CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

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


***    ***

elNémo ID: 23042112320854199

Job options:

ID        	=	 23042112320854199
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   3137  N   VAL L 199     -18.565  59.831  99.951  1.00 68.35
ATOM   3138  CA  VAL L 199     -18.601  61.137  99.234  1.00 64.72
ATOM   3139  C   VAL L 199     -19.408  61.020  97.937  1.00 60.41
ATOM   3140  O   VAL L 199     -20.473  61.629  97.826  1.00 65.82
ATOM   3141  CB  VAL L 199     -17.181  61.670  98.948  1.00 63.70
ATOM   3142  CG1 VAL L 199     -17.159  63.044  98.247  1.00  0.00
ATOM   3143  CG2 VAL L 199     -16.324  61.728 100.226  1.00  0.00
ATOM   3154  N   LEU L 200     -18.923  60.236  96.969  1.00 54.40
ATOM   3155  CA  LEU L 200     -19.654  60.026  95.709  1.00 46.38
ATOM   3156  C   LEU L 200     -20.840  59.060  95.861  1.00 40.00
ATOM   3157  O   LEU L 200     -20.692  57.843  95.887  1.00 36.17
ATOM   3158  CB  LEU L 200     -18.734  59.534  94.600  1.00 46.68
ATOM   3159  CG  LEU L 200     -17.738  60.550  94.049  1.00 52.07
ATOM   3160  CD1 LEU L 200     -17.015  59.940  92.858  1.00 51.64
ATOM   3161  CD2 LEU L 200     -18.420  61.851  93.654  1.00 51.82
ATOM   3173  N   ARG L 201     -22.032  59.617  95.954  1.00 38.24
ATOM   3174  CA  ARG L 201     -23.224  58.793  96.093  1.00 37.52
ATOM   3175  C   ARG L 201     -24.417  59.591  95.610  1.00 33.23
ATOM   3176  O   ARG L 201     -24.338  60.815  95.511  1.00 30.40
ATOM   3177  CB  ARG L 201     -23.392  58.396  97.556  1.00 39.32
ATOM   3178  CG  ARG L 201     -23.724  59.584  98.426  1.00 44.81
ATOM   3179  CD  ARG L 201     -23.474  59.345  99.905  1.00 49.65
ATOM   3180  NE  ARG L 201     -24.373  60.206 100.668  1.00 56.96
ATOM   3181  CZ  ARG L 201     -24.254  61.531 100.782  1.00 62.95
ATOM   3182  NH1 ARG L 201     -23.250  62.191 100.205  1.00 64.76
ATOM   3183  NH2 ARG L 201     -25.150  62.207 101.493  1.00 67.89
ATOM   3197  N   SER L 202     -25.519  58.910  95.315  1.00 32.67
ATOM   3198  CA  SER L 202     -26.743  59.614  94.962  1.00 32.97
ATOM   3199  C   SER L 202     -27.365  60.213  96.221  1.00 36.25
ATOM   3200  O   SER L 202     -27.245  59.668  97.324  1.00 35.53
ATOM   3201  CB  SER L 202     -27.752  58.697  94.270  1.00 31.47
ATOM   3202  OG  SER L 202     -27.312  58.309  92.976  1.00 28.51
ATOM   3208  N   VAL L 203     -28.028  61.346  96.038  1.00 38.87
ATOM   3209  CA  VAL L 203     -28.855  61.944  97.083  1.00 40.60
ATOM   3210  C   VAL L 203     -30.282  61.428  96.901  1.00 40.81
ATOM   3211  O   VAL L 203     -30.817  61.450  95.788  1.00 37.99
ATOM   3212  CB  VAL L 203     -28.820  63.474  96.971  1.00 41.97
ATOM   3213  CG1 VAL L 203     -29.689  64.108  98.031  1.00 45.14
ATOM   3214  CG2 VAL L 203     -27.381  63.968  97.094  1.00 43.17
ATOM   3224  N   ASN L 204     -30.905  60.978  97.987  1.00 39.63
ATOM   3225  CA  ASN L 204     -32.247  60.416  97.917  1.00 39.22
ATOM   3226  C   ASN L 204     -33.294  61.534  97.906  1.00 40.45
ATOM   3227  O   ASN L 204     -34.012  61.751  98.881  1.00 40.73
ATOM   3228  CB  ASN L 204     -32.455  59.438  99.076  1.00 40.75
ATOM   3229  CG  ASN L 204     -33.792  58.719  99.018  1.00 42.71
ATOM   3230  ND2 ASN L 204     -34.168  58.131 100.144  1.00 46.52
ATOM   3231  OD1 ASN L 204     -34.483  58.691  97.991  1.00 38.96
ATOM   3238  N   SER L 205     -33.363  62.245  96.781  1.00 39.84
ATOM   3239  CA  SER L 205     -34.201  63.438  96.652  1.00 38.84
ATOM   3240  C   SER L 205     -35.678  63.106  96.481  1.00 39.07
ATOM   3241  O   SER L 205     -36.531  63.889  96.848  1.00 40.44
ATOM   3242  CB  SER L 205     -33.734  64.271  95.452  1.00 36.99
ATOM   3243  OG  SER L 205     -33.979  63.592  94.230  1.00 35.51
ATOM   3249  N   ARG L 206     -35.958  61.942  95.902  1.00 40.65
ATOM   3250  CA  ARG L 206     -37.294  61.556  95.463  1.00 43.58
ATOM   3251  C   ARG L 206     -37.901  62.540  94.469  1.00 42.14
ATOM   3252  O   ARG L 206     -39.101  62.560  94.289  1.00 42.86
ATOM   3253  CB  ARG L 206     -38.246  61.336  96.644  1.00 49.29
ATOM   3254  CG  ARG L 206     -37.918  60.125  97.488  1.00 54.20
ATOM   3255  CD  ARG L 206     -38.887  60.022  98.651  1.00 61.62
ATOM   3256  NE  ARG L 206     -38.251  59.501  99.862  1.00 72.97
ATOM   3257  CZ  ARG L 206     -37.359  60.157 100.615  1.00 80.15
ATOM   3258  NH1 ARG L 206     -36.948  61.385 100.299  1.00 80.10
ATOM   3259  NH2 ARG L 206     -36.861  59.569 101.699  1.00 81.40
ATOM   3273  N   GLU L 207     -37.081  63.323  93.788  1.00 41.94
ATOM   3274  CA  GLU L 207     -37.610  64.237  92.790  1.00 44.41
ATOM   3275  C   GLU L 207     -37.387  63.676  91.394  1.00 40.88
ATOM   3276  O   GLU L 207     -36.244  63.569  90.950  1.00 39.20
ATOM   3277  CB  GLU L 207     -36.958  65.597  92.935  1.00 49.31
ATOM   3278  CG  GLU L 207     -37.402  66.305  94.192  1.00 54.93
ATOM   3279  CD  GLU L 207     -36.837  67.694  94.269  1.00 62.70
ATOM   3280  OE1 GLU L 207     -37.224  68.514  93.411  1.00 69.49
ATOM   3281  OE2 GLU L 207     -36.013  67.955  95.175  1.00 64.02
ATOM   3288  N   PRO L 208     -38.477  63.298  90.698  1.00 40.23
ATOM   3289  CA  PRO L 208     -38.291  62.704  89.377  1.00 38.36
ATOM   3290  C   PRO L 208     -37.494  63.577  88.412  1.00 35.83
ATOM   3291  O   PRO L 208     -37.561  64.804  88.452  1.00 36.64
ATOM   3292  CB  PRO L 208     -39.724  62.512  88.864  1.00 40.20
ATOM   3293  CG  PRO L 208     -40.556  62.408  90.094  1.00 42.35
ATOM   3294  CD  PRO L 208     -39.896  63.304  91.100  1.00 42.64
ATOM   3302  N   SER L 209     -36.729  62.918  87.562  1.00 34.07
ATOM   3303  CA  SER L 209     -36.094  63.556  86.437  1.00 33.84
ATOM   3304  C   SER L 209     -36.107  62.519  85.316  1.00 33.34
ATOM   3305  O   SER L 209     -35.655  61.379  85.510  1.00 30.58
ATOM   3306  CB  SER L 209     -34.664  63.975  86.784  1.00 32.81
ATOM   3307  OG  SER L 209     -33.957  64.426  85.634  1.00 32.18
ATOM   3313  N   GLN L 210     -36.645  62.910  84.164  1.00 34.19
ATOM   3314  CA  GLN L 210     -36.660  62.046  82.980  1.00 36.39
ATOM   3315  C   GLN L 210     -35.420  62.313  82.141  1.00 32.44
ATOM   3316  O   GLN L 210     -35.019  63.457  81.952  1.00 32.07
ATOM   3317  CB  GLN L 210     -37.929  62.262  82.150  1.00 43.48
ATOM   3318  CG  GLN L 210     -39.050  61.284  82.467  1.00 50.67
ATOM   3319  CD  GLN L 210     -39.653  61.488  83.839  1.00 63.19
ATOM   3320  NE2 GLN L 210     -40.601  62.409  83.929  1.00 71.98
ATOM   3321  OE1 GLN L 210     -39.280  60.818  84.809  1.00 70.69
ATOM   3330  N   VAL L 211     -34.829  61.239  81.641  1.00 31.04
ATOM   3331  CA  VAL L 211     -33.531  61.275  80.995  1.00 31.03
ATOM   3332  C   VAL L 211     -33.582  60.428  79.743  1.00 32.00
ATOM   3333  O   VAL L 211     -34.247  59.401  79.731  1.00 32.85
ATOM   3334  CB  VAL L 211     -32.454  60.652  81.906  1.00 30.10
ATOM   3335  CG1 VAL L 211     -31.098  60.628  81.214  1.00 30.30
ATOM   3336  CG2 VAL L 211     -32.396  61.379  83.247  1.00 30.71
ATOM   3346  N   ILE L 212     -32.870  60.839  78.697  1.00 32.07
ATOM   3347  CA  ILE L 212     -32.570  59.918  77.605  1.00 32.19
ATOM   3348  C   ILE L 212     -31.121  59.436  77.724  1.00 29.70
ATOM   3349  O   ILE L 212     -30.187  60.233  77.712  1.00 30.46
ATOM   3350  CB  ILE L 212     -32.770  60.551  76.217  1.00 33.88
ATOM   3351  CG1 ILE L 212     -34.093  61.319  76.141  1.00 35.44
ATOM   3352  CG2 ILE L 212     -32.700  59.471  75.141  1.00 33.91
ATOM   3353  CD1 ILE L 212     -35.321  60.471  76.369  1.00 37.55
ATOM   3365  N   PHE L 213     -30.945  58.132  77.877  1.00 27.50
ATOM   3366  CA  PHE L 213     -29.640  57.520  77.728  1.00 25.90
ATOM   3367  C   PHE L 213     -29.484  57.252  76.244  1.00 26.30
ATOM   3368  O   PHE L 213     -30.192  56.413  75.707  1.00 27.35
ATOM   3369  CB  PHE L 213     -29.547  56.186  78.488  1.00 26.13
ATOM   3370  CG  PHE L 213     -29.491  56.315  80.001  1.00 26.03
ATOM   3371  CD1 PHE L 213     -29.258  57.533  80.632  1.00 25.92
ATOM   3372  CD2 PHE L 213     -29.642  55.177  80.794  1.00 27.02
ATOM   3373  CE1 PHE L 213     -29.214  57.617  82.019  1.00 26.82
ATOM   3374  CE2 PHE L 213     -29.584  55.251  82.178  1.00 26.31
ATOM   3375  CZ  PHE L 213     -29.362  56.475  82.790  1.00 27.34
ATOM   3386  N   ASN L 214     -26.816  56.162  73.397  1.00 27.61
ATOM   3387  CA  ASN L 214     -25.508  55.543  73.222  1.00 25.25
ATOM   3388  C   ASN L 214     -25.001  55.914  71.822  1.00 27.15
ATOM   3389  O   ASN L 214     -25.349  55.267  70.845  1.00 25.47
ATOM   3390  CB  ASN L 214     -25.627  54.020  73.389  1.00 23.41
ATOM   3391  CG  ASN L 214     -24.303  53.278  73.209  1.00 24.18
ATOM   3392  ND2 ASN L 214     -24.369  51.939  73.241  1.00 24.41
ATOM   3393  OD1 ASN L 214     -23.236  53.881  73.071  1.00 25.82
ATOM   3401  N   ARG L 215     -24.205  56.974  71.744  1.00 28.49
ATOM   3402  CA  ARG L 215     -23.559  57.373  70.499  1.00 29.57
ATOM   3403  C   ARG L 215     -22.138  56.813  70.487  1.00 30.72
ATOM   3404  O   ARG L 215     -21.180  57.539  70.255  1.00 30.63
ATOM   3405  CB  ARG L 215     -23.517  58.888  70.389  1.00 33.80
ATOM   3406  CG  ARG L 215     -24.873  59.561  70.327  1.00 40.22
ATOM   3407  CD  ARG L 215     -24.724  61.003  69.866  1.00 47.24
ATOM   3408  NE  ARG L 215     -25.807  61.848  70.359  1.00 53.59
ATOM   3409  CZ  ARG L 215     -26.982  62.022  69.750  1.00 56.48
ATOM   3410  NH1 ARG L 215     -27.255  61.414  68.600  1.00 58.55
ATOM   3411  NH2 ARG L 215     -27.896  62.811  70.303  1.00 56.24
ATOM   3425  N   SER L 216     -22.011  55.521  70.782  1.00 28.26
ATOM   3426  CA  SER L 216     -20.739  54.856  70.743  1.00 26.54
ATOM   3427  C   SER L 216     -20.921  53.525  70.054  1.00 25.46
ATOM   3428  O   SER L 216     -22.043  53.075  69.871  1.00 25.98
ATOM   3429  CB  SER L 216     -20.203  54.636  72.174  1.00 25.58
ATOM   3430  OG  SER L 216     -20.639  53.391  72.692  1.00 23.52
ATOM   3436  N   PRO L 217     -19.813  52.866  69.697  1.00 25.93
ATOM   3437  CA  PRO L 217     -19.910  51.544  69.111  1.00 27.01
ATOM   3438  C   PRO L 217     -19.869  50.408  70.144  1.00 26.19
ATOM   3439  O   PRO L 217     -19.850  49.244  69.768  1.00 26.94
ATOM   3440  CB  PRO L 217     -18.693  51.504  68.189  1.00 29.40
ATOM   3441  CG  PRO L 217     -17.671  52.313  68.925  1.00 28.56
ATOM   3442  CD  PRO L 217     -18.431  53.376  69.672  1.00 26.94
ATOM   3450  N   ARG L 218     -19.888  50.731  71.438  1.00 26.41
ATOM   3451  CA  ARG L 218     -19.848  49.711  72.491  1.00 26.84
ATOM   3452  C   ARG L 218     -21.238  49.395  73.016  1.00 26.38
ATOM   3453  O   ARG L 218     -22.114  50.242  72.969  1.00 26.49
ATOM   3454  CB  ARG L 218     -19.006  50.196  73.679  1.00 26.36
ATOM   3455  CG  ARG L 218     -17.634  50.742  73.326  1.00 27.74
ATOM   3456  CD  ARG L 218     -16.785  49.774  72.517  1.00 30.00
ATOM   3457  NE  ARG L 218     -15.393  50.245  72.411  1.00 30.20
ATOM   3458  CZ  ARG L 218     -14.442  50.048  73.328  1.00 31.47
ATOM   3459  NH1 ARG L 218     -14.686  49.373  74.456  1.00 30.41
ATOM   3460  NH2 ARG L 218     -13.223  50.526  73.111  1.00 31.36
ATOM   3474  N   VAL L 219     -21.414  48.185  73.547  1.00 26.81
ATOM   3475  CA  VAL L 219     -22.573  47.860  74.381  1.00 26.79
ATOM   3476  C   VAL L 219     -22.324  48.564  75.700  1.00 26.38
ATOM   3477  O   VAL L 219     -21.298  48.333  76.344  1.00 24.38
ATOM   3478  CB  VAL L 219     -22.724  46.347  74.622  1.00 29.90
ATOM   3479  CG1 VAL L 219     -23.908  46.059  75.538  1.00 31.17
ATOM   3480  CG2 VAL L 219     -22.903  45.600  73.299  1.00 33.31
ATOM   3490  N   VAL L 220     -23.247  49.435  76.091  1.00 25.80
ATOM   3491  CA  VAL L 220     -23.046  50.291  77.249  1.00 25.06
ATOM   3492  C   VAL L 220     -23.780  49.738  78.479  1.00 24.57
ATOM   3493  O   VAL L 220     -24.965  49.391  78.418  1.00 25.25
ATOM   3494  CB  VAL L 220     -23.520  51.741  76.966  1.00 25.86
ATOM   3495  CG1 VAL L 220     -23.626  52.555  78.252  1.00 26.96
ATOM   3496  CG2 VAL L 220     -22.586  52.427  75.978  1.00 26.62
ATOM   3506  N   LEU L 221     -23.049  49.681  79.584  1.00 24.22
ATOM   3507  CA  LEU L 221     -23.596  49.403  80.906  1.00 25.11
ATOM   3508  C   LEU L 221     -23.781  50.734  81.652  1.00 23.10
ATOM   3509  O   LEU L 221     -22.799  51.388  81.996  1.00 22.87
ATOM   3510  CB  LEU L 221     -22.626  48.520  81.679  1.00 25.29
ATOM   3511  CG  LEU L 221     -22.941  48.189  83.127  1.00 25.19
ATOM   3512  CD1 LEU L 221     -24.123  47.248  83.188  1.00 25.68
ATOM   3513  CD2 LEU L 221     -21.727  47.541  83.779  1.00 27.97
ATOM   3525  N   PRO L 222     -25.033  51.147  81.885  1.00 21.57
ATOM   3526  CA  PRO L 222     -25.273  52.265  82.788  1.00 21.89
ATOM   3527  C   PRO L 222     -25.061  51.789  84.225  1.00 22.45
ATOM   3528  O   PRO L 222     -25.450  50.661  84.563  1.00 22.71
ATOM   3529  CB  PRO L 222     -26.750  52.626  82.540  1.00 22.00
ATOM   3530  CG  PRO L 222     -27.144  51.891  81.302  1.00 23.74
ATOM   3531  CD  PRO L 222     -26.275  50.677  81.253  1.00 23.79
ATOM   3539  N   VAL L 223     -24.412  52.620  85.035  1.00 22.88
ATOM   3540  CA  VAL L 223     -24.125  52.295  86.439  1.00 23.63
ATOM   3541  C   VAL L 223     -24.643  53.422  87.321  1.00 23.57
ATOM   3542  O   VAL L 223     -24.184  54.555  87.208  1.00 23.11
ATOM   3543  CB  VAL L 223     -22.613  52.091  86.672  1.00 25.31
ATOM   3544  CG1 VAL L 223     -22.309  51.880  88.144  1.00 27.18
ATOM   3545  CG2 VAL L 223     -22.120  50.888  85.882  1.00 27.54
ATOM   3555  N   TRP L 224     -25.596  53.104  88.196  1.00 24.14
ATOM   3556  CA  TRP L 224     -26.134  54.065  89.163  1.00 24.26
ATOM   3557  C   TRP L 224     -25.376  53.980  90.488  1.00 25.95
ATOM   3558  O   TRP L 224     -25.190  52.889  91.035  1.00 26.70
ATOM   3559  CB  TRP L 224     -27.625  53.782  89.398  1.00 23.76
ATOM   3560  CG  TRP L 224     -28.252  54.666  90.441  1.00 25.22
ATOM   3561  CD1 TRP L 224     -28.283  56.019  90.443  1.00 26.28
ATOM   3562  CD2 TRP L 224     -28.929  54.249  91.631  1.00 25.09
ATOM   3563  CE2 TRP L 224     -29.331  55.418  92.313  1.00 25.97
ATOM   3564  CE3 TRP L 224     -29.216  53.001  92.198  1.00 24.54
ATOM   3565  NE1 TRP L 224     -28.935  56.485  91.559  1.00 26.37
ATOM   3566  CZ2 TRP L 224     -30.020  55.380  93.529  1.00 26.42
ATOM   3567  CZ3 TRP L 224     -29.893  52.963  93.423  1.00 25.36
ATOM   3568  CH2 TRP L 224     -30.290  54.145  94.064  1.00 25.97
ATOM   3579  N   LEU L 225     -24.945  55.120  91.023  1.00 26.43
ATOM   3580  CA  LEU L 225     -24.370  55.117  92.361  1.00 29.14
ATOM   3581  C   LEU L 225     -25.482  55.221  93.380  1.00 28.10
ATOM   3582  O   LEU L 225     -26.180  56.223  93.452  1.00 28.19
ATOM   3583  CB  LEU L 225     -23.349  56.230  92.547  1.00 30.17
ATOM   3584  CG  LEU L 225     -22.195  56.181  91.544  1.00 30.70
ATOM   3585  CD1 LEU L 225     -21.136  57.160  92.002  1.00 32.20
ATOM   3586  CD2 LEU L 225     -21.596  54.788  91.408  1.00 30.25
ATOM   3598  N   ASN L 226     -25.644  54.164  94.167  1.00 28.72
ATOM   3599  CA  ASN L 226     -26.720  54.114  95.146  1.00 29.84
ATOM   3600  C   ASN L 226     -26.439  55.003  96.366  1.00 30.77
ATOM   3601  O   ASN L 226     -25.406  55.672  96.430  1.00 29.51
ATOM   3602  CB  ASN L 226     -27.031  52.664  95.522  1.00 30.81
ATOM   3603  CG  ASN L 226     -26.084  52.093  96.562  1.00 32.07
ATOM   3604  ND2 ASN L 226     -26.221  50.803  96.805  1.00 31.77
ATOM   3605  OD1 ASN L 226     -25.256  52.795  97.148  1.00 32.03
ATOM   3612  N   PHE L 227     -27.356  55.020  97.330  1.00 33.29
ATOM   3613  CA  PHE L 227     -27.282  56.006  98.414  1.00 34.72
ATOM   3614  C   PHE L 227     -26.080  55.820  99.344  1.00 38.09
ATOM   3615  O   PHE L 227     -25.732  56.737 100.082  1.00 41.59
ATOM   3616  CB  PHE L 227     -28.605  56.058  99.184  1.00 35.81
ATOM   3617  CG  PHE L 227     -29.809  56.257  98.291  1.00 35.56
ATOM   3618  CD1 PHE L 227     -29.851  57.317  97.381  1.00 34.99
ATOM   3619  CD2 PHE L 227     -30.875  55.373  98.327  1.00 35.97
ATOM   3620  CE1 PHE L 227     -30.937  57.501  96.543  1.00 33.78
ATOM   3621  CE2 PHE L 227     -31.963  55.548  97.481  1.00 36.62
ATOM   3622  CZ  PHE L 227     -31.995  56.616  96.591  1.00 34.76
ATOM   3632  N   ASP L 228     -25.450  54.644  99.290  1.00 38.93
ATOM   3633  CA  ASP L 228     -24.196  54.361  99.995  1.00 40.59
ATOM   3634  C   ASP L 228     -22.962  54.541  99.104  1.00 39.54
ATOM   3635  O   ASP L 228     -21.849  54.316  99.549  1.00 40.81
ATOM   3636  CB  ASP L 228     -24.189  52.909 100.490  1.00 44.21
ATOM   3637  CG  ASP L 228     -25.368  52.570 101.390  1.00 46.61
ATOM   3638  OD1 ASP L 228     -25.830  53.438 102.158  1.00 47.68
ATOM   3639  OD2 ASP L 228     -25.820  51.411 101.338  1.00 48.29
ATOM   3644  N   GLY L 229     -23.150  54.921  97.844  1.00 37.49
ATOM   3645  CA  GLY L 229     -22.034  55.046  96.908  1.00 37.14
ATOM   3646  C   GLY L 229     -21.619  53.747  96.235  1.00 35.16
ATOM   3647  O   GLY L 229     -20.601  53.706  95.555  1.00 36.50
ATOM   3651  N   GLU L 230     -22.421  52.695  96.398  1.00 33.37
ATOM   3652  CA  GLU L 230     -22.177  51.421  95.739  1.00 31.97
ATOM   3653  C   GLU L 230     -22.685  51.427  94.287  1.00 30.35
ATOM   3654  O   GLU L 230     -23.846  51.763  94.028  1.00 28.56
ATOM   3655  CB  GLU L 230     -22.866  50.309  96.518  1.00 34.79
ATOM   3656  CG  GLU L 230     -22.337  48.929  96.216  1.00 36.05
ATOM   3657  CD  GLU L 230     -20.921  48.705  96.711  1.00 37.71
ATOM   3658  OE1 GLU L 230     -20.123  48.157  95.932  1.00 35.36
ATOM   3659  OE2 GLU L 230     -20.615  49.040  97.886  1.00 39.53
ATOM   3666  N   PRO L 231     -21.818  51.054  93.333  1.00 30.11
ATOM   3667  CA  PRO L 231     -22.247  51.051  91.937  1.00 29.93
ATOM   3668  C   PRO L 231     -23.247  49.946  91.669  1.00 30.58
ATOM   3669  O   PRO L 231     -23.043  48.808  92.090  1.00 32.44
ATOM   3670  CB  PRO L 231     -20.957  50.820  91.155  1.00 30.76
ATOM   3671  CG  PRO L 231     -19.988  50.225  92.121  1.00 31.69
ATOM   3672  CD  PRO L 231     -20.440  50.555  93.507  1.00 31.44
ATOM   3680  N   GLN L 232     -24.331  50.300  90.996  1.00 29.20
ATOM   3681  CA  GLN L 232     -25.411  49.384  90.717  1.00 31.74
ATOM   3682  C   GLN L 232     -25.648  49.342  89.210  1.00 29.08
ATOM   3683  O   GLN L 232     -26.015  50.356  88.617  1.00 27.03
ATOM   3684  CB  GLN L 232     -26.654  49.878  91.433  1.00 37.68
ATOM   3685  CG  GLN L 232     -27.794  48.893  91.472  1.00 46.09
ATOM   3686  CD  GLN L 232     -28.550  49.003  92.781  1.00 57.53
ATOM   3687  NE2 GLN L 232     -27.970  48.840  93.866  1.00 57.13
ATOM   3688  OE1 GLN L 232     -29.842  49.301  92.692  1.00 63.08
ATOM   3697  N   PRO L 233     -25.406  48.180  88.586  1.00 28.30
ATOM   3698  CA  PRO L 233     -25.600  48.033  87.150  1.00 26.36
ATOM   3699  C   PRO L 233     -27.072  48.031  86.749  1.00 25.15
ATOM   3700  O   PRO L 233     -27.899  47.456  87.436  1.00 23.84
ATOM   3701  CB  PRO L 233     -24.942  46.695  86.825  1.00 28.40
ATOM   3702  CG  PRO L 233     -24.887  45.952  88.091  1.00 31.57
ATOM   3703  CD  PRO L 233     -25.049  46.909  89.237  1.00 30.50
ATOM   3711  N   TYR L 234     -27.366  48.691  85.633  1.00 25.47
ATOM   3712  CA  TYR L 234     -28.703  48.765  85.053  1.00 26.17
ATOM   3713  C   TYR L 234     -28.629  48.113  83.672  1.00 26.95
ATOM   3714  O   TYR L 234     -27.539  47.756  83.227  1.00 25.54
ATOM   3715  CB  TYR L 234     -29.140  50.226  84.972  1.00 26.16
ATOM   3716  CG  TYR L 234     -29.905  50.654  86.204  1.00 26.87
ATOM   3717  CD1 TYR L 234     -29.263  50.829  87.428  1.00 27.74
ATOM   3718  CD2 TYR L 234     -31.280  50.839  86.156  1.00 28.23
ATOM   3719  CE1 TYR L 234     -29.981  51.189  88.570  1.00 27.91
ATOM   3720  CE2 TYR L 234     -32.004  51.190  87.290  1.00 27.83
ATOM   3721  CZ  TYR L 234     -31.353  51.366  88.489  1.00 27.59
ATOM   3722  OH  TYR L 234     -32.074  51.726  89.604  1.00 27.00
ATOM   3732  N   PRO L 235     -29.782  47.915  83.009  1.00 26.92
ATOM   3733  CA  PRO L 235     -29.763  47.209  81.736  1.00 26.10
ATOM   3734  C   PRO L 235     -28.877  47.833  80.667  1.00 24.80
ATOM   3735  O   PRO L 235     -28.748  49.064  80.588  1.00 23.64
ATOM   3736  CB  PRO L 235     -31.232  47.223  81.315  1.00 26.86
ATOM   3737  CG  PRO L 235     -31.971  47.188  82.611  1.00 27.17
ATOM   3738  CD  PRO L 235     -31.166  48.093  83.502  1.00 26.97
ATOM   3746  N   THR L 236     -28.260  46.975  79.860  1.00 24.31
ATOM   3747  CA  THR L 236     -27.329  47.423  78.842  1.00 25.75
ATOM   3748  C   THR L 236     -28.033  48.032  77.634  1.00 26.86
ATOM   3749  O   THR L 236     -29.185  47.717  77.353  1.00 27.71
ATOM   3750  CB  THR L 236     -26.420  46.275  78.366  1.00 27.91
ATOM   3751  CG2 THR L 236     -25.599  45.712  79.555  1.00 27.97
ATOM   3752  OG1 THR L 236     -27.218  45.237  77.785  1.00 27.45
ATOM   3760  N   LEU L 237     -27.328  48.923  76.944  1.00 27.64
ATOM   3761  CA  LEU L 237     -27.817  49.551  75.722  1.00 28.62
ATOM   3762  C   LEU L 237     -26.921  49.156  74.565  1.00 27.26
ATOM   3763  O   LEU L 237     -25.721  49.445  74.594  1.00 25.17
ATOM   3764  CB  LEU L 237     -27.759  51.059  75.858  1.00 30.83
ATOM   3765  CG  LEU L 237     -28.685  51.692  76.888  1.00 35.41
ATOM   3766  CD1 LEU L 237     -27.917  52.704  77.718  1.00 37.60
ATOM   3767  CD2 LEU L 237     -29.857  52.356  76.197  1.00 39.84
ATOM   3779  N   PRO L 238     -27.488  48.512  73.527  1.00 28.50
ATOM   3780  CA  PRO L 238     -26.650  48.221  72.366  1.00 28.06
ATOM   3781  C   PRO L 238     -26.170  49.493  71.659  1.00 28.07
ATOM   3782  O   PRO L 238     -26.764  50.561  71.830  1.00 26.05
ATOM   3783  CB  PRO L 238     -27.578  47.398  71.455  1.00 30.83
ATOM   3784  CG  PRO L 238     -28.672  46.887  72.358  1.00 30.39
ATOM   3785  CD  PRO L 238     -28.843  47.944  73.393  1.00 29.34
ATOM   3793  N   PRO L 239     -25.088  49.387  70.871  1.00 29.20
ATOM   3794  CA  PRO L 239     -24.566  50.531  70.112  1.00 28.29
ATOM   3795  C   PRO L 239     -25.643  51.300  69.351  1.00 28.89
ATOM   3796  O   PRO L 239     -26.546  50.702  68.790  1.00 29.85
ATOM   3797  CB  PRO L 239     -23.614  49.886  69.103  1.00 29.93
ATOM   3798  CG  PRO L 239     -23.268  48.563  69.678  1.00 31.01
ATOM   3799  CD  PRO L 239     -24.441  48.118  70.495  1.00 30.73
ATOM   3807  N   GLY L 240     -25.553  52.620  69.349  1.00 29.51
ATOM   3808  CA  GLY L 240     -26.470  53.446  68.576  1.00 31.46
ATOM   3809  C   GLY L 240     -27.926  53.480  69.032  1.00 33.66
ATOM   3810  O   GLY L 240     -28.757  54.027  68.321  1.00 37.19
ATOM   3814  N   THR L 241     -28.252  52.897  70.193  1.00 31.07
ATOM   3815  CA  THR L 241     -29.621  52.923  70.708  1.00 31.71
ATOM   3816  C   THR L 241     -29.790  53.954  71.819  1.00 31.62
ATOM   3817  O   THR L 241     -28.819  54.380  72.440  1.00 29.78
ATOM   3818  CB  THR L 241     -30.051  51.548  71.275  1.00 32.63
ATOM   3819  CG2 THR L 241     -29.933  50.484  70.187  1.00 33.60
ATOM   3820  OG1 THR L 241     -29.240  51.197  72.424  1.00 30.40
ATOM   3828  N   GLY L 242     -31.035  54.332  72.074  1.00 32.44
ATOM   3829  CA  GLY L 242     -31.349  55.207  73.200  1.00 33.64
ATOM   3830  C   GLY L 242     -32.588  54.725  73.929  1.00 33.40
ATOM   3831  O   GLY L 242     -33.386  54.001  73.357  1.00 32.87
ATOM   3835  N   ARG L 243     -32.730  55.126  75.192  1.00 32.43
ATOM   3836  CA  ARG L 243     -33.906  54.811  75.990  1.00 33.31
ATOM   3837  C   ARG L 243     -34.262  55.980  76.887  1.00 31.98
ATOM   3838  O   ARG L 243     -33.375  56.640  77.443  1.00 29.00
ATOM   3839  CB  ARG L 243     -33.649  53.576  76.851  1.00 36.18
ATOM   3840  CG  ARG L 243     -33.457  52.328  76.006  1.00 40.34
ATOM   3841  CD  ARG L 243     -33.549  51.067  76.827  1.00 42.80
ATOM   3842  NE  ARG L 243     -33.095  49.911  76.049  1.00 46.47
ATOM   3843  CZ  ARG L 243     -32.285  48.945  76.498  1.00 45.54
ATOM   3844  NH1 ARG L 243     -31.801  48.970  77.743  1.00 41.33
ATOM   3845  NH2 ARG L 243     -31.946  47.945  75.686  1.00 44.54
ATOM   3859  N   ARG L 244     -35.561  56.233  77.004  1.00 31.82
ATOM   3860  CA  ARG L 244     -36.085  57.212  77.934  1.00 32.86
ATOM   3861  C   ARG L 244     -36.262  56.495  79.254  1.00 31.12
ATOM   3862  O   ARG L 244     -36.962  55.506  79.310  1.00 33.02
ATOM   3863  CB  ARG L 244     -37.423  57.767  77.449  1.00 36.70
ATOM   3864  CG  ARG L 244     -37.933  58.920  78.303  1.00 40.45
ATOM   3865  CD  ARG L 244     -39.115  59.624  77.675  1.00 44.34
ATOM   3866  NE  ARG L 244     -40.320  58.870  77.954  1.00 51.39
ATOM   3867  CZ  ARG L 244     -41.024  58.962  79.078  1.00 53.24
ATOM   3868  NH1 ARG L 244     -40.672  59.799  80.053  1.00 48.68
ATOM   3869  NH2 ARG L 244     -42.096  58.206  79.220  1.00 59.13
ATOM   3883  N   ILE L 245     -35.613  56.978  80.306  1.00 30.74
ATOM   3884  CA  ILE L 245     -35.631  56.300  81.605  1.00 30.12
ATOM   3885  C   ILE L 245     -36.031  57.247  82.725  1.00 31.27
ATOM   3886  O   ILE L 245     -35.955  58.486  82.586  1.00 29.74
ATOM   3887  CB  ILE L 245     -34.265  55.636  81.952  1.00 31.04
ATOM   3888  CG1 ILE L 245     -33.139  56.675  82.075  1.00 30.96
ATOM   3889  CG2 ILE L 245     -33.907  54.563  80.935  1.00 31.70
ATOM   3890  CD1 ILE L 245     -32.991  57.257  83.472  1.00 30.94
ATOM   3902  N   HIS L 246     -36.454  56.654  83.840  1.00 32.25
ATOM   3903  CA  HIS L 246     -36.884  57.423  85.006  1.00 35.44
ATOM   3904  C   HIS L 246     -35.810  57.453  86.082  1.00 31.54
ATOM   3905  O   HIS L 246     -35.396  56.419  86.593  1.00 28.69
ATOM   3906  CB  HIS L 246     -38.189  56.862  85.541  1.00 38.39
ATOM   3907  CG  HIS L 246     -39.312  56.982  84.563  1.00 45.96
ATOM   3908  CD2 HIS L 246     -39.940  56.058  83.798  1.00 48.58
ATOM   3909  ND1 HIS L 246     -39.879  58.195  84.239  1.00 49.23
ATOM   3910  CE1 HIS L 246     -40.831  58.010  83.344  1.00 50.47
ATOM   3911  NE2 HIS L 246     -40.887  56.723  83.057  1.00 51.40
ATOM   3919  N   SER L 247     -35.326  58.651  86.384  1.00 30.96
ATOM   3920  CA  SER L 247     -34.316  58.818  87.424  1.00 30.00
ATOM   3921  C   SER L 247     -34.749  59.981  88.318  1.00 30.58
ATOM   3922  O   SER L 247     -35.936  60.343  88.369  1.00 32.47
ATOM   3923  CB  SER L 247     -32.915  59.008  86.815  1.00 27.87
ATOM   3924  OG  SER L 247     -31.877  58.812  87.779  1.00 26.75
ATOM   3930  N   TYR L 248     -33.809  60.547  89.054  1.00 30.02
ATOM   3931  CA  TYR L 248     -34.154  61.487  90.098  1.00 31.39
ATOM   3932  C   TYR L 248     -33.070  62.512  90.208  1.00 31.14
ATOM   3933  O   TYR L 248     -31.896  62.216  89.943  1.00 30.66
ATOM   3934  CB  TYR L 248     -34.327  60.757  91.436  1.00 33.35
ATOM   3935  CG  TYR L 248     -35.515  59.808  91.470  1.00 35.47
ATOM   3936  CD1 TYR L 248     -35.400  58.505  91.013  1.00 34.32
ATOM   3937  CD2 TYR L 248     -36.745  60.221  91.957  1.00 38.59
ATOM   3938  CE1 TYR L 248     -36.476  57.647  91.028  1.00 35.83
ATOM   3939  CE2 TYR L 248     -37.839  59.366  91.969  1.00 39.48
ATOM   3940  CZ  TYR L 248     -37.691  58.082  91.507  1.00 37.87
ATOM   3941  OH  TYR L 248     -38.752  57.228  91.519  1.00 39.07
ATOM   3951  N   ARG L 249     -33.453  63.722  90.592  1.00 31.98
ATOM   3952  CA  ARG L 249     -32.491  64.798  90.733  1.00 32.73
ATOM   3953  C   ARG L 249     -31.460  64.408  91.772  1.00 32.16
ATOM   3954  O   ARG L 249     -31.774  63.705  92.739  1.00 32.17
ATOM   3955  CB  ARG L 249     -33.191  66.079  91.136  1.00 36.45
ATOM   3956  CG  ARG L 249     -34.102  66.618  90.046  1.00 38.03
ATOM   3957  CD  ARG L 249     -34.931  67.782  90.539  1.00 39.01
ATOM   3958  NE  ARG L 249     -34.091  68.934  90.795  1.00 39.66
ATOM   3959  CZ  ARG L 249     -34.451  69.984  91.516  1.00 42.50
ATOM   3960  NH1 ARG L 249     -35.654  70.051  92.065  1.00 44.19
ATOM   3961  NH2 ARG L 249     -33.599  70.985  91.684  1.00 45.46
ATOM   3975  N   GLY L 250     -30.216  64.811  91.541  1.00 32.41
ATOM   3976  CA  GLY L 250     -29.121  64.508  92.460  1.00 31.98
ATOM   3977  C   GLY L 250     -28.632  63.072  92.421  1.00 30.65
ATOM   3978  O   GLY L 250     -27.776  62.686  93.220  1.00 31.25
ATOM   3982  N   HIE L 251     -29.158  62.263  91.510  1.00 27.87
ATOM   3983  CA  HIE L 251     -28.649  60.921  91.368  1.00 27.77
ATOM   3984  C   HIE L 251     -27.389  60.921  90.525  1.00 27.46
ATOM   3985  O   HIE L 251     -27.189  61.802  89.694  1.00 28.86
ATOM   3986  CB  HIE L 251     -29.702  60.011  90.783  1.00 27.49
ATOM   3987  CG  HIE L 251     -30.724  59.586  91.781  1.00 29.17
ATOM   3988  CD2 HIE L 251     -31.117  60.157  92.945  1.00 31.13
ATOM   3989  ND1 HIE L 251     -31.428  58.410  91.670  1.00 29.50
ATOM   3990  CE1 HIE L 251     -32.231  58.286  92.712  1.00 32.18
ATOM   3991  NE2 HIE L 251     -32.073  59.341  93.492  1.00 32.57
ATOM   3999  N   LEU L 252     -26.526  59.943  90.753  1.00 27.10
ATOM   4000  CA  LEU L 252     -25.252  59.898  90.038  1.00 28.45
ATOM   4001  C   LEU L 252     -25.154  58.681  89.146  1.00 26.05
ATOM   4002  O   LEU L 252     -25.414  57.565  89.585  1.00 25.91
ATOM   4003  CB  LEU L 252     -24.085  59.895  91.016  1.00 31.50
ATOM   4004  CG  LEU L 252     -23.362  61.218  91.271  1.00 36.25
ATOM   4005  CD1 LEU L 252     -24.333  62.291  91.731  1.00 39.15
ATOM   4006  CD2 LEU L 252     -22.281  61.003  92.327  1.00 35.96
ATOM   4018  N   TRP L 253     -24.731  58.898  87.908  1.00 26.44
ATOM   4019  CA  TRP L 253     -24.531  57.803  86.953  1.00 25.68
ATOM   4020  C   TRP L 253     -23.180  57.864  86.291  1.00 25.65
ATOM   4021  O   TRP L 253     -22.592  58.928  86.150  1.00 25.47
ATOM   4022  CB  TRP L 253     -25.546  57.867  85.843  1.00 24.12
ATOM   4023  CG  TRP L 253     -26.924  57.690  86.248  1.00 23.07
ATOM   4024  CD1 TRP L 253     -27.770  58.649  86.724  1.00 24.13
ATOM   4025  CD2 TRP L 253     -27.674  56.489  86.167  1.00 21.78
ATOM   4026  CE2 TRP L 253     -28.976  56.784  86.605  1.00 22.84
ATOM   4027  CE3 TRP L 253     -27.378  55.191  85.747  1.00 21.30
ATOM   4028  NE1 TRP L 253     -29.006  58.113  86.941  1.00 23.83
ATOM   4029  CZ2 TRP L 253     -29.972  55.825  86.667  1.00 24.21
ATOM   4030  CZ3 TRP L 253     -28.377  54.242  85.786  1.00 22.06
ATOM   4031  CH2 TRP L 253     -29.654  54.556  86.257  1.00 22.67
ATOM   4042  N   LEU L 254     -22.693  56.704  85.881  1.00 27.03
ATOM   4043  CA  LEU L 254     -21.595  56.648  84.938  1.00 29.82
ATOM   4044  C   LEU L 254     -21.836  55.504  83.955  1.00 26.95
ATOM   4045  O   LEU L 254     -22.782  54.741  84.129  1.00 25.97
ATOM   4046  CB  LEU L 254     -20.243  56.569  85.650  1.00 33.45
ATOM   4047  CG  LEU L 254     -19.980  55.522  86.707  1.00 38.66
ATOM   4048  CD1 LEU L 254     -19.608  54.194  86.066  1.00 39.31
ATOM   4049  CD2 LEU L 254     -18.843  56.026  87.587  1.00 42.50
ATOM   4061  N   PHE L 255     -20.996  55.411  82.921  1.00 24.72
ATOM   4062  CA  PHE L 255     -21.252  54.523  81.803  1.00 23.43
ATOM   4063  C   PHE L 255     -19.975  53.822  81.372  1.00 24.63
ATOM   4064  O   PHE L 255     -18.897  54.441  81.271  1.00 23.48
ATOM   4065  CB  PHE L 255     -21.885  55.320  80.663  1.00 22.75
ATOM   4066  CG  PHE L 255     -23.193  55.941  81.041  1.00 21.41
ATOM   4067  CD1 PHE L 255     -23.228  57.153  81.709  1.00 22.05
ATOM   4068  CD2 PHE L 255     -24.379  55.284  80.799  1.00 21.09
ATOM   4069  CE1 PHE L 255     -24.428  57.705  82.118  1.00 21.86
ATOM   4070  CE2 PHE L 255     -25.587  55.841  81.181  1.00 20.77
ATOM   4071  CZ  PHE L 255     -25.609  57.052  81.843  1.00 21.57
ATOM   4081  N   ARG L 256     -20.101  52.515  81.147  1.00 25.08
ATOM   4082  CA  ARG L 256     -18.955  51.656  80.865  1.00 24.67
ATOM   4083  C   ARG L 256     -19.292  50.728  79.736  1.00 24.07
ATOM   4084  O   ARG L 256     -20.461  50.469  79.472  1.00 22.72
ATOM   4085  CB  ARG L 256     -18.621  50.781  82.069  1.00 28.23
ATOM   4086  CG  ARG L 256     -18.647  51.499  83.392  1.00 31.66
ATOM   4087  CD  ARG L 256     -17.582  52.567  83.449  1.00 36.67
ATOM   4088  NE  ARG L 256     -16.284  51.985  83.725  1.00 39.04
ATOM   4089  CZ  ARG L 256     -15.283  52.616  84.324  1.00 42.36
ATOM   4090  NH1 ARG L 256     -15.408  53.890  84.710  1.00 39.62
ATOM   4091  NH2 ARG L 256     -14.145  51.953  84.542  1.00 43.15
ATOM   4105  N   ASP L 257     -18.258  50.208  79.083  1.00 23.21
ATOM   4106  CA  ASP L 257     -18.430  49.094  78.170  1.00 24.74
ATOM   4107  C   ASP L 257     -18.883  47.881  79.000  1.00 25.32
ATOM   4108  O   ASP L 257     -18.233  47.500  79.971  1.00 26.65
ATOM   4109  CB  ASP L 257     -17.115  48.823  77.429  1.00 26.23
ATOM   4110  CG  ASP L 257     -17.194  47.641  76.494  1.00 27.95
ATOM   4111  OD1 ASP L 257     -17.419  46.503  76.958  1.00 29.04
ATOM   4112  OD2 ASP L 257     -16.967  47.845  75.293  1.00 29.57
ATOM   4117  N   ALA L 258     -20.007  47.294  78.623  1.00 25.98
ATOM   4118  CA  ALA L 258     -20.596  46.193  79.373  1.00 27.30
ATOM   4119  C   ALA L 258     -19.761  44.915  79.371  1.00 28.50
ATOM   4120  O   ALA L 258     -19.881  44.095  80.279  1.00 29.26
ATOM   4121  CB  ALA L 258     -21.991  45.901  78.833  1.00 29.64
ATOM   4127  N   GLY L 259     -18.939  44.730  78.342  1.00 30.23
ATOM   4128  CA  GLY L 259     -18.100  43.546  78.226  1.00 29.84
ATOM   4129  C   GLY L 259     -16.762  43.687  78.934  1.00 29.73
