data_4664

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

save_entry_information
   _Entry.Sf_category                    entry_information
   _Entry.Sf_framecode                   entry_information
   _Entry.ID                             4664
   _Entry.Title                         
;
Sequence-Specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in 
v-myc-Transformed Avian Fibroblasts
;
   _Entry.Type                           .
   _Entry.Version_type                   original
   _Entry.Submission_date                2000-02-07
   _Entry.Accession_date                 2000-02-10
   _Entry.Last_release_date              .
   _Entry.Original_release_date          .
   _Entry.Origination                    author
   _Entry.NMR_STAR_version               3.1.1.61
   _Entry.Original_NMR_STAR_version      2.1
   _Entry.Experimental_method            NMR
   _Entry.Experimental_method_subtype    .
   _Entry.Details                        .
   _Entry.BMRB_internal_directory_name   .

   loop_
      _Entry_author.Ordinal
      _Entry_author.Given_name
      _Entry_author.Family_name
      _Entry_author.First_initial
      _Entry_author.Middle_initials
      _Entry_author.Family_title
      _Entry_author.Entry_ID

      1 Georg    Kontaxis . . . 4664 
      2 Theresia Matt     . . . 4664 
      3 Wolfgang Schuler  . . . 4664 
      4 Bernhard Krautler . . . 4664 
      5 Klaus    Bister   . . . 4664 
      6 Robert   Konrat   . . . 4664 

   stop_

   loop_
      _Data_set.Type
      _Data_set.Count
      _Data_set.Entry_ID

      assigned_chemical_shifts 1 4664 

   stop_

   loop_
      _Datum.Type
      _Datum.Count
      _Datum.Entry_ID

      '1H chemical shifts'  493 4664 
      '13C chemical shifts' 419 4664 
      '15N chemical shifts' 138 4664 

   stop_

   loop_
      _Release.Release_number
      _Release.Format_type
      _Release.Format_version
      _Release.Date
      _Release.Submission_date
      _Release.Type
      _Release.Author
      _Release.Detail
      _Release.Entry_ID

      1 . . 2001-07-05 . update   author 'residue 115 reassigned as a tyrosine' 4664 
      2 . . 2000-07-08 . original author 'original release date'                4664 

   stop_

save_


###############
#  Citations  #
###############

save_entry_citation
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 entry_citation
   _Citation.Entry_ID                     4664
   _Citation.ID                           1
   _Citation.Class                       'entry citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              20377250
   _Citation.DOI                          .
   _Citation.PubMed_ID                    .
   _Citation.Full_citation                .
   _Citation.Title                       
;
Sequence-specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in 
v-myc-transformed Avian Fibroblasts
;
   _Citation.Status                       published
   _Citation.Type                         journal
   _Citation.Journal_abbrev              'J. Biomol. NMR'
   _Citation.Journal_name_full           'Journal of Biomolecular NMR'
   _Citation.Journal_volume               17
   _Citation.Journal_issue                2
   _Citation.Journal_ASTM                 .
   _Citation.Journal_ISSN                 .
   _Citation.Journal_CSD                  .
   _Citation.Book_title                   .
   _Citation.Book_chapter_title           .
   _Citation.Book_volume                  .
   _Citation.Book_series                  .
   _Citation.Book_publisher               .
   _Citation.Book_publisher_city          .
   _Citation.Book_ISBN                    .
   _Citation.Conference_title             .
   _Citation.Conference_site              .
   _Citation.Conference_state_province    .
   _Citation.Conference_country           .
   _Citation.Conference_start_date        .
   _Citation.Conference_end_date          .
   _Citation.Conference_abstract_number   .
   _Citation.Thesis_institution           .
   _Citation.Thesis_institution_city      .
   _Citation.Thesis_institution_country   .
   _Citation.WWW_URL                      .
   _Citation.Page_first                   177
   _Citation.Page_last                    178
   _Citation.Year                         2000
   _Citation.Details                     'G. Kontaxis and T. Matt contributed equally'

   loop_
      _Citation_author.Ordinal
      _Citation_author.Given_name
      _Citation_author.Family_name
      _Citation_author.First_initial
      _Citation_author.Middle_initials
      _Citation_author.Family_title
      _Citation_author.Entry_ID
      _Citation_author.Citation_ID

      1 Georg    Kontaxis . . . 4664 1 
      2 Theresia Matt     . . . 4664 1 
      3 Wolfgang Schuler  . . . 4664 1 
      4 Bernhard Krautler . . . 4664 1 
      5 Klaus    Bister   . . . 4664 1 
      6 Robert   Konrat   . . . 4664 1 

   stop_

   loop_
      _Citation_keyword.Keyword
      _Citation_keyword.Entry_ID
      _Citation_keyword.Citation_ID

      'NMR assignments'    4664 1 
      'protein structure'  4664 1 
      'cell proliferation' 4664 1 
       oncogenes           4664 1 

