CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***    ***

elNémo ID: 22062900114366549

Job options:

ID        	=	 22062900114366549
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   GLN A  28       1.149 -35.955   2.653  1.00 47.23           N  
ANISOU    1  N   GLN A  28     6386   5910   5648   -219   1248    -27       N  
ATOM      2  CA  GLN A  28       2.526 -35.900   2.158  1.00 47.18           C  
ANISOU    2  CA  GLN A  28     6352   5928   5647   -261   1237    -93       C  
ATOM      3  C   GLN A  28       2.623 -36.529   0.763  1.00 45.52           C  
ANISOU    3  C   GLN A  28     6085   5742   5467   -215   1202    -96       C  
ATOM      4  O   GLN A  28       1.859 -37.447   0.458  1.00 46.47           O  
ANISOU    4  O   GLN A  28     6165   5878   5613   -162   1144    -58       O  
ATOM      5  CB  GLN A  28       3.466 -36.622   3.139  1.00 50.30           C  
ANISOU    5  CB  GLN A  28     6708   6353   6052   -311   1156   -137       C  
ATOM      6  CG  GLN A  28       4.927 -36.186   3.008  1.00 56.46           C  
ANISOU    6  CG  GLN A  28     7474   7149   6830   -374   1168   -215       C  
ATOM      7  CD  GLN A  28       5.898 -37.125   3.690  1.00 62.77           C  
ANISOU    7  CD  GLN A  28     8214   7990   7648   -405   1067   -261       C  
ATOM      8  NE2 GLN A  28       7.156 -36.708   3.768  1.00 63.89           N  
ANISOU    8  NE2 GLN A  28     8342   8146   7789   -466   1075   -333       N  
ATOM      9  OE1 GLN A  28       5.545 -38.227   4.141  1.00 64.50           O  
ANISOU    9  OE1 GLN A  28     8398   8227   7882   -375    982   -236       O  
ATOM     10  N   THR A  29       3.542 -36.037  -0.090  1.00 42.97           N  
ANISOU   10  N   THR A  29     5763   5420   5142   -236   1242   -141       N  
ATOM     11  CA  THR A  29       3.700 -36.598  -1.432  1.00 40.74           C  
ANISOU   11  CA  THR A  29     5438   5157   4886   -194   1214   -146       C  
ATOM     12  C   THR A  29       4.342 -37.990  -1.355  1.00 37.29           C  
ANISOU   12  C   THR A  29     4913   4766   4489   -200   1102   -173       C  
ATOM     13  O   THR A  29       5.326 -38.177  -0.652  1.00 38.27           O  
ANISOU   13  O   THR A  29     5011   4909   4621   -254   1069   -221       O  
ATOM     14  CB  THR A  29       4.525 -35.647  -2.328  1.00 42.83           C  
ANISOU   14  CB  THR A  29     5736   5401   5135   -218   1299   -190       C  
ATOM     15  CG2 THR A  29       4.873 -36.257  -3.678  1.00 42.79           C  
ANISOU   15  CG2 THR A  29     5690   5414   5156   -182   1270   -203       C  
ATOM     16  OG1 THR A  29       3.774 -34.452  -2.555  1.00 45.02           O  
ANISOU   16  OG1 THR A  29     6100   5633   5372   -195   1402   -155       O  
ATOM     17  N   ASN A  30       3.770 -38.968  -2.053  1.00 32.66           N  
ANISOU   17  N   ASN A  30     4282   4198   3928   -143   1041   -142       N  
ATOM     18  CA  ASN A  30       4.354 -40.310  -2.135  1.00 28.87           C  
ANISOU   18  CA  ASN A  30     3724   3758   3486   -142    941   -165       C  
ATOM     19  C   ASN A  30       5.575 -40.167  -3.051  1.00 26.70           C  
ANISOU   19  C   ASN A  30     3426   3494   3224   -165    958   -222       C  
ATOM     20  O   ASN A  30       5.412 -39.807  -4.211  1.00 25.98           O  
ANISOU   20  O   ASN A  30     3355   3387   3128   -134   1003   -216       O  
ATOM     21  CB  ASN A  30       3.318 -41.256  -2.750  1.00 26.63           C  
ANISOU   21  CB  ASN A  30     3409   3485   3224    -75    888   -117       C  
ATOM     22  CG  ASN A  30       3.853 -42.642  -3.008  1.00 25.14           C  
ANISOU   22  CG  ASN A  30     3147   3334   3073    -67    793   -136       C  
ATOM     23  ND2 ASN A  30       2.969 -43.541  -3.372  1.00 25.73           N  
ANISOU   23  ND2 ASN A  30     3192   3417   3167    -17    743    -99       N  
ATOM     24  OD1 ASN A  30       5.055 -42.899  -2.908  1.00 25.12           O  
ANISOU   24  OD1 ASN A  30     3110   3350   3082   -105    767   -187       O  
ATOM     25  N   PRO A  31       6.810 -40.432  -2.572  1.00 25.69           N  
ANISOU   25  N   PRO A  31     3258   3391   3113   -218    924   -281       N  
ATOM     26  CA  PRO A  31       7.984 -40.216  -3.434  1.00 25.58           C  
ANISOU   26  CA  PRO A  31     3221   3383   3117   -244    952   -340       C  
ATOM     27  C   PRO A  31       8.074 -41.151  -4.641  1.00 24.81           C  
ANISOU   27  C   PRO A  31     3076   3302   3049   -199    908   -337       C  
ATOM     28  O   PRO A  31       8.885 -40.910  -5.537  1.00 24.76           O  
ANISOU   28  O   PRO A  31     3063   3291   3055   -213    946   -378       O  
ATOM     29  CB  PRO A  31       9.164 -40.451  -2.492  1.00 27.41           C  
ANISOU   29  CB  PRO A  31     3407   3644   3365   -304    906   -401       C  
ATOM     30  CG  PRO A  31       8.629 -41.377  -1.451  1.00 28.28           C  
ANISOU   30  CG  PRO A  31     3497   3774   3476   -286    817   -367       C  
ATOM     31  CD  PRO A  31       7.204 -40.915  -1.234  1.00 26.45           C  
ANISOU   31  CD  PRO A  31     3329   3508   3212   -253    860   -299       C  
ATOM     32  N   TYR A  32       7.278 -42.233  -4.636  1.00 23.71           N  
ANISOU   32  N   TYR A  32     2907   3180   2923   -150    831   -292       N  
ATOM     33  CA  TYR A  32       7.333 -43.200  -5.742  1.00 22.93           C  
ANISOU   33  CA  TYR A  32     2765   3097   2852   -108    784   -289       C  
ATOM     34  C   TYR A  32       6.244 -43.017  -6.789  1.00 22.74           C  
ANISOU   34  C   TYR A  32     2778   3051   2812    -48    814   -241       C  
ATOM     35  O   TYR A  32       6.220 -43.764  -7.764  1.00 22.04           O  
ANISOU   35  O   TYR A  32     2661   2972   2740    -11    778   -237       O  
ATOM     36  CB  TYR A  32       7.231 -44.641  -5.195  1.00 21.90           C  
ANISOU   36  CB  TYR A  32     2573   3000   2749    -92    675   -276       C  
ATOM     37  CG  TYR A  32       8.177 -44.927  -4.055  1.00 22.72           C  
ANISOU   37  CG  TYR A  32     2643   3127   2862   -139    630   -318       C  
ATOM     38  CD1 TYR A  32       9.501 -44.502  -4.103  1.00 23.66           C  
ANISOU   38  CD1 TYR A  32     2740   3256   2993   -187    653   -384       C  
ATOM     39  CD2 TYR A  32       7.781 -45.696  -2.979  1.00 23.62           C  
ANISOU   39  CD2 TYR A  32     2745   3255   2977   -133    562   -294       C  
ATOM     40  CE1 TYR A  32      10.386 -44.786  -3.070  1.00 25.42           C  
ANISOU   40  CE1 TYR A  32     2927   3507   3226   -226    602   -426       C  
ATOM     41  CE2 TYR A  32       8.650 -45.973  -1.934  1.00 25.17           C  
ANISOU   41  CE2 TYR A  32     2916   3473   3176   -168    515   -332       C  
ATOM     42  CZ  TYR A  32       9.954 -45.528  -1.991  1.00 26.94           C  
ANISOU   42  CZ  TYR A  32     3114   3711   3411   -213    529   -399       C  
ATOM     43  OH  TYR A  32      10.813 -45.826  -0.966  1.00 30.66           O  
ANISOU   43  OH  TYR A  32     3556   4209   3885   -243    473   -440       O  
ATOM     44  N   ALA A  33       5.315 -42.059  -6.586  1.00 22.50           N  
ANISOU   44  N   ALA A  33     2810   2991   2747    -33    876   -203       N  
ATOM     45  CA  ALA A  33       4.236 -41.852  -7.541  1.00 22.79           C  
ANISOU   45  CA  ALA A  33     2882   3009   2767     32    899   -158       C  
ATOM     46  C   ALA A  33       4.801 -41.271  -8.828  1.00 23.75           C  
ANISOU   46  C   ALA A  33     3039   3110   2875     42    961   -184       C  
ATOM     47  O   ALA A  33       5.499 -40.245  -8.806  1.00 25.12           O  
ANISOU   47  O   ALA A  33     3256   3259   3029      2   1043   -217       O  
ATOM     48  CB  ALA A  33       3.179 -40.921  -6.954  1.00 23.06           C  
ANISOU   48  CB  ALA A  33     2975   3017   2769     46    954   -115       C  
ATOM     49  N   ARG A  34       4.492 -41.903  -9.949  1.00 22.18           N  
ANISOU   49  N   ARG A  34     2826   2917   2683     95    927   -170       N  
ATOM     50  CA  ARG A  34       4.956 -41.450 -11.249  1.00 22.02           C  
ANISOU   50  CA  ARG A  34     2847   2873   2647    113    983   -191       C  
ATOM     51  C   ARG A  34       3.786 -41.332 -12.215  1.00 23.25           C  
ANISOU   51  C   ARG A  34     3045   3015   2775    194    986   -144       C  
ATOM     52  O   ARG A  34       2.809 -42.081 -12.128  1.00 23.21           O  
ANISOU   52  O   ARG A  34     3005   3032   2783    235    915   -107       O  
ATOM     53  CB  ARG A  34       5.954 -42.451 -11.870  1.00 22.34           C  
ANISOU   53  CB  ARG A  34     2830   2934   2723    100    934   -231       C  
ATOM     54  CG  ARG A  34       7.153 -42.815 -11.000  1.00 24.35           C  
ANISOU   54  CG  ARG A  34     3025   3213   3013     31    909   -281       C  
ATOM     55  CD  ARG A  34       8.303 -41.800 -11.072  1.00 22.92           C  
ANISOU   55  CD  ARG A  34     2875   3008   2828    -26   1001   -338       C  
ATOM     56  NE  ARG A  34       9.310 -42.141 -10.074  1.00 24.04           N  
ANISOU   56  NE  ARG A  34     2952   3179   3003    -89    964   -385       N  
ATOM     57  CZ  ARG A  34       9.311 -41.704  -8.822  1.00 24.98           C  
ANISOU   57  CZ  ARG A  34     3073   3305   3114   -130    967   -389       C  
ATOM     58  NH1 ARG A  34       8.449 -40.761  -8.436  1.00 26.12           N1+
ANISOU   58  NH1 ARG A  34     3284   3421   3218   -123   1023   -353       N1+
ATOM     59  NH2 ARG A  34      10.222 -42.142  -7.962  1.00 25.00           N  
ANISOU   59  NH2 ARG A  34     3014   3339   3146   -179    918   -433       N  
ATOM     60  N   GLY A  35       3.904 -40.381 -13.138  1.00 23.44           N  
ANISOU   60  N   GLY A  35     3145   2999   2760    216   1070   -149       N  
ATOM     61  CA  GLY A  35       2.948 -40.248 -14.222  1.00 23.56           C  
ANISOU   61  CA  GLY A  35     3208   3001   2744    299   1071   -112       C  
ATOM     62  C   GLY A  35       1.621 -39.589 -13.889  1.00 23.82           C  
ANISOU   62  C   GLY A  35     3280   3023   2747    347   1089    -60       C  
ATOM     63  O   GLY A  35       1.301 -39.274 -12.740  1.00 21.86           O  
ANISOU   63  O   GLY A  35     3023   2779   2504    318   1098    -46       O  
ATOM     64  N   PRO A  36       0.822 -39.375 -14.944  1.00 25.76           N  
ANISOU   64  N   PRO A  36     3572   3255   2959    428   1092    -32       N  
ATOM     65  CA  PRO A  36      -0.488 -38.738 -14.756  1.00 26.02           C  
ANISOU   65  CA  PRO A  36     3642   3281   2965    486   1107     17       C  
ATOM     66  C   PRO A  36      -1.460 -39.588 -13.971  1.00 25.61           C  
ANISOU   66  C   PRO A  36     3508   3268   2953    495   1020     46       C  
ATOM     67  O   PRO A  36      -1.297 -40.821 -13.872  1.00 25.87           O  
ANISOU   67  O   PRO A  36     3462   3336   3031    477    935     34       O  
ATOM     68  CB  PRO A  36      -1.000 -38.536 -16.197  1.00 27.17           C  
ANISOU   68  CB  PRO A  36     3846   3409   3070    575   1111     32       C  
ATOM     69  CG  PRO A  36       0.181 -38.734 -17.090  1.00 28.61           C  
ANISOU   69  CG  PRO A  36     4049   3574   3246    553   1133    -10       C  
ATOM     70  CD  PRO A  36       1.091 -39.682 -16.367  1.00 26.25           C  
ANISOU   70  CD  PRO A  36     3661   3307   3006    472   1083    -45       C  
ATOM     71  N   ASN A  37      -2.517 -38.969 -13.452  1.00 25.07           N  
ANISOU   71  N   ASN A  37     3462   3193   2872    527   1043     84       N  
ATOM     72  CA  ASN A  37      -3.557 -39.694 -12.723  1.00 24.93           C  
ANISOU   72  CA  ASN A  37     3373   3207   2894    540    973    113       C  
ATOM     73  C   ASN A  37      -4.233 -40.688 -13.658  1.00 25.38           C  
ANISOU   73  C   ASN A  37     3379   3293   2970    601    883    120       C  
ATOM     74  O   ASN A  37      -4.494 -40.396 -14.834  1.00 25.95           O  
ANISOU   74  O   ASN A  37     3495   3356   3009    666    888    125       O  
ATOM     75  CB  ASN A  37      -4.584 -38.746 -12.115  1.00 24.86           C  
ANISOU   75  CB  ASN A  37     3401   3178   2865    570   1025    152       C  
ATOM     76  CG  ASN A  37      -4.030 -37.891 -11.013  1.00 25.72           C  
ANISOU   76  CG  ASN A  37     3551   3260   2961    503   1105    146       C  
ATOM     77  ND2 ASN A  37      -4.739 -36.797 -10.696  1.00 26.56           N  
ANISOU   77  ND2 ASN A  37     3718   3337   3035    532   1177    177       N  
ATOM     78  OD1 ASN A  37      -2.969 -38.178 -10.432  1.00 24.17           O  
ANISOU   78  OD1 ASN A  37     3335   3068   2780    427   1104    112       O  
ATOM     79  N   PRO A  38      -4.378 -41.944 -13.194  1.00 23.91           N  
ANISOU   79  N   PRO A  38     3106   3143   2837    575    800    115       N  
ATOM     80  CA  PRO A  38      -4.906 -42.974 -14.090  1.00 22.85           C  
ANISOU   80  CA  PRO A  38     2921   3037   2724    622    714    114       C  
ATOM     81  C   PRO A  38      -6.394 -42.901 -14.372  1.00 22.56           C  
ANISOU   81  C   PRO A  38     2869   3013   2690    696    685    146       C  
ATOM     82  O   PRO A  38      -7.187 -42.495 -13.534  1.00 23.88           O  
ANISOU   82  O   PRO A  38     3028   3176   2868    700    707    172       O  
ATOM     83  CB  PRO A  38      -4.588 -44.274 -13.346  1.00 23.33           C  
ANISOU   83  CB  PRO A  38     2900   3126   2840    565    646     99       C  
ATOM     84  CG  PRO A  38      -4.628 -43.873 -11.896  1.00 23.71           C  
ANISOU   84  CG  PRO A  38     2947   3163   2898    515    685    111       C  
ATOM     85  CD  PRO A  38      -4.048 -42.474 -11.858  1.00 22.81           C  
ANISOU   85  CD  PRO A  38     2916   3014   2735    503    782    108       C  
ATOM     86  N   THR A  39      -6.767 -43.362 -15.563  1.00 22.47           N  
ANISOU   86  N   THR A  39     2849   3017   2672    756    630    142       N  
ATOM     87  CA  THR A  39      -8.157 -43.565 -15.930  1.00 22.70           C  
ANISOU   87  CA  THR A  39     2841   3068   2714    826    578    162       C  
ATOM     88  C   THR A  39      -8.285 -45.004 -16.448  1.00 23.27           C  
ANISOU   88  C   THR A  39     2838   3175   2827    826    480    141       C  
ATOM     89  O   THR A  39      -7.287 -45.609 -16.871  1.00 22.05           O  
ANISOU   89  O   THR A  39     2684   3021   2671    793    461    115       O  
ATOM     90  CB  THR A  39      -8.611 -42.583 -17.010  1.00 23.81           C  
ANISOU   90  CB  THR A  39     3058   3192   2796    915    607    175       C  
ATOM     91  CG2 THR A  39      -8.489 -41.119 -16.556  1.00 24.55           C  
ANISOU   91  CG2 THR A  39     3238   3247   2845    918    713    196       C  
ATOM     92  OG1 THR A  39      -7.906 -42.833 -18.220  1.00 24.51           O  
ANISOU   92  OG1 THR A  39     3185   3275   2852    935    589    153       O  
ATOM     93  N   ALA A  40      -9.521 -45.527 -16.517  1.00 23.91           N  
ANISOU   93  N   ALA A  40     2856   3285   2943    866    419    150       N  
ATOM     94  CA  ALA A  40      -9.736 -46.863 -17.088  1.00 24.96           C  
ANISOU   94  CA  ALA A  40     2920   3450   3112    869    327    128       C  
ATOM     95  C   ALA A  40      -9.241 -46.904 -18.543  1.00 24.90           C  
ANISOU   95  C   ALA A  40     2962   3440   3059    914    304    110       C  
ATOM     96  O   ALA A  40      -8.532 -47.832 -18.937  1.00 24.28           O  
ANISOU   96  O   ALA A  40     2865   3369   2993    883    264     86       O  
ATOM     97  CB  ALA A  40     -11.215 -47.227 -17.025  1.00 26.09           C  
ANISOU   97  CB  ALA A  40     2993   3623   3297    912    274    135       C  
ATOM     98  N   ALA A  41      -9.510 -45.829 -19.315  1.00 24.18           N  
ANISOU   98  N   ALA A  41     2947   3332   2910    985    338    123       N  
ATOM     99  CA  ALA A  41      -9.068 -45.763 -20.705  1.00 24.14           C  
ANISOU   99  CA  ALA A  41     3004   3315   2852   1034    325    109       C  
ATOM    100  C   ALA A  41      -7.556 -45.775 -20.826  1.00 23.11           C  
ANISOU  100  C   ALA A  41     2922   3156   2703    976    373     90       C  
ATOM    101  O   ALA A  41      -7.040 -46.472 -21.699  1.00 25.00           O  
ANISOU  101  O   ALA A  41     3166   3398   2935    978    334     68       O  
ATOM    102  CB  ALA A  41      -9.642 -44.524 -21.400  1.00 24.85           C  
ANISOU  102  CB  ALA A  41     3178   3386   2877   1125    362    130       C  
ATOM    103  N   SER A  42      -6.841 -45.000 -19.957  1.00 22.44           N  
ANISOU  103  N   SER A  42     2873   3044   2611    923    458     96       N  
ATOM    104  CA  SER A  42      -5.374 -44.990 -20.068  1.00 23.56           C  
ANISOU  104  CA  SER A  42     3051   3159   2739    866    505     71       C  
ATOM    105  C   SER A  42      -4.787 -46.339 -19.696  1.00 22.91           C  
ANISOU  105  C   SER A  42     2889   3102   2713    801    446     48       C  
ATOM    106  O   SER A  42      -3.796 -46.733 -20.277  1.00 24.38           O  
ANISOU  106  O   SER A  42     3091   3278   2893    780    448     23       O  
ATOM    107  CB  SER A  42      -4.740 -43.865 -19.249  1.00 25.50           C  
ANISOU  107  CB  SER A  42     3350   3373   2967    822    606     76       C  
ATOM    108  OG  SER A  42      -4.851 -44.007 -17.831  1.00 27.41           O  
ANISOU  108  OG  SER A  42     3534   3628   3252    763    609     84       O  
ATOM    109  N   LEU A  43      -5.399 -47.034 -18.724  1.00 21.23           N  
ANISOU  109  N   LEU A  43     2594   2919   2554    773    400     56       N  
ATOM    110  CA  LEU A  43      -4.883 -48.346 -18.309  1.00 20.36           C  
ANISOU  110  CA  LEU A  43     2413   2830   2494    715    345     36       C  
ATOM    111  C   LEU A  43      -5.260 -49.469 -19.269  1.00 20.87           C  
ANISOU  111  C   LEU A  43     2440   2917   2573    747    262     23       C  
ATOM    112  O   LEU A  43      -4.607 -50.513 -19.268  1.00 20.34           O  
ANISOU  112  O   LEU A  43     2335   2860   2535    707    225      3       O  
ATOM    113  CB  LEU A  43      -5.409 -48.657 -16.914  1.00 19.36           C  
ANISOU  113  CB  LEU A  43     2226   2718   2414    675    335     51       C  
ATOM    114  CG  LEU A  43      -4.684 -47.923 -15.813  1.00 22.05           C  
ANISOU  114  CG  LEU A  43     2592   3038   2749    619    404     53       C  
ATOM    115  CD1 LEU A  43      -5.438 -48.084 -14.508  1.00 22.64           C  
ANISOU  115  CD1 LEU A  43     2622   3121   2859    594    399     73       C  
ATOM    116  CD2 LEU A  43      -3.266 -48.528 -15.630  1.00 25.34           C  
ANISOU  116  CD2 LEU A  43     2997   3454   3178    558    401     23       C  
ATOM    117  N   GLU A  44      -6.333 -49.301 -20.044  1.00 21.49           N  
ANISOU  117  N   GLU A  44     2525   3006   2634    818    228     34       N  
ATOM    118  CA  GLU A  44      -6.760 -50.317 -21.016  1.00 21.53           C  
ANISOU  118  CA  GLU A  44     2498   3033   2649    851    146     18       C  
ATOM    119  C   GLU A  44      -6.093 -50.175 -22.388  1.00 22.79           C  
ANISOU  119  C   GLU A  44     2730   3173   2757    888    151      2       C  
ATOM    120  O   GLU A  44      -6.184 -51.085 -23.224  1.00 22.96           O  
ANISOU  120  O   GLU A  44     2734   3208   2783    906     87    -15       O  
ATOM    121  CB  GLU A  44      -8.289 -50.265 -21.195  1.00 22.79           C  
ANISOU  121  CB  GLU A  44     2622   3219   2819    913     97     30       C  
ATOM    122  CG  GLU A  44      -9.032 -50.672 -19.931  1.00 24.00           C  
ANISOU  122  CG  GLU A  44     2694   3392   3034    874     84     40       C  
ATOM    123  CD  GLU A  44     -10.520 -50.392 -19.938  1.00 30.18           C  
ANISOU  123  CD  GLU A  44     3440   4197   3832    931     56     52       C  
ATOM    124  OE1 GLU A  44     -11.035 -49.924 -20.980  1.00 33.71           O  
ANISOU  124  OE1 GLU A  44     3920   4649   4239   1007     34     52       O  
ATOM    125  OE2 GLU A  44     -11.172 -50.610 -18.892  1.00 30.26           O1-
ANISOU  125  OE2 GLU A  44     3389   4217   3892    901     57     61       O1-
ATOM    126  N   ALA A  45      -5.474 -49.006 -22.645  1.00 23.08           N  
ANISOU  126  N   ALA A  45     2855   3173   2741    902    231      8       N  
ATOM    127  CA  ALA A  45      -4.809 -48.758 -23.925  1.00 23.70           C  
ANISOU  127  CA  ALA A  45     3016   3223   2766    937    253     -6       C  
ATOM    128  C   ALA A  45      -3.604 -49.684 -24.139  1.00 24.04           C  
ANISOU  128  C   ALA A  45     3042   3259   2831    880    245    -35       C  
ATOM    129  O   ALA A  45      -3.067 -50.239 -23.175  1.00 24.06           O  
ANISOU  129  O   ALA A  45     2985   3274   2883    811    244    -42       O  
ATOM    130  CB  ALA A  45      -4.359 -47.301 -23.977  1.00 24.00           C  
ANISOU  130  CB  ALA A  45     3151   3218   2750    952    355      5       C  
ATOM    131  N   SER A  46      -3.151 -49.845 -25.397  1.00 23.52           N  
ANISOU  131  N   SER A  46     3036   3173   2729    913    242    -51       N  
ATOM    132  CA  SER A  46      -1.998 -50.706 -25.667  1.00 24.02           C  
ANISOU  132  CA  SER A  46     3086   3227   2813    864    240    -78       C  
ATOM    133  C   SER A  46      -0.725 -50.167 -25.025  1.00 23.73           C  
ANISOU  133  C   SER A  46     3066   3165   2787    800    326    -91       C  
ATOM    134  O   SER A  46       0.210 -50.939 -24.775  1.00 23.90           O  
ANISOU  134  O   SER A  46     3045   3189   2846    744    320   -113       O  
ATOM    135  CB  SER A  46      -1.796 -50.912 -27.173  1.00 28.04           C  
ANISOU  135  CB  SER A  46     3665   3713   3277    914    227    -92       C  
ATOM    136  OG  SER A  46      -1.595 -49.641 -27.768  1.00 33.04           O  
ANISOU  136  OG  SER A  46     4406   4302   3845    957    306    -86       O  
ATOM    137  N   ALA A  47      -0.652 -48.855 -24.764  1.00 23.88           N  
ANISOU  137  N   ALA A  47     3146   3157   2772    806    407    -80       N  
ATOM    138  CA  ALA A  47       0.511 -48.285 -24.100  1.00 24.41           C  
ANISOU  138  CA  ALA A  47     3224   3202   2851    741    490    -97       C  
ATOM    139  C   ALA A  47       0.081 -47.132 -23.222  1.00 24.02           C  
ANISOU  139  C   ALA A  47     3195   3146   2787    738    546    -75       C  
ATOM    140  O   ALA A  47      -0.895 -46.451 -23.514  1.00 24.81           O  
ANISOU  140  O   ALA A  47     3338   3240   2847    800    550    -49       O  
ATOM    141  CB  ALA A  47       1.537 -47.804 -25.125  1.00 25.20           C  
ANISOU  141  CB  ALA A  47     3410   3252   2912    746    565   -121       C  
ATOM    142  N   GLY A  48       0.822 -46.941 -22.145  1.00 23.10           N  
ANISOU  142  N   GLY A  48     3044   3030   2702    666    585    -88       N  
ATOM    143  CA  GLY A  48       0.646 -45.844 -21.212  1.00 23.93           C  
ANISOU  143  CA  GLY A  48     3171   3125   2796    647    648    -73       C  
ATOM    144  C   GLY A  48       1.290 -44.562 -21.708  1.00 24.28           C  
ANISOU  144  C   GLY A  48     3316   3117   2790    651    759    -85       C  
ATOM    145  O   GLY A  48       1.679 -44.450 -22.880  1.00 23.99           O  
ANISOU  145  O   GLY A  48     3344   3050   2720    683    787    -99       O  
ATOM    146  N   PRO A  49       1.530 -43.636 -20.773  1.00 24.29           N  
ANISOU  146  N   PRO A  49     3334   3106   2789    610    829    -85       N  
ATOM    147  CA  PRO A  49       2.027 -42.304 -21.176  1.00 24.71           C  
ANISOU  147  CA  PRO A  49     3490   3105   2792    613    946    -95       C  
ATOM    148  C   PRO A  49       3.508 -42.197 -21.534  1.00 26.19           C  
ANISOU  148  C   PRO A  49     3700   3262   2988    557   1013   -144       C  
ATOM    149  O   PRO A  49       3.884 -41.248 -22.244  1.00 27.61           O  
ANISOU  149  O   PRO A  49     3979   3391   3122    573   1109   -155       O  
ATOM    150  CB  PRO A  49       1.687 -41.424 -19.971  1.00 25.24           C  
ANISOU  150  CB  PRO A  49     3560   3171   2857    584    991    -78       C  
ATOM    151  CG  PRO A  49       1.718 -42.403 -18.785  1.00 25.46           C  
ANISOU  151  CG  PRO A  49     3476   3249   2949    528    913    -81       C  
ATOM    152  CD  PRO A  49       1.125 -43.675 -19.351  1.00 23.65           C  
ANISOU  152  CD  PRO A  49     3190   3054   2742    570    806    -70       C  
ATOM    153  N   PHE A  50       4.362 -43.079 -20.998  1.00 24.20           N  
ANISOU  153  N   PHE A  50     3361   3039   2794    491    973   -175       N  
ATOM    154  CA  PHE A  50       5.794 -42.956 -21.226  1.00 24.41           C  
ANISOU  154  CA  PHE A  50     3396   3040   2839    433   1039   -227       C  
ATOM    155  C   PHE A  50       6.283 -43.636 -22.479  1.00 25.31           C  
ANISOU  155  C   PHE A  50     3525   3138   2952    458   1026   -246       C  
ATOM    156  O   PHE A  50       5.824 -44.723 -22.831  1.00 24.08           O  
ANISOU  156  O   PHE A  50     3326   3013   2811    491    933   -230       O  
ATOM    157  CB  PHE A  50       6.590 -43.491 -20.031  1.00 24.58           C  
ANISOU  157  CB  PHE A  50     3319   3099   2923    353   1007   -256       C  
ATOM    158  CG  PHE A  50       6.307 -42.752 -18.753  1.00 25.61           C  
ANISOU  158  CG  PHE A  50     3442   3238   3053    317   1032   -246       C  
ATOM    159  CD1 PHE A  50       6.545 -41.391 -18.650  1.00 27.27           C  
ANISOU  159  CD1 PHE A  50     3728   3405   3227    298   1142   -256       C  
ATOM    160  CD2 PHE A  50       5.749 -43.402 -17.670  1.00 26.50           C  
ANISOU  160  CD2 PHE A  50     3479   3396   3195    305    950   -223       C  
ATOM    161  CE1 PHE A  50       6.294 -40.713 -17.463  1.00 28.01           C  
ANISOU  161  CE1 PHE A  50     3818   3505   3318    264   1167   -247       C  
ATOM    162  CE2 PHE A  50       5.490 -42.720 -16.483  1.00 27.29           C  
ANISOU  162  CE2 PHE A  50     3578   3499   3291    273    975   -213       C  
ATOM    163  CZ  PHE A  50       5.747 -41.377 -16.392  1.00 27.23           C  
ANISOU  163  CZ  PHE A  50     3645   3452   3250    253   1082   -224       C  
ATOM    164  N   THR A  51       7.255 -43.000 -23.154  1.00 26.66           N  
ANISOU  164  N   THR A  51     3763   3260   3107    438   1126   -282       N  
ATOM    165  CA  THR A  51       7.901 -43.585 -24.311  1.00 27.99           C  
ANISOU  165  CA  THR A  51     3951   3405   3278    452   1131   -307       C  
ATOM    166  C   THR A  51       8.816 -44.705 -23.839  1.00 27.03           C  
ANISOU  166  C   THR A  51     3719   3321   3229    392   1075   -341       C  
ATOM    167  O   THR A  51       9.516 -44.539 -22.837  1.00 28.11           O  
ANISOU  167  O   THR A  51     3797   3475   3407    323   1094   -370       O  
ATOM    168  CB  THR A  51       8.720 -42.519 -25.061  1.00 31.54           C  
ANISOU  168  CB  THR A  51     4505   3784   3694    440   1269   -339       C  
ATOM    169  CG2 THR A  51       9.612 -43.110 -26.152  1.00 32.94           C  
ANISOU  169  CG2 THR A  51     4700   3933   3884    439   1290   -374       C  
ATOM    170  OG1 THR A  51       7.799 -41.576 -25.599  1.00 33.52           O  
ANISOU  170  OG1 THR A  51     4868   3998   3870    510   1312   -302       O  
ATOM    171  N   VAL A  52       8.794 -45.837 -24.527  1.00 26.08           N  
ANISOU  171  N   VAL A  52     3570   3216   3124    420   1004   -339       N  
ATOM    172  CA  VAL A  52       9.602 -46.980 -24.161  1.00 25.71           C  
ANISOU  172  CA  VAL A  52     3423   3203   3142    374    947   -368       C  
ATOM    173  C   VAL A  52      10.723 -47.251 -25.142  1.00 26.67           C  
ANISOU  173  C   VAL A  52     3565   3288   3278    361    999   -410       C  
ATOM    174  O   VAL A  52      10.530 -47.205 -26.354  1.00 27.90           O  
ANISOU  174  O   VAL A  52     3802   3405   3393    410   1024   -402       O  
ATOM    175  CB  VAL A  52       8.701 -48.242 -24.078  1.00 25.83           C  
ANISOU  175  CB  VAL A  52     3378   3265   3170    412    820   -332       C  
ATOM    176  CG1 VAL A  52       9.516 -49.517 -23.817  1.00 25.70           C  
ANISOU  176  CG1 VAL A  52     3269   3281   3217    375    760   -359       C  
ATOM    177  CG2 VAL A  52       7.643 -48.066 -22.998  1.00 26.03           C  
ANISOU  177  CG2 VAL A  52     3371   3327   3192    418    771   -295       C  
ATOM    178  N   ARG A  53      11.888 -47.552 -24.602  1.00 26.39           N  
ANISOU  178  N   ARG A  53     3457   3268   3304    295   1012   -456       N  
ATOM    179  CA AARG A  53      13.018 -47.993 -25.403  0.50 27.02           C  
ANISOU  179  CA AARG A  53     3533   3321   3414    277   1051   -500       C  
ATOM    180  CA BARG A  53      13.028 -47.990 -25.399  0.50 27.36           C  
ANISOU  180  CA BARG A  53     3575   3364   3457    276   1052   -500       C  
ATOM    181  C   ARG A  53      13.443 -49.369 -24.851  1.00 26.97           C  
ANISOU  181  C   ARG A  53     3409   3368   3471    254    953   -511       C  
ATOM    182  O   ARG A  53      13.044 -49.747 -23.726  1.00 26.30           O  
ANISOU  182  O   ARG A  53     3253   3334   3407    241    877   -493       O  
ATOM    183  CB AARG A  53      14.173 -46.985 -25.369  0.50 28.77           C  
ANISOU  183  CB AARG A  53     3776   3503   3653    218   1176   -556       C  
ATOM    184  CB BARG A  53      14.204 -47.006 -25.327  0.50 30.03           C  
ANISOU  184  CB BARG A  53     3931   3664   3815    215   1174   -557       C  
ATOM    185  CG AARG A  53      13.820 -45.621 -25.965  0.50 32.20           C  
ANISOU  185  CG AARG A  53     4339   3875   4021    240   1286   -547       C  
ATOM    186  CG BARG A  53      14.072 -45.759 -26.206  0.50 35.25           C  
ANISOU  186  CG BARG A  53     4726   4254   4414    238   1295   -557       C  
ATOM    187  CD AARG A  53      15.026 -44.691 -26.009  0.50 35.53           C  
ANISOU  187  CD AARG A  53     4784   4252   4465    176   1419   -609       C  
ATOM    188  CD BARG A  53      14.179 -46.001 -27.704  0.50 39.77           C  
ANISOU  188  CD BARG A  53     5386   4771   4953    285   1334   -557       C  
ATOM    189  NE AARG A  53      16.098 -45.232 -26.843  0.50 38.55           N  
ANISOU  189  NE AARG A  53     5155   4605   4885    159   1458   -655       N  
ATOM    190  NE BARG A  53      15.551 -46.072 -28.219  0.50 43.30           N  
ANISOU  190  NE BARG A  53     5823   5182   5445    239   1415   -617       N  
ATOM    191  CZ AARG A  53      17.269 -44.633 -27.051  0.50 42.10           C  
ANISOU  191  CZ AARG A  53     5616   5013   5368    102   1574   -718       C  
ATOM    192  CZ BARG A  53      16.156 -47.202 -28.577  0.50 45.00           C  
ANISOU  192  CZ BARG A  53     5980   5412   5707    235   1368   -635       C  
ATOM    193  NH1AARG A  53      17.541 -43.472 -26.471  0.50 43.04           N1+
ANISOU  193  NH1AARG A  53     5756   5113   5483     53   1662   -745       N1+
ATOM    194  NH2AARG A  53      18.184 -45.202 -27.825  0.50 41.49           N  
ANISOU  194  NH2AARG A  53     5526   4910   5328     90   1606   -757       N  
ATOM    195  NH1BARG A  53      17.392 -47.177 -29.054  0.50 45.18           N1+
ANISOU  195  NH1BARG A  53     5994   5398   5773    193   1451   -693       N1+
ATOM    196  NH2BARG A  53      15.542 -48.370 -28.427  0.50 44.27           N  
ANISOU  196  NH2BARG A  53     5832   5369   5620    271   1241   -598       N  
ATOM    197  N   SER A  54      14.215 -50.115 -25.619  1.00 26.78           N  
ANISOU  197  N   SER A  54     3372   3329   3475    254    957   -538       N  
ATOM    198  CA  SER A  54      14.646 -51.425 -25.190  1.00 27.30           C  
ANISOU  198  CA  SER A  54     3336   3439   3596    239    871   -548       C  
ATOM    199  C   SER A  54      16.023 -51.797 -25.693  1.00 29.01           C  
ANISOU  199  C   SER A  54     3522   3636   3864    208    919   -602       C  
ATOM    200  O   SER A  54      16.517 -51.216 -26.664  1.00 29.68           O  
ANISOU  200  O   SER A  54     3678   3665   3933    208   1016   -627       O  
ATOM    201  CB  SER A  54      13.620 -52.478 -25.605  1.00 29.58           C  
ANISOU  201  CB  SER A  54     3628   3747   3863    296    773   -500       C  
ATOM    202  OG  SER A  54      13.558 -52.644 -27.014  1.00 32.38           O  
ANISOU  202  OG  SER A  54     4061   4057   4186    338    802   -496       O  
ATOM    203  N   PHE A  55      16.653 -52.764 -25.030  1.00 28.03           N  
ANISOU  203  N   PHE A  55     3295   3557   3800    183    855   -622       N  
ATOM    204  CA  PHE A  55      17.936 -53.285 -25.480  1.00 27.57           C  
ANISOU  204  CA  PHE A  55     3194   3485   3796    159    887   -673       C  
ATOM    205  C   PHE A  55      18.092 -54.740 -25.066  1.00 27.71           C  
ANISOU  205  C   PHE A  55     3124   3551   3856    170    782   -666       C  
ATOM    206  O   PHE A  55      17.468 -55.201 -24.102  1.00 27.49           O  
ANISOU  206  O   PHE A  55     3049   3570   3826    176    693   -635       O  
ATOM    207  CB  PHE A  55      19.124 -52.437 -24.974  1.00 27.36           C  
ANISOU  207  CB  PHE A  55     3127   3454   3815     94    970   -738       C  
ATOM    208  CG  PHE A  55      19.293 -52.398 -23.465  1.00 28.12           C  
ANISOU  208  CG  PHE A  55     3132   3609   3944     56    913   -750       C  
ATOM    209  CD1 PHE A  55      20.102 -53.318 -22.816  1.00 28.93           C  
ANISOU  209  CD1 PHE A  55     3127   3757   4109     38    849   -780       C  
ATOM    210  CD2 PHE A  55      18.693 -51.403 -22.712  1.00 29.00           C  
ANISOU  210  CD2 PHE A  55     3270   3727   4022     40    928   -735       C  
ATOM    211  CE1 PHE A  55      20.263 -53.270 -21.436  1.00 29.60           C  
ANISOU  211  CE1 PHE A  55     3136   3894   4217      8    794   -792       C  
ATOM    212  CE2 PHE A  55      18.849 -51.361 -21.332  1.00 29.67           C  
ANISOU  212  CE2 PHE A  55     3280   3863   4132      6    876   -746       C  
ATOM    213  CZ  PHE A  55      19.638 -52.286 -20.702  1.00 28.81           C  
ANISOU  213  CZ  PHE A  55     3068   3799   4081     -9    808   -776       C  
ATOM    214  N   THR A  56      18.946 -55.465 -25.781  1.00 27.81           N  
ANISOU  214  N   THR A  56     3116   3546   3904    171    797   -694       N  
ATOM    215  CA  THR A  56      19.242 -56.844 -25.457  1.00 28.22           C  
ANISOU  215  CA  THR A  56     3088   3636   3998    182    709   -692       C  
ATOM    216  C   THR A  56      20.414 -56.835 -24.494  1.00 29.58           C  
ANISOU  216  C   THR A  56     3158   3844   4238    135    709   -746       C  
ATOM    217  O   THR A  56      21.408 -56.148 -24.755  1.00 30.48           O  
ANISOU  217  O   THR A  56     3264   3933   4384     98    799   -801       O  
ATOM    218  CB  THR A  56      19.646 -57.602 -26.756  1.00 29.87           C  
ANISOU  218  CB  THR A  56     3330   3806   4215    207    734   -699       C  
ATOM    219  CG2 THR A  56      20.129 -59.021 -26.477  1.00 31.00           C  
ANISOU  219  CG2 THR A  56     3391   3983   4406    217    657   -704       C  
ATOM    220  OG1 THR A  56      18.514 -57.639 -27.638  1.00 30.69           O  
ANISOU  220  OG1 THR A  56     3528   3880   4251    254    723   -651       O  
ATOM    221  N   VAL A  57      20.335 -57.598 -23.385  1.00 29.09           N  
ANISOU  221  N   VAL A  57     3017   3837   4197    137    612   -734       N  
ATOM    222  CA  VAL A  57      21.448 -57.672 -22.426  1.00 29.78           C  
ANISOU  222  CA  VAL A  57     3005   3965   4346    101    596   -786       C  
ATOM    223  C   VAL A  57      22.632 -58.363 -23.123  1.00 31.62           C  
ANISOU  223  C   VAL A  57     3193   4184   4636    100    623   -831       C  
ATOM    224  O   VAL A  57      22.487 -59.488 -23.590  1.00 31.44           O  
ANISOU  224  O   VAL A  57     3171   4160   4615    138    576   -806       O  
ATOM    225  CB  VAL A  57      21.020 -58.422 -21.147  1.00 29.71           C  
ANISOU  225  CB  VAL A  57     2938   4013   4337    114    482   -757       C  
ATOM    226  CG1 VAL A  57      22.196 -58.577 -20.188  1.00 30.58           C  
ANISOU  226  CG1 VAL A  57     2947   4166   4507     86    456   -812       C  
ATOM    227  CG2 VAL A  57      19.851 -57.710 -20.468  1.00 29.19           C  
ANISOU  227  CG2 VAL A  57     2917   3956   4218    113    464   -715       C  
ATOM    228  N   SER A  58      23.776 -57.680 -23.225  1.00 33.59           N  
ANISOU  228  N   SER A  58     3408   4421   4934     57    704   -898       N  
ATOM    229  CA ASER A  58      24.943 -58.207 -23.939  0.50 35.11           C  
ANISOU  229  CA ASER A  58     3558   4595   5187     53    746   -946       C  
ATOM    230  CA BSER A  58      24.929 -58.221 -23.948  0.50 35.18           C  
ANISOU  230  CA BSER A  58     3567   4603   5195     54    745   -945       C  
ATOM    231  C   SER A  58      25.520 -59.497 -23.356  1.00 36.20           C  
ANISOU  231  C   SER A  58     3598   4782   5374     74    653   -955       C  
ATOM    232  O   SER A  58      25.793 -60.445 -24.102  1.00 38.23           O  
ANISOU  232  O   SER A  58     3854   5021   5648    104    647   -949       O  
ATOM    233  CB ASER A  58      26.032 -57.139 -24.037  0.50 36.76           C  
ANISOU  233  CB ASER A  58     3740   4784   5444     -5    854  -1023       C  
ATOM    234  CB BSER A  58      26.017 -57.161 -24.102  0.50 37.06           C  
ANISOU  234  CB BSER A  58     3782   4818   5480     -3    856  -1021       C  
ATOM    235  OG ASER A  58      25.548 -55.978 -24.689  0.50 39.23           O  
ANISOU  235  OG ASER A  58     4156   5042   5709    -21    952  -1015       O  
ATOM    236  OG BSER A  58      27.083 -57.668 -24.888  0.50 39.83           O  
ANISOU  236  OG BSER A  58     4098   5144   5890     -5    906  -1066       O  
ATOM    237  N   ARG A  59      25.768 -59.515 -22.038  1.00 35.34           N  
ANISOU  237  N   ARG A  59     3409   4731   5287     60    584   -972       N  
ATOM    238  CA  ARG A  59      26.349 -60.688 -21.400  1.00 34.72           C  
ANISOU  238  CA  ARG A  59     3241   4700   5251     86    494   -982       C  
ATOM    239  C   ARG A  59      25.449 -61.086 -20.222  1.00 32.79           C  
ANISOU  239  C   ARG A  59     2993   4500   4963    109    386   -931       C  
ATOM    240  O   ARG A  59      25.712 -60.717 -19.070  1.00 33.14           O  
ANISOU  240  O   ARG A  59     2985   4588   5019     89    347   -954       O  
ATOM    241  CB  ARG A  59      27.772 -60.371 -20.891  1.00 37.51           C  
ANISOU  241  CB  ARG A  59     3488   5084   5682     49    515  -1066       C  
ATOM    242  CG  ARG A  59      28.763 -59.937 -21.977  1.00 44.01           C  
ANISOU  242  CG  ARG A  59     4304   5861   6558     19    633  -1127       C  
ATOM    243  CD  ARG A  59      29.176 -61.102 -22.855  1.00 50.63           C  
ANISOU  243  CD  ARG A  59     5133   6678   7425     59    630  -1121       C  
ATOM    244  NE  ARG A  59      30.187 -60.726 -23.850  1.00 57.62           N  
ANISOU  244  NE  ARG A  59     6008   7517   8367     30    746  -1182       N  
ATOM    245  CZ  ARG A  59      29.913 -60.393 -25.110  1.00 62.37           C  
ANISOU  245  CZ  ARG A  59     6707   8048   8941     28    842  -1168       C  
ATOM    246  NH1 ARG A  59      28.657 -60.376 -25.543  1.00 62.42           N1+
ANISOU  246  NH1 ARG A  59     6825   8027   8866     55    830  -1097       N1+
ATOM    247  NH2 ARG A  59      30.894 -60.076 -25.947  1.00 63.34           N  
ANISOU  247  NH2 ARG A  59     6820   8127   9120      0    952  -1228       N  
ATOM    248  N   PRO A  60      24.362 -61.821 -20.507  1.00 31.15           N  
