data_16321

#######################
#  Entry information  #
#######################

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
Backbone 1H, 13C and 15N resonance assignments for the E2 conjugating enzyme, UbcH8
;
   _BMRB_accession_number   16321
   _BMRB_flat_file_name     bmr16321.str
   _Entry_type              original
   _Submission_date         2009-05-28
   _Accession_date          2009-05-28
   _Entry_origination       author
   _NMR_STAR_version        2.1.1
   _Experimental_method     NMR
   _Details                 .

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Serniwka Stephanie A. . 
      2 Shaw     Gary      S. . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  362 
      "13C chemical shifts" 460 
      "15N chemical shifts" 140 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2010-04-19 update   author 'Update citations' 
      2009-10-14 original author 'original release' 

   stop_

save_


#############################
#  Citation for this entry  #
#############################

save_Citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              'The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site'
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    19928833

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Serniwka Stephanie A. . 
      2 Shaw     Gary      S. . 

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               48
   _Journal_issue                51
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   12169
   _Page_last                    12179
   _Year                         2009
   _Details                      .

save_


#######################################
#  Cited references within the entry  #
#######################################

save_Citation_2
   _Saveframe_category           citation

   _Citation_full                .
   _Citation_title              '1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7'
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    19636915

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Serniwka Stephanie A. . 
      2 Shaw     Gary      S. . 

   stop_

   _Journal_abbreviation        'Biomol. NMR Assign.'
   _Journal_name_full           'Biomolecular NMR assignments'
   _Journal_volume               2
   _Journal_issue                1
   _Journal_CSD                  .
   _Book_title                   .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_publisher               .
   _Book_publisher_city          .
   _Book_ISBN                    .
   _Conference_title             .
   _Conference_site              .
   _Conference_state_province    .
   _Conference_country           .
   _Conference_start_date        .
   _Conference_end_date          .
   _Conference_abstract_number   .
   _Thesis_institution           .
   _Thesis_institution_city      .
   _Thesis_institution_country   .
   _Page_first                   21
   _Page_last                    23
   _Year                         2008
   _Details                      .

save_


##################################
#  Molecular system description  #
##################################

save_assembly
   _Saveframe_category         molecular_system

   _Mol_system_name            UbcH8
   _Enzyme_commission_number   6.3.2.19

   loop_
      _Mol_system_component_name
      _Mol_label

      UbcH8 $UbcH8 

   stop_

   _System_molecular_weight    17638
   _System_physical_state      native
   _System_oligomer_state      ?
   _System_paramagnetic        no
   _System_thiol_state         .

   loop_
      _Biological_function

      'E2 ubiquitin conjugating enzyme' 

   stop_

   _Database_query_date        .
   _Details                    .

save_


    ########################
    #  Monomeric polymers  #
    ########################

save_UbcH8
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 UbcH8
   _Molecular_mass                              17638
   _Mol_thiol_state                            'all free'

   loop_
      _Biological_function

      'E2 ubiquitin conjugating enzyme' 

   stop_

   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               152
   _Mol_residue_sequence                       
;
MASMRVVKELEDLQKKPPPY
LRNLSSDDANVLVWHALLLP
DQPPYHLKAFNLRISFPPEY
PFKPPMIKFTTKIYHPNVDE
NGQICLPIISSENWKPSTKT
SQVLEALNVLVNRPNIREPL
RMDLADLLTQNPELFRKNAE
EFTLRFGVDRPS
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 ALA    3 SER    4 MET    5 ARG 
        6 VAL    7 VAL    8 LYS    9 GLU   10 LEU 
       11 GLU   12 ASP   13 LEU   14 GLN   15 LYS 
       16 LYS   17 PRO   18 PRO   19 PRO   20 TYR 
       21 LEU   22 ARG   23 ASN   24 LEU   25 SER 
       26 SER   27 ASP   28 ASP   29 ALA   30 ASN 
       31 VAL   32 LEU   33 VAL   34 TRP   35 HIS 
       36 ALA   37 LEU   38 LEU   39 LEU   40 PRO 
       41 ASP   42 GLN   43 PRO   44 PRO   45 TYR 
       46 HIS   47 LEU   48 LYS   49 ALA   50 PHE 
       51 ASN   52 LEU   53 ARG   54 ILE   55 SER 
       56 PHE   57 PRO   58 PRO   59 GLU   60 TYR 
       61 PRO   62 PHE   63 LYS   64 PRO   65 PRO 
       66 MET   67 ILE   68 LYS   69 PHE   70 THR 
       71 THR   72 LYS   73 ILE   74 TYR   75 HIS 
       76 PRO   77 ASN   78 VAL   79 ASP   80 GLU 
       81 ASN   82 GLY   83 GLN   84 ILE   85 CYS 
       86 LEU   87 PRO   88 ILE   89 ILE   90 SER 
       91 SER   92 GLU   93 ASN   94 TRP   95 LYS 
       96 PRO   97 SER   98 THR   99 LYS  100 THR 
      101 SER  102 GLN  103 VAL  104 LEU  105 GLU 
      106 ALA  107 LEU  108 ASN  109 VAL  110 LEU 
      111 VAL  112 ASN  113 ARG  114 PRO  115 ASN 
      116 ILE  117 ARG  118 GLU  119 PRO  120 LEU 
      121 ARG  122 MET  123 ASP  124 LEU  125 ALA 
      126 ASP  127 LEU  128 LEU  129 THR  130 GLN 
      131 ASN  132 PRO  133 GLU  134 LEU  135 PHE 
      136 ARG  137 LYS  138 ASN  139 ALA  140 GLU 
      141 GLU  142 PHE  143 THR  144 LEU  145 ARG 
      146 PHE  147 GLY  148 VAL  149 ASP  150 ARG 
      151 PRO  152 SER 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-10-28

   loop_
      _Database_name
      _Database_accession_code
      _Database_entry_mol_name
      _Sequence_query_to_submitted_percentage
      _Sequence_subject_length
      _Sequence_identity
      _Sequence_positive
      _Sequence_homology_expectation_value

      PDB  1WZV         "Crystal Structure Of Ubch8"                                                                                                      100.00 155 98.68 98.68 1.40e-103 
      PDB  1WZW         "Crystal Structure Of Ubch8"                                                                                                      100.00 155 98.68 98.68 1.40e-103 
      PDB  2KJH         "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex"                                                                       100.00 152 98.68 98.68 1.34e-103 
      DBJ  BAG38109     "unnamed protein product [Homo sapiens]"                                                                                          100.00 153 98.68 98.68 1.30e-103 
      EMBL CAB64566     "ubiquitin-conjugating enzyme [Homo sapiens]"                                                                                     100.00 152 98.68 98.68 1.34e-103 
      EMBL CAG33407     "UBE2L6 [Homo sapiens]"                                                                                                           100.00 153 98.68 98.68 1.30e-103 
      GB   AAB86433     "ubiquitin conjugating enzyme [Homo sapiens]"                                                                                     100.00 152 98.68 98.68 1.34e-103 
      GB   AAD17525     "ubiquitin-conjugating enzyme RIG-B [Homo sapiens]"                                                                               100.00 153 98.68 98.68 1.30e-103 
      GB   AAH32491     "Ubiquitin-conjugating enzyme E2L 6 [Homo sapiens]"                                                                               100.00 153 98.68 98.68 1.30e-103 
      GB   ABM82217     "ubiquitin-conjugating enzyme E2L 6 [synthetic construct]"                                                                        100.00 153 98.68 98.68 1.30e-103 
      GB   ABM85401     "ubiquitin-conjugating enzyme E2L 6 [synthetic construct]"                                                                        100.00 153 98.68 98.68 1.30e-103 
      REF  NP_004214    "ubiquitin/ISG15-conjugating enzyme E2 L6 isoform 1 [Homo sapiens]"                                                               100.00 153 98.68 98.68 1.30e-103 
      REF  NP_937826    "ubiquitin/ISG15-conjugating enzyme E2 L6 isoform 2 [Homo sapiens]"                                                                57.24  87 97.70 97.70 1.63e-53  
      REF  XP_003318029 "PREDICTED: ubiquitin/ISG15-conjugating enzyme E2 L6 isoform X2 [Pan troglodytes]"                                                 57.24  87 97.70 97.70 1.63e-53  
      REF  XP_003826475 "PREDICTED: ubiquitin/ISG15-conjugating enzyme E2 L6 isoform X1 [Pan paniscus]"                                                   100.00 153 98.68 98.68 1.30e-103 
      REF  XP_004051215 "PREDICTED: ubiquitin/ISG15-conjugating enzyme E2 L6 isoform 1 [Gorilla gorilla gorilla]"                                         100.00 153 97.37 98.03 3.67e-102 
      SP   O14933       "RecName: Full=Ubiquitin/ISG15-conjugating enzyme E2 L6; AltName: Full=E2 ubiquitin-conjugating enzyme L6; AltName: Full=Retinoi" 100.00 153 98.68 98.68 1.30e-103 

   stop_

save_


    ####################
    #  Natural source  #
    ####################

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Gene_mnemonic

      $UbcH8 Human 9606 Eukaryota Metazoa Homo sapiens UBE2L6 

   stop_

save_


    #########################
    #  Experimental source  #
    #########################

save_experimental_source
   _Saveframe_category   experimental_source


   loop_
      _Mol_label
      _Production_method
      _Host_organism_name_common
      _Genus
      _Species
      _Strain
      _Vector_name