   stop_

save_


save_ref-1
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 ref-1
   _Citation.Entry_ID                     4664
   _Citation.ID                           2
   _Citation.Class                       'reference citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              .
   _Citation.DOI                          .
   _Citation.PubMed_ID                    8361751
   _Citation.Full_citation               
;
Oncogene 1993 Sep;8(9):2317-24 
Suppression in transformed avian fibroblasts of a gene (crp) encoding a
cysteine-rich protein containing LIM domains.
Weiskirchen R, Bister K
;
   _Citation.Title                       'Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains.'
   _Citation.Status                       published
   _Citation.Type                         journal
   _Citation.Journal_abbrev               Oncogene
   _Citation.Journal_name_full            Oncogene
   _Citation.Journal_volume               8
   _Citation.Journal_issue                9
   _Citation.Journal_ASTM                 .
   _Citation.Journal_ISSN                 0950-9232
   _Citation.Journal_CSD                  .
   _Citation.Book_title                   .
   _Citation.Book_chapter_title           .
   _Citation.Book_volume                  .
   _Citation.Book_series                  .
   _Citation.Book_publisher               .
   _Citation.Book_publisher_city          .
   _Citation.Book_ISBN                    .
   _Citation.Conference_title             .
   _Citation.Conference_site              .
   _Citation.Conference_state_province    .
   _Citation.Conference_country           .
   _Citation.Conference_start_date        .
   _Citation.Conference_end_date          .
   _Citation.Conference_abstract_number   .
   _Citation.Thesis_institution           .
   _Citation.Thesis_institution_city      .
   _Citation.Thesis_institution_country   .
   _Citation.WWW_URL                      .
   _Citation.Page_first                   2317
   _Citation.Page_last                    2324
   _Citation.Year                         1993
   _Citation.Details                     
;
Using cDNA subtraction and differential hybridization techniques, a cDNA library
derived from normal quail embryo fibroblasts was screened for clones
corresponding to genes whose expression was suppressed in v-myc-transformed, as
compared with normal, quail embryo fibroblasts. One of the isolated cDNA clones
corresponded to a 0.9-kb mRNA that was present in normal quail and chicken
embryo fibroblasts, but was virtually absent from all transformed avian cells
tested: quail embryo fibroblasts transformed by the v-myc, v-myc/v-mil or v-src
oncogenes, cells derived from a methylcholanthrene-induced quail fibrosarcoma
or v-myc-transformed chicken macrophages. Nucleotide sequence analysis of the
original and supplementary cDNA clones indicated that the corresponding gene
encodes a 194 amino acid cysteine-rich protein (M(r) 20,911). A database search
revealed that the gene is the avian homolog of a human primary response gene
(crp) of unknown function. Both the quail and human CRP proteins contain two
copies of a cysteine-rich amino acid sequence motif (LIM) with putative
zinc-binding activity that was previously identified in several proteins with
presumed regulatory functions essential for cell growth or differentiation.
;

   loop_
      _Citation_author.Ordinal
      _Citation_author.Given_name
      _Citation_author.Family_name
      _Citation_author.First_initial
      _Citation_author.Middle_initials
      _Citation_author.Family_title
      _Citation_author.Entry_ID
      _Citation_author.Citation_ID

      1 R Weiskirchen R. . . 4664 2 
      2 K Bister      K. . . 4664 2 

   stop_

save_


save_ref-2
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 ref-2
   _Citation.Entry_ID                     4664
   _Citation.ID                           3
   _Citation.Class                       'reference citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              .
   _Citation.DOI                          .
   _Citation.PubMed_ID                    8520220
   _Citation.Full_citation               
;
J Biomol NMR 1995 Nov;6(3):277-93 
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A
;
   _Citation.Title                       'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
   _Citation.Status                       published
   _Citation.Type                         journal
   _Citation.Journal_abbrev              'J. Biomol. NMR'
   _Citation.Journal_name_full           'Journal of biomolecular NMR'
   _Citation.Journal_volume               6
   _Citation.Journal_issue                3
   _Citation.Journal_ASTM                 .
   _Citation.Journal_ISSN                 0925-2738
   _Citation.Journal_CSD                  .
   _Citation.Book_title                   .
   _Citation.Book_chapter_title           .
   _Citation.Book_volume                  .
   _Citation.Book_series                  .
   _Citation.Book_publisher               .
   _Citation.Book_publisher_city          .
   _Citation.Book_ISBN                    .
   _Citation.Conference_title             .
   _Citation.Conference_site              .
   _Citation.Conference_state_province    .
   _Citation.Conference_country           .
   _Citation.Conference_start_date        .
   _Citation.Conference_end_date          .
   _Citation.Conference_abstract_number   .
   _Citation.Thesis_institution           .
   _Citation.Thesis_institution_city      .
   _Citation.Thesis_institution_country   .
   _Citation.WWW_URL                      .
   _Citation.Page_first                   277
   _Citation.Page_last                    293
   _Citation.Year                         1995
   _Citation.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.
;

   loop_
      _Citation_author.Ordinal
      _Citation_author.Given_name
      _Citation_author.Family_name
      _Citation_author.First_initial
      _Citation_author.Middle_initials
      _Citation_author.Family_title
      _Citation_author.Entry_ID
      _Citation_author.Citation_ID

      1  F    Delaglio F. .  . 4664 3 
      2  S    Grzesiek S. .  . 4664 3 
      3 'G W' Vuister  G. W. . 4664 3 
      4  G    Zhu      G. .  . 4664 3 
      5  J    Pfeifer  J. .  . 4664 3 
      6  A    Bax      A. .  . 4664 3 

   stop_

save_


save_ref-3
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 ref-3
   _Citation.Entry_ID                     4664
   _Citation.ID                           4
   _Citation.Class                       'reference citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              .
   _Citation.DOI                          .
   _Citation.PubMed_ID                    .
   _Citation.Full_citation               'Kraulis, P.J., J. Magn. Reson. (1989) 24, 627-633'
   _Citation.Title                        .
   _Citation.Status                       .
   _Citation.Type                         .
   _Citation.Journal_abbrev               .
   _Citation.Journal_name_full            .
   _Citation.Journal_volume               .
   _Citation.Journal_issue                .
   _Citation.Journal_ASTM                 .
   _Citation.Journal_ISSN                 .
   _Citation.Journal_CSD                  .
   _Citation.Book_title                   .
   _Citation.Book_chapter_title           .
   _Citation.Book_volume                  .
   _Citation.Book_series                  .
   _Citation.Book_publisher               .
   _Citation.Book_publisher_city          .
   _Citation.Book_ISBN                    .
   _Citation.Conference_title             .
   _Citation.Conference_site              .
   _Citation.Conference_state_province    .
   _Citation.Conference_country           .
   _Citation.Conference_start_date        .
   _Citation.Conference_end_date          .
   _Citation.Conference_abstract_number   .
   _Citation.Thesis_institution           .
   _Citation.Thesis_institution_city      .
   _Citation.Thesis_institution_country   .
   _Citation.WWW_URL                      .
   _Citation.Page_first                   .
   _Citation.Page_last                    .
   _Citation.Year                         .
   _Citation.Details                      .