ANISOU  248  N   PRO A  60     2848   4282   4708    151    340   -862       N  
ATOM    249  CA  PRO A  60      23.448 -62.214 -19.418  1.00 30.74           C  
ANISOU  249  CA  PRO A  60     2800   4265   4616    171    246   -813       C  
ATOM    250  C   PRO A  60      24.159 -63.057 -18.359  1.00 30.61           C  
ANISOU  250  C   PRO A  60     2697   4299   4635    188    162   -834       C  
ATOM    251  O   PRO A  60      24.909 -63.976 -18.678  1.00 30.81           O  
ANISOU  251  O   PRO A  60     2678   4329   4700    213    145   -852       O  
ATOM    252  CB  PRO A  60      22.326 -62.975 -20.129  1.00 31.09           C  
ANISOU  252  CB  PRO A  60     2916   4283   4615    210    223   -749       C  
ATOM    253  CG  PRO A  60      22.864 -63.312 -21.485  1.00 31.69           C  
ANISOU  253  CG  PRO A  60     3010   4317   4713    220    281   -766       C  
ATOM    254  CD  PRO A  60      23.914 -62.309 -21.825  1.00 30.10           C  
ANISOU  254  CD  PRO A  60     2784   4101   4552    178    372   -830       C  
ATOM    255  N   SER A  61      23.934 -62.720 -17.096  1.00 29.54           N  
ANISOU  255  N   SER A  61     2542   4201   4484    177    111   -831       N  
ATOM    256  CA  SER A  61      24.603 -63.382 -15.987  1.00 29.86           C  
ANISOU  256  CA  SER A  61     2507   4290   4550    196     29   -853       C  
ATOM    257  C   SER A  61      23.624 -64.160 -15.122  1.00 28.71           C  
ANISOU  257  C   SER A  61     2393   4159   4356    232    -58   -792       C  
ATOM    258  O   SER A  61      22.826 -63.558 -14.410  1.00 28.44           O  
ANISOU  258  O   SER A  61     2394   4129   4281    217    -70   -766       O  
ATOM    259  CB  SER A  61      25.354 -62.354 -15.146  1.00 32.71           C  
ANISOU  259  CB  SER A  61     2813   4682   4935    152     40   -913       C  
ATOM    260  OG  SER A  61      25.950 -62.943 -14.000  1.00 36.96           O  
ANISOU  260  OG  SER A  61     3284   5270   5490    174    -49   -934       O  
ATOM    261  N   GLY A  62      23.700 -65.484 -15.192  1.00 28.21           N  
ANISOU  261  N   GLY A  62     2320   4100   4299    280   -113   -770       N  
ATOM    262  CA  GLY A  62      22.839 -66.337 -14.387  1.00 28.62           C  
ANISOU  262  CA  GLY A  62     2404   4161   4310    316   -189   -716       C  
ATOM    263  C   GLY A  62      21.507 -66.695 -15.015  1.00 27.99           C  
ANISOU  263  C   GLY A  62     2403   4045   4187    327   -178   -653       C  
ATOM    264  O   GLY A  62      20.644 -67.248 -14.331  1.00 29.49           O  
ANISOU  264  O   GLY A  62     2626   4238   4342    347   -230   -608       O  
ATOM    265  N   TYR A  63      21.336 -66.407 -16.311  1.00 25.59           N  
ANISOU  265  N   TYR A  63     2131   3705   3886    315   -112   -651       N  
ATOM    266  CA  TYR A  63      20.135 -66.738 -17.091  1.00 24.81           C  
ANISOU  266  CA  TYR A  63     2104   3574   3750    328   -101   -600       C  
ATOM    267  C   TYR A  63      20.493 -66.769 -18.595  1.00 25.79           C  
ANISOU  267  C   TYR A  63     2246   3662   3892    328    -38   -615       C  
ATOM    268  O   TYR A  63      21.630 -66.439 -18.958  1.00 26.24           O  
ANISOU  268  O   TYR A  63     2261   3718   3990    314      4   -665       O  
ATOM    269  CB  TYR A  63      18.938 -65.821 -16.754  1.00 23.57           C  
ANISOU  269  CB  TYR A  63     1997   3410   3548    306    -89   -567       C  
ATOM    270  CG  TYR A  63      19.224 -64.368 -17.040  1.00 23.19           C  
ANISOU  270  CG  TYR A  63     1955   3355   3503    267    -17   -598       C  
ATOM    271  CD1 TYR A  63      19.956 -63.594 -16.147  1.00 22.93           C  
ANISOU  271  CD1 TYR A  63     1876   3348   3487    238    -12   -638       C  
ATOM    272  CD2 TYR A  63      18.788 -63.773 -18.215  1.00 22.98           C  
ANISOU  272  CD2 TYR A  63     1982   3291   3459    259     49   -590       C  
ATOM    273  CE1 TYR A  63      20.266 -62.272 -16.427  1.00 23.84           C  
ANISOU  273  CE1 TYR A  63     1999   3452   3607    198     62   -671       C  
ATOM    274  CE2 TYR A  63      19.077 -62.448 -18.500  1.00 23.49           C  
ANISOU  274  CE2 TYR A  63     2060   3342   3522    225    123   -619       C  
ATOM    275  CZ  TYR A  63      19.828 -61.702 -17.608  1.00 24.05           C  
ANISOU  275  CZ  TYR A  63     2084   3437   3615    191    133   -660       C  
ATOM    276  OH  TYR A  63      20.135 -60.395 -17.896  1.00 24.69           O  
ANISOU  276  OH  TYR A  63     2182   3501   3697    154    214   -692       O  
ATOM    277  N   GLY A  64      19.571 -67.213 -19.448  1.00 25.48           N  
ANISOU  277  N   GLY A  64     2267   3592   3822    344    -33   -575       N  
ATOM    278  CA  GLY A  64      19.879 -67.421 -20.868  1.00 25.70           C  
ANISOU  278  CA  GLY A  64     2322   3583   3861    351     19   -586       C  
ATOM    279  C   GLY A  64      20.054 -66.181 -21.709  1.00 26.02           C  
ANISOU  279  C   GLY A  64     2393   3595   3897    323    104   -610       C  
ATOM    280  O   GLY A  64      21.052 -66.027 -22.417  1.00 26.25           O  
ANISOU  280  O   GLY A  64     2408   3606   3961    314    160   -650       O  
ATOM    281  N   ALA A  65      19.034 -65.321 -21.700  1.00 24.25           N  
ANISOU  281  N   ALA A  65     2221   3363   3629    312    119   -584       N  
ATOM    282  CA  ALA A  65      19.048 -64.087 -22.481  1.00 24.07           C  
ANISOU  282  CA  ALA A  65     2244   3309   3591    290    202   -600       C  
ATOM    283  C   ALA A  65      18.052 -63.115 -21.859  1.00 23.37           C  
ANISOU  283  C   ALA A  65     2187   3230   3462    277    200   -574       C  
ATOM    284  O   ALA A  65      17.149 -63.552 -21.132  1.00 22.51           O  
ANISOU  284  O   ALA A  65     2077   3142   3332    290    136   -536       O  
ATOM    285  CB  ALA A  65      18.635 -64.384 -23.920  1.00 24.26           C  
ANISOU  285  CB  ALA A  65     2339   3288   3590    313    233   -584       C  
ATOM    286  N   GLY A  66      18.210 -61.828 -22.129  1.00 23.17           N  
ANISOU  286  N   GLY A  66     2191   3185   3427    252    274   -595       N  
ATOM    287  CA  GLY A  66      17.288 -60.849 -21.585  1.00 23.48           C  
ANISOU  287  CA  GLY A  66     2265   3231   3427    242    280   -570       C  
ATOM    288  C   GLY A  66      17.078 -59.656 -22.485  1.00 24.41           C  
ANISOU  288  C   GLY A  66     2456   3307   3513    235    367   -575       C  
ATOM    289  O   GLY A  66      17.966 -59.295 -23.269  1.00 25.40           O  
ANISOU  289  O   GLY A  66     2593   3401   3657    222    440   -614       O  
ATOM    290  N   THR A  67      15.873 -59.098 -22.420  1.00 22.22           N  
ANISOU  290  N   THR A  67     2231   3024   3186    249    362   -535       N  
ATOM    291  CA  THR A  67      15.544 -57.851 -23.096  1.00 22.47           C  
ANISOU  291  CA  THR A  67     2339   3019   3179    248    441   -534       C  
ATOM    292  C   THR A  67      15.070 -56.909 -21.996  1.00 22.83           C  
ANISOU  292  C   THR A  67     2381   3085   3209    226    444   -524       C  
ATOM    293  O   THR A  67      14.213 -57.291 -21.190  1.00 22.71           O  
ANISOU  293  O   THR A  67     2346   3099   3183    237    375   -488       O  
ATOM    294  CB  THR A  67      14.438 -58.013 -24.146  1.00 22.98           C  
ANISOU  294  CB  THR A  67     2481   3058   3194    295    431   -494       C  
ATOM    295  CG2 THR A  67      14.177 -56.688 -24.896  1.00 24.10           C  
ANISOU  295  CG2 THR A  67     2711   3157   3290    302    517   -495       C  
ATOM    296  OG1 THR A  67      14.837 -59.024 -25.096  1.00 24.12           O  
ANISOU  296  OG1 THR A  67     2628   3185   3352    315    419   -502       O  
ATOM    297  N   VAL A  68      15.635 -55.713 -21.940  1.00 22.08           N  
ANISOU  297  N   VAL A  68     2305   2971   3114    193    526   -556       N  
ATOM    298  CA  VAL A  68      15.237 -54.714 -20.946  1.00 22.10           C  
ANISOU  298  CA  VAL A  68     2312   2987   3099    169    541   -548       C  
ATOM    299  C   VAL A  68      14.421 -53.627 -21.627  1.00 22.94           C  
ANISOU  299  C   VAL A  68     2514   3054   3148    189    605   -524       C  
ATOM    300  O   VAL A  68      14.847 -53.097 -22.653  1.00 23.68           O  
ANISOU  300  O   VAL A  68     2663   3104   3230    192    685   -545       O  
ATOM    301  CB  VAL A  68      16.469 -54.110 -20.242  1.00 22.86           C  
ANISOU  301  CB  VAL A  68     2358   3094   3236    113    586   -606       C  
ATOM    302  CG1 VAL A  68      16.078 -52.925 -19.338  1.00 23.23           C  
ANISOU  302  CG1 VAL A  68     2425   3144   3256     85    617   -602       C  
ATOM    303  CG2 VAL A  68      17.212 -55.187 -19.449  1.00 23.10           C  
ANISOU  303  CG2 VAL A  68     2291   3168   3317    102    509   -628       C  
ATOM    304  N   TYR A  69      13.249 -53.321 -21.085  1.00 21.42           N  
ANISOU  304  N   TYR A  69     2344   2875   2921    207    574   -480       N  
ATOM    305  CA  TYR A  69      12.353 -52.259 -21.551  1.00 22.24           C  
ANISOU  305  CA  TYR A  69     2534   2948   2969    233    626   -452       C  
ATOM    306  C   TYR A  69      12.365 -51.179 -20.481  1.00 22.68           C  
ANISOU  306  C   TYR A  69     2589   3010   3019    195    665   -458       C  
ATOM    307  O   TYR A  69      12.273 -51.484 -19.282  1.00 21.43           O  
ANISOU  307  O   TYR A  69     2371   2890   2881    173    610   -453       O  
ATOM    308  CB  TYR A  69      10.921 -52.797 -21.698  1.00 21.49           C  
ANISOU  308  CB  TYR A  69     2456   2866   2843    286    553   -397       C  
ATOM    309  CG  TYR A  69      10.793 -53.902 -22.724  1.00 20.91           C  
ANISOU  309  CG  TYR A  69     2386   2788   2771    323    507   -389       C  
ATOM    310  CD1 TYR A  69      11.046 -55.230 -22.388  1.00 21.72           C  
ANISOU  310  CD1 TYR A  69     2418   2922   2915    317    431   -392       C  
ATOM    311  CD2 TYR A  69      10.474 -53.617 -24.045  1.00 21.69           C  
ANISOU  311  CD2 TYR A  69     2565   2848   2829    365    542   -382       C  
ATOM    312  CE1 TYR A  69      10.926 -56.249 -23.329  1.00 22.10           C  
ANISOU  312  CE1 TYR A  69     2472   2962   2963    349    392   -386       C  
ATOM    313  CE2 TYR A  69      10.368 -54.624 -24.998  1.00 22.95           C  
ANISOU  313  CE2 TYR A  69     2732   3000   2986    397    500   -377       C  
ATOM    314  CZ  TYR A  69      10.606 -55.943 -24.642  1.00 23.58           C  
ANISOU  314  CZ  TYR A  69     2738   3112   3110    387    427   -380       C  
ATOM    315  OH  TYR A  69      10.510 -56.941 -25.597  1.00 26.23           O  
ANISOU  315  OH  TYR A  69     3085   3438   3443    416    389   -376       O  
ATOM    316  N   TYR A  70      12.433 -49.899 -20.884  1.00 23.02           N  
ANISOU  316  N   TYR A  70     2705   3013   3030    188    762   -469       N  
ATOM    317  CA  TYR A  70      12.488 -48.820 -19.910  1.00 23.85           C  
ANISOU  317  CA  TYR A  70     2816   3120   3127    148    809   -478       C  
ATOM    318  C   TYR A  70      11.834 -47.556 -20.402  1.00 24.48           C  
ANISOU  318  C   TYR A  70     2996   3156   3149    171    892   -457       C  
ATOM    319  O   TYR A  70      11.816 -47.297 -21.610  1.00 24.76           O  
ANISOU  319  O   TYR A  70     3104   3149   3155    204    943   -457       O  
ATOM    320  CB  TYR A  70      13.939 -48.576 -19.467  1.00 25.18           C  
ANISOU  320  CB  TYR A  70     2933   3291   3343     82    854   -544       C  
ATOM    321  CG  TYR A  70      14.819 -48.070 -20.587  1.00 27.16           C  
ANISOU  321  CG  TYR A  70     3230   3493   3597     70    955   -587       C  
ATOM    322  CD1 TYR A  70      15.422 -48.951 -21.475  1.00 28.93           C  
ANISOU  322  CD1 TYR A  70     3434   3709   3848     83    943   -606       C  
ATOM    323  CD2 TYR A  70      15.052 -46.706 -20.758  1.00 29.40           C  
ANISOU  323  CD2 TYR A  70     3583   3733   3855     44   1069   -609       C  
ATOM    324  CE1 TYR A  70      16.214 -48.490 -22.523  1.00 30.94           C  
ANISOU  324  CE1 TYR A  70     3738   3912   4106     73   1042   -645       C  
ATOM    325  CE2 TYR A  70      15.849 -46.238 -21.799  1.00 31.13           C  
ANISOU  325  CE2 TYR A  70     3853   3900   4077     32   1171   -650       C  
ATOM    326  CZ  TYR A  70      16.449 -47.136 -22.661  1.00 32.49           C  
ANISOU  326  CZ  TYR A  70     4003   4064   4278     45   1158   -669       C  
ATOM    327  OH  TYR A  70      17.226 -46.693 -23.716  1.00 35.99           O  
ANISOU  327  OH  TYR A  70     4501   4449   4724     34   1265   -709       O  
ATOM    328  N   PRO A  71      11.298 -46.761 -19.467  1.00 23.65           N  
ANISOU  328  N   PRO A  71     2904   3058   3024    157    906   -439       N  
ATOM    329  CA  PRO A  71      10.644 -45.503 -19.854  1.00 25.06           C  
ANISOU  329  CA  PRO A  71     3182   3194   3145    182    988   -417       C  
ATOM    330  C   PRO A  71      11.612 -44.322 -19.904  1.00 28.43           C  
ANISOU  330  C   PRO A  71     3654   3581   3569    131   1110   -466       C  
ATOM    331  O   PRO A  71      12.594 -44.278 -19.168  1.00 28.01           O  
ANISOU  331  O   PRO A  71     3540   3543   3558     65   1122   -513       O  
ATOM    332  CB  PRO A  71       9.661 -45.271 -18.699  1.00 24.26           C  
ANISOU  332  CB  PRO A  71     3066   3121   3031    185    946   -377       C  
ATOM    333  CG  PRO A  71      10.402 -45.796 -17.502  1.00 24.34           C  
ANISOU  333  CG  PRO A  71     2984   3172   3093    125    899   -407       C  
ATOM    334  CD  PRO A  71      11.218 -46.978 -18.001  1.00 22.25           C  
ANISOU  334  CD  PRO A  71     2657   2924   2872    121    849   -436       C  
ATOM    335  N   THR A  72      11.288 -43.329 -20.732  1.00 30.70           N  
ANISOU  335  N   THR A  72     4049   3815   3803    162   1200   -454       N  
ATOM    336  CA  THR A  72      12.065 -42.090 -20.809  1.00 32.42           C  
ANISOU  336  CA  THR A  72     4326   3984   4009    116   1330   -497       C  
ATOM    337  C   THR A  72      11.417 -41.024 -19.943  1.00 33.35           C  
ANISOU  337  C   THR A  72     4483   4096   4092    106   1369   -474       C  
ATOM    338  O   THR A  72      10.199 -40.809 -20.025  1.00 33.22           O  
ANISOU  338  O   THR A  72     4516   4078   4029    168   1345   -416       O  
ATOM    339  CB  THR A  72      12.143 -41.585 -22.280  1.00 34.10           C  
ANISOU  339  CB  THR A  72     4650   4130   4177    158   1421   -500       C  
ATOM    340  CG2 THR A  72      12.922 -40.282 -22.412  1.00 35.26           C  
ANISOU  340  CG2 THR A  72     4869   4219   4310    110   1569   -545       C  
ATOM    341  OG1 THR A  72      12.684 -42.588 -23.127  1.00 36.42           O  
ANISOU  341  OG1 THR A  72     4914   4425   4500    170   1387   -518       O  
ATOM    342  N   ASN A  73      12.213 -40.341 -19.106  1.00 33.30           N  
ANISOU  342  N   ASN A  73     4456   4089   4109     30   1428   -520       N  
ATOM    343  CA  ASN A  73      11.739 -39.251 -18.260  1.00 34.09           C  
ANISOU  343  CA  ASN A  73     4599   4177   4176     11   1479   -505       C  
ATOM    344  C   ASN A  73      10.505 -39.613 -17.432  1.00 33.44           C  
ANISOU  344  C   ASN A  73     4490   4136   4080     49   1384   -443       C  
ATOM    345  O   ASN A  73       9.506 -38.874 -17.425  1.00 34.49           O  
ANISOU  345  O   ASN A  73     4696   4248   4162     91   1415   -397       O  
ATOM    346  CB  ASN A  73      11.508 -37.966 -19.068  1.00 36.11           C  
ANISOU  346  CB  ASN A  73     4989   4362   4370     37   1609   -497       C  
ATOM    347  CG  ASN A  73      11.521 -36.704 -18.235  1.00 39.38           C  
ANISOU  347  CG  ASN A  73     5448   4752   4761    -10   1697   -508       C  
ATOM    348  ND2 ASN A  73      11.224 -35.561 -18.840  1.00 40.52           N  
ANISOU  348  ND2 ASN A  73     5717   4834   4847     17   1811   -496       N  
ATOM    349  OD1 ASN A  73      11.772 -36.736 -17.023  1.00 40.31           O  
ANISOU  349  OD1 ASN A  73     5498   4908   4911    -68   1664   -526       O  
ATOM    350  N   ALA A  74      10.595 -40.717 -16.674  1.00 31.63           N  
ANISOU  350  N   ALA A  74     4156   3964   3898     32   1273   -443       N  
ATOM    351  CA  ALA A  74       9.480 -41.120 -15.812  1.00 30.57           C  
ANISOU  351  CA  ALA A  74     3993   3867   3758     60   1188   -389       C  
ATOM    352  C   ALA A  74       9.205 -40.165 -14.640  1.00 30.50           C  
ANISOU  352  C   ALA A  74     4006   3854   3730     23   1229   -383       C  
ATOM    353  O   ALA A  74       8.140 -40.245 -14.028  1.00 28.97           O  
ANISOU  353  O   ALA A  74     3811   3675   3520     53   1184   -333       O  
ATOM    354  CB  ALA A  74       9.699 -42.539 -15.306  1.00 30.03           C  
ANISOU  354  CB  ALA A  74     3818   3853   3740     51   1069   -394       C  
ATOM    355  N   GLY A  75      10.126 -39.254 -14.344  1.00 30.75           N  
ANISOU  355  N   GLY A  75     4059   3862   3764    -41   1318   -433       N  
ATOM    356  CA  GLY A  75       9.957 -38.304 -13.245  1.00 31.18           C  
ANISOU  356  CA  GLY A  75     4140   3909   3799    -83   1364   -433       C  
ATOM    357  C   GLY A  75      10.724 -38.650 -11.980  1.00 31.36           C  
ANISOU  357  C   GLY A  75     4080   3973   3864   -154   1314   -475       C  
ATOM    358  O   GLY A  75      10.640 -37.948 -10.979  1.00 33.53           O  
ANISOU  358  O   GLY A  75     4372   4244   4124   -193   1343   -478       O  
ATOM    359  N   GLY A  76      11.486 -39.735 -12.035  1.00 29.31           N  
ANISOU  359  N   GLY A  76     3733   3750   3654   -168   1239   -508       N  
ATOM    360  CA  GLY A  76      12.274 -40.229 -10.918  1.00 27.92           C  
ANISOU  360  CA  GLY A  76     3472   3617   3518   -225   1176   -550       C  
ATOM    361  C   GLY A  76      12.644 -41.683 -11.156  1.00 25.85           C  
ANISOU  361  C   GLY A  76     3124   3397   3302   -204   1072   -556       C  
ATOM    362  O   GLY A  76      12.305 -42.239 -12.197  1.00 25.69           O  
ANISOU  362  O   GLY A  76     3112   3368   3280   -152   1056   -530       O  
ATOM    363  N   THR A  77      13.343 -42.300 -10.192  1.00 24.93           N  
ANISOU  363  N   THR A  77     2927   3323   3221   -242   1000   -591       N  
ATOM    364  CA  THR A  77      13.696 -43.714 -10.328  1.00 24.69           C  
ANISOU  364  CA  THR A  77     2817   3332   3232   -219    900   -595       C  
ATOM    365  C   THR A  77      12.429 -44.563 -10.262  1.00 23.35           C  
ANISOU  365  C   THR A  77     2654   3175   3045   -155    822   -521       C  
ATOM    366  O   THR A  77      11.447 -44.177  -9.627  1.00 22.93           O  
ANISOU  366  O   THR A  77     2640   3114   2958   -143    822   -476       O  
ATOM    367  CB  THR A  77      14.725 -44.110  -9.282  1.00 26.86           C  
ANISOU  367  CB  THR A  77     3012   3649   3544   -268    842   -650       C  
ATOM    368  CG2 THR A  77      16.084 -43.433  -9.518  1.00 27.82           C  
ANISOU  368  CG2 THR A  77     3110   3764   3698   -331    913   -735       C  
ATOM    369  OG1 THR A  77      14.196 -43.825  -7.982  1.00 26.79           O  
ANISOU  369  OG1 THR A  77     3017   3651   3509   -283    813   -628       O  
ATOM    370  N   VAL A  78      12.436 -45.712 -10.960  1.00 22.99           N  
ANISOU  370  N   VAL A  78     2569   3144   3022   -115    760   -510       N  
ATOM    371  CA  VAL A  78      11.255 -46.579 -10.979  1.00 22.20           C  
ANISOU  371  CA  VAL A  78     2470   3055   2911    -58    689   -446       C  
ATOM    372  C   VAL A  78      11.629 -48.008 -10.560  1.00 21.59           C  
ANISOU  372  C   VAL A  78     2316   3018   2871    -51    584   -452       C  
ATOM    373  O   VAL A  78      12.798 -48.384 -10.596  1.00 22.18           O  
ANISOU  373  O   VAL A  78     2338   3110   2981    -76    569   -504       O  
ATOM    374  CB  VAL A  78      10.582 -46.585 -12.382  1.00 21.90           C  
ANISOU  374  CB  VAL A  78     2479   2988   2853     -4    717   -414       C  
ATOM    375  CG1 VAL A  78      10.070 -45.181 -12.740  1.00 22.76           C  
ANISOU  375  CG1 VAL A  78     2675   3055   2917      0    817   -399       C  
ATOM    376  CG2 VAL A  78      11.535 -47.122 -13.461  1.00 23.08           C  
ANISOU  376  CG2 VAL A  78     2603   3135   3033     -2    722   -453       C  
ATOM    377  N   GLY A  79      10.626 -48.787 -10.183  1.00 20.28           N  
ANISOU  377  N   GLY A  79     2145   2864   2698    -14    518   -401       N  
ATOM    378  CA  GLY A  79      10.858 -50.175  -9.814  1.00 20.30           C  
ANISOU  378  CA  GLY A  79     2087   2898   2730      0    424   -401       C  
ATOM    379  C   GLY A  79      11.198 -51.051 -11.006  1.00 20.19           C  
ANISOU  379  C   GLY A  79     2047   2885   2740     29    403   -409       C  
ATOM    380  O   GLY A  79      10.949 -50.684 -12.160  1.00 20.37           O  
ANISOU  380  O   GLY A  79     2107   2883   2750     49    451   -402       O  
ATOM    381  N   ALA A  80      11.716 -52.263 -10.731  1.00 18.88           N  
ANISOU  381  N   ALA A  80     1823   2746   2603     36    328   -421       N  
ATOM    382  CA  ALA A  80      12.081 -53.215 -11.792  1.00 19.29           C  
ANISOU  382  CA  ALA A  80     1849   2800   2681     63    303   -429       C  
ATOM    383  C   ALA A  80      11.273 -54.498 -11.668  1.00 18.82           C  
ANISOU  383  C   ALA A  80     1775   2751   2623    102    225   -387       C  
ATOM    384  O   ALA A  80      11.001 -54.946 -10.546  1.00 18.26           O  
ANISOU  384  O   ALA A  80     1690   2697   2551    100    175   -371       O  
ATOM    385  CB  ALA A  80      13.577 -53.547 -11.730  1.00 20.14           C  
ANISOU  385  CB  ALA A  80     1898   2928   2828     37    291   -489       C  
ATOM    386  N   ILE A  81      10.866 -55.069 -12.806  1.00 18.45           N  
ANISOU  386  N   ILE A  81     1739   2694   2579    137    219   -369       N  
ATOM    387  CA  ILE A  81      10.093 -56.315 -12.820  1.00 17.61           C  
ANISOU  387  CA  ILE A  81     1620   2595   2477    171    151   -334       C  
ATOM    388  C   ILE A  81      10.799 -57.309 -13.727  1.00 18.48           C  
ANISOU  388  C   ILE A  81     1701   2707   2613    187    127   -354       C  
ATOM    389  O   ILE A  81      11.189 -56.939 -14.836  1.00 18.64           O  
ANISOU  389  O   ILE A  81     1739   2710   2634    191    173   -373       O  
ATOM    390  CB  ILE A  81       8.657 -56.032 -13.357  1.00 17.13           C  
ANISOU  390  CB  ILE A  81     1604   2516   2389    201    165   -289       C  
ATOM    391  CG1 ILE A  81       7.944 -54.987 -12.484  1.00 18.79           C  
ANISOU  391  CG1 ILE A  81     1844   2720   2574    187    197   -268       C  
ATOM    392  CG2 ILE A  81       7.813 -57.325 -13.440  1.00 17.18           C  
ANISOU  392  CG2 ILE A  81     1593   2529   2404    231     99   -258       C  
ATOM    393  CD1 ILE A  81       6.650 -54.468 -13.144  1.00 19.62           C  
ANISOU  393  CD1 ILE A  81     1994   2808   2654    219    223   -231       C  
ATOM    394  N   ALA A  82      10.917 -58.580 -13.286  1.00 17.81           N  
ANISOU  394  N   ALA A  82     1580   2640   2548    200     59   -349       N  
ATOM    395  CA  ALA A  82      11.529 -59.643 -14.094  1.00 18.29           C  
ANISOU  395  CA  ALA A  82     1615   2701   2634    218     33   -364       C  
ATOM    396  C   ALA A  82      10.447 -60.653 -14.459  1.00 18.25           C  
ANISOU  396  C   ALA A  82     1622   2690   2622    251    -10   -325       C  
ATOM    397  O   ALA A  82       9.702 -61.114 -13.590  1.00 18.43           O  
ANISOU  397  O   ALA A  82     1644   2719   2639    255    -48   -297       O  
ATOM    398  CB  ALA A  82      12.659 -60.326 -13.333  1.00 18.93           C  
ANISOU  398  CB  ALA A  82     1644   2806   2743    210     -8   -395       C  
ATOM    399  N   ILE A  83      10.351 -60.991 -15.765  1.00 16.47           N  
ANISOU  399  N   ILE A  83     1412   2449   2397    272      0   -325       N  
ATOM    400  CA  ILE A  83       9.277 -61.862 -16.268  1.00 16.94           C  
ANISOU  400  CA  ILE A  83     1485   2501   2449    300    -37   -293       C  
ATOM    401  C   ILE A  83       9.865 -63.093 -16.917  1.00 17.20           C  
ANISOU  401  C   ILE A  83     1499   2532   2504    315    -67   -306       C  
ATOM    402  O   ILE A  83      10.760 -62.982 -17.760  1.00 17.67           O  
ANISOU  402  O   ILE A  83     1559   2583   2573    315    -37   -334       O  
ATOM    403  CB  ILE A  83       8.389 -61.097 -17.255  1.00 17.50           C  
ANISOU  403  CB  ILE A  83     1602   2554   2492    317     -2   -278       C  
ATOM    404  CG1 ILE A  83       7.995 -59.699 -16.680  1.00 18.46           C  
ANISOU  404  CG1 ILE A  83     1748   2675   2592    302     42   -269       C  
ATOM    405  CG2 ILE A  83       7.142 -61.922 -17.598  1.00 17.58           C  
ANISOU  405  CG2 ILE A  83     1619   2564   2498    342    -46   -248       C  
ATOM    406  CD1 ILE A  83       6.948 -58.921 -17.472  1.00 19.09           C  
ANISOU  406  CD1 ILE A  83     1875   2739   2640    327     70   -248       C  
ATOM    407  N   VAL A  84       9.346 -64.270 -16.540  1.00 16.37           N  
ANISOU  407  N   VAL A  84     1381   2432   2406    327   -119   -286       N  
ATOM    408  CA  VAL A  84       9.889 -65.566 -17.000  1.00 17.45           C  
ANISOU  408  CA  VAL A  84     1500   2566   2563    342   -150   -296       C  
ATOM    409  C   VAL A  84       8.825 -66.383 -17.717  1.00 18.10           C  
ANISOU  409  C   VAL A  84     1603   2636   2637    361   -176   -274       C  
ATOM    410  O   VAL A  84       7.711 -66.512 -17.222  1.00 17.68           O  
ANISOU  410  O   VAL A  84     1555   2584   2576    361   -195   -249       O  
ATOM    411  CB  VAL A  84      10.456 -66.359 -15.791  1.00 19.37           C  
ANISOU  411  CB  VAL A  84     1712   2825   2824    340   -191   -299       C  
ATOM    412  CG1 VAL A  84      11.154 -67.656 -16.255  1.00 18.84           C  
ANISOU  412  CG1 VAL A  84     1629   2754   2777    359   -217   -310       C  
ATOM    413  CG2 VAL A  84      11.417 -65.516 -14.969  1.00 20.72           C  
ANISOU  413  CG2 VAL A  84     1860   3013   3001    320   -174   -324       C  
ATOM    414  N   PRO A  85       9.151 -66.972 -18.870  1.00 17.81           N  
ANISOU  414  N   PRO A  85     1576   2585   2605    376   -175   -285       N  
ATOM    415  CA  PRO A  85       8.161 -67.825 -19.569  1.00 18.03           C  
ANISOU  415  CA  PRO A  85     1622   2603   2626    392   -203   -269       C  
ATOM    416  C   PRO A  85       8.052 -69.223 -18.928  1.00 18.19           C  
ANISOU  416  C   PRO A  85     1623   2624   2663    393   -247   -260       C  
ATOM    417  O   PRO A  85       8.686 -69.497 -17.896  1.00 17.84           O  
ANISOU  417  O   PRO A  85     1556   2590   2633    388   -258   -262       O  
ATOM    418  CB  PRO A  85       8.737 -67.941 -20.990  1.00 19.18           C  
ANISOU  418  CB  PRO A  85     1790   2729   2767    405   -182   -288       C  
ATOM    419  CG  PRO A  85      10.213 -67.764 -20.817  1.00 19.61           C  
ANISOU  419  CG  PRO A  85     1824   2786   2843    397   -155   -315       C  
ATOM    420  CD  PRO A  85      10.424 -66.871 -19.609  1.00 17.70           C  
ANISOU  420  CD  PRO A  85     1559   2563   2604    377   -144   -316       C  
ATOM    421  N   GLY A  86       7.217 -70.080 -19.526  1.00 18.09           N  
ANISOU  421  N   GLY A  86     1623   2601   2649    402   -271   -251       N  
ATOM    422  CA  GLY A  86       7.009 -71.443 -19.060  1.00 18.37           C  
ANISOU  422  CA  GLY A  86     1651   2631   2699    403   -304   -243       C  
ATOM    423  C   GLY A  86       7.881 -72.471 -19.752  1.00 19.29           C  
ANISOU  423  C   GLY A  86     1770   2733   2825    415   -310   -258       C  
ATOM    424  O   GLY A  86       8.718 -72.144 -20.606  1.00 19.29           O  
ANISOU  424  O   GLY A  86     1777   2728   2824    423   -287   -276       O  
ATOM    425  N   TYR A  87       7.672 -73.733 -19.388  1.00 19.25           N  
ANISOU  425  N   TYR A  87     1766   2719   2829    418   -335   -250       N  
ATOM    426  CA  TYR A  87       8.371 -74.901 -19.938  1.00 19.21           C  
ANISOU  426  CA  TYR A  87     1768   2697   2834    431   -342   -260       C  
ATOM    427  C   TYR A  87       8.226 -74.907 -21.467  1.00 19.38           C  
ANISOU  427  C   TYR A  87     1813   2704   2845    437   -332   -272       C  
ATOM    428  O   TYR A  87       7.114 -74.773 -21.978  1.00 19.91           O  
ANISOU  428  O   TYR A  87     1896   2770   2900    431   -341   -268       O  
ATOM    429  CB  TYR A  87       7.705 -76.130 -19.328  1.00 20.11           C  
ANISOU  429  CB  TYR A  87     1890   2798   2952    429   -366   -246       C  
ATOM    430  CG  TYR A  87       8.403 -77.454 -19.565  1.00 21.15           C  
ANISOU  430  CG  TYR A  87     2033   2911   3093    445   -373   -251       C  
ATOM    431  CD1 TYR A  87       9.540 -77.800 -18.844  1.00 22.41           C  
ANISOU  431  CD1 TYR A  87     2179   3075   3261    464   -377   -254       C  
ATOM    432  CD2 TYR A  87       7.838 -78.414 -20.391  1.00 21.94           C  
ANISOU  432  CD2 TYR A  87     2157   2989   3191    442   -378   -254       C  
ATOM    433  CE1 TYR A  87      10.111 -79.071 -18.963  1.00 23.64           C  
ANISOU  433  CE1 TYR A  87     2348   3211   3423    484   -383   -255       C  
ATOM    434  CE2 TYR A  87       8.419 -79.671 -20.543  1.00 22.46           C  
ANISOU  434  CE2 TYR A  87     2238   3033   3263    456   -381   -256       C  
ATOM    435  CZ  TYR A  87       9.559 -79.986 -19.841  1.00 23.91           C  
ANISOU  435  CZ  TYR A  87     2410   3219   3454    479   -381   -256       C  
ATOM    436  OH  TYR A  87      10.100 -81.253 -20.020  1.00 25.48           O  
ANISOU  436  OH  TYR A  87     2628   3395   3657    498   -382   -256       O  
ATOM    437  N   THR A  88       9.361 -75.076 -22.179  1.00 19.88           N  
ANISOU  437  N   THR A  88     1881   2757   2915    449   -313   -289       N  
ATOM    438  CA  THR A  88       9.543 -75.067 -23.644  1.00 20.68           C  
ANISOU  438  CA  THR A  88     2014   2839   3006    458   -295   -303       C  
ATOM    439  C   THR A  88       9.453 -73.692 -24.286  1.00 21.87           C  
ANISOU  439  C   THR A  88     2180   2991   3137    457   -266   -311       C  
ATOM    440  O   THR A  88       9.669 -73.573 -25.500  1.00 23.17           O  
ANISOU  440  O   THR A  88     2380   3136   3288    467   -245   -323       O  
ATOM    441  CB  THR A  88       8.576 -76.024 -24.414  1.00 22.45           C  
ANISOU  441  CB  THR A  88     2267   3044   3217    458   -319   -300       C  
ATOM    442  CG2 THR A  88       8.482 -77.389 -23.786  1.00 23.28           C  
ANISOU  442  CG2 THR A  88     2367   3142   3338    456   -342   -292       C  
ATOM    443  OG1 THR A  88       7.262 -75.433 -24.546  1.00 23.11           O  
ANISOU  443  OG1 THR A  88     2359   3140   3284    450   -335   -293       O  
ATOM    444  N   ALA A  89       9.052 -72.665 -23.521  1.00 20.41           N  
ANISOU  444  N   ALA A  89     1980   2828   2948    447   -262   -302       N  
ATOM    445  CA  ALA A  89       8.750 -71.360 -24.087  1.00 21.21           C  
ANISOU  445  CA  ALA A  89     2104   2928   3025    449   -234   -304       C  
ATOM    446  C   ALA A  89       9.872 -70.334 -23.929  1.00 20.98           C  
ANISOU  446  C   ALA A  89     2066   2902   3004    444   -187   -321       C  
ATOM    447  O   ALA A  89      10.838 -70.545 -23.177  1.00 20.86           O  
ANISOU  447  O   ALA A  89     2014   2896   3016    436   -183   -331       O  
ATOM    448  CB  ALA A  89       7.426 -70.848 -23.500  1.00 21.33           C  
ANISOU  448  CB  ALA A  89     2114   2961   3028    443   -256   -285       C  
ATOM    449  N   ARG A  90       9.779 -69.230 -24.702  1.00 20.20           N  
ANISOU  449  N   ARG A  90     2003   2791   2881    449   -149   -327       N  
ATOM    450  CA  ARG A  90      10.786 -68.201 -24.721  1.00 20.60           C  
ANISOU  450  CA  ARG A  90     2054   2837   2937    440    -93   -347       C  
ATOM    451  C   ARG A  90      10.174 -66.815 -24.459  1.00 20.26           C  
ANISOU  451  C   ARG A  90     2028   2801   2869    435    -69   -338       C  
ATOM    452  O   ARG A  90       8.975 -66.694 -24.146  1.00 20.75           O  
ANISOU  452  O   ARG A  90     2095   2876   2914    440   -100   -315       O  
ATOM    453  CB  ARG A  90      11.502 -68.239 -26.094  1.00 22.01           C  
ANISOU  453  CB  ARG A  90     2274   2981   3109    452    -51   -368       C  
ATOM    454  CG  ARG A  90      12.316 -69.528 -26.253  1.00 26.78           C  
ANISOU  454  CG  ARG A  90     2856   3577   3744    456    -65   -380       C  
ATOM    455  CD  ARG A  90      13.049 -69.577 -27.581  1.00 32.07           C  
ANISOU  455  CD  ARG A  90     3568   4208   4409    467    -17   -401       C  
ATOM    456  NE  ARG A  90      14.060 -70.642 -27.574  1.00 38.07           N  
ANISOU  456  NE  ARG A  90     4297   4962   5206    468    -18   -416       N  
ATOM    457  CZ  ARG A  90      13.817 -71.911 -27.890  1.00 40.17           C  
ANISOU  457  CZ  ARG A  90     4571   5219   5472    481    -55   -406       C  
ATOM    458  NH1 ARG A  90      12.598 -72.291 -28.249  1.00 40.56           N1+
ANISOU  458  NH1 ARG A  90     4655   5266   5489    489    -95   -385       N1+
ATOM    459  NH2 ARG A  90      14.789 -72.810 -27.849  1.00 40.06           N  
ANISOU  459  NH2 ARG A  90     4530   5198   5492    485    -51   -419       N  
ATOM    460  N   GLN A  91      10.993 -65.765 -24.568  1.00 19.34           N  
ANISOU  460  N   GLN A  91     1921   2675   2753    424     -9   -358       N  
ATOM    461  CA  GLN A  91      10.540 -64.392 -24.311  1.00 20.50           C  
ANISOU  461  CA  GLN A  91     2091   2824   2876    419     25   -352       C  
ATOM    462  C   GLN A  91       9.313 -64.013 -25.108  1.00 19.98           C  
ANISOU  462  C   GLN A  91     2080   2746   2765    447     17   -330       C  
ATOM    463  O   GLN A  91       8.455 -63.302 -24.597  1.00 19.69           O  
ANISOU  463  O   GLN A  91     2047   2723   2712    449     12   -312       O  
ATOM    464  CB  GLN A  91      11.645 -63.373 -24.620  1.00 21.33           C  
ANISOU  464  CB  GLN A  91     2211   2908   2984    403    102   -383       C  
ATOM    465  CG  GLN A  91      12.805 -63.429 -23.676  1.00 21.77           C  
ANISOU  465  CG  GLN A  91     2204   2982   3084    373    111   -409       C  
ATOM    466  CD  GLN A  91      13.851 -62.418 -24.058  1.00 23.19           C  
ANISOU  466  CD  GLN A  91     2397   3141   3272    353    193   -446       C  
ATOM    467  NE2 GLN A  91      15.027 -62.908 -24.453  1.00 24.06           N  
ANISOU  467  NE2 GLN A  91     2482   3240   3418    346    216   -479       N  
ATOM    468  OE1 GLN A  91      13.631 -61.202 -24.006  1.00 23.75           O  
ANISOU  468  OE1 GLN A  91     2500   3202   3320    344    241   -447       O  
ATOM    469  N   SER A  92       9.194 -64.500 -26.367  1.00 20.38           N  
ANISOU  469  N   SER A  92     2174   2772   2796    473     13   -334       N  
ATOM    470  CA  SER A  92       8.054 -64.106 -27.200  1.00 21.28           C  
ANISOU  470  CA  SER A  92     2343   2876   2864    506      1   -318       C  
ATOM    471  C   SER A  92       6.698 -64.344 -26.522  1.00 20.75           C  
ANISOU  471  C   SER A  92     2248   2841   2797    511    -61   -292       C  
ATOM    472  O   SER A  92       5.799 -63.510 -26.645  1.00 21.71           O  
ANISOU  472  O   SER A  92     2396   2966   2888    532    -60   -278       O  
ATOM    473  CB  SER A  92       8.105 -64.849 -28.541  1.00 24.37           C  
ANISOU  473  CB  SER A  92     2781   3240   3237    531    -10   -327       C  
ATOM    474  OG  SER A  92       6.909 -64.621 -29.274  1.00 29.85           O  
ANISOU  474  OG  SER A  92     3521   3932   3887    567    -40   -313       O  
ATOM    475  N   SER A  93       6.573 -65.453 -25.757  1.00 19.64           N  
ANISOU  475  N   SER A  93     2052   2722   2691    493   -110   -287       N  
ATOM    476  CA  SER A  93       5.299 -65.784 -25.116  1.00 19.32           C  
ANISOU  476  CA  SER A  93     1981   2705   2655    494   -161   -267       C  
ATOM    477  C   SER A  93       4.864 -64.787 -24.047  1.00 19.51           C  
ANISOU  477  C   SER A  93     1987   2747   2679    483   -146   -251       C  
ATOM    478  O   SER A  93       3.678 -64.705 -23.756  1.00 20.03           O  
ANISOU  478  O   SER A  93     2043   2828   2741    491   -175   -234       O  
ATOM    479  CB  SER A  93       5.365 -67.175 -24.495  1.00 20.65           C  
ANISOU  479  CB  SER A  93     2104   2884   2858    475   -204   -266       C  
ATOM    480  OG  SER A  93       6.283 -67.222 -23.414  1.00 20.35           O  
ANISOU  480  OG  SER A  93     2030   2855   2849    450   -188   -269       O  
ATOM    481  N   ILE A  94       5.799 -64.064 -23.441  1.00 18.99           N  
ANISOU  481  N   ILE A  94     1915   2679   2620    463   -100   -258       N  
ATOM    482  CA  ILE A  94       5.439 -63.102 -22.369  1.00 18.85           C  
ANISOU  482  CA  ILE A  94     1885   2676   2602    449    -82   -244       C  
ATOM    483  C   ILE A  94       5.891 -61.661 -22.669  1.00 19.81           C  
ANISOU  483  C   ILE A  94     2049   2782   2697    451    -15   -252       C  
ATOM    484  O   ILE A  94       5.700 -60.779 -21.828  1.00 20.28           O  
ANISOU  484  O   ILE A  94     2104   2849   2753    438      9   -242       O  
ATOM    485  CB  ILE A  94       6.013 -63.583 -20.994  1.00 20.55           C  
ANISOU  485  CB  ILE A  94     2049   2908   2852    416    -95   -245       C  
ATOM    486  CG1 ILE A  94       7.501 -63.969 -21.096  1.00 23.30           C  
ANISOU  486  CG1 ILE A  94     2382   3250   3221    401    -78   -273       C  
ATOM    487  CG2 ILE A  94       5.210 -64.795 -20.489  1.00 21.16           C  
ANISOU  487  CG2 ILE A  94     2094   2997   2947    415   -153   -230       C  
ATOM    488  CD1 ILE A  94       8.498 -62.886 -21.080  1.00 25.53           C  
ANISOU  488  CD1 ILE A  94     2674   3524   3500    386    -18   -295       C  
ATOM    489  N   LYS A  95       6.462 -61.402 -23.865  1.00 20.38           N  
ANISOU  489  N   LYS A  95     2168   2827   2748    468     21   -269       N  
ATOM    490  CA  LYS A  95       7.073 -60.106 -24.115  1.00 21.48           C  
ANISOU  490  CA  LYS A  95     2350   2945   2867    464     97   -282       C  
ATOM    491  C   LYS A  95       6.105 -58.954 -24.211  1.00 20.11           C  
ANISOU  491  C   LYS A  95     2222   2767   2653    489    119   -261       C  
ATOM    492  O   LYS A  95       6.544 -57.814 -23.990  1.00 21.58           O  
ANISOU  492  O   LYS A  95     2434   2939   2826    476    184   -268       O  
ATOM    493  CB  LYS A  95       7.998 -60.142 -25.323  1.00 26.03           C  
ANISOU  493  CB  LYS A  95     2970   3488   3434    473    139   -307       C  
ATOM    494  CG  LYS A  95       7.314 -60.207 -26.647  1.00 31.95           C  
ANISOU  494  CG  LYS A  95     3783   4215   4141    519    129   -299       C  
ATOM    495  CD  LYS A  95       8.393 -60.080 -27.730  1.00 38.84           C  
ANISOU  495  CD  LYS A  95     4707   5046   5004    522    190   -326       C  
ATOM    496  CE  LYS A  95       7.822 -59.892 -29.101  1.00 45.02           C  
ANISOU  496  CE  LYS A  95     5575   5798   5733    571    194   -320       C  