ATOM   4130  O   GLY L 259     -16.346  42.779  79.629  1.00 32.06
ATOM   4134  N   THR L 260     -16.102  44.833  78.768  1.00 28.37
ATOM   4135  CA  THR L 260     -14.718  45.033  79.217  1.00 29.56
ATOM   4136  C   THR L 260     -14.531  46.013  80.386  1.00 29.14
ATOM   4137  O   THR L 260     -13.423  46.115  80.930  1.00 27.88
ATOM   4138  CB  THR L 260     -13.901  45.647  78.091  1.00 29.16
ATOM   4139  CG2 THR L 260     -14.035  44.827  76.804  1.00 30.26
ATOM   4140  OG1 THR L 260     -14.381  46.972  77.870  1.00 28.54
ATOM   4148  N   HIS L 261     -15.589  46.762  80.701  1.00 26.74
ATOM   4149  CA  HIS L 261     -15.585  47.867  81.666  1.00 28.04
ATOM   4150  C   HIS L 261     -14.775  49.123  81.326  1.00 27.56
ATOM   4151  O   HIS L 261     -14.549  49.987  82.202  1.00 25.76
ATOM   4152  CB  HIS L 261     -15.272  47.340  83.061  1.00 30.66
ATOM   4153  CG  HIS L 261     -16.279  46.344  83.525  1.00 33.51
ATOM   4154  CD2 HIS L 261     -17.606  46.469  83.754  1.00 34.12
ATOM   4155  ND1 HIS L 261     -15.982  45.012  83.704  1.00 36.38
ATOM   4156  CE1 HIS L 261     -17.073  44.370  84.086  1.00 37.61
ATOM   4157  NE2 HIS L 261     -18.073  45.231  84.118  1.00 35.01
ATOM   4165  N   ASP L 262     -14.404  49.262  80.053  1.00 26.52
ATOM   4166  CA  ASP L 262     -13.728  50.451  79.590  1.00 27.02
ATOM   4167  C   ASP L 262     -14.590  51.651  79.950  1.00 27.10
ATOM   4168  O   ASP L 262     -15.814  51.596  79.863  1.00 26.21
ATOM   4169  CB  ASP L 262     -13.490  50.399  78.061  1.00 28.35
ATOM   4170  CG  ASP L 262     -12.525  49.288  77.650  1.00 28.86
ATOM   4171  OD1 ASP L 262     -11.623  48.959  78.437  1.00 30.92
ATOM   4172  OD2 ASP L 262     -12.664  48.733  76.541  1.00 30.50
ATOM   4177  N   GLY L 263     -13.945  52.730  80.375  1.00 28.61
ATOM   4178  CA  GLY L 263     -14.631  53.978  80.680  1.00 27.55
ATOM   4179  C   GLY L 263     -15.182  54.648  79.444  1.00 28.84
ATOM   4180  O   GLY L 263     -14.541  54.649  78.383  1.00 29.55
ATOM   4184  N   LEU L 264     -16.391  55.194  79.575  1.00 28.00
ATOM   4185  CA  LEU L 264     -17.014  55.987  78.514  1.00 27.05
ATOM   4186  C   LEU L 264     -17.367  57.365  79.039  1.00 27.93
ATOM   4187  O   LEU L 264     -17.428  57.579  80.255  1.00 27.73
ATOM   4188  CB  LEU L 264     -18.269  55.301  78.002  1.00 27.82
ATOM   4189  CG  LEU L 264     -17.985  53.952  77.329  1.00 29.22
ATOM   4190  CD1 LEU L 264     -19.288  53.253  77.045  1.00 27.34
ATOM   4191  CD2 LEU L 264     -17.166  54.123  76.051  1.00 29.80
ATOM   4203  N   LEU L 265     -17.603  58.301  78.122  1.00 27.16
ATOM   4204  CA  LEU L 265     -17.938  59.662  78.519  1.00 28.36
ATOM   4205  C   LEU L 265     -19.425  59.859  78.403  1.00 26.33
ATOM   4206  O   LEU L 265     -20.079  59.235  77.561  1.00 25.71
ATOM   4207  CB  LEU L 265     -17.219  60.691  77.653  1.00 29.19
ATOM   4208  CG  LEU L 265     -15.700  60.725  77.721  1.00 31.06
ATOM   4209  CD1 LEU L 265     -15.172  61.746  76.716  1.00 33.04
ATOM   4210  CD2 LEU L 265     -15.231  61.041  79.136  1.00 32.38
ATOM   4222  N   VAL L 266     -19.948  60.724  79.260  1.00 24.48
ATOM   4223  CA  VAL L 266     -21.345  61.111  79.211  1.00 25.54
ATOM   4224  C   VAL L 266     -21.408  62.635  79.273  1.00 26.65
ATOM   4225  O   VAL L 266     -20.882  63.271  80.193  1.00 26.79
ATOM   4226  CB  VAL L 266     -22.188  60.434  80.331  1.00 24.68
ATOM   4227  CG1 VAL L 266     -21.650  60.752  81.718  1.00 25.08
ATOM   4228  CG2 VAL L 266     -23.642  60.853  80.215  1.00 25.35
ATOM   4238  N   ASN L 267     -22.015  63.211  78.249  1.00 29.25
ATOM   4239  CA  ASN L 267     -21.921  64.640  77.985  1.00 29.90
ATOM   4240  C   ASN L 267     -20.512  65.148  78.209  1.00 31.28
ATOM   4241  O   ASN L 267     -20.308  66.117  78.912  1.00 31.77
ATOM   4242  CB  ASN L 267     -22.932  65.408  78.824  1.00 30.00
ATOM   4243  CG  ASN L 267     -24.362  64.995  78.525  1.00 30.05
ATOM   4244  ND2 ASN L 267     -25.271  65.326  79.426  1.00 32.28
ATOM   4245  OD1 ASN L 267     -24.639  64.348  77.519  1.00 28.65
ATOM   4252  N   GLN L 268     -19.548  64.454  77.611  1.00 33.50
ATOM   4253  CA  GLN L 268     -18.124  64.848  77.630  1.00 37.88
ATOM   4254  C   GLN L 268     -17.411  64.709  78.965  1.00 35.17
ATOM   4255  O   GLN L 268     -16.242  65.067  79.062  1.00 36.77
ATOM   4256  CB  GLN L 268     -17.924  66.294  77.140  1.00 42.66
ATOM   4257  CG  GLN L 268     -18.535  66.593  75.787  1.00 49.02
ATOM   4258  CD  GLN L 268     -17.993  65.688  74.706  1.00 53.82
ATOM   4259  NE2 GLN L 268     -16.788  65.439  74.632  1.00 58.48
ATOM   4260  OE1 GLN L 268     -18.885  65.182  73.862  1.00 55.67
ATOM   4269  N   THR L 269     -18.072  64.176  79.979  1.00 32.96
ATOM   4270  CA  THR L 269     -17.419  64.024  81.269  1.00 33.74
ATOM   4271  C   THR L 269     -17.684  62.637  81.883  1.00 30.64
ATOM   4272  O   THR L 269     -18.286  61.769  81.265  1.00 30.52
ATOM   4273  CB  THR L 269     -17.781  65.208  82.199  1.00 34.95
ATOM   4274  CG2 THR L 269     -19.288  65.256  82.499  1.00 33.74
ATOM   4275  OG1 THR L 269     -17.027  65.126  83.417  1.00 37.70
ATOM   4283  N   GLU L 270     -17.199  62.432  83.092  1.00 31.42
ATOM   4284  CA  GLU L 270     -17.245  61.119  83.741  1.00 31.86
ATOM   4285  C   GLU L 270     -18.611  60.794  84.323  1.00 28.39
ATOM   4286  O   GLU L 270     -19.112  59.692  84.172  1.00 28.30
ATOM   4287  CB  GLU L 270     -16.234  61.100  84.881  1.00 37.65
ATOM   4288  CG  GLU L 270     -14.786  61.210  84.447  1.00 44.82
ATOM   4289  CD  GLU L 270     -14.167  59.845  84.345  1.00 52.16
ATOM   4290  OE1 GLU L 270     -13.163  59.578  85.041  1.00 55.69
ATOM   4291  OE2 GLU L 270     -14.729  59.027  83.593  1.00 57.62
ATOM   4298  N   LEU L 271     -19.186  61.759  85.023  1.00 28.43
ATOM   4299  CA  LEU L 271     -20.378  61.541  85.820  1.00 29.76
ATOM   4300  C   LEU L 271     -21.535  62.315  85.226  1.00 29.39
ATOM   4301  O   LEU L 271     -21.348  63.397  84.671  1.00 30.49
ATOM   4302  CB  LEU L 271     -20.133  62.012  87.251  1.00 32.26
ATOM   4303  CG  LEU L 271     -19.131  61.229  88.105  1.00 34.29
ATOM   4304  CD1 LEU L 271     -18.905  61.961  89.417  1.00 35.80
ATOM   4305  CD2 LEU L 271     -19.613  59.811  88.371  1.00 34.28
ATOM   4317  N   PHE L 272     -22.728  61.754  85.354  1.00 29.15
ATOM   4318  CA  PHE L 272     -23.956  62.392  84.871  1.00 29.91
ATOM   4319  C   PHE L 272     -24.945  62.478  86.012  1.00 29.48
ATOM   4320  O   PHE L 272     -25.237  61.467  86.656  1.00 28.64
ATOM   4321  CB  PHE L 272     -24.594  61.596  83.726  1.00 27.74
ATOM   4322  CG  PHE L 272     -25.966  62.106  83.337  1.00 29.30
ATOM   4323  CD1 PHE L 272     -26.099  63.294  82.624  1.00 29.63
ATOM   4324  CD2 PHE L 272     -27.111  61.418  83.711  1.00 28.47
ATOM   4325  CE1 PHE L 272     -27.345  63.770  82.284  1.00 30.88
ATOM   4326  CE2 PHE L 272     -28.360  61.892  83.379  1.00 31.42
ATOM   4327  CZ  PHE L 272     -28.479  63.073  82.668  1.00 32.28
ATOM   4337  N   VAL L 273     -25.458  63.681  86.247  1.00 31.94
ATOM   4338  CA  VAL L 273     -26.408  63.933  87.326  1.00 33.33
ATOM   4339  C   VAL L 273     -27.707  64.477  86.741  1.00 33.32
ATOM   4340  O   VAL L 273     -27.694  65.542  86.143  1.00 35.29
ATOM   4341  CB  VAL L 273     -25.841  64.954  88.332  1.00 34.69
ATOM   4342  CG1 VAL L 273     -26.824  65.182  89.476  1.00 35.14
ATOM   4343  CG2 VAL L 273     -24.497  64.483  88.844  1.00 34.37
ATOM   4353  N   PRO L 274     -28.826  63.744  86.901  1.00 33.23
ATOM   4354  CA  PRO L 274     -30.106  64.251  86.389  1.00 34.02
ATOM   4355  C   PRO L 274     -30.548  65.521  87.086  1.00 34.97
ATOM   4356  O   PRO L 274     -30.434  65.648  88.310  1.00 34.49
ATOM   4357  CB  PRO L 274     -31.085  63.111  86.691  1.00 34.27
ATOM   4358  CG  PRO L 274     -30.233  61.892  86.716  1.00 33.57
ATOM   4359  CD  PRO L 274     -28.953  62.348  87.360  1.00 32.72
ATOM   4367  N   SER L 275     -31.041  66.451  86.290  1.00 36.95
ATOM   4368  CA  SER L 275     -31.450  67.760  86.760  1.00 40.19
ATOM   4369  C   SER L 275     -32.957  67.903  86.550  1.00 41.33
ATOM   4370  O   SER L 275     -33.610  66.996  86.025  1.00 40.54
ATOM   4371  CB  SER L 275     -30.696  68.824  85.974  1.00 39.92
ATOM   4372  OG  SER L 275     -30.777  68.541  84.592  1.00 40.81
ATOM   4378  N   LEU L 276     -33.494  69.040  86.984  1.00 43.20
ATOM   4379  CA  LEU L 276     -34.895  69.394  86.791  1.00 44.75
ATOM   4380  C   LEU L 276     -35.218  69.571  85.303  1.00 45.97
ATOM   4381  O   LEU L 276     -34.456  70.200  84.568  1.00 45.55
ATOM   4382  CB  LEU L 276     -35.189  70.700  87.534  1.00 47.01
ATOM   4383  CG  LEU L 276     -36.616  71.234  87.484  1.00 49.20
ATOM   4384  CD1 LEU L 276     -37.529  70.353  88.321  1.00 48.63
ATOM   4385  CD2 LEU L 276     -36.662  72.683  87.956  1.00 52.50
ATOM   4397  N   ASN L 277     -36.364  69.040  84.882  1.00 48.36
ATOM   4398  CA  ASN L 277     -36.802  69.090  83.480  1.00 50.41
ATOM   4399  C   ASN L 277     -37.395  70.441  83.083  1.00 55.69
ATOM   4400  O   ASN L 277     -38.310  70.923  83.730  1.00 55.15
ATOM   4401  CB  ASN L 277     -37.822  67.989  83.233  1.00 48.84
ATOM   4402  CG  ASN L 277     -37.212  66.611  83.335  1.00 47.06
ATOM   4403  ND2 ASN L 277     -36.397  66.255  82.362  1.00 45.78
ATOM   4404  OD1 ASN L 277     -37.460  65.883  84.287  1.00 50.13
ATOM   4411  N   VAL L 278     -36.888  71.028  81.998  1.00 66.74
ATOM   4412  CA  VAL L 278     -37.169  72.437  81.656  1.00 75.55
ATOM   4413  C   VAL L 278     -38.596  72.726  81.189  1.00 81.86
ATOM   4414  O   VAL L 278     -39.131  73.789  81.485  1.00 93.96
ATOM   4415  CB  VAL L 278     -36.175  72.983  80.589  1.00 80.59
ATOM   4416  CG1 VAL L 278     -36.489  72.440  79.198  1.00 83.58
ATOM   4417  CG2 VAL L 278     -36.170  74.510  80.567  1.00 85.38
ATOM   4427  N   ASP L 279     -39.204  71.804  80.453  1.00 79.23
ATOM   4428  CA  ASP L 279     -40.525  72.047  79.874  1.00 81.87
ATOM   4429  C   ASP L 279     -41.126  70.739  79.395  1.00 81.65
ATOM   4430  O   ASP L 279     -41.568  70.625  78.253  1.00 85.86
ATOM   4431  CB  ASP L 279     -40.415  73.034  78.706  1.00 83.99
ATOM   4432  CG  ASP L 279     -41.738  73.632  78.205  1.00  0.00
ATOM   4433  OD1 ASP L 279     -42.697  73.710  79.002  1.00  0.00
ATOM   4434  OD2 ASP L 279     -41.765  74.029  77.021  1.00  0.00
ATOM   4439  N   GLY L 280     -41.118  69.741  80.275  1.00 82.24
ATOM   4440  CA  GLY L 280     -41.422  68.370  79.882  1.00 77.48
ATOM   4441  C   GLY L 280     -40.284  67.706  79.112  1.00 72.64
ATOM   4442  O   GLY L 280     -40.272  66.485  78.979  1.00 74.30
ATOM   4446  N   GLN L 281     -39.336  68.501  78.600  1.00 65.46
ATOM   4447  CA  GLN L 281     -38.153  67.978  77.919  1.00 56.90
ATOM   4448  C   GLN L 281     -37.361  67.073  78.847  1.00 51.08
ATOM   4449  O   GLN L 281     -37.057  67.462  79.982  1.00 48.27
ATOM   4450  CB  GLN L 281     -37.216  69.103  77.483  1.00 57.66
ATOM   4451  CG  GLN L 281     -37.606  69.843  76.221  1.00 61.49
ATOM   4452  CD  GLN L 281     -36.496  70.760  75.737  1.00 63.62
ATOM   4453  NE2 GLN L 281     -36.872  71.952  75.306  1.00 69.56
ATOM   4454  OE1 GLN L 281     -35.315  70.401  75.752  1.00 59.62
ATOM   4463  N   PRO L 282     -37.002  65.874  78.362  1.00 44.78
ATOM   4464  CA  PRO L 282     -36.132  65.026  79.138  1.00 41.76
ATOM   4465  C   PRO L 282     -34.702  65.535  78.996  1.00 40.00
ATOM   4466  O   PRO L 282     -34.398  66.293  78.059  1.00 40.48
ATOM   4467  CB  PRO L 282     -36.310  63.658  78.482  1.00 40.06
ATOM   4468  CG  PRO L 282     -36.569  63.978  77.056  1.00 41.84
ATOM   4469  CD  PRO L 282     -37.279  65.304  77.033  1.00 44.53
ATOM   4477  N   ILE L 283     -33.851  65.135  79.930  1.00 36.91
ATOM   4478  CA  ILE L 283     -32.459  65.536  79.934  1.00 36.86
ATOM   4479  C   ILE L 283     -31.694  64.522  79.107  1.00 35.32
ATOM   4480  O   ILE L 283     -31.752  63.327  79.387  1.00 32.02
ATOM   4481  CB  ILE L 283     -31.856  65.519  81.367  1.00 38.52
ATOM   4482  CG1 ILE L 283     -32.712  66.318  82.370  1.00 41.53
ATOM   4483  CG2 ILE L 283     -30.414  66.017  81.339  1.00 38.22
ATOM   4484  CD1 ILE L 283     -32.940  67.776  82.009  1.00 44.05
ATOM   4496  N   PHE L 284     -30.960  64.982  78.104  1.00 35.44
ATOM   4497  CA  PHE L 284     -30.127  64.076  77.312  1.00 34.58
ATOM   4498  C   PHE L 284     -28.816  63.710  77.974  1.00 33.25
ATOM   4499  O   PHE L 284     -28.060  64.585  78.371  1.00 34.87
ATOM   4500  CB  PHE L 284     -29.847  64.668  75.930  1.00 36.29
ATOM   4501  CG  PHE L 284     -30.539  63.941  74.839  1.00 37.17
ATOM   4502  CD1 PHE L 284     -31.886  64.107  74.631  1.00 40.17
ATOM   4503  CD2 PHE L 284     -29.846  63.046  74.061  1.00 39.36
ATOM   4504  CE1 PHE L 284     -32.528  63.412  73.634  1.00 42.66
ATOM   4505  CE2 PHE L 284     -30.470  62.350  73.061  1.00 39.56
ATOM   4506  CZ  PHE L 284     -31.811  62.529  72.850  1.00 41.75
ATOM   4516  N   ALA L 285     -28.555  62.408  78.080  1.00 31.34
ATOM   4517  CA  ALA L 285     -27.257  61.897  78.483  1.00 30.56
ATOM   4518  C   ALA L 285     -26.613  61.252  77.265  1.00 31.81
ATOM   4519  O   ALA L 285     -26.921  60.107  76.914  1.00 32.92
ATOM   4520  CB  ALA L 285     -27.391  60.880  79.608  1.00 29.63
ATOM   4526  N   ASN L 286     -25.736  62.002  76.614  1.00 32.47
ATOM   4527  CA  ASN L 286     -25.047  61.527  75.421  1.00 33.61
ATOM   4528  C   ASN L 286     -23.789  60.790  75.793  1.00 28.89
ATOM   4529  O   ASN L 286     -22.856  61.392  76.291  1.00 30.47
ATOM   4530  CB  ASN L 286     -24.703  62.693  74.503  1.00 36.32
ATOM   4531  CG  ASN L 286     -25.933  63.248  73.812  1.00 45.31
ATOM   4532  ND2 ASN L 286     -26.139  64.551  73.917  1.00 46.43
ATOM   4533  OD1 ASN L 286     -26.691  62.504  73.188  1.00 50.39
ATOM   4540  N   ILE L 287     -23.785  59.490  75.527  1.00 27.39
ATOM   4541  CA  ILE L 287     -22.699  58.596  75.885  1.00 26.65
ATOM   4542  C   ILE L 287     -21.844  58.340  74.646  1.00 27.70
ATOM   4543  O   ILE L 287     -22.368  57.917  73.624  1.00 25.81
ATOM   4544  CB  ILE L 287     -23.241  57.251  76.388  1.00 26.00
ATOM   4545  CG1 ILE L 287     -24.276  57.476  77.501  1.00 27.88
ATOM   4546  CG2 ILE L 287     -22.101  56.372  76.872  1.00 25.50
ATOM   4547  CD1 ILE L 287     -25.335  56.398  77.561  1.00 29.67
ATOM   4559  N   THR L 288     -20.536  58.593  74.763  1.00 28.88
ATOM   4560  CA  THR L 288     -19.613  58.545  73.633  1.00 30.53
ATOM   4561  C   THR L 288     -18.331  57.822  74.020  1.00 29.81
ATOM   4562  O   THR L 288     -18.016  57.699  75.214  1.00 27.25
ATOM   4563  CB  THR L 288     -19.261  59.976  73.137  1.00 32.39
ATOM   4564  CG2 THR L 288     -20.494  60.687  72.579  1.00 34.09
ATOM   4565  OG1 THR L 288     -18.737  60.759  74.219  1.00 34.96
ATOM   4573  N   LEU L 289     -17.591  57.328  73.023  1.00 28.48
ATOM   4574  CA  LEU L 289     -16.215  56.905  73.281  1.00 29.17
ATOM   4575  C   LEU L 289     -15.384  58.123  73.649  1.00 28.05
ATOM   4576  O   LEU L 289     -15.475  59.158  72.993  1.00 28.27
ATOM   4577  CB  LEU L 289     -15.534  56.311  72.057  1.00 30.00
ATOM   4578  CG  LEU L 289     -15.778  54.901  71.556  1.00 32.50
ATOM   4579  CD1 LEU L 289     -14.838  54.660  70.374  1.00 33.79
ATOM   4580  CD2 LEU L 289     -15.587  53.851  72.626  1.00 30.78
ATOM   4592  N   PRO L 290     -14.526  57.988  74.656  1.00 27.14
ATOM   4593  CA  PRO L 290     -13.456  58.957  74.736  1.00 28.15
ATOM   4594  C   PRO L 290     -12.465  58.740  73.604  1.00 27.10
ATOM   4595  O   PRO L 290     -12.473  57.693  72.963  1.00 26.07
ATOM   4596  CB  PRO L 290     -12.772  58.634  76.073  1.00 29.07
ATOM   4597  CG  PRO L 290     -13.503  57.474  76.660  1.00 28.85
ATOM   4598  CD  PRO L 290     -14.322  56.865  75.576  1.00 27.79
ATOM   4606  N   VAL L 291     -11.613  59.727  73.387  1.00 28.04
ATOM   4607  CA  VAL L 291     -10.412  59.527  72.615  1.00 29.09
ATOM   4608  C   VAL L 291      -9.410  58.888  73.566  1.00 29.95
ATOM   4609  O   VAL L 291      -8.703  59.582  74.292  1.00 30.64
ATOM   4610  CB  VAL L 291      -9.850  60.850  72.068  1.00 31.17
ATOM   4611  CG1 VAL L 291      -8.584  60.609  71.254  1.00 32.56
ATOM   4612  CG2 VAL L 291     -10.894  61.560  71.235  1.00 32.60
ATOM   4622  N   TYR L 292      -9.365  57.559  73.583  1.00 28.18
ATOM   4623  CA  TYR L 292      -8.406  56.867  74.412  1.00 28.48
ATOM   4624  C   TYR L 292      -6.979  57.223  73.998  1.00 29.43
ATOM   4625  O   TYR L 292      -6.730  57.601  72.846  1.00 30.30
ATOM   4626  CB  TYR L 292      -8.617  55.351  74.321  1.00 28.35
ATOM   4627  CG  TYR L 292      -9.963  54.860  74.837  1.00 28.60
ATOM   4628  CD1 TYR L 292     -10.302  54.958  76.196  1.00 28.51
ATOM   4629  CD2 TYR L 292     -10.877  54.263  73.982  1.00 27.11
ATOM   4630  CE1 TYR L 292     -11.519  54.489  76.668  1.00 25.99
ATOM   4631  CE2 TYR L 292     -12.094  53.800  74.449  1.00 27.91
ATOM   4632  CZ  TYR L 292     -12.405  53.907  75.794  1.00 26.73
ATOM   4633  OH  TYR L 292     -13.633  53.451  76.232  1.00 26.93
ATOM   4643  N   THR L 293      -6.030  57.108  74.927  1.00 31.09
ATOM   4644  CA  THR L 293      -4.622  57.217  74.542  1.00 32.52
ATOM   4645  C   THR L 293      -4.336  55.995  73.692  1.00 31.09
ATOM   4646  O   THR L 293      -5.016  54.964  73.822  1.00 29.44
ATOM   4647  CB  THR L 293      -3.651  57.188  75.721  1.00 34.99
ATOM   4648  CG2 THR L 293      -3.954  58.315  76.709  1.00 37.27
ATOM   4649  OG1 THR L 293      -3.720  55.908  76.360  1.00 34.71
ATOM   4657  N   LEU L 294      -3.331  56.093  72.838  1.00 29.82
ATOM   4658  CA  LEU L 294      -2.999  54.979  71.980  1.00 29.15
ATOM   4659  C   LEU L 294      -2.681  53.761  72.837  1.00 29.97
ATOM   4660  O   LEU L 294      -3.152  52.654  72.550  1.00 28.16
ATOM   4661  CB  LEU L 294      -1.837  55.337  71.070  1.00 29.70
ATOM   4662  CG  LEU L 294      -1.384  54.223  70.126  1.00 30.74
ATOM   4663  CD1 LEU L 294      -2.531  53.791  69.228  1.00 29.38
ATOM   4664  CD2 LEU L 294      -0.182  54.670  69.303  1.00 32.62
ATOM   4676  N   LYS L 295      -1.918  53.986  73.911  1.00 32.01
ATOM   4677  CA  LYS L 295      -1.552  52.923  74.847  1.00 33.17
ATOM   4678  C   LYS L 295      -2.775  52.227  75.441  1.00 31.61
ATOM   4679  O   LYS L 295      -2.854  50.993  75.421  1.00 29.50
ATOM   4680  CB  LYS L 295      -0.678  53.477  75.979  1.00 36.24
ATOM   4681  CG  LYS L 295      -0.194  52.408  76.934  1.00 38.64
ATOM   4682  CD  LYS L 295       0.579  53.001  78.097  1.00 42.88
ATOM   4683  CE  LYS L 295       0.987  51.911  79.072  1.00 45.68
ATOM   4684  NZ  LYS L 295       1.842  52.425  80.177  1.00 50.19
ATOM   4698  N   GLU L 296      -3.726  53.003  75.966  1.00 32.36
ATOM   4699  CA  GLU L 296      -4.957  52.398  76.511  1.00 32.92
ATOM   4700  C   GLU L 296      -5.687  51.609  75.440  1.00 30.02
ATOM   4701  O   GLU L 296      -6.140  50.476  75.666  1.00 28.96
ATOM   4702  CB  GLU L 296      -5.908  53.435  77.126  1.00 34.83
ATOM   4703  CG  GLU L 296      -7.056  52.787  77.921  1.00 39.38
ATOM   4704  CD  GLU L 296      -6.587  51.697  78.900  1.00 43.47
ATOM   4705  OE1 GLU L 296      -5.582  51.950  79.594  1.00 47.42
ATOM   4706  OE2 GLU L 296      -7.201  50.593  78.978  1.00 38.31
ATOM   4713  N   ARG L 297      -5.787  52.193  74.256  1.00 28.14
ATOM   4714  CA  ARG L 297      -6.426  51.482  73.167  1.00 26.38
ATOM   4715  C   ARG L 297      -5.705  50.162  72.859  1.00 25.81
ATOM   4716  O   ARG L 297      -6.349  49.139  72.716  1.00 24.51
ATOM   4717  CB  ARG L 297      -6.542  52.359  71.929  1.00 25.97
ATOM   4718  CG  ARG L 297      -7.352  51.733  70.819  1.00 25.03
ATOM   4719  CD  ARG L 297      -8.775  51.411  71.187  1.00 24.32
ATOM   4720  NE  ARG L 297      -9.296  50.601  70.108  1.00 25.29
ATOM   4721  CZ  ARG L 297      -9.999  49.480  70.226  1.00 25.57
ATOM   4722  NH1 ARG L 297     -10.420  49.013  71.403  1.00 25.08
ATOM   4723  NH2 ARG L 297     -10.350  48.852  69.112  1.00 26.77
ATOM   4737  N   CYS L 298      -4.377  50.179  72.799  1.00 27.46
ATOM   4738  CA  CYS L 298      -3.617  48.957  72.574  1.00 28.36
ATOM   4739  C   CYS L 298      -3.839  47.946  73.714  1.00 30.43
ATOM   4740  O   CYS L 298      -3.983  46.740  73.485  1.00 31.45
ATOM   4741  CB  CYS L 298      -2.119  49.277  72.417  1.00 30.61
ATOM   4742  SG  CYS L 298      -1.676  50.108  70.857  1.00 30.66
ATOM   4748  N   LEU L 299      -3.893  48.416  74.952  1.00 30.75
ATOM   4749  CA  LEU L 299      -4.137  47.499  76.047  1.00 32.56
ATOM   4750  C   LEU L 299      -5.507  46.854  75.873  1.00 34.65
ATOM   4751  O   LEU L 299      -5.653  45.646  76.108  1.00 35.86
ATOM   4752  CB  LEU L 299      -4.037  48.208  77.403  1.00 32.67
ATOM   4753  CG  LEU L 299      -2.623  48.655  77.798  1.00 35.40
ATOM   4754  CD1 LEU L 299      -2.648  49.667  78.932  1.00 36.38
ATOM   4755  CD2 LEU L 299      -1.740  47.477  78.168  1.00 36.84
ATOM   4767  N   GLN L 300      -6.501  47.649  75.455  1.00 33.41
ATOM   4768  CA  GLN L 300      -7.851  47.120  75.217  1.00 30.87
ATOM   4769  C   GLN L 300      -7.810  45.990  74.212  1.00 31.60
ATOM   4770  O   GLN L 300      -8.376  44.921  74.446  1.00 31.18
ATOM   4771  CB  GLN L 300      -8.808  48.194  74.704  1.00 28.19
ATOM   4772  CG  GLN L 300      -9.321  49.151  75.767  1.00 26.29
ATOM   4773  CD  GLN L 300     -10.076  50.325  75.171  1.00 25.38
ATOM   4774  NE2 GLN L 300     -10.291  51.348  75.981  1.00 24.99
ATOM   4775  OE1 GLN L 300     -10.446  50.324  73.986  1.00 25.39
ATOM   4784  N   VAL L 301      -7.108  46.210  73.105  1.00 32.61
ATOM   4785  CA  VAL L 301      -7.081  45.218  72.044  1.00 33.86
ATOM   4786  C   VAL L 301      -6.295  43.983  72.486  1.00 37.76
ATOM   4787  O   VAL L 301      -6.737  42.863  72.242  1.00 39.64
ATOM   4788  CB  VAL L 301      -6.540  45.782  70.720  1.00 32.99
ATOM   4789  CG1 VAL L 301      -6.398  44.673  69.691  1.00 35.69
ATOM   4790  CG2 VAL L 301      -7.479  46.844  70.192  1.00 31.80
ATOM   4800  N   VAL L 302      -5.154  44.170  73.143  1.00 39.69
ATOM   4801  CA  VAL L 302      -4.371  43.017  73.584  1.00 42.92
ATOM   4802  C   VAL L 302      -5.252  42.206  74.556  1.00 46.19
ATOM   4803  O   VAL L 302      -5.465  41.013  74.335  1.00 48.80
ATOM   4804  CB  VAL L 302      -3.007  43.417  74.201  1.00 43.73
ATOM   4805  CG1 VAL L 302      -2.300  42.216  74.829  1.00 44.89
ATOM   4806  CG2 VAL L 302      -2.100  44.034  73.142  1.00 44.13
ATOM   4816  N   ARG L 303      -5.825  42.868  75.567  1.00 44.47
ATOM   4817  CA  ARG L 303      -6.691  42.193  76.553  1.00 45.62
ATOM   4818  C   ARG L 303      -7.794  41.373  75.901  1.00 47.64
ATOM   4819  O   ARG L 303      -8.167  40.332  76.430  1.00 49.13
ATOM   4820  CB  ARG L 303      -7.342  43.191  77.518  1.00 41.42
ATOM   4821  CG  ARG L 303      -6.410  43.811  78.540  1.00 40.70
ATOM   4822  CD  ARG L 303      -7.165  44.797  79.408  1.00 38.65
ATOM   4823  NE  ARG L 303      -6.279  45.678  80.172  1.00 38.79
ATOM   4824  CZ  ARG L 303      -6.357  47.013  80.199  1.00 38.86
ATOM   4825  NH1 ARG L 303      -7.295  47.668  79.510  1.00 36.62
ATOM   4826  NH2 ARG L 303      -5.496  47.714  80.936  1.00 38.12
ATOM   4840  N   SER L 304      -8.325  41.841  74.772  1.00 46.64
ATOM   4841  CA  SER L 304      -9.396  41.123  74.077  1.00 47.88
ATOM   4842  C   SER L 304      -8.902  39.847  73.375  1.00 52.49
ATOM   4843  O   SER L 304      -9.680  38.935  73.128  1.00 56.41
ATOM   4844  CB  SER L 304     -10.092  42.036  73.069  1.00 45.18
ATOM   4845  OG  SER L 304      -9.282  42.243  71.919  1.00 47.61
ATOM   4851  N   LEU L 305      -7.613  39.787  73.061  1.00 54.92
ATOM   4852  CA  LEU L 305      -7.059  38.684  72.279  1.00 59.85
ATOM   4853  C   LEU L 305      -6.391  37.622  73.142  1.00 63.28
ATOM   4854  O   LEU L 305      -6.339  36.453  72.767  1.00 64.40
ATOM   4855  CB  LEU L 305      -6.039  39.221  71.275  1.00 59.95
ATOM   4856  CG  LEU L 305      -6.596  40.129  70.180  1.00 59.11
ATOM   4857  CD1 LEU L 305      -5.476  40.917  69.520  1.00 59.56
ATOM   4858  CD2 LEU L 305      -7.369  39.332  69.138  1.00 60.24
ATOM   4870  N   VAL L 306      -5.863  38.041  74.284  1.00 65.16
ATOM   4871  CA  VAL L 306      -5.120  37.162  75.161  1.00 71.46
ATOM   4872  C   VAL L 306      -5.961  36.862  76.402  1.00 76.79
ATOM   4873  O   VAL L 306      -6.572  37.765  76.981  1.00 70.84
ATOM   4874  CB  VAL L 306      -3.796  37.828  75.579  1.00 74.00
ATOM   4875  CG1 VAL L 306      -2.972  36.897  76.450  1.00 74.38
ATOM   4876  CG2 VAL L 306      -3.004  38.244  74.343  1.00 77.97
ATOM   4886  N   LYS L 307      -6.005  35.591  76.799  1.00 82.81
ATOM   4887  CA  LYS L 307      -6.647  35.214  78.057  1.00 82.57
ATOM   4888  C   LYS L 307      -5.742  35.620  79.222  1.00 79.61
ATOM   4889  O   LYS L 307      -4.521  35.498  79.125  1.00 86.20
ATOM   4890  CB  LYS L 307      -6.973  33.720  78.100  1.00 86.06
ATOM   4891  CG  LYS L 307      -8.198  33.353  77.271  1.00 86.54
ATOM   4892  CD  LYS L 307      -8.931  32.142  77.837  1.00 91.23
ATOM   4893  CE  LYS L 307      -8.259  30.838  77.443  1.00 93.88
ATOM   4894  NZ  LYS L 307      -8.361  30.572  75.977  1.00 92.60
ATOM   4908  N   PRO L 308      -6.339  36.104  80.327  1.00 73.15
ATOM   4909  CA  PRO L 308      -5.589  36.756  81.415  1.00 71.92
ATOM   4910  C   PRO L 308      -4.430  35.958  82.026  1.00 75.91
ATOM   4911  O   PRO L 308      -3.543  36.544  82.660  1.00 73.56
ATOM   4912  CB  PRO L 308      -6.673  37.020  82.480  1.00 70.71
ATOM   4913  CG  PRO L 308      -7.965  37.006  81.736  1.00 67.57
ATOM   4914  CD  PRO L 308      -7.781  36.010  80.637  1.00 70.46
ATOM   4922  N   GLU L 309      -4.444  34.638  81.855  1.00 78.93
ATOM   4923  CA  GLU L 309      -3.358  33.793  82.334  1.00 84.91
ATOM   4924  C   GLU L 309      -2.017  34.088  81.638  1.00 89.12
ATOM   4925  O   GLU L 309      -0.960  33.859  82.223  1.00 92.96
ATOM   4926  CB  GLU L 309      -3.727  32.317  82.153  1.00 84.99
ATOM   4927  CG  GLU L 309      -5.138  31.893  82.621  1.00  0.00
ATOM   4928  CD  GLU L 309      -6.206  32.024  81.537  1.00  0.00
ATOM   4929  OE1 GLU L 309      -6.044  31.378  80.479  1.00  0.00
ATOM   4930  OE2 GLU L 309      -7.159  32.792  81.771  1.00  0.00
ATOM   4937  N   ASN L 310      -2.065  34.623  80.414  1.00 87.96
ATOM   4938  CA  ASN L 310      -0.885  34.700  79.541  1.00 87.95
ATOM   4939  C   ASN L 310      -0.105  36.020  79.540  1.00 84.87
ATOM   4940  O   ASN L 310       1.016  36.056  79.036  1.00 87.11
ATOM   4941  CB  ASN L 310      -1.294  34.409  78.091  1.00 87.46
ATOM   4942  CG  ASN L 310      -2.266  33.249  77.968  1.00 89.87
ATOM   4943  ND2 ASN L 310      -2.109  32.246  78.819  1.00 93.37
ATOM   4944  OD1 ASN L 310      -3.149  33.259  77.112  1.00 88.67
ATOM   4951  N   TYR L 311      -0.685  37.094  80.081  1.00 79.63
ATOM   4952  CA  TYR L 311      -0.101  38.451  79.963  1.00 77.40
ATOM   4953  C   TYR L 311       1.394  38.506  80.346  1.00 81.01
ATOM   4954  O   TYR L 311       2.219  39.142  79.670  1.00 73.48
ATOM   4955  CB  TYR L 311      -0.881  39.483  80.812  1.00 74.11
ATOM   4956  CG  TYR L 311      -2.381  39.652  80.529  1.00 68.46
ATOM   4957  CD1 TYR L 311      -2.990  39.128  79.380  1.00 64.81
ATOM   4958  CD2 TYR L 311      -3.184  40.372  81.420  1.00 67.13
ATOM   4959  CE1 TYR L 311      -4.351  39.302  79.140  1.00 61.72
ATOM   4960  CE2 TYR L 311      -4.540  40.559  81.190  1.00 62.00
ATOM   4961  CZ  TYR L 311      -5.128  40.026  80.056  1.00 61.80
ATOM   4962  OH  TYR L 311      -6.485  40.207  79.858  1.00 53.17
ATOM   4972  N   ARG L 312       1.727  37.815  81.432  1.00 85.14
ATOM   4973  CA  ARG L 312       3.097  37.738  81.945  1.00 83.07
ATOM   4974  C   ARG L 312       4.089  37.195  80.904  1.00 84.42
ATOM   4975  O   ARG L 312       5.266  37.563  80.901  1.00 84.97
ATOM   4976  CB  ARG L 312       3.118  36.847  83.200  1.00 86.34
ATOM   4977  CG  ARG L 312       2.388  37.433  84.408  1.00 83.42
ATOM   4978  CD  ARG L 312       3.312  38.366  85.169  1.00 83.43
ATOM   4979  NE  ARG L 312       2.604  39.398  85.921  1.00 80.06
ATOM   4980  CZ  ARG L 312       3.202  40.413  86.546  1.00 79.30
ATOM   4981  NH1 ARG L 312       4.527  40.544  86.522  1.00 84.67
ATOM   4982  NH2 ARG L 312       2.478  41.312  87.195  1.00 73.92
ATOM   4996  N   ARG L 313       3.604  36.324  80.022  1.00 81.19
ATOM   4997  CA  ARG L 313       4.432  35.679  79.010  1.00 78.23
ATOM   4998  C   ARG L 313       4.863  36.590  77.823  1.00 78.16
ATOM   4999  O   ARG L 313       5.763  36.225  77.071  1.00 79.83
ATOM   5000  CB  ARG L 313       3.684  34.445  78.489  1.00 75.05
ATOM   5001  CG  ARG L 313       3.146  33.511  79.594  1.00  0.00
ATOM   5002  CD  ARG L 313       2.325  32.333  79.053  1.00  0.00
ATOM   5003  NE  ARG L 313       1.405  31.831  80.085  1.00  0.00
ATOM   5004  CZ  ARG L 313       0.520  30.834  79.946  1.00  0.00
ATOM   5005  NH1 ARG L 313       0.435  30.135  78.810  1.00  0.00
ATOM   5006  NH2 ARG L 313      -0.296  30.548  80.964  1.00  0.00
ATOM   5020  N   LEU L 314       4.244  37.762  77.661  1.00 74.94
ATOM   5021  CA  LEU L 314       4.457  38.608  76.460  1.00 68.90
ATOM   5022  C   LEU L 314       5.849  39.249  76.408  1.00 69.40
ATOM   5023  O   LEU L 314       6.346  39.769  77.414  1.00 67.01
ATOM   5024  CB  LEU L 314       3.402  39.716  76.390  1.00 63.60
ATOM   5025  CG  LEU L 314       1.923  39.303  76.421  1.00 62.41
ATOM   5026  CD1 LEU L 314       1.052  40.526  76.687  1.00 59.10
ATOM   5027  CD2 LEU L 314       1.483  38.576  75.150  1.00 61.65
ATOM   5039  N   ASP L 315       6.483  39.228  75.240  1.00 68.86
ATOM   5040  CA  ASP L 315       7.839  39.753  75.143  1.00 73.87
ATOM   5041  C   ASP L 315       7.785  41.276  75.157  1.00 72.28
ATOM   5042  O   ASP L 315       7.985  41.915  74.124  1.00 75.22
ATOM   5043  CB  ASP L 315       8.562  39.231  73.892  1.00 75.43
ATOM   5044  CG  ASP L 315       8.616  37.707  73.803  1.00  0.00
ATOM   5045  OD1 ASP L 315       9.570  37.132  74.367  1.00  0.00
ATOM   5046  OD2 ASP L 315       7.703  37.135  73.171  1.00  0.00
ATOM   5051  N   ILE L 316       7.513  41.851  76.328  1.00 67.23
ATOM   5052  CA  ILE L 316       7.412  43.304  76.467  1.00 66.50
ATOM   5053  C   ILE L 316       7.981  43.824  77.787  1.00 68.58
ATOM   5054  O   ILE L 316       8.228  43.057  78.712  1.00 66.29
ATOM   5055  CB  ILE L 316       5.948  43.797  76.326  1.00 64.58
ATOM   5056  CG1 ILE L 316       5.053  43.253  77.455  1.00 62.96
ATOM   5057  CG2 ILE L 316       5.394  43.423  74.956  1.00 62.89
ATOM   5058  CD1 ILE L 316       3.684  43.909  77.520  1.00 59.73
ATOM   5070  N   VAL L 317       8.157  45.146  77.850  1.00 69.92
ATOM   5071  CA  VAL L 317       8.694  45.840  79.026  1.00 72.10
ATOM   5072  C   VAL L 317       7.834  45.544  80.260  1.00 70.99
ATOM   5073  O   VAL L 317       6.608  45.742  80.232  1.00 66.08
ATOM   5074  CB  VAL L 317       8.772  47.372  78.785  1.00 72.74
ATOM   5075  CG1 VAL L 317       8.992  48.137  80.090  1.00 76.89
ATOM   5076  CG2 VAL L 317       9.875  47.701  77.778  1.00 73.12
ATOM   5086  N   ARG L 318       8.484  45.110  81.344  1.00 67.92
ATOM   5087  CA  ARG L 318       7.768  44.554  82.495  1.00 67.89
ATOM   5088  C   ARG L 318       6.681  45.500  83.023  1.00 63.50
ATOM   5089  O   ARG L 318       5.630  45.064  83.476  1.00 60.07
ATOM   5090  CB  ARG L 318       8.743  44.170  83.621  1.00 72.14
ATOM   5091  CG  ARG L 318       9.847  43.204  83.204  1.00 76.88
ATOM   5092  CD  ARG L 318      10.479  42.448  84.375  1.00 81.51
ATOM   5093  NE  ARG L 318       9.603  41.368  84.836  1.00 81.59
ATOM   5094  CZ  ARG L 318       8.705  41.465  85.814  1.00 83.06
ATOM   5095  NH1 ARG L 318       8.550  42.594  86.504  1.00 84.69
ATOM   5096  NH2 ARG L 318       7.953  40.413  86.123  1.00 84.53
ATOM   5110  N   SER L 319       6.970  46.795  82.940  1.00 64.48
ATOM   5111  CA  SER L 319       6.059  47.884  83.277  1.00 62.47
ATOM   5112  C   SER L 319       4.655  47.693  82.693  1.00 59.51
ATOM   5113  O   SER L 319       3.651  47.938  83.372  1.00 54.43
ATOM   5114  CB  SER L 319       6.663  49.200  82.757  1.00 64.26
ATOM   5115  OG  SER L 319       6.025  50.332  83.313  1.00 66.51
ATOM   5121  N   LEU L 320       4.609  47.259  81.430  1.00 60.13
ATOM   5122  CA  LEU L 320       3.361  47.028  80.704  1.00 57.49
ATOM   5123  C   LEU L 320       2.530  45.842  81.251  1.00 57.32
ATOM   5124  O   LEU L 320       1.315  45.797  81.030  1.00 52.06
ATOM   5125  CB  LEU L 320       3.645  46.840  79.198  1.00 58.05
ATOM   5126  CG  LEU L 320       4.285  48.042  78.466  1.00 57.30
ATOM   5127  CD1 LEU L 320       4.824  47.663  77.094  1.00 56.99
ATOM   5128  CD2 LEU L 320       3.308  49.204  78.367  1.00 53.94
ATOM   5140  N   TYR L 321       3.162  44.900  81.961  1.00 57.72
ATOM   5141  CA  TYR L 321       2.418  43.768  82.545  1.00 58.95
ATOM   5142  C   TYR L 321       1.411  44.267  83.565  1.00 59.46
ATOM   5143  O   TYR L 321       0.244  43.868  83.560  1.00 54.52
ATOM   5144  CB  TYR L 321       3.336  42.780  83.263  1.00 62.54
ATOM   5145  CG  TYR L 321       4.448  42.196  82.439  1.00 61.85
ATOM   5146  CD1 TYR L 321       4.258  41.848  81.103  1.00 61.38
ATOM   5147  CD2 TYR L 321       5.687  41.969  83.010  1.00 63.00
ATOM   5148  CE1 TYR L 321       5.296  41.303  80.361  1.00 62.33
