data_5937

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
1H, 13C and 15N Chemical Sift Assignments for PDZ2b domain of PTP-Bas (hPTP1E)
;
   _BMRB_accession_number   5937
   _BMRB_flat_file_name     bmr5937.str
   _Entry_type              original
   _Submission_date         2003-09-08
   _Accession_date          2003-09-08
   _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 Kachel     Norman       . . 
      2 Erdmann   'Kai Sven'    . . 
      3 Kremer     Werner       . . 
      4 Wolff      Peter        . . 
      5 Gronwald   Wolfram      . . 
      6 Heumann    Rolf         . . 
      7 Kalbitzer 'Hans Robert' . . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  514 
      "13C chemical shifts" 318 
      "15N chemical shifts" 104 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2003-12-19 original author . 

   stop_

   _Original_release_date   2003-12-19

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas 
(hPTP1E): Splicing-induced modulation of ligand specificity
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    14596806

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Kachel     Norman       . . 
      2 Erdmann   'Kai Sven'    . . 
      3 Kremer     Werner       . . 
      4 Wolff      Peter        . . 
      5 Gronwald   Wolfram      . . 
      6 Heumann    Rolf         . . 
      7 Kalbitzer 'Hans Robert' . . 

   stop_

   _Journal_abbreviation        'J. Mol. Biol.'
   _Journal_volume               334
   _Journal_issue                1
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   143
   _Page_last                    155
   _Year                         2003
   _Details                      .

save_


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

save_PDZ2b_of_hPTP1E
   _Saveframe_category         molecular_system

   _Mol_system_name           'PDZ2b domain of PTP-Bas (hPTP1E)'
   _Abbreviation_common       'PDZ2b of hPTP1E'
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      'PDZ2b of PTP-Bas, PDZ2b' $PDZ2b 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state        'not present'
   _Database_query_date        .
   _Details                    .

save_


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

save_PDZ2b
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'PDZ2b domain of PTP-Bas'
   _Name_variant                               'Splicing variant b of PDZ2'
   _Abbreviation_common                        'PDZ2b of PTP-Bas'
   _Molecular_mass                              .
   _Mol_thiol_state                            'not present'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               108
   _Mol_residue_sequence                       
;
GSSPPKPGDIFEVELAKNDN
SLGISVTVLFDKGGVNTSVR
HGGIYVKAVIPQGAAESDGR
IHKGDRVLAVNGVSLEGATH
KQAVETLRNTGQVVHLLLEK
GQSPTSKE
;

   loop_
      _Residue_seq_code
      _Residue_label

        1 GLY    2 SER    3 SER    4 PRO    5 PRO 
        6 LYS    7 PRO    8 GLY    9 ASP   10 ILE 
       11 PHE   12 GLU   13 VAL   14 GLU   15 LEU 
       16 ALA   17 LYS   18 ASN   19 ASP   20 ASN 
       21 SER   22 LEU   23 GLY   24 ILE   25 SER 
       26 VAL   27 THR   28 VAL   29 LEU   30 PHE 
       31 ASP   32 LYS   33 GLY   34 GLY   35 VAL 
       36 ASN   37 THR   38 SER   39 VAL   40 ARG 
       41 HIS   42 GLY   43 GLY   44 ILE   45 TYR 
       46 VAL   47 LYS   48 ALA   49 VAL   50 ILE 
       51 PRO   52 GLN   53 GLY   54 ALA   55 ALA 
       56 GLU   57 SER   58 ASP   59 GLY   60 ARG 
       61 ILE   62 HIS   63 LYS   64 GLY   65 ASP 
       66 ARG   67 VAL   68 LEU   69 ALA   70 VAL 
       71 ASN   72 GLY   73 VAL   74 SER   75 LEU 
       76 GLU   77 GLY   78 ALA   79 THR   80 HIS 
       81 LYS   82 GLN   83 ALA   84 VAL   85 GLU 
       86 THR   87 LEU   88 ARG   89 ASN   90 THR 
       91 GLY   92 GLN   93 VAL   94 VAL   95 HIS 
       96 LEU   97 LEU   98 LEU   99 GLU  100 LYS 
      101 GLY  102 GLN  103 SER  104 PRO  105 THR 
      106 SER  107 LYS  108 GLU 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2008-08-19

   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 1Q7X 'Solution Structure Of The Alternatively Spliced Pdz2 Domain (Pdz2b) Of Ptp-Bas (Hptp1e)' 100.00 108 100.00 100.00 7.26e-55 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $PDZ2b 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_type
      _Vector_name

      $PDZ2b 'recombinant technology' E.coli Escherichia coli C600 plasmid pGEX2T 

   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
      _Isotopic_labeling

      $PDZ2b 2 mM '[U-13C; U-15N]' 

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $PDZ2b 2 mM [U-15N] 

   stop_

save_


save_sample_3
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $PDZ2b 2 mM . 

   stop_

save_


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

save_XWIN-NMR
   _Saveframe_category   software

   _Name                 XWIN-NMR
   _Version              .

   loop_
      _Task

      'data acquisition' 
       processing        

   stop_

   _Details              .

save_


save_Auremol
   _Saveframe_category   software

   _Name                 AUREMOL
   _Version              .

   loop_
      _Task

      'automated assignment of NOESYs' 
      'manual assignment'              

   stop_

   _Details             'See http://www.biologie.uni-regensburg.de/Biophysik/Kalbitzer/software/'

save_


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

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

save_NMR_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _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_15N-HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      15N-HSQC
   _Sample_label         .

save_


save_13C-HSQC_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      13C-HSQC
   _Sample_label         .

save_


save_HNCA_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCA
   _Sample_label         .

save_


save_HNCO_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCO
   _Sample_label         .

save_


save_CBCANH_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCANH
   _Sample_label         .

save_


save_CBCA(CO)NH_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCA(CO)NH
   _Sample_label         .

save_


save_HCCH-TOCSY_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HCCH-TOCSY
   _Sample_label         .

save_


save_15N-TOCSY-HSQC_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      15N-TOCSY-HSQC
   _Sample_label         .

save_


save_15N-NOESY-HSQC_9
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      15N-NOESY-HSQC
   _Sample_label         .

save_


save_13C-NOESY-HSQC_10
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      13C-NOESY-HSQC
   _Sample_label         .

save_


save_1H-1H-NOESY_11
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      1H-1H-NOESY
   _Sample_label         .

save_


save_NMR_spec_expt__0_1
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        15N-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_2
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        13C-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_3
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCA
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_4
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HNCO
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_5
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCANH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_6
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        CBCA(CO)NH
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_7
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        HCCH-TOCSY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_8
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        15N-TOCSY-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_9
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        15N-NOESY-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_10
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        13C-NOESY-HSQC
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


save_NMR_spec_expt__0_11
   _Saveframe_category                     NMR_applied_experiment

   _Experiment_name                        1H-1H-NOESY
   _BMRB_pulse_sequence_accession_number   .
   _Details                                .