ATOM    497  NZ  LYS A  95       8.870 -60.078 -30.145  1.00 48.87           N1+
ANISOU  497  NZ  LYS A  95     6110   6243   6217    573    246   -347       N1+
ATOM    498  N   TRP A  96       4.806 -59.197 -24.468  1.00 19.22           N  
ANISOU  498  N   TRP A  96     2114   2665   2522    523     68   -238       N  
ATOM    499  CA  TRP A  96       3.858 -58.059 -24.547  1.00 19.44           C  
ANISOU  499  CA  TRP A  96     2183   2690   2512    553     89   -218       C  
ATOM    500  C   TRP A  96       3.842 -57.221 -23.243  1.00 18.66           C  
ANISOU  500  C   TRP A  96     2061   2603   2424    523    121   -207       C  
ATOM    501  O   TRP A  96       3.599 -56.008 -23.270  1.00 19.03           O  
ANISOU  501  O   TRP A  96     2155   2637   2440    537    171   -198       O  
ATOM    502  CB  TRP A  96       2.430 -58.552 -24.879  1.00 19.89           C  
ANISOU  502  CB  TRP A  96     2230   2766   2559    592     20   -199       C  
ATOM    503  CG  TRP A  96       1.683 -59.168 -23.728  1.00 18.97           C  
ANISOU  503  CG  TRP A  96     2044   2683   2483    570    -29   -184       C  
ATOM    504  CD1 TRP A  96       1.818 -60.443 -23.245  1.00 18.98           C  
ANISOU  504  CD1 TRP A  96     1989   2699   2525    542    -76   -189       C  
ATOM    505  CD2 TRP A  96       0.624 -58.563 -22.979  1.00 18.38           C  
ANISOU  505  CD2 TRP A  96     1952   2623   2407    578    -34   -161       C  
ATOM    506  CE2 TRP A  96       0.184 -59.512 -22.029  1.00 18.62           C  
ANISOU  506  CE2 TRP A  96     1917   2676   2481    550    -80   -155       C  
ATOM    507  CE3 TRP A  96       0.042 -57.281 -22.979  1.00 18.87           C  
ANISOU  507  CE3 TRP A  96     2054   2680   2437    606      3   -145       C  
ATOM    508  NE1 TRP A  96       0.899 -60.663 -22.239  1.00 18.30           N  
ANISOU  508  NE1 TRP A  96     1856   2634   2462    530   -106   -172       N  
ATOM    509  CZ2 TRP A  96      -0.842 -59.243 -21.127  1.00 19.08           C  
ANISOU  509  CZ2 TRP A  96     1945   2750   2553    548    -89   -135       C  
ATOM    510  CZ3 TRP A  96      -0.976 -57.016 -22.081  1.00 19.24           C  
ANISOU  510  CZ3 TRP A  96     2067   2746   2498    606    -10   -124       C  
ATOM    511  CH2 TRP A  96      -1.397 -57.982 -21.158  1.00 19.10           C  
ANISOU  511  CH2 TRP A  96     1982   2749   2526    575    -54   -120       C  
ATOM    512  N   TRP A  97       4.180 -57.863 -22.120  1.00 18.80           N  
ANISOU  512  N   TRP A  97     2017   2643   2485    482     96   -209       N  
ATOM    513  CA  TRP A  97       4.224 -57.168 -20.833  1.00 18.98           C  
ANISOU  513  CA  TRP A  97     2019   2676   2517    451    122   -202       C  
ATOM    514  C   TRP A  97       5.344 -56.127 -20.747  1.00 19.65           C  
ANISOU  514  C   TRP A  97     2133   2741   2593    425    199   -224       C  
ATOM    515  O   TRP A  97       5.226 -55.167 -19.980  1.00 19.43           O  
ANISOU  515  O   TRP A  97     2115   2713   2556    409    237   -217       O  
ATOM    516  CB  TRP A  97       4.468 -58.202 -19.720  1.00 18.32           C  
ANISOU  516  CB  TRP A  97     1869   2615   2476    417     75   -203       C  
ATOM    517  CG  TRP A  97       3.264 -58.981 -19.294  1.00 16.61           C  
ANISOU  517  CG  TRP A  97     1621   2417   2274    428     16   -179       C  
ATOM    518  CD1 TRP A  97       3.095 -60.339 -19.362  1.00 16.59           C  
ANISOU  518  CD1 TRP A  97     1583   2423   2296    428    -41   -180       C  
ATOM    519  CD2 TRP A  97       2.111 -58.462 -18.617  1.00 15.84           C  
ANISOU  519  CD2 TRP A  97     1521   2328   2171    435     14   -153       C  
ATOM    520  CE2 TRP A  97       1.280 -59.563 -18.303  1.00 16.67           C  
ANISOU  520  CE2 TRP A  97     1586   2447   2303    436    -43   -142       C  
ATOM    521  CE3 TRP A  97       1.698 -57.166 -18.261  1.00 16.12           C  
ANISOU  521  CE3 TRP A  97     1586   2357   2183    440     61   -138       C  
ATOM    522  NE1 TRP A  97       1.910 -60.695 -18.746  1.00 16.81           N  
ANISOU  522  NE1 TRP A  97     1586   2464   2336    431    -75   -159       N  
ATOM    523  CZ2 TRP A  97       0.079 -59.414 -17.609  1.00 16.31           C  
ANISOU  523  CZ2 TRP A  97     1522   2409   2264    440    -54   -119       C  
ATOM    524  CZ3 TRP A  97       0.497 -57.015 -17.580  1.00 16.31           C  
ANISOU  524  CZ3 TRP A  97     1594   2391   2213    447     47   -113       C  
ATOM    525  CH2 TRP A  97      -0.305 -58.131 -17.285  1.00 16.60           C  
ANISOU  525  CH2 TRP A  97     1586   2442   2280    448    -10   -104       C  
ATOM    526  N   GLY A  98       6.431 -56.332 -21.504  1.00 19.98           N  
ANISOU  526  N   GLY A  98     2186   2765   2639    418    225   -254       N  
ATOM    527  CA  GLY A  98       7.587 -55.437 -21.449  1.00 20.54           C  
ANISOU  527  CA  GLY A  98     2276   2816   2711    386    302   -284       C  
ATOM    528  C   GLY A  98       7.232 -53.994 -21.764  1.00 20.62           C  
ANISOU  528  C   GLY A  98     2358   2800   2677    401    374   -276       C  
ATOM    529  O   GLY A  98       7.321 -53.101 -20.915  1.00 20.95           O  
ANISOU  529  O   GLY A  98     2401   2843   2716    374    414   -277       O  
ATOM    530  N   PRO A  99       6.780 -53.748 -22.990  1.00 20.53           N  
ANISOU  530  N   PRO A  99     2412   2763   2626    448    390   -268       N  
ATOM    531  CA  PRO A  99       6.372 -52.368 -23.336  1.00 20.99           C  
ANISOU  531  CA  PRO A  99     2549   2792   2635    473    459   -257       C  
ATOM    532  C   PRO A  99       5.147 -51.908 -22.544  1.00 21.06           C  
ANISOU  532  C   PRO A  99     2551   2821   2630    489    435   -220       C  
ATOM    533  O   PRO A  99       5.064 -50.723 -22.182  1.00 22.22           O  
ANISOU  533  O   PRO A  99     2738   2952   2753    484    498   -215       O  
ATOM    534  CB  PRO A  99       6.057 -52.465 -24.841  1.00 22.51           C  
ANISOU  534  CB  PRO A  99     2812   2956   2787    530    460   -253       C  
ATOM    535  CG  PRO A  99       6.645 -53.735 -25.301  1.00 23.66           C  
ANISOU  535  CG  PRO A  99     2918   3107   2963    521    416   -271       C  
ATOM    536  CD  PRO A  99       6.657 -54.665 -24.143  1.00 21.08           C  
ANISOU  536  CD  PRO A  99     2497   2825   2690    484    350   -269       C  
ATOM    537  N   ARG A 100       4.192 -52.814 -22.282  1.00 20.09           N  
ANISOU  537  N   ARG A 100     2380   2730   2524    508    350   -197       N  
ATOM    538  CA  ARG A 100       2.974 -52.428 -21.567  1.00 18.90           C  
ANISOU  538  CA  ARG A 100     2218   2597   2366    526    329   -164       C  
ATOM    539  C   ARG A 100       3.279 -51.879 -20.157  1.00 19.31           C  
ANISOU  539  C   ARG A 100     2243   2658   2437    475    361   -163       C  
ATOM    540  O   ARG A 100       2.862 -50.775 -19.817  1.00 20.02           O  
ANISOU  540  O   ARG A 100     2370   2735   2500    482    410   -148       O  
ATOM    541  CB  ARG A 100       1.974 -53.603 -21.522  1.00 18.93           C  
ANISOU  541  CB  ARG A 100     2167   2632   2393    546    237   -147       C  
ATOM    542  CG  ARG A 100       0.673 -53.292 -20.787  1.00 18.94           C  
ANISOU  542  CG  ARG A 100     2149   2652   2396    563    215   -116       C  
ATOM    543  CD  ARG A 100      -0.081 -52.108 -21.408  1.00 20.12           C  
ANISOU  543  CD  ARG A 100     2366   2784   2494    618    254    -98       C  
ATOM    544  NE  ARG A 100      -1.480 -52.051 -20.963  1.00 20.11           N  
ANISOU  544  NE  ARG A 100     2336   2803   2499    647    217    -70       N  
ATOM    545  CZ  ARG A 100      -2.479 -52.720 -21.535  1.00 20.25           C  
ANISOU  545  CZ  ARG A 100     2329   2842   2524    689    149    -64       C  
ATOM    546  NH1 ARG A 100      -2.250 -53.503 -22.592  1.00 21.44           N1+
ANISOU  546  NH1 ARG A 100     2485   2991   2668    707    108    -82       N1+
ATOM    547  NH2 ARG A 100      -3.715 -52.624 -21.046  1.00 19.75           N  
ANISOU  547  NH2 ARG A 100     2233   2798   2475    710    122    -43       N  
ATOM    548  N   LEU A 101       4.061 -52.613 -19.370  1.00 18.76           N  
ANISOU  548  N   LEU A 101     2114   2606   2408    426    337   -182       N  
ATOM    549  CA  LEU A 101       4.432 -52.139 -18.029  1.00 19.16           C  
ANISOU  549  CA  LEU A 101     2142   2665   2474    378    361   -185       C  
ATOM    550  C   LEU A 101       5.428 -50.972 -18.099  1.00 18.89           C  
ANISOU  550  C   LEU A 101     2151   2603   2422    349    451   -213       C  
ATOM    551  O   LEU A 101       5.260 -49.984 -17.366  1.00 19.57           O  
ANISOU  551  O   LEU A 101     2259   2682   2493    332    497   -206       O  
ATOM    552  CB  LEU A 101       5.051 -53.291 -17.236  1.00 19.32           C  
ANISOU  552  CB  LEU A 101     2091   2710   2539    342    305   -200       C  
ATOM    553  CG  LEU A 101       4.034 -54.268 -16.686  1.00 19.90           C  
ANISOU  553  CG  LEU A 101     2123   2807   2632    355    232   -172       C  
ATOM    554  CD1 LEU A 101       4.689 -55.636 -16.442  1.00 19.17           C  
ANISOU  554  CD1 LEU A 101     1976   2731   2576    336    175   -189       C  
ATOM    555  CD2 LEU A 101       3.415 -53.734 -15.399  1.00 21.39           C  
ANISOU  555  CD2 LEU A 101     2307   3002   2820    337    242   -150       C  
ATOM    556  N   ALA A 102       6.469 -51.065 -18.985  1.00 19.23           N  
ANISOU  556  N   ALA A 102     2208   2628   2469    342    481   -248       N  
ATOM    557  CA  ALA A 102       7.443 -49.959 -19.040  1.00 20.46           C  
ANISOU  557  CA  ALA A 102     2403   2757   2614    308    574   -280       C  
ATOM    558  C   ALA A 102       6.790 -48.623 -19.373  1.00 20.28           C  
ANISOU  558  C   ALA A 102     2464   2702   2540    335    646   -260       C  
ATOM    559  O   ALA A 102       7.173 -47.600 -18.809  1.00 21.37           O  
ANISOU  559  O   ALA A 102     2626   2824   2668    301    715   -274       O  
ATOM    560  CB  ALA A 102       8.553 -50.250 -20.030  1.00 20.64           C  
ANISOU  560  CB  ALA A 102     2434   2759   2649    300    604   -320       C  
ATOM    561  N   SER A 103       5.767 -48.651 -20.233  1.00 19.73           N  
ANISOU  561  N   SER A 103     2437   2622   2435    399    627   -228       N  
ATOM    562  CA  SER A 103       5.088 -47.398 -20.623  1.00 20.49           C  
ANISOU  562  CA  SER A 103     2620   2688   2478    438    691   -206       C  
ATOM    563  C   SER A 103       4.309 -46.738 -19.503  1.00 20.89           C  
ANISOU  563  C   SER A 103     2665   2750   2521    431    699   -178       C  
ATOM    564  O   SER A 103       3.845 -45.611 -19.679  1.00 21.32           O  
ANISOU  564  O   SER A 103     2791   2777   2532    458    762   -161       O  
ATOM    565  CB  SER A 103       4.184 -47.649 -21.819  1.00 21.25           C  
ANISOU  565  CB  SER A 103     2760   2776   2538    514    657   -182       C  
ATOM    566  OG  SER A 103       3.063 -48.437 -21.441  1.00 23.03           O  
ANISOU  566  OG  SER A 103     2929   3040   2781    541    566   -151       O  
ATOM    567  N   HIS A 104       4.155 -47.416 -18.353  1.00 20.19           N  
ANISOU  567  N   HIS A 104     2500   2698   2473    397    639   -172       N  
ATOM    568  CA  HIS A 104       3.515 -46.848 -17.182  1.00 20.71           C  
ANISOU  568  CA  HIS A 104     2559   2772   2537    383    648   -148       C  
ATOM    569  C   HIS A 104       4.514 -46.476 -16.083  1.00 22.05           C  
ANISOU  569  C   HIS A 104     2708   2943   2726    310    685   -177       C  
ATOM    570  O   HIS A 104       4.090 -45.943 -15.064  1.00 23.91           O  
ANISOU  570  O   HIS A 104     2946   3181   2956    292    701   -161       O  
ATOM    571  CB  HIS A 104       2.390 -47.749 -16.649  1.00 21.05           C  
ANISOU  571  CB  HIS A 104     2547   2849   2604    405    562   -114       C  
ATOM    572  CG  HIS A 104       1.186 -47.766 -17.529  1.00 19.62           C  
ANISOU  572  CG  HIS A 104     2390   2666   2398    477    536    -84       C  
ATOM    573  CD2 HIS A 104       0.873 -48.608 -18.542  1.00 20.16           C  
ANISOU  573  CD2 HIS A 104     2447   2745   2469    518    479    -84       C  
ATOM    574  ND1 HIS A 104       0.160 -46.826 -17.383  1.00 20.79           N  
ANISOU  574  ND1 HIS A 104     2579   2804   2517    515    568    -52       N  
ATOM    575  CE1 HIS A 104      -0.737 -47.129 -18.311  1.00 21.24           C  
ANISOU  575  CE1 HIS A 104     2643   2867   2560    580    525    -36       C  
ATOM    576  NE2 HIS A 104      -0.369 -48.214 -19.016  1.00 21.32           N  
ANISOU  576  NE2 HIS A 104     2622   2890   2588    582    469    -54       N  
ATOM    577  N   GLY A 105       5.806 -46.720 -16.293  1.00 20.71           N  
ANISOU  577  N   GLY A 105     2520   2772   2579    270    701   -223       N  
ATOM    578  CA  GLY A 105       6.830 -46.322 -15.335  1.00 22.17           C  
ANISOU  578  CA  GLY A 105     2681   2960   2782    202    734   -260       C  
ATOM    579  C   GLY A 105       7.485 -47.461 -14.576  1.00 21.55           C  
ANISOU  579  C   GLY A 105     2518   2919   2752    167    658   -281       C  
ATOM    580  O   GLY A 105       7.524 -47.441 -13.343  1.00 21.80           O  
ANISOU  580  O   GLY A 105     2521   2969   2794    133    639   -282       O  
ATOM    581  N   PHE A 106       8.031 -48.425 -15.302  1.00 21.07           N  
ANISOU  581  N   PHE A 106     2422   2868   2716    177    619   -300       N  
ATOM    582  CA  PHE A 106       8.753 -49.558 -14.708  1.00 20.37           C  
ANISOU  582  CA  PHE A 106     2256   2813   2672    150    549   -323       C  
ATOM    583  C   PHE A 106       9.888 -49.943 -15.637  1.00 20.66           C  
ANISOU  583  C   PHE A 106     2276   2842   2732    142    564   -366       C  
ATOM    584  O   PHE A 106       9.785 -49.761 -16.854  1.00 21.03           O  
ANISOU  584  O   PHE A 106     2369   2861   2760    173    600   -363       O  
ATOM    585  CB  PHE A 106       7.844 -50.796 -14.558  1.00 19.76           C  
ANISOU  585  CB  PHE A 106     2143   2759   2606    186    457   -284       C  
ATOM    586  CG  PHE A 106       6.710 -50.604 -13.588  1.00 18.59           C  
ANISOU  586  CG  PHE A 106     2001   2618   2444    193    438   -243       C  
ATOM    587  CD1 PHE A 106       6.926 -50.679 -12.221  1.00 20.20           C  
ANISOU  587  CD1 PHE A 106     2176   2838   2660    157    416   -248       C  
ATOM    588  CD2 PHE A 106       5.452 -50.250 -14.033  1.00 19.99           C  
ANISOU  588  CD2 PHE A 106     2218   2783   2595    237    447   -203       C  
ATOM    589  CE1 PHE A 106       5.889 -50.443 -11.326  1.00 20.92           C  
ANISOU  589  CE1 PHE A 106     2281   2929   2737    162    409   -210       C  
ATOM    590  CE2 PHE A 106       4.407 -50.021 -13.130  1.00 20.90           C  
ANISOU  590  CE2 PHE A 106     2337   2902   2702    243    437   -167       C  
ATOM    591  CZ  PHE A 106       4.639 -50.117 -11.785  1.00 21.02           C  
ANISOU  591  CZ  PHE A 106     2327   2929   2730    203    422   -170       C  
ATOM    592  N   VAL A 107      10.959 -50.507 -15.089  1.00 19.63           N  
ANISOU  592  N   VAL A 107     2083   2736   2642    106    534   -405       N  
ATOM    593  CA  VAL A 107      12.010 -51.100 -15.915  1.00 20.34           C  
ANISOU  593  CA  VAL A 107     2143   2822   2762    102    537   -444       C  
ATOM    594  C   VAL A 107      11.689 -52.598 -15.929  1.00 20.95           C  
ANISOU  594  C   VAL A 107     2175   2926   2860    133    441   -421       C  
ATOM    595  O   VAL A 107      11.501 -53.182 -14.863  1.00 21.19           O  
ANISOU  595  O   VAL A 107     2163   2985   2902    127    377   -409       O  
ATOM    596  CB  VAL A 107      13.424 -50.796 -15.407  1.00 21.68           C  
ANISOU  596  CB  VAL A 107     2267   3002   2968     46    566   -507       C  
ATOM    597  CG1 VAL A 107      14.445 -51.707 -16.096  1.00 22.84           C  
ANISOU  597  CG1 VAL A 107     2366   3155   3157     47    548   -544       C  
ATOM    598  CG2 VAL A 107      13.767 -49.320 -15.647  1.00 22.30           C  
ANISOU  598  CG2 VAL A 107     2399   3045   3027     13    676   -535       C  
ATOM    599  N   VAL A 108      11.530 -53.197 -17.113  1.00 19.38           N  
ANISOU  599  N   VAL A 108     1992   2712   2659    169    433   -412       N  
ATOM    600  CA  VAL A 108      11.116 -54.595 -17.176  1.00 18.51           C  
ANISOU  600  CA  VAL A 108     1847   2623   2565    199    348   -389       C  
ATOM    601  C   VAL A 108      12.149 -55.409 -17.876  1.00 19.52           C  
ANISOU  601  C   VAL A 108     1943   2749   2725    199    339   -422       C  
ATOM    602  O   VAL A 108      12.572 -55.041 -18.963  1.00 20.15           O  
ANISOU  602  O   VAL A 108     2057   2799   2799    204    397   -441       O  
ATOM    603  CB  VAL A 108       9.768 -54.723 -17.936  1.00 18.87           C  
ANISOU  603  CB  VAL A 108     1939   2655   2577    248    332   -343       C  
ATOM    604  CG1 VAL A 108       9.282 -56.173 -17.965  1.00 19.06           C  
ANISOU  604  CG1 VAL A 108     1927   2698   2618    273    247   -322       C  
ATOM    605  CG2 VAL A 108       8.702 -53.806 -17.334  1.00 20.02           C  
ANISOU  605  CG2 VAL A 108     2118   2798   2690    253    349   -310       C  
ATOM    606  N   ILE A 109      12.495 -56.576 -17.314  1.00 18.99           N  
ANISOU  606  N   ILE A 109     1816   2711   2690    199    269   -426       N  
ATOM    607  CA  ILE A 109      13.384 -57.497 -18.021  1.00 18.86           C  
ANISOU  607  CA  ILE A 109     1768   2692   2705    206    255   -452       C  
ATOM    608  C   ILE A 109      12.641 -58.792 -18.326  1.00 19.79           C  
ANISOU  608  C   ILE A 109     1882   2816   2821    244    186   -418       C  
ATOM    609  O   ILE A 109      12.102 -59.417 -17.409  1.00 19.63           O  
ANISOU  609  O   ILE A 109     1837   2818   2803    248    125   -393       O  
ATOM    610  CB  ILE A 109      14.733 -57.729 -17.284  1.00 19.53           C  
ANISOU  610  CB  ILE A 109     1785   2801   2834    174    245   -500       C  
ATOM    611  CG1 ILE A 109      15.664 -58.621 -18.128  1.00 21.05           C  
ANISOU  611  CG1 ILE A 109     1948   2988   3062    185    241   -528       C  
ATOM    612  CG2 ILE A 109      14.553 -58.267 -15.869  1.00 19.99           C  
ANISOU  612  CG2 ILE A 109     1801   2895   2898    170    172   -487       C  
ATOM    613  CD1 ILE A 109      17.093 -58.616 -17.636  1.00 21.67           C  
ANISOU  613  CD1 ILE A 109     1959   3086   3187    155    248   -585       C  
ATOM    614  N   THR A 110      12.555 -59.165 -19.614  1.00 19.37           N  
ANISOU  614  N   THR A 110     1860   2738   2760    270    198   -415       N  
ATOM    615  CA  THR A 110      11.948 -60.439 -20.003  1.00 19.72           C  
ANISOU  615  CA  THR A 110     1900   2787   2806    301    136   -389       C  
ATOM    616  C   THR A 110      13.109 -61.378 -20.263  1.00 20.73           C  
ANISOU  616  C   THR A 110     1987   2917   2972    298    123   -420       C  
ATOM    617  O   THR A 110      14.072 -60.975 -20.934  1.00 21.85           O  
ANISOU  617  O   THR A 110     2135   3040   3128    287    180   -455       O  
ATOM    618  CB  THR A 110      11.085 -60.285 -21.251  1.00 21.16           C  
ANISOU  618  CB  THR A 110     2146   2943   2953    334    151   -369       C  
ATOM    619  CG2 THR A 110       9.894 -59.350 -21.018  1.00 21.15           C  
ANISOU  619  CG2 THR A 110     2181   2940   2913    344    161   -338       C  
ATOM    620  OG1 THR A 110      11.884 -59.795 -22.330  1.00 21.31           O  
ANISOU  620  OG1 THR A 110     2200   2929   2968    334    217   -397       O  
ATOM    621  N   ILE A 111      13.019 -62.628 -19.780  1.00 19.35           N  
ANISOU  621  N   ILE A 111     1775   2761   2814    310     56   -407       N  
ATOM    622  CA  ILE A 111      14.163 -63.524 -19.972  1.00 18.97           C  
ANISOU  622  CA  ILE A 111     1687   2715   2804    312     44   -436       C  
ATOM    623  C   ILE A 111      13.869 -64.814 -20.678  1.00 19.48           C  
ANISOU  623  C   ILE A 111     1761   2769   2870    340      6   -419       C  
ATOM    624  O   ILE A 111      12.739 -65.297 -20.704  1.00 19.11           O  
ANISOU  624  O   ILE A 111     1737   2723   2802    357    -32   -385       O  
ATOM    625  CB  ILE A 111      14.870 -63.834 -18.615  1.00 20.42           C  
ANISOU  625  CB  ILE A 111     1809   2933   3016    298      5   -451       C  
ATOM    626  CG1 ILE A 111      14.019 -64.769 -17.724  1.00 21.92           C  
ANISOU  626  CG1 ILE A 111     1993   3140   3196    314    -66   -414       C  
ATOM    627  CG2 ILE A 111      15.272 -62.554 -17.877  1.00 20.59           C  
ANISOU  627  CG2 ILE A 111     1818   2966   3038    264     43   -475       C  
ATOM    628  CD1 ILE A 111      14.868 -65.401 -16.541  1.00 23.20           C  
ANISOU  628  CD1 ILE A 111     2101   3331   3384    314   -113   -431       C  
ATOM    629  N   ASP A 112      14.927 -65.355 -21.283  1.00 19.23           N  
ANISOU  629  N   ASP A 112     1712   2728   2867    345     22   -448       N  
ATOM    630  CA  ASP A 112      14.971 -66.726 -21.701  1.00 19.57           C  
ANISOU  630  CA  ASP A 112     1750   2765   2921    368    -17   -439       C  
ATOM    631  C   ASP A 112      15.750 -67.447 -20.611  1.00 20.75           C  
ANISOU  631  C   ASP A 112     1837   2943   3104    368    -59   -452       C  
ATOM    632  O   ASP A 112      16.746 -66.920 -20.096  1.00 21.54           O  
ANISOU  632  O   ASP A 112     1896   3059   3231    352    -40   -485       O  
ATOM    633  CB  ASP A 112      15.707 -66.908 -23.037  1.00 20.37           C  
ANISOU  633  CB  ASP A 112     1873   2834   3034    377     30   -463       C  
ATOM    634  CG  ASP A 112      14.814 -66.504 -24.164  1.00 24.57           C  
ANISOU  634  CG  ASP A 112     2477   3336   3524    389     55   -445       C  
ATOM    635  OD1 ASP A 112      13.633 -66.894 -24.140  1.00 25.04           O  
ANISOU  635  OD1 ASP A 112     2559   3400   3556    403     10   -412       O  
ATOM    636  OD2 ASP A 112      15.291 -65.797 -25.065  1.00 26.82           O1-
ANISOU  636  OD2 ASP A 112     2796   3591   3803    385    120   -467       O1-
ATOM    637  N   THR A 113      15.332 -68.683 -20.304  1.00 20.59           N  
ANISOU  637  N   THR A 113     1813   2927   3082    389   -115   -427       N  
ATOM    638  CA  THR A 113      16.042 -69.469 -19.291  1.00 21.47           C  
ANISOU  638  CA  THR A 113     1876   3062   3219    399   -159   -436       C  
ATOM    639  C   THR A 113      17.246 -70.195 -19.924  1.00 22.44           C  
ANISOU  639  C   THR A 113     1972   3176   3377    415   -148   -465       C  
ATOM    640  O   THR A 113      17.338 -70.314 -21.156  1.00 22.70           O  
ANISOU  640  O   THR A 113     2033   3180   3411    420   -111   -471       O  
ATOM    641  CB  THR A 113      15.059 -70.424 -18.592  1.00 22.52           C  
ANISOU  641  CB  THR A 113     2024   3199   3333    415   -216   -397       C  
ATOM    642  CG2 THR A 113      14.028 -69.643 -17.748  1.00 22.97           C  
ANISOU  642  CG2 THR A 113     2097   3267   3363    397   -224   -373       C  
ATOM    643  OG1 THR A 113      14.357 -71.166 -19.597  1.00 23.36           O  
ANISOU  643  OG1 THR A 113     2170   3280   3427    427   -217   -378       O  
ATOM    644  N   ASN A 114      18.168 -70.682 -19.081  1.00 22.73           N  
ANISOU  644  N   ASN A 114     1957   3237   3442    428   -179   -484       N  
ATOM    645  CA  ASN A 114      19.373 -71.413 -19.528  1.00 23.69           C  
ANISOU  645  CA  ASN A 114     2042   3356   3603    448   -173   -513       C  
ATOM    646  C   ASN A 114      18.989 -72.586 -20.426  1.00 24.81           C  
ANISOU  646  C   ASN A 114     2224   3467   3736    472   -178   -489       C  
ATOM    647  O   ASN A 114      19.615 -72.802 -21.469  1.00 25.76           O  
ANISOU  647  O   ASN A 114     2347   3564   3876    477   -139   -509       O  
ATOM    648  CB  ASN A 114      20.175 -71.896 -18.326  1.00 24.59           C  
ANISOU  648  CB  ASN A 114     2100   3504   3739    467   -224   -529       C  
ATOM    649  CG  ASN A 114      20.848 -70.767 -17.596  1.00 27.88           C  
ANISOU  649  CG  ASN A 114     2468   3951   4174    442   -215   -566       C  
ATOM    650  ND2 ASN A 114      20.933 -70.863 -16.277  1.00 28.55           N  
ANISOU  650  ND2 ASN A 114     2528   4068   4252    452   -270   -565       N  
ATOM    651  OD1 ASN A 114      21.289 -69.783 -18.203  1.00 29.22           O  
ANISOU  651  OD1 ASN A 114     2627   4114   4361    412   -155   -599       O  
ATOM    652  N   SER A 115      17.898 -73.273 -20.070  1.00 23.41           N  
ANISOU  652  N   SER A 115     2082   3285   3527    482   -220   -449       N  
ATOM    653  CA  SER A 115      17.301 -74.327 -20.880  1.00 23.18           C  
ANISOU  653  CA  SER A 115     2097   3226   3484    498   -226   -425       C  
ATOM    654  C   SER A 115      15.791 -74.097 -20.873  1.00 21.99           C  
ANISOU  654  C   SER A 115     1991   3069   3294    483   -238   -392       C  
ATOM    655  O   SER A 115      15.234 -73.756 -19.822  1.00 21.65           O  
ANISOU  655  O   SER A 115     1942   3046   3239    474   -264   -377       O  
ATOM    656  CB  SER A 115      17.606 -75.717 -20.305  1.00 24.76           C  
ANISOU  656  CB  SER A 115     2287   3428   3693    530   -269   -415       C  
ATOM    657  OG  SER A 115      16.791 -76.704 -20.928  1.00 26.86           O  
ANISOU  657  OG  SER A 115     2602   3665   3939    538   -277   -389       O  
ATOM    658  N   THR A 116      15.113 -74.334 -22.005  1.00 21.72           N  
ANISOU  658  N   THR A 116     2004   3008   3243    482   -223   -382       N  
ATOM    659  CA  THR A 116      13.645 -74.239 -22.008  1.00 22.33           C  
ANISOU  659  CA  THR A 116     2116   3082   3288    471   -242   -354       C  
ATOM    660  C   THR A 116      13.012 -75.315 -21.104  1.00 21.20           C  
ANISOU  660  C   THR A 116     1973   2942   3141    479   -288   -330       C  
ATOM    661  O   THR A 116      11.822 -75.224 -20.820  1.00 20.73           O  
ANISOU  661  O   THR A 116     1931   2884   3063    467   -304   -309       O  
ATOM    662  CB  THR A 116      13.060 -74.309 -23.406  1.00 25.93           C  
ANISOU  662  CB  THR A 116     2619   3510   3724    472   -224   -352       C  
ATOM    663  CG2 THR A 116      13.640 -73.247 -24.333  1.00 27.62           C  
ANISOU  663  CG2 THR A 116     2847   3712   3936    468   -171   -375       C  
ATOM    664  OG1 THR A 116      13.261 -75.626 -23.925  1.00 26.97           O  
ANISOU  664  OG1 THR A 116     2765   3620   3861    488   -235   -351       O  
ATOM    665  N   LEU A 117      13.782 -76.327 -20.648  1.00 21.00           N  
ANISOU  665  N   LEU A 117     1931   2915   3132    500   -305   -333       N  
ATOM    666  CA  LEU A 117      13.228 -77.376 -19.801  1.00 20.70           C  
ANISOU  666  CA  LEU A 117     1905   2874   3087    509   -341   -310       C  
ATOM    667  C   LEU A 117      13.480 -77.144 -18.304  1.00 21.02           C  
ANISOU  667  C   LEU A 117     1921   2938   3128    515   -365   -305       C  
ATOM    668  O   LEU A 117      13.166 -78.018 -17.494  1.00 21.38           O  
ANISOU  668  O   LEU A 117     1980   2976   3165    528   -391   -287       O  
ATOM    669  CB  LEU A 117      13.761 -78.763 -20.218  1.00 21.04           C  
ANISOU  669  CB  LEU A 117     1961   2893   3139    535   -345   -311       C  
ATOM    670  CG  LEU A 117      13.645 -79.027 -21.729  1.00 22.20           C  
ANISOU  670  CG  LEU A 117     2138   3014   3284    531   -320   -319       C  
ATOM    671  CD1 LEU A 117      14.206 -80.410 -22.069  1.00 23.16           C  
ANISOU  671  CD1 LEU A 117     2274   3110   3414    556   -321   -320       C  
ATOM    672  CD2 LEU A 117      12.201 -78.936 -22.224  1.00 22.88           C  
ANISOU  672  CD2 LEU A 117     2258   3089   3345    507   -325   -306       C  
ATOM    673  N   ASP A 118      13.970 -75.949 -17.920  1.00 19.65           N  
ANISOU  673  N   ASP A 118     1716   2790   2961    503   -355   -320       N  
ATOM    674  CA  ASP A 118      14.244 -75.664 -16.499  1.00 19.45           C  
ANISOU  674  CA  ASP A 118     1669   2788   2933    508   -381   -319       C  
ATOM    675  C   ASP A 118      12.954 -75.722 -15.675  1.00 19.91           C  
ANISOU  675  C   ASP A 118     1758   2840   2966    496   -397   -288       C  
ATOM    676  O   ASP A 118      11.873 -75.378 -16.175  1.00 19.71           O  
ANISOU  676  O   ASP A 118     1754   2806   2931    474   -381   -275       O  
ATOM    677  CB  ASP A 118      14.914 -74.299 -16.349  1.00 20.97           C  
ANISOU  677  CB  ASP A 118     1825   3006   3136    490   -361   -345       C  
ATOM    678  CG  ASP A 118      16.349 -74.275 -16.844  1.00 25.20           C  
ANISOU  678  CG  ASP A 118     2320   3550   3704    503   -347   -382       C  
ATOM    679  OD1 ASP A 118      16.991 -75.356 -16.874  1.00 25.64           O  
ANISOU  679  OD1 ASP A 118     2368   3601   3775    534   -366   -386       O  
ATOM    680  OD2 ASP A 118      16.828 -73.185 -17.208  1.00 25.47           O1-
ANISOU  680  OD2 ASP A 118     2332   3593   3751    482   -312   -409       O1-
ATOM    681  N   GLN A 119      13.063 -76.204 -14.440  1.00 20.32           N  
ANISOU  681  N   GLN A 119     1814   2896   3009    513   -427   -277       N  
ATOM    682  CA  GLN A 119      11.921 -76.336 -13.529  1.00 19.77           C  
ANISOU  682  CA  GLN A 119     1778   2816   2918    502   -436   -249       C  
ATOM    683  C   GLN A 119      11.688 -75.015 -12.753  1.00 20.59           C  
ANISOU  683  C   GLN A 119     1871   2941   3012    480   -431   -249       C  
ATOM    684  O   GLN A 119      12.518 -74.105 -12.805  1.00 20.93           O  
ANISOU  684  O   GLN A 119     1880   3007   3064    474   -424   -273       O  
ATOM    685  CB  GLN A 119      12.224 -77.486 -12.548  1.00 20.76           C  
ANISOU  685  CB  GLN A 119     1925   2929   3032    536   -466   -237       C  
ATOM    686  CG  GLN A 119      12.184 -78.862 -13.220  1.00 22.04           C  
ANISOU  686  CG  GLN A 119     2112   3063   3199    555   -465   -231       C  
ATOM    687  CD  GLN A 119      10.751 -79.303 -13.370  1.00 27.22           C  
ANISOU  687  CD  GLN A 119     2807   3691   3846    530   -449   -210       C  
ATOM    688  NE2 GLN A 119      10.419 -79.957 -14.489  1.00 27.36           N  
ANISOU  688  NE2 GLN A 119     2835   3688   3872    524   -435   -212       N  
ATOM    689  OE1 GLN A 119       9.924 -79.105 -12.460  1.00 27.16           O  
ANISOU  689  OE1 GLN A 119     2820   3676   3824    517   -448   -192       O  
ATOM    690  N   PRO A 120      10.564 -74.897 -12.019  1.00 20.90           N  
ANISOU  690  N   PRO A 120     1938   2968   3033    464   -429   -224       N  
ATOM    691  CA  PRO A 120      10.279 -73.641 -11.309  1.00 20.42           C  
ANISOU  691  CA  PRO A 120     1872   2924   2962    442   -419   -222       C  
ATOM    692  C   PRO A 120      11.361 -73.110 -10.363  1.00 20.68           C  
ANISOU  692  C   PRO A 120     1885   2982   2990    452   -438   -240       C  
ATOM    693  O   PRO A 120      11.552 -71.894 -10.351  1.00 21.04           O  
ANISOU  693  O   PRO A 120     1912   3046   3037    430   -420   -254       O  
ATOM    694  CB  PRO A 120       8.986 -73.962 -10.556  1.00 21.31           C  
ANISOU  694  CB  PRO A 120     2024   3014   3061    432   -416   -192       C  
ATOM    695  CG  PRO A 120       8.288 -74.994 -11.432  1.00 21.35           C  
ANISOU  695  CG  PRO A 120     2043   2995   3076    433   -410   -184       C  
ATOM    696  CD  PRO A 120       9.448 -75.861 -11.899  1.00 20.89           C  
ANISOU  696  CD  PRO A 120     1974   2937   3025    462   -428   -200       C  
ATOM    697  N   SER A 121      12.075 -73.966  -9.580  1.00 21.25           N  
ANISOU  697  N   SER A 121     1963   3055   3056    485   -474   -243       N  
ATOM    698  CA  SER A 121      13.108 -73.443  -8.670  1.00 22.39           C  
ANISOU  698  CA  SER A 121     2085   3228   3196    496   -501   -265       C  
ATOM    699  C   SER A 121      14.272 -72.823  -9.441  1.00 21.45           C  
ANISOU  699  C   SER A 121     1908   3136   3105    491   -493   -305       C  
ATOM    700  O   SER A 121      14.781 -71.765  -9.058  1.00 21.23           O  
ANISOU  700  O   SER A 121     1853   3133   3079    473   -489   -329       O  
ATOM    701  CB  SER A 121      13.636 -74.553  -7.757  1.00 27.49           C  
ANISOU  701  CB  SER A 121     2751   3868   3825    542   -545   -260       C  
ATOM    702  OG  SER A 121      12.728 -74.670  -6.678  1.00 35.66           O  
ANISOU  702  OG  SER A 121     3840   4881   4828    540   -548   -230       O  
ATOM    703  N   SER A 122      14.640 -73.446 -10.567  1.00 21.33           N  
ANISOU  703  N   SER A 122     1878   3115   3114    503   -483   -314       N  
ATOM    704  CA  SER A 122      15.691 -72.921 -11.435  1.00 21.94           C  
ANISOU  704  CA  SER A 122     1904   3210   3222    497   -463   -353       C  
ATOM    705  C   SER A 122      15.211 -71.618 -12.091  1.00 20.85           C  
ANISOU  705  C   SER A 122     1765   3072   3086    454   -414   -358       C  
ATOM    706  O   SER A 122      15.950 -70.644 -12.143  1.00 22.24           O  
ANISOU  706  O   SER A 122     1907   3267   3276    436   -395   -391       O  
ATOM    707  CB  SER A 122      16.036 -73.939 -12.518  1.00 24.32           C  
ANISOU  707  CB  SER A 122     2203   3495   3544    519   -457   -356       C  
ATOM    708  OG  SER A 122      16.943 -73.395 -13.459  1.00 26.71           O  
ANISOU  708  OG  SER A 122     2463   3807   3877    509   -427   -392       O  
ATOM    709  N   ARG A 123      13.937 -71.574 -12.514  1.00 19.85           N  
ANISOU  709  N   ARG A 123     1678   2922   2942    439   -394   -327       N  
ATOM    710  CA  ARG A 123      13.375 -70.346 -13.101  1.00 18.80           C  
ANISOU  710  CA  ARG A 123     1551   2787   2803    406   -349   -327       C  
ATOM    711  C   ARG A 123      13.406 -69.212 -12.071  1.00 18.80           C  
ANISOU  711  C   ARG A 123     1547   2806   2792    384   -345   -333       C  
ATOM    712  O   ARG A 123      13.721 -68.074 -12.419  1.00 19.44           O  
ANISOU  712  O   ARG A 123     1615   2895   2878    361   -308   -355       O  
ATOM    713  CB  ARG A 123      11.930 -70.579 -13.588  1.00 19.01           C  
ANISOU  713  CB  ARG A 123     1617   2790   2814    401   -339   -293       C  
ATOM    714  CG  ARG A 123      11.908 -71.480 -14.823  1.00 18.50           C  
ANISOU  714  CG  ARG A 123     1561   2707   2761    415   -336   -294       C  
ATOM    715  CD  ARG A 123      10.511 -71.787 -15.359  1.00 17.66           C  
ANISOU  715  CD  ARG A 123     1487   2581   2642    410   -333   -267       C  
ATOM    716  NE  ARG A 123      10.702 -72.833 -16.363  1.00 17.93           N  
ANISOU  716  NE  ARG A 123     1529   2599   2686    426   -338   -272       N  
ATOM    717  CZ  ARG A 123      10.906 -72.617 -17.656  1.00 18.63           C  
ANISOU  717  CZ  ARG A 123     1622   2679   2777    426   -314   -286       C  
ATOM    718  NH1 ARG A 123      10.746 -71.399 -18.170  1.00 19.24           N1+
ANISOU  718  NH1 ARG A 123     1705   2760   2846    413   -283   -293       N1+
ATOM    719  NH2 ARG A 123      11.310 -73.605 -18.438  1.00 19.19           N  
ANISOU  719  NH2 ARG A 123     1699   2734   2858    442   -318   -293       N  
ATOM    720  N   SER A 124      13.104 -69.531 -10.799  1.00 19.14           N  
ANISOU  720  N   SER A 124     1605   2852   2817    392   -378   -316       N  
ATOM    721  CA  SER A 124      13.154 -68.509  -9.739  1.00 19.27           C  
ANISOU  721  CA  SER A 124     1622   2884   2817    372   -377   -322       C  
ATOM    722  C   SER A 124      14.586 -67.981  -9.566  1.00 19.89           C  
ANISOU  722  C   SER A 124     1651   2990   2914    368   -383   -370       C  
ATOM    723  O   SER A 124      14.775 -66.764  -9.490  1.00 20.52           O  
ANISOU  723  O   SER A 124     1721   3081   2994    337   -351   -389       O  
ATOM    724  CB  SER A 124      12.641 -69.076  -8.419  1.00 19.87           C  
ANISOU  724  CB  SER A 124     1731   2952   2868    386   -413   -295       C  
ATOM    725  OG  SER A 124      12.832 -68.116  -7.392  1.00 20.25           O  
ANISOU  725  OG  SER A 124     1780   3015   2899    368   -414   -305       O  
ATOM    726  N   SER A 125      15.595 -68.881  -9.544  1.00 21.11           N  
ANISOU  726  N   SER A 125     1776   3158   3088    399   -419   -391       N  
ATOM    727  CA  SER A 125      16.992 -68.449  -9.399  1.00 22.51           C  
ANISOU  727  CA  SER A 125     1896   3366   3291    396   -428   -443       C  
ATOM    728  C   SER A 125      17.410 -67.520 -10.536  1.00 22.09           C  
ANISOU  728  C   SER A 125     1816   3312   3265    364   -368   -474       C  
ATOM    729  O   SER A 125      18.061 -66.489 -10.310  1.00 22.67           O  
ANISOU  729  O   SER A 125     1859   3405   3350    335   -347   -512       O  
ATOM    730  CB  SER A 125      17.925 -69.659  -9.370  1.00 26.28           C  
ANISOU  730  CB  SER A 125     2343   3854   3787    441   -474   -458       C  
ATOM    731  OG  SER A 125      17.686 -70.420  -8.201  1.00 30.57           O  
ANISOU  731  OG  SER A 125     2917   4398   4302    474   -529   -435       O  
ATOM    732  N   GLN A 126      16.972 -67.853 -11.758  1.00 21.11           N  
ANISOU  732  N   GLN A 126     1710   3163   3147    368   -335   -457       N  
ATOM    733  CA  GLN A 126      17.306 -67.070 -12.934  1.00 20.33           C  
ANISOU  733  CA  GLN A 126     1602   3055   3069    343   -273   -483       C  
ATOM    734  C   GLN A 126      16.568 -65.734 -12.940  1.00 19.64           C  
ANISOU  734  C   GLN A 126     1546   2959   2959    308   -226   -474       C  
ATOM    735  O   GLN A 126      17.134 -64.718 -13.333  1.00 21.31           O  
ANISOU  735  O   GLN A 126     1742   3171   3183    280   -176   -508       O  
ATOM    736  CB  GLN A 126      17.002 -67.880 -14.187  1.00 21.39           C  
ANISOU  736  CB  GLN A 126     1757   3162   3209    363   -259   -465       C  
ATOM    737  CG  GLN A 126      17.898 -69.112 -14.252  1.00 21.35           C  
ANISOU  737  CG  GLN A 126     1718   3163   3230    397   -295   -480       C  
ATOM    738  CD  GLN A 126      17.583 -69.903 -15.478  1.00 23.52           C  
ANISOU  738  CD  GLN A 126     2019   3408   3508    413   -279   -463       C  
ATOM    739  NE2 GLN A 126      17.120 -71.132 -15.298  1.00 23.04           N  
ANISOU  739  NE2 GLN A 126     1980   3337   3436    442   -319   -433       N  
ATOM    740  OE1 GLN A 126      17.753 -69.419 -16.596  1.00 23.56           O  
ANISOU  740  OE1 GLN A 126     2031   3396   3524    399   -227   -478       O  
ATOM    741  N   GLN A 127      15.324 -65.714 -12.437  1.00 18.82           N  
ANISOU  741  N   GLN A 127     1485   2845   2820    308   -238   -430       N  
ATOM    742  CA  GLN A 127      14.538 -64.490 -12.329  1.00 18.82           C  
ANISOU  742  CA  GLN A 127     1517   2837   2797    280   -197   -416       C  
ATOM    743  C   GLN A 127      15.229 -63.522 -11.362  1.00 19.82           C  
ANISOU  743  C   GLN A 127     1621   2986   2924    252   -190   -448       C  
ATOM    744  O   GLN A 127      15.342 -62.324 -11.654  1.00 20.34           O  
ANISOU  744  O   GLN A 127     1694   3047   2987    222   -134   -467       O  
ATOM    745  CB  GLN A 127      13.146 -64.856 -11.810  1.00 19.53           C  
