data_4312

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

save_entry_information
   _Saveframe_category      entry_information

   _Entry_title            
;
1H, 15N and 13C Resonance Assignments for the Bromodomain of the 
Histone Acetyltransferase hsP/CAF
;
   _BMRB_accession_number   4312
   _BMRB_flat_file_name     bmr4312.str
   _Entry_type              original
   _Submission_date         1999-02-28
   _Accession_date          1999-03-01
   _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 Dhalluin Christophe .  . 
      2 Carlson  Justin     .  . 
      3 Zeng     Lei        .  . 
      4 He       Cheng      .  . 
      5 Aggarwal Aneel      K. . 
      6 Zhou     Ming-Ming  .  . 

   stop_

   loop_
      _Saveframe_category_type
      _Saveframe_category_type_count

      assigned_chemical_shifts 1 

   stop_

   loop_
      _Data_type
      _Data_type_count

      "1H chemical shifts"  608 
      "13C chemical shifts" 382 
      "15N chemical shifts" 107 

   stop_

   loop_
      _Revision_date
      _Revision_keyword
      _Revision_author
      _Revision_detail

      1999-03-03 original author . 

   stop_

   _Original_release_date   1999-03-03

save_


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

save_entry_citation
   _Saveframe_category           entry_citation

   _Citation_full               
;
Dhalluin, C., Carlson, J., Zeng, L., He, C., Aggarwal, A. K., and 
Zhou, M-M., "1H, 15N and 13C Resonance Assignments for the 
Bromodomain of the Histone Acetyltransferase hsP/CAF," 
J. Biomol. NMR, in preparation.
;
   _Citation_title              
;
1H, 15N and 13C Resonance Assignments for the Bromodomain of the 
Histone Acetyltransferase hsP/CAF
;
   _Citation_status             'in preparation'
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    ?

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Dhalluin Christophe .  . 
      2 Carlson  Justin     .  . 
      3 Zeng     Lei        .  . 
      4 He       Cheng      .  . 
      5 Aggarwal Aneel      K. . 
      6 Zhou     Ming-Ming  .  . 

   stop_

   _Journal_abbreviation        'J. Biomol. NMR'
   _Journal_volume               .
   _Journal_issue                .
   _Journal_CSD                  .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_ISBN                    .
   _Conference_state_province    .
   _Conference_abstract_number   .
   _Page_first                   .
   _Page_last                    .
   _Year                         .
   _Details                      .

   loop_
      _Keyword

      'histone acetyltransferase bromodomain' 

   stop_

save_


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

save_ref_1
   _Saveframe_category           citation

   _Citation_full               
;
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G. 
Pfeifer, J. and Bax, A (1995) J. Biomol. NMR 6, 277-293.
;
   _Citation_title              'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    8520220

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Delaglio  F    .  . 
      2 Grzesiek  S    .  . 
      3 Vuister  'G W' W. . 
      4 Zhu       G    .  . 
      5 Pfeifer   J    .  . 
      6 Bax       A    .  . 

   stop_

   _Journal_abbreviation        'J. Biomol. NMR'
   _Journal_name_full           'Journal of biomolecular NMR'
   _Journal_volume               6
   _Journal_issue                3
   _Journal_CSD                  .
   _Book_title                   .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_publisher               .
   _Book_publisher_city          .
   _Book_ISBN                    .
   _Conference_title             .
   _Conference_site              .
   _Conference_state_province    .
   _Conference_country           .
   _Conference_start_date        .
   _Conference_end_date          .
   _Conference_abstract_number   .
   _Thesis_institution           .
   _Thesis_institution_city      .
   _Thesis_institution_country   .
   _Page_first                   277
   _Page_last                    293
   _Year                         1995
   _Details                     
;
The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.
;

save_


save_ref_2
   _Saveframe_category           citation

   _Citation_full               'Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614.'
   _Citation_title               .
   _Citation_status              .
   _Citation_type                .
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    ?
   _Journal_abbreviation         .
   _Journal_name_full            .
   _Journal_volume               .
   _Journal_issue                .
   _Journal_CSD                  .
   _Book_title                   .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_publisher               .
   _Book_publisher_city          .
   _Book_ISBN                    .
   _Conference_title             .
   _Conference_site              .
   _Conference_state_province    .
   _Conference_country           .
   _Conference_start_date        .
   _Conference_end_date          .
   _Conference_abstract_number   .
   _Thesis_institution           .
   _Thesis_institution_city      .
   _Thesis_institution_country   .
   _Page_first                   .
   _Page_last                    .
   _Year                         .
   _Details                      .

save_


save_ref_3
   _Saveframe_category           citation

   _Citation_full               'X.J.Yang,V.V.Ogryzko,J.I.Nishikawa,B.H.Howard,Y.Nakatani, Nature (1996) 382, 319.'
   _Citation_title              'A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.'
   _Citation_status              published
   _Citation_type                journal
   _CAS_abstract_code            .
   _MEDLINE_UI_code              .
   _PubMed_ID                    8684459

   loop_
      _Author_ordinal
      _Author_family_name
      _Author_given_name
      _Author_middle_initials
      _Author_family_title

      1 Yang      'X J' J. . 
      2 Ogryzko   'V V' V. . 
      3 Nishikawa  J    .  . 
      4 Howard    'B H' H. . 
      5 Nakatani   Y    .  . 

   stop_

   _Journal_abbreviation         Nature
   _Journal_name_full            Nature
   _Journal_volume               382
   _Journal_issue                6589
   _Journal_CSD                  .
   _Book_title                   .
   _Book_chapter_title           .
   _Book_volume                  .
   _Book_series                  .
   _Book_publisher               .
   _Book_publisher_city          .
   _Book_ISBN                    .
   _Conference_title             .
   _Conference_site              .
   _Conference_state_province    .
   _Conference_country           .
   _Conference_start_date        .
   _Conference_end_date          .
   _Conference_abstract_number   .
   _Thesis_institution           .
   _Thesis_institution_city      .
   _Thesis_institution_country   .
   _Page_first                   319
   _Page_last                    324
   _Year                         1996
   _Details                     
;
The adenoviral oncoprotein E1A induces progression through the cell cycle by
binding to the products of the p300/CBP and retinoblastoma gene families. A new
cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase
activity has been identified that competes with E1A. Exogenous expression of
P/CAF in HeLa cells inhibits cell-cycle progression and counteracts the
mitogenic activity of E1A. E1A disturbs the normal cellular interaction between
p300/CBP and its associated histone acetylase.
;

save_


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

save_brd
   _Saveframe_category         molecular_system

   _Mol_system_name            bromodomain
   _Abbreviation_common        brd
   _Enzyme_commission_number   2.3.1.48

   loop_
      _Mol_system_component_name
      _Mol_label

      'brd subunit 1' $brd_monomer 

   stop_

   _System_molecular_weight    .
   _System_physical_state      native
   _System_oligomer_state      monomer
   _System_paramagnetic        no
   _System_thiol_state         .

   loop_
      _Biological_function

      'histone acetylated lysine recognition' 

   stop_

   _Database_query_date        .
   _Details                    .

save_


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

save_brd_monomer
   _Saveframe_category                          monomeric_polymer

   _Mol_type                                    polymer
   _Mol_polymer_class                           protein
   _Name_common                                'histone acetyltransferase bromodomain'
   _Abbreviation_common                         brd
   _Molecular_mass                              .
   _Mol_thiol_state                             .
   _Details                                    
;
The first 4 residues (GSHM) do not belong to the protein.
First residue (Ser 719), last residue (Lys 832)

No disulfides exist in the molecule
;

   	##############################
   	#  Polymer residue sequence  #
   	##############################
   
      _Residue_count                               118
   _Mol_residue_sequence                       
;
GSHMSKEPRDPDQLYSTLKS
ILQQVKSHQSAWPFMEPVKR
TEAPGYYEVIRSPMDLKTMS
ERLKNRYYVSKKLFMADLQR
VFTNCKEYNAPESEYYKCAN
ILEKFFFSKIKEAGLIDK
;

   loop_
      _Residue_seq_code
      _Residue_author_seq_code
      _Residue_label

        1  -4 GLY    2  -3 SER    3  -2 HIS    4  -1 MET    5 719 SER 
        6 720 LYS    7 721 GLU    8 722 PRO    9 723 ARG   10 724 ASP 
       11 725 PRO   12 726 ASP   13 727 GLN   14 728 LEU   15 729 TYR 
       16 730 SER   17 731 THR   18 732 LEU   19 733 LYS   20 734 SER 
       21 735 ILE   22 736 LEU   23 737 GLN   24 738 GLN   25 739 VAL 
       26 740 LYS   27 741 SER   28 742 HIS   29 743 GLN   30 744 SER 
       31 745 ALA   32 746 TRP   33 747 PRO   34 748 PHE   35 749 MET 
       36 750 GLU   37 751 PRO   38 752 VAL   39 753 LYS   40 754 ARG 
       41 755 THR   42 756 GLU   43 757 ALA   44 758 PRO   45 759 GLY 
       46 760 TYR   47 761 TYR   48 762 GLU   49 763 VAL   50 764 ILE 
       51 765 ARG   52 766 SER   53 767 PRO   54 768 MET   55 769 ASP 
       56 770 LEU   57 771 LYS   58 772 THR   59 773 MET   60 774 SER 
       61 775 GLU   62 776 ARG   63 777 LEU   64 778 LYS   65 779 ASN 
       66 780 ARG   67 781 TYR   68 782 TYR   69 783 VAL   70 784 SER 
       71 785 LYS   72 786 LYS   73 787 LEU   74 788 PHE   75 789 MET 
       76 790 ALA   77 791 ASP   78 792 LEU   79 793 GLN   80 794 ARG 
       81 795 VAL   82 796 PHE   83 797 THR   84 798 ASN   85 799 CYS 
       86 800 LYS   87 801 GLU   88 802 TYR   89 803 ASN   90 804 ALA 
       91 805 PRO   92 806 GLU   93 807 SER   94 808 GLU   95 809 TYR 
       96 810 TYR   97 811 LYS   98 812 CYS   99 813 ALA  100 814 ASN 
      101 815 ILE  102 816 LEU  103 817 GLU  104 818 LYS  105 819 PHE 
      106 820 PHE  107 821 PHE  108 822 SER  109 823 LYS  110 824 ILE 
      111 825 LYS  112 826 GLU  113 827 ALA  114 828 GLY  115 829 LEU 
      116 830 ILE  117 831 ASP  118 832 LYS 

   stop_

   _Sequence_homology_query_date                .
   _Sequence_homology_query_revised_last_date   2015-02-04

