###################################
     #  Assigned chemical shift lists  #
     ###################################

###################################################################
#       Chemical Shift Ambiguity Index Value Definitions          #
#                                                                 #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains.                              #
#                                                                 #
#   Index Value            Definition                             #
#                                                                 #
#      1             Unique (including isolated methyl protons,   #
#                         geminal atoms, and geminal methyl       #
#                         groups with identical chemical shifts)  #
#                         (e.g. ILE HD11, HD12, HD13 protons)     #
#      2             Ambiguity of geminal atoms or geminal methyl #
#                         proton groups (e.g. ASP HB2 and HB3     #
#                         protons, LEU CD1 and CD2 carbons, or    #
#                         LEU HD11, HD12, HD13 and HD21, HD22,    #
#                         HD23 methyl protons)                    #
#      3             Aromatic atoms on opposite sides of          #
#                         symmetrical rings (e.g. TYR HE1 and HE2 #
#                         protons)                                #
#      4             Intraresidue ambiguities (e.g. LYS HG and    #
#                         HD protons or TRP HZ2 and HZ3 protons)  #
#      5             Interresidue ambiguities (LYS 12 vs. LYS 27) #
#      6             Intermolecular ambiguities (e.g. ASP 31 CA   #
#                         in monomer 1 and ASP 31 CA in monomer 2 #
#                         of an asymmetrical homodimer, duplex    #
#                         DNA assignments, or other assignments   #
#                         that may apply to atoms in one or more  #
#                         molecule in the molecular assembly)     #
#      9             Ambiguous, specific ambiguity not defined    #
#                                                                 #
###################################################################

save_assigned_chemical_shifts_1
   _Assigned_chem_shift_list.Sf_category                  assigned_chemical_shifts
   _Assigned_chem_shift_list.Sf_framecode                 assigned_chemical_shifts_1
   _Assigned_chem_shift_list.Entry_ID                     50428
   _Assigned_chem_shift_list.ID                           1
   _Assigned_chem_shift_list.Name                         chemical_shifts
   _Assigned_chem_shift_list.Sample_condition_list_ID     2
   _Assigned_chem_shift_list.Sample_condition_list_label  $sample_conditions_2
   _Assigned_chem_shift_list.Chem_shift_reference_ID      1
   _Assigned_chem_shift_list.Chem_shift_reference_label   $chem_shift_reference_1
   _Assigned_chem_shift_list.Chem_shift_1H_err            0.1
   _Assigned_chem_shift_list.Chem_shift_13C_err           0.3
   _Assigned_chem_shift_list.Chem_shift_15N_err           0.3
   _Assigned_chem_shift_list.Chem_shift_31P_err           .
   _Assigned_chem_shift_list.Chem_shift_2H_err            .
   _Assigned_chem_shift_list.Chem_shift_19F_err           .
   _Assigned_chem_shift_list.Error_derivation_method      .
   _Assigned_chem_shift_list.Details                      .
   _Assigned_chem_shift_list.Text_data_format             .
   _Assigned_chem_shift_list.Text_data                    .

   loop_
      _Chem_shift_experiment.Experiment_ID
      _Chem_shift_experiment.Experiment_name
      _Chem_shift_experiment.Sample_ID
      _Chem_shift_experiment.Sample_label
      _Chem_shift_experiment.Sample_state
      _Chem_shift_experiment.Entry_ID
      _Chem_shift_experiment.Assigned_chem_shift_list_ID

     1    '3D NCOCX'            .   .   .   50428   1    
     2    '3D NCACX'            .   .   .   50428   1    
     3    '3D CONCA'            .   .   .   50428   1    
     4    '3D CANCO'            .   .   .   50428   1    
     5    '2D DARR'             .   .   .   50428   1    
     6    '2D RFDR'             .   .   .   50428   1    
     9    '2D NCO'              .   .   .   50428   1    
     10   '2D NCA'              .   .   .   50428   1    
     11   '3D (H)NCAH'          .   .   .   50428   1    
     12   '3D (H)CBCAH'         .   .   .   50428   1    
     13   '3D (H)COCAH'         .   .   .   50428   1    
     14   '3D (H)CCH-TOCSY'     .   .   .   50428   1    
     15   '2D 1H-13C CP-HSQC'   .   .   .   50428   1    

   stop_

   loop_
      _Chem_shift_software.Software_ID
      _Chem_shift_software.Software_label
      _Chem_shift_software.Method_ID
      _Chem_shift_software.Method_label
      _Chem_shift_software.Entry_ID
      _Chem_shift_software.Assigned_chem_shift_list_ID

     2   $software_2   .   .   50428   1    

   stop_

   loop_
      _Atom_chem_shift.ID
      _Atom_chem_shift.Assembly_atom_ID
      _Atom_chem_shift.Entity_assembly_ID
      _Atom_chem_shift.Entity_assembly_asym_ID
      _Atom_chem_shift.Entity_ID
      _Atom_chem_shift.Comp_index_ID
      _Atom_chem_shift.Seq_ID
      _Atom_chem_shift.Comp_ID
      _Atom_chem_shift.Atom_ID
      _Atom_chem_shift.Atom_type
      _Atom_chem_shift.Atom_isotope_number
      _Atom_chem_shift.Val
      _Atom_chem_shift.Val_err
      _Atom_chem_shift.Assign_fig_of_merit
      _Atom_chem_shift.Ambiguity_code
      _Atom_chem_shift.Ambiguity_set_ID
      _Atom_chem_shift.Occupancy
      _Atom_chem_shift.Resonance_ID
      _Atom_chem_shift.Auth_entity_assembly_ID
      _Atom_chem_shift.Auth_asym_ID
      _Atom_chem_shift.Auth_seq_ID
      _Atom_chem_shift.Auth_comp_ID
      _Atom_chem_shift.Auth_atom_ID
      _Atom_chem_shift.Details
      _Atom_chem_shift.Entry_ID
      _Atom_chem_shift.Assigned_chem_shift_list_ID

     1     .   1   .   1   5    5    ILE   HA     H   1    3.194     0.100   .   1   .   .   .   .   .   5    ILE   HA     .   50428   1    
     2     .   1   .   1   5    5    ILE   HB     H   1    1.504     0.100   .   1   .   .   .   .   .   5    ILE   HB     .   50428   1    
     3     .   1   .   1   5    5    ILE   HG12   H   1    1.072     0.100   .   1   .   .   .   .   .   5    ILE   HG12   .   50428   1    
     4     .   1   .   1   5    5    ILE   HG13   H   1    1.072     0.100   .   1   .   .   .   .   .   5    ILE   HG13   .   50428   1    
     5     .   1   .   1   5    5    ILE   HG21   H   1    0.372     0.100   .   1   .   .   .   .   .   5    ILE   HG2    .   50428   1    
     6     .   1   .   1   5    5    ILE   HG22   H   1    0.372     0.100   .   1   .   .   .   .   .   5    ILE   HG2    .   50428   1    
     7     .   1   .   1   5    5    ILE   HG23   H   1    0.372     0.100   .   1   .   .   .   .   .   5    ILE   HG2    .   50428   1    
     8     .   1   .   1   5    5    ILE   HD11   H   1    0.309     0.100   .   1   .   .   .   .   .   5    ILE   HD1    .   50428   1    
     9     .   1   .   1   5    5    ILE   HD12   H   1    0.309     0.100   .   1   .   .   .   .   .   5    ILE   HD1    .   50428   1    
     10    .   1   .   1   5    5    ILE   HD13   H   1    0.309     0.100   .   1   .   .   .   .   .   5    ILE   HD1    .   50428   1    
     11    .   1   .   1   5    5    ILE   C      C   13   177.537   0.3     .   1   .   .   .   .   .   5    ILE   C      .   50428   1    
     12    .   1   .   1   5    5    ILE   CA     C   13   63.566    0.3     .   1   .   .   .   .   .   5    ILE   CA     .   50428   1    
     13    .   1   .   1   5    5    ILE   CB     C   13   36.786    0.3     .   1   .   .   .   .   .   5    ILE   CB     .   50428   1    
     14    .   1   .   1   5    5    ILE   CG1    C   13   28.910    0.3     .   1   .   .   .   .   .   5    ILE   CG1    .   50428   1    
     15    .   1   .   1   5    5    ILE   CG2    C   13   17.278    0.3     .   1   .   .   .   .   .   5    ILE   CG2    .   50428   1    
     16    .   1   .   1   5    5    ILE   CD1    C   13   12.757    0.3     .   1   .   .   .   .   .   5    ILE   CD1    .   50428   1    
     17    .   1   .   1   5    5    ILE   N      N   15   120.095   0.3     .   1   .   .   .   .   .   5    ILE   N      .   50428   1    
     18    .   1   .   1   6    6    GLU   HA     H   1    3.521     0.100   .   1   .   .   .   .   .   6    GLU   HA     .   50428   1    
     19    .   1   .   1   6    6    GLU   HB2    H   1    1.589     0.100   .   1   .   .   .   .   .   6    GLU   HB2    .   50428   1    
