data_5898

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
Backbone 1H, 13C and 15N resonance assignments for the 24.4 kDa human gankyrin 
protein 
;
   _BMRB_accession_number   5898
   _BMRB_flat_file_name     bmr5898.str
   _Entry_type              original
   _Submission_date         2003-08-05
   _Accession_date          2003-08-05
   _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 Yuan  Chunhua  .  . 
      2 Li    Junan    .  . 
      3 Poi   Mingjye  .  . 
      4 Byeon In-Ja    L. . 
      5 Tsai  Ming-Daw .  . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  428 
      "13C chemical shifts" 642 
      "15N chemical shifts" 217 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2004-10-25 original author . 

   stop_

   _Original_release_date   2004-10-25

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Solution structure of the human oncogenic protein gankyrin containing seven
ankyrin repeats and analysis of its structure--function relationship.
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    15379554

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Yuan    Chunhua  .  . 
      2 Li      Junan    .  . 
      3 Mahajan A.       .  . 
      4 Poi     Mingjye  .  . 
      5 Byeon   In-Ja    L. . 
      6 Tsai    Ming-Daw .  . 

   stop_

   _Journal_abbreviation         Biochemistry
   _Journal_volume               43
   _Journal_issue                38
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   12152
   _Page_last                    12161
   _Year                         2004
   _Details                      .

   loop_
      _Keyword

       gankyrin              
       oncoprotein           
      'resonance assignment' 
       TROSY                 

   stop_

save_


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

save_system_gankyrin
   _Saveframe_category         molecular_system

   _Mol_system_name           '26S proteasome non-ATPase regulatory subunit 10'
   _Abbreviation_common        gankyrin
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      gankyrin $gankyrin 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'all free'
   _Database_query_date        .
   _Details                    .

save_


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

save_gankyrin
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 gankyrin
   _Abbreviation_common                         gankyrin
   _Molecular_mass                              .
   _Mol_thiol_state                            'all free'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               226
   _Mol_residue_sequence                       
;
MEGCVSNLMVCNLAYSGKLE
ELKESILADKSLATRTDQDS
RTALHWACSAGHTEIVEFLL
QLGVPVNDKDDAGWSPLHIA
ASAGRDEIVKALLGKGAQVN
AVNQNGCTPLHYAASKNRHE
IAVMLLEGGANPDAKDHYEA
TAMHRAAAKGNLKMIHILLY
YKASTNIQDTEGNTPLHLAC
DEERVEEAKLLVSQGASIYI
ENKEEKTPLQVAKGGLGLIL
KRMVEG
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 MET    2 GLU    3 GLY    4 CYS    5 VAL 
        6 SER    7 ASN    8 LEU    9 MET   10 VAL 
       11 CYS   12 ASN   13 LEU   14 ALA   15 TYR 
       16 SER   17 GLY   18 LYS   19 LEU   20 GLU 
       21 GLU   22 LEU   23 LYS   24 GLU   25 SER 
       26 ILE   27 LEU   28 ALA   29 ASP   30 LYS 
       31 SER   32 LEU   33 ALA   34 THR   35 ARG 
       36 THR   37 ASP   38 GLN   39 ASP   40 SER 
       41 ARG   42 THR   43 ALA   44 LEU   45 HIS 
       46 TRP   47 ALA   48 CYS   49 SER   50 ALA 
       51 GLY   52 HIS   53 THR   54 GLU   55 ILE 
       56 VAL   57 GLU   58 PHE   59 LEU   60 LEU 
       61 GLN   62 LEU   63 GLY   64 VAL   65 PRO 
       66 VAL   67 ASN   68 ASP   69 LYS   70 ASP 
       71 ASP   72 ALA   73 GLY   74 TRP   75 SER 
       76 PRO   77 LEU   78 HIS   79 ILE   80 ALA 
       81 ALA   82 SER   83 ALA   84 GLY   85 ARG 
       86 ASP   87 GLU   88 ILE   89 VAL   90 LYS 
       91 ALA   92 LEU   93 LEU   94 GLY   95 LYS 
       96 GLY   97 ALA   98 GLN   99 VAL  100 ASN 
      101 ALA  102 VAL  103 ASN  104 GLN  105 ASN 
      106 GLY  107 CYS  108 THR  109 PRO  110 LEU 
      111 HIS  112 TYR  113 ALA  114 ALA  115 SER 
      116 LYS  117 ASN  118 ARG  119 HIS  120 GLU 
      121 ILE  122 ALA  123 VAL  124 MET  125 LEU 
      126 LEU  127 GLU  128 GLY  129 GLY  130 ALA 
      131 ASN  132 PRO  133 ASP  134 ALA  135 LYS 
      136 ASP  137 HIS  138 TYR  139 GLU  140 ALA 
      141 THR  142 ALA  143 MET  144 HIS  145 ARG 
      146 ALA  147 ALA  148 ALA  149 LYS  150 GLY 
      151 ASN  152 LEU  153 LYS  154 MET  155 ILE 
      156 HIS  157 ILE  158 LEU  159 LEU  160 TYR 
      161 TYR  162 LYS  163 ALA  164 SER  165 THR 
      166 ASN  167 ILE  168 GLN  169 ASP  170 THR 
      171 GLU  172 GLY  173 ASN  174 THR  175 PRO 
      176 LEU  177 HIS  178 LEU  179 ALA  180 CYS 
      181 ASP  182 GLU  183 GLU  184 ARG  185 VAL 
      186 GLU  187 GLU  188 ALA  189 LYS  190 LEU 
      191 LEU  192 VAL  193 SER  194 GLN  195 GLY 
      196 ALA  197 SER  198 ILE  199 TYR  200 ILE 
      201 GLU  202 ASN  203 LYS  204 GLU  205 GLU 
      206 LYS  207 THR  208 PRO  209 LEU  210 GLN 
      211 VAL  212 ALA  213 LYS  214 GLY  215 GLY 
      216 LEU  217 GLY  218 LEU  219 ILE  220 LEU 
      221 LYS  222 ARG  223 MET  224 VAL  225 GLU 
      226 GLY 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-01-28

   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 1QYM         "X-Ray Structure Of Human Gankyrin"                                                                                                99.56 227 100.00 100.00 8.27e-163 
      PDB 1TR4         "Solution Structure Of Human Oncogenic Protein Gankyrin"                                                                          100.00 226 100.00 100.00 9.77e-164 
      PDB 1UOH         "Human Gankyrin"                                                                                                                  100.00 226 100.00 100.00 9.77e-164 
      PDB 4NIK         "Structure Of Human Gankyrin In Complex To The Single Chain Antibody F5"                                                          100.00 230 100.00 100.00 1.77e-163 
      DBJ BAA33215     "26S proteasome subunit p28 [Homo sapiens]"                                                                                       100.00 226 100.00 100.00 9.77e-164 
      DBJ BAA34594     "gankyrin [Homo sapiens]"                                                                                                         100.00 226 100.00 100.00 9.77e-164 
      DBJ BAE87161     "unnamed protein product [Macaca fascicularis]"                                                                                   100.00 226  99.56  99.56 9.51e-163 
      DBJ BAE87972     "unnamed protein product [Macaca fascicularis]"                                                                                   100.00 226  99.56  99.56 9.51e-163 
      DBJ BAE88401     "unnamed protein product [Macaca fascicularis]"                                                                                   100.00 226  99.56  99.56 9.51e-163 
      GB  AAH11960     "Proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]"                                                      100.00 226 100.00 100.00 9.77e-164 
      GB  AAV38495     "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]"                                                      100.00 226  99.56  99.56 4.05e-163 
      GB  AAX41449     "proteasome 26S subunit 10 [synthetic construct]"                                                                                 100.00 226  99.56  99.56 4.05e-163 
      GB  AAY18907     "proteasome 26S subunit non-ATPase 10-like [synthetic construct]"                                                                  99.56 250 100.00 100.00 5.00e-162 
      GB  ACT64478     "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 protein [synthetic construct]"                                       100.00 226 100.00 100.00 9.77e-164 
      REF NP_001248034 "26S proteasome non-ATPase regulatory subunit 10 [Macaca mulatta]"                                                                100.00 226  99.56  99.56 9.51e-163 
      REF NP_002805    "26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Homo sapiens]"                                                        100.00 226 100.00 100.00 9.77e-164 
      REF XP_001926942 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Sus scrofa]"                                                99.56 226  99.56  99.56 4.03e-162 
      REF XP_002763200 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Callithrix jacchus]"                                      100.00 226  98.23  98.67 2.55e-160 
      REF XP_002832022 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Pongo abelii]"                                            100.00 226 100.00 100.00 9.77e-164 
      SP  O75832       "RecName: Full=26S proteasome non-ATPase regulatory subunit 10; AltName: Full=26S proteasome regulatory subunit p28; AltName: Fu" 100.00 226 100.00 100.00 9.77e-164 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $gankyrin Human 9606 Eukaryota Metazoa Homo sapiens 

   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

      $gankyrin 'recombinant technology' . . . . . 

   stop_

save_


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

save_sample_1
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Concentration_min_value
      _Concentration_max_value
      _Isotopic_labeling

      $gankyrin  . mM 0.4 0.5 '[U-13C; U-15N; U-70% 2H]' 
       HEPES    5 mM  .   .   .                         
       EDTA     1 uM  .   .   .                         
       DTT      1 mM  .   .   .                         

   stop_

save_


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

save_XWINNMR
   _Saveframe_category   software

   _Name                 XWINNMR
   _Version              3.1
   _Details              .

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DMX
   _Field_strength       600
   _Details              .

save_


save_NMR_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       800
   _Details              .

save_


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

save_TROSY-HNCA_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      TROSY-HNCA
   _Sample_label         .

save_


save_TROSY-HN(CO)CA_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      TROSY-HN(CO)CA
   _Sample_label         .

save_


save_TROSY-HNCACB_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      TROSY-HNCACB
   _Sample_label         .

save_


save_TROSY-HNCO_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      TROSY-HNCO
   _Sample_label         .

save_


save_15N-edited_NOESY-HSQC_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N-edited NOESY-HSQC'
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        TROSY-HNCA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        TROSY-HN(CO)CA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        TROSY-HNCACB
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        TROSY-HNCO
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                       '15N-edited NOESY-HSQC'
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


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

save_Ex-cond_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            7.4 0.2 n/a 
      temperature 300   1   K   

   stop_

save_


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

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

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

save_chemical_shift_reference
   _Saveframe_category   chemical_shift_reference

   _Details             
;
Calibation followed the reference Journal of Biolmolecular NMR 6 (1995) 135-140.
1H, 13C and 15N chemical shift referencing in biomolecular NMR 
by Wishart et al.
;