   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 1JM4 "Nmr Structure Of PCAF BROMODOMAIN IN COMPLEX WITH HIV-1 Tat Peptide"                                                             100.00 118 98.31 98.31 1.64e-79 
      PDB 1N72 "Structure And Ligand Of A Histone Acetyltransferase Bromodomain"                                                                 100.00 118 98.31 98.31 1.64e-79 
      PDB 1WUG "Complex Structure Of Pcaf Bromodomain With Small Chemical Ligand Np1"                                                            100.00 118 98.31 98.31 1.64e-79 
      PDB 1WUM "Complex Structure Of Pcaf Bromodomain With Small Chemical Ligand Np2"                                                            100.00 118 98.31 98.31 1.64e-79 
      PDB 1ZS5 "Structure-Based Evaluation Of Selective And Non-Selective Small Molecules That Block Hiv-1 Tat And Pcaf Association"             100.00 118 98.31 98.31 1.64e-79 
      PDB 2RNW "The Structural Basis For Site-Specific Lysine-Acetylated Histone Recognition By The Bromodomains Of The Human Transcriptional C" 100.00 118 98.31 98.31 1.64e-79 
      PDB 2RNX "The Structural Basis For Site-Specific Lysine-Acetylated Histone Recognition By The Bromodomains Of The Human Transcriptional C" 100.00 118 98.31 98.31 1.64e-79 

   stop_

save_


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

save_natural_source
   _Saveframe_category   natural_source


   loop_
      _Mol_label
      _Organism_name_common
      _NCBI_taxonomy_ID
      _Superkingdom
      _Kingdom
      _Genus
      _Species
      _Fraction

      $brd_monomer human 9606 Eukaryota Metazoa Homo sapiens cytoplasm 

   stop_

save_


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

save_experimental_source
   _Saveframe_category   experimental_source


   loop_
      _Mol_label
      _Production_method
      _Host_organism_name_common
      _Genus
      _Species
      _Strain
      _Cell_line
      _Vector_type
      _Vector_name

      $brd_monomer 'recombinant technology' 'E. Coli' Escherichia coli . BL21(DE3) plasmid pET14b 

   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

      $brd_monomer          1.0 mM '[U-13C; U-15N; U-75% 2H]' 
      'phosphate buffer'  100   mM  .                         
      'perdeuterated DTT'   5   mM  .                         
       EDTA                 0.5 mM  .                         
       H2O                 90   %   .                         
       D2O                 10   %   .                         

   stop_

save_


save_sample_2
   _Saveframe_category   sample

   _Sample_type          solution
   _Details              .

   loop_
      _Mol_label
      _Concentration_value
      _Concentration_value_units
      _Isotopic_labeling

      $brd_monomer          1.0 mM '[U-13C; U-15N]' 
      'phosphate buffer'  100   mM  .               
      'perdeuterated DTT'   5   mM  .               
       EDTA                 0.5 mM  .               
       H2O                 90   %   .               
       D2O                 10   %   .               

   stop_

save_


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

save_NMRPipe
   _Saveframe_category   software

   _Name                 NMRPipe
   _Version              3.1

   loop_
      _Task

      'spectra Processing' 

   stop_

   _Details              .
   _Citation_label      $ref_1

save_


save_NMRVIEW
   _Saveframe_category   software

   _Name                 NMRVIEW
   _Version              3.1

   loop_
      _Task

      'spectra analysis' 

   stop_

   _Details              .
   _Citation_label      $ref_2

save_


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

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

save_spectrometer_1
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       500
   _Details              .

save_


save_spectrometer_2
   _Saveframe_category   NMR_spectrometer

   _Manufacturer         Bruker
   _Model                DRX
   _Field_strength       600
   _Details              .

save_


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

save_2D_1H-15N_HSQC_1
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-15N HSQC'
   _Sample_label         .

save_


save_2D_1H-13C_HSQC_2
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '2D 1H-13C HSQC'
   _Sample_label         .

save_


save_3D_HNCACB_3
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNCACB'
   _Sample_label         .

save_


save_3D_HN(CO)CACB_4
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HN(CO)CACB'
   _Sample_label         .

save_


save_3D_(H)C(CO)NH-TOCSY_5
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D (H)C(CO)NH-TOCSY'
   _Sample_label         .

save_


save_3D_HNHA_6
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HNHA'
   _Sample_label         .

save_


save_3D_HCCH_TOCSY_7
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '3D HCCH TOCSY'
   _Sample_label         .

save_


save_15N_edited_TOCSY_8
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N edited TOCSY'
   _Sample_label         .

save_


save_15N_edited_NOESY_9
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '15N edited NOESY'
   _Sample_label         .

save_


save_13C_edited_NOESY_10
   _Saveframe_category   NMR_applied_experiment

   _Experiment_name     '13C edited NOESY'
   _Sample_label         .

save_


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

save_Ex-cond_1
   _Saveframe_category   sample_conditions

   _Details              .

   loop_
      _Variable_type
      _Variable_value
      _Variable_value_error
      _Variable_value_units

      pH            6.5 0.1 na 
      temperature 303   0.1 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   . . . 1.000000000 
      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_2 

