Content for NMR-STAR saveframe, "assigned_chemical_shifts_3"

    save_assigned_chemical_shifts_3
   _Assigned_chem_shift_list.Sf_category                   assigned_chemical_shifts
   _Assigned_chem_shift_list.Sf_framecode                  assigned_chemical_shifts_3
   _Assigned_chem_shift_list.Entry_ID                      50745
   _Assigned_chem_shift_list.ID                            3
   _Assigned_chem_shift_list.Name                          'reduced SelW1 chemical shifts'
   _Assigned_chem_shift_list.Sample_condition_list_ID      1
   _Assigned_chem_shift_list.Sample_condition_list_label   $sample_conditions_1
   _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             .
   _Assigned_chem_shift_list.Chem_shift_13C_err            .
   _Assigned_chem_shift_list.Chem_shift_15N_err            .
   _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 HNCACB'         .   .   .   50745   3
      2   '3D HNCO'           .   .   .   50745   3
      3   '3D HNCA'           .   .   .   50745   3
      4   '3D HBHA(CO)NH'     .   .   .   50745   3
      5   '3D HN(CA)CO'       .   .   .   50745   3
      6   '3D 1H-15N TOCSY'   .   .   .   50745   3
      7   '3D 1H-15N NOESY'   .   .   .   50745   3
   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

      1   $software_1   .   .   50745   3
      2   $software_2   .   .   50745   3
   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     .   3   .   1   3    3    PRO   HA     H   1    4.772     0.005   .   1   .   .   769    .   .   3    PRO   HA     .   50745   3
      2     .   3   .   1   3    3    PRO   HB2    H   1    1.765     .       .   2   .   .   773    .   .   3    PRO   HB2    .   50745   3
      3     .   3   .   1   3    3    PRO   HB3    H   1    2.227     0.024   .   2   .   .   774    .   .   3    PRO   HB3    .   50745   3
      4     .   3   .   1   3    3    PRO   C      C   13   176.513   0.013   .   1   .   .   566    .   .   3    PRO   C      .   50745   3
      5     .   3   .   1   3    3    PRO   CA     C   13   62.210    0.034   .   1   .   .   567    .   .   3    PRO   CA     .   50745   3
      6     .   3   .   1   3    3    PRO   CB     C   13   31.731    0.037   .   1   .   .   568    .   .   3    PRO   CB     .   50745   3
      7     .   3   .   1   4    4    VAL   H      H   1    8.248     0.002   .   1   .   .   475    .   .   4    VAL   H      .   50745   3
      8     .   3   .   1   4    4    VAL   HA     H   1    4.286     0.01    .   1   .   .   777    .   .   4    VAL   HA     .   50745   3
      9     .   3   .   1   4    4    VAL   C      C   13   174.191   0.02    .   1   .   .   559    .   .   4    VAL   C      .   50745   3
      10    .   3   .   1   4    4    VAL   CA     C   13   61.832    0.032   .   1   .   .   564    .   .   4    VAL   CA     .   50745   3
      11    .   3   .   1   4    4    VAL   CB     C   13   33.724    0.041   .   1   .   .   565    .   .   4    VAL   CB     .   50745   3
      12    .   3   .   1   4    4    VAL   N      N   15   122.065   0.015   .   1   .   .   476    .   .   4    VAL   N      .   50745   3
      13    .   3   .   1   5    5    GLN   H      H   1    8.686     0.006   .   1   .   .   555    .   .   5    GLN   H      .   50745   3
      14    .   3   .   1   5    5    GLN   HA     H   1    4.821     0.001   .   1   .   .   775    .   .   5    GLN   HA     .   50745   3
      15    .   3   .   1   5    5    GLN   HB2    H   1    2.160     0.003   .   1   .   .   782    .   .   5    GLN   HB2    .   50745   3
      16    .   3   .   1   5    5    GLN   HB3    H   1    2.160     0.003   .   1   .   .   783    .   .   5    GLN   HB3    .   50745   3
      17    .   3   .   1   5    5    GLN   HE21   H   1    7.303     0.003   .   1   .   .   629    .   .   5    GLN   HE21   .   50745   3
      18    .   3   .   1   5    5    GLN   HE22   H   1    6.736     0.004   .   1   .   .   631    .   .   5    GLN   HE22   .   50745   3