   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 H  1 'methyl protons' ppm 0.0 external direct   . . . 1.0         
      DSS C 13 'methyl carbons' ppm 0.0 external direct   . . . 1.0         
      DSS N 15 'methyl protons' ppm 0.0 external 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_shift_set_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $Ex-cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name        gankyrin
   _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 MET H   H   8.37 0.03 1 
         2 .   1 MET C   C 176.1  0.1  1 
         3 .   1 MET CA  C  56.0  0.1  1 
         4 .   1 MET CB  C  33.1  0.1  1 
         5 .   1 MET N   N 122.2  0.1  1 
         6 .   2 GLU H   H   8.29 0.03 1 
         7 .   2 GLU HA  H   4.22 0.03 1 
         8 .   2 GLU C   C 176.9  0.1  1 
         9 .   2 GLU CA  C  57.5  0.1  1 
        10 .   2 GLU CB  C  30.3  0.1  1 
        11 .   2 GLU N   N 121.7  0.1  1 
        12 .   3 GLY H   H   8.39 0.03 1 
        13 .   3 GLY C   C 173.5  0.1  1 
        14 .   3 GLY CA  C  45.9  0.1  1 
        15 .   3 GLY N   N 110.2  0.1  1 
        16 .   4 CYS H   H   7.86 0.03 1 
        17 .   4 CYS C   C 174.4  0.1  1 
        18 .   4 CYS CA  C  58.9  0.1  1 
        19 .   4 CYS CB  C  28.7  0.1  1 
        20 .   4 CYS N   N 119.1  0.1  1 
        21 .   5 VAL H   H   7.42 0.03 1 
        22 .   5 VAL HA  H   3.96 0.03 1 
        23 .   5 VAL C   C 174.8  0.1  1 
        24 .   5 VAL CA  C  61.7  0.1  1 
        25 .   5 VAL CB  C  32.6  0.1  1 
        26 .   5 VAL N   N 117.5  0.1  1 
        27 .   6 SER H   H   7.83 0.03 1 
        28 .   6 SER HA  H   4.64 0.03 1 
        29 .   6 SER C   C 174.6  0.1  1 
        30 .   6 SER CA  C  57.5  0.1  1 
        31 .   6 SER CB  C  63.8  0.1  1 
        32 .   6 SER N   N 115.1  0.1  1 
        33 .   7 ASN H   H   8.78 0.03 1 
        34 .   7 ASN HA  H   4.55 0.03 1 
        35 .   7 ASN C   C 175.0  0.1  1 
        36 .   7 ASN CA  C  54.3  0.1  1 
        37 .   7 ASN CB  C  37.4  0.1  1 
        38 .   7 ASN N   N 123.3  0.1  1 
        39 .   8 LEU H   H   8.18 0.03 1 
        40 .   8 LEU CA  C  53.4  0.1  1 
        41 .   8 LEU CB  C  43.9  0.1  1 
        42 .   8 LEU N   N 121.1  0.1  1 
        43 .   9 MET C   C 179.2  0.1  1 
        44 .   9 MET CA  C  59.4  0.1  1 
        45 .  10 VAL H   H   8.88 0.03 1 
        46 .  10 VAL HA  H   3.89 0.03 1 
        47 .  10 VAL C   C 177.0  0.1  1 
        48 .  10 VAL CA  C  66.3  0.1  1 
        49 .  10 VAL CB  C  31.6  0.1  1 
        50 .  10 VAL N   N 115.0  0.1  1 
        51 .  11 CYS H   H   6.80 0.03 1 
        52 .  11 CYS HA  H   4.02 0.03 1 
        53 .  11 CYS C   C 175.8  0.1  1 
        54 .  11 CYS CA  C  63.1  0.1  1 
        55 .  11 CYS CB  C  27.8  0.1  1 
        56 .  11 CYS N   N 118.6  0.1  1 
        57 .  12 ASN H   H   7.31 0.03 1 
        58 .  12 ASN HA  H   4.37 0.03 1 
        59 .  12 ASN C   C 178.9  0.1  1 
        60 .  12 ASN CA  C  57.2  0.1  1 
        61 .  12 ASN CB  C  38.4  0.1  1 
        62 .  12 ASN N   N 118.6  0.1  1 
        63 .  13 LEU H   H   8.68 0.03 1 
        64 .  13 LEU HA  H   4.00 0.03 1 
        65 .  13 LEU C   C 178.5  0.1  1 
        66 .  13 LEU CA  C  58.5  0.1  1 
        67 .  13 LEU CB  C  42.5  0.1  1 
        68 .  13 LEU N   N 121.2  0.1  1 
        69 .  14 ALA H   H   7.71 0.03 1 
        70 .  14 ALA HA  H   4.05 0.03 1 
        71 .  14 ALA C   C 178.5  0.1  1 
        72 .  14 ALA CA  C  55.6  0.1  1 
        73 .  14 ALA CB  C  20.1  0.1  1 
        74 .  14 ALA N   N 120.2  0.1  1 
        75 .  15 TYR H   H   8.26 0.03 1 
        76 .  15 TYR HA  H   4.26 0.03 1 
        77 .  15 TYR C   C 177.3  0.1  1 
        78 .  15 TYR CA  C  61.2  0.1  1 
        79 .  15 TYR CB  C  39.9  0.1  1 
        80 .  15 TYR N   N 116.3  0.1  1 
        81 .  16 SER H   H   8.10 0.03 1 
        82 .  16 SER HA  H   4.34 0.03 1 
        83 .  16 SER C   C 174.7  0.1  1 
        84 .  16 SER CA  C  59.9  0.1  1 
        85 .  16 SER CB  C  64.6  0.1  1 
        86 .  16 SER N   N 110.4  0.1  1 
        87 .  17 GLY H   H   7.27 0.03 1 
        88 .  17 GLY HA2 H   3.15 0.03 2 
        89 .  17 GLY HA3 H   2.65 0.03 2 
        90 .  17 GLY C   C 174.9  0.1  1 
        91 .  17 GLY CA  C  44.7  0.1  1 
        92 .  17 GLY N   N 109.6  0.1  1 
        93 .  18 LYS H   H   7.69 0.03 1 
        94 .  18 LYS HA  H   4.36 0.03 1 
        95 .  18 LYS C   C 174.6  0.1  1 
        96 .  18 LYS CA  C  55.1  0.1  1 
        97 .  18 LYS CB  C  30.6  0.1  1 
        98 .  18 LYS N   N 123.2  0.1  1 
        99 .  19 LEU H   H   7.43 0.03 1 
       100 .  19 LEU HA  H   3.62 0.03 1 
       101 .  19 LEU C   C 177.2  0.1  1 
       102 .  19 LEU CA  C  59.1  0.1  1 
       103 .  19 LEU CB  C  41.6  0.1  1 
       104 .  19 LEU N   N 124.2  0.1  1 
       105 .  20 GLU H   H   8.70 0.03 1 
       106 .  20 GLU HA  H   3.76 0.03 1 
       107 .  20 GLU C   C 179.3  0.1  1 
       108 .  20 GLU CA  C  60.8  0.1  1 
       109 .  20 GLU CB  C  28.4  0.1  1 
       110 .  20 GLU N   N 117.8  0.1  1 
       111 .  21 GLU H   H   8.82 0.03 1 
       112 .  21 GLU HA  H   3.99 0.03 1 
       113 .  21 GLU C   C 179.6  0.1  1 
       114 .  21 GLU CA  C  60.3  0.1  1 
       115 .  21 GLU CB  C  29.9  0.1  1 
       116 .  21 GLU N   N 120.4  0.1  1 
       117 .  22 LEU H   H   8.30 0.03 1 
       118 .  22 LEU HA  H   3.88 0.03 1 
       119 .  22 LEU C   C 178.1  0.1  1 
       120 .  22 LEU CA  C  59.3  0.1  1 
       121 .  22 LEU CB  C  41.6  0.1  1 
       122 .  22 LEU N   N 123.1  0.1  1 
       123 .  23 LYS H   H   8.67 0.03 1 
       124 .  23 LYS HA  H   3.56 0.03 1 
       125 .  23 LYS C   C 178.5  0.1  1 
       126 .  23 LYS CA  C  60.8  0.1  1 
       127 .  23 LYS CB  C  32.3  0.1  1 
       128 .  23 LYS N   N 119.8  0.1  1 
       129 .  24 GLU H   H   7.83 0.03 1 
       130 .  24 GLU HA  H   3.93 0.03 1 
       131 .  24 GLU C   C 179.7  0.1  1 
       132 .  24 GLU CA  C  59.9  0.1  1 
       133 .  24 GLU CB  C  29.8  0.1  1 
       134 .  24 GLU N   N 117.4  0.1  1 
       135 .  25 SER H   H   7.85 0.03 1 
       136 .  25 SER HA  H   4.22 0.03 1 
       137 .  25 SER C   C 176.7  0.1  1 
       138 .  25 SER CA  C  62.7  0.1  1 
       139 .  25 SER CB  C  63.8  0.1  1 
       140 .  25 SER N   N 114.9  0.1  1 
       141 .  26 ILE H   H   8.09 0.03 1 
       142 .  26 ILE HA  H   3.97 0.03 1 
       143 .  26 ILE C   C 177.1  0.1  1 
       144 .  26 ILE CA  C  63.7  0.1  1 
       145 .  26 ILE CB  C  38.4  0.1  1 
       146 .  26 ILE N   N 122.0  0.1  1 
       147 .  27 LEU H   H   8.52 0.03 1 
       148 .  27 LEU HA  H   4.13 0.03 1 
       149 .  27 LEU C   C 179.6  0.1  1 
       150 .  27 LEU CA  C  58.2  0.1  1 
       151 .  27 LEU CB  C  41.1  0.1  1 
       152 .  27 LEU N   N 119.3  0.1  1 
       153 .  28 ALA H   H   7.10 0.03 1 
       154 .  28 ALA HA  H   4.28 0.03 1 
       155 .  28 ALA C   C 178.0  0.1  1 
       156 .  28 ALA CA  C  54.1  0.1  1 
       157 .  28 ALA CB  C  19.4  0.1  1 
       158 .  28 ALA N   N 118.8  0.1  1 
       159 .  29 ASP H   H   7.45 0.03 1 
       160 .  29 ASP HA  H   4.66 0.03 1 
       161 .  29 ASP C   C 175.3  0.1  1 
       162 .  29 ASP CA  C  54.0  0.1  1 
       163 .  29 ASP CB  C  40.6  0.1  1 
       164 .  29 ASP N   N 117.4  0.1  1 
       165 .  30 LYS H   H   8.73 0.03 1 
       166 .  30 LYS HA  H   4.40 0.03 1 
       167 .  30 LYS C   C 180.0  0.1  1 
       168 .  30 LYS CA  C  59.6  0.1  1 
       169 .  30 LYS CB  C  32.4  0.1  1 
       170 .  30 LYS N   N 125.6  0.1  1 
       171 .  31 SER H   H   8.31 0.03 1 
       172 .  31 SER HA  H   4.26 0.03 1 
       173 .  31 SER C   C 176.3  0.1  1 
       174 .  31 SER CA  C  61.7  0.1  1 
