data_7061

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
NMR structure of talin-PTB in complex with PIPKI
;
   _BMRB_accession_number   7061
   _BMRB_flat_file_name     bmr7061.str
   _Entry_type              original
   _Submission_date         2006-04-10
   _Accession_date          2006-04-12
   _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 Kong  X. . . 
      2 Wang  X. . . 
      3 Misra S. . . 
      4 Qin   J. . . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 2 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  740 
      "13C chemical shifts" 441 
      "15N chemical shifts" 123 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      2008-07-17 update BMRB 'Updating non-standard residue' 

   stop_

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full                .
   _Citation_title              
;
Structural Basis for the Phosphorylation-regulated Focal Adhesion Targeting of
Type Igamma Phosphatidylinositol Phosphate Kinase (PIPKIgamma) by Talin
;
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    16616931

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Kong  X. . . 
      2 Wang  X. . . 
      3 Misra S. . . 
      4 Qin   J. . . 

   stop_

   _Journal_abbreviation        'J. Mol. Biol.'
   _Journal_volume               359
   _Journal_issue                1
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   47
   _Page_last                    54
   _Year                         2006
   _Details                      .

   loop_
      _Keyword

       PIPKI       
      'PTB DOMAIN' 
       TALIN       

   stop_

save_


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

save_system_Talin-1
   _Saveframe_category         molecular_system

   _Mol_system_name            Talin-1
   _Abbreviation_common        Talin-1
   _Enzyme_commission_number   .

   loop_
      _Mol_system_component_name
      _Mol_label

      Talin-1 $Talin-1  
      peptide $SWVXSPLH 

   stop_

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

save_


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

save_Talin-1
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 Talin-1
   _Abbreviation_common                         Talin-1
   _Molecular_mass                              .
   _Mol_thiol_state                            'all free'
   _Details                                     .

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               106
   _Mol_residue_sequence                       
;
LKTYGVSFFLVKEKMKGKNK
LVPRLLGITKECVMRVDEKT
KEVIQEWSLTNIKRWAASPK
SFTLDFGDYQDGYYSVQTTE
GEQIAQLIAGYIDIILKKKK
SKDHFG
;

   loop_
      _Residue_seq_code
      _Residue_label

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

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2014-05-12

   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

      BMRB        15792  talin-F2F3                                                                                                                        95.28  201 100.00 100.00 1.35e-51 
      PDB  1MIX          "Crystal Structure Of A Ferm Domain Of Talin"                                                                                      90.57  206 100.00 100.00 3.29e-49 
      PDB  1MIZ          "Crystal Structure Of An Integrin Beta3-Talin Chimera"                                                                             90.57  201 100.00 100.00 2.50e-49 
      PDB  1MK7          "Crystal Structure Of An Integrin Beta3-Talin Chimera"                                                                             90.57  192 100.00 100.00 3.27e-49 
      PDB  1MK9          "Crystal Structure Of An Integrin Beta3-Talin Chimera"                                                                             90.57  192 100.00 100.00 3.27e-49 
      PDB  1Y19          "Structural Basis For Phosphatidylinositol Phosphate Kinase Type I-Gamma Binding To Talin At Focal Adhesions"                     100.00  202 100.00 100.00 4.55e-55 
      PDB  2G35          "Nmr Structure Of Talin-Ptb In Complex With Pipki"                                                                                 94.34  100 100.00 100.00 9.04e-51 
      PDB  2H7D          "Solution Structure Of The Talin F3 Domain In Complex With A Chimeric Beta3 Integrin-Pip Kinase Peptide"                           91.51  101  98.97  98.97 5.44e-48 
      PDB  2H7E          "Solution Structure Of The Talin F3 Domain In Complex With A Chimeric Beta3 Integrin-Pip Kinase Peptide- Minimized Average Struc"  91.51  101  98.97  98.97 5.44e-48 
      PDB  2K00          "Solution Structure Of The Talin F3 In Complex With Layilin Cytodomain"                                                            86.79   92 100.00 100.00 1.24e-46 
      PDB  2KGX          "Haddock Structure Of The Talin F3 Domain In Complex With Talin 1655-1822"                                                         85.85   91  98.90  98.90 5.49e-45 
      PDB  3IVF          "Crystal Structure Of The Talin Head Ferm Domain"                                                                                  90.57  371 100.00 100.00 2.34e-49 
      DBJ  BAA82979      "KIAA1027 protein [Homo sapiens]"                                                                                                 100.00 2550  99.06 100.00 7.14e-57 
      DBJ  BAC30516      "unnamed protein product [Mus musculus]"                                                                                           89.62  300 100.00 100.00 4.92e-49 
      DBJ  BAC65702      "mKIAA1027 protein [Mus musculus]"                                                                                                100.00 2564 100.00 100.00 2.65e-57 
      DBJ  BAE27781      "unnamed protein product [Mus musculus]"                                                                                          100.00 2541 100.00 100.00 2.74e-57 
      DBJ  BAG09941      "talin-1 [synthetic construct]"                                                                                                   100.00 2541  99.06 100.00 7.08e-57 
      EMBL CAA39588      "talin [Mus musculus]"                                                                                                            100.00 2541 100.00 100.00 2.65e-57 
      EMBL CAI10978      "talin 1 [Homo sapiens]"                                                                                                          100.00 2429  99.06 100.00 7.76e-57 
      EMBL CAM17190      "talin 1 [Mus musculus]"                                                                                                          100.00 2541 100.00 100.00 2.69e-57 
      GB   AAD13152      "talin [Homo sapiens]"                                                                                                            100.00 2541  99.06 100.00 6.85e-57 
      GB   AAF23322      "talin [Homo sapiens]"                                                                                                            100.00 2541  99.06 100.00 6.85e-57 
      GB   AAF27330      "talin [Homo sapiens]"                                                                                                            100.00 2540  99.06 100.00 7.08e-57 
      GB   AAH42923      "Talin 1 [Homo sapiens]"                                                                                                          100.00 2541  99.06 100.00 7.08e-57 
      GB   AAI21760      "Tln1 protein [Danio rerio]"                                                                                                       94.34  405  99.00  99.00 5.62e-50 
      PRF  1617167A       talin                                                                                                                            100.00 2541 100.00 100.00 2.65e-57 
      REF  NP_001034114  "talin-1 [Rattus norvegicus]"                                                                                                     100.00 2541 100.00 100.00 2.41e-57 
      REF  NP_006280     "talin-1 [Homo sapiens]"                                                                                                          100.00 2541  99.06 100.00 7.08e-57 
      REF  NP_035732     "talin-1 [Mus musculus]"                                                                                                          100.00 2541 100.00 100.00 2.69e-57 
      REF  NP_989854     "talin-1 [Gallus gallus]"                                                                                                         100.00 2541 100.00 100.00 1.27e-56 
      REF  XP_001084941  "PREDICTED: talin-1 [Macaca mulatta]"                                                                                             100.00 2428  99.06 100.00 7.70e-57 
      SP   P26039        "RecName: Full=Talin-1"                                                                                                           100.00 2541 100.00 100.00 2.65e-57 
      SP   P54939        "RecName: Full=Talin-1"                                                                                                           100.00 2541 100.00 100.00 1.27e-56 
      SP   Q9Y490        "RecName: Full=Talin-1"                                                                                                           100.00 2541  99.06 100.00 7.08e-57 

   stop_

save_


save_SWVXSPLH
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                 SWVXSPLH
   _Abbreviation_common                         SWVXSPLH
   _Molecular_mass                              .
   _Mol_thiol_state                            'not present'
   _Details                                     .
   _Residue_count                               8
   _Mol_residue_sequence                        SWVXSPLH

   loop_
      _Residue_seq_code
      _Residue_label

      1 SER  2 TRP  3 VAL  4 PTR  5 SER 
      6 PRO  7 LEU  8 HIS 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   .

save_


    ######################
    #  Polymer residues  #
    ######################

save_chem_comp_PTR
   _Saveframe_category            polymer_residue

   _Mol_type                     'L-PEPTIDE LINKING'
   _Name_common                   O-PHOSPHOTYROSINE
   _BMRB_code                     .
   _PDB_code                      PTR
   _Standard_residue_derivative   .
   _Molecular_mass                261.168
   _Mol_paramagnetic              .
   _Details                      
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Sep 29 12:29:47 2011
;

   loop_
      _Atom_name
      _PDB_atom_name
      _Atom_type
      _Atom_chirality
      _Atom_charge
      _Atom_oxidation_number
      _Atom_unpaired_electrons

      N    N    N . 0 . ? 
      CA   CA   C . 0 . ? 
      C    C    C . 0 . ? 
      O    O    O . 0 . ? 
      OXT  OXT  O . 0 . ? 
      CB   CB   C . 0 . ? 
      CG   CG   C . 0 . ? 
      CD1  CD1  C . 0 . ? 
      CD2  CD2  C . 0 . ? 
      CE1  CE1  C . 0 . ? 
      CE2  CE2  C . 0 . ? 
      CZ   CZ   C . 0 . ? 
      OH   OH   O . 0 . ? 
      P    P    P . 0 . ? 
      O1P  O1P  O . 0 . ? 
      O2P  O2P  O . 0 . ? 
      O3P  O3P  O . 0 . ? 
      H    H    H . 0 . ? 
      HN2  HN2  H . 0 . ? 
      HA   HA   H . 0 . ? 
      HXT  HXT  H . 0 . ? 
      HB2  HB2  H . 0 . ? 
      HB3  HB3  H . 0 . ? 
      HD1  HD1  H . 0 . ? 
      HD2  HD2  H . 0 . ? 
      HE1  HE1  H . 0 . ? 
      HE2  HE2  H . 0 . ? 
      HO2P HO2P H . 0 . ? 
      HO3P HO3P H . 0 . ? 

   stop_

   loop_
      _Bond_order
      _Bond_atom_one_atom_name
      _Bond_atom_two_atom_name
      _PDB_bond_atom_one_atom_name
      _PDB_bond_atom_two_atom_name

      SING N   CA   ? ? 
      SING N   H    ? ? 
      SING N   HN2  ? ? 
      SING CA  C    ? ? 
      SING CA  CB   ? ? 
      SING CA  HA   ? ? 
      DOUB C   O    ? ? 
      SING C   OXT  ? ? 
      SING OXT HXT  ? ? 
      SING CB  CG   ? ? 
      SING CB  HB2  ? ? 
      SING CB  HB3  ? ? 
      DOUB CG  CD1  ? ? 
      SING CG  CD2  ? ? 
      SING CD1 CE1  ? ? 
      SING CD1 HD1  ? ? 
      DOUB CD2 CE2  ? ? 
      SING CD2 HD2  ? ? 
      DOUB CE1 CZ   ? ? 
      SING CE1 HE1  ? ? 
      SING CE2 CZ   ? ? 
      SING CE2 HE2  ? ? 
      SING CZ  OH   ? ? 
      SING OH  P    ? ? 
      DOUB P   O1P  ? ? 
      SING P   O2P  ? ? 
      SING P   O3P  ? ? 
      SING O2P HO2P ? ? 
      SING O3P HO3P ? ? 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species

      $Talin-1  Mouse 10090 Eukaryota Metazoa . . 
      $SWVXSPLH .          . .         .       . . 

   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

      $Talin-1  'recombinant technology' . . . . . 
      $SWVXSPLH 'chemical synthesis'     . . . . . 