save_


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

save_Con_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.8 0.1 n/a 
      temperature 293   1   K   

   stop_

save_


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

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

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

save_chemical_shift_reference
   _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 0.0 .        indirect . . . 0.251449530 
      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.0         
      DSS N 15 'methyl protons' ppm 0.0 .        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 
      $sample_2 
      $sample_3 

   stop_

   _Sample_conditions_label         $Con_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'PDZ2b of PTP-Bas, PDZ2b'
   _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 GLY CA   C  44.958 . 1 
        2 .   1 GLY HA2  H   3.873 . 2 
        3 .   1 GLY HA3  H   4.145 . 2 
        4 .   1 GLY C    C 176.494 . 1 
        5 .   2 SER H    H   7.91  . 1 
        6 .   2 SER N    N 118.885 . 1 
        7 .   2 SER CA   C  57.745 . 1 
        8 .   2 SER HA   H   4.466 . 1 
        9 .   2 SER C    C 173.993 . 1 
       10 .   2 SER CB   C  63.596 . 1 
       11 .   2 SER HB2  H   3.865 . 1 
       12 .   2 SER HB3  H   3.865 . 1 
       13 .   3 SER H    H   8.464 . 1 
       14 .   3 SER N    N 118.829 . 1 
       15 .   3 SER CA   C  56.275 . 1 
       16 .   3 SER HA   H   4.78  . 1 
       17 .   3 SER C    C 174.63  . 1 
       18 .   3 SER CB   C  62.47  . 1 
       19 .   3 SER HB2  H   3.77  . 2 
       20 .   3 SER HB3  H   3.789 . 2 
       21 .   5 PRO CA   C  62.573 . 1 
       22 .   5 PRO C    C 175.244 . 1 
       23 .   5 PRO CB   C  30.921 . 1 
       24 .   6 LYS H    H   9.081 . 1 
       25 .   6 LYS N    N 124.198 . 1 
       26 .   6 LYS CA   C  53.184 . 1 
       27 .   6 LYS HA   H   5.181 . 1 
       28 .   6 LYS C    C 176.55  . 1 
       29 .   6 LYS CB   C  30.921 . 1 
       30 .   6 LYS HG2  H   1.483 . 1 
       31 .   6 LYS HG3  H   1.483 . 1 
       32 .   6 LYS HD2  H   1.715 . 1 
       33 .   6 LYS HD3  H   1.715 . 1 
       34 .   7 PRO CA   C  64.049 . 1 
       35 .   7 PRO HA   H   4.534 . 1 
       36 .   7 PRO C    C 177.431 . 1 
       37 .   7 PRO CB   C  31.422 . 1 
       38 .   7 PRO HB2  H   1.947 . 2 
       39 .   7 PRO HB3  H   2.446 . 2 
       40 .   7 PRO HG2  H   1.886 . 1 
       41 .   7 PRO HG3  H   1.886 . 1 
       42 .   7 PRO HD2  H   3.893 . 1 
       43 .   7 PRO HD3  H   3.893 . 1 
       44 .   8 GLY H    H   9.054 . 1 
       45 .   8 GLY N    N 113.884 . 1 
       46 .   8 GLY CA   C  44.902 . 1 
       47 .   8 GLY HA2  H   4.363 . 2 
       48 .   8 GLY HA3  H   3.873 . 2 
       49 .   8 GLY C    C 173.71  . 1 
       50 .   9 ASP H    H   8.39  . 1 
       51 .   9 ASP N    N 121.698 . 1 
       52 .   9 ASP CA   C  53.735 . 1 
       53 .   9 ASP HA   H   4.581 . 1 
       54 .   9 ASP C    C 175.869 . 1 
       55 .   9 ASP CB   C  41.288 . 1 
       56 .   9 ASP HB2  H   2.629 . 2 
       57 .   9 ASP HB3  H   2.947 . 2 
       58 .  10 ILE H    H   8.475 . 1 
       59 .  10 ILE N    N 122.01  . 1 
       60 .  10 ILE CA   C  59.39  . 1 
       61 .  10 ILE HA   H   4.254 . 1 
       62 .  10 ILE C    C 176.494 . 1 
       63 .  10 ILE CB   C  37.61  . 1 
       64 .  10 ILE HB   H   1.693 . 1 
       65 .  10 ILE CG2  C  17.53  . 1 
       66 .  10 ILE HG2  H   1.366 . 1 
       67 .  10 ILE CG1  C  27.59  . 1 
       68 .  10 ILE HG12 H   1.128 . 1 
       69 .  10 ILE HG13 H   1.128 . 1 
       70 .  10 ILE CD1  C  14.18  . 1 
       71 .  10 ILE HD1  H   0.705 . 1 
       72 .  11 PHE H    H   7.91  . 1 
       73 .  11 PHE N    N 126.073 . 1 
       74 .  11 PHE CA   C  54.81  . 1 
       75 .  11 PHE HA   H   5.072 . 1 
       76 .  11 PHE C    C 175.869 . 1 
       77 .  11 PHE CB   C  41.248 . 1 
       78 .  11 PHE HB2  H   1.748 . 1 
       79 .  11 PHE HB3  H   1.748 . 1 
       80 .  11 PHE HD1  H   7.065 . 1 
       81 .  11 PHE HD2  H   7.065 . 1 
       82 .  11 PHE HE1  H   6.805 . 1 
       83 .  11 PHE HE2  H   6.805 . 1 
       84 .  11 PHE HZ   H   7.367 . 1 
       85 .  12 GLU H    H   8.563 . 1 
       86 .  12 GLU N    N 118.885 . 1 
       87 .  12 GLU CA   C  53.638 . 1 
       88 .  12 GLU HA   H   5.072 . 1 
       89 .  12 GLU C    C 175.869 . 1 
       90 .  12 GLU CB   C  33.038 . 1 
       91 .  12 GLU HB2  H   3.764 . 1 
       92 .  12 GLU HB3  H   3.764 . 1 
       93 .  12 GLU HG2  H   4.69  . 1 
       94 .  12 GLU HG3  H   4.69  . 1 
       95 .  13 VAL H    H   8.631 . 1 
       96 .  13 VAL N    N 120.135 . 1 
       97 .  13 VAL CA   C  60.914 . 1 
       98 .  13 VAL HA   H   4.69  . 1 
       99 .  13 VAL C    C 173.056 . 1 
      100 .  13 VAL CB   C  36.086 . 1 
      101 .  13 VAL HB   H   4.091 . 1 
      102 .  13 VAL CG1  C  21.14  . 1 
      103 .  13 VAL HG1  H   0.767 . 1 
      104 .  13 VAL HG2  H   1.802 . 1 
      105 .  14 GLU H    H   7.869 . 1 
      106 .  14 GLU N    N 126.073 . 1 
      107 .  14 GLU CA   C  54.228 . 1 
      108 .  14 GLU HA   H   4.908 . 1 
      109 .  14 GLU C    C 176.33  . 1 
      110 .  14 GLU CB   C  30.431 . 1 
      111 .  14 GLU HB2  H   1.802 . 1 
      112 .  14 GLU HB3  H   1.802 . 1 
      113 .  14 GLU HG2  H   2.038 . 1 
      114 .  14 GLU HG3  H   2.038 . 1 
      115 .  15 LEU H    H   8.904 . 1 