      $UbcH8 'recombinant technology' . Escherichia coli BL21(DE3) p11 

   stop_

save_


#####################################
#  Sample contents and methodology  #
#####################################
	 
    ########################
    #  Sample description  #
    ########################

save_sample_UbcH8
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $UbcH8               0.5 mM '[U-100% 13C; U-100% 15N]' 
      'sodium phosphate'  20   mM 'natural abundance'        
       EDTA                1   mM 'natural abundance'        
       DTT                 1   mM 'natural abundance'        
      'sodium chloride'  150   mM 'natural abundance'        
       Arginine           50   mM 'natural abundance'        
      'Glutamic Acid'     50   mM 'natural abundance'        
       H2O                90   %  'natural abundance'        
       D2O                10   %  'natural abundance'        

   stop_

save_


############################
#  Computer software used  #
############################

save_NMRView
   _Saveframe_category   software

   _Name                 NMRView
   _Version              .

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Johnson, One Moon Scientific' . . 

   stop_

   loop_
      _Task

      'chemical shift assignment' 

   stop_

   _Details              .

save_


save_NMRPipe
   _Saveframe_category   software

   _Name                 NMRPipe
   _Version              .

   loop_
      _Vendor
      _Address
      _Electronic_address

      'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 

   stop_

   loop_
      _Task

      processing 

   stop_

   _Details              .

save_


save_VNMRJ
   _Saveframe_category   software

   _Name                 VNMRJ
   _Version              2.1B

   loop_
      _Vendor
      _Address
      _Electronic_address

      Varian . . 

   stop_

   loop_
      _Task

      collection 

   stop_

   _Details              .

save_


#########################
#  Experimental detail  #
#########################

    ##################################
    #  NMR Spectrometer definitions  #
    ##################################

save_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Varian
   _Model                INOVA
   _Field_strength       600
   _Details              .

save_


    #############################
    #  NMR applied experiments  #
    #############################

save_2D_1H-15N_HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-15N HSQC'
   _Sample_label        $sample_UbcH8

save_


save_3D_CBCA(CO)NH_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D CBCA(CO)NH'
   _Sample_label        $sample_UbcH8

save_


save_3D_HNCACB_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCACB'
   _Sample_label        $sample_UbcH8

save_


save_3D_HNCO_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCO'
   _Sample_label        $sample_UbcH8

save_


save_3D_C(CO)NH_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D C(CO)NH'
   _Sample_label        $sample_UbcH8

save_


save_3D_H(CCO)NH_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D H(CCO)NH'
   _Sample_label        $sample_UbcH8

save_


#######################
#  Sample conditions  #
#######################

save_sample_conditions_for_UbcH8
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      'ionic strength' 150   . mM  
       pH                7.4 . pH  
       pressure          1   . atm 
       temperature     298   . K   

   stop_

save_


####################
#  NMR parameters  #
####################

    ##############################
    #  Assigned chemical shifts  #
    ##############################

	################################
	#  Chemical shift referencing  #
	################################

save_Chemical_Shift_Reference_for_UbcH8
   _Saveframe_category   chemical_shift_reference

   _Details              .

   loop_
      _Mol_common_name
      _Atom_type
      _Atom_isotope_number
      _Atom_group
      _Chem_shift_units
      _Chem_shift_value
      _Reference_method
      _Reference_type
      _External_reference_sample_geometry
      _External_reference_location
      _External_reference_axis
      _Indirect_shift_ratio

      DSS C 13 'methyl protons' ppm 0.00 .        indirect . . . 0.251449530 
      DSS H  1 'methyl protons' ppm 0.00 internal direct   . . . 1.000000000 
      DSS N 15 'methyl protons' ppm 0.00 .        indirect . . . 0.101329118 

   stop_

save_


	###################################
	#  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_for_UbcH8
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Software_label

      $NMRView 

   stop_

   loop_
      _Experiment_label

      '2D 1H-15N HSQC' 
      '3D CBCA(CO)NH'  
      '3D HNCACB'      
      '3D HNCO'        
      '3D C(CO)NH'     
      '3D H(CCO)NH'    

   stop_

   loop_
      _Sample_label

      $sample_UbcH8 

   stop_

   _Sample_conditions_label         $sample_conditions_for_UbcH8
   _Chem_shift_reference_set_label  $Chemical_Shift_Reference_for_UbcH8
   _Mol_system_component_name        UbcH8
   _Text_data_format                 .
   _Text_data                        .

   loop_
      _Atom_shift_assign_ID
      _Residue_author_seq_code
      _Residue_seq_code
      _Residue_label
      _Atom_name
      _Atom_type
      _Chem_shift_value
      _Chem_shift_value_error
      _Chem_shift_ambiguity_code