   stop_

   _Sample_conditions_label         $Ex-cond_1
   _Chem_shift_reference_set_label  $chemical_shift_reference
   _Mol_system_component_name       'brd subunit 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 .   6 LYS HA   H   4.36 . 1 
         2 .   6 LYS HB2  H   1.68 . 1 
         3 .   6 LYS HB3  H   1.88 . 1 
         4 .   6 LYS HG2  H   1.43 . 1 
         5 .   6 LYS HG3  H   1.58 . 1 
         6 .   6 LYS HD3  H   1.70 . 1 
         7 .   6 LYS HE3  H   3.00 . 1 
         8 .   6 LYS CA   C  56.30 . 1 
         9 .   6 LYS CB   C  33.14 . 1 
        10 .   6 LYS CG   C  25.43 . 1 
        11 .   6 LYS CD   C  29.83 . 1 
        12 .   6 LYS CE   C  41.96 . 1 
        13 .   7 GLU H    H   8.32 . 1 
        14 .   7 GLU HA   H   4.54 . 1 
        15 .   7 GLU HB2  H   1.89 . 1 
        16 .   7 GLU HB3  H   2.02 . 1 
        17 .   7 GLU HG3  H   2.27 . 1 
        18 .   7 GLU CA   C  54.62 . 1 
        19 .   7 GLU CB   C  29.83 . 1 
        20 .   7 GLU CG   C  35.89 . 1 
        21 .   7 GLU N    N 122.99 . 1 
        22 .   8 PRO HA   H   4.39 . 1 
        23 .   8 PRO HB2  H   1.88 . 1 
        24 .   8 PRO HB3  H   2.22 . 1 
        25 .   8 PRO HG3  H   2.03 . 1 
        26 .   8 PRO HD2  H   3.66 . 1 
        27 .   8 PRO HD3  H   3.80 . 1 
        28 .   8 PRO CA   C  63.43 . 1 
        29 .   8 PRO CB   C  32.03 . 1 
        30 .   8 PRO CG   C  27.63 . 1 
        31 .   8 PRO CD   C  50.76 . 1 
        32 .   9 ARG H    H   8.42 . 1 
        33 .   9 ARG HA   H   4.33 . 1 
        34 .   9 ARG HB2  H   1.76 . 1 
        35 .   9 ARG HB3  H   1.81 . 1 
        36 .   9 ARG HG3  H   1.68 . 1 
        37 .   9 ARG HD3  H   3.16 . 1 
        38 .   9 ARG CA   C  63.43 . 1 
        39 .   9 ARG CB   C  30.93 . 1 
        40 .   9 ARG CG   C  27.63 . 1 
        41 .   9 ARG CD   C  43.60 . 1 
        42 .   9 ARG N    N 121.19 . 1 
        43 .  10 ASP H    H   8.27 . 1 
        44 .  10 ASP HA   H   4.87 . 1 
        45 .  10 ASP HB2  H   2.69 . 1 
        46 .  10 ASP HB3  H   2.75 . 1 
        47 .  10 ASP CA   C  52.41 . 1 
        48 .  10 ASP CB   C  41.40 . 1 
        49 .  10 ASP N    N 122.01 . 1 
        50 .  11 PRO HA   H   4.33 . 1 
        51 .  11 PRO HB2  H   1.97 . 1 
        52 .  11 PRO HB3  H   2.33 . 1 
        53 .  11 PRO HG3  H   2.03 . 1 
        54 .  11 PRO HD3  H   3.87 . 1 
        55 .  11 PRO CA   C  65.08 . 1 
        56 .  11 PRO CB   C  32.59 . 1 
        57 .  11 PRO CG   C  27.63 . 1 
        58 .  11 PRO CD   C  51.31 . 1 
        59 .  12 ASP H    H   8.40 . 1 
        60 .  12 ASP HA   H   4.69 . 1 
        61 .  12 ASP HB2  H   2.73 . 1 
        62 .  12 ASP HB3  H   2.79 . 1 
        63 .  12 ASP CA   C  55.72 . 1 
        64 .  12 ASP CB   C  40.55 . 1 
        65 .  12 ASP N    N 119.72 . 1 
        66 .  13 GLN H    H   8.20 . 1 
        67 .  13 GLN HA   H   4.16 . 1 
        68 .  13 GLN HB3  H   2.15 . 1 
        69 .  13 GLN HG2  H   2.37 . 1 
        70 .  13 GLN HG3  H   2.52 . 1 
        71 .  13 GLN CA   C  55.92 . 1 
        72 .  13 GLN CB   C  28.73 . 1 
        73 .  13 GLN CG   C  34.24 . 1 
        74 .  13 GLN N    N 121.36 . 1 
        75 .  14 LEU H    H   8.21 . 1 
        76 .  14 LEU HA   H   4.04 . 1 
        77 .  14 LEU HB2  H   1.55 . 1 
        78 .  14 LEU HB3  H   1.85 . 1 
        79 .  14 LEU HG   H   1.48 . 1 
        80 .  14 LEU HD1  H   0.79 . 1 
        81 .  14 LEU HD2  H   0.79 . 1 
        82 .  14 LEU CA   C  58.47 . 1 
        83 .  14 LEU CB   C  41.40 . 1 
        84 .  14 LEU CG   C  27.08 . 1 
        85 .  14 LEU CD1  C  25.97 . 1 
        86 .  14 LEU CD2  C  23.23 . 1 
        87 .  14 LEU N    N 121.36 . 1 
        88 .  15 TYR H    H   8.02 . 1 
        89 .  15 TYR HA   H   4.04 . 1 
        90 .  15 TYR HB2  H   3.02 . 1 
        91 .  15 TYR HB3  H   3.21 . 1 
        92 .  15 TYR HD1  H   7.05 . 3 
        93 .  15 TYR HE1  H   6.88 . 3 
        94 .  15 TYR CA   C  62.32 . 1 
        95 .  15 TYR CB   C  38.64 . 1 
        96 .  15 TYR CD1  C 134.35 . 3 
        97 .  15 TYR CE1  C 119.48 . 3 
        98 .  15 TYR N    N 119.06 . 1 
        99 .  16 SER H    H   8.17 . 1 
       100 .  16 SER HA   H   3.92 . 1 
       101 .  16 SER HB3  H   4.00 . 1 
       102 .  16 SER N    N 112.17 . 1 
       103 .  17 THR H    H   8.06 . 1 
       104 .  17 THR HA   H   3.92 . 1 
       105 .  17 THR HB   H   4.25 . 1 
       106 .  17 THR HG2  H   1.14 . 1 
       107 .  17 THR CA   C  66.73 . 1 
       108 .  17 THR CB   C  68.93 . 1 
       109 .  17 THR CG2  C  21.57 . 1 
       110 .  17 THR N    N 120.37 . 1 
       111 .  18 LEU H    H   8.46 . 1 
       112 .  18 LEU HA   H   3.29 . 1 
       113 .  18 LEU HB2  H   0.29 . 1 
       114 .  18 LEU HB3  H   1.53 . 1 
       115 .  18 LEU HG   H   1.68 . 1 
       116 .  18 LEU HD1  H   0.47 . 1 
       117 .  18 LEU HD2  H  -0.19 . 1 
       118 .  18 LEU CA   C  57.92 . 1 
       119 .  18 LEU CB   C  39.75 . 1 
       120 .  18 LEU CG   C  24.88 . 1 
       121 .  18 LEU CD1  C  25.43 . 1 
       122 .  18 LEU CD2  C  19.92 . 1 
       123 .  18 LEU N    N 120.54 . 1 
       124 .  19 LYS H    H   8.56 . 1 
       125 .  19 LYS HA   H   3.68 . 1 
       126 .  19 LYS HB2  H   1.36 . 1 
       127 .  19 LYS HB3  H   1.73 . 1 
       128 .  19 LYS HG3  H   1.28 . 1 
       129 .  19 LYS HD3  H   1.58 . 1 
       130 .  19 LYS HE3  H   2.92 . 1 
       131 .  19 LYS CA   C  60.12 . 1 
       132 .  19 LYS CB   C  32.59 . 1 
       133 .  19 LYS CG   C  24.88 . 1 
       134 .  19 LYS CD   C  29.84 . 1 
       135 .  19 LYS CE   C  41.96 . 1 
       136 .  19 LYS N    N 118.57 . 1 
       137 .  20 SER H    H   7.54 . 1 
       138 .  20 SER HA   H   4.28 . 1 
       139 .  20 SER HB3  H   4.06 . 1 
       140 .  20 SER CA   C  61.23 . 1 
       141 .  20 SER CB   C  63.88 . 1 
       142 .  20 SER N    N 113.16 . 1 
       143 .  21 ILE H    H   7.95 . 1 
       144 .  21 ILE HA   H   3.79 . 1 
       145 .  21 ILE HB   H   1.88 . 1 
       146 .  21 ILE HG12 H   1.05 . 1 
       147 .  21 ILE HG13 H   1.75 . 1 
       148 .  21 ILE HG2  H   1.00 . 1 
       149 .  21 ILE HD1  H   0.62 . 1 
       150 .  21 ILE CA   C  65.08 . 1 
       151 .  21 ILE CB   C  38.09 . 1 
       152 .  21 ILE CG1  C  28.73 . 1 
       153 .  21 ILE CG2  C  17.17 . 1 
       154 .  21 ILE CD1  C  13.86 . 1 
       155 .  21 ILE N    N 120.70 . 1 
       156 .  22 LEU H    H   8.84 . 1 
       157 .  22 LEU HA   H   4.09 . 1 
       158 .  22 LEU HB2  H   1.70 . 1 
       159 .  22 LEU HB3  H   2.09 . 1 
       160 .  22 LEU HG   H   1.76 . 1 
       161 .  22 LEU HD1  H   1.06 . 1 
       162 .  22 LEU HD2  H   0.98 . 1 
       163 .  22 LEU CA   C  58.47 . 1 
       164 .  22 LEU CB   C  41.95 . 1 
       165 .  22 LEU CG   C  27.33 . 1 
       166 .  22 LEU CD1  C  26.53 . 1 
       167 .  22 LEU CD2  C  23.78 . 1 
       168 .  22 LEU N    N 119.88 . 1 
       169 .  23 GLN H    H   8.51 . 1 
       170 .  23 GLN HA   H   4.03 . 1 
       171 .  23 GLN HB2  H   2.26 . 1 
       172 .  23 GLN HB3  H   2.33 . 1 
       173 .  23 GLN HG2  H   2.46 . 1 
       174 .  23 GLN HG3  H   2.54 . 1 
       175 .  23 GLN CA   C  59.02 . 1 
       176 .  23 GLN CB   C  28.18 . 1 
       177 .  23 GLN CG   C  34.24 . 1 
       178 .  23 GLN N    N 117.26 . 1 
       179 .  24 GLN H    H   8.03 . 1 