save_


#############################################
#  Molecular system (assembly) description  #
#############################################

save_system_Q83
   _Assembly.Sf_category                       assembly
   _Assembly.Sf_framecode                      system_Q83
   _Assembly.Entry_ID                          4664
   _Assembly.ID                                1
   _Assembly.Name                             'lipocalin Q83'
   _Assembly.BMRB_code                         .
   _Assembly.Number_of_components              .
   _Assembly.Organic_ligands                   .
   _Assembly.Metal_ions                        .
   _Assembly.Non_standard_bonds                .
   _Assembly.Ambiguous_conformational_states   .
   _Assembly.Ambiguous_chem_comp_sites         .
   _Assembly.Molecules_in_chemical_exchange    .
   _Assembly.Paramagnetic                      no
   _Assembly.Thiol_state                      'all disulfide bound'
   _Assembly.Molecular_mass                    .
   _Assembly.Enzyme_commission_number          .
   _Assembly.Details                           .
   _Assembly.DB_query_date                     .
   _Assembly.DB_query_revised_last_date        .

   loop_
      _Assembly_type.Type
      _Assembly_type.Entry_ID
      _Assembly_type.Assembly_ID

      monomer 4664 1 

   stop_

   loop_
      _Entity_assembly.ID
      _Entity_assembly.Entity_assembly_name
      _Entity_assembly.Entity_ID
      _Entity_assembly.Entity_label
      _Entity_assembly.Asym_ID
      _Entity_assembly.PDB_chain_ID
      _Entity_assembly.Experimental_data_reported
      _Entity_assembly.Physical_state
      _Entity_assembly.Conformational_isomer
      _Entity_assembly.Chemical_exchange_state
      _Entity_assembly.Magnetic_equivalence_group_code
      _Entity_assembly.Role
      _Entity_assembly.Details
      _Entity_assembly.Entry_ID
      _Entity_assembly.Assembly_ID

      1 Q83 1 $Q83 . . . native . . . . . 4664 1 

   stop_

   loop_
      _Bond.ID
      _Bond.Type
      _Bond.Value_order
      _Bond.Assembly_atom_ID_1
      _Bond.Entity_assembly_ID_1
      _Bond.Entity_assembly_name_1
      _Bond.Entity_ID_1
      _Bond.Comp_ID_1
      _Bond.Comp_index_ID_1
      _Bond.Seq_ID_1
      _Bond.Atom_ID_1
      _Bond.Assembly_atom_ID_2
      _Bond.Entity_assembly_ID_2
      _Bond.Entity_assembly_name_2
      _Bond.Entity_ID_2
      _Bond.Comp_ID_2
      _Bond.Comp_index_ID_2
      _Bond.Seq_ID_2
      _Bond.Atom_ID_2
      _Bond.Auth_entity_assembly_ID_1
      _Bond.Auth_entity_assembly_name_1
      _Bond.Auth_seq_ID_1
      _Bond.Auth_comp_ID_1
      _Bond.Auth_atom_ID_1
      _Bond.Auth_entity_assembly_ID_2
      _Bond.Auth_entity_assembly_name_2
      _Bond.Auth_seq_ID_2
      _Bond.Auth_comp_ID_2
      _Bond.Auth_atom_ID_2
      _Bond.Entry_ID
      _Bond.Assembly_ID

      1 disulfide single . 1 . . CYS 59 59 SG . 1 . 1 CYS 152 152 SG . . . . . . . . . . 4664 1 

   stop_

   loop_
      _Entity_deleted_atom.ID
      _Entity_deleted_atom.Entity_atom_list_ID
      _Entity_deleted_atom.Entity_assembly_ID
      _Entity_deleted_atom.Entity_ID
      _Entity_deleted_atom.Comp_ID
      _Entity_deleted_atom.Comp_index_ID
      _Entity_deleted_atom.Seq_ID
      _Entity_deleted_atom.Atom_ID
      _Entity_deleted_atom.Auth_entity_assembly_ID
      _Entity_deleted_atom.Auth_seq_ID
      _Entity_deleted_atom.Auth_comp_ID
      _Entity_deleted_atom.Auth_atom_ID
      _Entity_deleted_atom.Entry_ID
      _Entity_deleted_atom.Assembly_ID

      . 1 1 1 CYS  59  59 HG . . . . 4664 1 
      . 2 1 1 CYS 152 152 HG . . . . 4664 1 

   stop_

   loop_
      _Assembly_common_name.Name
      _Assembly_common_name.Type
      _Assembly_common_name.Entry_ID
      _Assembly_common_name.Assembly_ID

      'lipocalin Q83' system       4664 1 
       Q83            abbreviation 4664 1 

   stop_

save_


    ####################################
    #  Biological polymers and ligands #
    ####################################

save_Q83
   _Entity.Sf_category                       entity
   _Entity.Sf_framecode                      Q83
   _Entity.Entry_ID                          4664
   _Entity.ID                                1
   _Entity.BMRB_code                         .
   _Entity.Name                              Q83
   _Entity.Type                              polymer
   _Entity.Polymer_common_type               .
   _Entity.Polymer_type                      polypeptide(L)
   _Entity.Polymer_type_details              .
   _Entity.Polymer_strand_ID                 .
   _Entity.Polymer_seq_one_letter_code_can   .
   _Entity.Polymer_seq_one_letter_code      
;
MTVPDRSEIAGKWYVVALAS
NTEFFLREKDKMKMAMARIS
FLGEDELKVSYAVPKPNGCR
KWETTFKKTSDDGEVYYSEE
AKKKVEVLDTDYKSYAVIYA
TRVKDGRTLHMMRLYSRSPE
VSPAATAIFRKLAGERNYTD
EMVAMLPRQEECTVDEV
;
   _Entity.Target_identifier                 .
   _Entity.Polymer_author_defined_seq        .
   _Entity.Polymer_author_seq_details        .
   _Entity.Ambiguous_conformational_states   .
   _Entity.Ambiguous_chem_comp_sites         .
   _Entity.Nstd_monomer                      .
   _Entity.Nstd_chirality                    .
   _Entity.Nstd_linkage                      .
   _Entity.Nonpolymer_comp_ID                .
   _Entity.Nonpolymer_comp_label             .
   _Entity.Number_of_monomers                157
   _Entity.Number_of_nonpolymer_components   .
   _Entity.Paramagnetic                      .
   _Entity.Thiol_state                      'all disulfide bound'
   _Entity.Src_method                        .
   _Entity.Parent_entity_ID                  1
   _Entity.Fragment                          .
   _Entity.Mutation                          .
   _Entity.EC_number                         .
   _Entity.Calc_isoelectric_point            .
   _Entity.Formula_weight                    .
   _Entity.Formula_weight_exptl              .
   _Entity.Formula_weight_exptl_meth         .
   _Entity.Details                           .
   _Entity.DB_query_date                     .
   _Entity.DB_query_revised_last_date        2015-11-24