   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

      $Talin-1            1 mM '[U-13C; U-15N]' 
      $SWVXSPLH           1 mM  .               
      'phosphate buffer' 20 mM  .               
       Ca2+               5 mM  .               
       D2O               10 %   .               
       H2O               90 %   .               

   stop_

save_


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

save_TALOS
   _Saveframe_category   software

   _Name                 TALOS
   _Version              .

   loop_
      _Task

      'data analysis' 

   stop_

   _Details              .

save_


save_X-PLOR
   _Saveframe_category   software

   _Name                 X-PLOR
   _Version              .

   loop_
      _Task

      refinement 

   stop_

   _Details              .

save_


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

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

save_NMR_spectrometer
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         VARIAN
   _Model                INOVA
   _Field_strength       600
   _Details              .

save_


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

save_HNCACB_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCACB
   _Sample_label        $sample_1

save_


save_CBCA(CO)NH_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      CBCA(CO)NH
   _Sample_label        $sample_1

save_


save_HCCH-TOCSY_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HCCH-TOCSY
   _Sample_label        $sample_1

save_


save_HNCO_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name      HNCO
   _Sample_label        $sample_1

save_


save_edited_NOESY_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     'edited NOESY'
   _Sample_label        $sample_1

save_


save_filtered_NOESY_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     'filtered NOESY'
   _Sample_label        $sample_1

save_


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

save_sample_cond_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.3 . pH 
      temperature 298   . 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
      _Indirect_shift_ratio_citation_label
      _Correction_value_citation_label

      DSS C 13 'methyl protons' ppm 0.0 .        indirect . . . 0.251449530 $entry_citation $entry_citation 
      DSS H  1 'methyl protons' ppm 0.0 internal direct   . . . 1.0         $entry_citation $entry_citation 
      DSS N 15 'methyl protons' ppm 0.0 .        indirect . . . 0.101329118 $entry_citation $entry_citation 