     20    .   1   .   1   6    6    GLU   HB3    H   1    1.589     0.100   .   1   .   .   .   .   .   6    GLU   HB3    .   50428   1    
     21    .   1   .   1   6    6    GLU   HG2    H   1    1.835     0.100   .   1   .   .   .   .   .   6    GLU   HG2    .   50428   1    
     22    .   1   .   1   6    6    GLU   HG3    H   1    1.835     0.100   .   1   .   .   .   .   .   6    GLU   HG3    .   50428   1    
     23    .   1   .   1   6    6    GLU   C      C   13   179.233   0.3     .   1   .   .   .   .   .   6    GLU   C      .   50428   1    
     24    .   1   .   1   6    6    GLU   CA     C   13   59.143    0.3     .   1   .   .   .   .   .   6    GLU   CA     .   50428   1    
     25    .   1   .   1   6    6    GLU   CB     C   13   28.763    0.3     .   1   .   .   .   .   .   6    GLU   CB     .   50428   1    
     26    .   1   .   1   6    6    GLU   CG     C   13   35.860    0.3     .   1   .   .   .   .   .   6    GLU   CG     .   50428   1    
     27    .   1   .   1   6    6    GLU   CD     C   13   182.664   0.3     .   1   .   .   .   .   .   6    GLU   CD     .   50428   1    
     28    .   1   .   1   6    6    GLU   N      N   15   122.295   0.3     .   1   .   .   .   .   .   6    GLU   N      .   50428   1    
     29    .   1   .   1   7    7    ASN   HA     H   1    3.996     0.100   .   1   .   .   .   .   .   7    ASN   HA     .   50428   1    
     30    .   1   .   1   7    7    ASN   HB2    H   1    2.325     0.100   .   1   .   .   .   .   .   7    ASN   HB2    .   50428   1    
     31    .   1   .   1   7    7    ASN   HB3    H   1    2.325     0.100   .   1   .   .   .   .   .   7    ASN   HB3    .   50428   1    
     32    .   1   .   1   7    7    ASN   C      C   13   177.545   0.3     .   1   .   .   .   .   .   7    ASN   C      .   50428   1    
     33    .   1   .   1   7    7    ASN   CA     C   13   55.264    0.3     .   1   .   .   .   .   .   7    ASN   CA     .   50428   1    
     34    .   1   .   1   7    7    ASN   CB     C   13   37.255    0.3     .   1   .   .   .   .   .   7    ASN   CB     .   50428   1    
     35    .   1   .   1   7    7    ASN   CG     C   13   175.140   0.3     .   1   .   .   .   .   .   7    ASN   CG     .   50428   1    
     36    .   1   .   1   7    7    ASN   N      N   15   117.407   0.3     .   1   .   .   .   .   .   7    ASN   N      .   50428   1    
     37    .   1   .   1   8    8    LEU   H      H   1    8.223     0.100   .   1   .   .   .   .   .   8    LEU   H      .   50428   1    
     38    .   1   .   1   8    8    LEU   HA     H   1    3.758     0.100   .   1   .   .   .   .   .   8    LEU   HA     .   50428   1    
     39    .   1   .   1   8    8    LEU   HB2    H   1    1.178     0.100   .   1   .   .   .   .   .   8    LEU   HB2    .   50428   1    
     40    .   1   .   1   8    8    LEU   HB3    H   1    1.178     0.100   .   1   .   .   .   .   .   8    LEU   HB3    .   50428   1    
     41    .   1   .   1   8    8    LEU   HG     H   1    1.098     0.100   .   1   .   .   .   .   .   8    LEU   HG     .   50428   1    
     42    .   1   .   1   8    8    LEU   HD11   H   1    0.487     0.100   .   1   .   .   .   .   .   8    LEU   HD1    .   50428   1    
     43    .   1   .   1   8    8    LEU   HD12   H   1    0.487     0.100   .   1   .   .   .   .   .   8    LEU   HD1    .   50428   1    
     44    .   1   .   1   8    8    LEU   HD13   H   1    0.487     0.100   .   1   .   .   .   .   .   8    LEU   HD1    .   50428   1    
     45    .   1   .   1   8    8    LEU   HD21   H   1    0.305     0.100   .   1   .   .   .   .   .   8    LEU   HD2    .   50428   1    
     46    .   1   .   1   8    8    LEU   HD22   H   1    0.305     0.100   .   1   .   .   .   .   .   8    LEU   HD2    .   50428   1    
     47    .   1   .   1   8    8    LEU   HD23   H   1    0.305     0.100   .   1   .   .   .   .   .   8    LEU   HD2    .   50428   1    
     48    .   1   .   1   8    8    LEU   C      C   13   177.449   0.3     .   1   .   .   .   .   .   8    LEU   C      .   50428   1    
     49    .   1   .   1   8    8    LEU   CA     C   13   57.190    0.3     .   1   .   .   .   .   .   8    LEU   CA     .   50428   1    
     50    .   1   .   1   8    8    LEU   CB     C   13   40.737    0.3     .   1   .   .   .   .   .   8    LEU   CB     .   50428   1    
     51    .   1   .   1   8    8    LEU   CG     C   13   27.006    0.3     .   1   .   .   .   .   .   8    LEU   CG     .   50428   1    
     52    .   1   .   1   8    8    LEU   CD1    C   13   23.374    0.3     .   1   .   .   .   .   .   8    LEU   CD1    .   50428   1    
     53    .   1   .   1   8    8    LEU   CD2    C   13   25.679    0.3     .   1   .   .   .   .   .   8    LEU   CD2    .   50428   1    
     54    .   1   .   1   8    8    LEU   N      N   15   123.342   0.3     .   1   .   .   .   .   .   8    LEU   N      .   50428   1    
     55    .   1   .   1   9    9    ASN   HA     H   1    3.605     0.100   .   1   .   .   .   .   .   9    ASN   HA     .   50428   1    
     56    .   1   .   1   9    9    ASN   HB2    H   1    2.253     0.100   .   1   .   .   .   .   .   9    ASN   HB2    .   50428   1    
     57    .   1   .   1   9    9    ASN   HB3    H   1    2.253     0.100   .   1   .   .   .   .   .   9    ASN   HB3    .   50428   1    
     58    .   1   .   1   9    9    ASN   C      C   13   175.911   0.3     .   1   .   .   .   .   .   9    ASN   C      .   50428   1    
     59    .   1   .   1   9    9    ASN   CA     C   13   57.095    0.3     .   1   .   .   .   .   .   9    ASN   CA     .   50428   1    
     60    .   1   .   1   9    9    ASN   CB     C   13   39.351    0.3     .   1   .   .   .   .   .   9    ASN   CB     .   50428   1    
     61    .   1   .   1   9    9    ASN   N      N   15   117.511   0.3     .   1   .   .   .   .   .   9    ASN   N      .   50428   1    
     62    .   1   .   1   10   10   LYS   HA     H   1    3.583     0.100   .   1   .   .   .   .   .   10   LYS   HA     .   50428   1    
     63    .   1   .   1   10   10   LYS   HB2    H   1    1.431     0.100   .   1   .   .   .   .   .   10   LYS   HB2    .   50428   1    
     64    .   1   .   1   10   10   LYS   HB3    H   1    1.431     0.100   .   1   .   .   .   .   .   10   LYS   HB3    .   50428   1    
     65    .   1   .   1   10   10   LYS   C      C   13   177.109   0.3     .   1   .   .   .   .   .   10   LYS   C      .   50428   1    
     66    .   1   .   1   10   10   LYS   CA     C   13   59.063    0.3     .   1   .   .   .   .   .   10   LYS   CA     .   50428   1    
     67    .   1   .   1   10   10   LYS   CB     C   13   31.963    0.3     .   1   .   .   .   .   .   10   LYS   CB     .   50428   1    
     68    .   1   .   1   10   10   LYS   CG     C   13   24.696    0.3     .   1   .   .   .   .   .   10   LYS   CG     .   50428   1    
     69    .   1   .   1   10   10   LYS   CD     C   13   28.886    0.3     .   1   .   .   .   .   .   10   LYS   CD     .   50428   1    
     70    .   1   .   1   10   10   LYS   CE     C   13   41.656    0.3     .   1   .   .   .   .   .   10   LYS   CE     .   50428   1    
     71    .   1   .   1   10   10   LYS   N      N   15   117.302   0.3     .   1   .   .   .   .   .   10   LYS   N      .   50428   1    
     72    .   1   .   1   11   11   LYS   HA     H   1    3.612     0.100   .   1   .   .   .   .   .   11   LYS   HA     .   50428   1    
     73    .   1   .   1   11   11   LYS   HB2    H   1    1.443     0.100   .   1   .   .   .   .   .   11   LYS   HB2    .   50428   1    
     74    .   1   .   1   11   11   LYS   HB3    H   1    1.443     0.100   .   1   .   .   .   .   .   11   LYS   HB3    .   50428   1    
     75    .   1   .   1   11   11   LYS   C      C   13   179.742   0.3     .   1   .   .   .   .   .   11   LYS   C      .   50428   1    
     76    .   1   .   1   11   11   LYS   CA     C   13   59.073    0.3     .   1   .   .   .   .   .   11   LYS   CA     .   50428   1    
     77    .   1   .   1   11   11   LYS   CB     C   13   31.811    0.3     .   1   .   .   .   .   .   11   LYS   CB     .   50428   1    
     78    .   1   .   1   11   11   LYS   CG     C   13   24.811    0.3     .   1   .   .   .   .   .   11   LYS   CG     .   50428   1    
     79    .   1   .   1   11   11   LYS   CD     C   13   29.930    0.3     .   1   .   .   .   .   .   11   LYS   CD     .   50428   1    
     80    .   1   .   1   11   11   LYS   CE     C   13   41.592    0.3     .   1   .   .   .   .   .   11   LYS   CE     .   50428   1    