        1   1   1 MET HA   H   4.419 . 1 
        2   1   1 MET HB2  H   2.608 . 2 
        3   1   1 MET C    C 177.128 . 1 
        4   1   1 MET CA   C  56.828 . 1 
        5   1   1 MET CB   C  32.757 . 1 
        6   2   2 ALA H    H   8.730 . 1 
        7   2   2 ALA HB   H   1.607 . 1 
        8   2   2 ALA C    C 178.821 . 1 
        9   2   2 ALA CA   C  54.930 . 1 
       10   2   2 ALA CB   C  19.897 . 1 
       11   2   2 ALA N    N 125.200 . 1 
       12   3   3 SER H    H   8.246 . 1 
       13   3   3 SER HB2  H   4.017 . 2 
       14   3   3 SER C    C 176.498 . 1 
       15   3   3 SER CA   C  61.192 . 1 
       16   3   3 SER CB   C  62.575 . 1 
       17   3   3 SER N    N 111.876 . 1 
       18   4   4 MET H    H   8.835 . 1 
       19   4   4 MET CA   C  58.720 . 1 
       20   4   4 MET CB   C  29.478 . 1 
       21   4   4 MET N    N 118.609 . 1 
       22   5   5 ARG HA   H   4.221 . 1 
       23   5   5 ARG HD2  H   2.921 . 2 
       24   5   5 ARG C    C 177.998 . 1 
       25   5   5 ARG CA   C  58.854 . 1 
       26   5   5 ARG CB   C  31.927 . 1 
       27   6   6 VAL H    H   8.175 . 1 
       28   6   6 VAL HA   H   3.350 . 1 
       29   6   6 VAL HB   H   1.886 . 1 
       30   6   6 VAL HG1  H   1.101 . 4 
       31   6   6 VAL C    C 177.686 . 1 
       32   6   6 VAL CA   C  67.276 . 1 
       33   6   6 VAL CG1  C  22.243 . 2 
       34   6   6 VAL N    N 118.972 . 1 
       35   7   7 VAL H    H   8.011 . 1 
       36   7   7 VAL HA   H   3.695 . 1 
       37   7   7 VAL HG1  H   1.039 . 4 
       38   7   7 VAL C    C 178.005 . 1 
       39   7   7 VAL CA   C  66.775 . 1 
       40   7   7 VAL CB   C  31.938 . 1 
       41   7   7 VAL CG1  C  23.227 . 2 
       42   7   7 VAL CG2  C  21.182 . 2 
       43   7   7 VAL N    N 118.082 . 1 
       44   8   8 LYS H    H   7.348 . 1 
       45   8   8 LYS HA   H   4.196 . 1 
       46   8   8 LYS C    C 178.842 . 1 
       47   8   8 LYS CA   C  58.710 . 1 
       48   8   8 LYS CB   C  32.080 . 1 
       49   8   8 LYS N    N 120.115 . 1 
       50   9   9 GLU H    H   8.424 . 1 
       51   9   9 GLU HA   H   4.183 . 1 
       52   9   9 GLU C    C 179.794 . 1 
       53   9   9 GLU CA   C  60.521 . 1 
       54   9   9 GLU CB   C  30.790 . 1 
       55   9   9 GLU N    N 118.525 . 1 
       56  10  10 LEU H    H   8.542 . 1 
       57  10  10 LEU HA   H   3.931 . 1 
       58  10  10 LEU HB2  H   1.297 . 2 
       59  10  10 LEU C    C 177.922 . 1 
       60  10  10 LEU CA   C  57.776 . 1 
       61  10  10 LEU CB   C  40.075 . 1 
       62  10  10 LEU N    N 121.165 . 1 
       63  11  11 GLU H    H   8.105 . 1 
       64  11  11 GLU HB2  H   2.157 . 2 
       65  11  11 GLU HB3  H   2.506 . 2 
       66  11  11 GLU C    C 179.568 . 1 
       67  11  11 GLU CA   C  59.540 . 1 
       68  11  11 GLU CB   C  29.693 . 1 
       69  11  11 GLU N    N 118.478 . 1 
       70  12  12 ASP H    H   8.097 . 1 
       71  12  12 ASP HB2  H   2.775 . 2 
       72  12  12 ASP C    C 179.292 . 1 
       73  12  12 ASP CA   C  57.582 . 1 
       74  12  12 ASP CB   C  40.676 . 1 
       75  12  12 ASP N    N 118.478 . 1 
       76  13  13 LEU H    H   7.663 . 1 
       77  13  13 LEU HB2  H   1.767 . 2 
       78  13  13 LEU HD1  H   0.924 . 4 
       79  13  13 LEU HD2  H   1.121 . 4 
       80  13  13 LEU C    C 177.864 . 1 
       81  13  13 LEU CA   C  57.601 . 1 
       82  13  13 LEU CB   C  43.248 . 1 
       83  13  13 LEU CD1  C  24.400 . 2 
       84  13  13 LEU N    N 121.381 . 1 
       85  14  14 GLN H    H   8.351 . 1 
       86  14  14 GLN HA   H   3.863 . 1 
       87  14  14 GLN HB2  H   1.993 . 2 
       88  14  14 GLN HE21 H   7.767 . 2 
       89  14  14 GLN HE22 H   6.845 . 2 
       90  14  14 GLN C    C 179.003 . 1 
       91  14  14 GLN CA   C  58.289 . 1 
       92  14  14 GLN CB   C  28.920 . 1 
       93  14  14 GLN CG   C  34.814 . 1 
       94  14  14 GLN N    N 114.554 . 1 
       95  14  14 GLN NE2  N 111.048 . 1 
       96  15  15 LYS H    H   7.718 . 1 
       97  15  15 LYS HA   H   4.089 . 1 
       98  15  15 LYS HD2  H   1.674 . 2 
       99  15  15 LYS C    C 177.237 . 1 
      100  15  15 LYS CA   C  58.385 . 1 
      101  15  15 LYS CB   C  33.226 . 1 
      102  15  15 LYS N    N 117.534 . 1 
      103  16  16 LYS H    H   7.161 . 1 
      104  16  16 LYS CA   C  53.599 . 1 
      105  16  16 LYS CB   C  32.912 . 1 
      106  16  16 LYS N    N 117.931 . 1 
      107  19  19 PRO HB2  H   2.152 . 2 
      108  19  19 PRO C    C 176.222 . 1 
      109  19  19 PRO CA   C  64.837 . 1 
      110  19  19 PRO CB   C  31.814 . 1 
      111  20  20 TYR H    H   5.947 . 1 
      112  20  20 TYR HB2  H   2.849 . 2 
      113  20  20 TYR HB3  H   3.529 . 2 
      114  20  20 TYR C    C 173.746 . 1 
      115  20  20 TYR CA   C  54.887 . 1 
      116  20  20 TYR CB   C  37.785 . 1 
      117  20  20 TYR N    N 108.910 . 1 
      118  21  21 LEU H    H   7.369 . 1 
      119  21  21 LEU HB2  H   1.175 . 2 
      120  21  21 LEU HB3  H   1.490 . 2 
      121  21  21 LEU HD1  H   0.865 . 4 
      122  21  21 LEU C    C 176.387 . 1 
      123  21  21 LEU CA   C  53.205 . 1 
      124  21  21 LEU CB   C  46.989 . 1 
      125  21  21 LEU CD1  C  25.692 . 2 
      126  21  21 LEU N    N 123.178 . 1 
      127  22  22 ARG H    H   9.107 . 1 
      128  22  22 ARG HA   H   4.758 . 1 
      129  22  22 ARG C    C 174.523 . 1 
      130  22  22 ARG CA   C  52.812 . 1 
      131  22  22 ARG CB   C  34.308 . 1 
      132  22  22 ARG N    N 120.573 . 1 
      133  23  23 ASN H    H   9.001 . 1 
      134  23  23 ASN HB2  H   2.784 . 2 
      135  23  23 ASN HB3  H   2.984 . 2 
      136  23  23 ASN HD21 H   7.344 . 2 
      137  23  23 ASN HD22 H   6.839 . 2 
      138  23  23 ASN C    C 174.206 . 1 
      139  23  23 ASN CA   C  53.232 . 1 
      140  23  23 ASN CB   C  36.387 . 1 
      141  23  23 ASN N    N 116.352 . 1 
      142  23  23 ASN ND2  N 110.516 . 1 
      143  24  24 LEU H    H   7.975 . 1 
      144  24  24 LEU HA   H   4.939 . 1 
      145  24  24 LEU HB2  H   1.597 . 2 
      146  24  24 LEU HD1  H   0.558 . 4 
      147  24  24 LEU HD2  H   0.709 . 4 
      148  24  24 LEU C    C 177.358 . 1 
      149  24  24 LEU CA   C  55.709 . 1 
      150  24  24 LEU CB   C  41.916 . 1 
      151  24  24 LEU CD1  C  23.741 . 2 
      152  24  24 LEU CG   C  27.457 . 1 
      153  24  24 LEU N    N 119.619 . 1 
      154  25  25 SER H    H   9.163 . 1 
      155  25  25 SER HB2  H   3.743 . 2 
      156  25  25 SER C    C 172.467 . 1 
      157  25  25 SER CA   C  57.493 . 1 
      158  25  25 SER CB   C  65.969 . 1 
      159  25  25 SER N    N 122.243 . 1 
      160  26  26 SER H    H   8.397 . 1 
      161  26  26 SER HB2  H   3.832 . 2 
      162  26  26 SER C    C 175.213 . 1 
      163  26  26 SER CA   C  57.344 . 1 
      164  26  26 SER CB   C  65.505 . 1 