   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_chemical_shift_set_1
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $sample_cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name        Talin-1
   _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 LEU H    H   7.3200 . . 
         2 .   1 LEU HA   H   4.2700 . . 
         3 .   1 LEU HB2  H  -0.1000 . . 
         4 .   1 LEU HB3  H   0.6000 . . 
         5 .   1 LEU HG   H   1.2200 . . 
         6 .   1 LEU HD1  H   0.0500 . . 
         7 .   1 LEU HD2  H   0.3700 . . 
         8 .   1 LEU CA   C  56.2300 . . 
         9 .   1 LEU CB   C  41.3800 . . 
        10 .   1 LEU CG   C  26.0900 . . 
        11 .   1 LEU CD1  C  24.6200 . . 
        12 .   1 LEU CD2  C  21.6700 . . 
        13 .   1 LEU N    N 120.4000 . . 
        14 .   2 LYS H    H   8.5000 . . 
        15 .   2 LYS HA   H   4.2200 . . 
        16 .   2 LYS HB2  H   1.8000 . . 
        17 .   2 LYS HB3  H   1.8800 . . 
        18 .   2 LYS HG2  H   1.4400 . . 
        19 .   2 LYS HG3  H   1.4400 . . 
        20 .   2 LYS HD2  H   1.6700 . . 
        21 .   2 LYS HD3  H   1.6700 . . 
        22 .   2 LYS HE2  H   2.9800 . . 
        23 .   2 LYS HE3  H   2.9800 . . 
        24 .   2 LYS CA   C  56.7400 . . 
        25 .   2 LYS CB   C  32.3900 . . 
        26 .   2 LYS CG   C  24.5000 . . 
        27 .   2 LYS CD   C  28.9200 . . 
        28 .   2 LYS CE   C  42.1900 . . 
        29 .   2 LYS N    N 120.6600 . . 
        30 .   3 THR H    H   7.9200 . . 
        31 .   3 THR HA   H   4.2500 . . 
        32 .   3 THR HB   H   4.2300 . . 
        33 .   3 THR HG2  H   1.1200 . . 
        34 .   3 THR CA   C  61.5600 . . 
        35 .   3 THR CB   C  69.4000 . . 
        36 .   3 THR CG2  C  21.5500 . . 
        37 .   3 THR N    N 112.5300 . . 
        38 .   4 TYR H    H   7.9800 . . 
        39 .   4 TYR HA   H   4.5700 . . 
        40 .   4 TYR HB2  H   3.0500 . . 
        41 .   4 TYR HB3  H   2.9600 . . 
        42 .   4 TYR HD1  H   7.1000 . . 
        43 .   4 TYR HD2  H   7.1000 . . 
        44 .   4 TYR HE1  H   6.7800 . . 
        45 .   4 TYR HE2  H   6.7800 . . 
        46 .   4 TYR CA   C  57.9300 . . 
        47 .   4 TYR CB   C  38.5100 . . 
        48 .   4 TYR CD1  C 132.6700 . . 
        49 .   4 TYR CD2  C 132.6700 . . 
        50 .   4 TYR CE1  C 117.8700 . . 
        51 .   4 TYR CE2  C 117.8700 . . 
        52 .   4 TYR N    N 122.8800 . . 
        53 .   5 GLY H    H   8.3500 . . 
        54 .   5 GLY HA2  H   3.8000 . . 
        55 .   5 GLY HA3  H   3.8000 . . 
        56 .   5 GLY CA   C  45.3200 . . 
        57 .   5 GLY N    N 111.4200 . . 
        58 .   6 VAL H    H   7.6500 . . 
        59 .   6 VAL HA   H   4.0800 . . 
        60 .   6 VAL HB   H   1.5400 . . 
        61 .   6 VAL HG1  H   0.0800 . . 
        62 .   6 VAL HG2  H   0.3600 . . 
        63 .   6 VAL CA   C  60.7000 . . 
        64 .   6 VAL CB   C  33.3200 . . 
        65 .   6 VAL CG1  C  20.3700 . . 
        66 .   6 VAL CG2  C  20.3700 . . 
        67 .   6 VAL N    N 120.8300 . . 
        68 .   7 SER H    H   8.0000 . . 
        69 .   7 SER HA   H   4.5600 . . 
        70 .   7 SER HB2  H   3.6500 . . 
        71 .   7 SER HB3  H   3.6500 . . 
        72 .   7 SER CA   C  57.5500 . . 
        73 .   7 SER CB   C  63.9400 . . 
        74 .   7 SER N    N 123.3500 . . 
        75 .   8 PHE H    H   8.5600 . . 
        76 .   8 PHE HA   H   5.6300 . . 
        77 .   8 PHE HB2  H   2.7800 . . 
        78 .   8 PHE HB3  H   2.7800 . . 
        79 .   8 PHE HD1  H   6.7500 . . 
        80 .   8 PHE HD2  H   6.7500 . . 
        81 .   8 PHE HE1  H   7.1700 . . 
        82 .   8 PHE HE2  H   7.1700 . . 
        83 .   8 PHE HZ   H   7.2700 . . 
        84 .   8 PHE CA   C  57.1400 . . 
        85 .   8 PHE CB   C  42.6700 . . 
        86 .   8 PHE CD1  C 131.3200 . . 
        87 .   8 PHE CD2  C 131.3200 . . 
        88 .   8 PHE CE1  C 129.4800 . . 
        89 .   8 PHE CE2  C 129.4800 . . 
        90 .   8 PHE CZ   C 130.9500 . . 
        91 .   8 PHE N    N 122.7500 . . 
        92 .   9 PHE H    H   9.2000 . . 
        93 .   9 PHE HA   H   4.6300 . . 
        94 .   9 PHE HB2  H   2.7000 . . 
        95 .   9 PHE HB3  H   3.0600 . . 
        96 .   9 PHE HD1  H   7.2000 . . 
        97 .   9 PHE HD2  H   7.2000 . . 
        98 .   9 PHE HE1  H   6.9700 . . 
        99 .   9 PHE HE2  H   6.9700 . . 
       100 .   9 PHE HZ   H   7.1700 . . 
       101 .   9 PHE CA   C  56.7600 . . 
       102 .   9 PHE CB   C  41.7800 . . 
       103 .   9 PHE CD1  C 132.1000 . . 
       104 .   9 PHE CD2  C 132.1000 . . 
       105 .   9 PHE CE1  C 130.5400 . . 
       106 .   9 PHE CE2  C 130.5400 . . 
       107 .   9 PHE CZ   C 130.9500 . . 
       108 .   9 PHE N    N 120.1800 . . 
       109 .  10 LEU H    H   9.4600 . . 
       110 .  10 LEU HA   H   4.9400 . . 
       111 .  10 LEU HB2  H   1.4300 . . 
       112 .  10 LEU HB3  H   2.0200 . . 
       113 .  10 LEU HG   H   1.5700 . . 
       114 .  10 LEU HD1  H   0.9200 . . 
       115 .  10 LEU HD2  H   0.9200 . . 
       116 .  10 LEU CA   C  55.3400 . . 
       117 .  10 LEU CB   C  41.3800 . . 
       118 .  10 LEU CG   C  25.7000 . . 
       119 .  10 LEU CD1  C  25.2500 . . 
       120 .  10 LEU CD2  C  22.9100 . . 
       121 .  10 LEU N    N 127.6100 . . 
       122 .  11 VAL H    H   9.3300 . . 
       123 .  11 VAL HA   H   5.1100 . . 
       124 .  11 VAL HB   H   2.2100 . . 
       125 .  11 VAL HG1  H   0.9300 . . 
       126 .  11 VAL HG2  H   0.9300 . . 
       127 .  11 VAL CA   C  58.7000 . . 
       128 .  11 VAL CB   C  35.3400 . . 
       129 .  11 VAL CG1  C  18.4900 . . 
       130 .  11 VAL CG2  C  21.0000 . . 
       131 .  11 VAL N    N 124.1000 . . 
       132 .  12 LYS H    H   8.3400 . . 
       133 .  12 LYS HA   H   5.2500 . . 
       134 .  12 LYS HB2  H   1.5600 . . 
       135 .  12 LYS HB3  H   1.7100 . . 
       136 .  12 LYS HG2  H   1.1900 . . 
       137 .  12 LYS HG3  H   1.1900 . . 
       138 .  12 LYS HD2  H   1.5600 . . 
       139 .  12 LYS HD3  H   1.5600 . . 
       140 .  12 LYS HE2  H   2.8600 . . 
       141 .  12 LYS HE3  H   2.8600 . . 
       142 .  12 LYS CA   C  54.9500 . . 
       143 .  12 LYS CB   C  36.1300 . . 
       144 .  12 LYS CG   C  25.4800 . . 
       145 .  12 LYS CD   C  29.4500 . . 
       146 .  12 LYS CE   C  44.6000 . . 
       147 .  12 LYS N    N 116.7200 . . 
       148 .  13 GLU H    H   9.1900 . . 
       149 .  13 GLU HA   H   4.7700 . . 
       150 .  13 GLU HB2  H   2.0800 . . 
       151 .  13 GLU HB3  H   2.1400 . . 
       152 .  13 GLU HG2  H   2.3400 . . 
       153 .  13 GLU HG3  H   2.4700 . . 
       154 .  13 GLU CA   C  53.9800 . . 
       155 .  13 GLU CB   C  33.0700 . . 
       156 .  13 GLU CG   C  36.2700 . . 
       157 .  13 GLU N    N 123.1000 . . 
       158 .  14 LYS H    H   8.8400 . . 
       159 .  14 LYS HA   H   4.6500 . . 
       160 .  14 LYS HB2  H   1.5900 . . 
       161 .  14 LYS HB3  H   1.8200 . . 
       162 .  14 LYS HG2  H   1.3500 . . 
       163 .  14 LYS HG3  H   1.5200 . . 
       164 .  14 LYS HD2  H   0.0300 . . 
       165 .  14 LYS HD3  H   0.9600 . . 
       166 .  14 LYS HE2  H   2.7700 . . 
       167 .  14 LYS HE3  H   2.7700 . . 
       168 .  14 LYS CA   C  55.7100 . . 
       169 .  14 LYS CB   C  33.0400 . . 
       170 .  14 LYS CG   C  24.6100 . . 
       171 .  14 LYS CD   C  29.0300 . . 
       172 .  14 LYS CE   C  42.1000 . . 
       173 .  14 LYS N    N 124.2300 . . 
       174 .  15 MET H    H   8.9100 . . 
       175 .  15 MET HA   H   4.6200 . . 
       176 .  15 MET HB2  H   2.1000 . . 
       177 .  15 MET HB3  H   1.9000 . . 
       178 .  15 MET HG2  H   2.5900 . . 
       179 .  15 MET HG3  H   2.5900 . . 
       180 .  15 MET HE   H   1.8000 . . 
       181 .  15 MET CA   C  54.7300 . . 
       182 .  15 MET CB   C  34.3200 . . 
       183 .  15 MET CG   C  32.1900 . . 
       184 .  15 MET CE   C  16.2000 . . 
       185 .  15 MET N    N 127.0900 . . 
       186 .  16 LYS H    H   8.6700 . . 
       187 .  16 LYS HA   H   4.1500 . . 
       188 .  16 LYS HB2  H   1.8500 . . 
       189 .  16 LYS HB3  H   1.9200 . . 
       190 .  16 LYS HG2  H   1.4400 . . 
       191 .  16 LYS HG3  H   1.5500 . . 
       192 .  16 LYS HD2  H   1.6700 . . 
       193 .  16 LYS HD3  H   1.7600 . . 
       194 .  16 LYS HE2  H   3.0100 . . 
       195 .  16 LYS HE3  H   3.0100 . . 
       196 .  16 LYS CA   C  57.9300 . . 
       197 .  16 LYS CB   C  32.2700 . . 
       198 .  16 LYS CG   C  24.6700 . . 
       199 .  16 LYS CD   C  29.1700 . . 
       200 .  16 LYS CE   C  42.3900 . . 
       201 .  16 LYS N    N 125.2800 . . 
       202 .  17 GLY H    H   8.9300 . . 
       203 .  17 GLY HA2  H   3.7800 . . 
       204 .  17 GLY HA3  H   4.1700 . . 
       205 .  17 GLY CA   C  45.4700 . . 
       206 .  17 GLY N    N 113.4100 . . 
       207 .  18 LYS H    H   7.7100 . . 
       208 .  18 LYS HA   H   4.6400 . . 
       209 .  18 LYS HB2  H   1.9000 . . 
       210 .  18 LYS HB3  H   1.7400 . . 
       211 .  18 LYS HG2  H   1.3600 . . 
       212 .  18 LYS HG3  H   1.4300 . . 
       213 .  18 LYS HD2  H   1.6700 . . 
       214 .  18 LYS HD3  H   1.7200 . . 
       215 .  18 LYS HE2  H   2.9900 . . 
       216 .  18 LYS HE3  H   2.9900 . . 
       217 .  18 LYS CA   C  54.6000 . . 
       218 .  18 LYS CB   C  34.9000 . . 
       219 .  18 LYS CG   C  24.6900 . . 
       220 .  18 LYS CD   C  28.8100 . . 
       221 .  18 LYS CE   C  42.4500 . . 
       222 .  18 LYS N    N 118.9200 . . 
       223 .  19 ASN HA   H   4.7000 . . 
       224 .  19 ASN HB2  H   2.8800 . . 
       225 .  19 ASN HB3  H   2.7600 . . 
       226 .  19 ASN HD21 H   6.9300 . . 
       227 .  19 ASN HD22 H   7.6400 . . 
       228 .  19 ASN CA   C  53.2400 . . 
       229 .  19 ASN CB   C  37.9700 . . 
       230 .  19 ASN ND2  N 113.2300 . . 
       231 .  20 LYS H    H   7.4700 . . 
       232 .  20 LYS HA   H   4.4800 . . 
       233 .  20 LYS HB2  H   1.7000 . . 
       234 .  20 LYS HB3  H   1.7600 . . 
       235 .  20 LYS HG2  H   1.4000 . . 
       236 .  20 LYS HG3  H   1.4000 . . 
       237 .  20 LYS HD2  H   1.7000 . . 