ANISOU  745  CB  GLN A 127     1647   2915   2857    290   -220   -366       C  
ATOM    746  CG  GLN A 127      12.189 -63.696 -11.680  1.00 19.06           C  
ANISOU  746  CG  GLN A 127     1623   2846   2774    268   -180   -346       C  
ATOM    747  CD  GLN A 127      10.821 -64.240 -11.368  1.00 18.98           C  
ANISOU  747  CD  GLN A 127     1645   2822   2746    281   -201   -300       C  
ATOM    748  NE2 GLN A 127       9.808 -63.806 -12.121  1.00 17.00           N  
ANISOU  748  NE2 GLN A 127     1420   2555   2483    281   -171   -278       N  
ATOM    749  OE1 GLN A 127      10.652 -65.082 -10.476  1.00 19.71           O  
ANISOU  749  OE1 GLN A 127     1738   2915   2834    293   -243   -285       O  
ATOM    750  N   MET A 128      15.707 -64.046 -10.221  1.00 20.51           N  
ANISOU  750  N   MET A 128     1686   3095   3012    263   -246   -457       N  
ATOM    751  CA  MET A 128      16.403 -63.180  -9.254  1.00 20.72           C  
ANISOU  751  CA  MET A 128     1690   3146   3038    237   -249   -492       C  
ATOM    752  C   MET A 128      17.768 -62.718  -9.795  1.00 20.88           C  
ANISOU  752  C   MET A 128     1653   3182   3098    218   -221   -555       C  
ATOM    753  O   MET A 128      18.136 -61.547  -9.592  1.00 21.83           O  
ANISOU  753  O   MET A 128     1765   3310   3221    179   -181   -587       O  
ATOM    754  CB  MET A 128      16.545 -63.876  -7.886  1.00 21.53           C  
ANISOU  754  CB  MET A 128     1789   3266   3124    260   -321   -486       C  
ATOM    755  CG  MET A 128      15.199 -64.294  -7.265  1.00 22.55           C  
ANISOU  755  CG  MET A 128     1978   3373   3216    274   -338   -427       C  
ATOM    756  SD  MET A 128      14.000 -62.945  -7.128  1.00 22.31           S  
ANISOU  756  SD  MET A 128     1997   3323   3156    235   -278   -399       S  
ATOM    757  CE  MET A 128      14.889 -61.801  -6.086  1.00 22.73           C  
ANISOU  757  CE  MET A 128     2031   3402   3203    201   -276   -444       C  
ATOM    758  N   ALA A 129      18.449 -63.580 -10.568  1.00 22.00           N  
ANISOU  758  N   ALA A 129     1762   3326   3273    243   -232   -571       N  
ATOM    759  CA  ALA A 129      19.719 -63.186 -11.206  1.00 22.38           C  
ANISOU  759  CA  ALA A 129     1754   3384   3366    224   -196   -632       C  
ATOM    760  C   ALA A 129      19.457 -62.059 -12.216  1.00 22.26           C  
ANISOU  760  C   ALA A 129     1769   3341   3350    189   -106   -638       C  
ATOM    761  O   ALA A 129      20.250 -61.115 -12.312  1.00 22.60           O  
ANISOU  761  O   ALA A 129     1783   3389   3415    152    -58   -689       O  
ATOM    762  CB  ALA A 129      20.357 -64.373 -11.904  1.00 23.09           C  
ANISOU  762  CB  ALA A 129     1812   3473   3489    261   -219   -641       C  
ATOM    763  N   ALA A 130      18.309 -62.124 -12.951  1.00 21.16           N  
ANISOU  763  N   ALA A 130     1690   3169   3181    200    -82   -589       N  
ATOM    764  CA  ALA A 130      17.974 -61.071 -13.902  1.00 21.89           C  
ANISOU  764  CA  ALA A 130     1823   3232   3263    176      0   -590       C  
ATOM    765  C   ALA A 130      17.737 -59.733 -13.185  1.00 22.49           C  
ANISOU  765  C   ALA A 130     1918   3311   3317    138     36   -597       C  
ATOM    766  O   ALA A 130      18.187 -58.678 -13.670  1.00 22.64           O  
ANISOU  766  O   ALA A 130     1943   3315   3343    105    109   -631       O  
ATOM    767  CB  ALA A 130      16.742 -61.467 -14.711  1.00 21.59           C  
ANISOU  767  CB  ALA A 130     1843   3165   3194    203      4   -535       C  
ATOM    768  N   LEU A 131      17.044 -59.765 -12.022  1.00 21.94           N  
ANISOU  768  N   LEU A 131     1863   3255   3219    141    -10   -567       N  
ATOM    769  CA  LEU A 131      16.836 -58.538 -11.257  1.00 21.93           C  
ANISOU  769  CA  LEU A 131     1882   3256   3196    104     22   -574       C  
ATOM    770  C   LEU A 131      18.183 -57.986 -10.755  1.00 23.12           C  
ANISOU  770  C   LEU A 131     1977   3432   3377     69     32   -642       C  
ATOM    771  O   LEU A 131      18.379 -56.772 -10.798  1.00 24.39           O  
ANISOU  771  O   LEU A 131     2150   3583   3534     28     97   -669       O  
ATOM    772  CB  LEU A 131      15.900 -58.779 -10.057  1.00 21.55           C  
ANISOU  772  CB  LEU A 131     1859   3215   3113    116    -30   -530       C  
ATOM    773  CG  LEU A 131      14.432 -58.989 -10.430  1.00 21.01           C  
ANISOU  773  CG  LEU A 131     1846   3121   3014    139    -25   -467       C  
ATOM    774  CD1 LEU A 131      13.603 -59.429  -9.207  1.00 20.89           C  
ANISOU  774  CD1 LEU A 131     1851   3112   2974    151    -77   -428       C  
ATOM    775  CD2 LEU A 131      13.837 -57.702 -11.015  1.00 21.06           C  
ANISOU  775  CD2 LEU A 131     1899   3103   2999    119     53   -458       C  
ATOM    776  N   ARG A 132      19.096 -58.856 -10.329  1.00 23.51           N  
ANISOU  776  N   ARG A 132     1964   3511   3456     84    -30   -672       N  
ATOM    777  CA  ARG A 132      20.429 -58.415  -9.885  1.00 24.36           C  
ANISOU  777  CA  ARG A 132     2007   3648   3601     54    -30   -745       C  
ATOM    778  C   ARG A 132      21.203 -57.782 -11.037  1.00 24.80           C  
ANISOU  778  C   ARG A 132     2042   3686   3695     24     55   -793       C  
ATOM    779  O   ARG A 132      21.905 -56.792 -10.806  1.00 24.89           O  
ANISOU  779  O   ARG A 132     2028   3704   3724    -23    100   -848       O  
ATOM    780  CB  ARG A 132      21.237 -59.579  -9.297  1.00 24.78           C  
ANISOU  780  CB  ARG A 132     1998   3739   3681     88   -118   -766       C  
ATOM    781  CG  ARG A 132      20.707 -60.047  -7.941  1.00 28.10           C  
ANISOU  781  CG  ARG A 132     2438   4176   4061    112   -199   -732       C  
ATOM    782  CD  ARG A 132      21.748 -60.907  -7.212  1.00 29.45           C  
ANISOU  782  CD  ARG A 132     2545   4389   4257    142   -282   -769       C  
ATOM    783  NE  ARG A 132      22.061 -62.155  -7.925  1.00 29.71           N  
ANISOU  783  NE  ARG A 132     2553   4420   4317    188   -310   -760       N  
ATOM    784  CZ  ARG A 132      21.346 -63.272  -7.844  1.00 29.70           C  
ANISOU  784  CZ  ARG A 132     2590   4406   4290    235   -354   -704       C  
ATOM    785  NH1 ARG A 132      20.228 -63.304  -7.124  1.00 28.08           N1+
ANISOU  785  NH1 ARG A 132     2449   4186   4035    241   -373   -651       N1+
ATOM    786  NH2 ARG A 132      21.732 -64.364  -8.499  1.00 30.23           N  
ANISOU  786  NH2 ARG A 132     2632   4470   4383    274   -375   -702       N  
ATOM    787  N   GLN A 133      21.033 -58.288 -12.270  1.00 24.46           N  
ANISOU  787  N   GLN A 133     2017   3615   3662     48     84   -774       N  
ATOM    788  CA  GLN A 133      21.723 -57.679 -13.414  1.00 24.71           C  
ANISOU  788  CA  GLN A 133     2043   3620   3725     21    174   -817       C  
ATOM    789  C   GLN A 133      21.126 -56.335 -13.772  1.00 25.21           C  
ANISOU  789  C   GLN A 133     2174   3649   3756    -13    263   -809       C  
ATOM    790  O   GLN A 133      21.865 -55.419 -14.101  1.00 25.55           O  
ANISOU  790  O   GLN A 133     2207   3679   3823    -56    340   -862       O  
ATOM    791  CB  GLN A 133      21.808 -58.591 -14.630  1.00 25.64           C  
ANISOU  791  CB  GLN A 133     2165   3715   3860     56    183   -804       C  
ATOM    792  CG  GLN A 133      22.786 -58.009 -15.663  1.00 27.07           C  
ANISOU  792  CG  GLN A 133     2330   3872   4084     26    275   -861       C  
ATOM    793  CD  GLN A 133      23.295 -59.054 -16.621  1.00 28.65           C  
ANISOU  793  CD  GLN A 133     2508   4060   4318     58    271   -867       C  
ATOM    794  NE2 GLN A 133      24.454 -58.800 -17.217  1.00 29.07           N  
ANISOU  794  NE2 GLN A 133     2517   4102   4425     33    333   -930       N  
ATOM    795  OE1 GLN A 133      22.679 -60.105 -16.817  1.00 28.05           O  
ANISOU  795  OE1 GLN A 133     2452   3982   4223    103    216   -817       O  
ATOM    796  N   VAL A 134      19.800 -56.160 -13.612  1.00 24.61           N  
ANISOU  796  N   VAL A 134     2168   3558   3626      4    255   -744       N  
ATOM    797  CA  VAL A 134      19.177 -54.851 -13.818  1.00 25.24           C  
ANISOU  797  CA  VAL A 134     2315   3607   3670    -22    335   -733       C  
ATOM    798  C   VAL A 134      19.743 -53.868 -12.772  1.00 26.37           C  
ANISOU  798  C   VAL A 134     2432   3769   3818    -74    354   -779       C  
ATOM    799  O   VAL A 134      20.104 -52.739 -13.134  1.00 27.46           O  
ANISOU  799  O   VAL A 134     2593   3883   3959   -115    444   -815       O  
ATOM    800  CB  VAL A 134      17.626 -54.945 -13.719  1.00 26.03           C  
ANISOU  800  CB  VAL A 134     2481   3693   3715     12    310   -656       C  
ATOM    801  CG1 VAL A 134      16.995 -53.555 -13.597  1.00 26.96           C  
ANISOU  801  CG1 VAL A 134     2662   3787   3794    -14    382   -644       C  
ATOM    802  CG2 VAL A 134      17.062 -55.685 -14.935  1.00 25.99           C  
ANISOU  802  CG2 VAL A 134     2509   3664   3702     56    308   -619       C  
ATOM    803  N   ALA A 135      19.897 -54.316 -11.518  1.00 27.04           N  
ANISOU  803  N   ALA A 135     2474   3895   3906    -73    272   -782       N  
ATOM    804  CA  ALA A 135      20.495 -53.447 -10.486  1.00 28.05           C  
ANISOU  804  CA  ALA A 135     2575   4044   4039   -122    280   -832       C  
ATOM    805  C   ALA A 135      21.970 -53.112 -10.858  1.00 29.43           C  
ANISOU  805  C   ALA A 135     2681   4228   4273   -162    324   -919       C  
ATOM    806  O   ALA A 135      22.387 -51.961 -10.710  1.00 30.53           O  
ANISOU  806  O   ALA A 135     2823   4358   4417   -216    394   -966       O  
ATOM    807  CB  ALA A 135      20.419 -54.107  -9.117  1.00 28.47           C  
ANISOU  807  CB  ALA A 135     2600   4138   4081   -105    176   -820       C  
ATOM    808  N   SER A 136      22.732 -54.080 -11.398  1.00 29.82           N  
ANISOU  808  N   SER A 136     2670   4290   4368   -138    294   -943       N  
ATOM    809  CA  SER A 136      24.125 -53.819 -11.828  1.00 30.81           C  
ANISOU  809  CA  SER A 136     2725   4422   4558   -175    341  -1028       C  
ATOM    810  C   SER A 136      24.170 -52.814 -12.993  1.00 30.88           C  
ANISOU  810  C   SER A 136     2785   4378   4570   -209    472  -1046       C  
ATOM    811  O   SER A 136      24.999 -51.900 -12.995  1.00 31.46           O  
ANISOU  811  O   SER A 136     2831   4445   4675   -265    543  -1116       O  
ATOM    812  CB  SER A 136      24.830 -55.114 -12.211  1.00 33.83           C  
ANISOU  812  CB  SER A 136     3039   4826   4987   -134    283  -1042       C  
ATOM    813  OG  SER A 136      26.110 -54.864 -12.774  1.00 38.65           O  
ANISOU  813  OG  SER A 136     3583   5436   5665   -168    340  -1123       O  
ATOM    814  N   LEU A 137      23.243 -52.948 -13.956  1.00 29.65           N  
ANISOU  814  N   LEU A 137     2709   4180   4378   -174    505   -984       N  
ATOM    815  CA  LEU A 137      23.162 -52.025 -15.081  1.00 29.84           C  
ANISOU  815  CA  LEU A 137     2801   4147   4392   -195    627   -992       C  
ATOM    816  C   LEU A 137      22.749 -50.629 -14.649  1.00 29.95           C  
ANISOU  816  C   LEU A 137     2871   4141   4367   -238    695   -995       C  
ATOM    817  O   LEU A 137      23.214 -49.647 -15.220  1.00 30.64           O  
ANISOU  817  O   LEU A 137     2986   4191   4466   -279    805  -1038       O  
ATOM    818  CB  LEU A 137      22.232 -52.575 -16.168  1.00 29.61           C  
ANISOU  818  CB  LEU A 137     2843   4082   4326   -140    631   -924       C  
ATOM    819  CG  LEU A 137      22.770 -53.829 -16.849  1.00 30.50           C  
ANISOU  819  CG  LEU A 137     2910   4200   4479   -105    592   -930       C  
ATOM    820  CD1 LEU A 137      21.731 -54.415 -17.795  1.00 30.65           C  
ANISOU  820  CD1 LEU A 137     3002   4188   4456    -51    582   -861       C  
ATOM    821  CD2 LEU A 137      24.085 -53.537 -17.591  1.00 31.52           C  
ANISOU  821  CD2 LEU A 137     2999   4308   4668   -141    676  -1007       C  
ATOM    822  N   ASN A 138      21.905 -50.527 -13.610  1.00 29.02           N  
ANISOU  822  N   ASN A 138     2774   4045   4207   -230    637   -951       N  
ATOM    823  CA  ASN A 138      21.529 -49.237 -13.039  1.00 30.20           C  
ANISOU  823  CA  ASN A 138     2975   4180   4320   -271    695   -954       C  
ATOM    824  C   ASN A 138      22.777 -48.469 -12.531  1.00 31.95           C  
ANISOU  824  C   ASN A 138     3137   4416   4587   -342    739  -1047       C  
ATOM    825  O   ASN A 138      22.749 -47.246 -12.471  1.00 32.56           O  
ANISOU  825  O   ASN A 138     3261   4465   4646   -387    828  -1068       O  
ATOM    826  CB  ASN A 138      20.541 -49.436 -11.880  1.00 30.00           C  
ANISOU  826  CB  ASN A 138     2967   4180   4250   -249    612   -897       C  
ATOM    827  CG  ASN A 138      20.142 -48.125 -11.239  1.00 30.19           C  
ANISOU  827  CG  ASN A 138     3046   4189   4237   -291    672   -898       C  
ATOM    828  ND2 ASN A 138      20.553 -47.908 -10.001  1.00 33.40           N  
ANISOU  828  ND2 ASN A 138     3411   4630   4649   -326    631   -932       N  
ATOM    829  OD1 ASN A 138      19.504 -47.300 -11.865  1.00 29.27           O  
ANISOU  829  OD1 ASN A 138     3010   4026   4084   -289    755   -871       O  
ATOM    830  N   GLY A 139      23.807 -49.192 -12.112  1.00 33.16           N  
ANISOU  830  N   GLY A 139     3188   4615   4797   -349    674  -1100       N  
ATOM    831  CA  GLY A 139      25.031 -48.576 -11.620  1.00 35.69           C  
ANISOU  831  CA  GLY A 139     3436   4956   5167   -415    704  -1195       C  
ATOM    832  C   GLY A 139      26.172 -48.599 -12.624  1.00 37.93           C  
ANISOU  832  C   GLY A 139     3670   5224   5519   -439    775  -1265       C  
ATOM    833  O   GLY A 139      27.324 -48.386 -12.236  1.00 38.92           O  
ANISOU  833  O   GLY A 139     3708   5378   5703   -487    780  -1352       O  
ATOM    834  N   THR A 140      25.857 -48.815 -13.926  1.00 37.90           N  
ANISOU  834  N   THR A 140     3722   5171   5508   -408    835  -1231       N  
ATOM    835  CA  THR A 140      26.834 -48.873 -15.031  1.00 38.79           C  
ANISOU  835  CA  THR A 140     3804   5254   5679   -424    916  -1288       C  
ATOM    836  C   THR A 140      26.610 -47.668 -15.951  1.00 39.79           C  
ANISOU  836  C   THR A 140     4031   5307   5779   -456   1066  -1292       C  
ATOM    837  O   THR A 140      25.602 -47.613 -16.658  1.00 39.03           O  
ANISOU  837  O   THR A 140     4036   5169   5624   -414   1093  -1221       O  
ATOM    838  CB  THR A 140      26.678 -50.210 -15.787  1.00 39.65           C  
ANISOU  838  CB  THR A 140     3904   5364   5797   -357    858  -1243       C  
ATOM    839  CG2 THR A 140      27.690 -50.352 -16.939  1.00 39.60           C  
ANISOU  839  CG2 THR A 140     3868   5325   5853   -371    941  -1300       C  
ATOM    840  OG1 THR A 140      26.840 -51.290 -14.863  1.00 40.37           O  
ANISOU  840  OG1 THR A 140     3912   5519   5906   -325    722  -1236       O  
ATOM    841  N   SER A 141      27.530 -46.683 -15.923  1.00 41.26           N  
ANISOU  841  N   SER A 141     4193   5478   6006   -530   1164  -1378       N  
ATOM    842  CA  SER A 141      27.376 -45.437 -16.688  1.00 42.66           C  
ANISOU  842  CA  SER A 141     4472   5581   6155   -565   1317  -1389       C  
ATOM    843  C   SER A 141      27.124 -45.614 -18.194  1.00 43.22           C  
ANISOU  843  C   SER A 141     4626   5585   6209   -525   1395  -1355       C  
ATOM    844  O   SER A 141      26.459 -44.769 -18.789  1.00 44.64           O  
ANISOU  844  O   SER A 141     4925   5705   6332   -520   1488  -1321       O  
ATOM    845  CB  SER A 141      28.556 -44.497 -16.456  1.00 44.57           C  
ANISOU  845  CB  SER A 141     4661   5816   6457   -655   1412  -1498       C  
ATOM    846  OG  SER A 141      29.742 -45.066 -16.978  1.00 48.47           O  
ANISOU  846  OG  SER A 141     5062   6318   7037   -671   1428  -1568       O  
ATOM    847  N   SER A 142      27.607 -46.697 -18.802  1.00 42.53           N  
ANISOU  847  N   SER A 142     4486   5508   6167   -492   1356  -1361       N  
ATOM    848  CA  SER A 142      27.390 -46.937 -20.233  1.00 42.56           C  
ANISOU  848  CA  SER A 142     4571   5448   6152   -452   1424  -1330       C  
ATOM    849  C   SER A 142      26.001 -47.528 -20.561  1.00 42.03           C  
ANISOU  849  C   SER A 142     4587   5375   6006   -371   1352  -1222       C  
ATOM    850  O   SER A 142      25.641 -47.628 -21.733  1.00 42.46           O  
ANISOU  850  O   SER A 142     4727   5376   6031   -333   1404  -1189       O  
ATOM    851  CB  SER A 142      28.469 -47.868 -20.777  1.00 44.17           C  
ANISOU  851  CB  SER A 142     4687   5661   6436   -450   1417  -1380       C  
ATOM    852  OG  SER A 142      28.327 -49.170 -20.229  1.00 47.33           O  
ANISOU  852  OG  SER A 142     5009   6126   6849   -401   1268  -1346       O  
ATOM    853  N   SER A 143      25.241 -47.957 -19.541  1.00 40.48           N  
ANISOU  853  N   SER A 143     4365   5234   5780   -344   1231  -1172       N  
ATOM    854  CA  SER A 143      23.940 -48.575 -19.771  1.00 39.38           C  
ANISOU  854  CA  SER A 143     4290   5096   5578   -272   1157  -1077       C  
ATOM    855  C   SER A 143      22.845 -47.565 -20.009  1.00 37.86           C  
ANISOU  855  C   SER A 143     4218   4859   5306   -259   1217  -1027       C  
ATOM    856  O   SER A 143      22.754 -46.572 -19.288  1.00 37.50           O  
ANISOU  856  O   SER A 143     4189   4815   5245   -299   1255  -1041       O  
ATOM    857  CB  SER A 143      23.542 -49.449 -18.579  1.00 40.14           C  
ANISOU  857  CB  SER A 143     4315   5264   5674   -249   1012  -1044       C  
ATOM    858  OG  SER A 143      22.330 -50.139 -18.852  1.00 41.12           O  
ANISOU  858  OG  SER A 143     4492   5387   5746   -183    944   -960       O  
ATOM    859  N   PRO A 144      21.912 -47.874 -20.928  1.00 36.48           N  
ANISOU  859  N   PRO A 144     4129   4652   5079   -196   1213   -961       N  
ATOM    860  CA  PRO A 144      20.755 -46.983 -21.113  1.00 35.28           C  
ANISOU  860  CA  PRO A 144     4090   4465   4849   -170   1254   -907       C  
ATOM    861  C   PRO A 144      19.904 -46.824 -19.840  1.00 34.32           C  
ANISOU  861  C   PRO A 144     3952   4389   4699   -169   1177   -866       C  
ATOM    862  O   PRO A 144      19.198 -45.821 -19.717  1.00 35.07           O  
ANISOU  862  O   PRO A 144     4126   4459   4742   -168   1229   -840       O  
ATOM    863  CB  PRO A 144      19.964 -47.679 -22.225  1.00 35.90           C  
ANISOU  863  CB  PRO A 144     4234   4519   4888    -97   1226   -848       C  
ATOM    864  CG  PRO A 144      20.994 -48.508 -22.970  1.00 36.93           C  
ANISOU  864  CG  PRO A 144     4317   4640   5074   -101   1235   -890       C  
ATOM    865  CD  PRO A 144      21.874 -49.013 -21.868  1.00 35.89           C  
ANISOU  865  CD  PRO A 144     4054   4570   5012   -145   1172   -937       C  
ATOM    866  N   ILE A 145      19.966 -47.783 -18.883  1.00 32.76           N  
ANISOU  866  N   ILE A 145     3659   4255   4532   -167   1059   -861       N  
ATOM    867  CA  ILE A 145      19.178 -47.627 -17.636  1.00 31.66           C  
ANISOU  867  CA  ILE A 145     3510   4153   4365   -167    992   -824       C  
ATOM    868  C   ILE A 145      19.993 -47.103 -16.459  1.00 32.71           C  
ANISOU  868  C   ILE A 145     3579   4318   4533   -234    996   -883       C  
ATOM    869  O   ILE A 145      19.549 -47.192 -15.306  1.00 31.69           O  
ANISOU  869  O   ILE A 145     3424   4226   4390   -237    925   -861       O  
ATOM    870  CB  ILE A 145      18.406 -48.910 -17.235  1.00 30.14           C  
ANISOU  870  CB  ILE A 145     3281   4003   4166   -116    861   -766       C  
ATOM    871  CG1 ILE A 145      19.352 -50.093 -17.034  1.00 30.11           C  
ANISOU  871  CG1 ILE A 145     3177   4040   4224   -119    788   -802       C  
ATOM    872  CG2 ILE A 145      17.334 -49.226 -18.254  1.00 29.66           C  
ANISOU  872  CG2 ILE A 145     3295   3914   4061    -52    855   -704       C  
ATOM    873  CD1 ILE A 145      18.654 -51.320 -16.360  1.00 30.04           C  
ANISOU  873  CD1 ILE A 145     3129   4074   4209    -76    660   -750       C  
ATOM    874  N   TYR A 146      21.164 -46.500 -16.723  1.00 33.60           N  
ANISOU  874  N   TYR A 146     3668   4412   4687   -290   1083   -960       N  
ATOM    875  CA  TYR A 146      21.990 -45.925 -15.658  1.00 34.45           C  
ANISOU  875  CA  TYR A 146     3712   4548   4828   -358   1091  -1026       C  
ATOM    876  C   TYR A 146      21.197 -44.902 -14.830  1.00 33.95           C  
ANISOU  876  C   TYR A 146     3710   4478   4711   -376   1114   -998       C  
ATOM    877  O   TYR A 146      20.652 -43.957 -15.391  1.00 34.75           O  
ANISOU  877  O   TYR A 146     3910   4527   4767   -374   1209   -975       O  
ATOM    878  CB  TYR A 146      23.208 -45.230 -16.277  1.00 35.82           C  
ANISOU  878  CB  TYR A 146     3872   4687   5050   -417   1210  -1112       C  
ATOM    879  CG  TYR A 146      24.119 -44.569 -15.266  1.00 37.97           C  
ANISOU  879  CG  TYR A 146     4077   4988   5362   -494   1227  -1191       C  
ATOM    880  CD1 TYR A 146      24.722 -45.305 -14.259  1.00 39.53           C  
ANISOU  880  CD1 TYR A 146     4160   5254   5604   -505   1117  -1225       C  
ATOM    881  CD2 TYR A 146      24.436 -43.220 -15.364  1.00 40.50           C  
ANISOU  881  CD2 TYR A 146     4447   5264   5676   -555   1356  -1238       C  
ATOM    882  CE1 TYR A 146      25.606 -44.716 -13.362  1.00 41.57           C  
ANISOU  882  CE1 TYR A 146     4353   5542   5901   -575   1127  -1305       C  
ATOM    883  CE2 TYR A 146      25.299 -42.615 -14.461  1.00 42.23           C  
ANISOU  883  CE2 TYR A 146     4600   5509   5934   -631   1373  -1318       C  
ATOM    884  CZ  TYR A 146      25.888 -43.368 -13.464  1.00 43.79           C  
ANISOU  884  CZ  TYR A 146     4680   5780   6177   -641   1255  -1353       C  
ATOM    885  OH  TYR A 146      26.743 -42.770 -12.560  1.00 47.02           O  
ANISOU  885  OH  TYR A 146     5023   6220   6625   -714   1264  -1437       O  
ATOM    886  N   GLY A 147      21.078 -45.148 -13.531  1.00 33.76           N  
ANISOU  886  N   GLY A 147     3634   4505   4688   -387   1025   -993       N  
ATOM    887  CA  GLY A 147      20.361 -44.266 -12.612  1.00 33.50           C  
ANISOU  887  CA  GLY A 147     3652   4469   4606   -406   1038   -968       C  
ATOM    888  C   GLY A 147      18.852 -44.214 -12.778  1.00 32.93           C  
ANISOU  888  C   GLY A 147     3669   4376   4469   -347   1026   -874       C  
ATOM    889  O   GLY A 147      18.200 -43.349 -12.185  1.00 33.65           O  
ANISOU  889  O   GLY A 147     3816   4453   4516   -360   1059   -850       O  
ATOM    890  N   LYS A 148      18.266 -45.135 -13.571  1.00 31.22           N  
ANISOU  890  N   LYS A 148     3463   4156   4244   -283    980   -823       N  
ATOM    891  CA  LYS A 148      16.809 -45.114 -13.790  1.00 29.78           C  
ANISOU  891  CA  LYS A 148     3357   3955   4004   -225    966   -739       C  
ATOM    892  C   LYS A 148      16.004 -45.990 -12.818  1.00 27.71           C  
ANISOU  892  C   LYS A 148     3060   3736   3732   -193    848   -687       C  
ATOM    893  O   LYS A 148      14.782 -45.857 -12.742  1.00 27.01           O  
ANISOU  893  O   LYS A 148     3026   3636   3600   -155    837   -624       O  
ATOM    894  CB  LYS A 148      16.479 -45.543 -15.231  1.00 30.80           C  
ANISOU  894  CB  LYS A 148     3528   4053   4123   -171    985   -711       C  
ATOM    895  CG  LYS A 148      16.819 -44.500 -16.299  1.00 35.09           C  
ANISOU  895  CG  LYS A 148     4149   4536   4650   -184   1118   -738       C  
ATOM    896  CD  LYS A 148      16.141 -44.837 -17.613  1.00 40.01           C  
ANISOU  896  CD  LYS A 148     4837   5125   5240   -117   1127   -692       C  
ATOM    897  CE  LYS A 148      16.227 -43.734 -18.647  1.00 44.87           C  
ANISOU  897  CE  LYS A 148     5555   5672   5821   -116   1259   -704       C  
ATOM    898  NZ  LYS A 148      17.631 -43.460 -19.045  1.00 48.72           N1+
ANISOU  898  NZ  LYS A 148     6019   6137   6356   -173   1342   -784       N1+
ATOM    899  N   VAL A 149      16.676 -46.871 -12.089  1.00 27.04           N  
ANISOU  899  N   VAL A 149     2889   3697   3688   -207    764   -715       N  
ATOM    900  CA  VAL A 149      16.017 -47.856 -11.238  1.00 26.90           C  
ANISOU  900  CA  VAL A 149     2841   3716   3663   -174    653   -670       C  
ATOM    901  C   VAL A 149      16.158 -47.587  -9.745  1.00 26.80           C  
ANISOU  901  C   VAL A 149     2806   3732   3646   -210    616   -685       C  
ATOM    902  O   VAL A 149      17.245 -47.244  -9.267  1.00 27.87           O  
ANISOU  902  O   VAL A 149     2896   3884   3809   -260    627   -751       O  
ATOM    903  CB  VAL A 149      16.592 -49.270 -11.548  1.00 27.55           C  
ANISOU  903  CB  VAL A 149     2852   3828   3789   -147    573   -682       C  
ATOM    904  CG1 VAL A 149      15.845 -50.365 -10.784  1.00 27.61           C  
ANISOU  904  CG1 VAL A 149     2840   3864   3787   -108    467   -631       C  
ATOM    905  CG2 VAL A 149      16.610 -49.567 -13.059  1.00 27.92           C  
ANISOU  905  CG2 VAL A 149     2921   3844   3843   -116    612   -675       C  
ATOM    906  N   ASP A 150      15.072 -47.814  -8.992  1.00 24.08           N  
ANISOU  906  N   ASP A 150     2488   3392   3267   -184    567   -626       N  
ATOM    907  CA  ASP A 150      15.109 -47.837  -7.542  1.00 23.82           C  
ANISOU  907  CA  ASP A 150     2438   3387   3226   -206    514   -631       C  
ATOM    908  C   ASP A 150      15.270 -49.327  -7.260  1.00 24.76           C  
ANISOU  908  C   ASP A 150     2498   3541   3370   -170    405   -621       C  
ATOM    909  O   ASP A 150      14.289 -50.089  -7.307  1.00 23.79           O  
ANISOU  909  O   ASP A 150     2393   3415   3232   -124    360   -562       O  
ATOM    910  CB  ASP A 150      13.802 -47.328  -6.908  1.00 22.93           C  
ANISOU  910  CB  ASP A 150     2393   3254   3065   -193    527   -570       C  
ATOM    911  CG  ASP A 150      13.877 -47.291  -5.384  1.00 25.49           C  
ANISOU  911  CG  ASP A 150     2709   3599   3376   -219    479   -577       C  
ATOM    912  OD1 ASP A 150      14.762 -47.975  -4.811  1.00 25.40           O  
ANISOU  912  OD1 ASP A 150     2636   3624   3390   -229    409   -616       O  
ATOM    913  OD2 ASP A 150      13.045 -46.577  -4.759  1.00 26.51           O1-
ANISOU  913  OD2 ASP A 150     2897   3709   3468   -226    511   -542       O1-
ATOM    914  N   THR A 151      16.506 -49.751  -6.982  1.00 25.69           N  
ANISOU  914  N   THR A 151     2545   3691   3526   -190    365   -681       N  
ATOM    915  CA  THR A 151      16.786 -51.181  -6.798  1.00 26.50           C  
ANISOU  915  CA  THR A 151     2592   3825   3652   -152    266   -676       C  
ATOM    916  C   THR A 151      16.187 -51.790  -5.526  1.00 25.33           C  
ANISOU  916  C   THR A 151     2455   3694   3477   -131    185   -638       C  
ATOM    917  O   THR A 151      16.224 -53.011  -5.364  1.00 26.25           O  
ANISOU  917  O   THR A 151     2541   3828   3604    -92    108   -623       O  
ATOM    918  CB  THR A 151      18.278 -51.439  -6.900  1.00 29.85           C  
ANISOU  918  CB  THR A 151     2936   4279   4126   -174    248   -752       C  
ATOM    919  CG2 THR A 151      18.872 -50.914  -8.221  1.00 30.68           C  
ANISOU  919  CG2 THR A 151     3034   4360   4262   -194    337   -790       C  
ATOM    920  OG1 THR A 151      18.901 -50.848  -5.755  1.00 32.41           O  
ANISOU  920  OG1 THR A 151     3238   4627   4448   -217    233   -800       O  
ATOM    921  N   ALA A 152      15.581 -50.978  -4.655  1.00 23.42           N  
ANISOU  921  N   ALA A 152     2263   3440   3197   -153    208   -619       N  
ATOM    922  CA  ALA A 152      14.880 -51.477  -3.480  1.00 23.68           C  
ANISOU  922  CA  ALA A 152     2321   3478   3199   -133    145   -578       C  
ATOM    923  C   ALA A 152      13.435 -51.897  -3.802  1.00 22.71           C  
ANISOU  923  C   ALA A 152     2247   3327   3055    -91    149   -501       C  
ATOM    924  O   ALA A 152      12.743 -52.394  -2.909  1.00 24.15           O  
ANISOU  924  O   ALA A 152     2454   3507   3214    -72    104   -462       O  
ATOM    925  CB  ALA A 152      14.850 -50.391  -2.402  1.00 24.76           C  
ANISOU  925  CB  ALA A 152     2495   3610   3304   -177    173   -592       C  
ATOM    926  N   ARG A 153      12.934 -51.622  -5.036  1.00 20.75           N  
ANISOU  926  N   ARG A 153     2017   3056   2811    -78    206   -480       N  
ATOM    927  CA  ARG A 153      11.524 -51.893  -5.337  1.00 20.26           C  
ANISOU  927  CA  ARG A 153     1996   2970   2730    -41    211   -413       C  
ATOM    928  C   ARG A 153      11.448 -52.776  -6.566  1.00 19.47           C  
ANISOU  928  C   ARG A 153     1873   2870   2654     -4    194   -402       C  
ATOM    929  O   ARG A 153      11.659 -52.318  -7.692  1.00 19.40           O  
ANISOU  929  O   ARG A 153     1869   2849   2653     -5    247   -416       O  
ATOM    930  CB  ARG A 153      10.790 -50.562  -5.555  1.00 20.18           C  
ANISOU  930  CB  ARG A 153     2046   2930   2691    -56    298   -393       C  
ATOM    931  CG  ARG A 153      10.848 -49.716  -4.276  1.00 21.40           C  
ANISOU  931  CG  ARG A 153     2229   3082   2820    -95    315   -403       C  
ATOM    932  CD  ARG A 153       9.954 -48.498  -4.357  1.00 22.51           C  
ANISOU  932  CD  ARG A 153     2435   3189   2929   -103    398   -373       C  
ATOM    933  NE  ARG A 153      10.413 -47.524  -5.350  1.00 21.44           N  
ANISOU  933  NE  ARG A 153     2315   3037   2794   -121    479   -402       N  
ATOM    934  CZ  ARG A 153       9.726 -47.178  -6.440  1.00 20.84           C  
ANISOU  934  CZ  ARG A 153     2273   2936   2708    -91    529   -373       C  
ATOM    935  NH1 ARG A 153       8.583 -47.786  -6.734  1.00 19.50           N1+
ANISOU  935  NH1 ARG A 153     2113   2762   2534    -42    499   -318       N1+
ATOM    936  NH2 ARG A 153      10.185 -46.226  -7.250  1.00 20.82           N  
ANISOU  936  NH2 ARG A 153     2297   2913   2700   -109    611   -401       N  
ATOM    937  N   MET A 154      11.249 -54.077  -6.340  1.00 18.47           N  
ANISOU  937  N   MET A 154     1723   2756   2539     28    121   -382       N  
ATOM    938  CA  MET A 154      11.250 -55.065  -7.423  1.00 19.14           C  
ANISOU  938  CA  MET A 154     1783   2843   2647     62     96   -375       C  
ATOM    939  C   MET A 154      10.041 -55.989  -7.388  1.00 19.08           C  
ANISOU  939  C   MET A 154     1792   2826   2633     98     58   -321       C  
ATOM    940  O   MET A 154       9.432 -56.218  -6.340  1.00 19.05           O  
ANISOU  940  O   MET A 154     1806   2819   2614    101     32   -294       O  
ATOM    941  CB  MET A 154      12.563 -55.865  -7.411  1.00 20.48           C  
ANISOU  941  CB  MET A 154     1894   3039   2849     62     48   -420       C  
ATOM    942  CG  MET A 154      13.760 -55.018  -7.726  1.00 22.34           C  
ANISOU  942  CG  MET A 154     2104   3283   3103     25     93   -480       C  
ATOM    943  SD  MET A 154      15.224 -56.022  -7.561  1.00 24.90           S  
ANISOU  943  SD  MET A 154     2351   3643   3469     31     28   -533       S  
ATOM    944  CE  MET A 154      16.442 -54.980  -8.447  1.00 26.94           C  
ANISOU  944  CE  MET A 154     2580   3898   3759    -12    107   -604       C  
ATOM    945  N   GLY A 155       9.680 -56.491  -8.563  1.00 18.89           N  
ANISOU  945  N   GLY A 155     1765   2794   2621    126     60   -307       N  
ATOM    946  CA  GLY A 155       8.524 -57.366  -8.705  1.00 18.09           C  
ANISOU  946  CA  GLY A 155     1672   2682   2517    158     28   -263       C  
ATOM    947  C   GLY A 155       8.808 -58.511  -9.645  1.00 17.26           C  
ANISOU  947  C   GLY A 155     1540   2583   2436    183     -8   -269       C  
ATOM    948  O   GLY A 155       9.788 -58.476 -10.418  1.00 17.25           O  
ANISOU  948  O   GLY A 155     1518   2586   2450    180      5   -303       O  
ATOM    949  N   VAL A 156       7.955 -59.544  -9.573  1.00 16.33           N  
ANISOU  949  N   VAL A 156     1423   2460   2322    207    -48   -237       N  
ATOM    950  CA  VAL A 156       8.136 -60.760 -10.356  1.00 15.94           C  
ANISOU  950  CA  VAL A 156     1351   2412   2292    231    -85   -240       C  
ATOM    951  C   VAL A 156       6.874 -61.189 -11.059  1.00 16.39           C  
ANISOU  951  C   VAL A 156     1423   2456   2348    253    -89   -209       C  
ATOM    952  O   VAL A 156       5.785 -61.134 -10.496  1.00 15.67           O  
ANISOU  952  O   VAL A 156     1348   2357   2250    254    -89   -179       O  
ATOM    953  CB  VAL A 156       8.687 -61.898  -9.460  1.00 16.47           C  
ANISOU  953  CB  VAL A 156     1398   2490   2370    237   -141   -246       C  
ATOM    954  CG1 VAL A 156      10.164 -61.649  -9.109  1.00 17.60           C  
ANISOU  954  CG1 VAL A 156     1511   2653   2522    223   -148   -289       C  
ATOM    955  CG2 VAL A 156       7.837 -62.101  -8.198  1.00 15.70           C  
ANISOU  955  CG2 VAL A 156     1324   2384   2257    235   -158   -215       C  
ATOM    956  N   MET A 157       7.022 -61.635 -12.302  1.00 15.38           N  
ANISOU  956  N   MET A 157     1289   2325   2230    271    -92   -218       N  
ATOM    957  CA  MET A 157       5.883 -62.131 -13.092  1.00 15.91           C  
ANISOU  957  CA  MET A 157     1364   2382   2297    293   -104   -195       C  
ATOM    958  C   MET A 157       6.372 -63.322 -13.941  1.00 15.70           C  
ANISOU  958  C   MET A 157     1322   2356   2289    309   -136   -208       C  
ATOM    959  O   MET A 157       7.585 -63.541 -14.095  1.00 16.22           O  
ANISOU  959  O   MET A 157     1371   2426   2364    305   -137   -235       O  
ATOM    960  CB  MET A 157       5.342 -61.048 -14.024  1.00 15.99           C  
ANISOU  960  CB  MET A 157     1403   2384   2289    303    -61   -190       C  
ATOM    961  CG  MET A 157       4.720 -59.905 -13.241  1.00 17.37           C  
ANISOU  961  CG  MET A 157     1597   2556   2445    291    -27   -172       C  
ATOM    962  SD  MET A 157       4.188 -58.545 -14.311  1.00 17.91           S  
ANISOU  962  SD  MET A 157     1707   2612   2485    310     28   -167       S  
ATOM    963  CE  MET A 157       2.781 -59.296 -15.176  1.00 19.98           C  
ANISOU  963  CE  MET A 157     1965   2874   2751    348    -11   -145       C  
ATOM    964  N   GLY A 158       5.440 -64.097 -14.465  1.00 15.21           N  
ANISOU  964  N   GLY A 158     1263   2287   2231    326   -160   -192       N  
ATOM    965  CA  GLY A 158       5.815 -65.233 -15.315  1.00 16.54           C  
ANISOU  965  CA  GLY A 158     1421   2451   2412    340   -187   -204       C  
ATOM    966  C   GLY A 158       4.663 -66.158 -15.582  1.00 16.87           C  
ANISOU  966  C   GLY A 158     1462   2485   2460    351   -217   -187       C  
ATOM    967  O   GLY A 158       3.674 -66.159 -14.831  1.00 16.22           O  
ANISOU  967  O   GLY A 158     1379   2402   2380    344   -222   -167       O  
ATOM    968  N   HIS A 159       4.837 -67.001 -16.607  1.00 16.63           N  
ANISOU  968  N   HIS A 159     1434   2450   2437    364   -235   -197       N  
ATOM    969  CA  HIS A 159       3.784 -67.893 -17.038  1.00 16.96           C  
ANISOU  969  CA  HIS A 159     1474   2484   2485    372   -263   -189       C  
ATOM    970  C   HIS A 159       4.043 -69.347 -16.700  1.00 17.06           C  
ANISOU  970  C   HIS A 159     1477   2489   2517    369   -292   -191       C  
ATOM    971  O   HIS A 159       5.152 -69.827 -16.952  1.00 17.05           O  
ANISOU  971  O   HIS A 159     1474   2486   2520    375   -295   -205       O  
ATOM    972  CB  HIS A 159       3.649 -67.780 -18.573  1.00 17.92           C  
ANISOU  972  CB  HIS A 159     1612   2601   2594    391   -262   -200       C  
ATOM    973  CG  HIS A 159       2.662 -68.742 -19.172  1.00 17.64           C  
ANISOU  973  CG  HIS A 159     1575   2561   2567    398   -295   -200       C  
ATOM    974  CD2 HIS A 159       1.367 -68.974 -18.844  1.00 18.60           C  
ANISOU  974  CD2 HIS A 159     1682   2686   2699    393   -313   -189       C  
ATOM    975  ND1 HIS A 159       2.994 -69.508 -20.275  1.00 18.47           N  
ANISOU  975  ND1 HIS A 159     1692   2657   2670    409   -310   -215       N  
ATOM    976  CE1 HIS A 159       1.911 -70.224 -20.565  1.00 18.94           C  
ANISOU  976  CE1 HIS A 159     1745   2715   2738    409   -340   -215       C  
ATOM    977  NE2 HIS A 159       0.895 -69.935 -19.743  1.00 19.04           N  
ANISOU  977  NE2 HIS A 159     1738   2736   2761    399   -342   -201       N  
ATOM    978  N   SER A 160       3.046 -70.059 -16.158  1.00 16.89           N  
ANISOU  978  N   SER A 160     1450   2460   2506    361   -309   -178       N  
ATOM    979  CA  SER A 160       3.127 -71.509 -15.944  1.00 17.94           C  
ANISOU  979  CA  SER A 160     1583   2579   2653    360   -331   -179       C  
ATOM    980  C   SER A 160       4.295 -71.869 -15.021  1.00 18.59           C  
ANISOU  980  C   SER A 160     1668   2660   2736    362   -334   -179       C  
ATOM    981  O   SER A 160       4.275 -71.358 -13.900  1.00 17.61           O  
ANISOU  981  O   SER A 160     1544   2539   2606    354   -326   -168       O  
ATOM    982  CB  SER A 160       3.139 -72.216 -17.297  1.00 20.01           C  
ANISOU  982  CB  SER A 160     1850   2834   2918    370   -345   -194       C  
ATOM    983  OG  SER A 160       2.733 -73.558 -17.085  1.00 22.57           O  
ANISOU  983  OG  SER A 160     2177   3142   3257    363   -362   -193       O  
ATOM    984  N   MET A 161       5.321 -72.670 -15.431  1.00 18.23           N  
ANISOU  984  N   MET A 161     1622   2610   2694    376   -346   -193       N  
ATOM    985  CA  MET A 161       6.464 -72.906 -14.541  1.00 17.97           C  
ANISOU  985  CA  MET A 161     1586   2582   2661    385   -353   -196       C  
ATOM    986  C   MET A 161       7.166 -71.586 -14.160  1.00 18.25           C  
ANISOU  986  C   MET A 161     1607   2637   2689    380   -337   -204       C  
ATOM    987  O   MET A 161       7.752 -71.511 -13.075  1.00 18.56           O  
ANISOU  987  O   MET A 161     1644   2684   2724    381   -346   -204       O  
ATOM    988  CB  MET A 161       7.463 -73.876 -15.153  1.00 18.51           C  
ANISOU  988  CB  MET A 161     1652   2643   2738    404   -366   -211       C  
ATOM    989  CG  MET A 161       7.001 -75.314 -15.129  1.00 20.00           C  
ANISOU  989  CG  MET A 161     1860   2808   2931    410   -381   -202       C  
ATOM    990  SD  MET A 161       8.411 -76.320 -15.643  1.00 21.22           S  
ANISOU  990  SD  MET A 161     2013   2957   3094    438   -391   -218       S  
ATOM    991  CE  MET A 161       7.612 -77.976 -15.725  1.00 21.62           C  
ANISOU  991  CE  MET A 161     2097   2973   3147    440   -400   -207       C  
ATOM    992  N   GLY A 162       7.134 -70.584 -15.042  1.00 17.32           N  
ANISOU  992  N   GLY A 162     1487   2527   2567    374   -313   -214       N  
ATOM    993  CA  GLY A 162       7.688 -69.262 -14.721  1.00 17.88           C  
ANISOU  993  CA  GLY A 162     1550   2614   2630    364   -289   -224       C  