      165  26  26 SER N    N 115.593 . 1 
      166  27  27 ASP H    H   8.706 . 1 
      167  27  27 ASP HA   H   4.684 . 1 
      168  27  27 ASP HB2  H   2.591 . 2 
      169  27  27 ASP HB3  H   3.257 . 2 
      170  27  27 ASP CA   C  54.611 . 1 
      171  27  27 ASP CB   C  42.390 . 1 
      172  27  27 ASP N    N 124.439 . 1 
      173  28  28 ASP H    H   8.718 . 1 
      174  28  28 ASP HB2  H   2.677 . 2 
      175  28  28 ASP C    C 176.501 . 1 
      176  28  28 ASP CA   C  56.846 . 1 
      177  28  28 ASP CB   C  41.012 . 1 
      178  28  28 ASP N    N 125.173 . 1 
      179  29  29 ALA H    H   8.583 . 1 
      180  29  29 ALA HB   H   1.409 . 1 
      181  29  29 ALA C    C 177.461 . 1 
      182  29  29 ALA CA   C  52.411 . 1 
      183  29  29 ALA CB   C  19.572 . 1 
      184  29  29 ALA N    N 120.876 . 1 
      185  30  30 ASN H    H   7.765 . 1 
      186  30  30 ASN HA   H   4.805 . 1 
      187  30  30 ASN C    C 174.196 . 1 
      188  30  30 ASN CA   C  52.557 . 1 
      189  30  30 ASN CB   C  38.940 . 1 
      190  30  30 ASN N    N 116.583 . 1 
      191  31  31 VAL H    H   8.277 . 1 
      192  31  31 VAL HB   H   2.260 . 1 
      193  31  31 VAL HG1  H   1.020 . 4 
      194  31  31 VAL C    C 174.011 . 1 
      195  31  31 VAL CA   C  62.710 . 1 
      196  31  31 VAL CB   C  31.838 . 1 
      197  31  31 VAL CG1  C  20.592 . 2 
      198  31  31 VAL N    N 120.548 . 1 
      199  32  32 LEU H    H   7.656 . 1 
      200  32  32 LEU HA   H   4.334 . 1 
      201  32  32 LEU HD1  H   0.637 . 4 
      202  32  32 LEU HD2  H   0.923 . 4 
      203  32  32 LEU C    C 175.549 . 1 
      204  32  32 LEU CA   C  54.560 . 1 
      205  32  32 LEU CB   C  39.540 . 1 
      206  32  32 LEU CD1  C  25.202 . 2 
      207  32  32 LEU N    N 114.488 . 1 
      208  33  33 VAL H    H   7.654 . 1 
      209  33  33 VAL C    C 174.559 . 1 
      210  33  33 VAL CA   C  61.826 . 1 
      211  33  33 VAL CB   C  34.873 . 1 
      212  33  33 VAL CG1  C  21.758 . 2 
      213  33  33 VAL N    N 120.018 . 1 
      214  34  34 TRP H    H   9.663 . 1 
      215  34  34 TRP C    C 175.495 . 1 
      216  34  34 TRP CA   C  52.669 . 1 
      217  34  34 TRP CB   C  33.494 . 1 
      218  34  34 TRP N    N 125.372 . 1 
      219  35  35 HIS H    H   9.076 . 1 
      220  35  35 HIS HB2  H   2.993 . 2 
      221  35  35 HIS C    C 173.706 . 1 
      222  35  35 HIS CA   C  54.399 . 1 
      223  35  35 HIS CB   C  33.034 . 1 
      224  35  35 HIS N    N 118.149 . 1 
      225  36  36 ALA H    H   8.241 . 1 
      226  36  36 ALA HB   H   1.317 . 1 
      227  36  36 ALA C    C 174.123 . 1 
      228  36  36 ALA CA   C  51.659 . 1 
      229  36  36 ALA CB   C  23.549 . 1 
      230  36  36 ALA N    N 118.864 . 1 
      231  37  37 LEU H    H   8.718 . 1 
      232  37  37 LEU HD1  H   0.737 . 4 
      233  37  37 LEU HD2  H   1.478 . 4 
      234  37  37 LEU C    C 174.719 . 1 
      235  37  37 LEU CA   C  53.832 . 1 
      236  37  37 LEU CB   C  45.085 . 1 
      237  37  37 LEU CD1  C  24.879 . 2 
      238  37  37 LEU N    N 119.331 . 1 
      239  38  38 LEU H    H   9.512 . 1 
      240  38  38 LEU HB2  H   1.848 . 2 
      241  38  38 LEU HD1  H   0.553 . 4 
      242  38  38 LEU C    C 176.536 . 1 
      243  38  38 LEU CA   C  53.767 . 1 
      244  38  38 LEU CB   C  45.118 . 1 
      245  38  38 LEU CD1  C  27.396 . 2 
      246  38  38 LEU N    N 125.138 . 1 
      247  39  39 LEU H    H   9.405 . 1 
      248  39  39 LEU CA   C  53.885 . 1 
      249  39  39 LEU N    N 130.234 . 1 
      250  40  40 PRO C    C 176.379 . 1 
      251  40  40 PRO CA   C  63.217 . 1 
      252  40  40 PRO CB   C  33.430 . 1 
      253  41  41 ASP H    H   9.023 . 1 
      254  41  41 ASP HA   H   5.155 . 1 
      255  41  41 ASP HB2  H   2.718 . 2 
      256  41  41 ASP HB3  H   2.869 . 2 
      257  41  41 ASP C    C 176.154 . 1 
      258  41  41 ASP CA   C  53.973 . 1 
      259  41  41 ASP CB   C  43.363 . 1 
      260  41  41 ASP N    N 120.417 . 1 
      261  42  42 GLN H    H   7.683 . 1 
      262  42  42 GLN CA   C  52.444 . 1 
      263  42  42 GLN CB   C  30.387 . 1 
      264  42  42 GLN N    N 120.276 . 1 
      265  44  44 PRO C    C 174.771 . 1 
      266  44  44 PRO CA   C  64.389 . 1 
      267  44  44 PRO CB   C  33.900 . 1 
      268  45  45 TYR H    H   7.812 . 1 
      269  45  45 TYR HB2  H   2.894 . 2 
      270  45  45 TYR HB3  H   3.373 . 2 
      271  45  45 TYR C    C 174.822 . 1 
      272  45  45 TYR CA   C  59.808 . 1 
      273  45  45 TYR CB   C  38.217 . 1 
      274  45  45 TYR N    N 123.010 . 1 
      275  46  46 HIS H    H   8.278 . 1 
      276  46  46 HIS HB2  H   3.682 . 2 
      277  46  46 HIS C    C 175.556 . 1 
      278  46  46 HIS CA   C  56.843 . 1 
      279  46  46 HIS CB   C  30.299 . 1 
      280  46  46 HIS N    N 114.221 . 1 
      281  47  47 LEU H    H   7.306 . 1 
      282  47  47 LEU HG   H   1.367 . 1 
      283  47  47 LEU C    C 178.426 . 1 
      284  47  47 LEU CA   C  56.130 . 1 
      285  47  47 LEU CB   C  43.600 . 1 
      286  47  47 LEU CG   C  25.452 . 1 
      287  47  47 LEU N    N 119.228 . 1 
      288  48  48 LYS H    H   7.610 . 1 
      289  48  48 LYS HD2  H   0.828 . 2 
      290  48  48 LYS HG2  H   1.466 . 2 
      291  48  48 LYS C    C 171.987 . 1 
      292  48  48 LYS CA   C  53.031 . 1 
      293  48  48 LYS CB   C  37.156 . 1 
      294  48  48 LYS N    N 115.857 . 1 
      295  49  49 ALA H    H   9.106 . 1 
      296  49  49 ALA HB   H   1.209 . 1 
      297  49  49 ALA C    C 174.804 . 1 
      298  49  49 ALA CA   C  49.926 . 1 
      299  49  49 ALA CB   C  23.545 . 1 
      300  49  49 ALA N    N 121.160 . 1 
      301  50  50 PHE H    H   8.544 . 1 
      302  50  50 PHE HB2  H   2.881 . 2 
      303  50  50 PHE HB3  H   3.176 . 2 
      304  50  50 PHE C    C 174.544 . 1 
      305  50  50 PHE CA   C  57.529 . 1 
      306  50  50 PHE CB   C  44.048 . 1 
      307  50  50 PHE N    N 114.451 . 1 
      308  51  51 ASN H    H   9.529 . 1 
      309  51  51 ASN HA   H   5.246 . 1 
      310  51  51 ASN HB2  H   2.745 . 2 
      311  51  51 ASN C    C 174.647 . 1 
      312  51  51 ASN CA   C  54.883 . 1 
      313  51  51 ASN CB   C  40.257 . 1 
      314  51  51 ASN N    N 122.966 . 1 
      315  52  52 LEU H    H   9.280 . 1 
      316  52  52 LEU HA   H   5.029 . 1 
      317  52  52 LEU HB2  H   1.030 . 2 
      318  52  52 LEU HD1  H   0.087 . 4 
      319  52  52 LEU C    C 175.657 . 1 
      320  52  52 LEU CA   C  53.479 . 1 
      321  52  52 LEU CB   C  46.556 . 1 
      322  52  52 LEU CD1  C  24.306 . 2 
      323  52  52 LEU CG   C  25.879 . 1 
      324  52  52 LEU N    N 121.904 . 1 
      325  53  53 ARG H    H   9.008 . 1 
      326  53  53 ARG HD2  H   3.073 . 2 
      327  53  53 ARG C    C 174.929 . 1 
      328  53  53 ARG CA   C  55.018 . 1 
      329  53  53 ARG CB   C  33.980 . 1 