       238 .  20 LYS HD3  H   1.7000 . . 
       239 .  20 LYS HE2  H   2.9900 . . 
       240 .  20 LYS HE3  H   2.9900 . . 
       241 .  20 LYS CA   C  55.3700 . . 
       242 .  20 LYS CB   C  34.6900 . . 
       243 .  20 LYS CG   C  24.5800 . . 
       244 .  20 LYS CD   C  29.0200 . . 
       245 .  20 LYS CE   C  42.2800 . . 
       246 .  20 LYS N    N 119.6500 . . 
       247 .  21 LEU H    H   8.4800 . . 
       248 .  21 LEU HA   H   4.9600 . . 
       249 .  21 LEU HB2  H   1.6800 . . 
       250 .  21 LEU HB3  H   1.6800 . . 
       251 .  21 LEU HG   H   1.2200 . . 
       252 .  21 LEU HD1  H   0.8600 . . 
       253 .  21 LEU HD2  H   0.7100 . . 
       254 .  21 LEU CA   C  54.0300 . . 
       255 .  21 LEU CB   C  43.6700 . . 
       256 .  21 LEU CG   C  27.0200 . . 
       257 .  21 LEU CD1  C  25.7200 . . 
       258 .  21 LEU CD2  C  23.3800 . . 
       259 .  21 LEU N    N 124.3400 . . 
       260 .  22 VAL H    H   9.2900 . . 
       261 .  22 VAL HA   H   4.7800 . . 
       262 .  22 VAL HB   H   2.1800 . . 
       263 .  22 VAL HG1  H   1.0100 . . 
       264 .  22 VAL HG2  H   1.0100 . . 
       265 .  22 VAL CA   C  58.5000 . . 
       266 .  22 VAL CB   C  34.8300 . . 
       267 .  22 VAL CG1  C  19.4600 . . 
       268 .  22 VAL CG2  C  20.7100 . . 
       269 .  22 VAL N    N 122.0900 . . 
       270 .  23 PRO HA   H   5.0800 . . 
       271 .  23 PRO HB2  H   2.2500 . . 
       272 .  23 PRO HB3  H   1.9400 . . 
       273 .  23 PRO HG2  H   1.9200 . . 
       274 .  23 PRO HG3  H   2.2400 . . 
       275 .  23 PRO HD2  H   3.8700 . . 
       276 .  23 PRO HD3  H   3.9300 . . 
       277 .  23 PRO CA   C  62.3300 . . 
       278 .  23 PRO CB   C  32.4900 . . 
       279 .  23 PRO CG   C  27.8900 . . 
       280 .  23 PRO CD   C  50.9500 . . 
       281 .  24 ARG H    H   9.1500 . . 
       282 .  24 ARG HA   H   4.4900 . . 
       283 .  24 ARG HB2  H   1.7000 . . 
       284 .  24 ARG HB3  H   1.7800 . . 
       285 .  24 ARG HG2  H   1.6200 . . 
       286 .  24 ARG HG3  H   1.7700 . . 
       287 .  24 ARG HD2  H   2.9000 . . 
       288 .  24 ARG HD3  H   3.6600 . . 
       289 .  24 ARG HE   H   7.2000 . . 
       290 .  24 ARG CA   C  53.7500 . . 
       291 .  24 ARG CB   C  34.3200 . . 
       292 .  24 ARG CG   C  25.7000 . . 
       293 .  24 ARG CD   C  42.5500 . . 
       294 .  24 ARG N    N 123.5800 . . 
       295 .  24 ARG NE   N  85.1300 . . 
       296 .  25 LEU H    H   8.3600 . . 
       297 .  25 LEU HA   H   5.3200 . . 
       298 .  25 LEU HB2  H   1.0900 . . 
       299 .  25 LEU HB3  H   1.6000 . . 
       300 .  25 LEU HG   H   1.3300 . . 
       301 .  25 LEU HD1  H   0.3700 . . 
       302 .  25 LEU HD2  H   0.6900 . . 
       303 .  25 LEU CA   C  53.7500 . . 
       304 .  25 LEU CB   C  43.5700 . . 
       305 .  25 LEU CG   C  26.9900 . . 
       306 .  25 LEU CD1  C  25.4000 . . 
       307 .  25 LEU CD2  C  23.1200 . . 
       308 .  25 LEU N    N 121.9500 . . 
       309 .  26 LEU H    H   9.7200 . . 
       310 .  26 LEU HA   H   5.5700 . . 
       311 .  26 LEU HB2  H   1.5900 . . 
       312 .  26 LEU HB3  H   2.1500 . . 
       313 .  26 LEU HG   H   1.6500 . . 
       314 .  26 LEU HD1  H   0.9400 . . 
       315 .  26 LEU HD2  H   1.2300 . . 
       316 .  26 LEU CA   C  53.3700 . . 
       317 .  26 LEU CB   C  45.4900 . . 
       318 .  26 LEU CG   C  27.7700 . . 
       319 .  26 LEU CD1  C  26.4200 . . 
       320 .  26 LEU CD2  C  24.8500 . . 
       321 .  26 LEU N    N 127.2000 . . 
       322 .  27 GLY H    H   9.8100 . . 
       323 .  27 GLY HA2  H   2.8800 . . 
       324 .  27 GLY HA3  H   5.2500 . . 
       325 .  27 GLY CA   C  44.5700 . . 
       326 .  27 GLY N    N 113.6700 . . 
       327 .  28 ILE H    H   8.8500 . . 
       328 .  28 ILE HA   H   5.0300 . . 
       329 .  28 ILE HB   H   1.9600 . . 
       330 .  28 ILE HG12 H   1.3900 . . 
       331 .  28 ILE HG13 H   1.5300 . . 
       332 .  28 ILE HG2  H   1.0500 . . 
       333 .  28 ILE HD1  H   0.8300 . . 
       334 .  28 ILE CA   C  60.0700 . . 
       335 .  28 ILE CB   C  40.1400 . . 
       336 .  28 ILE CG1  C  28.0800 . . 
       337 .  28 ILE CG2  C  18.6900 . . 
       338 .  28 ILE CD1  C  13.9300 . . 
       339 .  28 ILE N    N 123.6000 . . 
       340 .  29 THR H    H   9.2300 . . 
       341 .  29 THR HA   H   4.8600 . . 
       342 .  29 THR HB   H   4.5900 . . 
       343 .  29 THR HG2  H   1.0800 . . 
       344 .  29 THR CA   C  58.3200 . . 
       345 .  29 THR CB   C  71.8200 . . 
       346 .  29 THR CG2  C  22.4100 . . 
       347 .  29 THR N    N 121.6600 . . 
       348 .  30 LYS H    H   7.8700 . . 
       349 .  30 LYS HA   H   4.2200 . . 
       350 .  30 LYS HB2  H   1.7000 . . 
       351 .  30 LYS HB3  H   1.7000 . . 
       352 .  30 LYS HG2  H   1.3600 . . 
       353 .  30 LYS HG3  H   1.5700 . . 
       354 .  30 LYS HD2  H   0.0300 . . 
       355 .  30 LYS HD3  H   0.9600 . . 
       356 .  30 LYS HE2  H   2.9700 . . 
       357 .  30 LYS HE3  H   2.9700 . . 
       358 .  30 LYS CA   C  57.3700 . . 
       359 .  30 LYS CB   C  32.1200 . . 
       360 .  30 LYS CG   C  24.6400 . . 
       361 .  30 LYS CD   C  28.4900 . . 
       362 .  30 LYS CE   C  42.1800 . . 
       363 .  30 LYS N    N 112.1900 . . 
       364 .  31 GLU H    H   7.9100 . . 
       365 .  31 GLU HA   H   4.5700 . . 
       366 .  31 GLU HB2  H   1.8200 . . 
       367 .  31 GLU HB3  H   1.8200 . . 
       368 .  31 GLU HG2  H   2.1500 . . 
       369 .  31 GLU HG3  H   2.1500 . . 
       370 .  31 GLU CA   C  56.6500 . . 
       371 .  31 GLU CB   C  33.2400 . . 
       372 .  31 GLU CG   C  36.4100 . . 
       373 .  31 GLU N    N 112.9500 . . 
       374 .  32 CYS H    H   8.1800 . . 
       375 .  32 CYS HA   H   5.4400 . . 
       376 .  32 CYS HB2  H   2.9600 . . 
       377 .  32 CYS HB3  H   2.7800 . . 
       378 .  32 CYS CA   C  56.7600 . . 
       379 .  32 CYS CB   C  32.4400 . . 
       380 .  32 CYS N    N 119.1100 . . 
       381 .  33 VAL H    H   8.9000 . . 
       382 .  33 VAL HA   H   5.1200 . . 
       383 .  33 VAL HB   H   2.2000 . . 
       384 .  33 VAL HG1  H   1.1800 . . 
       385 .  33 VAL HG2  H   1.1100 . . 
       386 .  33 VAL CA   C  60.5500 . . 
       387 .  33 VAL CB   C  34.6700 . . 
       388 .  33 VAL CG1  C  21.9000 . . 
       389 .  33 VAL CG2  C  22.1100 . . 
       390 .  33 VAL N    N 117.8500 . . 
       391 .  34 MET H    H   9.8100 . . 
       392 .  34 MET HA   H   5.3600 . . 
       393 .  34 MET HB2  H   1.8400 . . 
       394 .  34 MET HB3  H   1.8400 . . 
       395 .  34 MET HG2  H   2.4400 . . 
       396 .  34 MET HG3  H   2.4400 . . 
       397 .  34 MET HE   H   2.0400 . . 
       398 .  34 MET CA   C  54.1100 . . 
       399 .  34 MET CB   C  37.3800 . . 
       400 .  34 MET CG   C  31.3500 . . 
       401 .  34 MET CE   C  16.8900 . . 
       402 .  34 MET N    N 122.9300 . . 
       403 .  35 ARG H    H   8.8000 . . 
       404 .  35 ARG HA   H   4.9900 . . 
       405 .  35 ARG HB2  H   1.5100 . . 
       406 .  35 ARG HB3  H   1.6900 . . 
       407 .  35 ARG HG2  H   1.6900 . . 
       408 .  35 ARG HG3  H   1.6900 . . 
       409 .  35 ARG HD2  H   3.0600 . . 
       410 .  35 ARG HD3  H   3.0600 . . 
       411 .  35 ARG HE   H   8.8400 . . 
       412 .  35 ARG CA   C  55.3200 . . 
       413 .  35 ARG CB   C  33.1500 . . 
       414 .  35 ARG CG   C  27.0500 . . 
       415 .  35 ARG CD   C  44.5900 . . 
       416 .  35 ARG N    N 123.2100 . . 
       417 .  35 ARG NE   N  85.4200 . . 
       418 .  36 VAL H    H   9.4200 . . 
       419 .  36 VAL HA   H   4.8200 . . 
       420 .  36 VAL HB   H   2.0100 . . 
       421 .  36 VAL HG1  H   0.6500 . . 
       422 .  36 VAL HG2  H   0.9800 . . 
       423 .  36 VAL CA   C  60.5400 . . 
       424 .  36 VAL CB   C  35.3200 . . 
       425 .  36 VAL CG1  C  20.4000 . . 
       426 .  36 VAL CG2  C  22.7300 . . 
       427 .  36 VAL N    N 126.5300 . . 
       428 .  37 ASP H    H   8.7100 . . 
       429 .  37 ASP HA   H   4.5500 . . 
       430 .  37 ASP HB2  H   2.4600 . . 
       431 .  37 ASP HB3  H   3.0700 . . 
       432 .  37 ASP CA   C  55.0200 . . 
       433 .  37 ASP CB   C  43.6100 . . 
       434 .  37 ASP N    N 128.0700 . . 
       435 .  38 GLU H    H   9.2200 . . 
       436 .  38 GLU HA   H   3.7500 . . 
       437 .  38 GLU HB2  H   1.8200 . . 
       438 .  38 GLU HB3  H   1.9100 . . 
       439 .  38 GLU HG2  H   2.1500 . . 
       440 .  38 GLU HG3  H   2.1500 . . 
       441 .  38 GLU CA   C  58.8600 . . 
       442 .  38 GLU CB   C  29.3600 . . 
       443 .  38 GLU CG   C  34.9400 . . 
       444 .  38 GLU N    N 128.8300 . . 
       445 .  39 LYS H    H   8.4900 . . 
       446 .  39 LYS HA   H   4.2700 . . 
       447 .  39 LYS HB2  H   1.9000 . . 
       448 .  39 LYS HB3  H   1.9900 . . 
       449 .  39 LYS HG2  H   1.3400 . . 
       450 .  39 LYS HG3  H   1.4800 . . 
       451 .  39 LYS HD2  H   1.6900 . . 
       452 .  39 LYS HD3  H   1.6900 . . 
       453 .  39 LYS HE2  H   2.9800 . . 
       454 .  39 LYS HE3  H   2.9800 . . 
       455 .  39 LYS CA   C  57.7800 . . 
       456 .  39 LYS CB   C  33.1300 . . 
       457 .  39 LYS CG   C  24.8400 . . 
       458 .  39 LYS CD   C  28.6500 . . 
       459 .  39 LYS CE   C  42.1800 . . 
       460 .  39 LYS N    N 118.0600 . . 
       461 .  40 THR H    H   8.4400 . . 
       462 .  40 THR HA   H   4.2300 . . 
       463 .  40 THR HB   H   4.3400 . . 
       464 .  40 THR HG2  H   1.1600 . . 
       465 .  40 THR CA   C  61.8700 . . 
       466 .  40 THR CB   C  70.1000 . . 
       467 .  40 THR CG2  C  21.2400 . . 
       468 .  40 THR N    N 109.0300 . . 
       469 .  41 LYS H    H   7.9500 . . 
       470 .  41 LYS HA   H   3.8100 . . 
       471 .  41 LYS HB2  H   1.1700 . . 
       472 .  41 LYS HB3  H   1.3500 . . 
       473 .  41 LYS HG2  H   0.9900 . . 
       474 .  41 LYS HG3  H   0.9900 . . 
       475 .  41 LYS HD2  H   0.0300 . . 
       476 .  41 LYS HD3  H   0.9600 . . 
       477 .  41 LYS HE2  H   2.6500 . . 
       478 .  41 LYS HE3  H   2.6500 . . 
       479 .  41 LYS CA   C  57.0100 . . 
       480 .  41 LYS CB   C  28.3900 . . 
       481 .  41 LYS CG   C  25.3700 . . 