       175 .  31 SER CB  C  63.4  0.1  1 
       176 .  31 SER N   N 116.9  0.1  1 
       177 .  32 LEU H   H   8.08 0.03 1 
       178 .  32 LEU HA  H   4.07 0.03 1 
       179 .  32 LEU C   C 178.2  0.1  1 
       180 .  32 LEU CA  C  57.5  0.1  1 
       181 .  32 LEU CB  C  42.7  0.1  1 
       182 .  32 LEU N   N 122.3  0.1  1 
       183 .  33 ALA H   H   7.63 0.03 1 
       184 .  33 ALA HA  H   3.96 0.03 1 
       185 .  33 ALA C   C 176.0  0.1  1 
       186 .  33 ALA CA  C  55.3  0.1  1 
       187 .  33 ALA CB  C  19.5  0.1  1 
       188 .  33 ALA N   N 117.2  0.1  1 
       189 .  34 THR H   H   7.14 0.03 1 
       190 .  34 THR HA  H   4.49 0.03 1 
       191 .  34 THR C   C 173.8  0.1  1 
       192 .  34 THR CA  C  60.4  0.1  1 
       193 .  34 THR CB  C  69.5  0.1  1 
       194 .  34 THR N   N  99.6  0.1  1 
       195 .  35 ARG H   H   7.00 0.03 1 
       196 .  35 ARG HA  H   4.29 0.03 1 
       197 .  35 ARG C   C 175.2  0.1  1 
       198 .  35 ARG CA  C  57.0  0.1  1 
       199 .  35 ARG CB  C  30.7  0.1  1 
       200 .  35 ARG N   N 125.1  0.1  1 
       201 .  36 THR H   H   7.88 0.03 1 
       202 .  36 THR HA  H   4.73 0.03 1 
       203 .  36 THR C   C 175.7  0.1  1 
       204 .  36 THR CA  C  59.5  0.1  1 
       205 .  36 THR CB  C  71.7  0.1  1 
       206 .  36 THR N   N 112.4  0.1  1 
       207 .  37 ASP H   H   9.10 0.03 1 
       208 .  37 ASP C   C 179.1  0.1  1 
       209 .  37 ASP CA  C  52.1  0.1  1 
       210 .  37 ASP CB  C  42.2  0.1  1 
       211 .  37 ASP N   N 123.6  0.1  1 
       212 .  38 GLN H   H   8.78 0.03 1 
       213 .  38 GLN HA  H   4.29 0.03 1 
       214 .  38 GLN C   C 176.0  0.1  1 
       215 .  38 GLN CA  C  58.6  0.1  1 
       216 .  38 GLN CB  C  27.2  0.1  1 
       217 .  38 GLN N   N 118.2  0.1  1 
       218 .  39 ASP H   H   8.39 0.03 1 
       219 .  39 ASP HA  H   5.11 0.03 1 
       220 .  39 ASP C   C 175.4  0.1  1 
       221 .  39 ASP CA  C  55.0  0.1  1 
       222 .  39 ASP CB  C  42.2  0.1  1 
       223 .  39 ASP N   N 122.6  0.1  1 
       224 .  40 SER H   H   8.46 0.03 1 
       225 .  40 SER HA  H   3.81 0.03 1 
       226 .  40 SER C   C 172.5  0.1  1 
       227 .  40 SER CA  C  60.5  0.1  1 
       228 .  40 SER CB  C  62.2  0.1  1 
       229 .  40 SER N   N 111.6  0.1  1 
       230 .  41 ARG H   H   8.25 0.03 1 
       231 .  41 ARG HA  H   3.92 0.03 1 
       232 .  41 ARG C   C 176.2  0.1  1 
       233 .  41 ARG CA  C  55.8  0.1  1 
       234 .  41 ARG CB  C  33.4  0.1  1 
       235 .  41 ARG N   N 116.9  0.1  1 
       236 .  42 THR H   H   9.73 0.03 1 
       237 .  42 THR HA  H   5.04 0.03 1 
       238 .  42 THR C   C 177.0  0.1  1 
       239 .  42 THR CA  C  59.8  0.1  1 
       240 .  42 THR CB  C  72.7  0.1  1 
       241 .  42 THR N   N 112.3  0.1  1 
       242 .  43 ALA H   H   9.62 0.03 1 
       243 .  43 ALA HA  H   4.13 0.03 1 
       244 .  43 ALA C   C 178.5  0.1  1 
       245 .  43 ALA CA  C  56.3  0.1  1 
       246 .  43 ALA CB  C  18.5  0.1  1 
       247 .  43 ALA N   N 121.7  0.1  1 
       248 .  44 LEU H   H   8.25 0.03 1 
       249 .  44 LEU HA  H   4.00 0.03 1 
       250 .  44 LEU C   C 178.9  0.1  1 
       251 .  44 LEU CA  C  58.8  0.1  1 
       252 .  44 LEU CB  C  41.9  0.1  1 
       253 .  44 LEU N   N 115.4  0.1  1 
       254 .  45 HIS H   H   7.65 0.03 1 
       255 .  45 HIS HA  H   3.64 0.03 1 
       256 .  45 HIS C   C 178.1  0.1  1 
       257 .  45 HIS CA  C  64.3  0.1  1 
       258 .  45 HIS CB  C  31.5  0.1  1 
       259 .  45 HIS N   N 117.6  0.1  1 
       260 .  46 TRP H   H   7.39 0.03 1 
       261 .  46 TRP HA  H   4.60 0.03 1 
       262 .  46 TRP C   C 178.6  0.1  1 
       263 .  46 TRP CA  C  60.7  0.1  1 
       264 .  46 TRP CB  C  31.4  0.1  1 
       265 .  46 TRP N   N 116.3  0.1  1 
       266 .  47 ALA H   H   8.85 0.03 1 
       267 .  47 ALA HA  H   4.35 0.03 1 
       268 .  47 ALA C   C 180.2  0.1  1 
       269 .  47 ALA CA  C  56.0  0.1  1 
       270 .  47 ALA CB  C  19.6  0.1  1 
       271 .  47 ALA N   N 122.1  0.1  1 
       272 .  48 CYS H   H   8.04 0.03 1 
       273 .  48 CYS HA  H   4.10 0.03 1 
       274 .  48 CYS C   C 175.3  0.1  1 
       275 .  48 CYS CA  C  65.1  0.1  1 
       276 .  48 CYS CB  C  27.7  0.1  1 
       277 .  48 CYS N   N 114.2  0.1  1 
       278 .  49 SER H   H   7.54 0.03 1 
       279 .  49 SER HA  H   3.77 0.03 1 
       280 .  49 SER C   C 177.1  0.1  1 
       281 .  49 SER CA  C  61.6  0.1  1 
       282 .  49 SER CB  C  64.0  0.1  1 
       283 .  49 SER N   N 113.0  0.1  1 
       284 .  50 ALA H   H   7.69 0.03 1 
       285 .  50 ALA HA  H   4.15 0.03 1 
       286 .  50 ALA C   C 177.1  0.1  1 
       287 .  50 ALA CA  C  53.4  0.1  1 
       288 .  50 ALA CB  C  22.2  0.1  1 
       289 .  50 ALA N   N 119.0  0.1  1 
       290 .  51 GLY H   H   7.40 0.03 1 
       291 .  51 GLY HA2 H   3.83 0.03 2 
       292 .  51 GLY HA3 H   3.28 0.03 2 
       293 .  51 GLY C   C 173.7  0.1  1 
       294 .  51 GLY CA  C  46.6  0.1  1 
       295 .  51 GLY N   N 103.7  0.1  1 
       296 .  52 HIS H   H   7.20 0.03 1 
       297 .  52 HIS HA  H   5.26 0.03 1 
       298 .  52 HIS C   C 175.6  0.1  1 
       299 .  52 HIS CA  C  55.0  0.1  1 
       300 .  52 HIS CB  C  30.6  0.1  1 
       301 .  52 HIS N   N 118.7  0.1  1 
       302 .  53 THR H   H   8.51 0.03 1 
       303 .  53 THR HA  H   3.44 0.03 1 
       304 .  53 THR C   C 175.5  0.1  1 
       305 .  53 THR CA  C  67.2  0.1  1 
       306 .  53 THR CB  C  69.1  0.1  1 
       307 .  53 THR N   N 125.8  0.1  1 
       308 .  54 GLU H   H   9.60 0.03 1 
       309 .  54 GLU HA  H   4.20 0.03 1 
       310 .  54 GLU C   C 180.1  0.1  1 
       311 .  54 GLU CA  C  60.4  0.1  1 
       312 .  54 GLU CB  C  29.2  0.1  1 
       313 .  54 GLU N   N 119.8  0.1  1 
       314 .  55 ILE H   H   7.38 0.03 1 
       315 .  55 ILE HA  H   3.81 0.03 1 
       316 .  55 ILE C   C 177.0  0.1  1 
       317 .  55 ILE CA  C  65.8  0.1  1 
       318 .  55 ILE CB  C  37.4  0.1  1 
       319 .  55 ILE N   N 119.5  0.1  1 
       320 .  56 VAL H   H   7.78 0.03 1 
       321 .  56 VAL HA  H   3.38 0.03 1 
       322 .  56 VAL C   C 177.0  0.1  1 
       323 .  56 VAL CA  C  68.8  0.1  1 
       324 .  56 VAL CB  C  31.6  0.1  1 
       325 .  56 VAL N   N 120.1  0.1  1 
       326 .  57 GLU H   H   8.74 0.03 1 
       327 .  57 GLU HA  H   3.87 0.03 1 
       328 .  57 GLU C   C 178.7  0.1  1 
       329 .  57 GLU CA  C  60.6  0.1  1 
       330 .  57 GLU CB  C  29.8  0.1  1 
       331 .  57 GLU N   N 117.7  0.1  1 
       332 .  58 PHE H   H   7.60 0.03 1 
       333 .  58 PHE HA  H   4.35 0.03 1 
       334 .  58 PHE C   C 176.8  0.1  1 
       335 .  58 PHE CA  C  61.2  0.1  1 
       336 .  58 PHE CB  C  39.3  0.1  1 
       337 .  58 PHE N   N 119.7  0.1  1 
       338 .  59 LEU H   H   8.13 0.03 1 
       339 .  59 LEU HA  H   3.67 0.03 1 
       340 .  59 LEU C   C 179.3  0.1  1 
       341 .  59 LEU CA  C  58.0  0.1  1 
       342 .  59 LEU CB  C  41.4  0.1  1 
       343 .  59 LEU N   N 118.9  0.1  1 
       344 .  60 LEU H   H   8.88 0.03 1 
       345 .  60 LEU HA  H   4.00 0.03 1 
       346 .  60 LEU C   C 181.9  0.1  1 
       347 .  60 LEU CA  C  58.4  0.1  1 
       348 .  60 LEU CB  C  40.2  0.1  1 
       349 .  60 LEU N   N 118.4  0.1  1 
       350 .  61 GLN H   H   8.07 0.03 1 
       351 .  61 GLN HA  H   4.09 0.03 1 
       352 .  61 GLN C   C 177.7  0.1  1 
       353 .  61 GLN CA  C  58.6  0.1  1 
       354 .  61 GLN CB  C  28.0  0.1  1 
       355 .  61 GLN N   N 120.4  0.1  1 
       356 .  62 LEU H   H   7.36 0.03 1 
       357 .  62 LEU HA  H   4.10 0.03 1 
       358 .  62 LEU C   C 178.0  0.1  1 
       359 .  62 LEU CA  C  56.1  0.1  1 
       360 .  62 LEU CB  C  42.5  0.1  1 