   loop_
      _Entity_db_link.Ordinal
      _Entity_db_link.Author_supplied
      _Entity_db_link.Database_code
      _Entity_db_link.Accession_code
      _Entity_db_link.Entry_mol_code
      _Entity_db_link.Entry_mol_name
      _Entity_db_link.Entry_experimental_method
      _Entity_db_link.Entry_structure_resolution
      _Entity_db_link.Entry_relation_type
      _Entity_db_link.Entry_details
      _Entity_db_link.Chimera_segment_ID
      _Entity_db_link.Seq_query_to_submitted_percent
      _Entity_db_link.Seq_subject_length
      _Entity_db_link.Seq_identity
      _Entity_db_link.Seq_positive
      _Entity_db_link.Seq_homology_expectation_val
      _Entity_db_link.Seq_align_begin
      _Entity_db_link.Seq_align_end
      _Entity_db_link.Seq_difference_details
      _Entity_db_link.Seq_alignment_details
      _Entity_db_link.Entry_ID
      _Entity_db_link.Entity_ID

      1 no BMRB    16682 .  Q83                                                                                                                              . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 
      2 no BMRB    17577 .  Q83                                                                                                                              . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 
      3 no PDB  1JZU      . "Cell Transformation By The Myc Oncogene Activates Expression Of A Lipocalin: Analysis Of The Gene (Q83) And Solution Structure " . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 
      4 no PDB  2KT4      . "Lipocalin Q83 Is A Siderocalin"                                                                                                  . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 
      5 no PDB  2LBV      . "Siderocalin Q83 Reveals A Dual Ligand Binding Mode"                                                                              . . . . . 100.00 157 100.00 100.00 2.31e-110 . . . . 4664 1 
      6 no GB   AAF35894  . "lipocalin Q83 [Coturnix coturnix]"                                                                                               . . . . .  99.36 178 100.00 100.00 7.26e-110 . . . . 4664 1 
      7 no GB   AAK31634  . "lipocalin Q83 [Coturnix coturnix]"                                                                                               . . . . .  99.36 178  99.36 100.00 3.14e-109 . . . . 4664 1 
      8 no SP   Q9I9P7    . "RecName: Full=Extracellular fatty acid-binding protein; Short=Ex-FABP; AltName: Full=Lipocalin Q83; Flags: Precursor"            . . . . .  99.36 178 100.00 100.00 7.26e-110 . . . . 4664 1 

   stop_

   loop_
      _Entity_common_name.Name
      _Entity_common_name.Type
      _Entity_common_name.Entry_ID
      _Entity_common_name.Entity_ID

      Q83 common       4664 1 
      Q83 abbreviation 4664 1 

   stop_

   loop_
      _Entity_comp_index.ID
      _Entity_comp_index.Auth_seq_ID
      _Entity_comp_index.Comp_ID
      _Entity_comp_index.Comp_label
      _Entity_comp_index.Entry_ID
      _Entity_comp_index.Entity_ID

        1 . MET . 4664 1 
        2 . THR . 4664 1 
        3 . VAL . 4664 1 
        4 . PRO . 4664 1 
        5 . ASP . 4664 1 
        6 . ARG . 4664 1 
        7 . SER . 4664 1 
        8 . GLU . 4664 1 
        9 . ILE . 4664 1 
       10 . ALA . 4664 1 
       11 . GLY . 4664 1 
       12 . LYS . 4664 1 
       13 . TRP . 4664 1 
       14 . TYR . 4664 1 
       15 . VAL . 4664 1 
       16 . VAL . 4664 1 
       17 . ALA . 4664 1 
       18 . LEU . 4664 1 
       19 . ALA . 4664 1 
       20 . SER . 4664 1 
       21 . ASN . 4664 1 
       22 . THR . 4664 1 
       23 . GLU . 4664 1 
       24 . PHE . 4664 1 
       25 . PHE . 4664 1 
       26 . LEU . 4664 1 
       27 . ARG . 4664 1 
       28 . GLU . 4664 1 
       29 . LYS . 4664 1 
       30 . ASP . 4664 1 
       31 . LYS . 4664 1 
       32 . MET . 4664 1 
       33 . LYS . 4664 1 
       34 . MET . 4664 1 
       35 . ALA . 4664 1 
       36 . MET . 4664 1 
       37 . ALA . 4664 1 
       38 . ARG . 4664 1 
       39 . ILE . 4664 1 
       40 . SER . 4664 1 
       41 . PHE . 4664 1 
       42 . LEU . 4664 1 
       43 . GLY . 4664 1 
       44 . GLU . 4664 1 
       45 . ASP . 4664 1 
       46 . GLU . 4664 1 
       47 . LEU . 4664 1 
       48 . LYS . 4664 1 
       49 . VAL . 4664 1 
       50 . SER . 4664 1 
       51 . TYR . 4664 1 
       52 . ALA . 4664 1 
       53 . VAL . 4664 1 
       54 . PRO . 4664 1 
       55 . LYS . 4664 1 
       56 . PRO . 4664 1 
       57 . ASN . 4664 1 
       58 . GLY . 4664 1 
       59 . CYS . 4664 1 
       60 . ARG . 4664 1 
       61 . LYS . 4664 1 
       62 . TRP . 4664 1 
       63 . GLU . 4664 1 
       64 . THR . 4664 1 
       65 . THR . 4664 1 
       66 . PHE . 4664 1 
       67 . LYS . 4664 1 
       68 . LYS . 4664 1 
       69 . THR . 4664 1 
       70 . SER . 4664 1 
       71 . ASP . 4664 1 
       72 . ASP . 4664 1 
       73 . GLY . 4664 1 
       74 . GLU . 4664 1 
       75 . VAL . 4664 1 
       76 . TYR . 4664 1 
       77 . TYR . 4664 1 
       78 . SER . 4664 1 
       79 . GLU . 4664 1 
       80 . GLU . 4664 1 
       81 . ALA . 4664 1 
       82 . LYS . 4664 1 
       83 . LYS . 4664 1 
       84 . LYS . 4664 1 
       85 . VAL . 4664 1 
       86 . GLU . 4664 1 
       87 . VAL . 4664 1 
       88 . LEU . 4664 1 
       89 . ASP . 4664 1 
       90 . THR . 4664 1 
       91 . ASP . 4664 1 
       92 . TYR . 4664 1 
       93 . LYS . 4664 1 
       94 . SER . 4664 1 
       95 . TYR . 4664 1 
       96 . ALA . 4664 1 
       97 . VAL . 4664 1 
       98 . ILE . 4664 1 
       99 . TYR . 4664 1 
      100 . ALA . 4664 1 
      101 . THR . 4664 1 
      102 . ARG . 4664 1 
      103 . VAL . 4664 1 
      104 . LYS . 4664 1 
      105 . ASP . 4664 1 
      106 . GLY . 4664 1 
      107 . ARG . 4664 1 
      108 . THR . 4664 1 
      109 . LEU . 4664 1 
      110 . HIS . 4664 1 
      111 . MET . 4664 1 
      112 . MET . 4664 1 
      113 . ARG . 4664 1 
      114 . LEU . 4664 1 
      115 . TYR . 4664 1 
      116 . SER . 4664 1 
      117 . ARG . 4664 1 
      118 . SER . 4664 1 
      119 . PRO . 4664 1 
      120 . GLU . 4664 1 
      121 . VAL . 4664 1 
      122 . SER . 4664 1 
      123 . PRO . 4664 1 
      124 . ALA . 4664 1 
      125 . ALA . 4664 1 
      126 . THR . 4664 1 
      127 . ALA . 4664 1 
      128 . ILE . 4664 1 
      129 . PHE . 4664 1 
      130 . ARG . 4664 1 
      131 . LYS . 4664 1 
      132 . LEU . 4664 1 
      133 . ALA . 4664 1 
      134 . GLY . 4664 1 
      135 . GLU . 4664 1 
      136 . ARG . 4664 1 
      137 . ASN . 4664 1 
      138 . TYR . 4664 1 
      139 . THR . 4664 1 
      140 . ASP . 4664 1 
      141 . GLU . 4664 1 
      142 . MET . 4664 1 
      143 . VAL . 4664 1 
      144 . ALA . 4664 1 
      145 . MET . 4664 1 
      146 . LEU . 4664 1 
      147 . PRO . 4664 1 
      148 . ARG . 4664 1 
      149 . GLN . 4664 1 
      150 . GLU . 4664 1 
      151 . GLU . 4664 1 
      152 . CYS . 4664 1 
      153 . THR . 4664 1 
      154 . VAL . 4664 1 
      155 . ASP . 4664 1 
      156 . GLU . 4664 1 
      157 . VAL . 4664 1 