      330  53  53 ARG N    N 122.756 . 1 
      331  54  54 ILE H    H   9.080 . 1 
      332  54  54 ILE HG12 H   1.392 . 9 
      333  54  54 ILE HG2  H  -0.089 . 4 
      334  54  54 ILE C    C 173.329 . 1 
      335  54  54 ILE CA   C  60.101 . 1 
      336  54  54 ILE CB   C  40.159 . 1 
      337  54  54 ILE CD1  C  14.921 . 1 
      338  54  54 ILE CG1  C  27.911 . 1 
      339  54  54 ILE CG2  C  17.620 . 1 
      340  54  54 ILE N    N 129.706 . 1 
      341  55  55 SER H    H   8.852 . 1 
      342  55  55 SER HB2  H   3.565 . 2 
      343  55  55 SER C    C 172.862 . 1 
      344  55  55 SER CA   C  55.777 . 1 
      345  55  55 SER CB   C  64.868 . 1 
      346  55  55 SER N    N 119.778 . 1 
      347  56  56 PHE H    H   8.924 . 1 
      348  56  56 PHE CA   C  55.490 . 1 
      349  56  56 PHE CB   C  39.520 . 1 
      350  56  56 PHE N    N 124.903 . 1 
      351  58  58 PRO HB2  H   2.169 . 2 
      352  58  58 PRO C    C 177.616 . 1 
      353  58  58 PRO CA   C  65.012 . 1 
      354  58  58 PRO CB   C  31.588 . 1 
      355  59  59 GLU H    H   8.478 . 1 
      356  59  59 GLU HA   H   4.361 . 1 
      357  59  59 GLU C    C 176.831 . 1 
      358  59  59 GLU CA   C  57.112 . 1 
      359  59  59 GLU CB   C  29.446 . 1 
      360  59  59 GLU N    N 112.148 . 1 
      361  60  60 TYR H    H   8.231 . 1 
      362  60  60 TYR CA   C  58.057 . 1 
      363  60  60 TYR CB   C  39.461 . 1 
      364  60  60 TYR N    N 123.770 . 1 
      365  61  61 PRO C    C 175.039 . 1 
      366  61  61 PRO CA   C  63.786 . 1 
      367  61  61 PRO CB   C  33.074 . 1 
      368  62  62 PHE H    H   9.349 . 1 
      369  62  62 PHE HB2  H   3.119 . 2 
      370  62  62 PHE HB3  H   3.387 . 2 
      371  62  62 PHE C    C 175.710 . 1 
      372  62  62 PHE CA   C  60.739 . 1 
      373  62  62 PHE CB   C  38.054 . 1 
      374  62  62 PHE N    N 125.952 . 1 
      375  63  63 LYS H    H   7.055 . 1 
      376  63  63 LYS CA   C  52.935 . 1 
      377  63  63 LYS CB   C  35.896 . 1 
      378  63  63 LYS N    N 117.679 . 1 
      379  65  65 PRO HA   H   4.230 . 1 
      380  65  65 PRO C    C 174.298 . 1 
      381  65  65 PRO CA   C  61.621 . 1 
      382  65  65 PRO CB   C  31.843 . 1 
      383  66  66 MET H    H   8.325 . 1 
      384  66  66 MET HA   H   4.475 . 1 
      385  66  66 MET HB2  H   2.343 . 2 
      386  66  66 MET C    C 174.788 . 1 
      387  66  66 MET CA   C  54.182 . 1 
      388  66  66 MET CB   C  34.803 . 1 
      389  66  66 MET N    N 117.327 . 1 
      390  67  67 ILE H    H   8.316 . 1 
      391  67  67 ILE HA   H   4.699 . 1 
      392  67  67 ILE HG12 H   1.202 . 9 
      393  67  67 ILE HG2  H   0.464 . 4 
      394  67  67 ILE C    C 173.257 . 1 
      395  67  67 ILE CA   C  59.865 . 1 
      396  67  67 ILE CB   C  40.573 . 1 
      397  67  67 ILE CD1  C  13.913 . 1 
      398  67  67 ILE CG1  C  27.488 . 1 
      399  67  67 ILE CG2  C  17.178 . 1 
      400  67  67 ILE N    N 123.247 . 1 
      401  68  68 LYS H    H   8.439 . 1 
      402  68  68 LYS HB2  H   1.570 . 2 
      403  68  68 LYS HG2  H   1.271 . 2 
      404  68  68 LYS C    C 175.759 . 1 
      405  68  68 LYS CA   C  54.387 . 1 
      406  68  68 LYS CB   C  36.793 . 1 
      407  68  68 LYS N    N 123.834 . 1 
      408  69  69 PHE H    H   9.576 . 1 
      409  69  69 PHE HB2  H   2.974 . 2 
      410  69  69 PHE HB3  H   3.586 . 2 
      411  69  69 PHE C    C 177.410 . 1 
      412  69  69 PHE CA   C  59.213 . 1 
      413  69  69 PHE CB   C  39.957 . 1 
      414  69  69 PHE N    N 122.830 . 1 
      415  70  70 THR H    H   8.932 . 1 
      416  70  70 THR HA   H   4.481 . 1 
      417  70  70 THR HG2  H   1.117 . 1 
      418  70  70 THR C    C 175.453 . 1 
      419  70  70 THR CA   C  61.980 . 1 
      420  70  70 THR CB   C  67.365 . 1 
      421  70  70 THR N    N 114.574 . 1 
      422  71  71 THR H    H   7.494 . 1 
      423  71  71 THR HB   H   3.757 . 1 
      424  71  71 THR C    C 173.984 . 1 
      425  71  71 THR CA   C  62.088 . 1 
      426  71  71 THR CB   C  71.269 . 1 
      427  71  71 THR N    N 121.982 . 1 
      428  72  72 LYS H    H   8.853 . 1 
      429  72  72 LYS HA   H   4.222 . 1 
      430  72  72 LYS HG2  H   1.335 . 2 
      431  72  72 LYS C    C 174.993 . 1 
      432  72  72 LYS CA   C  58.020 . 1 
      433  72  72 LYS CB   C  33.097 . 1 
      434  72  72 LYS N    N 126.631 . 1 
      435  73  73 ILE H    H   7.975 . 1 
      436  73  73 ILE C    C 171.675 . 1 
      437  73  73 ILE CA   C  59.501 . 1 
      438  73  73 ILE CB   C  41.168 . 1 
      439  73  73 ILE N    N 119.643 . 1 
      440  74  74 TYR H    H   8.634 . 1 
      441  74  74 TYR HB2  H   3.140 . 2 
      442  74  74 TYR C    C 172.534 . 1 
      443  74  74 TYR CA   C  57.135 . 1 
      444  74  74 TYR CB   C  37.969 . 1 
      445  74  74 TYR N    N 132.209 . 1 
      446  75  75 HIS H    H   8.947 . 1 
      447  75  75 HIS CA   C  55.224 . 1 
      448  75  75 HIS CB   C  36.270 . 1 
      449  75  75 HIS N    N 129.199 . 1 
      450  76  76 PRO HA   H   4.317 . 1 
      451  76  76 PRO HG2  H   1.578 . 2 
      452  76  76 PRO C    C 176.948 . 1 
      453  76  76 PRO CA   C  64.660 . 1 
      454  76  76 PRO CB   C  32.231 . 1 
      455  77  77 ASN H    H  11.483 . 1 
      456  77  77 ASN HB2  H   2.415 . 2 
      457  77  77 ASN HB3  H   3.389 . 2 
      458  77  77 ASN C    C 170.889 . 1 
      459  77  77 ASN CA   C  54.688 . 1 
      460  77  77 ASN CB   C  40.756 . 1 
      461  77  77 ASN N    N 118.947 . 1 
      462  78  78 VAL H    H   7.498 . 1 
      463  78  78 VAL HA   H   3.560 . 1 
      464  78  78 VAL C    C 175.930 . 1 
      465  78  78 VAL CA   C  60.590 . 1 
      466  78  78 VAL CB   C  35.341 . 1 
      467  78  78 VAL CG1  C  20.402 . 2 
      468  78  78 VAL N    N 119.348 . 1 
      469  79  79 ASP H    H   8.917 . 1 
      470  79  79 ASP HB2  H   2.594 . 2 
      471  79  79 ASP C    C 177.944 . 1 
      472  79  79 ASP CA   C  53.058 . 1 
      473  79  79 ASP CB   C  41.280 . 1 
      474  79  79 ASP N    N 125.634 . 1 
      475  80  80 GLU H    H   9.251 . 1 
      476  80  80 GLU HA   H   4.115 . 1 
      477  80  80 GLU HB2  H   2.206 . 2 
      478  80  80 GLU C    C 176.578 . 1 
      479  80  80 GLU CA   C  59.347 . 1 
      480  80  80 GLU CB   C  29.804 . 1 
      481  80  80 GLU N    N 117.232 . 1 
      482  81  81 ASN H    H   8.395 . 1 
      483  81  81 ASN HA   H   4.884 . 1 
      484  81  81 ASN HB2  H   2.908 . 2 
      485  81  81 ASN HD21 H   7.825 . 2 
      486  81  81 ASN HD22 H   6.988 . 2 
      487  81  81 ASN C    C 175.380 . 1 
      488  81  81 ASN CA   C  52.992 . 1 
      489  81  81 ASN CB   C  39.648 . 1 
      490  81  81 ASN N    N 116.375 . 1 
      491  81  81 ASN ND2  N 114.650 . 1 
      492  82  82 GLY H    H   8.141 . 1 
      493  82  82 GLY HA2  H   3.636 . 2 