     81    .   1   .   1   11   11   LYS   N      N   15   119.327   0.3     .   1   .   .   .   .   .   11   LYS   N      .   50428   1    
     82    .   1   .   1   12   12   VAL   H      H   1    8.467     0.100   .   1   .   .   .   .   .   12   VAL   H      .   50428   1    
     83    .   1   .   1   12   12   VAL   HA     H   1    2.928     0.100   .   1   .   .   .   .   .   12   VAL   HA     .   50428   1    
     84    .   1   .   1   12   12   VAL   HB     H   1    1.616     0.100   .   1   .   .   .   .   .   12   VAL   HB     .   50428   1    
     85    .   1   .   1   12   12   VAL   HG11   H   1    -0.083    0.100   .   1   .   .   .   .   .   12   VAL   HG1    .   50428   1    
     86    .   1   .   1   12   12   VAL   HG12   H   1    -0.083    0.100   .   1   .   .   .   .   .   12   VAL   HG1    .   50428   1    
     87    .   1   .   1   12   12   VAL   HG13   H   1    -0.083    0.100   .   1   .   .   .   .   .   12   VAL   HG1    .   50428   1    
     88    .   1   .   1   12   12   VAL   HG21   H   1    0.294     0.100   .   1   .   .   .   .   .   12   VAL   HG2    .   50428   1    
     89    .   1   .   1   12   12   VAL   HG22   H   1    0.294     0.100   .   1   .   .   .   .   .   12   VAL   HG2    .   50428   1    
     90    .   1   .   1   12   12   VAL   HG23   H   1    0.294     0.100   .   1   .   .   .   .   .   12   VAL   HG2    .   50428   1    
     91    .   1   .   1   12   12   VAL   C      C   13   175.780   0.3     .   1   .   .   .   .   .   12   VAL   C      .   50428   1    
     92    .   1   .   1   12   12   VAL   CA     C   13   66.591    0.3     .   1   .   .   .   .   .   12   VAL   CA     .   50428   1    
     93    .   1   .   1   12   12   VAL   CB     C   13   31.123    0.3     .   1   .   .   .   .   .   12   VAL   CB     .   50428   1    
     94    .   1   .   1   12   12   VAL   CG1    C   13   21.793    0.3     .   1   .   .   .   .   .   12   VAL   CG1    .   50428   1    
     95    .   1   .   1   12   12   VAL   CG2    C   13   24.355    0.3     .   1   .   .   .   .   .   12   VAL   CG2    .   50428   1    
     96    .   1   .   1   12   12   VAL   N      N   15   120.130   0.3     .   1   .   .   .   .   .   12   VAL   N      .   50428   1    
     97    .   1   .   1   13   13   ASP   HA     H   1    3.943     0.100   .   1   .   .   .   .   .   13   ASP   HA     .   50428   1    
     98    .   1   .   1   13   13   ASP   HB2    H   1    2.302     0.100   .   1   .   .   .   .   .   13   ASP   HB2    .   50428   1    
     99    .   1   .   1   13   13   ASP   HB3    H   1    2.302     0.100   .   1   .   .   .   .   .   13   ASP   HB3    .   50428   1    
     100   .   1   .   1   13   13   ASP   C      C   13   178.980   0.3     .   1   .   .   .   .   .   13   ASP   C      .   50428   1    
     101   .   1   .   1   13   13   ASP   CA     C   13   57.591    0.3     .   1   .   .   .   .   .   13   ASP   CA     .   50428   1    
     102   .   1   .   1   13   13   ASP   CB     C   13   39.578    0.3     .   1   .   .   .   .   .   13   ASP   CB     .   50428   1    
     103   .   1   .   1   13   13   ASP   N      N   15   119.676   0.3     .   1   .   .   .   .   .   13   ASP   N      .   50428   1    
     104   .   1   .   1   14   14   ASP   HA     H   1    3.891     0.100   .   1   .   .   .   .   .   14   ASP   HA     .   50428   1    
     105   .   1   .   1   14   14   ASP   HB2    H   1    2.239     0.100   .   1   .   .   .   .   .   14   ASP   HB2    .   50428   1    
     106   .   1   .   1   14   14   ASP   HB3    H   1    2.239     0.100   .   1   .   .   .   .   .   14   ASP   HB3    .   50428   1    
     107   .   1   .   1   14   14   ASP   C      C   13   178.196   0.3     .   1   .   .   .   .   .   14   ASP   C      .   50428   1    
     108   .   1   .   1   14   14   ASP   CA     C   13   56.658    0.3     .   1   .   .   .   .   .   14   ASP   CA     .   50428   1    
     109   .   1   .   1   14   14   ASP   CB     C   13   39.535    0.3     .   1   .   .   .   .   .   14   ASP   CB     .   50428   1    
     110   .   1   .   1   14   14   ASP   N      N   15   120.060   0.3     .   1   .   .   .   .   .   14   ASP   N      .   50428   1    
     111   .   1   .   1   15   15   GLY   H      H   1    8.402     0.100   .   1   .   .   .   .   .   15   GLY   H      .   50428   1    
     112   .   1   .   1   15   15   GLY   HA2    H   1    2.983     0.100   .   2   .   .   .   .   .   15   GLY   HA2    .   50428   1    
     113   .   1   .   1   15   15   GLY   HA3    H   1    3.312     0.100   .   2   .   .   .   .   .   15   GLY   HA3    .   50428   1    
     114   .   1   .   1   15   15   GLY   C      C   13   177.158   0.3     .   1   .   .   .   .   .   15   GLY   C      .   50428   1    
     115   .   1   .   1   15   15   GLY   CA     C   13   46.829    0.3     .   1   .   .   .   .   .   15   GLY   CA     .   50428   1    
     116   .   1   .   1   15   15   GLY   N      N   15   108.469   0.3     .   1   .   .   .   .   .   15   GLY   N      .   50428   1    
     117   .   1   .   1   16   16   PHE   HA     H   1    4.294     0.100   .   1   .   .   .   .   .   16   PHE   HA     .   50428   1    
     118   .   1   .   1   16   16   PHE   HB2    H   1    2.873     0.100   .   2   .   .   .   .   .   16   PHE   HB2    .   50428   1    
     119   .   1   .   1   16   16   PHE   HB3    H   1    3.130     0.100   .   2   .   .   .   .   .   16   PHE   HB3    .   50428   1    
     120   .   1   .   1   16   16   PHE   C      C   13   177.977   0.3     .   1   .   .   .   .   .   16   PHE   C      .   50428   1    
     121   .   1   .   1   16   16   PHE   CA     C   13   57.765    0.3     .   1   .   .   .   .   .   16   PHE   CA     .   50428   1    
     122   .   1   .   1   16   16   PHE   CB     C   13   36.156    0.3     .   1   .   .   .   .   .   16   PHE   CB     .   50428   1    
     123   .   1   .   1   16   16   PHE   CG     C   13   140.147   0.3     .   1   .   .   .   .   .   16   PHE   CG     .   50428   1    
     124   .   1   .   1   16   16   PHE   CD1    C   13   130.195   0.3     .   1   .   .   .   .   .   16   PHE   CD1    .   50428   1    
     125   .   1   .   1   16   16   PHE   CE1    C   13   128.454   0.3     .   1   .   .   .   .   .   16   PHE   CE1    .   50428   1    
     126   .   1   .   1   16   16   PHE   CZ     C   13   128.745   0.3     .   1   .   .   .   .   .   16   PHE   CZ     .   50428   1    
     127   .   1   .   1   16   16   PHE   N      N   15   121.142   0.3     .   1   .   .   .   .   .   16   PHE   N      .   50428   1    
     128   .   1   .   1   17   17   LEU   HA     H   1    3.912     0.100   .   1   .   .   .   .   .   17   LEU   HA     .   50428   1    
     129   .   1   .   1   17   17   LEU   HB2    H   1    1.297     0.100   .   2   .   .   .   .   .   17   LEU   HB2    .   50428   1    
     130   .   1   .   1   17   17   LEU   HB3    H   1    1.576     0.100   .   2   .   .   .   .   .   17   LEU   HB3    .   50428   1    
     131   .   1   .   1   17   17   LEU   HG     H   1    1.218     0.100   .   1   .   .   .   .   .   17   LEU   HG     .   50428   1    
     132   .   1   .   1   17   17   LEU   HD11   H   1    0.382     0.100   .   1   .   .   .   .   .   17   LEU   HD1    .   50428   1    
     133   .   1   .   1   17   17   LEU   HD12   H   1    0.382     0.100   .   1   .   .   .   .   .   17   LEU   HD1    .   50428   1    
     134   .   1   .   1   17   17   LEU   HD13   H   1    0.382     0.100   .   1   .   .   .   .   .   17   LEU   HD1    .   50428   1    
     135   .   1   .   1   17   17   LEU   HD21   H   1    0.289     0.100   .   1   .   .   .   .   .   17   LEU   HD2    .   50428   1    
     136   .   1   .   1   17   17   LEU   HD22   H   1    0.289     0.100   .   1   .   .   .   .   .   17   LEU   HD2    .   50428   1    
     137   .   1   .   1   17   17   LEU   HD23   H   1    0.289     0.100   .   1   .   .   .   .   .   17   LEU   HD2    .   50428   1    
     138   .   1   .   1   17   17   LEU   C      C   13   180.251   0.3     .   1   .   .   .   .   .   17   LEU   C      .   50428   1    
     139   .   1   .   1   17   17   LEU   CA     C   13   58.231    0.3     .   1   .   .   .   .   .   17   LEU   CA     .   50428   1    
     140   .   1   .   1   17   17   LEU   CB     C   13   40.597    0.3     .   1   .   .   .   .   .   17   LEU   CB     .   50428   1    