      19    .   3   .   1   5    5    GLN   C      C   13   175.176   0.009   .   1   .   .   553    .   .   5    GLN   C      .   50745   3
      20    .   3   .   1   5    5    GLN   CA     C   13   54.508    0.057   .   1   .   .   557    .   .   5    GLN   CA     .   50745   3
      21    .   3   .   1   5    5    GLN   CB     C   13   29.893    0.05    .   1   .   .   563    .   .   5    GLN   CB     .   50745   3
      22    .   3   .   1   5    5    GLN   CG     C   13   33.609    0.032   .   1   .   .   627    .   .   5    GLN   CG     .   50745   3
      23    .   3   .   1   5    5    GLN   N      N   15   126.613   0.039   .   1   .   .   556    .   .   5    GLN   N      .   50745   3
      24    .   3   .   1   5    5    GLN   NE2    N   15   111.046   0.143   .   1   .   .   628    .   .   5    GLN   NE2    .   50745   3
      25    .   3   .   1   6    6    VAL   H      H   1    8.925     0.001   .   1   .   .   549    .   .   6    VAL   H      .   50745   3
      26    .   3   .   1   6    6    VAL   C      C   13   173.738   .       .   1   .   .   554    .   .   6    VAL   C      .   50745   3
      27    .   3   .   1   6    6    VAL   CA     C   13   61.544    0.038   .   1   .   .   552    .   .   6    VAL   CA     .   50745   3
      28    .   3   .   1   6    6    VAL   CB     C   13   32.767    .       .   1   .   .   551    .   .   6    VAL   CB     .   50745   3
      29    .   3   .   1   6    6    VAL   N      N   15   128.857   0.031   .   1   .   .   550    .   .   6    VAL   N      .   50745   3
      30    .   3   .   1   30   30   LYS   HA     H   1    3.789     .       .   1   .   .   1086   .   .   30   LYS   HA     .   50745   3
      31    .   3   .   1   30   30   LYS   HB2    H   1    0.940     .       .   2   .   .   1082   .   .   30   LYS   HB2    .   50745   3
      32    .   3   .   1   30   30   LYS   HB3    H   1    1.150     .       .   2   .   .   1083   .   .   30   LYS   HB3    .   50745   3
      33    .   3   .   1   31   31   PHE   H      H   1    7.694     0.001   .   1   .   .   592    .   .   31   PHE   H      .   50745   3
      34    .   3   .   1   31   31   PHE   HA     H   1    4.984     .       .   1   .   .   1087   .   .   31   PHE   HA     .   50745   3
      35    .   3   .   1   31   31   PHE   HB2    H   1    2.853     .       .   1   .   .   1084   .   .   31   PHE   HB2    .   50745   3
      36    .   3   .   1   31   31   PHE   HB3    H   1    2.853     .       .   1   .   .   1085   .   .   31   PHE   HB3    .   50745   3
      37    .   3   .   1   31   31   PHE   C      C   13   173.212   .       .   1   .   .   590    .   .   31   PHE   C      .   50745   3
      38    .   3   .   1   31   31   PHE   N      N   15   115.819   0.015   .   1   .   .   591    .   .   31   PHE   N      .   50745   3
      39    .   3   .   1   32   32   PRO   C      C   13   178.293   0.029   .   1   .   .   522    .   .   32   PRO   C      .   50745   3
      40    .   3   .   1   32   32   PRO   CA     C   13   64.976    0.083   .   1   .   .   525    .   .   32   PRO   CA     .   50745   3
      41    .   3   .   1   32   32   PRO   CB     C   13   32.054    0.057   .   1   .   .   527    .   .   32   PRO   CB     .   50745   3
      42    .   3   .   1   33   33   ASN   H      H   1    8.799     0.003   .   1   .   .   521    .   .   33   ASN   H      .   50745   3
      43    .   3   .   1   33   33   ASN   HA     H   1    4.867     .       .   1   .   .   1093   .   .   33   ASN   HA     .   50745   3
      44    .   3   .   1   33   33   ASN   HB2    H   1    2.784     .       .   2   .   .   1096   .   .   33   ASN   HB2    .   50745   3
      45    .   3   .   1   33   33   ASN   HB3    H   1    3.018     .       .   2   .   .   1097   .   .   33   ASN   HB3    .   50745   3
      46    .   3   .   1   33   33   ASN   C      C   13   174.361   0.018   .   1   .   .   513    .   .   33   ASN   C      .   50745   3
      47    .   3   .   1   33   33   ASN   CA     C   13   53.163    0.083   .   1   .   .   515    .   .   33   ASN   CA     .   50745   3