   stop_

   loop_
      _Entity_poly_seq.Hetero
      _Entity_poly_seq.Mon_ID
      _Entity_poly_seq.Num
      _Entity_poly_seq.Comp_index_ID
      _Entity_poly_seq.Entry_ID
      _Entity_poly_seq.Entity_ID

      . MET   1   1 4664 1 
      . THR   2   2 4664 1 
      . VAL   3   3 4664 1 
      . PRO   4   4 4664 1 
      . ASP   5   5 4664 1 
      . ARG   6   6 4664 1 
      . SER   7   7 4664 1 
      . GLU   8   8 4664 1 
      . ILE   9   9 4664 1 
      . ALA  10  10 4664 1 
      . GLY  11  11 4664 1 
      . LYS  12  12 4664 1 
      . TRP  13  13 4664 1 
      . TYR  14  14 4664 1 
      . VAL  15  15 4664 1 
      . VAL  16  16 4664 1 
      . ALA  17  17 4664 1 
      . LEU  18  18 4664 1 
      . ALA  19  19 4664 1 
      . SER  20  20 4664 1 
      . ASN  21  21 4664 1 
      . THR  22  22 4664 1 
      . GLU  23  23 4664 1 
      . PHE  24  24 4664 1 
      . PHE  25  25 4664 1 
      . LEU  26  26 4664 1 
      . ARG  27  27 4664 1 
      . GLU  28  28 4664 1 
      . LYS  29  29 4664 1 
      . ASP  30  30 4664 1 
      . LYS  31  31 4664 1 
      . MET  32  32 4664 1 
      . LYS  33  33 4664 1 
      . MET  34  34 4664 1 
      . ALA  35  35 4664 1 
      . MET  36  36 4664 1 
      . ALA  37  37 4664 1 
      . ARG  38  38 4664 1 
      . ILE  39  39 4664 1 
      . SER  40  40 4664 1 
      . PHE  41  41 4664 1 
      . LEU  42  42 4664 1 
      . GLY  43  43 4664 1 
      . GLU  44  44 4664 1 
      . ASP  45  45 4664 1 
      . GLU  46  46 4664 1 
      . LEU  47  47 4664 1 
      . LYS  48  48 4664 1 
      . VAL  49  49 4664 1 
      . SER  50  50 4664 1 
      . TYR  51  51 4664 1 
      . ALA  52  52 4664 1 
      . VAL  53  53 4664 1 
      . PRO  54  54 4664 1 
      . LYS  55  55 4664 1 
      . PRO  56  56 4664 1 
      . ASN  57  57 4664 1 
      . GLY  58  58 4664 1 
      . CYS  59  59 4664 1 
      . ARG  60  60 4664 1 
      . LYS  61  61 4664 1 
      . TRP  62  62 4664 1 
      . GLU  63  63 4664 1 
      . THR  64  64 4664 1 
      . THR  65  65 4664 1 
      . PHE  66  66 4664 1 
      . LYS  67  67 4664 1 
      . LYS  68  68 4664 1 
      . THR  69  69 4664 1 
      . SER  70  70 4664 1 
      . ASP  71  71 4664 1 
      . ASP  72  72 4664 1 
      . GLY  73  73 4664 1 
      . GLU  74  74 4664 1 
      . VAL  75  75 4664 1 
      . TYR  76  76 4664 1 
      . TYR  77  77 4664 1 
      . SER  78  78 4664 1 
      . GLU  79  79 4664 1 
      . GLU  80  80 4664 1 
      . ALA  81  81 4664 1 
      . LYS  82  82 4664 1 
      . LYS  83  83 4664 1 
      . LYS  84  84 4664 1 
      . VAL  85  85 4664 1 
      . GLU  86  86 4664 1 
      . VAL  87  87 4664 1 
      . LEU  88  88 4664 1 
      . ASP  89  89 4664 1 
      . THR  90  90 4664 1 
      . ASP  91  91 4664 1 
      . TYR  92  92 4664 1 
      . LYS  93  93 4664 1 
      . SER  94  94 4664 1 
      . TYR  95  95 4664 1 
      . ALA  96  96 4664 1 
      . VAL  97  97 4664 1 
      . ILE  98  98 4664 1 
      . TYR  99  99 4664 1 
      . ALA 100 100 4664 1 
      . THR 101 101 4664 1 
      . ARG 102 102 4664 1 
      . VAL 103 103 4664 1 
      . LYS 104 104 4664 1 
      . ASP 105 105 4664 1 
      . GLY 106 106 4664 1 
      . ARG 107 107 4664 1 
      . THR 108 108 4664 1 
      . LEU 109 109 4664 1 
      . HIS 110 110 4664 1 
      . MET 111 111 4664 1 
      . MET 112 112 4664 1 
      . ARG 113 113 4664 1 
      . LEU 114 114 4664 1 
      . TYR 115 115 4664 1 
      . SER 116 116 4664 1 
      . ARG 117 117 4664 1 
      . SER 118 118 4664 1 
      . PRO 119 119 4664 1 
      . GLU 120 120 4664 1 
      . VAL 121 121 4664 1 
      . SER 122 122 4664 1 
      . PRO 123 123 4664 1 
      . ALA 124 124 4664 1 
      . ALA 125 125 4664 1 
      . THR 126 126 4664 1 
      . ALA 127 127 4664 1 
      . ILE 128 128 4664 1 
      . PHE 129 129 4664 1 
      . ARG 130 130 4664 1 
      . LYS 131 131 4664 1 
      . LEU 132 132 4664 1 
      . ALA 133 133 4664 1 
      . GLY 134 134 4664 1 
      . GLU 135 135 4664 1 
      . ARG 136 136 4664 1 
      . ASN 137 137 4664 1 
      . TYR 138 138 4664 1 
      . THR 139 139 4664 1 
      . ASP 140 140 4664 1 
      . GLU 141 141 4664 1 
      . MET 142 142 4664 1 
      . VAL 143 143 4664 1 
      . ALA 144 144 4664 1 
      . MET 145 145 4664 1 
      . LEU 146 146 4664 1 
      . PRO 147 147 4664 1 
      . ARG 148 148 4664 1 
      . GLN 149 149 4664 1 
      . GLU 150 150 4664 1 
      . GLU 151 151 4664 1 
      . CYS 152 152 4664 1 
      . THR 153 153 4664 1 
      . VAL 154 154 4664 1 
      . ASP 155 155 4664 1 
      . GLU 156 156 4664 1 
      . VAL 157 157 4664 1 