       361 .  62 LEU N   N 119.5  0.1  1 
       362 .  63 GLY H   H   7.70 0.03 1 
       363 .  63 GLY HA2 H   4.15 0.03 2 
       364 .  63 GLY HA3 H   3.75 0.03 2 
       365 .  63 GLY C   C 175.0  0.1  1 
       366 .  63 GLY CA  C  45.8  0.1  1 
       367 .  63 GLY N   N 105.2  0.1  1 
       368 .  64 VAL H   H   6.84 0.03 1 
       369 .  64 VAL HA  H   4.26 0.03 1 
       370 .  64 VAL CA  C  60.8  0.1  1 
       371 .  64 VAL CB  C  30.1  0.1  1 
       372 .  64 VAL N   N 113.9  0.1  1 
       373 .  65 PRO HA  H   4.48 0.03 1 
       374 .  65 PRO C   C 179.2  0.1  1 
       375 .  65 PRO CA  C  63.4  0.1  1 
       376 .  65 PRO CB  C  32.9  0.1  1 
       377 .  66 VAL H   H   8.18 0.03 1 
       378 .  66 VAL HA  H   4.16 0.03 1 
       379 .  66 VAL C   C 174.8  0.1  1 
       380 .  66 VAL CA  C  62.2  0.1  1 
       381 .  66 VAL CB  C  33.4  0.1  1 
       382 .  66 VAL N   N 114.7  0.1  1 
       383 .  67 ASN H   H   7.89 0.03 1 
       384 .  67 ASN HA  H   5.16 0.03 1 
       385 .  67 ASN C   C 176.0  0.1  1 
       386 .  67 ASN CA  C  53.8  0.1  1 
       387 .  67 ASN CB  C  41.7  0.1  1 
       388 .  67 ASN N   N 116.6  0.1  1 
       389 .  68 ASP H   H   8.15 0.03 1 
       390 .  68 ASP HA  H   4.56 0.03 1 
       391 .  68 ASP C   C 176.2  0.1  1 
       392 .  68 ASP CA  C  56.0  0.1  1 
       393 .  68 ASP CB  C  40.6  0.1  1 
       394 .  68 ASP N   N 123.0  0.1  1 
       395 .  69 LYS H   H   8.78 0.03 1 
       396 .  69 LYS HA  H   4.63 0.03 1 
       397 .  69 LYS C   C 177.1  0.1  1 
       398 .  69 LYS CA  C  55.8  0.1  1 
       399 .  69 LYS CB  C  35.7  0.1  1 
       400 .  69 LYS N   N 122.6  0.1  1 
       401 .  70 ASP H   H   8.06 0.03 1 
       402 .  70 ASP HA  H   4.50 0.03 1 
       403 .  70 ASP C   C 178.1  0.1  1 
       404 .  70 ASP CA  C  52.7  0.1  1 
       405 .  70 ASP CB  C  42.2  0.1  1 
       406 .  70 ASP N   N 122.2  0.1  1 
       407 .  71 ASP H   H   7.91 0.03 1 
       408 .  71 ASP HA  H   4.44 0.03 1 
       409 .  71 ASP C   C 176.8  0.1  1 
       410 .  71 ASP CA  C  57.6  0.1  1 
       411 .  71 ASP CB  C  40.4  0.1  1 
       412 .  71 ASP N   N 117.0  0.1  1 
       413 .  72 ALA H   H   7.99 0.03 1 
       414 .  72 ALA HA  H   4.68 0.03 1 
       415 .  72 ALA C   C 177.7  0.1  1 
       416 .  72 ALA CA  C  51.7  0.1  1 
       417 .  72 ALA CB  C  19.6  0.1  1 
       418 .  72 ALA N   N 122.0  0.1  1 
       419 .  73 GLY H   H   8.68 0.03 1 
       420 .  73 GLY HA2 H   3.83 0.03 1 
       421 .  73 GLY HA3 H   4.07 0.03 1 
       422 .  73 GLY C   C 172.8  0.1  1 
       423 .  73 GLY CA  C  46.7  0.1  1 
       424 .  73 GLY N   N 110.8  0.1  1 
       425 .  74 TRP H   H   9.00 0.03 1 
       426 .  74 TRP HA  H   3.84 0.03 1 
       427 .  74 TRP C   C 176.1  0.1  1 
       428 .  74 TRP CA  C  59.8  0.1  1 
       429 .  74 TRP CB  C  27.7  0.1  1 
       430 .  74 TRP N   N 121.1  0.1  1 
       431 .  75 SER H   H   9.05 0.03 1 
       432 .  75 SER HA  H   5.31 0.03 1 
       433 .  75 SER CA  C  56.9  0.1  1 
       434 .  75 SER CB  C  65.1  0.1  1 
       435 .  75 SER N   N 123.2  0.1  1 
       436 .  76 PRO C   C 176.9  0.1  1 
       437 .  76 PRO CA  C  67.7  0.1  1 
       438 .  77 LEU H   H   8.82 0.03 1 
       439 .  77 LEU C   C 179.3  0.1  1 
       440 .  77 LEU CA  C  58.5  0.1  1 
       441 .  77 LEU CB  C  42.1  0.1  1 
       442 .  77 LEU N   N 116.5  0.1  1 
       443 .  78 HIS H   H   7.95 0.03 1 
       444 .  78 HIS C   C 177.4  0.1  1 
       445 .  78 HIS CA  C  64.6  0.1  1 
       446 .  78 HIS CB  C  32.3  0.1  1 
       447 .  78 HIS N   N 117.0  0.1  1 
       448 .  79 ILE H   H   7.94 0.03 1 
       449 .  79 ILE C   C 178.2  0.1  1 
       450 .  79 ILE CA  C  65.4  0.1  1 
       451 .  79 ILE CB  C  40.9  0.1  1 
       452 .  79 ILE N   N 117.5  0.1  1 
       453 .  80 ALA H   H   8.89 0.03 1 
       454 .  80 ALA HA  H   3.94 0.03 1 
       455 .  80 ALA C   C 178.4  0.1  1 
       456 .  80 ALA CA  C  55.2  0.1  1 
       457 .  80 ALA CB  C  20.6  0.1  1 
       458 .  80 ALA N   N 120.0  0.1  1 
       459 .  81 ALA H   H   8.35 0.03 1 
       460 .  81 ALA HA  H   4.12 0.03 1 
       461 .  81 ALA C   C 178.9  0.1  1 
       462 .  81 ALA CA  C  55.7  0.1  1 
       463 .  81 ALA CB  C  19.4  0.1  1 
       464 .  81 ALA N   N 118.5  0.1  1 
       465 .  82 SER H   H   8.03 0.03 1 
       466 .  82 SER HA  H   3.97 0.03 1 
       467 .  82 SER C   C 177.4  0.1  1 
       468 .  82 SER CA  C  62.0  0.1  1 
       469 .  82 SER CB  C  64.2  0.1  1 
       470 .  82 SER N   N 109.5  0.1  1 
       471 .  83 ALA H   H   8.06 0.03 1 
       472 .  83 ALA HA  H   4.44 0.03 1 
       473 .  83 ALA C   C 177.3  0.1  1 
       474 .  83 ALA CA  C  52.9  0.1  1 
       475 .  83 ALA CB  C  19.9  0.1  1 
       476 .  83 ALA N   N 118.1  0.1  1 
       477 .  84 GLY H   H   7.51 0.03 1 
       478 .  84 GLY HA2 H   3.84 0.03 2 
       479 .  84 GLY HA3 H   3.52 0.03 2 
       480 .  84 GLY C   C 174.0  0.1  1 
       481 .  84 GLY CA  C  47.7  0.1  1 
       482 .  84 GLY N   N 107.1  0.1  1 
       483 .  85 ARG H   H   8.17 0.03 1 
       484 .  85 ARG C   C 175.3  0.03 1 
       485 .  85 ARG CA  C  51.6  0.1  1 
       486 .  85 ARG CB  C  27.7  0.1  1 
       487 .  85 ARG N   N 117.0  0.1  1 
       488 .  86 ASP H   H   8.55 0.03 1 
       489 .  86 ASP HA  H   3.72 0.03 1 
       490 .  86 ASP C   C 177.1  0.1  1 
       491 .  86 ASP CA  C  59.5  0.1  1 
       492 .  86 ASP CB  C  40.5  0.1  1 
       493 .  86 ASP N   N 125.1  0.1  1 
       494 .  87 GLU H   H   8.92 0.03 1 
       495 .  87 GLU HA  H   3.95 0.03 1 
       496 .  87 GLU C   C 179.9  0.1  1 
       497 .  87 GLU CA  C  59.9  0.1  1 
       498 .  87 GLU CB  C  29.6  0.1  1 
       499 .  87 GLU N   N 116.3  0.1  1 
       500 .  88 ILE H   H   7.44 0.03 1 
       501 .  88 ILE HA  H   3.67 0.03 1 
       502 .  88 ILE C   C 177.1  0.1  1 
       503 .  88 ILE CA  C  65.4  0.1  1 
       504 .  88 ILE CB  C  38.0  0.1  1 
       505 .  88 ILE N   N 120.6  0.1  1 
       506 .  89 VAL H   H   8.10 0.03 1 
       507 .  89 VAL HA  H   3.26 0.03 1 
       508 .  89 VAL C   C 176.7  0.1  1 
       509 .  89 VAL CA  C  68.7  0.1  1 
       510 .  89 VAL CB  C  30.9  0.1  1 
       511 .  89 VAL N   N 121.0  0.1  1 
       512 .  90 LYS H   H   7.69 0.03 1 
       513 .  90 LYS HA  H   3.81 0.03 1 
       514 .  90 LYS C   C 179.3  0.1  1 
       515 .  90 LYS CA  C  60.4  0.1  1 
       516 .  90 LYS CB  C  33.1  0.1  1 
       517 .  90 LYS N   N 118.6  0.1  1 
       518 .  91 ALA H   H   7.66 0.03 1 
       519 .  91 ALA HA  H   4.12 0.03 1 
       520 .  91 ALA C   C 180.9  0.1  1 
       521 .  91 ALA CA  C  55.2  0.1  1 
       522 .  91 ALA CB  C  18.2  0.1  1 
       523 .  91 ALA N   N 122.1  0.1  1 
       524 .  92 LEU H   H   8.60 0.03 1 
       525 .  92 LEU HA  H   3.80 0.03 1 
       526 .  92 LEU C   C 180.2  0.1  1 
       527 .  92 LEU CA  C  58.1  0.1  1 
       528 .  92 LEU CB  C  41.7  0.1  1 
       529 .  92 LEU N   N 117.6  0.1  1 
       530 .  93 LEU H   H   8.62 0.03 1 
       531 .  93 LEU HA  H   3.98 0.03 1 
       532 .  93 LEU C   C 181.3  0.1  1 
       533 .  93 LEU CA  C  58.8  0.1  1 
       534 .  93 LEU CB  C  40.7  0.1  1 
       535 .  93 LEU N   N 120.1  0.1  1 
       536 .  94 GLY H   H   7.84 0.03 1 
       537 .  94 GLY HA2 H   4.09 0.03 2 
       538 .  94 GLY HA3 H   3.90 0.03 2 
       539 .  94 GLY C   C 174.3  0.1  1 
       540 .  94 GLY CA  C  46.7  0.1  1 
       541 .  94 GLY N   N 106.7  0.1  1 
       542 .  95 LYS H   H   7.24 0.03 1 
       543 .  95 LYS HA  H   4.62 0.03 1 
       544 .  95 LYS C   C 176.2  0.1  1 
       545 .  95 LYS CA  C  53.8  0.1  1 