      494  82  82 GLY HA3  H   4.791 . 2 
      495  82  82 GLY C    C 174.357 . 1 
      496  82  82 GLY CA   C  46.402 . 1 
      497  82  82 GLY N    N 108.824 . 1 
      498  83  83 GLN H    H   8.413 . 1 
      499  83  83 GLN HA   H   4.498 . 1 
      500  83  83 GLN HE21 H   7.599 . 2 
      501  83  83 GLN HE22 H   6.898 . 2 
      502  83  83 GLN HG2  H   2.432 . 2 
      503  83  83 GLN C    C 174.582 . 1 
      504  83  83 GLN CA   C  55.808 . 1 
      505  83  83 GLN CB   C  28.917 . 1 
      506  83  83 GLN CG   C  33.139 . 1 
      507  83  83 GLN N    N 119.859 . 1 
      508  83  83 GLN NE2  N 113.983 . 1 
      509  84  84 ILE H    H   8.433 . 1 
      510  84  84 ILE HB   H   1.600 . 1 
      511  84  84 ILE HG2  H   0.895 . 4 
      512  84  84 ILE C    C 175.349 . 1 
      513  84  84 ILE CA   C  59.455 . 1 
      514  84  84 ILE CB   C  42.546 . 1 
      515  84  84 ILE CD1  C  15.165 . 1 
      516  84  84 ILE CG1  C  26.793 . 1 
      517  84  84 ILE CG2  C  18.002 . 1 
      518  84  84 ILE N    N 116.337 . 1 
      519  85  85 CYS H    H   8.612 . 1 
      520  85  85 CYS HB2  H   2.769 . 2 
      521  85  85 CYS C    C 172.522 . 1 
      522  85  85 CYS CA   C  57.647 . 1 
      523  85  85 CYS CB   C  27.025 . 1 
      524  85  85 CYS N    N 125.657 . 1 
      525  86  86 LEU H    H   7.801 . 1 
      526  86  86 LEU CA   C  51.336 . 1 
      527  86  86 LEU CB   C  44.838 . 1 
      528  86  86 LEU N    N 126.780 . 1 
      529  87  87 PRO C    C 179.201 . 1 
      530  87  87 PRO CA   C  66.514 . 1 
      531  87  87 PRO CB   C  31.611 . 1 
      532  88  88 ILE H    H   8.053 . 1 
      533  88  88 ILE HA   H   4.212 . 1 
      534  88  88 ILE HG12 H   1.045 . 9 
      535  88  88 ILE C    C 174.631 . 1 
      536  88  88 ILE CA   C  64.303 . 1 
      537  88  88 ILE CB   C  38.090 . 1 
      538  88  88 ILE CD1  C  14.028 . 1 
      539  88  88 ILE N    N 115.417 . 1 
      540  89  89 ILE H    H   7.340 . 1 
      541  89  89 ILE HG2  H   0.934 . 4 
      542  89  89 ILE C    C 175.187 . 1 
      543  89  89 ILE CA   C  60.521 . 1 
      544  89  89 ILE CB   C  37.416 . 1 
      545  89  89 ILE CG2  C  20.674 . 1 
      546  89  89 ILE N    N 108.236 . 1 
      547  90  90 SER H    H   7.884 . 1 
      548  90  90 SER C    C 176.779 . 1 
      549  90  90 SER CA   C  58.283 . 1 
      550  90  90 SER CB   C  64.260 . 1 
      551  90  90 SER N    N 118.491 . 1 
      552  91  91 SER H    H  10.075 . 1 
      553  91  91 SER HB2  H   4.015 . 2 
      554  91  91 SER C    C 177.169 . 1 
      555  91  91 SER CA   C  61.454 . 1 
      556  91  91 SER N    N 118.314 . 1 
      557  92  92 GLU H    H   7.402 . 1 
      558  92  92 GLU HA   H   4.200 . 1 
      559  92  92 GLU HG2  H   2.265 . 2 
      560  92  92 GLU C    C 176.882 . 1 
      561  92  92 GLU CA   C  58.678 . 1 
      562  92  92 GLU CB   C  29.360 . 1 
      563  92  92 GLU N    N 122.653 . 1 
      564  93  93 ASN H    H   7.482 . 1 
      565  93  93 ASN HA   H   4.884 . 1 
      566  93  93 ASN HB2  H   2.810 . 2 
      567  93  93 ASN HB3  H   2.962 . 2 
      568  93  93 ASN C    C 176.072 . 1 
      569  93  93 ASN CA   C  53.051 . 1 
      570  93  93 ASN CB   C  40.559 . 1 
      571  93  93 ASN N    N 114.709 . 1 
      572  94  94 TRP H    H   8.129 . 1 
      573  94  94 TRP HB2  H   3.148 . 2 
      574  94  94 TRP C    C 175.258 . 1 
      575  94  94 TRP CA   C  58.537 . 1 
      576  94  94 TRP CB   C  29.809 . 1 
      577  94  94 TRP N    N 122.243 . 1 
      578  95  95 LYS H    H   6.439 . 1 
      579  95  95 LYS CA   C  52.006 . 1 
      580  95  95 LYS CB   C  34.504 . 1 
      581  95  95 LYS N    N 125.848 . 1 
      582  96  96 PRO HG2  H   1.684 . 2 
      583  96  96 PRO C    C 175.441 . 1 
      584  96  96 PRO CA   C  64.129 . 1 
      585  96  96 PRO CB   C  31.991 . 1 
      586  97  97 SER H    H   6.931 . 1 
      587  97  97 SER HB2  H   3.652 . 2 
      588  97  97 SER HB3  H   4.009 . 2 
      589  97  97 SER C    C 175.127 . 1 
      590  97  97 SER CA   C  57.955 . 1 
      591  97  97 SER CB   C  62.920 . 1 
      592  97  97 SER N    N 107.450 . 1 
      593  98  98 THR H    H   7.574 . 1 
      594  98  98 THR HG2  H   1.146 . 1 
      595  98  98 THR C    C 172.392 . 1 
      596  98  98 THR CA   C  63.952 . 1 
      597  98  98 THR CB   C  68.133 . 1 
      598  98  98 THR N    N 123.543 . 1 
      599  99  99 LYS H    H   8.326 . 1 
      600  99  99 LYS HB2  H   1.672 . 2 
      601  99  99 LYS C    C 178.874 . 1 
      602  99  99 LYS CA   C  54.833 . 1 
      603  99  99 LYS CB   C  33.974 . 1 
      604  99  99 LYS N    N 124.918 . 1 
      605 100 100 THR H    H   9.910 . 1 
      606 100 100 THR N    N 122.853 . 1 
      607 102 102 GLN HA   H   4.266 . 1 
      608 102 102 GLN HE21 H   7.766 . 2 
      609 102 102 GLN HE22 H   6.998 . 2 
      610 102 102 GLN HG2  H   2.363 . 2 
      611 102 102 GLN CB   C  29.313 . 1 
      612 102 102 GLN CG   C  35.221 . 1 
      613 102 102 GLN NE2  N 111.610 . 1 
      614 103 103 VAL H    H   7.720 . 1 
      615 103 103 VAL HA   H   3.567 . 1 
      616 103 103 VAL HG1  H   1.127 . 4 
      617 103 103 VAL C    C 177.325 . 1 
      618 103 103 VAL CA   C  66.523 . 1 
      619 103 103 VAL CB   C  31.741 . 1 
      620 103 103 VAL CG1  C  22.690 . 2 
      621 103 103 VAL N    N 122.593 . 1 
      622 104 104 LEU H    H   8.562 . 1 
      623 104 104 LEU C    C 177.935 . 1 
      624 104 104 LEU CA   C  57.723 . 1 
      625 104 104 LEU CB   C  41.608 . 1 
      626 104 104 LEU CD1  C  25.923 . 2 
      627 104 104 LEU N    N 118.134 . 1 
      628 105 105 GLU H    H   7.758 . 1 
      629 105 105 GLU HA   H   4.035 . 1 
      630 105 105 GLU HG2  H   2.360 . 2 
      631 105 105 GLU C    C 178.171 . 1 
      632 105 105 GLU CA   C  59.582 . 1 
      633 105 105 GLU CB   C  30.116 . 1 
      634 105 105 GLU N    N 120.177 . 1 
      635 106 106 ALA H    H   7.600 . 1 
      636 106 106 ALA HB   H   1.616 . 1 
      637 106 106 ALA C    C 180.607 . 1 
      638 106 106 ALA CA   C  54.880 . 1 
      639 106 106 ALA CB   C  18.166 . 1 
      640 106 106 ALA N    N 121.151 . 1 
      641 107 107 LEU H    H   8.383 . 1 
      642 107 107 LEU HD1  H   0.794 . 4 
      643 107 107 LEU C    C 176.559 . 1 
      644 107 107 LEU CA   C  57.921 . 1 
      645 107 107 LEU CB   C  41.603 . 1 
      646 107 107 LEU CD1  C  24.741 . 2 
      647 107 107 LEU CG   C  27.237 . 1 
      648 107 107 LEU N    N 121.104 . 1 
      649 108 108 ASN H    H   8.047 . 1 
      650 108 108 ASN HB2  H   2.368 . 2 
      651 108 108 ASN C    C 177.104 . 1 
      652 108 108 ASN CA   C  57.571 . 1 
      653 108 108 ASN CB   C  38.788 . 1 
      654 108 108 ASN N    N 117.770 . 1 
      655 109 109 VAL H    H   7.752 . 1 
      656 109 109 VAL HA   H   3.632 . 1 
      657 109 109 VAL HG1  H   1.019 . 4 