       180 .  24 GLN HA   H   4.20 . 1 
       181 .  24 GLN HB2  H   2.47 . 1 
       182 .  24 GLN HB3  H   2.48 . 1 
       183 .  24 GLN HG2  H   2.47 . 1 
       184 .  24 GLN HG3  H   2.84 . 1 
       185 .  24 GLN HE21 H   6.92 . 1 
       186 .  24 GLN HE22 H   7.02 . 1 
       187 .  24 GLN CA   C  59.57 . 1 
       188 .  24 GLN CB   C  29.84 . 1 
       189 .  24 GLN CG   C  35.34 . 1 
       190 .  24 GLN N    N 118.90 . 1 
       191 .  24 GLN NE2  N 110.37 . 1 
       192 .  25 VAL H    H   8.53 . 1 
       193 .  25 VAL HA   H   3.84 . 1 
       194 .  25 VAL HB   H   2.38 . 1 
       195 .  25 VAL HG1  H   1.18 . 1 
       196 .  25 VAL HG2  H   1.03 . 1 
       197 .  25 VAL CA   C  67.83 . 1 
       198 .  25 VAL CB   C  32.03 . 1 
       199 .  25 VAL CG1  C  23.33 . 1 
       200 .  25 VAL CG2  C  22.12 . 1 
       201 .  25 VAL N    N 119.72 . 1 
       202 .  26 LYS H    H   8.57 . 1 
       203 .  26 LYS HA   H   3.89 . 1 
       204 .  26 LYS HB3  H   1.87 . 1 
       205 .  26 LYS HG3  H   1.02 . 1 
       206 .  26 LYS HD3  H   1.52 . 1 
       207 .  26 LYS CA   C  59.57 . 1 
       208 .  26 LYS CB   C  32.38 . 1 
       209 .  26 LYS N    N 114.63 . 1 
       210 .  27 SER H    H   7.56 . 1 
       211 .  27 SER HA   H   4.45 . 1 
       212 .  27 SER HB3  H   4.00 . 1 
       213 .  27 SER CA   C  59.02 . 1 
       214 .  27 SER CB   C  63.98 . 1 
       215 .  27 SER N    N 110.37 . 1 
       216 .  28 HIS H    H   7.54 . 1 
       217 .  28 HIS HA   H   3.97 . 1 
       218 .  28 HIS HB2  H   2.80 . 1 
       219 .  28 HIS HB3  H   2.99 . 1 
       220 .  28 HIS HD2  H   4.98 . 1 
       221 .  28 HIS HE1  H   7.52 . 1 
       222 .  28 HIS CA   C  58.47 . 1 
       223 .  28 HIS CB   C  32.59 . 1 
       224 .  28 HIS CD2  C 118.93 . 1 
       225 .  28 HIS CE1  C 138.75 . 1 
       226 .  28 HIS N    N 125.62 . 1 
       227 .  29 GLN H    H   8.54 . 1 
       228 .  29 GLN HA   H   4.21 . 1 
       229 .  29 GLN HB3  H   2.11 . 1 
       230 .  29 GLN HG3  H   2.39 . 1 
       231 .  29 GLN HE21 H   6.87 . 1 
       232 .  29 GLN HE22 H   7.58 . 1 
       233 .  29 GLN CA   C  59.12 . 1 
       234 .  29 GLN CB   C  29.83 . 1 
       235 .  29 GLN CG   C  33.69 . 1 
       236 .  29 GLN N    N 128.57 . 1 
       237 .  29 GLN NE2  N 112.17 . 1 
       238 .  30 SER H    H  11.67 . 1 
       239 .  30 SER HA   H   4.84 . 1 
       240 .  30 SER HB2  H   3.93 . 1 
       241 .  30 SER HB3  H   4.33 . 1 
       242 .  30 SER CA   C  60.12 . 1 
       243 .  30 SER CB   C  63.98 . 1 
       244 .  30 SER N    N 119.06 . 1 
       245 .  31 ALA H    H   7.87 . 1 
       246 .  31 ALA HA   H   4.40 . 1 
       247 .  31 ALA HB   H   1.69 . 1 
       248 .  31 ALA CA   C  53.51 . 1 
       249 .  31 ALA CB   C  20.47 . 1 
       250 .  31 ALA N    N 117.58 . 1 
       251 .  32 TRP H    H   7.13 . 1 
       252 .  32 TRP HA   H   4.37 . 1 
       253 .  32 TRP HB2  H   3.35 . 1 
       254 .  32 TRP HB3  H   3.59 . 1 
       255 .  32 TRP HD1  H   7.90 . 1 
       256 .  32 TRP HE1  H  10.47 . 1 
       257 .  32 TRP HE3  H   7.34 . 1 
       258 .  32 TRP HZ2  H   7.38 . 1 
       259 .  32 TRP HZ3  H   7.20 . 1 
       260 .  32 TRP HH2  H   7.15 . 1 
       261 .  32 TRP CA   C  60.69 . 1 
       262 .  32 TRP CB   C  27.63 . 1 
       263 .  32 TRP CD1  C 128.84 . 1 
       264 .  32 TRP CE3  C 122.23 . 1 
       265 .  32 TRP CZ2  C 116.18 . 1 
       266 .  32 TRP CZ3  C 123.34 . 1 
       267 .  32 TRP CH2  C 126.09 . 1 
       268 .  32 TRP N    N 116.60 . 1 
       269 .  32 TRP NE1  N 131.86 . 1 
       270 .  33 PRO HA   H   3.76 . 1 
       271 .  33 PRO HB2  H  -0.78 . 1 
       272 .  33 PRO HB3  H   0.49 . 1 
       273 .  33 PRO HG2  H  -0.93 . 1 
       274 .  33 PRO HG3  H   0.23 . 1 
       275 .  33 PRO HD2  H   1.57 . 1 
       276 .  33 PRO HD3  H   2.18 . 1 
       277 .  33 PRO CA   C  64.53 . 1 
       278 .  33 PRO CB   C  29.84 . 1 
       279 .  33 PRO CG   C  26.53 . 1 
       280 .  33 PRO CD   C  50.21 . 1 
       281 .  34 PHE H    H   7.58 . 1 
       282 .  34 PHE HA   H   4.93 . 1 
       283 .  34 PHE HB2  H   2.53 . 1 
       284 .  34 PHE HB3  H   3.49 . 1 
       285 .  34 PHE HD1  H   7.10 . 3 
       286 .  34 PHE HE1  H   7.17 . 3 
       287 .  34 PHE HZ   H   7.30 . 1 
       288 .  34 PHE CA   C  55.72 . 1 
       289 .  34 PHE CB   C  39.20 . 1 
       290 .  34 PHE CD1  C 133.25 . 3 
       291 .  34 PHE N    N 113.32 . 1 
       292 .  35 MET H    H   7.12 . 1 
       293 .  35 MET HA   H   4.29 . 1 
       294 .  35 MET HB2  H   2.17 . 1 
       295 .  35 MET HB3  H   2.23 . 1 
       296 .  35 MET HG3  H   2.85 . 1 
       297 .  35 MET HE   H   2.17 . 1 
       298 .  35 MET CA   C  56.82 . 1 
       299 .  35 MET CB   C  32.59 . 1 
       300 .  35 MET CG   C  33.14 . 1 
       301 .  35 MET CE   C  17.17 . 1 
       302 .  35 MET N    N 117.75 . 1 
       303 .  36 GLU H    H   7.71 . 1 
       304 .  36 GLU HA   H   4.85 . 1 
       305 .  36 GLU HB2  H   1.73 . 1 
       306 .  36 GLU HB3  H   2.09 . 1 
       307 .  36 GLU HG3  H   2.16 . 1 
       308 .  36 GLU CA   C  53.52 . 1 
       309 .  36 GLU CB   C  31.49 . 1 
       310 .  36 GLU CG   C  35.89 . 1 
       311 .  36 GLU N    N 113.81 . 1 
       312 .  37 PRO HA   H   4.24 . 1 
       313 .  37 PRO HB2  H   1.68 . 1 
       314 .  37 PRO HB3  H   2.33 . 1 
       315 .  37 PRO HG2  H   1.98 . 1 
       316 .  37 PRO HG3  H   2.13 . 1 
       317 .  37 PRO HD3  H   3.67 . 1 
       318 .  37 PRO CA   C  62.88 . 1 
       319 .  37 PRO CB   C  32.04 . 1 
       320 .  37 PRO CG   C  27.08 . 1 
       321 .  37 PRO CD   C  50.76 . 1 
       322 .  38 VAL H    H   8.12 . 1 
       323 .  38 VAL HA   H   3.55 . 1 
       324 .  38 VAL HB   H   1.15 . 1 
       325 .  38 VAL HG1  H   0.46 . 1 
       326 .  38 VAL HG2  H   0.17 . 1 
       327 .  38 VAL CA   C  63.43 . 1 
       328 .  38 VAL CB   C  32.58 . 1 
       329 .  38 VAL CG1  C  21.57 . 1 
       330 .  38 VAL CG2  C  21.57 . 1 
       331 .  38 VAL N    N 124.45 . 1 
       332 .  39 LYS H    H   9.04 . 1 
       333 .  39 LYS HA   H   4.37 . 1 
       334 .  39 LYS HB3  H   1.87 . 1 
       335 .  39 LYS HG3  H   1.44 . 1 
       336 .  39 LYS HD3  H   1.67 . 1 
       337 .  39 LYS HE3  H   2.98 . 1 
       338 .  39 LYS CA   C  56.31 . 1 
       339 .  39 LYS CB   C  32.88 . 1 
       340 .  39 LYS N    N 129.88 . 1 
       341 .  40 ARG H    H   8.05 . 1 
       342 .  40 ARG N    N 120.21 . 1 
       343 .  41 THR HA   H   4.04 . 1 
       344 .  41 THR HB   H   4.29 . 1 
       345 .  41 THR HG2  H   1.27 . 1 
       346 .  41 THR CA   C  63.43 . 1 
       347 .  41 THR CB   C  68.38 . 1 
       348 .  41 THR CG2  C  22.67 . 1 
       349 .  42 GLU H    H   7.21 . 1 
       350 .  42 GLU HA   H   4.45 . 1 
       351 .  42 GLU HB2  H   2.00 . 1 
       352 .  42 GLU HB3  H   2.17 . 1 
       353 .  42 GLU HG3  H   2.29 . 1 
       354 .  42 GLU CA   C  56.27 . 1 
       355 .  42 GLU CB   C  30.93 . 1 
       356 .  42 GLU CG   C  36.44 . 1 
       357 .  42 GLU N    N 118.73 . 1 
       358 .  43 ALA H    H   7.38 . 1 
       359 .  43 ALA HA   H   4.94 . 1 
       360 .  43 ALA HB   H   1.08 . 1 
       361 .  43 ALA CA   C  50.22 . 1 
       362 .  43 ALA CB   C  19.37 . 1 
       363 .  43 ALA N    N 122.50 . 1 