ATOM   5149  CE2 TYR L 321       6.721  41.421  82.285  1.00 64.97
ATOM   5150  CZ  TYR L 321       6.523  41.095  80.969  1.00 63.57
ATOM   5151  OH  TYR L 321       7.567  40.559  80.272  1.00 68.43
ATOM   5161  N   GLU L 322       1.905  45.122  84.460  1.00 64.10
ATOM   5162  CA  GLU L 322       1.070  45.856  85.410  1.00 65.56
ATOM   5163  C   GLU L 322      -0.125  46.465  84.677  1.00 59.96
ATOM   5164  O   GLU L 322      -1.275  46.282  85.084  1.00 54.12
ATOM   5165  CB  GLU L 322       1.876  46.985  86.073  1.00 69.03
ATOM   5166  CG  GLU L 322       1.524  47.235  87.530  1.00 72.66
ATOM   5167  CD  GLU L 322       2.228  46.274  88.470  1.00 78.01
ATOM   5168  OE1 GLU L 322       3.189  45.605  88.027  1.00 79.34
ATOM   5169  OE2 GLU L 322       1.827  46.191  89.654  1.00 82.64
ATOM   5176  N   ASP L 323       0.166  47.174  83.584  1.00 55.69
ATOM   5177  CA  ASP L 323      -0.854  47.929  82.855  1.00 52.95
ATOM   5178  C   ASP L 323      -1.977  47.011  82.374  1.00 50.03
ATOM   5179  O   ASP L 323      -3.146  47.315  82.594  1.00 48.62
ATOM   5180  CB  ASP L 323      -0.231  48.700  81.684  1.00 51.96
ATOM   5181  CG  ASP L 323       0.856  49.673  82.128  1.00 53.35
ATOM   5182  OD1 ASP L 323       0.870  50.074  83.306  1.00 56.68
ATOM   5183  OD2 ASP L 323       1.707  50.043  81.300  1.00 50.85
ATOM   5188  N   LEU L 324      -1.611  45.884  81.755  1.00 49.28
ATOM   5189  CA  LEU L 324      -2.588  44.895  81.276  1.00 49.33
ATOM   5190  C   LEU L 324      -3.470  44.327  82.383  1.00 53.96
ATOM   5191  O   LEU L 324      -4.686  44.228  82.218  1.00 55.09
ATOM   5192  CB  LEU L 324      -1.882  43.741  80.555  1.00 49.73
ATOM   5193  CG  LEU L 324      -1.312  44.093  79.170  1.00 50.96
ATOM   5194  CD1 LEU L 324      -0.249  43.090  78.733  1.00 54.54
ATOM   5195  CD2 LEU L 324      -2.415  44.188  78.123  1.00 46.70
ATOM   5207  N   GLU L 325      -2.852  43.928  83.497  1.00 57.08
ATOM   5208  CA  GLU L 325      -3.583  43.334  84.630  1.00 56.38
ATOM   5209  C   GLU L 325      -4.409  44.346  85.394  1.00 52.46
ATOM   5210  O   GLU L 325      -5.317  43.973  86.124  1.00 53.55
ATOM   5211  CB  GLU L 325      -2.617  42.634  85.605  1.00 59.15
ATOM   5212  CG  GLU L 325      -2.224  41.235  85.150  1.00 61.76
ATOM   5213  CD  GLU L 325      -1.048  40.650  85.908  1.00 65.89
ATOM   5214  OE1 GLU L 325      -0.348  41.404  86.623  1.00 65.79
ATOM   5215  OE2 GLU L 325      -0.817  39.428  85.763  1.00 67.18
ATOM   5222  N   ASP L 326      -4.076  45.620  85.257  1.00 52.26
ATOM   5223  CA  ASP L 326      -4.878  46.687  85.832  1.00 55.77
ATOM   5224  C   ASP L 326      -6.103  46.968  84.923  1.00 52.02
ATOM   5225  O   ASP L 326      -6.180  48.002  84.259  1.00 48.08
ATOM   5226  CB  ASP L 326      -3.994  47.926  86.023  1.00 60.58
ATOM   5227  CG  ASP L 326      -4.701  49.060  86.736  1.00 67.23
ATOM   5228  OD1 ASP L 326      -5.910  48.945  87.033  1.00 68.35
ATOM   5229  OD2 ASP L 326      -4.037  50.084  86.990  1.00 73.31
ATOM   5234  N   HIS L 327      -7.052  46.028  84.911  1.00 53.23
ATOM   5235  CA  HIS L 327      -8.264  46.119  84.083  1.00 51.40
ATOM   5236  C   HIS L 327      -9.095  47.316  84.502  1.00 45.95
ATOM   5237  O   HIS L 327      -9.156  47.635  85.689  1.00 42.23
ATOM   5238  CB  HIS L 327      -9.141  44.869  84.244  1.00 55.10
ATOM   5239  CG  HIS L 327      -8.661  43.679  83.476  1.00 66.99
ATOM   5240  CD2 HIS L 327      -9.151  43.074  82.367  1.00 69.73
ATOM   5241  ND1 HIS L 327      -7.550  42.952  83.847  1.00 74.75
ATOM   5242  CE1 HIS L 327      -7.371  41.957  82.997  1.00 73.08
ATOM   5243  NE2 HIS L 327      -8.328  42.008  82.089  1.00 72.99
ATOM   5251  N   PRO L 328      -9.765  47.975  83.541  1.00 40.97
ATOM   5252  CA  PRO L 328     -10.660  49.049  83.949  1.00 40.56
ATOM   5253  C   PRO L 328     -11.660  48.557  85.002  1.00 40.95
ATOM   5254  O   PRO L 328     -12.218  47.468  84.876  1.00 42.36
ATOM   5255  CB  PRO L 328     -11.361  49.433  82.639  1.00 39.90
ATOM   5256  CG  PRO L 328     -10.355  49.079  81.584  1.00 40.28
ATOM   5257  CD  PRO L 328      -9.755  47.800  82.079  1.00 41.31
ATOM   5265  N   ASN L 329     -11.860  49.360  86.035  1.00 41.66
ATOM   5266  CA  ASN L 329     -12.555  48.931  87.242  1.00 41.92
ATOM   5267  C   ASN L 329     -13.275  50.153  87.782  1.00 39.99
ATOM   5268  O   ASN L 329     -12.641  51.162  88.092  1.00 41.26
ATOM   5269  CB  ASN L 329     -11.522  48.403  88.244  1.00 45.12
ATOM   5270  CG  ASN L 329     -12.149  47.769  89.481  1.00 47.27
ATOM   5271  ND2 ASN L 329     -11.970  46.457  89.639  1.00 44.61
ATOM   5272  OD1 ASN L 329     -12.753  48.452  90.301  1.00 46.15
ATOM   5279  N   VAL L 330     -14.598  50.071  87.867  1.00 35.15
ATOM   5280  CA  VAL L 330     -15.409  51.181  88.350  1.00 35.79
ATOM   5281  C   VAL L 330     -14.984  51.619  89.756  1.00 36.61
ATOM   5282  O   VAL L 330     -14.851  52.811  90.023  1.00 36.05
ATOM   5283  CB  VAL L 330     -16.913  50.813  88.368  1.00 36.83
ATOM   5284  CG1 VAL L 330     -17.721  51.892  89.075  1.00 37.63
ATOM   5285  CG2 VAL L 330     -17.424  50.610  86.943  1.00 40.04
ATOM   5295  N   GLN L 331     -14.767  50.652  90.642  1.00 39.24
ATOM   5296  CA  GLN L 331     -14.422  50.961  92.032  1.00 45.67
ATOM   5297  C   GLN L 331     -13.145  51.795  92.103  1.00 45.24
ATOM   5298  O   GLN L 331     -13.113  52.827  92.760  1.00 46.92
ATOM   5299  CB  GLN L 331     -14.271  49.678  92.844  1.00 52.66
ATOM   5300  CG  GLN L 331     -14.554  49.839  94.320  1.00 60.33
ATOM   5301  CD  GLN L 331     -15.602  48.846  94.786  1.00 74.05
ATOM   5302  NE2 GLN L 331     -16.814  49.052  94.581  1.00 73.97
ATOM   5303  OE1 GLN L 331     -15.149  47.753  95.405  1.00 76.75
ATOM   5312  N   LYS L 332     -12.109  51.362  91.391  1.00 45.41
ATOM   5313  CA  LYS L 332     -10.857  52.113  91.321  1.00 45.70
ATOM   5314  C   LYS L 332     -11.034  53.508  90.698  1.00 43.60
ATOM   5315  O   LYS L 332     -10.362  54.450  91.093  1.00 41.54
ATOM   5316  CB  LYS L 332      -9.786  51.303  90.580  1.00 47.90
ATOM   5317  CG  LYS L 332      -8.349  51.842  90.694  1.00 52.31
ATOM   5318  CD  LYS L 332      -7.323  50.870  90.089  1.00  0.00
ATOM   5319  CE  LYS L 332      -5.883  51.389  90.191  1.00  0.00
ATOM   5320  NZ  LYS L 332      -4.916  50.373  89.750  1.00  0.00
ATOM   5334  N   ASP L 333     -11.945  53.643  89.737  1.00 43.46
ATOM   5335  CA  ASP L 333     -12.276  54.961  89.189  1.00 41.72
ATOM   5336  C   ASP L 333     -13.002  55.851  90.183  1.00 42.37
ATOM   5337  O   ASP L 333     -12.757  57.058  90.231  1.00 40.90
ATOM   5338  CB  ASP L 333     -13.142  54.818  87.953  1.00 42.74
ATOM   5339  CG  ASP L 333     -12.384  54.257  86.792  1.00 44.36
ATOM   5340  OD1 ASP L 333     -11.140  54.245  86.858  1.00 48.44
ATOM   5341  OD2 ASP L 333     -13.028  53.831  85.818  1.00 43.69
ATOM   5346  N   LEU L 334     -13.909  55.270  90.959  1.00 41.45
ATOM   5347  CA  LEU L 334     -14.586  56.035  92.002  1.00 42.98
ATOM   5348  C   LEU L 334     -13.564  56.520  93.020  1.00 45.87
ATOM   5349  O   LEU L 334     -13.606  57.677  93.433  1.00 47.15
ATOM   5350  CB  LEU L 334     -15.685  55.211  92.685  1.00 41.58
ATOM   5351  CG  LEU L 334     -16.880  54.849  91.800  1.00 41.62
ATOM   5352  CD1 LEU L 334     -17.891  54.027  92.573  1.00 41.17
ATOM   5353  CD2 LEU L 334     -17.539  56.095  91.238  1.00 42.61
ATOM   5365  N   GLU L 335     -12.646  55.641  93.417  1.00 50.14
ATOM   5366  CA  GLU L 335     -11.573  56.023  94.334  1.00 54.88
ATOM   5367  C   GLU L 335     -10.837  57.233  93.773  1.00 57.30
ATOM   5368  O   GLU L 335     -10.689  58.239  94.462  1.00 59.12
ATOM   5369  CB  GLU L 335     -10.583  54.875  94.555  1.00 59.82
ATOM   5370  CG  GLU L 335     -11.107  53.724  95.410  1.00 64.68
ATOM   5371  CD  GLU L 335     -10.147  52.536  95.460  1.00 69.89
ATOM   5372  OE1 GLU L 335      -8.925  52.732  95.258  1.00 73.88
ATOM   5373  OE2 GLU L 335     -10.611  51.397  95.699  1.00 67.30
ATOM   5380  N   ARG L 336     -10.400  57.139  92.515  1.00 53.30
ATOM   5381  CA  ARG L 336      -9.742  58.265  91.852  1.00 55.90
ATOM   5382  C   ARG L 336     -10.616  59.521  91.798  1.00 55.27
ATOM   5383  O   ARG L 336     -10.156  60.612  92.118  1.00 56.62
ATOM   5384  CB  ARG L 336      -9.314  57.892  90.429  1.00 57.61
ATOM   5385  CG  ARG L 336      -8.703  59.059  89.652  1.00 61.85
ATOM   5386  CD  ARG L 336      -8.360  58.706  88.215  1.00 62.91
ATOM   5387  NE  ARG L 336      -9.458  58.007  87.542  1.00 64.56
ATOM   5388  CZ  ARG L 336     -10.567  58.583  87.078  1.00 63.10
ATOM   5389  NH1 ARG L 336     -10.764  59.892  87.197  1.00 64.07
ATOM   5390  NH2 ARG L 336     -11.493  57.839  86.487  1.00 59.83
ATOM   5404  N   LEU L 337     -11.862  59.375  91.359  1.00 56.10
ATOM   5405  CA  LEU L 337     -12.764  60.522  91.256  1.00 56.61
ATOM   5406  C   LEU L 337     -12.863  61.215  92.618  1.00 58.83
ATOM   5407  O   LEU L 337     -12.678  62.427  92.713  1.00 64.10
ATOM   5408  CB  LEU L 337     -14.148  60.102  90.737  1.00 54.19
ATOM   5409  CG  LEU L 337     -14.263  59.826  89.229  1.00 55.10
ATOM   5410  CD1 LEU L 337     -15.491  58.996  88.888  1.00 53.85
ATOM   5411  CD2 LEU L 337     -14.287  61.124  88.440  1.00 57.31
ATOM   5423  N   THR L 338     -13.112  60.438  93.670  1.00 58.35
ATOM   5424  CA  THR L 338     -13.163  60.978  95.036  1.00 58.47
ATOM   5425  C   THR L 338     -11.872  61.703  95.394  1.00 62.51
ATOM   5426  O   THR L 338     -11.914  62.863  95.786  1.00 62.28
ATOM   5427  CB  THR L 338     -13.439  59.882  96.084  1.00 55.17
ATOM   5428  CG2 THR L 338     -13.556  60.473  97.485  1.00 58.07
ATOM   5429  OG1 THR L 338     -14.663  59.213  95.761  1.00 51.69
ATOM   5437  N   GLN L 339     -10.726  61.043  95.232  1.00 69.49
ATOM   5438  CA  GLN L 339      -9.433  61.661  95.572  1.00 77.75
ATOM   5439  C   GLN L 339      -9.150  62.823  94.610  1.00 83.64
ATOM   5440  O   GLN L 339      -8.149  62.811  93.896  1.00 91.00
ATOM   5441  CB  GLN L 339      -8.276  60.640  95.511  1.00 80.24
ATOM   5442  CG  GLN L 339      -8.443  59.367  96.341  1.00 81.59
ATOM   5443  CD  GLN L 339      -8.534  59.615  97.831  1.00 81.62
ATOM   5444  NE2 GLN L 339      -9.633  59.181  98.435  1.00 82.39
ATOM   5445  OE1 GLN L 339      -7.625  60.172  98.436  1.00 84.05
ATOM   5454  N   GLU L 340     -10.029  63.827  94.605  1.00 83.53
ATOM   5455  CA  GLU L 340     -10.011  64.876  93.584  1.00 78.28
ATOM   5456  C   GLU L 340     -11.038  65.949  93.900  1.00 73.59
ATOM   5457  O   GLU L 340     -12.229  65.661  93.973  1.00 74.47
ATOM   5458  CB  GLU L 340     -10.303  64.281  92.204  1.00 76.34
ATOM   5459  CG  GLU L 340      -9.295  64.684  91.106  1.00  0.00
ATOM   5460  CD  GLU L 340      -9.263  66.181  90.789  1.00  0.00
ATOM   5461  OE1 GLU L 340     -10.344  66.805  90.795  1.00  0.00
ATOM   5462  OE2 GLU L 340      -8.148  66.687  90.544  1.00  0.00
ATOM   5470  N   LEU L 341     -36.079  55.935  96.910  1.00 57.77
ATOM   5471  CA  LEU L 341     -36.660  55.733  95.593  1.00 51.89
ATOM   5472  C   LEU L 341     -35.511  55.616  94.596  1.00 49.47
ATOM   5473  O   LEU L 341     -34.839  56.612  94.317  1.00 48.83
ATOM   5474  CB  LEU L 341     -37.583  56.892  95.213  1.00 52.38
ATOM   5475  CG  LEU L 341     -38.834  57.089  96.088  1.00 56.02
ATOM   5476  CD1 LEU L 341     -39.743  58.221  95.568  1.00 55.86
ATOM   5477  CD2 LEU L 341     -39.625  55.780  96.227  1.00 59.05
ATOM   5489  N   ALA L 342     -35.280  54.412  94.073  1.00 44.15
ATOM   5490  CA  ALA L 342     -34.210  54.207  93.111  1.00 41.51
ATOM   5491  C   ALA L 342     -34.729  54.316  91.666  1.00 39.45
ATOM   5492  O   ALA L 342     -35.917  54.235  91.405  1.00 40.52
ATOM   5493  CB  ALA L 342     -33.548  52.866  93.350  1.00 43.81
ATOM   5499  N   PRO L 343     -33.826  54.532  90.729  1.00 37.91
ATOM   5500  CA  PRO L 343     -34.223  54.632  89.339  1.00 38.09
ATOM   5501  C   PRO L 343     -34.868  53.304  88.809  1.00 39.23
ATOM   5502  O   PRO L 343     -34.579  52.204  89.307  1.00 39.08
ATOM   5503  CB  PRO L 343     -32.946  54.961  88.501  1.00 38.13
ATOM   5504  CG  PRO L 343     -32.028  55.597  89.551  1.00 37.28
ATOM   5505  CD  PRO L 343     -32.351  54.835  90.861  1.00 37.29
ATOM   5513  N   TYR L 344     -35.683  53.433  87.781  1.00 44.28
ATOM   5514  CA  TYR L 344     -36.217  52.260  87.128  1.00 47.24
ATOM   5515  C   TYR L 344     -36.502  52.522  85.654  1.00 52.70
ATOM   5516  O   TYR L 344     -36.660  53.681  85.213  1.00 53.03
ATOM   5517  CB  TYR L 344     -37.477  51.797  87.855  1.00 45.05
ATOM   5518  CG  TYR L 344     -38.592  52.791  87.853  1.00 45.86
ATOM   5519  CD1 TYR L 344     -38.668  53.766  88.842  1.00 45.06
ATOM   5520  CD2 TYR L 344     -39.597  52.756  86.874  1.00 48.09
ATOM   5521  CE1 TYR L 344     -39.703  54.696  88.847  1.00 47.10
ATOM   5522  CE2 TYR L 344     -40.637  53.675  86.885  1.00 50.02
ATOM   5523  CZ  TYR L 344     -40.680  54.638  87.871  1.00 49.68
ATOM   5524  OH  TYR L 344     -41.704  55.550  87.898  1.00 52.48
ATOM   5534  N   ILE L 345     -36.563  51.430  84.901  1.00 56.51
ATOM   5535  CA  ILE L 345     -36.864  51.466  83.474  1.00 60.14
ATOM   5536  C   ILE L 345     -38.303  51.014  83.296  1.00 61.35
ATOM   5537  O   ILE L 345     -38.631  49.887  83.686  1.00 60.79
ATOM   5538  CB  ILE L 345     -35.910  50.577  82.676  1.00 61.75
ATOM   5539  CG1 ILE L 345     -34.492  51.098  82.847  1.00 61.00
ATOM   5540  CG2 ILE L 345     -36.304  50.560  81.206  1.00 65.04
ATOM   5541  CD1 ILE L 345     -33.440  50.080  82.540  1.00 62.89
ATOM   5553  N   PRO L 346     -39.184  51.832  82.723  1.00 62.37
ATOM   5554  CA  PRO L 346     -40.552  51.363  82.469  1.00 64.08
ATOM   5555  C   PRO L 346     -40.552  50.227  81.463  1.00 66.51
ATOM   5556  O   PRO L 346     -39.890  50.296  80.420  1.00 67.90
ATOM   5557  CB  PRO L 346     -41.266  52.601  81.917  1.00 65.47
ATOM   5558  CG  PRO L 346     -40.342  53.732  82.117  1.00 64.98
ATOM   5559  CD  PRO L 346     -38.962  53.181  82.195  1.00 63.83
ATOM   5567  N   MET L 347     -41.315  49.183  81.776  1.00 70.54
ATOM   5568  CA  MET L 347     -41.322  48.001  80.924  1.00 74.27
ATOM   5569  C   MET L 347     -41.891  48.324  79.543  1.00 77.88
ATOM   5570  O   MET L 347     -41.428  47.783  78.533  1.00 80.41
ATOM   5571  CB  MET L 347     -42.119  46.881  81.599  1.00 74.49
ATOM   5572  CG  MET L 347     -41.501  45.489  81.449  1.00 74.94
ATOM   5573  SD  MET L 347     -41.204  44.667  83.037  1.00 73.67
ATOM   5574  CE  MET L 347     -42.807  43.953  83.371  1.00 77.54
ATOM      1  N   SER A   2     -18.884  18.663 132.430  1.00 81.03
ATOM      2  CA  SER A   2     -19.609  17.503 131.900  1.00 80.14
ATOM      3  C   SER A   2     -20.216  17.806 130.514  1.00 83.29
ATOM      4  O   SER A   2     -20.725  16.905 129.825  1.00 83.40
ATOM      5  CB  SER A   2     -20.710  17.052 132.863  1.00 84.09
ATOM      6  OG  SER A   2     -20.669  17.659 134.148  1.00 98.20
ATOM     14  N   GLY A   3     -20.186  19.079 130.130  1.00 77.37
ATOM     15  CA  GLY A   3     -20.757  19.508 128.865  1.00 73.57
ATOM     16  C   GLY A   3     -22.279  19.543 128.864  1.00 72.52
ATOM     17  O   GLY A   3     -22.955  18.889 129.681  1.00 71.82
ATOM     21  N   PRO A   4     -22.863  20.298 127.915  1.00 64.10
ATOM     22  CA  PRO A   4     -24.326  20.389 127.866  1.00 60.86
ATOM     23  C   PRO A   4     -25.018  19.061 127.556  1.00 64.36
ATOM     24  O   PRO A   4     -24.443  18.191 126.892  1.00 65.51
ATOM     25  CB  PRO A   4     -24.579  21.436 126.787  1.00 60.51
ATOM     26  CG  PRO A   4     -23.342  21.494 125.994  1.00 65.34
ATOM     27  CD  PRO A   4     -22.227  21.131 126.876  1.00 63.52
ATOM     35  N   VAL A   5     -26.252  18.902 128.053  1.00 57.78
ATOM     36  CA  VAL A   5     -27.072  17.715 127.807  1.00 55.13
ATOM     37  C   VAL A   5     -27.605  17.829 126.384  1.00 57.22
ATOM     38  O   VAL A   5     -28.112  18.895 126.022  1.00 55.37
ATOM     39  CB  VAL A   5     -28.228  17.601 128.837  1.00 56.87
ATOM     40  CG1 VAL A   5     -29.215  16.489 128.485  1.00 54.84
ATOM     41  CG2 VAL A   5     -27.683  17.413 130.245  1.00 58.29
ATOM     51  N   PRO A   6     -27.524  16.749 125.574  1.00 53.95
ATOM     52  CA  PRO A   6     -28.046  16.832 124.200  1.00 52.34
ATOM     53  C   PRO A   6     -29.558  16.968 124.127  1.00 53.35
ATOM     54  O   PRO A   6     -30.268  16.654 125.083  1.00 54.15
ATOM     55  CB  PRO A   6     -27.550  15.543 123.543  1.00 55.15
ATOM     56  CG  PRO A   6     -27.259  14.620 124.656  1.00 60.30
ATOM     57  CD  PRO A   6     -26.933  15.423 125.854  1.00 56.64
ATOM     65  N   SER A   7     -30.045  17.457 122.991  1.00 46.48
ATOM     66  CA  SER A   7     -31.459  17.674 122.766  1.00 43.54
ATOM     67  C   SER A   7     -31.816  17.275 121.348  1.00 49.02
ATOM     68  O   SER A   7     -31.002  17.433 120.427  1.00 51.92
ATOM     69  CB  SER A   7     -31.789  19.148 123.008  1.00 43.91
ATOM     70  OG  SER A   7     -33.110  19.538 122.681  1.00 48.25
ATOM     76  N   ARG A   8     -33.044  16.774 121.169  1.00 44.03
ATOM     77  CA  ARG A   8     -33.650  16.430 119.875  1.00 43.61
ATOM     78  C   ARG A   8     -34.991  17.161 119.730  1.00 47.41
ATOM     79  O   ARG A   8     -35.676  17.379 120.727  1.00 48.17
ATOM     80  CB  ARG A   8     -33.899  14.918 119.773  1.00 44.19
ATOM     81  CG  ARG A   8     -32.643  14.103 119.467  1.00 62.63
ATOM     82  CD  ARG A   8     -32.823  12.583 119.637  1.00 73.64
ATOM     83  NE  ARG A   8     -33.684  11.936 118.635  1.00 76.48
ATOM     84  CZ  ARG A   8     -33.298  11.520 117.424  1.00 87.71
ATOM     85  NH1 ARG A   8     -32.049  11.706 117.010  1.00 61.11
ATOM     86  NH2 ARG A   8     -34.166  10.941 116.612  1.00 80.32
ATOM    100  N   ALA A   9     -35.390  17.518 118.506  1.00 43.31
ATOM    101  CA  ALA A   9     -36.721  18.117 118.261  1.00 41.36
ATOM    102  C   ALA A   9     -37.750  17.031 118.584  1.00 41.83
ATOM    103  O   ALA A   9     -37.498  15.870 118.307  1.00 40.74
ATOM    104  CB  ALA A   9     -36.864  18.540 116.793  1.00 40.78
ATOM    110  N   ARG A  10     -38.897  17.398 119.150  1.00 38.96
ATOM    111  CA  ARG A  10     -39.966  16.441 119.512  1.00 38.43
ATOM    112  C   ARG A  10     -40.713  15.988 118.301  1.00 44.17
ATOM    113  O   ARG A  10     -41.440  15.007 118.372  1.00 45.76
ATOM    114  CB  ARG A  10     -41.001  17.124 120.412  1.00 35.35
ATOM    115  CG  ARG A  10     -40.560  17.345 121.828  1.00 38.48
ATOM    116  CD  ARG A  10     -41.792  17.515 122.703  1.00 38.64
ATOM    117  NE  ARG A  10     -42.450  18.831 122.598  1.00 33.32
ATOM    118  CZ  ARG A  10     -43.669  19.042 122.087  1.00 50.70
ATOM    119  NH1 ARG A  10     -44.213  20.247 122.138  1.00 33.45
ATOM    120  NH2 ARG A  10     -44.358  18.037 121.542  1.00 32.58
ATOM    134  N   VAL A  11     -40.638  16.769 117.222  1.00 41.28
ATOM    135  CA  VAL A  11     -41.391  16.547 116.004  1.00 41.12
ATOM    136  C   VAL A  11     -40.448  16.732 114.779  1.00 42.72
ATOM    137  O   VAL A  11     -39.450  17.461 114.861  1.00 41.84
ATOM    138  CB  VAL A  11     -42.582  17.559 116.045  1.00 45.04
ATOM    139  CG1 VAL A  11     -42.152  18.986 115.655  1.00 43.19
ATOM    140  CG2 VAL A  11     -43.756  17.076 115.203  1.00 45.80
ATOM    150  N   TYR A  12     -40.758  16.051 113.665  1.00 36.82
ATOM    151  CA  TYR A  12     -40.005  16.150 112.400  1.00 35.72
ATOM    152  C   TYR A  12     -38.492  15.956 112.610  1.00 42.64
ATOM    153  O   TYR A  12     -37.693  16.560 111.895  1.00 46.28
ATOM    154  CB  TYR A  12     -40.292  17.503 111.689  1.00 34.43
ATOM    155  CG  TYR A  12     -41.756  17.859 111.520  1.00 34.57
ATOM    156  CD1 TYR A  12     -42.647  16.967 110.937  1.00 35.42
ATOM    157  CD2 TYR A  12     -42.244  19.113 111.899  1.00 35.40
ATOM    158  CE1 TYR A  12     -43.991  17.295 110.763  1.00 32.87
ATOM    159  CE2 TYR A  12     -43.585  19.464 111.703  1.00 36.40
ATOM    160  CZ  TYR A  12     -44.447  18.551 111.125  1.00 42.05
ATOM    161  OH  TYR A  12     -45.746  18.878 110.880  1.00 47.74
ATOM    171  N   THR A  13     -38.104  15.143 113.595  1.00 36.28
ATOM    172  CA  THR A  13     -36.727  14.950 114.012  1.00 35.51
ATOM    173  C   THR A  13     -35.807  14.493 112.901  1.00 41.41
ATOM    174  O   THR A  13     -34.739  15.080 112.715  1.00 41.74
ATOM    175  CB  THR A  13     -36.652  13.991 115.236  1.00 37.97
ATOM    176  CG2 THR A  13     -35.339  14.081 115.981  1.00 29.00
ATOM    177  OG1 THR A  13     -37.729  14.264 116.132  1.00 34.52
ATOM    185  N   ASP A  14     -36.203  13.432 112.179  1.00 37.81
ATOM    186  CA  ASP A  14     -35.343  12.788 111.186  1.00 35.86
ATOM    187  C   ASP A  14     -35.779  12.984 109.742  1.00 40.06
ATOM    188  O   ASP A  14     -35.325  12.251 108.859  1.00 41.12
ATOM    189  CB  ASP A  14     -35.201  11.304 111.519  1.00 37.28
ATOM    190  CG  ASP A  14     -35.007  10.997 112.997  1.00 46.20
ATOM    191  OD1 ASP A  14     -33.944  11.380 113.548  1.00 45.53
ATOM    192  OD2 ASP A  14     -35.934  10.378 113.613  1.00 49.25
ATOM    197  N   VAL A  15     -36.591  14.000 109.477  1.00 35.88
ATOM    198  CA  VAL A  15     -37.116  14.243 108.133  1.00 36.33
ATOM    199  C   VAL A  15     -36.049  14.394 107.079  1.00 43.80
ATOM    200  O   VAL A  15     -36.224  13.872 105.974  1.00 45.77
ATOM    201  CB  VAL A  15     -38.233  15.338 108.044  1.00 38.11
ATOM    202  CG1 VAL A  15     -39.431  14.967 108.909  1.00 37.53
ATOM    203  CG2 VAL A  15     -37.708  16.696 108.441  1.00 36.66
ATOM    213  N   ASN A  16     -34.925  15.051 107.429  1.00 38.95
ATOM    214  CA  ASN A  16     -33.821  15.235 106.494  1.00 37.53
ATOM    215  C   ASN A  16     -33.017  13.967 106.292  1.00 42.94
ATOM    216  O   ASN A  16     -32.572  13.718 105.169  1.00 43.09
ATOM    217  CB  ASN A  16     -32.947  16.401 106.923  1.00 29.49
ATOM    218  CG  ASN A  16     -33.585  17.718 106.626  1.00 39.13
ATOM    219  ND2 ASN A  16     -33.469  18.671 107.530  1.00 31.11
ATOM    220  OD1 ASN A  16     -34.227  17.892 105.595  1.00 30.11
ATOM    227  N   THR A  17     -32.846  13.154 107.364  1.00 39.15
ATOM    228  CA  THR A  17     -32.082  11.912 107.267  1.00 39.87
ATOM    229  C   THR A  17     -32.728  10.975 106.241  1.00 46.04
ATOM    230  O   THR A  17     -32.019  10.246 105.542  1.00 48.41
ATOM    231  CB  THR A  17     -31.969  11.262 108.644  1.00 42.26
ATOM    232  CG2 THR A  17     -30.973  10.133 108.669  1.00 36.97
ATOM    233  OG1 THR A  17     -31.632  12.251 109.618  1.00 39.67
ATOM    241  N   HIS A  18     -34.068  11.026 106.131  1.00 41.63
ATOM    242  CA  HIS A  18     -34.865  10.177 105.238  1.00 42.00
ATOM    243  C   HIS A  18     -35.047  10.729 103.849  1.00 46.89
ATOM    244  O   HIS A  18     -35.793  10.163 103.062  1.00 50.34
ATOM    245  CB  HIS A  18     -36.215   9.801 105.878  1.00 42.72
ATOM    246  CG  HIS A  18     -36.079   9.128 107.203  1.00 47.38
ATOM    247  CD2 HIS A  18     -35.227   8.150 107.594  1.00 50.97
ATOM    248  ND1 HIS A  18     -36.870   9.489 108.274  1.00 48.98
ATOM    249  CE1 HIS A  18     -36.488   8.711 109.276  1.00 49.63
ATOM    250  NE2 HIS A  18     -35.491   7.899 108.915  1.00 51.19
ATOM    258  N   ARG A  19     -34.359  11.804 103.518  1.00 42.31
ATOM    259  CA  ARG A  19     -34.423  12.381 102.179  1.00 41.63
ATOM    260  C   ARG A  19     -33.113  12.180 101.471  1.00 47.52
ATOM    261  O   ARG A  19     -32.095  11.968 102.136  1.00 48.26
ATOM    262  CB  ARG A  19     -34.733  13.863 102.278  1.00 38.87
ATOM    263  CG  ARG A  19     -36.171  14.069 102.657  1.00 42.98
ATOM    264  CD  ARG A  19     -36.394  15.510 102.907  1.00 57.52
ATOM    265  NE  ARG A  19     -37.717  15.826 103.436  1.00 68.98
ATOM    266  CZ  ARG A  19     -38.782  16.054 102.677  1.00 72.55
ATOM    267  NH1 ARG A  19     -39.938  16.394 103.235  1.00 60.07
ATOM    268  NH2 ARG A  19     -38.717  15.870 101.357  1.00 37.68
ATOM    282  N   PRO A  20     -33.061  12.255 100.123  1.00 43.74
ATOM    283  CA  PRO A  20     -31.743  12.128  99.465  1.00 42.62
ATOM    284  C   PRO A  20     -30.827  13.292  99.857  1.00 45.11
ATOM    285  O   PRO A  20     -31.313  14.399 100.099  1.00 41.49
ATOM    286  CB  PRO A  20     -32.068  12.164  97.968  1.00 43.75
ATOM    287  CG  PRO A  20     -33.419  12.648  97.846  1.00 46.70
ATOM    288  CD  PRO A  20     -34.146  12.492  99.143  1.00 42.79
ATOM    296  N   ARG A  21     -29.502  13.041  99.924  1.00 44.62
ATOM    297  CA  ARG A  21     -28.525  14.066 100.295  1.00 42.56
ATOM    298  C   ARG A  21     -28.669  15.360  99.522  1.00 42.79
ATOM    299  O   ARG A  21     -28.537  16.422 100.120  1.00 41.12
ATOM    300  CB  ARG A  21     -27.098  13.503 100.431  1.00 41.36
ATOM    301  CG  ARG A  21     -26.107  13.677  99.317  1.00 47.51
ATOM    302  CD  ARG A  21     -24.713  13.595  99.881  1.00 55.61
ATOM    303  NE  ARG A  21     -23.743  14.276  99.035  1.00 72.01
ATOM    304  CZ  ARG A  21     -22.907  13.645  98.220  1.00 92.98
ATOM    305  NH1 ARG A  21     -22.042  14.334  97.483  1.00 89.47
ATOM    306  NH2 ARG A  21     -22.929  12.318  98.131  1.00 71.39
ATOM    320  N   GLU A  22     -29.083  15.292  98.256  1.00 40.02
ATOM    321  CA  GLU A  22     -29.276  16.495  97.423  1.00 40.95
ATOM    322  C   GLU A  22     -30.280  17.475  98.021  1.00 42.63
ATOM    323  O   GLU A  22     -30.162  18.674  97.777  1.00 40.58
ATOM    324  CB  GLU A  22     -29.631  16.164  95.960  1.00 44.30
ATOM    325  CG  GLU A  22     -30.895  15.340  95.764  1.00 66.48
ATOM    326  CD  GLU A  22     -30.672  13.998  95.081  1.00101.31
ATOM    327  OE1 GLU A  22     -31.401  13.709  94.101  1.00110.34
ATOM    328  OE2 GLU A  22     -29.794  13.225  95.540  1.00 85.27
ATOM    335  N   TYR A  23     -31.226  16.982  98.854  1.00 36.35
ATOM    336  CA  TYR A  23     -32.231  17.816  99.474  1.00 32.30
ATOM    337  C   TYR A  23     -31.637  18.815 100.431  1.00 37.13
ATOM    338  O   TYR A  23     -32.035  19.980 100.424  1.00 36.82
ATOM    339  CB  TYR A  23     -33.292  16.966 100.161  1.00 31.71
ATOM    340  CG  TYR A  23     -34.398  17.786 100.788  1.00 32.22
ATOM    341  CD1 TYR A  23     -35.487  18.220 100.032  1.00 31.58
ATOM    342  CD2 TYR A  23     -34.339  18.164 102.136  1.00 33.36
ATOM    343  CE1 TYR A  23     -36.496  18.993 100.598  1.00 31.16
ATOM    344  CE2 TYR A  23     -35.331  18.975 102.707  1.00 33.70
ATOM    345  CZ  TYR A  23     -36.408  19.384 101.934  1.00 41.05
ATOM    346  OH  TYR A  23     -37.383  20.179 102.485  1.00 39.92
ATOM    356  N   TRP A  24     -30.723  18.362 101.285  1.00 34.71
ATOM    357  CA  TRP A  24     -30.167  19.183 102.342  1.00 33.69
ATOM    358  C   TRP A  24     -28.688  19.562 102.189  1.00 42.82
ATOM    359  O   TRP A  24     -28.224  20.437 102.913  1.00 46.04
ATOM    360  CB  TRP A  24     -30.430  18.493 103.681  1.00 32.39
ATOM    361  CG  TRP A  24     -30.061  17.037 103.701  1.00 34.95
ATOM    362  CD1 TRP A  24     -30.910  15.971 103.580  1.00 38.71
ATOM    363  CD2 TRP A  24     -28.740  16.483 103.886  1.00 35.68
ATOM    364  CE2 TRP A  24     -28.865  15.077 103.845  1.00 41.77
ATOM    365  CE3 TRP A  24     -27.454  17.040 104.058  1.00 36.32
ATOM    366  NE1 TRP A  24     -30.192  14.791 103.627  1.00 39.70
ATOM    367  CZ2 TRP A  24     -27.751  14.220 103.991  1.00 42.97
ATOM    368  CZ3 TRP A  24     -26.353  16.190 104.161  1.00 38.55
ATOM    369  CH2 TRP A  24     -26.503  14.804 104.122  1.00 40.51
ATOM    380  N   ASP A  25     -27.927  18.890 101.293  1.00 41.11
ATOM    381  CA  ASP A  25     -26.510  19.186 101.054  1.00 42.29
ATOM    382  C   ASP A  25     -26.427  20.328 100.045  1.00 47.30
ATOM    383  O   ASP A  25     -26.075  20.137  98.870  1.00 48.77
ATOM    384  CB  ASP A  25     -25.771  17.927 100.576  1.00 45.57
ATOM    385  CG  ASP A  25     -24.279  18.037 100.479  1.00 61.12
ATOM    386  OD1 ASP A  25     -23.723  19.003 101.032  1.00 64.83
ATOM    387  OD2 ASP A  25     -23.657  17.131  99.864  1.00 68.06
ATOM    392  N   TYR A  26     -26.826  21.518 100.504  1.00 41.54
ATOM    393  CA  TYR A  26     -26.915  22.722  99.679  1.00 40.02
ATOM    394  C   TYR A  26     -25.606  23.172  99.062  1.00 47.78
ATOM    395  O   TYR A  26     -25.624  23.812  98.013  1.00 46.90
ATOM    396  CB  TYR A  26     -27.574  23.862 100.447  1.00 38.72
ATOM    397  CG  TYR A  26     -26.884  24.231 101.744  1.00 39.30
ATOM    398  CD1 TYR A  26     -25.828  25.137 101.761  1.00 39.92
ATOM    399  CD2 TYR A  26     -27.335  23.730 102.963  1.00 40.56
ATOM    400  CE1 TYR A  26     -25.207  25.507 102.958  1.00 38.96
ATOM    401  CE2 TYR A  26     -26.732  24.106 104.166  1.00 42.77
ATOM    402  CZ  TYR A  26     -25.674  25.004 104.160  1.00 50.42
ATOM    403  OH  TYR A  26     -25.129  25.427 105.351  1.00 53.95
ATOM    413  N   GLU A  27     -24.462  22.808  99.671  1.00 47.64
ATOM    414  CA  GLU A  27     -23.180  23.226  99.097  1.00 48.23
ATOM    415  C   GLU A  27     -22.944  22.585  97.744  1.00 51.64
ATOM    416  O   GLU A  27     -22.210  23.147  96.919  1.00 51.55
ATOM    417  CB  GLU A  27     -22.031  22.919 100.042  1.00 51.20
ATOM    418  CG  GLU A  27     -22.102  23.652 101.375  1.00 65.50
ATOM    419  CD  GLU A  27     -21.161  23.043 102.394  1.00 84.02
ATOM    420  OE1 GLU A  27     -21.672  22.338 103.299  1.00 68.47
ATOM    421  OE2 GLU A  27     -19.930  23.067 102.142  1.00 58.93
ATOM    428  N   SER A  28     -23.581  21.418  97.508  1.00 49.36
ATOM    429  CA  SER A  28     -23.465  20.654  96.257  1.00 51.31
ATOM    430  C   SER A  28     -24.447  21.154  95.190  1.00 55.99
ATOM    431  O   SER A  28     -24.361  20.735  94.040  1.00 57.58
ATOM    432  CB  SER A  28     -23.694  19.158  96.505  1.00 56.33
ATOM    433  OG  SER A  28     -25.044  18.727  96.356  1.00 64.93
ATOM    439  N   HIS A  29     -25.396  21.999  95.580  1.00 50.61
ATOM    440  CA  HIS A  29     -26.420  22.504  94.686  1.00 49.53
ATOM    441  C   HIS A  29     -25.834  23.375  93.571  1.00 54.68
ATOM    442  O   HIS A  29     -25.084  24.324  93.840  1.00 55.13
ATOM    443  CB  HIS A  29     -27.513  23.245  95.471  1.00 48.47
ATOM    444  CG  HIS A  29     -28.611  23.751  94.615  1.00 51.73
ATOM    445  CD2 HIS A  29     -28.922  25.024  94.282  1.00 52.42
ATOM    446  ND1 HIS A  29     -29.491  22.884  93.985  1.00 53.79
ATOM    447  CE1 HIS A  29     -30.311  23.658  93.297  1.00 52.11
ATOM    448  NE2 HIS A  29     -30.004  24.950  93.439  1.00 51.91
ATOM    456  N   VAL A  30     -26.198  23.029  92.321  1.00 50.38
ATOM    457  CA  VAL A  30     -25.781  23.766  91.137  1.00 50.12
ATOM    458  C   VAL A  30     -26.857  24.804  90.868  1.00 51.96
ATOM    459  O   VAL A  30     -28.032  24.461  90.741  1.00 51.37
ATOM    460  CB  VAL A  30     -25.534  22.847  89.908  1.00 54.85
ATOM    461  CG1 VAL A  30     -25.324  23.681  88.637  1.00 55.50
ATOM    462  CG2 VAL A  30     -24.347  21.922  90.141  1.00 55.42
ATOM    472  N   VAL A  31     -26.463  26.068  90.821  1.00 48.26
ATOM    473  CA  VAL A  31     -27.375  27.174  90.581  1.00 46.73
ATOM    474  C   VAL A  31     -27.309  27.534  89.104  1.00 55.60
ATOM    475  O   VAL A  31     -26.240  27.600  88.516  1.00 56.58
ATOM    476  CB  VAL A  31     -27.032  28.369  91.502  1.00 48.45
ATOM    477  CG1 VAL A  31     -27.937  29.560  91.235  1.00 47.65
ATOM    478  CG2 VAL A  31     -27.110  27.978  92.980  1.00 47.45
ATOM    488  N   GLU A  32     -28.440  27.787  88.502  1.00 56.45
ATOM    489  CA  GLU A  32     -28.468  28.221  87.100  1.00 59.26
ATOM    490  C   GLU A  32     -28.930  29.671  87.092  1.00 64.19
ATOM    491  O   GLU A  32     -30.093  29.902  87.409  1.00 63.58
ATOM    492  CB  GLU A  32     -29.456  27.344  86.297  1.00 61.67
ATOM    493  CG  GLU A  32     -29.170  25.844  86.338  1.00 71.43
ATOM    494  CD  GLU A  32     -28.395  25.179  85.203  1.00 90.17
ATOM    495  OE1 GLU A  32     -27.731  25.901  84.415  1.00 61.10
ATOM    496  OE2 GLU A  32     -28.332  23.925  85.212  1.00 81.70
ATOM    503  N   TRP A  33     -28.038  30.618  86.737  1.00 62.30
ATOM    504  CA  TRP A  33     -28.285  32.060  86.805  1.00 62.45
ATOM    505  C   TRP A  33     -28.836  32.622  85.549  1.00 71.81
ATOM    506  O   TRP A  33     -28.141  32.596  84.532  1.00 74.03
ATOM    507  CB  TRP A  33     -26.996  32.833  87.132  1.00 60.47
ATOM    508  CG  TRP A  33     -26.241  32.288  88.283  1.00 60.79
ATOM    509  CD1 TRP A  33     -25.287  31.314  88.248  1.00 64.07
ATOM    510  CD2 TRP A  33     -26.364  32.693  89.653  1.00 59.98
ATOM    511  CE2 TRP A  33     -25.444  31.923  90.398  1.00 64.16
ATOM    512  CE3 TRP A  33     -27.170  33.624  90.329  1.00 60.78
ATOM    513  NE1 TRP A  33     -24.816  31.074  89.518  1.00 63.42
ATOM    514  CZ2 TRP A  33     -25.323  32.041  91.797  1.00 63.27
ATOM    515  CZ3 TRP A  33     -27.061  33.728  91.714  1.00 62.08
ATOM    516  CH2 TRP A  33     -26.161  32.928  92.437  1.00 62.80
ATOM    527  N   GLY A  34     -30.007  33.248  85.642  1.00 69.19
ATOM    528  CA  GLY A  34     -30.553  34.017  84.539  1.00 69.20
ATOM    529  C   GLY A  34     -29.810  35.354  84.391  1.00 71.93
ATOM    530  O   GLY A  34     -28.859  35.726  85.136  1.00 67.51
ATOM    534  N   ASN A  35     -30.276  36.097  83.398  1.00 70.25
ATOM    535  CA  ASN A  35     -29.721  37.410  83.137  1.00 69.53
ATOM    536  C   ASN A  35     -30.682  38.392  83.788  1.00 70.25