      48    .   3   .   1   33   33   ASN   CB     C   13   38.938    0.025   .   1   .   .   512    .   .   33   ASN   CB     .   50745   3
      49    .   3   .   1   33   33   ASN   N      N   15   115.539   0.026   .   1   .   .   520    .   .   33   ASN   N      .   50745   3
      50    .   3   .   1   34   34   ALA   H      H   1    7.329     0.002   .   1   .   .   388    .   .   34   ALA   H      .   50745   3
      51    .   3   .   1   34   34   ALA   HA     H   1    4.496     0.004   .   1   .   .   1092   .   .   34   ALA   HA     .   50745   3
      52    .   3   .   1   34   34   ALA   HB1    H   1    1.430     0.005   .   1   .   .   1111   .   .   34   ALA   HB1    .   50745   3
      53    .   3   .   1   34   34   ALA   HB2    H   1    1.430     0.005   .   1   .   .   1111   .   .   34   ALA   HB2    .   50745   3
      54    .   3   .   1   34   34   ALA   HB3    H   1    1.430     0.005   .   1   .   .   1111   .   .   34   ALA   HB3    .   50745   3
      55    .   3   .   1   34   34   ALA   C      C   13   177.078   0.032   .   1   .   .   503    .   .   34   ALA   C      .   50745   3
      56    .   3   .   1   34   34   ALA   CA     C   13   51.342    0.072   .   1   .   .   505    .   .   34   ALA   CA     .   50745   3
      57    .   3   .   1   34   34   ALA   CB     C   13   22.351    0.056   .   1   .   .   504    .   .   34   ALA   CB     .   50745   3
      58    .   3   .   1   34   34   ALA   N      N   15   122.325   0.002   .   1   .   .   387    .   .   34   ALA   N      .   50745   3
      59    .   3   .   1   35   35   ASP   H      H   1    8.671     0.001   .   1   .   .   136    .   .   35   ASP   H      .   50745   3
      60    .   3   .   1   35   35   ASP   HA     H   1    4.723     0.001   .   1   .   .   1091   .   .   35   ASP   HA     .   50745   3
      61    .   3   .   1   35   35   ASP   HB2    H   1    2.875     0.014   .   2   .   .   1054   .   .   35   ASP   HB2    .   50745   3
      62    .   3   .   1   35   35   ASP   HB3    H   1    2.469     0.007   .   2   .   .   1098   .   .   35   ASP   HB3    .   50745   3
      63    .   3   .   1   35   35   ASP   C      C   13   173.589   0.017   .   1   .   .   496    .   .   35   ASP   C      .   50745   3
      64    .   3   .   1   35   35   ASP   CA     C   13   53.580    0.037   .   1   .   .   495    .   .   35   ASP   CA     .   50745   3
      65    .   3   .   1   35   35   ASP   CB     C   13   39.458    0.075   .   1   .   .   261    .   .   35   ASP   CB     .   50745   3
      66    .   3   .   1   35   35   ASP   N      N   15   123.061   0.035   .   1   .   .   137    .   .   35   ASP   N      .   50745   3
      67    .   3   .   1   36   36   ILE   H      H   1    7.458     0.003   .   1   .   .   50     .   .   36   ILE   H      .   50745   3
      68    .   3   .   1   36   36   ILE   HA     H   1    4.553     0.011   .   1   .   .   1090   .   .   36   ILE   HA     .   50745   3
      69    .   3   .   1   36   36   ILE   HB     H   1    1.407     0.001   .   1   .   .   1101   .   .   36   ILE   HB     .   50745   3
      70    .   3   .   1   36   36   ILE   C      C   13   175.051   0.003   .   1   .   .   410    .   .   36   ILE   C      .   50745   3
      71    .   3   .   1   36   36   ILE   CA     C   13   59.367    0.069   .   1   .   .   409    .   .   36   ILE   CA     .   50745   3
      72    .   3   .   1   36   36   ILE   CB     C   13   40.382    0.068   .   1   .   .   497    .   .   36   ILE   CB     .   50745   3
      73    .   3   .   1   36   36   ILE   N      N   15   124.285   0.02    .   1   .   .   51     .   .   36   ILE   N      .   50745   3
      74    .   3   .   1   37   37   LYS   H      H   1    8.998     0.003   .   1   .   .   72     .   .   37   LYS   H      .   50745   3
      75    .   3   .   1   37   37   LYS   HA     H   1    4.681     0.007   .   1   .   .   1089   .   .   37   LYS   HA     .   50745   3