       482 .  41 LYS CD   C  28.4900 . . 
       483 .  41 LYS CE   C  42.3700 . . 
       484 .  41 LYS N    N 115.2800 . . 
       485 .  42 GLU H    H   7.5900 . . 
       486 .  42 GLU HA   H   4.1500 . . 
       487 .  42 GLU HB2  H   1.8100 . . 
       488 .  42 GLU HB3  H   1.8100 . . 
       489 .  42 GLU HG2  H   2.1800 . . 
       490 .  42 GLU HG3  H   2.0400 . . 
       491 .  42 GLU CA   C  56.1500 . . 
       492 .  42 GLU CB   C  30.9000 . . 
       493 .  42 GLU CG   C  36.1900 . . 
       494 .  42 GLU N    N 118.6300 . . 
       495 .  43 VAL H    H   8.8100 . . 
       496 .  43 VAL HA   H   3.9000 . . 
       497 .  43 VAL HB   H   2.0200 . . 
       498 .  43 VAL HG1  H   0.7500 . . 
       499 .  43 VAL HG2  H   1.0400 . . 
       500 .  43 VAL CA   C  63.5500 . . 
       501 .  43 VAL CB   C  31.6200 . . 
       502 .  43 VAL CG1  C  21.5100 . . 
       503 .  43 VAL CG2  C  21.8400 . . 
       504 .  43 VAL N    N 125.3200 . . 
       505 .  44 ILE H    H   9.0300 . . 
       506 .  44 ILE HA   H   3.9600 . . 
       507 .  44 ILE HB   H   1.5000 . . 
       508 .  44 ILE HG12 H  -0.2800 . . 
       509 .  44 ILE HG13 H   0.9900 . . 
       510 .  44 ILE HG2  H   0.8500 . . 
       511 .  44 ILE HD1  H   0.7700 . . 
       512 .  44 ILE CA   C  62.5600 . . 
       513 .  44 ILE CB   C  39.2900 . . 
       514 .  44 ILE CG1  C  26.2800 . . 
       515 .  44 ILE CG2  C  17.0700 . . 
       516 .  44 ILE CD1  C  13.4600 . . 
       517 .  44 ILE N    N 129.5000 . . 
       518 .  45 GLN H    H   7.4300 . . 
       519 .  45 GLN HA   H   4.1300 . . 
       520 .  45 GLN HB2  H   0.9800 . . 
       521 .  45 GLN HB3  H   0.9800 . . 
       522 .  45 GLN HG2  H   1.6400 . . 
       523 .  45 GLN HG3  H   0.7700 . . 
       524 .  45 GLN HE21 H   6.6600 . . 
       525 .  45 GLN HE22 H   7.0500 . . 
       526 .  45 GLN CA   C  55.2100 . . 
       527 .  45 GLN CB   C  32.1700 . . 
       528 .  45 GLN CG   C  32.6400 . . 
       529 .  45 GLN N    N 118.0400 . . 
       530 .  45 GLN NE2  N 110.9600 . . 
       531 .  46 GLU H    H   8.1300 . . 
       532 .  46 GLU HA   H   4.9600 . . 
       533 .  46 GLU HB2  H   1.7500 . . 
       534 .  46 GLU HB3  H   1.7500 . . 
       535 .  46 GLU HG2  H   1.9200 . . 
       536 .  46 GLU HG3  H   1.9200 . . 
       537 .  46 GLU CA   C  54.3100 . . 
       538 .  46 GLU CB   C  33.8800 . . 
       539 .  46 GLU CG   C  35.8500 . . 
       540 .  46 GLU N    N 122.9800 . . 
       541 .  47 TRP H    H   9.3200 . . 
       542 .  47 TRP HA   H   4.8500 . . 
       543 .  47 TRP HB2  H   2.7500 . . 
       544 .  47 TRP HB3  H   2.7500 . . 
       545 .  47 TRP HD1  H   6.3400 . . 
       546 .  47 TRP HE1  H   9.0500 . . 
       547 .  47 TRP HE3  H   7.3800 . . 
       548 .  47 TRP HZ2  H   6.9100 . . 
       549 .  47 TRP HZ3  H   7.0300 . . 
       550 .  47 TRP HH2  H   7.0820 . . 
       551 .  47 TRP CA   C  56.8300 . . 
       552 .  47 TRP CB   C  33.0800 . . 
       553 .  47 TRP CD1  C 126.5500 . . 
       554 .  47 TRP CE3  C 121.4200 . . 
       555 .  47 TRP CZ2  C 114.9100 . . 
       556 .  47 TRP CZ3  C 121.7600 . . 
       557 .  47 TRP CH2  C 124.6900 . . 
       558 .  47 TRP N    N 122.3000 . . 
       559 .  47 TRP NE1  N 129.1200 . . 
       560 .  48 SER H    H   8.7100 . . 
       561 .  48 SER HA   H   4.7300 . . 
       562 .  48 SER HB2  H   3.8900 . . 
       563 .  48 SER HB3  H   4.0100 . . 
       564 .  48 SER CA   C  57.9900 . . 
       565 .  48 SER CB   C  63.1300 . . 
       566 .  48 SER N    N 117.5600 . . 
       567 .  49 LEU H    H   8.3900 . . 
       568 .  49 LEU HA   H   4.1000 . . 
       569 .  49 LEU HB2  H   1.6200 . . 
       570 .  49 LEU HB3  H   1.6200 . . 
       571 .  49 LEU HG   H   1.3500 . . 
       572 .  49 LEU HD1  H   0.8600 . . 
       573 .  49 LEU HD2  H   0.3700 . . 
       574 .  49 LEU CA   C  57.9000 . . 
       575 .  49 LEU CB   C  41.6000 . . 
       576 .  49 LEU CG   C  26.7900 . . 
       577 .  49 LEU CD1  C  23.7200 . . 
       578 .  49 LEU CD2  C  21.6700 . . 
       579 .  49 LEU N    N 126.0900 . . 
       580 .  50 THR H    H   7.9700 . . 
       581 .  50 THR HA   H   4.0200 . . 
       582 .  50 THR HB   H   4.4300 . . 
       583 .  50 THR HG2  H   1.3000 . . 
       584 .  50 THR CA   C  63.8600 . . 
       585 .  50 THR CB   C  68.2200 . . 
       586 .  50 THR CG2  C  21.8700 . . 
       587 .  50 THR N    N 106.9800 . . 
       588 .  51 ASN H    H   7.8700 . . 
       589 .  51 ASN HA   H   4.9000 . . 
       590 .  51 ASN HB2  H   3.0100 . . 
       591 .  51 ASN HB3  H   2.7700 . . 
       592 .  51 ASN HD21 H   6.8500 . . 
       593 .  51 ASN HD22 H   7.6400 . . 
       594 .  51 ASN CA   C  53.4600 . . 
       595 .  51 ASN CB   C  39.4600 . . 
       596 .  51 ASN N    N 118.9400 . . 
       597 .  51 ASN ND2  N 112.4800 . . 
       598 .  52 ILE H    H   7.1200 . . 
       599 .  52 ILE HA   H   3.6600 . . 
       600 .  52 ILE HB   H   1.9700 . . 
       601 .  52 ILE HG12 H   1.9800 . . 
       602 .  52 ILE HG13 H   1.9800 . . 
       603 .  52 ILE HG2  H   0.9200 . . 
       604 .  52 ILE HD1  H   0.8000 . . 
       605 .  52 ILE CA   C  62.9900 . . 
       606 .  52 ILE CB   C  39.4200 . . 
       607 .  52 ILE CG1  C  27.2100 . . 
       608 .  52 ILE CG2  C  18.5400 . . 
       609 .  52 ILE CD1  C  13.8900 . . 
       610 .  52 ILE N    N 117.8600 . . 
       611 .  53 LYS H    H   9.2900 . . 
       612 .  53 LYS HA   H   4.2800 . . 
       613 .  53 LYS HB2  H   0.9900 . . 
       614 .  53 LYS HB3  H   1.4500 . . 
       615 .  53 LYS HG2  H   1.3500 . . 
       616 .  53 LYS HG3  H   1.4700 . . 
       617 .  53 LYS HD2  H   1.6700 . . 
       618 .  53 LYS HD3  H   1.6700 . . 
       619 .  53 LYS HE2  H   2.9900 . . 
       620 .  53 LYS HE3  H   2.9900 . . 
       621 .  53 LYS CA   C  57.7600 . . 
       622 .  53 LYS CB   C  34.0100 . . 
       623 .  53 LYS CG   C  24.6400 . . 
       624 .  53 LYS CD   C  28.9200 . . 
       625 .  53 LYS CE   C  42.1900 . . 
       626 .  53 LYS N    N 129.6600 . . 
       627 .  54 ARG H    H   7.8500 . . 
       628 .  54 ARG HA   H   4.8100 . . 
       629 .  54 ARG HB2  H   0.7800 . . 
       630 .  54 ARG HB3  H   1.0600 . . 
       631 .  54 ARG HG2  H   1.6200 . . 
       632 .  54 ARG HG3  H   1.7700 . . 
       633 .  54 ARG HD2  H   3.2600 . . 
       634 .  54 ARG HD3  H   3.3400 . . 
       635 .  54 ARG HE   H   7.4700 . . 
       636 .  54 ARG CA   C  54.0900 . . 
       637 .  54 ARG CB   C  32.1600 . . 
       638 .  54 ARG CG   C  25.3500 . . 
       639 .  54 ARG CD   C  42.8000 . . 
       640 .  54 ARG N    N 113.4100 . . 
       641 .  54 ARG NE   N  84.6200 . . 
       642 .  55 TRP H    H   8.7600 . . 
       643 .  55 TRP HA   H   5.5800 . . 
       644 .  55 TRP HB2  H   3.0100 . . 
       645 .  55 TRP HB3  H   3.2200 . . 
       646 .  55 TRP HD1  H   6.8700 . . 
       647 .  55 TRP HE1  H  10.3900 . . 
       648 .  55 TRP HE3  H   7.3800 . . 
       649 .  55 TRP HZ2  H   7.4000 . . 
       650 .  55 TRP HZ3  H   7.0300 . . 
       651 .  55 TRP HH2  H   6.9600 . . 
       652 .  55 TRP CA   C  56.0300 . . 
       653 .  55 TRP CB   C  32.5500 . . 
       654 .  55 TRP CD1  C 126.5500 . . 
       655 .  55 TRP CE3  C 121.4200 . . 
       656 .  55 TRP CZ2  C 114.9100 . . 
       657 .  55 TRP CZ3  C 121.7600 . . 
       658 .  55 TRP CH2  C 124.6900 . . 
       659 .  55 TRP N    N 117.6700 . . 
       660 .  55 TRP NE1  N 130.0200 . . 
       661 .  56 ALA H    H   8.4000 . . 
       662 .  56 ALA HA   H   4.6300 . . 
       663 .  56 ALA HB   H   0.2000 . . 
       664 .  56 ALA CA   C  51.1900 . . 
       665 .  56 ALA CB   C  21.5000 . . 
       666 .  56 ALA N    N 119.8300 . . 
       667 .  57 ALA H    H   9.2100 . . 
       668 .  57 ALA HA   H   5.1300 . . 
       669 .  57 ALA HB   H   1.4000 . . 
       670 .  57 ALA CA   C  50.6600 . . 
       671 .  57 ALA CB   C  21.3200 . . 
       672 .  57 ALA N    N 127.0600 . . 
       673 .  58 SER H    H   8.9400 . . 
       674 .  58 SER HA   H   5.0600 . . 
       675 .  58 SER HB2  H   3.6900 . . 
       676 .  58 SER HB3  H   4.2800 . . 
       677 .  58 SER CA   C  56.6800 . . 
       678 .  58 SER CB   C  65.1000 . . 
       679 .  58 SER N    N 121.8100 . . 
       680 .  59 PRO HA   H   4.5500 . . 
       681 .  59 PRO HB2  H   1.8400 . . 
       682 .  59 PRO HB3  H   1.8400 . . 
       683 .  59 PRO HG2  H   1.9900 . . 
       684 .  59 PRO HG3  H   2.1300 . . 
       685 .  59 PRO HD2  H   3.7300 . . 
       686 .  59 PRO HD3  H   3.9000 . . 
       687 .  59 PRO CA   C  65.1300 . . 
       688 .  59 PRO CB   C  32.3200 . . 
       689 .  59 PRO CG   C  27.8900 . . 
       690 .  59 PRO CD   C  50.1000 . . 
       691 .  60 LYS H    H   7.7700 . . 
       692 .  60 LYS HA   H   4.8000 . . 
       693 .  60 LYS HB2  H   1.9500 . . 
       694 .  60 LYS HB3  H   1.9500 . . 
       695 .  60 LYS HG2  H   1.3000 . . 
       696 .  60 LYS HG3  H   1.3000 . . 
       697 .  60 LYS HD2  H   1.6200 . . 
       698 .  60 LYS HD3  H   1.6600 . . 
       699 .  60 LYS HE2  H   2.9300 . . 
       700 .  60 LYS HE3  H   2.9300 . . 
       701 .  60 LYS CA   C  54.8700 . . 
       702 .  60 LYS CB   C  35.2900 . . 
       703 .  60 LYS CG   C  24.6000 . . 
       704 .  60 LYS CD   C  29.0400 . . 
       705 .  60 LYS CE   C  42.2000 . . 
       706 .  60 LYS N    N 111.4700 . . 
       707 .  61 SER H    H   7.7100 . . 
       708 .  61 SER HA   H   5.5400 . . 
       709 .  61 SER HB2  H   3.6400 . . 
       710 .  61 SER HB3  H   3.7100 . . 
       711 .  61 SER CA   C  57.4800 . . 
       712 .  61 SER CB   C  67.5000 . . 
       713 .  61 SER N    N 114.9300 . . 
       714 .  62 PHE H    H   8.6400 . . 
       715 .  62 PHE HA   H   5.0900 . . 
       716 .  62 PHE HB2  H   2.5000 . . 
       717 .  62 PHE HB3  H   2.8100 . . 
       718 .  62 PHE HD1  H   6.9300 . . 
       719 .  62 PHE HD2  H   6.7500 . . 
       720 .  62 PHE HE1  H   7.1700 . . 
       721 .  62 PHE HE2  H   7.1700 . . 
       722 .  62 PHE HZ   H   7.2700 . . 
       723 .  62 PHE CA   C  57.9000 . . 
       724 .  62 PHE CB   C  43.3900 . . 