ATOM    537  O   ASN A  35     -31.924  38.329  83.562  1.00 65.81
ATOM    538  CB  ASN A  35     -29.599  37.645  81.632  1.00 72.36
ATOM    539  CG  ASN A  35     -28.918  38.936  81.239  1.00 97.86
ATOM    540  ND2 ASN A  35     -28.562  39.048  79.966  1.00 87.17
ATOM    541  OD1 ASN A  35     -28.751  39.861  82.046  1.00 95.83
ATOM    548  N   GLN A  36     -30.092  39.308  84.596  1.00 69.07
ATOM    549  CA  GLN A  36     -30.859  40.323  85.291  1.00 70.57
ATOM    550  C   GLN A  36     -31.520  41.318  84.335  1.00 73.55
ATOM    551  O   GLN A  36     -32.449  42.006  84.744  1.00 73.94
ATOM    552  CB  GLN A  36     -30.052  40.994  86.403  1.00 72.94
ATOM    553  CG  GLN A  36     -30.938  41.703  87.436  1.00 81.70
ATOM    554  CD  GLN A  36     -30.119  42.186  88.605  1.00 82.71
ATOM    555  NE2 GLN A  36     -30.068  43.469  88.783  1.00 59.54
ATOM    556  OE1 GLN A  36     -29.480  41.426  89.333  1.00 85.67
ATOM    565  N   ASP A  37     -31.130  41.304  83.045  1.00 70.70
ATOM    566  CA  ASP A  37     -31.719  42.142  81.978  1.00 72.29
ATOM    567  C   ASP A  37     -33.217  41.857  81.718  1.00 73.20
ATOM    568  O   ASP A  37     -33.905  42.690  81.153  1.00 75.79
ATOM    569  CB  ASP A  37     -30.928  42.052  80.655  1.00 75.69
ATOM    570  CG  ASP A  37     -29.489  42.586  80.655  1.00 91.76
ATOM    571  OD1 ASP A  37     -29.101  43.296  81.627  1.00 90.33
ATOM    572  OD2 ASP A  37     -28.755  42.302  79.687  1.00103.09
ATOM    577  N   ASP A  38     -33.725  40.726  82.152  1.00 65.12
ATOM    578  CA  ASP A  38     -35.152  40.371  82.034  1.00 64.36
ATOM    579  C   ASP A  38     -36.014  41.230  83.057  1.00 62.95
ATOM    580  O   ASP A  38     -37.258  41.272  82.986  1.00 63.44
ATOM    581  CB  ASP A  38     -35.241  38.867  82.385  1.00 65.93
ATOM    582  CG  ASP A  38     -35.970  37.922  81.452  1.00 82.54
ATOM    583  OD1 ASP A  38     -36.840  37.163  81.945  1.00 82.64
ATOM    584  OD2 ASP A  38     -35.639  37.894  80.247  1.00 93.52
ATOM    589  N   TYR A  39     -35.303  41.885  84.022  1.00 53.82
ATOM    590  CA  TYR A  39     -35.836  42.704  85.122  1.00 49.84
ATOM    591  C   TYR A  39     -35.319  44.107  85.083  1.00 54.92
ATOM    592  O   TYR A  39     -34.124  44.351  84.874  1.00 58.06
ATOM    593  CB  TYR A  39     -35.494  42.063  86.467  1.00 46.30
ATOM    594  CG  TYR A  39     -35.986  40.641  86.512  1.00 42.67
ATOM    595  CD1 TYR A  39     -37.334  40.359  86.744  1.00 43.70
ATOM    596  CD2 TYR A  39     -35.133  39.577  86.210  1.00 41.68
ATOM    597  CE1 TYR A  39     -37.824  39.051  86.673  1.00 42.27
ATOM    598  CE2 TYR A  39     -35.611  38.265  86.136  1.00 40.84
ATOM    599  CZ  TYR A  39     -36.959  38.009  86.368  1.00 45.73
ATOM    600  OH  TYR A  39     -37.427  36.721  86.332  1.00 48.61
ATOM    610  N   GLN A  40     -36.217  45.042  85.219  1.00 48.82
ATOM    611  CA  GLN A  40     -35.858  46.449  85.204  1.00 46.90
ATOM    612  C   GLN A  40     -36.221  46.970  86.590  1.00 46.54
ATOM    613  O   GLN A  40     -37.364  46.809  87.020  1.00 44.00
ATOM    614  CB  GLN A  40     -36.646  47.150  84.118  1.00 49.19
ATOM    615  CG  GLN A  40     -35.789  47.947  83.206  1.00 57.65
ATOM    616  CD  GLN A  40     -36.482  48.165  81.903  1.00 72.03
ATOM    617  NE2 GLN A  40     -37.798  48.384  81.942  1.00 67.07
ATOM    618  OE1 GLN A  40     -35.855  48.110  80.853  1.00 68.51
ATOM    627  N   LEU A  41     -35.231  47.497  87.321  1.00 42.77
ATOM    628  CA  LEU A  41     -35.439  47.994  88.682  1.00 41.27
ATOM    629  C   LEU A  41     -36.268  49.268  88.621  1.00 43.23
ATOM    630  O   LEU A  41     -36.015  50.135  87.776  1.00 39.06
ATOM    631  CB  LEU A  41     -34.109  48.236  89.435  1.00 40.48
ATOM    632  CG  LEU A  41     -33.132  47.058  89.491  1.00 43.30
ATOM    633  CD1 LEU A  41     -31.903  47.423  90.261  1.00 44.30
ATOM    634  CD2 LEU A  41     -33.745  45.816  90.111  1.00 38.11
ATOM    646  N   VAL A  42     -37.295  49.342  89.505  1.00 41.03
ATOM    647  CA  VAL A  42     -38.204  50.493  89.589  1.00 42.81
ATOM    648  C   VAL A  42     -37.771  51.450  90.705  1.00 49.22
ATOM    649  O   VAL A  42     -37.595  52.638  90.447  1.00 52.07
ATOM    650  CB  VAL A  42     -39.691  50.059  89.689  1.00 45.74
ATOM    651  CG1 VAL A  42     -40.622  51.260  89.912  1.00 46.62
ATOM    652  CG2 VAL A  42     -40.098  49.306  88.426  1.00 45.63
ATOM    662  N   ARG A  43     -37.568  50.917  91.923  1.00 44.30
ATOM    663  CA  ARG A  43     -37.169  51.685  93.089  1.00 42.96
ATOM    664  C   ARG A  43     -36.615  50.784  94.183  1.00 42.35
ATOM    665  O   ARG A  43     -36.919  49.601  94.207  1.00 40.66
ATOM    666  CB  ARG A  43     -38.359  52.526  93.606  1.00 41.94
ATOM    667  CG  ARG A  43     -39.570  51.737  94.085  1.00 41.61
ATOM    668  CD  ARG A  43     -40.573  52.715  94.664  1.00 51.71
ATOM    669  NE  ARG A  43     -41.160  52.212  95.911  1.00 46.91
ATOM    670  CZ  ARG A  43     -42.406  51.789  95.991  1.00 73.25
ATOM    671  NH1 ARG A  43     -42.883  51.323  97.137  1.00 62.12
ATOM    672  NH2 ARG A  43     -43.207  51.858  94.930  1.00 71.53
ATOM    686  N   LYS A  44     -35.801  51.353  95.075  1.00 37.84
ATOM    687  CA  LYS A  44     -35.240  50.689  96.239  1.00 36.05
ATOM    688  C   LYS A  44     -36.318  50.631  97.315  1.00 40.07
ATOM    689  O   LYS A  44     -36.925  51.656  97.621  1.00 40.32
ATOM    690  CB  LYS A  44     -34.007  51.471  96.754  1.00 39.41
ATOM    691  CG  LYS A  44     -33.234  50.796  97.910  1.00 45.70
ATOM    692  CD  LYS A  44     -31.739  50.764  97.632  1.00 43.91
ATOM    693  CE  LYS A  44     -30.910  51.706  98.463  1.00 49.49
ATOM    694  NZ  LYS A  44     -29.607  52.008  97.780  1.00 69.21
ATOM    708  N   LEU A  45     -36.548  49.450  97.888  1.00 37.77
ATOM    709  CA  LEU A  45     -37.540  49.271  98.944  1.00 38.84
ATOM    710  C   LEU A  45     -36.879  49.362 100.309  1.00 45.32
ATOM    711  O   LEU A  45     -37.487  49.838 101.266  1.00 48.81
ATOM    712  CB  LEU A  45     -38.312  47.938  98.804  1.00 37.05
ATOM    713  CG  LEU A  45     -39.236  47.804  97.600  1.00 42.43
ATOM    714  CD1 LEU A  45     -39.902  46.428  97.600  1.00 41.87
ATOM    715  CD2 LEU A  45     -40.255  48.925  97.551  1.00 41.52
ATOM    727  N   GLY A  46     -35.644  48.920 100.386  1.00 39.82
ATOM    728  CA  GLY A  46     -34.880  48.924 101.615  1.00 40.20
ATOM    729  C   GLY A  46     -33.543  48.241 101.499  1.00 47.88
ATOM    730  O   GLY A  46     -33.209  47.635 100.481  1.00 46.25
ATOM    734  N   ARG A  47     -32.743  48.418 102.512  1.00 51.64
ATOM    735  CA  ARG A  47     -31.404  47.871 102.595  1.00 54.09
ATOM    736  C   ARG A  47     -31.363  47.003 103.840  1.00 62.38
ATOM    737  O   ARG A  47     -31.917  47.339 104.892  1.00 61.83
ATOM    738  CB  ARG A  47     -30.347  49.014 102.600  1.00 57.80
ATOM    739  CG  ARG A  47     -29.178  48.843 103.568  1.00 82.03
ATOM    740  CD  ARG A  47     -27.885  49.442 103.053  1.00108.71
ATOM    741  NE  ARG A  47     -27.292  48.698 101.932  1.00129.71
ATOM    742  CZ  ARG A  47     -26.558  47.591 102.049  1.00146.63
ATOM    743  NH1 ARG A  47     -26.325  47.064 103.244  1.00131.88
ATOM    744  NH2 ARG A  47     -26.047  47.008 100.972  1.00133.74
ATOM    758  N   GLY A  48     -30.736  45.868 103.679  1.00 62.81
ATOM    759  CA  GLY A  48     -30.558  44.934 104.766  1.00 63.87
ATOM    760  C   GLY A  48     -29.103  44.842 105.144  1.00 72.84
ATOM    761  O   GLY A  48     -28.239  45.530 104.574  1.00 71.93
ATOM    765  N   LYS A  49     -28.851  43.944 106.108  1.00 74.23
ATOM    766  CA  LYS A  49     -27.547  43.599 106.670  1.00 76.62
ATOM    767  C   LYS A  49     -26.665  43.038 105.550  1.00 82.81
ATOM    768  O   LYS A  49     -25.471  43.335 105.504  1.00 83.61
ATOM    769  CB  LYS A  49     -27.731  42.542 107.795  1.00 79.83
ATOM    770  CG  LYS A  49     -27.305  42.980 109.208  1.00102.33
ATOM    771  CD  LYS A  49     -27.093  41.781 110.151  1.00110.96
ATOM    772  CE  LYS A  49     -25.665  41.653 110.661  1.00120.45
ATOM    773  NZ  LYS A  49     -25.388  40.293 111.196  1.00125.28
ATOM    787  N   TYR A  50     -27.255  42.208 104.663  1.00 79.70
ATOM    788  CA  TYR A  50     -26.506  41.618 103.556  1.00 79.66
ATOM    789  C   TYR A  50     -27.250  41.636 102.200  1.00 76.89
ATOM    790  O   TYR A  50     -26.925  40.838 101.315  1.00 77.68
ATOM    791  CB  TYR A  50     -25.881  40.232 103.894  1.00 82.61
ATOM    792  CG  TYR A  50     -26.032  39.770 105.333  1.00 86.91
ATOM    793  CD1 TYR A  50     -25.026  40.002 106.272  1.00 90.46
ATOM    794  CD2 TYR A  50     -27.185  39.111 105.756  1.00 87.39
ATOM    795  CE1 TYR A  50     -25.170  39.600 107.605  1.00 91.87
ATOM    796  CE2 TYR A  50     -27.336  38.690 107.082  1.00 88.84
ATOM    797  CZ  TYR A  50     -26.328  38.945 108.009  1.00 98.53
ATOM    798  OH  TYR A  50     -26.478  38.545 109.328  1.00 97.96
ATOM    808  N   SER A  51     -28.214  42.565 102.019  1.00 65.23
ATOM    809  CA  SER A  51     -28.933  42.688 100.758  1.00 60.91
ATOM    810  C   SER A  51     -29.526  44.054 100.556  1.00 62.19
ATOM    811  O   SER A  51     -29.732  44.788 101.512  1.00 61.59
ATOM    812  CB  SER A  51     -30.007  41.613 100.594  1.00 59.34
ATOM    813  OG  SER A  51     -31.106  41.837 101.451  1.00 65.70
ATOM    819  N   GLU A  52     -29.799  44.401  99.299  1.00 56.54
ATOM    820  CA  GLU A  52     -30.504  45.614  98.929  1.00 55.28
ATOM    821  C   GLU A  52     -31.722  45.098  98.192  1.00 52.52
ATOM    822  O   GLU A  52     -31.555  44.278  97.286  1.00 52.50
ATOM    823  CB  GLU A  52     -29.663  46.516  98.018  1.00 58.05
ATOM    824  CG  GLU A  52     -28.411  47.098  98.626  1.00 71.50
ATOM    825  CD  GLU A  52     -28.210  48.505  98.115  1.00 89.91
ATOM    826  OE1 GLU A  52     -28.693  49.434  98.802  1.00 73.95
ATOM    827  OE2 GLU A  52     -27.792  48.652  96.941  1.00 86.06
ATOM    834  N   VAL A  53     -32.935  45.504  98.604  1.00 43.08
ATOM    835  CA  VAL A  53     -34.163  45.037  97.982  1.00 40.27
ATOM    836  C   VAL A  53     -34.799  46.112  97.134  1.00 44.09
ATOM    837  O   VAL A  53     -34.973  47.244  97.587  1.00 44.50
ATOM    838  CB  VAL A  53     -35.133  44.394  99.013  1.00 43.50
ATOM    839  CG1 VAL A  53     -36.409  43.890  98.340  1.00 42.65
ATOM    840  CG2 VAL A  53     -34.455  43.246  99.747  1.00 41.94
ATOM    850  N   PHE A  54     -35.168  45.747  95.894  1.00 42.50
ATOM    851  CA  PHE A  54     -35.775  46.645  94.909  1.00 43.41
ATOM    852  C   PHE A  54     -37.081  46.113  94.370  1.00 47.75
ATOM    853  O   PHE A  54     -37.234  44.902  94.167  1.00 47.82
ATOM    854  CB  PHE A  54     -34.830  46.812  93.700  1.00 45.19
ATOM    855  CG  PHE A  54     -33.505  47.457  94.014  1.00 47.04
ATOM    856  CD1 PHE A  54     -33.303  48.819  93.786  1.00 49.99
ATOM    857  CD2 PHE A  54     -32.457  46.711  94.549  1.00 47.25
ATOM    858  CE1 PHE A  54     -32.089  49.426  94.109  1.00 50.23
ATOM    859  CE2 PHE A  54     -31.249  47.319  94.870  1.00 50.07
ATOM    860  CZ  PHE A  54     -31.077  48.676  94.659  1.00 49.26
ATOM    870  N   GLU A  55     -37.995  47.027  94.059  1.00 43.84
ATOM    871  CA  GLU A  55     -39.207  46.680  93.326  1.00 43.43
ATOM    872  C   GLU A  55     -38.753  46.695  91.879  1.00 48.17
ATOM    873  O   GLU A  55     -38.000  47.599  91.472  1.00 50.66
ATOM    874  CB  GLU A  55     -40.297  47.729  93.536  1.00 46.41
ATOM    875  CG  GLU A  55     -41.545  47.457  92.713  1.00 51.89
ATOM    876  CD  GLU A  55     -42.672  48.443  92.892  1.00 64.32
ATOM    877  OE1 GLU A  55     -42.990  48.802  94.047  1.00 74.06
ATOM    878  OE2 GLU A  55     -43.282  48.814  91.871  1.00 70.22
ATOM    885  N   ALA A  56     -39.165  45.697  91.094  1.00 42.45
ATOM    886  CA  ALA A  56     -38.769  45.633  89.683  1.00 41.09
ATOM    887  C   ALA A  56     -39.930  45.201  88.801  1.00 46.99
ATOM    888  O   ALA A  56     -40.997  44.811  89.301  1.00 47.48
ATOM    889  CB  ALA A  56     -37.585  44.686  89.522  1.00 39.52
ATOM    895  N   ILE A  57     -39.715  45.257  87.494  1.00 44.20
ATOM    896  CA  ILE A  57     -40.690  44.813  86.520  1.00 44.94
ATOM    897  C   ILE A  57     -40.038  43.799  85.626  1.00 48.80
ATOM    898  O   ILE A  57     -38.930  44.027  85.122  1.00 47.29
ATOM    899  CB  ILE A  57     -41.357  46.004  85.743  1.00 50.73
ATOM    900  CG1 ILE A  57     -42.417  45.519  84.771  1.00 52.71
ATOM    901  CG2 ILE A  57     -40.345  46.922  85.040  1.00 51.00
ATOM    902  CD1 ILE A  57     -43.745  46.039  85.125  1.00 67.41
ATOM    914  N   ASN A  58     -40.727  42.664  85.433  1.00 48.57
ATOM    915  CA  ASN A  58     -40.274  41.633  84.509  1.00 49.77
ATOM    916  C   ASN A  58     -40.694  42.150  83.137  1.00 57.98
ATOM    917  O   ASN A  58     -41.892  42.237  82.859  1.00 57.99
ATOM    918  CB  ASN A  58     -40.952  40.308  84.808  1.00 50.44
ATOM    919  CG  ASN A  58     -40.478  39.201  83.902  1.00 67.42
ATOM    920  ND2 ASN A  58     -40.438  37.994  84.438  1.00 53.28
ATOM    921  OD1 ASN A  58     -40.129  39.415  82.727  1.00 58.19
ATOM    928  N   ILE A  59     -39.720  42.537  82.305  1.00 57.79
ATOM    929  CA  ILE A  59     -39.982  43.138  80.994  1.00 60.50
ATOM    930  C   ILE A  59     -40.668  42.206  79.993  1.00 71.22
ATOM    931  O   ILE A  59     -41.284  42.679  79.034  1.00 74.02
ATOM    932  CB  ILE A  59     -38.751  43.868  80.405  1.00 63.06
ATOM    933  CG1 ILE A  59     -37.642  42.881  79.999  1.00 62.16
ATOM    934  CG2 ILE A  59     -38.264  44.964  81.354  1.00 62.71
ATOM    935  CD1 ILE A  59     -36.549  43.493  79.122  1.00 72.55
ATOM    947  N   THR A  60     -40.580  40.892  80.234  1.00 69.18
ATOM    948  CA  THR A  60     -41.157  39.874  79.357  1.00 70.04
ATOM    949  C   THR A  60     -42.656  39.713  79.534  1.00 76.31
ATOM    950  O   THR A  60     -43.325  39.303  78.584  1.00 80.20
ATOM    951  CB  THR A  60     -40.429  38.516  79.487  1.00 73.01
ATOM    952  CG2 THR A  60     -38.889  38.649  79.497  1.00 68.31
ATOM    953  OG1 THR A  60     -40.900  37.812  80.642  1.00 66.26
ATOM    961  N   ASN A  61     -43.188  39.991  80.728  1.00 69.56
ATOM    962  CA  ASN A  61     -44.619  39.823  80.961  1.00 69.56
ATOM    963  C   ASN A  61     -45.274  40.945  81.770  1.00 74.50
ATOM    964  O   ASN A  61     -46.433  40.803  82.174  1.00 76.03
ATOM    965  CB  ASN A  61     -44.879  38.477  81.618  1.00 70.45
ATOM    966  CG  ASN A  61     -44.189  38.291  82.941  1.00 94.38
ATOM    967  ND2 ASN A  61     -44.076  37.052  83.366  1.00 94.86
ATOM    968  OD1 ASN A  61     -43.761  39.241  83.596  1.00 82.39
ATOM    975  N   ASN A  62     -44.527  42.031  82.049  1.00 69.23
ATOM    976  CA  ASN A  62     -44.995  43.190  82.809  1.00 68.76
ATOM    977  C   ASN A  62     -45.405  42.926  84.254  1.00 71.63
ATOM    978  O   ASN A  62     -46.098  43.759  84.868  1.00 71.73
ATOM    979  CB  ASN A  62     -46.013  44.010  82.014  1.00 71.22
ATOM    980  CG  ASN A  62     -45.366  44.757  80.862  1.00 88.71
ATOM    981  ND2 ASN A  62     -44.385  45.596  81.169  1.00 66.45
ATOM    982  OD1 ASN A  62     -45.702  44.574  79.683  1.00 92.12
ATOM    989  N   GLU A  63     -44.970  41.774  84.814  1.00 66.06
ATOM    990  CA  GLU A  63     -45.257  41.447  86.205  1.00 63.97
ATOM    991  C   GLU A  63     -44.341  42.261  87.119  1.00 61.97
ATOM    992  O   GLU A  63     -43.138  42.422  86.868  1.00 60.84
ATOM    993  CB  GLU A  63     -44.999  39.963  86.507  1.00 64.98
ATOM    994  CG  GLU A  63     -46.051  38.971  86.045  1.00 85.02
ATOM    995  CD  GLU A  63     -45.709  37.523  86.366  1.00112.33
ATOM    996  OE1 GLU A  63     -44.795  37.271  87.190  1.00 91.19
ATOM    997  OE2 GLU A  63     -46.367  36.632  85.782  1.00119.86
ATOM   1004  N   LYS A  64     -44.914  42.709  88.213  1.00 54.63
ATOM   1005  CA  LYS A  64     -44.216  43.405  89.255  1.00 51.63
ATOM   1006  C   LYS A  64     -43.578  42.315  90.131  1.00 51.90
ATOM   1007  O   LYS A  64     -44.242  41.356  90.528  1.00 52.83
ATOM   1008  CB  LYS A  64     -45.228  44.232  90.044  1.00 54.25
ATOM   1009  CG  LYS A  64     -44.587  45.296  90.890  1.00 69.46
ATOM   1010  CD  LYS A  64     -45.589  45.875  91.878  1.00 68.39
ATOM   1011  CE  LYS A  64     -46.360  47.078  91.388  1.00 63.88
ATOM   1012  NZ  LYS A  64     -47.344  47.568  92.409  1.00 57.64
ATOM   1026  N   VAL A  65     -42.273  42.425  90.393  1.00 43.05
ATOM   1027  CA  VAL A  65     -41.521  41.458  91.209  1.00 36.44
ATOM   1028  C   VAL A  65     -40.650  42.229  92.193  1.00 40.71
ATOM   1029  O   VAL A  65     -40.538  43.457  92.111  1.00 41.45
ATOM   1030  CB  VAL A  65     -40.636  40.518  90.339  1.00 33.91
ATOM   1031  CG1 VAL A  65     -41.470  39.609  89.452  1.00 33.27
ATOM   1032  CG2 VAL A  65     -39.596  41.291  89.538  1.00 31.22
ATOM   1042  N   VAL A  66     -39.943  41.503  93.039  1.00 37.38
ATOM   1043  CA  VAL A  66     -39.003  42.093  93.978  1.00 37.52
ATOM   1044  C   VAL A  66     -37.640  41.467  93.701  1.00 43.67
ATOM   1045  O   VAL A  66     -37.582  40.262  93.500  1.00 45.37
ATOM   1046  CB  VAL A  66     -39.537  41.913  95.417  1.00 39.52
ATOM   1047  CG1 VAL A  66     -38.420  41.845  96.432  1.00 38.25
ATOM   1048  CG2 VAL A  66     -40.534  43.024  95.759  1.00 39.89
ATOM   1058  N   VAL A  67     -36.571  42.282  93.599  1.00 41.45
ATOM   1059  CA  VAL A  67     -35.189  41.814  93.369  1.00 41.19
ATOM   1060  C   VAL A  67     -34.350  42.086  94.622  1.00 44.42
ATOM   1061  O   VAL A  67     -34.182  43.236  95.019  1.00 45.51
ATOM   1062  CB  VAL A  67     -34.540  42.409  92.100  1.00 44.81
ATOM   1063  CG1 VAL A  67     -33.120  41.890  91.917  1.00 42.92
ATOM   1064  CG2 VAL A  67     -35.395  42.128  90.857  1.00 45.50
ATOM   1074  N   LYS A  68     -33.847  41.025  95.241  1.00 37.98
ATOM   1075  CA  LYS A  68     -33.004  41.057  96.447  1.00 35.86
ATOM   1076  C   LYS A  68     -31.565  40.837  95.993  1.00 37.88
ATOM   1077  O   LYS A  68     -31.140  39.711  95.709  1.00 35.57
ATOM   1078  CB  LYS A  68     -33.463  39.968  97.433  1.00 36.42
ATOM   1079  CG  LYS A  68     -32.689  39.878  98.732  1.00 30.71
ATOM   1080  CD  LYS A  68     -33.226  38.681  99.466  1.00 36.11
ATOM   1081  CE  LYS A  68     -32.551  38.467 100.758  1.00 39.65
ATOM   1082  NZ  LYS A  68     -33.241  37.377 101.455  1.00 44.45
ATOM   1096  N   ILE A  69     -30.840  41.934  95.856  1.00 36.38
ATOM   1097  CA  ILE A  69     -29.456  41.900  95.409  1.00 36.78
ATOM   1098  C   ILE A  69     -28.593  41.562  96.626  1.00 45.64
ATOM   1099  O   ILE A  69     -28.579  42.305  97.592  1.00 47.66
ATOM   1100  CB  ILE A  69     -29.065  43.206  94.700  1.00 38.77
ATOM   1101  CG1 ILE A  69     -30.037  43.506  93.537  1.00 38.55
ATOM   1102  CG2 ILE A  69     -27.628  43.131  94.248  1.00 35.41
ATOM   1103  CD1 ILE A  69     -29.707  44.821  92.783  1.00 39.41
ATOM   1115  N   LEU A  70     -27.919  40.443  96.588  1.00 44.97
ATOM   1116  CA  LEU A  70     -27.153  39.993  97.724  1.00 46.97
ATOM   1117  C   LEU A  70     -25.816  40.657  97.826  1.00 63.48
ATOM   1118  O   LEU A  70     -25.105  40.788  96.818  1.00 64.52
ATOM   1119  CB  LEU A  70     -26.974  38.474  97.639  1.00 45.69
ATOM   1120  CG  LEU A  70     -28.279  37.673  97.635  1.00 48.08
ATOM   1121  CD1 LEU A  70     -28.056  36.250  97.225  1.00 48.33
ATOM   1122  CD2 LEU A  70     -29.001  37.747  98.957  1.00 43.72
ATOM   1134  N   LYS A  71     -25.445  41.074  99.054  1.00 67.77
ATOM   1135  CA  LYS A  71     -24.105  41.629  99.277  1.00 71.98
ATOM   1136  C   LYS A  71     -23.203  40.404  99.412  1.00 79.58
ATOM   1137  O   LYS A  71     -23.708  39.307  99.742  1.00 76.98
ATOM   1138  CB  LYS A  71     -24.017  42.469 100.542  1.00 75.59
ATOM   1139  CG  LYS A  71     -24.715  43.814 100.468  1.00 90.54
ATOM   1140  CD  LYS A  71     -25.019  44.255 101.885  1.00 97.83
ATOM   1141  CE  LYS A  71     -23.846  44.730 102.722  1.00 99.94
ATOM   1142  NZ  LYS A  71     -24.217  44.927 104.149  1.00 90.20
ATOM   1156  N   PRO A  72     -21.888  40.528  99.151  1.00 80.01
ATOM   1157  CA  PRO A  72     -21.052  39.336  99.222  1.00 80.00
ATOM   1158  C   PRO A  72     -21.035  38.692 100.593  1.00 80.86
ATOM   1159  O   PRO A  72     -20.882  39.334 101.618  1.00 81.36
ATOM   1160  CB  PRO A  72     -19.725  39.820  98.708  1.00 84.02
ATOM   1161  CG  PRO A  72     -20.073  41.028  97.847  1.00 89.28
ATOM   1162  CD  PRO A  72     -21.107  41.689  98.685  1.00 83.80
ATOM   1170  N   VAL A  73     -21.372  37.424 100.568  1.00 75.39
ATOM   1171  CA  VAL A  73     -21.471  36.455 101.657  1.00 74.08
ATOM   1172  C   VAL A  73     -20.924  35.145 101.097  1.00 74.32
ATOM   1173  O   VAL A  73     -20.828  35.021  99.873  1.00 75.29
ATOM   1174  CB  VAL A  73     -22.937  36.273 102.147  1.00 77.21
ATOM   1175  CG1 VAL A  73     -23.332  37.393 103.102  1.00 77.50
ATOM   1176  CG2 VAL A  73     -23.934  36.134 100.985  1.00 75.96
ATOM   1186  N   LYS A  74     -20.585  34.173 101.956  1.00 66.26
ATOM   1187  CA  LYS A  74     -20.093  32.874 101.512  1.00 64.66
ATOM   1188  C   LYS A  74     -21.054  32.272 100.432  1.00 64.97
ATOM   1189  O   LYS A  74     -22.282  32.396 100.554  1.00 63.15
ATOM   1190  CB  LYS A  74     -19.967  31.917 102.712  1.00 66.85
ATOM   1191  CG  LYS A  74     -18.906  32.268 103.724  1.00 79.69
ATOM   1192  CD  LYS A  74     -19.141  31.513 105.030  1.00 86.71
ATOM   1193  CE  LYS A  74     -18.881  32.367 106.267  1.00 96.74
ATOM   1194  NZ  LYS A  74     -17.427  32.590 106.567  1.00 90.02
ATOM   1208  N   LYS A  75     -20.497  31.679  99.359  1.00 60.69
ATOM   1209  CA  LYS A  75     -21.324  31.074  98.290  1.00 59.28
ATOM   1210  C   LYS A  75     -22.235  30.019  98.914  1.00 58.39
ATOM   1211  O   LYS A  75     -23.362  29.847  98.490  1.00 57.90
ATOM   1212  CB  LYS A  75     -20.465  30.472  97.155  1.00 63.56
ATOM   1213  CG  LYS A  75     -19.899  31.505  96.163  1.00 88.52
ATOM   1214  CD  LYS A  75     -18.584  32.220  96.616  1.00 98.82
ATOM   1215  CE  LYS A  75     -18.811  33.689  96.930  1.00100.17
ATOM   1216  NZ  LYS A  75     -17.600  34.363  97.477  1.00103.90
ATOM   1230  N   LYS A  76     -21.745  29.385  99.985  1.00 51.34
ATOM   1231  CA  LYS A  76     -22.366  28.389 100.839  1.00 48.07
ATOM   1232  C   LYS A  76     -23.722  28.923 101.328  1.00 50.23
ATOM   1233  O   LYS A  76     -24.723  28.236 101.205  1.00 50.72
ATOM   1234  CB  LYS A  76     -21.414  28.200 102.043  1.00 49.26
ATOM   1235  CG  LYS A  76     -21.458  26.877 102.716  1.00 45.71
ATOM   1236  CD  LYS A  76     -20.731  26.875 104.038  1.00 60.14
ATOM   1237  CE  LYS A  76     -21.317  25.815 104.969  1.00 82.85
ATOM   1238  NZ  LYS A  76     -20.641  25.781 106.300  1.00 86.80
ATOM   1252  N   LYS A  77     -23.738  30.149 101.868  1.00 44.96
ATOM   1253  CA  LYS A  77     -24.894  30.856 102.410  1.00 43.44
ATOM   1254  C   LYS A  77     -25.919  31.237 101.325  1.00 49.38
ATOM   1255  O   LYS A  77     -27.120  31.162 101.578  1.00 50.84
ATOM   1256  CB  LYS A  77     -24.425  32.088 103.179  1.00 46.38
ATOM   1257  CG  LYS A  77     -25.180  32.363 104.467  1.00 67.71
ATOM   1258  CD  LYS A  77     -24.759  33.687 105.117  1.00 82.96
ATOM   1259  CE  LYS A  77     -23.371  33.686 105.735  1.00102.81
ATOM   1260  NZ  LYS A  77     -23.191  32.615 106.756  1.00109.04
ATOM   1274  N   ILE A  78     -25.475  31.644 100.124  1.00 45.30
ATOM   1275  CA  ILE A  78     -26.373  31.966  99.001  1.00 43.49
ATOM   1276  C   ILE A  78     -27.057  30.671  98.544  1.00 44.17
ATOM   1277  O   ILE A  78     -28.275  30.636  98.337  1.00 42.61
ATOM   1278  CB  ILE A  78     -25.553  32.615  97.824  1.00 47.68
ATOM   1279  CG1 ILE A  78     -25.020  34.001  98.211  1.00 49.09
ATOM   1280  CG2 ILE A  78     -26.366  32.682  96.533  1.00 48.25
ATOM   1281  CD1 ILE A  78     -23.932  34.541  97.314  1.00 57.65
ATOM   1293  N   LYS A  79     -26.256  29.599  98.380  1.00 40.52
ATOM   1294  CA  LYS A  79     -26.751  28.291  97.970  1.00 38.70
ATOM   1295  C   LYS A  79     -27.743  27.769  98.990  1.00 39.64
ATOM   1296  O   LYS A  79     -28.714  27.160  98.605  1.00 41.16
ATOM   1297  CB  LYS A  79     -25.608  27.315  97.761  1.00 41.75
ATOM   1298  CG  LYS A  79     -24.851  27.527  96.478  1.00 41.02
ATOM   1299  CD  LYS A  79     -23.804  26.448  96.279  1.00 51.88
ATOM   1300  CE  LYS A  79     -23.008  26.675  95.015  1.00 59.83
ATOM   1301  NZ  LYS A  79     -22.430  25.398  94.496  1.00 70.47
ATOM   1315  N   ARG A  80     -27.553  28.059 100.271  1.00 35.47
ATOM   1316  CA  ARG A  80     -28.475  27.638 101.348  1.00 34.38
ATOM   1317  C   ARG A  80     -29.815  28.319 101.188  1.00 39.07
ATOM   1318  O   ARG A  80     -30.822  27.613 101.131  1.00 39.88
ATOM   1319  CB  ARG A  80     -27.893  27.970 102.730  1.00 29.96
ATOM   1320  CG  ARG A  80     -28.656  27.329 103.860  1.00 32.28
ATOM   1321  CD  ARG A  80     -27.984  27.662 105.177  1.00 36.45
ATOM   1322  NE  ARG A  80     -28.087  29.089 105.505  1.00 37.47
ATOM   1323  CZ  ARG A  80     -27.451  29.653 106.516  1.00 46.45
ATOM   1324  NH1 ARG A  80     -26.665  28.934 107.291  1.00 32.94
ATOM   1325  NH2 ARG A  80     -27.601  30.950 106.765  1.00 40.76
ATOM   1339  N   GLU A  81     -29.837  29.679 101.089  1.00 33.39
ATOM   1340  CA  GLU A  81     -31.078  30.412 100.891  1.00 31.98
ATOM   1341  C   GLU A  81     -31.835  29.920  99.642  1.00 35.29
ATOM   1342  O   GLU A  81     -33.026  29.670  99.714  1.00 34.65
ATOM   1343  CB  GLU A  81     -30.807  31.897 100.798  1.00 33.55
ATOM   1344  CG  GLU A  81     -32.102  32.678 100.781  1.00 35.80
ATOM   1345  CD  GLU A  81     -32.010  34.172 100.962  1.00 43.23
ATOM   1346  OE1 GLU A  81     -30.916  34.689 101.278  1.00 37.55
ATOM   1347  OE2 GLU A  81     -33.061  34.831 100.814  1.00 51.59
ATOM   1354  N   ILE A  82     -31.138  29.748  98.519  1.00 34.13
ATOM   1355  CA  ILE A  82     -31.727  29.255  97.268  1.00 34.31
ATOM   1356  C   ILE A  82     -32.295  27.848  97.446  1.00 38.85
ATOM   1357  O   ILE A  82     -33.459  27.610  97.120  1.00 39.86
ATOM   1358  CB  ILE A  82     -30.707  29.318  96.100  1.00 38.08
ATOM   1359  CG1 ILE A  82     -30.313  30.776  95.743  1.00 38.69
ATOM   1360  CG2 ILE A  82     -31.248  28.569  94.892  1.00 38.23
ATOM   1361  CD1 ILE A  82     -29.156  30.859  94.750  1.00 50.32
ATOM   1373  N   LYS A  83     -31.483  26.910  97.958  1.00 34.77
ATOM   1374  CA  LYS A  83     -31.942  25.543  98.151  1.00 33.70
ATOM   1375  C   LYS A  83     -33.171  25.481  99.065  1.00 38.32
ATOM   1376  O   LYS A  83     -34.139  24.803  98.717  1.00 41.72
ATOM   1377  CB  LYS A  83     -30.807  24.646  98.650  1.00 35.30
ATOM   1378  CG  LYS A  83     -31.140  23.155  98.633  1.00 39.99
ATOM   1379  CD  LYS A  83     -31.365  22.614  97.209  1.00 40.94
ATOM   1380  CE  LYS A  83     -32.099  21.306  97.257  1.00 37.16
ATOM   1381  NZ  LYS A  83     -32.134  20.639  95.943  1.00 47.03
ATOM   1395  N   ILE A  84     -33.161  26.206 100.193  1.00 30.08
ATOM   1396  CA  ILE A  84     -34.319  26.269 101.080  1.00 30.32
ATOM   1397  C   ILE A  84     -35.564  26.827 100.358  1.00 39.81
ATOM   1398  O   ILE A  84     -36.643  26.228 100.438  1.00 41.69
ATOM   1399  CB  ILE A  84     -33.972  27.040 102.374  1.00 32.39
ATOM   1400  CG1 ILE A  84     -33.049  26.163 103.239  1.00 33.24
ATOM   1401  CG2 ILE A  84     -35.236  27.467 103.129  1.00 30.22
ATOM   1402  CD1 ILE A  84     -32.454  26.777 104.463  1.00 31.63
ATOM   1414  N   LEU A  85     -35.407  27.944  99.622  1.00 36.48
ATOM   1415  CA  LEU A  85     -36.521  28.543  98.892  1.00 35.97
ATOM   1416  C   LEU A  85     -37.077  27.592  97.829  1.00 40.23
ATOM   1417  O   LEU A  85     -38.291  27.532  97.632  1.00 40.82
ATOM   1418  CB  LEU A  85     -36.100  29.863  98.262  1.00 35.85
ATOM   1419  CG  LEU A  85     -35.967  31.020  99.202  1.00 38.92
ATOM   1420  CD1 LEU A  85     -35.121  32.102  98.585  1.00 37.47
ATOM   1421  CD2 LEU A  85     -37.346  31.533  99.638  1.00 42.31
ATOM   1433  N   GLU A  86     -36.203  26.838  97.168  1.00 36.04
ATOM   1434  CA  GLU A  86     -36.652  25.869  96.168  1.00 36.13
ATOM   1435  C   GLU A  86     -37.386  24.703  96.807  1.00 36.13
ATOM   1436  O   GLU A  86     -38.469  24.336  96.337  1.00 34.33
ATOM   1437  CB  GLU A  86     -35.499  25.401  95.289  1.00 37.89
ATOM   1438  CG  GLU A  86     -34.993  26.522  94.393  1.00 53.25
ATOM   1439  CD  GLU A  86     -33.890  26.152  93.426  1.00 96.84
ATOM   1440  OE1 GLU A  86     -33.360  25.023  93.544  1.00107.03
ATOM   1441  OE2 GLU A  86     -33.565  26.980  92.542  1.00 99.20
ATOM   1448  N   ASN A  87     -36.859  24.193  97.929  1.00 31.90
ATOM   1449  CA  ASN A  87     -37.502  23.122  98.691  1.00 31.69
ATOM   1450  C   ASN A  87     -38.877  23.502  99.209  1.00 36.36
ATOM   1451  O   ASN A  87     -39.779  22.651  99.214  1.00 38.43
ATOM   1452  CB  ASN A  87     -36.625  22.700  99.866  1.00 32.23
ATOM   1453  CG  ASN A  87     -35.379  21.960  99.455  1.00 43.99
ATOM   1454  ND2 ASN A  87     -34.451  21.784 100.379  1.00 38.08
ATOM   1455  OD1 ASN A  87     -35.261  21.482  98.328  1.00 33.87
ATOM   1462  N   LEU A  88     -39.044  24.768  99.644  1.00 31.99
ATOM   1463  CA  LEU A  88     -40.306  25.274 100.197  1.00 32.87
ATOM   1464  C   LEU A  88     -41.270  25.890  99.189  1.00 41.08
ATOM   1465  O   LEU A  88     -42.426  26.170  99.541  1.00 40.70
ATOM   1466  CB  LEU A  88     -40.028  26.270 101.325  1.00 31.87
ATOM   1467  CG  LEU A  88     -39.213  25.753 102.490  1.00 35.14
ATOM   1468  CD1 LEU A  88     -38.967  26.857 103.458  1.00 35.70
ATOM   1469  CD2 LEU A  88     -39.876  24.579 103.172  1.00 31.29
ATOM   1481  N   ARG A  89     -40.824  26.084  97.951  1.00 41.58
ATOM   1482  CA  ARG A  89     -41.649  26.707  96.930  1.00 43.92
ATOM   1483  C   ARG A  89     -42.996  26.039  96.727  1.00 48.78
ATOM   1484  O   ARG A  89     -43.059  24.836  96.526  1.00 49.94
ATOM   1485  CB  ARG A  89     -40.902  26.850  95.604  1.00 46.60
ATOM   1486  CG  ARG A  89     -41.600  27.814  94.629  1.00 59.60
ATOM   1487  CD  ARG A  89     -40.702  28.319  93.518  1.00 69.13
ATOM   1488  NE  ARG A  89     -39.902  27.240  92.961  1.00 71.70
ATOM   1489  CZ  ARG A  89     -38.645  27.384  92.566  1.00 91.86
ATOM   1490  NH1 ARG A  89     -38.060  28.574  92.612  1.00 74.13
ATOM   1491  NH2 ARG A  89     -37.959  26.339  92.129  1.00 91.89
ATOM   1505  N   GLY A  90     -44.061  26.835  96.803  1.00 43.42
ATOM   1506  CA  GLY A  90     -45.413  26.325  96.648  1.00 42.75
ATOM   1507  C   GLY A  90     -46.065  25.956  97.969  1.00 46.34
ATOM   1508  O   GLY A  90     -47.263  25.664  98.006  1.00 48.55
ATOM   1512  N   GLY A  91     -45.295  25.993  99.055  1.00 38.80
ATOM   1513  CA  GLY A  91     -45.813  25.693 100.370  1.00 38.89
ATOM   1514  C   GLY A  91     -46.690  26.802 100.888  1.00 43.45
ATOM   1515  O   GLY A  91     -46.558  27.940 100.443  1.00 45.86
ATOM   1519  N   PRO A  92     -47.600  26.500 101.834  1.00 38.66
ATOM   1520  CA  PRO A  92     -48.519  27.537 102.315  1.00 36.74
ATOM   1521  C   PRO A  92     -47.840  28.741 102.927  1.00 39.57
ATOM   1522  O   PRO A  92     -47.037  28.598 103.850  1.00 38.81
ATOM   1523  CB  PRO A  92     -49.366  26.791 103.350  1.00 37.90
ATOM   1524  CG  PRO A  92     -48.561  25.617 103.737  1.00 42.21
ATOM   1525  CD  PRO A  92     -47.894  25.196 102.479  1.00 38.79
ATOM   1533  N   ASN A  93     -48.152  29.940 102.388  1.00 36.35
ATOM   1534  CA  ASN A  93     -47.668  31.215 102.914  1.00 35.23
ATOM   1535  C   ASN A  93     -46.161  31.401 102.879  1.00 39.03
ATOM   1536  O   ASN A  93     -45.622  32.267 103.586  1.00 36.18
ATOM   1537  CB  ASN A  93     -48.243  31.479 104.303  1.00 34.48
ATOM   1538  CG  ASN A  93     -49.746  31.504 104.284  1.00 48.31
ATOM   1539  ND2 ASN A  93     -50.323  31.058 105.363  1.00 29.75
ATOM   1540  OD1 ASN A  93     -50.394  31.845 103.279  1.00 44.31
ATOM   1547  N   ILE A  94     -45.481  30.625 102.007  1.00 35.42
ATOM   1548  CA  ILE A  94     -44.047  30.756 101.809  1.00 33.24
ATOM   1549  C   ILE A  94     -43.863  31.667 100.585  1.00 36.06
ATOM   1550  O   ILE A  94     -44.448  31.406  99.537  1.00 36.57
ATOM   1551  CB  ILE A  94     -43.349  29.365 101.573  1.00 34.42
ATOM   1552  CG1 ILE A  94     -43.684  28.294 102.644  1.00 33.31
ATOM   1553  CG2 ILE A  94     -41.844  29.557 101.341  1.00 30.88
ATOM   1554  CD1 ILE A  94     -43.227  28.610 104.027  1.00 34.29
ATOM   1566  N   ILE A  95     -43.006  32.681 100.699  1.00 32.67
ATOM   1567  CA  ILE A  95     -42.681  33.536  99.555  1.00 32.87
ATOM   1568  C   ILE A  95     -42.126  32.688  98.388  1.00 36.05
ATOM   1569  O   ILE A  95     -41.389  31.718  98.605  1.00 36.68
ATOM   1570  CB  ILE A  95     -41.724  34.694  99.950  1.00 34.96
ATOM   1571  CG1 ILE A  95     -41.794  35.862  98.961  1.00 35.17
ATOM   1572  CG2 ILE A  95     -40.289  34.217 100.153  1.00 32.72
ATOM   1573  CD1 ILE A  95     -43.022  36.677  99.023  1.00 38.09
ATOM   1585  N   THR A  96     -42.534  33.022  97.176  1.00 31.73
ATOM   1586  CA  THR A  96     -42.111  32.335  95.997  1.00 30.71
ATOM   1587  C   THR A  96     -40.875  32.965  95.400  1.00 38.70
ATOM   1588  O   THR A  96     -40.853  34.155  95.047  1.00 39.82
ATOM   1589  CB  THR A  96     -43.246  32.292  94.980  1.00 32.79
ATOM   1590  CG2 THR A  96     -42.865  31.571  93.711  1.00 24.03