      116 .  15 LEU N    N 126.386 . 1 
      117 .  15 LEU CA   C  52.719 . 1 
      118 .  15 LEU HA   H   4.636 . 1 
      119 .  15 LEU C    C 173.681 . 1 
      120 .  15 LEU CB   C  45.443 . 1 
      121 .  15 LEU HB2  H   1.248 . 2 
      122 .  15 LEU HB3  H   1.388 . 2 
      123 .  15 LEU HD1  H   0.713 . 1 
      124 .  15 LEU HD2  H   0.713 . 1 
      125 .  16 ALA H    H   8.543 . 1 
      126 .  16 ALA N    N 126.699 . 1 
      127 .  16 ALA CA   C  49.4   . 1 
      128 .  16 ALA HA   H   5.072 . 1 
      129 .  16 ALA C    C 177.12  . 1 
      130 .  16 ALA CB   C  19.015 . 1 
      131 .  16 ALA HB   H   1.312 . 1 
      132 .  17 LYS H    H   8.536 . 1 
      133 .  17 LYS N    N 120.135 . 1 
      134 .  17 LYS CA   C  57.505 . 1 
      135 .  17 LYS HA   H   4.581 . 1 
      136 .  17 LYS C    C 176.181 . 1 
      137 .  17 LYS CB   C  34.2   . 1 
      138 .  17 LYS HB2  H   1.748 . 1 
      139 .  17 LYS HB3  H   1.748 . 1 
      140 .  17 LYS HG2  H   1.421 . 1 
      141 .  17 LYS HG3  H   1.421 . 1 
      142 .  17 LYS HE2  H   3.764 . 1 
      143 .  17 LYS HE3  H   3.764 . 1 
      144 .  18 ASN H    H   8.134 . 1 
      145 .  18 ASN N    N 117.322 . 1 
      146 .  18 ASN CA   C  52.26  . 1 
      147 .  18 ASN HA   H   4.854 . 1 
      148 .  18 ASN C    C 174.931 . 1 
      149 .  18 ASN CB   C  40.2   . 1 
      150 .  18 ASN HB2  H   2.783 . 1 
      151 .  18 ASN HB3  H   2.783 . 1 
      152 .  18 ASN CG   C 175.96  . 1 
      153 .  18 ASN ND2  N 113.09  . 1 
      154 .  19 ASP H    H   9.299 . 1 
      155 .  19 ASP N    N 125.761 . 1 
      156 .  19 ASP CA   C  55.32  . 1 
      157 .  19 ASP HA   H   4.63  . 1 
      158 .  19 ASP C    C 175.244 . 1 
      159 .  19 ASP CB   C  38.661 . 1 
      160 .  19 ASP HB2  H   2.783 . 1 
      161 .  19 ASP HB3  H   2.783 . 1 
      162 .  20 ASN H    H   8.952 . 1 
      163 .  20 ASN N    N 110.446 . 1 
      164 .  20 ASN CA   C  53.726 . 1 
      165 .  20 ASN HA   H   4.254 . 1 
      166 .  20 ASN C    C 174.306 . 1 
      167 .  20 ASN CB   C  38.183 . 1 
      168 .  20 ASN HB2  H   2.776 . 2 
      169 .  20 ASN HB3  H   3.1   . 2 
      170 .  21 SER H    H   7.95  . 1 
      171 .  21 SER N    N 112.009 . 1 
      172 .  21 SER CA   C  55.856 . 1 
      173 .  21 SER HA   H   4.854 . 1 
      174 .  21 SER C    C 176.494 . 1 
      175 .  21 SER CB   C  64.588 . 1 
      176 .  21 SER HB2  H   3.764 . 1 
      177 .  21 SER HB3  H   3.764 . 1 
      178 .  22 LEU H    H   9.43  . 1 
      179 .  22 LEU N    N 127.8   . 1 
      180 .  22 LEU CA   C  55.76  . 1 
      181 .  22 LEU HA   H   4.35  . 1 
      182 .  22 LEU C    C 176.806 . 1 
      183 .  22 LEU CB   C  42.846 . 1 
      184 .  22 LEU HB2  H   1.748 . 1 
      185 .  22 LEU HB3  H   1.748 . 1 
      186 .  22 LEU CG   C  26.77  . 1 
      187 .  22 LEU CD1  C  24.63  . 1 
      188 .  22 LEU HD1  H   0.88  . 1 
      189 .  22 LEU CD2  C  24.2   . 1 
      190 .  22 LEU HD2  H   0.71  . 1 
      191 .  22 LEU HG   H   1.475 . 1 
      192 .  23 GLY H    H   8.795 . 1 
      193 .  23 GLY N    N 105.133 . 1 
      194 .  23 GLY CA   C  46.478 . 1 
      195 .  23 GLY HA2  H   4.145 . 2 
      196 .  23 GLY HA3  H   3.818 . 2 
      197 .  23 GLY C    C 175.869 . 1 
      198 .  24 ILE H    H   7.705 . 1 
      199 .  24 ILE N    N 114.822 . 1 
      200 .  24 ILE CA   C  59.3   . 1 
      201 .  24 ILE HA   H   5.017 . 1 
      202 .  24 ILE C    C 173.681 . 1 
      203 .  24 ILE CB   C  41.976 . 1 
      204 .  24 ILE HB   H   1.7   . 1 
      205 .  24 ILE CG2  C  17.53  . 1 
      206 .  24 ILE HG2  H   0.705 . 1 
      207 .  24 ILE HD1  H   0.657 . 1 
      208 .  25 SER H    H   8.638 . 1 
      209 .  25 SER N    N 119.51  . 1 
      210 .  25 SER CA   C  55.72  . 1 
      211 .  25 SER HA   H   5.017 . 1 
      212 .  25 SER C    C 174.931 . 1 
      213 .  25 SER CB   C  64.65  . 1 
      214 .  25 SER HB2  H   3.818 . 1 
      215 .  25 SER HB3  H   3.818 . 1 
      216 .  26 VAL H    H   9.197 . 1 
      217 .  26 VAL N    N 117.009 . 1 
      218 .  26 VAL CA   C  58.842 . 1 
      219 .  26 VAL HA   H   5.558 . 1 
      220 .  26 VAL C    C 177.119 . 1 
      221 .  26 VAL CB   C  35.031 . 1 
      222 .  26 VAL HB   H   2.06  . 1 
      223 .  26 VAL HG1  H   0.604 . 1 
      224 .  26 VAL HG2  H   0.589 . 1 
      225 .  27 THR H    H   9.054 . 1 
      226 .  27 THR N    N 114.197 . 1 
      227 .  27 THR CA   C  59.518 . 1 
      228 .  27 THR HA   H   4.418 . 1 
      229 .  27 THR C    C 170.868 . 1 
      230 .  27 THR CB   C  70.343 . 1 
      231 .  27 THR HB   H   3.927 . 1 
      232 .  27 THR HG2  H   1.046 . 1 
      233 .  28 VAL H    H   8.066 . 1 
      234 .  28 VAL N    N 123.573 . 1 
      235 .  28 VAL CA   C  60.49  . 1 
      236 .  28 VAL HA   H   3.927 . 1 
      237 .  28 VAL C    C 175.244 . 1 
      238 .  28 VAL CB   C  32.63  . 1 
      239 .  28 VAL HB   H   2.184 . 1 
      240 .  28 VAL HG1  H   0.876 . 1 
      241 .  28 VAL HG2  H   1.421 . 1 
      242 .  29 LEU H    H   8.809 . 1 
      243 .  29 LEU N    N 123.573 . 1 
      244 .  29 LEU CA   C  53.23  . 1 
      245 .  29 LEU HA   H   4.363 . 1 
      246 .  29 LEU C    C 175.869 . 1 
      247 .  29 LEU CB   C  43.3   . 1 
      248 .  29 LEU HB2  H   1.645 . 1 
      249 .  29 LEU HB3  H   1.645 . 1 
      250 .  29 LEU CD1  C  24.63  . 1 
      251 .  29 LEU HD1  H   1.098 . 1 
      252 .  29 LEU CD2  C  24.2   . 1 
