.62           C  
ANISOU    2  CA  SER A  96     3702   2999   4553   1218    -36    918       C  
ATOM      3  C   SER A  96      11.093 -16.151  32.284  1.00 28.29           C  
ANISOU    3  C   SER A  96     3743   2738   4269    652    312    663       C  
ATOM      4  O   SER A  96      11.200 -15.463  31.262  1.00 28.77           O  
ANISOU    4  O   SER A  96     3881   2675   4376    467    529    848       O  
ATOM      5  CB  SER A  96      13.569 -16.479  32.286  1.00 30.60           C  
ANISOU    5  CB  SER A  96     3640   3285   4702   1156     -4   1050       C  
ATOM      6  OG  SER A  96      14.587 -17.457  32.375  1.00 32.71           O  
ANISOU    6  OG  SER A  96     3939   3666   4822    921     -7   1117       O  
ATOM      7  N   VAL A  97       9.999 -16.163  33.042  1.00 25.05           N  
ANISOU    7  N   VAL A  97     3345   2491   3683    322    533    318       N  
ATOM      8  CA  VAL A  97       8.881 -15.263  32.797  1.00 22.33           C  
ANISOU    8  CA  VAL A  97     3026   2232   3225     59    619     22       C  
ATOM      9  C   VAL A  97       8.449 -14.636  34.118  1.00 22.07           C  
ANISOU    9  C   VAL A  97     2813   2482   3089   -233    380   -168       C  
ATOM     10  O   VAL A  97       8.244 -15.348  35.106  1.00 22.30           O  
ANISOU   10  O   VAL A  97     2756   2565   3154   -503    500   -345       O  
ATOM     11  CB  VAL A  97       7.680 -15.985  32.135  1.00 22.67           C  
ANISOU   11  CB  VAL A  97     3289   2127   3199    -44    824    -59       C  
ATOM     12  CG1 VAL A  97       6.554 -15.011  31.889  1.00 23.20           C  
ANISOU   12  CG1 VAL A  97     3360   2288   3169   -291    796     79       C  
ATOM     13  CG2 VAL A  97       8.081 -16.622  30.821  1.00 23.30           C  
ANISOU   13  CG2 VAL A  97     3570   2082   3200   -143    512   -279       C  
ATOM     14  N   PRO A  98       8.330 -13.298  34.149  1.00 21.23           N  
ANISOU   14  N   PRO A  98     2685   2543   2837   -137    390   -351       N  
ATOM     15  CA  PRO A  98       7.876 -12.600  35.357  1.00 21.08           C  
ANISOU   15  CA  PRO A  98     2584   2655   2769     57    645   -444       C  
ATOM     16  C   PRO A  98       6.452 -13.003  35.738  1.00 21.56           C  
ANISOU   16  C   PRO A  98     2609   2884   2699    -16    641   -482       C  
ATOM     17  O   PRO A  98       5.643 -13.267  34.850  1.00 21.69           O  
ANISOU   17  O   PRO A  98     2588   3051   2605   -173    648   -767       O  
ATOM     18  CB  PRO A  98       7.896 -11.129  34.934  1.00 20.94           C  
ANISOU   18  CB  PRO A  98     2538   2586   2832    136    751   -373       C  
ATOM     19  CG  PRO A  98       8.875 -11.070  33.805  1.00 21.89           C  
ANISOU   19  CG  PRO A  98     2797   2655   2864    172    470   -408       C  
ATOM     20  CD  PRO A  98       8.699 -12.360  33.074  1.00 20.58           C  
ANISOU   20  CD  PRO A  98     2630   2440   2748     -1    457   -479       C  
ATOM     21  N   SER A  99       6.148 -13.054  37.033  1.00 21.89           N  
ANISOU   21  N   SER A  99     2733   2807   2779     26    687   -216       N  
ATOM     22  CA  SER A  99       4.789 -13.355  37.474  1.00 21.93           C  
ANISOU   22  CA  SER A  99     2885   2693   2757     -3    857     13       C  
ATOM     23  C   SER A  99       3.836 -12.237  37.051  1.00 21.54           C  
ANISOU   23  C   SER A  99     2910   2535   2740     30    990     16       C  
ATOM     24  O   SER A  99       4.208 -11.067  37.048  1.00 20.85           O  
ANISOU   24  O   SER A  99     3001   2202   2720    -22   1017    -87       O  
ATOM     25  CB  SER A  99       4.736 -13.545  38.993  1.00 22.70           C  
ANISOU   25  CB  SER A  99     2952   2902   2770      5    838    175       C  
ATOM     26  OG  SER A  99       3.406 -13.727  39.447  1.00 23.34           O  
ANISOU   26  OG  SER A  99     3097   2946   2827    141    927    232       O  
ATOM     27  N   GLN A 100       2.613 -12.603  36.681  1.00 22.28           N  
ANISOU   27  N   GLN A 100     2971   2746   2747      8    860     40       N  
ATOM     28  CA  GLN A 100       1.595 -11.608  36.364  1.00 24.12           C  
ANISOU   28  CA  GLN A 100     3170   3111   2882   -177    607    151       C  
ATOM     29  C   GLN A 100       0.409 -11.721  37.321  1.00 22.54           C  
ANISOU   29  C   GLN A 100     2800   2992   2773   -312    472    160       C  
ATOM     30  O   GLN A 100      -0.680 -11.208  37.053  1.00 22.09           O  
ANISOU   30  O   GLN A 100     2493   3159   2743   -269    247    344       O  
ATOM     31  CB  GLN A 100       1.135 -11.760  34.916  1.00 27.78           C  
ANISOU   31  CB  GLN A 100     3813   3514   3228   -231    511     97       C  
ATOM     32  CG  GLN A 100       0.429 -13.072  34.621  1.00 30.85           C  
ANISOU   32  CG  GLN A 100     4351   3896   3476   -123    586    108       C  
ATOM     33  CD  GLN A 100       0.223 -13.303  33.135  1.00 33.34           C  
ANISOU   33  CD  GLN A 100     4704   4277   3687   -101    711     33       C  
ATOM     34  NE2 GLN A 100      -0.915 -12.853  32.612  1.00 33.16           N  
ANISOU   34  NE2 GLN A 100     4648   4258   3693   -316    371    231       N  
ATOM     35  OE1 GLN A 100       1.079 -13.881  32.466  1.00 34.67           O  
ANISOU   35  OE1 GLN A 100     4894   4549   3731     75   1115   -150       O  
ATOM     36  N   LYS A 101       0.629 -12.389  38.449  1.00 20.97           N  
ANISOU   36  N   LYS A 101     2598   2795   2573   -402    665     -2       N  
ATOM     37  CA  LYS A 101      -0.450 -12.612  39.404  1.00 20.53           C  
ANISOU   37  CA  LYS A 101     2725   2634   2442   -318    530   -115       C  
ATOM     38  C   LYS A 101      -0.785 -11.323  40.142  1.00 19.63           C  
ANISOU   38  C   LYS A 101     2516   2602   2340   -265    297     -9       C  
ATOM     39  O   LYS A 101       0.094 -10.674  40.707  1.00 20.43           O  
ANISOU   39  O   LYS A 101     2622   2625   2517   -225    277   -155       O  
ATOM     40  CB  LYS A 101      -0.084 -13.718  40.393  1.00 22.07           C  
ANISOU   40  CB  LYS A 101     3026   2753   2605   -307    635    -56       C  
ATOM     41  CG  LYS A 101      -1.221 -14.086  41.330  1.00 24.94           C  
ANISOU   41  CG  LYS A 101     3454   3035   2986   -146    648    138       C  
ATOM     42  CD  LYS A 101      -0.877 -15.275  42.216  1.00 27.70           C  
ANISOU   42  CD  LYS A 101     3840   3372   3311   -161    688    371       C  
ATOM     43  CE  LYS A 101      -1.984 -15.534  43.231  1.00 29.52           C  
ANISOU   43  CE  LYS A 101     4116   3531   3569   -208    648    631       C  
ATOM     44  NZ  LYS A 101      -1.739 -16.765  44.035  1.00 31.24           N1+
ANISOU   44  NZ  LYS A 101     4294   3744   3831    -93    626    687       N1+
ATOM     45  N   THR A 102      -2.061 -10.948  40.114  1.00 17.70           N  
ANISOU   45  N   THR A 102     2074   2433   2219   -345    244    197       N  
ATOM     46  CA  THR A 102      -2.532  -9.758  40.816  1.00 17.74           C  
ANISOU   46  CA  THR A 102     2072   2550   2118   -188    -95    238       C  
ATOM     47  C   THR A 102      -2.360  -9.960  42.317  1.00 18.08           C  
ANISOU   47  C   THR A 102     2208   2676   1987   -156   -225    372       C  
ATOM     48  O   THR A 102      -2.677 -11.027  42.850  1.00 18.11           O  
ANISOU   48  O   THR A 102     2398   2610   1872   -127    -69    335       O  
ATOM     49  CB  THR A 102      -4.008  -9.450  40.476  1.00 16.94           C  
ANISOU   49  CB  THR A 102     1839   2439   2158      3   -455    244       C  
ATOM     50  CG2 THR A 102      -4.525  -8.273  41.288  1.00 16.52           C  
ANISOU   50  CG2 THR A 102     1655   2536   2087     82   -514     93       C  
ATOM     51  OG1 THR A 102      -4.117  -9.143  39.080  1.00 18.08           O  
ANISOU   51  OG1 THR A 102     1947   2611   2314     85   -401    234       O  
ATOM     52  N   TYR A 103      -1.851  -8.935  42.992  1.00 17.96           N  
ANISOU   52  N   TYR A 103     2070   2825   1928   -172   -399    373       N  
ATOM     53  CA  TYR A 103      -1.535  -9.013  44.412  1.00 18.83           C  
ANISOU   53  CA  TYR A 103     2128   3068   1957   -181   -414    543       C  
ATOM     54  C   TYR A 103      -1.687  -7.623  45.010  1.00 17.32           C  
ANISOU   54  C   TYR A 103     1722   3127   1731   -135   -407    651       C  
ATOM     55  O   TYR A 103      -0.806  -6.783  44.866  1.00 17.58           O  
ANISOU   55  O   TYR A 103     1674   3269   1735     47   -204    781       O  
ATOM     56  CB  TYR A 103      -0.106  -9.547  44.587  1.00 20.81           C  
ANISOU   56  CB  TYR A 103     2596   3144   2169   -248   -586    549       C  
ATOM     57  CG  TYR A 103       0.468  -9.476  45.985  1.00 22.20           C  
ANISOU   57  CG  TYR A 103     2747   3216   2472   -136   -713    491       C  
ATOM     58  CD1 TYR A 103      -0.128 -10.150  47.041  1.00 22.82           C  
ANISOU   58  CD1 TYR A 103     2774   3343   2554     30   -796    457       C  
ATOM     59  CD2 TYR A 103       1.635  -8.762  46.238  1.00 22.48           C  
ANISOU   59  CD2 TYR A 103     2800   3138   2605   -247   -747    501       C  
ATOM     60  CE1 TYR A 103       0.411 -10.093  48.323  1.00 23.70           C  
ANISOU   60  CE1 TYR A 103     2845   3551   2609    -82   -669    356       C  
ATOM     61  CE2 TYR A 103       2.180  -8.697  47.505  1.00 23.37           C  
ANISOU   61  CE2 TYR A 103     2862   3286   2732   -363   -685    612       C  
ATOM     62  CZ  TYR A 103       1.568  -9.361  48.546  1.00 24.21           C  
ANISOU   62  CZ  TYR A 103     2879   3603   2715   -351   -577    365       C  
ATOM     63  OH  TYR A 103       2.123  -9.296  49.806  1.00 25.24           O  
ANISOU   63  OH  TYR A 103     2886   3786   2917   -487   -461    227       O  
ATOM     64  N   GLN A 104      -2.818  -7.369  45.659  1.00 15.71           N  
ANISOU   64  N   GLN A 104     1228   3137   1603    -77   -352    634       N  
ATOM     65  CA  GLN A 104      -3.064  -6.051  46.231  1.00 17.53           C  
ANISOU   65  CA  GLN A 104     1608   3352   1701     15    -58    741       C  
ATOM     66  C   GLN A 104      -2.164  -5.774  47.432  1.00 16.80           C  
ANISOU   66  C   GLN A 104     1845   3092   1445     -2    242    603       C  
ATOM     67  O   GLN A 104      -1.776  -4.634  47.674  1.00 16.31           O  
ANISOU   67  O   GLN A 104     2186   2869   1143     58    356    460       O  
ATOM     68  CB  GLN A 104      -4.543  -5.868  46.587  1.00 20.81           C  
ANISOU   68  CB  GLN A 104     1929   3816   2162     71   -155    854       C  
ATOM     69  CG  GLN A 104      -5.440  -5.739  45.366  1.00 24.88           C  
ANISOU   69  CG  GLN A 104     2414   4287   2751    171    -27    991       C  
ATOM     70  CD  GLN A 104      -6.886  -5.472  45.722  1.00 28.98           C  
ANISOU   70  CD  GLN A 104     3155   4650   3206    237    126   1081       C  
ATOM     71  NE2 GLN A 104      -7.757  -5.486  44.713  1.00 29.40           N  
ANISOU   71  NE2 GLN A 104     3302   4485   3384    209     47   1280       N  
ATOM     72  OE1 GLN A 104      -7.222  -5.260  46.890  1.00 31.82           O  
ANISOU   72  OE1 GLN A 104     3501   5087   3504    332    265    994       O  
ATOM     73  N   GLY A 105      -1.821  -6.820  48.176  1.00 16.84           N  
ANISOU   73  N   GLY A 105     2036   2969   1393   -224    221    623       N  
ATOM     74  CA  GLY A 105      -0.843  -6.696  49.244  1.00 17.65           C  
ANISOU   74  CA  GLY A 105     2301   3021   1384   -292    135    422       C  
ATOM     75  C   GLY A 105      -1.336  -5.939  50.464  1.00 18.51           C  
ANISOU   75  C   GLY A 105     2405   3178   1450   -487   -136    480       C  
ATOM     76  O   GLY A 105      -2.534  -5.689  50.623  1.00 18.53           O  
ANISOU   76  O   GLY A 105     2300   3201   1540   -465   -216    306       O  
ATOM     77  N   SER A 106      -0.402  -5.564  51.330  1.00 18.91           N  
ANISOU   77  N   SER A 106     2404   3292   1491   -573   -364    514       N  
ATOM     78  CA  SER A 106      -0.750  -4.950  52.604  1.00 20.02           C  
ANISOU   78  CA  SER A 106     2608   3406   1594   -265   -304    437       C  
ATOM     79  C   SER A 106      -1.331  -3.551  52.471  1.00 19.23           C  
ANISOU   79  C   SER A 106     2486   3279   1542   -316   -122    369       C  
ATOM     80  O   SER A 106      -2.035  -3.089  53.367  1.00 18.94           O  
ANISOU   80  O   SER A 106     2558   3095   1543   -490    -44    174       O  
ATOM     81  CB  SER A 106       0.466  -4.905  53.524  1.00 21.60           C  
ANISOU   81  CB  SER A 106     2905   3735   1568    -33   -496    419       C  
ATOM     82  OG  SER A 106       0.896  -6.210  53.840  1.00 23.75           O  
ANISOU   82  OG  SER A 106     3129   4197   1699    -82   -362    465       O  
ATOM     83  N   TYR A 107      -1.029  -2.879  51.363  1.00 18.65           N  
ANISOU   83  N   TYR A 107     2240   3305   1542   -319    -58    345       N  
ATOM     84  CA  TYR A 107      -1.438  -1.492  51.187  1.00 17.91           C  
ANISOU   84  CA  TYR A 107     2064   3147   1596   -263    -19    310       C  
ATOM     85  C   TYR A 107      -2.637  -1.343  50.254  1.00 17.51           C  
ANISOU   85  C   TYR A 107     2108   3123   1422     -7    -88    117       C  
ATOM     86  O   TYR A 107      -3.048  -0.228  49.933  1.00 18.51           O  
ANISOU   86  O   TYR A 107     2430   3236   1367    -53    -26     51       O  
ATOM     87  CB  TYR A 107      -0.248  -0.646  50.717  1.00 18.22           C  
ANISOU   87  CB  TYR A 107     1951   3140   1832   -359     31    209       C  
ATOM     88  CG  TYR A 107       0.947  -0.806  51.625  1.00 19.33           C  
ANISOU   88  CG  TYR A 107     2093   3183   2067   -385   -231    182       C  
ATOM     89  CD1 TYR A 107       1.033  -0.097  52.814  1.00 19.78           C  
ANISOU   89  CD1 TYR A 107     2101   3184   2232   -417   -228     73       C  
ATOM     90  CD2 TYR A 107       1.971  -1.690  51.312  1.00 20.21           C  
ANISOU   90  CD2 TYR A 107     2139   3293   2247   -398   -478    152       C  
ATOM     91  CE1 TYR A 107       2.107  -0.250  53.660  1.00 20.98           C  
ANISOU   91  CE1 TYR A 107     2173   3343   2457   -430   -254     33       C  
ATOM     92  CE2 TYR A 107       3.056  -1.853  52.155  1.00 21.51           C  
ANISOU   92  CE2 TYR A 107     2285   3377   2511   -445   -476     10       C  
ATOM     93  CZ  TYR A 107       3.116  -1.129  53.328  1.00 22.06           C  
ANISOU   93  CZ  TYR A 107     2293   3467   2622   -445   -378    -25       C  
ATOM     94  OH  TYR A 107       4.184  -1.281  54.176  1.00 23.91           O  
ANISOU   94  OH  TYR A 107     2519   3622   2942   -456   -379    -77       O  
ATOM     95  N   GLY A 108      -3.206  -2.471  49.840  1.00 16.02           N  
ANISOU   95  N   GLY A 108     1805   2914   1369     93   -117     41       N  
ATOM     96  CA  GLY A 108      -4.372  -2.460  48.973  1.00 16.55           C  
ANISOU   96  CA  GLY A 108     1866   3037   1385    309    -96    107       C  
ATOM     97  C   GLY A 108      -4.079  -1.783  47.649  1.00 16.30           C  
ANISOU   97  C   GLY A 108     1823   3100   1270    368   -174    424       C  
ATOM     98  O   GLY A 108      -4.756  -0.834  47.264  1.00 17.22           O  
ANISOU   98  O   GLY A 108     2002   3303   1239    388    -59    661       O  
ATOM     99  N   PHE A 109      -3.055  -2.276  46.962  1.00 16.13           N  
ANISOU   99  N   PHE A 109     1717   3111   1301    174     92    337       N  
ATOM    100  CA  PHE A 109      -2.570  -1.670  45.730  1.00 15.40           C  
ANISOU  100  CA  PHE A 109     1682   2925   1246     50     20    508       C  
ATOM    101  C   PHE A 109      -3.470  -2.032  44.562  1.00 15.57           C  
ANISOU  101  C   PHE A 109     1791   2740   1384    -43     52    348       C  
ATOM    102  O   PHE A 109      -3.647  -3.210  44.263  1.00 15.44           O  
ANISOU  102  O   PHE A 109     1895   2483   1490     76     93    480       O  
ATOM    103  CB  PHE A 109      -1.136  -2.138  45.455  1.00 16.49           C  
ANISOU  103  CB  PHE A 109     1953   2965   1348      0    106    469       C  
ATOM    104  CG  PHE A 109      -0.580  -1.679  44.134  1.00 17.00           C  
ANISOU  104  CG  PHE A 109     2140   2845   1476   -145     86    444       C  
ATOM    105  CD1 PHE A 109      -0.637  -0.341  43.764  1.00 18.11           C  
ANISOU  105  CD1 PHE A 109     2396   2920   1564   -110    247    392       C  
ATOM    106  CD2 PHE A 109       0.033  -2.585  43.276  1.00 16.66           C  
ANISOU  106  CD2 PHE A 109     2013   2772   1546   -278    123    340       C  
ATOM    107  CE1 PHE A 109      -0.112   0.083  42.553  1.00 18.14           C  
ANISOU  107  CE1 PHE A 109     2537   2803   1551    -80    380    509       C  
ATOM    108  CE2 PHE A 109       0.562  -2.175  42.061  1.00 16.82           C  
ANISOU  108  CE2 PHE A 109     2100   2696   1594   -241    275    437       C  
ATOM    109  CZ  PHE A 109       0.491  -0.837  41.698  1.00 17.33           C  
ANISOU  109  CZ  PHE A 109     2218   2772   1595      0    462    529       C  
ATOM    110  N   ARG A 110      -4.037  -1.011  43.916  1.00 16.03           N  
ANISOU  110  N   ARG A 110     1871   2830   1389    -26   -248    460       N  
ATOM    111  CA  ARG A 110      -4.894  -1.182  42.741  1.00 16.22           C  
ANISOU  111  CA  ARG A 110     1807   2876   1480     19   -126    398       C  
ATOM    112  C   ARG A 110      -4.507  -0.178  41.662  1.00 14.40           C  
ANISOU  112  C   ARG A 110     1509   2566   1397   -351    -32    336       C  
ATOM    113  O   ARG A 110      -3.887   0.845  41.946  1.00 14.96           O  
ANISOU  113  O   ARG A 110     1716   2568   1399   -425    -49    539       O  
ATOM    114  CB  ARG A 110      -6.373  -0.968  43.101  1.00 19.14           C  
ANISOU  114  CB  ARG A 110     2134   3260   1879    -88    -40    568       C  
ATOM    115  CG  ARG A 110      -6.917  -1.865  44.187  1.00 23.15           C  
ANISOU  115  CG  ARG A 110     2634   3721   2441    -60    123    625       C  
ATOM    116  CD  ARG A 110      -8.266  -1.350  44.706  1.00 28.20           C  
ANISOU  116  CD  ARG A 110     3506   4201   3008   -324     -7    685       C  
ATOM    117  NE  ARG A 110      -8.171   0.011  45.241  1.00 32.67           N  
ANISOU  117  NE  ARG A 110     4238   4734   3441   -567     58    856       N  
ATOM    118  CZ  ARG A 110      -7.743   0.310  46.466  1.00 35.19           C  
ANISOU  118  CZ  ARG A 110     4589   5010   3771   -811     13   1096       C  
ATOM    119  NH1 ARG A 110      -7.363  -0.656  47.294  1.00 36.02           N1+
ANISOU  119  NH1 ARG A 110     4557   5227   3902   -652   -126   1269       N1+
ATOM    120  NH2 ARG A 110      -7.695   1.575  46.868  1.00 35.61           N  
ANISOU  120  NH2 ARG A 110     4790   4882   3859  -1112     47   1123       N  
ATOM    121  N   LEU A 111      -4.887  -0.467  40.423  1.00 13.52           N  
ANISOU  121  N   LEU A 111     1379   2386   1372   -425    261    356       N  
ATOM    122  CA  LEU A 111      -4.693   0.483  39.334  1.00 12.49           C  
ANISOU  122  CA  LEU A 111     1224   2140   1381   -369     23     90       C  
ATOM    123  C   LEU A 111      -6.031   1.125  38.989  1.00 13.86           C  
ANISOU  123  C   LEU A 111     1455   2238   1571   -317    -16     55       C  
ATOM    124  O   LEU A 111      -7.079   0.494  39.111  1.00 15.66           O  
ANISOU  124  O   LEU A 111     1486   2714   1751   -455     67     37       O  
ATOM    125  CB  LEU A 111      -4.106  -0.208  38.099  1.00 12.24           C  
ANISOU  125  CB  LEU A 111     1314   1826   1510   -378    189    188       C  
ATOM    126  CG  LEU A 111      -2.709  -0.802  38.260  1.00 12.23           C  
ANISOU  126  CG  LEU A 111     1379   1729   1538   -168    141     86       C  
ATOM    127  CD1 LEU A 111      -2.233  -1.416  36.961  1.00 12.47           C  
ANISOU  127  CD1 LEU A 111     1627   1508   1601    -18    -24    265       C  
ATOM    128  CD2 LEU A 111      -1.734   0.268  38.719  1.00 11.99           C  
ANISOU  128  CD2 LEU A 111     1477   1668   1412   -168     98   -198       C  
ATOM    129  N   GLY A 112      -5.992   2.383  38.575  1.00 13.65           N  
ANISOU  129  N   GLY A 112     1669   2003   1515    -32    -14     83       N  
ATOM    130  CA  GLY A 112      -7.176   3.060  38.082  1.00 12.53           C  
ANISOU  130  CA  GLY A 112     1626   1815   1319     86    -55    221       C  
ATOM    131  C   GLY A 112      -6.837   3.759  36.781  1.00 13.34           C  
ANISOU  131  C   GLY A 112     1788   1921   1358    208   -310     70       C  
ATOM    132  O   GLY A 112      -5.666   4.058  36.510  1.00 13.52           O  
ANISOU  132  O   GLY A 112     1829   2043   1266      0   -489    189       O  
ATOM    133  N   PHE A 113      -7.856   4.011  35.966  1.00 12.94           N  
ANISOU  133  N   PHE A 113     1577   1875   1463    256   -255   -120       N  
ATOM    134  CA  PHE A 113      -7.646   4.629  34.666  1.00 12.54           C  
ANISOU  134  CA  PHE A 113     1588   1690   1487    376   -181     19       C  
ATOM    135  C   PHE A 113      -8.700   5.709  34.432  1.00 14.07           C  
ANISOU  135  C   PHE A 113     1683   1966   1698    146    -19    170       C  
ATOM    136  O   PHE A 113      -9.765   5.699  35.061  1.00 13.84           O  
ANISOU  136  O   PHE A 113     1285   2133   1840    231    -21    280       O  
ATOM    137  CB  PHE A 113      -7.704   3.573  33.553  1.00 12.11           C  
ANISOU  137  CB  PHE A 113     1567   1552   1483    384   -107    -78       C  
ATOM    138  CG  PHE A 113      -6.781   2.398  33.771  1.00 11.64           C  
ANISOU  138  CG  PHE A 113     1664   1482   1276    426   -328   -232       C  
ATOM    139  CD1 PHE A 113      -7.192   1.309  34.529  1.00 11.60           C  
ANISOU  139  CD1 PHE A 113     1736   1586   1084    496   -372   -185       C  
ATOM    140  CD2 PHE A 113      -5.513   2.382  33.205  1.00 11.67           C  
ANISOU  140  CD2 PHE A 113     1618   1495   1322    470   -307   -270       C  
ATOM    141  CE1 PHE A 113      -6.348   0.221  34.736  1.00 11.49           C  
ANISOU  141  CE1 PHE A 113     1751   1552   1060    834   -136   -115       C  
ATOM    142  CE2 PHE A 113      -4.659   1.299  33.399  1.00 12.50           C  
ANISOU  142  CE2 PHE A 113     1835   1447   1466    462   -122     -9       C  
ATOM    143  CZ  PHE A 113      -5.077   0.217  34.169  1.00 13.02           C  
ANISOU  143  CZ  PHE A 113     1900   1574   1472    618   -230     -6       C  
ATOM    144  N   LEU A 114      -8.396   6.650  33.542  1.00 14.25           N  
ANISOU  144  N   LEU A 114     1751   1961   1701    -49     72    -15       N  
ATOM    145  CA  LEU A 114      -9.356   7.684  33.188  1.00 13.36           C  
ANISOU  145  CA  LEU A 114     1605   1741   1731     59    -53   -257       C  
ATOM    146  C   LEU A 114     -10.513   7.051  32.418  1.00 13.80           C  
ANISOU  146  C   LEU A 114     1633   1854   1755    105    -62   -227       C  
ATOM    147  O   LEU A 114     -10.348   6.015  31.773  1.00 14.12           O  
ANISOU  147  O   LEU A 114     1547   1841   1976    213   -229   -269       O  
ATOM    148  CB  LEU A 114      -8.697   8.781  32.349  1.00 13.93           C  
ANISOU  148  CB  LEU A 114     1816   1676   1801    -62    -45   -531       C  
ATOM    149  CG  LEU A 114      -7.601   9.648  32.967  1.00 13.33           C  
ANISOU  149  CG  LEU A 114     1856   1431   1778    -68     79   -543       C  
ATOM    150  CD1 LEU A 114      -7.227  10.766  32.013  1.00 13.41           C  
ANISOU  150  CD1 LEU A 114     1684   1487   1922    -55    250   -592       C  
ATOM    151  CD2 LEU A 114      -8.051  10.226  34.301  1.00 14.64           C  
ANISOU  151  CD2 LEU A 114     2251   1395   1915    -74   -142   -528       C  
ATOM    152  N   HIS A 115     -11.686   7.672  32.494  1.00 13.76           N  
ANISOU  152  N   HIS A 115     1497   2055   1677    123   -210   -430       N  
ATOM    153  CA  HIS A 115     -12.863   7.186  31.779  1.00 13.48           C  
ANISOU  153  CA  HIS A 115     1551   1851   1719     -9   -271   -375       C  
ATOM    154  C   HIS A 115     -13.070   8.075  30.557  1.00 13.08           C  
ANISOU  154  C   HIS A 115     1481   1777   1710      3   -137   -349       C  
ATOM    155  O   HIS A 115     -13.937   8.949  30.533  1.00 13.94           O  
ANISOU  155  O   HIS A 115     1588   2033   1675   -210    193   -216       O  
ATOM    156  CB  HIS A 115     -14.081   7.188  32.702  1.00 14.35           C  
ANISOU  156  CB  HIS A 115     1747   1749   1956   -157   -407   -134       C  
ATOM    157  CG  HIS A 115     -13.805   6.615  34.058  1.00 16.46           C  
ANISOU  157  CG  HIS A 115     2148   1706   2399   -189   -393    -69       C  
ATOM    158  CD2 HIS A 115     -13.777   7.190  35.283  1.00 16.81           C  
ANISOU  158  CD2 HIS A 115     2221   1761   2406   -210   -639    -78       C  
ATOM    159  ND1 HIS A 115     -13.490   5.286  34.254  1.00 18.04           N  
ANISOU  159  ND1 HIS A 115     2489   1711   2655   -238   -371     59       N  
ATOM    160  CE1 HIS A 115     -13.290   5.069  35.543  1.00 17.93           C  
ANISOU  160  CE1 HIS A 115     2566   1761   2487   -187   -608   -122       C  
ATOM    161  NE2 HIS A 115     -13.458   6.210  36.189  1.00 17.14           N  
ANISOU  161  NE2 HIS A 115     2415   1715   2381    -98   -660    -47       N  
ATOM    162  N   SER A 116     -12.250   7.829  29.541  1.00 12.75           N  
ANISOU  162  N   SER A 116     1403   1687   1756     20    -83   -247       N  
ATOM    163  CA  SER A 116     -12.091   8.744  28.419  1.00 12.97           C  
ANISOU  163  CA  SER A 116     1338   1895   1696     51   -150    -57       C  
ATOM    164  C   SER A 116     -13.037   8.539  27.248  1.00 12.39           C  
ANISOU  164  C   SER A 116     1148   1894   1666    163   -385   -138       C  
ATOM    165  O   SER A 116     -13.153   9.417  26.389  1.00 13.56           O  
ANISOU  165  O   SER A 116     1254   2192   1705     34   -216   -121       O  
ATOM    166  CB  SER A 116     -10.652   8.699  27.928  1.00 13.89           C  
ANISOU  166  CB  SER A 116     1100   2293   1885     43   -164    135       C  
ATOM    167  OG  SER A 116      -9.793   9.008  28.999  1.00 15.47           O  
ANISOU  167  OG  SER A 116     1154   2599   2124   -142     71    210       O  
ATOM    168  N   GLY A 117     -13.699   7.389  27.196  1.00 11.86           N  
ANISOU  168  N   GLY A 117     1086   1751   1668    231   -541   -261       N  
ATOM    169  CA  GLY A 117     -14.608   7.106  26.092  1.00 12.60           C  
ANISOU  169  CA  GLY A 117     1540   1757   1490     72   -174   -176       C  
ATOM    170  C   GLY A 117     -13.897   6.696  24.807  1.00 12.80           C  
ANISOU  170  C   GLY A 117     1682   1871   1309   -117    137    -85       C  
ATOM    171  O   GLY A 117     -12.687   6.514  24.801  1.00 13.07           O  
ANISOU  171  O   GLY A 117     1838   1887   1242   -366    344     38       O  
ATOM    172  N   THR A 118     -14.650   6.544  23.718  1.00 13.35           N  
ANISOU  172  N   THR A 118     1723   2082   1266    -52     63     41       N  
ATOM    173  CA  THR A 118     -14.071   6.081  22.450  1.00 13.67           C  
ANISOU  173  CA  THR A 118     1507   2288   1399   -109   -115    292       C  
ATOM    174  C   THR A 118     -14.276   7.008  21.250  1.00 14.82           C  
ANISOU  174  C   THR A 118     1599   2490   1540   -201   -101    429       C  
ATOM    175  O   THR A 118     -14.255   6.545  20.108  1.00 16.16           O  
ANISOU  175  O   THR A 118     1879   2640   1620   -152    -71    357       O  
ATOM    176  CB  THR A 118     -14.592   4.688  22.049  1.00 13.28           C  
ANISOU  176  CB  THR A 118     1430   2208   1407     29   -268    298       C  
ATOM    177  CG2 THR A 118     -14.265   3.650  23.120  1.00 12.34           C  
ANISOU  177  CG2 THR A 118     1429   1910   1350    193   -358    199       C  
ATOM    178  OG1 THR A 118     -16.010   4.747  21.839  1.00 14.21           O  
ANISOU  178  OG1 THR A 118     1470   2516   1414    -92   -535    360       O  
ATOM    179  N   ALA A 119     -14.473   8.303  21.491  1.00 14.45           N  
ANISOU  179  N   ALA A 119     1500   2463   1528   -461   -115    634       N  
ATOM    180  CA  ALA A 119     -14.526   9.262  20.384  1.00 15.44           C  
ANISOU  180  CA  ALA A 119     1818   2634   1415   -526   -201    690       C  
ATOM    181  C   ALA A 119     -13.217   9.224  19.606  1.00 17.57           C  
ANISOU  181  C   ALA A 119     2268   3007   1400   -633   -267    623       C  
ATOM    182  O   ALA A 119     -12.167   8.944  20.178  1.00 17.43           O  
ANISOU  182  O   ALA A 119     2172   3161   1288   -513     15    625       O  
ATOM    183  CB  ALA A 119     -14.780  10.652  20.895  1.00 15.79           C  
ANISOU  183  CB  ALA A 119     1829   2627   1544   -519   -289    808       C  
ATOM    184  N   LYS A 120     -13.275   9.525  18.310  1.00 20.14           N  
ANISOU  184  N   LYS A 120     2758   3318   1576   -897   -379    552       N  
ATOM    185  CA  LYS A 120     -12.088   9.452  17.455  1.00 23.97           C  
ANISOU  185  CA  LYS A 120     3451   3938   1720   -829   -621    589       C  
ATOM    186  C   LYS A 120     -10.902  10.290  17.937  1.00 25.01           C  
ANISOU  186  C   LYS A 120     3567   3995   1941   -541   -500    724       C  
ATOM    187  O   LYS A 120      -9.751   9.942  17.680  1.00 26.01           O  
ANISOU  187  O   LYS A 120     3612   4186   2085   -333   -542    885       O  
ATOM    188  CB  LYS A 120     -12.438   9.819  16.010  1.00 26.87           C  
ANISOU  188  CB  LYS A 120     4070   4424   1716   -864  -1011    344       C  
ATOM    189  CG  LYS A 120     -12.574   8.600  15.110  1.00 30.77           C  
ANISOU  189  CG  LYS A 120     4730   4973   1989   -840   -983    223       C  
ATOM    190  CD  LYS A 120     -13.208   8.917  13.757  1.00 33.04           C  
ANISOU  190  CD  LYS A 120     5180   5364   2009   -881   -748    -21       C  
ATOM    191  CE  LYS A 120     -13.769   7.637  13.129  1.00 34.22           C  
ANISOU  191  CE  LYS A 120     5480   5606   1916   -902   -736   -200       C  
ATOM    192  NZ  LYS A 120     -14.352   7.810  11.765  1.00 34.83           N1+
ANISOU  192  NZ  LYS A 120     5588   5809   1838   -794   -704   -193       N1+
ATOM    193  N   SER A 121     -11.185  11.382  18.637  1.00 25.05           N  