ATOM   1591  OG1 THR A  96     -44.331  31.591  95.580  1.00 41.75
ATOM   1599  N   LEU A  97     -39.849  32.125  95.238  1.00 36.05
ATOM   1600  CA  LEU A  97     -38.648  32.497  94.531  1.00 35.15
ATOM   1601  C   LEU A  97     -38.993  32.308  93.048  1.00 38.99
ATOM   1602  O   LEU A  97     -39.189  31.173  92.602  1.00 40.78
ATOM   1603  CB  LEU A  97     -37.474  31.579  94.938  1.00 33.26
ATOM   1604  CG  LEU A  97     -36.134  31.822  94.200  1.00 34.08
ATOM   1605  CD1 LEU A  97     -35.573  33.225  94.484  1.00 32.50
ATOM   1606  CD2 LEU A  97     -35.136  30.793  94.595  1.00 32.52
ATOM   1618  N   ALA A  98     -39.099  33.414  92.315  1.00 32.96
ATOM   1619  CA  ALA A  98     -39.421  33.401  90.890  1.00 32.26
ATOM   1620  C   ALA A  98     -38.210  33.160  90.005  1.00 35.09
ATOM   1621  O   ALA A  98     -38.356  32.564  88.952  1.00 35.61
ATOM   1622  CB  ALA A  98     -40.091  34.714  90.494  1.00 33.36
ATOM   1628  N   ASP A  99     -37.028  33.655  90.383  1.00 32.13
ATOM   1629  CA  ASP A  99     -35.839  33.553  89.539  1.00 32.44
ATOM   1630  C   ASP A  99     -34.582  33.863  90.327  1.00 36.90
ATOM   1631  O   ASP A  99     -34.667  34.386  91.435  1.00 36.88
ATOM   1632  CB  ASP A  99     -35.977  34.530  88.348  1.00 35.14
ATOM   1633  CG  ASP A  99     -35.266  34.140  87.057  1.00 40.75
ATOM   1634  OD1 ASP A  99     -34.461  33.154  87.082  1.00 38.13
ATOM   1635  OD2 ASP A  99     -35.456  34.859  86.032  1.00 38.69
ATOM   1640  N   ILE A 100     -33.421  33.518  89.762  1.00 35.23
ATOM   1641  CA  ILE A 100     -32.079  33.692  90.322  1.00 36.25
ATOM   1642  C   ILE A 100     -31.288  34.235  89.156  1.00 44.30
ATOM   1643  O   ILE A 100     -31.195  33.598  88.109  1.00 46.02
ATOM   1644  CB  ILE A 100     -31.492  32.368  90.844  1.00 39.74
ATOM   1645  CG1 ILE A 100     -32.413  31.699  91.868  1.00 39.62
ATOM   1646  CG2 ILE A 100     -30.150  32.633  91.486  1.00 41.84
ATOM   1647  CD1 ILE A 100     -32.216  30.166  91.888  1.00 57.57
ATOM   1659  N   VAL A 101     -30.807  35.450  89.292  1.00 41.25
ATOM   1660  CA  VAL A 101     -30.148  36.128  88.187  1.00 42.17
ATOM   1661  C   VAL A 101     -28.835  36.751  88.637  1.00 46.63
ATOM   1662  O   VAL A 101     -28.490  36.784  89.813  1.00 42.42
ATOM   1663  CB  VAL A 101     -31.100  37.187  87.544  1.00 45.71
ATOM   1664  CG1 VAL A 101     -32.348  36.526  86.967  1.00 45.58
ATOM   1665  CG2 VAL A 101     -31.479  38.266  88.557  1.00 45.04
ATOM   1675  N   LYS A 102     -28.123  37.281  87.687  1.00 49.72
ATOM   1676  CA  LYS A 102     -26.888  37.943  87.995  1.00 51.57
ATOM   1677  C   LYS A 102     -26.759  39.111  87.062  1.00 64.96
ATOM   1678  O   LYS A 102     -27.113  39.009  85.863  1.00 65.09
ATOM   1679  CB  LYS A 102     -25.760  36.951  87.782  1.00 52.42
ATOM   1680  CG  LYS A 102     -24.444  37.407  88.284  1.00 56.54
ATOM   1681  CD  LYS A 102     -23.417  36.318  88.119  1.00 68.58
ATOM   1682  CE  LYS A 102     -23.500  35.220  89.169  1.00 83.09
ATOM   1683  NZ  LYS A 102     -22.579  34.081  88.828  1.00 91.57
ATOM   1697  N   ASP A 103     -26.270  40.241  87.621  1.00 69.82
ATOM   1698  CA  ASP A 103     -26.020  41.397  86.776  1.00 74.80
ATOM   1699  C   ASP A 103     -24.859  41.034  85.827  1.00 89.85
ATOM   1700  O   ASP A 103     -23.818  40.566  86.320  1.00 91.22
ATOM   1701  CB  ASP A 103     -25.674  42.642  87.578  1.00 76.11
ATOM   1702  CG  ASP A 103     -25.373  43.795  86.658  1.00 82.08
ATOM   1703  OD1 ASP A 103     -26.317  44.310  86.025  1.00 84.11
ATOM   1704  OD2 ASP A 103     -24.186  44.063  86.427  1.00 84.79
ATOM   1709  N   PRO A 104     -25.036  41.225  84.477  1.00 91.09
ATOM   1710  CA  PRO A 104     -23.964  40.860  83.518  1.00 92.74
ATOM   1711  C   PRO A 104     -22.578  41.465  83.778  1.00 99.30
ATOM   1712  O   PRO A 104     -21.564  40.810  83.528  1.00 99.57
ATOM   1713  CB  PRO A 104     -24.524  41.328  82.163  1.00 95.02
ATOM   1714  CG  PRO A 104     -26.004  41.357  82.340  1.00 98.22
ATOM   1715  CD  PRO A 104     -26.238  41.735  83.772  1.00 92.86
ATOM   1723  N   VAL A 105     -22.537  42.706  84.283  1.00 97.05
ATOM   1724  CA  VAL A 105     -21.309  43.465  84.509  1.00 98.08
ATOM   1725  C   VAL A 105     -20.661  43.188  85.868  1.00101.80
ATOM   1726  O   VAL A 105     -19.517  42.733  85.900  1.00103.68
ATOM   1727  CB  VAL A 105     -21.533  44.986  84.237  1.00102.30
ATOM   1728  CG1 VAL A 105     -20.275  45.801  84.513  1.00103.23
ATOM   1729  CG2 VAL A 105     -22.043  45.227  82.822  1.00102.44
ATOM   1739  N   SER A 106     -21.375  43.480  86.974  1.00 94.91
ATOM   1740  CA  SER A 106     -20.850  43.325  88.330  1.00 93.03
ATOM   1741  C   SER A 106     -20.715  41.868  88.796  1.00 93.23
ATOM   1742  O   SER A 106     -19.938  41.599  89.718  1.00 93.42
ATOM   1743  CB  SER A 106     -21.687  44.134  89.322  1.00 94.80
ATOM   1744  OG  SER A 106     -22.966  43.551  89.507  1.00 99.05
ATOM   1750  N   ARG A 107     -21.498  40.940  88.202  1.00 85.50
ATOM   1751  CA  ARG A 107     -21.549  39.519  88.572  1.00 82.39
ATOM   1752  C   ARG A 107     -22.215  39.305  89.963  1.00 78.95
ATOM   1753  O   ARG A 107     -22.174  38.195  90.513  1.00 77.64
ATOM   1754  CB  ARG A 107     -20.164  38.835  88.490  1.00 84.39
ATOM   1755  CG  ARG A 107     -19.383  39.079  87.196  1.00 94.47
ATOM   1756  CD  ARG A 107     -20.209  38.809  85.959  1.00101.79
ATOM   1757  NE  ARG A 107     -20.660  37.418  85.906  1.00109.58
ATOM   1758  CZ  ARG A 107     -21.305  36.880  84.876  1.00122.34
ATOM   1759  NH1 ARG A 107     -21.606  37.619  83.813  1.00113.70
ATOM   1760  NH2 ARG A 107     -21.658  35.604  84.901  1.00101.73
ATOM   1774  N   THR A 108     -22.837  40.359  90.518  1.00 69.42
ATOM   1775  CA  THR A 108     -23.508  40.245  91.802  1.00 66.12
ATOM   1776  C   THR A 108     -24.767  39.370  91.656  1.00 63.98
ATOM   1777  O   THR A 108     -25.585  39.617  90.754  1.00 64.63
ATOM   1778  CB  THR A 108     -23.845  41.634  92.359  1.00 70.42
ATOM   1779  CG2 THR A 108     -24.358  41.580  93.796  1.00 58.66
ATOM   1780  OG1 THR A 108     -22.700  42.500  92.226  1.00 70.11
ATOM   1788  N   PRO A 109     -24.922  38.348  92.532  1.00 54.51
ATOM   1789  CA  PRO A 109     -26.117  37.502  92.468  1.00 52.35
ATOM   1790  C   PRO A 109     -27.350  38.143  93.116  1.00 54.36
ATOM   1791  O   PRO A 109     -27.266  38.829  94.156  1.00 53.39
ATOM   1792  CB  PRO A 109     -25.698  36.252  93.253  1.00 52.65
ATOM   1793  CG  PRO A 109     -24.739  36.697  94.209  1.00 56.27
ATOM   1794  CD  PRO A 109     -24.045  37.922  93.646  1.00 53.80
ATOM   1802  N   ALA A 110     -28.516  37.865  92.523  1.00 47.95
ATOM   1803  CA  ALA A 110     -29.765  38.433  93.001  1.00 45.08
ATOM   1804  C   ALA A 110     -30.842  37.442  92.918  1.00 46.23
ATOM   1805  O   ALA A 110     -30.843  36.629  92.005  1.00 46.19
ATOM   1806  CB  ALA A 110     -30.139  39.642  92.170  1.00 45.67
ATOM   1812  N   LEU A 111     -31.781  37.517  93.877  1.00 40.25
ATOM   1813  CA  LEU A 111     -32.933  36.633  93.960  1.00 37.57
ATOM   1814  C   LEU A 111     -34.167  37.404  93.609  1.00 40.36
ATOM   1815  O   LEU A 111     -34.344  38.529  94.089  1.00 39.30
ATOM   1816  CB  LEU A 111     -33.063  35.991  95.350  1.00 35.78
ATOM   1817  CG  LEU A 111     -31.825  35.276  95.936  1.00 36.58
ATOM   1818  CD1 LEU A 111     -32.160  34.672  97.269  1.00 32.96
ATOM   1819  CD2 LEU A 111     -31.273  34.251  95.002  1.00 37.64
ATOM   1831  N   VAL A 112     -35.014  36.829  92.731  1.00 36.12
ATOM   1832  CA  VAL A 112     -36.253  37.480  92.275  1.00 34.89
ATOM   1833  C   VAL A 112     -37.430  36.800  92.938  1.00 36.73
ATOM   1834  O   VAL A 112     -37.571  35.572  92.841  1.00 35.87
ATOM   1835  CB  VAL A 112     -36.375  37.445  90.741  1.00 38.14
ATOM   1836  CG1 VAL A 112     -37.614  38.178  90.280  1.00 37.69
ATOM   1837  CG2 VAL A 112     -35.134  38.032  90.070  1.00 38.88
ATOM   1847  N   PHE A 113     -38.261  37.590  93.617  1.00 32.08
ATOM   1848  CA  PHE A 113     -39.422  37.075  94.326  1.00 32.14
ATOM   1849  C   PHE A 113     -40.721  37.661  93.844  1.00 41.15
ATOM   1850  O   PHE A 113     -40.791  38.754  93.254  1.00 41.30
ATOM   1851  CB  PHE A 113     -39.323  37.430  95.815  1.00 32.62
ATOM   1852  CG  PHE A 113     -38.162  36.813  96.546  1.00 32.09
ATOM   1853  CD1 PHE A 113     -38.284  35.575  97.157  1.00 33.94
ATOM   1854  CD2 PHE A 113     -36.967  37.498  96.682  1.00 32.87
ATOM   1855  CE1 PHE A 113     -37.225  35.027  97.875  1.00 33.86
ATOM   1856  CE2 PHE A 113     -35.899  36.940  97.382  1.00 34.30
ATOM   1857  CZ  PHE A 113     -36.040  35.712  97.984  1.00 31.53
ATOM   1867  N   GLU A 114     -41.765  36.938  94.203  1.00 40.92
ATOM   1868  CA  GLU A 114     -43.161  37.290  94.085  1.00 43.08
ATOM   1869  C   GLU A 114     -43.317  38.641  94.814  1.00 49.65
ATOM   1870  O   GLU A 114     -42.685  38.864  95.841  1.00 51.56
ATOM   1871  CB  GLU A 114     -43.953  36.154  94.808  1.00 44.09
ATOM   1872  CG  GLU A 114     -45.146  36.560  95.649  1.00 50.92
ATOM   1873  CD  GLU A 114     -45.829  35.459  96.420  1.00 58.20
ATOM   1874  OE1 GLU A 114     -45.134  34.558  96.944  1.00 49.26
ATOM   1875  OE2 GLU A 114     -47.076  35.511  96.503  1.00 58.66
ATOM   1882  N   HIS A 115     -44.146  39.513  94.287  1.00 48.26
ATOM   1883  CA  HIS A 115     -44.455  40.785  94.921  1.00 48.51
ATOM   1884  C   HIS A 115     -45.698  40.658  95.854  1.00 55.46
ATOM   1885  O   HIS A 115     -46.695  40.035  95.480  1.00 57.13
ATOM   1886  CB  HIS A 115     -44.620  41.897  93.872  1.00 49.49
ATOM   1887  CG  HIS A 115     -45.030  43.208  94.464  1.00 53.43
ATOM   1888  CD2 HIS A 115     -46.329  43.661  94.349  1.00 53.41
ATOM   1889  ND1 HIS A 115     -44.324  44.119  95.162  1.00 56.56
ATOM   1890  CE1 HIS A 115     -45.195  45.100  95.528  1.00 55.62
ATOM   1891  NE2 HIS A 115     -46.361  44.822  94.979  1.00 54.44
ATOM   1899  N   VAL A 116     -45.606  41.216  97.084  1.00 50.26
ATOM   1900  CA  VAL A 116     -46.691  41.270  98.056  1.00 49.70
ATOM   1901  C   VAL A 116     -47.002  42.752  98.277  1.00 59.72
ATOM   1902  O   VAL A 116     -46.082  43.554  98.502  1.00 59.11
ATOM   1903  CB  VAL A 116     -46.321  40.599  99.411  1.00 50.99
ATOM   1904  CG1 VAL A 116     -47.500  40.636 100.411  1.00 51.45
ATOM   1905  CG2 VAL A 116     -45.776  39.181  99.228  1.00 48.15
ATOM   1915  N   ASN A 117     -48.284  43.114  98.268  1.00 61.37
ATOM   1916  CA  ASN A 117     -48.644  44.503  98.549  1.00 65.81
ATOM   1917  C   ASN A 117     -48.726  44.677 100.094  1.00 77.31
ATOM   1918  O   ASN A 117     -49.805  44.629 100.672  1.00 79.03
ATOM   1919  CB  ASN A 117     -49.953  44.871  97.838  1.00 70.15
ATOM   1920  CG  ASN A 117     -49.891  44.980  96.313  1.00 94.45
ATOM   1921  ND2 ASN A 117     -50.186  43.894  95.598  1.00 80.21
ATOM   1922  OD1 ASN A 117     -49.689  46.066  95.751  1.00 94.80
ATOM   1929  N   ASN A 118     -47.573  44.798 100.759  1.00 77.34
ATOM   1930  CA  ASN A 118     -47.478  44.881 102.223  1.00 77.98
ATOM   1931  C   ASN A 118     -47.929  46.207 102.845  1.00 84.47
ATOM   1932  O   ASN A 118     -47.699  47.266 102.260  1.00 85.68
ATOM   1933  CB  ASN A 118     -46.034  44.573 102.670  1.00 77.88
ATOM   1934  CG  ASN A 118     -45.814  44.478 104.176  1.00109.19
ATOM   1935  ND2 ASN A 118     -44.873  45.269 104.680  1.00108.18
ATOM   1936  OD1 ASN A 118     -46.477  43.710 104.903  1.00 94.18
ATOM   1943  N   THR A 119     -48.540  46.135 104.055  1.00 81.58
ATOM   1944  CA  THR A 119     -48.831  47.265 104.938  1.00 83.44
ATOM   1945  C   THR A 119     -47.872  47.057 106.098  1.00 87.31
ATOM   1946  O   THR A 119     -47.998  46.058 106.814  1.00 86.30
ATOM   1947  CB  THR A 119     -50.288  47.328 105.431  1.00 94.42
ATOM   1948  CG2 THR A 119     -50.526  48.513 106.409  1.00 91.71
ATOM   1949  OG1 THR A 119     -51.163  47.443 104.308  1.00 99.60
ATOM   1957  N   ASP A 120     -46.894  47.955 106.271  1.00 85.24
ATOM   1958  CA  ASP A 120     -45.911  47.798 107.348  1.00 84.78
ATOM   1959  C   ASP A 120     -46.557  47.601 108.724  1.00 86.35
ATOM   1960  O   ASP A 120     -47.532  48.277 109.047  1.00 86.89
ATOM   1961  CB  ASP A 120     -44.873  48.934 107.371  1.00 88.37
ATOM   1962  CG  ASP A 120     -43.755  48.672 108.371  1.00108.09
ATOM   1963  OD1 ASP A 120     -42.885  47.795 108.086  1.00109.43
ATOM   1964  OD2 ASP A 120     -43.794  49.270 109.472  1.00117.79
ATOM   1969  N   PHE A 121     -46.003  46.665 109.520  1.00 80.02
ATOM   1970  CA  PHE A 121     -46.496  46.326 110.851  1.00 78.80
ATOM   1971  C   PHE A 121     -46.664  47.528 111.761  1.00 80.25
ATOM   1972  O   PHE A 121     -47.575  47.519 112.574  1.00 78.65
ATOM   1973  CB  PHE A 121     -45.650  45.230 111.517  1.00 78.76
ATOM   1974  CG  PHE A 121     -44.306  45.669 112.044  1.00 80.33
ATOM   1975  CD1 PHE A 121     -44.137  45.996 113.389  1.00 84.20
ATOM   1976  CD2 PHE A 121     -43.194  45.724 111.205  1.00 81.76
ATOM   1977  CE1 PHE A 121     -42.884  46.386 113.882  1.00 85.44
ATOM   1978  CE2 PHE A 121     -41.940  46.114 111.702  1.00 84.70
ATOM   1979  CZ  PHE A 121     -41.796  46.455 113.033  1.00 83.66
ATOM   1989  N   LYS A 122     -45.804  48.556 111.627  1.00 78.09
ATOM   1990  CA  LYS A 122     -45.879  49.766 112.461  1.00 81.24
ATOM   1991  C   LYS A 122     -47.175  50.567 112.242  1.00 88.14
ATOM   1992  O   LYS A 122     -47.580  51.329 113.117  1.00 90.38
ATOM   1993  CB  LYS A 122     -44.618  50.647 112.309  1.00 84.93
ATOM   1994  CG  LYS A 122     -43.318  50.006 112.823  1.00100.67
ATOM   1995  CD  LYS A 122     -42.958  50.479 114.251  1.00112.27
ATOM   1996  CE  LYS A 122     -41.775  49.748 114.866  1.00116.82
ATOM   1997  NZ  LYS A 122     -41.881  49.646 116.346  1.00115.52
ATOM   2011  N   GLN A 123     -47.835  50.354 111.087  1.00 84.28
ATOM   2012  CA  GLN A 123     -49.098  50.985 110.701  1.00 84.94
ATOM   2013  C   GLN A 123     -50.234  49.969 110.830  1.00 84.28
ATOM   2014  O   GLN A 123     -51.308  50.328 111.301  1.00 84.89
ATOM   2015  CB  GLN A 123     -49.007  51.506 109.252  1.00 87.23
ATOM   2016  CG  GLN A 123     -50.227  52.276 108.746  1.00116.09
ATOM   2017  CD  GLN A 123     -50.249  52.411 107.234  1.00147.95
ATOM   2018  NE2 GLN A 123     -51.426  52.236 106.637  1.00140.36
ATOM   2019  OE1 GLN A 123     -49.230  52.696 106.588  1.00147.86
ATOM   2028  N   LEU A 124     -49.994  48.699 110.421  1.00 75.80
ATOM   2029  CA  LEU A 124     -50.998  47.634 110.435  1.00 72.76
ATOM   2030  C   LEU A 124     -51.417  47.113 111.792  1.00 76.57
ATOM   2031  O   LEU A 124     -52.615  46.980 112.030  1.00 77.26
ATOM   2032  CB  LEU A 124     -50.566  46.463 109.542  1.00 69.22
ATOM   2033  CG  LEU A 124     -51.545  45.294 109.391  1.00 70.83
ATOM   2034  CD1 LEU A 124     -52.802  45.701 108.632  1.00 72.16
ATOM   2035  CD2 LEU A 124     -50.888  44.148 108.696  1.00 66.42
ATOM   2047  N   TYR A 125     -50.453  46.737 112.641  1.00 71.73
ATOM   2048  CA  TYR A 125     -50.734  46.103 113.934  1.00 71.58
ATOM   2049  C   TYR A 125     -51.697  46.873 114.822  1.00 80.03
ATOM   2050  O   TYR A 125     -52.593  46.251 115.391  1.00 82.55
ATOM   2051  CB  TYR A 125     -49.457  45.672 114.693  1.00 70.20
ATOM   2052  CG  TYR A 125     -48.687  44.505 114.100  1.00 69.02
ATOM   2053  CD1 TYR A 125     -48.989  44.011 112.830  1.00 70.75
ATOM   2054  CD2 TYR A 125     -47.619  43.931 114.783  1.00 67.94
ATOM   2055  CE1 TYR A 125     -48.272  42.956 112.273  1.00 71.56
ATOM   2056  CE2 TYR A 125     -46.890  42.875 114.234  1.00 66.80
ATOM   2057  CZ  TYR A 125     -47.225  42.384 112.980  1.00 76.03
ATOM   2058  OH  TYR A 125     -46.522  41.346 112.408  1.00 73.68
ATOM   2068  N   GLN A 126     -51.573  48.213 114.877  1.00 75.82
ATOM   2069  CA  GLN A 126     -52.450  49.082 115.666  1.00 77.30
ATOM   2070  C   GLN A 126     -53.942  49.062 115.201  1.00 78.93
ATOM   2071  O   GLN A 126     -54.815  49.470 115.972  1.00 79.79
ATOM   2072  CB  GLN A 126     -51.879  50.523 115.745  1.00 80.41
ATOM   2073  CG  GLN A 126     -51.979  51.298 114.431  1.00 99.76
ATOM   2074  CD  GLN A 126     -51.169  52.581 114.330  1.00118.82
ATOM   2075  NE2 GLN A 126     -49.932  52.588 114.440  1.00106.92
ATOM   2076  OE1 GLN A 126     -51.825  53.635 113.862  1.00111.71
ATOM   2085  N   THR A 127     -54.220  48.589 113.965  1.00 71.96
ATOM   2086  CA  THR A 127     -55.565  48.524 113.371  1.00 71.86
ATOM   2087  C   THR A 127     -56.220  47.137 113.501  1.00 71.34
ATOM   2088  O   THR A 127     -57.417  46.996 113.227  1.00 71.25
ATOM   2089  CB  THR A 127     -55.539  48.930 111.870  1.00 78.40
ATOM   2090  CG2 THR A 127     -54.769  50.214 111.603  1.00 77.68
ATOM   2091  OG1 THR A 127     -55.023  47.859 111.077  1.00 76.52
ATOM   2099  N   LEU A 128     -55.422  46.114 113.853  1.00 64.12
ATOM   2100  CA  LEU A 128     -55.892  44.730 113.907  1.00 61.76
ATOM   2101  C   LEU A 128     -56.855  44.470 115.019  1.00 64.82
ATOM   2102  O   LEU A 128     -56.660  44.935 116.147  1.00 64.54
ATOM   2103  CB  LEU A 128     -54.756  43.685 113.936  1.00 58.44
ATOM   2104  CG  LEU A 128     -53.744  43.716 112.789  1.00 60.73
ATOM   2105  CD1 LEU A 128     -52.733  42.633 112.953  1.00 57.17
ATOM   2106  CD2 LEU A 128     -54.416  43.588 111.414  1.00 64.75
ATOM   2118  N   THR A 129     -57.904  43.720 114.680  1.00 58.84
ATOM   2119  CA  THR A 129     -58.900  43.299 115.634  1.00 58.85
ATOM   2120  C   THR A 129     -58.389  42.003 116.273  1.00 62.34
ATOM   2121  O   THR A 129     -57.415  41.387 115.793  1.00 62.05
ATOM   2122  CB  THR A 129     -60.247  43.041 114.928  1.00 56.71
ATOM   2123  CG2 THR A 129     -60.794  44.264 114.233  1.00 47.62
ATOM   2124  OG1 THR A 129     -60.089  41.967 113.997  1.00 54.88
ATOM   2132  N   ASP A 130     -59.090  41.564 117.326  1.00 56.28
ATOM   2133  CA  ASP A 130     -58.812  40.308 117.981  1.00 51.87
ATOM   2134  C   ASP A 130     -58.882  39.188 116.916  1.00 52.03
ATOM   2135  O   ASP A 130     -57.939  38.399 116.827  1.00 51.73
ATOM   2136  CB  ASP A 130     -59.818  40.089 119.117  1.00 53.94
ATOM   2137  CG  ASP A 130     -59.689  38.787 119.889  1.00 62.95
ATOM   2138  OD1 ASP A 130     -58.557  38.202 119.920  1.00 63.89
ATOM   2139  OD2 ASP A 130     -60.698  38.346 120.459  1.00 63.44
ATOM   2144  N   TYR A 131     -59.934  39.171 116.063  1.00 46.81
ATOM   2145  CA  TYR A 131     -60.062  38.173 115.006  1.00 46.49
ATOM   2146  C   TYR A 131     -58.885  38.208 114.026  1.00 52.97
ATOM   2147  O   TYR A 131     -58.373  37.150 113.651  1.00 51.56
ATOM   2148  CB  TYR A 131     -61.382  38.301 114.245  1.00 50.39
ATOM   2149  CG  TYR A 131     -61.581  37.185 113.238  1.00 53.09
ATOM   2150  CD1 TYR A 131     -62.095  35.949 113.626  1.00 54.99
ATOM   2151  CD2 TYR A 131     -61.233  37.356 111.903  1.00 53.82
ATOM   2152  CE1 TYR A 131     -62.247  34.905 112.712  1.00 54.37
ATOM   2153  CE2 TYR A 131     -61.360  36.311 110.984  1.00 54.42
ATOM   2154  CZ  TYR A 131     -61.880  35.091 111.389  1.00 62.30
ATOM   2155  OH  TYR A 131     -62.067  34.084 110.468  1.00 65.03
ATOM   2165  N   ASP A 132     -58.444  39.415 113.627  1.00 51.71
ATOM   2166  CA  ASP A 132     -57.310  39.574 112.698  1.00 50.89
ATOM   2167  C   ASP A 132     -56.046  38.963 113.252  1.00 54.41
ATOM   2168  O   ASP A 132     -55.303  38.320 112.501  1.00 53.35
ATOM   2169  CB  ASP A 132     -57.004  41.051 112.402  1.00 53.89
ATOM   2170  CG  ASP A 132     -58.065  41.796 111.595  1.00 64.56
ATOM   2171  OD1 ASP A 132     -58.740  41.146 110.763  1.00 63.13
ATOM   2172  OD2 ASP A 132     -58.223  43.043 111.805  1.00 67.19
ATOM   2177  N   ILE A 133     -55.752  39.205 114.539  1.00 49.67
ATOM   2178  CA  ILE A 133     -54.546  38.639 115.161  1.00 46.31
ATOM   2179  C   ILE A 133     -54.620  37.123 115.114  1.00 48.53
ATOM   2180  O   ILE A 133     -53.660  36.484 114.692  1.00 47.95
ATOM   2181  CB  ILE A 133     -54.293  39.193 116.593  1.00 48.23
ATOM   2182  CG1 ILE A 133     -54.102  40.731 116.572  1.00 48.37
ATOM   2183  CG2 ILE A 133     -53.093  38.509 117.234  1.00 45.61
ATOM   2184  CD1 ILE A 133     -54.108  41.380 117.933  1.00 53.64
ATOM   2196  N   ARG A 134     -55.772  36.555 115.468  1.00 45.67
ATOM   2197  CA  ARG A 134     -55.947  35.094 115.434  1.00 45.04
ATOM   2198  C   ARG A 134     -55.744  34.566 114.018  1.00 47.80
ATOM   2199  O   ARG A 134     -54.969  33.624 113.812  1.00 43.03
ATOM   2200  CB  ARG A 134     -57.336  34.683 115.964  1.00 43.03
ATOM   2201  CG  ARG A 134     -57.551  35.059 117.404  1.00 47.41
ATOM   2202  CD  ARG A 134     -58.953  34.771 117.855  1.00 56.16
ATOM   2203  NE  ARG A 134     -59.290  35.452 119.107  1.00 54.22
ATOM   2204  CZ  ARG A 134     -59.785  34.841 120.173  1.00 65.70
ATOM   2205  NH1 ARG A 134     -59.948  33.526 120.173  1.00 55.20
ATOM   2206  NH2 ARG A 134     -60.104  35.537 121.258  1.00 50.38
ATOM   2220  N   PHE A 135     -56.411  35.220 113.042  1.00 46.81
ATOM   2221  CA  PHE A 135     -56.351  34.855 111.633  1.00 46.37
ATOM   2222  C   PHE A 135     -54.908  34.830 111.107  1.00 49.06
ATOM   2223  O   PHE A 135     -54.485  33.830 110.517  1.00 48.71
ATOM   2224  CB  PHE A 135     -57.248  35.796 110.801  1.00 49.80
ATOM   2225  CG  PHE A 135     -57.211  35.468 109.332  1.00 50.76
ATOM   2226  CD1 PHE A 135     -58.060  34.506 108.795  1.00 54.30
ATOM   2227  CD2 PHE A 135     -56.299  36.088 108.488  1.00 51.07
ATOM   2228  CE1 PHE A 135     -57.988  34.170 107.434  1.00 54.76
ATOM   2229  CE2 PHE A 135     -56.220  35.741 107.135  1.00 53.37
ATOM   2230  CZ  PHE A 135     -57.068  34.788 106.617  1.00 51.88
ATOM   2240  N   TYR A 136     -54.168  35.931 111.302  1.00 45.19
ATOM   2241  CA  TYR A 136     -52.793  36.025 110.819  1.00 43.11
ATOM   2242  C   TYR A 136     -51.835  35.134 111.550  1.00 47.39
ATOM   2243  O   TYR A 136     -50.926  34.581 110.934  1.00 47.08
ATOM   2244  CB  TYR A 136     -52.318  37.476 110.737  1.00 44.14
ATOM   2245  CG  TYR A 136     -53.034  38.258 109.656  1.00 46.29
ATOM   2246  CD1 TYR A 136     -53.054  37.806 108.337  1.00 47.79
ATOM   2247  CD2 TYR A 136     -53.661  39.462 109.941  1.00 48.81
ATOM   2248  CE1 TYR A 136     -53.701  38.525 107.334  1.00 48.80
ATOM   2249  CE2 TYR A 136     -54.291  40.203 108.942  1.00 51.50
ATOM   2250  CZ  TYR A 136     -54.312  39.725 107.639  1.00 57.36
ATOM   2251  OH  TYR A 136     -54.964  40.421 106.650  1.00 57.88
ATOM   2261  N   MET A 137     -52.059  34.926 112.848  1.00 44.98
ATOM   2262  CA  MET A 137     -51.235  33.981 113.609  1.00 43.31
ATOM   2263  C   MET A 137     -51.421  32.568 113.040  1.00 44.63
ATOM   2264  O   MET A 137     -50.440  31.842 112.870  1.00 45.03
ATOM   2265  CB  MET A 137     -51.560  34.053 115.111  1.00 45.88
ATOM   2266  CG  MET A 137     -50.896  35.233 115.807  1.00 48.65
ATOM   2267  SD  MET A 137     -49.186  34.828 116.151  1.00 51.42
ATOM   2268  CE  MET A 137     -48.443  36.377 116.045  1.00 47.06
ATOM   2278  N   TYR A 138     -52.652  32.207 112.675  1.00 39.45
ATOM   2279  CA  TYR A 138     -52.924  30.906 112.064  1.00 39.35
ATOM   2280  C   TYR A 138     -52.219  30.759 110.697  1.00 42.03
ATOM   2281  O   TYR A 138     -51.642  29.712 110.407  1.00 41.82
ATOM   2282  CB  TYR A 138     -54.435  30.679 111.956  1.00 42.05
ATOM   2283  CG  TYR A 138     -54.810  29.233 111.751  1.00 43.95
ATOM   2284  CD1 TYR A 138     -54.728  28.317 112.793  1.00 45.86
ATOM   2285  CD2 TYR A 138     -55.289  28.785 110.526  1.00 45.39
ATOM   2286  CE1 TYR A 138     -55.080  26.976 112.610  1.00 47.75
ATOM   2287  CE2 TYR A 138     -55.666  27.455 110.337  1.00 46.37
ATOM   2288  CZ  TYR A 138     -55.534  26.544 111.373  1.00 53.82
ATOM   2289  OH  TYR A 138     -55.912  25.230 111.196  1.00 53.30
ATOM   2299  N   GLU A 139     -52.174  31.848 109.918  1.00 38.07
ATOM   2300  CA  GLU A 139     -51.467  31.870 108.628  1.00 36.99
ATOM   2301  C   GLU A 139     -49.964  31.692 108.775  1.00 39.90
ATOM   2302  O   GLU A 139     -49.346  30.950 108.003  1.00 39.66
ATOM   2303  CB  GLU A 139     -51.795  33.136 107.831  1.00 39.14
ATOM   2304  CG  GLU A 139     -53.261  33.240 107.450  1.00 46.34
ATOM   2305  CD  GLU A 139     -53.727  32.131 106.531  1.00 58.71
ATOM   2306  OE1 GLU A 139     -53.216  32.067 105.392  1.00 67.14
ATOM   2307  OE2 GLU A 139     -54.613  31.343 106.932  1.00 54.48
ATOM   2314  N   ILE A 140     -49.375  32.312 109.809  1.00 36.99
ATOM   2315  CA  ILE A 140     -47.941  32.148 110.087  1.00 34.01
ATOM   2316  C   ILE A 140     -47.701  30.713 110.470  1.00 40.74
ATOM   2317  O   ILE A 140     -46.744  30.120 109.986  1.00 43.57
ATOM   2318  CB  ILE A 140     -47.408  33.120 111.155  1.00 35.42
ATOM   2319  CG1 ILE A 140     -47.668  34.577 110.730  1.00 34.94
ATOM   2320  CG2 ILE A 140     -45.894  32.876 111.397  1.00 32.87
ATOM   2321  CD1 ILE A 140     -47.551  35.586 111.842  1.00 37.71
ATOM   2333  N   LEU A 141     -48.592  30.130 111.295  1.00 37.06
ATOM   2334  CA  LEU A 141     -48.467  28.738 111.729  1.00 35.83
ATOM   2335  C   LEU A 141     -48.494  27.766 110.590  1.00 41.49
ATOM   2336  O   LEU A 141     -47.750  26.791 110.607  1.00 42.82
ATOM   2337  CB  LEU A 141     -49.523  28.396 112.773  1.00 36.18
ATOM   2338  CG  LEU A 141     -49.289  29.014 114.164  1.00 37.51
ATOM   2339  CD1 LEU A 141     -50.519  28.872 115.018  1.00 36.53
ATOM   2340  CD2 LEU A 141     -48.076  28.396 114.835  1.00 32.30
ATOM   2352  N   LYS A 142     -49.286  28.048 109.555  1.00 39.20
ATOM   2353  CA  LYS A 142     -49.312  27.208 108.352  1.00 37.52
ATOM   2354  C   LYS A 142     -47.915  27.187 107.706  1.00 43.15
ATOM   2355  O   LYS A 142     -47.437  26.130 107.338  1.00 45.84
ATOM   2356  CB  LYS A 142     -50.347  27.741 107.358  1.00 36.96
ATOM   2357  CG  LYS A 142     -51.764  27.429 107.745  1.00 37.57
ATOM   2358  CD  LYS A 142     -52.678  28.117 106.785  1.00 36.38
ATOM   2359  CE  LYS A 142     -54.115  27.801 107.054  1.00 41.41
ATOM   2360  NZ  LYS A 142     -55.000  28.466 106.069  1.00 55.66
ATOM   2374  N   ALA A 143     -47.255  28.351 107.609  1.00 39.68
ATOM   2375  CA  ALA A 143     -45.923  28.478 107.023  1.00 38.50
ATOM   2376  C   ALA A 143     -44.877  27.747 107.862  1.00 42.44
ATOM   2377  O   ALA A 143     -44.030  27.028 107.299  1.00 40.45
ATOM   2378  CB  ALA A 143     -45.546  29.942 106.874  1.00 38.58
ATOM   2384  N   LEU A 144     -44.936  27.926 109.209  1.00 37.06
ATOM   2385  CA  LEU A 144     -43.996  27.289 110.123  1.00 34.90
ATOM   2386  C   LEU A 144     -44.146  25.797 110.191  1.00 38.23
ATOM   2387  O   LEU A 144     -43.152  25.085 110.085  1.00 37.80
ATOM   2388  CB  LEU A 144     -44.052  27.915 111.512  1.00 34.59
ATOM   2389  CG  LEU A 144     -43.618  29.380 111.603  1.00 36.27
ATOM   2390  CD1 LEU A 144     -43.763  29.877 113.019  1.00 35.92
ATOM   2391  CD2 LEU A 144     -42.196  29.572 111.124  1.00 32.81
ATOM   2403  N   ASP A 145     -45.376  25.295 110.318  1.00 36.48
ATOM   2404  CA  ASP A 145     -45.568  23.838 110.330  1.00 35.06
ATOM   2405  C   ASP A 145     -45.078  23.258 109.016  1.00 36.84
ATOM   2406  O   ASP A 145     -44.411  22.227 109.022  1.00 36.42
ATOM   2407  CB  ASP A 145     -47.021  23.431 110.598  1.00 35.89
ATOM   2408  CG  ASP A 145     -47.162  21.931 110.769  1.00 40.14
ATOM   2409  OD1 ASP A 145     -46.356  21.341 111.507  1.00 41.74
ATOM   2410  OD2 ASP A 145     -48.104  21.362 110.209  1.00 48.38
ATOM   2415  N   TYR A 146     -45.357  23.940 107.903  1.00 33.31
ATOM   2416  CA  TYR A 146     -44.861  23.476 106.617  1.00 33.85
ATOM   2417  C   TYR A 146     -43.317  23.409 106.556  1.00 37.51
ATOM   2418  O   TYR A 146     -42.776  22.334 106.259  1.00 39.06
ATOM   2419  CB  TYR A 146     -45.430  24.289 105.449  1.00 33.59
ATOM   2420  CG  TYR A 146     -44.909  23.802 104.111  1.00 33.90
ATOM   2421  CD1 TYR A 146     -45.352  22.598 103.555  1.00 33.95
ATOM   2422  CD2 TYR A 146     -43.925  24.507 103.431  1.00 33.51
ATOM   2423  CE1 TYR A 146     -44.861  22.146 102.329  1.00 32.95
ATOM   2424  CE2 TYR A 146     -43.448  24.077 102.192  1.00 32.98
ATOM   2425  CZ  TYR A 146     -43.927  22.901 101.638  1.00 40.07
ATOM   2426  OH  TYR A 146     -43.460  22.430 100.426  1.00 44.98
ATOM   2436  N   CYS A 147     -42.627  24.522 106.847  1.00 31.23
ATOM   2437  CA  CYS A 147     -41.164  24.510 106.778  1.00 30.47
ATOM   2438  C   CYS A 147     -40.541  23.546 107.769  1.00 34.46
ATOM   2439  O   CYS A 147     -39.650  22.773 107.382  1.00 32.74
ATOM   2440  CB  CYS A 147     -40.518  25.902 106.774  1.00 31.09
ATOM   2441  SG  CYS A 147     -40.557  26.789 108.365  1.00 35.71
ATOM   2447  N   HIS A 148     -41.091  23.458 108.992  1.00 30.72
ATOM   2448  CA  HIS A 148     -40.597  22.494 109.970  1.00 29.14
ATOM   2449  C   HIS A 148     -40.775  21.083 109.475  1.00 34.86
ATOM   2450  O   HIS A 148     -39.832  20.291 109.561  1.00 39.90
ATOM   2451  CB  HIS A 148     -41.276  22.698 111.324  1.00 29.71
ATOM   2452  CG  HIS A 148     -41.008  24.032 111.961  1.00 32.03
ATOM   2453  CD2 HIS A 148     -40.070  24.964 111.683  1.00 33.09
ATOM   2454  ND1 HIS A 148     -41.780  24.480 113.008  1.00 34.37
ATOM   2455  CE1 HIS A 148     -41.278  25.653 113.356  1.00 33.70
ATOM   2456  NE2 HIS A 148     -40.245  25.987 112.588  1.00 33.55
ATOM   2464  N   SER A 149     -41.947  20.768 108.882  1.00 29.12
ATOM   2465  CA  SER A 149     -42.204  19.442 108.308  1.00 28.56
ATOM   2466  C   SER A 149     -41.241  19.102 107.164  1.00 33.61
ATOM   2467  O   SER A 149     -40.967  17.928 106.896  1.00 34.98
ATOM   2468  CB  SER A 149     -43.651  19.312 107.852  1.00 28.98
ATOM   2469  OG  SER A 149     -43.863  19.953 106.607  1.00 38.21
ATOM   2475  N   MET A 150     -40.741  20.138 106.496  1.00 30.43
ATOM   2476  CA  MET A 150     -39.792  20.057 105.392  1.00 29.32
ATOM   2477  C   MET A 150     -38.332  20.113 105.899  1.00 33.78
ATOM   2478  O   MET A 150     -37.410  20.214 105.093  1.00 32.38
ATOM   2479  CB  MET A 150     -40.111  21.143 104.359  1.00 30.33
ATOM   2480  CG  MET A 150     -41.483  20.938 103.719  1.00 33.15
ATOM   2481  SD  MET A 150     -41.580  19.516 102.583  1.00 37.01
ATOM   2482  CE  MET A 150     -40.616  20.259 101.170  1.00 33.46
ATOM   2492  N   GLY A 151     -38.139  19.975 107.217  1.00 30.61
ATOM   2493  CA  GLY A 151     -36.823  19.937 107.848  1.00 29.56
ATOM   2494  C   GLY A 151     -36.069  21.237 107.922  1.00 33.41
ATOM   2495  O   GLY A 151     -34.850  21.228 108.077  1.00 32.44
ATOM   2499  N   ILE A 152     -36.781  22.353 107.890  1.00 31.73
ATOM   2500  CA  ILE A 152     -36.172  23.669 107.917  1.00 32.41
ATOM   2501  C   ILE A 152     -36.648  24.523 109.108  1.00 41.43
ATOM   2502  O   ILE A 152     -37.857  24.581 109.408  1.00 42.28
ATOM   2503  CB  ILE A 152     -36.435  24.344 106.527  1.00 34.70
ATOM   2504  CG1 ILE A 152     -35.643  23.570 105.406  1.00 35.28
ATOM   2505  CG2 ILE A 152     -36.085  25.850 106.553  1.00 33.36
ATOM   2506  CD1 ILE A 152     -36.203  23.685 104.017  1.00 34.13
ATOM   2518  N   MET A 153     -35.683  25.212 109.759  1.00 35.78
ATOM   2519  CA  MET A 153     -35.922  26.186 110.818  1.00 33.56
ATOM   2520  C   MET A 153     -35.767  27.539 110.096  1.00 36.17
ATOM   2521  O   MET A 153     -34.766  27.737 109.391  1.00 33.66
ATOM   2522  CB  MET A 153     -34.822  26.148 111.901  1.00 35.48
ATOM   2523  CG  MET A 153     -34.526  24.835 112.488  1.00 38.80
ATOM   2524  SD  MET A 153     -33.133  24.973 113.640  1.00 42.60
ATOM   2525  CE  MET A 153     -31.838  24.579 112.616  1.00 39.49
ATOM   2535  N   HIS A 154     -36.679  28.493 110.347  1.00 31.70
ATOM   2536  CA  HIS A 154     -36.570  29.824 109.726  1.00 30.41
ATOM   2537  C   HIS A 154     -35.459  30.668 110.383  1.00 36.38
ATOM   2538  O   HIS A 154     -34.671  31.302 109.684  1.00 38.06
ATOM   2539  CB  HIS A 154     -37.936  30.538 109.751  1.00 28.92
ATOM   2540  CG  HIS A 154     -37.923  31.838 109.046  1.00 30.77
ATOM   2541  CD2 HIS A 154     -38.363  32.157 107.808  1.00 30.73
ATOM   2542  ND1 HIS A 154     -37.393  32.962 109.638  1.00 32.80
ATOM   2543  CE1 HIS A 154     -37.518  33.927 108.744  1.00 31.89
ATOM   2544  NE2 HIS A 154     -38.095  33.485 107.629  1.00 31.09
ATOM   2552  N   ARG A 155     -35.434  30.693 111.730  1.00 32.38
ATOM   2553  CA  ARG A 155     -34.441  31.363 112.562  1.00 30.82
ATOM   2554  C   ARG A 155     -34.447  32.879 112.530  1.00 36.17
ATOM   2555  O   ARG A 155     -33.546  33.498 113.095  1.00 36.15
ATOM   2556  CB  ARG A 155     -33.021  30.798 112.347  1.00 27.27
ATOM   2557  CG  ARG A 155     -32.923  29.269 112.422  1.00 24.65
ATOM   2558  CD  ARG A 155     -31.491  28.829 112.671  1.00 24.20
ATOM   2559  NE  ARG A 155     -30.602  29.288 111.591  1.00 37.76
ATOM   2560  CZ  ARG A 155     -29.303  29.019 111.486  1.00 46.67
ATOM   2561  NH1 ARG A 155     -28.687  28.300 112.411  1.00 41.90
ATOM   2562  NH2 ARG A 155     -28.614  29.463 110.452  1.00 34.94
ATOM   2576  N   ASP A 156     -35.467  33.493 111.919  1.00 33.78
ATOM   2577  CA  ASP A 156     -35.586  34.951 111.901  1.00 33.25
ATOM   2578  C   ASP A 156     -37.044  35.377 111.824  1.00 38.17
ATOM   2579  O   ASP A 156     -37.413  36.263 111.047  1.00 39.96
ATOM   2580  CB  ASP A 156     -34.684  35.604 110.844  1.00 35.12
ATOM   2581  CG  ASP A 156     -34.407  37.092 111.028  1.00 51.45
ATOM   2582  OD1 ASP A 156     -34.479  37.582 112.183  1.00 57.11