ATOM    994  C   GLY A 162       6.833 -68.499 -13.709  1.00 19.00           C  
ANISOU  994  C   GLY A 162     1700   2758   2760    349   -279   -204       C  
ATOM    995  O   GLY A 162       7.320 -67.586 -13.019  1.00 19.65           O  
ANISOU  995  O   GLY A 162     1779   2852   2835    337   -264   -210       O  
ATOM    996  N   GLY A 163       5.546 -68.848 -13.643  1.00 18.48           N  
ANISOU  996  N   GLY A 163     1645   2681   2694    347   -285   -183       N  
ATOM    997  CA  GLY A 163       4.590 -68.333 -12.661  1.00 18.51           C  
ANISOU  997  CA  GLY A 163     1658   2682   2691    334   -274   -162       C  
ATOM    998  C   GLY A 163       4.846 -68.989 -11.314  1.00 18.78           C  
ANISOU  998  C   GLY A 163     1701   2710   2726    331   -291   -153       C  
ATOM    999  O   GLY A 163       4.962 -68.311 -10.288  1.00 18.67           O  
ANISOU  999  O   GLY A 163     1696   2700   2700    322   -281   -147       O  
ATOM   1000  N   GLY A 164       5.060 -70.313 -11.318  1.00 17.72           N  
ANISOU 1000  N   GLY A 164     1570   2564   2600    343   -316   -154       N  
ATOM   1001  CA  GLY A 164       5.477 -71.009 -10.094  1.00 17.93           C  
ANISOU 1001  CA  GLY A 164     1613   2580   2619    350   -334   -148       C  
ATOM   1002  C   GLY A 164       6.829 -70.464  -9.628  1.00 17.94           C  
ANISOU 1002  C   GLY A 164     1602   2602   2610    357   -344   -166       C  
ATOM   1003  O   GLY A 164       7.026 -70.201  -8.439  1.00 17.86           O  
ANISOU 1003  O   GLY A 164     1607   2593   2585    356   -350   -161       O  
ATOM   1004  N   GLY A 165       7.732 -70.196 -10.569  1.00 18.13           N  
ANISOU 1004  N   GLY A 165     1601   2644   2644    363   -343   -190       N  
ATOM   1005  CA  GLY A 165       9.041 -69.610 -10.244  1.00 18.40           C  
ANISOU 1005  CA  GLY A 165     1613   2700   2677    364   -349   -215       C  
ATOM   1006  C   GLY A 165       8.896 -68.240  -9.599  1.00 18.12           C  
ANISOU 1006  C   GLY A 165     1581   2675   2627    341   -325   -216       C  
ATOM   1007  O   GLY A 165       9.655 -67.883  -8.694  1.00 17.75           O  
ANISOU 1007  O   GLY A 165     1529   2643   2573    339   -338   -230       O  
ATOM   1008  N   SER A 166       7.902 -67.450 -10.031  1.00 16.69           N  
ANISOU 1008  N   SER A 166     1412   2488   2443    325   -292   -201       N  
ATOM   1009  CA  SER A 166       7.662 -66.123  -9.458  1.00 15.75           C  
ANISOU 1009  CA  SER A 166     1302   2375   2308    303   -262   -198       C  
ATOM   1010  C   SER A 166       7.170 -66.248  -8.009  1.00 16.47           C  
ANISOU 1010  C   SER A 166     1419   2455   2383    299   -273   -178       C  
ATOM   1011  O   SER A 166       7.567 -65.452  -7.146  1.00 17.02           O  
ANISOU 1011  O   SER A 166     1496   2534   2438    285   -267   -185       O  
ATOM   1012  CB  SER A 166       6.604 -65.377 -10.285  1.00 16.82           C  
ANISOU 1012  CB  SER A 166     1447   2501   2441    296   -226   -184       C  
ATOM   1013  OG  SER A 166       7.091 -65.107 -11.592  1.00 17.49           O  
ANISOU 1013  OG  SER A 166     1520   2591   2532    301   -210   -204       O  
ATOM   1014  N   LEU A 167       6.300 -67.252  -7.753  1.00 16.90           N  
ANISOU 1014  N   LEU A 167     1492   2489   2440    308   -286   -154       N  
ATOM   1015  CA  LEU A 167       5.800 -67.508  -6.393  1.00 18.55           C  
ANISOU 1015  CA  LEU A 167     1735   2679   2633    306   -291   -133       C  
ATOM   1016  C   LEU A 167       6.936 -67.979  -5.503  1.00 19.16           C  
ANISOU 1016  C   LEU A 167     1820   2765   2697    322   -328   -147       C  
ATOM   1017  O   LEU A 167       7.013 -67.567  -4.340  1.00 19.32           O  
ANISOU 1017  O   LEU A 167     1866   2782   2694    317   -331   -142       O  
ATOM   1018  CB  LEU A 167       4.663 -68.524  -6.440  1.00 18.78           C  
ANISOU 1018  CB  LEU A 167     1781   2680   2673    310   -289   -110       C  
ATOM   1019  CG  LEU A 167       3.402 -67.990  -7.128  1.00 20.54           C  
ANISOU 1019  CG  LEU A 167     1995   2898   2911    296   -257    -98       C  
ATOM   1020  CD1 LEU A 167       2.588 -69.119  -7.737  1.00 21.34           C  
ANISOU 1020  CD1 LEU A 167     2091   2982   3033    301   -263    -92       C  
ATOM   1021  CD2 LEU A 167       2.565 -67.168  -6.159  1.00 22.03           C  
ANISOU 1021  CD2 LEU A 167     2207   3074   3089    279   -225    -77       C  
ATOM   1022  N   ILE A 168       7.850 -68.821  -6.058  1.00 18.51           N  
ANISOU 1022  N   ILE A 168     1714   2693   2626    345   -359   -165       N  
ATOM   1023  CA  ILE A 168       9.029 -69.262  -5.286  1.00 18.77           C  
ANISOU 1023  CA  ILE A 168     1746   2738   2647    368   -401   -183       C  
ATOM   1024  C   ILE A 168       9.931 -68.053  -4.997  1.00 18.58           C  
ANISOU 1024  C   ILE A 168     1696   2744   2618    352   -400   -213       C  
ATOM   1025  O   ILE A 168      10.441 -67.895  -3.882  1.00 18.93           O  
ANISOU 1025  O   ILE A 168     1754   2796   2640    358   -426   -221       O  
ATOM   1026  CB  ILE A 168       9.780 -70.343  -6.058  1.00 19.54           C  
ANISOU 1026  CB  ILE A 168     1820   2842   2764    396   -428   -198       C  
ATOM   1027  CG1 ILE A 168       8.907 -71.623  -6.134  1.00 20.01           C  
ANISOU 1027  CG1 ILE A 168     1914   2867   2823    410   -429   -170       C  
ATOM   1028  CG2 ILE A 168      11.156 -70.628  -5.412  1.00 20.66           C  
ANISOU 1028  CG2 ILE A 168     1946   3005   2898    424   -473   -224       C  
ATOM   1029  CD1 ILE A 168       9.488 -72.720  -7.057  1.00 22.09           C  
ANISOU 1029  CD1 ILE A 168     2158   3129   3105    435   -446   -181       C  
ATOM   1030  N   SER A 169      10.098 -67.147  -5.976  1.00 17.94           N  
ANISOU 1030  N   SER A 169     1583   2678   2554    330   -368   -230       N  
ATOM   1031  CA  SER A 169      10.898 -65.933  -5.771  1.00 18.24           C  
ANISOU 1031  CA  SER A 169     1599   2741   2590    307   -355   -262       C  
ATOM   1032  C   SER A 169      10.285 -65.104  -4.646  1.00 19.05           C  
ANISOU 1032  C   SER A 169     1739   2835   2664    287   -339   -245       C  
ATOM   1033  O   SER A 169      11.008 -64.673  -3.751  1.00 20.11           O  
ANISOU 1033  O   SER A 169     1872   2985   2784    281   -358   -267       O  
ATOM   1034  CB  SER A 169      10.943 -65.095  -7.045  1.00 18.44           C  
ANISOU 1034  CB  SER A 169     1601   2771   2635    287   -308   -276       C  
ATOM   1035  OG  SER A 169      11.775 -65.701  -8.023  1.00 18.67           O  
ANISOU 1035  OG  SER A 169     1594   2809   2689    303   -319   -300       O  
ATOM   1036  N   ALA A 170       8.949 -64.962  -4.625  1.00 18.18           N  
ANISOU 1036  N   ALA A 170     1663   2699   2546    278   -308   -208       N  
ATOM   1037  CA  ALA A 170       8.271 -64.195  -3.575  1.00 18.47           C  
ANISOU 1037  CA  ALA A 170     1739   2722   2557    258   -286   -189       C  
ATOM   1038  C   ALA A 170       8.421 -64.879  -2.208  1.00 19.79           C  
ANISOU 1038  C   ALA A 170     1943   2879   2699    275   -325   -181       C  
ATOM   1039  O   ALA A 170       8.655 -64.191  -1.200  1.00 20.89           O  
ANISOU 1039  O   ALA A 170     2105   3021   2813    262   -326   -187       O  
ATOM   1040  CB  ALA A 170       6.793 -64.060  -3.911  1.00 18.40           C  
ANISOU 1040  CB  ALA A 170     1751   2687   2552    251   -246   -153       C  
ATOM   1041  N   ALA A 171       8.293 -66.224  -2.168  1.00 19.17           N  
ANISOU 1041  N   ALA A 171     1876   2785   2624    305   -355   -167       N  
ATOM   1042  CA  ALA A 171       8.440 -66.932  -0.881  1.00 19.78           C  
ANISOU 1042  CA  ALA A 171     1999   2846   2670    328   -390   -157       C  
ATOM   1043  C   ALA A 171       9.857 -66.822  -0.363  1.00 21.14           C  
ANISOU 1043  C   ALA A 171     2153   3050   2829    343   -439   -194       C  
ATOM   1044  O   ALA A 171      10.043 -66.692   0.859  1.00 21.69           O  
ANISOU 1044  O   ALA A 171     2262   3114   2863    350   -461   -194       O  
ATOM   1045  CB  ALA A 171       8.077 -68.397  -1.058  1.00 20.06           C  
ANISOU 1045  CB  ALA A 171     2053   2856   2713    358   -405   -138       C  
ATOM   1046  N   ASN A 172      10.854 -66.882  -1.237  1.00 20.68           N  
ANISOU 1046  N   ASN A 172     2034   3024   2798    350   -458   -228       N  
ATOM   1047  CA  ASN A 172      12.257 -66.801  -0.789  1.00 20.90           C  
ANISOU 1047  CA  ASN A 172     2032   3087   2822    365   -508   -270       C  
ATOM   1048  C   ASN A 172      12.745 -65.396  -0.571  1.00 21.13           C  
ANISOU 1048  C   ASN A 172     2037   3142   2849    327   -491   -303       C  
ATOM   1049  O   ASN A 172      13.758 -65.203   0.112  1.00 20.85           O  
ANISOU 1049  O   ASN A 172     1985   3134   2804    335   -533   -339       O  
ATOM   1050  CB  ASN A 172      13.183 -67.497  -1.784  1.00 21.97           C  
ANISOU 1050  CB  ASN A 172     2109   3245   2992    389   -531   -297       C  
ATOM   1051  CG  ASN A 172      13.056 -68.997  -1.745  1.00 27.41           C  
ANISOU 1051  CG  ASN A 172     2824   3914   3677    435   -563   -274       C  
ATOM   1052  ND2 ASN A 172      13.436 -69.657  -2.839  1.00 26.66           N  
ANISOU 1052  ND2 ASN A 172     2691   3825   3614    450   -564   -283       N  
ATOM   1053  OD1 ASN A 172      12.625 -69.564  -0.726  1.00 31.40           O  
ANISOU 1053  OD1 ASN A 172     3389   4394   4147    457   -582   -249       O  
ATOM   1054  N   ASN A 173      12.073 -64.408  -1.162  1.00 20.07           N  
ANISOU 1054  N   ASN A 173     1901   2999   2725    288   -430   -293       N  
ATOM   1055  CA  ASN A 173      12.518 -63.032  -1.087  1.00 20.12           C  
ANISOU 1055  CA  ASN A 173     1889   3025   2731    249   -401   -325       C  
ATOM   1056  C   ASN A 173      11.364 -62.110  -0.709  1.00 20.76           C  
ANISOU 1056  C   ASN A 173     2020   3079   2789    218   -347   -292       C  
ATOM   1057  O   ASN A 173      10.852 -61.363  -1.560  1.00 20.07           O  
ANISOU 1057  O   ASN A 173     1925   2985   2716    195   -291   -285       O  
ATOM   1058  CB  ASN A 173      13.142 -62.595  -2.426  1.00 20.13           C  
ANISOU 1058  CB  ASN A 173     1831   3045   2772    232   -371   -358       C  
ATOM   1059  CG  ASN A 173      14.261 -63.490  -2.861  1.00 20.96           C  
ANISOU 1059  CG  ASN A 173     1884   3174   2904    262   -416   -390       C  
ATOM   1060  ND2 ASN A 173      15.461 -63.150  -2.434  1.00 18.38           N  
ANISOU 1060  ND2 ASN A 173     1517   2880   2585    256   -446   -441       N  
ATOM   1061  OD1 ASN A 173      14.056 -64.514  -3.555  1.00 23.41           O  
ANISOU 1061  OD1 ASN A 173     2190   3474   3230    290   -427   -371       O  
ATOM   1062  N   PRO A 174      10.954 -62.148   0.570  1.00 20.86           N  
ANISOU 1062  N   PRO A 174     2087   3075   2765    222   -362   -272       N  
ATOM   1063  CA  PRO A 174       9.838 -61.279   1.004  1.00 20.96           C  
ANISOU 1063  CA  PRO A 174     2149   3058   2757    195   -307   -240       C  
ATOM   1064  C   PRO A 174      10.094 -59.781   0.830  1.00 20.97           C  
ANISOU 1064  C   PRO A 174     2137   3072   2757    152   -260   -265       C  
ATOM   1065  O   PRO A 174       9.157 -59.009   0.948  1.00 21.58           O  
ANISOU 1065  O   PRO A 174     2250   3125   2822    131   -206   -238       O  
ATOM   1066  CB  PRO A 174       9.634 -61.639   2.480  1.00 22.22           C  
ANISOU 1066  CB  PRO A 174     2370   3197   2874    208   -337   -223       C  
ATOM   1067  CG  PRO A 174      10.393 -62.897   2.702  1.00 23.63           C  
ANISOU 1067  CG  PRO A 174     2539   3387   3051    252   -406   -236       C  
ATOM   1068  CD  PRO A 174      11.435 -63.033   1.651  1.00 21.42           C  
ANISOU 1068  CD  PRO A 174     2183   3146   2809    257   -427   -276       C  
ATOM   1069  N   SER A 175      11.344 -59.376   0.548  1.00 20.91           N  
ANISOU 1069  N   SER A 175     2081   3100   2764    138   -276   -318       N  
ATOM   1070  CA  SER A 175      11.719 -58.004   0.228  1.00 21.77           C  
ANISOU 1070  CA  SER A 175     2174   3219   2878     95   -224   -349       C  
ATOM   1071  C   SER A 175      11.143 -57.565  -1.135  1.00 21.20           C  
ANISOU 1071  C   SER A 175     2090   3135   2829     87   -161   -334       C  
ATOM   1072  O   SER A 175      11.089 -56.364  -1.399  1.00 21.81           O  
ANISOU 1072  O   SER A 175     2176   3207   2903     54   -101   -345       O  
ATOM   1073  CB  SER A 175      13.238 -57.845   0.187  1.00 24.98           C  
ANISOU 1073  CB  SER A 175     2523   3666   3303     84   -257   -415       C  
ATOM   1074  OG  SER A 175      13.886 -58.765  -0.683  1.00 30.28           O  
ANISOU 1074  OG  SER A 175     3139   4355   4010    112   -289   -432       O  
ATOM   1075  N   LEU A 176      10.703 -58.518  -1.986  1.00 20.08           N  
ANISOU 1075  N   LEU A 176     1934   2985   2708    118   -172   -309       N  
ATOM   1076  CA  LEU A 176      10.026 -58.143  -3.239  1.00 19.03           C  
ANISOU 1076  CA  LEU A 176     1801   2840   2591    116   -118   -291       C  
ATOM   1077  C   LEU A 176       8.709 -57.434  -2.918  1.00 18.93           C  
ANISOU 1077  C   LEU A 176     1838   2798   2556    107    -70   -249       C  
ATOM   1078  O   LEU A 176       8.080 -57.713  -1.890  1.00 19.30           O  
ANISOU 1078  O   LEU A 176     1920   2829   2583    112    -85   -221       O  
ATOM   1079  CB  LEU A 176       9.720 -59.393  -4.075  1.00 18.38           C  
ANISOU 1079  CB  LEU A 176     1699   2754   2531    152   -147   -273       C  
ATOM   1080  CG  LEU A 176      10.946 -60.060  -4.723  1.00 19.46           C  
ANISOU 1080  CG  LEU A 176     1785   2915   2696    165   -181   -312       C  
ATOM   1081  CD1 LEU A 176      10.600 -61.472  -5.213  1.00 20.70           C  
ANISOU 1081  CD1 LEU A 176     1934   3064   2867    201   -219   -289       C  
ATOM   1082  CD2 LEU A 176      11.497 -59.193  -5.868  1.00 20.40           C  
ANISOU 1082  CD2 LEU A 176     1879   3039   2833    145   -130   -343       C  
ATOM   1083  N   LYS A 177       8.302 -56.479  -3.776  1.00 18.64           N  
ANISOU 1083  N   LYS A 177     1809   2753   2521     96     -9   -244       N  
ATOM   1084  CA  LYS A 177       7.127 -55.660  -3.496  1.00 18.08           C  
ANISOU 1084  CA  LYS A 177     1784   2657   2430     89     41   -208       C  
ATOM   1085  C   LYS A 177       5.841 -56.129  -4.131  1.00 18.10           C  
ANISOU 1085  C   LYS A 177     1792   2642   2442    117     48   -165       C  
ATOM   1086  O   LYS A 177       4.762 -55.735  -3.676  1.00 17.82           O  
ANISOU 1086  O   LYS A 177     1789   2586   2395    118     77   -132       O  
ATOM   1087  CB  LYS A 177       7.395 -54.188  -3.881  1.00 20.55           C  
ANISOU 1087  CB  LYS A 177     2111   2966   2731     61    110   -227       C  
ATOM   1088  CG  LYS A 177       8.662 -53.626  -3.239  1.00 25.66           C  
ANISOU 1088  CG  LYS A 177     2748   3630   3371     24    108   -276       C  
ATOM   1089  CD  LYS A 177       8.623 -53.734  -1.739  1.00 28.72           C  
ANISOU 1089  CD  LYS A 177     3160   4016   3736     13     77   -270       C  
ATOM   1090  CE  LYS A 177       9.855 -53.136  -1.109  1.00 34.44           C  
ANISOU 1090  CE  LYS A 177     3873   4761   4453    -23     71   -324       C  
ATOM   1091  NZ  LYS A 177       9.918 -53.461   0.345  1.00 36.26           N1+
ANISOU 1091  NZ  LYS A 177     4128   4993   4658    -25     23   -321       N1+
ATOM   1092  N   ALA A 178       5.926 -56.980  -5.169  1.00 17.40           N  
ANISOU 1092  N   ALA A 178     1672   2562   2377    141     22   -169       N  
ATOM   1093  CA  ALA A 178       4.702 -57.464  -5.827  1.00 17.12           C  
ANISOU 1093  CA  ALA A 178     1637   2514   2353    168     22   -135       C  
ATOM   1094  C   ALA A 178       5.004 -58.674  -6.665  1.00 16.85           C  
ANISOU 1094  C   ALA A 178     1570   2490   2343    190    -22   -144       C  
ATOM   1095  O   ALA A 178       6.123 -58.820  -7.185  1.00 16.81           O  
ANISOU 1095  O   ALA A 178     1540   2500   2346    188    -34   -177       O  
ATOM   1096  CB  ALA A 178       4.109 -56.377  -6.723  1.00 17.88           C  
ANISOU 1096  CB  ALA A 178     1750   2603   2442    173     78   -126       C  
ATOM   1097  N   ALA A 179       3.999 -59.517  -6.855  1.00 16.37           N  
ANISOU 1097  N   ALA A 179     1507   2419   2295    209    -41   -118       N  
ATOM   1098  CA  ALA A 179       4.116 -60.662  -7.749  1.00 16.39           C  
ANISOU 1098  CA  ALA A 179     1481   2426   2318    230    -78   -125       C  
ATOM   1099  C   ALA A 179       2.821 -60.756  -8.554  1.00 16.31           C  
ANISOU 1099  C   ALA A 179     1471   2408   2318    248    -68   -102       C  
ATOM   1100  O   ALA A 179       1.741 -60.513  -8.008  1.00 16.93           O  
ANISOU 1100  O   ALA A 179     1563   2474   2396    246    -51    -77       O  
ATOM   1101  CB  ALA A 179       4.334 -61.942  -6.949  1.00 16.32           C  
ANISOU 1101  CB  ALA A 179     1469   2414   2316    235   -124   -122       C  
ATOM   1102  N   ALA A 180       2.908 -61.101  -9.851  1.00 16.24           N  
ANISOU 1102  N   ALA A 180     1446   2405   2318    266    -79   -113       N  
ATOM   1103  CA  ALA A 180       1.681 -61.245 -10.647  1.00 16.00           C  
ANISOU 1103  CA  ALA A 180     1413   2371   2297    286    -79    -97       C  
ATOM   1104  C   ALA A 180       1.841 -62.365 -11.683  1.00 16.21           C  
ANISOU 1104  C   ALA A 180     1419   2401   2340    302   -116   -109       C  
ATOM   1105  O   ALA A 180       1.855 -62.108 -12.911  1.00 16.93           O  
ANISOU 1105  O   ALA A 180     1512   2495   2425    320   -112   -119       O  
ATOM   1106  CB  ALA A 180       1.290 -59.926 -11.304  1.00 16.51           C  
ANISOU 1106  CB  ALA A 180     1496   2435   2343    296    -37    -92       C  
ATOM   1107  N   PRO A 181       1.969 -63.609 -11.200  1.00 15.43           N  
ANISOU 1107  N   PRO A 181     1308   2298   2257    299   -151   -110       N  
ATOM   1108  CA  PRO A 181       2.099 -64.751 -12.127  1.00 15.50           C  
ANISOU 1108  CA  PRO A 181     1301   2307   2280    312   -184   -121       C  
ATOM   1109  C   PRO A 181       0.816 -65.029 -12.905  1.00 15.69           C  
ANISOU 1109  C   PRO A 181     1317   2328   2315    325   -193   -113       C  
ATOM   1110  O   PRO A 181      -0.275 -64.668 -12.463  1.00 17.33           O  
ANISOU 1110  O   PRO A 181     1524   2532   2529    322   -180    -97       O  
ATOM   1111  CB  PRO A 181       2.407 -65.921 -11.191  1.00 17.27           C  
ANISOU 1111  CB  PRO A 181     1524   2523   2515    305   -211   -119       C  
ATOM   1112  CG  PRO A 181       1.683 -65.556  -9.911  1.00 16.91           C  
ANISOU 1112  CG  PRO A 181     1492   2466   2465    291   -193    -98       C  
ATOM   1113  CD  PRO A 181       1.926 -64.059  -9.791  1.00 15.36           C  
ANISOU 1113  CD  PRO A 181     1307   2279   2250    284   -159    -98       C  
ATOM   1114  N   GLN A 182       0.943 -65.759 -14.041  1.00 14.82           N  
ANISOU 1114  N   GLN A 182     1199   2220   2211    339   -217   -127       N  
ATOM   1115  CA  GLN A 182      -0.219 -66.086 -14.869  1.00 14.40           C  
ANISOU 1115  CA  GLN A 182     1135   2167   2168    352   -233   -127       C  
ATOM   1116  C   GLN A 182      -0.219 -67.571 -15.159  1.00 15.28           C  
ANISOU 1116  C   GLN A 182     1236   2272   2300    350   -267   -137       C  
ATOM   1117  O   GLN A 182       0.822 -68.161 -15.481  1.00 14.91           O  
ANISOU 1117  O   GLN A 182     1194   2221   2249    352   -278   -149       O  
ATOM   1118  CB  GLN A 182      -0.221 -65.275 -16.186  1.00 15.52           C  
ANISOU 1118  CB  GLN A 182     1290   2316   2289    377   -226   -135       C  
ATOM   1119  CG  GLN A 182       1.030 -65.526 -17.043  1.00 17.26           C  
ANISOU 1119  CG  GLN A 182     1524   2534   2498    384   -229   -155       C  
ATOM   1120  CD  GLN A 182       1.190 -64.411 -18.046  1.00 17.77           C  
ANISOU 1120  CD  GLN A 182     1618   2600   2535    406   -203   -160       C  
ATOM   1121  NE2 GLN A 182       1.300 -64.745 -19.349  1.00 17.76           N  
ANISOU 1121  NE2 GLN A 182     1632   2594   2522    427   -217   -174       N  
ATOM   1122  OE1 GLN A 182       1.215 -63.235 -17.671  1.00 18.34           O  
ANISOU 1122  OE1 GLN A 182     1705   2672   2590    405   -167   -152       O  
ATOM   1123  N   ALA A 183      -1.381 -68.200 -15.012  1.00 15.09           N  
ANISOU 1123  N   ALA A 183     1195   2242   2298    343   -279   -134       N  
ATOM   1124  CA  ALA A 183      -1.567 -69.681 -15.151  1.00 16.93           C  
ANISOU 1124  CA  ALA A 183     1419   2462   2551    334   -304   -144       C  
ATOM   1125  C   ALA A 183      -0.432 -70.454 -14.457  1.00 18.09           C  
ANISOU 1125  C   ALA A 183     1582   2596   2696    327   -306   -143       C  
ATOM   1126  O   ALA A 183       0.236 -71.312 -15.068  1.00 18.72           O  
ANISOU 1126  O   ALA A 183     1666   2671   2774    334   -324   -155       O  
ATOM   1127  CB  ALA A 183      -1.624 -70.051 -16.639  1.00 17.89           C  
ANISOU 1127  CB  ALA A 183     1538   2590   2669    350   -330   -163       C  
ATOM   1128  N   PRO A 184      -0.172 -70.128 -13.176  1.00 17.76           N  
ANISOU 1128  N   PRO A 184     1550   2548   2648    317   -288   -128       N  
ATOM   1129  CA  PRO A 184       0.987 -70.711 -12.510  1.00 18.32           C  
ANISOU 1129  CA  PRO A 184     1637   2612   2711    319   -295   -128       C  
ATOM   1130  C   PRO A 184       0.870 -72.194 -12.329  1.00 20.65           C  
ANISOU 1130  C   PRO A 184     1942   2886   3020    316   -310   -130       C  
ATOM   1131  O   PRO A 184      -0.220 -72.749 -12.191  1.00 21.39           O  
ANISOU 1131  O   PRO A 184     2033   2963   3132    303   -304   -128       O  
ATOM   1132  CB  PRO A 184       1.012 -69.981 -11.152  1.00 18.83           C  
ANISOU 1132  CB  PRO A 184     1716   2674   2765    309   -275   -112       C  
ATOM   1133  CG  PRO A 184      -0.424 -69.653 -10.902  1.00 19.33           C  
ANISOU 1133  CG  PRO A 184     1773   2730   2843    297   -256   -100       C  
ATOM   1134  CD  PRO A 184      -0.884 -69.193 -12.284  1.00 17.90           C  
ANISOU 1134  CD  PRO A 184     1570   2566   2666    307   -262   -111       C  
ATOM   1135  N   TRP A 185       2.023 -72.804 -12.296  1.00 21.17           N  
ANISOU 1135  N   TRP A 185     2017   2948   3077    329   -325   -137       N  
ATOM   1136  CA  TRP A 185       2.115 -74.207 -11.933  1.00 23.16           C  
ANISOU 1136  CA  TRP A 185     2288   3176   3335    332   -334   -136       C  
ATOM   1137  C   TRP A 185       3.344 -74.430 -11.107  1.00 22.60           C  
ANISOU 1137  C   TRP A 185     2235   3105   3248    350   -345   -133       C  
ATOM   1138  O   TRP A 185       4.419 -73.900 -11.396  1.00 21.67           O  
ANISOU 1138  O   TRP A 185     2102   3008   3121    363   -355   -144       O  
ATOM   1139  CB  TRP A 185       2.122 -75.147 -13.132  1.00 24.60           C  
ANISOU 1139  CB  TRP A 185     2466   3353   3529    337   -348   -151       C  
ATOM   1140  CG  TRP A 185       2.193 -76.611 -12.730  1.00 26.36           C  
ANISOU 1140  CG  TRP A 185     2715   3546   3756    340   -351   -150       C  
ATOM   1141  CD1 TRP A 185       1.148 -77.441 -12.435  1.00 27.45           C  
ANISOU 1141  CD1 TRP A 185     2866   3656   3909    321   -338   -147       C  
ATOM   1142  CD2 TRP A 185       3.387 -77.366 -12.478  1.00 27.00           C  
ANISOU 1142  CD2 TRP A 185     2816   3618   3825    364   -364   -150       C  
ATOM   1143  CE2 TRP A 185       2.991 -78.676 -12.119  1.00 27.74           C  
ANISOU 1143  CE2 TRP A 185     2941   3677   3923    362   -357   -146       C  
ATOM   1144  CE3 TRP A 185       4.759 -77.092 -12.622  1.00 27.73           C  
ANISOU 1144  CE3 TRP A 185     2900   3731   3908    388   -379   -157       C  
ATOM   1145  NE1 TRP A 185       1.620 -78.706 -12.123  1.00 27.52           N  
ANISOU 1145  NE1 TRP A 185     2907   3636   3912    332   -339   -146       N  
ATOM   1146  CZ2 TRP A 185       3.913 -79.686 -11.856  1.00 29.25           C  
ANISOU 1146  CZ2 TRP A 185     3160   3851   4103    388   -366   -144       C  
ATOM   1147  CZ3 TRP A 185       5.668 -78.078 -12.302  1.00 29.04           C  
ANISOU 1147  CZ3 TRP A 185     3084   3883   4066    414   -392   -158       C  
ATOM   1148  CH2 TRP A 185       5.247 -79.359 -11.925  1.00 29.75           C  
ANISOU 1148  CH2 TRP A 185     3211   3937   4155    417   -387   -149       C  
ATOM   1149  N   ASP A 186       3.197 -75.307 -10.123  1.00 22.68           N  
ANISOU 1149  N   ASP A 186     2276   3088   3253    353   -344   -122       N  
ATOM   1150  CA  ASP A 186       4.308 -75.814  -9.328  1.00 22.48           C  
ANISOU 1150  CA  ASP A 186     2274   3058   3209    379   -362   -120       C  
ATOM   1151  C   ASP A 186       3.877 -77.189  -8.818  1.00 22.80           C  
ANISOU 1151  C   ASP A 186     2356   3058   3249    384   -355   -110       C  
ATOM   1152  O   ASP A 186       2.673 -77.433  -8.665  1.00 22.04           O  
ANISOU 1152  O   ASP A 186     2271   2937   3165    360   -330   -103       O  
ATOM   1153  CB  ASP A 186       4.674 -74.902  -8.145  1.00 25.50           C  
ANISOU 1153  CB  ASP A 186     2667   3451   3571    381   -362   -112       C  
ATOM   1154  CG  ASP A 186       5.989 -75.312  -7.483  1.00 34.49           C  
ANISOU 1154  CG  ASP A 186     3820   4596   4690    414   -393   -118       C  
ATOM   1155  OD1 ASP A 186       7.037 -75.311  -8.173  1.00 35.68           O  
ANISOU 1155  OD1 ASP A 186     3940   4769   4846    431   -413   -137       O  
ATOM   1156  OD2 ASP A 186       5.957 -75.729  -6.308  1.00 39.14           O1-
ANISOU 1156  OD2 ASP A 186     4452   5163   5258    427   -396   -104       O1-
ATOM   1157  N   SER A 187       4.833 -78.053  -8.485  1.00 22.78           N  
ANISOU 1157  N   SER A 187     2378   3045   3231    416   -374   -111       N  
ATOM   1158  CA  SER A 187       4.504 -79.371  -7.912  1.00 23.82           C  
ANISOU 1158  CA  SER A 187     2562   3133   3355    426   -363   -100       C  
ATOM   1159  C   SER A 187       3.736 -79.197  -6.603  1.00 24.40           C  
ANISOU 1159  C   SER A 187     2677   3178   3414    414   -338    -81       C  
ATOM   1160  O   SER A 187       2.753 -79.899  -6.365  1.00 25.32           O  
ANISOU 1160  O   SER A 187     2826   3256   3540    395   -306    -75       O  
ATOM   1161  CB  SER A 187       5.782 -80.161  -7.625  1.00 25.61           C  
ANISOU 1161  CB  SER A 187     2813   3357   3561    472   -391   -101       C  
ATOM   1162  OG  SER A 187       6.439 -80.447  -8.844  1.00 29.32           O  
ANISOU 1162  OG  SER A 187     3248   3845   4047    482   -405   -118       O  
ATOM   1163  N   SER A 188       4.154 -78.212  -5.793  1.00 23.70           N  
ANISOU 1163  N   SER A 188     2590   3110   3307    421   -350    -76       N  
ATOM   1164  CA  SER A 188       3.498 -77.947  -4.524  1.00 24.21           C  
ANISOU 1164  CA  SER A 188     2699   3147   3354    411   -325    -57       C  
ATOM   1165  C   SER A 188       2.680 -76.682  -4.671  1.00 22.92           C  
ANISOU 1165  C   SER A 188     2500   3002   3208    375   -304    -56       C  
ATOM   1166  O   SER A 188       3.191 -75.692  -5.187  1.00 25.28           O  
ANISOU 1166  O   SER A 188     2754   3342   3510    373   -321    -67       O  
ATOM   1167  CB  SER A 188       4.540 -77.722  -3.426  1.00 27.29           C  
ANISOU 1167  CB  SER A 188     3121   3544   3705    447   -356    -53       C  
ATOM   1168  OG  SER A 188       3.925 -77.204  -2.252  1.00 30.80           O  
ANISOU 1168  OG  SER A 188     3608   3966   4129    434   -332    -36       O  
ATOM   1169  N   THR A 189       1.414 -76.703  -4.220  1.00 21.17           N  
ANISOU 1169  N   THR A 189     2298   2748   2999    347   -262    -45       N  
ATOM   1170  CA  THR A 189       0.588 -75.491  -4.282  1.00 21.20           C  
ANISOU 1170  CA  THR A 189     2269   2767   3018    317   -239    -42       C  
ATOM   1171  C   THR A 189       0.613 -74.710  -2.954  1.00 21.46           C  
ANISOU 1171  C   THR A 189     2341   2790   3024    317   -225    -25       C  
ATOM   1172  O   THR A 189      -0.097 -73.706  -2.830  1.00 22.62           O  
ANISOU 1172  O   THR A 189     2471   2944   3181    294   -200    -19       O  
ATOM   1173  CB  THR A 189      -0.846 -75.855  -4.617  1.00 22.69           C  
ANISOU 1173  CB  THR A 189     2445   2930   3244    286   -200    -43       C  
ATOM   1174  CG2 THR A 189      -0.988 -76.465  -6.011  1.00 23.19           C  
ANISOU 1174  CG2 THR A 189     2466   3008   3336    281   -216    -63       C  
ATOM   1175  OG1 THR A 189      -1.350 -76.740  -3.607  1.00 25.40           O  
ANISOU 1175  OG1 THR A 189     2849   3219   3582    281   -166    -32       O  
ATOM   1176  N   ASN A 190       1.459 -75.118  -1.995  1.00 20.61           N  
ANISOU 1176  N   ASN A 190     2285   2667   2877    346   -244    -19       N  
ATOM   1177  CA  ASN A 190       1.504 -74.477  -0.702  1.00 20.61           C  
ANISOU 1177  CA  ASN A 190     2332   2653   2845    348   -235     -4       C  
ATOM   1178  C   ASN A 190       2.433 -73.314  -0.702  1.00 20.51           C  
ANISOU 1178  C   ASN A 190     2289   2688   2816    354   -266    -15       C  
ATOM   1179  O   ASN A 190       3.642 -73.481  -0.574  1.00 22.10           O  
ANISOU 1179  O   ASN A 190     2492   2911   2995    384   -311    -26       O  
ATOM   1180  CB  ASN A 190       1.907 -75.491   0.375  1.00 22.31           C  
ANISOU 1180  CB  ASN A 190     2627   2827   3021    381   -241      6       C  
ATOM   1181  CG  ASN A 190       1.793 -74.936   1.776  1.00 26.28           C  
ANISOU 1181  CG  ASN A 190     3194   3305   3487    383   -226     23       C  
ATOM   1182  ND2 ASN A 190       1.990 -75.801   2.763  1.00 29.83           N  
ANISOU 1182  ND2 ASN A 190     3725   3710   3897    413   -225     34       N  
ATOM   1183  OD1 ASN A 190       1.513 -73.745   1.993  1.00 24.87           O  
ANISOU 1183  OD1 ASN A 190     2997   3143   3310    359   -212     25       O  
ATOM   1184  N   PHE A 191       1.883 -72.122  -0.788  1.00 19.46           N  
ANISOU 1184  N   PHE A 191     2130   2570   2693    326   -241    -12       N  
ATOM   1185  CA  PHE A 191       2.653 -70.872  -0.729  1.00 19.34           C  
ANISOU 1185  CA  PHE A 191     2091   2594   2663    323   -259    -22       C  
ATOM   1186  C   PHE A 191       2.210 -70.047   0.503  1.00 19.51           C  
ANISOU 1186  C   PHE A 191     2160   2595   2659    309   -230     -6       C  
ATOM   1187  O   PHE A 191       2.203 -68.814   0.479  1.00 19.89           O  
ANISOU 1187  O   PHE A 191     2188   2664   2704    290   -217     -9       O  
ATOM   1188  CB  PHE A 191       2.502 -70.075  -2.051  1.00 18.97           C  
ANISOU 1188  CB  PHE A 191     1977   2584   2647    306   -252    -35       C  
ATOM   1189  CG  PHE A 191       3.345 -70.708  -3.145  1.00 18.83           C  
ANISOU 1189  CG  PHE A 191     1920   2591   2643    324   -287    -56       C  
ATOM   1190  CD1 PHE A 191       4.701 -70.442  -3.238  1.00 18.87           C  
ANISOU 1190  CD1 PHE A 191     1906   2629   2635    341   -323    -77       C  
ATOM   1191  CD2 PHE A 191       2.789 -71.615  -4.032  1.00 19.10           C  
ANISOU 1191  CD2 PHE A 191     1938   2613   2704    325   -284    -56       C  
ATOM   1192  CE1 PHE A 191       5.485 -71.063  -4.204  1.00 20.34           C  
ANISOU 1192  CE1 PHE A 191     2059   2833   2836    359   -350    -96       C  
ATOM   1193  CE2 PHE A 191       3.580 -72.249  -5.001  1.00 20.37           C  
ANISOU 1193  CE2 PHE A 191     2072   2793   2876    342   -313    -74       C  
ATOM   1194  CZ  PHE A 191       4.916 -71.949  -5.090  1.00 20.42           C  
ANISOU 1194  CZ  PHE A 191     2060   2829   2869    360   -344    -92       C  
ATOM   1195  N   SER A 192       1.889 -70.755   1.600  1.00 19.64           N  
ANISOU 1195  N   SER A 192     2245   2565   2651    319   -218     11       N  
ATOM   1196  CA  SER A 192       1.361 -70.106   2.807  1.00 20.80           C  
ANISOU 1196  CA  SER A 192     2448   2681   2773    306   -183     29       C  
ATOM   1197  C   SER A 192       2.285 -69.072   3.443  1.00 21.31           C  
ANISOU 1197  C   SER A 192     2523   2773   2800    309   -210     19       C  
ATOM   1198  O   SER A 192       1.792 -68.203   4.159  1.00 22.53           O  
ANISOU 1198  O   SER A 192     2709   2913   2941    289   -175     32       O  
ATOM   1199  CB  SER A 192       0.966 -71.163   3.836  1.00 22.84           C  
ANISOU 1199  CB  SER A 192     2790   2879   3008    321   -164     47       C  
ATOM   1200  OG  SER A 192       2.097 -71.939   4.203  1.00 25.96           O  
ANISOU 1200  OG  SER A 192     3218   3279   3368    363   -218     38       O  
ATOM   1201  N   SER A 193       3.606 -69.160   3.192  1.00 20.84           N  
ANISOU 1201  N   SER A 193     2437   2755   2727    332   -269     -5       N  
ATOM   1202  CA  SER A 193       4.525 -68.178   3.809  1.00 20.91           C  
ANISOU 1202  CA  SER A 193     2449   2792   2703    332   -296    -22       C  
ATOM   1203  C   SER A 193       4.554 -66.835   3.090  1.00 20.87           C  
ANISOU 1203  C   SER A 193     2386   2823   2719    298   -275    -36       C  
ATOM   1204  O   SER A 193       5.144 -65.893   3.614  1.00 22.16           O  
ANISOU 1204  O   SER A 193     2555   3006   2858    288   -284    -51       O  
ATOM   1205  CB  SER A 193       5.957 -68.709   3.837  1.00 22.16           C  
ANISOU 1205  CB  SER A 193     2594   2983   2844    369   -366    -50       C  
ATOM   1206  OG  SER A 193       6.555 -68.642   2.545  1.00 23.85           O  
ANISOU 1206  OG  SER A 193     2727   3240   3096    366   -383    -74       O  
ATOM   1207  N   VAL A 194       4.011 -66.757   1.850  1.00 19.71           N  
ANISOU 1207  N   VAL A 194     2186   2689   2615    284   -251    -35       N  
ATOM   1208  CA  VAL A 194       4.149 -65.550   1.056  1.00 19.01           C  
ANISOU 1208  CA  VAL A 194     2047   2633   2542    261   -233    -49       C  
ATOM   1209  C   VAL A 194       3.475 -64.318   1.688  1.00 19.51           C  
ANISOU 1209  C   VAL A 194     2139   2682   2590    233   -184    -35       C  
ATOM   1210  O   VAL A 194       2.269 -64.300   1.948  1.00 20.42           O  
ANISOU 1210  O   VAL A 194     2279   2764   2715    222   -141     -7       O  
ATOM   1211  CB  VAL A 194       3.667 -65.799  -0.395  1.00 18.95           C  
ANISOU 1211  CB  VAL A 194     1987   2636   2576    259   -220    -50       C  
ATOM   1212  CG1 VAL A 194       3.657 -64.493  -1.183  1.00 18.50           C  
ANISOU 1212  CG1 VAL A 194     1894   2605   2530    239   -191    -60       C  
ATOM   1213  CG2 VAL A 194       4.553 -66.856  -1.094  1.00 19.22           C  
ANISOU 1213  CG2 VAL A 194     1991   2688   2622    285   -267    -69       C  
ATOM   1214  N   THR A 195       4.269 -63.269   1.881  1.00 18.68           N  
ANISOU 1214  N   THR A 195     2026   2603   2468    219   -188    -56       N  
ATOM   1215  CA  THR A 195       3.773 -61.992   2.407  1.00 19.48           C  
ANISOU 1215  CA  THR A 195     2154   2694   2553    191   -140    -46       C  
ATOM   1216  C   THR A 195       3.757 -60.881   1.345  1.00 19.37           C  
ANISOU 1216  C   THR A 195     2096   2705   2558    172   -107    -57       C  
ATOM   1217  O   THR A 195       3.309 -59.769   1.620  1.00 20.24           O  
ANISOU 1217  O   THR A 195     2227   2807   2657    150    -60    -47       O  
ATOM   1218  CB  THR A 195       4.584 -61.544   3.635  1.00 21.41           C  
ANISOU 1218  CB  THR A 195     2441   2941   2754    185   -162    -61       C  
ATOM   1219  CG2 THR A 195       4.388 -62.486   4.816  1.00 23.59           C  
ANISOU 1219  CG2 THR A 195     2782   3181   3000    206   -184    -43       C  
ATOM   1220  OG1 THR A 195       5.988 -61.451   3.293  1.00 22.24           O  
ANISOU 1220  OG1 THR A 195     2503   3090   2858    189   -210   -103       O  
ATOM   1221  N   VAL A 196       4.237 -61.187   0.131  1.00 18.13           N  
ANISOU 1221  N   VAL A 196     1886   2576   2428    182   -126    -76       N  
ATOM   1222  CA  VAL A 196       4.284 -60.266  -0.992  1.00 18.37           C  
ANISOU 1222  CA  VAL A 196     1881   2626   2473    171    -95    -88       C  
ATOM   1223  C   VAL A 196       2.892 -60.190  -1.615  1.00 18.73           C  
ANISOU 1223  C   VAL A 196     1924   2653   2539    175    -56    -57       C  
ATOM   1224  O   VAL A 196       2.273 -61.227  -1.856  1.00 18.71           O  
ANISOU 1224  O   VAL A 196     1915   2639   2557    191    -72    -43       O  
ATOM   1225  CB  VAL A 196       5.303 -60.822  -2.021  1.00 19.20           C  
ANISOU 1225  CB  VAL A 196     1937   2761   2599    184   -132   -119       C  
ATOM   1226  CG1 VAL A 196       5.336 -59.976  -3.293  1.00 20.22           C  
ANISOU 1226  CG1 VAL A 196     2037   2902   2741    177    -96   -130       C  
ATOM   1227  CG2 VAL A 196       6.704 -60.935  -1.413  1.00 20.07           C  
ANISOU 1227  CG2 VAL A 196     2038   2892   2695    184   -175   -154       C  
ATOM   1228  N   PRO A 197       2.420 -58.974  -1.942  1.00 19.18           N  
ANISOU 1228  N   PRO A 197     1986   2709   2593    162     -7    -50       N  
ATOM   1229  CA  PRO A 197       1.114 -58.829  -2.621  1.00 18.35           C  
ANISOU 1229  CA  PRO A 197     1872   2592   2507    173     25    -25       C  
ATOM   1230  C   PRO A 197       1.096 -59.572  -3.953  1.00 18.15           C  
ANISOU 1230  C   PRO A 197     1804   2583   2508    194     -2    -34       C  
ATOM   1231  O   PRO A 197       1.900 -59.269  -4.837  1.00 17.87           O  
ANISOU 1231  O   PRO A 197     1750   2569   2473    197     -8    -58       O  
ATOM   1232  CB  PRO A 197       1.043 -57.323  -2.877  1.00 18.63           C  
ANISOU 1232  CB  PRO A 197     1920   2631   2527    162     77    -25       C  
ATOM   1233  CG  PRO A 197       1.808 -56.734  -1.682  1.00 20.28           C  
ANISOU 1233  CG  PRO A 197     2164   2836   2705    136     84    -36       C  
ATOM   1234  CD  PRO A 197       3.012 -57.648  -1.645  1.00 19.97           C  
ANISOU 1234  CD  PRO A 197     2103   2817   2669    139     25    -66       C  
ATOM   1235  N   THR A 198       0.194 -60.547  -4.075  1.00 16.84           N  
ANISOU 1235  N   THR A 198     1628   2404   2366    207    -16    -19       N  
ATOM   1236  CA  THR A 198       0.220 -61.449  -5.227  1.00 16.02           C  
ANISOU 1236  CA  THR A 198     1489   2313   2286    225    -48    -30       C  
ATOM   1237  C   THR A 198      -1.077 -61.511  -5.968  1.00 16.48           C  
ANISOU 1237  C   THR A 198     1526   2367   2368    237    -36    -16       C  
ATOM   1238  O   THR A 198      -2.110 -61.875  -5.392  1.00 16.53           O  
ANISOU 1238  O   THR A 198     1537   2353   2391    233    -23      1       O  
ATOM   1239  CB  THR A 198       0.606 -62.859  -4.739  1.00 17.58           C  
ANISOU 1239  CB  THR A 198     1688   2501   2490    228    -89    -34       C  
ATOM   1240  CG2 THR A 198       0.615 -63.874  -5.879  1.00 17.88           C  
ANISOU 1240  CG2 THR A 198     1694   2548   2551    245   -121    -45       C  
ATOM   1241  OG1 THR A 198       1.921 -62.804  -4.164  1.00 17.93           O  
ANISOU 1241  OG1 THR A 198     1743   2556   2512    224   -111    -52       O  
ATOM   1242  N   LEU A 199      -1.027 -61.186  -7.265  1.00 15.09           N  