       725 .  62 PHE CD1  C 131.3200 . . 
       726 .  62 PHE CD2  C 131.3200 . . 
       727 .  62 PHE CE1  C 129.4800 . . 
       728 .  62 PHE CE2  C 129.4800 . . 
       729 .  62 PHE CZ   C 130.9500 . . 
       730 .  62 PHE N    N 119.6000 . . 
       731 .  63 THR H    H   7.8900 . . 
       732 .  63 THR HA   H   5.0200 . . 
       733 .  63 THR HB   H   3.3000 . . 
       734 .  63 THR HG2  H   0.9700 . . 
       735 .  63 THR CA   C  61.3700 . . 
       736 .  63 THR CB   C  71.1200 . . 
       737 .  63 THR CG2  C  21.6400 . . 
       738 .  63 THR N    N 123.0300 . . 
       739 .  64 LEU H    H   9.1100 . . 
       740 .  64 LEU HA   H   4.3500 . . 
       741 .  64 LEU HB2  H   0.4600 . . 
       742 .  64 LEU HB3  H   1.4600 . . 
       743 .  64 LEU HG   H   0.9100 . . 
       744 .  64 LEU HD1  H   0.0500 . . 
       745 .  64 LEU HD2  H   0.3700 . . 
       746 .  64 LEU CA   C  53.6200 . . 
       747 .  64 LEU CB   C  46.3100 . . 
       748 .  64 LEU CG   C  24.7900 . . 
       749 .  64 LEU CD1  C  24.6200 . . 
       750 .  64 LEU CD2  C  21.6700 . . 
       751 .  64 LEU N    N 125.3200 . . 
       752 .  65 ASP H    H   7.9400 . . 
       753 .  65 ASP HA   H   4.8300 . . 
       754 .  65 ASP HB2  H   1.6600 . . 
       755 .  65 ASP HB3  H   2.3100 . . 
       756 .  65 ASP CA   C  51.8700 . . 
       757 .  65 ASP CB   C  42.9600 . . 
       758 .  65 ASP N    N 119.9300 . . 
       759 .  66 PHE H    H   9.2600 . . 
       760 .  66 PHE HA   H   4.9400 . . 
       761 .  66 PHE HB2  H   2.7300 . . 
       762 .  66 PHE HB3  H   3.5400 . . 
       763 .  66 PHE HD1  H   6.7000 . . 
       764 .  66 PHE HD2  H   6.7000 . . 
       765 .  66 PHE HE1  H   6.2300 . . 
       766 .  66 PHE HE2  H   6.2300 . . 
       767 .  66 PHE HZ   H   7.0900 . . 
       768 .  66 PHE CA   C  57.3200 . . 
       769 .  66 PHE CB   C  39.1600 . . 
       770 .  66 PHE CD1  C 129.6700 . . 
       771 .  66 PHE CD2  C 129.6700 . . 
       772 .  66 PHE CE1  C 129.6700 . . 
       773 .  66 PHE CE2  C 129.6700 . . 
       774 .  66 PHE CZ   C 130.9500 . . 
       775 .  66 PHE N    N 126.3800 . . 
       776 .  67 GLY H    H   9.2800 . . 
       777 .  67 GLY HA2  H   3.6900 . . 
       778 .  67 GLY HA3  H   3.9300 . . 
       779 .  67 GLY CA   C  46.6800 . . 
       780 .  67 GLY N    N 111.5000 . . 
       781 .  68 ASP H    H   8.6700 . . 
       782 .  68 ASP HA   H   4.5800 . . 
       783 .  68 ASP HB2  H   2.5300 . . 
       784 .  68 ASP HB3  H   2.7100 . . 
       785 .  68 ASP CA   C  54.5400 . . 
       786 .  68 ASP CB   C  40.6000 . . 
       787 .  68 ASP N    N 123.4400 . . 
       788 .  69 TYR H    H   8.2500 . . 
       789 .  69 TYR HA   H   4.2900 . . 
       790 .  69 TYR HB2  H   3.2700 . . 
       791 .  69 TYR HB3  H   3.2700 . . 
       792 .  69 TYR HD1  H   7.2900 . . 
       793 .  69 TYR HD2  H   7.2900 . . 
       794 .  69 TYR HE1  H   6.8800 . . 
       795 .  69 TYR HE2  H   6.8800 . . 
       796 .  69 TYR CA   C  59.9700 . . 
       797 .  69 TYR CB   C  38.6100 . . 
       798 .  69 TYR CD1  C 132.7800 . . 
       799 .  69 TYR CD2  C 132.7800 . . 
       800 .  69 TYR CE1  C 118.2100 . . 
       801 .  69 TYR CE2  C 118.2100 . . 
       802 .  69 TYR N    N 120.0900 . . 
       803 .  70 GLN H    H   7.7200 . . 
       804 .  70 GLN HA   H   4.4200 . . 
       805 .  70 GLN HB2  H   2.0900 . . 
       806 .  70 GLN HB3  H   2.2200 . . 
       807 .  70 GLN HG2  H   2.3600 . . 
       808 .  70 GLN HG3  H   2.3600 . . 
       809 .  70 GLN HE21 H   6.8500 . . 
       810 .  70 GLN HE22 H   7.7100 . . 
       811 .  70 GLN CA   C  55.6500 . . 
       812 .  70 GLN CB   C  31.1300 . . 
       813 .  70 GLN CG   C  33.4200 . . 
       814 .  70 GLN N    N 116.3600 . . 
       815 .  70 GLN NE2  N 114.4100 . . 
       816 .  71 ASP H    H   8.3800 . . 
       817 .  71 ASP HA   H   4.6700 . . 
       818 .  71 ASP HB2  H   2.6100 . . 
       819 .  71 ASP HB3  H   2.7700 . . 
       820 .  71 ASP CA   C  54.3600 . . 
       821 .  71 ASP CB   C  40.8100 . . 
       822 .  71 ASP N    N 121.5000 . . 
       823 .  72 GLY H    H   8.2400 . . 
       824 .  72 GLY HA2  H   3.7300 . . 
       825 .  72 GLY HA3  H   4.1800 . . 
       826 .  72 GLY CA   C  44.6900 . . 
       827 .  72 GLY N    N 112.2100 . . 
       828 .  73 TYR H    H   8.1700 . . 
       829 .  73 TYR HA   H   5.2000 . . 
       830 .  73 TYR HB2  H   3.1400 . . 
       831 .  73 TYR HB3  H   2.8400 . . 
       832 .  73 TYR HD1  H   7.0900 . . 
       833 .  73 TYR HD2  H   7.0900 . . 
       834 .  73 TYR HE1  H   6.8200 . . 
       835 .  73 TYR HE2  H   6.8200 . . 
       836 .  73 TYR CA   C  54.9300 . . 
       837 .  73 TYR CB   C  38.5000 . . 
       838 .  73 TYR CD1  C 131.3100 . . 
       839 .  73 TYR CD2  C 131.3100 . . 
       840 .  73 TYR CE1  C 118.1600 . . 
       841 .  73 TYR CE2  C 118.1600 . . 
       842 .  73 TYR N    N 121.3400 . . 
       843 .  74 TYR H    H   8.8400 . . 
       844 .  74 TYR HA   H   5.1700 . . 
       845 .  74 TYR HB2  H   3.1200 . . 
       846 .  74 TYR HB3  H   2.7800 . . 
       847 .  74 TYR HD1  H   7.1100 . . 
       848 .  74 TYR HD2  H   7.1100 . . 
       849 .  74 TYR HE1  H   6.8100 . . 
       850 .  74 TYR HE2  H   6.8100 . . 
       851 .  74 TYR CA   C  57.0400 . . 
       852 .  74 TYR CB   C  40.4100 . . 
       853 .  74 TYR CD1  C 132.1600 . . 
       854 .  74 TYR CD2  C 132.1600 . . 
       855 .  74 TYR CE1  C 117.9100 . . 
       856 .  74 TYR CE2  C 117.9100 . . 
       857 .  74 TYR N    N 123.4900 . . 
       858 .  75 SER H    H   8.3700 . . 
       859 .  75 SER HA   H   5.3500 . . 
       860 .  75 SER HB2  H   3.5100 . . 
       861 .  75 SER HB3  H   3.7000 . . 
       862 .  75 SER CA   C  56.1200 . . 
       863 .  75 SER CB   C  65.2200 . . 
       864 .  75 SER N    N 122.9200 . . 
       865 .  76 VAL H    H   8.8200 . . 
       866 .  76 VAL HA   H   4.9400 . . 
       867 .  76 VAL HB   H   2.0100 . . 
       868 .  76 VAL HG1  H   0.8700 . . 
       869 .  76 VAL HG2  H   0.7000 . . 
       870 .  76 VAL CA   C  58.1100 . . 
       871 .  76 VAL CB   C  36.0500 . . 
       872 .  76 VAL CG1  C  17.8800 . . 
       873 .  76 VAL CG2  C  23.1500 . . 
       874 .  76 VAL N    N 117.0800 . . 
       875 .  77 GLN H    H   9.1500 . . 
       876 .  77 GLN HA   H   4.8500 . . 
       877 .  77 GLN HB2  H   1.9200 . . 
       878 .  77 GLN HB3  H   2.1700 . . 
       879 .  77 GLN HG2  H   2.4300 . . 
       880 .  77 GLN HG3  H   2.4300 . . 
       881 .  77 GLN HE21 H   6.8500 . . 
       882 .  77 GLN HE22 H   7.7100 . . 
       883 .  77 GLN CA   C  55.0200 . . 
       884 .  77 GLN CB   C  29.7900 . . 
       885 .  77 GLN CG   C  34.0800 . . 
       886 .  77 GLN N    N 121.4000 . . 
       887 .  77 GLN NE2  N 114.4100 . . 
       888 .  78 THR H    H   7.8500 . . 
       889 .  78 THR HA   H   4.8400 . . 
       890 .  78 THR HB   H   4.6800 . . 
       891 .  78 THR HG2  H   0.8400 . . 
       892 .  78 THR CA   C  60.0100 . . 
       893 .  78 THR CB   C  66.9600 . . 
       894 .  78 THR CG2  C  18.5000 . . 
       895 .  78 THR N    N 121.1500 . . 
       896 .  79 THR H    H   8.7100 . . 
       897 .  79 THR HA   H   4.8500 . . 
       898 .  79 THR HB   H   4.7200 . . 
       899 .  79 THR HG2  H   1.3500 . . 
       900 .  79 THR CA   C  62.2900 . . 
       901 .  79 THR CB   C  68.3300 . . 
       902 .  79 THR CG2  C  21.5700 . . 
       903 .  79 THR N    N 118.3500 . . 
       904 .  80 GLU H    H   9.1700 . . 
       905 .  80 GLU HA   H   4.7900 . . 
       906 .  80 GLU HB2  H   1.7100 . . 
       907 .  80 GLU HB3  H   2.4900 . . 
       908 .  80 GLU HG2  H   2.1400 . . 
       909 .  80 GLU HG3  H   2.2700 . . 
       910 .  80 GLU CA   C  55.4500 . . 
       911 .  80 GLU CB   C  30.0700 . . 
       912 .  80 GLU CG   C  37.5600 . . 
       913 .  80 GLU N    N 124.5100 . . 
       914 .  81 GLY H    H   9.3900 . . 
       915 .  81 GLY HA2  H   3.2400 . . 
       916 .  81 GLY HA3  H   3.7800 . . 
       917 .  81 GLY CA   C  47.7300 . . 
       918 .  81 GLY N    N 111.2100 . . 
       919 .  82 GLU H    H   8.7600 . . 
       920 .  82 GLU HA   H   3.9900 . . 
       921 .  82 GLU HB2  H   1.9000 . . 
       922 .  82 GLU HB3  H   1.9000 . . 
       923 .  82 GLU HG2  H   2.1100 . . 
       924 .  82 GLU HG3  H   2.2500 . . 
       925 .  82 GLU CA   C  59.1700 . . 
       926 .  82 GLU CB   C  28.8300 . . 
       927 .  82 GLU CG   C  35.8800 . . 
       928 .  82 GLU N    N 119.5300 . . 
       929 .  83 GLN H    H   7.5100 . . 
       930 .  83 GLN HA   H   3.9500 . . 
       931 .  83 GLN HB2  H   2.0700 . . 
       932 .  83 GLN HB3  H   2.2300 . . 
       933 .  83 GLN HG2  H   2.5600 . . 
       934 .  83 GLN HG3  H   2.3700 . . 
       935 .  83 GLN HE21 H   6.9800 . . 
       936 .  83 GLN HE22 H   7.5800 . . 
       937 .  83 GLN CA   C  59.2700 . . 
       938 .  83 GLN CB   C  28.3200 . . 
       939 .  83 GLN CG   C  34.7600 . . 
       940 .  83 GLN N    N 120.0800 . . 
       941 .  83 GLN NE2  N 112.5000 . . 
       942 .  84 ILE H    H   7.5700 . . 
       943 .  84 ILE HA   H   2.6100 . . 
       944 .  84 ILE HB   H   0.4900 . . 
       945 .  84 ILE HG12 H  -1.2400 . . 
       946 .  84 ILE HG13 H   0.4400 . . 
       947 .  84 ILE HG2  H  -0.4200 . . 
       948 .  84 ILE HD1  H  -0.0300 . . 
       949 .  84 ILE CA   C  65.2300 . . 
       950 .  84 ILE CB   C  37.6800 . . 
       951 .  84 ILE CG1  C  25.9900 . . 
       952 .  84 ILE CG2  C  16.6900 . . 
       953 .  84 ILE CD1  C  13.2000 . . 
       954 .  84 ILE N    N 121.9800 . . 
       955 .  85 ALA H    H   7.9700 . . 
       956 .  85 ALA HA   H   3.2800 . . 
       957 .  85 ALA HB   H   1.5800 . . 
       958 .  85 ALA CA   C  54.8700 . . 
       959 .  85 ALA CB   C  18.6600 . . 
       960 .  85 ALA N    N 119.8100 . . 
       961 .  86 GLN H    H   7.6400 . . 
       962 .  86 GLN HA   H   3.9800 . . 
       963 .  86 GLN HB2  H   2.0100 . . 
       964 .  86 GLN HB3  H   2.0900 . . 
       965 .  86 GLN HG2  H   2.5100 . . 
       966 .  86 GLN HG3  H   2.4000 . . 
       967 .  86 GLN HE21 H   6.7900 . . 
       968 .  86 GLN HE22 H   7.5100 . . 