ATOM   2583  OD2 ASP A 156     -34.111  37.766 110.025  1.00 53.27
ATOM   2588  N   VAL A 157     -37.891  34.745 112.651  1.00 33.85
ATOM   2589  CA  VAL A 157     -39.306  35.107 112.693  1.00 33.93
ATOM   2590  C   VAL A 157     -39.449  36.430 113.446  1.00 39.44
ATOM   2591  O   VAL A 157     -38.945  36.556 114.558  1.00 41.94
ATOM   2592  CB  VAL A 157     -40.197  33.980 113.275  1.00 36.02
ATOM   2593  CG1 VAL A 157     -41.652  34.448 113.442  1.00 36.34
ATOM   2594  CG2 VAL A 157     -40.117  32.720 112.412  1.00 34.01
ATOM   2604  N   LYS A 158     -40.058  37.426 112.810  1.00 35.27
ATOM   2605  CA  LYS A 158     -40.260  38.773 113.368  1.00 35.34
ATOM   2606  C   LYS A 158     -41.223  39.533 112.489  1.00 40.92
ATOM   2607  O   LYS A 158     -41.402  39.141 111.341  1.00 41.34
ATOM   2608  CB  LYS A 158     -38.940  39.542 113.502  1.00 37.00
ATOM   2609  CG  LYS A 158     -38.162  39.703 112.203  1.00 30.87
ATOM   2610  CD  LYS A 158     -36.931  40.525 112.433  1.00 25.77
ATOM   2611  CE  LYS A 158     -36.226  40.787 111.133  1.00 30.00
ATOM   2612  NZ  LYS A 158     -35.013  41.569 111.408  1.00 46.78
ATOM   2626  N   PRO A 159     -41.852  40.625 112.979  1.00 40.34
ATOM   2627  CA  PRO A 159     -42.837  41.334 112.151  1.00 40.84
ATOM   2628  C   PRO A 159     -42.368  41.748 110.766  1.00 47.66
ATOM   2629  O   PRO A 159     -43.150  41.546 109.840  1.00 50.33
ATOM   2630  CB  PRO A 159     -43.274  42.506 113.040  1.00 43.03
ATOM   2631  CG  PRO A 159     -43.038  42.052 114.401  1.00 45.66
ATOM   2632  CD  PRO A 159     -41.796  41.221 114.335  1.00 41.30
ATOM   2640  N   HIS A 160     -41.110  42.251 110.597  1.00 45.10
ATOM   2641  CA  HIS A 160     -40.621  42.643 109.251  1.00 45.36
ATOM   2642  C   HIS A 160     -40.635  41.484 108.284  1.00 47.87
ATOM   2643  O   HIS A 160     -40.904  41.690 107.099  1.00 48.24
ATOM   2644  CB  HIS A 160     -39.216  43.281 109.224  1.00 47.21
ATOM   2645  CG  HIS A 160     -38.783  43.668 107.825  1.00 52.21
ATOM   2646  CD2 HIS A 160     -39.077  44.777 107.115  1.00 55.02
ATOM   2647  ND1 HIS A 160     -38.065  42.785 106.983  1.00 53.83
ATOM   2648  CE1 HIS A 160     -37.922  43.426 105.831  1.00 53.05
ATOM   2649  NE2 HIS A 160     -38.521  44.614 105.862  1.00 53.96
ATOM   2657  N   ASN A 161     -40.389  40.266 108.776  1.00 42.08
ATOM   2658  CA  ASN A 161     -40.332  39.078 107.917  1.00 39.76
ATOM   2659  C   ASN A 161     -41.669  38.431 107.599  1.00 42.85
ATOM   2660  O   ASN A 161     -41.713  37.381 106.962  1.00 42.50
ATOM   2661  CB  ASN A 161     -39.275  38.079 108.393  1.00 33.29
ATOM   2662  CG  ASN A 161     -37.872  38.586 108.211  1.00 44.16
ATOM   2663  ND2 ASN A 161     -36.941  37.985 108.908  1.00 34.52
ATOM   2664  OD1 ASN A 161     -37.587  39.466 107.393  1.00 47.66
ATOM   2671  N   VAL A 162     -42.761  39.090 107.976  1.00 39.78
ATOM   2672  CA  VAL A 162     -44.124  38.619 107.699  1.00 39.55
ATOM   2673  C   VAL A 162     -44.835  39.705 106.858  1.00 45.18
ATOM   2674  O   VAL A 162     -45.280  40.712 107.414  1.00 45.97
ATOM   2675  CB  VAL A 162     -44.883  38.288 109.017  1.00 41.10
ATOM   2676  CG1 VAL A 162     -46.313  37.871 108.733  1.00 40.01
ATOM   2677  CG2 VAL A 162     -44.148  37.211 109.823  1.00 39.28
ATOM   2687  N   MET A 163     -44.890  39.510 105.528  1.00 40.74
ATOM   2688  CA  MET A 163     -45.494  40.445 104.589  1.00 42.34
ATOM   2689  C   MET A 163     -46.973  40.166 104.505  1.00 48.64
ATOM   2690  O   MET A 163     -47.357  39.045 104.210  1.00 50.74
ATOM   2691  CB  MET A 163     -44.819  40.329 103.215  1.00 44.74
ATOM   2692  CG  MET A 163     -43.363  40.748 103.230  1.00 48.43
ATOM   2693  SD  MET A 163     -43.144  42.548 102.982  1.00 55.74
ATOM   2694  CE  MET A 163     -42.038  42.957 104.246  1.00 51.98
ATOM   2704  N   ILE A 164     -47.803  41.162 104.816  1.00 46.42
ATOM   2705  CA  ILE A 164     -49.259  41.020 104.829  1.00 47.15
ATOM   2706  C   ILE A 164     -49.931  41.958 103.871  1.00 51.86
ATOM   2707  O   ILE A 164     -49.768  43.166 103.996  1.00 50.83
ATOM   2708  CB  ILE A 164     -49.847  41.192 106.267  1.00 50.48
ATOM   2709  CG1 ILE A 164     -49.269  40.161 107.241  1.00 48.64
ATOM   2710  CG2 ILE A 164     -51.381  41.139 106.256  1.00 53.05
ATOM   2711  CD1 ILE A 164     -49.516  40.475 108.753  1.00 55.02
ATOM   2723  N   ASP A 165     -50.691  41.395 102.924  1.00 50.83
ATOM   2724  CA  ASP A 165     -51.550  42.143 102.026  1.00 52.16
ATOM   2725  C   ASP A 165     -52.909  42.083 102.764  1.00 59.91
ATOM   2726  O   ASP A 165     -53.668  41.121 102.613  1.00 60.45
ATOM   2727  CB  ASP A 165     -51.593  41.484 100.648  1.00 52.74
ATOM   2728  CG  ASP A 165     -52.522  42.125  99.641  1.00 66.07
ATOM   2729  OD1 ASP A 165     -53.300  43.039 100.031  1.00 70.11
ATOM   2730  OD2 ASP A 165     -52.523  41.675  98.478  1.00 70.66
ATOM   2735  N   HIS A 166     -53.155  43.067 103.642  1.00 58.42
ATOM   2736  CA  HIS A 166     -54.370  43.106 104.462  1.00 60.20
ATOM   2737  C   HIS A 166     -55.660  43.154 103.649  1.00 67.73
ATOM   2738  O   HIS A 166     -56.603  42.446 103.992  1.00 68.59
ATOM   2739  CB  HIS A 166     -54.309  44.217 105.516  1.00 61.48
ATOM   2740  CG  HIS A 166     -55.360  44.121 106.586  1.00 65.77
ATOM   2741  CD2 HIS A 166     -56.155  45.088 107.098  1.00 68.91
ATOM   2742  ND1 HIS A 166     -55.595  42.943 107.279  1.00 65.89
ATOM   2743  CE1 HIS A 166     -56.537  43.229 108.158  1.00 66.37
ATOM   2744  NE2 HIS A 166     -56.910  44.501 108.077  1.00 68.67
ATOM   2752  N   GLU A 167     -55.675  43.916 102.538  1.00 65.40
ATOM   2753  CA  GLU A 167     -56.814  43.999 101.630  1.00 67.30
ATOM   2754  C   GLU A 167     -57.255  42.589 101.177  1.00 70.76
ATOM   2755  O   GLU A 167     -58.451  42.292 101.200  1.00 72.30
ATOM   2756  CB  GLU A 167     -56.454  44.868 100.413  1.00 69.91
ATOM   2757  CG  GLU A 167     -57.612  45.172  99.466  1.00 87.17
ATOM   2758  CD  GLU A 167     -57.253  45.747  98.102  1.00120.91
ATOM   2759  OE1 GLU A 167     -58.135  45.741  97.212  1.00108.87
ATOM   2760  OE2 GLU A 167     -56.095  46.190  97.913  1.00125.86
ATOM   2767  N   HIS A 168     -56.288  41.715 100.813  1.00 63.98
ATOM   2768  CA  HIS A 168     -56.576  40.356 100.346  1.00 62.85
ATOM   2769  C   HIS A 168     -56.439  39.252 101.395  1.00 65.05
ATOM   2770  O   HIS A 168     -56.634  38.079 101.060  1.00 63.79
ATOM   2771  CB  HIS A 168     -55.767  40.037  99.091  1.00 62.84
ATOM   2772  CG  HIS A 168     -56.048  40.986  97.969  1.00 68.58
ATOM   2773  CD2 HIS A 168     -57.205  41.241  97.323  1.00 72.32
ATOM   2774  ND1 HIS A 168     -55.065  41.821  97.467  1.00 70.55
ATOM   2775  CE1 HIS A 168     -55.646  42.529  96.518  1.00 71.48
ATOM   2776  NE2 HIS A 168     -56.933  42.216  96.399  1.00 73.31
ATOM   2785  N   ARG A 169     -56.166  39.630 102.673  1.00 61.55
ATOM   2786  CA  ARG A 169     -55.991  38.723 103.831  1.00 59.68
ATOM   2787  C   ARG A 169     -54.966  37.632 103.462  1.00 60.42
ATOM   2788  O   ARG A 169     -55.189  36.443 103.682  1.00 59.76
ATOM   2789  CB  ARG A 169     -57.335  38.116 104.312  1.00 58.60
ATOM   2790  CG  ARG A 169     -58.492  39.113 104.336  1.00 64.21
ATOM   2791  CD  ARG A 169     -59.429  38.899 105.485  1.00 75.29
ATOM   2792  NE  ARG A 169     -59.054  39.769 106.585  1.00 80.87
ATOM   2793  CZ  ARG A 169     -59.100  39.443 107.875  1.00 89.76
ATOM   2794  NH1 ARG A 169     -58.728  40.313 108.793  1.00 75.12
ATOM   2795  NH2 ARG A 169     -59.550  38.253 108.253  1.00 65.93
ATOM   2809  N   LYS A 170     -53.886  38.063 102.812  1.00 54.66
ATOM   2810  CA  LYS A 170     -52.826  37.224 102.285  1.00 51.72
ATOM   2811  C   LYS A 170     -51.524  37.550 103.042  1.00 51.94
ATOM   2812  O   LYS A 170     -51.180  38.717 103.233  1.00 51.66
ATOM   2813  CB  LYS A 170     -52.699  37.438 100.751  1.00 54.21
ATOM   2814  CG  LYS A 170     -51.419  36.868 100.115  1.00 74.25
ATOM   2815  CD  LYS A 170     -51.357  37.026  98.607  1.00 80.83
ATOM   2816  CE  LYS A 170     -50.860  38.371  98.166  1.00 84.24
ATOM   2817  NZ  LYS A 170     -50.893  38.499  96.685  1.00 92.72
ATOM   2831  N   LEU A 171     -50.809  36.514 103.452  1.00 44.85
ATOM   2832  CA  LEU A 171     -49.598  36.634 104.234  1.00 41.93
ATOM   2833  C   LEU A 171     -48.492  35.815 103.608  1.00 43.03
ATOM   2834  O   LEU A 171     -48.749  34.712 103.141  1.00 42.31
ATOM   2835  CB  LEU A 171     -49.945  36.108 105.647  1.00 41.46
ATOM   2836  CG  LEU A 171     -48.902  36.156 106.699  1.00 44.06
ATOM   2837  CD1 LEU A 171     -49.542  36.397 108.023  1.00 44.27
ATOM   2838  CD2 LEU A 171     -48.108  34.849 106.733  1.00 44.30
ATOM   2850  N   ARG A 172     -47.243  36.325 103.639  1.00 39.81
ATOM   2851  CA  ARG A 172     -46.072  35.562 103.165  1.00 37.84
ATOM   2852  C   ARG A 172     -44.946  35.693 104.150  1.00 40.40
ATOM   2853  O   ARG A 172     -44.669  36.795 104.606  1.00 43.72
ATOM   2854  CB  ARG A 172     -45.588  35.993 101.766  1.00 37.17
ATOM   2855  CG  ARG A 172     -46.581  35.790 100.635  1.00 42.18
ATOM   2856  CD  ARG A 172     -46.819  34.332 100.338  1.00 52.32
ATOM   2857  NE  ARG A 172     -47.766  34.162  99.241  1.00 63.47
ATOM   2858  CZ  ARG A 172     -49.041  33.827  99.383  1.00 72.55
ATOM   2859  NH1 ARG A 172     -49.546  33.608 100.587  1.00 61.38
ATOM   2860  NH2 ARG A 172     -49.817  33.695  98.320  1.00 65.34
ATOM   2874  N   LEU A 173     -44.317  34.565 104.511  1.00 34.29
ATOM   2875  CA  LEU A 173     -43.141  34.519 105.383  1.00 31.43
ATOM   2876  C   LEU A 173     -41.939  34.645 104.451  1.00 36.94
ATOM   2877  O   LEU A 173     -41.770  33.840 103.508  1.00 35.39
ATOM   2878  CB  LEU A 173     -43.099  33.223 106.191  1.00 30.13
ATOM   2879  CG  LEU A 173     -41.890  33.005 107.149  1.00 32.62
ATOM   2880  CD1 LEU A 173     -41.736  34.141 108.173  1.00 31.03
ATOM   2881  CD2 LEU A 173     -42.028  31.687 107.892  1.00 29.98
ATOM   2893  N   ILE A 174     -41.163  35.751 104.647  1.00 33.41
ATOM   2894  CA  ILE A 174     -40.038  36.114 103.789  1.00 30.43
ATOM   2895  C   ILE A 174     -38.705  35.943 104.475  1.00 34.36
ATOM   2896  O   ILE A 174     -38.664  35.549 105.630  1.00 29.62
ATOM   2897  CB  ILE A 174     -40.224  37.544 103.192  1.00 32.13
ATOM   2898  CG1 ILE A 174     -40.172  38.629 104.262  1.00 32.48
ATOM   2899  CG2 ILE A 174     -41.508  37.648 102.389  1.00 31.30
ATOM   2900  CD1 ILE A 174     -39.624  39.981 103.877  1.00 30.18
ATOM   2912  N   ASP A 175     -37.607  36.287 103.751  1.00 34.89
ATOM   2913  CA  ASP A 175     -36.237  36.310 104.229  1.00 35.35
ATOM   2914  C   ASP A 175     -35.758  35.025 104.866  1.00 38.22
ATOM   2915  O   ASP A 175     -35.634  34.883 106.093  1.00 36.92
ATOM   2916  CB  ASP A 175     -35.999  37.500 105.139  1.00 38.58
ATOM   2917  CG  ASP A 175     -34.576  37.998 105.058  1.00 44.74
ATOM   2918  OD1 ASP A 175     -33.672  37.185 104.774  1.00 42.09
ATOM   2919  OD2 ASP A 175     -34.368  39.196 105.268  1.00 51.79
ATOM   2924  N   TRP A 176     -35.420  34.107 103.987  1.00 34.26
ATOM   2925  CA  TRP A 176     -34.951  32.786 104.352  1.00 33.71
ATOM   2926  C   TRP A 176     -33.418  32.703 104.416  1.00 36.34
ATOM   2927  O   TRP A 176     -32.862  31.596 104.442  1.00 35.18
ATOM   2928  CB  TRP A 176     -35.585  31.756 103.408  1.00 32.38
ATOM   2929  CG  TRP A 176     -37.087  31.718 103.551  1.00 33.41
ATOM   2930  CD1 TRP A 176     -38.000  32.560 102.973  1.00 36.03
ATOM   2931  CD2 TRP A 176     -37.828  30.856 104.420  1.00 32.46
ATOM   2932  CE2 TRP A 176     -39.195  31.194 104.279  1.00 35.07
ATOM   2933  CE3 TRP A 176     -37.471  29.796 105.273  1.00 33.52
ATOM   2934  NE1 TRP A 176     -39.267  32.249 103.406  1.00 33.69
ATOM   2935  CZ2 TRP A 176     -40.205  30.538 104.998  1.00 34.40
ATOM   2936  CZ3 TRP A 176     -38.470  29.142 105.980  1.00 34.74
ATOM   2937  CH2 TRP A 176     -39.817  29.517 105.839  1.00 35.65
ATOM   2948  N   GLY A 177     -32.761  33.870 104.500  1.00 32.39
ATOM   2949  CA  GLY A 177     -31.305  34.006 104.568  1.00 31.94
ATOM   2950  C   GLY A 177     -30.632  33.444 105.807  1.00 36.60
ATOM   2951  O   GLY A 177     -29.436  33.158 105.778  1.00 39.13
ATOM   2955  N   LEU A 178     -31.364  33.308 106.899  1.00 31.97
ATOM   2956  CA  LEU A 178     -30.834  32.752 108.141  1.00 32.11
ATOM   2957  C   LEU A 178     -31.342  31.329 108.376  1.00 35.62
ATOM   2958  O   LEU A 178     -30.887  30.683 109.309  1.00 34.51
ATOM   2959  CB  LEU A 178     -31.222  33.642 109.346  1.00 32.92
ATOM   2960  CG  LEU A 178     -30.292  34.844 109.615  1.00 36.77
ATOM   2961  CD1 LEU A 178     -30.841  35.691 110.712  1.00 35.93
ATOM   2962  CD2 LEU A 178     -28.917  34.383 110.007  1.00 39.29
ATOM   2974  N   ALA A 179     -32.272  30.831 107.523  1.00 31.30
ATOM   2975  CA  ALA A 179     -32.860  29.507 107.636  1.00 28.43
ATOM   2976  C   ALA A 179     -31.851  28.415 107.495  1.00 35.65
ATOM   2977  O   ALA A 179     -30.847  28.566 106.801  1.00 37.61
ATOM   2978  CB  ALA A 179     -34.009  29.335 106.654  1.00 28.24
ATOM   2984  N   GLU A 180     -32.102  27.291 108.168  1.00 33.11
ATOM   2985  CA  GLU A 180     -31.162  26.187 108.151  1.00 32.50
ATOM   2986  C   GLU A 180     -31.883  24.859 108.228  1.00 35.50
ATOM   2987  O   GLU A 180     -33.032  24.805 108.646  1.00 36.13
ATOM   2988  CB  GLU A 180     -30.155  26.382 109.311  1.00 33.97
ATOM   2989  CG  GLU A 180     -28.933  25.497 109.341  1.00 37.03
ATOM   2990  CD  GLU A 180     -28.130  25.302 108.073  1.00 52.41
ATOM   2991  OE1 GLU A 180     -27.001  25.840 107.985  1.00 46.77
ATOM   2992  OE2 GLU A 180     -28.570  24.486 107.231  1.00 44.45
ATOM   2999  N   PHE A 181     -31.218  23.786 107.764  1.00 31.43
ATOM   3000  CA  PHE A 181     -31.750  22.436 107.817  1.00 29.14
ATOM   3001  C   PHE A 181     -31.563  21.894 109.233  1.00 32.99
ATOM   3002  O   PHE A 181     -30.499  22.049 109.828  1.00 33.22
ATOM   3003  CB  PHE A 181     -31.046  21.534 106.794  1.00 30.34
ATOM   3004  CG  PHE A 181     -31.364  21.901 105.365  1.00 31.33
ATOM   3005  CD1 PHE A 181     -32.435  21.311 104.702  1.00 34.42
ATOM   3006  CD2 PHE A 181     -30.622  22.873 104.695  1.00 32.79
ATOM   3007  CE1 PHE A 181     -32.755  21.676 103.391  1.00 34.97
ATOM   3008  CE2 PHE A 181     -30.940  23.241 103.386  1.00 35.83
ATOM   3009  CZ  PHE A 181     -32.006  22.642 102.744  1.00 34.43
ATOM   3019  N   TYR A 182     -32.601  21.261 109.773  1.00 29.93
ATOM   3020  CA  TYR A 182     -32.501  20.628 111.060  1.00 29.45
ATOM   3021  C   TYR A 182     -31.941  19.211 110.917  1.00 34.86
ATOM   3022  O   TYR A 182     -32.523  18.371 110.204  1.00 35.73
ATOM   3023  CB  TYR A 182     -33.857  20.605 111.800  1.00 30.06
ATOM   3024  CG  TYR A 182     -33.733  19.870 113.120  1.00 28.74
ATOM   3025  CD1 TYR A 182     -32.982  20.401 114.160  1.00 28.42
ATOM   3026  CD2 TYR A 182     -34.246  18.580 113.275  1.00 30.25
ATOM   3027  CE1 TYR A 182     -32.753  19.680 115.329  1.00 31.47
ATOM   3028  CE2 TYR A 182     -34.025  17.846 114.447  1.00 32.16
ATOM   3029  CZ  TYR A 182     -33.290  18.407 115.478  1.00 40.09
ATOM   3030  OH  TYR A 182     -33.097  17.694 116.633  1.00 40.79
ATOM   3040  N   HIS A 183     -30.832  18.943 111.634  1.00 31.53
ATOM   3041  CA  HIS A 183     -30.176  17.641 111.702  1.00 31.40
ATOM   3042  C   HIS A 183     -30.002  17.333 113.173  1.00 41.29
ATOM   3043  O   HIS A 183     -29.332  18.087 113.887  1.00 42.88
ATOM   3044  CB  HIS A 183     -28.841  17.640 110.984  1.00 30.92
ATOM   3045  CG  HIS A 183     -28.983  17.901 109.518  1.00 33.47
ATOM   3046  CD2 HIS A 183     -29.599  16.995 108.661  1.00 34.13
ATOM   3047  ND1 HIS A 183     -28.572  18.958 108.796  1.00 34.91
ATOM   3048  CE1 HIS A 183     -28.902  18.696 107.488  1.00 33.31
ATOM   3049  NE2 HIS A 183     -29.520  17.528 107.457  1.00 33.68
ATOM   3057  N   PRO A 184     -30.624  16.246 113.664  1.00 39.79
ATOM   3058  CA  PRO A 184     -30.526  15.939 115.097  1.00 40.11
ATOM   3059  C   PRO A 184     -29.083  15.773 115.559  1.00 44.35
ATOM   3060  O   PRO A 184     -28.325  15.053 114.908  1.00 46.21
ATOM   3061  CB  PRO A 184     -31.355  14.649 115.238  1.00 41.23
ATOM   3062  CG  PRO A 184     -31.459  14.085 113.896  1.00 44.43
ATOM   3063  CD  PRO A 184     -31.445  15.240 112.956  1.00 40.59
ATOM   3071  N   GLY A 185     -28.716  16.464 116.640  1.00 38.59
ATOM   3072  CA  GLY A 185     -27.364  16.434 117.189  1.00 39.26
ATOM   3073  C   GLY A 185     -26.468  17.584 116.743  1.00 44.80
ATOM   3074  O   GLY A 185     -25.397  17.796 117.328  1.00 44.71
ATOM   3078  N   GLN A 186     -26.898  18.352 115.724  1.00 39.44
ATOM   3079  CA  GLN A 186     -26.104  19.462 115.261  1.00 39.68
ATOM   3080  C   GLN A 186     -26.072  20.645 116.263  1.00 45.20
ATOM   3081  O   GLN A 186     -27.086  21.035 116.834  1.00 43.72
ATOM   3082  CB  GLN A 186     -26.566  19.917 113.881  1.00 39.87
ATOM   3083  CG  GLN A 186     -25.708  21.025 113.315  1.00 43.19
ATOM   3084  CD  GLN A 186     -25.869  21.259 111.852  1.00 53.25
ATOM   3085  NE2 GLN A 186     -25.180  22.272 111.385  1.00 54.12
ATOM   3086  OE1 GLN A 186     -26.600  20.576 111.128  1.00 49.87
ATOM   3095  N   GLU A 187     -24.879  21.204 116.446  1.00 43.18
ATOM   3096  CA  GLU A 187     -24.652  22.356 117.294  1.00 41.66
ATOM   3097  C   GLU A 187     -24.595  23.526 116.350  1.00 44.34
ATOM   3098  O   GLU A 187     -23.651  23.656 115.563  1.00 46.86
ATOM   3099  CB  GLU A 187     -23.369  22.194 118.113  1.00 43.78
ATOM   3100  CG  GLU A 187     -23.485  21.080 119.131  1.00 43.92
ATOM   3101  CD  GLU A 187     -22.372  21.049 120.151  1.00 61.72
ATOM   3102  OE1 GLU A 187     -21.189  20.922 119.751  1.00 64.16
ATOM   3103  OE2 GLU A 187     -22.691  21.099 121.361  1.00 51.96
ATOM   3110  N   TYR A 188     -25.648  24.346 116.376  1.00 36.17
ATOM   3111  CA  TYR A 188     -25.789  25.482 115.479  1.00 33.85
ATOM   3112  C   TYR A 188     -25.223  26.769 116.042  1.00 41.14
ATOM   3113  O   TYR A 188     -24.990  26.880 117.242  1.00 41.63
ATOM   3114  CB  TYR A 188     -27.272  25.710 115.185  1.00 32.14
ATOM   3115  CG  TYR A 188     -27.906  24.605 114.399  1.00 29.78
ATOM   3116  CD1 TYR A 188     -27.723  24.510 113.017  1.00 30.89
ATOM   3117  CD2 TYR A 188     -28.662  23.618 115.033  1.00 30.11
ATOM   3118  CE1 TYR A 188     -28.294  23.465 112.280  1.00 32.12
ATOM   3119  CE2 TYR A 188     -29.208  22.554 114.316  1.00 30.83
ATOM   3120  CZ  TYR A 188     -29.022  22.481 112.938  1.00 38.48
ATOM   3121  OH  TYR A 188     -29.585  21.459 112.219  1.00 37.87
ATOM   3131  N   ASN A 189     -25.084  27.773 115.172  1.00 39.38
ATOM   3132  CA  ASN A 189     -24.648  29.101 115.547  1.00 40.95
ATOM   3133  C   ASN A 189     -25.789  29.755 116.301  1.00 45.44
ATOM   3134  O   ASN A 189     -26.917  29.745 115.836  1.00 44.70
ATOM   3135  CB  ASN A 189     -24.329  29.911 114.279  1.00 43.45
ATOM   3136  CG  ASN A 189     -23.779  31.297 114.474  1.00 52.10
ATOM   3137  ND2 ASN A 189     -23.480  31.931 113.382  1.00 49.23
ATOM   3138  OD1 ASN A 189     -23.609  31.807 115.575  1.00 55.96
ATOM   3145  N   VAL A 190     -25.500  30.351 117.445  1.00 44.35
ATOM   3146  CA  VAL A 190     -26.531  31.048 118.211  1.00 43.20
ATOM   3147  C   VAL A 190     -26.710  32.518 117.765  1.00 48.50
ATOM   3148  O   VAL A 190     -27.634  33.175 118.216  1.00 48.51
ATOM   3149  CB  VAL A 190     -26.358  30.891 119.744  1.00 45.30
ATOM   3150  CG1 VAL A 190     -26.407  29.430 120.169  1.00 43.86
ATOM   3151  CG2 VAL A 190     -25.091  31.580 120.246  1.00 46.21
ATOM   3161  N   ARG A 191     -25.828  33.030 116.904  1.00 48.27
ATOM   3162  CA  ARG A 191     -25.890  34.415 116.405  1.00 49.28
ATOM   3163  C   ARG A 191     -26.860  34.519 115.224  1.00 52.74
ATOM   3164  O   ARG A 191     -26.476  34.799 114.081  1.00 52.36
ATOM   3165  CB  ARG A 191     -24.488  34.934 116.078  1.00 50.18
ATOM   3166  CG  ARG A 191     -23.618  35.034 117.339  1.00 77.23
ATOM   3167  CD  ARG A 191     -22.797  36.308 117.447  1.00104.77
ATOM   3168  NE  ARG A 191     -23.194  37.157 118.583  1.00123.35
ATOM   3169  CZ  ARG A 191     -22.697  37.060 119.814  1.00139.09
ATOM   3170  NH1 ARG A 191     -23.099  37.894 120.765  1.00126.79
ATOM   3171  NH2 ARG A 191     -21.775  36.146 120.097  1.00125.08
ATOM   3185  N   VAL A 192     -28.118  34.186 115.515  1.00 46.90
ATOM   3186  CA  VAL A 192     -29.209  34.180 114.549  1.00 45.61
ATOM   3187  C   VAL A 192     -30.376  34.978 115.149  1.00 47.72
ATOM   3188  O   VAL A 192     -30.306  35.390 116.308  1.00 46.10
ATOM   3189  CB  VAL A 192     -29.610  32.741 114.087  1.00 48.59
ATOM   3190  CG1 VAL A 192     -28.428  32.024 113.429  1.00 47.68
ATOM   3191  CG2 VAL A 192     -30.181  31.909 115.244  1.00 48.38
ATOM   3201  N   ALA A 193     -31.435  35.196 114.357  1.00 44.26
ATOM   3202  CA  ALA A 193     -32.631  35.953 114.743  1.00 43.78
ATOM   3203  C   ALA A 193     -32.265  37.418 115.046  1.00 50.19
ATOM   3204  O   ALA A 193     -31.117  37.815 114.896  1.00 53.52
ATOM   3205  CB  ALA A 193     -33.350  35.285 115.934  1.00 43.85
ATOM   3211  N   SER A 194     -33.236  38.232 115.417  1.00 44.16
ATOM   3212  CA  SER A 194     -33.016  39.620 115.781  1.00 43.19
ATOM   3213  C   SER A 194     -33.137  39.665 117.298  1.00 47.43
ATOM   3214  O   SER A 194     -33.949  38.922 117.846  1.00 47.74
ATOM   3215  CB  SER A 194     -34.074  40.508 115.129  1.00 48.17
ATOM   3216  OG  SER A 194     -34.586  41.477 116.048  1.00 64.46
ATOM   3222  N   ARG A 195     -32.351  40.519 117.994  1.00 44.79
ATOM   3223  CA  ARG A 195     -32.301  40.607 119.453  1.00 43.69
ATOM   3224  C   ARG A 195     -33.595  40.342 120.180  1.00 49.37
ATOM   3225  O   ARG A 195     -33.629  39.479 121.047  1.00 50.26
ATOM   3226  CB  ARG A 195     -31.724  41.933 119.907  1.00 41.96
ATOM   3227  CG  ARG A 195     -31.488  41.959 121.416  1.00 50.29
ATOM   3228  CD  ARG A 195     -30.282  42.748 121.724  1.00 60.99
ATOM   3229  NE  ARG A 195     -30.683  44.117 121.914  1.00 61.40
ATOM   3230  CZ  ARG A 195     -30.236  45.142 121.212  1.00 68.99
ATOM   3231  NH1 ARG A 195     -30.694  46.356 121.451  1.00 60.21
ATOM   3232  NH2 ARG A 195     -29.338  44.957 120.257  1.00 55.73
ATOM   3246  N   TYR A 196     -34.644  41.105 119.864  1.00 46.27
ATOM   3247  CA  TYR A 196     -35.919  41.055 120.568  1.00 46.50
ATOM   3248  C   TYR A 196     -36.678  39.749 120.439  1.00 46.23
ATOM   3249  O   TYR A 196     -37.543  39.438 121.279  1.00 45.03
ATOM   3250  CB  TYR A 196     -36.793  42.269 120.192  1.00 48.74
ATOM   3251  CG  TYR A 196     -36.087  43.604 120.326  1.00 51.98
ATOM   3252  CD1 TYR A 196     -35.304  43.897 121.448  1.00 55.51
ATOM   3253  CD2 TYR A 196     -36.210  44.579 119.345  1.00 52.18
ATOM   3254  CE1 TYR A 196     -34.661  45.119 121.579  1.00 56.50
ATOM   3255  CE2 TYR A 196     -35.578  45.808 119.473  1.00 54.10
ATOM   3256  CZ  TYR A 196     -34.799  46.067 120.589  1.00 62.14
ATOM   3257  OH  TYR A 196     -34.111  47.235 120.731  1.00 68.63
ATOM   3267  N   PHE A 197     -36.316  38.966 119.406  1.00 39.46
ATOM   3268  CA  PHE A 197     -36.950  37.690 119.056  1.00 35.64
ATOM   3269  C   PHE A 197     -36.093  36.467 119.338  1.00 39.16
ATOM   3270  O   PHE A 197     -36.538  35.343 119.107  1.00 37.55
ATOM   3271  CB  PHE A 197     -37.438  37.733 117.611  1.00 35.65
ATOM   3272  CG  PHE A 197     -38.324  38.920 117.378  1.00 36.58
ATOM   3273  CD1 PHE A 197     -39.688  38.847 117.638  1.00 37.91
ATOM   3274  CD2 PHE A 197     -37.783  40.150 117.009  1.00 37.87
ATOM   3275  CE1 PHE A 197     -40.490  39.983 117.525  1.00 38.63
ATOM   3276  CE2 PHE A 197     -38.592  41.272 116.878  1.00 39.38
ATOM   3277  CZ  PHE A 197     -39.933  41.181 117.144  1.00 37.26
ATOM   3287  N   LYS A 198     -34.895  36.676 119.918  1.00 38.23
ATOM   3288  CA  LYS A 198     -33.974  35.611 120.266  1.00 37.89
ATOM   3289  C   LYS A 198     -34.507  34.795 121.415  1.00 42.67
ATOM   3290  O   LYS A 198     -34.843  35.331 122.452  1.00 44.45
ATOM   3291  CB  LYS A 198     -32.603  36.179 120.636  1.00 40.72
ATOM   3292  CG  LYS A 198     -31.787  36.654 119.455  1.00 37.53
ATOM   3293  CD  LYS A 198     -30.473  37.262 119.974  1.00 51.50
ATOM   3294  CE  LYS A 198     -29.662  37.981 118.917  1.00 43.20
ATOM   3295  NZ  LYS A 198     -28.888  37.048 118.089  1.00 45.92
ATOM   3309  N   GLY A 199     -34.564  33.498 121.229  1.00 39.34
ATOM   3310  CA  GLY A 199     -34.987  32.597 122.281  1.00 37.60
ATOM   3311  C   GLY A 199     -33.931  32.476 123.351  1.00 40.32
ATOM   3312  O   GLY A 199     -32.742  32.676 123.075  1.00 39.80
ATOM   3316  N   PRO A 200     -34.343  32.107 124.594  1.00 37.89
ATOM   3317  CA  PRO A 200     -33.350  31.963 125.680  1.00 38.96
ATOM   3318  C   PRO A 200     -32.189  31.024 125.345  1.00 43.75
ATOM   3319  O   PRO A 200     -31.065  31.283 125.783  1.00 42.79
ATOM   3320  CB  PRO A 200     -34.168  31.501 126.877  1.00 40.06
ATOM   3321  CG  PRO A 200     -35.518  31.274 126.379  1.00 42.45
ATOM   3322  CD  PRO A 200     -35.721  31.880 125.073  1.00 36.71
ATOM   3330  N   GLU A 201     -32.433  29.990 124.511  1.00 40.94
ATOM   3331  CA  GLU A 201     -31.377  29.062 124.083  1.00 40.61
ATOM   3332  C   GLU A 201     -30.227  29.817 123.376  1.00 46.74
ATOM   3333  O   GLU A 201     -29.056  29.478 123.569  1.00 48.90
ATOM   3334  CB  GLU A 201     -31.922  27.915 123.204  1.00 39.23
ATOM   3335  CG  GLU A 201     -32.672  28.329 121.949  1.00 33.97
ATOM   3336  CD  GLU A 201     -34.165  28.500 122.089  1.00 43.74
ATOM   3337  OE1 GLU A 201     -34.604  29.281 122.965  1.00 47.99
ATOM   3338  OE2 GLU A 201     -34.902  27.867 121.298  1.00 45.89
ATOM   3345  N   LEU A 202     -30.557  30.858 122.607  1.00 40.55
ATOM   3346  CA  LEU A 202     -29.535  31.645 121.925  1.00 40.21
ATOM   3347  C   LEU A 202     -28.784  32.498 122.931  1.00 48.44
ATOM   3348  O   LEU A 202     -27.552  32.541 122.899  1.00 51.14
ATOM   3349  CB  LEU A 202     -30.142  32.517 120.831  1.00 37.92
ATOM   3350  CG  LEU A 202     -31.043  31.832 119.793  1.00 40.35
ATOM   3351  CD1 LEU A 202     -31.472  32.835 118.714  1.00 40.18
ATOM   3352  CD2 LEU A 202     -30.373  30.650 119.143  1.00 39.66
ATOM   3364  N   LEU A 203     -29.532  33.129 123.861  1.00 43.59
ATOM   3365  CA  LEU A 203     -29.013  34.038 124.889  1.00 42.76
ATOM   3366  C   LEU A 203     -28.050  33.408 125.887  1.00 46.89
ATOM   3367  O   LEU A 203     -27.093  34.072 126.296  1.00 47.63
ATOM   3368  CB  LEU A 203     -30.158  34.765 125.566  1.00 42.46
ATOM   3369  CG  LEU A 203     -31.116  35.483 124.585  1.00 45.69
ATOM   3370  CD1 LEU A 203     -32.314  36.048 125.312  1.00 46.22
ATOM   3371  CD2 LEU A 203     -30.395  36.578 123.769  1.00 44.28
ATOM   3383  N   VAL A 204     -28.273  32.119 126.228  1.00 43.40
ATOM   3384  CA  VAL A 204     -27.437  31.327 127.138  1.00 44.29
ATOM   3385  C   VAL A 204     -26.393  30.469 126.389  1.00 51.91
ATOM   3386  O   VAL A 204     -25.631  29.722 127.025  1.00 52.51
ATOM   3387  CB  VAL A 204     -28.261  30.474 128.133  1.00 46.48
ATOM   3388  CG1 VAL A 204     -29.234  31.328 128.930  1.00 45.85
ATOM   3389  CG2 VAL A 204     -28.978  29.323 127.440  1.00 44.73
ATOM   3399  N   ASP A 205     -26.368  30.571 125.049  1.00 49.46
ATOM   3400  CA  ASP A 205     -25.442  29.823 124.200  1.00 50.28
ATOM   3401  C   ASP A 205     -25.649  28.290 124.261  1.00 54.31
ATOM   3402  O   ASP A 205     -24.707  27.528 124.465  1.00 56.71
ATOM   3403  CB  ASP A 205     -23.983  30.281 124.421  1.00 54.18
ATOM   3404  CG  ASP A 205     -22.988  29.876 123.359  1.00 72.27
ATOM   3405  OD1 ASP A 205     -23.424  29.395 122.279  1.00 72.61
ATOM   3406  OD2 ASP A 205     -21.769  30.028 123.603  1.00 85.32
ATOM   3411  N   TYR A 206     -26.904  27.846 124.098  1.00 47.65
ATOM   3412  CA  TYR A 206     -27.226  26.430 124.001  1.00 45.13
ATOM   3413  C   TYR A 206     -27.417  26.170 122.524  1.00 47.41
ATOM   3414  O   TYR A 206     -28.397  26.629 121.935  1.00 46.81
ATOM   3415  CB  TYR A 206     -28.451  26.036 124.820  1.00 44.19
ATOM   3416  CG  TYR A 206     -28.716  24.549 124.713  1.00 43.63
ATOM   3417  CD1 TYR A 206     -27.975  23.633 125.457  1.00 44.51
ATOM   3418  CD2 TYR A 206     -29.645  24.051 123.808  1.00 44.73
ATOM   3419  CE1 TYR A 206     -28.160  22.261 125.313  1.00 40.27
ATOM   3420  CE2 TYR A 206     -29.870  22.677 123.685  1.00 46.47
ATOM   3421  CZ  TYR A 206     -29.124  21.787 124.444  1.00 48.40
ATOM   3422  OH  TYR A 206     -29.313  20.436 124.321  1.00 47.55
ATOM   3432  N   GLN A 207     -26.451  25.475 121.917  1.00 43.42
ATOM   3433  CA  GLN A 207     -26.379  25.289 120.470  1.00 41.00
ATOM   3434  C   GLN A 207     -27.236  24.215 119.833  1.00 44.96
ATOM   3435  O   GLN A 207     -27.485  24.284 118.626  1.00 45.03
ATOM   3436  CB  GLN A 207     -24.937  25.086 120.051  1.00 42.59
ATOM   3437  CG  GLN A 207     -24.024  26.254 120.376  1.00 33.35
ATOM   3438  CD  GLN A 207     -22.659  25.962 119.840  1.00 52.87
ATOM   3439  NE2 GLN A 207     -22.439  26.281 118.568  1.00 47.67
ATOM   3440  OE1 GLN A 207     -21.835  25.339 120.509  1.00 50.79
ATOM   3449  N   MET A 208     -27.643  23.200 120.590  1.00 41.84
ATOM   3450  CA  MET A 208     -28.404  22.079 120.030  1.00 39.64
ATOM   3451  C   MET A 208     -29.890  22.369 119.970  1.00 41.96
ATOM   3452  O   MET A 208     -30.720  21.605 120.486  1.00 42.62
ATOM   3453  CB  MET A 208     -28.078  20.788 120.790  1.00 42.34
ATOM   3454  CG  MET A 208     -28.097  19.576 119.893  1.00 45.03
ATOM   3455  SD  MET A 208     -27.543  18.091 120.737  1.00 47.75
ATOM   3456  CE  MET A 208     -25.816  18.315 120.691  1.00 42.98
ATOM   3466  N   TYR A 209     -30.234  23.506 119.347  1.00 35.50
ATOM   3467  CA  TYR A 209     -31.621  23.948 119.253  1.00 32.71
ATOM   3468  C   TYR A 209     -32.305  23.386 118.002  1.00 37.34
ATOM   3469  O   TYR A 209     -31.684  22.661 117.199  1.00 35.34
ATOM   3470  CB  TYR A 209     -31.713  25.473 119.401  1.00 33.03
ATOM   3471  CG  TYR A 209     -31.015  26.259 118.306  1.00 34.87
ATOM   3472  CD1 TYR A 209     -31.601  26.416 117.054  1.00 35.16
ATOM   3473  CD2 TYR A 209     -29.818  26.929 118.554  1.00 36.26
ATOM   3474  CE1 TYR A 209     -30.989  27.158 116.057  1.00 35.71
ATOM   3475  CE2 TYR A 209     -29.184  27.666 117.551  1.00 36.99
ATOM   3476  CZ  TYR A 209     -29.791  27.798 116.311  1.00 42.85
ATOM   3477  OH  TYR A 209     -29.214  28.512 115.284  1.00 40.69
ATOM   3487  N   ASP A 210     -33.598  23.688 117.848  1.00 35.17
ATOM   3488  CA  ASP A 210     -34.355  23.127 116.742  1.00 33.91
ATOM   3489  C   ASP A 210     -35.466  24.088 116.289  1.00 38.12
ATOM   3490  O   ASP A 210     -35.422  25.279 116.615  1.00 37.75
ATOM   3491  CB  ASP A 210     -34.903  21.741 117.164  1.00 35.21
ATOM   3492  CG  ASP A 210     -35.739  21.749 118.424  1.00 44.51
ATOM   3493  OD1 ASP A 210     -36.849  22.342 118.396  1.00 43.56
ATOM   3494  OD2 ASP A 210     -35.313  21.114 119.429  1.00 44.79
ATOM   3499  N   TYR A 211     -36.475  23.562 115.566  1.00 32.11
ATOM   3500  CA  TYR A 211     -37.646  24.305 115.098  1.00 30.44
ATOM   3501  C   TYR A 211     -38.318  25.133 116.188  1.00 33.74
ATOM   3502  O   TYR A 211     -38.918  26.161 115.892  1.00 33.55
ATOM   3503  CB  TYR A 211     -38.711  23.328 114.580  1.00 31.73
ATOM   3504  CG  TYR A 211     -38.201  22.206 113.709  1.00 31.92
ATOM   3505  CD1 TYR A 211     -37.674  22.464 112.442  1.00 33.43
ATOM   3506  CD2 TYR A 211     -38.318  20.879 114.113  1.00 32.15
ATOM   3507  CE1 TYR A 211     -37.252  21.427 111.611  1.00 34.22
ATOM   3508  CE2 TYR A 211     -37.872  19.833 113.299  1.00 33.61
ATOM   3509  CZ  TYR A 211     -37.358  20.113 112.041  1.00 39.25
ATOM   3510  OH  TYR A 211     -36.967  19.098 111.214  1.00 36.44
ATOM   3520  N   SER A 212     -38.285  24.647 117.437  1.00 33.30
ATOM   3521  CA  SER A 212     -38.907  25.320 118.577  1.00 34.08
ATOM   3522  C   SER A 212     -38.412  26.748 118.786  1.00 39.75
ATOM   3523  O   SER A 212     -39.125  27.545 119.403  1.00 41.67
ATOM   3524  CB  SER A 212     -38.758  24.496 119.846  1.00 34.74
ATOM   3525  OG  SER A 212     -37.393  24.241 120.113  1.00 39.50
ATOM   3531  N   LEU A 213     -37.221  27.080 118.238  1.00 35.64
ATOM   3532  CA  LEU A 213     -36.674  28.443 118.245  1.00 34.69
ATOM   3533  C   LEU A 213     -37.689  29.394 117.615  1.00 37.14
ATOM   3534  O   LEU A 213     -37.937  30.454 118.169  1.00 39.07
ATOM   3535  CB  LEU A 213     -35.351  28.510 117.448  1.00 33.81
ATOM   3536  CG  LEU A 213     -34.750  29.913 117.299  1.00 38.95
ATOM   3537  CD1 LEU A 213     -34.421  30.560 118.677  1.00 40.17
ATOM   3538  CD2 LEU A 213     -33.547  29.903 116.366  1.00 37.34
ATOM   3550  N   ASP A 214     -38.277  29.000 116.472  1.00 30.76
ATOM   3551  CA  ASP A 214     -39.243  29.814 115.754  1.00 29.98
ATOM   3552  C   ASP A 214     -40.513  30.066 116.549  1.00 37.22
ATOM   3553  O   ASP A 214     -41.164  31.100 116.359  1.00 38.32
ATOM   3554  CB  ASP A 214     -39.590  29.182 114.407  1.00 30.04
ATOM   3555  CG  ASP A 214     -38.480  29.124 113.390  1.00 33.86
ATOM   3556  OD1 ASP A 214     -37.587  29.989 113.434  1.00 31.97
ATOM   3557  OD2 ASP A 214     -38.554  28.278 112.494  1.00 40.39
ATOM   3562  N   MET A 215     -40.879  29.106 117.417  1.00 33.88
ATOM   3563  CA  MET A 215     -42.073  29.192 118.261  1.00 31.75
ATOM   3564  C   MET A 215     -41.895  30.214 119.367  1.00 34.54