ANISOU  193  N   SER A 121     3611   3715   2193   -456   -410    486       N  
ATOM    194  CA  SER A 121     -10.139  12.307  19.057  1.00 26.96           C  
ANISOU  194  CA  SER A 121     3676   3685   2881   -354   -205    329       C  
ATOM    195  C   SER A 121      -9.335  11.847  20.286  1.00 26.44           C  
ANISOU  195  C   SER A 121     3395   3693   2959   -355    -63    555       C  
ATOM    196  O   SER A 121      -8.292  12.434  20.588  1.00 27.83           O  
ANISOU  196  O   SER A 121     3596   3903   3074   -483   -186    825       O  
ATOM    197  CB  SER A 121     -10.734  13.693  19.315  1.00 29.58           C  
ANISOU  197  CB  SER A 121     4137   3636   3466   -456   -159    105       C  
ATOM    198  OG  SER A 121     -11.625  13.659  20.422  1.00 31.14           O  
ANISOU  198  OG  SER A 121     4439   3580   3813   -604    -75     48       O  
ATOM    199  N   VAL A 122      -9.795  10.815  20.995  1.00 23.50           N  
ANISOU  199  N   VAL A 122     2732   3306   2892   -204    279    463       N  
ATOM    200  CA  VAL A 122      -9.058  10.356  22.180  1.00 21.88           C  
ANISOU  200  CA  VAL A 122     2231   3273   2811   -126    381    391       C  
ATOM    201  C   VAL A 122      -7.675   9.797  21.826  1.00 22.18           C  
ANISOU  201  C   VAL A 122     2040   3449   2938   -326    446    632       C  
ATOM    202  O   VAL A 122      -7.495   9.145  20.797  1.00 22.52           O  
ANISOU  202  O   VAL A 122     1914   3505   3137   -200    324    630       O  
ATOM    203  CB  VAL A 122      -9.853   9.332  23.039  1.00 20.78           C  
ANISOU  203  CB  VAL A 122     2019   3165   2712   -368    513    199       C  
ATOM    204  CG1 VAL A 122     -11.195   9.909  23.443  1.00 20.79           C  
ANISOU  204  CG1 VAL A 122     2005   3112   2781   -740    497    287       C  
ATOM    205  CG2 VAL A 122     -10.029   8.012  22.312  1.00 20.45           C  
ANISOU  205  CG2 VAL A 122     2013   3203   2554   -313    608    295       C  
ATOM    206  N   THR A 123      -6.698  10.071  22.683  1.00 21.71           N  
ANISOU  206  N   THR A 123     1927   3401   2921   -383    605    721       N  
ATOM    207  CA  THR A 123      -5.328   9.634  22.437  1.00 23.06           C  
ANISOU  207  CA  THR A 123     2341   3498   2922   -279    473    750       C  
ATOM    208  C   THR A 123      -5.002   8.434  23.301  1.00 20.81           C  
ANISOU  208  C   THR A 123     2088   3283   2538   -388    410    641       C  
ATOM    209  O   THR A 123      -3.985   7.767  23.115  1.00 20.49           O  
ANISOU  209  O   THR A 123     2273   3132   2380   -317    488    647       O  
ATOM    210  CB  THR A 123      -4.323  10.750  22.724  1.00 25.31           C  
ANISOU  210  CB  THR A 123     2865   3766   2986   -156    441    793       C  
ATOM    211  CG2 THR A 123      -4.564  11.934  21.791  1.00 26.23           C  
ANISOU  211  CG2 THR A 123     2910   3837   3221     67    513    845       C  
ATOM    212  OG1 THR A 123      -4.464  11.180  24.078  1.00 25.69           O  
ANISOU  212  OG1 THR A 123     3170   3952   2640   -171    393    765       O  
ATOM    213  N   CYS A 124      -5.886   8.172  24.252  1.00 19.70           N  
ANISOU  213  N   CYS A 124     1881   3180   2425   -321    240    232       N  
ATOM    214  CA  CYS A 124      -5.688   7.109  25.213  1.00 19.19           C  
ANISOU  214  CA  CYS A 124     1683   3209   2399   -354    135    -73       C  
ATOM    215  C   CYS A 124      -7.036   6.736  25.815  1.00 17.08           C  
ANISOU  215  C   CYS A 124     1521   2685   2283   -391    107    -21       C  
ATOM    216  O   CYS A 124      -7.763   7.608  26.291  1.00 17.81           O  
ANISOU  216  O   CYS A 124     1408   2741   2618   -309    335    129       O  
ATOM    217  CB  CYS A 124      -4.728   7.596  26.301  1.00 21.17           C  
ANISOU  217  CB  CYS A 124     1721   3727   2595   -348    -46   -101       C  
ATOM    218  SG  CYS A 124      -4.302   6.378  27.523  1.00 24.34           S  
ANISOU  218  SG  CYS A 124     1997   4465   2786   -509   -299   -426       S  
ATOM    219  N   THR A 125      -7.378   5.450  25.781  1.00 13.88           N  
ANISOU  219  N   THR A 125     1398   1998   1878   -400   -262    -70       N  
ATOM    220  CA  THR A 125      -8.622   4.982  26.400  1.00 13.33           C  
ANISOU  220  CA  THR A 125     1505   1662   1898   -313   -449     -1       C  
ATOM    221  C   THR A 125      -8.541   3.549  26.936  1.00 13.71           C  
ANISOU  221  C   THR A 125     1728   1633   1848   -158   -438     20       C  
ATOM    222  O   THR A 125      -7.981   2.661  26.289  1.00 16.51           O  
ANISOU  222  O   THR A 125     2262   1865   2144    -12   -261    175       O  
ATOM    223  CB  THR A 125      -9.835   5.135  25.448  1.00 13.36           C  
ANISOU  223  CB  THR A 125     1538   1581   1957   -554   -238    175       C  
ATOM    224  CG2 THR A 125      -9.748   4.156  24.272  1.00 13.55           C  
ANISOU  224  CG2 THR A 125     1637   1619   1893   -421   -367    162       C  
ATOM    225  OG1 THR A 125     -11.049   4.922  26.183  1.00 13.64           O  
ANISOU  225  OG1 THR A 125     1597   1616   1969   -654    180    488       O  
ATOM    226  N   TYR A 126      -9.109   3.336  28.120  1.00 12.13           N  
ANISOU  226  N   TYR A 126     1624   1557   1428   -122   -680   -194       N  
ATOM    227  CA  TYR A 126      -9.024   2.052  28.809  1.00 10.90           C  
ANISOU  227  CA  TYR A 126     1590   1379   1171   -183   -615     77       C  
ATOM    228  C   TYR A 126     -10.343   1.293  28.765  1.00 11.33           C  
ANISOU  228  C   TYR A 126     1658   1453   1195      1   -492    280       C  
ATOM    229  O   TYR A 126     -11.407   1.866  29.009  1.00 11.90           O  
ANISOU  229  O   TYR A 126     1750   1603   1167   -157   -576    263       O  
ATOM    230  CB  TYR A 126      -8.591   2.256  30.266  1.00 11.18           C  
ANISOU  230  CB  TYR A 126     1680   1463   1107   -206   -290     57       C  
ATOM    231  CG  TYR A 126      -8.676   1.013  31.107  1.00 11.43           C  
ANISOU  231  CG  TYR A 126     1611   1469   1264   -189   -382    -33       C  
ATOM    232  CD1 TYR A 126      -7.728   0.003  30.993  1.00 11.18           C  
ANISOU  232  CD1 TYR A 126     1377   1527   1344   -321   -609    -23       C  
ATOM    233  CD2 TYR A 126      -9.702   0.850  32.035  1.00 12.16           C  
ANISOU  233  CD2 TYR A 126     1905   1493   1223    -43   -408    -90       C  
ATOM    234  CE1 TYR A 126      -7.808  -1.140  31.778  1.00 11.23           C  
ANISOU  234  CE1 TYR A 126     1557   1386   1323   -407   -697     44       C  
ATOM    235  CE2 TYR A 126      -9.790  -0.289  32.817  1.00 10.44           C  
ANISOU  235  CE2 TYR A 126     1763   1272    930   -156   -566    -37       C  
ATOM    236  CZ  TYR A 126      -8.843  -1.273  32.687  1.00 11.34           C  
ANISOU  236  CZ  TYR A 126     1852   1333   1125   -315   -529    -58       C  
ATOM    237  OH  TYR A 126      -8.942  -2.402  33.473  1.00 13.43           O  
ANISOU  237  OH  TYR A 126     1998   1732   1374   -384   -155    -90       O  
ATOM    238  N   SER A 127     -10.267   0.001  28.458  1.00 11.68           N  
ANISOU  238  N   SER A 127     1718   1523   1195    -48   -397    164       N  
ATOM    239  CA  SER A 127     -11.437  -0.878  28.463  1.00 12.14           C  
ANISOU  239  CA  SER A 127     1922   1512   1179     13   -417    -21       C  
ATOM    240  C   SER A 127     -11.545  -1.719  29.744  1.00 11.74           C  
ANISOU  240  C   SER A 127     1803   1467   1190     35   -357    127       C  
ATOM    241  O   SER A 127     -10.753  -2.644  29.943  1.00 11.44           O  
ANISOU  241  O   SER A 127     1793   1362   1192    330   -360    222       O  
ATOM    242  CB  SER A 127     -11.385  -1.813  27.259  1.00 11.51           C  
ANISOU  242  CB  SER A 127     1948   1322   1104     65   -414   -248       C  
ATOM    243  OG  SER A 127     -12.378  -2.813  27.354  1.00 11.49           O  
ANISOU  243  OG  SER A 127     1783   1376   1206     38   -665   -231       O  
ATOM    244  N   PRO A 128     -12.535  -1.412  30.607  1.00 12.16           N  
ANISOU  244  N   PRO A 128     1956   1263   1400   -148   -408     95       N  
ATOM    245  CA  PRO A 128     -12.750  -2.223  31.814  1.00 12.27           C  
ANISOU  245  CA  PRO A 128     1867   1207   1587   -228    -79    171       C  
ATOM    246  C   PRO A 128     -13.078  -3.659  31.451  1.00 11.75           C  
ANISOU  246  C   PRO A 128     1570   1201   1695   -158   -160    208       C  
ATOM    247  O   PRO A 128     -12.540  -4.581  32.060  1.00 12.35           O  
ANISOU  247  O   PRO A 128     1474   1332   1887   -388   -570    178       O  
ATOM    248  CB  PRO A 128     -13.981  -1.577  32.465  1.00 12.10           C  
ANISOU  248  CB  PRO A 128     1913   1101   1584    -35    393    192       C  
ATOM    249  CG  PRO A 128     -14.015  -0.193  31.936  1.00 12.91           C  
ANISOU  249  CG  PRO A 128     2007   1189   1710    145    205    205       C  
ATOM    250  CD  PRO A 128     -13.474  -0.278  30.533  1.00 11.87           C  
ANISOU  250  CD  PRO A 128     1977   1148   1385    131   -133     64       C  
ATOM    251  N   ALA A 129     -13.953  -3.846  30.468  1.00 12.06           N  
ANISOU  251  N   ALA A 129     1427   1385   1769    -91     -2    308       N  
ATOM    252  CA  ALA A 129     -14.383  -5.187  30.082  1.00 13.71           C  
ANISOU  252  CA  ALA A 129     1607   1740   1863    -60    -84    -12       C  
ATOM    253  C   ALA A 129     -13.222  -6.060  29.619  1.00 13.68           C  
ANISOU  253  C   ALA A 129     1767   1529   1904    -57   -135     62       C  
ATOM    254  O   ALA A 129     -13.211  -7.260  29.875  1.00 14.41           O  
ANISOU  254  O   ALA A 129     1825   1756   1894   -200   -222    585       O  
ATOM    255  CB  ALA A 129     -15.453  -5.114  29.012  1.00 13.70           C  
ANISOU  255  CB  ALA A 129     1764   1852   1588    -97   -310    -24       C  
ATOM    256  N   LEU A 130     -12.253  -5.453  28.936  1.00 13.81           N  
ANISOU  256  N   LEU A 130     1827   1516   1905     -4    -44   -122       N  
ATOM    257  CA  LEU A 130     -11.102  -6.183  28.395  1.00 13.73           C  
ANISOU  257  CA  LEU A 130     1811   1576   1831   -147    -18    166       C  
ATOM    258  C   LEU A 130      -9.840  -6.046  29.252  1.00 13.38           C  
ANISOU  258  C   LEU A 130     1626   1660   1796     92    -61    130       C  
ATOM    259  O   LEU A 130      -8.819  -6.660  28.947  1.00 14.72           O  
ANISOU  259  O   LEU A 130     1908   1619   2068    128   -114     28       O  
ATOM    260  CB  LEU A 130     -10.791  -5.703  26.975  1.00 13.61           C  
ANISOU  260  CB  LEU A 130     1922   1576   1674   -144    -61    197       C  
ATOM    261  CG  LEU A 130     -11.910  -5.785  25.936  1.00 13.09           C  
ANISOU  261  CG  LEU A 130     1845   1418   1709     32   -281    407       C  
ATOM    262  CD1 LEU A 130     -11.457  -5.131  24.653  1.00 12.75           C  
ANISOU  262  CD1 LEU A 130     1898   1296   1650    108   -415    645       C  
ATOM    263  CD2 LEU A 130     -12.288  -7.220  25.676  1.00 14.17           C  
ANISOU  263  CD2 LEU A 130     1894   1534   1956    -20   -201    256       C  
ATOM    264  N   ASN A 131      -9.923  -5.251  30.319  1.00 13.33           N  
ANISOU  264  N   ASN A 131     1590   1897   1576    -28   -104     72       N  
ATOM    265  CA  ASN A 131      -8.746  -4.831  31.092  1.00 12.81           C  
ANISOU  265  CA  ASN A 131     1551   1914   1401     59     25    208       C  
ATOM    266  C   ASN A 131      -7.616  -4.444  30.148  1.00 12.42           C  
ANISOU  266  C   ASN A 131     1644   1839   1238   -128    -77     89       C  
ATOM    267  O   ASN A 131      -6.498  -4.951  30.234  1.00 13.51           O  
ANISOU  267  O   ASN A 131     2085   1965   1084   -153     62   -145       O  
ATOM    268  CB  ASN A 131      -8.287  -5.911  32.077  1.00 12.27           C  
ANISOU  268  CB  ASN A 131     1417   1862   1384    317   -140    396       C  
ATOM    269  CG  ASN A 131      -7.164  -5.432  32.977  1.00 13.05           C  
ANISOU  269  CG  ASN A 131     1773   1746   1439    207     34    308       C  
ATOM    270  ND2 ASN A 131      -6.288  -6.346  33.369  1.00 13.06           N  
ANISOU  270  ND2 ASN A 131     1740   1788   1435    205     11    493       N  
ATOM    271  OD1 ASN A 131      -7.070  -4.244  33.290  1.00 12.94           O  
ANISOU  271  OD1 ASN A 131     1858   1615   1442    200     34    -30       O  
ATOM    272  N   LYS A 132      -7.929  -3.543  29.230  1.00 12.82           N  
ANISOU  272  N   LYS A 132     1702   1756   1414    -83   -121     19       N  
ATOM    273  CA  LYS A 132      -7.031  -3.266  28.131  1.00 12.37           C  
ANISOU  273  CA  LYS A 132     1805   1513   1383    111      4   -189       C  
ATOM    274  C   LYS A 132      -6.936  -1.784  27.846  1.00 11.26           C  
ANISOU  274  C   LYS A 132     1683   1396   1201    290     63   -240       C  
ATOM    275  O   LYS A 132      -7.937  -1.081  27.716  1.00 10.21           O  
ANISOU  275  O   LYS A 132     1436   1160   1283    224    -53    -83       O  
ATOM    276  CB  LYS A 132      -7.461  -4.037  26.885  1.00 11.98           C  
ANISOU  276  CB  LYS A 132     1713   1440   1399     92   -101   -271       C  
ATOM    277  CG  LYS A 132      -6.585  -3.813  25.670  1.00 10.62           C  
ANISOU  277  CG  LYS A 132     1575   1167   1293   -148    -55   -345       C  
ATOM    278  CD  LYS A 132      -6.812  -4.911  24.647  1.00 11.34           C  
ANISOU  278  CD  LYS A 132     1804   1238   1267    103   -185   -641       C  
ATOM    279  CE  LYS A 132      -5.889  -4.741  23.456  1.00 12.78           C  
ANISOU  279  CE  LYS A 132     2138   1270   1447     13   -138   -785       C  
ATOM    280  NZ  LYS A 132      -6.008  -5.892  22.526  1.00 13.81           N1+
ANISOU  280  NZ  LYS A 132     2306   1382   1560     83     16   -870       N1+
ATOM    281  N   MET A 133      -5.698  -1.329  27.768  1.00 12.41           N  
ANISOU  281  N   MET A 133     1743   1807   1165    489     87   -291       N  
ATOM    282  CA AMET A 133      -5.407   0.061  27.468  0.76 12.69           C  
ANISOU  282  CA AMET A 133     1656   1954   1212    474    -11   -419       C  
ATOM    283  CA BMET A 133      -5.381   0.053  27.470  0.24 13.04           C  
ANISOU  283  CA BMET A 133     1858   1830   1267    586    -24   -342       C  
ATOM    284  C   MET A 133      -5.143   0.227  25.973  1.00 12.89           C  
ANISOU  284  C   MET A 133     1763   1906   1229    512    103   -390       C  
ATOM    285  O   MET A 133      -4.365  -0.517  25.382  1.00 13.94           O  
ANISOU  285  O   MET A 133     1830   2094   1371    371    147   -604       O  
ATOM    286  CB AMET A 133      -4.194   0.534  28.271  0.76 13.48           C  
ANISOU  286  CB AMET A 133     1784   2131   1206    362   -203   -582       C  
ATOM    287  CB BMET A 133      -4.115   0.424  28.231  0.24 14.19           C  
ANISOU  287  CB BMET A 133     2180   1811   1399    730   -260   -346       C  
ATOM    288  CG AMET A 133      -3.724   1.928  27.906  0.76 16.54           C  
ANISOU  288  CG AMET A 133     2266   2445   1573    448   -129   -709       C  
ATOM    289  CG BMET A 133      -3.727   1.867  28.150  0.24 16.05           C  
ANISOU  289  CG BMET A 133     2612   1850   1634    933   -370   -360       C  
ATOM    290  SD AMET A 133      -4.956   3.201  28.243  0.76 20.03           S  
ANISOU  290  SD AMET A 133     2488   2915   2208    277   -192   -617       S  
ATOM    291  SD BMET A 133      -3.314   2.412  29.807  0.24 18.14           S  
ANISOU  291  SD BMET A 133     2962   1995   1937    968   -473   -339       S  
ATOM    292  CE AMET A 133      -4.540   3.647  29.928  0.76 21.38           C  
ANISOU  292  CE AMET A 133     2801   3025   2298    293     65   -625       C  
ATOM    293  CE BMET A 133      -4.528   3.710  30.016  0.24 18.57           C  
ANISOU  293  CE BMET A 133     3058   2002   1994    965   -388   -358       C  
ATOM    294  N   PHE A 134      -5.811   1.200  25.358  1.00 11.97           N  
ANISOU  294  N   PHE A 134     1554   1886   1108    321    -58    -37       N  
ATOM    295  CA  PHE A 134      -5.559   1.526  23.953  1.00 11.21           C  
ANISOU  295  CA  PHE A 134     1152   1893   1213    242     -2    129       C  
ATOM    296  C   PHE A 134      -4.950   2.922  23.895  1.00 12.31           C  
ANISOU  296  C   PHE A 134     1105   2111   1460    516     93    270       C  
ATOM    297  O   PHE A 134      -5.549   3.888  24.355  1.00 11.95           O  
ANISOU  297  O   PHE A 134     1028   1951   1563    753     32    182       O  
ATOM    298  CB  PHE A 134      -6.851   1.487  23.130  1.00 11.82           C  
ANISOU  298  CB  PHE A 134     1353   1876   1264    272     57     59       C  
ATOM    299  CG  PHE A 134      -7.525   0.134  23.099  1.00 12.31           C  
ANISOU  299  CG  PHE A 134     1607   1592   1477    444    102   -178       C  
ATOM    300  CD1 PHE A 134      -8.290  -0.309  24.179  1.00 12.75           C  
ANISOU  300  CD1 PHE A 134     1856   1376   1612    482     -6      3       C  
ATOM    301  CD2 PHE A 134      -7.422  -0.676  21.978  1.00 11.99           C  
ANISOU  301  CD2 PHE A 134     1627   1394   1536    377     80   -353       C  
ATOM    302  CE1 PHE A 134      -8.927  -1.545  24.146  1.00 13.27           C  
ANISOU  302  CE1 PHE A 134     1994   1432   1616    368    -96    -61       C  
ATOM    303  CE2 PHE A 134      -8.046  -1.916  21.934  1.00 12.46           C  
ANISOU  303  CE2 PHE A 134     1824   1439   1471    205    140   -142       C  
ATOM    304  CZ  PHE A 134      -8.803  -2.352  23.017  1.00 12.84           C  
ANISOU  304  CZ  PHE A 134     1900   1384   1595    257    -25    -90       C  
ATOM    305  N   CYS A 135      -3.744   3.031  23.359  1.00 15.36           N  
ANISOU  305  N   CYS A 135     1778   2459   1600    158    383    415       N  
ATOM    306  CA  CYS A 135      -3.038   4.301  23.398  1.00 17.26           C  
ANISOU  306  CA  CYS A 135     1799   2817   1943      1    464    480       C  
ATOM    307  C   CYS A 135      -2.243   4.543  22.125  1.00 17.92           C  
ANISOU  307  C   CYS A 135     1938   2817   2054   -218    546    635       C  
ATOM    308  O   CYS A 135      -2.022   3.627  21.336  1.00 18.95           O  
ANISOU  308  O   CYS A 135     1928   2879   2392      2    588    615       O  
ATOM    309  CB  CYS A 135      -2.118   4.350  24.615  1.00 19.72           C  
ANISOU  309  CB  CYS A 135     2068   3084   2340    101    331    464       C  
ATOM    310  SG  CYS A 135      -0.783   3.128  24.599  1.00 20.99           S  
ANISOU  310  SG  CYS A 135     2162   3376   2437    268    258    500       S  
ATOM    311  N   GLN A 136      -1.822   5.787  21.932  1.00 18.61           N  
ANISOU  311  N   GLN A 136     2274   2777   2019   -354    607    715       N  
ATOM    312  CA  GLN A 136      -1.046   6.147  20.757  1.00 19.02           C  
ANISOU  312  CA  GLN A 136     2216   2932   2080   -305    428    676       C  
ATOM    313  C   GLN A 136       0.443   6.192  21.057  1.00 19.18           C  
ANISOU  313  C   GLN A 136     2292   2999   1995   -261    225    541       C  
ATOM    314  O   GLN A 136       0.850   6.405  22.205  1.00 19.10           O  
ANISOU  314  O   GLN A 136     2330   3061   1865   -350    227    507       O  
ATOM    315  CB  GLN A 136      -1.501   7.499  20.215  1.00 20.94           C  
ANISOU  315  CB  GLN A 136     2354   3125   2477   -311     97    755       C  
ATOM    316  CG  GLN A 136      -2.873   7.496  19.569  1.00 22.95           C  
ANISOU  316  CG  GLN A 136     2601   3214   2906   -154   -507    871       C  
ATOM    317  CD  GLN A 136      -3.320   8.890  19.188  1.00 25.50           C  
ANISOU  317  CD  GLN A 136     2984   3383   3320    -35  -1050    936       C  
ATOM    318  NE2 GLN A 136      -4.370   8.977  18.383  1.00 28.09           N  
ANISOU  318  NE2 GLN A 136     3513   3672   3489   -290  -1009    844       N  
ATOM    319  OE1 GLN A 136      -2.726   9.879  19.614  1.00 25.91           O  
ANISOU  319  OE1 GLN A 136     3045   3263   3535    223  -1157    998       O  
ATOM    320  N   LEU A 137       1.238   5.992  20.005  1.00 19.35           N  
ANISOU  320  N   LEU A 137     2240   3100   2013   -102    107    156       N  
ATOM    321  CA  LEU A 137       2.699   6.022  20.064  1.00 19.79           C  
ANISOU  321  CA  LEU A 137     2240   3245   2035     28    140    -90       C  
ATOM    322  C   LEU A 137       3.223   7.329  20.649  1.00 18.51           C  
ANISOU  322  C   LEU A 137     2093   3092   1848     -1     11    -58       C  
ATOM    323  O   LEU A 137       2.896   8.411  20.158  1.00 17.57           O  
ANISOU  323  O   LEU A 137     1877   2984   1814     98    -86    126       O  
ATOM    324  CB  LEU A 137       3.278   5.819  18.656  1.00 21.33           C  
ANISOU  324  CB  LEU A 137     2344   3466   2296    296    426   -178       C  
ATOM    325  CG  LEU A 137       4.766   6.096  18.424  1.00 23.42           C  
ANISOU  325  CG  LEU A 137     2770   3727   2403    781    548   -265       C  
ATOM    326  CD1 LEU A 137       5.585   5.225  19.312  1.00 22.12           C  
ANISOU  326  CD1 LEU A 137     2380   3621   2405   1270    398   -155       C  
ATOM    327  CD2 LEU A 137       5.152   5.847  16.983  1.00 25.08           C  
ANISOU  327  CD2 LEU A 137     3094   3886   2551    830    541   -473       C  
ATOM    328  N   ALA A 138       4.028   7.209  21.705  1.00 18.61           N  
ANISOU  328  N   ALA A 138     2372   3021   1679    -53   -141    -72       N  
ATOM    329  CA  ALA A 138       4.698   8.343  22.358  1.00 19.52           C  
ANISOU  329  CA  ALA A 138     2578   3098   1742    -85   -198     16       C  
ATOM    330  C   ALA A 138       3.780   9.350  23.068  1.00 19.40           C  
ANISOU  330  C   ALA A 138     2651   3003   1719   -159   -174    100       C  
ATOM    331  O   ALA A 138       4.265  10.325  23.642  1.00 20.81           O  
ANISOU  331  O   ALA A 138     2745   2995   2165   -402    -24      4       O  
ATOM    332  CB  ALA A 138       5.634   9.067  21.378  1.00 19.38           C  
ANISOU  332  CB  ALA A 138     2534   3090   1738   -117   -193    -40       C  
ATOM    333  N   LYS A 139       2.471   9.115  23.039  1.00 18.99           N  
ANISOU  333  N   LYS A 139     2682   3017   1515    -87   -122    418       N  
ATOM    334  CA  LYS A 139       1.515  10.020  23.681  1.00 19.05           C  
ANISOU  334  CA  LYS A 139     2635   2891   1713   -118   -160    672       C  
ATOM    335  C   LYS A 139       1.336   9.678  25.160  1.00 17.07           C  
ANISOU  335  C   LYS A 139     2189   2563   1732    -55   -161    744       C  
ATOM    336  O   LYS A 139       1.603   8.553  25.583  1.00 15.30           O  
ANISOU  336  O   LYS A 139     1848   2486   1479    -66   -275   1037       O  
ATOM    337  CB  LYS A 139       0.151   9.971  22.976  1.00 21.32           C  
ANISOU  337  CB  LYS A 139     3047   3144   1909   -253    -21    904       C  
ATOM    338  CG  LYS A 139       0.132  10.456  21.529  1.00 23.70           C  
ANISOU  338  CG  LYS A 139     3527   3285   2192   -274    116   1040       C  
ATOM    339  CD  LYS A 139      -0.139  11.948  21.427  1.00 26.86           C  
ANISOU  339  CD  LYS A 139     4065   3628   2512   -406    288   1040       C  
ATOM    340  CE  LYS A 139      -0.566  12.347  20.009  1.00 29.27           C  
ANISOU  340  CE  LYS A 139     4531   3848   2742   -626    555    996       C  
ATOM    341  NZ  LYS A 139       0.343  11.792  18.964  1.00 30.84           N1+
ANISOU  341  NZ  LYS A 139     4866   3996   2856   -822    601   1095       N1+
ATOM    342  N   THR A 140       0.870  10.655  25.935  1.00 16.91           N  
ANISOU  342  N   THR A 140     2180   2363   1884     18   -259    443       N  
ATOM    343  CA  THR A 140       0.639  10.468  27.362  1.00 16.74           C  
ANISOU  343  CA  THR A 140     2077   2216   2066    241   -300    189       C  
ATOM    344  C   THR A 140      -0.341   9.331  27.619  1.00 16.12           C  
ANISOU  344  C   THR A 140     1876   2176   2074    356   -400    219       C  
ATOM    345  O   THR A 140      -1.374   9.214  26.963  1.00 16.49           O  
ANISOU  345  O   THR A 140     1750   2259   2257    243   -655    460       O  
ATOM    346  CB  THR A 140       0.100  11.750  28.025  1.00 17.41           C  
ANISOU  346  CB  THR A 140     2292   2122   2200    446   -346   -102       C  
ATOM    347  CG2 THR A 140      -0.169  11.528  29.510  1.00 17.59           C  
ANISOU  347  CG2 THR A 140     2419   2129   2134    521   -576    -67       C  
ATOM    348  OG1 THR A 140       1.060  12.799  27.876  1.00 19.02           O  
ANISOU  348  OG1 THR A 140     2434   2399   2393    408   -180   -116       O  
ATOM    349  N   CYS A 141       0.009   8.491  28.583  1.00 15.79           N  
ANISOU  349  N   CYS A 141     1802   2161   2038    485   -260    104       N  
ATOM    350  CA ACYS A 141      -0.841   7.385  29.003  0.39 14.90           C  
ANISOU  350  CA ACYS A 141     1742   1945   1975    311   -208    -48       C  
ATOM    351  CA BCYS A 141      -0.830   7.380  28.989  0.61 15.53           C  
ANISOU  351  CA BCYS A 141     1745   2091   2066    332   -265   -147       C  
ATOM    352  C   CYS A 141      -0.974   7.402  30.513  1.00 14.29           C  
ANISOU  352  C   CYS A 141     1723   1887   1818    248   -146    120       C  
ATOM    353  O   CYS A 141      -0.119   6.873  31.225  1.00 12.06           O  
ANISOU  353  O   CYS A 141     1267   1815   1500    213   -241    285       O  
ATOM    354  CB ACYS A 141      -0.244   6.053  28.566  0.39 15.41           C  
ANISOU  354  CB ACYS A 141     1818   2007   2032    160   -147   -276       C  
ATOM    355  CB BCYS A 141      -0.190   6.074  28.521  0.61 17.65           C  
ANISOU  355  CB BCYS A 141     1896   2526   2284    211   -265   -531       C  
ATOM    356  SG ACYS A 141      -0.046   5.884  26.804  0.39 15.76           S  
ANISOU  356  SG ACYS A 141     1841   2081   2066     93    -77   -428       S  
ATOM    357  SG BCYS A 141      -1.194   4.611  28.728  0.61 19.44           S  
ANISOU  357  SG BCYS A 141     1975   2927   2484    223   -287   -781       S  
ATOM    358  N   PRO A 142      -2.045   8.034  31.017  1.00 14.31           N  
ANISOU  358  N   PRO A 142     2086   1713   1639    293   -155     63       N  
ATOM    359  CA  PRO A 142      -2.205   8.125  32.472  1.00 14.41           C  
ANISOU  359  CA  PRO A 142     2250   1665   1559    319   -107    -61       C  
ATOM    360  C   PRO A 142      -2.581   6.790  33.115  1.00 13.72           C  
ANISOU  360  C   PRO A 142     2141   1513   1560    369   -160   -248       C  
ATOM    361  O   PRO A 142      -3.496   6.107  32.657  1.00 13.86           O  
ANISOU  361  O   PRO A 142     2074   1679   1515    534   -185   -224       O  
ATOM    362  CB  PRO A 142      -3.353   9.129  32.644  1.00 16.08           C  
ANISOU  362  CB  PRO A 142     2533   1874   1703    433    -91    -48       C  
ATOM    363  CG  PRO A 142      -3.460   9.847  31.327  1.00 15.03           C  
ANISOU  363  CG  PRO A 142     2433   1758   1520    502   -189    -97       C  
ATOM    364  CD  PRO A 142      -3.058   8.829  30.301  1.00 14.22           C  
ANISOU  364  CD  PRO A 142     2247   1722   1432    397   -175    -45       C  
ATOM    365  N   VAL A 143      -1.858   6.430  34.169  1.00 13.55           N  
ANISOU  365  N   VAL A 143     2057   1454   1636    305   -239   -218       N  
ATOM    366  CA  VAL A 143      -2.189   5.271  34.982  1.00 13.81           C  
ANISOU  366  CA  VAL A 143     2041   1382   1823    -70   -139   -260       C  
ATOM    367  C   VAL A 143      -2.216   5.724  36.433  1.00 14.21           C  
ANISOU  367  C   VAL A 143     2013   1417   1970   -156   -197   -309       C  
ATOM    368  O   VAL A 143      -1.297   6.403  36.894  1.00 13.56           O  
ANISOU  368  O   VAL A 143     2108   1203   1842   -167   -353   -762       O  
ATOM    369  CB  VAL A 143      -1.175   4.118  34.807  1.00 13.88           C  
ANISOU  369  CB  VAL A 143     2180   1300   1792    -77   -122   -185       C  
ATOM    370  CG1 VAL A 143      -1.585   2.921  35.664  1.00 12.36           C  
ANISOU  370  CG1 VAL A 143     1944   1093   1661   -236   -297   -211       C  
ATOM    371  CG2 VAL A 143      -1.074   3.704  33.348  1.00 14.16           C  
ANISOU  371  CG2 VAL A 143     2225   1445   1708   -195   -258     63       C  
ATOM    372  N   GLN A 144      -3.279   5.364  37.145  1.00 14.14           N  
ANISOU  372  N   GLN A 144     1702   1551   2120    112    110   -216       N  
ATOM    373  CA  GLN A 144      -3.437   5.770  38.532  1.00 13.58           C  
ANISOU  373  CA  GLN A 144     1662   1397   2099    464     89   -285       C  
ATOM    374  C   GLN A 144      -3.049   4.654  39.483  1.00 13.79           C  
ANISOU  374  C   GLN A 144     1505   1694   2040    401     45   -267       C  
ATOM    375  O   GLN A 144      -3.452   3.506  39.303  1.00 14.70           O  
ANISOU  375  O   GLN A 144     1632   1831   2123    426   -192   -133       O  
ATOM    376  CB  GLN A 144      -4.888   6.190  38.804  1.00 13.05           C  
ANISOU  376  CB  GLN A 144     1744   1071   2145    494    -97   -211       C  
ATOM    377  CG  GLN A 144      -5.338   7.425  38.034  1.00 13.57           C  
ANISOU  377  CG  GLN A 144     1983   1026   2147    486   -371   -302       C  
ATOM    378  CD  GLN A 144      -6.823   7.629  38.115  1.00 15.44           C  
ANISOU  378  CD  GLN A 144     2415   1249   2202    336   -769   -166       C  
ATOM    379  NE2 GLN A 144      -7.284   8.816  37.729  1.00 16.87           N  
ANISOU  379  NE2 GLN A 144     2769   1280   2359    284   -785    -27       N  
ATOM    380  OE1 GLN A 144      -7.555   6.733  38.533  1.00 16.85           O  
ANISOU  380  OE1 GLN A 144     2517   1749   2137    250   -881   -301       O  
ATOM    381  N   LEU A 145      -2.267   5.003  40.498  1.00 12.48           N  
ANISOU  381  N   LEU A 145     1075   1870   1797    166     35   -417       N  
ATOM    382  CA  LEU A 145      -1.950   4.078  41.577  1.00 13.90           C  
ANISOU  382  CA  LEU A 145     1191   2249   1841    128     71   -591       C  
ATOM    383  C   LEU A 145      -2.867   4.374  42.765  1.00 15.49           C  
ANISOU  383  C   LEU A 145     1751   2405   1729    161    197   -339       C  
ATOM    384  O   LEU A 145      -2.820   5.472  43.326  1.00 16.70           O  
ANISOU  384  O   LEU A 145     2079   2441   1826    183    130   -397       O  