       546 .  95 LYS CB  C  32.7  0.1  1 
       547 .  95 LYS N   N 119.1  0.1  1 
       548 .  96 GLY H   H   7.66 0.03 1 
       549 .  96 GLY HA2 H   4.14 0.03 2 
       550 .  96 GLY HA3 H   3.80 0.03 2 
       551 .  96 GLY C   C 175.8  0.1  1 
       552 .  96 GLY CA  C  46.4  0.1  1 
       553 .  96 GLY N   N 105.2  0.1  1 
       554 .  97 ALA H   H   7.76 0.03 1 
       555 .  97 ALA HA  H   4.40 0.03 1 
       556 .  97 ALA C   C 177.4  0.1  1 
       557 .  97 ALA CA  C  52.9  0.1  1 
       558 .  97 ALA CB  C  20.6  0.1  1 
       559 .  97 ALA N   N 122.8  0.1  1 
       560 .  98 GLN H   H   8.84 0.03 1 
       561 .  98 GLN HA  H   4.25 0.03 1 
       562 .  98 GLN C   C 177.5  0.1  1 
       563 .  98 GLN CA  C  56.1  0.1  1 
       564 .  98 GLN CB  C  28.8  0.1  1 
       565 .  98 GLN N   N 121.2  0.1  1 
       566 .  99 VAL H   H   8.16 0.03 1 
       567 .  99 VAL HA  H   3.62 0.03 1 
       568 .  99 VAL C   C 174.7  0.1  1 
       569 .  99 VAL CA  C  64.6  0.1  1 
       570 .  99 VAL CB  C  32.7  0.1  1 
       571 .  99 VAL N   N 124.5  0.1  1 
       572 . 100 ASN H   H   8.59 0.03 1 
       573 . 100 ASN HA  H   5.07 0.03 1 
       574 . 100 ASN C   C 173.9  0.1  1 
       575 . 100 ASN CA  C  52.8  0.1  1 
       576 . 100 ASN CB  C  39.2  0.1  1 
       577 . 100 ASN N   N 116.8  0.1  1 
       578 . 101 ALA H   H   6.46 0.03 1 
       579 . 101 ALA HA  H   4.25 0.03 1 
       580 . 101 ALA C   C 170.5  0.1  1 
       581 . 101 ALA CA  C  53.1  0.1  1 
       582 . 101 ALA CB  C  21.0  0.1  1 
       583 . 101 ALA N   N 121.5  0.1  1 
       584 . 102 VAL H   H   8.21 0.03 1 
       585 . 102 VAL HA  H   5.00 0.03 1 
       586 . 102 VAL C   C 176.0  0.1  1 
       587 . 102 VAL CA  C  59.3  0.1  1 
       588 . 102 VAL CB  C  35.7  0.1  1 
       589 . 102 VAL N   N 111.6  0.1  1 
       590 . 103 ASN H   H   7.34 0.03 1 
       591 . 103 ASN HA  H   5.23 0.03 1 
       592 . 103 ASN C   C 178.3  0.1  1 
       593 . 103 ASN CA  C  50.8  0.1  1 
       594 . 103 ASN CB  C  40.1  0.1  1 
       595 . 103 ASN N   N 119.9  0.1  1 
       596 . 104 GLN H   H   7.88 0.03 1 
       597 . 104 GLN HA  H   4.20 0.03 1 
       598 . 104 GLN C   C 175.5  0.1  1 
       599 . 104 GLN CA  C  59.0  0.1  1 
       600 . 104 GLN CB  C  28.1  0.1  1 
       601 . 104 GLN N   N 117.1  0.1  1 
       602 . 105 ASN H   H   7.23 0.03 1 
       603 . 105 ASN HA  H   4.89 0.03 1 
       604 . 105 ASN C   C 174.7  0.1  1 
       605 . 105 ASN CA  C  53.5  0.1  1 
       606 . 105 ASN CB  C  40.3  0.1  1 
       607 . 105 ASN N   N 114.8  0.1  1 
       608 . 106 GLY H   H   7.90 0.03 1 
       609 . 106 GLY HA2 H   3.35 0.03 1 
       610 . 106 GLY HA3 H   3.54 0.03 1 
       611 . 106 GLY C   C 172.9  0.1  1 
       612 . 106 GLY CA  C  46.1  0.1  1 
       613 . 106 GLY N   N 108.0  0.1  1 
       614 . 107 CYS H   H   7.33 0.03 1 
       615 . 107 CYS HA  H   4.35 0.03 1 
       616 . 107 CYS C   C 176.5  0.1  1 
       617 . 107 CYS CA  C  58.7  0.1  1 
       618 . 107 CYS CB  C  30.2  0.1  1 
       619 . 107 CYS N   N 116.0  0.1  1 
       620 . 108 THR H   H  10.76 0.03 1 
       621 . 108 THR HA  H   5.67 0.03 1 
       622 . 108 THR CA  C  59.8  0.1  1 
       623 . 108 THR CB  C  69.3  0.1  1 
       624 . 108 THR N   N 121.4  0.1  1 
       625 . 109 PRO C   C 177.0  0.1  1 
       626 . 109 PRO CA  C  66.7  0.1  1 
       627 . 109 PRO CB  C  29.7  0.1  9 
       628 . 110 LEU H   H   8.36 0.03 1 
       629 . 110 LEU HA  H   3.94 0.03 1 
       630 . 110 LEU C   C 177.9  0.1  1 
       631 . 110 LEU CA  C  57.9  0.1  1 
       632 . 110 LEU CB  C  40.8  0.1  1 
       633 . 110 LEU N   N 117.0  0.1  1 
       634 . 111 HIS H   H   7.60 0.03 1 
       635 . 111 HIS HA  H   3.71 0.03 1 
       636 . 111 HIS C   C 178.3  0.1  1 
       637 . 111 HIS CA  C  64.5  0.1  1 
       638 . 111 HIS CB  C  31.0  0.1  1 
       639 . 111 HIS N   N 117.9  0.1  1 
       640 . 112 TYR H   H   6.74 0.03 1 
       641 . 112 TYR HA  H   4.40 0.03 1 
       642 . 112 TYR C   C 177.8  0.1  1 
       643 . 112 TYR CA  C  61.6  0.1  1 
       644 . 112 TYR CB  C  38.4  0.1  1 
       645 . 112 TYR N   N 114.9  0.1  1 
       646 . 113 ALA H   H   8.27 0.03 1 
       647 . 113 ALA HA  H   3.90 0.03 1 
       648 . 113 ALA C   C 179.0  0.1  1 
       649 . 113 ALA CA  C  55.6  0.1  1 
       650 . 113 ALA CB  C  18.7  0.1  1 
       651 . 113 ALA N   N 121.5  0.1  1 
       652 . 114 ALA H   H   8.64 0.03 1 
       653 . 114 ALA HA  H   4.24 0.03 1 
       654 . 114 ALA C   C 179.8  0.1  1 
       655 . 114 ALA CA  C  55.1  0.1  1 
       656 . 114 ALA CB  C  20.0  0.1  1 
       657 . 114 ALA N   N 117.1  0.1  1 
       658 . 115 SER H   H   7.90 0.03 1 
       659 . 115 SER C   C 175.7  0.1  1 
       660 . 115 SER CA  C  62.3  0.1  1 
       661 . 115 SER N   N 112.4  0.1  1 
       662 . 116 LYS H   H   7.61 0.03 1 
       663 . 116 LYS HA  H   4.54 0.03 1 
       664 . 116 LYS C   C 175.1  0.1  1 
       665 . 116 LYS CA  C  55.4  0.1  1 
       666 . 116 LYS CB  C  32.5  0.1  1 
       667 . 116 LYS N   N 116.4  0.1  1 
       668 . 117 ASN H   H   7.44 0.03 1 
       669 . 117 ASN HA  H   4.04 0.03 1 
       670 . 117 ASN C   C 174.3  0.1  1 
       671 . 117 ASN CA  C  54.7  0.1  1 
       672 . 117 ASN CB  C  37.8  0.1  1 
       673 . 117 ASN N   N 115.5  0.1  1 
       674 . 118 ARG H   H   8.53 0.03 1 
       675 . 118 ARG HA  H   4.62 0.03 1 
       676 . 118 ARG C   C 175.8  0.1  1 
       677 . 118 ARG CA  C  52.2  0.1  1 
       678 . 118 ARG CB  C  27.1  0.1  1 
       679 . 118 ARG N   N 115.6  0.1  1 
       680 . 119 HIS H   H   7.39 0.03 1 
       681 . 119 HIS HA  H   3.85 0.03 1 
       682 . 119 HIS C   C 176.3  0.1  1 
       683 . 119 HIS CA  C  62.1  0.1  1 
       684 . 119 HIS CB  C  31.2  0.1  1 
       685 . 119 HIS N   N 121.9  0.1  1 
       686 . 120 GLU H   H   8.87 0.03 1 
       687 . 120 GLU HA  H   4.01 0.03 1 
       688 . 120 GLU C   C 180.6  0.1  1 
       689 . 120 GLU CA  C  60.7  0.1  1 
       690 . 120 GLU CB  C  28.2  0.1  1 
       691 . 120 GLU N   N 118.8  0.1  1 
       692 . 121 ILE H   H   8.12 0.03 1 
       693 . 121 ILE HA  H   3.70 0.03 1 
       694 . 121 ILE C   C 176.7  0.1  1 
       695 . 121 ILE CA  C  65.6  0.1  1 
       696 . 121 ILE CB  C  38.5  0.1  1 
       697 . 121 ILE N   N 121.0  0.1  1 
       698 . 122 ALA H   H   8.44 0.03 1 
       699 . 122 ALA HA  H   3.67 0.03 1 
       700 . 122 ALA C   C 178.4  0.1  1 
       701 . 122 ALA CA  C  56.7  0.1  1 
       702 . 122 ALA CB  C  18.2  0.1  1 
       703 . 122 ALA N   N 121.9  0.1  1 
       704 . 123 VAL H   H   7.82 0.03 1 
       705 . 123 VAL HA  H   3.31 0.03 1 
       706 . 123 VAL C   C 177.3  0.1  1 
       707 . 123 VAL CA  C  68.2  0.1  1 
       708 . 123 VAL CB  C  32.2  0.1  1 
       709 . 123 VAL N   N 116.4  0.1  1 
       710 . 124 MET H   H   7.77 0.03 1 
       711 . 124 MET HA  H   3.86 0.03 1 
       712 . 124 MET C   C 180.0  0.1  1 
       713 . 124 MET CA  C  60.4  0.1  1 
       714 . 124 MET CB  C  34.0  0.1  1 
       715 . 124 MET N   N 117.5  0.1  1 
       716 . 125 LEU H   H   8.36 0.03 1 
       717 . 125 LEU HA  H   3.75 0.03 1 
       718 . 125 LEU C   C 178.5  0.1  1 
       719 . 125 LEU CA  C  58.0  0.1  1 
       720 . 125 LEU CB  C  40.8  0.1  1 
       721 . 125 LEU N   N 117.4  0.1  1 
       722 . 126 LEU H   H   8.39 0.03 1 
       723 . 126 LEU HA  H   3.73 0.03 1 
       724 . 126 LEU C   C 181.7  0.1  1 
       725 . 126 LEU CA  C  59.0  0.1  1 
       726 . 126 LEU CB  C  38.9  0.1  1 
       727 . 126 LEU N   N 122.3  0.1  1 
       728 . 127 GLU H   H   9.20 0.03 1 
       729 . 127 GLU HA  H   4.04 0.03 1 
       730 . 127 GLU C   C 177.9  0.1  1 
       731 . 127 GLU CA  C  59.5  0.1  1 