ATOM   3565  O   MET A 215     -42.839  30.921 119.700  1.00 37.43
ATOM   3566  CB  MET A 215     -42.472  27.808 118.757  1.00 33.37
ATOM   3567  CG  MET A 215     -42.728  26.813 117.606  1.00 35.60
ATOM   3568  SD  MET A 215     -43.926  27.391 116.366  1.00 38.20
ATOM   3569  CE  MET A 215     -45.448  27.529 117.385  1.00 34.29
ATOM   3579  N   TRP A 216     -40.677  30.374 119.875  1.00 30.38
ATOM   3580  CA  TRP A 216     -40.408  31.439 120.849  1.00 31.04
ATOM   3581  C   TRP A 216     -40.640  32.798 120.144  1.00 37.22
ATOM   3582  O   TRP A 216     -41.343  33.660 120.672  1.00 37.19
ATOM   3583  CB  TRP A 216     -38.951  31.366 121.375  1.00 29.33
ATOM   3584  CG  TRP A 216     -38.604  32.554 122.220  1.00 31.37
ATOM   3585  CD1 TRP A 216     -38.131  33.760 121.785  1.00 35.15
ATOM   3586  CD2 TRP A 216     -38.832  32.698 123.627  1.00 32.30
ATOM   3587  CE2 TRP A 216     -38.457  34.019 123.984  1.00 37.67
ATOM   3588  CE3 TRP A 216     -39.330  31.845 124.624  1.00 33.71
ATOM   3589  NE1 TRP A 216     -38.005  34.636 122.843  1.00 36.16
ATOM   3590  CZ2 TRP A 216     -38.544  34.494 125.297  1.00 37.27
ATOM   3591  CZ3 TRP A 216     -39.397  32.312 125.921  1.00 35.85
ATOM   3592  CH2 TRP A 216     -39.008  33.622 126.247  1.00 37.25
ATOM   3603  N   SER A 217     -40.017  32.986 118.957  1.00 35.38
ATOM   3604  CA  SER A 217     -40.116  34.214 118.177  1.00 36.31
ATOM   3605  C   SER A 217     -41.564  34.564 117.900  1.00 42.09
ATOM   3606  O   SER A 217     -41.956  35.725 118.039  1.00 42.06
ATOM   3607  CB  SER A 217     -39.331  34.087 116.878  1.00 38.65
ATOM   3608  OG  SER A 217     -37.971  33.771 117.127  1.00 41.69
ATOM   3614  N   LEU A 218     -42.379  33.547 117.560  1.00 39.15
ATOM   3615  CA  LEU A 218     -43.811  33.729 117.329  1.00 37.56
ATOM   3616  C   LEU A 218     -44.507  34.242 118.579  1.00 41.72
ATOM   3617  O   LEU A 218     -45.362  35.128 118.489  1.00 43.82
ATOM   3618  CB  LEU A 218     -44.442  32.427 116.839  1.00 36.56
ATOM   3619  CG  LEU A 218     -45.864  32.565 116.306  1.00 40.74
ATOM   3620  CD1 LEU A 218     -45.928  33.419 115.028  1.00 38.36
ATOM   3621  CD2 LEU A 218     -46.476  31.218 116.083  1.00 40.74
ATOM   3633  N   GLY A 219     -44.143  33.693 119.729  1.00 37.01
ATOM   3634  CA  GLY A 219     -44.689  34.121 121.011  1.00 37.99
ATOM   3635  C   GLY A 219     -44.350  35.570 121.310  1.00 43.09
ATOM   3636  O   GLY A 219     -45.203  36.320 121.794  1.00 43.79
ATOM   3640  N   CYS A 220     -43.122  36.006 120.963  1.00 38.69
ATOM   3641  CA  CYS A 220     -42.721  37.421 121.110  1.00 38.70
ATOM   3642  C   CYS A 220     -43.617  38.320 120.256  1.00 44.50
ATOM   3643  O   CYS A 220     -44.027  39.389 120.710  1.00 46.87
ATOM   3644  CB  CYS A 220     -41.263  37.613 120.739  1.00 37.84
ATOM   3645  SG  CYS A 220     -40.100  36.782 121.843  1.00 41.53
ATOM   3651  N   MET A 221     -43.919  37.886 119.022  1.00 39.92
ATOM   3652  CA  MET A 221     -44.802  38.618 118.123  1.00 40.51
ATOM   3653  C   MET A 221     -46.190  38.702 118.688  1.00 46.25
ATOM   3654  O   MET A 221     -46.764  39.794 118.731  1.00 46.97
ATOM   3655  CB  MET A 221     -44.859  37.951 116.764  1.00 42.38
ATOM   3656  CG  MET A 221     -43.649  38.225 115.936  1.00 46.30
ATOM   3657  SD  MET A 221     -43.845  37.537 114.283  1.00 51.23
ATOM   3658  CE  MET A 221     -45.260  38.422 113.709  1.00 48.34
ATOM   3668  N   LEU A 222     -46.731  37.561 119.162  1.00 41.73
ATOM   3669  CA  LEU A 222     -48.072  37.542 119.737  1.00 42.43
ATOM   3670  C   LEU A 222     -48.193  38.469 120.941  1.00 48.26
ATOM   3671  O   LEU A 222     -49.140  39.253 121.015  1.00 51.19
ATOM   3672  CB  LEU A 222     -48.465  36.122 120.089  1.00 42.08
ATOM   3673  CG  LEU A 222     -49.839  35.899 120.719  1.00 46.79
ATOM   3674  CD1 LEU A 222     -50.980  36.244 119.748  1.00 48.28
ATOM   3675  CD2 LEU A 222     -49.950  34.483 121.262  1.00 43.23
ATOM   3687  N   ALA A 223     -47.224  38.427 121.857  1.00 43.41
ATOM   3688  CA  ALA A 223     -47.251  39.282 123.039  1.00 43.89
ATOM   3689  C   ALA A 223     -47.258  40.772 122.635  1.00 51.93
ATOM   3690  O   ALA A 223     -48.045  41.550 123.184  1.00 54.06
ATOM   3691  CB  ALA A 223     -46.066  38.970 123.936  1.00 43.67
ATOM   3697  N   SER A 224     -46.445  41.156 121.632  1.00 48.46
ATOM   3698  CA  SER A 224     -46.414  42.547 121.175  1.00 49.82
ATOM   3699  C   SER A 224     -47.737  42.982 120.564  1.00 54.37
ATOM   3700  O   SER A 224     -48.110  44.134 120.728  1.00 56.17
ATOM   3701  CB  SER A 224     -45.266  42.799 120.198  1.00 52.83
ATOM   3702  OG  SER A 224     -45.521  42.237 118.922  1.00 62.52
ATOM   3708  N   MET A 225     -48.449  42.057 119.897  1.00 49.23
ATOM   3709  CA  MET A 225     -49.732  42.318 119.258  1.00 49.54
ATOM   3710  C   MET A 225     -50.872  42.430 120.247  1.00 53.82
ATOM   3711  O   MET A 225     -51.582  43.435 120.244  1.00 55.72
ATOM   3712  CB  MET A 225     -50.024  41.273 118.187  1.00 51.07
ATOM   3713  CG  MET A 225     -49.096  41.389 117.007  1.00 54.93
ATOM   3714  SD  MET A 225     -49.109  39.941 115.927  1.00 58.66
ATOM   3715  CE  MET A 225     -50.266  40.386 114.853  1.00 56.72
ATOM   3725  N   ILE A 226     -51.051  41.424 121.103  1.00 48.25
ATOM   3726  CA  ILE A 226     -52.153  41.443 122.067  1.00 47.65
ATOM   3727  C   ILE A 226     -51.966  42.481 123.172  1.00 54.66
ATOM   3728  O   ILE A 226     -52.961  42.993 123.675  1.00 58.12
ATOM   3729  CB  ILE A 226     -52.536  40.033 122.584  1.00 47.48
ATOM   3730  CG1 ILE A 226     -51.467  39.461 123.523  1.00 45.29
ATOM   3731  CG2 ILE A 226     -52.892  39.084 121.415  1.00 44.56
ATOM   3732  CD1 ILE A 226     -51.904  38.201 124.292  1.00 36.88
ATOM   3744  N   PHE A 227     -50.709  42.826 123.516  1.00 49.47
ATOM   3745  CA  PHE A 227     -50.439  43.813 124.560  1.00 50.41
ATOM   3746  C   PHE A 227     -50.124  45.200 124.063  1.00 57.43
ATOM   3747  O   PHE A 227     -50.032  46.127 124.885  1.00 59.20
ATOM   3748  CB  PHE A 227     -49.348  43.344 125.517  1.00 50.94
ATOM   3749  CG  PHE A 227     -49.671  42.081 126.271  1.00 52.45
ATOM   3750  CD1 PHE A 227     -50.892  41.932 126.929  1.00 56.93
ATOM   3751  CD2 PHE A 227     -48.740  41.059 126.368  1.00 53.26
ATOM   3752  CE1 PHE A 227     -51.179  40.773 127.643  1.00 57.29
ATOM   3753  CE2 PHE A 227     -49.019  39.906 127.092  1.00 55.82
ATOM   3754  CZ  PHE A 227     -50.238  39.770 127.723  1.00 55.75
ATOM   3764  N   ARG A 228     -49.986  45.364 122.725  1.00 54.31
ATOM   3765  CA  ARG A 228     -49.633  46.652 122.106  1.00 55.43
ATOM   3766  C   ARG A 228     -48.356  47.198 122.755  1.00 62.63
ATOM   3767  O   ARG A 228     -48.329  48.327 123.245  1.00 63.63
ATOM   3768  CB  ARG A 228     -50.788  47.658 122.144  1.00 54.35
ATOM   3769  CG  ARG A 228     -51.962  47.187 121.343  1.00 67.18
ATOM   3770  CD  ARG A 228     -52.972  48.283 121.169  1.00 92.04
ATOM   3771  NE  ARG A 228     -53.882  47.955 120.081  1.00106.71
ATOM   3772  CZ  ARG A 228     -54.954  48.668 119.765  1.00130.04
ATOM   3773  NH1 ARG A 228     -55.249  49.772 120.443  1.00123.76
ATOM   3774  NH2 ARG A 228     -55.740  48.287 118.766  1.00118.35
ATOM   3788  N   LYS A 229     -47.322  46.344 122.821  1.00 59.83
ATOM   3789  CA  LYS A 229     -46.032  46.691 123.399  1.00 60.84
ATOM   3790  C   LYS A 229     -45.027  46.096 122.435  1.00 68.58
ATOM   3791  O   LYS A 229     -44.729  44.897 122.496  1.00 67.66
ATOM   3792  CB  LYS A 229     -45.887  46.146 124.828  1.00 61.79
ATOM   3793  CG  LYS A 229     -44.567  46.535 125.508  1.00 66.37
ATOM   3794  CD  LYS A 229     -44.441  45.917 126.911  1.00 79.29
ATOM   3795  CE  LYS A 229     -43.125  46.294 127.545  1.00 96.71
ATOM   3796  NZ  LYS A 229     -42.555  45.178 128.356  1.00109.92
ATOM   3810  N   GLU A 230     -44.576  46.928 121.480  1.00 67.34
ATOM   3811  CA  GLU A 230     -43.671  46.498 120.428  1.00 66.16
ATOM   3812  C   GLU A 230     -42.269  47.117 120.583  1.00 71.77
ATOM   3813  O   GLU A 230     -42.146  48.330 120.505  1.00 74.03
ATOM   3814  CB  GLU A 230     -44.288  46.775 119.058  1.00 67.25
ATOM   3815  CG  GLU A 230     -43.920  45.745 117.994  1.00 84.25
ATOM   3816  CD  GLU A 230     -42.480  45.734 117.504  1.00115.47
ATOM   3817  OE1 GLU A 230     -41.923  46.824 117.242  1.00122.92
ATOM   3818  OE2 GLU A 230     -41.911  44.629 117.365  1.00107.30
ATOM   3825  N   PRO A 231     -41.206  46.317 120.829  1.00 66.84
ATOM   3826  CA  PRO A 231     -41.209  44.858 121.030  1.00 64.18
ATOM   3827  C   PRO A 231     -41.588  44.541 122.475  1.00 68.42
ATOM   3828  O   PRO A 231     -41.519  45.408 123.355  1.00 71.99
ATOM   3829  CB  PRO A 231     -39.757  44.485 120.733  1.00 64.97
ATOM   3830  CG  PRO A 231     -38.996  45.647 121.312  1.00 71.82
ATOM   3831  CD  PRO A 231     -39.847  46.870 121.015  1.00 68.57
ATOM   3839  N   PHE A 232     -41.975  43.300 122.734  1.00 61.75
ATOM   3840  CA  PHE A 232     -42.367  42.906 124.088  1.00 58.39
ATOM   3841  C   PHE A 232     -41.193  42.844 125.071  1.00 60.66
ATOM   3842  O   PHE A 232     -41.316  43.358 126.182  1.00 62.60
ATOM   3843  CB  PHE A 232     -43.161  41.608 124.062  1.00 56.80
ATOM   3844  CG  PHE A 232     -43.792  41.321 125.395  1.00 57.49
ATOM   3845  CD1 PHE A 232     -44.836  42.104 125.872  1.00 60.53
ATOM   3846  CD2 PHE A 232     -43.350  40.263 126.178  1.00 57.50
ATOM   3847  CE1 PHE A 232     -45.416  41.842 127.119  1.00 61.74
ATOM   3848  CE2 PHE A 232     -43.940  39.998 127.421  1.00 60.30
ATOM   3849  CZ  PHE A 232     -44.964  40.792 127.884  1.00 59.39
ATOM   3859  N   PHE A 233     -40.080  42.201 124.674  1.00 53.74
ATOM   3860  CA  PHE A 233     -38.873  42.091 125.493  1.00 54.40
ATOM   3861  C   PHE A 233     -37.845  43.012 124.846  1.00 65.68
ATOM   3862  O   PHE A 233     -37.337  42.718 123.755  1.00 65.33
ATOM   3863  CB  PHE A 233     -38.378  40.642 125.527  1.00 53.81
ATOM   3864  CG  PHE A 233     -39.327  39.621 126.111  1.00 53.22
ATOM   3865  CD1 PHE A 233     -39.704  39.680 127.452  1.00 54.28
ATOM   3866  CD2 PHE A 233     -39.786  38.559 125.344  1.00 51.89
ATOM   3867  CE1 PHE A 233     -40.528  38.699 128.002  1.00 53.45
ATOM   3868  CE2 PHE A 233     -40.604  37.573 125.899  1.00 53.07
ATOM   3869  CZ  PHE A 233     -40.965  37.646 127.219  1.00 51.43
ATOM   3879  N   HIS A 234     -37.587  44.164 125.473  1.00 66.98
ATOM   3880  CA  HIS A 234     -36.781  45.229 124.892  1.00 67.84
ATOM   3881  C   HIS A 234     -35.401  45.369 125.511  1.00 73.58
ATOM   3882  O   HIS A 234     -35.111  46.374 126.143  1.00 75.91
ATOM   3883  CB  HIS A 234     -37.597  46.528 124.995  1.00 70.08
ATOM   3884  CG  HIS A 234     -37.081  47.674 124.181  1.00 74.32
ATOM   3885  CD2 HIS A 234     -36.833  47.753 122.857  1.00 74.61
ATOM   3886  ND1 HIS A 234     -36.808  48.900 124.758  1.00 78.35
ATOM   3887  CE1 HIS A 234     -36.403  49.676 123.770  1.00 77.98
ATOM   3888  NE2 HIS A 234     -36.425  49.034 122.606  1.00 76.06
ATOM   3896  N   GLY A 235     -34.557  44.370 125.326  1.00 69.54
ATOM   3897  CA  GLY A 235     -33.212  44.398 125.887  1.00 71.34
ATOM   3898  C   GLY A 235     -32.270  45.329 125.164  1.00 79.11
ATOM   3899  O   GLY A 235     -32.418  45.544 123.962  1.00 78.26
ATOM   3903  N   HIS A 236     -31.297  45.886 125.894  1.00 80.02
ATOM   3904  CA  HIS A 236     -30.309  46.825 125.332  1.00 82.44
ATOM   3905  C   HIS A 236     -29.189  46.092 124.567  1.00 80.59
ATOM   3906  O   HIS A 236     -28.496  46.696 123.741  1.00 79.18
ATOM   3907  CB  HIS A 236     -29.709  47.717 126.449  1.00 87.85
ATOM   3908  CG  HIS A 236     -30.703  48.587 127.186  1.00 94.63
ATOM   3909  CD2 HIS A 236     -31.939  49.020 126.816  1.00 97.25
ATOM   3910  ND1 HIS A 236     -30.412  49.108 128.454  1.00 99.36
ATOM   3911  CE1 HIS A 236     -31.467  49.833 128.802  1.00100.16
ATOM   3912  NE2 HIS A 236     -32.413  49.811 127.854  1.00 99.31
ATOM   3920  N   ASP A 237     -29.003  44.792 124.870  1.00 73.47
ATOM   3921  CA  ASP A 237     -27.968  43.934 124.286  1.00 70.41
ATOM   3922  C   ASP A 237     -28.408  42.476 124.535  1.00 69.26
ATOM   3923  O   ASP A 237     -29.485  42.268 125.096  1.00 67.20
ATOM   3924  CB  ASP A 237     -26.600  44.254 124.918  1.00 73.28
ATOM   3925  CG  ASP A 237     -26.629  44.190 126.432  1.00 86.64
ATOM   3926  OD1 ASP A 237     -26.874  43.099 126.970  1.00 86.44
ATOM   3927  OD2 ASP A 237     -26.500  45.256 127.081  1.00 95.95
ATOM   3932  N   ASN A 238     -27.612  41.480 124.125  1.00 64.12
ATOM   3933  CA  ASN A 238     -28.011  40.084 124.292  1.00 62.01
ATOM   3934  C   ASN A 238     -28.110  39.619 125.722  1.00 66.16
ATOM   3935  O   ASN A 238     -28.940  38.757 126.021  1.00 62.60
ATOM   3936  CB  ASN A 238     -27.155  39.151 123.467  1.00 60.01
ATOM   3937  CG  ASN A 238     -27.302  39.308 121.971  1.00 74.49
ATOM   3938  ND2 ASN A 238     -28.255  39.904 121.421  1.00 70.25
ATOM   3939  OD1 ASN A 238     -26.395  38.670 121.294  1.00 60.96
ATOM   3946  N   TYR A 239     -27.306  40.215 126.610  1.00 66.15
ATOM   3947  CA  TYR A 239     -27.309  39.900 128.040  1.00 67.76
ATOM   3948  C   TYR A 239     -28.556  40.469 128.713  1.00 68.41
ATOM   3949  O   TYR A 239     -29.302  39.728 129.363  1.00 66.73
ATOM   3950  CB  TYR A 239     -26.003  40.378 128.713  1.00 73.45
ATOM   3951  CG  TYR A 239     -24.794  39.644 128.178  1.00 80.52
ATOM   3952  CD1 TYR A 239     -24.408  38.418 128.710  1.00 83.28
ATOM   3953  CD2 TYR A 239     -24.107  40.113 127.063  1.00 83.29
ATOM   3954  CE1 TYR A 239     -23.345  37.690 128.168  1.00 86.53
ATOM   3955  CE2 TYR A 239     -23.048  39.391 126.504  1.00 85.70
ATOM   3956  CZ  TYR A 239     -22.661  38.182 127.067  1.00 98.84
ATOM   3957  OH  TYR A 239     -21.607  37.460 126.537  1.00104.55
ATOM   3967  N   ASP A 240     -28.818  41.774 128.492  1.00 62.87
ATOM   3968  CA  ASP A 240     -29.990  42.454 129.033  1.00 61.26
ATOM   3969  C   ASP A 240     -31.273  41.873 128.462  1.00 60.87
ATOM   3970  O   ASP A 240     -32.290  41.878 129.152  1.00 60.72
ATOM   3971  CB  ASP A 240     -29.901  43.964 128.798  1.00 62.98
ATOM   3972  CG  ASP A 240     -31.016  44.730 129.450  1.00 64.17
ATOM   3973  OD1 ASP A 240     -31.168  44.619 130.706  1.00 66.66
ATOM   3974  OD2 ASP A 240     -31.748  45.422 128.723  1.00 60.86
ATOM   3979  N   GLN A 241     -31.218  41.314 127.241  1.00 54.35
ATOM   3980  CA  GLN A 241     -32.384  40.658 126.640  1.00 51.01
ATOM   3981  C   GLN A 241     -32.870  39.528 127.554  1.00 53.26
ATOM   3982  O   GLN A 241     -34.074  39.429 127.804  1.00 52.77
ATOM   3983  CB  GLN A 241     -32.061  40.124 125.239  1.00 49.20
ATOM   3984  CG  GLN A 241     -33.288  39.589 124.486  1.00 41.81
ATOM   3985  CD  GLN A 241     -34.343  40.620 124.172  1.00 52.37
ATOM   3986  NE2 GLN A 241     -35.576  40.188 123.961  1.00 47.68
ATOM   3987  OE1 GLN A 241     -34.077  41.809 124.096  1.00 50.21
ATOM   3996  N   LEU A 242     -31.932  38.710 128.082  1.00 48.03
ATOM   3997  CA  LEU A 242     -32.292  37.634 128.989  1.00 46.67
ATOM   3998  C   LEU A 242     -32.853  38.177 130.282  1.00 54.81
ATOM   3999  O   LEU A 242     -33.787  37.586 130.817  1.00 57.58
ATOM   4000  CB  LEU A 242     -31.116  36.686 129.255  1.00 45.86
ATOM   4001  CG  LEU A 242     -31.469  35.359 129.963  1.00 46.22
ATOM   4002  CD1 LEU A 242     -32.500  34.541 129.156  1.00 43.62
ATOM   4003  CD2 LEU A 242     -30.227  34.538 130.228  1.00 38.40
ATOM   4015  N   VAL A 243     -32.330  39.316 130.764  1.00 52.01
ATOM   4016  CA  VAL A 243     -32.830  39.967 131.975  1.00 52.50
ATOM   4017  C   VAL A 243     -34.286  40.385 131.768  1.00 54.95
ATOM   4018  O   VAL A 243     -35.113  40.106 132.637  1.00 55.76
ATOM   4019  CB  VAL A 243     -31.942  41.160 132.403  1.00 58.23
ATOM   4020  CG1 VAL A 243     -32.511  41.836 133.642  1.00 59.47
ATOM   4021  CG2 VAL A 243     -30.511  40.710 132.668  1.00 58.81
ATOM   4031  N   ARG A 244     -34.611  41.015 130.620  1.00 50.50
ATOM   4032  CA  ARG A 244     -35.987  41.418 130.301  1.00 50.81
ATOM   4033  C   ARG A 244     -36.944  40.230 130.327  1.00 55.08
ATOM   4034  O   ARG A 244     -38.050  40.348 130.852  1.00 57.29
ATOM   4035  CB  ARG A 244     -36.068  42.120 128.927  1.00 50.84
ATOM   4036  CG  ARG A 244     -35.236  43.394 128.807  1.00 59.75
ATOM   4037  CD  ARG A 244     -35.404  44.370 129.957  1.00 69.72
ATOM   4038  NE  ARG A 244     -35.924  45.654 129.495  1.00 79.07
ATOM   4039  CZ  ARG A 244     -35.183  46.712 129.205  1.00 93.66
ATOM   4040  NH1 ARG A 244     -35.752  47.816 128.751  1.00 86.30
ATOM   4041  NH2 ARG A 244     -33.872  46.686 129.389  1.00 83.83
ATOM   4055  N   ILE A 245     -36.506  39.086 129.770  1.00 48.71
ATOM   4056  CA  ILE A 245     -37.289  37.846 129.759  1.00 45.83
ATOM   4057  C   ILE A 245     -37.450  37.360 131.183  1.00 51.36
ATOM   4058  O   ILE A 245     -38.568  37.037 131.576  1.00 53.77
ATOM   4059  CB  ILE A 245     -36.636  36.774 128.839  1.00 46.26
ATOM   4060  CG1 ILE A 245     -36.651  37.211 127.362  1.00 44.55
ATOM   4061  CG2 ILE A 245     -37.312  35.419 128.997  1.00 45.38
ATOM   4062  CD1 ILE A 245     -35.724  36.434 126.476  1.00 46.06
ATOM   4074  N   ALA A 246     -36.350  37.306 131.957  1.00 48.11
ATOM   4075  CA  ALA A 246     -36.362  36.837 133.345  1.00 48.99
ATOM   4076  C   ALA A 246     -37.285  37.659 134.258  1.00 56.37
ATOM   4077  O   ALA A 246     -37.881  37.113 135.187  1.00 57.19
ATOM   4078  CB  ALA A 246     -34.954  36.783 133.901  1.00 50.51
ATOM   4084  N   LYS A 247     -37.455  38.953 133.961  1.00 53.58
ATOM   4085  CA  LYS A 247     -38.344  39.817 134.747  1.00 54.06
ATOM   4086  C   LYS A 247     -39.817  39.495 134.511  1.00 54.96
ATOM   4087  O   LYS A 247     -40.655  39.853 135.325  1.00 55.34
ATOM   4088  CB  LYS A 247     -38.017  41.297 134.508  1.00 57.82
ATOM   4089  CG  LYS A 247     -36.737  41.714 135.214  1.00 67.24
ATOM   4090  CD  LYS A 247     -36.331  43.146 134.908  1.00 74.31
ATOM   4091  CE  LYS A 247     -35.162  43.557 135.776  1.00 88.79
ATOM   4092  NZ  LYS A 247     -34.803  44.985 135.599  1.00 94.27
ATOM   4106  N   VAL A 248     -40.118  38.748 133.440  1.00 49.43
ATOM   4107  CA  VAL A 248     -41.476  38.309 133.119  1.00 47.57
ATOM   4108  C   VAL A 248     -41.674  36.833 133.453  1.00 50.35
ATOM   4109  O   VAL A 248     -42.589  36.488 134.206  1.00 51.15
ATOM   4110  CB  VAL A 248     -41.809  38.603 131.644  1.00 48.60
ATOM   4111  CG1 VAL A 248     -43.203  38.090 131.286  1.00 47.23
ATOM   4112  CG2 VAL A 248     -41.683  40.094 131.350  1.00 48.86
ATOM   4122  N   LEU A 249     -40.828  35.964 132.867  1.00 45.17
ATOM   4123  CA  LEU A 249     -40.922  34.508 133.062  1.00 43.74
ATOM   4124  C   LEU A 249     -40.356  34.015 134.382  1.00 45.62
ATOM   4125  O   LEU A 249     -40.581  32.860 134.729  1.00 45.27
ATOM   4126  CB  LEU A 249     -40.261  33.762 131.887  1.00 41.61
ATOM   4127  CG  LEU A 249     -40.870  33.866 130.509  1.00 42.61
ATOM   4128  CD1 LEU A 249     -40.317  32.771 129.659  1.00 39.91
ATOM   4129  CD2 LEU A 249     -42.416  33.786 130.542  1.00 44.61
ATOM   4141  N   GLY A 250     -39.625  34.881 135.083  1.00 42.19
ATOM   4142  CA  GLY A 250     -39.025  34.586 136.372  1.00 42.61
ATOM   4143  C   GLY A 250     -37.689  33.897 136.277  1.00 48.78
ATOM   4144  O   GLY A 250     -37.361  33.278 135.255  1.00 48.73
ATOM   4148  N   THR A 251     -36.921  33.978 137.353  1.00 48.75
ATOM   4149  CA  THR A 251     -35.600  33.352 137.398  1.00 50.65
ATOM   4150  C   THR A 251     -35.615  31.879 137.780  1.00 57.63
ATOM   4151  O   THR A 251     -34.686  31.161 137.391  1.00 58.06
ATOM   4152  CB  THR A 251     -34.648  34.157 138.291  1.00 61.86
ATOM   4153  CG2 THR A 251     -34.220  35.472 137.641  1.00 61.28
ATOM   4154  OG1 THR A 251     -35.269  34.374 139.567  1.00 57.78
ATOM   4162  N   GLU A 252     -36.624  31.417 138.559  1.00 54.32
ATOM   4163  CA  GLU A 252     -36.654  30.017 138.986  1.00 54.22
ATOM   4164  C   GLU A 252     -36.645  29.073 137.774  1.00 55.40
ATOM   4165  O   GLU A 252     -35.817  28.156 137.706  1.00 55.61
ATOM   4166  CB  GLU A 252     -37.886  29.722 139.874  1.00 56.58
ATOM   4167  CG  GLU A 252     -37.867  30.189 141.318  1.00 67.16
ATOM   4168  CD  GLU A 252     -39.212  30.576 141.920  1.00 76.97
ATOM   4169  OE1 GLU A 252     -40.151  30.954 141.173  1.00 61.43
ATOM   4170  OE2 GLU A 252     -39.276  30.616 143.173  1.00 65.04
ATOM   4177  N   ASP A 253     -37.538  29.310 136.809  1.00 49.32
ATOM   4178  CA  ASP A 253     -37.592  28.446 135.629  1.00 47.70
ATOM   4179  C   ASP A 253     -36.370  28.574 134.737  1.00 53.33
ATOM   4180  O   ASP A 253     -36.024  27.607 134.057  1.00 52.50
ATOM   4181  CB  ASP A 253     -38.857  28.694 134.832  1.00 47.88
ATOM   4182  CG  ASP A 253     -40.145  28.299 135.507  1.00 50.20
ATOM   4183  OD1 ASP A 253     -40.089  27.588 136.553  1.00 52.14
ATOM   4184  OD2 ASP A 253     -41.212  28.695 135.002  1.00 50.18
ATOM   4189  N   LEU A 254     -35.721  29.759 134.741  1.00 50.46
ATOM   4190  CA  LEU A 254     -34.506  30.000 133.969  1.00 49.10
ATOM   4191  C   LEU A 254     -33.395  29.112 134.524  1.00 55.10
ATOM   4192  O   LEU A 254     -32.769  28.369 133.773  1.00 54.18
ATOM   4193  CB  LEU A 254     -34.096  31.490 134.038  1.00 48.96
ATOM   4194  CG  LEU A 254     -32.789  31.889 133.347  1.00 51.16
ATOM   4195  CD1 LEU A 254     -32.704  31.342 131.895  1.00 48.71
ATOM   4196  CD2 LEU A 254     -32.638  33.385 133.338  1.00 49.93
ATOM   4208  N   TYR A 255     -33.164  29.184 135.836  1.00 53.16
ATOM   4209  CA  TYR A 255     -32.137  28.376 136.468  1.00 54.05
ATOM   4210  C   TYR A 255     -32.438  26.872 136.395  1.00 60.00
ATOM   4211  O   TYR A 255     -31.503  26.088 136.221  1.00 60.13
ATOM   4212  CB  TYR A 255     -31.828  28.882 137.871  1.00 56.26
ATOM   4213  CG  TYR A 255     -31.045  30.180 137.857  1.00 58.76
ATOM   4214  CD1 TYR A 255     -29.793  30.255 137.250  1.00 61.01
ATOM   4215  CD2 TYR A 255     -31.553  31.332 138.449  1.00 59.67
ATOM   4216  CE1 TYR A 255     -29.070  31.446 137.224  1.00 62.98
ATOM   4217  CE2 TYR A 255     -30.828  32.524 138.450  1.00 61.99
ATOM   4218  CZ  TYR A 255     -29.579  32.574 137.845  1.00 74.32
ATOM   4219  OH  TYR A 255     -28.821  33.728 137.865  1.00 81.12
ATOM   4229  N   ASP A 256     -33.736  26.480 136.407  1.00 56.39
ATOM   4230  CA  ASP A 256     -34.128  25.078 136.231  1.00 55.84
ATOM   4231  C   ASP A 256     -33.764  24.588 134.826  1.00 57.98
ATOM   4232  O   ASP A 256     -33.280  23.465 134.679  1.00 58.78
ATOM   4233  CB  ASP A 256     -35.625  24.862 136.520  1.00 57.39
ATOM   4234  CG  ASP A 256     -35.998  24.859 137.983  1.00 71.39
ATOM   4235  OD1 ASP A 256     -35.075  24.765 138.838  1.00 74.15
ATOM   4236  OD2 ASP A 256     -37.206  24.933 138.281  1.00 80.71
ATOM   4241  N   TYR A 257     -33.988  25.443 133.805  1.00 51.85
ATOM   4242  CA  TYR A 257     -33.647  25.190 132.399  1.00 48.74
ATOM   4243  C   TYR A 257     -32.128  24.985 132.246  1.00 52.59
ATOM   4244  O   TYR A 257     -31.715  24.021 131.609  1.00 52.38
ATOM   4245  CB  TYR A 257     -34.087  26.390 131.532  1.00 46.56
ATOM   4246  CG  TYR A 257     -33.673  26.327 130.080  1.00 44.49
ATOM   4247  CD1 TYR A 257     -34.060  25.266 129.273  1.00 44.08
ATOM   4248  CD2 TYR A 257     -32.985  27.384 129.483  1.00 44.18
ATOM   4249  CE1 TYR A 257     -33.777  25.252 127.915  1.00 42.92
ATOM   4250  CE2 TYR A 257     -32.666  27.362 128.131  1.00 43.52
ATOM   4251  CZ  TYR A 257     -33.090  26.303 127.342  1.00 51.41
ATOM   4252  OH  TYR A 257     -32.850  26.285 125.981  1.00 57.65
ATOM   4262  N   ILE A 258     -31.318  25.903 132.819  1.00 48.86
ATOM   4263  CA  ILE A 258     -29.859  25.867 132.816  1.00 48.87
ATOM   4264  C   ILE A 258     -29.393  24.567 133.465  1.00 55.12
ATOM   4265  O   ILE A 258     -28.553  23.870 132.900  1.00 56.91
ATOM   4266  CB  ILE A 258     -29.288  27.156 133.472  1.00 51.76
ATOM   4267  CG1 ILE A 258     -29.479  28.363 132.503  1.00 50.19
ATOM   4268  CG2 ILE A 258     -27.813  27.000 133.880  1.00 52.22
ATOM   4269  CD1 ILE A 258     -29.593  29.677 133.195  1.00 61.23
ATOM   4281  N   ASP A 259     -30.008  24.196 134.581  1.00 51.84
ATOM   4282  CA  ASP A 259     -29.731  22.957 135.287  1.00 53.28
ATOM   4283  C   ASP A 259     -30.032  21.733 134.453  1.00 57.52
ATOM   4284  O   ASP A 259     -29.189  20.846 134.336  1.00 61.39
ATOM   4285  CB  ASP A 259     -30.554  22.886 136.567  1.00 56.37
ATOM   4286  CG  ASP A 259     -29.699  22.909 137.794  1.00 78.83
ATOM   4287  OD1 ASP A 259     -29.652  21.869 138.504  1.00 82.56
ATOM   4288  OD2 ASP A 259     -29.019  23.950 138.024  1.00 86.24
ATOM   4293  N   LYS A 260     -31.237  21.668 133.894  1.00 49.72
ATOM   4294  CA  LYS A 260     -31.701  20.542 133.105  1.00 47.24
ATOM   4295  C   LYS A 260     -30.755  20.214 131.960  1.00 52.08
ATOM   4296  O   LYS A 260     -30.460  19.046 131.725  1.00 54.52
ATOM   4297  CB  LYS A 260     -33.130  20.817 132.596  1.00 46.55
ATOM   4298  CG  LYS A 260     -33.663  19.729 131.682  1.00 46.19
ATOM   4299  CD  LYS A 260     -35.099  19.915 131.286  1.00 43.75
ATOM   4300  CE  LYS A 260     -35.449  18.948 130.179  1.00 48.26
ATOM   4301  NZ  LYS A 260     -36.892  18.977 129.826  1.00 59.91
ATOM   4315  N   TYR A 261     -30.279  21.230 131.257  1.00 46.82
ATOM   4316  CA  TYR A 261     -29.405  21.044 130.110  1.00 46.11
ATOM   4317  C   TYR A 261     -27.916  21.171 130.426  1.00 56.16
ATOM   4318  O   TYR A 261     -27.096  21.104 129.507  1.00 57.68
ATOM   4319  CB  TYR A 261     -29.831  21.975 128.961  1.00 43.29
ATOM   4320  CG  TYR A 261     -31.184  21.605 128.399  1.00 42.04
ATOM   4321  CD1 TYR A 261     -31.317  20.575 127.469  1.00 42.83
ATOM   4322  CD2 TYR A 261     -32.347  22.217 128.864  1.00 41.41
ATOM   4323  CE1 TYR A 261     -32.570  20.188 126.996  1.00 42.24
ATOM   4324  CE2 TYR A 261     -33.601  21.851 128.378  1.00 40.51
ATOM   4325  CZ  TYR A 261     -33.706  20.835 127.448  1.00 46.03
ATOM   4326  OH  TYR A 261     -34.933  20.467 126.974  1.00 47.29
ATOM   4336  N   ASN A 262     -27.557  21.345 131.711  1.00 52.61
ATOM   4337  CA  ASN A 262     -26.170  21.496 132.139  1.00 53.52
ATOM   4338  C   ASN A 262     -25.472  22.583 131.350  1.00 57.08
ATOM   4339  O   ASN A 262     -24.361  22.386 130.852  1.00 59.14
ATOM   4340  CB  ASN A 262     -25.412  20.164 132.086  1.00 54.64
ATOM   4341  CG  ASN A 262     -24.203  20.131 132.966  1.00 76.13
ATOM   4342  ND2 ASN A 262     -23.164  19.533 132.443  1.00 73.27
ATOM   4343  OD1 ASN A 262     -24.163  20.658 134.078  1.00 68.72
ATOM   4350  N   ILE A 263     -26.149  23.719 131.207  1.00 50.83
ATOM   4351  CA  ILE A 263     -25.642  24.870 130.484  1.00 50.21
ATOM   4352  C   ILE A 263     -24.649  25.638 131.361  1.00 61.30
ATOM   4353  O   ILE A 263     -24.949  25.923 132.525  1.00 63.75
ATOM   4354  CB  ILE A 263     -26.832  25.768 129.994  1.00 50.41
ATOM   4355  CG1 ILE A 263     -27.657  25.028 128.931  1.00 48.42
ATOM   4356  CG2 ILE A 263     -26.348  27.128 129.433  1.00 48.54
ATOM   4357  CD1 ILE A 263     -28.988  25.607 128.644  1.00 43.20
ATOM   4369  N   GLU A 264     -23.470  25.961 130.808  1.00 61.03
ATOM   4370  CA  GLU A 264     -22.466  26.769 131.496  1.00 64.19
ATOM   4371  C   GLU A 264     -22.858  28.210 131.154  1.00 66.49
ATOM   4372  O   GLU A 264     -22.783  28.640 129.995  1.00 63.88
ATOM   4373  CB  GLU A 264     -21.032  26.452 131.010  1.00 67.58
ATOM   4374  CG  GLU A 264     -19.925  26.928 131.949  1.00 85.91
ATOM   4375  CD  GLU A 264     -18.529  27.122 131.360  1.00112.68
ATOM   4376  OE1 GLU A 264     -17.732  27.866 131.977  1.00116.78
ATOM   4377  OE2 GLU A 264     -18.240  26.569 130.272  1.00100.70
ATOM   4384  N   LEU A 265     -23.367  28.909 132.156  1.00 63.57
ATOM   4385  CA  LEU A 265     -23.836  30.274 132.014  1.00 62.25
ATOM   4386  C   LEU A 265     -22.663  31.254 132.100  1.00 71.80
ATOM   4387  O   LEU A 265     -21.820  31.141 133.004  1.00 72.63
ATOM   4388  CB  LEU A 265     -24.885  30.541 133.119  1.00 60.89
ATOM   4389  CG  LEU A 265     -25.775  31.761 132.980  1.00 60.65
ATOM   4390  CD1 LEU A 265     -26.641  31.668 131.764  1.00 55.84
ATOM   4391  CD2 LEU A 265     -26.614  31.932 134.224  1.00 62.41
ATOM   4403  N   ASP A 266     -22.613  32.212 131.139  1.00 71.60
ATOM   4404  CA  ASP A 266     -21.595  33.268 131.066  1.00 74.75
ATOM   4405  C   ASP A 266     -21.573  33.980 132.416  1.00 87.87
ATOM   4406  O   ASP A 266     -22.650  34.317 132.928  1.00 88.23
ATOM   4407  CB  ASP A 266     -21.908  34.262 129.940  1.00 74.59
ATOM   4408  CG  ASP A 266     -20.814  35.267 129.637  1.00 82.86
ATOM   4409  OD1 ASP A 266     -20.482  36.078 130.540  1.00 85.75
ATOM   4410  OD2 ASP A 266     -20.338  35.294 128.477  1.00 87.16
ATOM   4415  N   PRO A 267     -20.373  34.133 133.043  1.00 90.72
ATOM   4416  CA  PRO A 267     -20.304  34.732 134.396  1.00 93.08
ATOM   4417  C   PRO A 267     -20.943  36.107 134.629  1.00 97.41
ATOM   4418  O   PRO A 267     -21.340  36.373 135.772  1.00 98.08
ATOM   4419  CB  PRO A 267     -18.809  34.710 134.729  1.00 97.49
ATOM   4420  CG  PRO A 267     -18.111  34.563 133.415  1.00101.28
ATOM   4421  CD  PRO A 267     -19.028  33.735 132.568  1.00 94.02
ATOM   4429  N   ARG A 268     -21.108  36.956 133.581  1.00 92.70
ATOM   4430  CA  ARG A 268     -21.757  38.262 133.794  1.00 92.61
ATOM   4431  C   ARG A 268     -23.257  38.183 134.104  1.00 92.49
ATOM   4432  O   ARG A 268     -23.803  39.077 134.765  1.00 94.55
ATOM   4433  CB  ARG A 268     -21.426  39.282 132.707  1.00 93.23
ATOM   4434  CG  ARG A 268     -21.981  38.956 131.360  1.00101.33
ATOM   4435  CD  ARG A 268     -21.600  40.041 130.387  1.00117.14
ATOM   4436  NE  ARG A 268     -20.576  39.569 129.466  1.00129.80
ATOM   4437  CZ  ARG A 268     -20.124  40.272 128.439  1.00146.69
ATOM   4438  NH1 ARG A 268     -20.608  41.484 128.190  1.00134.51
ATOM   4439  NH2 ARG A 268     -19.188  39.769 127.645  1.00136.46
ATOM   4453  N   PHE A 269     -23.897  37.083 133.701  1.00 83.05
ATOM   4454  CA  PHE A 269     -25.305  36.870 134.008  1.00 79.92
ATOM   4455  C   PHE A 269     -25.611  36.783 135.496  1.00 89.18
ATOM   4456  O   PHE A 269     -26.674  37.226 135.922  1.00 88.43
ATOM   4457  CB  PHE A 269     -25.800  35.615 133.319  1.00 77.03
ATOM   4458  CG  PHE A 269     -26.157  35.829 131.881  1.00 73.43
ATOM   4459  CD1 PHE A 269     -27.107  36.770 131.521  1.00 72.93
ATOM   4460  CD2 PHE A 269     -25.586  35.047 130.884  1.00 73.05
ATOM   4461  CE1 PHE A 269     -27.490  36.920 130.193  1.00 71.86
ATOM   4462  CE2 PHE A 269     -25.970  35.190 129.551  1.00 72.97
ATOM   4463  CZ  PHE A 269     -26.923  36.126 129.212  1.00 70.08
ATOM   4473  N   ASN A 270     -24.680  36.209 136.277  1.00 90.73
ATOM   4474  CA  ASN A 270     -24.788  36.034 137.728  1.00 93.37
ATOM   4475  C   ASN A 270     -25.155  37.337 138.447  1.00 97.21
ATOM   4476  O   ASN A 270     -26.037  37.332 139.303  1.00 97.21
ATOM   4477  CB  ASN A 270     -23.481  35.453 138.292  1.00101.56
ATOM   4478  CG  ASN A 270     -23.003  34.189 137.603  1.00138.03
ATOM   4479  ND2 ASN A 270     -21.688  33.978 137.618  1.00134.17
ATOM   4480  OD1 ASN A 270     -23.794  33.399 137.051  1.00129.38
ATOM   4487  N   ASP A 271     -24.535  38.450 138.052  1.00 93.42
ATOM   4488  CA  ASP A 271     -24.802  39.739 138.668  1.00 94.71
ATOM   4489  C   ASP A 271     -26.058  40.439 138.132  1.00 94.28
ATOM   4490  O   ASP A 271     -26.764  41.092 138.904  1.00 97.19
ATOM   4491  CB  ASP A 271     -23.572  40.659 138.550  1.00 99.18
ATOM   4492  CG  ASP A 271     -22.283  40.065 139.104  1.00111.13
ATOM   4493  OD1 ASP A 271     -21.360  39.800 138.299  1.00111.92
ATOM   4494  OD2 ASP A 271     -22.202  39.856 140.345  1.00113.82
ATOM   4499  N   ILE A 272     -26.336  40.313 136.833  1.00 82.53
ATOM   4500  CA  ILE A 272     -27.443  41.039 136.212  1.00 78.21
ATOM   4501  C   ILE A 272     -28.822  40.406 136.301  1.00 77.89
ATOM   4502  O   ILE A 272     -29.821  41.126 136.273  1.00 78.79
ATOM   4503  CB  ILE A 272     -27.073  41.523 134.785  1.00 78.69
ATOM   4504  CG1 ILE A 272     -26.971  40.328 133.786  1.00 75.32
ATOM   4505  CG2 ILE A 272     -25.791  42.366 134.837  1.00 79.96
ATOM   4506  CD1 ILE A 272     -26.758  40.658 132.354  1.00 70.02
ATOM   4518  N   LEU A 273     -28.891  39.081 136.388  1.00 70.54
ATOM   4519  CA  LEU A 273     -30.189  38.390 136.404  1.00 68.17
ATOM   4520  C   LEU A 273     -31.011  38.603 137.639  1.00 74.75
ATOM   4521  O   LEU A 273     -32.234  38.653 137.540  1.00 74.72
ATOM   4522  CB  LEU A 273     -30.074  36.888 136.107  1.00 65.87
ATOM   4523  CG  LEU A 273     -29.693  36.490 134.685  1.00 66.28
ATOM   4524  CD1 LEU A 273     -29.338  35.027 134.640  1.00 65.98
ATOM   4525  CD2 LEU A 273     -30.798  36.826 133.691  1.00 63.27
ATOM   4537  N   GLY A 274     -30.356  38.672 138.790  1.00 72.20
ATOM   4538  CA  GLY A 274     -31.027  38.863 140.065  1.00 72.62
ATOM   4539  C   GLY A 274     -31.995  37.749 140.384  1.00 74.88
ATOM   4540  O   GLY A 274     -31.782  36.601 139.989  1.00 74.87
ATOM   4544  N   ARG A 275     -33.074  38.094 141.080  1.00 69.82
ATOM   4545  CA  ARG A 275     -34.107  37.139 141.472  1.00 67.60
ATOM   4546  C   ARG A 275     -35.445  37.762 141.150  1.00 68.31
ATOM   4547  O   ARG A 275     -35.722  38.872 141.596  1.00 69.61