ATOM    385  CB  LEU A 145      -0.491   4.248  42.004  1.00 14.80           C  
ANISOU  385  CB  LEU A 145     1227   2332   2066     74    -14   -866       C  
ATOM    386  CG  LEU A 145       0.543   4.311  40.882  1.00 15.74           C  
ANISOU  386  CG  LEU A 145     1403   2413   2164     -2    -87  -1267       C  
ATOM    387  CD1 LEU A 145       1.937   4.514  41.458  1.00 17.37           C  
ANISOU  387  CD1 LEU A 145     1527   2674   2399     40   -143  -1225       C  
ATOM    388  CD2 LEU A 145       0.481   3.041  40.056  1.00 16.46           C  
ANISOU  388  CD2 LEU A 145     1780   2352   2123     28    156  -1320       C  
ATOM    389  N   TRP A 146      -3.703   3.406  43.138  1.00 15.32           N  
ANISOU  389  N   TRP A 146     1876   2405   1541    204    425    220       N  
ATOM    390  CA  TRP A 146      -4.569   3.540  44.313  1.00 15.45           C  
ANISOU  390  CA  TRP A 146     1944   2433   1494    425    495    357       C  
ATOM    391  C   TRP A 146      -4.086   2.618  45.424  1.00 16.54           C  
ANISOU  391  C   TRP A 146     2344   2588   1351    422    403    412       C  
ATOM    392  O   TRP A 146      -3.709   1.470  45.170  1.00 16.48           O  
ANISOU  392  O   TRP A 146     2497   2594   1171    356    520    402       O  
ATOM    393  CB  TRP A 146      -6.026   3.199  43.969  1.00 15.10           C  
ANISOU  393  CB  TRP A 146     1710   2260   1767    386    433    570       C  
ATOM    394  CG  TRP A 146      -6.682   4.163  43.021  1.00 15.92           C  
ANISOU  394  CG  TRP A 146     1652   2287   2111    512    430    562       C  
ATOM    395  CD1 TRP A 146      -6.387   4.341  41.704  1.00 16.30           C  
ANISOU  395  CD1 TRP A 146     1620   2274   2298    540    337    590       C  
ATOM    396  CD2 TRP A 146      -7.759   5.067  43.312  1.00 17.14           C  
ANISOU  396  CD2 TRP A 146     1662   2540   2308    535    488    621       C  
ATOM    397  CE2 TRP A 146      -8.052   5.765  42.125  1.00 16.13           C  
ANISOU  397  CE2 TRP A 146     1454   2424   2251    581    538    753       C  
ATOM    398  CE3 TRP A 146      -8.500   5.355  44.465  1.00 18.00           C  
ANISOU  398  CE3 TRP A 146     1786   2664   2389    562    538    512       C  
ATOM    399  NE1 TRP A 146      -7.201   5.303  41.158  1.00 16.32           N  
ANISOU  399  NE1 TRP A 146     1477   2389   2337    382    347    647       N  
ATOM    400  CZ2 TRP A 146      -9.056   6.738  42.056  1.00 17.01           C  
ANISOU  400  CZ2 TRP A 146     1419   2630   2413    702    642    594       C  
ATOM    401  CZ3 TRP A 146      -9.494   6.319  44.393  1.00 17.77           C  
ANISOU  401  CZ3 TRP A 146     1627   2743   2382    834    546    471       C  
ATOM    402  CH2 TRP A 146      -9.761   6.999  43.201  1.00 17.45           C  
ANISOU  402  CH2 TRP A 146     1497   2725   2410    844    609    463       C  
ATOM    403  N   VAL A 147      -4.091   3.129  46.653  1.00 17.40           N  
ANISOU  403  N   VAL A 147     2461   2790   1360    393     54    470       N  
ATOM    404  CA  VAL A 147      -3.747   2.333  47.832  1.00 18.71           C  
ANISOU  404  CA  VAL A 147     2491   3038   1580    530    206    386       C  
ATOM    405  C   VAL A 147      -4.723   2.625  48.974  1.00 20.64           C  
ANISOU  405  C   VAL A 147     2605   3414   1825    398    219     63       C  
ATOM    406  O   VAL A 147      -5.228   3.748  49.100  1.00 20.59           O  
ANISOU  406  O   VAL A 147     2463   3482   1879    595    305   -282       O  
ATOM    407  CB  VAL A 147      -2.293   2.597  48.320  1.00 17.87           C  
ANISOU  407  CB  VAL A 147     2266   2899   1625    719     -9    495       C  
ATOM    408  CG1 VAL A 147      -1.277   2.172  47.272  1.00 17.99           C  
ANISOU  408  CG1 VAL A 147     2184   3006   1646    765     14    593       C  
ATOM    409  CG2 VAL A 147      -2.099   4.061  48.675  1.00 18.61           C  
ANISOU  409  CG2 VAL A 147     2265   3047   1761    421    -32    420       C  
ATOM    410  N   ASP A 148      -4.993   1.614  49.794  1.00 21.27           N  
ANISOU  410  N   ASP A 148     2735   3495   1850    267    240    185       N  
ATOM    411  CA  ASP A 148      -5.829   1.799  50.978  1.00 22.43           C  
ANISOU  411  CA  ASP A 148     2866   3692   1963    305    531    -64       C  
ATOM    412  C   ASP A 148      -5.029   2.440  52.113  1.00 22.90           C  
ANISOU  412  C   ASP A 148     3049   3817   1837    457    633    -12       C  
ATOM    413  O   ASP A 148      -5.578   3.172  52.934  1.00 22.78           O  
ANISOU  413  O   ASP A 148     3255   3860   1539    581    704    -66       O  
ATOM    414  CB  ASP A 148      -6.414   0.466  51.453  1.00 24.91           C  
ANISOU  414  CB  ASP A 148     3150   3842   2471    436    393   -255       C  
ATOM    415  CG  ASP A 148      -7.337  -0.170  50.435  1.00 27.10           C  
ANISOU  415  CG  ASP A 148     3345   4019   2931    386    436   -195       C  
ATOM    416  OD1 ASP A 148      -7.927   0.561  49.608  1.00 27.47           O  
ANISOU  416  OD1 ASP A 148     3377   4067   2995    317    317   -208       O  
ATOM    417  OD2 ASP A 148      -7.477  -1.413  50.468  1.00 28.54           O1-
ANISOU  417  OD2 ASP A 148     3445   4228   3171    340    568   -194       O1-
ATOM    418  N   SER A 149      -3.732   2.149  52.149  1.00 23.68           N  
ANISOU  418  N   SER A 149     3063   3881   2053    532    396     27       N  
ATOM    419  CA  SER A 149      -2.825   2.700  53.148  1.00 24.52           C  
ANISOU  419  CA  SER A 149     3027   3995   2295    316    375    230       C  
ATOM    420  C   SER A 149      -1.537   3.156  52.468  1.00 23.26           C  
ANISOU  420  C   SER A 149     2672   3861   2305    268    295    133       C  
ATOM    421  O   SER A 149      -1.071   2.512  51.531  1.00 21.04           O  
ANISOU  421  O   SER A 149     2473   3660   1859    458    205    257       O  
ATOM    422  CB  SER A 149      -2.502   1.648  54.204  1.00 26.57           C  
ANISOU  422  CB  SER A 149     3263   4269   2562    278    365    498       C  
ATOM    423  OG  SER A 149      -3.581   0.754  54.369  1.00 28.88           O  
ANISOU  423  OG  SER A 149     3683   4548   2741    540    247    571       O  
ATOM    424  N   THR A 150      -0.964   4.259  52.948  1.00 24.55           N  
ANISOU  424  N   THR A 150     2741   3977   2610     76    256   -153       N  
ATOM    425  CA  THR A 150       0.270   4.808  52.378  1.00 25.42           C  
ANISOU  425  CA  THR A 150     2713   4087   2861   -202    242   -501       C  
ATOM    426  C   THR A 150       1.476   3.908  52.658  1.00 24.97           C  
ANISOU  426  C   THR A 150     2485   4265   2737   -553    148   -702       C  
ATOM    427  O   THR A 150       1.763   3.595  53.810  1.00 25.06           O  
ANISOU  427  O   THR A 150     2311   4346   2865   -700     78   -875       O  
ATOM    428  CB  THR A 150       0.566   6.221  52.922  1.00 27.56           C  
ANISOU  428  CB  THR A 150     3106   4165   3200   -227    101   -529       C  
ATOM    429  CG2 THR A 150       1.802   6.799  52.264  1.00 27.44           C  
ANISOU  429  CG2 THR A 150     3204   4015   3206   -307    130   -575       C  
ATOM    430  OG1 THR A 150      -0.549   7.088  52.672  1.00 29.81           O  
ANISOU  430  OG1 THR A 150     3514   4364   3448   -314    -11   -508       O  
ATOM    431  N   PRO A 151       2.189   3.494  51.592  1.00 24.59           N  
ANISOU  431  N   PRO A 151     2488   4366   2491   -573     58   -717       N  
ATOM    432  CA  PRO A 151       3.375   2.632  51.674  1.00 24.46           C  
ANISOU  432  CA  PRO A 151     2435   4482   2376   -578    258   -654       C  
ATOM    433  C   PRO A 151       4.564   3.380  52.276  1.00 25.48           C  
ANISOU  433  C   PRO A 151     2590   4706   2384   -838    272   -528       C  
ATOM    434  O   PRO A 151       4.558   4.610  52.275  1.00 26.58           O  
ANISOU  434  O   PRO A 151     2723   4842   2535   -845    588   -708       O  
ATOM    435  CB  PRO A 151       3.655   2.282  50.204  1.00 24.14           C  
ANISOU  435  CB  PRO A 151     2355   4481   2336   -336    223   -747       C  
ATOM    436  CG  PRO A 151       2.400   2.584  49.478  1.00 23.85           C  
ANISOU  436  CG  PRO A 151     2292   4414   2356   -316    113   -718       C  
ATOM    437  CD  PRO A 151       1.808   3.747  50.196  1.00 24.65           C  
ANISOU  437  CD  PRO A 151     2521   4427   2416   -425    -31   -649       C  
ATOM    438  N   PRO A 152       5.566   2.645  52.787  1.00 26.22           N  
ANISOU  438  N   PRO A 152     2772   4872   2320  -1069   -266   -242       N  
ATOM    439  CA  PRO A 152       6.740   3.213  53.464  1.00 26.65           C  
ANISOU  439  CA  PRO A 152     2839   4929   2356  -1317   -698   -262       C  
ATOM    440  C   PRO A 152       7.491   4.261  52.644  1.00 27.13           C  
ANISOU  440  C   PRO A 152     3000   4957   2352  -1434   -694   -533       C  
ATOM    441  O   PRO A 152       7.351   4.307  51.417  1.00 26.92           O  
ANISOU  441  O   PRO A 152     2894   4914   2422  -1245   -796   -596       O  
ATOM    442  CB  PRO A 152       7.647   1.994  53.657  1.00 27.28           C  
ANISOU  442  CB  PRO A 152     2873   5028   2464  -1351   -875    -73       C  
ATOM    443  CG  PRO A 152       6.716   0.838  53.720  1.00 27.61           C  
ANISOU  443  CG  PRO A 152     2853   5151   2487  -1317   -824     56       C  
ATOM    444  CD  PRO A 152       5.609   1.171  52.763  1.00 26.91           C  
ANISOU  444  CD  PRO A 152     2840   5039   2344  -1278   -551    -52       C  
ATOM    445  N   PRO A 153       8.290   5.101  53.326  1.00 28.53           N  
ANISOU  445  N   PRO A 153     3465   5030   2343  -1619   -346   -696       N  
ATOM    446  CA  PRO A 153       9.246   5.982  52.648  1.00 28.30           C  
ANISOU  446  CA  PRO A 153     3491   4959   2301  -1496   -139   -666       C  
ATOM    447  C   PRO A 153      10.160   5.127  51.793  1.00 26.53           C  
ANISOU  447  C   PRO A 153     3111   4740   2229  -1356   -295   -572       C  
ATOM    448  O   PRO A 153      10.564   4.058  52.253  1.00 28.14           O  
ANISOU  448  O   PRO A 153     3300   5043   2350  -1220   -371   -555       O  
ATOM    449  CB  PRO A 153      10.070   6.569  53.801  1.00 28.87           C  
ANISOU  449  CB  PRO A 153     3602   5034   2332  -1624    -38   -796       C  
ATOM    450  CG  PRO A 153       9.198   6.462  55.003  1.00 29.38           C  
ANISOU  450  CG  PRO A 153     3783   5085   2296  -1708    -67   -675       C  
ATOM    451  CD  PRO A 153       8.304   5.272  54.792  1.00 29.25           C  
ANISOU  451  CD  PRO A 153     3679   5112   2320  -1689   -113   -653       C  
ATOM    452  N   GLY A 154      10.469   5.564  50.577  1.00 22.91           N  
ANISOU  452  N   GLY A 154     2565   4246   1893  -1375   -395   -419       N  
ATOM    453  CA  GLY A 154      11.402   4.828  49.742  1.00 19.85           C  
ANISOU  453  CA  GLY A 154     2040   3801   1701   -932   -247   -326       C  
ATOM    454  C   GLY A 154      10.764   3.766  48.869  1.00 18.54           C  
ANISOU  454  C   GLY A 154     1868   3493   1684   -347   -108   -135       C  
ATOM    455  O   GLY A 154      11.460   3.067  48.137  1.00 19.07           O  
ANISOU  455  O   GLY A 154     1845   3318   2081    230   -265   -197       O  
ATOM    456  N   THR A 155       9.442   3.638  48.950  1.00 16.97           N  
ANISOU  456  N   THR A 155     1614   3405   1427    -78   -365     71       N  
ATOM    457  CA  THR A 155       8.702   2.710  48.101  1.00 15.73           C  
ANISOU  457  CA  THR A 155     1518   3123   1335     17   -344    302       C  
ATOM    458  C   THR A 155       8.864   3.157  46.648  1.00 16.06           C  
ANISOU  458  C   THR A 155     1565   3125   1411    199   -106    223       C  
ATOM    459  O   THR A 155       8.906   4.360  46.366  1.00 15.88           O  
ANISOU  459  O   THR A 155     1499   3150   1384     84    155    274       O  
ATOM    460  CB  THR A 155       7.193   2.684  48.467  1.00 15.73           C  
ANISOU  460  CB  THR A 155     1551   2921   1506   -313   -305    670       C  
ATOM    461  CG2 THR A 155       6.404   1.793  47.518  1.00 15.24           C  
ANISOU  461  CG2 THR A 155     1298   2888   1605   -462   -469    762       C  
ATOM    462  OG1 THR A 155       7.028   2.204  49.803  1.00 17.00           O  
ANISOU  462  OG1 THR A 155     1598   2901   1962   -153   -374    736       O  
ATOM    463  N   ARG A 156       8.966   2.187  45.739  1.00 15.22           N  
ANISOU  463  N   ARG A 156     1489   2955   1338    226   -452     40       N  
ATOM    464  CA  ARG A 156       9.069   2.447  44.304  1.00 13.98           C  
ANISOU  464  CA  ARG A 156     1488   2609   1217     50   -361   -172       C  
ATOM    465  C   ARG A 156       8.009   1.647  43.544  1.00 14.27           C  
ANISOU  465  C   ARG A 156     1660   2551   1211    148    -68    -57       C  
ATOM    466  O   ARG A 156       7.504   0.646  44.049  1.00 15.01           O  
ANISOU  466  O   ARG A 156     1923   2608   1173     68   -115    -60       O  
ATOM    467  CB  ARG A 156      10.469   2.078  43.798  1.00 12.90           C  
ANISOU  467  CB  ARG A 156     1051   2305   1543    201   -475   -212       C  
ATOM    468  CG  ARG A 156      11.496   3.191  43.957  1.00 14.14           C  
ANISOU  468  CG  ARG A 156     1189   2426   1758    494   -486   -166       C  
ATOM    469  CD  ARG A 156      12.823   2.692  44.510  1.00 15.58           C  
ANISOU  469  CD  ARG A 156     1569   2403   1949    413   -407   -376       C  
ATOM    470  NE  ARG A 156      13.508   1.696  43.678  1.00 15.74           N  
ANISOU  470  NE  ARG A 156     1842   2359   1779    267   -408   -518       N  
ATOM    471  CZ  ARG A 156      14.348   1.983  42.684  1.00 15.96           C  
ANISOU  471  CZ  ARG A 156     2116   2337   1610     92   -690   -553       C  
ATOM    472  NH1 ARG A 156      14.591   3.241  42.355  1.00 16.14           N1+
ANISOU  472  NH1 ARG A 156     2224   2273   1635     18   -556   -582       N1+
ATOM    473  NH2 ARG A 156      14.939   1.009  42.005  1.00 16.36           N  
ANISOU  473  NH2 ARG A 156     2205   2485   1525      7   -921   -369       N  
ATOM    474  N   VAL A 157       7.647   2.100  42.334  1.00  0.00           N  
ATOM    475  CA  VAL A 157       6.823   1.241  41.487  1.00  0.00           C  
ATOM    476  C   VAL A 157       7.424   1.106  40.108  1.00  0.00           C  
ATOM    477  O   VAL A 157       7.967   2.042  39.546  1.00  0.00           O  
ATOM    478  CB  VAL A 157       5.355   1.819  41.406  1.00  0.00           C  
ATOM    479  CG1 VAL A 157       5.208   3.251  40.823  1.00  0.00           C  
ATOM    480  CG2 VAL A 157       4.381   0.941  40.582  1.00  0.00           C  
ATOM    481  N   ARG A 158       7.322  -0.115  39.582  1.00 11.94           N  
ANISOU  481  N   ARG A 158     1651   1745   1140    361   -272    -68       N  
ATOM    482  CA  ARG A 158       8.039  -0.534  38.383  1.00 10.91           C  
ANISOU  482  CA  ARG A 158     1350   1666   1128    453   -178     57       C  
ATOM    483  C   ARG A 158       7.062  -0.997  37.295  1.00 11.69           C  
ANISOU  483  C   ARG A 158     1435   1880   1127    282    -40    222       C  
ATOM    484  O   ARG A 158       6.078  -1.671  37.589  1.00 12.81           O  
ANISOU  484  O   ARG A 158     1553   2148   1165    -74    117    235       O  
ATOM    485  CB  ARG A 158       8.973  -1.691  38.747  1.00 10.41           C  
ANISOU  485  CB  ARG A 158     1207   1536   1212    522   -275    -16       C  
ATOM    486  CG  ARG A 158       9.838  -2.196  37.600  1.00 11.31           C  
ANISOU  486  CG  ARG A 158     1521   1457   1319    681   -333   -118       C  
ATOM    487  CD  ARG A 158      10.760  -3.314  38.068  1.00 10.91           C  
ANISOU  487  CD  ARG A 158     1285   1556   1305    462   -370   -120       C  
ATOM    488  NE  ARG A 158      11.547  -2.897  39.227  1.00 12.07           N  
ANISOU  488  NE  ARG A 158     1309   1823   1453    137   -264    -69       N  
ATOM    489  CZ  ARG A 158      12.743  -2.321  39.157  1.00 12.20           C  
ANISOU  489  CZ  ARG A 158     1266   1851   1519    108   -286   -277       C  
ATOM    490  NH1 ARG A 158      13.310  -2.106  37.978  1.00 11.88           N1+
ANISOU  490  NH1 ARG A 158     1135   1880   1500    169   -173   -316       N1+
ATOM    491  NH2 ARG A 158      13.375  -1.966  40.270  1.00 12.15           N  
ANISOU  491  NH2 ARG A 158     1327   1859   1430     61   -216   -389       N  
ATOM    492  N   ALA A 159       7.330  -0.639  36.041  1.00 10.95           N  
ANISOU  492  N   ALA A 159     1245   1671   1242    175    -29     65       N  
ATOM    493  CA  ALA A 159       6.529  -1.137  34.922  1.00  9.76           C  
ANISOU  493  CA  ALA A 159     1134   1369   1207    140   -157    -15       C  
ATOM    494  C   ALA A 159       7.400  -1.981  34.006  1.00 11.71           C  
ANISOU  494  C   ALA A 159     1345   1747   1357   -139     -5   -310       C  
ATOM    495  O   ALA A 159       8.541  -1.620  33.710  1.00 12.59           O  
ANISOU  495  O   ALA A 159     1365   2149   1271   -462    197   -192       O  
ATOM    496  CB  ALA A 159       5.922   0.004  34.144  1.00  7.94           C  
ANISOU  496  CB  ALA A 159      945   1042   1031    403   -407     72       C  
ATOM    497  N   MET A 160       6.849  -3.105  33.564  1.00 11.50           N  
ANISOU  497  N   MET A 160     1293   1517   1560    -28    -98   -485       N  
ATOM    498  CA  MET A 160       7.544  -4.028  32.675  1.00 12.83           C  
ANISOU  498  CA  MET A 160     1409   1658   1807    204   -161   -290       C  
ATOM    499  C   MET A 160       6.537  -4.630  31.704  1.00 12.74           C  
ANISOU  499  C   MET A 160     1338   1792   1712    285   -167   -267       C  
ATOM    500  O   MET A 160       5.415  -4.957  32.093  1.00 13.40           O  
ANISOU  500  O   MET A 160     1108   2235   1749    180   -225   -186       O  
ATOM    501  CB  MET A 160       8.196  -5.143  33.494  1.00 14.18           C  
ANISOU  501  CB  MET A 160     1598   1645   2146    556   -307   -331       C  
ATOM    502  CG  MET A 160       8.853  -6.233  32.667  1.00 15.51           C  
ANISOU  502  CG  MET A 160     1682   1703   2511    509   -433    102       C  
ATOM    503  SD  MET A 160       9.434  -7.587  33.703  1.00 18.00           S  
ANISOU  503  SD  MET A 160     1797   2178   2865    352   -713    244       S  
ATOM    504  CE  MET A 160      10.573  -6.728  34.781  1.00 17.47           C  
ANISOU  504  CE  MET A 160     1882   1945   2811    298   -992    -58       C  
ATOM    505  N   ALA A 161       6.928  -4.777  30.443  1.00 11.83           N  
ANISOU  505  N   ALA A 161     1346   1592   1556    406   -413   -294       N  
ATOM    506  CA  ALA A 161       6.046  -5.383  29.453  1.00 13.05           C  
ANISOU  506  CA  ALA A 161     1744   1520   1696    392   -176   -376       C  
ATOM    507  C   ALA A 161       6.441  -6.834  29.184  1.00 13.51           C  
ANISOU  507  C   ALA A 161     1673   1710   1749    251    121   -292       C  
ATOM    508  O   ALA A 161       7.624  -7.166  29.140  1.00 13.65           O  
ANISOU  508  O   ALA A 161     1556   1849   1782    347    217   -178       O  
ATOM    509  CB  ALA A 161       6.053  -4.575  28.159  1.00 12.73           C  
ANISOU  509  CB  ALA A 161     1989   1442   1405    255   -525   -525       C  
ATOM    510  N   ILE A 162       5.443  -7.698  29.026  1.00 13.99           N  
ANISOU  510  N   ILE A 162     1816   1806   1694    229    138   -315       N  
ATOM    511  CA  ILE A 162       5.664  -9.066  28.568  1.00 13.28           C  
ANISOU  511  CA  ILE A 162     1683   1754   1608    -13     93   -310       C  
ATOM    512  C   ILE A 162       4.665  -9.384  27.458  1.00 14.12           C  
ANISOU  512  C   ILE A 162     1667   1911   1787   -205    -24   -265       C  
ATOM    513  O   ILE A 162       3.624  -8.733  27.352  1.00 13.43           O  
ANISOU  513  O   ILE A 162     1561   1899   1643   -348   -391   -164       O  
ATOM    514  CB  ILE A 162       5.532 -10.112  29.709  1.00 13.16           C  
ANISOU  514  CB  ILE A 162     1622   1793   1587    -91    163   -154       C  
ATOM    515  CG1 ILE A 162       4.099 -10.189  30.231  1.00 13.64           C  
ANISOU  515  CG1 ILE A 162     1876   1877   1431   -240    163     36       C  
ATOM    516  CG2 ILE A 162       6.488  -9.810  30.844  1.00 12.50           C  
ANISOU  516  CG2 ILE A 162     1400   1761   1589     -3    147   -253       C  
ATOM    517  CD1 ILE A 162       3.864 -11.372  31.152  1.00 13.79           C  
ANISOU  517  CD1 ILE A 162     2074   1833   1333   -191    142     10       C  
ATOM    518  N   TYR A 163       4.981 -10.372  26.627  1.00 14.97           N  
ANISOU  518  N   TYR A 163     1771   1990   1927   -165   -171   -395       N  
ATOM    519  CA  TYR A 163       4.024 -10.830  25.629  1.00 15.74           C  
ANISOU  519  CA  TYR A 163     1753   2318   1910   -210   -273   -333       C  
ATOM    520  C   TYR A 163       2.889 -11.608  26.281  1.00 17.90           C  
ANISOU  520  C   TYR A 163     2054   2607   2140   -164   -333   -106       C  
ATOM    521  O   TYR A 163       3.116 -12.435  27.163  1.00 18.96           O  
ANISOU  521  O   TYR A 163     2258   2629   2316   -253   -201    -40       O  
ATOM    522  CB  TYR A 163       4.712 -11.638  24.530  1.00 16.68           C  
ANISOU  522  CB  TYR A 163     1805   2462   2068   -281   -281   -584       C  
ATOM    523  CG  TYR A 163       5.505 -10.746  23.609  1.00 17.55           C  
ANISOU  523  CG  TYR A 163     1885   2731   2052   -290    -71   -664       C  
ATOM    524  CD1 TYR A 163       4.866  -9.793  22.823  1.00 17.16           C  
ANISOU  524  CD1 TYR A 163     1823   2738   1959   -185    -19   -877       C  
ATOM    525  CD2 TYR A 163       6.889 -10.827  23.550  1.00 18.30           C  
ANISOU  525  CD2 TYR A 163     1907   2910   2135   -186    192   -605       C  
ATOM    526  CE1 TYR A 163       5.584  -8.954  21.992  1.00 17.69           C  
ANISOU  526  CE1 TYR A 163     1871   2917   1934   -135     71   -825       C  
ATOM    527  CE2 TYR A 163       7.616  -9.996  22.724  1.00 18.50           C  
ANISOU  527  CE2 TYR A 163     1917   3032   2080   -163    216   -663       C  
ATOM    528  CZ  TYR A 163       6.957  -9.064  21.947  1.00 18.05           C  
ANISOU  528  CZ  TYR A 163     1843   3023   1991   -133    144   -615       C  
ATOM    529  OH  TYR A 163       7.667  -8.230  21.122  1.00 18.44           O  
ANISOU  529  OH  TYR A 163     1975   3093   1937    -22     -7   -416       O  
ATOM    530  N   LYS A 164       1.666 -11.309  25.857  1.00 18.80           N  
ANISOU  530  N   LYS A 164     2081   2871   2190   -159   -412     -1       N  
ATOM    531  CA  LYS A 164       0.473 -11.896  26.455  1.00 19.87           C  
ANISOU  531  CA  LYS A 164     2220   2952   2376   -194   -269    117       C  
ATOM    532  C   LYS A 164       0.335 -13.384  26.127  1.00 20.91           C  
ANISOU  532  C   LYS A 164     2261   3130   2556   -135   -427    343       C  
ATOM    533  O   LYS A 164      -0.121 -14.170  26.956  1.00 20.99           O  
ANISOU  533  O   LYS A 164     2171   3242   2561    -74   -484    464       O  
ATOM    534  CB  LYS A 164      -0.768 -11.124  25.994  1.00 20.78           C  
ANISOU  534  CB  LYS A 164     2499   2940   2456   -168     75     68       C  
ATOM    535  CG  LYS A 164      -2.079 -11.631  26.559  1.00 23.15           C  
ANISOU  535  CG  LYS A 164     3033   3047   2714      8    328    197       C  
ATOM    536  CD  LYS A 164      -3.242 -10.794  26.049  1.00 25.40           C  
ANISOU  536  CD  LYS A 164     3456   3289   2907     16    420    398       C  
ATOM    537  CE  LYS A 164      -4.559 -11.212  26.679  1.00 28.01           C  
ANISOU  537  CE  LYS A 164     3856   3540   3245     22    393    340       C  
ATOM    538  NZ  LYS A 164      -5.371 -12.028  25.736  1.00 29.74           N1+
ANISOU  538  NZ  LYS A 164     4139   3732   3428     95    498    229       N1+
ATOM    539  N   GLN A 165       0.737 -13.768  24.919  1.00 22.20           N  
ANISOU  539  N   GLN A 165     2502   3068   2866   -178   -383    108       N  
ATOM    540  CA  GLN A 165       0.603 -15.150  24.472  1.00 23.57           C  
ANISOU  540  CA  GLN A 165     2910   2929   3117   -253   -475    -74       C  
ATOM    541  C   GLN A 165       1.718 -16.003  25.045  1.00 24.17           C  
ANISOU  541  C   GLN A 165     3264   2832   3087   -321   -548    -99       C  
ATOM    542  O   GLN A 165       2.886 -15.630  24.977  1.00 23.27           O  
ANISOU  542  O   GLN A 165     3163   2706   2971   -293   -455    -98       O  
ATOM    543  CB  GLN A 165       0.635 -15.226  22.945  1.00 25.76           C  
ANISOU  543  CB  GLN A 165     3316   3050   3421   -304   -583   -323       C  
ATOM    544  CG  GLN A 165      -0.434 -14.405  22.258  1.00 28.17           C  
ANISOU  544  CG  GLN A 165     3820   3241   3642   -485   -750   -515       C  
ATOM    545  CD  GLN A 165      -0.139 -14.192  20.794  1.00 31.19           C  
ANISOU  545  CD  GLN A 165     4399   3401   4051   -616   -775   -624       C  
ATOM    546  NE2 GLN A 165      -0.470 -15.180  19.973  1.00 32.84           N  
ANISOU  546  NE2 GLN A 165     4679   3639   4158   -714   -807   -703       N  
ATOM    547  OE1 GLN A 165       0.386 -13.152  20.403  1.00 32.81           O  
ANISOU  547  OE1 GLN A 165     4596   3551   4318   -514   -873   -660       O  
ATOM    548  N   SER A 166       1.351 -17.157  25.593  1.00 25.98           N  
ANISOU  548  N   SER A 166     3615   3002   3255   -247   -766   -295       N  
ATOM    549  CA  SER A 166       2.307 -18.057  26.232  1.00 27.08           C  
ANISOU  549  CA  SER A 166     3897   3001   3391    -95   -889   -335       C  
ATOM    550  C   SER A 166       3.440 -18.498  25.306  1.00 27.38           C  
ANISOU  550  C   SER A 166     3945   2976   3483     71   -778   -507       C  
ATOM    551  O   SER A 166       4.568 -18.698  25.756  1.00 27.08           O  
ANISOU  551  O   SER A 166     3806   3114   3371     24   -938   -569       O  
ATOM    552  CB  SER A 166       1.590 -19.273  26.819  1.00 27.67           C  
ANISOU  552  CB  SER A 166     4072   2961   3479   -384  -1044   -194       C  
ATOM    553  OG  SER A 166       0.787 -19.898  25.840  1.00 29.24           O  
ANISOU  553  OG  SER A 166     4368   3170   3571   -325   -961    -21       O  
ATOM    554  N   GLN A 167       3.154 -18.638  24.014  1.00 27.69           N  
ANISOU  554  N   GLN A 167     3993   2842   3687    128   -563   -624       N  
ATOM    555  CA  GLN A 167       4.193 -19.065  23.072  1.00 28.86           C  
ANISOU  555  CA  GLN A 167     4014   3010   3942    153   -499   -721       C  
ATOM    556  C   GLN A 167       5.206 -17.955  22.753  1.00 27.08           C  
ANISOU  556  C   GLN A 167     3759   2703   3829    127   -290  -1080       C  
ATOM    557  O   GLN A 167       6.171 -18.177  22.020  1.00 27.67           O  
ANISOU  557  O   GLN A 167     3972   2529   4013    -26   -311  -1268       O  
ATOM    558  CB  GLN A 167       3.595 -19.659  21.786  1.00 31.42           C  
ANISOU  558  CB  GLN A 167     4269   3375   4295    157   -560   -549       C  
ATOM    559  CG  GLN A 167       3.032 -18.645  20.799  1.00 34.15           C  
ANISOU  559  CG  GLN A 167     4520   3831   4623    138   -613   -434       C  
ATOM    560  CD  GLN A 167       1.563 -18.343  21.035  1.00 36.75           C  
ANISOU  560  CD  GLN A 167     4892   4251   4821    126   -807   -306       C  
ATOM    561  NE2 GLN A 167       0.887 -17.861  19.997  1.00 36.87           N  
ANISOU  561  NE2 GLN A 167     4925   4302   4782    100  -1046   -162       N  
ATOM    562  OE1 GLN A 167       1.038 -18.550  22.135  1.00 37.87           O  
ANISOU  562  OE1 GLN A 167     5054   4453   4883    218   -691   -353       O  
ATOM    563  N   HIS A 168       4.993 -16.768  23.313  1.00 25.63           N  
ANISOU  563  N   HIS A 168     3309   2865   3566    189   -239  -1244       N  
ATOM    564  CA  HIS A 168       5.913 -15.650  23.112  1.00 23.66           C  
ANISOU  564  CA  HIS A 168     2813   2879   3299     71   -171  -1284       C  
ATOM    565  C   HIS A 168       6.443 -15.083  24.428  1.00 22.64           C  
ANISOU  565  C   HIS A 168     2573   2911   3117   -115   -275  -1087       C  
ATOM    566  O   HIS A 168       7.284 -14.185  24.421  1.00 21.72           O  
ANISOU  566  O   HIS A 168     2343   2901   3010   -313   -293  -1017       O  
ATOM    567  CB  HIS A 168       5.234 -14.519  22.333  1.00 23.15           C  
ANISOU  567  CB  HIS A 168     2743   2897   3158    156   -237  -1446       C  
ATOM    568  CG  HIS A 168       4.785 -14.907  20.960  1.00 23.06           C  
ANISOU  568  CG  HIS A 168     2799   2877   3088    197   -396  -1624       C  
ATOM    569  CD2 HIS A 168       3.621 -14.679  20.309  1.00 22.80           C  
ANISOU  569  CD2 HIS A 168     2657   2905   3102    131   -439  -1709       C  
ATOM    570  ND1 HIS A 168       5.587 -15.603  20.083  1.00 23.87           N  
ANISOU  570  ND1 HIS A 168     2866   2977   3228    109   -498  -1600       N  
ATOM    571  CE1 HIS A 168       4.934 -15.796  18.951  1.00 23.47           C  
ANISOU  571  CE1 HIS A 168     2808   2924   3185    128   -649  -1697       C  
ATOM    572  NE2 HIS A 168       3.738 -15.245  19.062  1.00 23.57           N  
ANISOU  572  NE2 HIS A 168     2824   2908   3223    111   -671  -1712       N  
ATOM    573  N   MET A 169       5.950 -15.604  25.550  1.00 23.13           N  
ANISOU  573  N   MET A 169     2698   2916   3173    -35   -253   -945       N  
ATOM    574  CA  MET A 169       6.236 -15.019  26.868  1.00 24.06           C  
ANISOU  574  CA  MET A 169     2923   2939   3280     50   -166   -819       C  
ATOM    575  C   MET A 169       7.719 -14.918  27.243  1.00 22.28           C  
ANISOU  575  C   MET A 169     2683   2685   3099    259   -318  -1015       C  
ATOM    576  O   MET A 169       8.120 -13.980  27.938  1.00 21.53           O  
ANISOU  576  O   MET A 169     2675   2598   2907    488   -456  -1141       O  
ATOM    577  CB  MET A 169       5.439 -15.726  27.978  1.00 26.53           C  
ANISOU  577  CB  MET A 169     3312   3238   3528   -344    134   -427       C  
ATOM    578  CG  MET A 169       3.940 -15.429  27.932  1.00 30.06           C  
ANISOU  578  CG  MET A 169     4005   3570   3845   -750    288    -63       C  
ATOM    579  SD  MET A 169       2.938 -16.091  29.282  1.00 33.33           S  
ANISOU  579  SD  MET A 169     4681   3895   4087  -1006    546    268       S  