      253 .  29 LEU HD2  H   0.824 . 1 
      254 .  29 LEU HG   H   1.415 . 1 
      255 .  30 PHE H    H   8.611 . 1 
      256 .  30 PHE N    N 121.073 . 1 
      257 .  30 PHE CA   C  56.82  . 1 
      258 .  30 PHE HA   H   4.581 . 1 
      259 .  30 PHE C    C 174.931 . 1 
      260 .  30 PHE CB   C  39.879 . 1 
      261 .  30 PHE HB2  H   3.056 . 2 
      262 .  30 PHE HB3  H   2.783 . 2 
      263 .  30 PHE HD1  H   7.95  . 1 
      264 .  30 PHE HD2  H   7.95  . 1 
      265 .  30 PHE HE1  H   7.127 . 1 
      266 .  30 PHE HE2  H   7.127 . 1 
      267 .  30 PHE HZ   H   7.279 . 1 
      268 .  31 ASP H    H   8.911 . 1 
      269 .  31 ASP N    N 122.01  . 1 
      270 .  31 ASP CA   C  53.7   . 1 
      271 .  31 ASP HA   H   4.745 . 1 
      272 .  31 ASP C    C 176.86  . 1 
      273 .  31 ASP CB   C  41.258 . 1 
      274 .  31 ASP HB2  H   2.62  . 1 
      275 .  31 ASP HB3  H   2.62  . 1 
      276 .  32 LYS H    H   7.962 . 1 
      277 .  32 LYS N    N 112.135 . 1 
      278 .  32 LYS CA   C  55.828 . 1 
      279 .  32 LYS HA   H   4.636 . 1 
      280 .  32 LYS C    C 175.244 . 1 
      281 .  32 LYS CB   C  30.444 . 1 
      282 .  32 LYS HB2  H   1.77  . 1 
      283 .  32 LYS HB3  H   1.77  . 1 
      284 .  32 LYS HD2  H   1.654 . 1 
      285 .  32 LYS HD3  H   1.654 . 1 
      286 .  32 LYS HE2  H   3.156 . 1 
      287 .  32 LYS HE3  H   3.156 . 1 
      288 .  33 GLY H    H   8.727 . 1 
      289 .  33 GLY N    N 112.009 . 1 
      290 .  33 GLY CA   C  44.905 . 1 
      291 .  33 GLY HA2  H   3.927 . 2 
      292 .  33 GLY HA3  H   3.709 . 2 
      293 .  33 GLY C    C 174.306 . 1 
      294 .  34 GLY H    H   8.209 . 1 
      295 .  34 GLY N    N 108.883 . 1 
      296 .  34 GLY CA   C  44.918 . 1 
      297 .  34 GLY HA2  H   3.927 . 1 
      298 .  34 GLY HA3  H   3.927 . 1 
      299 .  34 GLY C    C 173.993 . 1 
      300 .  35 VAL H    H   8.196 . 1 
      301 .  35 VAL N    N 118.572 . 1 
      302 .  35 VAL CA   C  62.536 . 1 
      303 .  35 VAL HA   H   4.12  . 1 
      304 .  35 VAL C    C 176.181 . 1 
      305 .  35 VAL CB   C  31.986 . 1 
      306 .  35 VAL HB   H   2.02  . 1 
      307 .  35 VAL HG1  H   0.876 . 1 
      308 .  35 VAL HG2  H   0.876 . 1 
      309 .  36 ASN H    H   8.645 . 1 
      310 .  36 ASN N    N 120.448 . 1 
      311 .  36 ASN CA   C  52.697 . 1 
      312 .  36 ASN HA   H   4.745 . 1 
      313 .  36 ASN C    C 174.931 . 1 
      314 .  36 ASN CB   C  38.177 . 1 
      315 .  36 ASN HB2  H   2.764 . 2 
      316 .  36 ASN HB3  H   2.891 . 2 
      317 .  37 THR H    H   8.039 . 1 
      318 .  37 THR N    N 113.259 . 1 
      319 .  37 THR CA   C  61.515 . 1 
      320 .  37 THR HA   H   3.873 . 1 
      321 .  37 THR C    C 174.306 . 1 
      322 .  37 THR CB   C  69.212 . 1 
      323 .  37 THR HB   H   3.873 . 1 
      324 .  37 THR HG2  H   1.148 . 1 
      325 .  38 SER H    H   8.386 . 1 
      326 .  38 SER N    N 117.322 . 1 
      327 .  38 SER CA   C  58.42  . 1 
      328 .  38 SER HA   H   4.309 . 1 
      329 .  38 SER C    C 174.306 . 1 
      330 .  38 SER CB   C  63.495 . 1 
      331 .  38 SER HB2  H   3.873 . 1 
      332 .  38 SER HB3  H   3.873 . 1 
      333 .  39 VAL H    H   7.971 . 1 
      334 .  39 VAL N    N 120.448 . 1 
      335 .  39 VAL CA   C  61.875 . 1 
      336 .  39 VAL HA   H   4.091 . 1 
      337 .  39 VAL C    C 175.244 . 1 
      338 .  39 VAL CB   C  32.37  . 1 
      339 .  39 VAL HB   H   1.966 . 1 
      340 .  39 VAL HG1  H   0.822 . 1 
      341 .  39 VAL HG2  H   0.822 . 1 
      342 .  40 ARG H    H   8.366 . 1 
      343 .  40 ARG N    N 123.884 . 1 
      344 .  40 ARG CA   C  55.278 . 1 
      345 .  40 ARG HA   H   4.309 . 1 
      346 .  40 ARG C    C 175.556 . 1 
      347 .  40 ARG CB   C  30.408 . 1 
      348 .  40 ARG HB2  H   1.639 . 1 
      349 .  40 ARG HB3  H   1.639 . 1 
      350 .  41 HIS H    H   8.564 . 1 
      351 .  41 HIS N    N 121.3   . 1 
      352 .  41 HIS CA   C  56.192 . 1 
      353 .  41 HIS HA   H   4.254 . 1 
      354 .  41 HIS C    C 176.806 . 1 
      355 .  41 HIS CB   C  32.426 . 1 
      356 .  41 HIS HB2  H   1.366 . 2 
      357 .  41 HIS HB3  H   1.748 . 2 
      358 .  41 HIS HD2  H   7.13  . 1 
      359 .  41 HIS HE1  H   7.95  . 1 
      360 .  42 GLY H    H   8.563 . 1 
      361 .  42 GLY N    N 109.508 . 1 
      362 .  42 GLY CA   C  44.835 . 1 
      363 .  42 GLY HA2  H   3.715 . 1 
      364 .  42 GLY HA3  H   3.715 . 1 
      365 .  42 GLY C    C 173.056 . 1 
      366 .  43 GLY H    H   8.427 . 1 
      367 .  43 GLY N    N 108.258 . 1 
      368 .  43 GLY CA   C  43.994 . 1 
      369 .  43 GLY HA2  H   3.929 . 1 
      370 .  43 GLY HA3  H   3.929 . 1 
      371 .  43 GLY C    C 170.243 . 1 
      372 .  44 ILE H    H   8.502 . 1 
      373 .  44 ILE N    N 120.76  . 1 
      374 .  44 ILE CA   C  57.3   . 1 
      375 .  44 ILE HA   H   4.636 . 1 
      376 .  44 ILE C    C 176.84  . 1 
      377 .  44 ILE CB   C  35.181 . 1 
      378 .  44 ILE HB   H   2.129 . 1 
      379 .  44 ILE HG2  H   0.604 . 1 
      380 .  45 TYR H    H   9.081 . 1 
      381 .  45 TYR N    N 124.198 . 1 
      382 .  45 TYR CA   C  55.727 . 1 
      383 .  45 TYR HA   H   5.181 . 1 
      384 .  45 TYR C    C 175.869 . 1 
      385 .  45 TYR CB   C  42.37  . 1 
      386 .  45 TYR HB2  H   2.403 . 2 
      387 .  45 TYR HB3  H   3.149 . 2 
      388 .  45 TYR HD1  H   6.98  . 1 
      389 .  45 TYR HD2  H   6.98  . 1 