ATOM   4548  CB  ARG A 275     -34.003  36.815 142.971  1.00 72.04
ATOM   4549  CG  ARG A 275     -34.301  35.361 143.297  1.00 88.62
ATOM   4550  CD  ARG A 275     -35.472  35.185 144.254  1.00105.64
ATOM   4551  NE  ARG A 275     -36.699  34.756 143.571  1.00122.71
ATOM   4552  CZ  ARG A 275     -37.002  33.492 143.278  1.00146.78
ATOM   4553  NH1 ARG A 275     -36.166  32.509 143.591  1.00138.66
ATOM   4554  NH2 ARG A 275     -38.139  33.208 142.660  1.00138.62
ATOM   4568  N   HIS A 276     -36.245  37.093 140.317  1.00 62.12
ATOM   4569  CA  HIS A 276     -37.529  37.633 139.869  1.00 61.48
ATOM   4570  C   HIS A 276     -38.604  36.576 139.831  1.00 62.76
ATOM   4571  O   HIS A 276     -38.363  35.448 139.382  1.00 61.19
ATOM   4572  CB  HIS A 276     -37.398  38.261 138.470  1.00 61.30
ATOM   4573  CG  HIS A 276     -36.360  39.325 138.384  1.00 65.90
ATOM   4574  CD2 HIS A 276     -35.121  39.270 137.854  1.00 67.42
ATOM   4575  ND1 HIS A 276     -36.565  40.577 138.927  1.00 69.83
ATOM   4576  CE1 HIS A 276     -35.454  41.252 138.690  1.00 70.41
ATOM   4577  NE2 HIS A 276     -34.557  40.506 138.039  1.00 69.29
ATOM   4585  N   SER A 277     -39.807  36.955 140.273  1.00 57.90
ATOM   4586  CA  SER A 277     -40.972  36.087 140.261  1.00 55.58
ATOM   4587  C   SER A 277     -41.512  36.002 138.848  1.00 58.14
ATOM   4588  O   SER A 277     -41.294  36.940 138.071  1.00 56.94
ATOM   4589  CB  SER A 277     -42.067  36.661 141.152  1.00 56.77
ATOM   4590  OG  SER A 277     -42.387  37.991 140.781  1.00 64.06
ATOM   4596  N   ARG A 278     -42.244  34.907 138.516  1.00 52.68
ATOM   4597  CA  ARG A 278     -42.924  34.774 137.225  1.00 50.33
ATOM   4598  C   ARG A 278     -44.138  35.696 137.282  1.00 55.12
ATOM   4599  O   ARG A 278     -44.941  35.572 138.207  1.00 56.85
ATOM   4600  CB  ARG A 278     -43.380  33.319 137.032  1.00 46.53
ATOM   4601  CG  ARG A 278     -44.031  33.028 135.678  1.00 45.71
ATOM   4602  CD  ARG A 278     -44.080  31.535 135.371  1.00 47.67
ATOM   4603  NE  ARG A 278     -44.803  30.733 136.374  1.00 47.95
ATOM   4604  CZ  ARG A 278     -46.106  30.485 136.341  1.00 57.51
ATOM   4605  NH1 ARG A 278     -46.674  29.767 137.298  1.00 63.52
ATOM   4606  NH2 ARG A 278     -46.854  30.973 135.367  1.00 43.40
ATOM   4620  N   LYS A 279     -44.244  36.646 136.344  1.00 50.10
ATOM   4621  CA  LYS A 279     -45.347  37.595 136.340  1.00 50.45
ATOM   4622  C   LYS A 279     -46.620  37.015 135.718  1.00 55.19
ATOM   4623  O   LYS A 279     -46.553  36.213 134.772  1.00 54.48
ATOM   4624  CB  LYS A 279     -44.934  38.909 135.657  1.00 51.84
ATOM   4625  CG  LYS A 279     -43.854  39.728 136.372  1.00 58.61
ATOM   4626  CD  LYS A 279     -43.854  39.668 137.909  1.00 58.03
ATOM   4627  CE  LYS A 279     -42.624  40.317 138.498  1.00 57.17
ATOM   4628  NZ  LYS A 279     -41.352  39.722 137.973  1.00 64.21
ATOM   4642  N   ARG A 280     -47.783  37.392 136.285  1.00 50.95
ATOM   4643  CA  ARG A 280     -49.076  36.999 135.731  1.00 49.46
ATOM   4644  C   ARG A 280     -49.353  37.889 134.523  1.00 55.34
ATOM   4645  O   ARG A 280     -49.156  39.104 134.601  1.00 57.44
ATOM   4646  CB  ARG A 280     -50.205  37.108 136.757  1.00 47.70
ATOM   4647  CG  ARG A 280     -50.209  35.937 137.731  1.00 45.72
ATOM   4648  CD  ARG A 280     -51.223  36.139 138.818  1.00 48.52
ATOM   4649  NE  ARG A 280     -50.750  35.629 140.113  1.00 49.03
ATOM   4650  CZ  ARG A 280     -51.025  34.416 140.555  1.00 60.05
ATOM   4651  NH1 ARG A 280     -50.544  34.005 141.710  1.00 44.91
ATOM   4652  NH2 ARG A 280     -51.765  33.593 139.831  1.00 64.37
ATOM   4666  N   TRP A 281     -49.765  37.278 133.393  1.00 50.85
ATOM   4667  CA  TRP A 281     -50.037  37.976 132.146  1.00 49.97
ATOM   4668  C   TRP A 281     -51.012  39.163 132.300  1.00 56.43
ATOM   4669  O   TRP A 281     -50.884  40.148 131.576  1.00 56.54
ATOM   4670  CB  TRP A 281     -50.464  36.989 131.054  1.00 47.27
ATOM   4671  CG  TRP A 281     -49.435  35.930 130.713  1.00 46.61
ATOM   4672  CD1 TRP A 281     -49.541  34.593 130.936  1.00 48.86
ATOM   4673  CD2 TRP A 281     -48.156  36.132 130.075  1.00 45.70
ATOM   4674  CE2 TRP A 281     -47.546  34.863 129.946  1.00 48.51
ATOM   4675  CE3 TRP A 281     -47.447  37.272 129.629  1.00 47.54
ATOM   4676  NE1 TRP A 281     -48.419  33.939 130.468  1.00 47.46
ATOM   4677  CZ2 TRP A 281     -46.268  34.690 129.371  1.00 46.98
ATOM   4678  CZ3 TRP A 281     -46.183  37.103 129.053  1.00 48.14
ATOM   4679  CH2 TRP A 281     -45.608  35.823 128.923  1.00 47.58
ATOM   4690  N   GLU A 282     -51.893  39.131 133.314  1.00 55.29
ATOM   4691  CA  GLU A 282     -52.848  40.224 133.572  1.00 58.06
ATOM   4692  C   GLU A 282     -52.142  41.576 133.856  1.00 64.69
ATOM   4693  O   GLU A 282     -52.705  42.654 133.592  1.00 65.82
ATOM   4694  CB  GLU A 282     -53.813  39.858 134.718  1.00 60.61
ATOM   4695  CG  GLU A 282     -53.168  40.063 136.080  1.00 69.21
ATOM   4696  CD  GLU A 282     -53.688  39.337 137.301  1.00 84.29
ATOM   4697  OE1 GLU A 282     -53.079  39.532 138.378  1.00 76.52
ATOM   4698  OE2 GLU A 282     -54.673  38.571 137.196  1.00 74.16
ATOM   4705  N   ARG A 283     -50.904  41.516 134.355  1.00 59.61
ATOM   4706  CA  ARG A 283     -50.181  42.724 134.664  1.00 59.41
ATOM   4707  C   ARG A 283     -49.873  43.597 133.413  1.00 61.95
ATOM   4708  O   ARG A 283     -49.596  44.795 133.530  1.00 61.41
ATOM   4709  CB  ARG A 283     -48.996  42.356 135.566  1.00 59.69
ATOM   4710  CG  ARG A 283     -47.596  42.456 135.007  1.00 75.60
ATOM   4711  CD  ARG A 283     -46.735  43.340 135.914  1.00 90.79
ATOM   4712  NE  ARG A 283     -46.210  42.626 137.088  1.00 98.29
ATOM   4713  CZ  ARG A 283     -46.751  42.630 138.309  1.00102.29
ATOM   4714  NH1 ARG A 283     -47.878  43.293 138.544  1.00 88.93
ATOM   4715  NH2 ARG A 283     -46.167  41.972 139.303  1.00 76.45
ATOM   4729  N   PHE A 284     -49.937  42.977 132.211  1.00 57.31
ATOM   4730  CA  PHE A 284     -49.683  43.634 130.923  1.00 55.29
ATOM   4731  C   PHE A 284     -50.943  44.136 130.239  1.00 59.00
ATOM   4732  O   PHE A 284     -50.862  44.794 129.195  1.00 59.93
ATOM   4733  CB  PHE A 284     -48.885  42.706 130.005  1.00 54.87
ATOM   4734  CG  PHE A 284     -47.589  42.256 130.632  1.00 55.88
ATOM   4735  CD1 PHE A 284     -46.499  43.122 130.719  1.00 59.89
ATOM   4736  CD2 PHE A 284     -47.469  40.986 131.189  1.00 55.74
ATOM   4737  CE1 PHE A 284     -45.326  42.727 131.377  1.00 60.17
ATOM   4738  CE2 PHE A 284     -46.274  40.576 131.781  1.00 57.52
ATOM   4739  CZ  PHE A 284     -45.217  41.450 131.885  1.00 56.60
ATOM   4749  N   VAL A 285     -52.100  43.830 130.823  1.00 55.07
ATOM   4750  CA  VAL A 285     -53.417  44.193 130.298  1.00 55.12
ATOM   4751  C   VAL A 285     -53.794  45.574 130.802  1.00 64.78
ATOM   4752  O   VAL A 285     -53.629  45.876 131.988  1.00 67.56
ATOM   4753  CB  VAL A 285     -54.500  43.113 130.625  1.00 56.48
ATOM   4754  CG1 VAL A 285     -55.836  43.443 129.989  1.00 56.93
ATOM   4755  CG2 VAL A 285     -54.053  41.725 130.185  1.00 53.20
ATOM   4765  N   HIS A 286     -54.289  46.417 129.885  1.00 63.03
ATOM   4766  CA AHIS A 286     -54.729  47.782 130.179  0.50 65.09
ATOM   4768  C   HIS A 286     -55.913  48.152 129.294  1.00 71.94
ATOM   4769  O   HIS A 286     -56.266  47.378 128.398  1.00 71.16
ATOM   4770  CB AHIS A 286     -53.571  48.803 130.100  0.50 65.39
ATOM   4772  CG AHIS A 286     -52.830  48.859 128.799  0.50 66.51
ATOM   4774  CD2AHIS A 286     -51.562  48.489 128.516  0.50 66.01
ATOM   4776  ND1AHIS A 286     -53.368  49.478 127.686  0.50 68.79
ATOM   4778  CE1AHIS A 286     -52.436  49.415 126.750  0.50 66.26
ATOM   4780  NE2AHIS A 286     -51.333  48.827 127.200  0.50 65.06
ATOM   4795  N   SER A 287     -56.562  49.303 129.549  1.00 73.76
ATOM   4796  CA  SER A 287     -57.726  49.751 128.788  1.00 75.65
ATOM   4797  C   SER A 287     -57.521  49.761 127.262  1.00 78.87
ATOM   4798  O   SER A 287     -58.474  49.516 126.526  1.00 79.54
ATOM   4799  CB  SER A 287     -58.170  51.123 129.276  1.00 83.63
ATOM   4800  OG  SER A 287     -57.154  52.088 129.048  1.00 97.32
ATOM   4806  N   GLU A 288     -56.295  50.016 126.791  1.00 74.30
ATOM   4807  CA  GLU A 288     -56.016  50.118 125.360  1.00 73.83
ATOM   4808  C   GLU A 288     -55.766  48.811 124.626  1.00 75.03
ATOM   4809  O   GLU A 288     -55.837  48.785 123.397  1.00 73.97
ATOM   4810  CB  GLU A 288     -54.913  51.154 125.076  1.00 76.02
ATOM   4811  CG  GLU A 288     -55.162  52.518 125.715  1.00 96.92
ATOM   4812  CD  GLU A 288     -56.574  53.067 125.568  1.00133.35
ATOM   4813  OE1 GLU A 288     -56.964  53.407 124.427  1.00136.02
ATOM   4814  OE2 GLU A 288     -57.306  53.101 126.584  1.00129.83
ATOM   4821  N   ASN A 289     -55.494  47.723 125.351  1.00 69.58
ATOM   4822  CA  ASN A 289     -55.247  46.433 124.716  1.00 66.20
ATOM   4823  C   ASN A 289     -56.213  45.345 125.140  1.00 69.39
ATOM   4824  O   ASN A 289     -56.179  44.267 124.552  1.00 67.80
ATOM   4825  CB  ASN A 289     -53.791  45.991 124.951  1.00 63.02
ATOM   4826  CG  ASN A 289     -53.441  45.735 126.400  1.00 70.43
ATOM   4827  ND2 ASN A 289     -52.164  45.796 126.735  1.00 62.98
ATOM   4828  OD1 ASN A 289     -54.298  45.444 127.234  1.00 54.64
ATOM   4835  N   GLN A 290     -57.058  45.602 126.157  1.00 68.03
ATOM   4836  CA  GLN A 290     -57.954  44.582 126.718  1.00 67.92
ATOM   4837  C   GLN A 290     -58.825  43.813 125.722  1.00 71.25
ATOM   4838  O   GLN A 290     -59.077  42.625 125.920  1.00 71.74
ATOM   4839  CB  GLN A 290     -58.749  45.098 127.930  1.00 71.49
ATOM   4840  CG  GLN A 290     -59.754  46.227 127.637  1.00 98.85
ATOM   4841  CD  GLN A 290     -61.065  45.769 127.023  1.00128.53
ATOM   4842  NE2 GLN A 290     -61.616  44.717 127.366  1.00120.93
ATOM   4843  OE1 GLN A 290     -61.603  46.562 126.104  1.00127.36
ATOM   4852  N   HIS A 291     -59.260  44.481 124.651  1.00 66.35
ATOM   4853  CA  HIS A 291     -60.120  43.921 123.608  1.00 64.85
ATOM   4854  C   HIS A 291     -59.419  42.835 122.776  1.00 67.10
ATOM   4855  O   HIS A 291     -60.085  42.080 122.068  1.00 67.70
ATOM   4856  CB  HIS A 291     -60.689  45.055 122.720  1.00 66.23
ATOM   4857  CG  HIS A 291     -59.638  45.815 121.957  1.00 67.52
ATOM   4858  CD2 HIS A 291     -59.361  45.813 120.632  1.00 66.53
ATOM   4859  ND1 HIS A 291     -58.746  46.658 122.599  1.00 68.80
ATOM   4860  CE1 HIS A 291     -57.956  47.129 121.650  1.00 66.17
ATOM   4861  NE2 HIS A 291     -58.288  46.646 120.451  1.00 65.45
ATOM   4869  N   LEU A 292     -58.085  42.773 122.856  1.00 61.30
ATOM   4870  CA  LEU A 292     -57.249  41.813 122.138  1.00 58.10
ATOM   4871  C   LEU A 292     -56.839  40.656 123.049  1.00 60.73
ATOM   4872  O   LEU A 292     -56.260  39.662 122.578  1.00 60.65
ATOM   4873  CB  LEU A 292     -55.975  42.524 121.621  1.00 56.86
ATOM   4874  CG  LEU A 292     -56.181  43.793 120.799  1.00 61.74
ATOM   4875  CD1 LEU A 292     -54.868  44.465 120.530  1.00 61.10
ATOM   4876  CD2 LEU A 292     -56.920  43.499 119.509  1.00 61.94
ATOM   4888  N   VAL A 293     -57.104  40.798 124.348  1.00 55.90
ATOM   4889  CA  VAL A 293     -56.734  39.807 125.359  1.00 54.00
ATOM   4890  C   VAL A 293     -57.943  38.987 125.763  1.00 56.19
ATOM   4891  O   VAL A 293     -59.062  39.512 125.842  1.00 58.85
ATOM   4892  CB  VAL A 293     -56.045  40.473 126.573  1.00 58.02
ATOM   4893  CG1 VAL A 293     -55.584  39.425 127.578  1.00 56.00
ATOM   4894  CG2 VAL A 293     -54.864  41.346 126.133  1.00 57.19
ATOM   4904  N   SER A 294     -57.724  37.694 125.960  1.00 48.33
ATOM   4905  CA  SER A 294     -58.754  36.741 126.351  1.00 47.44
ATOM   4906  C   SER A 294     -58.034  35.619 127.093  1.00 49.88
ATOM   4907  O   SER A 294     -56.828  35.416 126.877  1.00 46.29
ATOM   4908  CB  SER A 294     -59.442  36.162 125.107  1.00 48.42
ATOM   4909  OG  SER A 294     -58.511  35.518 124.246  1.00 63.52
ATOM   4915  N   PRO A 295     -58.763  34.830 127.910  1.00 47.33
ATOM   4916  CA  PRO A 295     -58.141  33.650 128.524  1.00 45.82
ATOM   4917  C   PRO A 295     -57.468  32.746 127.496  1.00 49.95
ATOM   4918  O   PRO A 295     -56.369  32.238 127.781  1.00 49.16
ATOM   4919  CB  PRO A 295     -59.332  32.941 129.177  1.00 47.99
ATOM   4920  CG  PRO A 295     -60.278  34.056 129.510  1.00 53.51
ATOM   4921  CD  PRO A 295     -60.185  34.949 128.311  1.00 49.41
ATOM   4929  N   GLU A 296     -58.093  32.562 126.290  1.00 46.67
ATOM   4930  CA  GLU A 296     -57.507  31.697 125.223  1.00 44.28
ATOM   4931  C   GLU A 296     -56.164  32.250 124.751  1.00 46.93
ATOM   4932  O   GLU A 296     -55.201  31.479 124.632  1.00 45.38
ATOM   4933  CB  GLU A 296     -58.416  31.501 123.998  1.00 45.53
ATOM   4934  CG  GLU A 296     -59.872  31.147 124.234  1.00 55.97
ATOM   4935  CD  GLU A 296     -60.694  32.400 124.447  1.00 88.13
ATOM   4936  OE1 GLU A 296     -60.847  32.806 125.621  1.00 66.35
ATOM   4937  OE2 GLU A 296     -61.060  33.055 123.441  1.00 94.21
ATOM   4944  N   ALA A 297     -56.090  33.592 124.495  1.00 41.84
ATOM   4945  CA  ALA A 297     -54.852  34.248 124.041  1.00 38.96
ATOM   4946  C   ALA A 297     -53.744  34.077 125.057  1.00 44.01
ATOM   4947  O   ALA A 297     -52.600  33.806 124.683  1.00 42.27
ATOM   4948  CB  ALA A 297     -55.087  35.727 123.789  1.00 39.72
ATOM   4954  N   LEU A 298     -54.075  34.220 126.349  1.00 41.66
ATOM   4955  CA  LEU A 298     -53.059  34.112 127.390  1.00 40.33
ATOM   4956  C   LEU A 298     -52.576  32.686 127.577  1.00 45.35
ATOM   4957  O   LEU A 298     -51.379  32.478 127.759  1.00 43.05
ATOM   4958  CB  LEU A 298     -53.510  34.736 128.711  1.00 40.28
ATOM   4959  CG  LEU A 298     -53.878  36.191 128.680  1.00 42.73
ATOM   4960  CD1 LEU A 298     -54.289  36.641 130.036  1.00 43.70
ATOM   4961  CD2 LEU A 298     -52.735  37.072 128.157  1.00 38.88
ATOM   4973  N   ASP A 299     -53.490  31.705 127.473  1.00 43.38
ATOM   4974  CA  ASP A 299     -53.129  30.304 127.577  1.00 42.89
ATOM   4975  C   ASP A 299     -52.199  29.933 126.435  1.00 48.93
ATOM   4976  O   ASP A 299     -51.166  29.305 126.669  1.00 49.63
ATOM   4977  CB  ASP A 299     -54.381  29.424 127.580  1.00 45.68
ATOM   4978  CG  ASP A 299     -54.042  27.979 127.851  1.00 62.25
ATOM   4979  OD1 ASP A 299     -53.739  27.652 129.009  1.00 67.54
ATOM   4980  OD2 ASP A 299     -53.998  27.197 126.899  1.00 67.62
ATOM   4985  N   PHE A 300     -52.540  30.365 125.206  1.00 45.32
ATOM   4986  CA  PHE A 300     -51.730  30.118 124.028  1.00 43.21
ATOM   4987  C   PHE A 300     -50.335  30.762 124.169  1.00 48.59
ATOM   4988  O   PHE A 300     -49.335  30.076 123.975  1.00 49.75
ATOM   4989  CB  PHE A 300     -52.466  30.631 122.792  1.00 44.80
ATOM   4990  CG  PHE A 300     -51.694  30.512 121.508  1.00 43.98
ATOM   4991  CD1 PHE A 300     -51.018  29.335 121.186  1.00 44.54
ATOM   4992  CD2 PHE A 300     -51.647  31.571 120.612  1.00 46.18
ATOM   4993  CE1 PHE A 300     -50.289  29.233 120.002  1.00 44.51
ATOM   4994  CE2 PHE A 300     -50.922  31.474 119.420  1.00 48.13
ATOM   4995  CZ  PHE A 300     -50.246  30.306 119.117  1.00 44.73
ATOM   5005  N   LEU A 301     -50.270  32.063 124.516  1.00 45.12
ATOM   5006  CA  LEU A 301     -49.003  32.781 124.704  1.00 43.34
ATOM   5007  C   LEU A 301     -48.142  32.109 125.769  1.00 47.70
ATOM   5008  O   LEU A 301     -46.949  31.914 125.556  1.00 48.40
ATOM   5009  CB  LEU A 301     -49.280  34.232 125.103  1.00 44.07
ATOM   5010  CG  LEU A 301     -48.057  35.115 125.370  1.00 47.19
ATOM   5011  CD1 LEU A 301     -47.235  35.249 124.107  1.00 45.95
ATOM   5012  CD2 LEU A 301     -48.469  36.474 125.956  1.00 45.77
ATOM   5024  N   ASP A 302     -48.750  31.713 126.886  1.00 43.53
ATOM   5025  CA  ASP A 302     -48.053  31.051 127.968  1.00 42.35
ATOM   5026  C   ASP A 302     -47.329  29.790 127.498  1.00 45.06
ATOM   5027  O   ASP A 302     -46.265  29.470 128.033  1.00 45.06
ATOM   5028  CB  ASP A 302     -49.021  30.670 129.073  1.00 43.86
ATOM   5029  CG  ASP A 302     -48.274  30.322 130.334  1.00 53.13
ATOM   5030  OD1 ASP A 302     -47.771  31.258 131.000  1.00 58.34
ATOM   5031  OD2 ASP A 302     -48.126  29.102 130.631  1.00 49.32
ATOM   5036  N   LYS A 303     -47.906  29.077 126.509  1.00 38.40
ATOM   5037  CA  LYS A 303     -47.396  27.817 125.972  1.00 35.71
ATOM   5038  C   LYS A 303     -46.327  27.954 124.894  1.00 39.99
ATOM   5039  O   LYS A 303     -45.691  26.961 124.524  1.00 40.22
ATOM   5040  CB  LYS A 303     -48.557  26.939 125.535  1.00 35.30
ATOM   5041  CG  LYS A 303     -49.367  26.460 126.712  1.00 28.91
ATOM   5042  CD  LYS A 303     -50.640  25.716 126.310  1.00 33.23
ATOM   5043  CE  LYS A 303     -51.311  25.170 127.563  1.00 42.00
ATOM   5044  NZ  LYS A 303     -52.700  24.697 127.318  1.00 58.97
ATOM   5058  N   LEU A 304     -46.100  29.196 124.418  1.00 36.81
ATOM   5059  CA  LEU A 304     -45.056  29.550 123.448  1.00 33.55
ATOM   5060  C   LEU A 304     -43.856  30.098 124.174  1.00 35.39
ATOM   5061  O   LEU A 304     -42.743  29.688 123.899  1.00 35.14
ATOM   5062  CB  LEU A 304     -45.557  30.613 122.457  1.00 33.72
ATOM   5063  CG  LEU A 304     -46.699  30.206 121.543  1.00 39.02
ATOM   5064  CD1 LEU A 304     -47.157  31.385 120.741  1.00 38.43
ATOM   5065  CD2 LEU A 304     -46.307  29.034 120.623  1.00 39.74
ATOM   5077  N   LEU A 305     -44.088  31.020 125.118  1.00 34.20
ATOM   5078  CA  LEU A 305     -43.046  31.693 125.868  1.00 35.02
ATOM   5079  C   LEU A 305     -42.560  30.871 127.042  1.00 40.83
ATOM   5080  O   LEU A 305     -42.866  31.177 128.178  1.00 44.13
ATOM   5081  CB  LEU A 305     -43.453  33.147 126.241  1.00 35.06
ATOM   5082  CG  LEU A 305     -43.639  34.121 125.067  1.00 38.34
ATOM   5083  CD1 LEU A 305     -43.896  35.529 125.578  1.00 41.00
ATOM   5084  CD2 LEU A 305     -42.431  34.128 124.114  1.00 35.27
ATOM   5096  N   ARG A 306     -41.802  29.808 126.753  1.00 36.58
ATOM   5097  CA  ARG A 306     -41.186  28.924 127.760  1.00 36.64
ATOM   5098  C   ARG A 306     -39.667  28.889 127.543  1.00 44.20
ATOM   5099  O   ARG A 306     -39.209  28.822 126.390  1.00 43.47
ATOM   5100  CB  ARG A 306     -41.688  27.479 127.617  1.00 30.01
ATOM   5101  CG  ARG A 306     -43.174  27.256 127.780  1.00 37.78
ATOM   5102  CD  ARG A 306     -43.667  27.478 129.196  1.00 39.78
ATOM   5103  NE  ARG A 306     -45.112  27.377 129.220  1.00 37.40
ATOM   5104  CZ  ARG A 306     -45.771  26.270 129.527  1.00 51.90
ATOM   5105  NH1 ARG A 306     -45.114  25.174 129.884  1.00 38.48
ATOM   5106  NH2 ARG A 306     -47.093  26.255 129.508  1.00 41.26
ATOM   5120  N   TYR A 307     -38.886  28.857 128.628  1.00 42.49
ATOM   5121  CA  TYR A 307     -37.430  28.738 128.506  1.00 42.64
ATOM   5122  C   TYR A 307     -37.036  27.428 127.829  1.00 43.83
ATOM   5123  O   TYR A 307     -36.244  27.426 126.877  1.00 42.61
ATOM   5124  CB  TYR A 307     -36.768  28.753 129.882  1.00 45.23
ATOM   5125  CG  TYR A 307     -36.832  30.079 130.594  1.00 47.29
ATOM   5126  CD1 TYR A 307     -36.093  31.168 130.146  1.00 48.49
ATOM   5127  CD2 TYR A 307     -37.568  30.225 131.768  1.00 49.33
ATOM   5128  CE1 TYR A 307     -36.114  32.382 130.826  1.00 49.47
ATOM   5129  CE2 TYR A 307     -37.576  31.426 132.473  1.00 51.37
ATOM   5130  CZ  TYR A 307     -36.852  32.504 131.992  1.00 57.09
ATOM   5131  OH  TYR A 307     -36.828  33.674 132.695  1.00 56.30
ATOM   5141  N   ASP A 308     -37.570  26.309 128.351  1.00 39.36
ATOM   5142  CA  ASP A 308     -37.278  24.987 127.834  1.00 37.94
ATOM   5143  C   ASP A 308     -37.914  24.839 126.475  1.00 41.34
ATOM   5144  O   ASP A 308     -39.135  24.730 126.365  1.00 43.01
ATOM   5145  CB  ASP A 308     -37.758  23.917 128.813  1.00 39.75
ATOM   5146  CG  ASP A 308     -37.320  22.516 128.481  1.00 44.89
ATOM   5147  OD1 ASP A 308     -36.854  22.284 127.332  1.00 43.59
ATOM   5148  OD2 ASP A 308     -37.464  21.637 129.354  1.00 52.89
ATOM   5153  N   HIS A 309     -37.088  24.856 125.440  1.00 36.23
ATOM   5154  CA  HIS A 309     -37.510  24.765 124.046  1.00 34.26
ATOM   5155  C   HIS A 309     -38.354  23.520 123.772  1.00 42.08
ATOM   5156  O   HIS A 309     -39.295  23.580 122.987  1.00 44.29
ATOM   5157  CB  HIS A 309     -36.286  24.841 123.137  1.00 33.97
ATOM   5158  CG  HIS A 309     -35.208  23.843 123.469  1.00 37.33
ATOM   5159  CD2 HIS A 309     -34.914  22.659 122.880  1.00 38.07
ATOM   5160  ND1 HIS A 309     -34.306  24.064 124.503  1.00 38.98
ATOM   5161  CE1 HIS A 309     -33.512  23.010 124.511  1.00 38.55
ATOM   5162  NE2 HIS A 309     -33.843  22.135 123.561  1.00 38.54
ATOM   5170  N   GLN A 310     -38.092  22.421 124.493  1.00 38.86
ATOM   5171  CA  GLN A 310     -38.846  21.171 124.349  1.00 37.38
ATOM   5172  C   GLN A 310     -40.284  21.284 124.837  1.00 41.69
ATOM   5173  O   GLN A 310     -41.145  20.525 124.380  1.00 42.44
ATOM   5174  CB  GLN A 310     -38.137  20.026 125.068  1.00 38.22
ATOM   5175  CG  GLN A 310     -36.813  19.678 124.416  1.00 69.13
ATOM   5176  CD  GLN A 310     -36.068  18.492 124.974  1.00 97.44
ATOM   5177  NE2 GLN A 310     -36.619  17.783 125.977  1.00 94.88
ATOM   5178  OE1 GLN A 310     -34.955  18.203 124.506  1.00 87.51
ATOM   5187  N   SER A 311     -40.544  22.204 125.776  1.00 36.66
ATOM   5188  CA  SER A 311     -41.859  22.374 126.375  1.00 35.35
ATOM   5189  C   SER A 311     -42.770  23.339 125.623  1.00 42.09
ATOM   5190  O   SER A 311     -43.949  23.435 125.964  1.00 45.05
ATOM   5191  CB  SER A 311     -41.729  22.741 127.843  1.00 35.52
ATOM   5192  OG  SER A 311     -41.282  24.075 127.965  1.00 53.68
ATOM   5198  N   ARG A 312     -42.263  24.019 124.586  1.00 37.10
ATOM   5199  CA  ARG A 312     -43.088  24.947 123.798  1.00 35.72
ATOM   5200  C   ARG A 312     -44.013  24.167 122.883  1.00 39.30
ATOM   5201  O   ARG A 312     -43.685  23.050 122.458  1.00 37.85
ATOM   5202  CB  ARG A 312     -42.205  25.855 122.913  1.00 31.89
ATOM   5203  CG  ARG A 312     -41.252  26.711 123.687  1.00 28.48
ATOM   5204  CD  ARG A 312     -40.301  27.499 122.829  1.00 34.95
ATOM   5205  NE  ARG A 312     -39.202  27.992 123.665  1.00 42.31
ATOM   5206  CZ  ARG A 312     -37.955  28.181 123.249  1.00 49.56
ATOM   5207  NH1 ARG A 312     -37.646  28.026 121.973  1.00 28.05
ATOM   5208  NH2 ARG A 312     -37.010  28.544 124.105  1.00 39.80
ATOM   5222  N   LEU A 313     -45.140  24.776 122.516  1.00 35.95
ATOM   5223  CA  LEU A 313     -46.030  24.137 121.560  1.00 35.63
ATOM   5224  C   LEU A 313     -45.293  24.033 120.233  1.00 40.92
ATOM   5225  O   LEU A 313     -44.525  24.941 119.865  1.00 40.94
ATOM   5226  CB  LEU A 313     -47.276  25.020 121.321  1.00 36.09
ATOM   5227  CG  LEU A 313     -48.336  25.077 122.409  1.00 39.45
ATOM   5228  CD1 LEU A 313     -49.350  26.191 122.129  1.00 38.76
ATOM   5229  CD2 LEU A 313     -49.029  23.781 122.559  1.00 38.16
ATOM   5241  N   THR A 314     -45.566  22.959 119.484  1.00 37.44
ATOM   5242  CA  THR A 314     -45.068  22.838 118.118  1.00 36.38
ATOM   5243  C   THR A 314     -46.046  23.673 117.276  1.00 43.67
ATOM   5244  O   THR A 314     -47.115  24.069 117.768  1.00 44.35
ATOM   5245  CB  THR A 314     -45.062  21.381 117.661  1.00 35.93
ATOM   5246  CG2 THR A 314     -44.154  20.484 118.521  1.00 29.54
ATOM   5247  OG1 THR A 314     -46.401  20.894 117.682  1.00 38.62
ATOM   5255  N   ALA A 315     -45.704  23.936 116.007  1.00 40.28
ATOM   5256  CA  ALA A 315     -46.610  24.681 115.136  1.00 38.34
ATOM   5257  C   ALA A 315     -47.937  23.906 114.943  1.00 43.32
ATOM   5258  O   ALA A 315     -48.991  24.516 114.982  1.00 44.38
ATOM   5259  CB  ALA A 315     -45.943  24.941 113.810  1.00 37.62
ATOM   5265  N   ARG A 316     -47.879  22.561 114.825  1.00 39.78
ATOM   5266  CA  ARG A 316     -49.069  21.734 114.683  1.00 41.31
ATOM   5267  C   ARG A 316     -49.944  21.771 115.948  1.00 45.72
ATOM   5268  O   ARG A 316     -51.170  21.892 115.843  1.00 45.97
ATOM   5269  CB  ARG A 316     -48.687  20.291 114.357  1.00 45.42
ATOM   5270  CG  ARG A 316     -49.481  19.601 113.238  1.00 68.32
ATOM   5271  CD  ARG A 316     -51.017  19.617 113.326  1.00 90.08
ATOM   5272  NE  ARG A 316     -51.643  20.624 112.448  1.00104.07
ATOM   5273  CZ  ARG A 316     -51.829  20.488 111.133  1.00119.18
ATOM   5274  NH1 ARG A 316     -51.410  19.394 110.502  1.00102.24
ATOM   5275  NH2 ARG A 316     -52.411  21.457 110.436  1.00107.11
ATOM   5289  N   GLU A 317     -49.324  21.684 117.130  1.00 40.87
ATOM   5290  CA  GLU A 317     -50.043  21.740 118.400  1.00 40.33
ATOM   5291  C   GLU A 317     -50.694  23.121 118.551  1.00 44.45
ATOM   5292  O   GLU A 317     -51.854  23.214 118.986  1.00 44.07
ATOM   5293  CB  GLU A 317     -49.092  21.472 119.579  1.00 40.54
ATOM   5294  CG  GLU A 317     -48.675  20.022 119.754  1.00 36.29
ATOM   5295  CD  GLU A 317     -47.475  19.809 120.665  1.00 45.66
ATOM   5296  OE1 GLU A 317     -46.875  20.809 121.109  1.00 42.14
ATOM   5297  OE2 GLU A 317     -47.117  18.639 120.926  1.00 50.69
ATOM   5304  N   ALA A 318     -49.949  24.195 118.172  1.00 39.14
ATOM   5305  CA  ALA A 318     -50.450  25.577 118.235  1.00 37.27
ATOM   5306  C   ALA A 318     -51.694  25.750 117.372  1.00 41.54
ATOM   5307  O   ALA A 318     -52.653  26.375 117.805  1.00 42.64
ATOM   5308  CB  ALA A 318     -49.369  26.553 117.808  1.00 36.09
ATOM   5314  N   MET A 319     -51.714  25.144 116.182  1.00 38.54
ATOM   5315  CA  MET A 319     -52.863  25.250 115.279  1.00 39.25
ATOM   5316  C   MET A 319     -54.137  24.644 115.846  1.00 46.77
ATOM   5317  O   MET A 319     -55.230  25.008 115.415  1.00 49.63
ATOM   5318  CB  MET A 319     -52.522  24.621 113.932  1.00 40.74
ATOM   5319  CG  MET A 319     -51.534  25.448 113.135  1.00 43.22
ATOM   5320  SD  MET A 319     -51.000  24.621 111.626  1.00 45.81
ATOM   5321  CE  MET A 319     -52.381  24.903 110.595  1.00 43.36
ATOM   5331  N   GLU A 320     -53.994  23.711 116.798  1.00 42.14
ATOM   5332  CA  GLU A 320     -55.100  23.011 117.420  1.00 42.70
ATOM   5333  C   GLU A 320     -55.582  23.706 118.683  1.00 46.14
ATOM   5334  O   GLU A 320     -56.539  23.235 119.286  1.00 47.56
ATOM   5335  CB  GLU A 320     -54.703  21.555 117.725  1.00 44.15
ATOM   5336  CG  GLU A 320     -54.427  20.688 116.498  1.00 56.21
ATOM   5337  CD  GLU A 320     -53.544  19.455 116.704  1.00 88.38
ATOM   5338  OE1 GLU A 320     -53.400  18.677 115.730  1.00 91.04
ATOM   5339  OE2 GLU A 320     -52.987  19.268 117.815  1.00 77.84
ATOM   5346  N   HIS A 321     -54.963  24.822 119.067  1.00 42.04
ATOM   5347  CA  HIS A 321     -55.319  25.543 120.281  1.00 42.76
ATOM   5348  C   HIS A 321     -56.690  26.230 120.197  1.00 50.15
ATOM   5349  O   HIS A 321     -57.007  26.819 119.162  1.00 52.50
ATOM   5350  CB  HIS A 321     -54.229  26.578 120.642  1.00 41.97
ATOM   5351  CG  HIS A 321     -54.368  27.127 122.034  1.00 45.17
ATOM   5352  CD2 HIS A 321     -53.765  26.740 123.176  1.00 44.71
ATOM   5353  ND1 HIS A 321     -55.270  28.155 122.336  1.00 47.52
ATOM   5354  CE1 HIS A 321     -55.181  28.346 123.639  1.00 46.26
ATOM   5355  NE2 HIS A 321     -54.284  27.529 124.185  1.00 45.55
ATOM   5363  N   PRO A 322     -57.482  26.232 121.298  1.00 47.01
ATOM   5364  CA  PRO A 322     -58.780  26.963 121.298  1.00 47.43
ATOM   5365  C   PRO A 322     -58.770  28.418 120.790  1.00 49.42
ATOM   5366  O   PRO A 322     -59.781  28.861 120.248  1.00 50.69
ATOM   5367  CB  PRO A 322     -59.212  26.896 122.764  1.00 48.60
ATOM   5368  CG  PRO A 322     -58.649  25.609 123.232  1.00 52.29
ATOM   5369  CD  PRO A 322     -57.283  25.529 122.586  1.00 47.43
ATOM   5377  N   TYR A 323     -57.639  29.137 120.917  1.00 42.53
ATOM   5378  CA  TYR A 323     -57.485  30.514 120.429  1.00 41.32
ATOM   5379  C   TYR A 323     -57.879  30.610 118.936  1.00 47.71
ATOM   5380  O   TYR A 323     -58.425  31.638 118.505  1.00 47.22
ATOM   5381  CB  TYR A 323     -56.035  30.989 120.661  1.00 39.08
ATOM   5382  CG  TYR A 323     -55.683  32.384 120.207  1.00 40.24
ATOM   5383  CD1 TYR A 323     -56.252  33.505 120.816  1.00 44.27
ATOM   5384  CD2 TYR A 323     -54.676  32.596 119.274  1.00 39.90
ATOM   5385  CE1 TYR A 323     -55.866  34.801 120.459  1.00 44.33
ATOM   5386  CE2 TYR A 323     -54.281  33.888 118.909  1.00 40.96
ATOM   5387  CZ  TYR A 323     -54.877  34.985 119.508  1.00 51.20
ATOM   5388  OH  TYR A 323     -54.510  36.250 119.136  1.00 56.89
ATOM   5398  N   PHE A 324     -57.665  29.512 118.168  1.00 44.07
ATOM   5399  CA  PHE A 324     -57.966  29.473 116.745  1.00 43.38
ATOM   5400  C   PHE A 324     -59.271  28.808 116.362  1.00 51.70
ATOM   5401  O   PHE A 324     -59.515  28.672 115.159  1.00 53.47
ATOM   5402  CB  PHE A 324     -56.822  28.799 116.002  1.00 41.67
ATOM   5403  CG  PHE A 324     -55.505  29.470 116.242  1.00 40.27
ATOM   5404  CD1 PHE A 324     -55.248  30.739 115.728  1.00 41.84
ATOM   5405  CD2 PHE A 324     -54.507  28.834 116.977  1.00 39.43
ATOM   5406  CE1 PHE A 324     -54.007  31.355 115.937  1.00 40.96
ATOM   5407  CE2 PHE A 324     -53.274  29.454 117.191  1.00 39.73
ATOM   5408  CZ  PHE A 324     -53.036  30.717 116.680  1.00 37.64
ATOM   5418  N   TYR A 325     -60.093  28.361 117.332  1.00 48.64
ATOM   5419  CA  TYR A 325     -61.332  27.642 117.024  1.00 49.57
ATOM   5420  C   TYR A 325     -62.247  28.361 116.048  1.00 55.78
ATOM   5421  O   TYR A 325     -62.859  27.716 115.177  1.00 56.12
ATOM   5422  CB  TYR A 325     -62.098  27.242 118.300  1.00 51.22
ATOM   5423  CG  TYR A 325     -61.537  26.043 119.041  1.00 51.78
ATOM   5424  CD1 TYR A 325     -60.464  25.309 118.524  1.00 50.24
ATOM   5425  CD2 TYR A 325     -62.083  25.635 120.260  1.00 53.89
ATOM   5426  CE1 TYR A 325     -59.949  24.203 119.200  1.00 49.76
ATOM   5427  CE2 TYR A 325     -61.562  24.537 120.956  1.00 54.19
ATOM   5428  CZ  TYR A 325     -60.503  23.818 120.414  1.00 61.29
ATOM   5429  OH  TYR A 325     -59.977  22.748 121.096  1.00 64.02
ATOM   5439  N   THR A 326     -62.353  29.685 116.187  1.00 54.19
ATOM   5440  CA  THR A 326     -63.232  30.453 115.305  1.00 57.02
ATOM   5441  C   THR A 326     -62.646  30.631 113.902  1.00 62.19
ATOM   5442  O   THR A 326     -63.385  30.644 112.924  1.00 64.32
ATOM   5443  CB  THR A 326     -63.651  31.763 115.936  1.00 68.87
ATOM   5444  CG2 THR A 326     -64.508  31.574 117.150  1.00 67.39
ATOM   5445  OG1 THR A 326     -62.479  32.531 116.235  1.00 77.10
ATOM   5453  N   VAL A 327     -61.319  30.712 113.800  1.00 56.15
ATOM   5454  CA  VAL A 327     -60.651  30.856 112.501  1.00 55.44
ATOM   5455  C   VAL A 327     -60.885  29.568 111.662  1.00 60.98
ATOM   5456  O   VAL A 327     -61.293  29.637 110.499  1.00 62.61
ATOM   5457  CB  VAL A 327     -59.132  31.018 112.692  1.00 55.55
ATOM   5458  CG1 VAL A 327     -58.436  31.180 111.358  1.00 53.51
ATOM   5459  CG2 VAL A 327     -58.758  32.118 113.683  1.00 55.00
ATOM   5469  N   VAL A 328     -60.568  28.411 112.285  1.00 55.29
ATOM   5470  CA  VAL A 328     -60.690  27.053 111.753  1.00 54.53
ATOM   5471  C   VAL A 328     -62.137  26.781 111.305  1.00 63.43
ATOM   5472  O   VAL A 328     -62.347  26.242 110.218  1.00 64.63
ATOM   5473  CB  VAL A 328     -60.165  26.025 112.781  1.00 54.86
ATOM   5474  CG1 VAL A 328     -60.488  24.604 112.368  1.00 54.62
ATOM   5475  CG2 VAL A 328     -58.668  26.179 112.988  1.00 51.66
ATOM   5485  N   LYS A 329     -63.119  27.211 112.103  1.00 62.62
ATOM   5486  CA  LYS A 329     -64.529  27.059 111.756  1.00 65.31
ATOM   5487  C   LYS A 329     -64.817  27.830 110.460  1.00 73.67
ATOM   5488  O   LYS A 329     -65.336  27.240 109.519  1.00 75.32
ATOM   5489  CB  LYS A 329     -65.425  27.543 112.909  1.00 68.69
ATOM   5490  CG  LYS A 329     -66.890  27.108 112.797  1.00 84.80
ATOM   5491  CD  LYS A 329     -67.856  28.097 113.476  1.00 96.01
ATOM   5492  CE  LYS A 329     -68.126  29.349 112.661  1.00107.16
ATOM   5493  NZ  LYS A 329     -69.560  29.477 112.293  1.00112.85
ATOM   5507  N   ASP A 330     -64.420  29.117 110.398  1.00 72.11
ATOM   5508  CA  ASP A 330     -64.594  30.023 109.253  1.00 73.18
ATOM   5509  C   ASP A 330     -63.838  29.581 107.989  1.00 77.34
ATOM   5510  O   ASP A 330     -64.286  29.899 106.891  1.00 77.70
ATOM   5511  CB  ASP A 330     -64.187  31.454 109.630  1.00 74.61
ATOM   5512  CG  ASP A 330     -65.019  32.177 110.676  1.00 94.37
ATOM   5513  OD1 ASP A 330     -65.960  31.554 111.254  1.00 98.33
ATOM   5514  OD2 ASP A 330     -64.750  33.357 110.915  1.00103.04
ATOM   5519  N   GLN A 331     -62.714  28.853 108.130  1.00 73.48
ATOM   5520  CA  GLN A 331     -61.960  28.356 106.972  1.00 73.79
ATOM   5521  C   GLN A 331     -62.546  27.055 106.353  1.00 80.63
ATOM   5522  O   GLN A 331     -61.918  26.473 105.453  1.00 80.70
ATOM   5523  CB  GLN A 331     -60.461  28.197 107.293  1.00 72.90
ATOM   5524  CG  GLN A 331     -59.685  29.519 107.308  1.00 82.02
ATOM   5525  CD  GLN A 331     -58.201  29.328 107.497  1.00 94.13
ATOM   5526  NE2 GLN A 331     -57.522  30.416 107.874  1.00 77.94
ATOM   5527  OE1 GLN A 331     -57.648  28.226 107.303  1.00 88.67
ATOM   5536  N   ALA A 332     -63.747  26.623 106.801  1.00 77.61
ATOM   5537  CA  ALA A 332     -64.421  25.429 106.299  1.00 82.97
ATOM   5538  C   ALA A 332     -65.877  25.738 105.881  1.00119.25
ATOM   5539  O   ALA A 332     -66.136  26.591 105.021  1.00 87.26
ATOM   5540  CB  ALA A 332     -64.385  24.336 107.361  1.00 82.98



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: April 25th, 2023.