      76    .   3   .   1   37   37   LYS   HB2    H   1    1.700     0.012   .   2   .   .   1099   .   .   37   LYS   HB2    .   50745   3
      77    .   3   .   1   37   37   LYS   HB3    H   1    1.700     0.012   .   2   .   .   1100   .   .   37   LYS   HB3    .   50745   3
      78    .   3   .   1   37   37   LYS   C      C   13   174.779   0.052   .   1   .   .   489    .   .   37   LYS   C      .   50745   3
      79    .   3   .   1   37   37   LYS   CA     C   13   54.267    0.086   .   1   .   .   488    .   .   37   LYS   CA     .   50745   3
      80    .   3   .   1   37   37   LYS   CB     C   13   34.074    0.039   .   1   .   .   487    .   .   37   LYS   CB     .   50745   3
      81    .   3   .   1   37   37   LYS   N      N   15   127.972   0.04    .   1   .   .   73     .   .   37   LYS   N      .   50745   3
      82    .   3   .   1   38   38   PHE   H      H   1    8.975     0.003   .   1   .   .   44     .   .   38   PHE   H      .   50745   3
      83    .   3   .   1   38   38   PHE   HA     H   1    5.642     .       .   1   .   .   1088   .   .   38   PHE   HA     .   50745   3
      84    .   3   .   1   38   38   PHE   HB2    H   1    3.545     .       .   2   .   .   1094   .   .   38   PHE   HB2    .   50745   3
      85    .   3   .   1   38   38   PHE   HB3    H   1    2.952     .       .   2   .   .   1095   .   .   38   PHE   HB3    .   50745   3
      86    .   3   .   1   38   38   PHE   C      C   13   176.464   .       .   1   .   .   484    .   .   38   PHE   C      .   50745   3
      87    .   3   .   1   38   38   PHE   CA     C   13   57.820    .       .   1   .   .   491    .   .   38   PHE   CA     .   50745   3
      88    .   3   .   1   38   38   PHE   CB     C   13   41.414    .       .   1   .   .   485    .   .   38   PHE   CB     .   50745   3
      89    .   3   .   1   38   38   PHE   N      N   15   123.819   0.019   .   1   .   .   45     .   .   38   PHE   N      .   50745   3
      90    .   3   .   1   53   53   GLU   C      C   13   176.257   0.02    .   1   .   .   541    .   .   53   GLU   C      .   50745   3
      91    .   3   .   1   54   54   VAL   H      H   1    8.794     0.001   .   1   .   .   539    .   .   54   VAL   H      .   50745   3
      92    .   3   .   1   54   54   VAL   HA     H   1    4.768     0.014   .   1   .   .   912    .   .   54   VAL   HA     .   50745   3
      93    .   3   .   1   54   54   VAL   HB     H   1    1.971     .       .   1   .   .   1103   .   .   54   VAL   HB     .   50745   3
      94    .   3   .   1   54   54   VAL   C      C   13   176.276   0.028   .   1   .   .   534    .   .   54   VAL   C      .   50745   3
      95    .   3   .   1   54   54   VAL   CA     C   13   60.984    0.003   .   1   .   .   537    .   .   54   VAL   CA     .   50745   3
      96    .   3   .   1   54   54   VAL   CB     C   13   33.727    0.015   .   1   .   .   281    .   .   54   VAL   CB     .   50745   3
      97    .   3   .   1   54   54   VAL   N      N   15   120.867   0.004   .   1   .   .   540    .   .   54   VAL   N      .   50745   3
      98    .   3   .   1   55   55   ASN   H      H   1    10.077    0.003   .   1   .   .   48     .   .   55   ASN   H      .   50745   3
      99    .   3   .   1   55   55   ASN   HA     H   1    4.526     0.01    .   1   .   .   1102   .   .   55   ASN   HA     .   50745   3
      100   .   3   .   1   55   55   ASN   HB2    H   1    2.830     0.008   .   2   .   .   920    .   .   55   ASN   HB2    .   50745   3
      101   .   3   .   1   55   55   ASN   HB3    H   1    3.261     .       .   2   .   .   921    .   .   55   ASN   HB3    .   50745   3
      102   .   3   .   1   55   55   ASN   HD21   H   1    7.962     0.0     .   1   .   .   66     .   .   55   ASN   HD21   .   50745   3
      103   .   3   .   1   55   55   ASN   HD22   H   1    6.881     0.0     .   1   .   .   191    .   .   55   ASN   HD22   .   50745   3