      390 .  45 TYR HE1  H   6.772 . 1 
      391 .  45 TYR HE2  H   6.772 . 1 
      392 .  45 TYR HH   H   9.95  . 1 
      393 .  46 VAL H    H   9.224 . 1 
      394 .  46 VAL N    N 119.51  . 1 
      395 .  46 VAL CA   C  63.552 . 1 
      396 .  46 VAL HA   H   3.818 . 1 
      397 .  46 VAL C    C 175.556 . 1 
      398 .  46 VAL CB   C  30.954 . 1 
      399 .  46 VAL HB   H   2.06  . 1 
      400 .  46 VAL HG1  H   0.604 . 1 
      401 .  46 VAL HG2  H   0.604 . 1 
      402 .  47 LYS H    H   9.544 . 1 
      403 .  47 LYS N    N 134.825 . 1 
      404 .  47 LYS CA   C  56.872 . 1 
      405 .  47 LYS HA   H   4.23  . 1 
      406 .  47 LYS C    C 174.618 . 1 
      407 .  47 LYS CB   C  33.5   . 1 
      408 .  47 LYS HG2  H   1.53  . 1 
      409 .  47 LYS HG3  H   1.53  . 1 
      410 .  48 ALA H    H   7.508 . 1 
      411 .  48 ALA N    N 117.009 . 1 
      412 .  48 ALA CA   C  51.14  . 1 
      413 .  48 ALA HA   H   4.19  . 1 
      414 .  48 ALA C    C 175.244 . 1 
      415 .  48 ALA CB   C  21.792 . 1 
      416 .  48 ALA HB   H   1.257 . 1 
      417 .  49 VAL H    H   8.727 . 1 
      418 .  49 VAL N    N 121.073 . 1 
      419 .  49 VAL CA   C  61.431 . 1 
      420 .  49 VAL HA   H   4.2   . 1 
      421 .  49 VAL C    C 175.556 . 1 
      422 .  49 VAL CB   C  31.388 . 1 
      423 .  49 VAL HB   H   1.966 . 1 
      424 .  49 VAL HG1  H   0.658 . 1 
      425 .  49 VAL HG2  H   0.658 . 1 
      426 .  50 ILE H    H   7.882 . 1 
      427 .  50 ILE N    N 128.886 . 1 
      428 .  50 ILE CA   C  58.338 . 1 
      429 .  50 ILE HA   H   4.2   . 1 
      430 .  50 ILE C    C 176.84  . 1 
      431 .  50 ILE CB   C  37.397 . 1 
      432 .  50 ILE HB   H   1.584 . 1 
      433 .  50 ILE CG2  C  17.53  . 1 
      434 .  50 ILE HG2  H   0.849 . 1 
      435 .  50 ILE CG1  C  27.59  . 1 
      436 .  50 ILE CD1  C  14.18  . 1 
      437 .  50 ILE HD1  H   0.801 . 1 
      438 .  51 PRO CA   C  63.975 . 1 
      439 .  51 PRO HA   H   4.472 . 1 
      440 .  51 PRO C    C 177.119 . 1 
      441 .  51 PRO CB   C  31.4   . 1 
      442 .  51 PRO HB2  H   2.347 . 1 
      443 .  51 PRO HB3  H   2.347 . 1 
      444 .  51 PRO HG2  H   1.857 . 1 
      445 .  51 PRO HG3  H   1.857 . 1 
      446 .  52 GLN H    H   9.408 . 1 
      447 .  52 GLN N    N 116.697 . 1 
      448 .  52 GLN CA   C  57.79  . 1 
      449 .  52 GLN HA   H   3.818 . 1 
      450 .  52 GLN C    C 175.244 . 1 
      451 .  52 GLN CB   C  26.309 . 1 
      452 .  52 GLN CG   C  33.63  . 1 
      453 .  52 GLN HG2  H   2.347 . 1 
      454 .  52 GLN HG3  H   2.347 . 1 
      455 .  52 GLN CD   C 177.66  . 1 
      456 .  52 GLN NE2  N 111.61  . 1 
      457 .  53 GLY H    H   7.855 . 1 
      458 .  53 GLY N    N 106.07  . 1 
      459 .  53 GLY CA   C  44.39  . 1 
      460 .  53 GLY HA2  H   4.309 . 1 
      461 .  53 GLY HA3  H   4.309 . 1 
      462 .  53 GLY C    C 174.306 . 1 
      463 .  54 ALA H    H   8.973 . 1 
      464 .  54 ALA N    N 120.114 . 1 
      465 .  54 ALA CA   C  54.517 . 1 
      466 .  54 ALA HA   H   4.036 . 1 
      467 .  54 ALA C    C 174.306 . 1 
      468 .  54 ALA CB   C  18.265 . 1 
      469 .  54 ALA HB   H   1.496 . 1 
      470 .  55 ALA H    H   7.848 . 1 
      471 .  55 ALA N    N 119.197 . 1 
      472 .  55 ALA CA   C  54.367 . 1 
      473 .  55 ALA HA   H   4.036 . 1 
      474 .  55 ALA C    C 180.557 . 1 
      475 .  55 ALA CB   C  18.265 . 1 
      476 .  55 ALA HB   H   1.257 . 1 
      477 .  56 GLU H    H   9.401 . 1 
      478 .  56 GLU N    N 124.511 . 1 
      479 .  56 GLU CA   C  59.389 . 1 
      480 .  56 GLU HA   H   3.764 . 1 
      481 .  56 GLU C    C 180.557 . 1 
      482 .  56 GLU CB   C  29.372 . 1 
      483 .  56 GLU HB2  H   2.057 . 1 
      484 .  56 GLU HB3  H   2.057 . 1 
      485 .  57 SER H    H   7.99  . 1 
      486 .  57 SER N    N 113.048 . 1 
      487 .  57 SER CA   C  60.941 . 1 
      488 .  57 SER HA   H   4.036 . 1 
      489 .  57 SER C    C 177.744 . 1 
      490 .  57 SER CB   C  62.519 . 1 
      491 .  57 SER HB2  H   3.873 . 1 
      492 .  57 SER HB3  H   3.873 . 1 
      493 .  58 ASP H    H   7.664 . 1 
      494 .  58 ASP N    N 119.822 . 1 
      495 .  58 ASP CA   C  56.77  . 1 
      496 .  58 ASP HA   H   4.363 . 1 
      497 .  58 ASP C    C 175.556 . 1 
      498 .  58 ASP CB   C  43.934 . 1 
      499 .  58 ASP HB2  H   2.685 . 1 
      500 .  58 ASP HB3  H   2.565 . 1 
      501 .  59 GLY H    H   7.392 . 1 
      502 .  59 GLY N    N 102.632 . 1 
      503 .  59 GLY CA   C  45.901 . 1 
      504 .  59 GLY HA2  H   4.036 . 2 
      505 .  59 GLY HA3  H   3.873 . 2 
      506 .  59 GLY C    C 177.431 . 1 
      507 .  60 ARG H    H   7.957 . 1 
      508 .  60 ARG N    N 117.322 . 1 
      509 .  60 ARG CA   C  57.4   . 1 
      510 .  60 ARG HA   H   4.309 . 1 
      511 .  60 ARG C    C 174.618 . 1 
      512 .  60 ARG CB   C  32.47  . 1 
      513 .  60 ARG HB2  H   1.966 . 1 
      514 .  60 ARG HB3  H   1.966 . 1 
      515 .  60 ARG HG2  H   1.312 . 1 
      516 .  60 ARG HG3  H   1.312 . 1 
      517 .  61 ILE H    H   8.318 . 1 
      518 .  61 ILE N    N 120.135 . 1 
      519 .  61 ILE CA   C  60.966 . 1 
      520 .  61 ILE HA   H   4.2   . 1 
      521 .  61 ILE C    C 175.556 . 1 
      522 .  61 ILE CB   C  39.128 . 1 
      523 .  61 ILE HB   H   1.756 . 1 
      524 .  61 ILE HG2  H   0.896 . 1 
      525 .  61 ILE HG12 H   1.429 . 2 
      526 .  61 ILE HG13 H   1.366 . 2 