       364 .  44 PRO HA   H   4.50 . 1 
       365 .  44 PRO HB2  H   2.03 . 1 
       366 .  44 PRO HB3  H   2.37 . 1 
       367 .  44 PRO HG2  H   2.04 . 1 
       368 .  44 PRO HG3  H   2.12 . 1 
       369 .  44 PRO HD2  H   3.52 . 1 
       370 .  44 PRO HD3  H   3.72 . 1 
       371 .  44 PRO CA   C  65.08 . 1 
       372 .  44 PRO CB   C  31.49 . 1 
       373 .  44 PRO CG   C  27.63 . 1 
       374 .  44 PRO CD   C  50.21 . 1 
       375 .  46 TYR H    H   7.95 . 1 
       376 .  46 TYR HA   H   3.54 . 1 
       377 .  46 TYR HB2  H   2.49 . 1 
       378 .  46 TYR HB3  H   2.69 . 1 
       379 .  46 TYR HD1  H   5.12 . 3 
       380 .  46 TYR HE1  H   6.07 . 3 
       381 .  46 TYR CA   C  62.33 . 1 
       382 .  46 TYR CB   C  39.75 . 1 
       383 .  46 TYR CD1  C 133.80 . 3 
       384 .  46 TYR CE1  C 118.38 . 3 
       385 .  46 TYR N    N 122.50 . 1 
       386 .  47 TYR H    H   8.22 . 1 
       387 .  47 TYR HA   H   4.10 . 1 
       388 .  47 TYR HB2  H   2.80 . 1 
       389 .  47 TYR HB3  H   3.19 . 1 
       390 .  47 TYR HD1  H   7.34 . 3 
       391 .  47 TYR HE1  H   6.65 . 3 
       392 .  47 TYR CA   C  60.68 . 1 
       393 .  47 TYR CB   C  37.55 . 1 
       394 .  47 TYR CD1  C 134.90 . 3 
       395 .  47 TYR CE1  C 118.93 . 3 
       396 .  47 TYR N    N 113.16 . 1 
       397 .  48 GLU H    H   7.70 . 1 
       398 .  48 GLU HA   H   4.21 . 1 
       399 .  48 GLU HB3  H   2.09 . 1 
       400 .  48 GLU HG2  H   2.27 . 1 
       401 .  48 GLU HG3  H   2.33 . 1 
       402 .  48 GLU CA   C  57.92 . 1 
       403 .  48 GLU CB   C  29.48 . 1 
       404 .  48 GLU CG   C  37.55 . 1 
       405 .  48 GLU N    N 117.91 . 1 
       406 .  49 VAL H    H   7.13 . 1 
       407 .  49 VAL HA   H   4.08 . 1 
       408 .  49 VAL HB   H   2.02 . 1 
       409 .  49 VAL HG1  H   1.04 . 1 
       410 .  49 VAL HG2  H   0.99 . 1 
       411 .  49 VAL CA   C  63.43 . 1 
       412 .  49 VAL CB   C  33.69 . 1 
       413 .  49 VAL CG1  C  21.02 . 1 
       414 .  49 VAL CG2  C  21.57 . 1 
       415 .  49 VAL N    N 115.45 . 1 
       416 .  50 ILE H    H   7.95 . 1 
       417 .  50 ILE HA   H   3.92 . 1 
       418 .  50 ILE HB   H   1.21 . 1 
       419 .  50 ILE HG12 H   0.22 . 1 
       420 .  50 ILE HG13 H   0.80 . 1 
       421 .  50 ILE HG2  H   0.38 . 1 
       422 .  50 ILE HD1  H   0.54 . 1 
       423 .  50 ILE CA   C  57.92 . 1 
       424 .  50 ILE CB   C  34.24 . 1 
       425 .  50 ILE CG1  C  24.88 . 1 
       426 .  50 ILE CG2  C  16.62 . 1 
       427 .  50 ILE CD1  C   9.46 . 1 
       428 .  50 ILE N    N 122.83 . 1 
       429 .  51 ARG H    H   7.75 . 1 
       430 .  51 ARG HA   H   3.88 . 1 
       431 .  51 ARG HB2  H   1.21 . 1 
       432 .  51 ARG HB3  H   1.39 . 1 
       433 .  51 ARG HG2  H   1.17 . 1 
       434 .  51 ARG HG3  H   1.32 . 1 
       435 .  51 ARG HD3  H   2.97 . 1 
       436 .  51 ARG CA   C  57.37 . 1 
       437 .  51 ARG CB   C  30.94 . 1 
       438 .  51 ARG CG   C  27.08 . 1 
       439 .  51 ARG CD   C  43.05 . 1 
       440 .  51 ARG N    N 125.29 . 1 
       441 .  52 SER H    H   8.39 . 1 
       442 .  52 SER HA   H   4.98 . 1 
       443 .  52 SER HB2  H   2.91 . 1 
       444 .  52 SER HB3  H   3.03 . 1 
       445 .  52 SER CA   C  54.62 . 1 
       446 .  52 SER CB   C  66.20 . 1 
       447 .  52 SER N    N 116.60 . 1 
       448 .  53 PRO HA   H   4.08 . 1 
       449 .  53 PRO HB3  H   2.21 . 1 
       450 .  53 PRO HG2  H   1.88 . 1 
       451 .  53 PRO HG3  H   2.18 . 1 
       452 .  53 PRO HD2  H   3.39 . 1 
       453 .  53 PRO HD3  H   3.62 . 1 
       454 .  53 PRO CA   C  63.43 . 1 
       455 .  53 PRO CB   C  32.59 . 1 
       456 .  53 PRO CG   C  28.18 . 1 
       457 .  53 PRO CD   C  50.76 . 1 
       458 .  54 MET H    H   8.43 . 1 
       459 .  54 MET HA   H   4.93 . 1 
       460 .  54 MET HB2  H   1.35 . 1 
       461 .  54 MET HB3  H   1.99 . 1 
       462 .  54 MET HG3  H   2.69 . 1 
       463 .  54 MET HE   H   1.93 . 1 
       464 .  54 MET CA   C  54.07 . 1 
       465 .  54 MET CB   C  31.49 . 1 
       466 .  54 MET CG   C  30.93 . 1 
       467 .  54 MET CE   C  14.41 . 1 
       468 .  54 MET N    N 119.06 . 1 
       469 .  55 ASP H    H   7.37 . 1 
       470 .  55 ASP HA   H   4.75 . 1 
       471 .  55 ASP HB3  H   2.37 . 1 
       472 .  55 ASP CA   C  53.52 . 1 
       473 .  55 ASP CB   C  44.15 . 1 
       474 .  55 ASP N    N 119.06 . 1 
       475 .  56 LEU H    H   9.05 . 1 
       476 .  56 LEU HA   H   4.04 . 1 
       477 .  56 LEU HB2  H   1.40 . 1 
       478 .  56 LEU HB3  H   2.10 . 1 
       479 .  56 LEU HG   H   1.71 . 1 
       480 .  56 LEU HD1  H   0.94 . 1 
       481 .  56 LEU HD2  H   0.63 . 1 
       482 .  56 LEU CA   C  57.92 . 1 
       483 .  56 LEU CB   C  41.40 . 1 
       484 .  56 LEU CG   C  27.08 . 1 
       485 .  56 LEU CD1  C  27.08 . 1 
       486 .  56 LEU CD2  C  22.68 . 1 
       487 .  56 LEU N    N 116.27 . 1 
       488 .  57 LYS H    H   8.74 . 1 
       489 .  57 LYS HA   H   4.20 . 1 
       490 .  57 LYS HB2  H   2.22 . 1 
       491 .  57 LYS HB3  H   2.33 . 1 
       492 .  57 LYS HG2  H   1.40 . 1 
       493 .  57 LYS HG3  H   1.48 . 1 
       494 .  57 LYS HD2  H   1.70 . 1 
       495 .  57 LYS HD3  H   1.79 . 1 
       496 .  57 LYS HE3  H   2.96 . 1 
       497 .  57 LYS CA   C  60.68 . 1 
       498 .  57 LYS CB   C  32.04 . 1 
       499 .  57 LYS CG   C  25.28 . 1 
       500 .  57 LYS CD   C  30.39 . 1 
       501 .  57 LYS CE   C  41.95 . 1 
       502 .  57 LYS N    N 128.08 . 1 
       503 .  58 THR H    H   9.45 . 1 
       504 .  58 THR HA   H   3.85 . 1 
       505 .  58 THR HB   H   4.09 . 1 
       506 .  58 THR HG2  H   1.06 . 1 
       507 .  58 THR CA   C  67.04 . 1 
       508 .  58 THR CB   C  67.83 . 1 
       509 .  58 THR CG2  C  22.12 . 1 
       510 .  58 THR N    N 122.18 . 1 
       511 .  59 MET H    H   7.88 . 1 
       512 .  59 MET HA   H   4.32 . 1 
       513 .  59 MET HB2  H   1.92 . 1 
       514 .  59 MET HB3  H   2.09 . 1 
       515 .  59 MET HG2  H   2.50 . 1 
       516 .  59 MET HG3  H   2.62 . 1 
       517 .  59 MET HE   H   1.24 . 1 
       518 .  59 MET CA   C  60.68 . 1 
       519 .  59 MET CB   C  33.34 . 1 
       520 .  59 MET CG   C  33.14 . 1 
       521 .  59 MET CE   C  16.62 . 1 
       522 .  59 MET N    N 117.91 . 1 
       523 .  60 SER H    H   7.96 . 1 
       524 .  60 SER HA   H   4.20 . 1 
       525 .  60 SER HB2  H   4.04 . 1 
       526 .  60 SER HB3  H   4.37 . 1 
       527 .  60 SER CA   C  62.88 . 1 
       528 .  60 SER CB   C  62.88 . 1 
       529 .  60 SER N    N 116.11 . 1 
       530 .  61 GLU H    H   8.15 . 1 
       531 .  61 GLU HA   H   4.04 . 1 
       532 .  61 GLU HB2  H   2.06 . 1 
       533 .  61 GLU HB3  H   2.25 . 1 
       534 .  61 GLU HG2  H   2.18 . 1 
       535 .  61 GLU HG3  H   2.35 . 1 
       536 .  61 GLU CA   C  59.57 . 1 
       537 .  61 GLU CB   C  29.28 . 1 
       538 .  61 GLU CG   C  36.44 . 1 
       539 .  61 GLU N    N 124.47 . 1 
       540 .  62 ARG H    H   8.39 . 1 
       541 .  62 ARG HA   H   3.87 . 1 
       542 .  62 ARG HB2  H   1.08 . 1 
       543 .  62 ARG HB3  H   2.05 . 1 
       544 .  62 ARG HG2  H   0.88 . 1 
       545 .  62 ARG HG3  H   1.72 . 1 
       546 .  62 ARG HD2  H   2.05 . 1 
       547 .  62 ARG HD3  H   2.58 . 1 