      104   .   3   .   1   55   55   ASN   C      C   13   175.731   0.012   .   1   .   .   445    .   .   55   ASN   C      .   50745   3
      105   .   3   .   1   55   55   ASN   CA     C   13   53.896    0.034   .   1   .   .   447    .   .   55   ASN   CA     .   50745   3
      106   .   3   .   1   55   55   ASN   CB     C   13   36.806    0.036   .   1   .   .   280    .   .   55   ASN   CB     .   50745   3
      107   .   3   .   1   55   55   ASN   N      N   15   130.404   0.035   .   1   .   .   49     .   .   55   ASN   N      .   50745   3
      108   .   3   .   1   55   55   ASN   ND2    N   15   111.239   0.014   .   1   .   .   67     .   .   55   ASN   ND2    .   50745   3
      109   .   3   .   1   56   56   GLY   H      H   1    9.131     0.003   .   1   .   .   192    .   .   56   GLY   H      .   50745   3
      110   .   3   .   1   56   56   GLY   HA2    H   1    4.086     0.007   .   2   .   .   918    .   .   56   GLY   HA2    .   50745   3
      111   .   3   .   1   56   56   GLY   HA3    H   1    3.687     0.007   .   2   .   .   919    .   .   56   GLY   HA3    .   50745   3
      112   .   3   .   1   56   56   GLY   C      C   13   172.978   .       .   1   .   .   293    .   .   56   GLY   C      .   50745   3
      113   .   3   .   1   56   56   GLY   CA     C   13   45.471    0.007   .   1   .   .   292    .   .   56   GLY   CA     .   50745   3
      114   .   3   .   1   56   56   GLY   N      N   15   103.561   0.036   .   1   .   .   193    .   .   56   GLY   N      .   50745   3
      115   .   3   .   1   83   83   GLY   HA2    H   1    4.139     0.001   .   2   .   .   1106   .   .   83   GLY   HA2    .   50745   3
      116   .   3   .   1   83   83   GLY   HA3    H   1    3.615     .       .   2   .   .   1107   .   .   83   GLY   HA3    .   50745   3
      117   .   3   .   1   83   83   GLY   C      C   13   176.979   0.029   .   1   .   .   583    .   .   83   GLY   C      .   50745   3
      118   .   3   .   1   83   83   GLY   CA     C   13   47.350    0.076   .   1   .   .   582    .   .   83   GLY   CA     .   50745   3
      119   .   3   .   1   84   84   GLU   H      H   1    8.034     0.002   .   1   .   .   141    .   .   84   GLU   H      .   50745   3
      120   .   3   .   1   84   84   GLU   HA     H   1    4.070     .       .   1   .   .   972    .   .   84   GLU   HA     .   50745   3
      121   .   3   .   1   84   84   GLU   HB2    H   1    2.179     0.017   .   1   .   .   973    .   .   84   GLU   HB2    .   50745   3
      122   .   3   .   1   84   84   GLU   HB3    H   1    2.179     0.017   .   1   .   .   974    .   .   84   GLU   HB3    .   50745   3
      123   .   3   .   1   84   84   GLU   C      C   13   178.760   0.046   .   1   .   .   463    .   .   84   GLU   C      .   50745   3
      124   .   3   .   1   84   84   GLU   CA     C   13   59.138    0.025   .   1   .   .   464    .   .   84   GLU   CA     .   50745   3
      125   .   3   .   1   84   84   GLU   CB     C   13   30.146    0.094   .   1   .   .   584    .   .   84   GLU   CB     .   50745   3
      126   .   3   .   1   84   84   GLU   N      N   15   121.323   0.032   .   1   .   .   142    .   .   84   GLU   N      .   50745   3
      127   .   3   .   1   85   85   ALA   H      H   1    7.665     0.002   .   1   .   .   84     .   .   85   ALA   H      .   50745   3
      128   .   3   .   1   85   85   ALA   HA     H   1    4.126     0.008   .   1   .   .   966    .   .   85   ALA   HA     .   50745   3
      129   .   3   .   1   85   85   ALA   HB1    H   1    1.493     0.008   .   1   .   .   967    .   .   85   ALA   HB1    .   50745   3
      130   .   3   .   1   85   85   ALA   HB2    H   1    1.493     0.008   .   1   .   .   967    .   .   85   ALA   HB2    .   50745   3
      131   .   3   .   1   85   85   ALA   HB3    H   1    1.493     0.008   .   1   .   .   967    .   .   85   ALA   HB3    .   50745   3
      132   .   3   .   1   85   85   ALA   C      C   13   180.313   0.029   .   1   .   .   452    .   .   85   ALA   C      .   50745   3