       732 . 127 GLU CB  C  29.8  0.1  1 
       733 . 127 GLU N   N 122.8  0.1  1 
       734 . 128 GLY H   H   7.47 0.03 1 
       735 . 128 GLY HA2 H   4.34 0.03 2 
       736 . 128 GLY HA3 H   3.44 0.03 2 
       737 . 128 GLY C   C 173.6  0.1  1 
       738 . 128 GLY CA  C  45.4  0.1  1 
       739 . 128 GLY N   N 105.2  0.1  1 
       740 . 129 GLY H   H   7.33 0.03 1 
       741 . 129 GLY HA2 H   3.76 0.03 1 
       742 . 129 GLY HA3 H   4.35 0.03 1 
       743 . 129 GLY C   C 175.2  0.1  1 
       744 . 129 GLY CA  C  45.3  0.1  1 
       745 . 129 GLY N   N 104.9  0.1  1 
       746 . 130 ALA H   H   8.51 0.03 1 
       747 . 130 ALA HA  H   3.98 0.03 1 
       748 . 130 ALA C   C 176.1  0.1  1 
       749 . 130 ALA CA  C  52.9  0.1  1 
       750 . 130 ALA CB  C  19.3  0.1  1 
       751 . 130 ALA N   N 123.9  0.1  1 
       752 . 131 ASN H   H   9.04 0.03 1 
       753 . 131 ASN HA  H   4.93 0.03 1 
       754 . 131 ASN CA  C  50.1  0.1  1 
       755 . 131 ASN CB  C  38.4  0.1  1 
       756 . 131 ASN N   N 121.2  0.1  1 
       757 . 132 PRO C   C 177.3  0.1  1 
       758 . 132 PRO CA  C  64.5  0.1  1 
       759 . 133 ASP H   H   7.63 0.03 1 
       760 . 133 ASP HA  H   4.79 0.03 9 
       761 . 133 ASP C   C 174.3  0.1  1 
       762 . 133 ASP CA  C  53.6  0.1  1 
       763 . 133 ASP CB  C  40.8  0.1  1 
       764 . 133 ASP N   N 118.6  0.1  1 
       765 . 134 ALA H   H   6.62 0.03 1 
       766 . 134 ALA HA  H   4.03 0.03 1 
       767 . 134 ALA C   C 177.9  0.1  1 
       768 . 134 ALA CA  C  54.3  0.1  1 
       769 . 134 ALA CB  C  19.1  0.1  1 
       770 . 134 ALA N   N 122.6  0.1  1 
       771 . 135 LYS H   H   8.85 0.03 1 
       772 . 135 LYS C   C 176.9  0.1  1 
       773 . 135 LYS CA  C  55.4  0.1  1 
       774 . 135 LYS CB  C  36.8  0.1  1 
       775 . 135 LYS N   N 123.7  0.1  1 
       776 . 136 ASP H   H   8.55 0.03 1 
       777 . 136 ASP HA  H   4.82 0.03 1 
       778 . 136 ASP C   C 178.8  0.1  1 
       779 . 136 ASP CA  C  52.9  0.1  1 
       780 . 136 ASP CB  C  42.2  0.1  1 
       781 . 136 ASP N   N 124.0  0.1  1 
       782 . 137 HIS H   H   7.67 0.03 1 
       783 . 137 HIS HA  H   4.57 0.03 1 
       784 . 137 HIS C   C 176.1  0.1  1 
       785 . 137 HIS CA  C  57.6  0.1  1 
       786 . 137 HIS CB  C  30.2  0.1  1 
       787 . 137 HIS N   N 115.6  0.1  1 
       788 . 138 TYR H   H   8.52 0.03 1 
       789 . 138 TYR HA  H   4.59 0.03 1 
       790 . 138 TYR C   C 174.0  0.1  1 
       791 . 138 TYR CA  C  57.9  0.1  1 
       792 . 138 TYR CB  C  38.0  0.1  1 
       793 . 138 TYR N   N 122.1  0.1  1 
       794 . 139 GLU H   H   8.23 0.03 1 
       795 . 139 GLU HA  H   3.62 0.03 1 
       796 . 139 GLU C   C 171.3  0.1  1 
       797 . 139 GLU CA  C  58.2  0.1  1 
       798 . 139 GLU CB  C  27.0  0.1  1 
       799 . 139 GLU N   N 113.2  0.1  1 
       800 . 140 ALA H   H   8.11 0.03 1 
       801 . 140 ALA HA  H   4.15 0.03 1 
       802 . 140 ALA C   C 179.2  0.1  1 
       803 . 140 ALA CA  C  51.1  0.1  1 
       804 . 140 ALA CB  C  21.6  0.1  1 
       805 . 140 ALA N   N 116.1  0.1  1 
       806 . 141 THR H   H   9.14 0.03 1 
       807 . 141 THR HA  H   5.23 0.03 1 
       808 . 141 THR C   C 176.9  0.1  1 
       809 . 141 THR CA  C  60.8  0.1  1 
       810 . 141 THR CB  C  74.5  0.1  1 
       811 . 141 THR N   N 114.6  0.1  1 
       812 . 142 ALA H   H  10.24 0.03 1 
       813 . 142 ALA HA  H   3.90 0.03 1 
       814 . 142 ALA C   C 178.4  0.1  1 
       815 . 142 ALA CA  C  56.1  0.1  1 
       816 . 142 ALA CB  C  18.3  0.1  1 
       817 . 142 ALA N   N 125.3  0.1  1 
       818 . 143 MET H   H   9.15 0.03 1 
       819 . 143 MET HA  H   3.90 0.03 1 
       820 . 143 MET C   C 178.8  0.1  1 
       821 . 143 MET CA  C  58.5  0.1  1 
       822 . 143 MET CB  C  31.6  0.1  1 
       823 . 143 MET N   N 119.0  0.1  1 
       824 . 144 HIS H   H   8.04 0.03 1 
       825 . 144 HIS HA  H   3.73 0.03 1 
       826 . 144 HIS C   C 177.5  0.1  1 
       827 . 144 HIS CA  C  64.6  0.1  1 
       828 . 144 HIS CB  C  30.9  0.1  1 
       829 . 144 HIS N   N 118.8  0.1  1 
       830 . 145 ARG H   H   7.26 0.03 1 
       831 . 145 ARG HA  H   4.10 0.03 1 
       832 . 145 ARG C   C 178.5  0.1  1 
       833 . 145 ARG CA  C  58.2  0.1  1 
       834 . 145 ARG CB  C  30.2  0.1  1 
       835 . 145 ARG N   N 115.2  0.1  1 
       836 . 146 ALA H   H   8.37 0.03 1 
       837 . 146 ALA HA  H   4.11 0.03 1 
       838 . 146 ALA C   C 179.0  0.1  1 
       839 . 146 ALA CA  C  55.2  0.1  1 
       840 . 146 ALA CB  C  19.3  0.1  1 
       841 . 146 ALA N   N 119.5  0.1  1 
       842 . 147 ALA H   H   8.43 0.03 1 
       843 . 147 ALA HA  H   3.85 0.03 1 
       844 . 147 ALA C   C 178.0  0.1  1 
       845 . 147 ALA CA  C  56.0  0.1  1 
       846 . 147 ALA CB  C  20.2  0.1  1 
       847 . 147 ALA N   N 119.5  0.1  1 
       848 . 148 ALA H   H   7.59 0.03 1 
       849 . 148 ALA HA  H   3.83 0.03 1 
       850 . 148 ALA C   C 179.5  0.1  1 
       851 . 148 ALA CA  C  55.3  0.1  1 
       852 . 148 ALA CB  C  20.2  0.1  1 
       853 . 148 ALA N   N 116.2  0.1  1 
       854 . 149 LYS H   H   7.36 0.03 1 
       855 . 149 LYS HA  H   4.28 0.03 1 
       856 . 149 LYS CA  C  55.7  0.1  1 
       857 . 149 LYS CB  C  33.4  0.1  1 
       858 . 149 LYS N   N 111.4  0.1  1 
       859 . 150 GLY C   C 173.3  0.1  1 
       860 . 150 GLY CA  C  47.1  0.1  1 
       861 . 151 ASN H   H   8.25 0.03 1 
       862 . 151 ASN HA  H   5.11 0.03 1 
       863 . 151 ASN C   C 175.2  0.1  1 
       864 . 151 ASN CA  C  51.7  0.1  1 
       865 . 151 ASN CB  C  38.5  0.1  1 
       866 . 151 ASN N   N 119.4  0.1  1 
       867 . 152 LEU H   H   7.60 0.03 1 
       868 . 152 LEU C   C 178.0  0.1  1 
       869 . 152 LEU CA  C  59.9  0.1  1 
       870 . 152 LEU N   N 124.3  0.1  1 
       871 . 153 LYS H   H   8.53 0.03 1 
       872 . 153 LYS C   C 178.7  0.1  1 
       873 . 153 LYS CA  C  60.1  0.1  1 
       874 . 153 LYS CB  C  31.9  0.1  1 
       875 . 153 LYS N   N 117.8  0.1  1 
       876 . 154 MET H   H   7.90 0.03 1 
       877 . 154 MET C   C 177.7  0.1  1 
       878 . 154 MET CA  C  56.2  0.1  1 
       879 . 154 MET N   N 116.7  0.1  1 
       880 . 155 ILE H   H   7.88 0.03 1 
       881 . 155 ILE HA  H   3.51 0.03 1 
       882 . 155 ILE C   C 177.4  0.1  1 
       883 . 155 ILE CA  C  67.1  0.1  1 
       884 . 155 ILE CB  C  37.6  0.1  1 
       885 . 155 ILE N   N 119.6  0.1  1 
       886 . 156 HIS H   H   7.98 0.03 1 
       887 . 156 HIS HA  H   4.09 0.03 1 
       888 . 156 HIS C   C 179.3  0.1  1 
       889 . 156 HIS CA  C  61.8  0.1  1 
       890 . 156 HIS N   N 117.7  0.1  1 
       891 . 157 ILE H   H   8.05 0.03 1 
       892 . 157 ILE HA  H   3.82 0.03 1 
       893 . 157 ILE C   C 177.5  0.1  1 
       894 . 157 ILE CA  C  66.0  0.1  1 
       895 . 157 ILE CB  C  39.1  0.1  1 
       896 . 157 ILE N   N 120.9  0.1  1 
       897 . 158 LEU H   H   8.30 0.03 1 
       898 . 158 LEU C   C 179.4  0.1  1 
       899 . 158 LEU CA  C  59.3  0.1  1 
       900 . 158 LEU CB  C  41.2  0.1  1 
       901 . 158 LEU N   N 119.0  0.1  1 
       902 . 159 LEU H   H   8.64 0.03 1 
       903 . 159 LEU HA  H   4.08 0.03 1 
       904 . 159 LEU C   C 181.4  0.1  1 
       905 . 159 LEU CA  C  58.2  0.1  1 
       906 . 159 LEU CB  C  41.4  0.1  1 
       907 . 159 LEU N   N 117.8  0.1  1 
       908 . 160 TYR H   H   8.32 0.03 1 
       909 . 160 TYR HA  H   4.03 0.03 1 
       910 . 160 TYR C   C 177.3  0.1  1 
       911 . 160 TYR CA  C  61.9  0.1  1 
       912 . 160 TYR CB  C  37.9  0.1  1 
       913 . 160 TYR N   N 124.5  0.1  1 
       914 . 161 TYR H   H   7.49 0.03 1 
       915 . 161 TYR HA  H   4.29 0.03 1 
       916 . 161 TYR C   C 173.2  0.1  1 