       548 .  62 ARG CA   C  60.68 . 1 
       549 .  62 ARG CB   C  30.39 . 1 
       550 .  62 ARG CG   C  29.28 . 1 
       551 .  62 ARG CD   C  44.15 . 1 
       552 .  62 ARG N    N 120.37 . 1 
       553 .  63 LEU H    H   8.86 . 1 
       554 .  63 LEU HA   H   4.69 . 1 
       555 .  63 LEU HB2  H   1.93 . 1 
       556 .  63 LEU HB3  H   2.29 . 1 
       557 .  63 LEU HG   H   1.83 . 1 
       558 .  63 LEU HD1  H   1.07 . 1 
       559 .  63 LEU HD2  H   0.87 . 1 
       560 .  63 LEU CA   C  58.47 . 1 
       561 .  63 LEU CB   C  42.62 . 1 
       562 .  63 LEU CG   C  27.08 . 1 
       563 .  63 LEU CD1  C  25.43 . 1 
       564 .  63 LEU CD2  C  27.08 . 1 
       565 .  63 LEU N    N 120.21 . 1 
       566 .  64 LYS H    H   7.96 . 1 
       567 .  64 LYS HA   H   4.33 . 1 
       568 .  64 LYS HB3  H   2.06 . 1 
       569 .  64 LYS HG3  H   1.60 . 1 
       570 .  64 LYS HD3  H   1.80 . 1 
       571 .  64 LYS HE3  H   2.99 . 1 
       572 .  64 LYS CA   C  59.57 . 1 
       573 .  64 LYS CB   C  32.59 . 1 
       574 .  64 LYS CG   C  24.88 . 1 
       575 .  64 LYS CD   C  29.84 . 1 
       576 .  64 LYS CE   C  41.95 . 1 
       577 .  64 LYS N    N 120.37 . 1 
       578 .  65 ASN H    H   7.95 . 1 
       579 .  65 ASN HA   H   4.77 . 1 
       580 .  65 ASN HB2  H   2.77 . 1 
       581 .  65 ASN HB3  H   3.02 . 1 
       582 .  65 ASN HD21 H   6.97 . 1 
       583 .  65 ASN HD22 H   7.60 . 1 
       584 .  65 ASN CA   C  53.51 . 1 
       585 .  65 ASN CB   C  38.09 . 1 
       586 .  65 ASN N    N 116.11 . 1 
       587 .  65 ASN ND2  N 112.67 . 1 
       588 .  66 ARG H    H   8.16 . 1 
       589 .  66 ARG HA   H   4.41 . 1 
       590 .  66 ARG HB2  H   2.02 . 1 
       591 .  66 ARG HB3  H   2.10 . 1 
       592 .  66 ARG HG2  H   1.53 . 1 
       593 .  66 ARG HG3  H   1.54 . 1 
       594 .  66 ARG HD2  H   3.02 . 1 
       595 .  66 ARG HD3  H   3.06 . 1 
       596 .  66 ARG CA   C  56.82 . 1 
       597 .  66 ARG CB   C  25.43 . 1 
       598 .  66 ARG CG   C  27.63 . 1 
       599 .  66 ARG CD   C  43.05 . 1 
       600 .  66 ARG N    N 114.14 . 1 
       601 .  67 TYR H    H   8.22 . 1 
       602 .  67 TYR HA   H   4.06 . 1 
       603 .  67 TYR HB2  H   2.06 . 1 
       604 .  67 TYR HB3  H   2.95 . 1 
       605 .  67 TYR HD1  H   6.29 . 3 
       606 .  67 TYR HE1  H   6.71 . 3 
       607 .  67 TYR CA   C  60.12 . 1 
       608 .  67 TYR CB   C  40.85 . 1 
       609 .  67 TYR CD1  C 134.35 . 3 
       610 .  67 TYR CE1  C 118.93 . 3 
       611 .  67 TYR N    N 116.76 . 1 
       612 .  68 TYR H    H   8.01 . 1 
       613 .  68 TYR HA   H   4.53 . 1 
       614 .  68 TYR HB2  H   2.91 . 1 
       615 .  68 TYR HB3  H   3.06 . 1 
       616 .  68 TYR HD1  H   7.17 . 3 
       617 .  68 TYR HE1  H   7.29 . 3 
       618 .  68 TYR CA   C  57.92 . 1 
       619 .  68 TYR CB   C  36.44 . 1 
       620 .  68 TYR CD1  C 133.25 . 3 
       621 .  68 TYR CE1  C 120.58 . 3 
       622 .  68 TYR N    N 114.63 . 1 
       623 .  69 VAL H    H   7.70 . 1 
       624 .  69 VAL HA   H   4.08 . 1 
       625 .  69 VAL HB   H   2.32 . 1 
       626 .  69 VAL HG1  H   0.94 . 1 
       627 .  69 VAL HG2  H   0.82 . 1 
       628 .  69 VAL CA   C  62.33 . 1 
       629 .  69 VAL CB   C  31.50 . 1 
       630 .  69 VAL CG1  C  21.57 . 1 
       631 .  69 VAL CG2  C  18.82 . 1 
       632 .  69 VAL N    N 115.78 . 1 
       633 .  70 SER H    H   7.42 . 1 
       634 .  70 SER HA   H   4.74 . 1 
       635 .  70 SER HB2  H   3.75 . 1 
       636 .  70 SER HB3  H   4.20 . 1 
       637 .  70 SER CA   C  55.72 . 1 
       638 .  70 SER CB   C  66.18 . 1 
       639 .  70 SER N    N 111.35 . 1 
       640 .  71 LYS HA   H   4.02 . 1 
       641 .  71 LYS CA   C  59.03 . 1 
       642 .  71 LYS CB   C  31.59 . 1 
       643 .  72 LYS H    H   8.24 . 1 
       644 .  72 LYS HA   H   4.06 . 1 
       645 .  72 LYS HB3  H   1.78 . 1 
       646 .  72 LYS HD3  H   1.68 . 1 
       647 .  72 LYS HE2  H   3.04 . 1 
       648 .  72 LYS HE3  H   3.14 . 1 
       649 .  72 LYS CA   C  59.72 . 1 
       650 .  72 LYS CB   C  30.39 . 1 
       651 .  72 LYS CG   C  24.53 . 1 
       652 .  72 LYS CD   C  28.18 . 1 
       653 .  72 LYS CE   C  41.67 . 1 
       654 .  72 LYS N    N 120.21 . 1 
       655 .  73 LEU H    H   7.42 . 1 
       656 .  73 LEU HA   H   4.21 . 1 
       657 .  73 LEU HB2  H   1.89 . 1 
       658 .  73 LEU HB3  H   2.00 . 1 
       659 .  73 LEU HG   H   1.79 . 1 
       660 .  73 LEU HD1  H   0.92 . 1 
       661 .  73 LEU HD2  H   0.90 . 1 
       662 .  73 LEU CA   C  57.92 . 1 
       663 .  73 LEU CB   C  43.60 . 1 
       664 .  73 LEU CG   C  27.63 . 1 
       665 .  73 LEU CD1  C  25.98 . 1 
       666 .  73 LEU CD2  C  23.78 . 1 
       667 .  73 LEU N    N 118.73 . 1 
       668 .  74 PHE H    H   6.93 . 1 
       669 .  74 PHE HA   H   3.76 . 1 
       670 .  74 PHE HB2  H   2.38 . 1 
       671 .  74 PHE HB3  H   2.94 . 1 
       672 .  74 PHE HD1  H   6.40 . 3 
       673 .  74 PHE HE1  H   6.93 . 3 
       674 .  74 PHE CA   C  60.68 . 1 
       675 .  74 PHE CB   C  39.75 . 1 
       676 .  74 PHE CD1  C 133.80 . 3 
       677 .  74 PHE CE1  C 131.60 . 3 
       678 .  74 PHE N    N 118.73 . 1 
       679 .  75 MET H    H   8.49 . 1 
       680 .  75 MET HA   H   3.91 . 1 
       681 .  75 MET HB2  H   2.21 . 1 
       682 .  75 MET HB3  H   2.32 . 1 
       683 .  75 MET HG2  H   2.61 . 1 
       684 .  75 MET HG3  H   2.94 . 1 
       685 .  75 MET HE   H   2.03 . 1 
       686 .  75 MET CA   C  59.02 . 1 
       687 .  75 MET CB   C  32.59 . 1 
       688 .  75 MET CG   C  33.14 . 1 
       689 .  75 MET CE   C  17.17 . 1 
       690 .  75 MET N    N 116.27 . 1 
       691 .  76 ALA H    H   8.00 . 1 
       692 .  76 ALA HA   H   4.08 . 1 
       693 .  76 ALA HB   H   1.49 . 1 
       694 .  76 ALA CA   C  55.17 . 1 
       695 .  76 ALA CB   C  18.27 . 1 
       696 .  76 ALA N    N 119.72 . 1 
       697 .  77 ASP H    H   7.38 . 1 
       698 .  77 ASP HA   H   4.37 . 1 
       699 .  77 ASP HB3  H   2.73 . 1 
       700 .  77 ASP CA   C  57.37 . 1 
       701 .  77 ASP CB   C  38.65 . 1 
       702 .  77 ASP N    N 119.72 . 1 
       703 .  78 LEU H    H   7.36 . 1 
       704 .  78 LEU HA   H   3.40 . 1 
       705 .  78 LEU HB2  H   0.44 . 1 
       706 .  78 LEU HB3  H   0.76 . 1 
       707 .  78 LEU HG   H   0.71 . 1 
       708 .  78 LEU HD1  H   0.18 . 1 
       709 .  78 LEU HD2  H   0.06 . 1 
       710 .  78 LEU CA   C  57.92 . 1 
       711 .  78 LEU CB   C  40.30 . 1 
       712 .  78 LEU CG   C  27.63 . 1 
       713 .  78 LEU CD1  C  24.33 . 1 
       714 .  78 LEU CD2  C  25.98 . 1 
       715 .  78 LEU N    N 119.55 . 1 
       716 .  79 GLN H    H   8.07 . 1 
       717 .  79 GLN HA   H   3.80 . 1 
       718 .  79 GLN HB2  H   2.10 . 1 
       719 .  79 GLN HB3  H   2.16 . 1 
       720 .  79 GLN HG3  H   2.46 . 1 
       721 .  79 GLN HE21 H   7.22 . 1 
       722 .  79 GLN HE22 H   7.32 . 1 
       723 .  79 GLN CA   C  59.02 . 1 
       724 .  79 GLN CB   C  28.73 . 1 
       725 .  79 GLN CG   C  35.34 . 1 
       726 .  79 GLN N    N 114.14 . 1 
       727 .  79 GLN NE2  N 111.35 . 1 
       728 .  80 ARG H    H   7.38 . 1 
       729 .  80 ARG HA   H   4.08 . 1 
       730 .  80 ARG HB2  H   1.89 . 1 
       731 .  80 ARG HB3  H   1.97 . 1 