     141   .   1   .   1   17   17   LEU   CG     C   13   26.844    0.3     .   1   .   .   .   .   .   17   LEU   CG     .   50428   1    
     142   .   1   .   1   17   17   LEU   CD1    C   13   22.765    0.3     .   1   .   .   .   .   .   17   LEU   CD1    .   50428   1    
     143   .   1   .   1   17   17   LEU   CD2    C   13   25.252    0.3     .   1   .   .   .   .   .   17   LEU   CD2    .   50428   1    
     144   .   1   .   1   17   17   LEU   N      N   15   120.828   0.3     .   1   .   .   .   .   .   17   LEU   N      .   50428   1    
     145   .   1   .   1   18   18   ASP   H      H   1    8.714     0.100   .   1   .   .   .   .   .   18   ASP   H      .   50428   1    
     146   .   1   .   1   18   18   ASP   HA     H   1    3.985     0.100   .   1   .   .   .   .   .   18   ASP   HA     .   50428   1    
     147   .   1   .   1   18   18   ASP   HB2    H   1    2.200     0.100   .   1   .   .   .   .   .   18   ASP   HB2    .   50428   1    
     148   .   1   .   1   18   18   ASP   HB3    H   1    2.200     0.100   .   1   .   .   .   .   .   18   ASP   HB3    .   50428   1    
     149   .   1   .   1   18   18   ASP   C      C   13   179.471   0.3     .   1   .   .   .   .   .   18   ASP   C      .   50428   1    
     150   .   1   .   1   18   18   ASP   CA     C   13   57.397    0.3     .   1   .   .   .   .   .   18   ASP   CA     .   50428   1    
     151   .   1   .   1   18   18   ASP   CB     C   13   40.162    0.3     .   1   .   .   .   .   .   18   ASP   CB     .   50428   1    
     152   .   1   .   1   18   18   ASP   N      N   15   121.631   0.3     .   1   .   .   .   .   .   18   ASP   N      .   50428   1    
     153   .   1   .   1   19   19   ILE   H      H   1    8.166     0.100   .   1   .   .   .   .   .   19   ILE   H      .   50428   1    
     154   .   1   .   1   19   19   ILE   HA     H   1    2.919     0.100   .   1   .   .   .   .   .   19   ILE   HA     .   50428   1    
     155   .   1   .   1   19   19   ILE   HB     H   1    1.118     0.100   .   1   .   .   .   .   .   19   ILE   HB     .   50428   1    
     156   .   1   .   1   19   19   ILE   HG12   H   1    -0.572    0.100   .   2   .   .   .   .   .   19   ILE   HG12   .   50428   1    
     157   .   1   .   1   19   19   ILE   HG13   H   1    1.204     0.100   .   2   .   .   .   .   .   19   ILE   HG13   .   50428   1    
     158   .   1   .   1   19   19   ILE   HG21   H   1    -0.534    0.100   .   1   .   .   .   .   .   19   ILE   HG2    .   50428   1    
     159   .   1   .   1   19   19   ILE   HG22   H   1    -0.534    0.100   .   1   .   .   .   .   .   19   ILE   HG2    .   50428   1    
     160   .   1   .   1   19   19   ILE   HG23   H   1    -0.534    0.100   .   1   .   .   .   .   .   19   ILE   HG2    .   50428   1    
     161   .   1   .   1   19   19   ILE   HD11   H   1    0.077     0.100   .   1   .   .   .   .   .   19   ILE   HD1    .   50428   1    
     162   .   1   .   1   19   19   ILE   HD12   H   1    0.077     0.100   .   1   .   .   .   .   .   19   ILE   HD1    .   50428   1    
     163   .   1   .   1   19   19   ILE   HD13   H   1    0.077     0.100   .   1   .   .   .   .   .   19   ILE   HD1    .   50428   1    
     164   .   1   .   1   19   19   ILE   C      C   13   177.294   0.3     .   1   .   .   .   .   .   19   ILE   C      .   50428   1    
     165   .   1   .   1   19   19   ILE   CA     C   13   64.675    0.3     .   1   .   .   .   .   .   19   ILE   CA     .   50428   1    
     166   .   1   .   1   19   19   ILE   CB     C   13   37.801    0.3     .   1   .   .   .   .   .   19   ILE   CB     .   50428   1    
     167   .   1   .   1   19   19   ILE   CG1    C   13   30.686    0.3     .   1   .   .   .   .   .   19   ILE   CG1    .   50428   1    
     168   .   1   .   1   19   19   ILE   CG2    C   13   16.541    0.3     .   1   .   .   .   .   .   19   ILE   CG2    .   50428   1    
     169   .   1   .   1   19   19   ILE   CD1    C   13   15.266    0.3     .   1   .   .   .   .   .   19   ILE   CD1    .   50428   1    
     170   .   1   .   1   19   19   ILE   N      N   15   121.914   0.3     .   1   .   .   .   .   .   19   ILE   N      .   50428   1    
     171   .   1   .   1   20   20   TRP   H      H   1    8.961     0.100   .   1   .   .   .   .   .   20   TRP   H      .   50428   1    
     172   .   1   .   1   20   20   TRP   HA     H   1    3.693     0.100   .   1   .   .   .   .   .   20   TRP   HA     .   50428   1    
     173   .   1   .   1   20   20   TRP   HB2    H   1    2.466     0.100   .   2   .   .   .   .   .   20   TRP   HB2    .   50428   1    
     174   .   1   .   1   20   20   TRP   HB3    H   1    2.694     0.100   .   2   .   .   .   .   .   20   TRP   HB3    .   50428   1    
     175   .   1   .   1   20   20   TRP   C      C   13   177.871   0.3     .   1   .   .   .   .   .   20   TRP   C      .   50428   1    
     176   .   1   .   1   20   20   TRP   CA     C   13   61.454    0.3     .   1   .   .   .   .   .   20   TRP   CA     .   50428   1    
     177   .   1   .   1   20   20   TRP   CB     C   13   28.023    0.3     .   1   .   .   .   .   .   20   TRP   CB     .   50428   1    
     178   .   1   .   1   20   20   TRP   CG     C   13   111.413   0.3     .   1   .   .   .   .   .   20   TRP   CG     .   50428   1    
     179   .   1   .   1   20   20   TRP   CD1    C   13   128.622   0.3     .   1   .   .   .   .   .   20   TRP   CD1    .   50428   1    
     180   .   1   .   1   20   20   TRP   CD2    C   13   128.224   0.3     .   1   .   .   .   .   .   20   TRP   CD2    .   50428   1    
     181   .   1   .   1   20   20   TRP   CE2    C   13   138.757   0.3     .   1   .   .   .   .   .   20   TRP   CE2    .   50428   1    
     182   .   1   .   1   20   20   TRP   CE3    C   13   117.673   0.3     .   1   .   .   .   .   .   20   TRP   CE3    .   50428   1    
     183   .   1   .   1   20   20   TRP   CZ2    C   13   114.860   0.3     .   1   .   .   .   .   .   20   TRP   CZ2    .   50428   1    
     184   .   1   .   1   20   20   TRP   CZ3    C   13   120.580   0.3     .   1   .   .   .   .   .   20   TRP   CZ3    .   50428   1    
     185   .   1   .   1   20   20   TRP   CH2    C   13   123.486   0.3     .   1   .   .   .   .   .   20   TRP   CH2    .   50428   1    
     186   .   1   .   1   20   20   TRP   N      N   15   120.374   0.3     .   1   .   .   .   .   .   20   TRP   N      .   50428   1    
     187   .   1   .   1   20   20   TRP   NE1    N   15   130.400   0.3     .   1   .   .   .   .   .   20   TRP   NE1    .   50428   1    
     188   .   1   .   1   21   21   THR   H      H   1    8.940     0.100   .   1   .   .   .   .   .   21   THR   H      .   50428   1    
     189   .   1   .   1   21   21   THR   HA     H   1    3.384     0.100   .   1   .   .   .   .   .   21   THR   HA     .   50428   1    
     190   .   1   .   1   21   21   THR   HB     H   1    3.936     0.100   .   1   .   .   .   .   .   21   THR   HB     .   50428   1    
     191   .   1   .   1   21   21   THR   HG21   H   1    0.753     0.100   .   1   .   .   .   .   .   21   THR   HG2    .   50428   1    
     192   .   1   .   1   21   21   THR   HG22   H   1    0.753     0.100   .   1   .   .   .   .   .   21   THR   HG2    .   50428   1    
     193   .   1   .   1   21   21   THR   HG23   H   1    0.753     0.100   .   1   .   .   .   .   .   21   THR   HG2    .   50428   1    
     194   .   1   .   1   21   21   THR   C      C   13   175.367   0.3     .   1   .   .   .   .   .   21   THR   C      .   50428   1    
     195   .   1   .   1   21   21   THR   CA     C   13   67.172    0.3     .   1   .   .   .   .   .   21   THR   CA     .   50428   1    
     196   .   1   .   1   21   21   THR   CB     C   13   68.249    0.3     .   1   .   .   .   .   .   21   THR   CB     .   50428   1    
     197   .   1   .   1   21   21   THR   CG2    C   13   20.676    0.3     .   1   .   .   .   .   .   21   THR   CG2    .   50428   1    
     198   .   1   .   1   21   21   THR   N      N   15   116.746   0.3     .   1   .   .   .   .   .   21   THR   N      .   50428   1    
     199   .   1   .   1   22   22   TYR   H      H   1    7.833     0.100   .   1   .   .   .   .   .   22   TYR   H      .   50428   1    
     200   .   1   .   1   22   22   TYR   HA     H   1    3.517     0.100   .   1   .   .   .   .   .   22   TYR   HA     .   50428   1    
     201   .   1   .   1   22   22   TYR   HB2    H   1    2.412     0.100   .   1   .   .   .   .   .   22   TYR   HB2    .   50428   1    