      658 109 109 VAL C    C 177.044 . 1 
      659 109 109 VAL CA   C  66.522 . 1 
      660 109 109 VAL CB   C  31.707 . 1 
      661 109 109 VAL CG1  C  23.182 . 2 
      662 109 109 VAL CG2  C  21.072 . 2 
      663 109 109 VAL N    N 117.480 . 1 
      664 110 110 LEU H    H   7.453 . 1 
      665 110 110 LEU HB2  H   1.894 . 2 
      666 110 110 LEU HD1  H   1.080 . 4 
      667 110 110 LEU C    C 178.179 . 1 
      668 110 110 LEU CA   C  56.991 . 1 
      669 110 110 LEU CB   C  42.782 . 1 
      670 110 110 LEU CG   C  26.848 . 1 
      671 110 110 LEU N    N 119.986 . 1 
      672 111 111 VAL H    H   8.126 . 1 
      673 111 111 VAL HB   H   2.998 . 1 
      674 111 111 VAL HG1  H   0.351 . 4 
      675 111 111 VAL HG2  H   0.551 . 4 
      676 111 111 VAL C    C 177.031 . 1 
      677 111 111 VAL CA   C  65.828 . 1 
      678 111 111 VAL CB   C  30.613 . 1 
      679 111 111 VAL CG1  C  23.537 . 2 
      680 111 111 VAL N    N 115.819 . 1 
      681 112 112 ASN H    H   7.265 . 1 
      682 112 112 ASN HA   H   4.585 . 1 
      683 112 112 ASN HB2  H   2.757 . 2 
      684 112 112 ASN HD21 H   7.178 . 2 
      685 112 112 ASN HD22 H   6.778 . 2 
      686 112 112 ASN C    C 175.432 . 1 
      687 112 112 ASN CA   C  55.573 . 1 
      688 112 112 ASN CB   C  40.280 . 1 
      689 112 112 ASN N    N 112.843 . 1 
      690 112 112 ASN ND2  N 112.455 . 1 
      691 113 113 ARG H    H   8.329 . 1 
      692 113 113 ARG CA   C  53.020 . 1 
      693 113 113 ARG CB   C  30.533 . 1 
      694 113 113 ARG N    N 121.241 . 1 
      695 114 114 PRO HA   H   4.502 . 1 
      696 114 114 PRO C    C 175.828 . 1 
      697 114 114 PRO CA   C  63.185 . 1 
      698 114 114 PRO CB   C  32.182 . 1 
      699 115 115 ASN H    H   8.843 . 1 
      700 115 115 ASN HB2  H   2.819 . 2 
      701 115 115 ASN HD21 H   7.650 . 2 
      702 115 115 ASN HD22 H   7.111 . 2 
      703 115 115 ASN C    C 176.748 . 1 
      704 115 115 ASN CA   C  51.382 . 1 
      705 115 115 ASN CB   C  39.226 . 1 
      706 115 115 ASN N    N 120.208 . 1 
      707 115 115 ASN ND2  N 111.962 . 1 
      708 116 116 ILE H    H   8.369 . 1 
      709 116 116 ILE HA   H   3.743 . 1 
      710 116 116 ILE HB   H   1.768 . 1 
      711 116 116 ILE HG12 H   1.223 . 9 
      712 116 116 ILE HG2  H   0.768 . 4 
      713 116 116 ILE C    C 175.492 . 1 
      714 116 116 ILE CA   C  62.185 . 1 
      715 116 116 ILE CB   C  37.625 . 1 
      716 116 116 ILE CD1  C  13.812 . 1 
      717 116 116 ILE CG1  C  26.439 . 1 
      718 116 116 ILE CG2  C  19.717 . 1 
      719 116 116 ILE N    N 118.323 . 1 
      720 117 117 ARG H    H   7.925 . 1 
      721 117 117 ARG HA   H   4.154 . 1 
      722 117 117 ARG HD2  H   3.197 . 2 
      723 117 117 ARG HG2  H   1.640 . 2 
      724 117 117 ARG C    C 176.861 . 1 
      725 117 117 ARG CA   C  57.406 . 1 
      726 117 117 ARG CB   C  30.156 . 1 
      727 117 117 ARG N    N 119.300 . 1 
      728 118 118 GLU H    H   6.933 . 1 
      729 118 118 GLU CA   C  53.666 . 1 
      730 118 118 GLU CB   C  30.216 . 1 
      731 118 118 GLU N    N 116.577 . 1 
      732 119 119 PRO HB2  H   1.750 . 2 
      733 119 119 PRO HG2  H   1.468 . 2 
      734 119 119 PRO C    C 176.476 . 1 
      735 119 119 PRO CA   C  63.071 . 1 
      736 120 120 LEU H    H   8.311 . 1 
      737 120 120 LEU HB2  H   1.385 . 2 
      738 120 120 LEU HD1  H   0.843 . 4 
      739 120 120 LEU C    C 177.480 . 1 
      740 120 120 LEU CA   C  55.685 . 1 
      741 120 120 LEU CB   C  44.083 . 1 
      742 120 120 LEU CD1  C  23.185 . 2 
      743 120 120 LEU CG   C  25.979 . 1 
      744 120 120 LEU N    N 117.768 . 1 
      745 121 121 ARG H    H   7.852 . 1 
      746 121 121 ARG C    C 176.137 . 1 
      747 121 121 ARG CA   C  54.781 . 1 
      748 121 121 ARG CB   C  31.421 . 1 
      749 121 121 ARG N    N 118.603 . 1 
      750 122 122 MET H    H   9.138 . 1 
      751 122 122 MET HA   H   3.939 . 1 
      752 122 122 MET HB2  H   2.604 . 2 
      753 122 122 MET C    C 177.212 . 1 
      754 122 122 MET CA   C  58.392 . 1 
      755 122 122 MET CB   C  31.874 . 1 
      756 122 122 MET N    N 125.881 . 1 
      757 123 123 ASP H    H   9.207 . 1 
      758 123 123 ASP HB2  H   2.562 . 2 
      759 123 123 ASP HB3  H   2.829 . 2 
      760 123 123 ASP C    C 179.451 . 1 
      761 123 123 ASP CA   C  56.025 . 1 
      762 123 123 ASP CB   C  37.583 . 1 
      763 123 123 ASP N    N 116.699 . 1 
      764 124 124 LEU H    H   7.283 . 1 
      765 124 124 LEU HB2  H   1.467 . 2 
      766 124 124 LEU C    C 178.111 . 1 
      767 124 124 LEU CA   C  58.511 . 1 
      768 124 124 LEU CB   C  42.384 . 1 
      769 124 124 LEU N    N 122.696 . 1 
      770 125 125 ALA H    H   7.633 . 1 
      771 125 125 ALA HA   H   4.959 . 1 
      772 125 125 ALA HB   H   1.482 . 1 
      773 125 125 ALA C    C 178.791 . 1 
      774 125 125 ALA CA   C  55.398 . 1 
      775 125 125 ALA CB   C  18.448 . 1 
      776 125 125 ALA N    N 121.231 . 1 
      777 126 126 ASP H    H   8.360 . 1 
      778 126 126 ASP HB2  H   2.641 . 2 
      779 126 126 ASP C    C 177.973 . 1 
      780 126 126 ASP CA   C  57.275 . 1 
      781 126 126 ASP CB   C  40.562 . 1 
      782 126 126 ASP N    N 118.450 . 1 
      783 127 127 LEU H    H   7.704 . 1 
      784 127 127 LEU HA   H   4.009 . 1 
      785 127 127 LEU HD1  H   0.734 . 4 
      786 127 127 LEU CA   C  58.131 . 1 
      787 127 127 LEU CB   C  42.548 . 1 
      788 127 127 LEU CG   C  25.800 . 1 
      789 127 127 LEU N    N 121.051 . 1 
      790 128 128 LEU H    H   8.032 . 1 
      791 128 128 LEU HD1  H   0.301 . 4 
      792 128 128 LEU HD2  H   0.650 . 4 
      793 128 128 LEU C    C 177.656 . 1 
      794 128 128 LEU CA   C  58.468 . 1 
      795 128 128 LEU CB   C  41.242 . 1 
      796 128 128 LEU CD1  C  22.797 . 2 
      797 128 128 LEU CG   C  25.507 . 1 
      798 128 128 LEU N    N 118.217 . 1 
      799 129 129 THR H    H   7.539 . 1 
      800 129 129 THR HA   H   4.237 . 1 
      801 129 129 THR HB   H   3.949 . 1 
      802 129 129 THR HG2  H   1.191 . 1 
      803 129 129 THR C    C 176.216 . 1 
      804 129 129 THR CA   C  65.176 . 1 
      805 129 129 THR CB   C  69.241 . 1 
      806 129 129 THR N    N 109.693 . 1 
      807 130 130 GLN H    H   8.453 . 1 
      808 130 130 GLN HA   H   4.240 . 1 
      809 130 130 GLN HE21 H   7.598 . 2 
      810 130 130 GLN HE22 H   6.791 . 2 
      811 130 130 GLN HG2  H   2.502 . 2 
      812 130 130 GLN C    C 177.168 . 1 
      813 130 130 GLN CA   C  57.655 . 1 
      814 130 130 GLN CB   C  29.900 . 1 
      815 130 130 GLN CG   C  33.842 . 1 
      816 130 130 GLN N    N 118.774 . 1 
      817 130 130 GLN NE2  N 111.844 . 1 
      818 131 131 ASN H    H   9.098 . 1 
      819 131 131 ASN HD21 H   7.857 . 2 
      820 131 131 ASN HD22 H   6.890 . 2 
      821 131 131 ASN CA   C  50.967 . 1 