      527 .  61 ILE HD1  H   0.767 . 1 
      528 .  62 HIS H    H   8.996 . 1 
      529 .  62 HIS N    N 122.684 . 1 
      530 .  62 HIS CA   C  54.785 . 1 
      531 .  62 HIS HA   H   4.821 . 1 
      532 .  62 HIS C    C 174.306 . 1 
      533 .  62 HIS CB   C  33.457 . 1 
      534 .  62 HIS HB2  H   2.855 . 2 
      535 .  62 HIS HB3  H   3.251 . 2 
      536 .  63 LYS H    H   8.71  . 1 
      537 .  63 LYS N    N 120.114 . 1 
      538 .  63 LYS CA   C  57.896 . 1 
      539 .  63 LYS HA   H   4.364 . 1 
      540 .  63 LYS C    C 174.306 . 1 
      541 .  63 LYS CB   C  31.924 . 1 
      542 .  63 LYS HB2  H   1.756 . 2 
      543 .  63 LYS HB3  H   1.879 . 2 
      544 .  63 LYS HG2  H   1.442 . 1 
      545 .  63 LYS HG3  H   1.442 . 1 
      546 .  63 LYS HD2  H   1.661 . 1 
      547 .  63 LYS HD3  H   1.661 . 1 
      548 .  64 GLY H    H   9.124 . 1 
      549 .  64 GLY N    N 114.333 . 1 
      550 .  64 GLY CA   C  44.43  . 1 
      551 .  64 GLY HA2  H   4.671 . 2 
      552 .  64 GLY HA3  H   3.849 . 2 
      553 .  64 GLY C    C 176.806 . 1 
      554 .  65 ASP H    H   7.98  . 1 
      555 .  65 ASP N    N 121.39  . 1 
      556 .  65 ASP CA   C  55.24  . 1 
      557 .  65 ASP HA   H   4.951 . 1 
      558 .  65 ASP C    C 173.993 . 1 
      559 .  65 ASP CB   C  40.69  . 1 
      560 .  65 ASP HB2  H   2.61  . 2 
      561 .  65 ASP HB3  H   2.719 . 2 
      562 .  66 ARG H    H   8.989 . 1 
      563 .  66 ARG N    N 122.684 . 1 
      564 .  66 ARG CA   C  54.36  . 1 
      565 .  66 ARG HA   H   4.381 . 1 
      566 .  66 ARG C    C 174.306 . 1 
      567 .  66 ARG CB   C  33.48  . 1 
      568 .  66 ARG HB2  H   1.684 . 1 
      569 .  66 ARG HB3  H   1.684 . 1 
      570 .  66 ARG HG2  H   1.422 . 1 
      571 .  66 ARG HG3  H   1.422 . 1 
      572 .  66 ARG HD2  H   2.58  . 1 
      573 .  66 ARG HD3  H   2.58  . 1 
      574 .  67 VAL H    H   8.98  . 1 
      575 .  67 VAL N    N 126.073 . 1 
      576 .  67 VAL CA   C  61.73  . 1 
      577 .  67 VAL HA   H   3.873 . 1 
      578 .  67 VAL C    C 175.244 . 1 
      579 .  67 VAL CB   C  30.4   . 1 
      580 .  67 VAL HB   H   1.748 . 1 
      581 .  67 VAL HG1  H   0.594 . 1 
      582 .  67 VAL HG2  H   0.594 . 1 
      583 .  68 LEU H    H   9.17  . 1 
      584 .  68 LEU N    N 127.011 . 1 
      585 .  68 LEU CA   C  56.342 . 1 
      586 .  68 LEU HA   H   4.2   . 1 
      587 .  68 LEU C    C 173.993 . 1 
      588 .  68 LEU CB   C  41.794 . 1 
      589 .  68 LEU HG   H   1.312 . 1 
      590 .  69 ALA H    H   7.787 . 1 
      591 .  69 ALA N    N 118.572 . 1 
      592 .  69 ALA CA   C  51.59  . 1 
      593 .  69 ALA HA   H   4.963 . 1 
      594 .  69 ALA C    C 178.369 . 1 
      595 .  69 ALA CB   C  21.72  . 1 
      596 .  69 ALA HB   H   1.04  . 1 
      597 .  70 VAL H    H   8.202 . 1 
      598 .  70 VAL N    N 120.76  . 1 
      599 .  70 VAL CA   C  60.02  . 1 
      600 .  70 VAL HA   H   4.472 . 1 
      601 .  70 VAL C    C 178.369 . 1 
      602 .  70 VAL CB   C  33.453 . 1 
      603 .  70 VAL HB   H   1.693 . 1 
      604 .  70 VAL HG1  H   0.658 . 1 
      605 .  70 VAL HG2  H   0.604 . 1 
      606 .  71 ASN H    H  10.45  . 1 
      607 .  71 ASN N    N 128.886 . 1 
      608 .  71 ASN CA   C  53.663 . 1 
      609 .  71 ASN C    C 175.244 . 1 
      610 .  71 ASN CB   C  36.541 . 1 
      611 .  71 ASN HB2  H   3.11  . 1 
      612 .  71 ASN HB3  H   3.11  . 1 
      613 .  72 GLY H    H   9.108 . 1 
      614 .  72 GLY N    N 102.945 . 1 
      615 .  72 GLY CA   C  44.9   . 1 
      616 .  72 GLY HA2  H   4.036 . 2 
      617 .  72 GLY HA3  H   3.491 . 2 
      618 .  72 GLY C    C 174.931 . 1 
      619 .  73 VAL H    H   8.066 . 1 
      620 .  73 VAL N    N 123.886 . 1 
      621 .  73 VAL CA   C  61.978 . 1 
      622 .  73 VAL HA   H   3.982 . 1 
      623 .  73 VAL C    C 173.681 . 1 
      624 .  73 VAL CB   C  31.484 . 1 
      625 .  73 VAL HB   H   2.184 . 1 
      626 .  73 VAL HG1  H   0.931 . 1 
      627 .  73 VAL HG2  H   0.931 . 1 
      628 .  74 SER H    H   8.661 . 1 
      629 .  74 SER N    N 120.114 . 1 
      630 .  74 SER CA   C  57.83  . 1 
      631 .  74 SER HA   H   4.569 . 1 
      632 .  74 SER C    C 173.368 . 1 
      633 .  74 SER CB   C  63.06  . 1 
      634 .  74 SER HB2  H   3.879 . 1 
      635 .  74 SER HB3  H   3.879 . 1 
      636 .  75 LEU H    H   8.243 . 1 
      637 .  75 LEU N    N 125.448 . 1 
      638 .  75 LEU CA   C  53.28  . 1 
      639 .  75 LEU HA   H   4.363 . 1 
      640 .  75 LEU C    C 176.181 . 1 
      641 .  75 LEU CB   C  40.788 . 1 
      642 .  75 LEU HB2  H   1.911 . 2 
      643 .  75 LEU HB3  H   1.693 . 2 
      644 .  75 LEU HG   H   1.421 . 1 
      645 .  76 GLU H    H   8.284 . 1 
      646 .  76 GLU N    N 123.261 . 1 
      647 .  76 GLU CA   C  58.2   . 1 
      648 .  76 GLU HA   H   4.036 . 1 
      649 .  76 GLU C    C 176.494 . 1 
      650 .  76 GLU CB   C  28.791 . 1 
      651 .  76 GLU HB2  H   1.911 . 1 
      652 .  76 GLU HB3  H   1.911 . 1 
      653 .  77 GLY H    H   8.829 . 1 
      654 .  77 GLY N    N 115.134 . 1 
      655 .  77 GLY CA   C  44.96  . 1 
      656 .  77 GLY HA2  H   4.036 . 2 
      657 .  77 GLY HA3  H   3.655 . 2 
      658 .  77 GLY C    C 177.431 . 1 
      659 .  78 ALA H    H   7.726 . 1 
      660 .  78 ALA N    N 122.948 . 1 
      661 .  78 ALA CA   C  51.965 . 1 
      662 .  78 ALA HA   H   4.418 . 1 
      663 .  78 ALA C    C 173.368 . 1 