ANISOU 1242  N   LEU A 199     1329   2209   2195    253    -39    -27       N  
ATOM   1243  CA  LEU A 199      -2.201 -61.274  -8.161  1.00 15.03           C  
ANISOU 1243  CA  LEU A 199     1298   2204   2209    272    -39    -21       C  
ATOM   1244  C   LEU A 199      -1.988 -62.522  -9.001  1.00 16.66           C  
ANISOU 1244  C   LEU A 199     1479   2417   2433    282    -84    -37       C  
ATOM   1245  O   LEU A 199      -0.978 -62.634  -9.691  1.00 16.84           O  
ANISOU 1245  O   LEU A 199     1501   2453   2446    288   -101    -55       O  
ATOM   1246  CB  LEU A 199      -2.245 -60.030  -9.067  1.00 15.86           C  
ANISOU 1246  CB  LEU A 199     1409   2321   2296    289    -14    -22       C  
ATOM   1247  CG  LEU A 199      -3.076 -60.089 -10.335  1.00 17.68           C  
ANISOU 1247  CG  LEU A 199     1617   2562   2537    319    -28    -24       C  
ATOM   1248  CD1 LEU A 199      -4.576 -60.387 -10.039  1.00 18.49           C  
ANISOU 1248  CD1 LEU A 199     1696   2659   2671    324    -27    -10       C  
ATOM   1249  CD2 LEU A 199      -2.970 -58.746 -11.072  1.00 18.21           C  
ANISOU 1249  CD2 LEU A 199     1707   2636   2575    340      5    -23       C  
ATOM   1250  N   ILE A 200      -2.937 -63.422  -8.986  1.00 16.72           N  
ANISOU 1250  N   ILE A 200     1468   2416   2470    282    -97    -33       N  
ATOM   1251  CA  ILE A 200      -2.870 -64.628  -9.796  1.00 17.54           C  
ANISOU 1251  CA  ILE A 200     1550   2523   2591    289   -136    -49       C  
ATOM   1252  C   ILE A 200      -3.820 -64.515 -10.942  1.00 17.52           C  
ANISOU 1252  C   ILE A 200     1521   2534   2604    308   -146    -55       C  
ATOM   1253  O   ILE A 200      -5.036 -64.479 -10.735  1.00 18.51           O  
ANISOU 1253  O   ILE A 200     1627   2653   2751    306   -135    -48       O  
ATOM   1254  CB  ILE A 200      -3.173 -65.875  -8.928  1.00 18.75           C  
ANISOU 1254  CB  ILE A 200     1706   2653   2765    272   -143    -45       C  
ATOM   1255  CG1 ILE A 200      -2.003 -66.104  -7.914  1.00 21.76           C  
ANISOU 1255  CG1 ILE A 200     2121   3025   3123    264   -147    -43       C  
ATOM   1256  CG2 ILE A 200      -3.328 -67.146  -9.810  1.00 19.40           C  
ANISOU 1256  CG2 ILE A 200     1767   2736   2869    277   -177    -62       C  
ATOM   1257  CD1 ILE A 200      -2.332 -67.043  -6.879  1.00 25.72           C  
ANISOU 1257  CD1 ILE A 200     2642   3496   3633    252   -142    -34       C  
ATOM   1258  N   PHE A 201      -3.289 -64.480 -12.169  1.00 17.09           N  
ANISOU 1258  N   PHE A 201     1463   2494   2535    327   -167    -70       N  
ATOM   1259  CA  PHE A 201      -4.143 -64.554 -13.341  1.00 16.67           C  
ANISOU 1259  CA  PHE A 201     1387   2453   2492    349   -188    -80       C  
ATOM   1260  C   PHE A 201      -4.367 -66.036 -13.592  1.00 17.99           C  
ANISOU 1260  C   PHE A 201     1534   2615   2687    339   -222    -95       C  
ATOM   1261  O   PHE A 201      -3.402 -66.797 -13.655  1.00 18.54           O  
ANISOU 1261  O   PHE A 201     1615   2679   2751    332   -237   -104       O  
ATOM   1262  CB  PHE A 201      -3.441 -63.967 -14.571  1.00 17.00           C  
ANISOU 1262  CB  PHE A 201     1447   2508   2504    375   -194    -91       C  
ATOM   1263  CG  PHE A 201      -3.286 -62.472 -14.527  1.00 17.83           C  
ANISOU 1263  CG  PHE A 201     1578   2616   2580    387   -155    -80       C  
ATOM   1264  CD1 PHE A 201      -4.381 -61.647 -14.712  1.00 17.76           C  
ANISOU 1264  CD1 PHE A 201     1565   2612   2569    410   -142    -69       C  
ATOM   1265  CD2 PHE A 201      -2.046 -61.889 -14.284  1.00 18.04           C  
ANISOU 1265  CD2 PHE A 201     1633   2639   2583    377   -129    -82       C  
ATOM   1266  CE1 PHE A 201      -4.240 -60.262 -14.682  1.00 18.87           C  
ANISOU 1266  CE1 PHE A 201     1738   2752   2680    423   -100    -57       C  
ATOM   1267  CE2 PHE A 201      -1.905 -60.499 -14.297  1.00 19.47           C  
ANISOU 1267  CE2 PHE A 201     1842   2818   2736    385    -86    -75       C  
ATOM   1268  CZ  PHE A 201      -2.999 -59.704 -14.499  1.00 19.25           C  
ANISOU 1268  CZ  PHE A 201     1818   2793   2702    409    -71    -60       C  
ATOM   1269  N   ALA A 202      -5.608 -66.447 -13.770  1.00 17.34           N  
ANISOU 1269  N   ALA A 202     1420   2534   2635    338   -233   -101       N  
ATOM   1270  CA  ALA A 202      -5.924 -67.860 -14.039  1.00 18.38           C  
ANISOU 1270  CA  ALA A 202     1531   2657   2794    324   -261   -120       C  
ATOM   1271  C   ALA A 202      -6.728 -67.925 -15.340  1.00 19.39           C  
ANISOU 1271  C   ALA A 202     1630   2805   2931    345   -295   -141       C  
ATOM   1272  O   ALA A 202      -7.363 -66.956 -15.730  1.00 20.06           O  
ANISOU 1272  O   ALA A 202     1706   2908   3010    370   -294   -138       O  
ATOM   1273  CB  ALA A 202      -6.759 -68.425 -12.889  1.00 19.70           C  
ANISOU 1273  CB  ALA A 202     1685   2803   2997    295   -238   -114       C  
ATOM   1274  N   CYS A 203      -6.703 -69.075 -15.992  1.00 19.10           N  
ANISOU 1274  N   CYS A 203     1584   2766   2906    338   -326   -162       N  
ATOM   1275  CA  CYS A 203      -7.382 -69.247 -17.281  1.00 19.59           C  
ANISOU 1275  CA  CYS A 203     1623   2847   2973    358   -366   -187       C  
ATOM   1276  C   CYS A 203      -8.421 -70.339 -17.102  1.00 19.74           C  
ANISOU 1276  C   CYS A 203     1601   2858   3039    330   -377   -209       C  
ATOM   1277  O   CYS A 203      -8.064 -71.477 -16.847  1.00 20.05           O  
ANISOU 1277  O   CYS A 203     1650   2877   3091    304   -376   -217       O  
ATOM   1278  CB  CYS A 203      -6.342 -69.597 -18.345  1.00 21.33           C  
ANISOU 1278  CB  CYS A 203     1875   3068   3161    374   -390   -198       C  
ATOM   1279  SG  CYS A 203      -5.041 -68.323 -18.573  1.00 25.33           S  
ANISOU 1279  SG  CYS A 203     2429   3577   3617    400   -365   -178       S  
ATOM   1280  N   GLU A 204      -9.717 -69.994 -17.170  1.00 20.20           N  
ANISOU 1280  N   GLU A 204     1615   2933   3128    335   -384   -221       N  
ATOM   1281  CA  GLU A 204     -10.799 -70.902 -16.803  1.00 21.07           C  
ANISOU 1281  CA  GLU A 204     1679   3034   3292    302   -382   -245       C  
ATOM   1282  C   GLU A 204     -10.685 -72.334 -17.317  1.00 21.70           C  
ANISOU 1282  C   GLU A 204     1756   3102   3386    277   -405   -274       C  
ATOM   1283  O   GLU A 204     -10.873 -73.288 -16.551  1.00 22.75           O  
ANISOU 1283  O   GLU A 204     1887   3206   3551    238   -378   -280       O  
ATOM   1284  CB  GLU A 204     -12.165 -70.330 -17.216  1.00 22.91           C  
ANISOU 1284  CB  GLU A 204     1855   3296   3555    320   -402   -264       C  
ATOM   1285  CG  GLU A 204     -13.323 -71.123 -16.655  1.00 26.30           C  
ANISOU 1285  CG  GLU A 204     2230   3714   4050    280   -387   -290       C  
ATOM   1286  CD  GLU A 204     -14.680 -70.703 -17.176  1.00 32.37           C  
ANISOU 1286  CD  GLU A 204     2929   4514   4855    299   -415   -319       C  
ATOM   1287  OE1 GLU A 204     -14.740 -70.092 -18.266  1.00 31.64           O  
ANISOU 1287  OE1 GLU A 204     2833   4455   4732    345   -464   -327       O  
ATOM   1288  OE2 GLU A 204     -15.686 -70.978 -16.480  1.00 35.18           O1-
ANISOU 1288  OE2 GLU A 204     3236   4862   5270    269   -387   -335       O1-
ATOM   1289  N   ASN A 205     -10.429 -72.478 -18.618  1.00 21.31           N  
ANISOU 1289  N   ASN A 205     1713   3070   3312    300   -452   -293       N  
ATOM   1290  CA  ASN A 205     -10.405 -73.802 -19.239  1.00 22.03           C  
ANISOU 1290  CA  ASN A 205     1803   3152   3416    278   -477   -324       C  
ATOM   1291  C   ASN A 205      -9.020 -74.396 -19.395  1.00 22.08           C  
ANISOU 1291  C   ASN A 205     1865   3137   3387    277   -472   -311       C  
ATOM   1292  O   ASN A 205      -8.836 -75.324 -20.194  1.00 22.49           O  
ANISOU 1292  O   ASN A 205     1926   3182   3435    270   -497   -334       O  
ATOM   1293  CB  ASN A 205     -11.113 -73.731 -20.595  1.00 24.93           C  
ANISOU 1293  CB  ASN A 205     2141   3551   3781    302   -535   -359       C  
ATOM   1294  CG  ASN A 205     -12.589 -73.430 -20.473  1.00 30.54           C  
ANISOU 1294  CG  ASN A 205     2783   4283   4538    299   -546   -383       C  
ATOM   1295  ND2 ASN A 205     -13.221 -73.044 -21.580  1.00 32.21           N  
ANISOU 1295  ND2 ASN A 205     2968   4529   4741    334   -601   -409       N  
ATOM   1296  OD1 ASN A 205     -13.187 -73.547 -19.400  1.00 32.43           O  
ANISOU 1296  OD1 ASN A 205     2992   4509   4822    268   -506   -380       O  
ATOM   1297  N   ASP A 206      -8.062 -73.961 -18.569  1.00 20.46           N  
ANISOU 1297  N   ASP A 206     1696   2918   3160    281   -438   -276       N  
ATOM   1298  CA  ASP A 206      -6.692 -74.432 -18.632  1.00 19.59           C  
ANISOU 1298  CA  ASP A 206     1633   2791   3020    285   -433   -264       C  
ATOM   1299  C   ASP A 206      -6.649 -75.959 -18.450  1.00 20.30           C  
ANISOU 1299  C   ASP A 206     1730   2851   3131    253   -428   -280       C  
ATOM   1300  O   ASP A 206      -7.185 -76.485 -17.466  1.00 21.26           O  
ANISOU 1300  O   ASP A 206     1843   2952   3284    224   -399   -279       O  
ATOM   1301  CB  ASP A 206      -5.883 -73.740 -17.514  1.00 18.64           C  
ANISOU 1301  CB  ASP A 206     1537   2663   2883    289   -397   -230       C  
ATOM   1302  CG  ASP A 206      -4.385 -73.822 -17.697  1.00 19.55           C  
ANISOU 1302  CG  ASP A 206     1692   2771   2965    303   -396   -219       C  
ATOM   1303  OD1 ASP A 206      -3.900 -74.862 -18.224  1.00 19.64           O  
ANISOU 1303  OD1 ASP A 206     1718   2769   2975    299   -410   -233       O  
ATOM   1304  OD2 ASP A 206      -3.678 -72.859 -17.274  1.00 18.97           O1-
ANISOU 1304  OD2 ASP A 206     1634   2705   2870    317   -379   -200       O1-
ATOM   1305  N   SER A 207      -6.102 -76.662 -19.442  1.00 19.93           N  
ANISOU 1305  N   SER A 207     1703   2801   3068    259   -452   -296       N  
ATOM   1306  CA  SER A 207      -5.971 -78.122 -19.353  1.00 19.99           C  
ANISOU 1306  CA  SER A 207     1727   2778   3091    232   -445   -310       C  
ATOM   1307  C   SER A 207      -4.499 -78.554 -19.132  1.00 19.99           C  
ANISOU 1307  C   SER A 207     1775   2757   3062    245   -431   -290       C  
ATOM   1308  O   SER A 207      -4.212 -79.767 -19.096  1.00 21.31           O  
ANISOU 1308  O   SER A 207     1965   2897   3235    230   -422   -298       O  
ATOM   1309  CB  SER A 207      -6.523 -78.783 -20.625  1.00 21.22           C  
ANISOU 1309  CB  SER A 207     1870   2940   3252    225   -481   -348       C  
ATOM   1310  OG  SER A 207      -5.837 -78.277 -21.764  1.00 22.52           O  
ANISOU 1310  OG  SER A 207     2057   3122   3378    260   -510   -348       O  
ATOM   1311  N   ILE A 208      -3.574 -77.591 -19.000  1.00 18.92           N  
ANISOU 1311  N   ILE A 208     1654   2636   2900    273   -427   -267       N  
ATOM   1312  CA  ILE A 208      -2.153 -77.829 -18.783  1.00 18.46           C  
ANISOU 1312  CA  ILE A 208     1630   2566   2819    289   -417   -251       C  
ATOM   1313  C   ILE A 208      -1.823 -77.667 -17.293  1.00 19.23           C  
ANISOU 1313  C   ILE A 208     1737   2652   2919    284   -389   -226       C  
ATOM   1314  O   ILE A 208      -1.142 -78.517 -16.698  1.00 19.33           O  
ANISOU 1314  O   ILE A 208     1776   2641   2928    285   -378   -218       O  
ATOM   1315  CB  ILE A 208      -1.315 -76.925 -19.693  1.00 18.07           C  
ANISOU 1315  CB  ILE A 208     1590   2536   2741    318   -429   -250       C  
ATOM   1316  CG1 ILE A 208      -1.536 -77.313 -21.176  1.00 19.84           C  
ANISOU 1316  CG1 ILE A 208     1821   2762   2956    325   -456   -274       C  
ATOM   1317  CG2 ILE A 208       0.164 -76.902 -19.280  1.00 18.05           C  
ANISOU 1317  CG2 ILE A 208     1609   2527   2722    334   -414   -235       C  
ATOM   1318  CD1 ILE A 208      -0.798 -76.447 -22.171  1.00 21.42           C  
ANISOU 1318  CD1 ILE A 208     2039   2975   3125    355   -461   -275       C  
ATOM   1319  N   ALA A 209      -2.258 -76.552 -16.702  1.00 18.88           N  
ANISOU 1319  N   ALA A 209     1674   2624   2875    285   -379   -213       N  
ATOM   1320  CA  ALA A 209      -2.093 -76.318 -15.253  1.00 19.37           C  
ANISOU 1320  CA  ALA A 209     1748   2674   2937    279   -353   -190       C  
ATOM   1321  C   ALA A 209      -3.519 -75.995 -14.791  1.00 19.57           C  
ANISOU 1321  C   ALA A 209     1748   2699   2990    257   -337   -191       C  
ATOM   1322  O   ALA A 209      -3.876 -74.809 -14.644  1.00 19.59           O  
ANISOU 1322  O   ALA A 209     1733   2721   2989    263   -332   -182       O  
ATOM   1323  CB  ALA A 209      -1.181 -75.117 -15.017  1.00 20.40           C  
ANISOU 1323  CB  ALA A 209     1884   2826   3043    299   -350   -175       C  
ATOM   1324  N   PRO A 210      -4.388 -77.023 -14.664  1.00 19.69           N  
ANISOU 1324  N   PRO A 210     1757   2690   3033    231   -328   -206       N  
ATOM   1325  CA  PRO A 210      -5.809 -76.758 -14.366  1.00 19.56           C  
ANISOU 1325  CA  PRO A 210     1706   2674   3052    208   -313   -215       C  
ATOM   1326  C   PRO A 210      -6.015 -75.875 -13.155  1.00 20.06           C  
ANISOU 1326  C   PRO A 210     1774   2734   3114    206   -281   -190       C  
ATOM   1327  O   PRO A 210      -5.323 -76.026 -12.151  1.00 20.65           O  
ANISOU 1327  O   PRO A 210     1888   2787   3171    209   -261   -169       O  
ATOM   1328  CB  PRO A 210      -6.409 -78.149 -14.161  1.00 21.63           C  
ANISOU 1328  CB  PRO A 210     1973   2901   3343    176   -295   -235       C  
ATOM   1329  CG  PRO A 210      -5.525 -79.044 -14.945  1.00 22.20           C  
ANISOU 1329  CG  PRO A 210     2071   2967   3396    186   -317   -244       C  
ATOM   1330  CD  PRO A 210      -4.144 -78.470 -14.823  1.00 20.07           C  
ANISOU 1330  CD  PRO A 210     1829   2709   3086    220   -327   -219       C  
ATOM   1331  N   VAL A 211      -6.967 -74.942 -13.259  1.00 20.37           N  
ANISOU 1331  N   VAL A 211     1776   2794   3172    206   -278   -192       N  
ATOM   1332  CA  VAL A 211      -7.209 -74.016 -12.134  1.00 20.75           C  
ANISOU 1332  CA  VAL A 211     1829   2837   3218    204   -244   -168       C  
ATOM   1333  C   VAL A 211      -7.505 -74.719 -10.806  1.00 21.97           C  
ANISOU 1333  C   VAL A 211     2013   2947   3389    178   -200   -158       C  
ATOM   1334  O   VAL A 211      -6.969 -74.315  -9.772  1.00 21.36           O  
ANISOU 1334  O   VAL A 211     1972   2855   3288    183   -178   -133       O  
ATOM   1335  CB  VAL A 211      -8.340 -73.043 -12.507  1.00 21.54           C  
ANISOU 1335  CB  VAL A 211     1880   2962   3340    208   -246   -175       C  
ATOM   1336  CG1 VAL A 211      -8.710 -72.153 -11.313  1.00 22.54           C  
ANISOU 1336  CG1 VAL A 211     2016   3078   3471    203   -203   -150       C  
ATOM   1337  CG2 VAL A 211      -7.930 -72.205 -13.702  1.00 21.91           C  
ANISOU 1337  CG2 VAL A 211     1917   3047   3359    242   -284   -178       C  
ATOM   1338  N   ASN A 212      -8.283 -75.835 -10.840  1.00 22.61           N  
ANISOU 1338  N   ASN A 212     2083   3002   3507    149   -186   -181       N  
ATOM   1339  CA  ASN A 212      -8.652 -76.497  -9.589  1.00 24.20           C  
ANISOU 1339  CA  ASN A 212     2318   3153   3723    124   -134   -174       C  
ATOM   1340  C   ASN A 212      -7.501 -77.224  -8.896  1.00 23.88           C  
ANISOU 1340  C   ASN A 212     2347   3082   3644    135   -127   -155       C  
ATOM   1341  O   ASN A 212      -7.591 -77.455  -7.684  1.00 24.82           O  
ANISOU 1341  O   ASN A 212     2512   3160   3758    125    -85   -139       O  
ATOM   1342  CB  ASN A 212      -9.869 -77.410  -9.777  1.00 26.98           C  
ANISOU 1342  CB  ASN A 212     2639   3484   4129     86   -111   -208       C  
ATOM   1343  CG  ASN A 212      -9.661 -78.585 -10.693  1.00 32.91           C  
ANISOU 1343  CG  ASN A 212     3389   4231   4885     77   -135   -235       C  
ATOM   1344  ND2 ASN A 212     -10.753 -79.274 -11.029  1.00 35.98           N  
ANISOU 1344  ND2 ASN A 212     3739   4608   5323     42   -121   -272       N  
ATOM   1345  OD1 ASN A 212      -8.557 -78.876 -11.138  1.00 33.58           O  
ANISOU 1345  OD1 ASN A 212     3504   4323   4932    101   -166   -227       O  
ATOM   1346  N   SER A 213      -6.404 -77.505  -9.614  1.00 22.16           N  
ANISOU 1346  N   SER A 213     2142   2882   3396    159   -168   -156       N  
ATOM   1347  CA  SER A 213      -5.244 -78.148  -9.010  1.00 22.88           C  
ANISOU 1347  CA  SER A 213     2293   2950   3451    178   -168   -139       C  
ATOM   1348  C   SER A 213      -3.984 -77.324  -9.009  1.00 22.24           C  
ANISOU 1348  C   SER A 213     2221   2900   3330    211   -200   -121       C  
ATOM   1349  O   SER A 213      -2.961 -77.789  -8.503  1.00 22.64           O  
ANISOU 1349  O   SER A 213     2314   2936   3350    232   -207   -110       O  
ATOM   1350  CB  SER A 213      -4.985 -79.495  -9.667  1.00 24.93           C  
ANISOU 1350  CB  SER A 213     2567   3192   3714    175   -178   -157       C  
ATOM   1351  OG  SER A 213      -4.844 -79.350 -11.070  1.00 27.76           O  
ANISOU 1351  OG  SER A 213     2884   3588   4078    182   -219   -177       O  
ATOM   1352  N   SER A 214      -4.033 -76.066  -9.530  1.00 20.60           N  
ANISOU 1352  N   SER A 214     1974   2733   3120    219   -216   -121       N  
ATOM   1353  CA  SER A 214      -2.840 -75.232  -9.561  1.00 19.91           C  
ANISOU 1353  CA  SER A 214     1893   2673   2998    245   -239   -109       C  
ATOM   1354  C   SER A 214      -3.191 -73.795  -9.090  1.00 18.98           C  
ANISOU 1354  C   SER A 214     1764   2573   2876    243   -223    -96       C  
ATOM   1355  O   SER A 214      -3.097 -73.521  -7.900  1.00 18.89           O  
ANISOU 1355  O   SER A 214     1784   2544   2851    240   -201    -78       O  
ATOM   1356  CB  SER A 214      -2.217 -75.209 -10.963  1.00 23.64           C  
ANISOU 1356  CB  SER A 214     2342   3176   3466    261   -274   -126       C  
ATOM   1357  OG  SER A 214      -1.709 -76.484 -11.314  1.00 31.21           O  
ANISOU 1357  OG  SER A 214     3318   4117   4423    266   -287   -136       O  
ATOM   1358  N   ALA A 215      -3.656 -72.917  -9.980  1.00 18.37           N  
ANISOU 1358  N   ALA A 215     1647   2525   2808    245   -231   -103       N  
ATOM   1359  CA  ALA A 215      -3.909 -71.520  -9.598  1.00 17.70           C  
ANISOU 1359  CA  ALA A 215     1555   2455   2714    247   -213    -89       C  
ATOM   1360  C   ALA A 215      -4.794 -71.323  -8.350  1.00 18.59           C  
ANISOU 1360  C   ALA A 215     1682   2541   2840    228   -172    -73       C  
ATOM   1361  O   ALA A 215      -4.440 -70.494  -7.505  1.00 18.73           O  
ANISOU 1361  O   ALA A 215     1724   2558   2835    230   -155    -55       O  
ATOM   1362  CB  ALA A 215      -4.512 -70.745 -10.778  1.00 18.78           C  
ANISOU 1362  CB  ALA A 215     1652   2623   2861    257   -225   -100       C  
ATOM   1363  N   LEU A 216      -5.959 -72.019  -8.265  1.00 18.16           N  
ANISOU 1363  N   LEU A 216     1612   2465   2824    208   -153    -82       N  
ATOM   1364  CA  LEU A 216      -6.854 -71.771  -7.126  1.00 19.12           C  
ANISOU 1364  CA  LEU A 216     1746   2557   2962    188   -105    -68       C  
ATOM   1365  C   LEU A 216      -6.291 -72.312  -5.805  1.00 19.80           C  
ANISOU 1365  C   LEU A 216     1896   2603   3024    184    -83    -51       C  
ATOM   1366  O   LEU A 216      -6.234 -71.535  -4.868  1.00 19.15           O  
ANISOU 1366  O   LEU A 216     1841   2511   2923    184    -58    -32       O  
ATOM   1367  CB  LEU A 216      -8.287 -72.215  -7.393  1.00 20.06           C  
ANISOU 1367  CB  LEU A 216     1823   2666   3135    166    -85    -87       C  
ATOM   1368  CG  LEU A 216      -9.297 -71.911  -6.304  1.00 21.02           C  
ANISOU 1368  CG  LEU A 216     1950   2755   3281    145    -29    -76       C  
ATOM   1369  CD1 LEU A 216      -9.335 -70.417  -5.966  1.00 20.51           C  
ANISOU 1369  CD1 LEU A 216     1885   2709   3200    158    -15    -55       C  
ATOM   1370  CD2 LEU A 216     -10.689 -72.325  -6.744  1.00 22.94           C  
ANISOU 1370  CD2 LEU A 216     2137   2995   3586    123    -14   -103       C  
ATOM   1371  N   PRO A 217      -5.768 -73.553  -5.706  1.00 19.39           N  
ANISOU 1371  N   PRO A 217     1875   2528   2964    185    -93    -57       N  
ATOM   1372  CA  PRO A 217      -5.138 -73.962  -4.426  1.00 19.73           C  
ANISOU 1372  CA  PRO A 217     1989   2534   2974    192    -77    -39       C  
ATOM   1373  C   PRO A 217      -3.952 -73.069  -4.059  1.00 20.62           C  
ANISOU 1373  C   PRO A 217     2120   2672   3041    215   -103    -25       C  
ATOM   1374  O   PRO A 217      -3.765 -72.764  -2.876  1.00 20.64           O  
ANISOU 1374  O   PRO A 217     2172   2653   3018    217    -84     -8       O  
ATOM   1375  CB  PRO A 217      -4.638 -75.384  -4.687  1.00 20.79           C  
ANISOU 1375  CB  PRO A 217     2147   2648   3104    199    -93    -50       C  
ATOM   1376  CG  PRO A 217      -5.404 -75.851  -5.853  1.00 22.30           C  
ANISOU 1376  CG  PRO A 217     2284   2851   3337    182    -98    -74       C  
ATOM   1377  CD  PRO A 217      -5.815 -74.668  -6.670  1.00 19.99           C  
ANISOU 1377  CD  PRO A 217     1931   2604   3059    182   -114    -80       C  
ATOM   1378  N   ILE A 218      -3.164 -72.592  -5.062  1.00 19.29           N  
ANISOU 1378  N   ILE A 218     1916   2549   2864    231   -143    -36       N  
ATOM   1379  CA  ILE A 218      -2.066 -71.661  -4.749  1.00 18.27           C  
ANISOU 1379  CA  ILE A 218     1798   2445   2699    248   -162    -30       C  
ATOM   1380  C   ILE A 218      -2.643 -70.370  -4.087  1.00 18.35           C  
ANISOU 1380  C   ILE A 218     1812   2456   2704    234   -129    -15       C  
ATOM   1381  O   ILE A 218      -2.179 -69.951  -3.011  1.00 17.90           O  
ANISOU 1381  O   ILE A 218     1797   2388   2617    237   -121     -2       O  
ATOM   1382  CB  ILE A 218      -1.281 -71.311  -6.030  1.00 18.04           C  
ANISOU 1382  CB  ILE A 218     1727   2459   2667    262   -198    -47       C  
ATOM   1383  CG1 ILE A 218      -0.468 -72.529  -6.473  1.00 18.78           C  
ANISOU 1383  CG1 ILE A 218     1828   2550   2759    278   -230    -59       C  
ATOM   1384  CG2 ILE A 218      -0.370 -70.078  -5.795  1.00 19.49           C  
ANISOU 1384  CG2 ILE A 218     1912   2670   2823    269   -205    -45       C  
ATOM   1385  CD1 ILE A 218       0.193 -72.326  -7.878  1.00 18.96           C  
ANISOU 1385  CD1 ILE A 218     1811   2608   2786    290   -258    -77       C  
ATOM   1386  N   TYR A 219      -3.709 -69.824  -4.690  1.00 17.45           N  
ANISOU 1386  N   TYR A 219     1659   2351   2620    222   -109    -16       N  
ATOM   1387  CA  TYR A 219      -4.354 -68.611  -4.155  1.00 17.64           C  
ANISOU 1387  CA  TYR A 219     1685   2375   2644    213    -72     -1       C  
ATOM   1388  C   TYR A 219      -4.896 -68.891  -2.736  1.00 18.35           C  
ANISOU 1388  C   TYR A 219     1824   2416   2731    198    -31     16       C  
ATOM   1389  O   TYR A 219      -4.670 -68.108  -1.816  1.00 18.69           O  
ANISOU 1389  O   TYR A 219     1904   2451   2747    195    -11     31       O  
ATOM   1390  CB  TYR A 219      -5.528 -68.195  -5.067  1.00 17.58           C  
ANISOU 1390  CB  TYR A 219     1624   2382   2674    209    -61     -8       C  
ATOM   1391  CG  TYR A 219      -6.345 -67.058  -4.483  1.00 16.74           C  
ANISOU 1391  CG  TYR A 219     1519   2269   2572    201    -17      9       C  
ATOM   1392  CD1 TYR A 219      -5.912 -65.740  -4.580  1.00 17.81           C  
ANISOU 1392  CD1 TYR A 219     1659   2429   2681    211    -13     17       C  
ATOM   1393  CD2 TYR A 219      -7.530 -67.308  -3.794  1.00 18.31           C  
ANISOU 1393  CD2 TYR A 219     1719   2434   2803    183     26     16       C  
ATOM   1394  CE1 TYR A 219      -6.657 -64.697  -4.036  1.00 18.46           C  
ANISOU 1394  CE1 TYR A 219     1747   2502   2765    206     31     34       C  
ATOM   1395  CE2 TYR A 219      -8.273 -66.278  -3.236  1.00 18.97           C  
ANISOU 1395  CE2 TYR A 219     1805   2509   2893    178     70     32       C  
ATOM   1396  CZ  TYR A 219      -7.826 -64.972  -3.348  1.00 18.95           C  
ANISOU 1396  CZ  TYR A 219     1809   2531   2860    190     71     42       C  
ATOM   1397  OH  TYR A 219      -8.555 -63.944  -2.777  1.00 21.04           O  
ANISOU 1397  OH  TYR A 219     2081   2784   3128    186    119     60       O  
ATOM   1398  N   ASP A 220      -5.572 -70.031  -2.566  1.00 18.31           N  
ANISOU 1398  N   ASP A 220     1827   2378   2753    186    -14     12       N  
ATOM   1399  CA  ASP A 220      -6.173 -70.364  -1.264  1.00 19.80           C  
ANISOU 1399  CA  ASP A 220     2069   2512   2942    171     35     27       C  
ATOM   1400  C   ASP A 220      -5.142 -70.622  -0.169  1.00 21.39           C  
ANISOU 1400  C   ASP A 220     2345   2691   3091    186     25     40       C  
ATOM   1401  O   ASP A 220      -5.487 -70.547   1.022  1.00 23.48           O  
ANISOU 1401  O   ASP A 220     2667   2912   3341    177     66     56       O  
ATOM   1402  CB  ASP A 220      -7.101 -71.576  -1.404  1.00 21.17           C  
ANISOU 1402  CB  ASP A 220     2234   2650   3158    153     61     14       C  
ATOM   1403  CG  ASP A 220      -8.449 -71.223  -2.002  1.00 25.58           C  
ANISOU 1403  CG  ASP A 220     2728   3219   3773    133     87      2       C  
ATOM   1404  OD1 ASP A 220      -8.834 -70.025  -1.947  1.00 25.63           O  
ANISOU 1404  OD1 ASP A 220     2713   3243   3782    134    102     12       O  
ATOM   1405  OD2 ASP A 220      -9.131 -72.144  -2.505  1.00 27.65           O1-
ANISOU 1405  OD2 ASP A 220     2960   3469   4076    118     94    -19       O1-
ATOM   1406  N   SER A 221      -3.903 -70.969  -0.541  1.00 20.06           N  
ANISOU 1406  N   SER A 221     2179   2548   2895    209    -28     31       N  
ATOM   1407  CA  SER A 221      -2.875 -71.236   0.458  1.00 19.62           C  
ANISOU 1407  CA  SER A 221     2188   2477   2789    229    -47     39       C  
ATOM   1408  C   SER A 221      -2.349 -69.995   1.145  1.00 20.07           C  
ANISOU 1408  C   SER A 221     2264   2550   2810    231    -51     48       C  
ATOM   1409  O   SER A 221      -1.759 -70.109   2.212  1.00 20.30           O  
ANISOU 1409  O   SER A 221     2356   2559   2798    245    -59     56       O  
ATOM   1410  CB  SER A 221      -1.711 -72.003  -0.158  1.00 20.19           C  
ANISOU 1410  CB  SER A 221     2250   2574   2847    256   -104     24       C  
ATOM   1411  OG  SER A 221      -0.918 -71.142  -0.967  1.00 19.73           O  
ANISOU 1411  OG  SER A 221     2141   2571   2786    263   -140     11       O  
ATOM   1412  N   MET A 222      -2.502 -68.827   0.521  1.00 19.87           N  
ANISOU 1412  N   MET A 222     2190   2562   2798    220    -46     44       N  
ATOM   1413  CA  MET A 222      -1.910 -67.600   1.026  1.00 20.17           C  
ANISOU 1413  CA  MET A 222     2242   2618   2803    219    -49     48       C  
ATOM   1414  C   MET A 222      -2.800 -66.831   1.968  1.00 21.93           C  
ANISOU 1414  C   MET A 222     2501   2809   3021    199      7     68       C  
ATOM   1415  O   MET A 222      -3.729 -66.166   1.513  1.00 21.28           O  
ANISOU 1415  O   MET A 222     2384   2732   2970    185     42     74       O  
ATOM   1416  CB  MET A 222      -1.504 -66.714  -0.164  1.00 19.93           C  
ANISOU 1416  CB  MET A 222     2149   2639   2783    219    -68     32       C  
ATOM   1417  CG  MET A 222      -0.406 -67.343  -0.989  1.00 21.44           C  
ANISOU 1417  CG  MET A 222     2312   2862   2974    238   -121     11       C  
ATOM   1418  SD  MET A 222       0.158 -66.316  -2.395  1.00 20.83           S  
ANISOU 1418  SD  MET A 222     2172   2836   2905    239   -134     -9       S  
ATOM   1419  CE  MET A 222      -1.256 -66.321  -3.417  1.00 19.76           C  
ANISOU 1419  CE  MET A 222     1998   2699   2812    232   -108     -3       C  
ATOM   1420  N   SER A 223      -2.521 -66.926   3.296  1.00 22.37           N  
ANISOU 1420  N   SER A 223     2632   2831   3038    203     15     80       N  
ATOM   1421  CA  SER A 223      -3.348 -66.178   4.246  1.00 23.90           C  
ANISOU 1421  CA  SER A 223     2868   2988   3224    184     73    101       C  
ATOM   1422  C   SER A 223      -2.603 -64.978   4.862  1.00 24.67           C  
ANISOU 1422  C   SER A 223     2993   3103   3277    180     66    101       C  
ATOM   1423  O   SER A 223      -3.150 -64.354   5.776  1.00 26.96           O  
ANISOU 1423  O   SER A 223     3332   3360   3552    166    112    119       O  
ATOM   1424  CB  SER A 223      -3.864 -67.091   5.363  1.00 26.26           C  
ANISOU 1424  CB  SER A 223     3244   3222   3512    184    107    116       C  
ATOM   1425  OG  SER A 223      -4.755 -68.101   4.920  1.00 30.22           O  
ANISOU 1425  OG  SER A 223     3724   3698   4059    178    132    115       O  
ATOM   1426  N   ARG A 224      -1.381 -64.646   4.410  1.00 22.72           N  
ANISOU 1426  N   ARG A 224     2718   2903   3010    191     12     80       N  
ATOM   1427  CA  ARG A 224      -0.604 -63.557   5.022  1.00 22.86           C  
ANISOU 1427  CA  ARG A 224     2761   2938   2987    184      4     73       C  
ATOM   1428  C   ARG A 224      -0.385 -62.340   4.149  1.00 24.55           C  
ANISOU 1428  C   ARG A 224     2920   3194   3213    169     12     60       C  
ATOM   1429  O   ARG A 224       0.481 -61.506   4.483  1.00 27.48           O  
ANISOU 1429  O   ARG A 224     3302   3586   3552    161     -2     45       O  
ATOM   1430  CB  ARG A 224       0.787 -64.072   5.444  1.00 22.96           C  
ANISOU 1430  CB  ARG A 224     2793   2969   2961    206    -63     51       C  
ATOM   1431  CG  ARG A 224       0.745 -65.310   6.343  1.00 25.77           C  
ANISOU 1431  CG  ARG A 224     3216   3281   3293    230    -76     63       C  
ATOM   1432  CD  ARG A 224       2.143 -65.808   6.620  1.00 31.24           C  
ANISOU 1432  CD  ARG A 224     3918   4000   3951    260   -149     40       C  
ATOM   1433  NE  ARG A 224       2.135 -67.082   7.343  1.00 38.13           N  
ANISOU 1433  NE  ARG A 224     4858   4832   4800    291   -164     51       N  
ATOM   1434  CZ  ARG A 224       2.138 -67.191   8.663  1.00 42.17           C  
ANISOU 1434  CZ  ARG A 224     5461   5302   5261    304   -161     64       C  
ATOM   1435  NH1 ARG A 224       2.128 -66.101   9.428  1.00 43.83           N1+
ANISOU 1435  NH1 ARG A 224     5705   5508   5442    284   -143     66       N1+
ATOM   1436  NH2 ARG A 224       2.134 -68.389   9.235  1.00 39.73           N  
ANISOU 1436  NH2 ARG A 224     5217   4951   4928    337   -171     74       N  
ATOM   1437  N   ASN A 225      -1.114 -62.222   3.028  1.00 21.85           N  
ANISOU 1437  N   ASN A 225     2523   2866   2913    167     33     63       N  
ATOM   1438  CA  ASN A 225      -0.841 -61.120   2.115  1.00 20.02           C  
ANISOU 1438  CA  ASN A 225     2248   2672   2688    160     40     51       C  
ATOM   1439  C   ASN A 225      -2.058 -60.498   1.487  1.00 18.30           C  
ANISOU 1439  C   ASN A 225     2003   2448   2500    156     89     68       C  
ATOM   1440  O   ASN A 225      -3.169 -61.043   1.537  1.00 19.42           O  
ANISOU 1440  O   ASN A 225     2143   2565   2672    157    112     84       O  
ATOM   1441  CB  ASN A 225       0.111 -61.651   0.992  1.00 19.43           C  
ANISOU 1441  CB  ASN A 225     2121   2637   2626    176    -13     23       C  
ATOM   1442  CG  ASN A 225      -0.478 -62.817   0.179  1.00 21.07           C  
ANISOU 1442  CG  ASN A 225     2295   2841   2871    190    -27     27       C  
ATOM   1443  ND2 ASN A 225       0.141 -63.124  -0.976  1.00 19.23           N  
ANISOU 1443  ND2 ASN A 225     2016   2640   2652    203    -61      6       N  
ATOM   1444  OD1 ASN A 225      -1.483 -63.445   0.557  1.00 21.00           O  
ANISOU 1444  OD1 ASN A 225     2303   2799   2879    189     -5     45       O  
ATOM   1445  N   ALA A 226      -1.832 -59.358   0.830  1.00 17.02           N  
ANISOU 1445  N   ALA A 226     1821   2313   2334    152    105     60       N  
ATOM   1446  CA  ALA A 226      -2.780 -58.783  -0.118  1.00 17.14           C  
ANISOU 1446  CA  ALA A 226     1801   2335   2375    160    137     70       C  
ATOM   1447  C   ALA A 226      -2.728 -59.729  -1.327  1.00 17.68           C  
ANISOU 1447  C   ALA A 226     1817   2426   2474    178     94     55       C  
ATOM   1448  O   ALA A 226      -1.635 -60.117  -1.747  1.00 17.19           O  
ANISOU 1448  O   ALA A 226     1743   2387   2403    183     53     33       O  
ATOM   1449  CB  ALA A 226      -2.307 -57.403  -0.551  1.00 17.74           C  
ANISOU 1449  CB  ALA A 226     1878   2431   2430    155    161     62       C  
ATOM   1450  N   LYS A 227      -3.883 -60.191  -1.800  1.00 16.69           N  
ANISOU 1450  N   LYS A 227     1663   2292   2385    188    103     65       N  
ATOM   1451  CA  LYS A 227      -3.866 -61.145  -2.917  1.00 16.71           C  
ANISOU 1451  CA  LYS A 227     1621   2314   2413    203     62     49       C  
ATOM   1452  C   LYS A 227      -5.089 -61.026  -3.748  1.00 17.18           C  
ANISOU 1452  C   LYS A 227     1642   2379   2508    216     76     54       C  
ATOM   1453  O   LYS A 227      -6.124 -60.512  -3.295  1.00 18.21           O  
ANISOU 1453  O   LYS A 227     1776   2492   2652    213    117     72       O  
ATOM   1454  CB  LYS A 227      -3.691 -62.590  -2.396  1.00 17.78           C  
ANISOU 1454  CB  LYS A 227     1767   2430   2558    199     34     46       C  
ATOM   1455  CG  LYS A 227      -4.856 -63.001  -1.488  1.00 17.96           C  
ANISOU 1455  CG  LYS A 227     1810   2412   2602    188     71     64       C  
ATOM   1456  CD  LYS A 227      -4.759 -64.492  -1.104  1.00 18.03           C  
ANISOU 1456  CD  LYS A 227     1834   2398   2620    186     50     60       C  
ATOM   1457  CE  LYS A 227      -5.990 -64.906  -0.302  1.00 18.32           C  
ANISOU 1457  CE  LYS A 227     1889   2388   2683    171     98     74       C  
ATOM   1458  NZ  LYS A 227      -6.000 -66.397  -0.056  1.00 18.37           N1+
ANISOU 1458  NZ  LYS A 227     1913   2366   2700    169     86     68       N1+
ATOM   1459  N   GLN A 228      -5.007 -61.533  -4.977  1.00 16.29           N  
ANISOU 1459  N   GLN A 228     1490   2290   2411    233     39     37       N  
ATOM   1460  CA  GLN A 228      -6.155 -61.480  -5.876  1.00 16.19           C  
ANISOU 1460  CA  GLN A 228     1435   2287   2429    250     41     36       C  
ATOM   1461  C   GLN A 228      -6.095 -62.670  -6.811  1.00 17.16           C  
ANISOU 1461  C   GLN A 228     1524   2422   2573    257     -6     16       C  
ATOM   1462  O   GLN A 228      -5.026 -63.166  -7.114  1.00 16.78           O  
ANISOU 1462  O   GLN A 228     1484   2383   2510    258    -37      3       O  
ATOM   1463  CB  GLN A 228      -6.156 -60.157  -6.662  1.00 17.38           C  
ANISOU 1463  CB  GLN A 228     1585   2459   2560    272     56     39       C  
ATOM   1464  CG  GLN A 228      -7.418 -59.931  -7.502  1.00 17.03           C  
ANISOU 1464  CG  GLN A 228     1501   2426   2543    298     56     39       C  
ATOM   1465  CD  GLN A 228      -7.540 -58.468  -7.863  1.00 18.94           C  
ANISOU 1465  CD  GLN A 228     1761   2678   2759    321     88     51       C  
ATOM   1466  NE2 GLN A 228      -7.733 -57.641  -6.846  1.00 18.82           N  
ANISOU 1466  NE2 GLN A 228     1775   2643   2732    308    138     71       N  
ATOM   1467  OE1 GLN A 228      -7.478 -58.076  -9.033  1.00 19.16           O  
ANISOU 1467  OE1 GLN A 228     1780   2726   2773    351     72     42       O  
ATOM   1468  N   PHE A 229      -7.253 -63.135  -7.214  1.00 16.91           N  
ANISOU 1468  N   PHE A 229     1455   2390   2580    262     -9     11       N  
ATOM   1469  CA  PHE A 229      -7.444 -64.261  -8.127  1.00 18.11           C  
ANISOU 1469  CA  PHE A 229     1572   2552   2758    266    -51    -11       C  
ATOM   1470  C   PHE A 229      -8.368 -63.771  -9.229  1.00 18.37           C  
ANISOU 1470  C   PHE A 229     1563   2609   2808    292    -62    -20       C  
ATOM   1471  O   PHE A 229      -9.520 -63.410  -8.958  1.00 19.41           O  
ANISOU 1471  O   PHE A 229     1671   2736   2967    294    -38    -14       O  
ATOM   1472  CB  PHE A 229      -8.075 -65.439  -7.371  1.00 18.36           C  
ANISOU 1472  CB  PHE A 229     1598   2553   2825    241    -40    -14       C  
ATOM   1473  CG  PHE A 229      -8.354 -66.652  -8.220  1.00 18.56           C  
ANISOU 1473  CG  PHE A 229     1590   2583   2878    239    -76    -39       C  
ATOM   1474  CD1 PHE A 229      -7.346 -67.545  -8.530  1.00 19.85           C  
ANISOU 1474  CD1 PHE A 229     1770   2747   3026    239   -108    -49       C  
ATOM   1475  CD2 PHE A 229      -9.628 -66.903  -8.694  1.00 19.75           C  
ANISOU 1475  CD2 PHE A 229     1691   2739   3074    238    -77    -54       C  
ATOM   1476  CE1 PHE A 229      -7.618 -68.708  -9.248  1.00 20.64           C  
ANISOU 1476  CE1 PHE A 229     1846   2847   3151    234   -136    -72       C  
ATOM   1477  CE2 PHE A 229      -9.891 -68.038  -9.456  1.00 20.63           C  
ANISOU 1477  CE2 PHE A 229     1772   2854   3211    232   -109    -82       C  
ATOM   1478  CZ  PHE A 229      -8.890 -68.936  -9.724  1.00 20.60           C  
ANISOU 1478  CZ  PHE A 229     1792   2846   3188    228   -136    -89       C  
ATOM   1479  N   LEU A 230      -7.873 -63.728 -10.461  1.00 17.66           N  
ANISOU 1479  N   LEU A 230     1466   2544   2699    315    -99    -34       N  
ATOM   1480  CA  LEU A 230      -8.678 -63.231 -11.575  1.00 19.36           C  
ANISOU 1480  CA  LEU A 230     1650   2783   2921    349   -116    -43       C  
ATOM   1481  C   LEU A 230      -8.685 -64.310 -12.648  1.00 19.35           C  
ANISOU 1481  C   LEU A 230     1623   2795   2933    354   -167    -71       C  
ATOM   1482  O   LEU A 230      -7.676 -64.515 -13.289  1.00 18.19           O  
ANISOU 1482  O   LEU A 230     1499   2654   2759    361   -189    -78       O  
ATOM   1483  CB  LEU A 230      -8.072 -61.926 -12.100  1.00 20.38           C  
ANISOU 1483  CB  LEU A 230     1813   2926   3005    377   -104    -33       C  
ATOM   1484  CG  LEU A 230      -9.023 -61.142 -13.014  1.00 24.45           C  
ANISOU 1484  CG  LEU A 230     2309   3462   3519    420   -112    -35       C  
ATOM   1485  CD1 LEU A 230      -8.763 -59.666 -12.933  1.00 26.89           C  
ANISOU 1485  CD1 LEU A 230     2658   3769   3789    441    -71    -15       C  
ATOM   1486  CD2 LEU A 230      -8.938 -61.633 -14.428  1.00 26.50           C  
ANISOU 1486  CD2 LEU A 230     2557   3740   3771    446   -163    -59       C  
ATOM   1487  N   GLU A 231      -9.824 -64.946 -12.863  1.00 18.65           N  
ANISOU 1487  N   GLU A 231     1489   2711   2888    350   -184    -87       N  
ATOM   1488  CA  GLU A 231      -9.920 -66.038 -13.827  1.00 19.32           C  
ANISOU 1488  CA  GLU A 231     1548   2805   2987    350   -231   -117       C  
ATOM   1489  C   GLU A 231     -10.562 -65.547 -15.102  1.00 20.62           C  
ANISOU 1489  C   GLU A 231     1687   3001   3147    391   -268   -133       C  
ATOM   1490  O   GLU A 231     -11.664 -64.990 -15.069  1.00 22.22           O  
ANISOU 1490  O   GLU A 231     1855   3215   3372    408   -263   -134       O  
