Content for NMR-STAR saveframe, spectral_peak_list_1

    save_spectral_peak_list_1
   _Spectral_peak_list.Sf_category                      spectral_peak_list
   _Spectral_peak_list.Sf_framecode                     spectral_peak_list_1
   _Spectral_peak_list.Entry_ID                         34758
   _Spectral_peak_list.ID                               1
   _Spectral_peak_list.Name                             .
   _Spectral_peak_list.Sample_ID                        1
   _Spectral_peak_list.Sample_label                     $sample_1
   _Spectral_peak_list.Sample_condition_list_ID         1
   _Spectral_peak_list.Sample_condition_list_label      $sample_conditions_1
   _Spectral_peak_list.Chem_shift_reference_ID          1
   _Spectral_peak_list.Chem_shift_reference_label       $chem_shift_reference_1
   _Spectral_peak_list.Experiment_ID                    1
   _Spectral_peak_list.Experiment_name                  '3D 1H-13C NOESY'
   _Spectral_peak_list.Experiment_class                 .
   _Spectral_peak_list.Experiment_type                  .
   _Spectral_peak_list.Number_of_spectral_dimensions    3
   _Spectral_peak_list.Chemical_shift_list              .
   _Spectral_peak_list.Assigned_chem_shift_list_ID      1
   _Spectral_peak_list.Assigned_chem_shift_list_label   $assigned_chemical_shifts_1
   _Spectral_peak_list.Details
;
Methyl-Methyl NOEs for the residues from 98 to 136;
CNS restrained molecular dynamics protocol using a full Lenard-Jones potential and explicit water molecules: 
In brief, the explicit solvent refinement consisted of the five following steps: 
(i) immersion in a 7.0 A shell of water molecules and energy minimization; 
(ii) slow heating from 100 to 500 K in 100 K temperature steps with 200 MD steps per temperature step (time/step 3 fs), 
with harmonic position restraints on the protein heavy atoms that were slowly phased out during the heating stage; 
(iii) refinement at 500 K with 2,000 MD steps (time step 4 fs); (iv) slow cooling from 500 K to 25 K in 25 K temperature 
steps with 200 MD steps per temperature step (time step 4 fs); (v) final energy minimization (200 steps).
Brunger, A. T. et al. Crystallography and NMR System: A New Software Suite for Macromolecular Structure Determination. Acta Cryst (1998).
;
   _Spectral_peak_list.Text_data_format                 text
   _Spectral_peak_list.Text_data
;
data_CCP_assig_NOE_CH_R60A_400ms


   save_