ATOM    580  CE  MET A 169       3.323 -14.935  30.581  1.00 33.02           C  
ANISOU  580  CE  MET A 169     4735   3755   4057   -915    512    230       C  
ATOM    581  N   THR A 170       8.532 -15.865  26.779  1.00 21.99           N  
ANISOU  581  N   THR A 170     2608   2708   3039    344   -234  -1084       N  
ATOM    582  CA  THR A 170       9.959 -15.859  27.105  1.00 21.46           C  
ANISOU  582  CA  THR A 170     2354   2655   3146    532   -261  -1091       C  
ATOM    583  C   THR A 170      10.742 -14.839  26.287  1.00 21.20           C  
ANISOU  583  C   THR A 170     2221   2894   2939    397   -156   -962       C  
ATOM    584  O   THR A 170      11.886 -14.529  26.604  1.00 22.27           O  
ANISOU  584  O   THR A 170     2342   3131   2989    301   -118   -896       O  
ATOM    585  CB  THR A 170      10.606 -17.243  26.913  1.00 21.89           C  
ANISOU  585  CB  THR A 170     2567   2439   3310    734   -334  -1249       C  
ATOM    586  CG2 THR A 170       9.879 -18.296  27.735  1.00 20.56           C  
ANISOU  586  CG2 THR A 170     2429   2131   3251    813   -295  -1168       C  
ATOM    587  OG1 THR A 170      10.577 -17.591  25.524  1.00 22.83           O  
ANISOU  587  OG1 THR A 170     2776   2444   3455   1151   -320  -1207       O  
ATOM    588  N   GLU A 171      10.133 -14.323  25.229  1.00 20.22           N  
ANISOU  588  N   GLU A 171     2041   2871   2771    370    -25   -893       N  
ATOM    589  CA  GLU A 171      10.796 -13.305  24.422  1.00 21.17           C  
ANISOU  589  CA  GLU A 171     2255   3003   2787    293     43   -823       C  
ATOM    590  C   GLU A 171      10.726 -11.943  25.110  1.00 19.83           C  
ANISOU  590  C   GLU A 171     1862   2907   2766     76    119   -694       C  
ATOM    591  O   GLU A 171       9.668 -11.521  25.584  1.00 17.92           O  
ANISOU  591  O   GLU A 171     1271   2697   2843    -33    146   -680       O  
ATOM    592  CB  GLU A 171      10.192 -13.226  23.016  1.00 23.83           C  
ANISOU  592  CB  GLU A 171     2836   3361   2857    331    183   -538       C  
ATOM    593  CG  GLU A 171      10.857 -12.194  22.113  1.00 25.24           C  
ANISOU  593  CG  GLU A 171     3235   3490   2864    196    361   -371       C  
ATOM    594  CD  GLU A 171      10.348 -12.236  20.680  1.00 27.52           C  
ANISOU  594  CD  GLU A 171     3730   3723   3004     68    589   -255       C  
ATOM    595  OE1 GLU A 171       9.910 -13.316  20.223  1.00 28.42           O  
ANISOU  595  OE1 GLU A 171     3974   3864   2961     81    681   -491       O  
ATOM    596  OE2 GLU A 171      10.383 -11.181  20.012  1.00 28.26           O1-
ANISOU  596  OE2 GLU A 171     3846   3855   3038    -49    576     40       O1-
ATOM    597  N   VAL A 172      11.861 -11.261  25.176  1.00 18.88           N  
ANISOU  597  N   VAL A 172     1723   2943   2506     88    184   -669       N  
ATOM    598  CA  VAL A 172      11.909  -9.945  25.798  1.00 17.79           C  
ANISOU  598  CA  VAL A 172     1812   2851   2094    139    -14   -371       C  
ATOM    599  C   VAL A 172      11.234  -8.916  24.902  1.00 16.75           C  
ANISOU  599  C   VAL A 172     1690   2866   1807    233     59   -110       C  
ATOM    600  O   VAL A 172      11.545  -8.827  23.718  1.00 16.39           O  
ANISOU  600  O   VAL A 172     1668   2936   1623    420    300   -106       O  
ATOM    601  CB  VAL A 172      13.346  -9.503  26.079  1.00 17.67           C  
ANISOU  601  CB  VAL A 172     1845   2854   2015    -14   -191   -411       C  
ATOM    602  CG1 VAL A 172      13.370  -8.030  26.456  1.00 16.62           C  
ANISOU  602  CG1 VAL A 172     1683   2669   1962    -43   -188   -594       C  
ATOM    603  CG2 VAL A 172      13.974 -10.369  27.176  1.00 17.56           C  
ANISOU  603  CG2 VAL A 172     1886   2770   2015    -39   -102   -294       C  
ATOM    604  N   VAL A 173      10.309  -8.149  25.471  1.00 15.30           N  
ANISOU  604  N   VAL A 173     1445   2727   1641    382   -103   -203       N  
ATOM    605  CA  VAL A 173       9.633  -7.086  24.740  1.00 15.07           C  
ANISOU  605  CA  VAL A 173     1443   2624   1660    344    -28     -8       C  
ATOM    606  C   VAL A 173      10.568  -5.895  24.634  1.00 15.73           C  
ANISOU  606  C   VAL A 173     1391   2892   1692    223     21     44       C  
ATOM    607  O   VAL A 173      10.981  -5.330  25.649  1.00 15.93           O  
ANISOU  607  O   VAL A 173     1640   2992   1419    -70    110    312       O  
ATOM    608  CB  VAL A 173       8.343  -6.636  25.447  1.00 14.61           C  
ANISOU  608  CB  VAL A 173     1461   2405   1685    521   -190   -202       C  
ATOM    609  CG1 VAL A 173       7.665  -5.521  24.664  1.00 13.90           C  
ANISOU  609  CG1 VAL A 173     1472   2302   1508    621   -439   -159       C  
ATOM    610  CG2 VAL A 173       7.401  -7.811  25.634  1.00 14.50           C  
ANISOU  610  CG2 VAL A 173     1273   2446   1792    429   -122   -220       C  
ATOM    611  N   ARG A 174      10.894  -5.526  23.398  1.00 17.03           N  
ANISOU  611  N   ARG A 174     1435   3168   1869    458   -157    105       N  
ATOM    612  CA  ARG A 174      11.790  -4.411  23.113  1.00 19.48           C  
ANISOU  612  CA  ARG A 174     1630   3637   2135    395     -9     31       C  
ATOM    613  C   ARG A 174      11.311  -3.659  21.880  1.00 18.24           C  
ANISOU  613  C   ARG A 174     1522   3787   1619    139      6    -51       C  
ATOM    614  O   ARG A 174      10.472  -4.159  21.133  1.00 17.85           O  
ANISOU  614  O   ARG A 174     1422   3932   1428   -115   -116    -99       O  
ATOM    615  CB  ARG A 174      13.223  -4.914  22.893  1.00 23.17           C  
ANISOU  615  CB  ARG A 174     1993   4054   2759    624    242   -168       C  
ATOM    616  CG  ARG A 174      13.308  -6.259  22.178  1.00 27.16           C  
ANISOU  616  CG  ARG A 174     2419   4575   3325    746    236   -316       C  
ATOM    617  CD  ARG A 174      14.755  -6.646  21.888  1.00 31.30           C  
ANISOU  617  CD  ARG A 174     3046   5052   3796    892    138   -414       C  
ATOM    618  NE  ARG A 174      15.623  -6.384  23.037  1.00 36.25           N  
ANISOU  618  NE  ARG A 174     3753   5634   4389   1002    244   -521       N  
ATOM    619  CZ  ARG A 174      16.262  -7.320  23.740  1.00 39.38           C  
ANISOU  619  CZ  ARG A 174     4151   6121   4692    868    297   -739       C  
ATOM    620  NH1 ARG A 174      16.156  -8.606  23.412  1.00 40.40           N1+
ANISOU  620  NH1 ARG A 174     4303   6200   4845    825    450   -795       N1+
ATOM    621  NH2 ARG A 174      17.023  -6.969  24.771  1.00 39.79           N  
ANISOU  621  NH2 ARG A 174     4134   6302   4682    792    245   -906       N  
ATOM    622  N   ARG A 175      11.844  -2.460  21.670  1.00 18.08           N  
ANISOU  622  N   ARG A 175     1648   3803   1420    236      5      5       N  
ATOM    623  CA  ARG A 175      11.494  -1.683  20.489  1.00 18.81           C  
ANISOU  623  CA  ARG A 175     1907   3773   1468     36     57    -31       C  
ATOM    624  C   ARG A 175      12.047  -2.337  19.228  1.00 19.78           C  
ANISOU  624  C   ARG A 175     2008   3915   1592    107    118    110       C  
ATOM    625  O   ARG A 175      13.054  -3.046  19.277  1.00 19.87           O  
ANISOU  625  O   ARG A 175     1999   3907   1642    -28     25     74       O  
ATOM    626  CB  ARG A 175      12.011  -0.247  20.603  1.00 18.33           C  
ANISOU  626  CB  ARG A 175     1812   3699   1454   -492     52    -86       C  
ATOM    627  CG  ARG A 175      11.356   0.578  21.698  1.00 18.56           C  
ANISOU  627  CG  ARG A 175     1864   3717   1471   -637    -39   -187       C  
ATOM    628  CD  ARG A 175      12.037   1.922  21.820  1.00 21.23           C  
ANISOU  628  CD  ARG A 175     2484   3929   1654   -332     -6   -306       C  
ATOM    629  NE  ARG A 175      11.381   2.930  21.005  1.00 24.18           N  
ANISOU  629  NE  ARG A 175     3058   4276   1853   -495    199   -518       N  
ATOM    630  CZ  ARG A 175      11.884   4.128  20.744  1.00 24.84           C  
ANISOU  630  CZ  ARG A 175     3070   4516   1852   -447    401   -460       C  
ATOM    631  NH1 ARG A 175      13.065   4.472  21.229  1.00 24.71           N1+
ANISOU  631  NH1 ARG A 175     2803   4620   1966    -98    291   -383       N1+
ATOM    632  NH2 ARG A 175      11.199   4.979  19.999  1.00 25.57           N  
ANISOU  632  NH2 ARG A 175     3225   4669   1823   -531    554   -485       N  
ATOM    633  N   CYS A 176      11.369  -2.118  18.105  1.00 19.96           N  
ANISOU  633  N   CYS A 176     2060   4046   1477    245     91     57       N  
ATOM    634  CA  CYS A 176      11.866  -2.566  16.808  1.00 20.36           C  
ANISOU  634  CA  CYS A 176     2019   4309   1410    628    178    172       C  
ATOM    635  C   CYS A 176      13.130  -1.777  16.457  1.00 20.81           C  
ANISOU  635  C   CYS A 176     2092   4456   1360    946    313    304       C  
ATOM    636  O   CYS A 176      13.338  -0.679  16.977  1.00 20.02           O  
ANISOU  636  O   CYS A 176     2052   4274   1281   1012    278    438       O  
ATOM    637  CB  CYS A 176      10.794  -2.366  15.737  1.00 20.41           C  
ANISOU  637  CB  CYS A 176     1804   4393   1559    717     17     48       C  
ATOM    638  SG  CYS A 176      10.441  -0.634  15.370  1.00 21.83           S  
ANISOU  638  SG  CYS A 176     2013   4708   1574    758   -170   -133       S  
ATOM    639  N   PRO A 177      13.982  -2.338  15.582  1.00 22.66           N  
ANISOU  639  N   PRO A 177     2144   4706   1761    900    319    346       N  
ATOM    640  CA  PRO A 177      15.235  -1.668  15.216  1.00 22.48           C  
ANISOU  640  CA  PRO A 177     2005   4790   1745    777    354    377       C  
ATOM    641  C   PRO A 177      15.007  -0.243  14.721  1.00 21.87           C  
ANISOU  641  C   PRO A 177     1839   4842   1630    488     93    203       C  
ATOM    642  O   PRO A 177      15.790   0.636  15.064  1.00 21.53           O  
ANISOU  642  O   PRO A 177     1727   4930   1525    327   -298     50       O  
ATOM    643  CB  PRO A 177      15.784  -2.549  14.094  1.00 23.76           C  
ANISOU  643  CB  PRO A 177     2106   4841   2081    867    259    420       C  
ATOM    644  CG  PRO A 177      15.259  -3.911  14.416  1.00 23.37           C  
ANISOU  644  CG  PRO A 177     2103   4739   2037    951    321    358       C  
ATOM    645  CD  PRO A 177      13.875  -3.675  14.969  1.00 22.85           C  
ANISOU  645  CD  PRO A 177     2148   4720   1815   1046    434    223       C  
ATOM    646  N   HIS A 178      13.944  -0.025  13.947  1.00 20.55           N  
ANISOU  646  N   HIS A 178     1561   4718   1529    507     95     38       N  
ATOM    647  CA  HIS A 178      13.605   1.307  13.444  1.00 18.98           C  
ANISOU  647  CA  HIS A 178     1423   4425   1363    477    -41   -103       C  
ATOM    648  C   HIS A 178      13.428   2.334  14.557  1.00 18.97           C  
ANISOU  648  C   HIS A 178     1318   4482   1409    195     20     -8       C  
ATOM    649  O   HIS A 178      13.982   3.430  14.507  1.00 19.86           O  
ANISOU  649  O   HIS A 178     1337   4665   1542    129     58     28       O  
ATOM    650  CB  HIS A 178      12.321   1.256  12.619  1.00 18.28           C  
ANISOU  650  CB  HIS A 178     1459   4194   1294    389   -130   -306       C  
ATOM    651  CG  HIS A 178      11.695   2.598  12.400  1.00 18.71           C  
ANISOU  651  CG  HIS A 178     1806   4083   1219    392   -326   -420       C  
ATOM    652  CD2 HIS A 178      10.484   3.088  12.757  1.00 19.38           C  
ANISOU  652  CD2 HIS A 178     2109   4015   1238    464   -311   -453       C  
ATOM    653  ND1 HIS A 178      12.335   3.614  11.724  1.00 19.11           N  
ANISOU  653  ND1 HIS A 178     1914   4106   1243    512   -290   -566       N  
ATOM    654  CE1 HIS A 178      11.546   4.674  11.676  1.00 19.65           C  
ANISOU  654  CE1 HIS A 178     2151   4025   1288    559   -331   -556       C  
ATOM    655  NE2 HIS A 178      10.416   4.380  12.295  1.00 19.11           N  
ANISOU  655  NE2 HIS A 178     2060   3986   1216    509   -277   -495       N  
ATOM    656  N   HIS A 179      12.623   1.989  15.551  1.00 19.05           N  
ANISOU  656  N   HIS A 179     1425   4467   1346    160   -131      9       N  
ATOM    657  CA  HIS A 179      12.346   2.915  16.640  1.00 18.99           C  
ANISOU  657  CA  HIS A 179     1467   4559   1189     32    -38    148       C  
ATOM    658  C   HIS A 179      13.523   3.007  17.596  1.00 20.78           C  
ANISOU  658  C   HIS A 179     1700   4934   1263    119    -35    182       C  
ATOM    659  O   HIS A 179      13.754   4.046  18.204  1.00 21.78           O  
ANISOU  659  O   HIS A 179     1903   4980   1391    222   -243    320       O  
ATOM    660  CB  HIS A 179      11.055   2.537  17.363  1.00 17.65           C  
ANISOU  660  CB  HIS A 179     1386   4250   1068    -12      5    118       C  
ATOM    661  CG  HIS A 179       9.828   3.073  16.702  1.00 16.54           C  
ANISOU  661  CG  HIS A 179     1158   4020   1105     70     83    227       C  
ATOM    662  CD2 HIS A 179       9.527   4.320  16.265  1.00 17.66           C  
ANISOU  662  CD2 HIS A 179     1347   3976   1388    -22    311    368       C  
ATOM    663  ND1 HIS A 179       8.737   2.288  16.404  1.00 14.84           N  
ANISOU  663  ND1 HIS A 179      922   3675   1042    -45     13     99       N  
ATOM    664  CE1 HIS A 179       7.815   3.026  15.814  1.00 17.72           C  
ANISOU  664  CE1 HIS A 179     1536   3762   1436   -133    182    204       C  
ATOM    665  NE2 HIS A 179       8.270   4.264  15.713  1.00 18.77           N  
ANISOU  665  NE2 HIS A 179     1628   3955   1548    -69    267    529       N  
ATOM    666  N   GLU A 180      14.279   1.926  17.718  1.00 22.21           N  
ANISOU  666  N   GLU A 180     1771   5176   1492    -24    302    125       N  
ATOM    667  CA  GLU A 180      15.459   1.938  18.575  1.00 25.11           C  
ANISOU  667  CA  GLU A 180     1779   5828   1933   -178    271     59       C  
ATOM    668  C   GLU A 180      16.483   2.935  18.025  1.00 28.65           C  
ANISOU  668  C   GLU A 180     2232   6262   2391   -334     51     -5       C  
ATOM    669  O   GLU A 180      17.230   3.567  18.778  1.00 29.30           O  
ANISOU  669  O   GLU A 180     2388   6370   2374   -408    197    -67       O  
ATOM    670  CB  GLU A 180      16.051   0.532  18.652  1.00 25.93           C  
ANISOU  670  CB  GLU A 180     1757   5966   2127   -156     40     -5       C  
ATOM    671  CG  GLU A 180      17.327   0.424  19.463  1.00 28.28           C  
ANISOU  671  CG  GLU A 180     2079   6209   2459    -92      5   -244       C  
ATOM    672  CD  GLU A 180      18.007  -0.921  19.295  1.00 30.56           C  
ANISOU  672  CD  GLU A 180     2319   6501   2792     -2    -47   -510       C  
ATOM    673  OE1 GLU A 180      17.310  -1.918  19.015  1.00 30.25           O  
ANISOU  673  OE1 GLU A 180     2421   6425   2647     82   -149   -799       O  
ATOM    674  OE2 GLU A 180      19.244  -0.982  19.445  1.00 33.48           O1-
ANISOU  674  OE2 GLU A 180     2759   6790   3173    -12    177   -571       O1-
ATOM    675  N   ARG A 181      16.487   3.081  16.702  1.00 31.60           N  
ANISOU  675  N   ARG A 181     2686   6543   2776   -565     57     78       N  
ATOM    676  CA  ARG A 181      17.402   3.983  16.013  1.00 34.91           C  
ANISOU  676  CA  ARG A 181     3304   6767   3194   -834   -151     58       C  
ATOM    677  C   ARG A 181      16.786   5.349  15.734  1.00 33.79           C  
ANISOU  677  C   ARG A 181     3242   6534   3062  -1175   -534    303       C  
ATOM    678  O   ARG A 181      17.461   6.242  15.233  1.00 33.02           O  
ANISOU  678  O   ARG A 181     2984   6583   2978  -1328   -704    451       O  
ATOM    679  CB  ARG A 181      17.873   3.356  14.699  1.00 39.12           C  
ANISOU  679  CB  ARG A 181     3918   7246   3699   -701     39   -151       C  
ATOM    680  CG  ARG A 181      18.673   2.076  14.879  1.00 43.78           C  
ANISOU  680  CG  ARG A 181     4682   7787   4164   -580    -48   -339       C  
ATOM    681  CD  ARG A 181      19.496   1.773  13.634  1.00 47.79           C  
ANISOU  681  CD  ARG A 181     5312   8206   4641   -480   -402   -429       C  
ATOM    682  NE  ARG A 181      18.946   0.689  12.820  1.00 50.67           N  
ANISOU  682  NE  ARG A 181     5707   8556   4989   -474   -896   -404       N  
ATOM    683  CZ  ARG A 181      19.433  -0.550  12.809  1.00 53.09           C  
ANISOU  683  CZ  ARG A 181     5965   8888   5318   -496  -1299   -407       C  
ATOM    684  NH1 ARG A 181      20.472  -0.863  13.578  1.00 53.96           N1+
ANISOU  684  NH1 ARG A 181     6022   8984   5495   -448  -1533   -405       N1+
ATOM    685  NH2 ARG A 181      18.886  -1.480  12.036  1.00 53.61           N  
ANISOU  685  NH2 ARG A 181     6008   9043   5318   -487  -1436   -390       N  
ATOM    686  N   CYS A 182      15.504   5.507  16.045  1.00 34.26           N  
ANISOU  686  N   CYS A 182     3524   6350   3143  -1289   -704    354       N  
ATOM    687  CA  CYS A 182      14.841   6.800  15.892  1.00 35.22           C  
ANISOU  687  CA  CYS A 182     3838   6313   3232  -1242   -893    599       C  
ATOM    688  C   CYS A 182      15.470   7.851  16.801  1.00 35.97           C  
ANISOU  688  C   CYS A 182     3915   6212   3541  -1348   -623    787       C  
ATOM    689  O   CYS A 182      15.987   7.527  17.875  1.00 36.12           O  
ANISOU  689  O   CYS A 182     3877   6379   3468  -1433   -875    836       O  
ATOM    690  CB  CYS A 182      13.349   6.687  16.203  1.00 35.73           C  
ANISOU  690  CB  CYS A 182     4072   6386   3117  -1057  -1201    642       C  
ATOM    691  SG  CYS A 182      12.322   6.520  14.739  1.00 37.31           S  
ANISOU  691  SG  CYS A 182     4548   6575   3053   -911  -1187    712       S  
ATOM    692  N   SER A 183      15.421   9.110  16.373  1.00 35.76           N  
ANISOU  692  N   SER A 183     3976   5899   3714  -1386   -151    889       N  
ATOM    693  CA  SER A 183      15.964  10.206  17.168  1.00 36.41           C  
ANISOU  693  CA  SER A 183     4266   5698   3870  -1348    265    854       C  
ATOM    694  C   SER A 183      14.899  10.780  18.097  1.00 35.21           C  
ANISOU  694  C   SER A 183     4314   5354   3709  -1533    258    886       C  
ATOM    695  O   SER A 183      14.651  11.989  18.101  1.00 36.53           O  
ANISOU  695  O   SER A 183     4562   5429   3889  -1609    268    917       O  
ATOM    696  CB  SER A 183      16.525  11.302  16.260  1.00 38.22           C  
ANISOU  696  CB  SER A 183     4570   5883   4068  -1163    534    785       C  
ATOM    697  OG  SER A 183      17.572  10.805  15.445  1.00 39.49           O  
ANISOU  697  OG  SER A 183     4772   6015   4217  -1022    696    696       O  
ATOM    698  N   ASP A 184      14.273   9.907  18.882  1.00 31.36           N  
ANISOU  698  N   ASP A 184     3892   4800   3224  -1682    221   1066       N  
ATOM    699  CA  ASP A 184      13.174  10.314  19.754  1.00 29.49           C  
ANISOU  699  CA  ASP A 184     3518   4554   3132  -1321    184   1082       C  
ATOM    700  C   ASP A 184      13.543  10.267  21.233  1.00 28.34           C  
ANISOU  700  C   ASP A 184     3413   4363   2992  -1175    354   1171       C  
ATOM    701  O   ASP A 184      12.672  10.204  22.096  1.00 27.00           O  
ANISOU  701  O   ASP A 184     3286   4311   2663  -1259    553   1113       O  
ATOM    702  CB  ASP A 184      11.942   9.446  19.501  1.00 28.64           C  
ANISOU  702  CB  ASP A 184     3187   4561   3134  -1170    231   1131       C  
ATOM    703  CG  ASP A 184      12.218   7.961  19.680  1.00 28.89           C  
ANISOU  703  CG  ASP A 184     3062   4721   3194   -983    226   1096       C  
ATOM    704  OD1 ASP A 184      13.213   7.596  20.340  1.00 28.34           O  
ANISOU  704  OD1 ASP A 184     2735   4836   3197  -1051    257   1078       O  
ATOM    705  OD2 ASP A 184      11.423   7.148  19.165  1.00 29.44           O1-
ANISOU  705  OD2 ASP A 184     3238   4697   3252   -865    175   1180       O1-
ATOM    706  N   SER A 185      14.841  10.291  21.514  1.00 29.09           N  
ANISOU  706  N   SER A 185     3586   4287   3180   -872    237   1169       N  
ATOM    707  CA  SER A 185      15.337  10.161  22.877  1.00 28.63           C  
ANISOU  707  CA  SER A 185     3412   4159   3308   -649    128   1103       C  
ATOM    708  C   SER A 185      14.877  11.320  23.757  1.00 28.36           C  
ANISOU  708  C   SER A 185     3428   3919   3429   -647     82   1062       C  
ATOM    709  O   SER A 185      14.699  12.443  23.280  1.00 28.54           O  
ANISOU  709  O   SER A 185     3442   3832   3571   -558    242   1118       O  
ATOM    710  CB  SER A 185      16.863  10.068  22.873  1.00 28.81           C  
ANISOU  710  CB  SER A 185     3184   4319   3442   -429    147   1032       C  
ATOM    711  OG  SER A 185      17.362   9.881  24.181  1.00 29.37           O  
ANISOU  711  OG  SER A 185     3032   4483   3645   -267     45    744       O  
ATOM    712  N   ASP A 186      14.663  11.034  25.039  1.00 27.16           N  
ANISOU  712  N   ASP A 186     3271   3787   3262   -701    -51    863       N  
ATOM    713  CA  ASP A 186      14.324  12.070  26.003  1.00 25.25           C  
ANISOU  713  CA  ASP A 186     3076   3395   3124   -697   -163    669       C  
ATOM    714  C   ASP A 186      15.525  12.316  26.910  1.00 24.80           C  
ANISOU  714  C   ASP A 186     3230   3033   3159   -786    -91    543       C  
ATOM    715  O   ASP A 186      15.451  13.073  27.881  1.00 24.79           O  
ANISOU  715  O   ASP A 186     3639   2699   3080   -760   -160    399       O  
ATOM    716  CB  ASP A 186      13.083  11.677  26.814  1.00 25.00           C  
ANISOU  716  CB  ASP A 186     3023   3360   3115   -615   -324    623       C  
ATOM    717  CG  ASP A 186      13.266  10.385  27.596  1.00 24.32           C  
ANISOU  717  CG  ASP A 186     2956   3218   3066   -739   -122    510       C  
ATOM    718  OD1 ASP A 186      14.282   9.686  27.410  1.00 24.53           O  
ANISOU  718  OD1 ASP A 186     2991   3262   3069   -633   -117    473       O  
ATOM    719  OD2 ASP A 186      12.372  10.068  28.403  1.00 24.20           O1-
ANISOU  719  OD2 ASP A 186     2895   3209   3091   -813    -94    461       O1-
ATOM    720  N   GLY A 187      16.630  11.654  26.580  1.00 23.87           N  
ANISOU  720  N   GLY A 187     2863   3045   3161   -705   -146    441       N  
ATOM    721  CA  GLY A 187      17.878  11.819  27.303  1.00 22.65           C  
ANISOU  721  CA  GLY A 187     2554   3125   2926   -572   -322    394       C  
ATOM    722  C   GLY A 187      17.984  10.920  28.518  1.00 21.51           C  
ANISOU  722  C   GLY A 187     2243   3114   2816   -611   -494    415       C  
ATOM    723  O   GLY A 187      19.047  10.824  29.128  1.00 21.41           O  
ANISOU  723  O   GLY A 187     2059   3214   2863   -752   -503    291       O  
ATOM    724  N   LEU A 188      16.880  10.269  28.877  1.00 20.07           N  
ANISOU  724  N   LEU A 188     2046   2937   2642   -845   -637    424       N  
ATOM    725  CA  LEU A 188      16.845   9.423  30.069  1.00 19.54           C  
ANISOU  725  CA  LEU A 188     2002   2919   2502   -603   -568    169       C  
ATOM    726  C   LEU A 188      16.652   7.953  29.708  1.00 18.65           C  
ANISOU  726  C   LEU A 188     1909   2866   2312   -476   -673    265       C  
ATOM    727  O   LEU A 188      17.422   7.090  30.127  1.00 19.44           O  
ANISOU  727  O   LEU A 188     2088   2933   2365   -744   -892    342       O  
ATOM    728  CB  LEU A 188      15.739   9.886  31.028  1.00 19.01           C  
ANISOU  728  CB  LEU A 188     2043   2751   2431   -411   -470    -27       C  
ATOM    729  CG  LEU A 188      15.816  11.341  31.503  1.00 19.26           C  
ANISOU  729  CG  LEU A 188     2285   2632   2402   -249   -479   -189       C  
ATOM    730  CD1 LEU A 188      14.690  11.672  32.465  1.00 19.00           C  
ANISOU  730  CD1 LEU A 188     2312   2480   2428    100   -287   -474       C  
ATOM    731  CD2 LEU A 188      17.158  11.613  32.144  1.00 19.36           C  
ANISOU  731  CD2 LEU A 188     2516   2536   2305   -292   -886   -190       C  
ATOM    732  N   ALA A 189      15.621   7.677  28.917  1.00 16.91           N  
ANISOU  732  N   ALA A 189     1630   2848   1947   -270   -678     92       N  
ATOM    733  CA  ALA A 189      15.290   6.307  28.539  1.00 16.66           C  
ANISOU  733  CA  ALA A 189     1544   3042   1744    -14   -366    231       C  
ATOM    734  C   ALA A 189      16.301   5.700  27.563  1.00 16.32           C  
ANISOU  734  C   ALA A 189     1433   3167   1602   -222   -241    247       C  
ATOM    735  O   ALA A 189      16.755   6.371  26.626  1.00 15.91           O  
ANISOU  735  O   ALA A 189     1577   3156   1312   -532   -441    262       O  
ATOM    736  CB  ALA A 189      13.902   6.243  27.955  1.00 14.94           C  
ANISOU  736  CB  ALA A 189     1244   2908   1524    399   -240    468       C  
ATOM    737  N   PRO A 190      16.660   4.425  27.789  1.00 15.12           N  
ANISOU  737  N   PRO A 190     1128   3014   1601   -224   -117    267       N  
ATOM    738  CA  PRO A 190      17.491   3.666  26.850  1.00 16.37           C  
ANISOU  738  CA  PRO A 190     1430   3218   1570   -304   -256    272       C  
ATOM    739  C   PRO A 190      16.731   3.476  25.550  1.00 17.88           C  
ANISOU  739  C   PRO A 190     1628   3648   1516   -411   -149    203       C  
ATOM    740  O   PRO A 190      15.506   3.321  25.592  1.00 18.57           O  
ANISOU  740  O   PRO A 190     1757   3822   1476   -609   -159    336       O  
ATOM    741  CB  PRO A 190      17.679   2.317  27.557  1.00 17.01           C  
ANISOU  741  CB  PRO A 190     1613   3222   1629   -507    -40    188       C  
ATOM    742  CG  PRO A 190      17.459   2.611  29.008  1.00 16.20           C  
ANISOU  742  CG  PRO A 190     1378   3168   1610   -373   -109    149       C  
ATOM    743  CD  PRO A 190      16.397   3.671  29.025  1.00 14.91           C  
ANISOU  743  CD  PRO A 190     1066   3016   1584   -243    -54    126       C  
ATOM    744  N   PRO A 191      17.436   3.496  24.408  1.00 17.79           N  
ANISOU  744  N   PRO A 191     1395   3938   1425   -548     54    270       N  
ATOM    745  CA  PRO A 191      16.739   3.430  23.116  1.00 18.36           C  
ANISOU  745  CA  PRO A 191     1629   3985   1361   -390    245    139       C  
ATOM    746  C   PRO A 191      15.975   2.125  22.863  1.00 16.71           C  
ANISOU  746  C   PRO A 191     1493   3657   1199   -296    280    103       C  
ATOM    747  O   PRO A 191      15.052   2.142  22.061  1.00 15.77           O  
ANISOU  747  O   PRO A 191     1313   3569   1108   -400    -47     85       O  
ATOM    748  CB  PRO A 191      17.868   3.608  22.085  1.00 18.00           C  
ANISOU  748  CB  PRO A 191     1532   4048   1259   -562    258    140       C  
ATOM    749  CG  PRO A 191      19.119   3.242  22.803  1.00 18.28           C  
ANISOU  749  CG  PRO A 191     1458   4108   1380   -584    163     65       C  
ATOM    750  CD  PRO A 191      18.893   3.638  24.244  1.00 18.13           C  
ANISOU  750  CD  PRO A 191     1444   4071   1372   -520    154    127       C  
ATOM    751  N   GLN A 192      16.351   1.033  23.522  1.00 17.59           N  
ANISOU  751  N   GLN A 192     1824   3593   1265     23    435    250       N  
ATOM    752  CA  GLN A 192      15.678  -0.253  23.335  1.00 17.30           C  
ANISOU  752  CA  GLN A 192     1722   3390   1461    259    353    296       C  
ATOM    753  C   GLN A 192      14.354  -0.365  24.085  1.00 15.07           C  
ANISOU  753  C   GLN A 192     1291   3079   1356    394     77    219       C  
ATOM    754  O   GLN A 192      13.523  -1.215  23.758  1.00 14.16           O  
ANISOU  754  O   GLN A 192     1041   3045   1295    335    344     82       O  
ATOM    755  CB  GLN A 192      16.579  -1.409  23.783  1.00 20.69           C  
ANISOU  755  CB  GLN A 192     2045   3737   2081    658    689    105       C  
ATOM    756  CG  GLN A 192      17.683  -1.795  22.817  1.00 24.43           C  
ANISOU  756  CG  GLN A 192     2552   4171   2560    836    896    223       C  
ATOM    757  CD  GLN A 192      18.390  -3.075  23.242  1.00 27.90           C  
ANISOU  757  CD  GLN A 192     3064   4653   2884   1089   1051    267       C  
ATOM    758  NE2 GLN A 192      19.005  -3.754  22.281  1.00 29.14           N  
ANISOU  758  NE2 GLN A 192     3310   4777   2985   1063   1208    468       N  
ATOM    759  OE1 GLN A 192      18.369  -3.456  24.417  1.00 29.46           O  
ANISOU  759  OE1 GLN A 192     3186   4913   3094   1227    949    153       O  
ATOM    760  N   HIS A 193      14.170   0.482  25.095  1.00 13.09           N  
ANISOU  760  N   HIS A 193     1135   2682   1157    407   -134    207       N  
ATOM    761  CA  HIS A 193      13.032   0.362  26.008  1.00 11.51           C  
ANISOU  761  CA  HIS A 193     1018   2382    975    133   -257    100       C  
ATOM    762  C   HIS A 193      11.691   0.781  25.412  1.00 11.90           C  
ANISOU  762  C   HIS A 193     1032   2423   1068     84    -75    225       C  
ATOM    763  O   HIS A 193      11.540   1.899  24.918  1.00 14.20           O  
ANISOU  763  O   HIS A 193     1173   3037   1186   -177   -196    393       O  
ATOM    764  CB  HIS A 193      13.283   1.145  27.301  1.00 11.18           C  
ANISOU  764  CB  HIS A 193      970   2147   1129    -77   -501    -33       C  
ATOM    765  CG  HIS A 193      14.149   0.424  28.277  1.00 11.38           C  
ANISOU  765  CG  HIS A 193     1216   1934   1173   -145   -506   -171       C  
ATOM    766  CD2 HIS A 193      15.280  -0.300  28.102  1.00 11.85           C  
ANISOU  766  CD2 HIS A 193     1415   1835   1254     51   -607    -76       C  
ATOM    767  ND1 HIS A 193      13.884   0.401  29.629  1.00 12.62           N  
ANISOU  767  ND1 HIS A 193     1393   1963   1441   -175   -393   -468       N  
ATOM    768  CE1 HIS A 193      14.817  -0.303  30.246  1.00 12.06           C  
ANISOU  768  CE1 HIS A 193     1377   1840   1366     55   -487   -419       C  
ATOM    769  NE2 HIS A 193      15.675  -0.740  29.341  1.00 11.93           N  
ANISOU  769  NE2 HIS A 193     1392   1856   1286    136   -639   -232       N  
ATOM    770  N   LEU A 194      10.710  -0.113  25.490  1.00 12.59           N  
ANISOU  770  N   LEU A 194     1339   2258   1188    194     61    162       N  
ATOM    771  CA  LEU A 194       9.360   0.188  25.021  1.00 12.11           C  