ATOM   1491  CB  GLU A 231     -10.712 -67.187 -13.213  1.00 19.85           C  
ANISOU 1491  CB  GLU A 231     1582   2853   3107    314   -224   -132       C  
ATOM   1492  CG  GLU A 231     -10.770 -68.415 -14.095  1.00 22.18           C  
ANISOU 1492  CG  GLU A 231     1856   3154   3419    305   -267   -164       C  
ATOM   1493  CD  GLU A 231     -11.703 -69.459 -13.514  1.00 26.10           C  
ANISOU 1493  CD  GLU A 231     2316   3628   3971    267   -252   -183       C  
ATOM   1494  OE1 GLU A 231     -11.199 -70.415 -12.891  1.00 28.48           O  
ANISOU 1494  OE1 GLU A 231     2645   3899   4275    237   -234   -181       O  
ATOM   1495  OE2 GLU A 231     -12.937 -69.315 -13.662  1.00 27.04           O1-
ANISOU 1495  OE2 GLU A 231     2382   3760   4132    267   -254   -201       O1-
ATOM   1496  N   ILE A 232      -9.872 -65.731 -16.221  1.00 20.39           N  
ANISOU 1496  N   ILE A 232     1679   2983   3086    412   -304   -145       N  
ATOM   1497  CA  ILE A 232     -10.357 -65.299 -17.533  1.00 21.58           C  
ANISOU 1497  CA  ILE A 232     1819   3160   3220    457   -344   -161       C  
ATOM   1498  C   ILE A 232     -11.333 -66.316 -18.096  1.00 22.63           C  
ANISOU 1498  C   ILE A 232     1898   3306   3394    450   -390   -196       C  
ATOM   1499  O   ILE A 232     -11.000 -67.491 -18.259  1.00 22.55           O  
ANISOU 1499  O   ILE A 232     1886   3286   3397    422   -407   -214       O  
ATOM   1500  CB  ILE A 232      -9.148 -65.087 -18.463  1.00 23.04           C  
ANISOU 1500  CB  ILE A 232     2057   3344   3351    479   -356   -160       C  
ATOM   1501  CG1 ILE A 232      -8.213 -63.973 -17.917  1.00 24.44           C  
ANISOU 1501  CG1 ILE A 232     2284   3510   3492    483   -306   -131       C  
ATOM   1502  CG2 ILE A 232      -9.595 -64.827 -19.917  1.00 23.82           C  
ANISOU 1502  CG2 ILE A 232     2158   3465   3426    528   -402   -179       C  
ATOM   1503  CD1 ILE A 232      -8.889 -62.575 -17.902  1.00 26.53           C  
ANISOU 1503  CD1 ILE A 232     2554   3784   3740    519   -283   -114       C  
ATOM   1504  N   ASN A 233     -12.550 -65.855 -18.398  1.00 23.48           N  
ANISOU 1504  N   ASN A 233     1961   3436   3523    477   -408   -208       N  
ATOM   1505  CA  ASN A 233     -13.639 -66.661 -18.917  1.00 25.16           C  
ANISOU 1505  CA  ASN A 233     2112   3668   3781    472   -453   -248       C  
ATOM   1506  C   ASN A 233     -13.245 -67.333 -20.230  1.00 25.60           C  
ANISOU 1506  C   ASN A 233     2184   3735   3810    487   -510   -275       C  
ATOM   1507  O   ASN A 233     -12.792 -66.657 -21.159  1.00 26.50           O  
ANISOU 1507  O   ASN A 233     2340   3859   3870    533   -532   -269       O  
ATOM   1508  CB  ASN A 233     -14.864 -65.760 -19.149  1.00 27.18           C  
ANISOU 1508  CB  ASN A 233     2322   3953   4053    515   -469   -255       C  
ATOM   1509  CG  ASN A 233     -16.076 -66.515 -19.627  1.00 33.90           C  
ANISOU 1509  CG  ASN A 233     3096   4827   4958    510   -517   -302       C  
ATOM   1510  ND2 ASN A 233     -16.786 -65.934 -20.575  1.00 36.54           N  
ANISOU 1510  ND2 ASN A 233     3406   5197   5280    567   -567   -320       N  
ATOM   1511  OD1 ASN A 233     -16.390 -67.605 -19.150  1.00 34.54           O  
ANISOU 1511  OD1 ASN A 233     3140   4894   5090    457   -508   -325       O  
ATOM   1512  N   GLY A 234     -13.386 -68.658 -20.257  1.00 25.59           N  
ANISOU 1512  N   GLY A 234     2156   3724   3844    445   -527   -304       N  
ATOM   1513  CA  GLY A 234     -13.081 -69.501 -21.407  1.00 25.66           C  
ANISOU 1513  CA  GLY A 234     2177   3738   3834    448   -577   -333       C  
ATOM   1514  C   GLY A 234     -11.628 -69.555 -21.819  1.00 26.04           C  
ANISOU 1514  C   GLY A 234     2298   3767   3827    455   -569   -314       C  
ATOM   1515  O   GLY A 234     -11.308 -70.083 -22.892  1.00 27.87           O  
ANISOU 1515  O   GLY A 234     2552   4003   4036    467   -609   -335       O  
ATOM   1516  N   GLY A 235     -10.742 -69.066 -20.965  1.00 24.48           N  
ANISOU 1516  N   GLY A 235     2138   3551   3613    446   -518   -277       N  
ATOM   1517  CA  GLY A 235      -9.336 -68.988 -21.308  1.00 23.28           C  
ANISOU 1517  CA  GLY A 235     2048   3383   3414    454   -507   -261       C  
ATOM   1518  C   GLY A 235      -8.600 -70.308 -21.360  1.00 23.61           C  
ANISOU 1518  C   GLY A 235     2104   3404   3463    420   -510   -273       C  
ATOM   1519  O   GLY A 235      -8.783 -71.159 -20.490  1.00 24.31           O  
ANISOU 1519  O   GLY A 235     2171   3476   3589    379   -493   -276       O  
ATOM   1520  N   SER A 236      -7.735 -70.465 -22.363  1.00 21.94           N  
ANISOU 1520  N   SER A 236     1936   3187   3213    439   -528   -279       N  
ATOM   1521  CA  SER A 236      -6.845 -71.615 -22.412  1.00 22.17           C  
ANISOU 1521  CA  SER A 236     1986   3194   3244    412   -525   -285       C  
ATOM   1522  C   SER A 236      -5.631 -71.273 -21.514  1.00 21.93           C  
ANISOU 1522  C   SER A 236     1985   3146   3200    403   -478   -255       C  
ATOM   1523  O   SER A 236      -5.484 -70.125 -21.080  1.00 21.81           O  
ANISOU 1523  O   SER A 236     1979   3138   3170    418   -453   -234       O  
ATOM   1524  CB  SER A 236      -6.348 -71.848 -23.842  1.00 23.30           C  
ANISOU 1524  CB  SER A 236     2167   3336   3350    438   -556   -302       C  
ATOM   1525  OG  SER A 236      -5.298 -70.949 -24.185  1.00 25.14           O  
ANISOU 1525  OG  SER A 236     2449   3563   3540    466   -532   -284       O  
ATOM   1526  N   HIS A 237      -4.708 -72.206 -21.359  1.00 20.28           N  
ANISOU 1526  N   HIS A 237     1796   2917   2993    384   -470   -255       N  
ATOM   1527  CA  HIS A 237      -3.466 -71.991 -20.615  1.00 18.64           C  
ANISOU 1527  CA  HIS A 237     1613   2696   2773    380   -436   -234       C  
ATOM   1528  C   HIS A 237      -2.686 -70.746 -21.087  1.00 19.38           C  
ANISOU 1528  C   HIS A 237     1737   2798   2830    409   -419   -224       C  
ATOM   1529  O   HIS A 237      -1.885 -70.205 -20.328  1.00 19.78           O  
ANISOU 1529  O   HIS A 237     1797   2844   2874    404   -388   -208       O  
ATOM   1530  CB  HIS A 237      -2.590 -73.244 -20.792  1.00 17.88           C  
ANISOU 1530  CB  HIS A 237     1535   2580   2680    367   -440   -242       C  
ATOM   1531  CG  HIS A 237      -1.334 -73.240 -19.979  1.00 16.86           C  
ANISOU 1531  CG  HIS A 237     1423   2439   2544    363   -413   -226       C  
ATOM   1532  CD2 HIS A 237      -0.053 -73.406 -20.383  1.00 18.06           C  
ANISOU 1532  CD2 HIS A 237     1599   2583   2680    374   -407   -228       C  
ATOM   1533  ND1 HIS A 237      -1.368 -73.132 -18.607  1.00 18.44           N  
ANISOU 1533  ND1 HIS A 237     1614   2635   2758    347   -392   -208       N  
ATOM   1534  CE1 HIS A 237      -0.097 -73.221 -18.209  1.00 18.01           C  
ANISOU 1534  CE1 HIS A 237     1576   2573   2692    351   -380   -201       C  
ATOM   1535  NE2 HIS A 237       0.726 -73.388 -19.251  1.00 17.76           N  
ANISOU 1535  NE2 HIS A 237     1562   2541   2647    367   -387   -214       N  
ATOM   1536  N   PHE A 238      -2.880 -70.342 -22.344  1.00 18.65           N  
ANISOU 1536  N   PHE A 238     1663   2713   2712    438   -438   -236       N  
ATOM   1537  CA  PHE A 238      -2.139 -69.236 -22.954  1.00 18.63           C  
ANISOU 1537  CA  PHE A 238     1699   2709   2671    466   -416   -230       C  
ATOM   1538  C   PHE A 238      -2.913 -67.911 -22.930  1.00 19.70           C  
ANISOU 1538  C   PHE A 238     1835   2860   2789    491   -407   -219       C  
ATOM   1539  O   PHE A 238      -2.488 -66.962 -23.587  1.00 19.98           O  
ANISOU 1539  O   PHE A 238     1910   2892   2789    520   -388   -217       O  
ATOM   1540  CB  PHE A 238      -1.781 -69.619 -24.415  1.00 19.02           C  
ANISOU 1540  CB  PHE A 238     1785   2749   2693    489   -437   -250       C  
ATOM   1541  CG  PHE A 238      -1.073 -70.965 -24.455  1.00 19.35           C  
ANISOU 1541  CG  PHE A 238     1827   2773   2751    466   -443   -260       C  
ATOM   1542  CD1 PHE A 238       0.270 -71.068 -24.145  1.00 21.29           C  
ANISOU 1542  CD1 PHE A 238     2087   3005   2997    457   -412   -255       C  
ATOM   1543  CD2 PHE A 238      -1.778 -72.132 -24.706  1.00 20.58           C  
ANISOU 1543  CD2 PHE A 238     1964   2928   2927    452   -480   -277       C  
ATOM   1544  CE1 PHE A 238       0.915 -72.311 -24.124  1.00 21.91           C  
ANISOU 1544  CE1 PHE A 238     2166   3067   3091    442   -417   -263       C  
ATOM   1545  CE2 PHE A 238      -1.143 -73.379 -24.663  1.00 21.37           C  
ANISOU 1545  CE2 PHE A 238     2069   3009   3041    432   -480   -284       C  
ATOM   1546  CZ  PHE A 238       0.205 -73.461 -24.394  1.00 21.51           C  
ANISOU 1546  CZ  PHE A 238     2105   3012   3055    430   -450   -275       C  
ATOM   1547  N   CYS A 239      -3.981 -67.815 -22.103  1.00 19.83           N  
ANISOU 1547  N   CYS A 239     1811   2889   2834    480   -413   -212       N  
ATOM   1548  CA  CYS A 239      -4.911 -66.677 -22.090  1.00 20.93           C  
ANISOU 1548  CA  CYS A 239     1944   3044   2963    507   -409   -202       C  
ATOM   1549  C   CYS A 239      -4.289 -65.336 -21.689  1.00 20.77           C  
ANISOU 1549  C   CYS A 239     1956   3019   2916    518   -359   -181       C  
ATOM   1550  O   CYS A 239      -4.909 -64.297 -21.938  1.00 22.07           O  
ANISOU 1550  O   CYS A 239     2132   3193   3061    550   -352   -173       O  
ATOM   1551  CB  CYS A 239      -6.168 -66.985 -21.263  1.00 22.36           C  
ANISOU 1551  CB  CYS A 239     2070   3237   3188    488   -420   -202       C  
ATOM   1552  SG  CYS A 239      -6.016 -66.730 -19.467  1.00 25.44           S  
ANISOU 1552  SG  CYS A 239     2444   3616   3604    451   -371   -176       S  
ATOM   1553  N   ALA A 240      -3.102 -65.339 -21.042  1.00 18.92           N  
ANISOU 1553  N   ALA A 240     1737   2772   2681    492   -325   -173       N  
ATOM   1554  CA  ALA A 240      -2.447 -64.068 -20.690  1.00 18.49           C  
ANISOU 1554  CA  ALA A 240     1712   2711   2601    497   -275   -159       C  
ATOM   1555  C   ALA A 240      -1.100 -63.895 -21.422  1.00 18.80           C  
ANISOU 1555  C   ALA A 240     1793   2735   2613    502   -252   -171       C  
ATOM   1556  O   ALA A 240      -0.330 -62.988 -21.090  1.00 18.80           O  
ANISOU 1556  O   ALA A 240     1816   2728   2598    496   -206   -166       O  
ATOM   1557  CB  ALA A 240      -2.233 -63.990 -19.168  1.00 18.45           C  
ANISOU 1557  CB  ALA A 240     1687   2705   2619    461   -249   -144       C  
ATOM   1558  N   ASN A 241      -0.830 -64.733 -22.440  1.00 18.22           N  
ANISOU 1558  N   ASN A 241     1731   2655   2535    512   -280   -188       N  
ATOM   1559  CA  ASN A 241       0.426 -64.630 -23.177  1.00 17.93           C  
ANISOU 1559  CA  ASN A 241     1734   2601   2478    516   -253   -201       C  
ATOM   1560  C   ASN A 241       0.318 -63.593 -24.303  1.00 19.23           C  
ANISOU 1560  C   ASN A 241     1955   2755   2597    558   -232   -203       C  
ATOM   1561  O   ASN A 241      -0.759 -63.078 -24.589  1.00 20.69           O  
ANISOU 1561  O   ASN A 241     2147   2950   2765    588   -249   -195       O  
ATOM   1562  CB  ASN A 241       0.774 -66.016 -23.763  1.00 18.51           C  
ANISOU 1562  CB  ASN A 241     1801   2667   2565    510   -287   -217       C  
ATOM   1563  CG  ASN A 241       1.315 -66.964 -22.724  1.00 20.75           C  
ANISOU 1563  CG  ASN A 241     2047   2951   2885    474   -293   -216       C  
ATOM   1564  ND2 ASN A 241       1.925 -68.058 -23.183  1.00 20.60           N  
ANISOU 1564  ND2 ASN A 241     2030   2922   2877    468   -308   -230       N  
ATOM   1565  OD1 ASN A 241       1.194 -66.741 -21.507  1.00 21.24           O  
ANISOU 1565  OD1 ASN A 241     2083   3023   2966    453   -283   -203       O  
ATOM   1566  N   SER A 242       1.437 -63.298 -24.970  1.00 19.53           N  
ANISOU 1566  N   SER A 242     2037   2770   2614    562   -194   -215       N  
ATOM   1567  CA  SER A 242       1.444 -62.334 -26.081  1.00 20.41           C  
ANISOU 1567  CA  SER A 242     2217   2862   2676    602   -164   -218       C  
ATOM   1568  C   SER A 242       0.412 -62.720 -27.153  1.00 21.62           C  
ANISOU 1568  C   SER A 242     2390   3020   2805    644   -219   -222       C  
ATOM   1569  O   SER A 242       0.201 -63.925 -27.395  1.00 22.26           O  
ANISOU 1569  O   SER A 242     2445   3108   2907    635   -268   -232       O  
ATOM   1570  CB  SER A 242       2.833 -62.268 -26.693  1.00 20.95           C  
ANISOU 1570  CB  SER A 242     2326   2901   2735    594   -116   -236       C  
ATOM   1571  OG  SER A 242       3.775 -61.917 -25.687  1.00 21.02           O  
ANISOU 1571  OG  SER A 242     2308   2910   2770    555    -72   -239       O  
ATOM   1572  N   GLY A 243      -0.327 -61.724 -27.636  1.00 22.93           N  
ANISOU 1572  N   GLY A 243     2596   3185   2931    689   -214   -213       N  
ATOM   1573  CA  GLY A 243      -1.348 -61.978 -28.642  1.00 23.76           C  
ANISOU 1573  CA  GLY A 243     2720   3299   3010    735   -272   -219       C  
ATOM   1574  C   GLY A 243      -2.711 -62.331 -28.092  1.00 24.61           C  
ANISOU 1574  C   GLY A 243     2762   3443   3147    737   -331   -215       C  
ATOM   1575  O   GLY A 243      -3.642 -62.565 -28.876  1.00 26.22           O  
ANISOU 1575  O   GLY A 243     2970   3660   3334    775   -386   -225       O  
ATOM   1576  N   ASN A 244      -2.874 -62.346 -26.749  1.00 22.86           N  
ANISOU 1576  N   ASN A 244     2480   3238   2969    698   -319   -201       N  
ATOM   1577  CA  ASN A 244      -4.171 -62.707 -26.171  1.00 23.03           C  
ANISOU 1577  CA  ASN A 244     2437   3290   3025    695   -365   -199       C  
ATOM   1578  C   ASN A 244      -5.260 -61.672 -26.499  1.00 24.16           C  
ANISOU 1578  C   ASN A 244     2593   3447   3141    750   -377   -190       C  
ATOM   1579  O   ASN A 244      -4.951 -60.537 -26.847  1.00 23.92           O  
ANISOU 1579  O   ASN A 244     2623   3400   3064    783   -335   -179       O  
ATOM   1580  CB  ASN A 244      -4.059 -63.003 -24.660  1.00 22.40           C  
ANISOU 1580  CB  ASN A 244     2299   3216   2995    641   -345   -187       C  
ATOM   1581  CG  ASN A 244      -3.931 -61.762 -23.792  1.00 21.64           C  
ANISOU 1581  CG  ASN A 244     2215   3117   2891    639   -289   -164       C  
ATOM   1582  ND2 ASN A 244      -2.735 -61.471 -23.275  1.00 20.60           N  
ANISOU 1582  ND2 ASN A 244     2102   2968   2757    609   -239   -159       N  
ATOM   1583  OD1 ASN A 244      -4.907 -61.085 -23.520  1.00 22.23           O  
ANISOU 1583  OD1 ASN A 244     2276   3204   2965    661   -291   -152       O  
ATOM   1584  N   SER A 245      -6.532 -62.064 -26.381  1.00 25.58           N  
ANISOU 1584  N   SER A 245     2716   3654   3348    759   -430   -198       N  
ATOM   1585  CA  SER A 245      -7.652 -61.201 -26.713  1.00 27.84           C  
ANISOU 1585  CA  SER A 245     3004   3959   3613    816   -451   -193       C  
ATOM   1586  C   SER A 245      -8.182 -60.371 -25.537  1.00 27.45           C  
ANISOU 1586  C   SER A 245     2922   3919   3587    809   -414   -169       C  
ATOM   1587  O   SER A 245      -9.196 -59.686 -25.684  1.00 28.51           O  
ANISOU 1587  O   SER A 245     3048   4071   3713    856   -431   -164       O  
ATOM   1588  CB  SER A 245      -8.792 -62.026 -27.302  1.00 32.14           C  
ANISOU 1588  CB  SER A 245     3500   4533   4179    834   -533   -221       C  
ATOM   1589  OG  SER A 245      -9.193 -62.992 -26.343  1.00 37.11           O  
ANISOU 1589  OG  SER A 245     4049   5176   4877    777   -546   -229       O  
ATOM   1590  N   ASN A 246      -7.488 -60.390 -24.392  1.00 24.79           N  
ANISOU 1590  N   ASN A 246     2571   3569   3277    754   -364   -154       N  
ATOM   1591  CA  ASN A 246      -7.918 -59.636 -23.213  1.00 23.54           C  
ANISOU 1591  CA  ASN A 246     2389   3415   3140    742   -323   -131       C  
ATOM   1592  C   ASN A 246      -6.816 -58.711 -22.716  1.00 22.36           C  
ANISOU 1592  C   ASN A 246     2293   3240   2963    725   -249   -111       C  
ATOM   1593  O   ASN A 246      -6.680 -58.524 -21.503  1.00 21.45           O  
ANISOU 1593  O   ASN A 246     2156   3121   2873    686   -213    -96       O  
ATOM   1594  CB  ASN A 246      -8.356 -60.610 -22.105  1.00 24.41           C  
ANISOU 1594  CB  ASN A 246     2424   3535   3315    687   -337   -134       C  
ATOM   1595  CG  ASN A 246      -9.728 -61.166 -22.367  1.00 29.13           C  
ANISOU 1595  CG  ASN A 246     2960   4159   3948    704   -395   -152       C  
ATOM   1596  ND2 ASN A 246      -9.832 -62.460 -22.554  1.00 27.99           N  
ANISOU 1596  ND2 ASN A 246     2779   4021   3836    675   -437   -177       N  
ATOM   1597  OD1 ASN A 246     -10.711 -60.428 -22.401  1.00 32.40           O  
ANISOU 1597  OD1 ASN A 246     3359   4590   4363    744   -401   -147       O  
ATOM   1598  N   GLN A 247      -6.007 -58.136 -23.633  1.00 21.87           N  
ANISOU 1598  N   GLN A 247     2303   3157   2848    753   -224   -114       N  
ATOM   1599  CA  GLN A 247      -4.904 -57.271 -23.201  1.00 21.79           C  
ANISOU 1599  CA  GLN A 247     2341   3122   2816    731   -149   -102       C  
ATOM   1600  C   GLN A 247      -5.391 -55.996 -22.505  1.00 21.68           C  
ANISOU 1600  C   GLN A 247     2343   3106   2790    745   -100    -78       C  
ATOM   1601  O   GLN A 247      -4.684 -55.469 -21.638  1.00 21.56           O  
ANISOU 1601  O   GLN A 247     2339   3077   2777    707    -44    -69       O  
ATOM   1602  CB  GLN A 247      -3.958 -56.945 -24.355  1.00 22.96           C  
ANISOU 1602  CB  GLN A 247     2566   3244   2915    754   -123   -114       C  
ATOM   1603  CG  GLN A 247      -3.252 -58.204 -24.847  1.00 25.11           C  
ANISOU 1603  CG  GLN A 247     2824   3514   3205    729   -157   -137       C  
ATOM   1604  CD  GLN A 247      -2.488 -57.931 -26.120  1.00 29.55           C  
ANISOU 1604  CD  GLN A 247     3463   4046   3717    759   -134   -150       C  
ATOM   1605  NE2 GLN A 247      -2.712 -58.759 -27.140  1.00 30.93           N  
ANISOU 1605  NE2 GLN A 247     3646   4224   3883    783   -188   -166       N  
ATOM   1606  OE1 GLN A 247      -1.707 -56.977 -26.206  1.00 30.22           O  
ANISOU 1606  OE1 GLN A 247     3605   4104   3772    760    -65   -147       O  
ATOM   1607  N   ALA A 248      -6.605 -55.516 -22.837  1.00 21.26           N  
ANISOU 1607  N   ALA A 248     2287   3068   2725    800   -124    -69       N  
ATOM   1608  CA  ALA A 248      -7.122 -54.313 -22.177  1.00 21.31           C  
ANISOU 1608  CA  ALA A 248     2307   3069   2719    818    -76    -44       C  
ATOM   1609  C   ALA A 248      -7.337 -54.579 -20.676  1.00 20.62           C  
ANISOU 1609  C   ALA A 248     2159   2990   2685    761    -61    -33       C  
ATOM   1610  O   ALA A 248      -6.804 -53.841 -19.849  1.00 22.24           O  
ANISOU 1610  O   ALA A 248     2389   3177   2883    732      1    -18       O  
ATOM   1611  CB  ALA A 248      -8.416 -53.845 -22.826  1.00 22.23           C  
ANISOU 1611  CB  ALA A 248     2426   3204   2818    892   -110    -38       C  
ATOM   1612  N   LEU A 249      -8.037 -55.680 -20.322  1.00 20.80           N  
ANISOU 1612  N   LEU A 249     2108   3035   2761    740   -116    -42       N  
ATOM   1613  CA  LEU A 249      -8.289 -55.992 -18.917  1.00 21.64           C  
ANISOU 1613  CA  LEU A 249     2165   3143   2916    689   -100    -31       C  
ATOM   1614  C   LEU A 249      -7.038 -56.508 -18.214  1.00 20.15           C  
ANISOU 1614  C   LEU A 249     1981   2939   2736    627    -78    -36       C  
ATOM   1615  O   LEU A 249      -6.733 -56.073 -17.091  1.00 19.17           O  
ANISOU 1615  O   LEU A 249     1863   2803   2618    593    -32    -21       O  
ATOM   1616  CB  LEU A 249      -9.420 -57.025 -18.793  1.00 24.25           C  
ANISOU 1616  CB  LEU A 249     2418   3496   3300    685   -157    -44       C  
ATOM   1617  CG  LEU A 249      -9.670 -57.597 -17.383  1.00 28.59           C  
ANISOU 1617  CG  LEU A 249     2921   4041   3903    629   -141    -37       C  
ATOM   1618  CD1 LEU A 249     -10.080 -56.504 -16.408  1.00 29.33           C  
ANISOU 1618  CD1 LEU A 249     3026   4124   3995    630    -84     -9       C  
ATOM   1619  CD2 LEU A 249     -10.675 -58.718 -17.436  1.00 31.27           C  
ANISOU 1619  CD2 LEU A 249     3188   4397   4294    621   -194    -57       C  
ATOM   1620  N   ILE A 250      -6.354 -57.495 -18.833  1.00 19.68           N  
ANISOU 1620  N   ILE A 250     1917   2881   2680    614   -113    -57       N  
ATOM   1621  CA  ILE A 250      -5.180 -58.080 -18.190  1.00 19.01           C  
ANISOU 1621  CA  ILE A 250     1831   2784   2607    561   -100    -63       C  
ATOM   1622  C   ILE A 250      -4.079 -57.055 -17.990  1.00 18.69           C  
ANISOU 1622  C   ILE A 250     1844   2727   2533    550    -39    -59       C  
ATOM   1623  O   ILE A 250      -3.527 -56.959 -16.898  1.00 17.73           O  
ANISOU 1623  O   ILE A 250     1717   2598   2423    509    -11    -54       O  
ATOM   1624  CB  ILE A 250      -4.711 -59.330 -18.960  1.00 18.77           C  
ANISOU 1624  CB  ILE A 250     1787   2758   2587    555   -148    -87       C  
ATOM   1625  CG1 ILE A 250      -5.795 -60.414 -18.915  1.00 19.61           C  
ANISOU 1625  CG1 ILE A 250     1836   2879   2735    552   -202    -94       C  
ATOM   1626  CG2 ILE A 250      -3.386 -59.837 -18.423  1.00 18.69           C  
ANISOU 1626  CG2 ILE A 250     1781   2737   2585    511   -133    -94       C  
ATOM   1627  CD1 ILE A 250      -5.506 -61.603 -19.873  1.00 20.94           C  
ANISOU 1627  CD1 ILE A 250     1997   3052   2909    553   -251   -119       C  
ATOM   1628  N   GLY A 251      -3.818 -56.241 -19.016  1.00 18.78           N  
ANISOU 1628  N   GLY A 251     1907   2727   2500    587    -16    -62       N  
ATOM   1629  CA  GLY A 251      -2.829 -55.179 -18.897  1.00 19.34           C  
ANISOU 1629  CA  GLY A 251     2031   2778   2539    575     51    -62       C  
ATOM   1630  C   GLY A 251      -3.208 -54.127 -17.870  1.00 18.32           C  
ANISOU 1630  C   GLY A 251     1913   2643   2405    566    101    -41       C  
ATOM   1631  O   GLY A 251      -2.355 -53.650 -17.116  1.00 18.95           O  
ANISOU 1631  O   GLY A 251     2008   2711   2481    526    146    -43       O  
ATOM   1632  N   LYS A 252      -4.500 -53.754 -17.805  1.00 17.31           N  
ANISOU 1632  N   LYS A 252     1776   2523   2278    602     92    -21       N  
ATOM   1633  CA  LYS A 252      -4.974 -52.798 -16.789  1.00 17.99           C  
ANISOU 1633  CA  LYS A 252     1871   2602   2362    594    140      3       C  
ATOM   1634  C   LYS A 252      -4.706 -53.364 -15.381  1.00 17.34           C  
ANISOU 1634  C   LYS A 252     1750   2522   2318    534    140      5       C  
ATOM   1635  O   LYS A 252      -4.167 -52.663 -14.523  1.00 17.83           O  
ANISOU 1635  O   LYS A 252     1837   2569   2368    502    191     11       O  
ATOM   1636  CB  LYS A 252      -6.488 -52.542 -16.948  1.00 19.49           C  
ANISOU 1636  CB  LYS A 252     2041   2805   2559    645    121     20       C  
ATOM   1637  CG  LYS A 252      -7.086 -51.780 -15.762  1.00 20.47           C  
ANISOU 1637  CG  LYS A 252     2163   2921   2692    632    167     46       C  
ATOM   1638  CD  LYS A 252      -8.471 -51.216 -16.038  1.00 22.69           C  
ANISOU 1638  CD  LYS A 252     2437   3211   2973    692    162     63       C  
ATOM   1639  CE  LYS A 252      -9.476 -52.306 -16.277  1.00 23.19           C  
ANISOU 1639  CE  LYS A 252     2426   3301   3083    706     90     52       C  
ATOM   1640  NZ  LYS A 252     -10.852 -51.723 -16.389  1.00 25.14           N1+
ANISOU 1640  NZ  LYS A 252     2654   3560   3338    761     87     67       N1+
ATOM   1641  N   LYS A 253      -5.057 -54.650 -15.182  1.00 17.06           N  
ANISOU 1641  N   LYS A 253     1658   2500   2323    519     84     -2       N  
ATOM   1642  CA  LYS A 253      -4.879 -55.261 -13.850  1.00 16.56           C  
ANISOU 1642  CA  LYS A 253     1567   2435   2292    469     82      2       C  
ATOM   1643  C   LYS A 253      -3.414 -55.429 -13.470  1.00 16.37           C  
ANISOU 1643  C   LYS A 253     1558   2404   2259    428     94    -14       C  
ATOM   1644  O   LYS A 253      -3.050 -55.157 -12.330  1.00 17.13           O  
ANISOU 1644  O   LYS A 253     1661   2491   2355    393    121     -9       O  
ATOM   1645  CB  LYS A 253      -5.631 -56.601 -13.784  1.00 16.68           C  
ANISOU 1645  CB  LYS A 253     1524   2461   2351    465     26     -3       C  
ATOM   1646  CG  LYS A 253      -7.106 -56.426 -13.422  1.00 18.56           C  
ANISOU 1646  CG  LYS A 253     1734   2704   2615    483     28     13       C  
ATOM   1647  CD  LYS A 253      -7.220 -56.081 -11.935  1.00 20.20           C  
ANISOU 1647  CD  LYS A 253     1949   2894   2834    448     71     32       C  
ATOM   1648  CE  LYS A 253      -8.652 -56.050 -11.457  1.00 20.12           C  
ANISOU 1648  CE  LYS A 253     1904   2883   2858    459     78     46       C  
ATOM   1649  NZ  LYS A 253      -8.678 -55.669 -10.008  1.00 20.79           N1+
ANISOU 1649  NZ  LYS A 253     2008   2944   2947    424    128     66       N1+
ATOM   1650  N   GLY A 254      -2.574 -55.857 -14.414  1.00 16.34           N  
ANISOU 1650  N   GLY A 254     1559   2403   2246    433     74    -36       N  
ATOM   1651  CA  GLY A 254      -1.148 -56.035 -14.111  1.00 17.26           C  
ANISOU 1651  CA  GLY A 254     1683   2516   2360    397     84    -57       C  
ATOM   1652  C   GLY A 254      -0.475 -54.719 -13.759  1.00 17.75           C  
ANISOU 1652  C   GLY A 254     1786   2565   2392    381    148    -59       C  
ATOM   1653  O   GLY A 254       0.243 -54.609 -12.748  1.00 17.52           O  
ANISOU 1653  O   GLY A 254     1755   2534   2367    342    163    -66       O  
ATOM   1654  N   VAL A 255      -0.723 -53.672 -14.572  1.00 16.94           N  
ANISOU 1654  N   VAL A 255     1726   2451   2258    413    189    -54       N  
ATOM   1655  CA  VAL A 255      -0.147 -52.354 -14.277  1.00 17.69           C  
ANISOU 1655  CA  VAL A 255     1869   2530   2324    397    260    -57       C  
ATOM   1656  C   VAL A 255      -0.698 -51.817 -12.961  1.00 17.64           C  
ANISOU 1656  C   VAL A 255     1863   2519   2319    376    285    -36       C  
ATOM   1657  O   VAL A 255       0.080 -51.320 -12.155  1.00 19.01           O  
ANISOU 1657  O   VAL A 255     2050   2685   2486    335    320    -47       O  
ATOM   1658  CB  VAL A 255      -0.408 -51.359 -15.438  1.00 18.97           C  
ANISOU 1658  CB  VAL A 255     2087   2675   2445    442    303    -53       C  
ATOM   1659  CG1 VAL A 255      -0.100 -49.920 -15.023  1.00 19.18           C  
ANISOU 1659  CG1 VAL A 255     2169   2679   2440    428    385    -51       C  
ATOM   1660  CG2 VAL A 255       0.439 -51.738 -16.644  1.00 19.66           C  
ANISOU 1660  CG2 VAL A 255     2188   2757   2525    452    295    -80       C  
ATOM   1661  N   ALA A 256      -2.021 -51.911 -12.738  1.00 17.79           N  
ANISOU 1661  N   ALA A 256     1868   2542   2349    402    269     -8       N  
ATOM   1662  CA  ALA A 256      -2.590 -51.387 -11.493  1.00 17.84           C  
ANISOU 1662  CA  ALA A 256     1880   2540   2358    383    299     14       C  
ATOM   1663  C   ALA A 256      -2.043 -52.073 -10.270  1.00 17.29           C  
ANISOU 1663  C   ALA A 256     1787   2473   2310    334    279      8       C  
ATOM   1664  O   ALA A 256      -1.770 -51.430  -9.258  1.00 17.92           O  
ANISOU 1664  O   ALA A 256     1891   2541   2378    303    317     11       O  
ATOM   1665  CB  ALA A 256      -4.103 -51.464 -11.503  1.00 18.31           C  
ANISOU 1665  CB  ALA A 256     1920   2603   2434    420    285     41       C  
ATOM   1666  N   TRP A 257      -1.884 -53.410 -10.351  1.00 16.78           N  
ANISOU 1666  N   TRP A 257     1679   2422   2274    329    219     -3       N  
ATOM   1667  CA  TRP A 257      -1.334 -54.156  -9.213  1.00 16.58           C  
ANISOU 1667  CA  TRP A 257     1637   2397   2265    290    195    -10       C  
ATOM   1668  C   TRP A 257       0.108 -53.707  -8.940  1.00 16.42           C  
ANISOU 1668  C   TRP A 257     1635   2377   2226    257    214    -37       C  
ATOM   1669  O   TRP A 257       0.460 -53.459  -7.788  1.00 17.00           O  
ANISOU 1669  O   TRP A 257     1721   2446   2293    225    228    -38       O  
ATOM   1670  CB  TRP A 257      -1.359 -55.665  -9.542  1.00 15.87           C  
ANISOU 1670  CB  TRP A 257     1504   2319   2205    296    131    -18       C  
ATOM   1671  CG  TRP A 257      -1.146 -56.531  -8.333  1.00 16.08           C  
ANISOU 1671  CG  TRP A 257     1520   2342   2248    268    106    -17       C  
ATOM   1672  CD1 TRP A 257       0.018 -57.114  -7.928  1.00 16.84           C  
ANISOU 1672  CD1 TRP A 257     1611   2445   2344    246     80    -38       C  
ATOM   1673  CD2 TRP A 257      -2.126 -56.863  -7.360  1.00 15.82           C  
ANISOU 1673  CD2 TRP A 257     1485   2295   2231    261    108      6       C  
ATOM   1674  CE2 TRP A 257      -1.502 -57.679  -6.393  1.00 17.00           C  
ANISOU 1674  CE2 TRP A 257     1636   2440   2384    237     82      0       C  
ATOM   1675  CE3 TRP A 257      -3.495 -56.570  -7.221  1.00 15.97           C  
ANISOU 1675  CE3 TRP A 257     1500   2304   2264    275    130     30       C  
ATOM   1676  NE1 TRP A 257      -0.175 -57.766  -6.734  1.00 17.08           N  
ANISOU 1676  NE1 TRP A 257     1643   2465   2383    230     64    -27       N  
ATOM   1677  CZ2 TRP A 257      -2.179 -58.155  -5.278  1.00 16.59           C  
ANISOU 1677  CZ2 TRP A 257     1592   2367   2343    226     85     18       C  
ATOM   1678  CZ3 TRP A 257      -4.174 -57.083  -6.140  1.00 17.27           C  
ANISOU 1678  CZ3 TRP A 257     1664   2451   2447    260    133     46       C  
ATOM   1679  CH2 TRP A 257      -3.515 -57.864  -5.183  1.00 16.30           C  
ANISOU 1679  CH2 TRP A 257     1553   2318   2323    235    114     41       C  
ATOM   1680  N   MET A 258       0.932 -53.604  -9.991  1.00 16.87           N  
ANISOU 1680  N   MET A 258     1693   2440   2276    264    217    -62       N  
ATOM   1681  CA  MET A 258       2.339 -53.192  -9.785  1.00 17.23           C  
ANISOU 1681  CA  MET A 258     1747   2488   2312    230    238    -95       C  
ATOM   1682  C   MET A 258       2.432 -51.746  -9.288  1.00 18.49           C  
ANISOU 1682  C   MET A 258     1950   2631   2442    210    308    -94       C  
ATOM   1683  O   MET A 258       3.253 -51.436  -8.430  1.00 19.31           O  
ANISOU 1683  O   MET A 258     2058   2737   2542    171    320   -115       O  
ATOM   1684  CB  MET A 258       3.159 -53.407 -11.074  1.00 17.62           C  
ANISOU 1684  CB  MET A 258     1789   2541   2363    242    235   -123       C  
ATOM   1685  CG  MET A 258       3.218 -54.871 -11.498  1.00 18.82           C  
ANISOU 1685  CG  MET A 258     1900   2707   2543    257    168   -127       C  
ATOM   1686  SD  MET A 258       4.254 -55.722 -10.283  1.00 24.82           S  
ANISOU 1686  SD  MET A 258     2626   3482   3323    221    126   -148       S  
ATOM   1687  CE  MET A 258       4.008 -57.407 -10.673  1.00 25.41           C  
ANISOU 1687  CE  MET A 258     2664   3566   3426    243     56   -143       C  
ATOM   1688  N   LYS A 259       1.581 -50.877  -9.795  1.00 18.42           N  
ANISOU 1688  N   LYS A 259     1977   2609   2414    237    351    -72       N  
ATOM   1689  CA  LYS A 259       1.551 -49.485  -9.321  1.00 18.20           C  
ANISOU 1689  CA  LYS A 259     1999   2562   2356    221    424    -67       C  
ATOM   1690  C   LYS A 259       1.156 -49.435  -7.839  1.00 18.60           C  
ANISOU 1690  C   LYS A 259     2051   2608   2409    194    423    -49       C  
ATOM   1691  O   LYS A 259       1.820 -48.784  -7.029  1.00 19.43           O  
ANISOU 1691  O   LYS A 259     2177   2706   2498    154    456    -65       O  
ATOM   1692  CB  LYS A 259       0.532 -48.678 -10.139  1.00 19.45           C  
ANISOU 1692  CB  LYS A 259     2194   2704   2491    268    465    -40       C  
ATOM   1693  CG  LYS A 259       1.061 -48.275 -11.503  1.00 20.37           C  
ANISOU 1693  CG  LYS A 259     2339   2813   2589    291    492    -59       C  
ATOM   1694  CD  LYS A 259       1.965 -47.055 -11.333  1.00 23.60           C  
ANISOU 1694  CD  LYS A 259     2796   3200   2971    255    572    -83       C  
ATOM   1695  CE  LYS A 259       2.156 -46.342 -12.655  1.00 23.02           C  
ANISOU 1695  CE  LYS A 259     2774   3104   2867    287    624    -92       C  
ATOM   1696  NZ  LYS A 259       3.059 -45.153 -12.490  1.00 22.06           N1+
ANISOU 1696  NZ  LYS A 259     2702   2958   2722    247    712   -119       N1+
ATOM   1697  N   ARG A 260       0.079 -50.149  -7.469  1.00 18.00           N  
ANISOU 1697  N   ARG A 260     1953   2534   2352    215    387    -19       N  
ATOM   1698  CA  ARG A 260      -0.407 -50.075  -6.094  1.00 18.05           C  
ANISOU 1698  CA  ARG A 260     1971   2528   2357    193    396      1       C  
ATOM   1699  C   ARG A 260       0.643 -50.592  -5.127  1.00 18.63           C  
ANISOU 1699  C   ARG A 260     2035   2610   2433    151    365    -24       C  
ATOM   1700  O   ARG A 260       0.838 -50.017  -4.039  1.00 19.70           O  
ANISOU 1700  O   ARG A 260     2201   2734   2551    120    392    -24       O  
ATOM   1701  CB  ARG A 260      -1.749 -50.835  -5.947  1.00 19.24           C  
ANISOU 1701  CB  ARG A 260     2097   2678   2536    221    367     33       C  
ATOM   1702  CG  ARG A 260      -2.268 -50.918  -4.497  1.00 21.28           C  
ANISOU 1702  CG  ARG A 260     2370   2919   2798    198    377     54       C  
ATOM   1703  CD  ARG A 260      -2.517 -49.525  -3.927  1.00 21.95           C  
ANISOU 1703  CD  ARG A 260     2507   2981   2853    187    450     69       C  
ATOM   1704  NE  ARG A 260      -2.924 -49.507  -2.510  1.00 25.63           N  
ANISOU 1704  NE  ARG A 260     2997   3424   3315    162    467     87       N  
ATOM   1705  CZ  ARG A 260      -2.074 -49.478  -1.488  1.00 30.69           C  
ANISOU 1705  CZ  ARG A 260     3663   4060   3937    122    463     72       C  
ATOM   1706  NH1 ARG A 260      -0.764 -49.561  -1.699  1.00 27.03           N1+
ANISOU 1706  NH1 ARG A 260     3191   3616   3463    101    438     34       N1+
ATOM   1707  NH2 ARG A 260      -2.528 -49.394  -0.238  1.00 31.79           N  
ANISOU 1707  NH2 ARG A 260     3836   4174   4070    104    484     91       N  
ATOM   1708  N   PHE A 261       1.288 -51.724  -5.489  1.00 17.42           N  
ANISOU 1708  N   PHE A 261     1840   2476   2301    153    305    -45       N  
ATOM   1709  CA  PHE A 261       2.165 -52.373  -4.511  1.00 17.28           C  
ANISOU 1709  CA  PHE A 261     1811   2467   2287    125    264    -65       C  
ATOM   1710  C   PHE A 261       3.660 -52.079  -4.663  1.00 18.14           C  
ANISOU 1710  C   PHE A 261     1911   2593   2390     97    263   -112       C  
ATOM   1711  O   PHE A 261       4.368 -52.080  -3.620  1.00 21.35           O  
ANISOU 1711  O   PHE A 261     2321   3004   2787     68    248   -131       O  
ATOM   1712  CB  PHE A 261       1.865 -53.876  -4.485  1.00 17.14           C  
ANISOU 1712  CB  PHE A 261     1759   2458   2296    143    200    -56       C  
ATOM   1713  CG  PHE A 261       0.451 -54.096  -3.963  1.00 16.98           C  
ANISOU 1713  CG  PHE A 261     1749   2417   2284    157    208    -16       C  
ATOM   1714  CD1 PHE A 261       0.124 -53.792  -2.647  1.00 17.44           C  
ANISOU 1714  CD1 PHE A 261     1843   2455   2328    137    230      0       C  
ATOM   1715  CD2 PHE A 261      -0.547 -54.567  -4.795  1.00 18.03           C  
ANISOU 1715  CD2 PHE A 261     1860   2551   2441    188    199      2       C  
ATOM   1716  CE1 PHE A 261      -1.183 -53.965  -2.176  1.00 18.25           C  
ANISOU 1716  CE1 PHE A 261     1955   2535   2443    147    247     35       C  
ATOM   1717  CE2 PHE A 261      -1.860 -54.715  -4.336  1.00 17.93           C  
ANISOU 1717  CE2 PHE A 261     1849   2520   2442    198    212     32       C  
ATOM   1718  CZ  PHE A 261      -2.158 -54.458  -3.018  1.00 17.67           C  
ANISOU 1718  CZ  PHE A 261     1849   2465   2399    177    238     49       C  
ATOM   1719  N   MET A 262       4.168 -51.885  -5.883  1.00 17.63           N  
ANISOU 1719  N   MET A 262     1833   2536   2331    107    277   -133       N  
ATOM   1720  CA  MET A 262       5.584 -51.518  -5.999  1.00 17.63           C  
ANISOU 1720  CA  MET A 262     1821   2548   2331     76    287   -182       C  
ATOM   1721  C   MET A 262       5.796 -50.044  -5.713  1.00 18.58           C  
ANISOU 1721  C   MET A 262     1984   2652   2424     45    361   -194       C  
ATOM   1722  O   MET A 262       6.863 -49.673  -5.220  1.00 20.03           O  
ANISOU 1722  O   MET A 262     2160   2845   2606      7    368   -235       O  
ATOM   1723  CB  MET A 262       6.147 -51.850  -7.378  1.00 18.80           C  
ANISOU 1723  CB  MET A 262     1944   2704   2496     93    284   -204       C  
ATOM   1724  CG  MET A 262       6.158 -53.351  -7.608  1.00 19.81           C  
ANISOU 1724  CG  MET A 262     2029   2847   2651    118    210   -200       C  
ATOM   1725  SD  MET A 262       6.877 -53.823  -9.186  1.00 25.71           S  
ANISOU 1725  SD  MET A 262     2751   3601   3418    137    205   -227       S  
ATOM   1726  CE  MET A 262       8.469 -53.062  -9.092  1.00 21.95           C  
ANISOU 1726  CE  MET A 262     2263   3132   2946     93    241   -286       C  
ATOM   1727  N   ASP A 263       4.814 -49.206  -6.057  1.00 17.61           N  
ANISOU 1727  N   ASP A 263     1903   2507   2282     63    417   -162       N  
ATOM   1728  CA  ASP A 263       4.964 -47.758  -5.834  1.00 18.26           C  
ANISOU 1728  CA  ASP A 263     2034   2569   2335     36    497   -171       C  
ATOM   1729  C   ASP A 263       4.136 -47.281  -4.637  1.00 19.46           C  
ANISOU 1729  C   ASP A 263     2223   2704   2466     26    517   -139       C  
ATOM   1730  O   ASP A 263       4.109 -46.064  -4.395  1.00 19.36           O  
ANISOU 1730  O   ASP A 263     2258   2671   2426      5    587   -140       O  
ATOM   1731  CB  ASP A 263       4.494 -46.982  -7.082  1.00 19.08           C  
ANISOU 1731  CB  ASP A 263     2174   2653   2423     67    558   -158       C  
ATOM   1732  CG  ASP A 263       5.256 -47.230  -8.370  1.00 21.50           C  
ANISOU 1732  CG  ASP A 263     2464   2965   2742     78    558   -188       C  
ATOM   1733  OD1 ASP A 263       6.248 -48.003  -8.349  1.00 21.41           O  
ANISOU 1733  OD1 ASP A 263     2404   2974   2756     58    513   -224       O  
ATOM   1734  OD2 ASP A 263       4.880 -46.636  -9.413  1.00 22.52           O1-
ANISOU 1734  OD2 ASP A 263     2630   3074   2853    109    606   -178       O1-
ATOM   1735  N   ASN A 264       3.393 -48.175  -3.929  1.00 18.79           N  
ANISOU 1735  N   ASN A 264     2123   2623   2393     41    465   -108       N  
ATOM   1736  CA  ASN A 264       2.490 -47.778  -2.824  1.00 19.48           C  
ANISOU 1736  CA  ASN A 264     2249   2689   2464     35    489    -73       C  
ATOM   1737  C   ASN A 264       1.488 -46.717  -3.291  1.00 20.08           C  
ANISOU 1737  C   ASN A 264     2367   2741   2523     59    561    -41       C  
ATOM   1738  O   ASN A 264       1.096 -45.847  -2.513  1.00 21.33           O  
ANISOU 1738  O   ASN A 264     2571   2876   2658     42    613    -25       O  
ATOM   1739  CB  ASN A 264       3.289 -47.237  -1.611  1.00 20.54           C  
ANISOU 1739  CB  ASN A 264     2410   2820   2576    -16    502    -99       C  