   stop_

save_


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

save_natural_source
   _Entity_natural_src_list.Sf_category    natural_source
   _Entity_natural_src_list.Sf_framecode   natural_source
   _Entity_natural_src_list.Entry_ID       4664
   _Entity_natural_src_list.ID             1

   loop_
      _Entity_natural_src.ID
      _Entity_natural_src.Entity_ID
      _Entity_natural_src.Entity_label
      _Entity_natural_src.Entity_chimera_segment_ID
      _Entity_natural_src.NCBI_taxonomy_ID
      _Entity_natural_src.Type
      _Entity_natural_src.Common
      _Entity_natural_src.Organism_name_scientific
      _Entity_natural_src.Organism_name_common
      _Entity_natural_src.Organism_acronym
      _Entity_natural_src.ICTVdb_decimal_code
      _Entity_natural_src.Superkingdom
      _Entity_natural_src.Kingdom
      _Entity_natural_src.Genus
      _Entity_natural_src.Species
      _Entity_natural_src.Strain
      _Entity_natural_src.Variant
      _Entity_natural_src.Subvariant
      _Entity_natural_src.Organ
      _Entity_natural_src.Tissue
      _Entity_natural_src.Tissue_fraction
      _Entity_natural_src.Cell_line
      _Entity_natural_src.Cell_type
      _Entity_natural_src.ATCC_number
      _Entity_natural_src.Organelle
      _Entity_natural_src.Cellular_location
      _Entity_natural_src.Fragment
      _Entity_natural_src.Fraction
      _Entity_natural_src.Secretion
      _Entity_natural_src.Plasmid
      _Entity_natural_src.Plasmid_details
      _Entity_natural_src.Gene_mnemonic
      _Entity_natural_src.Dev_stage
      _Entity_natural_src.Details
      _Entity_natural_src.Citation_ID
      _Entity_natural_src.Citation_label
      _Entity_natural_src.Entry_ID
      _Entity_natural_src.Entity_natural_src_list_ID

      1 1 $Q83 . 9091 organism . 'Coturnix coturnix' quail . . Eukaryota Metazoa Coturnix coturnix . . . . . . . . . . . . . . . . . . . . . 4664 1 

   stop_

save_


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

save_experimental_source
   _Entity_experimental_src_list.Sf_category    experimental_source
   _Entity_experimental_src_list.Sf_framecode   experimental_source
   _Entity_experimental_src_list.Entry_ID       4664
   _Entity_experimental_src_list.ID             1