ANISOU  771  CA  LEU A 194     1225   2023   1353    166   -237    119       C  
ATOM    772  C   LEU A 194       8.643   1.219  25.897  1.00 12.48           C  
ANISOU  772  C   LEU A 194     1173   1943   1627    303   -393    285       C  
ATOM    773  O   LEU A 194       8.033   2.167  25.388  1.00 13.09           O  
ANISOU  773  O   LEU A 194     1213   2062   1698    150   -690    462       O  
ATOM    774  CB  LEU A 194       8.528  -1.094  24.956  1.00 11.51           C  
ANISOU  774  CB  LEU A 194     1176   1869   1328     -8   -284    229       C  
ATOM    775  CG  LEU A 194       7.046  -0.890  24.660  1.00 11.91           C  
ANISOU  775  CG  LEU A 194     1347   1729   1448   -272   -475     44       C  
ATOM    776  CD1 LEU A 194       6.872  -0.432  23.219  1.00 12.43           C  
ANISOU  776  CD1 LEU A 194     1415   1773   1535      3   -457     75       C  
ATOM    777  CD2 LEU A 194       6.259  -2.159  24.950  1.00 12.59           C  
ANISOU  777  CD2 LEU A 194     1266   1909   1607   -483   -447    -91       C  
ATOM    778  N   ILE A 195       8.703   1.021  27.210  1.00 12.71           N  
ANISOU  778  N   ILE A 195     1187   1889   1753    462   -243    111       N  
ATOM    779  CA  ILE A 195       7.968   1.873  28.144  1.00 12.96           C  
ANISOU  779  CA  ILE A 195     1334   1840   1749    168    -47    142       C  
ATOM    780  C   ILE A 195       8.841   2.985  28.743  1.00 13.99           C  
ANISOU  780  C   ILE A 195     1337   1994   1985    -38      2     58       C  
ATOM    781  O   ILE A 195       9.886   2.713  29.338  1.00 14.21           O  
ANISOU  781  O   ILE A 195     1231   2250   1917   -238   -146   -270       O  
ATOM    782  CB  ILE A 195       7.339   1.046  29.296  1.00 12.43           C  
ANISOU  782  CB  ILE A 195     1275   1661   1786     29    102    110       C  
ATOM    783  CG1 ILE A 195       6.497  -0.109  28.747  1.00 12.43           C  
ANISOU  783  CG1 ILE A 195     1285   1740   1698    296    119    -39       C  
ATOM    784  CG2 ILE A 195       6.497   1.940  30.209  1.00 11.57           C  
ANISOU  784  CG2 ILE A 195     1256   1414   1727    206     80     39       C  
ATOM    785  CD1 ILE A 195       5.837  -0.959  29.836  1.00 11.96           C  
ANISOU  785  CD1 ILE A 195     1075   1772   1699    567    163     79       C  
ATOM    786  N   ARG A 196       8.402   4.235  28.582  1.00 13.23           N  
ANISOU  786  N   ARG A 196     1289   1629   2107   -281    -94    224       N  
ATOM    787  CA  ARG A 196       9.038   5.378  29.238  1.00 13.09           C  
ANISOU  787  CA  ARG A 196     1265   1705   2004   -270   -138    309       C  
ATOM    788  C   ARG A 196       8.100   6.028  30.245  1.00 12.41           C  
ANISOU  788  C   ARG A 196     1411   1435   1867    -79   -381    276       C  
ATOM    789  O   ARG A 196       6.885   5.854  30.190  1.00 11.48           O  
ANISOU  789  O   ARG A 196     1256   1200   1905    459   -401    270       O  
ATOM    790  CB  ARG A 196       9.440   6.443  28.216  1.00 14.31           C  
ANISOU  790  CB  ARG A 196     1298   2064   2077   -415      8    386       C  
ATOM    791  CG  ARG A 196      10.440   5.994  27.191  1.00 15.20           C  
ANISOU  791  CG  ARG A 196     1343   2275   2158   -738   -110    564       C  
ATOM    792  CD  ARG A 196      10.864   7.157  26.319  1.00 16.69           C  
ANISOU  792  CD  ARG A 196     1646   2446   2248  -1054    -59    594       C  
ATOM    793  NE  ARG A 196      11.768   6.720  25.260  1.00 20.22           N  
ANISOU  793  NE  ARG A 196     2232   2786   2663  -1082    -28    646       N  
ATOM    794  CZ  ARG A 196      12.145   7.478  24.238  1.00 22.79           C  
ANISOU  794  CZ  ARG A 196     2588   3158   2913   -916   -177    648       C  
ATOM    795  NH1 ARG A 196      11.698   8.724  24.137  1.00 23.49           N1+
ANISOU  795  NH1 ARG A 196     2747   3211   2967   -809   -315    743       N1+
ATOM    796  NH2 ARG A 196      12.967   6.984  23.318  1.00 23.80           N  
ANISOU  796  NH2 ARG A 196     2667   3329   3045   -701   -202    425       N  
ATOM    797  N   VAL A 197       8.680   6.788  31.163  1.00 12.59           N  
ANISOU  797  N   VAL A 197     1606   1327   1851   -332   -290    -31       N  
ATOM    798  CA  VAL A 197       7.908   7.631  32.051  1.00 14.38           C  
ANISOU  798  CA  VAL A 197     2122   1391   1952   -223   -153    -78       C  
ATOM    799  C   VAL A 197       8.112   9.068  31.621  1.00 16.41           C  
ANISOU  799  C   VAL A 197     2448   1499   2290   -292     37   -163       C  
ATOM    800  O   VAL A 197       9.239   9.498  31.356  1.00 16.55           O  
ANISOU  800  O   VAL A 197     2396   1463   2428    -73    213   -290       O  
ATOM    801  CB  VAL A 197       8.322   7.463  33.522  1.00 12.97           C  
ANISOU  801  CB  VAL A 197     2199   1137   1593   -193   -118     82       C  
ATOM    802  CG1 VAL A 197       7.759   8.598  34.359  1.00 12.90           C  
ANISOU  802  CG1 VAL A 197     2336   1141   1425   -351   -186    209       C  
ATOM    803  CG2 VAL A 197       7.833   6.138  34.051  1.00 11.82           C  
ANISOU  803  CG2 VAL A 197     2117    828   1547   -221    -32    -15       C  
ATOM    804  N   GLU A 198       7.004   9.791  31.539  1.00 18.10           N  
ANISOU  804  N   GLU A 198     2755   1657   2466   -351   -129     -5       N  
ATOM    805  CA  GLU A 198       6.983  11.180  31.133  1.00 19.66           C  
ANISOU  805  CA  GLU A 198     3100   1638   2733   -224   -338    283       C  
ATOM    806  C   GLU A 198       6.935  12.081  32.372  1.00 20.07           C  
ANISOU  806  C   GLU A 198     3251   1622   2753   -165   -339    513       C  
ATOM    807  O   GLU A 198       6.290  11.746  33.370  1.00 20.52           O  
ANISOU  807  O   GLU A 198     3379   1669   2747    -38   -215    353       O  
ATOM    808  CB  GLU A 198       5.739  11.402  30.279  1.00 21.65           C  
ANISOU  808  CB  GLU A 198     3450   1717   3061    -84   -700    335       C  
ATOM    809  CG  GLU A 198       5.707  12.680  29.486  1.00 24.27           C  
ANISOU  809  CG  GLU A 198     3797   1943   3481     -5   -956    516       C  
ATOM    810  CD  GLU A 198       4.316  12.976  28.943  1.00 25.93           C  
ANISOU  810  CD  GLU A 198     3927   2045   3878    -32  -1000    778       C  
ATOM    811  OE1 GLU A 198       3.618  12.036  28.502  1.00 23.41           O  
ANISOU  811  OE1 GLU A 198     3612   1708   3573   -474  -1148    965       O  
ATOM    812  OE2 GLU A 198       3.917  14.157  28.972  1.00 29.24           O1-
ANISOU  812  OE2 GLU A 198     4217   2515   4380     25  -1018    696       O1-
ATOM    813  N   GLY A 199       7.639  13.210  32.308  1.00 20.08           N  
ANISOU  813  N   GLY A 199     3182   1701   2747   -165   -382    700       N  
ATOM    814  CA  GLY A 199       7.561  14.251  33.324  1.00 19.65           C  
ANISOU  814  CA  GLY A 199     3118   1557   2792     -9   -406    654       C  
ATOM    815  C   GLY A 199       8.006  13.910  34.736  1.00 20.01           C  
ANISOU  815  C   GLY A 199     3037   1729   2835    221   -221    389       C  
ATOM    816  O   GLY A 199       7.425  14.400  35.704  1.00 20.47           O  
ANISOU  816  O   GLY A 199     3135   1786   2858    354   -220    169       O  
ATOM    817  N   ASN A 200       9.035  13.076  34.858  1.00 19.69           N  
ANISOU  817  N   ASN A 200     2688   1960   2833    302   -235    386       N  
ATOM    818  CA  ASN A 200       9.582  12.707  36.161  1.00 17.87           C  
ANISOU  818  CA  ASN A 200     2364   1827   2598    308   -357     89       C  
ATOM    819  C   ASN A 200      11.082  12.457  36.065  1.00 17.84           C  
ANISOU  819  C   ASN A 200     2322   1767   2688    359   -213    -68       C  
ATOM    820  O   ASN A 200      11.514  11.437  35.541  1.00 16.75           O  
ANISOU  820  O   ASN A 200     2017   1665   2683    737    -47    -19       O  
ATOM    821  CB  ASN A 200       8.866  11.467  36.713  1.00 17.05           C  
ANISOU  821  CB  ASN A 200     2151   1761   2567    249   -542     48       C  
ATOM    822  CG  ASN A 200       9.162  11.219  38.183  1.00 17.18           C  
ANISOU  822  CG  ASN A 200     2204   1841   2484    303   -440    -97       C  
ATOM    823  ND2 ASN A 200       8.204  10.631  38.882  1.00 16.24           N  
ANISOU  823  ND2 ASN A 200     2117   1687   2365    543   -265     57       N  
ATOM    824  OD1 ASN A 200      10.241  11.542  38.681  1.00 18.62           O  
ANISOU  824  OD1 ASN A 200     2455   2215   2404    303   -770   -116       O  
ATOM    825  N   LEU A 201      11.867  13.387  36.595  1.00 19.35           N  
ANISOU  825  N   LEU A 201     2473   1916   2964    205   -239    -50       N  
ATOM    826  CA  LEU A 201      13.320  13.359  36.460  1.00 21.94           C  
ANISOU  826  CA  LEU A 201     2877   2125   3336   -102   -423    -75       C  
ATOM    827  C   LEU A 201      13.992  12.346  37.395  1.00 19.92           C  
ANISOU  827  C   LEU A 201     2615   1943   3012   -260   -481   -327       C  
ATOM    828  O   LEU A 201      15.202  12.135  37.322  1.00 20.69           O  
ANISOU  828  O   LEU A 201     2907   1911   3042   -626   -578   -448       O  
ATOM    829  CB  LEU A 201      13.906  14.765  36.663  1.00 25.67           C  
ANISOU  829  CB  LEU A 201     3291   2458   4005   -391   -610     45       C  
ATOM    830  CG  LEU A 201      13.766  15.764  35.504  1.00 30.05           C  
ANISOU  830  CG  LEU A 201     3818   2947   4652   -514   -678    -43       C  
ATOM    831  CD1 LEU A 201      12.311  16.139  35.233  1.00 32.26           C  
ANISOU  831  CD1 LEU A 201     4104   3219   4936   -411   -728    -20       C  
ATOM    832  CD2 LEU A 201      14.582  17.027  35.738  1.00 30.85           C  
ANISOU  832  CD2 LEU A 201     3951   2971   4801   -670   -579   -176       C  
ATOM    833  N   ARG A 202      13.205  11.709  38.257  1.00 17.87           N  
ANISOU  833  N   ARG A 202     2213   1950   2627    -28   -126   -369       N  
ATOM    834  CA  ARG A 202      13.735  10.687  39.156  1.00 17.53           C  
ANISOU  834  CA  ARG A 202     2056   2100   2506    -27      5   -130       C  
ATOM    835  C   ARG A 202      13.496   9.286  38.608  1.00 15.82           C  
ANISOU  835  C   ARG A 202     1759   1997   2256   -174      2    105       C  
ATOM    836  O   ARG A 202      13.721   8.286  39.290  1.00 16.90           O  
ANISOU  836  O   ARG A 202     1795   2165   2460    -47    -81     87       O  
ATOM    837  CB  ARG A 202      13.138  10.846  40.552  1.00 19.40           C  
ANISOU  837  CB  ARG A 202     2433   2271   2669     16    151   -282       C  
ATOM    838  CG  ARG A 202      13.409  12.214  41.160  1.00 22.44           C  
ANISOU  838  CG  ARG A 202     3003   2542   2980   -242    289   -484       C  
ATOM    839  CD  ARG A 202      12.377  12.572  42.207  1.00 26.90           C  
ANISOU  839  CD  ARG A 202     3978   2918   3325   -452    143   -639       C  
ATOM    840  NE  ARG A 202      12.586  11.844  43.453  1.00 30.75           N  
ANISOU  840  NE  ARG A 202     4665   3242   3779   -660    180   -731       N  
ATOM    841  CZ  ARG A 202      11.642  11.637  44.367  1.00 32.68           C  
ANISOU  841  CZ  ARG A 202     4995   3481   3942   -499    303   -798       C  
ATOM    842  NH1 ARG A 202      10.409  12.084  44.166  1.00 32.75           N1+
ANISOU  842  NH1 ARG A 202     4986   3438   4020   -148    324   -867       N1+
ATOM    843  NH2 ARG A 202      11.927  10.961  45.472  1.00 33.67           N  
ANISOU  843  NH2 ARG A 202     5202   3643   3949   -652    145   -794       N  
ATOM    844  N   VAL A 203      13.040   9.227  37.362  1.00 13.42           N  
ANISOU  844  N   VAL A 203     1462   1711   1927   -306      0     34       N  
ATOM    845  CA  VAL A 203      12.832   7.961  36.676  1.00 11.38           C  
ANISOU  845  CA  VAL A 203     1361   1327   1635   -355   -312   -137       C  
ATOM    846  C   VAL A 203      14.142   7.158  36.559  1.00 11.67           C  
ANISOU  846  C   VAL A 203     1519   1451   1464   -247   -406   -103       C  
ATOM    847  O   VAL A 203      15.227   7.720  36.365  1.00 11.30           O  
ANISOU  847  O   VAL A 203     1226   1723   1345    224    -28   -240       O  
ATOM    848  CB  VAL A 203      12.212   8.193  35.275  1.00 12.84           C  
ANISOU  848  CB  VAL A 203     1582   1376   1920   -492   -378    -87       C  
ATOM    849  CG1 VAL A 203      13.174   8.947  34.376  1.00 12.52           C  
ANISOU  849  CG1 VAL A 203     1669   1279   1810   -536   -197    -54       C  
ATOM    850  CG2 VAL A 203      11.830   6.889  34.642  1.00 15.32           C  
ANISOU  850  CG2 VAL A 203     1846   1832   2144   -362   -320     -9       C  
ATOM    851  N   GLU A 204      14.035   5.842  36.705  1.00 12.14           N  
ANISOU  851  N   GLU A 204     1684   1323   1607    -41   -407    195       N  
ATOM    852  CA  GLU A 204      15.191   4.961  36.603  1.00 11.12           C  
ANISOU  852  CA  GLU A 204     1696   1078   1450   -140   -467    405       C  
ATOM    853  C   GLU A 204      14.847   3.817  35.657  1.00 11.50           C  
ANISOU  853  C   GLU A 204     1631   1210   1528   -104   -405    425       C  
ATOM    854  O   GLU A 204      13.725   3.312  35.671  1.00 12.26           O  
ANISOU  854  O   GLU A 204     1584   1313   1762   -554   -184    210       O  
ATOM    855  CB  GLU A 204      15.576   4.438  37.991  1.00 11.20           C  
ANISOU  855  CB  GLU A 204     1713   1200   1342   -212   -354    409       C  
ATOM    856  CG  GLU A 204      16.609   3.323  38.006  1.00 12.51           C  
ANISOU  856  CG  GLU A 204     1917   1459   1375     62   -344    397       C  
ATOM    857  CD  GLU A 204      16.838   2.774  39.399  1.00 13.56           C  
ANISOU  857  CD  GLU A 204     1858   1701   1593    292   -588    142       C  
ATOM    858  OE1 GLU A 204      16.938   3.576  40.356  1.00 14.84           O  
ANISOU  858  OE1 GLU A 204     2182   2014   1442    151   -989    155       O  
ATOM    859  OE2 GLU A 204      16.907   1.535  39.546  1.00 14.38           O1-
ANISOU  859  OE2 GLU A 204     1758   1834   1873    561   -502    -75       O1-
ATOM    860  N   TYR A 205      15.800   3.437  34.812  1.00 11.70           N  
ANISOU  860  N   TYR A 205     1410   1472   1564     50   -427    483       N  
ATOM    861  CA  TYR A 205      15.595   2.341  33.866  1.00 11.83           C  
ANISOU  861  CA  TYR A 205     1511   1554   1429    149   -422    397       C  
ATOM    862  C   TYR A 205      16.571   1.195  34.106  1.00 12.89           C  
ANISOU  862  C   TYR A 205     1597   1725   1575    198   -379    382       C  
ATOM    863  O   TYR A 205      17.748   1.416  34.419  1.00 13.24           O  
ANISOU  863  O   TYR A 205     1559   1846   1625    647   -284    384       O  
ATOM    864  CB  TYR A 205      15.747   2.837  32.433  1.00 11.50           C  
ANISOU  864  CB  TYR A 205     1544   1659   1166    115   -693    258       C  
ATOM    865  CG  TYR A 205      14.697   3.824  31.999  1.00 11.62           C  
ANISOU  865  CG  TYR A 205     1756   1666    992    111   -311    286       C  
ATOM    866  CD1 TYR A 205      14.873   5.187  32.193  1.00 10.81           C  
ANISOU  866  CD1 TYR A 205     1670   1447    991    446   -295    344       C  
ATOM    867  CD2 TYR A 205      13.534   3.392  31.380  1.00  9.67           C  
ANISOU  867  CD2 TYR A 205     1441   1486    746    159   -393    379       C  
ATOM    868  CE1 TYR A 205      13.912   6.091  31.788  1.00 10.24           C  
ANISOU  868  CE1 TYR A 205     1448   1376   1067    211   -499    455       C  
ATOM    869  CE2 TYR A 205      12.575   4.282  30.973  1.00  9.34           C  
ANISOU  869  CE2 TYR A 205     1186   1482    879    214   -448    340       C  
ATOM    870  CZ  TYR A 205      12.765   5.625  31.181  1.00 10.49           C  
ANISOU  870  CZ  TYR A 205     1317   1516   1152    339   -532    395       C  
ATOM    871  OH  TYR A 205      11.798   6.505  30.769  1.00 11.56           O  
ANISOU  871  OH  TYR A 205     1388   1451   1552    457   -621    297       O  
ATOM    872  N   LEU A 206      16.076  -0.029  33.932  1.00 12.31           N  
ANISOU  872  N   LEU A 206     1432   1551   1694    -99   -325    492       N  
ATOM    873  CA  LEU A 206      16.862  -1.228  34.206  1.00 11.45           C  
ANISOU  873  CA  LEU A 206     1215   1400   1737   -186   -391    315       C  
ATOM    874  C   LEU A 206      16.867  -2.198  33.030  1.00 12.28           C  
ANISOU  874  C   LEU A 206     1250   1730   1687   -160   -322    149       C  
ATOM    875  O   LEU A 206      15.812  -2.502  32.468  1.00 12.45           O  
ANISOU  875  O   LEU A 206     1107   1908   1715    -58      2    224       O  
ATOM    876  CB  LEU A 206      16.314  -1.952  35.445  1.00 11.48           C  
ANISOU  876  CB  LEU A 206     1168   1344   1850   -111   -204    214       C  
ATOM    877  CG  LEU A 206      17.033  -3.248  35.840  1.00 12.19           C  
ANISOU  877  CG  LEU A 206     1254   1299   2078   -163   -212    283       C  
ATOM    878  CD1 LEU A 206      18.445  -2.960  36.335  1.00 13.58           C  
ANISOU  878  CD1 LEU A 206     1329   1494   2336   -179   -425    241       C  
ATOM    879  CD2 LEU A 206      16.250  -4.018  36.884  1.00 10.13           C  
ANISOU  879  CD2 LEU A 206     1014    893   1942     46   -112    399       C  
ATOM    880  N   ASP A 207      18.061  -2.657  32.656  1.00 12.78           N  
ANISOU  880  N   ASP A 207     1300   1753   1805     36   -410    276       N  
ATOM    881  CA  ASP A 207      18.222  -3.866  31.857  1.00 13.58           C  
ANISOU  881  CA  ASP A 207     1326   1849   1986    111   -543    255       C  
ATOM    882  C   ASP A 207      18.617  -4.942  32.847  1.00 15.14           C  
ANISOU  882  C   ASP A 207     1403   1875   2476    376   -681    -12       C  
ATOM    883  O   ASP A 207      19.699  -4.867  33.421  1.00 16.41           O  
ANISOU  883  O   ASP A 207     1671   1973   2590    566   -670   -100       O  
ATOM    884  CB  ASP A 207      19.371  -3.731  30.855  1.00 15.70           C  
ANISOU  884  CB  ASP A 207     1593   2376   1995    -40   -339    347       C  
ATOM    885  CG  ASP A 207      19.042  -2.841  29.665  1.00 16.90           C  
ANISOU  885  CG  ASP A 207     1512   2963   1947   -216   -243    592       C  
ATOM    886  OD1 ASP A 207      17.863  -2.538  29.423  1.00 17.65           O  
ANISOU  886  OD1 ASP A 207     1565   3152   1989     57   -317    636       O  
ATOM    887  OD2 ASP A 207      19.991  -2.456  28.951  1.00 17.41           O1-
ANISOU  887  OD2 ASP A 207     1437   3291   1888   -316   -102    687       O1-
ATOM    888  N   ASP A 208      17.760  -5.932  33.067  1.00 16.29           N  
ANISOU  888  N   ASP A 208     1628   1742   2822    457   -758    -67       N  
ATOM    889  CA  ASP A 208      18.093  -6.986  34.020  1.00 17.36           C  
ANISOU  889  CA  ASP A 208     1771   1538   3286    464   -553   -110       C  
ATOM    890  C   ASP A 208      19.290  -7.779  33.511  1.00 19.52           C  
ANISOU  890  C   ASP A 208     1784   1897   3734    351   -530   -256       C  
ATOM    891  O   ASP A 208      19.274  -8.288  32.397  1.00 19.45           O  
ANISOU  891  O   ASP A 208     1590   1884   3917    342   -602   -542       O  
ATOM    892  CB  ASP A 208      16.904  -7.919  34.258  1.00 17.26           C  
ANISOU  892  CB  ASP A 208     2048   1285   3227    400   -449    -33       C  
ATOM    893  CG  ASP A 208      17.067  -8.764  35.515  1.00 17.49           C  
ANISOU  893  CG  ASP A 208     2359   1182   3106    436   -379   -122       C  
ATOM    894  OD1 ASP A 208      17.751  -9.814  35.463  1.00 17.49           O  
ANISOU  894  OD1 ASP A 208     2320   1236   3091    163   -627   -170       O  
ATOM    895  OD2 ASP A 208      16.504  -8.375  36.560  1.00 17.06           O1-
ANISOU  895  OD2 ASP A 208     2506    995   2980    608   -167   -169       O1-
ATOM    896  N   ARG A 209      20.338  -7.871  34.320  1.00 21.90           N  
ANISOU  896  N   ARG A 209     2057   2218   4045    265   -551   -277       N  
ATOM    897  CA  ARG A 209      21.554  -8.547  33.880  1.00 25.72           C  
ANISOU  897  CA  ARG A 209     2629   2703   4440    412   -842   -320       C  
ATOM    898  C   ARG A 209      21.362 -10.056  33.717  1.00 24.80           C  
ANISOU  898  C   ARG A 209     2433   2410   4579    679   -908   -647       C  
ATOM    899  O   ARG A 209      22.122 -10.700  32.999  1.00 25.78           O  
ANISOU  899  O   ARG A 209     2538   2445   4811    598   -759   -687       O  
ATOM    900  CB  ARG A 209      22.703  -8.258  34.845  1.00 30.59           C  
ANISOU  900  CB  ARG A 209     3573   3360   4691    489   -934   -103       C  
ATOM    901  CG  ARG A 209      22.472  -8.853  36.208  1.00 35.56           C  
ANISOU  901  CG  ARG A 209     4377   4090   5044    554   -997     24       C  
ATOM    902  CD  ARG A 209      23.497  -8.402  37.227  1.00 39.78           C  
ANISOU  902  CD  ARG A 209     4988   4744   5383    584   -950    215       C  
ATOM    903  NE  ARG A 209      23.411  -9.226  38.429  1.00 43.26           N  
ANISOU  903  NE  ARG A 209     5491   5302   5644    679   -903    433       N  
ATOM    904  CZ  ARG A 209      22.431  -9.146  39.326  1.00 45.94           C  
ANISOU  904  CZ  ARG A 209     5764   5712   5980    782   -779    615       C  
ATOM    905  NH1 ARG A 209      21.441  -8.275  39.167  1.00 47.23           N1+
ANISOU  905  NH1 ARG A 209     5945   5917   6083    894   -782    727       N1+
ATOM    906  NH2 ARG A 209      22.442  -9.942  40.388  1.00 46.85           N  
ANISOU  906  NH2 ARG A 209     5826   5835   6138    672   -638    622       N  
ATOM    907  N   ASN A 210      20.348 -10.615  34.371  1.00 24.69           N  
ANISOU  907  N   ASN A 210     2486   2380   4516    824   -972   -869       N  
ATOM    908  CA  ASN A 210      20.093 -12.055  34.298  1.00 25.34           C  
ANISOU  908  CA  ASN A 210     2502   2601   4525    702  -1040   -954       C  
ATOM    909  C   ASN A 210      18.980 -12.472  33.333  1.00 24.43           C  
ANISOU  909  C   ASN A 210     2221   2440   4621    285   -886  -1040       C  
ATOM    910  O   ASN A 210      19.128 -13.438  32.578  1.00 24.62           O  
ANISOU  910  O   ASN A 210     1929   2504   4922     62   -940  -1088       O  
ATOM    911  CB  ASN A 210      19.815 -12.609  35.693  1.00 26.79           C  
ANISOU  911  CB  ASN A 210     2821   2897   4460    941  -1196   -968       C  
ATOM    912  CG  ASN A 210      21.032 -12.547  36.582  1.00 29.69           C  
ANISOU  912  CG  ASN A 210     3332   3337   4612    977  -1191  -1005       C  
ATOM    913  ND2 ASN A 210      20.875 -11.966  37.769  1.00 31.27           N  
ANISOU  913  ND2 ASN A 210     3618   3487   4777    904  -1064   -983       N  
ATOM    914  OD1 ASN A 210      22.115 -12.998  36.198  1.00 29.57           O  
ANISOU  914  OD1 ASN A 210     3248   3427   4559   1210  -1372  -1019       O  
ATOM    915  N   THR A 211      17.868 -11.744  33.367  1.00 23.86           N  
ANISOU  915  N   THR A 211     2342   2361   4364    113   -660  -1007       N  
ATOM    916  CA  THR A 211      16.714 -12.062  32.534  1.00 22.10           C  
ANISOU  916  CA  THR A 211     2189   2189   4019    -10   -557   -910       C  
ATOM    917  C   THR A 211      16.667 -11.211  31.268  1.00 22.07           C  
ANISOU  917  C   THR A 211     2382   2293   3709    -15   -451   -810       C  
ATOM    918  O   THR A 211      15.889 -11.500  30.358  1.00 22.93           O  
ANISOU  918  O   THR A 211     2572   2415   3727    -90   -650   -810       O  
ATOM    919  CB  THR A 211      15.397 -11.847  33.299  1.00 20.73           C  
ANISOU  919  CB  THR A 211     1952   1926   4001   -175   -442   -936       C  
ATOM    920  CG2 THR A 211      15.439 -12.538  34.647  1.00 20.72           C  
ANISOU  920  CG2 THR A 211     1961   1910   4000   -371   -424   -756       C  
ATOM    921  OG1 THR A 211      15.193 -10.445  33.493  1.00 20.00           O  
ANISOU  921  OG1 THR A 211     1901   1685   4012   -131   -302  -1051       O  
ATOM    922  N   PHE A 212      17.479 -10.156  31.238  1.00 19.78           N  
ANISOU  922  N   PHE A 212     2097   2097   3320    -55    -83   -754       N  
ATOM    923  CA  PHE A 212      17.553  -9.217  30.112  1.00 19.49           C  
ANISOU  923  CA  PHE A 212     2125   2149   3133    186    148   -633       C  
ATOM    924  C   PHE A 212      16.277  -8.416  29.884  1.00 18.13           C  
ANISOU  924  C   PHE A 212     1828   2337   2723     -2     76   -599       C  
ATOM    925  O   PHE A 212      16.170  -7.683  28.901  1.00 17.15           O  
ANISOU  925  O   PHE A 212     1574   2592   2351   -185      2   -790       O  
ATOM    926  CB  PHE A 212      17.999  -9.909  28.821  1.00 20.48           C  
ANISOU  926  CB  PHE A 212     2407   2036   3340    340    239   -662       C  
ATOM    927  CG  PHE A 212      19.096 -10.902  29.023  1.00 22.92           C  
ANISOU  927  CG  PHE A 212     2705   2272   3732    439    341   -687       C  
ATOM    928  CD1 PHE A 212      20.304 -10.517  29.584  1.00 23.95           C  
ANISOU  928  CD1 PHE A 212     2726   2417   3956    640    494   -736       C  
ATOM    929  CD2 PHE A 212      18.919 -12.222  28.653  1.00 24.38           C  
ANISOU  929  CD2 PHE A 212     2873   2403   3986    707    395   -705       C  
ATOM    930  CE1 PHE A 212      21.319 -11.437  29.779  1.00 25.42           C  
ANISOU  930  CE1 PHE A 212     3057   2440   4163    518    556   -777       C  
ATOM    931  CE2 PHE A 212      19.922 -13.149  28.840  1.00 25.75           C  
ANISOU  931  CE2 PHE A 212     3010   2558   4214    646    486   -743       C  
ATOM    932  CZ  PHE A 212      21.127 -12.757  29.405  1.00 25.97           C  
ANISOU  932  CZ  PHE A 212     3074   2550   4246    547    498   -834       C  
ATOM    933  N   ARG A 213      15.324  -8.544  30.805  1.00 18.04           N  
ANISOU  933  N   ARG A 213     1906   2254   2694    -15     49   -607       N  
ATOM    934  CA  ARG A 213      14.080  -7.775  30.748  1.00 17.37           C  
ANISOU  934  CA  ARG A 213     1974   2079   2548     48    -88   -436       C  
ATOM    935  C   ARG A 213      14.335  -6.281  30.969  1.00 15.32           C  
ANISOU  935  C   ARG A 213     1715   1871   2235    -36     -4   -443       C  
ATOM    936  O   ARG A 213      15.225  -5.885  31.735  1.00 14.01           O  
ANISOU  936  O   ARG A 213     1299   1799   2225   -136   -179   -642       O  
ATOM    937  CB  ARG A 213      13.063  -8.280  31.789  1.00 17.52           C  
ANISOU  937  CB  ARG A 213     1900   1927   2831   -136   -153   -169       C  
ATOM    938  CG  ARG A 213      12.730  -9.765  31.717  1.00 17.88           C  
ANISOU  938  CG  ARG A 213     1985   1877   2933   -193    -23   -238       C  
ATOM    939  CD  ARG A 213      11.613 -10.058  30.758  1.00 17.94           C  
ANISOU  939  CD  ARG A 213     2031   1761   3026   -182     75   -124       C  
ATOM    940  NE  ARG A 213      11.292 -11.485  30.703  1.00 17.85           N  
ANISOU  940  NE  ARG A 213     2081   1703   2999   -282    378    175       N  
ATOM    941  CZ  ARG A 213      10.412 -12.010  29.857  1.00 17.95           C  
ANISOU  941  CZ  ARG A 213     2146   1829   2846   -424    730    198       C  
ATOM    942  NH1 ARG A 213       9.775 -11.221  29.006  1.00 17.72           N1+
ANISOU  942  NH1 ARG A 213     1948   1883   2899   -363    712    137       N1+
ATOM    943  NH2 ARG A 213      10.172 -13.316  29.857  1.00 18.57           N  
ANISOU  943  NH2 ARG A 213     2346   2001   2707   -550    922    476       N  
ATOM    944  N   HIS A 214      13.548  -5.457  30.289  1.00 13.78           N  
ANISOU  944  N   HIS A 214     1637   1745   1853    -14    295   -313       N  
ATOM    945  CA  HIS A 214      13.592  -4.017  30.490  1.00 12.57           C  
ANISOU  945  CA  HIS A 214     1590   1574   1611    -98    252   -185       C  
ATOM    946  C   HIS A 214      12.500  -3.608  31.482  1.00 11.52           C  
ANISOU  946  C   HIS A 214     1574   1400   1403    -47    138    -13       C  
ATOM    947  O   HIS A 214      11.413  -4.188  31.507  1.00 11.26           O  
ANISOU  947  O   HIS A 214     1395   1310   1573   -151    460   -239       O  
ATOM    948  CB  HIS A 214      13.377  -3.290  29.161  1.00 12.43           C  
ANISOU  948  CB  HIS A 214     1580   1664   1477   -144    263   -256       C  
ATOM    949  CG  HIS A 214      14.345  -3.683  28.087  1.00 14.44           C  
ANISOU  949  CG  HIS A 214     1803   1957   1728    263    345   -576       C  
ATOM    950  CD2 HIS A 214      15.565  -4.269  28.155  1.00 15.02           C  
ANISOU  950  CD2 HIS A 214     1813   2055   1839    388    620   -747       C  
ATOM    951  ND1 HIS A 214      14.100  -3.461  26.749  1.00 16.26           N  
ANISOU  951  ND1 HIS A 214     2003   2271   1905    452    212   -684       N  
ATOM    952  CE1 HIS A 214      15.123  -3.899  26.037  1.00 16.33           C  
ANISOU  952  CE1 HIS A 214     2000   2338   1867    585    314   -770       C  
ATOM    953  NE2 HIS A 214      16.025  -4.392  26.866  1.00 15.99           N  
ANISOU  953  NE2 HIS A 214     1952   2241   1885    452    530   -700       N  
ATOM    954  N   SER A 215      12.786  -2.611  32.307  1.00 10.13           N  
ANISOU  954  N   SER A 215     1416   1350   1084    -33    -54    141       N  
ATOM    955  CA  SER A 215      11.757  -2.066  33.178  1.00 10.26           C  
ANISOU  955  CA  SER A 215     1069   1579   1250    -15   -136    156       C  
ATOM    956  C   SER A 215      12.076  -0.641  33.552  1.00 10.49           C  
ANISOU  956  C   SER A 215     1185   1629   1172    129     95    132       C  
ATOM    957  O   SER A 215      13.221  -0.206  33.459  1.00 12.31           O  
ANISOU  957  O   SER A 215     1585   1740   1353    235    395   -182       O  
ATOM    958  CB  SER A 215      11.581  -2.924  34.432  1.00  9.76           C  
ANISOU  958  CB  SER A 215      759   1573   1377   -317   -191    242       C  
ATOM    959  OG  SER A 215      12.775  -2.999  35.191  1.00 10.76           O  
ANISOU  959  OG  SER A 215      856   1662   1570   -327   -490    596       O  
ATOM    960  N   VAL A 216      11.055   0.082  33.986  1.00 10.39           N  
ANISOU  960  N   VAL A 216     1166   1794    987    141    -98     -7       N  
ATOM    961  CA  VAL A 216      11.223   1.476  34.359  1.00 10.65           C  
ANISOU  961  CA  VAL A 216     1301   1818    926    157   -158   -149       C  
ATOM    962  C   VAL A 216      10.628   1.709  35.742  1.00 11.36           C  