     202   .   1   .   1   22   22   TYR   C      C   13   176.002   0.3     .   1   .   .   .   .   .   22   TYR   C      .   50428   1    
     203   .   1   .   1   22   22   TYR   CA     C   13   61.724    0.3     .   1   .   .   .   .   .   22   TYR   CA     .   50428   1    
     204   .   1   .   1   22   22   TYR   CB     C   13   38.262    0.3     .   1   .   .   .   .   .   22   TYR   CB     .   50428   1    
     205   .   1   .   1   22   22   TYR   CG     C   13   127.230   0.3     .   1   .   .   .   .   .   22   TYR   CG     .   50428   1    
     206   .   1   .   1   22   22   TYR   CD1    C   13   132.385   0.3     .   1   .   .   .   .   .   22   TYR   CD1    .   50428   1    
     207   .   1   .   1   22   22   TYR   CE1    C   13   117.513   0.3     .   1   .   .   .   .   .   22   TYR   CE1    .   50428   1    
     208   .   1   .   1   22   22   TYR   CZ     C   13   158.669   0.3     .   1   .   .   .   .   .   22   TYR   CZ     .   50428   1    
     209   .   1   .   1   22   22   TYR   N      N   15   122.687   0.3     .   1   .   .   .   .   .   22   TYR   N      .   50428   1    
     210   .   1   .   1   23   23   ASN   HA     H   1    3.669     0.100   .   1   .   .   .   .   .   23   ASN   HA     .   50428   1    
     211   .   1   .   1   23   23   ASN   HB2    H   1    1.795     0.100   .   2   .   .   .   .   .   23   ASN   HB2    .   50428   1    
     212   .   1   .   1   23   23   ASN   HB3    H   1    2.239     0.100   .   2   .   .   .   .   .   23   ASN   HB3    .   50428   1    
     213   .   1   .   1   23   23   ASN   C      C   13   177.759   0.3     .   1   .   .   .   .   .   23   ASN   C      .   50428   1    
     214   .   1   .   1   23   23   ASN   CA     C   13   55.208    0.3     .   1   .   .   .   .   .   23   ASN   CA     .   50428   1    
     215   .   1   .   1   23   23   ASN   CB     C   13   36.589    0.3     .   1   .   .   .   .   .   23   ASN   CB     .   50428   1    
     216   .   1   .   1   23   23   ASN   N      N   15   116.091   0.3     .   1   .   .   .   .   .   23   ASN   N      .   50428   1    
     217   .   1   .   1   24   24   ALA   H      H   1    8.569     0.100   .   1   .   .   .   .   .   24   ALA   H      .   50428   1    
     218   .   1   .   1   24   24   ALA   HA     H   1    3.430     0.100   .   1   .   .   .   .   .   24   ALA   HA     .   50428   1    
     219   .   1   .   1   24   24   ALA   HB1    H   1    1.066     0.100   .   1   .   .   .   .   .   24   ALA   HB     .   50428   1    
     220   .   1   .   1   24   24   ALA   HB2    H   1    1.066     0.100   .   1   .   .   .   .   .   24   ALA   HB     .   50428   1    
     221   .   1   .   1   24   24   ALA   HB3    H   1    1.066     0.100   .   1   .   .   .   .   .   24   ALA   HB     .   50428   1    
     222   .   1   .   1   24   24   ALA   C      C   13   178.372   0.3     .   1   .   .   .   .   .   24   ALA   C      .   50428   1    
     223   .   1   .   1   24   24   ALA   CA     C   13   55.183    0.3     .   1   .   .   .   .   .   24   ALA   CA     .   50428   1    
     224   .   1   .   1   24   24   ALA   CB     C   13   18.175    0.3     .   1   .   .   .   .   .   24   ALA   CB     .   50428   1    
     225   .   1   .   1   24   24   ALA   N      N   15   122.923   0.3     .   1   .   .   .   .   .   24   ALA   N      .   50428   1    
     226   .   1   .   1   25   25   GLU   HA     H   1    3.593     0.100   .   1   .   .   .   .   .   25   GLU   HA     .   50428   1    
     227   .   1   .   1   25   25   GLU   HB2    H   1    1.616     0.100   .   1   .   .   .   .   .   25   GLU   HB2    .   50428   1    
     228   .   1   .   1   25   25   GLU   HB3    H   1    1.616     0.100   .   1   .   .   .   .   .   25   GLU   HB3    .   50428   1    
     229   .   1   .   1   25   25   GLU   HG2    H   1    1.855     0.100   .   1   .   .   .   .   .   25   GLU   HG2    .   50428   1    
     230   .   1   .   1   25   25   GLU   HG3    H   1    1.855     0.100   .   1   .   .   .   .   .   25   GLU   HG3    .   50428   1    
     231   .   1   .   1   25   25   GLU   C      C   13   179.169   0.3     .   1   .   .   .   .   .   25   GLU   C      .   50428   1    
     232   .   1   .   1   25   25   GLU   CA     C   13   58.770    0.3     .   1   .   .   .   .   .   25   GLU   CA     .   50428   1    
     233   .   1   .   1   25   25   GLU   CB     C   13   28.987    0.3     .   1   .   .   .   .   .   25   GLU   CB     .   50428   1    
     234   .   1   .   1   25   25   GLU   CG     C   13   36.129    0.3     .   1   .   .   .   .   .   25   GLU   CG     .   50428   1    
     235   .   1   .   1   25   25   GLU   CD     C   13   183.024   0.3     .   1   .   .   .   .   .   25   GLU   CD     .   50428   1    
     236   .   1   .   1   25   25   GLU   N      N   15   117.861   0.3     .   1   .   .   .   .   .   25   GLU   N      .   50428   1    
     237   .   1   .   1   26   26   LEU   C      C   13   177.563   0.3     .   1   .   .   .   .   .   26   LEU   C      .   50428   1    
     238   .   1   .   1   26   26   LEU   CA     C   13   57.311    0.3     .   1   .   .   .   .   .   26   LEU   CA     .   50428   1    
     239   .   1   .   1   26   26   LEU   CB     C   13   41.062    0.3     .   1   .   .   .   .   .   26   LEU   CB     .   50428   1    
     240   .   1   .   1   26   26   LEU   CG     C   13   26.900    0.3     .   1   .   .   .   .   .   26   LEU   CG     .   50428   1    
     241   .   1   .   1   26   26   LEU   CD1    C   13   21.903    0.3     .   1   .   .   .   .   .   26   LEU   CD1    .   50428   1    
     242   .   1   .   1   26   26   LEU   CD2    C   13   23.324    0.3     .   1   .   .   .   .   .   26   LEU   CD2    .   50428   1    
     243   .   1   .   1   26   26   LEU   N      N   15   118.140   0.3     .   1   .   .   .   .   .   26   LEU   N      .   50428   1    
     244   .   1   .   1   27   27   LEU   HB2    H   1    1.032     0.100   .   1   .   .   .   .   .   27   LEU   HB2    .   50428   1    
     245   .   1   .   1   27   27   LEU   HB3    H   1    1.032     0.100   .   1   .   .   .   .   .   27   LEU   HB3    .   50428   1    
     246   .   1   .   1   27   27   LEU   C      C   13   178.264   0.3     .   1   .   .   .   .   .   27   LEU   C      .   50428   1    
     247   .   1   .   1   27   27   LEU   CA     C   13   58.126    0.3     .   1   .   .   .   .   .   27   LEU   CA     .   50428   1    
     248   .   1   .   1   27   27   LEU   CB     C   13   41.415    0.3     .   1   .   .   .   .   .   27   LEU   CB     .   50428   1    
     249   .   1   .   1   27   27   LEU   CG     C   13   26.200    0.3     .   1   .   .   .   .   .   27   LEU   CG     .   50428   1    
     250   .   1   .   1   27   27   LEU   CD1    C   13   23.040    0.3     .   1   .   .   .   .   .   27   LEU   CD1    .   50428   1    
     251   .   1   .   1   27   27   LEU   CD2    C   13   25.037    0.3     .   1   .   .   .   .   .   27   LEU   CD2    .   50428   1    
     252   .   1   .   1   27   27   LEU   N      N   15   120.828   0.3     .   1   .   .   .   .   .   27   LEU   N      .   50428   1    
     253   .   1   .   1   28   28   VAL   H      H   1    8.193     0.100   .   1   .   .   .   .   .   28   VAL   H      .   50428   1    
     254   .   1   .   1   28   28   VAL   C      C   13   178.226   0.3     .   1   .   .   .   .   .   28   VAL   C      .   50428   1    
     255   .   1   .   1   28   28   VAL   CA     C   13   65.618    0.3     .   1   .   .   .   .   .   28   VAL   CA     .   50428   1    
     256   .   1   .   1   28   28   VAL   CB     C   13   31.238    0.3     .   1   .   .   .   .   .   28   VAL   CB     .   50428   1    
     257   .   1   .   1   28   28   VAL   CG1    C   13   21.024    0.3     .   1   .   .   .   .   .   28   VAL   CG1    .   50428   1    
     258   .   1   .   1   28   28   VAL   CG2    C   13   22.874    0.3     .   1   .   .   .   .   .   28   VAL   CG2    .   50428   1    
     259   .   1   .   1   28   28   VAL   N      N   15   115.615   0.3     .   1   .   .   .   .   .   28   VAL   N      .   50428   1    
     260   .   1   .   1   29   29   LEU   CA     C   13   58.020    0.3     .   1   .   .   .   .   .   29   LEU   CA     .   50428   1    
     261   .   1   .   1   29   29   LEU   CB     C   13   41.000    0.3     .   1   .   .   .   .   .   29   LEU   CB     .   50428   1    
     262   .   1   .   1   31   31   GLU   CB     C   13   29.370    0.3     .   1   .   .   .   .   .   31   GLU   CB     .   50428   1    