      664 .  78 ALA CB   C  19.39  . 1 
      665 .  78 ALA HB   H   1.312 . 1 
      666 .  79 THR H    H   8.032 . 1 
      667 .  79 THR N    N 109.508 . 1 
      668 .  79 THR CA   C  59.9   . 1 
      669 .  79 THR HA   H   4.745 . 1 
      670 .  79 THR C    C 178.057 . 1 
      671 .  79 THR CB   C  70.7   . 1 
      672 .  79 THR HB   H   4.473 . 1 
      673 .  79 THR HG2  H   1.312 . 1 
      674 .  80 HIS H    H   9.204 . 1 
      675 .  80 HIS N    N 120.76  . 1 
      676 .  80 HIS CA   C  61.18  . 1 
      677 .  80 HIS HA   H   3.818 . 1 
      678 .  80 HIS C    C 174.618 . 1 
      679 .  80 HIS CB   C  30.9   . 1 
      680 .  80 HIS HB2  H   3.164 . 1 
      681 .  80 HIS HB3  H   3.164 . 1 
      682 .  80 HIS HD2  H   6.728 . 1 
      683 .  80 HIS HE1  H   7.804 . 1 
      684 .  81 LYS H    H   8.448 . 1 
      685 .  81 LYS N    N 116.697 . 1 
      686 .  81 LYS CA   C  59.4   . 1 
      687 .  81 LYS HA   H   3.818 . 1 
      688 .  81 LYS C    C 176.494 . 1 
      689 .  81 LYS CB   C  32.5   . 1 
      690 .  81 LYS HB2  H   1.913 . 2 
      691 .  81 LYS HB3  H   1.722 . 2 
      692 .  81 LYS HG2  H   1.367 . 1 
      693 .  81 LYS HG3  H   1.367 . 1 
      694 .  82 GLN H    H   7.705 . 1 
      695 .  82 GLN N    N 117.322 . 1 
      696 .  82 GLN CA   C  57.845 . 1 
      697 .  82 GLN HA   H   4.036 . 1 
      698 .  82 GLN C    C 178.369 . 1 
      699 .  82 GLN CB   C  28.396 . 1 
      700 .  82 GLN HB2  H   1.911 . 2 
      701 .  82 GLN HB3  H   1.966 . 2 
      702 .  82 GLN HG2  H   2.238 . 1 
      703 .  82 GLN HG3  H   2.238 . 1 
      704 .  83 ALA H    H   8.72  . 1 
      705 .  83 ALA N    N 124.198 . 1 
      706 .  83 ALA CA   C  55.343 . 1 
      707 .  83 ALA HA   H   3.818 . 1 
      708 .  83 ALA C    C 179.307 . 1 
      709 .  83 ALA CB   C  18.42  . 1 
      710 .  83 ALA HB   H   1.312 . 1 
      711 .  84 VAL H    H   8.325 . 1 
      712 .  84 VAL N    N 116.697 . 1 
      713 .  84 VAL CA   C  66.7   . 1 
      714 .  84 VAL HA   H   3.382 . 1 
      715 .  84 VAL C    C 178.057 . 1 
      716 .  84 VAL CB   C  31.3   . 1 
      717 .  84 VAL HB   H   1.966 . 1 
      718 .  84 VAL HG1  H   0.713 . 1 
      719 .  84 VAL HG2  H   0.767 . 1 
      720 .  85 GLU H    H   8.134 . 1 
      721 .  85 GLU N    N 120.135 . 1 
      722 .  85 GLU CA   C  58.91  . 1 
      723 .  85 GLU HA   H   3.982 . 1 
      724 .  85 GLU C    C 178.994 . 1 
      725 .  85 GLU CB   C  28.7   . 1 
      726 .  85 GLU HB2  H   2.02  . 2 
      727 .  85 GLU HB3  H   2.075 . 2 
      728 .  85 GLU HG2  H   2.302 . 2 
      729 .  85 GLU HG3  H   2.371 . 2 
      730 .  86 THR H    H   8.248 . 1 
      731 .  86 THR N    N 117.009 . 1 
      732 .  86 THR CA   C  67.802 . 1 
      733 .  86 THR HA   H   4.145 . 1 
      734 .  86 THR C    C 174.931 . 1 
      735 .  86 THR CB   C  66.677 . 1 
      736 .  86 THR HB   H   3.824 . 1 
      737 .  86 THR HG2  H   1.04  . 1 
      738 .  87 LEU H    H   7.903 . 1 
      739 .  87 LEU N    N 119.51  . 1 
      740 .  87 LEU CA   C  57.7   . 1 
      741 .  87 LEU HA   H   3.818 . 1 
      742 .  87 LEU C    C 176.494 . 1 
      743 .  87 LEU CB   C  41.247 . 1 
      744 .  87 LEU HB2  H   1.857 . 1 
      745 .  87 LEU HB3  H   1.857 . 1 
      746 .  87 LEU HG   H   1.366 . 1 
      747 .  88 ARG H    H   8.202 . 1 
      748 .  88 ARG N    N 120.76  . 1 
      749 .  88 ARG CA   C  58.27  . 1 
      750 .  88 ARG HA   H   4.036 . 1 
      751 .  88 ARG C    C 178.369 . 1 
      752 .  88 ARG CB   C  30.274 . 1 
      753 .  88 ARG HB2  H   1.857 . 1 
      754 .  88 ARG HB3  H   1.857 . 1 
      755 .  89 ASN H    H   7.814 . 1 
      756 .  89 ASN N    N 119.197 . 1 
      757 .  89 ASN CA   C  52.29  . 1 
      758 .  89 ASN HA   H   4.908 . 1 
      759 .  89 ASN C    C 177.744 . 1 
      760 .  89 ASN CB   C  36.654 . 1 
      761 .  89 ASN HB2  H   2.729 . 2 
      762 .  89 ASN HB3  H   2.947 . 2 
      763 .  90 THR H    H   7.685 . 1 
      764 .  90 THR N    N 109.821 . 1 
      765 .  90 THR CA   C  59.471 . 1 
      766 .  90 THR HA   H   4.363 . 1 
      767 .  90 THR C    C 174.618 . 1 
      768 .  90 THR CB   C  72.3   . 1 
      769 .  90 THR HB   H   4.282 . 1 
      770 .  90 THR CG2  C  21.7   . 1 
      771 .  90 THR HG2  H   1.203 . 1 
      772 .  91 GLY H    H   8.495 . 1 
      773 .  91 GLY N    N 109.508 . 1 
      774 .  91 GLY CA   C  43.559 . 1 
      775 .  91 GLY HA2  H   4.363 . 2 
      776 .  91 GLY HA3  H   3.709 . 2 
      777 .  91 GLY C    C 174.931 . 1 
      778 .  92 GLN H    H   8.264 . 1 
      779 .  92 GLN N    N 117.322 . 1 
      780 .  92 GLN CA   C  57.8   . 1 
      781 .  92 GLN HA   H   3.927 . 1 
      782 .  92 GLN C    C 173.494 . 1 
      783 .  92 GLN CB   C  28.47  . 1 
      784 .  92 GLN HB2  H   2.075 . 1 
      785 .  92 GLN HB3  H   2.075 . 1 
      786 .  92 GLN HG2  H   2.402 . 1 
      787 .  92 GLN HG3  H   2.402 . 1 
      788 .  93 VAL H    H   7.78  . 1 
      789 .  93 VAL N    N 116.196 . 1 
      790 .  93 VAL CA   C  61.047 . 1 
      791 .  93 VAL HA   H   4.636 . 1 
      792 .  93 VAL C    C 174.931 . 1 
      793 .  93 VAL CB   C  32.676 . 1 
      794 .  93 VAL HB   H   1.802 . 1 
      795 .  93 VAL HG1  H   0.822 . 1 
      796 .  93 VAL HG2  H   0.658 . 1 
      797 .  94 VAL H    H   9.061 . 1 
      798 .  94 VAL N    N 128.574 . 1 
      799 .  94 VAL CA   C  60.75  . 1 
      800 .  94 VAL HA   H   4.363 . 1 