      822 131 131 ASN CB   C  38.539 . 1 
      823 131 131 ASN N    N 116.552 . 1 
      824 131 131 ASN ND2  N 112.448 . 1 
      825 132 132 PRO HA   H   4.393 . 1 
      826 132 132 PRO HB2  H   2.077 . 2 
      827 132 132 PRO C    C 179.476 . 1 
      828 132 132 PRO CA   C  65.438 . 1 
      829 132 132 PRO CB   C  31.556 . 1 
      830 133 133 GLU H    H   8.770 . 1 
      831 133 133 GLU HA   H   4.140 . 1 
      832 133 133 GLU HG2  H   2.341 . 2 
      833 133 133 GLU C    C 178.816 . 1 
      834 133 133 GLU CA   C  59.750 . 1 
      835 133 133 GLU CB   C  29.153 . 1 
      836 133 133 GLU N    N 118.261 . 1 
      837 134 134 LEU H    H   7.425 . 1 
      838 134 134 LEU HD1  H   0.948 . 4 
      839 134 134 LEU C    C 178.584 . 1 
      840 134 134 LEU CA   C  57.115 . 1 
      841 134 134 LEU CB   C  42.127 . 1 
      842 134 134 LEU CG   C  25.499 . 1 
      843 134 134 LEU N    N 123.115 . 1 
      844 135 135 PHE H    H   8.304 . 1 
      845 135 135 PHE HB2  H   2.821 . 2 
      846 135 135 PHE HB3  H   3.340 . 2 
      847 135 135 PHE C    C 176.453 . 1 
      848 135 135 PHE CA   C  63.436 . 1 
      849 135 135 PHE CB   C  39.134 . 1 
      850 135 135 PHE N    N 118.300 . 1 
      851 136 136 ARG H    H   8.464 . 1 
      852 136 136 ARG HB2  H   1.782 . 2 
      853 136 136 ARG C    C 178.005 . 1 
      854 136 136 ARG CA   C  60.234 . 1 
      855 136 136 ARG CB   C  29.374 . 1 
      856 136 136 ARG N    N 117.896 . 1 
      857 137 137 LYS H    H   7.850 . 1 
      858 137 137 LYS HA   H   3.988 . 1 
      859 137 137 LYS HB2  H   1.897 . 2 
      860 137 137 LYS HD2  H   1.615 . 2 
      861 137 137 LYS C    C 179.186 . 1 
      862 137 137 LYS CA   C  59.772 . 1 
      863 137 137 LYS CB   C  32.621 . 1 
      864 137 137 LYS N    N 120.498 . 1 
      865 138 138 ASN H    H   8.360 . 1 
      866 138 138 ASN HB2  H   2.604 . 2 
      867 138 138 ASN HD21 H   7.785 . 2 
      868 138 138 ASN HD22 H   7.274 . 2 
      869 138 138 ASN C    C 178.034 . 1 
      870 138 138 ASN CA   C  55.081 . 1 
      871 138 138 ASN CB   C  37.966 . 1 
      872 138 138 ASN N    N 119.456 . 1 
      873 138 138 ASN ND2  N 108.417 . 1 
      874 139 139 ALA H    H   8.882 . 1 
      875 139 139 ALA HB   H   1.093 . 1 
      876 139 139 ALA C    C 180.774 . 1 
      877 139 139 ALA CA   C  55.192 . 1 
      878 139 139 ALA CB   C  18.295 . 1 
      879 139 139 ALA N    N 123.033 . 1 
      880 140 140 GLU H    H   8.959 . 1 
      881 140 140 GLU HB2  H   2.152 . 2 
      882 140 140 GLU C    C 177.535 . 1 
      883 140 140 GLU CA   C  60.713 . 1 
      884 140 140 GLU CB   C  30.165 . 1 
      885 140 140 GLU N    N 124.475 . 1 
      886 141 141 GLU H    H   7.944 . 1 
      887 141 141 GLU HA   H   3.888 . 1 
      888 141 141 GLU HB2  H   2.121 . 2 
      889 141 141 GLU HG2  H   2.407 . 2 
      890 141 141 GLU C    C 179.201 . 1 
      891 141 141 GLU CA   C  59.843 . 1 
      892 141 141 GLU CB   C  29.417 . 1 
      893 141 141 GLU N    N 118.991 . 1 
      894 142 142 PHE H    H   8.269 . 1 
      895 142 142 PHE HB2  H   3.154 . 2 
      896 142 142 PHE C    C 179.790 . 1 
      897 142 142 PHE CA   C  62.270 . 1 
      898 142 142 PHE CB   C  39.503 . 1 
      899 142 142 PHE N    N 120.353 . 1 
      900 143 143 THR H    H   8.624 . 1 
      901 143 143 THR C    C 176.092 . 1 
      902 143 143 THR CA   C  67.705 . 1 
      903 143 143 THR CB   C  68.878 . 1 
      904 143 143 THR N    N 120.563 . 1 
      905 144 144 LEU H    H   8.227 . 1 
      906 144 144 LEU HB2  H   1.802 . 2 
      907 144 144 LEU HD1  H   0.849 . 4 
      908 144 144 LEU C    C 178.849 . 1 
      909 144 144 LEU CA   C  57.869 . 1 
      910 144 144 LEU CB   C  41.801 . 1 
      911 144 144 LEU CD1  C  25.235 . 2 
      912 144 144 LEU N    N 119.884 . 1 
      913 145 145 ARG H    H   7.825 . 1 
      914 145 145 ARG HD2  H   2.719 . 2 
      915 145 145 ARG HG2  H   1.360 . 2 
      916 145 145 ARG C    C 177.831 . 1 
      917 145 145 ARG CA   C  58.686 . 1 
      918 145 145 ARG CB   C  30.969 . 1 
      919 145 145 ARG N    N 118.067 . 1 
      920 146 146 PHE H    H   7.661 . 1 
      921 146 146 PHE HA   H   4.850 . 1 
      922 146 146 PHE HB2  H   2.641 . 2 
      923 146 146 PHE C    C 176.196 . 1 
      924 146 146 PHE CA   C  58.613 . 1 
      925 146 146 PHE CB   C  41.780 . 1 
      926 146 146 PHE N    N 112.361 . 1 
      927 147 147 GLY H    H   8.382 . 1 
      928 147 147 GLY HA2  H   3.429 . 2 
      929 147 147 GLY HA3  H   3.848 . 2 
      930 147 147 GLY C    C 172.655 . 1 
      931 147 147 GLY CA   C  45.113 . 1 
      932 147 147 GLY N    N 107.341 . 1 
      933 148 148 VAL H    H   8.310 . 1 
      934 148 148 VAL HA   H   4.224 . 1 
      935 148 148 VAL HB   H   1.792 . 1 
      936 148 148 VAL HG1  H   0.958 . 4 
      937 148 148 VAL C    C 175.566 . 1 
      938 148 148 VAL CA   C  61.066 . 1 
      939 148 148 VAL CB   C  33.130 . 1 
      940 148 148 VAL CG1  C  21.525 . 2 
      941 148 148 VAL N    N 120.324 . 1 
      942 149 149 ASP H    H   8.351 . 1 
      943 149 149 ASP HB2  H   2.445 . 2 
      944 149 149 ASP C    C 176.020 . 1 
      945 149 149 ASP CA   C  55.963 . 1 
      946 149 149 ASP CB   C  40.586 . 1 
      947 149 149 ASP N    N 123.869 . 1 
      948 150 150 ARG H    H   8.480 . 1 
      949 150 150 ARG CA   C  53.930 . 1 
      950 150 150 ARG CB   C  31.462 . 1 
      951 150 150 ARG N    N 122.597 . 1 
      952 151 151 PRO HA   H   4.510 . 1 
      953 151 151 PRO HB2  H   2.321 . 2 
      954 151 151 PRO HD2  H   3.307 . 2 
      955 151 151 PRO HG2  H   1.879 . 2 
      956 151 151 PRO C    C 175.440 . 1 
      957 151 151 PRO CA   C  62.889 . 1 
      958 151 151 PRO CB   C  32.089 . 1 
      959 152 152 SER H    H   8.109 . 1 
      960 152 152 SER CA   C  60.559 . 1 
      961 152 152 SER CB   C  64.463 . 1 
      962 152 152 SER N    N 121.332 . 1 

   stop_

   loop_
      _Atom_shift_assign_ID_ambiguity

                             30 
      '30,30'                    
      '37,37,37'                 
      '78,78,78,79,79,79'        
      '121,121,121'              
      '146,146,146,147,147,147'  
      '193,193,193'              
      '201,201,201,202,202,202'  
      '232,232,232,233,233,233'  
      '241,241,241'              
      '318,318,318'              
      '333,333,333'              
      '393,393,393'              
      '511,511,511'              
      '541,541,541'              
      '616,616,616'              
      '642,642,642'              
      '657,657,657'              
      '666,666,666'              
      '674,674,674,675,675,675'  
      '712,712,712'              
      '738,738,738'              
      '785,785,785'              
      '791,791,791,792,792,792'  
      '838,838,838'              
      '907,907,907'              
      '936,936,936'              

   stop_

save_