ATOM   1740  CG  ASN A 264       4.372 -48.188  -1.170  1.00 24.15           C  
ANISOU 1740  CG  ASN A 264     2825   3304   3046    -33    429   -136       C  
ATOM   1741  ND2 ASN A 264       5.522 -47.638  -0.787  1.00 24.62           N  
ANISOU 1741  ND2 ASN A 264     2886   3373   3094    -75    438   -183       N  
ATOM   1742  OD1 ASN A 264       4.189 -49.423  -1.167  1.00 25.08           O  
ANISOU 1742  OD1 ASN A 264     2911   3434   3186     -9    365   -125       O  
ATOM   1743  N   ASP A 265       1.102 -46.777  -4.576  1.00 19.23           N  
ANISOU 1743  N   ASP A 265     2247   2637   2424    100    564    -32       N  
ATOM   1744  CA  ASP A 265       0.351 -45.691  -5.187  1.00 18.68           C  
ANISOU 1744  CA  ASP A 265     2220   2545   2332    129    632     -9       C  
ATOM   1745  C   ASP A 265      -1.134 -45.877  -5.024  1.00 20.00           C  
ANISOU 1745  C   ASP A 265     2384   2704   2509    169    627     38       C  
ATOM   1746  O   ASP A 265      -1.750 -46.643  -5.774  1.00 20.61           O  
ANISOU 1746  O   ASP A 265     2425   2796   2610    209    584     50       O  
ATOM   1747  CB  ASP A 265       0.783 -45.549  -6.663  1.00 18.45           C  
ANISOU 1747  CB  ASP A 265     2189   2521   2299    155    642    -28       C  
ATOM   1748  CG  ASP A 265       0.386 -44.252  -7.312  1.00 21.02           C  
ANISOU 1748  CG  ASP A 265     2576   2821   2590    180    723    -14       C  
ATOM   1749  OD1 ASP A 265      -0.531 -43.592  -6.790  1.00 21.26           O  
ANISOU 1749  OD1 ASP A 265     2639   2833   2605    193    762     19       O  
ATOM   1750  OD2 ASP A 265       0.962 -43.934  -8.367  1.00 21.15           O1-
ANISOU 1750  OD2 ASP A 265     2609   2832   2594    191    748    -36       O1-
ATOM   1751  N   THR A 266      -1.726 -45.174  -4.027  1.00 21.22           N  
ANISOU 1751  N   THR A 266     2578   2836   2650    156    674     62       N  
ATOM   1752  CA  THR A 266      -3.144 -45.325  -3.742  1.00 21.83           C  
ANISOU 1752  CA  THR A 266     2649   2903   2743    190    676    104       C  
ATOM   1753  C   THR A 266      -4.051 -44.742  -4.804  1.00 21.41           C  
ANISOU 1753  C   THR A 266     2604   2845   2684    248    706    126       C  
ATOM   1754  O   THR A 266      -5.237 -45.092  -4.796  1.00 22.32           O  
ANISOU 1754  O   THR A 266     2694   2962   2824    283    691    155       O  
ATOM   1755  CB  THR A 266      -3.495 -44.791  -2.347  1.00 25.95           C  
ANISOU 1755  CB  THR A 266     3211   3398   3251    159    720    123       C  
ATOM   1756  CG2 THR A 266      -2.716 -45.523  -1.243  1.00 27.59           C  
ANISOU 1756  CG2 THR A 266     3411   3609   3462    111    678    103       C  
ATOM   1757  OG1 THR A 266      -3.197 -43.410  -2.333  1.00 28.24           O  
ANISOU 1757  OG1 THR A 266     3562   3667   3502    147    797    120       O  
ATOM   1758  N   ARG A 267      -3.501 -44.037  -5.831  1.00 19.84           N  
ANISOU 1758  N   ARG A 267     2434   2646   2458    263    737    110       N  
ATOM   1759  CA  ARG A 267      -4.340 -43.675  -6.979  1.00 19.89           C  
ANISOU 1759  CA  ARG A 267     2448   2652   2457    330    748    130       C  
ATOM   1760  C   ARG A 267      -4.805 -44.945  -7.721  1.00 20.06           C  
ANISOU 1760  C   ARG A 267     2403   2703   2517    365    665    129       C  
ATOM   1761  O   ARG A 267      -5.757 -44.897  -8.513  1.00 20.94           O  
ANISOU 1761  O   ARG A 267     2505   2821   2632    423    654    147       O  
ATOM   1762  CB  ARG A 267      -3.547 -42.817  -7.956  1.00 19.66           C  
ANISOU 1762  CB  ARG A 267     2470   2612   2390    338    795    109       C  
ATOM   1763  CG  ARG A 267      -3.186 -41.447  -7.379  1.00 21.38           C  
ANISOU 1763  CG  ARG A 267     2760   2797   2567    308    889    109       C  
ATOM   1764  CD  ARG A 267      -2.375 -40.665  -8.399  1.00 21.95           C  
ANISOU 1764  CD  ARG A 267     2884   2853   2603    315    942     85       C  
ATOM   1765  NE  ARG A 267      -1.106 -41.318  -8.711  1.00 21.54           N  
ANISOU 1765  NE  ARG A 267     2800   2817   2565    274    907     40       N  
ATOM   1766  CZ  ARG A 267      -0.302 -40.970  -9.702  1.00 22.30           C  
ANISOU 1766  CZ  ARG A 267     2926   2904   2643    276    939     11       C  
ATOM   1767  NH1 ARG A 267      -0.620 -39.950 -10.502  1.00 23.03           N1+
ANISOU 1767  NH1 ARG A 267     3089   2967   2694    319   1009     24       N1+
ATOM   1768  NH2 ARG A 267       0.836 -41.628  -9.902  1.00 22.80           N  
ANISOU 1768  NH2 ARG A 267     2952   2983   2727    238    906    -31       N  
ATOM   1769  N   TYR A 268      -4.112 -46.082  -7.493  1.00 18.91           N  
ANISOU 1769  N   TYR A 268     2212   2576   2396    330    604    106       N  
ATOM   1770  CA  TYR A 268      -4.420 -47.331  -8.158  1.00 19.12           C  
ANISOU 1770  CA  TYR A 268     2180   2627   2457    354    529    100       C  
ATOM   1771  C   TYR A 268      -5.134 -48.321  -7.250  1.00 19.74           C  
ANISOU 1771  C   TYR A 268     2214   2711   2577    341    488    114       C  
ATOM   1772  O   TYR A 268      -5.329 -49.468  -7.687  1.00 20.98           O  
ANISOU 1772  O   TYR A 268     2321   2887   2765    352    426    106       O  
ATOM   1773  CB  TYR A 268      -3.112 -47.938  -8.699  1.00 18.70           C  
ANISOU 1773  CB  TYR A 268     2114   2589   2404    331    495     64       C  
ATOM   1774  CG  TYR A 268      -2.561 -47.129  -9.856  1.00 18.27           C  
ANISOU 1774  CG  TYR A 268     2101   2527   2315    353    533     49       C  
ATOM   1775  CD1 TYR A 268      -1.797 -45.982  -9.632  1.00 19.10           C  
ANISOU 1775  CD1 TYR A 268     2260   2610   2386    325    604     36       C  
ATOM   1776  CD2 TYR A 268      -2.840 -47.483 -11.167  1.00 18.78           C  
ANISOU 1776  CD2 TYR A 268     2155   2601   2378    401    501     46       C  
ATOM   1777  CE1 TYR A 268      -1.280 -45.241 -10.697  1.00 19.43           C  
ANISOU 1777  CE1 TYR A 268     2348   2639   2396    343    649     21       C  
ATOM   1778  CE2 TYR A 268      -2.320 -46.762 -12.239  1.00 19.50           C  
ANISOU 1778  CE2 TYR A 268     2295   2679   2435    424    541     33       C  
ATOM   1779  CZ  TYR A 268      -1.570 -45.622 -11.994  1.00 19.91           C  
ANISOU 1779  CZ  TYR A 268     2404   2707   2455    396    619     22       C  
ATOM   1780  OH  TYR A 268      -1.070 -44.912 -13.064  1.00 20.64           O  
ANISOU 1780  OH  TYR A 268     2552   2780   2512    417    667      8       O  
ATOM   1781  N   SER A 269      -5.511 -47.940  -6.013  1.00 19.88           N  
ANISOU 1781  N   SER A 269     2251   2708   2594    316    525    133       N  
ATOM   1782  CA  SER A 269      -6.172 -48.899  -5.131  1.00 20.01           C  
ANISOU 1782  CA  SER A 269     2233   2722   2648    302    495    144       C  
ATOM   1783  C   SER A 269      -7.456 -49.467  -5.722  1.00 20.41           C  
ANISOU 1783  C   SER A 269     2234   2784   2737    346    466    157       C  
ATOM   1784  O   SER A 269      -7.659 -50.685  -5.637  1.00 20.19           O  
ANISOU 1784  O   SER A 269     2160   2765   2745    338    415    150       O  
ATOM   1785  CB  SER A 269      -6.444 -48.269  -3.781  1.00 20.85           C  
ANISOU 1785  CB  SER A 269     2380   2799   2744    274    549    164       C  
ATOM   1786  OG  SER A 269      -5.249 -47.933  -3.099  1.00 23.39           O  
ANISOU 1786  OG  SER A 269     2740   3113   3034    227    564    146       O  
ATOM   1787  N   THR A 270      -8.314 -48.623  -6.330  1.00 20.76           N  
ANISOU 1787  N   THR A 270     2286   2828   2775    393    496    174       N  
ATOM   1788  CA  THR A 270      -9.552 -49.144  -6.912  1.00 21.57           C  
ANISOU 1788  CA  THR A 270     2333   2945   2917    437    463    181       C  
ATOM   1789  C   THR A 270      -9.267 -50.053  -8.099  1.00 21.45           C  
ANISOU 1789  C   THR A 270     2279   2960   2913    456    393    156       C  
ATOM   1790  O   THR A 270      -9.779 -51.159  -8.128  1.00 21.98           O  
ANISOU 1790  O   THR A 270     2291   3038   3022    454    346    148       O  
ATOM   1791  CB  THR A 270     -10.543 -48.017  -7.235  1.00 24.72           C  
ANISOU 1791  CB  THR A 270     2748   3338   3305    488    507    204       C  
ATOM   1792  CG2 THR A 270     -11.823 -48.532  -7.854  1.00 26.79           C  
ANISOU 1792  CG2 THR A 270     2945   3621   3611    536    467    205       C  
ATOM   1793  OG1 THR A 270     -10.917 -47.420  -6.010  1.00 26.09           O  
ANISOU 1793  OG1 THR A 270     2950   3483   3480    465    569    227       O  
ATOM   1794  N   PHE A 271      -8.419 -49.630  -9.050  1.00 20.73           N  
ANISOU 1794  N   PHE A 271     2218   2876   2783    471    391    142       N  
ATOM   1795  CA  PHE A 271      -8.114 -50.477 -10.209  1.00 20.54           C  
ANISOU 1795  CA  PHE A 271     2165   2875   2765    490    329    119       C  
ATOM   1796  C   PHE A 271      -7.472 -51.806  -9.772  1.00 19.76           C  
ANISOU 1796  C   PHE A 271     2032   2783   2694    444    282    101       C  
ATOM   1797  O   PHE A 271      -7.796 -52.855 -10.322  1.00 20.45           O  
ANISOU 1797  O   PHE A 271     2073   2887   2811    455    226     88       O  
ATOM   1798  CB  PHE A 271      -7.156 -49.741 -11.162  1.00 20.97           C  
ANISOU 1798  CB  PHE A 271     2271   2927   2770    507    349    107       C  
ATOM   1799  CG  PHE A 271      -7.800 -48.531 -11.792  1.00 22.30           C  
ANISOU 1799  CG  PHE A 271     2479   3087   2905    563    390    125       C  
ATOM   1800  CD1 PHE A 271      -8.931 -48.663 -12.576  1.00 23.75           C  
ANISOU 1800  CD1 PHE A 271     2634   3288   3100    624    354    131       C  
ATOM   1801  CD2 PHE A 271      -7.264 -47.268 -11.605  1.00 23.85           C  
ANISOU 1801  CD2 PHE A 271     2745   3260   3057    558    464    132       C  
ATOM   1802  CE1 PHE A 271      -9.512 -47.547 -13.182  1.00 24.97           C  
ANISOU 1802  CE1 PHE A 271     2831   3436   3220    685    388    147       C  
ATOM   1803  CE2 PHE A 271      -7.858 -46.150 -12.192  1.00 24.86           C  
ANISOU 1803  CE2 PHE A 271     2919   3376   3149    615    505    150       C  
ATOM   1804  CZ  PHE A 271      -8.979 -46.303 -12.969  1.00 24.79           C  
ANISOU 1804  CZ  PHE A 271     2883   3386   3151    682    466    159       C  
ATOM   1805  N   ALA A 272      -6.577 -51.735  -8.768  1.00 18.39           N  
ANISOU 1805  N   ALA A 272     1884   2595   2509    395    306     98       N  
ATOM   1806  CA  ALA A 272      -5.897 -52.946  -8.327  1.00 18.62           C  
ANISOU 1806  CA  ALA A 272     1888   2628   2559    358    262     82       C  
ATOM   1807  C   ALA A 272      -6.847 -53.894  -7.603  1.00 19.35           C  
ANISOU 1807  C   ALA A 272     1942   2715   2695    349    241     92       C  
ATOM   1808  O   ALA A 272      -6.761 -55.110  -7.794  1.00 19.39           O  
ANISOU 1808  O   ALA A 272     1912   2729   2725    342    192     78       O  
ATOM   1809  CB  ALA A 272      -4.717 -52.595  -7.411  1.00 18.76           C  
ANISOU 1809  CB  ALA A 272     1943   2635   2552    314    288     74       C  
ATOM   1810  N   CYS A 273      -7.703 -53.363  -6.737  1.00 19.59           N  
ANISOU 1810  N   CYS A 273     1982   2727   2733    346    284    114       N  
ATOM   1811  CA  CYS A 273      -8.500 -54.217  -5.832  1.00 19.18           C  
ANISOU 1811  CA  CYS A 273     1905   2660   2723    327    280    123       C  
ATOM   1812  C   CYS A 273      -9.915 -54.526  -6.288  1.00 19.85           C  
ANISOU 1812  C   CYS A 273     1937   2752   2851    357    269    126       C  
ATOM   1813  O   CYS A 273     -10.545 -55.444  -5.731  1.00 19.79           O  
ANISOU 1813  O   CYS A 273     1899   2733   2885    339    261    125       O  
ATOM   1814  CB  CYS A 273      -8.507 -53.606  -4.432  1.00 18.45           C  
ANISOU 1814  CB  CYS A 273     1857   2537   2616    297    335    143       C  
ATOM   1815  SG  CYS A 273      -6.865 -53.474  -3.699  1.00 21.37           S  
ANISOU 1815  SG  CYS A 273     2279   2900   2941    256    335    130       S  
ATOM   1816  N   GLU A 274     -10.428 -53.804  -7.299  1.00 20.24           N  
ANISOU 1816  N   GLU A 274     1976   2820   2894    403    269    128       N  
ATOM   1817  CA  GLU A 274     -11.816 -53.990  -7.691  1.00 20.42           C  
ANISOU 1817  CA  GLU A 274     1945   2854   2961    435    258    128       C  
ATOM   1818  C   GLU A 274     -12.111 -55.274  -8.434  1.00 22.13           C  
ANISOU 1818  C   GLU A 274     2102   3091   3214    439    193    102       C  
ATOM   1819  O   GLU A 274     -11.299 -55.741  -9.221  1.00 22.09           O  
ANISOU 1819  O   GLU A 274     2100   3102   3190    441    150     84       O  
ATOM   1820  CB  GLU A 274     -12.307 -52.797  -8.549  1.00 21.34           C  
ANISOU 1820  CB  GLU A 274     2070   2984   3053    493    273    138       C  
ATOM   1821  CG  GLU A 274     -11.699 -52.779  -9.953  1.00 21.43           C  
ANISOU 1821  CG  GLU A 274     2090   3020   3031    527    229    121       C  
ATOM   1822  CD  GLU A 274     -12.063 -51.556 -10.781  1.00 28.39           C  
ANISOU 1822  CD  GLU A 274     3000   3909   3878    588    249    132       C  
ATOM   1823  OE1 GLU A 274     -11.463 -51.377 -11.869  1.00 27.85           O  
ANISOU 1823  OE1 GLU A 274     2958   3852   3772    616    226    121       O  
ATOM   1824  OE2 GLU A 274     -12.949 -50.781 -10.343  1.00 30.72           O1-
ANISOU 1824  OE2 GLU A 274     3295   4195   4181    610    290    153       O1-
ATOM   1825  N   ASN A 275     -13.354 -55.753  -8.286  1.00 22.47           N  
ANISOU 1825  N   ASN A 275     2089   3136   3313    444    188     97       N  
ATOM   1826  CA  ASN A 275     -13.890 -56.795  -9.125  1.00 24.22           C  
ANISOU 1826  CA  ASN A 275     2248   3381   3574    454    130     68       C  
ATOM   1827  C   ASN A 275     -14.201 -56.079 -10.451  1.00 25.35           C  
ANISOU 1827  C   ASN A 275     2381   3556   3695    517     99     62       C  
ATOM   1828  O   ASN A 275     -14.919 -55.072 -10.440  1.00 26.10           O  
ANISOU 1828  O   ASN A 275     2476   3653   3787    554    129     78       O  
ATOM   1829  CB  ASN A 275     -15.176 -57.362  -8.523  1.00 25.86           C  
ANISOU 1829  CB  ASN A 275     2397   3578   3850    439    144     61       C  
ATOM   1830  CG  ASN A 275     -15.747 -58.531  -9.297  1.00 28.46           C  
ANISOU 1830  CG  ASN A 275     2658   3929   4225    440     86     25       C  
ATOM   1831  ND2 ASN A 275     -16.414 -59.455  -8.602  1.00 29.23           N  
ANISOU 1831  ND2 ASN A 275     2717   4008   4381    402    101     12       N  
ATOM   1832  OD1 ASN A 275     -15.603 -58.630 -10.518  1.00 29.24           O  
ANISOU 1832  OD1 ASN A 275     2742   4060   4308    473     31      7       O  
ATOM   1833  N   PRO A 276     -13.628 -56.525 -11.576  1.00 25.36           N  
ANISOU 1833  N   PRO A 276     2382   3579   3674    533     44     42       N  
ATOM   1834  CA  PRO A 276     -13.895 -55.837 -12.852  1.00 27.45           C  
ANISOU 1834  CA  PRO A 276     2651   3870   3910    598     16     37       C  
ATOM   1835  C   PRO A 276     -15.365 -55.861 -13.252  1.00 29.85           C  
ANISOU 1835  C   PRO A 276     2887   4198   4258    638    -11     24       C  
ATOM   1836  O   PRO A 276     -15.732 -55.080 -14.114  1.00 31.30           O  
ANISOU 1836  O   PRO A 276     3079   4399   4414    700    -27     26       O  
ATOM   1837  CB  PRO A 276     -13.070 -56.640 -13.871  1.00 27.89           C  
ANISOU 1837  CB  PRO A 276     2713   3939   3944    597    -40     13       C  
ATOM   1838  CG  PRO A 276     -12.070 -57.382 -13.084  1.00 27.43           C  
ANISOU 1838  CG  PRO A 276     2674   3860   3888    537    -27     14       C  
ATOM   1839  CD  PRO A 276     -12.700 -57.659 -11.748  1.00 24.66           C  
ANISOU 1839  CD  PRO A 276     2298   3489   3583    498      9     24       C  
ATOM   1840  N   ASN A 277     -16.187 -56.799 -12.707  1.00 31.54           N  
ANISOU 1840  N   ASN A 277     3034   4411   4540    605    -20      7       N  
ATOM   1841  CA  ASN A 277     -17.614 -56.965 -13.061  1.00 33.72           C  
ANISOU 1841  CA  ASN A 277     3229   4712   4871    636    -49    -15       C  
ATOM   1842  C   ASN A 277     -17.738 -57.101 -14.579  1.00 35.05           C  
ANISOU 1842  C   ASN A 277     3381   4918   5018    690   -126    -41       C  
ATOM   1843  O   ASN A 277     -18.450 -56.344 -15.235  1.00 35.24           O  
ANISOU 1843  O   ASN A 277     3391   4966   5033    755   -145    -42       O  
ATOM   1844  CB  ASN A 277     -18.456 -55.795 -12.526  1.00 36.07           C  
ANISOU 1844  CB  ASN A 277     3523   5004   5179    669      2      9       C  
ATOM   1845  CG  ASN A 277     -18.479 -55.762 -11.026  1.00 41.25           C  
ANISOU 1845  CG  ASN A 277     4193   5621   5861    615     76     32       C  
ATOM   1846  ND2 ASN A 277     -18.509 -54.565 -10.457  1.00 42.56           N  
ANISOU 1846  ND2 ASN A 277     4403   5768   6000    633    137     66       N  
ATOM   1847  OD1 ASN A 277     -18.470 -56.805 -10.364  1.00 42.60           O  
ANISOU 1847  OD1 ASN A 277     4341   5773   6073    558     82     19       O  
ATOM   1848  N   SER A 278     -16.918 -57.978 -15.143  1.00 34.77           N  
ANISOU 1848  N   SER A 278     3361   4885   4964    667   -166    -59       N  
ATOM   1849  CA  SER A 278     -16.800 -58.119 -16.586  1.00 34.81           C  
ANISOU 1849  CA  SER A 278     3371   4919   4937    714   -234    -82       C  
ATOM   1850  C   SER A 278     -17.178 -59.504 -17.057  1.00 34.87           C  
ANISOU 1850  C   SER A 278     3315   4943   4989    688   -295   -124       C  
ATOM   1851  O   SER A 278     -16.873 -60.489 -16.383  1.00 34.86           O  
ANISOU 1851  O   SER A 278     3302   4922   5022    625   -280   -132       O  
ATOM   1852  CB  SER A 278     -15.360 -57.812 -16.993  1.00 35.78           C  
ANISOU 1852  CB  SER A 278     3580   5026   4989    714   -223    -65       C  
ATOM   1853  OG  SER A 278     -15.006 -58.211 -18.310  1.00 38.21           O  
ANISOU 1853  OG  SER A 278     3904   5351   5264    743   -283    -88       O  
ATOM   1854  N   THR A 279     -17.808 -59.588 -18.244  1.00 34.87           N  
ANISOU 1854  N   THR A 279     3283   4978   4987    740   -363   -154       N  
ATOM   1855  CA  THR A 279     -18.135 -60.874 -18.858  1.00 35.27           C  
ANISOU 1855  CA  THR A 279     3280   5047   5074    718   -426   -199       C  
ATOM   1856  C   THR A 279     -16.855 -61.631 -19.264  1.00 33.50           C  
ANISOU 1856  C   THR A 279     3111   4805   4811    686   -439   -201       C  
ATOM   1857  O   THR A 279     -16.922 -62.834 -19.497  1.00 34.35           O  
ANISOU 1857  O   THR A 279     3185   4917   4951    650   -473   -233       O  
ATOM   1858  CB  THR A 279     -19.044 -60.674 -20.083  1.00 37.85           C  
ANISOU 1858  CB  THR A 279     3568   5418   5397    787   -502   -231       C  
ATOM   1859  CG2 THR A 279     -20.346 -59.991 -19.726  1.00 38.82           C  
ANISOU 1859  CG2 THR A 279     3625   5561   5564    823   -495   -234       C  
ATOM   1860  OG1 THR A 279     -18.336 -59.893 -21.053  1.00 40.04           O  
ANISOU 1860  OG1 THR A 279     3927   5697   5590    847   -520   -214       O  
ATOM   1861  N   ARG A 280     -15.697 -60.941 -19.340  1.00 31.09           N  
ANISOU 1861  N   ARG A 280     2890   4482   4441    698   -407   -169       N  
ATOM   1862  CA  ARG A 280     -14.430 -61.589 -19.659  1.00 29.72           C  
ANISOU 1862  CA  ARG A 280     2767   4290   4234    669   -412   -170       C  
ATOM   1863  C   ARG A 280     -13.845 -62.337 -18.442  1.00 27.42           C  
ANISOU 1863  C   ARG A 280     2474   3970   3975    596   -368   -160       C  
ATOM   1864  O   ARG A 280     -12.844 -63.021 -18.607  1.00 26.52           O  
ANISOU 1864  O   ARG A 280     2391   3841   3842    570   -373   -163       O  
ATOM   1865  CB  ARG A 280     -13.410 -60.558 -20.154  1.00 31.87           C  
ANISOU 1865  CB  ARG A 280     3125   4551   4432    706   -388   -144       C  
ATOM   1866  CG  ARG A 280     -13.925 -59.725 -21.353  1.00 36.61           C  
ANISOU 1866  CG  ARG A 280     3748   5174   4990    786   -425   -149       C  
ATOM   1867  CD  ARG A 280     -13.037 -58.520 -21.598  1.00 41.43           C  
ANISOU 1867  CD  ARG A 280     4448   5765   5531    820   -378   -120       C  
ATOM   1868  NE  ARG A 280     -13.484 -57.709 -22.737  1.00 45.76           N  
ANISOU 1868  NE  ARG A 280     5031   6327   6029    902   -408   -122       N  
ATOM   1869  CZ  ARG A 280     -12.946 -57.761 -23.953  1.00 48.62           C  
ANISOU 1869  CZ  ARG A 280     5450   6685   6338    937   -438   -134       C  
ATOM   1870  NH1 ARG A 280     -11.928 -58.577 -24.203  1.00 48.08           N1+
ANISOU 1870  NH1 ARG A 280     5405   6601   6263    895   -440   -145       N1+
ATOM   1871  NH2 ARG A 280     -13.421 -56.995 -24.929  1.00 49.13           N  
ANISOU 1871  NH2 ARG A 280     5553   6760   6353   1018   -465   -135       N  
ATOM   1872  N   VAL A 281     -14.432 -62.180 -17.240  1.00 26.72           N  
ANISOU 1872  N   VAL A 281     2354   3869   3928    569   -323   -146       N  
ATOM   1873  CA  VAL A 281     -13.963 -62.799 -16.002  1.00 26.01           C  
ANISOU 1873  CA  VAL A 281     2272   3748   3863    507   -278   -134       C  
ATOM   1874  C   VAL A 281     -14.978 -63.818 -15.503  1.00 25.88           C  
ANISOU 1874  C   VAL A 281     2187   3728   3918    469   -282   -160       C  
ATOM   1875  O   VAL A 281     -16.153 -63.479 -15.300  1.00 26.49           O  
ANISOU 1875  O   VAL A 281     2212   3817   4036    482   -275   -168       O  
ATOM   1876  CB  VAL A 281     -13.716 -61.700 -14.940  1.00 26.54           C  
ANISOU 1876  CB  VAL A 281     2376   3796   3912    504   -213    -96       C  
ATOM   1877  CG1 VAL A 281     -13.301 -62.300 -13.598  1.00 26.89           C  
ANISOU 1877  CG1 VAL A 281     2433   3806   3977    446   -169    -83       C  
ATOM   1878  CG2 VAL A 281     -12.664 -60.717 -15.432  1.00 26.02           C  
ANISOU 1878  CG2 VAL A 281     2379   3730   3778    535   -202    -76       C  
ATOM   1879  N   SER A 282     -14.546 -65.067 -15.329  1.00 24.88           N  
ANISOU 1879  N   SER A 282     2061   3585   3809    424   -289   -175       N  
ATOM   1880  CA  SER A 282     -15.431 -66.117 -14.836  1.00 25.05           C  
ANISOU 1880  CA  SER A 282     2026   3594   3896    382   -283   -202       C  
ATOM   1881  C   SER A 282     -15.366 -66.310 -13.316  1.00 25.61           C  
ANISOU 1881  C   SER A 282     2116   3625   3991    336   -215   -180       C  
ATOM   1882  O   SER A 282     -16.257 -66.937 -12.754  1.00 26.63           O  
ANISOU 1882  O   SER A 282     2201   3738   4178    303   -192   -199       O  
ATOM   1883  CB  SER A 282     -15.135 -67.437 -15.539  1.00 25.72           C  
ANISOU 1883  CB  SER A 282     2104   3680   3988    360   -325   -235       C  
ATOM   1884  OG  SER A 282     -13.739 -67.690 -15.573  1.00 26.35           O  
ANISOU 1884  OG  SER A 282     2249   3743   4018    353   -324   -216       O  
ATOM   1885  N   ASP A 283     -14.314 -65.794 -12.646  1.00 24.05           N  
ANISOU 1885  N   ASP A 283     1984   3407   3747    333   -181   -144       N  
ATOM   1886  CA  ASP A 283     -14.195 -65.945 -11.194  1.00 23.57           C  
ANISOU 1886  CA  ASP A 283     1952   3305   3698    295   -121   -122       C  
ATOM   1887  C   ASP A 283     -13.265 -64.845 -10.701  1.00 23.10           C  
ANISOU 1887  C   ASP A 283     1953   3239   3583    310    -94    -84       C  
ATOM   1888  O   ASP A 283     -12.219 -64.589 -11.297  1.00 23.05           O  
ANISOU 1888  O   ASP A 283     1982   3247   3529    328   -119    -78       O  
ATOM   1889  CB  ASP A 283     -13.617 -67.342 -10.848  1.00 25.08           C  
ANISOU 1889  CB  ASP A 283     2164   3468   3896    254   -122   -133       C  
ATOM   1890  CG  ASP A 283     -13.707 -67.793  -9.395  1.00 30.55           C  
ANISOU 1890  CG  ASP A 283     2886   4114   4609    214    -62   -118       C  
ATOM   1891  OD1 ASP A 283     -13.895 -66.941  -8.520  1.00 31.57           O  
ANISOU 1891  OD1 ASP A 283     3035   4229   4733    215    -18    -93       O  
ATOM   1892  OD2 ASP A 283     -13.555 -69.006  -9.141  1.00 32.82           O1-
ANISOU 1892  OD2 ASP A 283     3184   4375   4912    184    -58   -132       O1-
ATOM   1893  N   PHE A 284     -13.668 -64.170  -9.633  1.00 21.78           N  
ANISOU 1893  N   PHE A 284     1798   3052   3425    301    -39    -61       N  
ATOM   1894  CA  PHE A 284     -12.877 -63.103  -9.061  1.00 21.39           C  
ANISOU 1894  CA  PHE A 284     1807   2994   3326    309     -8    -28       C  
ATOM   1895  C   PHE A 284     -12.881 -63.247  -7.555  1.00 21.04           C  
ANISOU 1895  C   PHE A 284     1797   2907   3290    273     48     -9       C  
ATOM   1896  O   PHE A 284     -13.948 -63.373  -6.942  1.00 21.46           O  
ANISOU 1896  O   PHE A 284     1823   2941   3390    258     84    -11       O  
ATOM   1897  CB  PHE A 284     -13.431 -61.718  -9.463  1.00 21.19           C  
ANISOU 1897  CB  PHE A 284     1771   2990   3290    350      4    -16       C  
ATOM   1898  CG  PHE A 284     -12.666 -60.604  -8.788  1.00 21.32           C  
ANISOU 1898  CG  PHE A 284     1850   2993   3257    352     45     16       C  
ATOM   1899  CD1 PHE A 284     -11.480 -60.129  -9.327  1.00 21.41           C  
ANISOU 1899  CD1 PHE A 284     1903   3017   3214    366     29     20       C  
ATOM   1900  CD2 PHE A 284     -13.082 -60.093  -7.567  1.00 21.70           C  
ANISOU 1900  CD2 PHE A 284     1918   3013   3315    334    105     38       C  
ATOM   1901  CE1 PHE A 284     -10.759 -59.133  -8.689  1.00 21.07           C  
ANISOU 1901  CE1 PHE A 284     1914   2961   3129    362     70     43       C  
ATOM   1902  CE2 PHE A 284     -12.345 -59.093  -6.923  1.00 21.86           C  
ANISOU 1902  CE2 PHE A 284     1998   3019   3288    332    143     64       C  
ATOM   1903  CZ  PHE A 284     -11.186 -58.633  -7.482  1.00 21.24           C  
ANISOU 1903  CZ  PHE A 284     1956   2957   3159    344    124     65       C  
ATOM   1904  N   ARG A 285     -11.704 -63.201  -6.950  1.00 19.65           N  
ANISOU 1904  N   ARG A 285     1680   2716   3070    260     56      7       N  
ATOM   1905  CA  ARG A 285     -11.592 -63.233  -5.487  1.00 19.49           C  
ANISOU 1905  CA  ARG A 285     1707   2654   3045    231    106     28       C  
ATOM   1906  C   ARG A 285     -10.461 -62.296  -5.081  1.00 20.08           C  
ANISOU 1906  C   ARG A 285     1838   2730   3060    236    115     48       C  
ATOM   1907  O   ARG A 285      -9.470 -62.197  -5.794  1.00 20.22           O  
ANISOU 1907  O   ARG A 285     1865   2773   3046    249     78     41       O  
ATOM   1908  CB  ARG A 285     -11.233 -64.652  -4.990  1.00 19.57           C  
ANISOU 1908  CB  ARG A 285     1736   2636   3064    202     98     17       C  
ATOM   1909  CG  ARG A 285     -12.175 -65.707  -5.557  1.00 22.50           C  
ANISOU 1909  CG  ARG A 285     2050   3006   3491    192     84    -11       C  
ATOM   1910  CD  ARG A 285     -11.840 -67.130  -5.168  1.00 25.56           C  
ANISOU 1910  CD  ARG A 285     2462   3364   3887    166     81    -22       C  
ATOM   1911  NE  ARG A 285     -12.625 -68.041  -6.008  1.00 27.53           N  
ANISOU 1911  NE  ARG A 285     2652   3622   4185    158     59    -55       N  
ATOM   1912  CZ  ARG A 285     -13.008 -69.267  -5.649  1.00 29.75           C  
ANISOU 1912  CZ  ARG A 285     2934   3869   4499    128     78    -72       C  
ATOM   1913  NH1 ARG A 285     -12.695 -69.743  -4.451  1.00 28.82           N1+
ANISOU 1913  NH1 ARG A 285     2879   3702   4367    108    120    -56       N1+
ATOM   1914  NH2 ARG A 285     -13.733 -70.008  -6.475  1.00 29.83           N  
ANISOU 1914  NH2 ARG A 285     2887   3892   4556    118     58   -107       N  
ATOM   1915  N   THR A 286     -10.567 -61.638  -3.913  1.00 19.43           N  
ANISOU 1915  N   THR A 286     1797   2619   2965    222    166     71       N  
ATOM   1916  CA  THR A 286      -9.440 -60.822  -3.440  1.00 18.13           C  
ANISOU 1916  CA  THR A 286     1688   2455   2745    221    174     85       C  
ATOM   1917  C   THR A 286      -9.447 -60.762  -1.923  1.00 18.42           C  
ANISOU 1917  C   THR A 286     1780   2448   2769    195    219    104       C  
ATOM   1918  O   THR A 286     -10.506 -60.934  -1.313  1.00 19.05           O  
ANISOU 1918  O   THR A 286     1856   2499   2884    184    261    112       O  
ATOM   1919  CB  THR A 286      -9.474 -59.422  -4.108  1.00 19.18           C  
ANISOU 1919  CB  THR A 286     1817   2614   2857    246    186     92       C  
ATOM   1920  CG2 THR A 286     -10.496 -58.499  -3.465  1.00 19.63           C  
ANISOU 1920  CG2 THR A 286     1881   2652   2928    249    245    114       C  
ATOM   1921  OG1 THR A 286      -8.180 -58.811  -4.044  1.00 19.99           O  
ANISOU 1921  OG1 THR A 286     1960   2725   2909    244    180     93       O  
ATOM   1922  N   ALA A 287      -8.286 -60.551  -1.318  1.00 17.68           N  
ANISOU 1922  N   ALA A 287     1739   2351   2629    186    212    108       N  
ATOM   1923  CA  ALA A 287      -8.197 -60.421   0.141  1.00 18.83           C  
ANISOU 1923  CA  ALA A 287     1947   2456   2751    165    251    126       C  
ATOM   1924  C   ALA A 287      -7.214 -59.330   0.515  1.00 20.05           C  
ANISOU 1924  C   ALA A 287     2145   2620   2854    162    256    131       C  
ATOM   1925  O   ALA A 287      -6.191 -59.159  -0.157  1.00 19.98           O  
ANISOU 1925  O   ALA A 287     2125   2644   2822    170    217    114       O  
ATOM   1926  CB  ALA A 287      -7.782 -61.741   0.788  1.00 18.25           C  
ANISOU 1926  CB  ALA A 287     1904   2357   2675    154    229    120       C  
ATOM   1927  N   ASN A 288      -7.501 -58.578   1.624  1.00 19.35           N  
ANISOU 1927  N   ASN A 288     2107   2499   2745    147    308    151       N  
ATOM   1928  CA  ASN A 288      -6.624 -57.502   2.108  1.00 19.46           C  
ANISOU 1928  CA  ASN A 288     2167   2518   2709    138    319    153       C  
ATOM   1929  C   ASN A 288      -6.314 -56.519   0.976  1.00 19.66           C  
ANISOU 1929  C   ASN A 288     2160   2583   2727    153    315    144       C  
ATOM   1930  O   ASN A 288      -5.157 -56.234   0.686  1.00 20.90           O  
ANISOU 1930  O   ASN A 288     2322   2764   2854    150    287    126       O  
ATOM   1931  CB  ASN A 288      -5.319 -58.057   2.696  1.00 21.00           C  
ANISOU 1931  CB  ASN A 288     2398   2715   2865    129    274    138       C  
ATOM   1932  CG  ASN A 288      -5.499 -58.973   3.857  1.00 25.67           C  
ANISOU 1932  CG  ASN A 288     3039   3264   3452    120    279    147       C  
ATOM   1933  ND2 ASN A 288      -4.853 -60.153   3.815  1.00 25.87           N  
ANISOU 1933  ND2 ASN A 288     3062   3293   3473    128    227    133       N  
ATOM   1934  OD1 ASN A 288      -6.202 -58.622   4.810  1.00 28.82           O  
ANISOU 1934  OD1 ASN A 288     3483   3622   3846    108    332    168       O  
ATOM   1935  N   CYS A 289      -7.353 -56.083   0.288  1.00 18.53           N  
ANISOU 1935  N   CYS A 289     1981   2445   2614    171    341    154       N  
ATOM   1936  CA  CYS A 289      -7.194 -55.222  -0.892  1.00 19.70           C  
ANISOU 1936  CA  CYS A 289     2104   2627   2755    193    338    147       C  
ATOM   1937  C   CYS A 289      -8.273 -54.223  -0.841  1.00 20.57           C  
ANISOU 1937  C   CYS A 289     2217   2724   2874    207    395    169       C  
ATOM   1938  O   CYS A 289      -9.357 -54.434  -1.393  1.00 20.87           O  
ANISOU 1938  O   CYS A 289     2211   2767   2953    230    396    173       O  
ATOM   1939  CB  CYS A 289      -7.274 -56.056  -2.172  1.00 21.23           C  
ANISOU 1939  CB  CYS A 289     2239   2851   2978    216    286    129       C  
ATOM   1940  SG  CYS A 289      -6.283 -55.411  -3.551  1.00 24.40           S  
ANISOU 1940  SG  CYS A 289     2630   3290   3350    236    261    109       S  
ATOM   1941  N   SER A 290      -7.993 -53.090  -0.189  1.00 19.74           N  
ANISOU 1941  N   SER A 290     2165   2603   2732    194    443    181       N  
ATOM   1942  CA  SER A 290      -8.990 -52.050  -0.050  1.00 21.10           C  
ANISOU 1942  CA  SER A 290     2348   2758   2909    209    505    205       C  
ATOM   1943  C   SER A 290      -9.104 -51.160  -1.266  1.00 21.23           C  
ANISOU 1943  C   SER A 290     2348   2802   2917    245    511    204       C  
ATOM   1944  O   SER A 290      -8.084 -50.839  -1.868  1.00 21.35           O  
ANISOU 1944  O   SER A 290     2375   2837   2901    245    493    187       O  
ATOM   1945  CB  SER A 290      -8.641 -51.197   1.172  1.00 23.57           C  
ANISOU 1945  CB  SER A 290     2734   3040   3183    179    558    219       C  
ATOM   1946  OG  SER A 290      -9.566 -50.135   1.328  1.00 26.36           O  
ANISOU 1946  OG  SER A 290     3105   3374   3538    194    624    244       O  
ATOM   1947  N   LEU A 291     -10.312 -50.725  -1.627  1.00 20.10           N  
ANISOU 1947  N   LEU A 291     2180   2656   2800    279    539    220       N  
ATOM   1948  CA  LEU A 291     -10.494 -49.758  -2.703  1.00 21.81           C  
ANISOU 1948  CA  LEU A 291     2393   2892   3000    322    552    223       C  
ATOM   1949  C   LEU A 291      -9.979 -48.383  -2.236  1.00 24.57           C  
ANISOU 1949  C   LEU A 291     2815   3223   3299    310    616    236       C  
ATOM   1950  O   LEU A 291      -9.789 -48.172  -1.039  1.00 25.63           O  
ANISOU 1950  O   LEU A 291     2991   3327   3419    273    652    246       O  
ATOM   1951  CB  LEU A 291     -11.980 -49.639  -3.094  1.00 21.28           C  
ANISOU 1951  CB  LEU A 291     2280   2828   2975    365    564    237       C  
ATOM   1952  CG  LEU A 291     -12.651 -50.960  -3.530  1.00 21.80           C  
ANISOU 1952  CG  LEU A 291     2271   2913   3098    374    507    221       C  
ATOM   1953  CD1 LEU A 291     -14.107 -50.719  -3.829  1.00 22.16           C  
ANISOU 1953  CD1 LEU A 291     2268   2963   3188    415    522    230       C  
ATOM   1954  CD2 LEU A 291     -11.936 -51.552  -4.771  1.00 22.91           C  
ANISOU 1954  CD2 LEU A 291     2386   3089   3229    389    437    194       C  
ATOM   1955  N   GLU A 292      -9.801 -47.458  -3.198  1.00 26.88           N  
ANISOU 1955  N   GLU A 292     3124   3528   3562    343    632    235       N  
ATOM   1956  CA  GLU A 292      -9.311 -46.102  -2.937  1.00 32.08           C  
ANISOU 1956  CA  GLU A 292     3852   4167   4170    335    698    244       C  
ATOM   1957  C   GLU A 292     -10.267 -45.380  -2.018  1.00 36.53           C  
ANISOU 1957  C   GLU A 292     4445   4698   4738    337    765    275       C  
ATOM   1958  O   GLU A 292     -11.459 -45.300  -2.334  1.00 37.72           O  
ANISOU 1958  O   GLU A 292     4562   4850   4919    381    774    293       O  
ATOM   1959  CB  GLU A 292      -9.163 -45.301  -4.242  1.00 34.27           C  
ANISOU 1959  CB  GLU A 292     4144   4459   4419    380    709    240       C  
ATOM   1960  CG  GLU A 292      -8.397 -43.999  -4.028  1.00 39.55           C  
ANISOU 1960  CG  GLU A 292     4889   5105   5032    361    778    240       C  
ATOM   1961  CD  GLU A 292      -8.123 -43.158  -5.265  1.00 47.34           C  
ANISOU 1961  CD  GLU A 292     5907   6096   5982    402    801    234       C  
ATOM   1962  OE1 GLU A 292      -8.817 -43.353  -6.290  1.00 46.65           O  
ANISOU 1962  OE1 GLU A 292     5789   6027   5908    461    770    239       O  
ATOM   1963  OE2 GLU A 292      -7.214 -42.295  -5.202  1.00 50.35           O1-
ANISOU 1963  OE2 GLU A 292     6348   6462   6322    375    851    222       O1-
ATOM   1964  N   HIS A 293      -9.768 -44.871  -0.879  1.00 38.63           N  
ANISOU 1964  N   HIS A 293     4768   4934   4975    291    812    280       N  
ATOM   1965  CA  HIS A 293     -10.644 -44.178   0.066  1.00 41.46           C  
ANISOU 1965  CA  HIS A 293     5162   5255   5335    290    882    311       C  
ATOM   1966  C   HIS A 293     -10.798 -42.755  -0.431  1.00 43.23           C  
ANISOU 1966  C   HIS A 293     5433   5470   5523    323    947    326       C  
ATOM   1967  O   HIS A 293      -9.782 -42.103  -0.688  1.00 44.21           O  
ANISOU 1967  O   HIS A 293     5602   5595   5600    305    964    311       O  
ATOM   1968  CB  HIS A 293     -10.034 -44.129   1.481  1.00 43.23           C  
ANISOU 1968  CB  HIS A 293     5442   5447   5534    229    909    311       C  
ATOM   1969  CG  HIS A 293      -9.630 -45.444   2.081  1.00 45.07           C  
ANISOU 1969  CG  HIS A 293     5653   5685   5788    195    850    295       C  
ATOM   1970  CD2 HIS A 293      -9.398 -46.643   1.494  1.00 46.02           C  
ANISOU 1970  CD2 HIS A 293     5713   5835   5936    201    775    275       C  
ATOM   1971  ND1 HIS A 293      -9.363 -45.555   3.435  1.00 46.58           N  
ANISOU 1971  ND1 HIS A 293     5893   5843   5961    151    870    299       N  
ATOM   1972  CE1 HIS A 293      -9.002 -46.813   3.631  1.00 47.12           C  
ANISOU 1972  CE1 HIS A 293     5933   5922   6048    136    806    283       C  
ATOM   1973  NE2 HIS A 293      -9.010 -47.507   2.492  1.00 47.13           N  
ANISOU 1973  NE2 HIS A 293     5867   5961   6079    164    750    268       N  
TER    1974      HIS A 293 
HETATM 1975  O1  SO4 A 301       6.148 -68.717 -27.739  1.00 37.25           O  
ANISOU 1975  O1  SO4 A 301     4303   4925   4925    518   -209   -303       O  
HETATM 1976  O2  SO4 A 301       8.285 -68.577 -28.731  1.00 38.19           O  
ANISOU 1976  O2  SO4 A 301     4464   4998   5048    518   -126   -333       O  
HETATM 1977  O3  SO4 A 301       7.828 -70.263 -27.158  1.00 38.65           O1-
ANISOU 1977  O3  SO4 A 301     4434   5094   5159    491   -202   -317       O1-
HETATM 1978  O4  SO4 A 301       8.012 -68.024 -26.459  1.00 37.69           O  
ANISOU 1978  O4  SO4 A 301     4314   4985   5022    484   -141   -314       O  
HETATM 1979  S   SO4 A 301       7.566 -68.894 -27.521  1.00 37.80           S  
ANISOU 1979  S   SO4 A 301     4359   4983   5020    502   -170   -316       S  
HETATM 1980 CL    CL A 302       5.136 -74.704 -17.849  1.00 32.93          CL  
HETATM 1981  O1  SO4 A 303      -5.866 -69.059 -25.762  1.00 71.56           O  
HETATM 1982  O2  SO4 A 303      -7.988 -68.120 -26.142  1.00 71.87           O  
HETATM 1983  O3  SO4 A 303      -7.241 -68.466 -23.944  1.00 71.31           O1-
HETATM 1984  O4  SO4 A 303      -6.251 -66.800 -25.271  1.00 71.76           O  
HETATM 1985  S   SO4 A 303      -6.837 -68.113 -25.279  1.00 71.64           S  
HETATM 1986  O1  SO4 A 304      15.724 -59.221  -3.837  1.00 87.62           O  
HETATM 1987  O2  SO4 A 304      16.025 -56.929  -4.253  1.00 87.92           O  
HETATM 1988  O3  SO4 A 304      13.936 -57.726  -3.531  1.00 87.70           O1-
HETATM 1989  O4  SO4 A 304      15.761 -57.694  -2.052  1.00 87.87           O  
HETATM 1990  S   SO4 A 304      15.361 -57.893  -3.419  1.00 87.85           S  
CONECT 1975 1979
CONECT 1976 1979
CONECT 1977 1979
CONECT 1978 1979
CONECT 1978 1979
CONECT 1979 1975 1976 1977
CONECT 1979 1978
CONECT 1979 1978
CONECT 1981 1985
CONECT 1982 1985
CONECT 1983 1985
CONECT 1984 1985
CONECT 1984 1985
CONECT 1985 1981 1982 1983
CONECT 1985 1984
CONECT 1985 1984
CONECT 1986 1990
CONECT 1987 1990
CONECT 1988 1990
CONECT 1989 1990
CONECT 1989 1990
CONECT 1990 1986 1987 1988
CONECT 1990 1989
CONECT 1990 1989
END



If you find results from this site helpful for your research, please cite one of our papers:

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