       732 .  80 ARG HG3  H   1.74 . 1 
       733 .  80 ARG HD2  H   3.33 . 1 
       734 .  80 ARG HD3  H   3.39 . 1 
       735 .  80 ARG CA   C  58.47 . 1 
       736 .  80 ARG CB   C  29.84 . 1 
       737 .  80 ARG CG   C  27.08 . 1 
       738 .  80 ARG CD   C  43.60 . 1 
       739 .  80 ARG N    N 118.57 . 1 
       740 .  81 VAL H    H   7.01 . 1 
       741 .  81 VAL HA   H   3.04 . 1 
       742 .  81 VAL HB   H   1.44 . 1 
       743 .  81 VAL HG1  H   0.48 . 1 
       744 .  81 VAL HG2  H   0.14 . 1 
       745 .  81 VAL CA   C  66.73 . 1 
       746 .  81 VAL CB   C  30.93 . 1 
       747 .  81 VAL CG1  C  22.12 . 1 
       748 .  81 VAL CG2  C  21.57 . 1 
       749 .  81 VAL N    N 117.91 . 1 
       750 .  82 PHE H    H   6.36 . 1 
       751 .  82 PHE HA   H   4.16 . 1 
       752 .  82 PHE HB2  H   2.94 . 1 
       753 .  82 PHE HB3  H   3.09 . 1 
       754 .  82 PHE HD1  H   6.64 . 3 
       755 .  82 PHE HE1  H   6.46 . 3 
       756 .  82 PHE HZ   H   6.41 . 1 
       757 .  82 PHE CA   C  58.47 . 1 
       758 .  82 PHE CB   C  38.10 . 1 
       759 .  82 PHE CD1  C 132.15 . 3 
       760 .  82 PHE CE1  C 131.60 . 3 
       761 .  82 PHE CZ   C 129.39 . 1 
       762 .  82 PHE N    N 116.93 . 1 
       763 .  83 THR H    H   9.05 . 1 
       764 .  83 THR HA   H   3.84 . 1 
       765 .  83 THR HB   H   4.21 . 1 
       766 .  83 THR HG2  H   1.30 . 1 
       767 .  83 THR CA   C  66.73 . 1 
       768 .  83 THR CB   C  68.38 . 1 
       769 .  83 THR CG2  C  22.12 . 1 
       770 .  83 THR N    N 115.29 . 1 
       771 .  84 ASN H    H   8.85 . 1 
       772 .  84 ASN HA   H   4.32 . 1 
       773 .  84 ASN HB2  H   2.66 . 1 
       774 .  84 ASN HB3  H   2.98 . 1 
       775 .  84 ASN CA   C  55.17 . 1 
       776 .  84 ASN CB   C  38.09 . 1 
       777 .  84 ASN N    N 120.70 . 1 
       778 .  85 CYS H    H   6.89 . 1 
       779 .  85 CYS HA   H   4.41 . 1 
       780 .  85 CYS HB2  H   3.03 . 1 
       781 .  85 CYS HB3  H   3.30 . 1 
       782 .  85 CYS CA   C  62.16 . 1 
       783 .  85 CYS CB   C  26.53 . 1 
       784 .  85 CYS N    N 116.93 . 1 
       785 .  86 LYS H    H   7.80 . 1 
       786 .  86 LYS HA   H   4.20 . 1 
       787 .  86 LYS HB3  H   1.74 . 1 
       788 .  86 LYS HG2  H   0.14 . 1 
       789 .  86 LYS HG3  H   1.31 . 1 
       790 .  86 LYS HD3  H   1.29 . 1 
       791 .  86 LYS HE2  H   2.42 . 1 
       792 .  86 LYS HE3  H   2.49 . 1 
       793 .  86 LYS CA   C  58.47 . 1 
       794 .  86 LYS CB   C  32.59 . 1 
       795 .  86 LYS CG   C  25.43 . 1 
       796 .  86 LYS CD   C  29.84 . 1 
       797 .  86 LYS CE   C  41.40 . 1 
       798 .  86 LYS N    N 116.76 . 1 
       799 .  87 GLU H    H   7.95 . 1 
       800 .  87 GLU HA   H   4.25 . 1 
       801 .  87 GLU HB2  H   2.00 . 1 
       802 .  87 GLU HB3  H   2.17 . 1 
       803 .  87 GLU HG2  H   2.20 . 1 
       804 .  87 GLU HG3  H   2.41 . 1 
       805 .  87 GLU CA   C  57.99 . 1 
       806 .  87 GLU CB   C  30.39 . 1 
       807 .  87 GLU CG   C  36.99 . 1 
       808 .  87 GLU N    N 117.91 . 1 
       809 .  88 TYR H    H   7.74 . 1 
       810 .  88 TYR HA   H   4.37 . 1 
       811 .  88 TYR HB3  H   2.93 . 1 
       812 .  88 TYR HD1  H   6.99 . 3 
       813 .  88 TYR HE1  H   6.82 . 3 
       814 .  88 TYR CA   C  60.68 . 1 
       815 .  88 TYR CB   C  41.40 . 1 
       816 .  88 TYR CD1  C 134.90 . 3 
       817 .  88 TYR CE1  C 119.48 . 3 
       818 .  88 TYR N    N 116.60 . 1 
       819 .  89 ASN H    H   8.24 . 1 
       820 .  89 ASN HA   H   5.02 . 1 
       821 .  89 ASN HB2  H   2.91 . 1 
       822 .  89 ASN HB3  H   3.07 . 1 
       823 .  89 ASN HD21 H   7.81 . 1 
       824 .  89 ASN HD22 H   8.32 . 1 
       825 .  89 ASN CA   C  51.86 . 1 
       826 .  89 ASN CB   C  40.85 . 1 
       827 .  89 ASN N    N 115.94 . 1 
       828 .  89 ASN ND2  N 118.73 . 1 
       829 .  91 PRO HA   H   2.42 . 1 
       830 .  91 PRO HB3  H   1.95 . 1 
       831 .  91 PRO HG2  H   1.56 . 1 
       832 .  91 PRO HG3  H   1.65 . 1 
       833 .  91 PRO HD2  H   3.60 . 1 
       834 .  91 PRO HD3  H   3.71 . 1 
       835 .  91 PRO CA   C  63.98 . 1 
       836 .  91 PRO CD   C  50.76 . 1 
       837 .  92 GLU H    H   8.25 . 1 
       838 .  92 GLU HA   H   4.18 . 1 
       839 .  92 GLU HB2  H   1.97 . 1 
       840 .  92 GLU HB3  H   2.10 . 1 
       841 .  92 GLU HG3  H   2.20 . 1 
       842 .  92 GLU CA   C  56.82 . 1 
       843 .  92 GLU CB   C  28.73 . 1 
       844 .  92 GLU CG   C  36.27 . 1 
       845 .  92 GLU N    N 112.99 . 1 
       846 .  93 SER H    H   8.11 . 1 
       847 .  93 SER HA   H   4.41 . 1 
       848 .  93 SER HB2  H   4.16 . 1 
       849 .  93 SER HB3  H   4.39 . 1 
       850 .  93 SER CA   C  58.47 . 1 
       851 .  93 SER CB   C  66.18 . 1 
       852 .  93 SER N    N 115.78 . 1 
       853 .  94 GLU H    H   9.06 . 1 
       854 .  94 GLU HA   H   4.23 . 1 
       855 .  94 GLU HB3  H   2.17 . 1 
       856 .  94 GLU HG3  H   2.53 . 1 
       857 .  94 GLU CA   C  59.57 . 1 
       858 .  94 GLU CB   C  29.84 . 1 
       859 .  94 GLU CG   C  36.44 . 1 
       860 .  94 GLU N    N 123.49 . 1 
       861 .  95 TYR H    H   8.07 . 1 
       862 .  95 TYR HA   H   3.83 . 1 
       863 .  95 TYR HB2  H   2.74 . 1 
       864 .  95 TYR HB3  H   3.02 . 1 
       865 .  95 TYR HD1  H   6.89 . 3 
       866 .  95 TYR HE1  H   7.01 . 3 
       867 .  95 TYR CA   C  60.12 . 1 
       868 .  95 TYR CB   C  37.55 . 1 
       869 .  95 TYR CD1  C 132.70 . 3 
       870 .  95 TYR CE1  C 120.03 . 3 
       871 .  95 TYR N    N 116.44 . 1 
       872 .  96 TYR H    H   7.36 . 1 
       873 .  96 TYR HA   H   3.82 . 1 
       874 .  96 TYR HB2  H   2.50 . 1 
       875 .  96 TYR HB3  H   3.39 . 1 
       876 .  96 TYR HD1  H   7.09 . 3 
       877 .  96 TYR HE1  H   7.00 . 3 
       878 .  96 TYR CA   C  61.78 . 1 
       879 .  96 TYR CB   C  40.30 . 1 
       880 .  96 TYR CD1  C 136.55 . 3 
       881 .  96 TYR CE1  C 119.48 . 3 
       882 .  96 TYR N    N 119.88 . 1 
       883 .  97 LYS H    H   8.07 . 1 
       884 .  97 LYS HA   H   4.20 . 1 
       885 .  97 LYS HB3  H   2.09 . 1 
       886 .  97 LYS HG2  H   1.58 . 1 
       887 .  97 LYS HG3  H   1.82 . 1 
       888 .  97 LYS HD3  H   1.81 . 1 
       889 .  97 LYS HE3  H   2.96 . 1 
       890 .  97 LYS CA   C  60.68 . 1 
       891 .  97 LYS CB   C  32.59 . 1 
       892 .  97 LYS CG   C  25.98 . 1 
       893 .  97 LYS CD   C  29.83 . 1 
       894 .  97 LYS CE   C  41.96 . 1 
       895 .  97 LYS N    N 118.08 . 1 
       896 .  98 CYS H    H   8.52 . 1 
       897 .  98 CYS HA   H   4.20 . 1 
       898 .  98 CYS HB2  H   3.06 . 1 
       899 .  98 CYS HB3  H   3.40 . 1 
       900 .  98 CYS CA   C  65.09 . 1 
       901 .  98 CYS CB   C  27.08 . 1 
       902 .  98 CYS N    N 116.76 . 1 
       903 .  99 ALA H    H   8.31 . 1 
       904 .  99 ALA HA   H   3.83 . 1 
       905 .  99 ALA HB   H   1.60 . 1 
       906 .  99 ALA CA   C  55.56 . 1 
       907 .  99 ALA CB   C  18.27 . 1 
       908 .  99 ALA N    N 120.70 . 1 
       909 . 100 ASN H    H   8.07 . 1 
       910 . 100 ASN HA   H   4.33 . 1 
       911 . 100 ASN HB2  H   2.83 . 1 
       912 . 100 ASN HB3  H   2.88 . 1 
       913 . 100 ASN CA   C  56.27 . 1 
       914 . 100 ASN CB   C  38.65 . 1 
       915 . 100 ASN N    N 115.45 . 1 