ANISOU  962  C   VAL A 216     1471   2045    803     38   -468    -67       C  
ATOM    963  O   VAL A 216       9.469   1.374  35.994  1.00 11.51           O  
ANISOU  963  O   VAL A 216     1550   2205    618     58   -250      6       O  
ATOM    964  CB  VAL A 216      10.571   2.414  33.327  1.00 11.60           C  
ANISOU  964  CB  VAL A 216     1479   1920   1008    200   -201   -380       C  
ATOM    965  CG1 VAL A 216       9.123   1.990  33.023  1.00 11.14           C  
ANISOU  965  CG1 VAL A 216     1329   2001    905    105   -522   -267       C  
ATOM    966  CG2 VAL A 216      10.633   3.824  33.816  1.00 11.74           C  
ANISOU  966  CG2 VAL A 216     1581   1745   1136    350     35   -472       C  
ATOM    967  N   VAL A 217      11.424   2.269  36.645  1.00 11.99           N  
ANISOU  967  N   VAL A 217     1470   2106    981    160   -623   -120       N  
ATOM    968  CA  VAL A 217      11.018   2.363  38.043  1.00 13.08           C  
ANISOU  968  CA  VAL A 217     1687   2093   1189    427   -334      3       C  
ATOM    969  C   VAL A 217      11.040   3.819  38.518  1.00 13.89           C  
ANISOU  969  C   VAL A 217     1761   2180   1339    506   -241    -33       C  
ATOM    970  O   VAL A 217      11.863   4.619  38.061  1.00 14.80           O  
ANISOU  970  O   VAL A 217     1920   2291   1412    384    -22   -240       O  
ATOM    971  CB  VAL A 217      11.876   1.412  38.946  1.00 12.19           C  
ANISOU  971  CB  VAL A 217     1578   2008   1046    632   -344    167       C  
ATOM    972  CG1 VAL A 217      13.331   1.850  38.978  1.00 11.14           C  
ANISOU  972  CG1 VAL A 217     1334   1650   1247    697   -204    361       C  
ATOM    973  CG2 VAL A 217      11.298   1.308  40.353  1.00 10.82           C  
ANISOU  973  CG2 VAL A 217     1321   2082    707    583   -180    108       C  
ATOM    974  N   VAL A 218      10.117   4.155  39.416  1.00 12.91           N  
ANISOU  974  N   VAL A 218     1407   2135   1365    719   -231    199       N  
ATOM    975  CA  VAL A 218       9.895   5.530  39.843  1.00 13.83           C  
ANISOU  975  CA  VAL A 218     1745   2199   1311    309   -279    219       C  
ATOM    976  C   VAL A 218       9.627   5.551  41.354  1.00 14.14           C  
ANISOU  976  C   VAL A 218     1742   2132   1499      8   -367    143       C  
ATOM    977  O   VAL A 218       8.959   4.658  41.865  1.00 13.07           O  
ANISOU  977  O   VAL A 218     1793   1866   1307     35   -408    548       O  
ATOM    978  CB  VAL A 218       8.672   6.125  39.093  1.00 14.35           C  
ANISOU  978  CB  VAL A 218     2114   2285   1051    468   -358    500       C  
ATOM    979  CG1 VAL A 218       8.255   7.446  39.693  1.00 16.45           C  
ANISOU  979  CG1 VAL A 218     2439   2281   1529    752   -506    603       C  
ATOM    980  CG2 VAL A 218       8.956   6.290  37.600  1.00 14.31           C  
ANISOU  980  CG2 VAL A 218     1990   2568    879    385   -392    236       C  
ATOM    981  N   PRO A 219      10.165   6.554  42.079  1.00 16.44           N  
ANISOU  981  N   PRO A 219     1973   2471   1803    -12   -296   -308       N  
ATOM    982  CA  PRO A 219       9.839   6.716  43.505  1.00 16.27           C  
ANISOU  982  CA  PRO A 219     1784   2652   1744   -130   -413   -385       C  
ATOM    983  C   PRO A 219       8.344   6.942  43.703  1.00 17.35           C  
ANISOU  983  C   PRO A 219     2036   2820   1735    -52   -303   -244       C  
ATOM    984  O   PRO A 219       7.785   7.811  43.030  1.00 17.05           O  
ANISOU  984  O   PRO A 219     2031   2784   1664    -92   -350   -196       O  
ATOM    985  CB  PRO A 219      10.568   8.005  43.885  1.00 16.99           C  
ANISOU  985  CB  PRO A 219     1897   2687   1873   -262   -384   -570       C  
ATOM    986  CG  PRO A 219      11.653   8.152  42.883  1.00 18.08           C  
ANISOU  986  CG  PRO A 219     2254   2761   1854   -343   -460   -617       C  
ATOM    987  CD  PRO A 219      11.123   7.573  41.609  1.00 17.49           C  
ANISOU  987  CD  PRO A 219     2095   2655   1896   -379   -497   -674       C  
ATOM    988  N   TYR A 220       7.709   6.190  44.599  1.00 17.37           N  
ANISOU  988  N   TYR A 220     1967   3021   1613     47   -107   -188       N  
ATOM    989  CA  TYR A 220       6.299   6.422  44.910  1.00 17.77           C  
ANISOU  989  CA  TYR A 220     2105   3034   1613    154    300   -397       C  
ATOM    990  C   TYR A 220       6.155   7.707  45.699  1.00 19.46           C  
ANISOU  990  C   TYR A 220     2292   3177   1923    231    333   -545       C  
ATOM    991  O   TYR A 220       6.897   7.942  46.647  1.00 20.21           O  
ANISOU  991  O   TYR A 220     2342   3252   2083    354    418   -511       O  
ATOM    992  CB  TYR A 220       5.705   5.267  45.723  1.00 17.08           C  
ANISOU  992  CB  TYR A 220     2151   2897   1440    174    371   -483       C  
ATOM    993  CG  TYR A 220       4.283   5.530  46.188  1.00 17.44           C  
ANISOU  993  CG  TYR A 220     2355   2866   1407    315    478   -419       C  
ATOM    994  CD1 TYR A 220       3.202   5.298  45.348  1.00 17.33           C  
ANISOU  994  CD1 TYR A 220     2109   2967   1509    313    562   -259       C  
ATOM    995  CD2 TYR A 220       4.026   6.004  47.463  1.00 18.12           C  
ANISOU  995  CD2 TYR A 220     2522   2837   1528    464    557   -563       C  
ATOM    996  CE1 TYR A 220       1.909   5.538  45.761  1.00 17.77           C  
ANISOU  996  CE1 TYR A 220     2358   2906   1487    316    634   -335       C  
ATOM    997  CE2 TYR A 220       2.735   6.243  47.888  1.00 17.44           C  
ANISOU  997  CE2 TYR A 220     2261   2921   1444    489    631   -506       C  
ATOM    998  CZ  TYR A 220       1.682   6.009  47.034  1.00 17.56           C  
ANISOU  998  CZ  TYR A 220     2342   3030   1300    351    445   -520       C  
ATOM    999  OH  TYR A 220       0.398   6.251  47.454  1.00 18.38           O  
ANISOU  999  OH  TYR A 220     2522   3354   1106    490    117   -601       O  
ATOM   1000  N   GLU A 221       5.201   8.541  45.304  1.00 22.25           N  
ANISOU 1000  N   GLU A 221     2790   3413   2251    265    251   -852       N  
ATOM   1001  CA  GLU A 221       4.821   9.695  46.104  1.00 25.83           C  
ANISOU 1001  CA  GLU A 221     3323   3825   2665    385    145  -1149       C  
ATOM   1002  C   GLU A 221       3.336   9.585  46.409  1.00 26.13           C  
ANISOU 1002  C   GLU A 221     3332   3811   2787    610    163  -1097       C  
ATOM   1003  O   GLU A 221       2.534   9.307  45.514  1.00 25.43           O  
ANISOU 1003  O   GLU A 221     3151   3735   2778    626    188  -1255       O  
ATOM   1004  CB  GLU A 221       5.137  11.010  45.380  1.00 29.88           C  
ANISOU 1004  CB  GLU A 221     3963   4254   3137    442    183  -1408       C  
ATOM   1005  CG  GLU A 221       6.628  11.286  45.177  1.00 34.34           C  
ANISOU 1005  CG  GLU A 221     4610   4831   3608    475    337  -1550       C  
ATOM   1006  CD  GLU A 221       7.359  11.639  46.469  1.00 38.81           C  
ANISOU 1006  CD  GLU A 221     5143   5470   4132    572    703  -1530       C  
ATOM   1007  OE1 GLU A 221       6.722  12.191  47.394  1.00 40.72           O  
ANISOU 1007  OE1 GLU A 221     5437   5760   4274    618    898  -1577       O  
ATOM   1008  OE2 GLU A 221       8.580  11.369  46.559  1.00 39.84           O1-
ANISOU 1008  OE2 GLU A 221     5156   5652   4331    466    718  -1505       O1-
ATOM   1009  N   PRO A 222       2.962   9.779  47.683  1.00 26.77           N  
ANISOU 1009  N   PRO A 222     3403   3792   2977    656     42  -1046       N  
ATOM   1010  CA  PRO A 222       1.549   9.685  48.065  1.00 27.48           C  
ANISOU 1010  CA  PRO A 222     3473   3773   3197    803     87   -997       C  
ATOM   1011  C   PRO A 222       0.774  10.829  47.427  1.00 28.20           C  
ANISOU 1011  C   PRO A 222     3456   3767   3492    995    249  -1033       C  
ATOM   1012  O   PRO A 222       1.397  11.825  47.057  1.00 28.55           O  
ANISOU 1012  O   PRO A 222     3488   3665   3694   1050    371   -851       O  
ATOM   1013  CB  PRO A 222       1.590   9.846  49.589  1.00 27.39           C  
ANISOU 1013  CB  PRO A 222     3471   3798   3136    640    -40  -1065       C  
ATOM   1014  CG  PRO A 222       2.846  10.618  49.852  1.00 26.93           C  
ANISOU 1014  CG  PRO A 222     3352   3819   3059    456   -290  -1051       C  
ATOM   1015  CD  PRO A 222       3.825  10.136  48.824  1.00 26.60           C  
ANISOU 1015  CD  PRO A 222     3308   3815   2985    426   -190  -1043       C  
ATOM   1016  N   PRO A 223      -0.555  10.688  47.275  1.00 28.70           N  
ANISOU 1016  N   PRO A 223     3515   3871   3518    965    331  -1322       N  
ATOM   1017  CA  PRO A 223      -1.312  11.773  46.638  1.00 29.54           C  
ANISOU 1017  CA  PRO A 223     3505   3920   3800   1190    362  -1322       C  
ATOM   1018  C   PRO A 223      -1.336  13.011  47.522  1.00 32.07           C  
ANISOU 1018  C   PRO A 223     3782   4141   4261   1313    266  -1093       C  
ATOM   1019  O   PRO A 223      -1.106  12.894  48.728  1.00 32.04           O  
ANISOU 1019  O   PRO A 223     3914   4016   4243   1349     36  -1169       O  
ATOM   1020  CB  PRO A 223      -2.731  11.202  46.526  1.00 28.40           C  
ANISOU 1020  CB  PRO A 223     3319   3830   3643   1148    502  -1477       C  
ATOM   1021  CG  PRO A 223      -2.597   9.724  46.734  1.00 28.23           C  
ANISOU 1021  CG  PRO A 223     3293   3882   3551   1012    524  -1429       C  
ATOM   1022  CD  PRO A 223      -1.408   9.540  47.627  1.00 28.14           C  
ANISOU 1022  CD  PRO A 223     3417   3871   3402    891    385  -1493       C  
ATOM   1023  N   GLU A 224      -1.610  14.173  46.933  1.00 34.79           N  
ANISOU 1023  N   GLU A 224     4105   4459   4655   1232    462   -966       N  
ATOM   1024  CA  GLU A 224      -1.899  15.372  47.709  1.00 36.55           C  
ANISOU 1024  CA  GLU A 224     4374   4584   4929   1355    535  -1038       C  
ATOM   1025  C   GLU A 224      -3.011  14.996  48.680  1.00 37.50           C  
ANISOU 1025  C   GLU A 224     4344   4815   5090   1583    589  -1276       C  
ATOM   1026  O   GLU A 224      -3.823  14.119  48.383  1.00 38.39           O  
ANISOU 1026  O   GLU A 224     4432   4978   5174   1618    615  -1395       O  
ATOM   1027  CB  GLU A 224      -2.374  16.495  46.787  1.00 37.57           C  
ANISOU 1027  CB  GLU A 224     4572   4587   5116   1343    443   -863       C  
ATOM   1028  CG  GLU A 224      -1.608  17.810  46.898  1.00 38.72           C  
ANISOU 1028  CG  GLU A 224     4806   4665   5240   1367    293   -777       C  
ATOM   1029  CD  GLU A 224      -2.225  18.891  46.028  1.00 38.92           C  
ANISOU 1029  CD  GLU A 224     4920   4619   5249   1372     91   -668       C  
ATOM   1030  OE1 GLU A 224      -3.030  18.535  45.143  1.00 38.95           O  
ANISOU 1030  OE1 GLU A 224     4879   4695   5226   1408    -18   -544       O  
ATOM   1031  OE2 GLU A 224      -1.920  20.086  46.228  1.00 38.93           O1-
ANISOU 1031  OE2 GLU A 224     5025   4491   5275   1250     78   -693       O1-
ATOM   1032  N   VAL A 225      -3.042  15.638  49.842  1.00 37.89           N  
ANISOU 1032  N   VAL A 225     4401   4867   5127   1686    609  -1327       N  
ATOM   1033  CA  VAL A 225      -4.011  15.286  50.880  1.00 38.49           C  
ANISOU 1033  CA  VAL A 225     4590   4853   5183   1702    452  -1350       C  
ATOM   1034  C   VAL A 225      -5.460  15.332  50.372  1.00 39.48           C  
ANISOU 1034  C   VAL A 225     4629   5030   5341   1892    473  -1351       C  
ATOM   1035  O   VAL A 225      -6.302  14.523  50.775  1.00 40.92           O  
ANISOU 1035  O   VAL A 225     4816   5269   5464   1705    335  -1300       O  
ATOM   1036  CB  VAL A 225      -3.812  16.160  52.132  1.00 37.27           C  
ANISOU 1036  CB  VAL A 225     4608   4522   5029   1656    301  -1454       C  
ATOM   1037  CG1 VAL A 225      -4.941  15.963  53.135  1.00 35.91           C  
ANISOU 1037  CG1 VAL A 225     4450   4342   4853   1673    352  -1397       C  
ATOM   1038  CG2 VAL A 225      -2.471  15.840  52.765  1.00 37.56           C  
ANISOU 1038  CG2 VAL A 225     4756   4471   5043   1519    246  -1537       C  
ATOM   1039  N   GLY A 226      -5.733  16.252  49.455  1.00 38.47           N  
ANISOU 1039  N   GLY A 226     4471   4830   5316   2265    518  -1453       N  
ATOM   1040  CA  GLY A 226      -7.057  16.353  48.870  1.00 38.33           C  
ANISOU 1040  CA  GLY A 226     4433   4702   5427   2162    660  -1492       C  
ATOM   1041  C   GLY A 226      -7.292  15.420  47.692  1.00 38.74           C  
ANISOU 1041  C   GLY A 226     4386   4789   5545   2037    718  -1428       C  
ATOM   1042  O   GLY A 226      -8.361  15.459  47.081  1.00 39.02           O  
ANISOU 1042  O   GLY A 226     4332   4877   5615   2107    741  -1506       O  
ATOM   1043  N   SER A 227      -6.302  14.582  47.377  1.00 37.97           N  
ANISOU 1043  N   SER A 227     4226   4647   5555   1856    800  -1286       N  
ATOM   1044  CA  SER A 227      -6.385  13.678  46.225  1.00 37.48           C  
ANISOU 1044  CA  SER A 227     4189   4608   5442   1521    854  -1036       C  
ATOM   1045  C   SER A 227      -6.530  12.203  46.611  1.00 36.04           C  
ANISOU 1045  C   SER A 227     3952   4437   5302   1333    896   -891       C  
ATOM   1046  O   SER A 227      -6.181  11.804  47.724  1.00 36.44           O  
ANISOU 1046  O   SER A 227     4035   4379   5430   1277    714   -690       O  
ATOM   1047  CB  SER A 227      -5.181  13.872  45.303  1.00 38.71           C  
ANISOU 1047  CB  SER A 227     4481   4716   5511   1361    745   -892       C  
ATOM   1048  OG  SER A 227      -5.222  15.150  44.702  1.00 39.74           O  
ANISOU 1048  OG  SER A 227     4680   4820   5598   1308    712   -829       O  
ATOM   1049  N   ASP A 228      -7.042  11.406  45.677  1.00 33.98           N  
ANISOU 1049  N   ASP A 228     3581   4318   5013   1205   1102   -955       N  
ATOM   1050  CA  ASP A 228      -7.357  10.004  45.933  1.00 33.28           C  
ANISOU 1050  CA  ASP A 228     3487   4365   4792    969   1192   -829       C  
ATOM   1051  C   ASP A 228      -6.251   9.054  45.485  1.00 29.84           C  
ANISOU 1051  C   ASP A 228     3107   4122   4107    652   1019   -639       C  
ATOM   1052  O   ASP A 228      -6.105   7.960  46.029  1.00 29.39           O  
ANISOU 1052  O   ASP A 228     3097   4019   4052    473   1245   -622       O  
ATOM   1053  CB  ASP A 228      -8.660   9.613  45.225  1.00 36.61           C  
ANISOU 1053  CB  ASP A 228     3819   4743   5349    856   1204   -835       C  
ATOM   1054  CG  ASP A 228      -9.893  10.210  45.876  1.00 41.31           C  
ANISOU 1054  CG  ASP A 228     4497   5210   5988    515    954   -841       C  
ATOM   1055  OD1 ASP A 228      -9.766  11.230  46.588  1.00 42.87           O  
ANISOU 1055  OD1 ASP A 228     4789   5329   6171    246    901   -835       O  
ATOM   1056  OD2 ASP A 228     -10.998   9.653  45.666  1.00 42.81           O1-
ANISOU 1056  OD2 ASP A 228     4608   5414   6245    545    817   -890       O1-
ATOM   1057  N   CYS A 229      -5.478   9.467  44.486  1.00 26.78           N  
ANISOU 1057  N   CYS A 229     2772   3895   3507    536    587   -588       N  
ATOM   1058  CA  CYS A 229      -4.490   8.577  43.890  1.00 23.48           C  
ANISOU 1058  CA  CYS A 229     2329   3512   3082    158    288   -545       C  
ATOM   1059  C   CYS A 229      -3.305   9.332  43.317  1.00 21.45           C  
ANISOU 1059  C   CYS A 229     2065   3386   2697   -213    284   -407       C  
ATOM   1060  O   CYS A 229      -3.302  10.562  43.245  1.00 21.39           O  
ANISOU 1060  O   CYS A 229     1959   3440   2729   -449    293   -203       O  
ATOM   1061  CB  CYS A 229      -5.128   7.738  42.783  1.00 22.41           C  
ANISOU 1061  CB  CYS A 229     2330   3258   2927     84    115   -691       C  
ATOM   1062  SG  CYS A 229      -5.853   8.734  41.470  1.00 22.82           S  
ANISOU 1062  SG  CYS A 229     2522   3179   2969    -59    189   -835       S  
ATOM   1063  N   THR A 230      -2.300   8.570  42.908  1.00 20.09           N  
ANISOU 1063  N   THR A 230     1979   3312   2343   -391     44   -536       N  
ATOM   1064  CA  THR A 230      -1.120   9.117  42.269  1.00 19.65           C  
ANISOU 1064  CA  THR A 230     2039   3327   2100   -430     61   -551       C  
ATOM   1065  C   THR A 230      -1.180   8.773  40.790  1.00 18.97           C  
ANISOU 1065  C   THR A 230     2152   2916   2141   -510    -16   -697       C  
ATOM   1066  O   THR A 230      -1.361   7.611  40.426  1.00 18.63           O  
ANISOU 1066  O   THR A 230     2359   2680   2041   -709   -117   -660       O  
ATOM   1067  CB  THR A 230       0.152   8.521  42.881  1.00 19.06           C  
ANISOU 1067  CB  THR A 230     1688   3568   1988   -393   -224   -447       C  
ATOM   1068  CG2 THR A 230       1.384   9.043  42.167  1.00 19.63           C  
ANISOU 1068  CG2 THR A 230     1811   3516   2132   -727   -462   -446       C  
ATOM   1069  OG1 THR A 230       0.218   8.873  44.267  1.00 20.85           O  
ANISOU 1069  OG1 THR A 230     1909   3834   2179    -37   -264   -175       O  
ATOM   1070  N   THR A 231      -1.036   9.782  39.937  1.00 18.39           N  
ANISOU 1070  N   THR A 231     2036   2637   2314   -431      9   -692       N  
ATOM   1071  CA  THR A 231      -1.052   9.558  38.497  1.00 18.67           C  
ANISOU 1071  CA  THR A 231     1837   2722   2533   -432     23   -661       C  
ATOM   1072  C   THR A 231       0.365   9.549  37.935  1.00 19.25           C  
ANISOU 1072  C   THR A 231     1874   2782   2660   -474    143   -593       C  
ATOM   1073  O   THR A 231       1.169  10.448  38.210  1.00 19.40           O  
ANISOU 1073  O   THR A 231     1697   2873   2799   -541    336   -542       O  
ATOM   1074  CB  THR A 231      -1.894  10.618  37.770  1.00 19.94           C  
ANISOU 1074  CB  THR A 231     2028   2886   2660   -357    142   -646       C  
ATOM   1075  CG2 THR A 231      -1.982  10.311  36.270  1.00 19.77           C  
ANISOU 1075  CG2 THR A 231     2031   2862   2619   -296    141   -530       C  
ATOM   1076  OG1 THR A 231      -3.211  10.637  38.331  1.00 20.92           O  
ANISOU 1076  OG1 THR A 231     2117   3079   2754   -187    179   -678       O  
ATOM   1077  N   ILE A 232       0.667   8.514  37.161  1.00 18.76           N  
ANISOU 1077  N   ILE A 232     1811   2800   2516   -427   -116   -564       N  
ATOM   1078  CA  ILE A 232       1.937   8.412  36.460  1.00 18.94           C  
ANISOU 1078  CA  ILE A 232     1972   2779   2444   -340   -371   -346       C  
ATOM   1079  C   ILE A 232       1.636   8.487  34.966  1.00 17.26           C  
ANISOU 1079  C   ILE A 232     1832   2406   2322   -355   -502   -250       C  
ATOM   1080  O   ILE A 232       0.595   8.004  34.518  1.00 18.18           O  
ANISOU 1080  O   ILE A 232     1977   2483   2449   -269   -643   -181       O  
ATOM   1081  CB  ILE A 232       2.689   7.106  36.847  1.00 20.40           C  
ANISOU 1081  CB  ILE A 232     2166   2938   2646    -77   -491   -192       C  
ATOM   1082  CG1 ILE A 232       4.052   7.025  36.166  1.00 21.13           C  
ANISOU 1082  CG1 ILE A 232     2229   3189   2611     15   -480   -243       C  
ATOM   1083  CG2 ILE A 232       1.865   5.883  36.522  1.00 21.32           C  
ANISOU 1083  CG2 ILE A 232     2399   2938   2762     54   -630      8       C  
ATOM   1084  CD1 ILE A 232       5.035   8.025  36.698  1.00 23.02           C  
ANISOU 1084  CD1 ILE A 232     2515   3505   2727    191   -385   -262       C  
ATOM   1085  N   HIS A 233       2.516   9.132  34.209  1.00 14.61           N  
ANISOU 1085  N   HIS A 233     1467   1976   2107   -370   -178   -228       N  
ATOM   1086  CA  HIS A 233       2.326   9.268  32.770  1.00 14.21           C  
ANISOU 1086  CA  HIS A 233     1638   1729   2033   -102   -259    -63       C  
ATOM   1087  C   HIS A 233       3.317   8.390  32.022  1.00 13.01           C  
ANISOU 1087  C   HIS A 233     1539   1743   1661    -13   -319     70       C  
ATOM   1088  O   HIS A 233       4.502   8.708  31.948  1.00 12.79           O  
ANISOU 1088  O   HIS A 233     1206   1886   1767    194    -91    -51       O  
ATOM   1089  CB  HIS A 233       2.502  10.726  32.328  1.00 14.90           C  
ANISOU 1089  CB  HIS A 233     1982   1407   2271    165   -300    -79       C  
ATOM   1090  CG  HIS A 233       1.350  11.613  32.685  1.00 17.00           C  
ANISOU 1090  CG  HIS A 233     2315   1475   2670    337     31    105       C  
ATOM   1091  CD2 HIS A 233       0.116  11.328  33.163  1.00 16.88           C  
ANISOU 1091  CD2 HIS A 233     2233   1382   2798    504     87    153       C  
ATOM   1092  ND1 HIS A 233       1.398  12.984  32.543  1.00 18.86           N  
ANISOU 1092  ND1 HIS A 233     2615   1739   2814    581    232     63       N  
ATOM   1093  CE1 HIS A 233       0.244  13.504  32.926  1.00 18.86           C  
ANISOU 1093  CE1 HIS A 233     2558   1748   2858    441    122    174       C  
ATOM   1094  NE2 HIS A 233      -0.551  12.520  33.306  1.00 17.36           N  
ANISOU 1094  NE2 HIS A 233     2318   1443   2837    197     42    240       N  
ATOM   1095  N   TYR A 234       2.835   7.284  31.472  1.00 11.44           N  
ANISOU 1095  N   TYR A 234     1329   1733   1287   -174   -592    346       N  
ATOM   1096  CA  TYR A 234       3.686   6.431  30.659  1.00 11.19           C  
ANISOU 1096  CA  TYR A 234     1274   1715   1265    -32   -409    319       C  
ATOM   1097  C   TYR A 234       3.614   6.817  29.183  1.00 12.11           C  
ANISOU 1097  C   TYR A 234     1430   1953   1220     65   -205    204       C  
ATOM   1098  O   TYR A 234       2.605   7.368  28.728  1.00 11.31           O  
ANISOU 1098  O   TYR A 234     1283   2079    935    418    120    -81       O  
ATOM   1099  CB  TYR A 234       3.291   4.964  30.828  1.00 10.80           C  
ANISOU 1099  CB  TYR A 234     1228   1534   1342    -76   -518    529       C  
ATOM   1100  CG  TYR A 234       3.628   4.388  32.174  1.00 12.15           C  
ANISOU 1100  CG  TYR A 234     1438   1557   1620   -186   -197    667       C  
ATOM   1101  CD1 TYR A 234       4.950   4.224  32.572  1.00 12.54           C  
ANISOU 1101  CD1 TYR A 234     1471   1489   1803   -209   -271    596       C  
ATOM   1102  CD2 TYR A 234       2.627   4.003  33.052  1.00 12.92           C  
ANISOU 1102  CD2 TYR A 234     1288   1819   1802   -382   -281    737       C  
ATOM   1103  CE1 TYR A 234       5.264   3.692  33.819  1.00 11.91           C  
ANISOU 1103  CE1 TYR A 234     1336   1441   1747    -40   -339    649       C  
ATOM   1104  CE2 TYR A 234       2.931   3.461  34.293  1.00 13.18           C  
ANISOU 1104  CE2 TYR A 234     1335   1942   1729   -196   -317    578       C  
ATOM   1105  CZ  TYR A 234       4.248   3.314  34.670  1.00 12.41           C  
ANISOU 1105  CZ  TYR A 234     1376   1699   1641     46   -386    669       C  
ATOM   1106  OH  TYR A 234       4.536   2.784  35.902  1.00 12.33           O  
ANISOU 1106  OH  TYR A 234     1415   1815   1454    -99   -430    525       O  
ATOM   1107  N   ASN A 235       4.695   6.533  28.455  1.00 12.44           N  
ANISOU 1107  N   ASN A 235     1307   2133   1288   -179   -249    167       N  
ATOM   1108  CA  ASN A 235       4.723   6.602  26.996  1.00 13.62           C  
ANISOU 1108  CA  ASN A 235     1510   2236   1428   -251   -706    108       C  
ATOM   1109  C   ASN A 235       5.155   5.246  26.450  1.00 13.11           C  
ANISOU 1109  C   ASN A 235     1363   2149   1469   -184   -644    395       C  
ATOM   1110  O   ASN A 235       6.135   4.670  26.914  1.00 13.83           O  
ANISOU 1110  O   ASN A 235     1492   2133   1630   -103   -517    482       O  
ATOM   1111  CB  ASN A 235       5.706   7.670  26.485  1.00 15.15           C  
ANISOU 1111  CB  ASN A 235     1680   2389   1686   -560   -699    126       C  
ATOM   1112  CG  ASN A 235       5.431   9.067  27.032  1.00 17.86           C  
ANISOU 1112  CG  ASN A 235     1920   2580   2287   -919   -860    300       C  
ATOM   1113  ND2 ASN A 235       4.164   9.403  27.219  1.00 18.28           N  
ANISOU 1113  ND2 ASN A 235     2056   2642   2248   -570   -897    401       N  
ATOM   1114  OD1 ASN A 235       6.362   9.834  27.279  1.00 20.29           O  
ANISOU 1114  OD1 ASN A 235     2130   2694   2887  -1071   -604    444       O  
ATOM   1115  N   TYR A 236       4.418   4.738  25.472  1.00 12.91           N  
ANISOU 1115  N   TYR A 236     1429   2156   1319   -405   -213    503       N  
ATOM   1116  CA  TYR A 236       4.785   3.509  24.787  1.00 11.89           C  
ANISOU 1116  CA  TYR A 236     1238   1993   1287   -267    110    652       C  
ATOM   1117  C   TYR A 236       5.411   3.886  23.448  1.00 13.35           C  
ANISOU 1117  C   TYR A 236     1320   2323   1430     -7    -73    718       C  
ATOM   1118  O   TYR A 236       4.789   4.571  22.626  1.00 13.77           O  
ANISOU 1118  O   TYR A 236     1469   2326   1439    356   -169    897       O  
ATOM   1119  CB  TYR A 236       3.561   2.609  24.608  1.00 11.69           C  
ANISOU 1119  CB  TYR A 236     1254   1878   1309   -153    109    308       C  
ATOM   1120  CG  TYR A 236       3.082   1.998  25.908  1.00 11.97           C  
ANISOU 1120  CG  TYR A 236     1372   1932   1242   -576    -97    214       C  
ATOM   1121  CD1 TYR A 236       2.292   2.727  26.789  1.00 12.44           C  
ANISOU 1121  CD1 TYR A 236     1294   1964   1467   -866     25    188       C  
ATOM   1122  CD2 TYR A 236       3.427   0.699  26.260  1.00 10.72           C  
ANISOU 1122  CD2 TYR A 236     1250   1764   1058   -744   -413    439       C  
ATOM   1123  CE1 TYR A 236       1.863   2.183  27.993  1.00 12.68           C  
ANISOU 1123  CE1 TYR A 236     1287   1963   1567   -867     -4    326       C  
ATOM   1124  CE2 TYR A 236       2.998   0.145  27.456  1.00 12.18           C  
ANISOU 1124  CE2 TYR A 236     1431   1926   1271   -696   -276    657       C  
ATOM   1125  CZ  TYR A 236       2.214   0.893  28.319  1.00 12.15           C  
ANISOU 1125  CZ  TYR A 236     1293   2025   1298   -561    -48    767       C  
ATOM   1126  OH  TYR A 236       1.780   0.355  29.511  1.00 13.68           O  
ANISOU 1126  OH  TYR A 236     1443   2523   1231   -377    -35    732       O  
ATOM   1127  N   MET A 237       6.650   3.449  23.240  1.00 14.51           N  
ANISOU 1127  N   MET A 237     1503   2478   1533   -322    140    400       N  
ATOM   1128  CA  MET A 237       7.489   4.008  22.180  1.00 14.32           C  
ANISOU 1128  CA  MET A 237     1353   2628   1461   -409    100    210       C  
ATOM   1129  C   MET A 237       7.566   3.169  20.904  1.00 14.70           C  
ANISOU 1129  C   MET A 237     1373   2888   1325   -219   -120     90       C  
ATOM   1130  O   MET A 237       8.392   3.442  20.038  1.00 13.89           O  
ANISOU 1130  O   MET A 237     1116   2842   1320   -383    -81    294       O  
ATOM   1131  CB  MET A 237       8.893   4.291  22.712  1.00 14.47           C  
ANISOU 1131  CB  MET A 237     1258   2536   1704   -817   -204    103       C  
ATOM   1132  CG  MET A 237       8.917   5.280  23.857  1.00 16.19           C  
ANISOU 1132  CG  MET A 237     1693   2463   1995   -676   -133     12       C  
ATOM   1133  SD  MET A 237       8.049   6.826  23.510  1.00 18.10           S  
ANISOU 1133  SD  MET A 237     2195   2284   2396   -645   -168   -141       S  
ATOM   1134  CE  MET A 237       9.022   7.456  22.148  1.00 19.07           C  
ANISOU 1134  CE  MET A 237     2350   2302   2595   -634   -275   -108       C  
ATOM   1135  N   CYS A 238       6.699   2.164  20.803  1.00 15.39           N  
ANISOU 1135  N   CYS A 238     1545   3011   1291    -49   -269   -159       N  
ATOM   1136  CA  CYS A 238       6.488   1.399  19.570  1.00 16.87           C  
ANISOU 1136  CA  CYS A 238     1719   3308   1384   -175    -89   -184       C  
ATOM   1137  C   CYS A 238       4.997   1.135  19.398  1.00 15.34           C  
ANISOU 1137  C   CYS A 238     1589   3103   1136   -414    266   -282       C  
ATOM   1138  O   CYS A 238       4.267   1.010  20.382  1.00 14.95           O  
ANISOU 1138  O   CYS A 238     1789   2917    976   -418    293   -531       O  
ATOM   1139  CB  CYS A 238       7.198   0.045  19.643  1.00 18.98           C  
ANISOU 1139  CB  CYS A 238     1866   3945   1399    -79    110   -281       C  
ATOM   1140  SG  CYS A 238       8.816  -0.065  18.899  1.00 20.34           S  
ANISOU 1140  SG  CYS A 238     2103   4443   1181    149     30    -40       S  
ATOM   1141  N   ASN A 239       4.550   1.037  18.151  1.00 15.98           N  
ANISOU 1141  N   ASN A 239     1714   3244   1115   -409    430   -118       N  
ATOM   1142  CA  ASN A 239       3.189   0.588  17.858  1.00 17.32           C  
ANISOU 1142  CA  ASN A 239     2022   3388   1169   -218    433    101       C  
ATOM   1143  C   ASN A 239       3.066  -0.931  17.958  1.00 16.50           C  
ANISOU 1143  C   ASN A 239     1986   3358    926   -169    195     82       C  
ATOM   1144  O   ASN A 239       4.043  -1.648  17.747  1.00 16.22           O  
ANISOU 1144  O   ASN A 239     1965   3349    850   -108     20   -144       O  
ATOM   1145  CB  ASN A 239       2.743   1.061  16.466  1.00 18.65           C  
ANISOU 1145  CB  ASN A 239     2301   3463   1324    -34    423    211       C  
ATOM   1146  CG  ASN A 239       2.134   2.444  16.488  1.00 20.11           C  
ANISOU 1146  CG  ASN A 239     2532   3708   1402    -38    612    398       C  
ATOM   1147  ND2 ASN A 239       2.518   3.271  15.525  1.00 19.91           N  
ANISOU 1147  ND2 ASN A 239     2623   3664   1279     18    643    493       N  
ATOM   1148  OD1 ASN A 239       1.334   2.773  17.368  1.00 21.69           O  
ANISOU 1148  OD1 ASN A 239     2701   3893   1646    -40    449    140       O  
ATOM   1149  N   SER A 240       1.869  -1.418  18.271  1.00 16.40           N  
ANISOU 1149  N   SER A 240     2057   3195    978   -268    358    284       N  
ATOM   1150  CA  SER A 240       1.639  -2.859  18.312  1.00 17.03           C  
ANISOU 1150  CA  SER A 240     1904   3401   1163   -335    356    -72       C  
ATOM   1151  C   SER A 240       1.948  -3.480  16.956  1.00 19.13           C  
ANISOU 1151  C   SER A 240     2071   3704   1492   -349    348   -223       C  
ATOM   1152  O   SER A 240       2.350  -4.636  16.876  1.00 20.36           O  
ANISOU 1152  O   SER A 240     2144   3786   1804   -306    298   -247       O  
ATOM   1153  CB  SER A 240       0.202  -3.184  18.727  1.00 16.78           C  
ANISOU 1153  CB  SER A 240     1885   3193   1298   -250    374    -83       C  