       917 . 161 TYR CA  C  59.8  0.1  1 
       918 . 161 TYR CB  C  38.1  0.1  1 
       919 . 161 TYR N   N 115.8  0.1  1 
       920 . 162 LYS H   H   7.67 0.03 1 
       921 . 162 LYS HA  H   3.85 0.03 1 
       922 . 162 LYS C   C 176.3  0.1  1 
       923 . 162 LYS CA  C  57.2  0.1  1 
       924 . 162 LYS CB  C  27.9  0.1  1 
       925 . 162 LYS N   N 109.5  0.1  1 
       926 . 163 ALA H   H   8.14 0.03 1 
       927 . 163 ALA HA  H   4.10 0.03 1 
       928 . 163 ALA C   C 177.2  0.1  1 
       929 . 163 ALA CA  C  53.2  0.1  1 
       930 . 163 ALA CB  C  21.5  0.1  1 
       931 . 163 ALA N   N 121.7  0.1  1 
       932 . 164 SER H   H  10.09 0.03 1 
       933 . 164 SER HA  H   4.51 0.03 1 
       934 . 164 SER C   C 176.3  0.1  1 
       935 . 164 SER CA  C  59.7  0.1  1 
       936 . 164 SER CB  C  63.6  0.1  1 
       937 . 164 SER N   N 118.9  0.1  1 
       938 . 165 THR H   H   8.43 0.03 1 
       939 . 165 THR HA  H   4.18 0.03 1 
       940 . 165 THR C   C 175.2  0.1  1 
       941 . 165 THR CA  C  63.1  0.1  1 
       942 . 165 THR CB  C  70.3  0.1  1 
       943 . 165 THR N   N 112.0  0.1  1 
       944 . 166 ASN H   H   8.08 0.03 1 
       945 . 166 ASN HA  H   5.11 0.03 1 
       946 . 166 ASN C   C 174.0  0.1  1 
       947 . 166 ASN CA  C  53.7  0.1  1 
       948 . 166 ASN CB  C  39.7  0.1  1 
       949 . 166 ASN N   N 119.0  0.1  1 
       950 . 167 ILE H   H   6.96 0.03 1 
       951 . 167 ILE HA  H   4.10 0.03 1 
       952 . 167 ILE C   C 174.9  0.1  1 
       953 . 167 ILE CA  C  62.4  0.1  1 
       954 . 167 ILE CB  C  38.6  0.1  1 
       955 . 167 ILE N   N 120.1  0.1  1 
       956 . 168 GLN H   H   8.52 0.03 1 
       957 . 168 GLN HA  H   4.57 0.03 1 
       958 . 168 GLN C   C 174.9  0.1  1 
       959 . 168 GLN CA  C  55.3  0.1  1 
       960 . 168 GLN CB  C  33.9  0.1  1 
       961 . 168 GLN N   N 124.7  0.1  1 
       962 . 169 ASP H   H   8.20 0.03 1 
       963 . 169 ASP HA  H   4.95 0.03 1 
       964 . 169 ASP C   C 179.8  0.1  1 
       965 . 169 ASP CA  C  53.4  0.1  1 
       966 . 169 ASP CB  C  41.7  0.1  1 
       967 . 169 ASP N   N 122.0  0.1  1 
       968 . 170 THR H   H   7.92 0.03 1 
       969 . 170 THR HA  H   4.01 0.03 1 
       970 . 170 THR C   C 176.1  0.1  1 
       971 . 170 THR CA  C  65.5  0.1  1 
       972 . 170 THR CB  C  69.4  0.1  1 
       973 . 170 THR N   N 111.3  0.1  1 
       974 . 171 GLU H   H   8.18 0.03 1 
       975 . 171 GLU HA  H   4.49 0.03 1 
       976 . 171 GLU C   C 177.0  0.1  1 
       977 . 171 GLU CA  C  56.7  0.1  1 
       978 . 171 GLU CB  C  30.0  0.1  1 
       979 . 171 GLU N   N 120.2  0.1  1 
       980 . 172 GLY H   H   8.73 0.03 1 
       981 . 172 GLY C   C 172.9  0.1  1 
       982 . 172 GLY CA  C  46.2  0.1  1 
       983 . 172 GLY N   N 110.6  0.1  1 
       984 . 173 ASN H   H   8.69 0.03 1 
       985 . 173 ASN HA  H   4.53 0.03 1 
       986 . 173 ASN C   C 178.0  0.1  1 
       987 . 173 ASN CA  C  54.3  0.1  1 
       988 . 173 ASN CB  C  39.4  0.1  1 
       989 . 173 ASN N   N 119.8  0.1  1 
       990 . 174 THR H   H  10.78 0.03 1 
       991 . 174 THR HA  H   5.63 0.03 1 
       992 . 174 THR CA  C  60.1  0.1  1 
       993 . 174 THR CB  C  69.1  0.1  1 
       994 . 174 THR N   N 122.1  0.1  1 
       995 . 175 PRO C   C 176.8  0.1  1 
       996 . 175 PRO CA  C  66.2  0.1  1 
       997 . 175 PRO CB  C  31.5  0.1  1 
       998 . 176 LEU H   H   8.60 0.03 1 
       999 . 176 LEU HA  H   4.01 0.03 1 
      1000 . 176 LEU C   C 179.3  0.1  1 
      1001 . 176 LEU CA  C  58.0  0.1  1 
      1002 . 176 LEU CB  C  41.5  0.1  1 
      1003 . 176 LEU N   N 115.3  0.1  1 
      1004 . 177 HIS H   H   7.82 0.03 1 
      1005 . 177 HIS HA  H   3.65 0.03 1 
      1006 . 177 HIS C   C 177.5  0.1  1 
      1007 . 177 HIS CA  C  64.7  0.1  1 
      1008 . 177 HIS CB  C  31.9  0.1  1 
      1009 . 177 HIS N   N 118.3  0.1  1 
      1010 . 178 LEU H   H   7.18 0.03 1 
      1011 . 178 LEU HA  H   4.16 0.03 1 
      1012 . 178 LEU C   C 179.2  0.1  1 
      1013 . 178 LEU CA  C  58.1  0.1  1 
      1014 . 178 LEU CB  C  40.4  0.1  1 
      1015 . 178 LEU N   N 114.7  0.1  1 
      1016 . 179 ALA H   H   8.22 0.03 1 
      1017 . 179 ALA C   C 179.7  0.1  1 
      1018 . 179 ALA CA  C  55.1  0.1  1 
      1019 . 179 ALA CB  C  18.2  0.1  1 
      1020 . 179 ALA N   N 119.7  0.1  1 
      1021 . 180 CYS H   H   8.22 0.03 1 
      1022 . 180 CYS HA  H   4.00 0.03 1 
      1023 . 180 CYS C   C 177.8  0.1  1 
      1024 . 180 CYS CA  C  65.0  0.1  1 
      1025 . 180 CYS CB  C  27.6  0.1  1 
      1026 . 180 CYS N   N 114.8  0.1  1 
      1027 . 181 ASP H   H   8.56 0.03 1 
      1028 . 181 ASP HA  H   4.55 0.03 1 
      1029 . 181 ASP C   C 177.2  0.1  1 
      1030 . 181 ASP CA  C  57.8  0.1  1 
      1031 . 181 ASP CB  C  42.6  0.1  1 
      1032 . 181 ASP N   N 122.5  0.1  1 
      1033 . 182 GLU H   H   7.40 0.03 1 
      1034 . 182 GLU HA  H   4.49 0.03 1 
      1035 . 182 GLU C   C 174.8  0.1  1 
      1036 . 182 GLU CA  C  56.6  0.1  1 
      1037 . 182 GLU CB  C  30.3  0.1  1 
      1038 . 182 GLU N   N 113.0  0.1  1 
      1039 . 183 GLU H   H   7.78 0.03 1 
      1040 . 183 GLU HA  H   3.46 0.03 1 
      1041 . 183 GLU C   C 174.9  0.1  1 
      1042 . 183 GLU CA  C  58.0  0.1  1 
      1043 . 183 GLU CB  C  28.9  0.1  1 
      1044 . 183 GLU N   N 118.2  0.1  1 
      1045 . 184 ARG H   H   8.83 0.03 1 
      1046 . 184 ARG HA  H   4.52 0.03 1 
      1047 . 184 ARG C   C 175.5  0.1  1 
      1048 . 184 ARG CA  C  53.1  0.1  1 
      1049 . 184 ARG CB  C  28.8  0.1  1 
      1050 . 184 ARG N   N 119.5  0.1  1 
      1051 . 185 VAL H   H   7.47 0.03 1 
      1052 . 185 VAL HA  H   3.46 0.03 1 
      1053 . 185 VAL C   C 177.6  0.1  1 
      1054 . 185 VAL CA  C  67.8  0.1  1 
      1055 . 185 VAL CB  C  32.8  0.1  1 
      1056 . 185 VAL N   N 122.1  0.1  1 
      1057 . 186 GLU H   H   8.79 0.03 1 
      1058 . 186 GLU HA  H   3.90 0.03 1 
      1059 . 186 GLU C   C 179.7  0.1  1 
      1060 . 186 GLU CA  C  59.5  0.1  1 
      1061 . 186 GLU CB  C  28.8  0.1  1 
      1062 . 186 GLU N   N 117.8  0.1  1 
      1063 . 187 GLU H   H  10.24 0.03 1 
      1064 . 187 GLU HA  H   3.58 0.03 1 
      1065 . 187 GLU C   C 177.4  0.1  1 
      1066 . 187 GLU CA  C  62.1  0.1  1 
      1067 . 187 GLU CB  C  28.2  0.1  1 
      1068 . 187 GLU N   N 123.7  0.1  1 
      1069 . 188 ALA H   H   8.45 0.03 1 
      1070 . 188 ALA HA  H   3.76 0.03 1 
      1071 . 188 ALA C   C 178.8  0.1  1 
      1072 . 188 ALA CA  C  55.7  0.1  1 
      1073 . 188 ALA CB  C  19.7  0.1  1 
      1074 . 188 ALA N   N 120.7  0.1  1 
      1075 . 189 LYS H   H   8.06 0.03 1 
      1076 . 189 LYS HA  H   3.57 0.03 1 
      1077 . 189 LYS C   C 178.6  0.1  1 
      1078 . 189 LYS CA  C  60.5  0.1  1 
      1079 . 189 LYS CB  C  32.9  0.1  1 
      1080 . 189 LYS N   N 115.6  0.1  1 
      1081 . 190 LEU H   H   7.92 0.03 1 
      1082 . 190 LEU HA  H   4.07 0.03 1 
      1083 . 190 LEU C   C 179.7  0.1  1 
      1084 . 190 LEU CA  C  58.0  0.1  1 
      1085 . 190 LEU CB  C  41.2  0.1  1 
      1086 . 190 LEU N   N 120.5  0.1  1 
      1087 . 191 LEU H   H   8.13 0.03 1 
      1088 . 191 LEU HA  H   3.70 0.03 1 
      1089 . 191 LEU C   C 179.2  0.1  1 
      1090 . 191 LEU CA  C  59.2  0.1  1 
      1091 . 191 LEU CB  C  41.1  0.1  1 
      1092 . 191 LEU N   N 118.6  0.1  1 
      1093 . 192 VAL H   H   8.20 0.03 1 
      1094 . 192 VAL HA  H   3.88 0.03 1 
      1095 . 192 VAL C   C 179.9  0.1  1 
      1096 . 192 VAL CA  C  67.4  0.1  1 
      1097 . 192 VAL CB  C  31.8  0.1  1 
      1098 . 192 VAL N   N 119.5  0.1  1 
      1099 . 193 SER H   H   8.56 0.03 1 
      1100 . 193 SER HA  H   4.30 0.03 1 
      1101 . 193 SER C   C 174.9  0.1  1 
      1102 . 193 SER CA  C  61.9  0.1  1 