       969 .  86 GLN CA   C  58.4300 . . 
       970 .  86 GLN CB   C  28.4900 . . 
       971 .  86 GLN CG   C  33.8000 . . 
       972 .  86 GLN N    N 115.8600 . . 
       973 .  86 GLN NE2  N 112.1500 . . 
       974 .  87 LEU H    H   7.4200 . . 
       975 .  87 LEU HA   H   3.7900 . . 
       976 .  87 LEU HB2  H   1.4100 . . 
       977 .  87 LEU HB3  H   1.6200 . . 
       978 .  87 LEU HG   H   0.8000 . . 
       979 .  87 LEU HD1  H   1.3250 . . 
       980 .  87 LEU HD2  H   1.3250 . . 
       981 .  87 LEU CA   C  57.2700 . . 
       982 .  87 LEU CB   C  42.4000 . . 
       983 .  87 LEU CG   C  24.5700 . . 
       984 .  87 LEU CD1  C  25.0000 . . 
       985 .  87 LEU CD2  C  25.0000 . . 
       986 .  87 LEU N    N 122.1800 . . 
       987 .  88 ILE H    H   7.7200 . . 
       988 .  88 ILE HA   H   3.2000 . . 
       989 .  88 ILE HB   H   1.1000 . . 
       990 .  88 ILE HG12 H   0.6700 . . 
       991 .  88 ILE HG13 H   1.4200 . . 
       992 .  88 ILE HG2  H   0.0000 . . 
       993 .  88 ILE HD1  H   0.4800 . . 
       994 .  88 ILE CA   C  65.7900 . . 
       995 .  88 ILE CB   C  37.6900 . . 
       996 .  88 ILE CG1  C  29.4900 . . 
       997 .  88 ILE CG2  C  16.1000 . . 
       998 .  88 ILE CD1  C  13.9200 . . 
       999 .  88 ILE N    N 118.1700 . . 
      1000 .  89 ALA H    H   8.3900 . . 
      1001 .  89 ALA HA   H   3.9000 . . 
      1002 .  89 ALA HB   H   1.6500 . . 
      1003 .  89 ALA CA   C  55.3700 . . 
      1004 .  89 ALA CB   C  18.7400 . . 
      1005 .  89 ALA N    N 120.4600 . . 
      1006 .  90 GLY H    H   7.9300 . . 
      1007 .  90 GLY HA2  H   3.8900 . . 
      1008 .  90 GLY HA3  H   3.9400 . . 
      1009 .  90 GLY CA   C  46.8300 . . 
      1010 .  90 GLY N    N 105.4800 . . 
      1011 .  91 TYR H    H   8.0900 . . 
      1012 .  91 TYR HA   H   4.8100 . . 
      1013 .  91 TYR HB2  H   2.9800 . . 
      1014 .  91 TYR HB3  H   3.0400 . . 
      1015 .  91 TYR HD1  H   6.8400 . . 
      1016 .  91 TYR HD2  H   6.8400 . . 
      1017 .  91 TYR HE1  H   6.5000 . . 
      1018 .  91 TYR HE2  H   6.5000 . . 
      1019 .  91 TYR CA   C  57.9100 . . 
      1020 .  91 TYR CB   C  37.0600 . . 
      1021 .  91 TYR CD1  C 131.4700 . . 
      1022 .  91 TYR CD2  C 131.4700 . . 
      1023 .  91 TYR CE1  C 116.7700 . . 
      1024 .  91 TYR CE2  C 116.7700 . . 
      1025 .  91 TYR N    N 122.5100 . . 
      1026 .  92 ILE H    H   8.7500 . . 
      1027 .  92 ILE HA   H   3.7700 . . 
      1028 .  92 ILE HB   H   2.0800 . . 
      1029 .  92 ILE HG12 H   1.9400 . . 
      1030 .  92 ILE HG13 H   1.9400 . . 
      1031 .  92 ILE HG2  H   1.1000 . . 
      1032 .  92 ILE HD1  H   0.9600 . . 
      1033 .  92 ILE CA   C  65.9200 . . 
      1034 .  92 ILE CB   C  37.1600 . . 
      1035 .  92 ILE CG1  C  26.2800 . . 
      1036 .  92 ILE CG2  C  17.5600 . . 
      1037 .  92 ILE CD1  C  14.4000 . . 
      1038 .  92 ILE N    N 123.3400 . . 
      1039 .  93 ASP H    H   8.0600 . . 
      1040 .  93 ASP HA   H   4.5000 . . 
      1041 .  93 ASP HB2  H   2.7500 . . 
      1042 .  93 ASP HB3  H   2.9000 . . 
      1043 .  93 ASP CA   C  57.8600 . . 
      1044 .  93 ASP CB   C  41.2400 . . 
      1045 .  93 ASP N    N 121.1100 . . 
      1046 .  94 ILE H    H   7.4000 . . 
      1047 .  94 ILE HA   H   3.7100 . . 
      1048 .  94 ILE HB   H   2.1000 . . 
      1049 .  94 ILE HG12 H   1.9700 . . 
      1050 .  94 ILE HG13 H   2.0100 . . 
      1051 .  94 ILE HG2  H   0.9800 . . 
      1052 .  94 ILE HD1  H   1.2300 . . 
      1053 .  94 ILE CA   C  65.1700 . . 
      1054 .  94 ILE CB   C  38.1000 . . 
      1055 .  94 ILE CG1  C  28.8600 . . 
      1056 .  94 ILE CG2  C  17.3200 . . 
      1057 .  94 ILE CD1  C  13.5200 . . 
      1058 .  94 ILE N    N 118.1800 . . 
      1059 .  95 ILE H    H   7.4400 . . 
      1060 .  95 ILE HA   H   3.6200 . . 
      1061 .  95 ILE HB   H   2.0900 . . 
      1062 .  95 ILE HG12 H  -0.2800 . . 
      1063 .  95 ILE HG13 H   1.1000 . . 
      1064 .  95 ILE HG2  H   0.9000 . . 
      1065 .  95 ILE HD1  H   0.1300 . . 
      1066 .  95 ILE CA   C  65.4600 . . 
      1067 .  95 ILE CB   C  38.2000 . . 
      1068 .  95 ILE CG1  C  26.2800 . . 
      1069 .  95 ILE CG2  C  17.7300 . . 
      1070 .  95 ILE CD1  C  13.8900 . . 
      1071 .  95 ILE N    N 121.7600 . . 
      1072 .  96 LEU H    H   8.6000 . . 
      1073 .  96 LEU HA   H   3.9100 . . 
      1074 .  96 LEU HB2  H   1.5300 . . 
      1075 .  96 LEU HB3  H   2.1100 . . 
      1076 .  96 LEU HG   H   1.6000 . . 
      1077 .  96 LEU HD1  H   0.9100 . . 
      1078 .  96 LEU HD2  H   0.3700 . . 
      1079 .  96 LEU CA   C  57.9700 . . 
      1080 .  96 LEU CB   C  42.1400 . . 
      1081 .  96 LEU CG   C  26.6800 . . 
      1082 .  96 LEU CD1  C  24.2100 . . 
      1083 .  96 LEU CD2  C  21.6700 . . 
      1084 .  96 LEU N    N 121.3500 . . 
      1085 .  97 LYS H    H   8.0400 . . 
      1086 .  97 LYS HA   H   3.9900 . . 
      1087 .  97 LYS HB2  H   1.9200 . . 
      1088 .  97 LYS HB3  H   2.0200 . . 
      1089 .  97 LYS HG2  H   1.4600 . . 
      1090 .  97 LYS HG3  H   1.4600 . . 
      1091 .  97 LYS HD2  H   1.6400 . . 
      1092 .  97 LYS HD3  H   1.9200 . . 
      1093 .  97 LYS HE2  H   2.9800 . . 
      1094 .  97 LYS HE3  H   2.9800 . . 
      1095 .  97 LYS CA   C  58.8700 . . 
      1096 .  97 LYS CB   C  32.5100 . . 
      1097 .  97 LYS CG   C  25.8500 . . 
      1098 .  97 LYS CD   C  28.8500 . . 
      1099 .  97 LYS CE   C  42.1900 . . 
      1100 .  97 LYS N    N 118.4800 . . 
      1101 .  98 LYS H    H   7.8200 . . 
      1102 .  98 LYS HA   H   4.1600 . . 
      1103 .  98 LYS HB2  H   1.8300 . . 
      1104 .  98 LYS HB3  H   1.9200 . . 
      1105 .  98 LYS HG2  H   1.4600 . . 
      1106 .  98 LYS HG3  H   1.5500 . . 
      1107 .  98 LYS HD2  H   1.6700 . . 
      1108 .  98 LYS HD3  H   1.7500 . . 
      1109 .  98 LYS HE2  H   3.0200 . . 
      1110 .  98 LYS HE3  H   3.0200 . . 
      1111 .  98 LYS CA   C  58.2100 . . 
      1112 .  98 LYS CB   C  32.4600 . . 
      1113 .  98 LYS CG   C  25.2100 . . 
      1114 .  98 LYS CD   C  29.2300 . . 
      1115 .  98 LYS CE   C  42.3900 . . 
      1116 .  98 LYS N    N 119.8700 . . 
      1117 .  99 LYS H    H   7.9500 . . 
      1118 .  99 LYS HA   H   4.1600 . . 
      1119 .  99 LYS HB2  H   1.8300 . . 
      1120 .  99 LYS HB3  H   1.9200 . . 
      1121 .  99 LYS HG2  H   1.4600 . . 
      1122 .  99 LYS HG3  H   1.5500 . . 
      1123 .  99 LYS HD2  H   1.6700 . . 
      1124 .  99 LYS HD3  H   1.7500 . . 
      1125 .  99 LYS HE2  H   3.0200 . . 
      1126 .  99 LYS HE3  H   3.0200 . . 
      1127 .  99 LYS CA   C  57.9000 . . 
      1128 .  99 LYS CB   C  32.5900 . . 
      1129 .  99 LYS CG   C  24.8400 . . 
      1130 .  99 LYS CD   C  29.2300 . . 
      1131 .  99 LYS CE   C  42.3900 . . 
      1132 .  99 LYS N    N 120.8300 . . 
      1133 . 100 LYS H    H   8.0800 . . 
      1134 . 100 LYS HA   H   4.3000 . . 
      1135 . 100 LYS HB2  H   1.7900 . . 
      1136 . 100 LYS HB3  H   1.8700 . . 
      1137 . 100 LYS HG2  H   1.4400 . . 
      1138 . 100 LYS HG3  H   1.5400 . . 
      1139 . 100 LYS HD2  H   1.6700 . . 
      1140 . 100 LYS HD3  H   1.6700 . . 
      1141 . 100 LYS HE2  H   2.9800 . . 
      1142 . 100 LYS HE3  H   2.9800 . . 
      1143 . 100 LYS CA   C  56.7900 . . 
      1144 . 100 LYS CB   C  32.6700 . . 
      1145 . 100 LYS CG   C  24.6700 . . 
      1146 . 100 LYS CD   C  28.8600 . . 
      1147 . 100 LYS CE   C  42.1900 . . 
      1148 . 100 LYS N    N 120.1000 . . 
      1149 . 101 SER H    H   8.0100 . . 
      1150 . 101 SER HA   H   4.4100 . . 
      1151 . 101 SER HB2  H   3.9400 . . 
      1152 . 101 SER HB3  H   3.9400 . . 
      1153 . 101 SER CA   C  58.7200 . . 
      1154 . 101 SER CB   C  63.6500 . . 
      1155 . 101 SER N    N 116.1500 . . 
      1156 . 102 LYS H    H   8.1700 . . 
      1157 . 102 LYS HA   H   4.3000 . . 
      1158 . 102 LYS HB2  H   1.7900 . . 
      1159 . 102 LYS HB3  H   1.8700 . . 
      1160 . 102 LYS HG2  H   1.4400 . . 
      1161 . 102 LYS HG3  H   1.5400 . . 
      1162 . 102 LYS HD2  H   1.6700 . . 
      1163 . 102 LYS HD3  H   1.6700 . . 
      1164 . 102 LYS HE2  H   2.9800 . . 
      1165 . 102 LYS HE3  H   2.9800 . . 
      1166 . 102 LYS CA   C  56.4900 . . 
      1167 . 102 LYS CB   C  32.6900 . . 
      1168 . 102 LYS CG   C  24.3600 . . 
      1169 . 102 LYS CD   C  28.9000 . . 
      1170 . 102 LYS CE   C  42.1900 . . 
      1171 . 102 LYS N    N 122.5900 . . 
      1172 . 103 ASP H    H   8.1500 . . 
      1173 . 103 ASP HA   H   4.5100 . . 
      1174 . 103 ASP HB2  H   2.5400 . . 
      1175 . 103 ASP HB3  H   2.5400 . . 
      1176 . 103 ASP CA   C  54.4000 . . 
      1177 . 103 ASP CB   C  41.1300 . . 
      1178 . 103 ASP N    N 120.5300 . . 
      1179 . 104 HIS H    H   8.0000 . . 
      1180 . 104 HIS HA   H   4.5900 . . 
      1181 . 104 HIS HB2  H   3.1200 . . 
      1182 . 104 HIS HB3  H   3.1200 . . 
      1183 . 104 HIS HD2  H   7.9800 . . 
      1184 . 104 HIS HE1  H   7.3300 . . 
      1185 . 104 HIS CA   C  55.2800 . . 
      1186 . 104 HIS CB   C  29.7200 . . 
      1187 . 104 HIS CD2  C 119.1000 . . 
      1188 . 104 HIS CE1  C 136.6900 . . 
      1189 . 104 HIS N    N 118.3000 . . 
      1190 . 105 PHE H    H   7.8700 . . 
      1191 . 105 PHE HA   H   4.4300 . . 
      1192 . 105 PHE HB2  H   2.9800 . . 
      1193 . 105 PHE HB3  H   3.1800 . . 
      1194 . 105 PHE HD1  H   6.7500 . . 
      1195 . 105 PHE HD2  H   6.7500 . . 
      1196 . 105 PHE HE1  H   7.1700 . . 
      1197 . 105 PHE HE2  H   7.1700 . . 
      1198 . 105 PHE HZ   H   7.2700 . . 
      1199 . 105 PHE CA   C  59.0600 . . 
      1200 . 105 PHE CB   C  39.9800 . . 
      1201 . 105 PHE CD1  C 131.3200 . . 
      1202 . 105 PHE CD2  C 131.3200 . . 
      1203 . 105 PHE CE1  C 129.4800 . . 
      1204 . 105 PHE CE2  C 129.4800 . . 
      1205 . 105 PHE CZ   C 130.9500 . . 
      1206 . 105 PHE N    N 126.7400 . . 
      1207 . 106 GLY H    H   8.1400 . . 
      1208 . 106 GLY HA2  H   3.6700 . . 
      1209 . 106 GLY HA3  H   4.1900 . . 
      1210 . 106 GLY CA   C  43.3900 . . 
      1211 . 106 GLY N    N 107.7200 . . 