   loop_
      _Entity_experimental_src.ID
      _Entity_experimental_src.Entity_ID
      _Entity_experimental_src.Entity_label
      _Entity_experimental_src.Entity_chimera_segment_ID
      _Entity_experimental_src.Production_method
      _Entity_experimental_src.Host_org_scientific_name
      _Entity_experimental_src.Host_org_name_common
      _Entity_experimental_src.Host_org_details
      _Entity_experimental_src.Host_org_NCBI_taxonomy_ID
      _Entity_experimental_src.Host_org_genus
      _Entity_experimental_src.Host_org_species
      _Entity_experimental_src.Host_org_strain
      _Entity_experimental_src.Host_org_variant
      _Entity_experimental_src.Host_org_subvariant
      _Entity_experimental_src.Host_org_organ
      _Entity_experimental_src.Host_org_tissue
      _Entity_experimental_src.Host_org_tissue_fraction
      _Entity_experimental_src.Host_org_cell_line
      _Entity_experimental_src.Host_org_cell_type
      _Entity_experimental_src.Host_org_cellular_location
      _Entity_experimental_src.Host_org_organelle
      _Entity_experimental_src.Host_org_gene
      _Entity_experimental_src.Host_org_culture_collection
      _Entity_experimental_src.Host_org_ATCC_number
      _Entity_experimental_src.Vector_type
      _Entity_experimental_src.PDBview_host_org_vector_name
      _Entity_experimental_src.PDBview_plasmid_name
      _Entity_experimental_src.Vector_name
      _Entity_experimental_src.Vector_details
      _Entity_experimental_src.Vendor_name
      _Entity_experimental_src.Host_org_dev_stage
      _Entity_experimental_src.Details
      _Entity_experimental_src.Citation_ID
      _Entity_experimental_src.Citation_label
      _Entity_experimental_src.Entry_ID
      _Entity_experimental_src.Entity_experimental_src_list_ID

      1 1 $Q83 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3)pLysS . . . . . . . . . . . . plasmid . . pET3d-Q83 . . . . . . 4664 1 

   stop_

save_


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

save_sample_1
   _Sample.Sf_category                      sample
   _Sample.Sf_framecode                     sample_1
   _Sample.Entry_ID                         4664
   _Sample.ID                               1
   _Sample.Type                             solution
   _Sample.Sub_type                         .
   _Sample.Details                          .
   _Sample.Aggregate_sample_number          .
   _Sample.Solvent_system                   .
   _Sample.Preparation_date                 .
   _Sample.Preparation_expiration_date      .
   _Sample.Polycrystallization_protocol     .
   _Sample.Single_crystal_protocol          .
   _Sample.Crystal_grow_apparatus           .
   _Sample.Crystal_grow_atmosphere          .
   _Sample.Crystal_grow_details             .
   _Sample.Crystal_grow_method              .
   _Sample.Crystal_grow_method_cit_ID       .
   _Sample.Crystal_grow_pH                  .
   _Sample.Crystal_grow_pH_range            .
   _Sample.Crystal_grow_pressure            .
   _Sample.Crystal_grow_pressure_esd        .
   _Sample.Crystal_grow_seeding             .
   _Sample.Crystal_grow_seeding_cit_ID      .
   _Sample.Crystal_grow_temp                .
   _Sample.Crystal_grow_temp_details        .
   _Sample.Crystal_grow_temp_esd            .
   _Sample.Crystal_grow_time                .
   _Sample.Oriented_sample_prep_protocol    .
   _Sample.Lyophilization_cryo_protectant   .
   _Sample.Storage_protocol                 .

   loop_
      _Sample_component.ID
      _Sample_component.Mol_common_name
      _Sample_component.Isotopic_labeling
      _Sample_component.Assembly_ID
      _Sample_component.Assembly_label
      _Sample_component.Entity_ID
      _Sample_component.Entity_label
      _Sample_component.Product_ID
      _Sample_component.Type
      _Sample_component.Concentration_val
      _Sample_component.Concentration_val_min
      _Sample_component.Concentration_val_max
      _Sample_component.Concentration_val_units
      _Sample_component.Concentration_val_err
      _Sample_component.Vendor
      _Sample_component.Vendor_product_name
      _Sample_component.Vendor_product_code
      _Sample_component.Entry_ID
      _Sample_component.Sample_ID

      1  Q83                  '[U-13C; U-15N]' . . 1 $Q83 . .  3.0 . . mM . . . . 4664 1 
      2 'potassium phosphate'  .               . .  .  .   . . 20   . . mM . . . . 4664 1 
      3 'potassium chloride'   .               . .  .  .   . . 50   . . mM . . . . 4664 1 
      4  dithiothreitol        .               . .  .  .   . .  0.5 . . mM . . . . 4664 1 

   stop_

save_


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

save_Ex-cond_1
   _Sample_condition_list.Sf_category    sample_conditions
   _Sample_condition_list.Sf_framecode   Ex-cond_1
   _Sample_condition_list.Entry_ID       4664
   _Sample_condition_list.ID             1
   _Sample_condition_list.Details        .

   loop_
      _Sample_condition_variable.Type
      _Sample_condition_variable.Val
      _Sample_condition_variable.Val_err
      _Sample_condition_variable.Val_units
      _Sample_condition_variable.Entry_ID
      _Sample_condition_variable.Sample_condition_list_ID

      pH            6.4 0.2 pH 4664 1 
      temperature 299   1   K  4664 1 

   stop_

save_


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

save_NMRPipe
   _Software.Sf_category    software
   _Software.Sf_framecode   NMRPipe
   _Software.Entry_ID       4664
   _Software.ID             1
   _Software.Name           NMRPipe
   _Software.Version        .
   _Software.Details        .

   loop_
      _Task.Task
      _Task.Entry_ID
      _Task.Software_ID

      'spectra processing' 4664 1 

   stop_

   loop_
      _Software_citation.Citation_ID
      _Software_citation.Citation_label
      _Software_citation.Entry_ID
      _Software_citation.Software_ID

      3 $ref-2 4664 1 

   stop_

save_


save_ANSIG
   _Software.Sf_category    software
   _Software.Sf_framecode   ANSIG
   _Software.Entry_ID       4664
   _Software.ID             2
   _Software.Name           ANSIG
   _Software.Version        .
   _Software.Details        .

   loop_
      _Task.Task
      _Task.Entry_ID
      _Task.Software_ID

      'spectra assignment and evaluation' 4664 2 

   stop_

   loop_
      _Software_citation.Citation_ID
      _Software_citation.Citation_label
      _Software_citation.Entry_ID
      _Software_citation.Software_ID