      1103 . 193 SER CB  C  63.6  0.1  1 
      1104 . 193 SER N   N 118.2  0.1  1 
      1105 . 194 GLN H   H   7.35 0.03 1 
      1106 . 194 GLN HA  H   4.53 0.03 1 
      1107 . 194 GLN C   C 175.7  0.1  1 
      1108 . 194 GLN CA  C  55.2  0.1  1 
      1109 . 194 GLN CB  C  28.4  0.1  1 
      1110 . 194 GLN N   N 118.3  0.1  1 
      1111 . 195 GLY H   H   7.53 0.03 1 
      1112 . 195 GLY HA2 H   4.37 0.03 2 
      1113 . 195 GLY HA3 H   3.72 0.03 2 
      1114 . 195 GLY C   C 174.9  0.1  1 
      1115 . 195 GLY CA  C  46.1  0.1  1 
      1116 . 195 GLY N   N 105.9  0.1  1 
      1117 . 196 ALA H   H   8.39 0.03 1 
      1118 . 196 ALA HA  H   4.38 0.03 1 
      1119 . 196 ALA C   C 177.2  0.1  1 
      1120 . 196 ALA CA  C  53.1  0.1  1 
      1121 . 196 ALA CB  C  20.8  0.1  1 
      1122 . 196 ALA N   N 125.8  0.1  1 
      1123 . 197 SER H   H   9.04 0.03 1 
      1124 . 197 SER HA  H   4.07 0.03 1 
      1125 . 197 SER C   C 177.7  0.1  1 
      1126 . 197 SER CA  C  57.4  0.1  1 
      1127 . 197 SER CB  C  64.5  0.1  1 
      1128 . 197 SER N   N 116.6  0.1  1 
      1129 . 198 ILE H   H   7.97 0.03 1 
      1130 . 198 ILE HA  H   3.87 0.03 1 
      1131 . 198 ILE C   C 175.0  0.1  1 
      1132 . 198 ILE CA  C  62.7  0.1  1 
      1133 . 198 ILE CB  C  37.7  0.1  1 
      1134 . 198 ILE N   N 118.4  0.1  1 
      1135 . 199 TYR H   H   8.12 0.03 1 
      1136 . 199 TYR HA  H   4.67 0.03 1 
      1137 . 199 TYR C   C 175.5  0.1  1 
      1138 . 199 TYR CA  C  58.4  0.1  1 
      1139 . 199 TYR CB  C  40.5  0.1  1 
      1140 . 199 TYR N   N 117.8  0.1  1 
      1141 . 200 ILE H   H   6.36 0.03 1 
      1142 . 200 ILE HA  H   3.98 0.03 1 
      1143 . 200 ILE C   C 174.6  0.1  1 
      1144 . 200 ILE CA  C  62.1  0.1  1 
      1145 . 200 ILE CB  C  39.8  0.1  1 
      1146 . 200 ILE N   N 120.1  0.1  1 
      1147 . 201 GLU H   H   8.57 0.03 1 
      1148 . 201 GLU HA  H   4.37 0.03 1 
      1149 . 201 GLU C   C 176.9  0.1  1 
      1150 . 201 GLU CA  C  55.8  0.1  1 
      1151 . 201 GLU CB  C  32.4  0.1  1 
      1152 . 201 GLU N   N 126.4  0.1  1 
      1153 . 202 ASN H   H   8.13 0.03 1 
      1154 . 202 ASN C   C 178.0  0.1  1 
      1155 . 202 ASN CA  C  51.4  0.1  1 
      1156 . 202 ASN CB  C  38.7  0.1  1 
      1157 . 202 ASN N   N 119.6  0.1  1 
      1158 . 203 LYS H   H   7.86 0.03 1 
      1159 . 203 LYS HA  H   4.08 0.03 1 
      1160 . 203 LYS C   C 177.6  0.1  1 
      1161 . 203 LYS CA  C  59.8  0.1  1 
      1162 . 203 LYS CB  C  32.3  0.1  1 
      1163 . 203 LYS N   N 117.4  0.1  1 
      1164 . 204 GLU H   H   7.44 0.03 1 
      1165 . 204 GLU HA  H   4.38 0.03 1 
      1166 . 204 GLU C   C 174.6  0.1  1 
      1167 . 204 GLU CA  C  56.5  0.1  1 
      1168 . 204 GLU CB  C  29.6  0.1  1 
      1169 . 204 GLU N   N 119.0  0.1  1 
      1170 . 205 GLU H   H   8.17 0.03 1 
      1171 . 205 GLU HA  H   3.76 0.03 1 
      1172 . 205 GLU C   C 174.8  0.1  1 
      1173 . 205 GLU CA  C  58.2  0.1  1 
      1174 . 205 GLU CB  C  26.7  0.1  1 
      1175 . 205 GLU N   N 112.7  0.1  1 
      1176 . 206 LYS H   H   7.67 0.03 1 
      1177 . 206 LYS HA  H   5.27 0.03 1 
      1178 . 206 LYS C   C 178.9  0.1  1 
      1179 . 206 LYS CA  C  54.3  0.1  1 
      1180 . 206 LYS CB  C  35.3  0.1  1 
      1181 . 206 LYS N   N 114.7  0.1  1 
      1182 . 207 THR H   H   9.29 0.03 1 
      1183 . 207 THR HA  H   5.33 0.03 1 
      1184 . 207 THR CA  C  60.8  0.1  1 
      1185 . 207 THR CB  C  69.0  0.1  1 
      1186 . 207 THR N   N 118.0  0.1  1 
      1187 . 208 PRO HA  H   3.90 0.03 1 
      1188 . 208 PRO C   C 176.8  0.1  1 
      1189 . 208 PRO CA  C  65.5  0.1  1 
      1190 . 209 LEU H   H   6.59 0.03 1 
      1191 . 209 LEU HA  H   3.80 0.03 1 
      1192 . 209 LEU C   C 179.2  0.1  1 
      1193 . 209 LEU CA  C  57.5  0.1  1 
      1194 . 209 LEU CB  C  40.6  0.1  1 
      1195 . 209 LEU N   N 107.2  0.1  1 
      1196 . 210 GLN H   H   7.35 0.03 1 
      1197 . 210 GLN HA  H   4.21 0.03 1 
      1198 . 210 GLN C   C 177.6  0.1  1 
      1199 . 210 GLN CA  C  58.1  0.1  1 
      1200 . 210 GLN CB  C  30.7  0.1  1 
      1201 . 210 GLN N   N 116.1  0.1  1 
      1202 . 211 VAL H   H   7.17 0.03 1 
      1203 . 211 VAL HA  H   4.40 0.03 1 
      1204 . 211 VAL C   C 175.2  0.1  1 
      1205 . 211 VAL CA  C  61.9  0.1  1 
      1206 . 211 VAL CB  C  32.3  0.1  1 
      1207 . 211 VAL N   N 112.2  0.1  1 
      1208 . 212 ALA H   H   6.94 0.03 1 
      1209 . 212 ALA HA  H   4.10 0.03 1 
      1210 . 212 ALA C   C 176.9  0.1  1 
      1211 . 212 ALA CA  C  52.9  0.1  1 
      1212 . 212 ALA CB  C  19.2  0.1  1 
      1213 . 212 ALA N   N 121.5  0.1  1 
      1214 . 213 LYS H   H   8.26 0.03 1 
      1215 . 213 LYS HA  H   4.57 0.03 1 
      1216 . 213 LYS C   C 177.9  0.1  1 
      1217 . 213 LYS CA  C  55.5  0.1  1 
      1218 . 213 LYS CB  C  35.3  0.1  1 
      1219 . 213 LYS N   N 123.2  0.1  1 
      1220 . 214 GLY H   H   8.76 0.03 1 
      1221 . 214 GLY CA  C  47.4  0.1  1 
      1222 . 214 GLY N   N 108.1  0.1  1 
      1223 . 215 GLY C   C 175.9  0.1  1 
      1224 . 215 GLY CA  C  45.7  0.1  1 
      1225 . 216 LEU H   H   7.73 0.03 1 
      1226 . 216 LEU HA  H   4.14 0.03 1 
      1227 . 216 LEU C   C 177.5  0.1  1 
      1228 . 216 LEU CA  C  58.0  0.1  1 
      1229 . 216 LEU CB  C  42.2  0.1  1 
      1230 . 216 LEU N   N 121.8  0.1  1 
      1231 . 217 GLY H   H   8.60 0.03 1 
      1232 . 217 GLY HA2 H   3.95 0.03 2 
      1233 . 217 GLY HA3 H   3.47 0.03 2 
      1234 . 217 GLY C   C 175.0  0.1  1 
      1235 . 217 GLY CA  C  47.8  0.1  1 
      1236 . 217 GLY N   N 106.2  0.1  1 
      1237 . 218 LEU H   H   7.38 0.03 1 
      1238 . 218 LEU HA  H   4.09 0.03 1 
      1239 . 218 LEU C   C 179.3  0.1  1 
      1240 . 218 LEU CA  C  58.0  0.1  1 
      1241 . 218 LEU CB  C  41.9  0.1  1 
      1242 . 218 LEU N   N 120.2  0.1  1 
      1243 . 219 ILE H   H   7.12 0.03 1 
      1244 . 219 ILE HA  H   3.60 0.03 1 
      1245 . 219 ILE C   C 179.0  0.1  1 
      1246 . 219 ILE CA  C  65.0  0.1  1 
      1247 . 219 ILE CB  C  38.6  0.1  1 
      1248 . 219 ILE N   N 119.1  0.1  1 
      1249 . 220 LEU H   H   7.96 0.03 1 
      1250 . 220 LEU C   C 178.4  0.1  1 
      1251 . 220 LEU CA  C  57.8  0.1  1 
      1252 . 220 LEU CB  C  39.0  0.1  1 
      1253 . 220 LEU N   N 117.4  0.1  1 
      1254 . 221 LYS H   H   8.07 0.03 1 
      1255 . 221 LYS C   C 178.8  0.1  1 
      1256 . 221 LYS CA  C  60.6  0.1  1 
      1257 . 221 LYS CB  C  33.4  0.1  1 
      1258 . 221 LYS N   N 118.3  0.1  1 
      1259 . 222 ARG H   H   7.82 0.03 1 
      1260 . 222 ARG HA  H   4.14 0.03 1 
      1261 . 222 ARG C   C 179.3  0.1  1 
      1262 . 222 ARG CA  C  58.9  0.1  1 
      1263 . 222 ARG CB  C  29.8  0.1  1 
      1264 . 222 ARG N   N 116.9  0.1  1 
      1265 . 223 MET H   H   7.68 0.03 1 
      1266 . 223 MET HA  H   4.00 0.03 1 
      1267 . 223 MET C   C 177.3  0.1  1 
      1268 . 223 MET CA  C  59.7  0.1  1 
      1269 . 223 MET CB  C  33.7  0.1  1 
      1270 . 223 MET N   N 118.1  0.1  1 
      1271 . 224 VAL H   H   7.26 0.03 1 
      1272 . 224 VAL HA  H   3.97 0.03 1 
      1273 . 224 VAL C   C 177.3  0.1  1 
      1274 . 224 VAL CA  C  65.2  0.1  1 
      1275 . 224 VAL CB  C  34.1  0.1  1 
      1276 . 224 VAL N   N 116.8  0.1  1 
      1277 . 225 GLU H   H   8.62 0.03 1 
      1278 . 225 GLU HA  H   4.33 0.03 1 
      1279 . 225 GLU C   C 176.9  0.1  1 
      1280 . 225 GLU CA  C  57.7  0.1  1 
      1281 . 225 GLU CB  C  30.8  0.1  1 
      1282 . 225 GLU N   N 117.9  0.1  1 
      1283 . 226 GLY H   H   7.74 0.03 1 
      1284 . 226 GLY HA2 H   3.98 0.03 2 
      1285 . 226 GLY HA3 H   3.68 0.03 2 
      1286 . 226 GLY CA  C  46.6  0.1  1 
      1287 . 226 GLY N   N 115.1  0.1  1 

   stop_

save_