   stop_

save_


save_chemical_shift_set_2
   _Saveframe_category               assigned_chemical_shifts

   _Details                          .

   loop_
      _Sample_label

      $sample_1 

   stop_

   _Sample_conditions_label         $sample_cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name        peptide
   _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 SER H   H   8.3700 . . 
       2 . 1 SER HA  H   5.3500 . . 
       3 . 1 SER HB2 H   3.5100 . . 
       4 . 1 SER HB3 H   3.7000 . . 
       5 . 1 SER CA  C  56.1200 . . 
       6 . 1 SER CB  C  65.2200 . . 
       7 . 1 SER N   N 122.9200 . . 
       8 . 2 TRP H   H   9.0000 . . 
       9 . 2 TRP HA  H   4.0000 . . 
      10 . 2 TRP HB2 H   3.2800 . . 
      11 . 2 TRP HB3 H   3.1800 . . 
      12 . 2 TRP HD1 H   7.2600 . . 
      13 . 2 TRP HE1 H  10.1200 . . 
      14 . 2 TRP HE3 H   7.1100 . . 
      15 . 2 TRP HZ2 H   7.4000 . . 
      16 . 2 TRP HZ3 H   7.5700 . . 
      17 . 2 TRP HH2 H   7.2200 . . 
      18 . 2 TRP CA  C  56.8300 . . 
      19 . 2 TRP CB  C  33.0800 . . 
      20 . 2 TRP CD1 C 126.5500 . . 
      21 . 2 TRP CE3 C 121.4200 . . 
      22 . 2 TRP CZ2 C 114.9100 . . 
      23 . 2 TRP CZ3 C 121.7600 . . 
      24 . 2 TRP CH2 C 124.6900 . . 
      25 . 2 TRP N   N 122.3000 . . 
      26 . 2 TRP NE1 N 129.1200 . . 
      27 . 3 VAL H   H   9.2600 . . 
      28 . 3 VAL HA  H   3.8800 . . 
      29 . 3 VAL HB  H   1.8700 . . 
      30 . 3 VAL HG1 H   0.7700 . . 
      31 . 3 VAL HG2 H   0.5200 . . 
      32 . 3 VAL CA  C  58.1100 . . 
      33 . 3 VAL CB  C  36.0500 . . 
      34 . 3 VAL CG1 C  17.8800 . . 
      35 . 3 VAL CG2 C  23.1500 . . 
      36 . 3 VAL N   N 117.0800 . . 
      37 . 4 PTR H   H   8.5800 . . 
      38 . 4 PTR HA  H   5.1700 . . 
      39 . 4 PTR HB2 H   3.1200 . . 
      40 . 4 PTR HB3 H   2.7800 . . 
      41 . 4 PTR HD1 H   6.0900 . . 
      42 . 4 PTR HD2 H   6.0900 . . 
      43 . 4 PTR HE1 H   5.8600 . . 
      44 . 4 PTR HE2 H   5.8600 . . 
      45 . 4 PTR CA  C  57.0400 . . 
      46 . 4 PTR CB  C  40.4100 . . 
      47 . 4 PTR CD1 C 132.1600 . . 
      48 . 4 PTR CD2 C 132.1600 . . 
      49 . 4 PTR CE1 C 117.9100 . . 
      50 . 4 PTR CE2 C 117.9100 . . 
      51 . 4 PTR N   N 123.4900 . . 
      52 . 5 SER H   H   7.8600 . . 
      53 . 5 SER HA  H   3.6000 . . 
      54 . 5 SER HB2 H   3.6000 . . 
      55 . 5 SER HB3 H   3.6000 . . 
      56 . 5 SER CA  C  56.1200 . . 
      57 . 5 SER CB  C  65.2200 . . 
      58 . 5 SER N   N 122.9200 . . 
      59 . 6 PRO HA  H   4.3500 . . 
      60 . 6 PRO HB2 H   1.8400 . . 
      61 . 6 PRO HB3 H   1.9500 . . 
      62 . 6 PRO HG2 H   2.2800 . . 
      63 . 6 PRO HG3 H   2.2800 . . 
      64 . 6 PRO HD2 H   3.5200 . . 
      65 . 6 PRO HD3 H   3.6300 . . 
      66 . 6 PRO CA  C  65.1300 . . 
      67 . 6 PRO CB  C  32.3200 . . 
      68 . 6 PRO CG  C  27.8900 . . 
      69 . 6 PRO CD  C  50.1000 . . 
      70 . 7 LEU H   H   8.3100 . . 
      71 . 7 LEU HA  H   4.1800 . . 
      72 . 7 LEU HB2 H   1.5300 . . 
      73 . 7 LEU HB3 H   1.4300 . . 
      74 . 7 LEU HG  H   1.4300 . . 
      75 . 7 LEU HD1 H   0.8500 . . 
      76 . 7 LEU HD2 H   0.7900 . . 
      77 . 7 LEU CA  C  57.9700 . . 
      78 . 7 LEU CB  C  42.1400 . . 
      79 . 7 LEU CG  C  26.6800 . . 
      80 . 7 LEU CD1 C  24.2100 . . 
      81 . 7 LEU CD2 C  21.6700 . . 
      82 . 7 LEU N   N 121.3500 . . 
      83 . 8 HIS H   H   8.2100 . . 
      84 . 8 HIS HA  H   4.6100 . . 
      85 . 8 HIS HB2 H   3.0800 . . 
      86 . 8 HIS HB3 H   3.2000 . . 
      87 . 8 HIS HD2 H   7.4600 . . 
      88 . 8 HIS HE1 H   7.1200 . . 
      89 . 8 HIS CA  C  55.2800 . . 
      90 . 8 HIS CB  C  29.7200 . . 
      91 . 8 HIS CD2 C 119.1000 . . 
      92 . 8 HIS CE1 C 136.6900 . . 
      93 . 8 HIS N   N 118.3000 . . 

   stop_

save_