ATOM   1154  OG  SER A 240       0.016  -2.991  20.109  1.00 15.83           O  
ANISOU 1154  OG  SER A 240     1808   2881   1324   -155    348   -234       O  
ATOM   1155  N   SER A 241       1.785  -2.686  15.902  1.00 19.42           N  
ANISOU 1155  N   SER A 241     2084   3968   1326   -301     16   -204       N  
ATOM   1156  CA  SER A 241       1.943  -3.153  14.527  1.00 21.75           C  
ANISOU 1156  CA  SER A 241     2491   4314   1458   -184    165   -199       C  
ATOM   1157  C   SER A 241       3.366  -2.994  13.972  1.00 23.25           C  
ANISOU 1157  C   SER A 241     2657   4629   1548   -123    265   -229       C  
ATOM   1158  O   SER A 241       3.595  -3.195  12.776  1.00 24.88           O  
ANISOU 1158  O   SER A 241     3002   4859   1592   -222    384   -214       O  
ATOM   1159  CB  SER A 241       0.965  -2.409  13.623  1.00 23.45           C  
ANISOU 1159  CB  SER A 241     2990   4319   1600    -34     75   -207       C  
ATOM   1160  OG  SER A 241       1.219  -1.020  13.667  1.00 24.68           O  
ANISOU 1160  OG  SER A 241     3201   4462   1716    126     -2   -244       O  
ATOM   1161  N   CYS A 242       4.321  -2.641  14.828  1.00 22.61           N  
ANISOU 1161  N   CYS A 242     2336   4649   1607     33    284    -96       N  
ATOM   1162  CA  CYS A 242       5.695  -2.423  14.365  1.00 22.44           C  
ANISOU 1162  CA  CYS A 242     2220   4686   1619    166    350     24       C  
ATOM   1163  C   CYS A 242       6.360  -3.694  13.836  1.00 24.00           C  
ANISOU 1163  C   CYS A 242     2666   4747   1708    404    577    133       C  
ATOM   1164  O   CYS A 242       6.523  -4.671  14.574  1.00 25.22           O  
ANISOU 1164  O   CYS A 242     3020   4706   1855    383    808    125       O  
ATOM   1165  CB  CYS A 242       6.554  -1.815  15.471  1.00 20.81           C  
ANISOU 1165  CB  CYS A 242     1733   4673   1500   -102    101    200       C  
ATOM   1166  SG  CYS A 242       6.517  -0.023  15.515  1.00 20.62           S  
ANISOU 1166  SG  CYS A 242     1696   4708   1430   -266     15    556       S  
ATOM   1167  N   MET A 243       6.748  -3.669  12.560  1.00 23.55           N  
ANISOU 1167  N   MET A 243     2631   4728   1588    470    390    139       N  
ATOM   1168  CA  MET A 243       7.492  -4.770  11.962  1.00 23.26           C  
ANISOU 1168  CA  MET A 243     2687   4630   1522    478    312    193       C  
ATOM   1169  C   MET A 243       8.851  -4.884  12.645  1.00 23.03           C  
ANISOU 1169  C   MET A 243     2732   4549   1468    664    427     26       C  
ATOM   1170  O   MET A 243       9.571  -3.891  12.781  1.00 23.38           O  
ANISOU 1170  O   MET A 243     2765   4669   1450    730    419     51       O  
ATOM   1171  CB  MET A 243       7.690  -4.537  10.463  1.00 24.59           C  
ANISOU 1171  CB  MET A 243     2910   4686   1748    294    143    513       C  
ATOM   1172  CG  MET A 243       6.412  -4.219   9.699  1.00 26.32           C  
ANISOU 1172  CG  MET A 243     3279   4759   1964     -5     30    686       C  
ATOM   1173  SD  MET A 243       6.714  -4.064   7.928  1.00 28.25           S  
ANISOU 1173  SD  MET A 243     3620   4841   2272     77   -184    795       S  
ATOM   1174  CE  MET A 243       7.242  -5.731   7.532  1.00 29.01           C  
ANISOU 1174  CE  MET A 243     3752   4934   2338    103   -188    913       C  
ATOM   1175  N   GLY A 244       9.195  -6.090  13.088  1.00 22.84           N  
ANISOU 1175  N   GLY A 244     2846   4259   1574    887    517   -276       N  
ATOM   1176  CA  GLY A 244      10.476  -6.317  13.734  1.00 23.64           C  
ANISOU 1176  CA  GLY A 244     3148   4055   1779    711    434   -449       C  
ATOM   1177  C   GLY A 244      10.466  -6.052  15.230  1.00 24.74           C  
ANISOU 1177  C   GLY A 244     3353   4022   2026    408    404   -347       C  
ATOM   1178  O   GLY A 244      11.454  -6.301  15.922  1.00 25.88           O  
ANISOU 1178  O   GLY A 244     3670   4006   2156    373    135   -447       O  
ATOM   1179  N   GLY A 245       9.353  -5.531  15.735  1.00 24.20           N  
ANISOU 1179  N   GLY A 245     3179   4011   2004     60    788   -403       N  
ATOM   1180  CA  GLY A 245       9.211  -5.312  17.161  1.00 24.72           C  
ANISOU 1180  CA  GLY A 245     3192   4032   2167    -29    885   -570       C  
ATOM   1181  C   GLY A 245       8.151  -6.231  17.737  1.00 24.69           C  
ANISOU 1181  C   GLY A 245     3280   3969   2132    248    993   -738       C  
ATOM   1182  O   GLY A 245       8.265  -7.457  17.649  1.00 24.64           O  
ANISOU 1182  O   GLY A 245     3327   3799   2237    583   1082   -964       O  
ATOM   1183  N   MET A 246       7.110  -5.642  18.318  1.00 23.19           N  
ANISOU 1183  N   MET A 246     3136   3877   1798    184    800   -969       N  
ATOM   1184  CA  MET A 246       5.987  -6.429  18.817  1.00 22.10           C  
ANISOU 1184  CA  MET A 246     2919   3838   1640    -14    537  -1064       C  
ATOM   1185  C   MET A 246       5.324  -7.231  17.701  1.00 23.79           C  
ANISOU 1185  C   MET A 246     3281   3931   1827   -190    339  -1278       C  
ATOM   1186  O   MET A 246       4.744  -8.286  17.953  1.00 24.15           O  
ANISOU 1186  O   MET A 246     3391   3929   1857   -118    214  -1341       O  
ATOM   1187  CB  MET A 246       4.978  -5.541  19.543  1.00 20.89           C  
ANISOU 1187  CB  MET A 246     2568   3791   1580   -142    318   -943       C  
ATOM   1188  CG  MET A 246       5.485  -5.070  20.893  1.00 19.76           C  
ANISOU 1188  CG  MET A 246     2403   3824   1279   -228    296   -663       C  
ATOM   1189  SD  MET A 246       4.397  -3.912  21.727  1.00 19.50           S  
ANISOU 1189  SD  MET A 246     2324   3866   1221   -116    125   -390       S  
ATOM   1190  CE  MET A 246       4.720  -2.402  20.814  1.00 20.71           C  
ANISOU 1190  CE  MET A 246     2628   3901   1341    -58    106   -188       C  
ATOM   1191  N   ASN A 247       5.418  -6.723  16.474  1.00 25.14           N  
ANISOU 1191  N   ASN A 247     3686   4019   1846   -295      5  -1360       N  
ATOM   1192  CA  ASN A 247       5.071  -7.500  15.285  1.00 27.16           C  
ANISOU 1192  CA  ASN A 247     4383   4134   1802   -171   -137  -1287       C  
ATOM   1193  C   ASN A 247       3.630  -8.010  15.336  1.00 26.34           C  
ANISOU 1193  C   ASN A 247     4336   3968   1704   -240   -316  -1205       C  
ATOM   1194  O   ASN A 247       3.364  -9.172  15.022  1.00 26.81           O  
ANISOU 1194  O   ASN A 247     4433   3954   1799   -358   -282  -1247       O  
ATOM   1195  CB  ASN A 247       6.055  -8.667  15.136  1.00 30.40           C  
ANISOU 1195  CB  ASN A 247     5123   4359   2069    236   -114  -1360       C  
ATOM   1196  CG  ASN A 247       6.012  -9.307  13.765  1.00 34.51           C  
ANISOU 1196  CG  ASN A 247     5886   4629   2597    702    -45  -1367       C  
ATOM   1197  ND2 ASN A 247       6.529 -10.529  13.669  1.00 35.21           N  
ANISOU 1197  ND2 ASN A 247     5945   4541   2892    913    124  -1425       N  
ATOM   1198  OD1 ASN A 247       5.525  -8.714  12.802  1.00 36.10           O  
ANISOU 1198  OD1 ASN A 247     6273   4856   2587    906   -186  -1405       O  
ATOM   1199  N   ARG A 248       2.724  -7.129  15.761  1.00 25.64           N  
ANISOU 1199  N   ARG A 248     4202   3836   1704   -119   -364  -1178       N  
ATOM   1200  CA  ARG A 248       1.290  -7.418  15.893  1.00 27.29           C  
ANISOU 1200  CA  ARG A 248     4294   4064   2012    -49   -330  -1069       C  
ATOM   1201  C   ARG A 248       0.927  -8.307  17.104  1.00 26.37           C  
ANISOU 1201  C   ARG A 248     3937   3962   2119     71   -537   -946       C  
ATOM   1202  O   ARG A 248      -0.226  -8.695  17.271  1.00 26.71           O  
ANISOU 1202  O   ARG A 248     3819   4032   2299    -20   -497   -831       O  
ATOM   1203  CB  ARG A 248       0.707  -7.958  14.575  1.00 30.18           C  
ANISOU 1203  CB  ARG A 248     4729   4392   2345    -73    -97  -1145       C  
ATOM   1204  CG  ARG A 248       0.939  -7.028  13.385  1.00 33.70           C  
ANISOU 1204  CG  ARG A 248     5304   4703   2797     47     -6  -1073       C  
ATOM   1205  CD  ARG A 248       0.741  -7.731  12.039  1.00 37.74           C  
ANISOU 1205  CD  ARG A 248     5782   5168   3390    147     56   -789       C  
ATOM   1206  NE  ARG A 248       1.588  -8.917  11.899  1.00 40.64           N  
ANISOU 1206  NE  ARG A 248     6087   5526   3827    274    276   -588       N  
ATOM   1207  CZ  ARG A 248       2.871  -8.891  11.545  1.00 42.34           C  
ANISOU 1207  CZ  ARG A 248     6219   5725   4144    207    278   -440       C  
ATOM   1208  NH1 ARG A 248       3.471  -7.736  11.294  1.00 43.12           N1+
ANISOU 1208  NH1 ARG A 248     6299   5825   4261     -6    218   -399       N1+
ATOM   1209  NH2 ARG A 248       3.558 -10.023  11.446  1.00 42.45           N  
ANISOU 1209  NH2 ARG A 248     6158   5722   4249    368    304   -459       N  
ATOM   1210  N   ARG A 249       1.904  -8.604  17.958  1.00 24.55           N  
ANISOU 1210  N   ARG A 249     3725   3747   1855    223   -517  -1068       N  
ATOM   1211  CA  ARG A 249       1.652  -9.433  19.137  1.00 22.90           C  
ANISOU 1211  CA  ARG A 249     3360   3510   1830    244   -434   -998       C  
ATOM   1212  C   ARG A 249       1.181  -8.594  20.325  1.00 21.61           C  
ANISOU 1212  C   ARG A 249     2925   3443   1842    112   -392   -820       C  
ATOM   1213  O   ARG A 249       1.793  -7.577  20.651  1.00 22.06           O  
ANISOU 1213  O   ARG A 249     2919   3680   1784     17   -371   -801       O  
ATOM   1214  CB  ARG A 249       2.908 -10.220  19.522  1.00 22.11           C  
ANISOU 1214  CB  ARG A 249     3231   3386   1784    305   -461   -922       C  
ATOM   1215  CG  ARG A 249       3.375 -11.198  18.458  1.00 22.22           C  
ANISOU 1215  CG  ARG A 249     3233   3358   1851    323   -298   -933       C  
ATOM   1216  CD  ARG A 249       4.749 -11.752  18.774  1.00 21.99           C  
ANISOU 1216  CD  ARG A 249     3301   3301   1752    110   -246  -1054       C  
ATOM   1217  NE  ARG A 249       5.790 -10.728  18.718  1.00 21.66           N  
ANISOU 1217  NE  ARG A 249     3485   3104   1640    -34   -109  -1216       N  
ATOM   1218  CZ  ARG A 249       7.080 -10.959  18.942  1.00 21.48           C  
ANISOU 1218  CZ  ARG A 249     3468   2976   1715    -18     56  -1256       C  
ATOM   1219  NH1 ARG A 249       7.492 -12.181  19.238  1.00 20.96           N1+
ANISOU 1219  NH1 ARG A 249     3456   2776   1732    157    158  -1228       N1+
ATOM   1220  NH2 ARG A 249       7.957  -9.968  18.870  1.00 21.74           N  
ANISOU 1220  NH2 ARG A 249     3370   3073   1819   -184    137  -1308       N  
ATOM   1221  N   PRO A 250       0.082  -9.017  20.973  1.00 20.31           N  
ANISOU 1221  N   PRO A 250     2553   3217   1944    -90   -352   -758       N  
ATOM   1222  CA  PRO A 250      -0.428  -8.338  22.173  1.00 19.54           C  
ANISOU 1222  CA  PRO A 250     2309   3058   2056   -321   -220   -805       C  
ATOM   1223  C   PRO A 250       0.552  -8.438  23.342  1.00 18.14           C  
ANISOU 1223  C   PRO A 250     2125   2773   1996   -444   -209   -642       C  
ATOM   1224  O   PRO A 250       1.229  -9.458  23.489  1.00 18.29           O  
ANISOU 1224  O   PRO A 250     2138   2858   1953   -700   -364   -375       O  
ATOM   1225  CB  PRO A 250      -1.710  -9.119  22.503  1.00 19.88           C  
ANISOU 1225  CB  PRO A 250     2351   2985   2216   -357    -29   -914       C  
ATOM   1226  CG  PRO A 250      -1.562 -10.438  21.790  1.00 20.79           C  
ANISOU 1226  CG  PRO A 250     2526   3090   2284   -303    -35   -843       C  
ATOM   1227  CD  PRO A 250      -0.804 -10.113  20.543  1.00 20.54           C  
ANISOU 1227  CD  PRO A 250     2617   3117   2070   -226   -223   -817       C  
ATOM   1228  N   ILE A 251       0.621  -7.385  24.154  1.00 16.85           N  
ANISOU 1228  N   ILE A 251     1962   2516   1924   -292   -211   -704       N  
ATOM   1229  CA  ILE A 251       1.480  -7.357  25.331  1.00 15.43           C  
ANISOU 1229  CA  ILE A 251     1852   2179   1833     67    -99   -672       C  
ATOM   1230  C   ILE A 251       0.675  -7.000  26.580  1.00 14.97           C  
ANISOU 1230  C   ILE A 251     1864   2149   1676    -98   -141   -512       C  
ATOM   1231  O   ILE A 251      -0.421  -6.439  26.486  1.00 14.38           O  
ANISOU 1231  O   ILE A 251     1855   2173   1437   -394   -214   -472       O  
ATOM   1232  CB  ILE A 251       2.621  -6.323  25.189  1.00 15.18           C  
ANISOU 1232  CB  ILE A 251     1814   1851   2103    443     98   -628       C  
ATOM   1233  CG1 ILE A 251       2.054  -4.916  24.982  1.00 15.10           C  
ANISOU 1233  CG1 ILE A 251     1801   1670   2267    379     29   -519       C  
ATOM   1234  CG2 ILE A 251       3.578  -6.699  24.056  1.00 14.92           C  
ANISOU 1234  CG2 ILE A 251     1824   1774   2071    553    280   -642       C  
ATOM   1235  CD1 ILE A 251       3.027  -3.798  25.305  1.00 14.80           C  
ANISOU 1235  CD1 ILE A 251     1797   1546   2281    353    158   -370       C  
ATOM   1236  N   LEU A 252       1.235  -7.326  27.743  1.00 15.03           N  
ANISOU 1236  N   LEU A 252     1762   2195   1754   -111   -318   -476       N  
ATOM   1237  CA  LEU A 252       0.714  -6.864  29.025  1.00 15.46           C  
ANISOU 1237  CA  LEU A 252     1871   2078   1924     89   -197   -372       C  
ATOM   1238  C   LEU A 252       1.748  -5.943  29.638  1.00 14.20           C  
ANISOU 1238  C   LEU A 252     1772   1955   1668    339   -315   -429       C  
ATOM   1239  O   LEU A 252       2.949  -6.135  29.441  1.00 14.73           O  
ANISOU 1239  O   LEU A 252     1817   1932   1848    496   -599   -558       O  
ATOM   1240  CB  LEU A 252       0.506  -8.025  29.992  1.00 17.64           C  
ANISOU 1240  CB  LEU A 252     2089   2354   2260    127    164    -77       C  
ATOM   1241  CG  LEU A 252      -0.198  -9.294  29.535  1.00 21.36           C  
ANISOU 1241  CG  LEU A 252     2555   2748   2814    303    295    524       C  
ATOM   1242  CD1 LEU A 252      -0.237 -10.280  30.687  1.00 23.26           C  
ANISOU 1242  CD1 LEU A 252     2901   2897   3039    438    353    669       C  
ATOM   1243  CD2 LEU A 252      -1.602  -8.990  29.033  1.00 22.67           C  
ANISOU 1243  CD2 LEU A 252     2586   2949   3079    328    286    594       C  
ATOM   1244  N   THR A 253       1.287  -4.947  30.384  1.00 12.32           N  
ANISOU 1244  N   THR A 253     1576   1809   1297    521      0   -333       N  
ATOM   1245  CA  THR A 253       2.176  -4.176  31.239  1.00 12.81           C  
ANISOU 1245  CA  THR A 253     1631   1934   1304    458   -143   -116       C  
ATOM   1246  C   THR A 253       1.930  -4.649  32.662  1.00 13.83           C  
ANISOU 1246  C   THR A 253     1642   2147   1466    291    -26     12       C  
ATOM   1247  O   THR A 253       0.780  -4.694  33.108  1.00 14.19           O  
ANISOU 1247  O   THR A 253     1905   2133   1352    113     23    212       O  
ATOM   1248  CB  THR A 253       1.894  -2.669  31.131  1.00 13.26           C  
ANISOU 1248  CB  THR A 253     1823   1897   1320    387   -314     65       C  
ATOM   1249  CG2 THR A 253       2.749  -1.876  32.117  1.00 13.02           C  
ANISOU 1249  CG2 THR A 253     1877   1982   1088    310   -447    202       C  
ATOM   1250  OG1 THR A 253       2.168  -2.227  29.794  1.00 15.13           O  
ANISOU 1250  OG1 THR A 253     2089   2167   1491    481   -255    -31       O  
ATOM   1251  N   ILE A 254       3.001  -5.024  33.362  1.00 12.47           N  
ANISOU 1251  N   ILE A 254     1338   2023   1376    199     42    -33       N  
ATOM   1252  CA  ILE A 254       2.918  -5.409  34.768  1.00 11.70           C  
ANISOU 1252  CA  ILE A 254     1509   1705   1232     66    -18    -58       C  
ATOM   1253  C   ILE A 254       3.474  -4.278  35.632  1.00 11.48           C  
ANISOU 1253  C   ILE A 254     1474   1742   1144   -100    109    -64       C  
ATOM   1254  O   ILE A 254       4.619  -3.848  35.445  1.00 10.63           O  
ANISOU 1254  O   ILE A 254     1359   1761    918      3    144   -102       O  
ATOM   1255  CB  ILE A 254       3.705  -6.707  35.055  1.00 13.08           C  
ANISOU 1255  CB  ILE A 254     1815   1865   1289   -207    -26    -71       C  
ATOM   1256  CG1 ILE A 254       3.192  -7.854  34.181  1.00 14.39           C  
ANISOU 1256  CG1 ILE A 254     2273   1944   1251     63    111    -75       C  
ATOM   1257  CG2 ILE A 254       3.599  -7.091  36.528  1.00 12.29           C  
ANISOU 1257  CG2 ILE A 254     1603   1811   1257   -204   -247   -134       C  
ATOM   1258  CD1 ILE A 254       4.107  -9.068  34.156  1.00 15.19           C  
ANISOU 1258  CD1 ILE A 254     2576   1955   1239     93     31   -102       C  
ATOM   1259  N   ILE A 255       2.657  -3.793  36.567  1.00 10.75           N  
ANISOU 1259  N   ILE A 255     1408   1640   1038   -263    249    -41       N  
ATOM   1260  CA  ILE A 255       3.085  -2.763  37.512  1.00 10.92           C  
ANISOU 1260  CA  ILE A 255     1575   1608    967   -317     17    200       C  
ATOM   1261  C   ILE A 255       3.290  -3.403  38.881  1.00 11.75           C  
ANISOU 1261  C   ILE A 255     1707   1684   1073   -553    247    319       C  
ATOM   1262  O   ILE A 255       2.347  -3.919  39.483  1.00 12.12           O  
ANISOU 1262  O   ILE A 255     1951   1559   1096   -601    269    437       O  
ATOM   1263  CB  ILE A 255       2.056  -1.617  37.651  1.00 11.45           C  
ANISOU 1263  CB  ILE A 255     2027   1370    955   -514   -187    323       C  
ATOM   1264  CG1 ILE A 255       1.589  -1.109  36.280  1.00 14.66           C  
ANISOU 1264  CG1 ILE A 255     2472   1785   1312   -802   -116    308       C  
ATOM   1265  CG2 ILE A 255       2.619  -0.484  38.515  1.00  8.76           C  
ANISOU 1265  CG2 ILE A 255     1727    921    681   -398   -162    283       C  
ATOM   1266  CD1 ILE A 255       2.609  -0.268  35.529  1.00 16.40           C  
ANISOU 1266  CD1 ILE A 255     2576   2083   1572  -1021   -443    207       C  
ATOM   1267  N   THR A 256       4.527  -3.373  39.370  1.00 12.11           N  
ANISOU 1267  N   THR A 256     1650   1809   1141   -642    349    383       N  
ATOM   1268  CA  THR A 256       4.821  -3.885  40.704  1.00 13.80           C  
ANISOU 1268  CA  THR A 256     1999   1829   1416   -464    204    174       C  
ATOM   1269  C   THR A 256       5.130  -2.741  41.661  1.00 15.03           C  
ANISOU 1269  C   THR A 256     2230   2045   1437   -337    118    242       C  
ATOM   1270  O   THR A 256       5.795  -1.767  41.294  1.00 16.11           O  
ANISOU 1270  O   THR A 256     2688   2138   1294   -653    193    156       O  
ATOM   1271  CB  THR A 256       5.988  -4.889  40.705  1.00 15.05           C  
ANISOU 1271  CB  THR A 256     2146   1704   1868   -448    273    -47       C  
ATOM   1272  CG2 THR A 256       5.587  -6.188  40.038  1.00 15.29           C  
ANISOU 1272  CG2 THR A 256     2148   1620   2041   -422    243   -280       C  
ATOM   1273  OG1 THR A 256       7.101  -4.332  40.003  1.00 16.48           O  
ANISOU 1273  OG1 THR A 256     2449   1773   2041   -507    356    -43       O  
ATOM   1274  N   LEU A 257       4.620  -2.863  42.879  1.00 14.83           N  
ANISOU 1274  N   LEU A 257     2133   2191   1310    155   -227    190       N  
ATOM   1275  CA  LEU A 257       4.956  -1.964  43.963  1.00 14.17           C  
ANISOU 1275  CA  LEU A 257     1809   2261   1313    332   -240     29       C  
ATOM   1276  C   LEU A 257       6.045  -2.670  44.769  1.00 14.85           C  
ANISOU 1276  C   LEU A 257     1641   2559   1441    279    -38   -124       C  
ATOM   1277  O   LEU A 257       5.913  -3.846  45.113  1.00 15.49           O  
ANISOU 1277  O   LEU A 257     1687   2713   1486    506   -266   -380       O  
ATOM   1278  CB  LEU A 257       3.719  -1.716  44.826  1.00 13.87           C  
ANISOU 1278  CB  LEU A 257     1713   2208   1349    446    -85    150       C  
ATOM   1279  CG  LEU A 257       3.782  -0.598  45.867  1.00 14.62           C  
ANISOU 1279  CG  LEU A 257     1884   2275   1397    199    304    160       C  
ATOM   1280  CD1 LEU A 257       3.908   0.748  45.183  1.00 14.30           C  
ANISOU 1280  CD1 LEU A 257     1896   2160   1378    276    518    399       C  
ATOM   1281  CD2 LEU A 257       2.555  -0.615  46.769  1.00 15.00           C  
ANISOU 1281  CD2 LEU A 257     1851   2374   1476   -208    476    242       C  
ATOM   1282  N   GLU A 258       7.137  -1.973  45.050  1.00 15.85           N  
ANISOU 1282  N   GLU A 258     1761   2830   1431    361    -39    -76       N  
ATOM   1283  CA  GLU A 258       8.238  -2.601  45.767  1.00 16.41           C  
ANISOU 1283  CA  GLU A 258     1637   3081   1518    146     58    171       C  
ATOM   1284  C   GLU A 258       8.813  -1.680  46.835  1.00 17.52           C  
ANISOU 1284  C   GLU A 258     1804   3334   1519    -49    165    292       C  
ATOM   1285  O   GLU A 258       8.687  -0.455  46.739  1.00 19.28           O  
ANISOU 1285  O   GLU A 258     2044   3716   1565   -234     83    257       O  
ATOM   1286  CB  GLU A 258       9.323  -3.061  44.789  1.00 17.23           C  
ANISOU 1286  CB  GLU A 258     1853   3185   1509     20    131    453       C  
ATOM   1287  CG  GLU A 258       9.879  -1.960  43.917  1.00 18.27           C  
ANISOU 1287  CG  GLU A 258     1915   3292   1736    207    361    509       C  
ATOM   1288  CD  GLU A 258      10.949  -2.446  42.964  1.00 19.47           C  
ANISOU 1288  CD  GLU A 258     2210   3359   1830    545    579    362       C  
ATOM   1289  OE1 GLU A 258      10.638  -3.286  42.095  1.00 20.19           O  
ANISOU 1289  OE1 GLU A 258     2340   3372   1961    794    624    299       O  
ATOM   1290  OE2 GLU A 258      12.105  -1.990  43.087  1.00 19.78           O1-
ANISOU 1290  OE2 GLU A 258     2247   3433   1834    477   1048    357       O1-
ATOM   1291  N   ASP A 259       9.431  -2.262  47.859  1.00 16.73           N  
ANISOU 1291  N   ASP A 259     1636   3309   1410   -242    172    423       N  
ATOM   1292  CA  ASP A 259      10.028  -1.444  48.912  1.00 17.83           C  
ANISOU 1292  CA  ASP A 259     1879   3298   1596   -185   -124    378       C  
ATOM   1293  C   ASP A 259      11.401  -0.934  48.482  1.00 18.15           C  
ANISOU 1293  C   ASP A 259     1997   3392   1507    -23   -219    135       C  
ATOM   1294  O   ASP A 259      11.852  -1.234  47.376  1.00 17.16           O  
ANISOU 1294  O   ASP A 259     2027   3362   1131     59   -328   -467       O  
ATOM   1295  CB  ASP A 259      10.074  -2.180  50.266  1.00 18.25           C  
ANISOU 1295  CB  ASP A 259     1996   3161   1778   -119   -428    309       C  
ATOM   1296  CG  ASP A 259      11.057  -3.346  50.292  1.00 19.28           C  
ANISOU 1296  CG  ASP A 259     2308   2993   2025   -160   -469     91       C  
ATOM   1297  OD1 ASP A 259      11.846  -3.529  49.345  1.00 18.42           O  
ANISOU 1297  OD1 ASP A 259     1978   2899   2121     -1   -478    -18       O  
ATOM   1298  OD2 ASP A 259      11.051  -4.082  51.300  1.00 20.80           O1-
ANISOU 1298  OD2 ASP A 259     2611   3021   2270   -359   -314     95       O1-
ATOM   1299  N   SER A 260      12.065  -0.173  49.346  1.00 19.17           N  
ANISOU 1299  N   SER A 260     2094   3512   1677    178   -306    248       N  
ATOM   1300  CA  SER A 260      13.360   0.410  48.999  1.00 20.52           C  
ANISOU 1300  CA  SER A 260     2063   3558   2174    335   -234    220       C  
ATOM   1301  C   SER A 260      14.431  -0.644  48.695  1.00 21.36           C  
ANISOU 1301  C   SER A 260     1969   3613   2533    408     32     11       C  
ATOM   1302  O   SER A 260      15.432  -0.341  48.041  1.00 22.45           O  
ANISOU 1302  O   SER A 260     1979   3661   2891    433    254   -276       O  
ATOM   1303  CB  SER A 260      13.845   1.358  50.100  1.00 20.90           C  
ANISOU 1303  CB  SER A 260     2116   3645   2181    497   -375    398       C  
ATOM   1304  OG  SER A 260      14.022   0.676  51.327  1.00 21.47           O  
ANISOU 1304  OG  SER A 260     2036   3800   2323    494   -275    528       O  
ATOM   1305  N   SER A 261      14.215  -1.871  49.167  1.00 20.60           N  
ANISOU 1305  N   SER A 261     1890   3479   2457    451    -93    207       N  
ATOM   1306  CA  SER A 261      15.138  -2.979  48.913  1.00 20.86           C  
ANISOU 1306  CA  SER A 261     1914   3532   2478    479      3    273       C  
ATOM   1307  C   SER A 261      14.703  -3.831  47.722  1.00 20.07           C  
ANISOU 1307  C   SER A 261     1783   3480   2363    497    290    341       C  
ATOM   1308  O   SER A 261      15.356  -4.817  47.386  1.00 20.16           O  
ANISOU 1308  O   SER A 261     1774   3393   2493    705    248    265       O  
ATOM   1309  CB  SER A 261      15.265  -3.869  50.149  1.00 22.38           C  
ANISOU 1309  CB  SER A 261     2122   3694   2688    636    -54    229       C  
ATOM   1310  OG  SER A 261      15.908  -3.190  51.209  1.00 24.27           O  
ANISOU 1310  OG  SER A 261     2381   3935   2906    622     -3    340       O  
ATOM   1311  N   GLY A 262      13.589  -3.461  47.099  1.00 19.50           N  
ANISOU 1311  N   GLY A 262     1718   3399   2293    291    209    462       N  
ATOM   1312  CA  GLY A 262      13.115  -4.176  45.929  1.00 19.87           C  
ANISOU 1312  CA  GLY A 262     1839   3283   2427    244    243    390       C  
ATOM   1313  C   GLY A 262      12.187  -5.335  46.249  1.00 20.80           C  
ANISOU 1313  C   GLY A 262     2154   3189   2560    352     10    363       C  
ATOM   1314  O   GLY A 262      11.789  -6.076  45.349  1.00 22.15           O  
ANISOU 1314  O   GLY A 262     2475   3244   2698    481    142    236       O  
ATOM   1315  N   ASN A 263      11.839  -5.498  47.523  1.00 19.79           N  
ANISOU 1315  N   ASN A 263     2002   3082   2435    177   -140    593       N  
ATOM   1316  CA  ASN A 263      10.887  -6.533  47.923  1.00 20.11           C  
ANISOU 1316  CA  ASN A 263     1971   3139   2532    448   -413    679       C  
ATOM   1317  C   ASN A 263       9.489  -6.248  47.373  1.00 18.73           C  
ANISOU 1317  C   ASN A 263     1687   2945   2485    393   -422    669       C  
ATOM   1318  O   ASN A 263       9.038  -5.105  47.382  1.00 17.61           O  
ANISOU 1318  O   ASN A 263     1244   2982   2467    485   -361    799       O  
ATOM   1319  CB  ASN A 263      10.817  -6.652  49.450  1.00 20.98           C  
ANISOU 1319  CB  ASN A 263     2103   3209   2659    587   -760    693       C  
ATOM   1320  CG  ASN A 263      12.143  -7.059  50.076  1.00 21.85           C  
ANISOU 1320  CG  ASN A 263     2154   3274   2875    761   -696    616       C  
ATOM   1321  ND2 ASN A 263      12.552  -6.332  51.108  1.00 21.70           N  
ANISOU 1321  ND2 ASN A 263     2183   3336   2725    771   -670    749       N  
ATOM   1322  OD1 ASN A 263      12.790  -8.013  49.639  1.00 22.62           O  
ANISOU 1322  OD1 ASN A 263     2254   3224   3116    945   -769    583       O  
ATOM   1323  N   LEU A 264       8.800  -7.292  46.918  1.00 18.24           N  
ANISOU 1323  N   LEU A 264     1884   2662   2386    295   -362    482       N  
ATOM   1324  CA  LEU A 264       7.451  -7.148  46.360  1.00 18.35           C  
ANISOU 1324  CA  LEU A 264     2352   2340   2281    142   -318    306       C  
ATOM   1325  C   LEU A 264       6.424  -6.715  47.406  1.00 17.43           C  
ANISOU 1325  C   LEU A 264     2253   2243   2127   -103   -208    386       C  
ATOM   1326  O   LEU A 264       6.323  -7.326  48.467  1.00 19.62           O  
ANISOU 1326  O   LEU A 264     2571   2646   2239    -55   -162    174       O  
ATOM   1327  CB  LEU A 264       7.005  -8.468  45.731  1.00 19.25           C  
ANISOU 1327  CB  LEU A 264     2779   2060   2473    192   -213    180       C  
ATOM   1328  CG  LEU A 264       5.599  -8.523  45.144  1.00 20.38           C  
ANISOU 1328  CG  LEU A 264     3078   1982   2685    155    142     57       C  
ATOM   1329  CD1 LEU A 264       5.520  -7.710  43.858  1.00 20.59           C  
ANISOU 1329  CD1 LEU A 264     3270   1883   2669    345    100    -58       C  
ATOM   1330  CD2 LEU A 264       5.201  -9.963  44.889  1.00 21.73           C  
ANISOU 1330  CD2 LEU A 264     3192   2204   2859    -11    334    161       C  
ATOM   1331  N   LEU A 265       5.661  -5.669  47.095  1.00 15.14           N  
ANISOU 1331  N   LEU A 265     1970   1835   1950   -119   -223    585       N  
ATOM   1332  CA  LEU A 265       4.608  -5.169  47.985  1.00 13.63           C  
ANISOU 1332  CA  LEU A 265     1854   1680   1644   -247   -143    552       C  
ATOM   1333  C   LEU A 265       3.221  -5.282  47.352  1.00 14.33           C  
ANISOU 1333  C   LEU A 265     2039   1784   1624   -151     17    625       C  
ATOM   1334  O   LEU A 265       2.212  -5.308  48.055  1.00 15.06           O  
ANISOU 1334  O   LEU A 265     2116   2027   1579   -225    155    587       O  
ATOM   1335  CB  LEU A 265       4.853  -3.705  48.349  1.00 12.79           C  
ANISOU 1335  CB  LEU A 265     1809   1613   1439   -220   -184    431       C  
ATOM   1336  CG  LEU A 265       6.087  -3.297  49.144  1.00 11.90           C  
ANISOU 1336  CG  LEU A 265     1845   1364   1313   -449   -276    395       C  
ATOM   1337  CD1 LEU A 265       6.080  -1.777  49.334  1.00 10.93           C  
ANISOU 1337  CD1 LEU A 265     1715   1127   1312   -513   -113    563       C  
ATOM   1338  CD2 LEU A 265       6.136  -4.011  50.483  1.00 13.04           C  
ANISOU 1338  CD2 LEU A 265     2073   1404   1480   -283    -60    464       C  
ATOM   1339  N   GLY A 266       3.179  -5.317  46.022  1.00 13.04           N  
ANISOU 1339  N   GLY A 266     1876   1622   1457   -157    -47    675       N  
ATOM   1340  CA  GLY A 266       1.930  -5.386  45.285  1.00 12.20           C  
ANISOU 1340  CA  GLY A 266     1557   1619   1458   -151   -180    759       C  
ATOM   1341  C   GLY A 266       2.188  -5.598  43.805  1.00 12.44           C  
ANISOU 1341  C   GLY A 266     1550   1666   1511   -297   -283    920       C  
ATOM   1342  O   GLY A 266       3.288  -5.328  43.328  1.00 13.12           O  
ANISOU 1342  O   GLY A 266     1580   1814   1591   -409   -228    971       O  
ATOM   1343  N   ARG A 267       1.186  -6.101  43.086  1.00 13.22           N  
ANISOU 1343  N   ARG A 267     1742   1806   1474     15   -392    860       N  
ATOM   1344  CA  ARG A 267       1.282  -6.279  41.638  1.00 12.59           C  
ANISOU 1344  CA  ARG A 267     1558   1802   1423   -150   -462    696       C  
ATOM   1345  C   ARG A 267      -0.086  -6.154  40.971  1.00 13.44           C  