     263   .   1   .   1   31   31   GLU   CG     C   13   36.370    0.3     .   1   .   .   .   .   .   31   GLU   CG     .   50428   1    
     264   .   1   .   1   32   32   ASN   C      C   13   177.673   0.3     .   1   .   .   .   .   .   32   ASN   C      .   50428   1    
     265   .   1   .   1   32   32   ASN   CA     C   13   55.801    0.3     .   1   .   .   .   .   .   32   ASN   CA     .   50428   1    
     266   .   1   .   1   32   32   ASN   CB     C   13   38.107    0.3     .   1   .   .   .   .   .   32   ASN   CB     .   50428   1    
     267   .   1   .   1   32   32   ASN   CG     C   13   175.544   0.3     .   1   .   .   .   .   .   32   ASN   CG     .   50428   1    
     268   .   1   .   1   32   32   ASN   N      N   15   120.584   0.3     .   1   .   .   .   .   .   32   ASN   N      .   50428   1    
     269   .   1   .   1   32   32   ASN   ND2    N   15   112.542   0.3     .   1   .   .   .   .   .   32   ASN   ND2    .   50428   1    
     270   .   1   .   1   33   33   GLU   HA     H   1    3.839     0.100   .   1   .   .   .   .   .   33   GLU   HA     .   50428   1    
     271   .   1   .   1   33   33   GLU   C      C   13   176.472   0.3     .   1   .   .   .   .   .   33   GLU   C      .   50428   1    
     272   .   1   .   1   33   33   GLU   CA     C   13   56.176    0.3     .   1   .   .   .   .   .   33   GLU   CA     .   50428   1    
     273   .   1   .   1   33   33   GLU   CB     C   13   29.697    0.3     .   1   .   .   .   .   .   33   GLU   CB     .   50428   1    
     274   .   1   .   1   33   33   GLU   CG     C   13   34.869    0.3     .   1   .   .   .   .   .   33   GLU   CG     .   50428   1    
     275   .   1   .   1   33   33   GLU   CD     C   13   183.740   0.3     .   1   .   .   .   .   .   33   GLU   CD     .   50428   1    
     276   .   1   .   1   33   33   GLU   N      N   15   115.661   0.3     .   1   .   .   .   .   .   33   GLU   N      .   50428   1    
     277   .   1   .   1   34   34   ARG   H      H   1    7.926     0.100   .   1   .   .   .   .   .   34   ARG   H      .   50428   1    
     278   .   1   .   1   34   34   ARG   HA     H   1    3.728     0.100   .   1   .   .   .   .   .   34   ARG   HA     .   50428   1    
     279   .   1   .   1   34   34   ARG   HB2    H   1    1.125     0.100   .   1   .   .   .   .   .   34   ARG   HB2    .   50428   1    
     280   .   1   .   1   34   34   ARG   HB3    H   1    1.125     0.100   .   1   .   .   .   .   .   34   ARG   HB3    .   50428   1    
     281   .   1   .   1   34   34   ARG   C      C   13   174.954   0.3     .   1   .   .   .   .   .   34   ARG   C      .   50428   1    
     282   .   1   .   1   34   34   ARG   CA     C   13   56.523    0.3     .   1   .   .   .   .   .   34   ARG   CA     .   50428   1    
     283   .   1   .   1   34   34   ARG   CB     C   13   27.120    0.3     .   1   .   .   .   .   .   34   ARG   CB     .   50428   1    
     284   .   1   .   1   34   34   ARG   CG     C   13   25.527    0.3     .   1   .   .   .   .   .   34   ARG   CG     .   50428   1    
     285   .   1   .   1   34   34   ARG   CD     C   13   42.189    0.3     .   1   .   .   .   .   .   34   ARG   CD     .   50428   1    
     286   .   1   .   1   34   34   ARG   CZ     C   13   158.966   0.3     .   1   .   .   .   .   .   34   ARG   CZ     .   50428   1    
     287   .   1   .   1   34   34   ARG   N      N   15   111.866   0.3     .   1   .   .   .   .   .   34   ARG   N      .   50428   1    
     288   .   1   .   1   35   35   THR   HA     H   1    3.210     0.100   .   1   .   .   .   .   .   35   THR   HA     .   50428   1    
     289   .   1   .   1   35   35   THR   HB     H   1    3.204     0.100   .   1   .   .   .   .   .   35   THR   HB     .   50428   1    
     290   .   1   .   1   35   35   THR   HG21   H   1    0.674     0.100   .   1   .   .   .   .   .   35   THR   HG2    .   50428   1    
     291   .   1   .   1   35   35   THR   HG22   H   1    0.674     0.100   .   1   .   .   .   .   .   35   THR   HG2    .   50428   1    
     292   .   1   .   1   35   35   THR   HG23   H   1    0.674     0.100   .   1   .   .   .   .   .   35   THR   HG2    .   50428   1    
     293   .   1   .   1   35   35   THR   C      C   13   176.098   0.3     .   1   .   .   .   .   .   35   THR   C      .   50428   1    
     294   .   1   .   1   35   35   THR   CA     C   13   65.703    0.3     .   1   .   .   .   .   .   35   THR   CA     .   50428   1    
     295   .   1   .   1   35   35   THR   CB     C   13   69.033    0.3     .   1   .   .   .   .   .   35   THR   CB     .   50428   1    
     296   .   1   .   1   35   35   THR   CG2    C   13   23.833    0.3     .   1   .   .   .   .   .   35   THR   CG2    .   50428   1    
     297   .   1   .   1   35   35   THR   N      N   15   119.045   0.3     .   1   .   .   .   .   .   35   THR   N      .   50428   1    
     298   .   1   .   1   36   36   LEU   HA     H   1    4.091     0.100   .   1   .   .   .   .   .   36   LEU   HA     .   50428   1    
     299   .   1   .   1   36   36   LEU   HB2    H   1    0.920     0.100   .   1   .   .   .   .   .   36   LEU   HB2    .   50428   1    
     300   .   1   .   1   36   36   LEU   HB3    H   1    0.920     0.100   .   1   .   .   .   .   .   36   LEU   HB3    .   50428   1    
     301   .   1   .   1   36   36   LEU   C      C   13   174.806   0.3     .   1   .   .   .   .   .   36   LEU   C      .   50428   1    
     302   .   1   .   1   36   36   LEU   CA     C   13   51.125    0.3     .   1   .   .   .   .   .   36   LEU   CA     .   50428   1    
     303   .   1   .   1   36   36   LEU   CB     C   13   43.906    0.3     .   1   .   .   .   .   .   36   LEU   CB     .   50428   1    
     304   .   1   .   1   36   36   LEU   CG     C   13   26.943    0.3     .   1   .   .   .   .   .   36   LEU   CG     .   50428   1    
     305   .   1   .   1   36   36   LEU   CD1    C   13   22.431    0.3     .   1   .   .   .   .   .   36   LEU   CD1    .   50428   1    
     306   .   1   .   1   36   36   LEU   CD2    C   13   25.654    0.3     .   1   .   .   .   .   .   36   LEU   CD2    .   50428   1    
     307   .   1   .   1   36   36   LEU   N      N   15   112.868   0.3     .   1   .   .   .   .   .   36   LEU   N      .   50428   1    
     308   .   1   .   1   37   37   ASP   HA     H   1    4.133     0.100   .   1   .   .   .   .   .   37   ASP   HA     .   50428   1    
     309   .   1   .   1   37   37   ASP   HB2    H   1    1.748     0.100   .   2   .   .   .   .   .   37   ASP   HB2    .   50428   1    
     310   .   1   .   1   37   37   ASP   HB3    H   1    2.624     0.100   .   2   .   .   .   .   .   37   ASP   HB3    .   50428   1    
     311   .   1   .   1   37   37   ASP   C      C   13   175.896   0.3     .   1   .   .   .   .   .   37   ASP   C      .   50428   1    
     312   .   1   .   1   37   37   ASP   CA     C   13   52.194    0.3     .   1   .   .   .   .   .   37   ASP   CA     .   50428   1    
     313   .   1   .   1   37   37   ASP   CB     C   13   41.312    0.3     .   1   .   .   .   .   .   37   ASP   CB     .   50428   1    
     314   .   1   .   1   37   37   ASP   CG     C   13   179.282   0.3     .   1   .   .   .   .   .   37   ASP   CG     .   50428   1    
     315   .   1   .   1   37   37   ASP   N      N   15   121.422   0.3     .   1   .   .   .   .   .   37   ASP   N      .   50428   1    
     316   .   1   .   1   38   38   TYR   HA     H   1    3.712     0.100   .   1   .   .   .   .   .   38   TYR   HA     .   50428   1    
     317   .   1   .   1   38   38   TYR   CA     C   13   59.471    0.3     .   1   .   .   .   .   .   38   TYR   CA     .   50428   1    
     318   .   1   .   1   38   38   TYR   CB     C   13   37.801    0.3     .   1   .   .   .   .   .   38   TYR   CB     .   50428   1    
     319   .   1   .   1   38   38   TYR   CG     C   13   129.879   0.3     .   1   .   .   .   .   .   38   TYR   CG     .   50428   1    
     320   .   1   .   1   38   38   TYR   CD1    C   13   132.439   0.3     .   1   .   .   .   .   .   38   TYR   CD1    .   50428   1    
     321   .   1   .   1   38   38   TYR   CE1    C   13   117.824   0.3     .   1   .   .   .   .   .   38   TYR   CE1    .   50428   1    
     322   .   1   .   1   38   38   TYR   N      N   15   126.030   0.3     .   1   .   .   .   .   .   38   TYR   N      .   50428   1    
     323   .   1   .   1   39   39   HIS   CA     C   13   56.304    0.3     .   1   .   .   .   .   .   39   HIS   CA     .   50428   1    