       916 . 101 ILE H    H   7.91 . 1 
       917 . 101 ILE HA   H   3.65 . 1 
       918 . 101 ILE HB   H   1.92 . 1 
       919 . 101 ILE HG12 H   1.20 . 1 
       920 . 101 ILE HG13 H   1.88 . 1 
       921 . 101 ILE HG2  H   1.02 . 1 
       922 . 101 ILE HD1  H   0.94 . 1 
       923 . 101 ILE CA   C  65.08 . 1 
       924 . 101 ILE CB   C  39.20 . 1 
       925 . 101 ILE CG1  C  29.28 . 1 
       926 . 101 ILE CG2  C  17.72 . 1 
       927 . 101 ILE CD1  C  13.86 . 1 
       928 . 101 ILE N    N 119.88 . 1 
       929 . 102 LEU H    H   8.56 . 1 
       930 . 102 LEU HA   H   3.67 . 1 
       931 . 102 LEU HB2  H   1.20 . 1 
       932 . 102 LEU HB3  H   1.41 . 1 
       933 . 102 LEU HG   H   1.58 . 1 
       934 . 102 LEU HD1  H   0.70 . 1 
       935 . 102 LEU HD2  H   0.70 . 1 
       936 . 102 LEU CA   C  56.82 . 1 
       937 . 102 LEU CB   C  41.95 . 1 
       938 . 102 LEU CG   C  26.53 . 1 
       939 . 102 LEU CD1  C  24.33 . 1 
       940 . 102 LEU CD2  C  25.43 . 1 
       941 . 102 LEU N    N 122.50 . 1 
       942 . 103 GLU H    H   8.07 . 1 
       943 . 103 GLU HA   H   3.19 . 1 
       944 . 103 GLU HB2  H   1.31 . 1 
       945 . 103 GLU HB3  H   1.72 . 1 
       946 . 103 GLU HG2  H   1.92 . 1 
       947 . 103 GLU HG3  H   2.00 . 1 
       948 . 103 GLU CA   C  60.12 . 1 
       949 . 103 GLU CB   C  29.84 . 1 
       950 . 103 GLU CG   C  37.55 . 1 
       951 . 103 GLU N    N 120.70 . 1 
       952 . 104 LYS H    H   7.14 . 1 
       953 . 104 LYS HA   H   4.08 . 1 
       954 . 104 LYS HB3  H   1.93 . 1 
       955 . 104 LYS HG3  H   1.49 . 1 
       956 . 104 LYS HD3  H   1.68 . 1 
       957 . 104 LYS HE3  H   2.96 . 1 
       958 . 104 LYS CA   C  59.69 . 1 
       959 . 104 LYS CB   C  32.59 . 1 
       960 . 104 LYS CG   C  25.64 . 1 
       961 . 104 LYS CD   C  29.28 . 1 
       962 . 104 LYS CE   C  41.96 . 1 
       963 . 104 LYS N    N 117.58 . 1 
       964 . 105 PHE H    H   7.87 . 1 
       965 . 105 PHE HA   H   4.33 . 1 
       966 . 105 PHE HB2  H   3.05 . 1 
       967 . 105 PHE HB3  H   3.13 . 1 
       968 . 105 PHE HD1  H   7.18 . 3 
       969 . 105 PHE CA   C  61.23 . 1 
       970 . 105 PHE CB   C  39.20 . 1 
       971 . 105 PHE CD1  C 133.80 . 3 
       972 . 105 PHE N    N 121.03 . 1 
       973 . 106 PHE H    H   9.13 . 1 
       974 . 106 PHE HA   H   3.96 . 1 
       975 . 106 PHE HB2  H   3.07 . 1 
       976 . 106 PHE HB3  H   3.29 . 1 
       977 . 106 PHE HD1  H   6.90 . 3 
       978 . 106 PHE HE1  H   7.01 . 3 
       979 . 106 PHE CA   C  60.69 . 1 
       980 . 106 PHE CB   C  38.64 . 1 
       981 . 106 PHE CD1  C 133.25 . 3 
       982 . 106 PHE CE1  C 132.70 . 3 
       983 . 106 PHE N    N 120.70 . 1 
       984 . 107 PHE H    H   8.36 . 1 
       985 . 107 PHE HA   H   3.84 . 1 
       986 . 107 PHE HB3  H   3.06 . 1 
       987 . 107 PHE HD1  H   7.17 . 3 
       988 . 107 PHE HE1  H   7.29 . 3 
       989 . 107 PHE HZ   H   7.43 . 1 
       990 . 107 PHE CA   C  61.77 . 1 
       991 . 107 PHE CB   C  38.09 . 1 
       992 . 107 PHE CD1  C 133.25 . 3 
       993 . 107 PHE CE1  C 132.70 . 3 
       994 . 107 PHE CZ   C 131.60 . 1 
       995 . 107 PHE N    N 118.08 . 1 
       996 . 108 SER H    H   7.91 . 1 
       997 . 108 SER HA   H   4.20 . 1 
       998 . 108 SER HB3  H   4.01 . 1 
       999 . 108 SER CA   C  61.77 . 1 
      1000 . 108 SER CB   C  62.88 . 1 
      1001 . 108 SER N    N 114.96 . 1 
      1002 . 109 LYS H    H   7.94 . 1 
      1003 . 109 LYS HA   H   4.01 . 1 
      1004 . 109 LYS HB2  H   1.57 . 1 
      1005 . 109 LYS HB3  H   1.73 . 1 
      1006 . 109 LYS HG3  H   0.83 . 1 
      1007 . 109 LYS HD3  H   1.40 . 1 
      1008 . 109 LYS HE2  H   2.42 . 1 
      1009 . 109 LYS HE3  H   2.57 . 1 
      1010 . 109 LYS CA   C  56.82 . 1 
      1011 . 109 LYS CB   C  31.49 . 1 
      1012 . 109 LYS CG   C  23.23 . 1 
      1013 . 109 LYS CD   C  27.08 . 1 
      1014 . 109 LYS CE   C  42.50 . 1 
      1015 . 109 LYS N    N 120.86 . 1 
      1016 . 110 ILE H    H   8.10 . 1 
      1017 . 110 ILE HA   H   3.82 . 1 
      1018 . 110 ILE HB   H   1.75 . 1 
      1019 . 110 ILE HG12 H   1.07 . 1 
      1020 . 110 ILE HG13 H   1.14 . 1 
      1021 . 110 ILE HG2  H   0.65 . 1 
      1022 . 110 ILE HD1  H   0.54 . 1 
      1023 . 110 ILE CA   C  64.53 . 1 
      1024 . 110 ILE CB   C  36.99 . 1 
      1025 . 110 ILE CG1  C  26.53 . 1 
      1026 . 110 ILE CG2  C  18.82 . 1 
      1027 . 110 ILE CD1  C  13.31 . 1 
      1028 . 110 ILE N    N 116.93 . 1 
      1029 . 111 LYS H    H   7.55 . 1 
      1030 . 111 LYS HA   H   4.04 . 1 
      1031 . 111 LYS HB2  H   1.76 . 1 
      1032 . 111 LYS HB3  H   1.88 . 1 
      1033 . 111 LYS HG2  H   1.30 . 1 
      1034 . 111 LYS HG3  H   1.39 . 1 
      1035 . 111 LYS HD3  H   1.63 . 1 
      1036 . 111 LYS HE3  H   2.91 . 1 
      1037 . 111 LYS CA   C  59.02 . 1 
      1038 . 111 LYS CB   C  32.36 . 1 
      1039 . 111 LYS CG   C  24.88 . 1 
      1040 . 111 LYS CD   C  29.28 . 1 
      1041 . 111 LYS CE   C  41.40 . 1 
      1042 . 111 LYS N    N 122.18 . 1 
      1043 . 112 GLU H    H   8.06 . 1 
      1044 . 112 GLU HA   H   4.00 . 1 
      1045 . 112 GLU HB3  H   2.06 . 1 
      1046 . 112 GLU HG2  H   2.21 . 1 
      1047 . 112 GLU HG3  H   2.34 . 1 
      1048 . 112 GLU CA   C  59.02 . 1 
      1049 . 112 GLU CB   C  29.83 . 1 
      1050 . 112 GLU CG   C  36.05 . 1 
      1051 . 112 GLU N    N 121.19 . 1 
      1052 . 113 ALA H    H   7.62 . 1 
      1053 . 113 ALA HA   H   4.29 . 1 
      1054 . 113 ALA HB   H   1.36 . 1 
      1055 . 113 ALA CA   C  52.41 . 1 
      1056 . 113 ALA CB   C  19.92 . 1 
      1057 . 113 ALA N    N 117.75 . 1 
      1058 . 114 GLY H    H   7.74 . 1 
      1059 . 114 GLY HA2  H   3.94 . 1 
      1060 . 114 GLY HA3  H   4.02 . 1 
      1061 . 114 GLY CA   C  45.90 . 1 
      1062 . 114 GLY N    N 105.85 . 1 
      1063 . 115 LEU H    H   7.74 . 1 
      1064 . 115 LEU HA   H   4.21 . 1 
      1065 . 115 LEU HB3  H   1.56 . 1 
      1066 . 115 LEU HG   H   1.54 . 1 
      1067 . 115 LEU HD1  H   0.71 . 1 
      1068 . 115 LEU CA   C  55.72 . 1 
      1069 . 115 LEU CB   C  43.05 . 1 
      1070 . 115 LEU CG   C  27.63 . 1 
      1071 . 115 LEU CD1  C  23.78 . 1 
      1072 . 115 LEU N    N 117.91 . 1 
      1073 . 116 ILE H    H   7.46 . 1 
      1074 . 116 ILE HA   H   4.23 . 1 
      1075 . 116 ILE HB   H   1.81 . 1 
      1076 . 116 ILE HG12 H   0.92 . 1 
      1077 . 116 ILE HG13 H   1.31 . 1 
      1078 . 116 ILE HG2  H   0.81 . 1 
      1079 . 116 ILE HD1  H   0.79 . 1 
      1080 . 116 ILE CA   C  60.68 . 1 
      1081 . 116 ILE CB   C  39.75 . 1 
      1082 . 116 ILE CG1  C  27.08 . 1 
      1083 . 116 ILE CG2  C  17.72 . 1 
      1084 . 116 ILE CD1  C  13.31 . 1 
      1085 . 116 ILE N    N 115.45 . 1 
      1086 . 117 ASP H    H   8.27 . 1 
      1087 . 117 ASP HA   H   4.57 . 1 
      1088 . 117 ASP HB2  H   2.54 . 1 
      1089 . 117 ASP HB3  H   2.69 . 1 
      1090 . 117 ASP CA   C  54.62 . 1 
      1091 . 117 ASP CB   C  41.40 . 1 
      1092 . 117 ASP N    N 123.49 . 1 
      1093 . 118 LYS H    H   7.77 . 1 
      1094 . 118 LYS HA   H   4.08 . 1 
      1095 . 118 LYS CA   C  57.72 . 1 
      1096 . 118 LYS CB   C  33.41 . 1 
      1097 . 118 LYS N    N 125.45 . 1 

   stop_

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