      801 .  94 VAL C    C 173.056 . 1 
      802 .  94 VAL CB   C  34.4   . 1 
      803 .  94 VAL HB   H   1.802 . 1 
      804 .  94 VAL HG1  H   0.822 . 1 
      805 .  94 VAL HG2  H   0.93  . 1 
      806 .  95 HIS H    H   8.788 . 1 
      807 .  95 HIS N    N 126.073 . 1 
      808 .  95 HIS CA   C  55.643 . 1 
      809 .  95 HIS HA   H   4.963 . 1 
      810 .  95 HIS CB   C  31.249 . 1 
      811 .  95 HIS HB2  H   3.11  . 1 
      812 .  95 HIS HB3  H   3.11  . 1 
      813 .  95 HIS HD2  H   7.028 . 1 
      814 .  95 HIS HE1  H   7.613 . 1 
      815 .  96 LEU H    H   9.054 . 1 
      816 .  96 LEU N    N 126.699 . 1 
      817 .  96 LEU CA   C  53.091 . 1 
      818 .  96 LEU HA   H   4.963 . 1 
      819 .  96 LEU C    C 173.993 . 1 
      820 .  96 LEU CB   C  44.6   . 1 
      821 .  96 LEU HB2  H   1.606 . 2 
      822 .  96 LEU HB3  H   1.53  . 2 
      823 .  96 LEU HD1  H   0.719 . 1 
      824 .  96 LEU HD2  H   0.651 . 1 
      825 .  96 LEU HG   H   1.019 . 1 
      826 .  97 LEU H    H   8.053 . 1 
      827 .  97 LEU N    N 124.511 . 1 
      828 .  97 LEU CA   C  53.16  . 1 
      829 .  97 LEU HA   H   4.69  . 1 
      830 .  97 LEU C    C 173.056 . 1 
      831 .  97 LEU CB   C  44.985 . 1 
      832 .  97 LEU HB2  H   1.388 . 2 
      833 .  97 LEU HB3  H   1.748 . 2 
      834 .  97 LEU HD1  H   0.76  . 1 
      835 .  97 LEU HD2  H   0.76  . 1 
      836 .  97 LEU HG   H   1.279 . 1 
      837 .  98 LEU H    H   8.924 . 1 
      838 .  98 LEU N    N 127.324 . 1 
      839 .  98 LEU CA   C  53.8   . 1 
      840 .  98 LEU HA   H   5.235 . 1 
      841 .  98 LEU C    C 174.306 . 1 
      842 .  98 LEU CB   C  45.6   . 1 
      843 .  98 LEU HD1  H   0.931 . 1 
      844 .  98 LEU HD2  H   0.168 . 1 
      845 .  98 LEU HG   H   1.203 . 1 
      846 .  99 GLU H    H   8.815 . 1 
      847 .  99 GLU N    N 118.885 . 1 
      848 .  99 GLU CA   C  53.24  . 1 
      849 .  99 GLU HA   H   5.072 . 1 
      850 .  99 GLU C    C 173.368 . 1 
      851 .  99 GLU CB   C  33.5   . 1 
      852 .  99 GLU HB2  H   1.911 . 1 
      853 .  99 GLU HB3  H   1.911 . 1 
      854 . 100 LYS H    H   9.376 . 1 
      855 . 100 LYS N    N 128.886 . 1 
      856 . 100 LYS CA   C  55.57  . 1 
      857 . 100 LYS HA   H   4.363 . 1 
      858 . 100 LYS CB   C  31.4   . 1 
      859 . 100 LYS HB2  H   1.75  . 2 
      860 . 100 LYS HB3  H   2.293 . 2 
      861 . 100 LYS HG2  H   1.436 . 1 
      862 . 100 LYS HG3  H   1.436 . 1 
      863 . 100 LYS HD2  H   1.584 . 1 
      864 . 100 LYS HD3  H   1.584 . 1 
      865 . 100 LYS HE2  H   1.985 . 1 
      866 . 100 LYS HE3  H   1.985 . 1 
      867 . 101 GLY H    H   9.742 . 1 
      868 . 101 GLY N    N 117.947 . 1 
      869 . 101 GLY CA   C  44.835 . 1 
      870 . 101 GLY HA2  H   4.254 . 2 
      871 . 101 GLY HA3  H   3.818 . 2 
      872 . 101 GLY C    C 177.744 . 1 
      873 . 102 GLN H    H   8.291 . 1 
      874 . 102 GLN N    N 116.697 . 1 
      875 . 102 GLN CA   C  54.73  . 1 
      876 . 102 GLN HA   H   4.254 . 1 
      877 . 102 GLN C    C 172.868 . 1 
      878 . 102 GLN CB   C  29.39  . 1 
      879 . 102 GLN HB2  H   1.857 . 1 
      880 . 102 GLN HB3  H   1.857 . 1 
      881 . 102 GLN HG2  H   2.347 . 1 
      882 . 102 GLN HG3  H   2.347 . 1 
      883 . 103 SER H    H   8.535 . 1 
      884 . 103 SER N    N 118.19  . 1 
      885 . 103 SER CA   C  56.331 . 1 
      886 . 103 SER HA   H   4.671 . 1 
      887 . 103 SER CB   C  62.532 . 1 
      888 . 103 SER HB2  H   3.804 . 1 
      889 . 103 SER HB3  H   3.804 . 1 
      890 . 104 PRO CA   C  63.019 . 1 
      891 . 104 PRO HA   H   4.472 . 1 
      892 . 104 PRO CB   C  31.439 . 1 
      893 . 104 PRO HB2  H   1.941 . 2 
      894 . 104 PRO HB3  H   2.238 . 2 
      895 . 104 PRO HG2  H   1.911 . 1 
      896 . 104 PRO HG3  H   1.911 . 1 
      897 . 104 PRO HD2  H   3.764 . 1 
      898 . 104 PRO HD3  H   3.764 . 1 
      899 . 105 THR H    H   8.277 . 1 
      900 . 105 THR N    N 113.571 . 1 
      901 . 105 THR CA   C  61.423 . 1 
      902 . 105 THR HA   H   4.241 . 1 
      903 . 105 THR C    C 176.806 . 1 
      904 . 105 THR CB   C  69.304 . 1 
      905 . 105 THR HB   H   4.2   . 1 
      906 . 105 THR HG2  H   1.148 . 1 
      907 . 106 SER H    H   8.257 . 1 
      908 . 106 SER N    N 118.26  . 1 
      909 . 106 SER CA   C  57.85  . 1 
      910 . 106 SER HA   H   4.254 . 1 
      911 . 106 SER C    C 174.306 . 1 
      912 . 106 SER CB   C  63.524 . 1 
      913 . 106 SER HB2  H   3.818 . 1 
      914 . 106 SER HB3  H   3.818 . 1 
      915 . 107 LYS H    H   8.427 . 1 
      916 . 107 LYS N    N 123.573 . 1 
      917 . 107 LYS CA   C  55.868 . 1 
      918 . 107 LYS HA   H   4.418 . 1 
      919 . 107 LYS C    C 173.993 . 1 
      920 . 107 LYS CB   C  32.525 . 1 
      921 . 107 LYS HB2  H   1.879 . 2 
      922 . 107 LYS HB3  H   1.693 . 2 
      923 . 107 LYS HG2  H   1.421 . 1 
      924 . 107 LYS HG3  H   1.421 . 1 
      925 . 107 LYS HD2  H   1.674 . 1 
      926 . 107 LYS HD3  H   1.674 . 1 
      927 . 107 LYS HE2  H   2.978 . 1 
      928 . 107 LYS HE3  H   2.978 . 1 
      929 . 108 GLU H    H   8.046 . 1 
      930 . 108 GLU N    N 127.011 . 1 
      931 . 108 GLU HA   H   4.309 . 1 
      932 . 108 GLU C    C 175.244 . 1 
      933 . 108 GLU HB2  H   1.748 . 1 
      934 . 108 GLU HB3  H   1.748 . 1 
      935 . 108 GLU HG2  H   2.184 . 1 
      936 . 108 GLU HG3  H   2.184 . 1 

   stop_

save_