     324   .   1   .   1   39   39   HIS   CB     C   13   28.537    0.3     .   1   .   .   .   .   .   39   HIS   CB     .   50428   1    
     325   .   1   .   1   39   39   HIS   CG     C   13   133.425   0.3     .   1   .   .   .   .   .   39   HIS   CG     .   50428   1    
     326   .   1   .   1   39   39   HIS   CD2    C   13   119.596   0.3     .   1   .   .   .   .   .   39   HIS   CD2    .   50428   1    
     327   .   1   .   1   39   39   HIS   CE1    C   13   136.954   0.3     .   1   .   .   .   .   .   39   HIS   CE1    .   50428   1    
     328   .   1   .   1   40   40   ASP   HA     H   1    4.101     0.100   .   1   .   .   .   .   .   40   ASP   HA     .   50428   1    
     329   .   1   .   1   40   40   ASP   HB2    H   1    2.200     0.100   .   1   .   .   .   .   .   40   ASP   HB2    .   50428   1    
     330   .   1   .   1   40   40   ASP   HB3    H   1    2.200     0.100   .   1   .   .   .   .   .   40   ASP   HB3    .   50428   1    
     331   .   1   .   1   40   40   ASP   C      C   13   177.586   0.3     .   1   .   .   .   .   .   40   ASP   C      .   50428   1    
     332   .   1   .   1   40   40   ASP   CA     C   13   53.316    0.3     .   1   .   .   .   .   .   40   ASP   CA     .   50428   1    
     333   .   1   .   1   40   40   ASP   CB     C   13   42.053    0.3     .   1   .   .   .   .   .   40   ASP   CB     .   50428   1    
     334   .   1   .   1   40   40   ASP   CG     C   13   179.375   0.3     .   1   .   .   .   .   .   40   ASP   CG     .   50428   1    
     335   .   1   .   1   40   40   ASP   N      N   15   120.724   0.3     .   1   .   .   .   .   .   40   ASP   N      .   50428   1    
     336   .   1   .   1   41   41   SER   HA     H   1    3.457     0.100   .   1   .   .   .   .   .   41   SER   HA     .   50428   1    
     337   .   1   .   1   41   41   SER   C      C   13   176.011   0.3     .   1   .   .   .   .   .   41   SER   C      .   50428   1    
     338   .   1   .   1   41   41   SER   CA     C   13   61.872    0.3     .   1   .   .   .   .   .   41   SER   CA     .   50428   1    
     339   .   1   .   1   41   41   SER   CB     C   13   62.212    0.3     .   1   .   .   .   .   .   41   SER   CB     .   50428   1    
     340   .   1   .   1   41   41   SER   N      N   15   123.737   0.3     .   1   .   .   .   .   .   41   SER   N      .   50428   1    
     341   .   1   .   1   42   42   ASN   H      H   1    9.144     0.100   .   1   .   .   .   .   .   42   ASN   H      .   50428   1    
     342   .   1   .   1   42   42   ASN   HA     H   1    3.986     0.100   .   1   .   .   .   .   .   42   ASN   HA     .   50428   1    
     343   .   1   .   1   42   42   ASN   HB2    H   1    2.399     0.100   .   1   .   .   .   .   .   42   ASN   HB2    .   50428   1    
     344   .   1   .   1   42   42   ASN   HB3    H   1    2.399     0.100   .   1   .   .   .   .   .   42   ASN   HB3    .   50428   1    
     345   .   1   .   1   42   42   ASN   C      C   13   177.640   0.3     .   1   .   .   .   .   .   42   ASN   C      .   50428   1    
     346   .   1   .   1   42   42   ASN   CA     C   13   55.809    0.3     .   1   .   .   .   .   .   42   ASN   CA     .   50428   1    
     347   .   1   .   1   42   42   ASN   CB     C   13   38.136    0.3     .   1   .   .   .   .   .   42   ASN   CB     .   50428   1    
     348   .   1   .   1   42   42   ASN   CG     C   13   175.924   0.3     .   1   .   .   .   .   .   42   ASN   CG     .   50428   1    
     349   .   1   .   1   42   42   ASN   N      N   15   118.489   0.3     .   1   .   .   .   .   .   42   ASN   N      .   50428   1    
     350   .   1   .   1   43   43   VAL   H      H   1    7.725     0.100   .   1   .   .   .   .   .   43   VAL   H      .   50428   1    
     351   .   1   .   1   43   43   VAL   HA     H   1    3.137     0.100   .   1   .   .   .   .   .   43   VAL   HA     .   50428   1    
     352   .   1   .   1   43   43   VAL   HB     H   1    2.040     0.100   .   1   .   .   .   .   .   43   VAL   HB     .   50428   1    
     353   .   1   .   1   43   43   VAL   HG11   H   1    0.415     0.100   .   1   .   .   .   .   .   43   VAL   HG1    .   50428   1    
     354   .   1   .   1   43   43   VAL   HG12   H   1    0.415     0.100   .   1   .   .   .   .   .   43   VAL   HG1    .   50428   1    
     355   .   1   .   1   43   43   VAL   HG13   H   1    0.415     0.100   .   1   .   .   .   .   .   43   VAL   HG1    .   50428   1    
     356   .   1   .   1   43   43   VAL   HG21   H   1    0.647     0.100   .   1   .   .   .   .   .   43   VAL   HG2    .   50428   1    
     357   .   1   .   1   43   43   VAL   HG22   H   1    0.647     0.100   .   1   .   .   .   .   .   43   VAL   HG2    .   50428   1    
     358   .   1   .   1   43   43   VAL   HG23   H   1    0.647     0.100   .   1   .   .   .   .   .   43   VAL   HG2    .   50428   1    
     359   .   1   .   1   43   43   VAL   C      C   13   177.966   0.3     .   1   .   .   .   .   .   43   VAL   C      .   50428   1    
     360   .   1   .   1   43   43   VAL   CA     C   13   65.679    0.3     .   1   .   .   .   .   .   43   VAL   CA     .   50428   1    
     361   .   1   .   1   43   43   VAL   CB     C   13   31.098    0.3     .   1   .   .   .   .   .   43   VAL   CB     .   50428   1    
     362   .   1   .   1   43   43   VAL   CG1    C   13   21.536    0.3     .   1   .   .   .   .   .   43   VAL   CG1    .   50428   1    
     363   .   1   .   1   43   43   VAL   CG2    C   13   24.850    0.3     .   1   .   .   .   .   .   43   VAL   CG2    .   50428   1    
     364   .   1   .   1   43   43   VAL   N      N   15   122.923   0.3     .   1   .   .   .   .   .   43   VAL   N      .   50428   1    
     365   .   1   .   1   44   44   LYS   HA     H   1    3.432     0.100   .   1   .   .   .   .   .   44   LYS   HA     .   50428   1    
     366   .   1   .   1   44   44   LYS   C      C   13   179.007   0.3     .   1   .   .   .   .   .   44   LYS   C      .   50428   1    
     367   .   1   .   1   44   44   LYS   CA     C   13   59.490    0.3     .   1   .   .   .   .   .   44   LYS   CA     .   50428   1    
     368   .   1   .   1   44   44   LYS   CB     C   13   31.214    0.3     .   1   .   .   .   .   .   44   LYS   CB     .   50428   1    
     369   .   1   .   1   44   44   LYS   CG     C   13   24.462    0.3     .   1   .   .   .   .   .   44   LYS   CG     .   50428   1    
     370   .   1   .   1   44   44   LYS   CD     C   13   29.258    0.3     .   1   .   .   .   .   .   44   LYS   CD     .   50428   1    
     371   .   1   .   1   44   44   LYS   CE     C   13   41.365    0.3     .   1   .   .   .   .   .   44   LYS   CE     .   50428   1    
     372   .   1   .   1   44   44   LYS   N      N   15   120.326   0.3     .   1   .   .   .   .   .   44   LYS   N      .   50428   1    
     373   .   1   .   1   45   45   ASN   HA     H   1    3.959     0.100   .   1   .   .   .   .   .   45   ASN   HA     .   50428   1    
     374   .   1   .   1   45   45   ASN   C      C   13   175.432   0.3     .   1   .   .   .   .   .   45   ASN   C      .   50428   1    
     375   .   1   .   1   45   45   ASN   CA     C   13   55.806    0.3     .   1   .   .   .   .   .   45   ASN   CA     .   50428   1    
     376   .   1   .   1   45   45   ASN   CB     C   13   37.955    0.3     .   1   .   .   .   .   .   45   ASN   CB     .   50428   1    
     377   .   1   .   1   45   45   ASN   N      N   15   115.067   0.3     .   1   .   .   .   .   .   45   ASN   N      .   50428   1    
     378   .   1   .   1   47   47   TYR   C      C   13   178.505   0.3     .   1   .   .   .   .   .   47   TYR   C      .   50428   1    
     379   .   1   .   1   47   47   TYR   CA     C   13   61.896    0.3     .   1   .   .   .   .   .   47   TYR   CA     .   50428   1    
     380   .   1   .   1   47   47   TYR   CB     C   13   38.469    0.3     .   1   .   .   .   .   .   47   TYR   CB     .   50428   1    
     381   .   1   .   1   47   47   TYR   CG     C   13   127.287   0.3     .   1   .   .   .   .   .   47   TYR   CG     .   50428   1    
     382   .   1   .   1   47   47   TYR   CD1    C   13   132.387   0.3     .   1   .   .   .   .   .   47   TYR   CD1    .   50428   1    
     383   .   1   .   1   47   47   TYR   CE1    C   13   117.700   0.3     .   1   .   .   .   .   .   47   TYR   CE1    .   50428   1    