ANISOU 1345  C   ARG A 267     1784   1933   1390   -537   -473    609       C  
ATOM   1346  O   ARG A 267      -1.090  -6.657  41.486  1.00 13.77           O  
ANISOU 1346  O   ARG A 267     1769   2013   1449   -929   -393    673       O  
ATOM   1347  CB  ARG A 267       1.890  -7.636  41.283  1.00 12.81           C  
ANISOU 1347  CB  ARG A 267     1633   1629   1606     53   -422    557       C  
ATOM   1348  CG  ARG A 267       2.091  -7.835  39.777  1.00 14.10           C  
ANISOU 1348  CG  ARG A 267     2165   1418   1774    345   -285    521       C  
ATOM   1349  CD  ARG A 267       2.538  -9.251  39.417  1.00 15.59           C  
ANISOU 1349  CD  ARG A 267     2512   1481   1929    419   -140    250       C  
ATOM   1350  NE  ARG A 267       3.774  -9.648  40.089  1.00 16.35           N  
ANISOU 1350  NE  ARG A 267     2684   1421   2106    475    -18     94       N  
ATOM   1351  CZ  ARG A 267       3.844 -10.485  41.123  1.00 17.38           C  
ANISOU 1351  CZ  ARG A 267     2977   1383   2245    541   -193     64       C  
ATOM   1352  NH1 ARG A 267       2.743 -11.025  41.627  1.00 17.48           N1+
ANISOU 1352  NH1 ARG A 267     3114   1325   2203    335   -196     29       N1+
ATOM   1353  NH2 ARG A 267       5.022 -10.780  41.656  1.00 18.06           N  
ANISOU 1353  NH2 ARG A 267     3179   1382   2302    716   -419    279       N  
ATOM   1354  N   ASN A 268      -0.114  -5.459  39.837  1.00 12.62           N  
ANISOU 1354  N   ASN A 268     1648   2075   1072   -450   -478    635       N  
ATOM   1355  CA  ASN A 268      -1.282  -5.412  38.972  1.00 14.68           C  
ANISOU 1355  CA  ASN A 268     2060   2392   1125   -504   -212    333       C  
ATOM   1356  C   ASN A 268      -0.820  -5.408  37.525  1.00 14.60           C  
ANISOU 1356  C   ASN A 268     1953   2467   1126   -523   -314    396       C  
ATOM   1357  O   ASN A 268       0.360  -5.165  37.235  1.00 16.33           O  
ANISOU 1357  O   ASN A 268     2271   2814   1120   -581   -171    552       O  
ATOM   1358  CB  ASN A 268      -2.127  -4.168  39.244  1.00 16.86           C  
ANISOU 1358  CB  ASN A 268     2254   2712   1439   -325    -86    236       C  
ATOM   1359  CG  ASN A 268      -2.997  -4.307  40.474  1.00 20.07           C  
ANISOU 1359  CG  ASN A 268     2669   2955   2002   -323    -14      7       C  
ATOM   1360  ND2 ASN A 268      -2.624  -3.612  41.548  1.00 20.45           N  
ANISOU 1360  ND2 ASN A 268     2961   2844   1967   -149     39   -131       N  
ATOM   1361  OD1 ASN A 268      -4.004  -5.021  40.459  1.00 21.23           O  
ANISOU 1361  OD1 ASN A 268     2537   3191   2341   -364     19   -100       O  
ATOM   1362  N   SER A 269      -1.743  -5.668  36.612  1.00 13.22           N  
ANISOU 1362  N   SER A 269     1741   2110   1171   -360   -502    182       N  
ATOM   1363  CA  SER A 269      -1.397  -5.700  35.200  1.00 12.63           C  
ANISOU 1363  CA  SER A 269     1760   1828   1213     54   -517     78       C  
ATOM   1364  C   SER A 269      -2.581  -5.328  34.311  1.00 11.74           C  
ANISOU 1364  C   SER A 269     1579   1601   1279    183   -284    113       C  
ATOM   1365  O   SER A 269      -3.732  -5.386  34.732  1.00 12.50           O  
ANISOU 1365  O   SER A 269     1544   1774   1431    369   -322    268       O  
ATOM   1366  CB  SER A 269      -0.859  -7.074  34.817  1.00 13.12           C  
ANISOU 1366  CB  SER A 269     2005   1681   1300    146   -411   -102       C  
ATOM   1367  OG  SER A 269      -1.827  -8.075  35.045  1.00 14.48           O  
ANISOU 1367  OG  SER A 269     2491   1602   1407    336   -234   -257       O  
ATOM   1368  N   PHE A 270      -2.274  -4.937  33.081  1.00 10.42           N  
ANISOU 1368  N   PHE A 270     1389   1445   1126    175    -26   -236       N  
ATOM   1369  CA  PHE A 270      -3.283  -4.616  32.083  1.00  9.97           C  
ANISOU 1369  CA  PHE A 270     1501   1228   1057    -71    177   -202       C  
ATOM   1370  C   PHE A 270      -2.714  -4.878  30.687  1.00 11.61           C  
ANISOU 1370  C   PHE A 270     1733   1468   1209   -172     37   -297       C  
ATOM   1371  O   PHE A 270      -1.503  -4.764  30.459  1.00 11.88           O  
ANISOU 1371  O   PHE A 270     1595   1636   1282   -193    161   -485       O  
ATOM   1372  CB  PHE A 270      -3.792  -3.171  32.241  1.00  9.26           C  
ANISOU 1372  CB  PHE A 270     1442   1050   1027    -77     -3      7       C  
ATOM   1373  CG  PHE A 270      -2.713  -2.117  32.142  1.00  9.80           C  
ANISOU 1373  CG  PHE A 270     1476   1070   1178     32    141      0       C  
ATOM   1374  CD1 PHE A 270      -2.037  -1.691  33.275  1.00 11.04           C  
ANISOU 1374  CD1 PHE A 270     1652   1186   1355    -78    227   -249       C  
ATOM   1375  CD2 PHE A 270      -2.391  -1.538  30.914  1.00  9.77           C  
ANISOU 1375  CD2 PHE A 270     1341   1107   1264    124    292    126       C  
ATOM   1376  CE1 PHE A 270      -1.050  -0.727  33.189  1.00 11.34           C  
ANISOU 1376  CE1 PHE A 270     1780   1124   1407   -112    237   -421       C  
ATOM   1377  CE2 PHE A 270      -1.409  -0.571  30.828  1.00 10.75           C  
ANISOU 1377  CE2 PHE A 270     1647   1084   1355     37    217    -86       C  
ATOM   1378  CZ  PHE A 270      -0.740  -0.163  31.968  1.00 11.04           C  
ANISOU 1378  CZ  PHE A 270     1566   1238   1390   -161    340   -234       C  
ATOM   1379  N   GLU A 271      -3.579  -5.270  29.762  1.00 11.90           N  
ANISOU 1379  N   GLU A 271     1700   1539   1284    -27   -316   -177       N  
ATOM   1380  CA  GLU A 271      -3.131  -5.494  28.397  1.00 12.90           C  
ANISOU 1380  CA  GLU A 271     1865   1757   1280     59   -380   -292       C  
ATOM   1381  C   GLU A 271      -2.977  -4.131  27.723  1.00 13.22           C  
ANISOU 1381  C   GLU A 271     1918   1858   1248     -8   -359   -155       C  
ATOM   1382  O   GLU A 271      -3.613  -3.162  28.128  1.00 13.39           O  
ANISOU 1382  O   GLU A 271     1961   2010   1116    -33   -406    -50       O  
ATOM   1383  CB  GLU A 271      -4.124  -6.380  27.644  1.00 14.48           C  
ANISOU 1383  CB  GLU A 271     1965   1913   1623    -20   -430   -460       C  
ATOM   1384  CG  GLU A 271      -3.642  -6.836  26.278  1.00 17.41           C  
ANISOU 1384  CG  GLU A 271     2274   2236   2104    -32   -757   -583       C  
ATOM   1385  CD  GLU A 271      -4.662  -7.700  25.577  1.00 20.53           C  
ANISOU 1385  CD  GLU A 271     2638   2616   2545    -49   -591   -658       C  
ATOM   1386  OE1 GLU A 271      -5.553  -8.226  26.281  1.00 21.94           O  
ANISOU 1386  OE1 GLU A 271     2562   2973   2803   -201   -374   -688       O  
ATOM   1387  OE2 GLU A 271      -4.578  -7.849  24.332  1.00 21.71           O1-
ANISOU 1387  OE2 GLU A 271     2960   2679   2610    116   -702   -792       O1-
ATOM   1388  N   VAL A 272      -2.101  -4.038  26.728  1.00 14.70           N  
ANISOU 1388  N   VAL A 272     2152   1955   1479      6   -263    -40       N  
ATOM   1389  CA  VAL A 272      -1.923  -2.787  25.997  1.00 14.48           C  
ANISOU 1389  CA  VAL A 272     2099   1985   1420   -162   -132   -199       C  
ATOM   1390  C   VAL A 272      -1.908  -3.026  24.492  1.00 14.62           C  
ANISOU 1390  C   VAL A 272     1997   2032   1526   -194    225   -278       C  
ATOM   1391  O   VAL A 272      -1.292  -3.975  24.008  1.00 14.31           O  
ANISOU 1391  O   VAL A 272     2006   1858   1574    -84    656   -440       O  
ATOM   1392  CB  VAL A 272      -0.615  -2.059  26.391  1.00 14.46           C  
ANISOU 1392  CB  VAL A 272     2022   2051   1422   -396   -464   -427       C  
ATOM   1393  CG1 VAL A 272      -0.570  -0.659  25.782  1.00 14.81           C  
ANISOU 1393  CG1 VAL A 272     1962   2254   1412   -393   -531   -490       C  
ATOM   1394  CG2 VAL A 272      -0.485  -1.975  27.882  1.00 14.95           C  
ANISOU 1394  CG2 VAL A 272     1990   2108   1582   -530   -671   -591       C  
ATOM   1395  N   ARG A 273      -2.612  -2.163  23.769  1.00 12.40           N  
ANISOU 1395  N   ARG A 273     1579   1902   1230     57    -52    -95       N  
ATOM   1396  CA  ARG A 273      -2.477  -2.056  22.328  1.00 13.60           C  
ANISOU 1396  CA  ARG A 273     1674   2145   1349    360     74   -267       C  
ATOM   1397  C   ARG A 273      -2.061  -0.629  22.014  1.00 12.87           C  
ANISOU 1397  C   ARG A 273     1558   2073   1260    451    335    -32       C  
ATOM   1398  O   ARG A 273      -2.763   0.319  22.372  1.00 13.10           O  
ANISOU 1398  O   ARG A 273     1841   1770   1368    512    649    145       O  
ATOM   1399  CB  ARG A 273      -3.805  -2.379  21.641  1.00 15.08           C  
ANISOU 1399  CB  ARG A 273     1962   2405   1365    463    -42   -471       C  
ATOM   1400  CG  ARG A 273      -3.842  -2.088  20.153  1.00 16.54           C  
ANISOU 1400  CG  ARG A 273     2135   2678   1471    551    -15   -386       C  
ATOM   1401  CD  ARG A 273      -5.188  -2.486  19.551  1.00 18.61           C  
ANISOU 1401  CD  ARG A 273     2477   3011   1584    575    -84   -486       C  
ATOM   1402  NE  ARG A 273      -5.294  -2.118  18.143  1.00 22.74           N  
ANISOU 1402  NE  ARG A 273     3075   3460   2104    687    -85   -509       N  
ATOM   1403  CZ  ARG A 273      -4.757  -2.821  17.153  1.00 26.15           C  
ANISOU 1403  CZ  ARG A 273     3593   3780   2562    788   -360   -611       C  
ATOM   1404  NH1 ARG A 273      -4.070  -3.919  17.430  1.00 28.14           N1+
ANISOU 1404  NH1 ARG A 273     4081   3938   2674    674   -578   -829       N1+
ATOM   1405  NH2 ARG A 273      -4.892  -2.427  15.891  1.00 27.24           N  
ANISOU 1405  NH2 ARG A 273     3479   4061   2812    738   -329   -526       N  
ATOM   1406  N   VAL A 274      -0.911  -0.467  21.372  1.00 13.18           N  
ANISOU 1406  N   VAL A 274     1403   2398   1205    467     82   -112       N  
ATOM   1407  CA  VAL A 274      -0.481   0.853  20.930  1.00 13.86           C  
ANISOU 1407  CA  VAL A 274     1448   2785   1033    223      1    -66       C  
ATOM   1408  C   VAL A 274      -0.872   0.997  19.457  1.00 14.80           C  
ANISOU 1408  C   VAL A 274     1494   2986   1141    -32   -373      4       C  
ATOM   1409  O   VAL A 274      -0.404   0.243  18.608  1.00 14.01           O  
ANISOU 1409  O   VAL A 274     1434   2930    958   -145   -391      2       O  
ATOM   1410  CB  VAL A 274       1.033   1.068  21.123  1.00 15.31           C  
ANISOU 1410  CB  VAL A 274     1831   2907   1079    210   -157   -297       C  
ATOM   1411  CG1 VAL A 274       1.386   2.534  20.916  1.00 16.22           C  
ANISOU 1411  CG1 VAL A 274     2061   2963   1138    366   -332   -473       C  
ATOM   1412  CG2 VAL A 274       1.459   0.620  22.514  1.00 14.53           C  
ANISOU 1412  CG2 VAL A 274     1735   2884    902    246    290   -324       C  
ATOM   1413  N   CYS A 275      -1.750   1.955  19.170  1.00 16.65           N  
ANISOU 1413  N   CYS A 275     1662   3215   1451    -76   -385     32       N  
ATOM   1414  CA  CYS A 275      -2.357   2.077  17.843  1.00 17.77           C  
ANISOU 1414  CA  CYS A 275     1773   3488   1491     85   -182   -121       C  
ATOM   1415  C   CYS A 275      -2.660   3.521  17.443  1.00 18.63           C  
ANISOU 1415  C   CYS A 275     1962   3641   1474    173     49      4       C  
ATOM   1416  O   CYS A 275      -2.639   4.431  18.277  1.00 18.80           O  
ANISOU 1416  O   CYS A 275     1959   3679   1505    217    156    125       O  
ATOM   1417  CB  CYS A 275      -3.640   1.236  17.768  1.00 18.52           C  
ANISOU 1417  CB  CYS A 275     1711   3722   1605    142   -195   -258       C  
ATOM   1418  SG  CYS A 275      -4.845   1.570  19.090  1.00 19.87           S  
ANISOU 1418  SG  CYS A 275     1564   4066   1918    393     23   -351       S  
ATOM   1419  N   ALA A 276      -2.967   3.717  16.165  1.00 18.85           N  
ANISOU 1419  N   ALA A 276     2073   3687   1400    438    386    123       N  
ATOM   1420  CA  ALA A 276      -3.265   5.044  15.651  1.00 19.67           C  
ANISOU 1420  CA  ALA A 276     2131   3890   1452    487    337    212       C  
ATOM   1421  C   ALA A 276      -4.619   5.581  16.110  1.00 20.33           C  
ANISOU 1421  C   ALA A 276     2100   4066   1560    135    154    357       C  
ATOM   1422  O   ALA A 276      -4.762   6.782  16.329  1.00 20.75           O  
ANISOU 1422  O   ALA A 276     2268   4074   1541     -5    155    389       O  
ATOM   1423  CB  ALA A 276      -3.188   5.057  14.135  1.00 20.08           C  
ANISOU 1423  CB  ALA A 276     2203   3981   1447    688    361    132       C  
ATOM   1424  N   CYS A 277      -5.614   4.704  16.248  1.00 19.70           N  
ANISOU 1424  N   CYS A 277     1706   4037   1742    -60   -220    456       N  
ATOM   1425  CA ACYS A 277      -6.962   5.124  16.630  0.58 20.37           C  
ANISOU 1425  CA ACYS A 277     1791   4097   1851   -129   -390    506       C  
ATOM   1426  CA BCYS A 277      -6.951   5.145  16.648  0.42 19.97           C  
ANISOU 1426  CA BCYS A 277     1633   4012   1941     50   -350    462       C  
ATOM   1427  C   CYS A 277      -7.492   4.355  17.834  1.00 18.73           C  
ANISOU 1427  C   CYS A 277     1540   3843   1732    -36   -324    282       C  
ATOM   1428  O   CYS A 277      -8.309   3.453  17.668  1.00 19.96           O  
ANISOU 1428  O   CYS A 277     1726   4142   1716   -103   -388     55       O  
ATOM   1429  CB ACYS A 277      -7.924   4.920  15.459  0.58 22.18           C  
ANISOU 1429  CB ACYS A 277     2006   4417   2005   -299   -611    708       C  
ATOM   1430  CB BCYS A 277      -7.927   5.071  15.472  0.42 21.13           C  
ANISOU 1430  CB BCYS A 277     1567   4169   2294    235   -502    602       C  
ATOM   1431  SG ACYS A 277      -7.480   5.799  13.951  0.58 24.38           S  
ANISOU 1431  SG ACYS A 277     2401   4709   2153   -385   -942    838       S  
ATOM   1432  SG BCYS A 277      -9.330   6.205  15.626  0.42 22.61           S  
ANISOU 1432  SG BCYS A 277     1709   4251   2632    452   -733    690       S  
ATOM   1433  N   PRO A 278      -7.030   4.702  19.045  1.00 15.56           N  
ANISOU 1433  N   PRO A 278     1182   3230   1499     96   -392     13       N  
ATOM   1434  CA  PRO A 278      -7.443   4.004  20.270  1.00 15.16           C  
ANISOU 1434  CA  PRO A 278     1194   3046   1521   -133   -314    -60       C  
ATOM   1435  C   PRO A 278      -8.961   3.888  20.454  1.00 15.49           C  
ANISOU 1435  C   PRO A 278     1395   2875   1615     76   -512   -284       C  
ATOM   1436  O   PRO A 278      -9.438   2.821  20.841  1.00 14.45           O  
ANISOU 1436  O   PRO A 278     1560   2404   1528    -24   -375   -279       O  
ATOM   1437  CB  PRO A 278      -6.873   4.887  21.378  1.00 14.57           C  
ANISOU 1437  CB  PRO A 278     1224   2940   1371   -504   -421   -119       C  
ATOM   1438  CG  PRO A 278      -5.667   5.502  20.779  1.00 15.20           C  
ANISOU 1438  CG  PRO A 278     1332   3013   1432   -375   -443    -45       C  
ATOM   1439  CD  PRO A 278      -6.031   5.748  19.323  1.00 14.64           C  
ANISOU 1439  CD  PRO A 278     1295   2980   1286    -23   -539    139       C  
ATOM   1440  N   GLY A 279      -9.700   4.967  20.202  1.00 15.65           N  
ANISOU 1440  N   GLY A 279     1358   3007   1581    364   -640   -427       N  
ATOM   1441  CA  GLY A 279     -11.140   4.955  20.384  1.00 16.28           C  
ANISOU 1441  CA  GLY A 279     1452   3303   1430    502   -499   -555       C  
ATOM   1442  C   GLY A 279     -11.824   3.972  19.452  1.00 16.85           C  
ANISOU 1442  C   GLY A 279     1577   3458   1369    588   -328   -532       C  
ATOM   1443  O   GLY A 279     -12.644   3.159  19.885  1.00 16.44           O  
ANISOU 1443  O   GLY A 279     1594   3398   1254    698    124   -522       O  
ATOM   1444  N   ARG A 280     -11.479   4.050  18.170  1.00 18.21           N  
ANISOU 1444  N   ARG A 280     1983   3678   1259    303   -510   -477       N  
ATOM   1445  CA  ARG A 280     -12.016   3.143  17.159  1.00 20.38           C  
ANISOU 1445  CA  ARG A 280     2552   3936   1254    216   -584   -343       C  
ATOM   1446  C   ARG A 280     -11.687   1.694  17.482  1.00 17.87           C  
ANISOU 1446  C   ARG A 280     2163   3531   1097    116   -466   -309       C  
ATOM   1447  O   ARG A 280     -12.556   0.827  17.442  1.00 16.90           O  
ANISOU 1447  O   ARG A 280     1963   3319   1139     15   -508   -389       O  
ATOM   1448  CB  ARG A 280     -11.447   3.493  15.782  1.00 24.96           C  
ANISOU 1448  CB  ARG A 280     3574   4469   1441     65   -527   -312       C  
ATOM   1449  CG  ARG A 280     -11.977   2.647  14.634  1.00 30.17           C  
ANISOU 1449  CG  ARG A 280     4593   5002   1867    -31   -269   -258       C  
ATOM   1450  CD  ARG A 280     -11.176   2.893  13.355  1.00 35.68           C  
ANISOU 1450  CD  ARG A 280     5475   5521   2562    -41   -161   -313       C  
ATOM   1451  NE  ARG A 280      -9.785   2.467  13.510  1.00 40.21           N  
ANISOU 1451  NE  ARG A 280     6265   5929   3083     69   -182   -328       N  
ATOM   1452  CZ  ARG A 280      -9.335   1.256  13.195  1.00 42.79           C  
ANISOU 1452  CZ  ARG A 280     6688   6211   3360    186   -396   -225       C  
ATOM   1453  NH1 ARG A 280     -10.166   0.345  12.703  1.00 43.94           N1+
ANISOU 1453  NH1 ARG A 280     6928   6293   3474    219   -415   -157       N1+
ATOM   1454  NH2 ARG A 280      -8.055   0.953  13.371  1.00 43.05           N  
ANISOU 1454  NH2 ARG A 280     6655   6340   3362    208   -610   -135       N  
ATOM   1455  N   ASP A 281     -10.423   1.437  17.804  1.00 17.42           N  
ANISOU 1455  N   ASP A 281     2208   3445    966    252   -161   -403       N  
ATOM   1456  CA  ASP A 281      -9.980   0.074  18.060  1.00 17.06           C  
ANISOU 1456  CA  ASP A 281     2150   3306   1025    342   -293   -500       C  
ATOM   1457  C   ASP A 281     -10.618  -0.524  19.309  1.00 17.04           C  
ANISOU 1457  C   ASP A 281     2155   2860   1458    -40   -326   -643       C  
ATOM   1458  O   ASP A 281     -10.977  -1.696  19.305  1.00 19.47           O  
ANISOU 1458  O   ASP A 281     2512   3043   1843   -124   -431   -970       O  
ATOM   1459  CB  ASP A 281      -8.451  -0.013  18.108  1.00 18.77           C  
ANISOU 1459  CB  ASP A 281     2217   3735   1181    584   -361   -364       C  
ATOM   1460  CG  ASP A 281      -7.820   0.053  16.724  1.00 20.79           C  
ANISOU 1460  CG  ASP A 281     2257   4053   1588    650   -633   -276       C  
ATOM   1461  OD1 ASP A 281      -8.573   0.074  15.726  1.00 21.07           O  
ANISOU 1461  OD1 ASP A 281     2225   4052   1730    944   -672     91       O  
ATOM   1462  OD2 ASP A 281      -6.573   0.071  16.633  1.00 22.05           O1-
ANISOU 1462  OD2 ASP A 281     2337   4211   1832    519   -727   -398       O1-
ATOM   1463  N   ARG A 282     -10.770   0.278  20.365  1.00 14.51           N  
ANISOU 1463  N   ARG A 282     1847   2533   1132    -22   -208   -446       N  
ATOM   1464  CA  ARG A 282     -11.460  -0.175  21.568  1.00 12.51           C  
ANISOU 1464  CA  ARG A 282     1510   2174   1068     25     68   -628       C  
ATOM   1465  C   ARG A 282     -12.905  -0.535  21.271  1.00 15.05           C  
ANISOU 1465  C   ARG A 282     1787   2566   1367    236   -222   -482       C  
ATOM   1466  O   ARG A 282     -13.371  -1.620  21.628  1.00 15.66           O  
ANISOU 1466  O   ARG A 282     1813   2748   1390    269   -662   -423       O  
ATOM   1467  CB  ARG A 282     -11.421   0.886  22.670  1.00 10.42           C  
ANISOU 1467  CB  ARG A 282     1340   1747    871    -30    414   -466       C  
ATOM   1468  CG  ARG A 282     -12.297   0.514  23.864  1.00 10.64           C  
ANISOU 1468  CG  ARG A 282     1407   1727    908   -162    604   -175       C  
ATOM   1469  CD  ARG A 282     -12.218   1.503  25.022  1.00 11.86           C  
ANISOU 1469  CD  ARG A 282     1546   1866   1094   -298    298   -203       C  
ATOM   1470  NE  ARG A 282     -13.291   1.239  25.981  1.00 11.86           N  
ANISOU 1470  NE  ARG A 282     1548   1981    978    -53     48   -302       N  
ATOM   1471  CZ  ARG A 282     -13.740   2.099  26.889  1.00 11.09           C  
ANISOU 1471  CZ  ARG A 282     1281   1928   1007    193     78   -369       C  
ATOM   1472  NH1 ARG A 282     -13.200   3.301  26.999  1.00 11.53           N1+
ANISOU 1472  NH1 ARG A 282     1186   1832   1363    392   -207   -521       N1+
ATOM   1473  NH2 ARG A 282     -14.731   1.742  27.692  1.00 11.69           N  
ANISOU 1473  NH2 ARG A 282     1319   2093   1028    214    322   -231       N  
ATOM   1474  N   ARG A 283     -13.612   0.378  20.615  1.00 15.95           N  
ANISOU 1474  N   ARG A 283     1857   2701   1504    162   -289   -267       N  
ATOM   1475  CA  ARG A 283     -15.024   0.170  20.295  1.00 16.61           C  
ANISOU 1475  CA  ARG A 283     1581   3036   1695    -84    -77   -121       C  
ATOM   1476  C   ARG A 283     -15.195  -1.093  19.454  1.00 18.56           C  
ANISOU 1476  C   ARG A 283     1828   3328   1898   -316    194   -123       C  
ATOM   1477  O   ARG A 283     -16.113  -1.882  19.683  1.00 19.49           O  
ANISOU 1477  O   ARG A 283     2138   3366   1900   -264    330    304       O  
ATOM   1478  CB  ARG A 283     -15.608   1.396  19.569  1.00 16.74           C  
ANISOU 1478  CB  ARG A 283     1456   3184   1722     28    -30    110       C  
ATOM   1479  CG  ARG A 283     -17.138   1.469  19.578  1.00 17.23           C  
ANISOU 1479  CG  ARG A 283     1739   3208   1598     64    -55    165       C  
ATOM   1480  CD  ARG A 283     -17.677   2.660  18.789  1.00 16.22           C  
ANISOU 1480  CD  ARG A 283     1807   3020   1335     17   -377    199       C  
ATOM   1481  NE  ARG A 283     -17.271   3.954  19.343  1.00 15.50           N  
ANISOU 1481  NE  ARG A 283     1837   2934   1117   -159   -610    111       N  
ATOM   1482  CZ  ARG A 283     -17.642   5.133  18.845  1.00 14.79           C  
ANISOU 1482  CZ  ARG A 283     1748   2709   1162   -147   -505    -17       C  
ATOM   1483  NH1 ARG A 283     -18.431   5.184  17.787  1.00 14.21           N1+
ANISOU 1483  NH1 ARG A 283     1784   2541   1073   -199   -682     23       N1+
ATOM   1484  NH2 ARG A 283     -17.226   6.261  19.404  1.00 15.08           N  
ANISOU 1484  NH2 ARG A 283     1815   2710   1203   -135     -7     82       N  
ATOM   1485  N   THR A 284     -14.289  -1.295  18.498  1.00 19.56           N  
ANISOU 1485  N   THR A 284     2006   3446   1981   -615     70   -461       N  
ATOM   1486  CA  THR A 284     -14.337  -2.474  17.637  1.00 19.92           C  
ANISOU 1486  CA  THR A 284     2193   3414   1963   -673     71   -784       C  
ATOM   1487  C   THR A 284     -14.079  -3.769  18.413  1.00 20.25           C  
ANISOU 1487  C   THR A 284     2085   3351   2258   -527    -35  -1334       C  
ATOM   1488  O   THR A 284     -14.770  -4.764  18.211  1.00 20.44           O  
ANISOU 1488  O   THR A 284     2205   3179   2383   -532   -135  -1467       O  
ATOM   1489  CB  THR A 284     -13.357  -2.349  16.443  1.00 21.83           C  
ANISOU 1489  CB  THR A 284     2778   3484   2032   -945   -189   -516       C  
ATOM   1490  CG2 THR A 284     -13.271  -3.649  15.673  1.00 22.16           C  
ANISOU 1490  CG2 THR A 284     2971   3469   1981   -973    -86   -570       C  
ATOM   1491  OG1 THR A 284     -13.816  -1.321  15.559  1.00 22.23           O  
ANISOU 1491  OG1 THR A 284     2956   3518   1972  -1250   -354   -158       O  
ATOM   1492  N   GLU A 285     -13.099  -3.755  19.309  1.00 22.05           N  
ANISOU 1492  N   GLU A 285     2340   3613   2425   -436   -150  -1476       N  
ATOM   1493  CA  GLU A 285     -12.741  -4.966  20.040  1.00 24.58           C  
ANISOU 1493  CA  GLU A 285     2703   3939   2699   -436   -284  -1430       C  
ATOM   1494  C   GLU A 285     -13.829  -5.356  21.026  1.00 27.00           C  
ANISOU 1494  C   GLU A 285     3030   4100   3129   -378   -745  -1312       C  
ATOM   1495  O   GLU A 285     -14.027  -6.533  21.311  1.00 29.71           O  
ANISOU 1495  O   GLU A 285     3548   4239   3502   -344   -733  -1214       O  
ATOM   1496  CB  GLU A 285     -11.391  -4.810  20.750  1.00 25.66           C  
ANISOU 1496  CB  GLU A 285     2807   4220   2724   -283   -267  -1664       C  
ATOM   1497  CG  GLU A 285     -10.203  -4.720  19.802  1.00 28.06           C  
ANISOU 1497  CG  GLU A 285     3100   4565   2997     13   -405  -1808       C  
ATOM   1498  CD  GLU A 285      -8.873  -5.034  20.468  1.00 30.01           C  
ANISOU 1498  CD  GLU A 285     3376   4883   3143     47   -202  -1886       C  
ATOM   1499  OE1 GLU A 285      -7.828  -4.866  19.796  1.00 30.85           O  
ANISOU 1499  OE1 GLU A 285     3334   4925   3462    -67    -89  -1865       O  
ATOM   1500  OE2 GLU A 285      -8.869  -5.462  21.646  1.00 29.28           O1-
ANISOU 1500  OE2 GLU A 285     3483   4998   2646    209   -225  -1957       O1-
ATOM   1501  N   GLU A 286     -14.539  -4.360  21.541  1.00 26.23           N  
ANISOU 1501  N   GLU A 286     2730   4181   3055   -400  -1168  -1174       N  
ATOM   1502  CA  GLU A 286     -15.633  -4.609  22.470  1.00 25.85           C  
ANISOU 1502  CA  GLU A 286     2540   4261   3020   -826  -1023   -961       C  
ATOM   1503  C   GLU A 286     -16.905  -5.073  21.751  1.00 30.48           C  
ANISOU 1503  C   GLU A 286     3238   4792   3552  -1083   -807  -1017       C  
ATOM   1504  O   GLU A 286     -17.810  -5.634  22.373  1.00 31.19           O  
ANISOU 1504  O   GLU A 286     3327   4894   3629  -1175   -798  -1010       O  
ATOM   1505  CB  GLU A 286     -15.904  -3.362  23.319  1.00 22.80           C  
ANISOU 1505  CB  GLU A 286     2120   3846   2696   -770   -746   -763       C  
ATOM   1506  CG  GLU A 286     -14.726  -2.972  24.214  1.00 21.36           C  
ANISOU 1506  CG  GLU A 286     1981   3565   2569   -622   -535   -554       C  
ATOM   1507  CD  GLU A 286     -14.976  -1.696  24.993  1.00 20.04           C  
ANISOU 1507  CD  GLU A 286     1653   3386   2574   -496   -427   -145       C  
ATOM   1508  OE1 GLU A 286     -15.903  -0.944  24.629  1.00 20.42           O  
ANISOU 1508  OE1 GLU A 286     1591   3494   2674   -303    -72      2       O  
ATOM   1509  OE2 GLU A 286     -14.248  -1.443  25.974  1.00 18.48           O1-
ANISOU 1509  OE2 GLU A 286     1448   3155   2421   -334   -554     19       O1-
ATOM   1510  N   GLU A 287     -16.965  -4.843  20.443  1.00 33.64           N  
ANISOU 1510  N   GLU A 287     3697   5210   3875  -1211   -695  -1098       N  
ATOM   1511  CA  GLU A 287     -18.087  -5.296  19.624  1.00 37.55           C  
ANISOU 1511  CA  GLU A 287     4198   5685   4384  -1123   -669  -1049       C  
ATOM   1512  C   GLU A 287     -18.248  -6.815  19.715  1.00 39.41           C  
ANISOU 1512  C   GLU A 287     4633   5584   4756  -1110   -364  -1130       C  
ATOM   1513  O   GLU A 287     -19.353  -7.341  19.593  1.00 39.97           O  
ANISOU 1513  O   GLU A 287     4692   5627   4869  -1006   -309  -1145       O  
ATOM   1514  CB  GLU A 287     -17.860  -4.874  18.171  1.00 40.27           C  
ANISOU 1514  CB  GLU A 287     4422   6258   4623  -1069   -815   -974       C  
ATOM   1515  CG  GLU A 287     -19.116  -4.552  17.382  1.00 43.73           C  
ANISOU 1515  CG  GLU A 287     4862   6826   4929  -1076   -778   -980       C  
ATOM   1516  CD  GLU A 287     -18.816  -3.769  16.110  1.00 46.25           C  
ANISOU 1516  CD  GLU A 287     5074   7285   5212  -1119   -835  -1121       C  
ATOM   1517  OE1 GLU A 287     -17.642  -3.383  15.908  1.00 46.66           O  
ANISOU 1517  OE1 GLU A 287     4997   7426   5306  -1288   -979  -1141       O  
ATOM   1518  OE2 GLU A 287     -19.752  -3.537  15.312  1.00 47.32           O1-
ANISOU 1518  OE2 GLU A 287     5197   7449   5332   -938   -687  -1182       O1-
ATOM   1519  N   ASN A 288     -17.139  -7.514  19.944  1.00 41.43           N  
ANISOU 1519  N   ASN A 288     5198   5502   5042  -1188     -4  -1137       N  
ATOM   1520  CA  ASN A 288     -17.136  -8.976  20.024  1.00 43.35           C  
ANISOU 1520  CA  ASN A 288     5579   5509   5382  -1210    246  -1191       C  
ATOM   1521  C   ASN A 288     -17.746  -9.543  21.311  1.00 42.05           C  
ANISOU 1521  C   ASN A 288     5437   5177   5363  -1373    445  -1176       C  
ATOM   1522  O   ASN A 288     -17.948 -10.754  21.426  1.00 41.76           O  
ANISOU 1522  O   ASN A 288     5431   4974   5460  -1272    420  -1180       O  
ATOM   1523  CB  ASN A 288     -15.712  -9.520  19.859  1.00 46.10           C  
ANISOU 1523  CB  ASN A 288     5981   5773   5762  -1098    119  -1258       C  
ATOM   1524  CG  ASN A 288     -15.091  -9.148  18.521  1.00 48.55           C  
ANISOU 1524  CG  ASN A 288     6299   5978   6169  -1011   -168  -1418       C  
ATOM   1525  ND2 ASN A 288     -15.665  -9.662  17.432  1.00 49.14           N  
ANISOU 1525  ND2 ASN A 288     6400   6011   6261  -1098   -289  -1525       N  
ATOM   1526  OD1 ASN A 288     -14.097  -8.418  18.467  1.00 49.22           O  
ANISOU 1526  OD1 ASN A 288     6366   6013   6321   -909   -358  -1474       O  
ATOM   1527  N   LEU A 289     -18.032  -8.670  22.274  1.00 40.10           N  
ANISOU 1527  N   LEU A 289     5193   4923   5119  -1593    646  -1204       N  
ATOM   1528  CA  LEU A 289     -18.534  -9.100  23.577  1.00 38.19           C  
ANISOU 1528  CA  LEU A 289     4938   4667   4906  -1730    766  -1121       C  
ATOM   1529  C   LEU A 289     -20.055  -9.288  23.585  1.00 38.37           C  
ANISOU 1529  C   LEU A 289     5089   4552   4938  -1921    799   -974       C  
ATOM   1530  O   LEU A 289     -20.752  -8.955  22.623  1.00 37.52           O  
ANISOU 1530  O   LEU A 289     5222   4392   4642  -1922    607  -1099       O  
ATOM   1531  CB  LEU A 289     -18.105  -8.108  24.665  1.00 35.81           C  
ANISOU 1531  CB  LEU A 289     4494   4463   4650  -1756    753  -1109       C  
ATOM   1532  CG  LEU A 289     -16.603  -7.825  24.760  1.00 34.32           C  
ANISOU 1532  CG  LEU A 289     4235   4283   4523  -1841    820  -1157       C  
ATOM   1533  CD1 LEU A 289     -16.289  -6.803  25.843  1.00 33.54           C  
ANISOU 1533  CD1 LEU A 289     4081   4265   4399  -1747    891  -1267       C  
ATOM   1534  CD2 LEU A 289     -15.824  -9.112  24.998  1.00 33.88           C  
ANISOU 1534  CD2 LEU A 289     4128   4233   4510  -1841    865  -1127       C  
TER    1535      LEU A 289 
HETATM 1536 ZN    ZN A 401       8.654   0.295  16.522  1.00 15.70          ZN  
CONECT  638 1536
CONECT  663 1536
CONECT 1140 1536
CONECT 1166 1536
CONECT 1536  638  663 1140 1166
END



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