      133   .   3   .   1   85   85   ALA   CA     C   13   54.934    0.014   .   1   .   .   433    .   .   85   ALA   CA     .   50745   3
      134   .   3   .   1   85   85   ALA   CB     C   13   18.596    0.079   .   1   .   .   422    .   .   85   ALA   CB     .   50745   3
      135   .   3   .   1   85   85   ALA   N      N   15   122.243   0.033   .   1   .   .   85     .   .   85   ALA   N      .   50745   3
      136   .   3   .   1   86   86   LEU   H      H   1    8.410     0.002   .   1   .   .   421    .   .   86   LEU   H      .   50745   3
      137   .   3   .   1   86   86   LEU   HA     H   1    4.089     0.001   .   1   .   .   962    .   .   86   LEU   HA     .   50745   3
      138   .   3   .   1   86   86   LEU   HB2    H   1    1.406     .       .   2   .   .   963    .   .   86   LEU   HB2    .   50745   3
      139   .   3   .   1   86   86   LEU   HB3    H   1    1.807     .       .   2   .   .   964    .   .   86   LEU   HB3    .   50745   3
      140   .   3   .   1   86   86   LEU   C      C   13   178.274   0.025   .   1   .   .   423    .   .   86   LEU   C      .   50745   3
      141   .   3   .   1   86   86   LEU   CA     C   13   57.205    0.017   .   1   .   .   462    .   .   86   LEU   CA     .   50745   3
      142   .   3   .   1   86   86   LEU   CB     C   13   42.389    0.078   .   1   .   .   238    .   .   86   LEU   CB     .   50745   3
      143   .   3   .   1   86   86   LEU   N      N   15   119.002   0.019   .   1   .   .   420    .   .   86   LEU   N      .   50745   3
      144   .   3   .   1   87   87   ALA   H      H   1    7.394     0.003   .   1   .   .   189    .   .   87   ALA   H      .   50745   3
      145   .   3   .   1   87   87   ALA   HA     H   1    4.285     0.009   .   1   .   .   1105   .   .   87   ALA   HA     .   50745   3
      146   .   3   .   1   87   87   ALA   HB1    H   1    1.492     0.007   .   1   .   .   961    .   .   87   ALA   HB1    .   50745   3
      147   .   3   .   1   87   87   ALA   HB2    H   1    1.492     0.007   .   1   .   .   961    .   .   87   ALA   HB2    .   50745   3
      148   .   3   .   1   87   87   ALA   HB3    H   1    1.492     0.007   .   1   .   .   961    .   .   87   ALA   HB3    .   50745   3
      149   .   3   .   1   87   87   ALA   C      C   13   177.795   0.016   .   1   .   .   455    .   .   87   ALA   C      .   50745   3
      150   .   3   .   1   87   87   ALA   CA     C   13   52.884    0.047   .   1   .   .   453    .   .   87   ALA   CA     .   50745   3
      151   .   3   .   1   87   87   ALA   CB     C   13   19.451    0.083   .   1   .   .   230    .   .   87   ALA   CB     .   50745   3
      152   .   3   .   1   87   87   ALA   N      N   15   119.559   0.032   .   1   .   .   190    .   .   87   ALA   N      .   50745   3
      153   .   3   .   1   88   88   LYS   H      H   1    7.225     0.003   .   1   .   .   98     .   .   88   LYS   H      .   50745   3
      154   .   3   .   1   88   88   LYS   HA     H   1    4.010     0.024   .   1   .   .   1104   .   .   88   LYS   HA     .   50745   3
      155   .   3   .   1   88   88   LYS   HB2    H   1    1.830     0.022   .   1   .   .   1108   .   .   88   LYS   HB2    .   50745   3
      156   .   3   .   1   88   88   LYS   HB3    H   1    1.830     0.022   .   1   .   .   1109   .   .   88   LYS   HB3    .   50745   3
      157   .   3   .   1   88   88   LYS   C      C   13   181.793   .       .   1   .   .   454    .   .   88   LYS   C      .   50745   3
      158   .   3   .   1   88   88   LYS   CA     C   13   59.440    0.041   .   1   .   .   645    .   .   88   LYS   CA     .   50745   3
      159   .   3   .   1   88   88   LYS   CB     C   13   33.450    .       .   1   .   .   225    .   .   88   LYS   CB     .   50745   3
      160   .   3   .   1   88   88   LYS   N      N   15   123.662   0.033   .   1   .   .   99     .   .   88   LYS   N      .   50745   3
   stop_
save_