     384   .   1   .   1   47   47   TYR   N      N   15   117.407   0.3     .   1   .   .   .   .   .   47   TYR   N      .   50428   1    
     385   .   1   .   1   48   48   GLU   C      C   13   179.219   0.3     .   1   .   .   .   .   .   48   GLU   C      .   50428   1    
     386   .   1   .   1   48   48   GLU   CA     C   13   58.794    0.3     .   1   .   .   .   .   .   48   GLU   CA     .   50428   1    
     387   .   1   .   1   48   48   GLU   CB     C   13   28.807    0.3     .   1   .   .   .   .   .   48   GLU   CB     .   50428   1    
     388   .   1   .   1   48   48   GLU   CG     C   13   36.442    0.3     .   1   .   .   .   .   .   48   GLU   CG     .   50428   1    
     389   .   1   .   1   48   48   GLU   CD     C   13   182.976   0.3     .   1   .   .   .   .   .   48   GLU   CD     .   50428   1    
     390   .   1   .   1   48   48   GLU   N      N   15   117.432   0.3     .   1   .   .   .   .   .   48   GLU   N      .   50428   1    
     391   .   1   .   1   49   49   LYS   HA     H   1    3.459     0.100   .   1   .   .   .   .   .   49   LYS   HA     .   50428   1    
     392   .   1   .   1   49   49   LYS   C      C   13   178.233   0.3     .   1   .   .   .   .   .   49   LYS   C      .   50428   1    
     393   .   1   .   1   49   49   LYS   CA     C   13   59.126    0.3     .   1   .   .   .   .   .   49   LYS   CA     .   50428   1    
     394   .   1   .   1   49   49   LYS   CB     C   13   31.270    0.3     .   1   .   .   .   .   .   49   LYS   CB     .   50428   1    
     395   .   1   .   1   49   49   LYS   CG     C   13   24.918    0.3     .   1   .   .   .   .   .   49   LYS   CG     .   50428   1    
     396   .   1   .   1   49   49   LYS   CD     C   13   29.583    0.3     .   1   .   .   .   .   .   49   LYS   CD     .   50428   1    
     397   .   1   .   1   49   49   LYS   CE     C   13   41.561    0.3     .   1   .   .   .   .   .   49   LYS   CE     .   50428   1    
     398   .   1   .   1   49   49   LYS   N      N   15   120.130   0.3     .   1   .   .   .   .   .   49   LYS   N      .   50428   1    
     399   .   1   .   1   50   50   VAL   H      H   1    8.306     0.100   .   1   .   .   .   .   .   50   VAL   H      .   50428   1    
     400   .   1   .   1   50   50   VAL   HA     H   1    2.854     0.100   .   1   .   .   .   .   .   50   VAL   HA     .   50428   1    
     401   .   1   .   1   50   50   VAL   HB     H   1    1.656     0.100   .   1   .   .   .   .   .   50   VAL   HB     .   50428   1    
     402   .   1   .   1   50   50   VAL   HG11   H   1    0.493     0.100   .   1   .   .   .   .   .   50   VAL   HG1    .   50428   1    
     403   .   1   .   1   50   50   VAL   HG12   H   1    0.493     0.100   .   1   .   .   .   .   .   50   VAL   HG1    .   50428   1    
     404   .   1   .   1   50   50   VAL   HG13   H   1    0.493     0.100   .   1   .   .   .   .   .   50   VAL   HG1    .   50428   1    
     405   .   1   .   1   50   50   VAL   HG21   H   1    0.581     0.100   .   1   .   .   .   .   .   50   VAL   HG2    .   50428   1    
     406   .   1   .   1   50   50   VAL   HG22   H   1    0.581     0.100   .   1   .   .   .   .   .   50   VAL   HG2    .   50428   1    
     407   .   1   .   1   50   50   VAL   HG23   H   1    0.581     0.100   .   1   .   .   .   .   .   50   VAL   HG2    .   50428   1    
     408   .   1   .   1   50   50   VAL   C      C   13   177.189   0.3     .   1   .   .   .   .   .   50   VAL   C      .   50428   1    
     409   .   1   .   1   50   50   VAL   CA     C   13   65.598    0.3     .   1   .   .   .   .   .   50   VAL   CA     .   50428   1    
     410   .   1   .   1   50   50   VAL   CB     C   13   31.151    0.3     .   1   .   .   .   .   .   50   VAL   CB     .   50428   1    
     411   .   1   .   1   50   50   VAL   CG1    C   13   22.212    0.3     .   1   .   .   .   .   .   50   VAL   CG1    .   50428   1    
     412   .   1   .   1   50   50   VAL   CG2    C   13   22.845    0.3     .   1   .   .   .   .   .   50   VAL   CG2    .   50428   1    
     413   .   1   .   1   50   50   VAL   N      N   15   117.197   0.3     .   1   .   .   .   .   .   50   VAL   N      .   50428   1    
     414   .   1   .   1   51   51   ARG   C      C   13   179.044   0.3     .   1   .   .   .   .   .   51   ARG   C      .   50428   1    
     415   .   1   .   1   51   51   ARG   CA     C   13   59.099    0.3     .   1   .   .   .   .   .   51   ARG   CA     .   50428   1    
     416   .   1   .   1   51   51   ARG   CB     C   13   29.989    0.3     .   1   .   .   .   .   .   51   ARG   CB     .   50428   1    
     417   .   1   .   1   51   51   ARG   CG     C   13   27.112    0.3     .   1   .   .   .   .   .   51   ARG   CG     .   50428   1    
     418   .   1   .   1   51   51   ARG   CD     C   13   43.197    0.3     .   1   .   .   .   .   .   51   ARG   CD     .   50428   1    
     419   .   1   .   1   51   51   ARG   N      N   15   118.072   0.3     .   1   .   .   .   .   .   51   ARG   N      .   50428   1    
     420   .   1   .   1   52   52   SER   HA     H   1    3.488     0.100   .   1   .   .   .   .   .   52   SER   HA     .   50428   1    
     421   .   1   .   1   52   52   SER   C      C   13   176.342   0.3     .   1   .   .   .   .   .   52   SER   C      .   50428   1    
     422   .   1   .   1   52   52   SER   CA     C   13   60.992    0.3     .   1   .   .   .   .   .   52   SER   CA     .   50428   1    
     423   .   1   .   1   52   52   SER   CB     C   13   62.512    0.3     .   1   .   .   .   .   .   52   SER   CB     .   50428   1    
     424   .   1   .   1   52   52   SER   N      N   15   113.008   0.3     .   1   .   .   .   .   .   52   SER   N      .   50428   1    
     425   .   1   .   1   53   53   GLN   C      C   13   178.549   0.3     .   1   .   .   .   .   .   53   GLN   C      .   50428   1    
     426   .   1   .   1   53   53   GLN   CA     C   13   56.786    0.3     .   1   .   .   .   .   .   53   GLN   CA     .   50428   1    
     427   .   1   .   1   53   53   GLN   CB     C   13   25.978    0.3     .   1   .   .   .   .   .   53   GLN   CB     .   50428   1    
     428   .   1   .   1   53   53   GLN   CG     C   13   30.187    0.3     .   1   .   .   .   .   .   53   GLN   CG     .   50428   1    
     429   .   1   .   1   53   53   GLN   CD     C   13   178.704   0.3     .   1   .   .   .   .   .   53   GLN   CD     .   50428   1    
     430   .   1   .   1   53   53   GLN   N      N   15   119.111   0.3     .   1   .   .   .   .   .   53   GLN   N      .   50428   1    
     431   .   1   .   1   53   53   GLN   NE2    N   15   109.400   0.3     .   1   .   .   .   .   .   53   GLN   NE2    .   50428   1    
     432   .   1   .   1   54   54   LEU   CD2    C   13   23.090    0.3     .   1   .   .   .   .   .   54   LEU   CD2    .   50428   1    
     433   .   1   .   1   56   56   ASN   CA     C   13   53.815    0.3     .   1   .   .   .   .   .   56   ASN   CA     .   50428   1    
     434   .   1   .   1   56   56   ASN   CB     C   13   38.526    0.3     .   1   .   .   .   .   .   56   ASN   CB     .   50428   1    
     435   .   1   .   1   57   57   ASN   CA     C   13   52.996    0.3     .   1   .   .   .   .   .   57   ASN   CA     .   50428   1    
     436   .   1   .   1   57   57   ASN   CB     C   13   39.376    0.3     .   1   .   .   .   .   .   57   ASN   CB     .   50428   1    
     437   .   1   .   1   58   58   ALA   HA     H   1    3.574     0.100   .   1   .   .   .   .   .   58   ALA   HA     .   50428   1    
     438   .   1   .   1   58   58   ALA   HB1    H   1    0.912     0.100   .   1   .   .   .   .   .   58   ALA   HB     .   50428   1    
     439   .   1   .   1   58   58   ALA   HB2    H   1    0.912     0.100   .   1   .   .   .   .   .   58   ALA   HB     .   50428   1    
     440   .   1   .   1   58   58   ALA   HB3    H   1    0.912     0.100   .   1   .   .   .   .   .   58   ALA   HB     .   50428   1    
     441   .   1   .   1   58   58   ALA   C      C   13   182.118   0.3     .   1   .   .   .   .   .   58   ALA   C      .   50428   1    
     442   .   1   .   1   58   58   ALA   CA     C   13   53.789    0.3     .   1   .   .   .   .   .   58   ALA   CA     .   50428   1    
     443   .   1   .   1   58   58   ALA   CB     C   13   19.528    0.3     .   1   .   .   .   .   .   58   ALA   CB     .   50428   1    
     444   .   1   .   1   58   58   ALA   N      N   15   127.881   0.3     .   1   .   .   .   .   .   58   ALA   N      .   50428   1    

   stop_

save_