      4 $ref-3 4664 2 

   stop_

save_


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

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

save_spectrometer_1
   _NMR_spectrometer.Sf_category      NMR_spectrometer
   _NMR_spectrometer.Sf_framecode     spectrometer_1
   _NMR_spectrometer.Entry_ID         4664
   _NMR_spectrometer.ID               1
   _NMR_spectrometer.Details          .
   _NMR_spectrometer.Manufacturer     Varian
   _NMR_spectrometer.Model           'Unity Plus'
   _NMR_spectrometer.Serial_number    .
   _NMR_spectrometer.Field_strength   500

save_


save_spectrometer_list
   _NMR_spectrometer_list.Sf_category    NMR_spectrometer_list
   _NMR_spectrometer_list.Sf_framecode   spectrometer_list
   _NMR_spectrometer_list.Entry_ID       4664
   _NMR_spectrometer_list.ID             1

   loop_
      _NMR_spectrometer_view.ID
      _NMR_spectrometer_view.Name
      _NMR_spectrometer_view.Manufacturer
      _NMR_spectrometer_view.Model
      _NMR_spectrometer_view.Serial_number
      _NMR_spectrometer_view.Field_strength
      _NMR_spectrometer_view.Details
      _NMR_spectrometer_view.Citation_ID
      _NMR_spectrometer_view.Citation_label
      _NMR_spectrometer_view.Entry_ID
      _NMR_spectrometer_view.NMR_spectrometer_list_ID

      1 spectrometer_1 Varian 'Unity Plus' . 500 . . . 4664 1 

   stop_

save_


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

save_experiment_list
   _Experiment_list.Sf_category    experiment_list
   _Experiment_list.Sf_framecode   experiment_list
   _Experiment_list.Entry_ID       4664
   _Experiment_list.ID             1
   _Experiment_list.Details        .

   loop_
      _Experiment.ID
      _Experiment.Name
      _Experiment.Raw_data_flag
      _Experiment.NMR_spec_expt_ID
      _Experiment.NMR_spec_expt_label
      _Experiment.MS_expt_ID
      _Experiment.MS_expt_label
      _Experiment.SAXS_expt_ID
      _Experiment.SAXS_expt_label
      _Experiment.FRET_expt_ID
      _Experiment.FRET_expt_label
      _Experiment.EMR_expt_ID
      _Experiment.EMR_expt_label
      _Experiment.Sample_ID
      _Experiment.Sample_label
      _Experiment.Sample_state
      _Experiment.Sample_volume
      _Experiment.Sample_volume_units
      _Experiment.Sample_condition_list_ID
      _Experiment.Sample_condition_list_label
      _Experiment.Sample_spinning_rate
      _Experiment.Sample_angle
      _Experiment.NMR_tube_type
      _Experiment.NMR_spectrometer_ID
      _Experiment.NMR_spectrometer_label
      _Experiment.NMR_spectrometer_probe_ID
      _Experiment.NMR_spectrometer_probe_label
      _Experiment.NMR_spectral_processing_ID
      _Experiment.NMR_spectral_processing_label
      _Experiment.Mass_spectrometer_ID
      _Experiment.Mass_spectrometer_label
      _Experiment.Xray_instrument_ID
      _Experiment.Xray_instrument_label
      _Experiment.Fluorescence_instrument_ID
      _Experiment.Fluorescence_instrument_label
      _Experiment.EMR_instrument_ID
      _Experiment.EMR_instrument_label
      _Experiment.Chromatographic_system_ID
      _Experiment.Chromatographic_system_label
      _Experiment.Chromatographic_column_ID
      _Experiment.Chromatographic_column_label
      _Experiment.Entry_ID
      _Experiment.Experiment_list_ID

      1 '1H-15N HSQC'       . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      2  HNCO               . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      3  HNCA               . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      4  CBCA(CO)NNH        . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      5  HNCACB             . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      6  HCCH-TOCSY         . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      7 '1H-15N TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 
      8 '1H-15N NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4664 1 

   stop_

save_


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

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

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

save_chemical_shift_reference
   _Chem_shift_reference.Sf_category    chem_shift_reference
   _Chem_shift_reference.Sf_framecode   chemical_shift_reference
   _Chem_shift_reference.Entry_ID       4664
   _Chem_shift_reference.ID             1
   _Chem_shift_reference.Details        .

   loop_
      _Chem_shift_ref.Atom_type
      _Chem_shift_ref.Atom_isotope_number
      _Chem_shift_ref.Mol_common_name
      _Chem_shift_ref.Atom_group
      _Chem_shift_ref.Concentration_val
      _Chem_shift_ref.Concentration_units
      _Chem_shift_ref.Solvent
      _Chem_shift_ref.Rank
      _Chem_shift_ref.Chem_shift_units
      _Chem_shift_ref.Chem_shift_val
      _Chem_shift_ref.Ref_method
      _Chem_shift_ref.Ref_type
      _Chem_shift_ref.Indirect_shift_ratio
      _Chem_shift_ref.External_ref_loc
      _Chem_shift_ref.External_ref_sample_geometry
      _Chem_shift_ref.External_ref_axis
      _Chem_shift_ref.Indirect_shift_ratio_cit_ID
      _Chem_shift_ref.Indirect_shift_ratio_cit_label
      _Chem_shift_ref.Ref_correction_type
      _Chem_shift_ref.Correction_val
      _Chem_shift_ref.Correction_val_cit_ID
      _Chem_shift_ref.Correction_val_cit_label
      _Chem_shift_ref.Entry_ID
      _Chem_shift_ref.Chem_shift_reference_ID

      H  1 DSS 'methyl protons' . . . . ppm 0.0 internal direct   1.0         . . . . . . . . . 4664 1 
      N 15 DSS 'methyl protons' . . . . ppm 0.0 .        indirect 0.101329118 . . . . . . . . . 4664 1 
      C 13 DSS 'methyl protons' . . . . ppm 0.0 .        indirect 0.251449530 . . . . . . . . . 4664 1 

   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
   _Assigned_chem_shift_list.Sf_category                   assigned_chemical_shifts
   _Assigned_chem_shift_list.Sf_framecode                  shift_set_1
   _Assigned_chem_shift_list.Entry_ID                      4664
   _Assigned_chem_shift_list.ID                            1
   _Assigned_chem_shift_list.Sample_condition_list_ID      1
   _Assigned_chem_shift_list.Sample_condition_list_label  $Ex-cond_1
   _Assigned_chem_shift_list.Chem_shift_reference_ID       1
   _Assigned_chem_shift_list.Chem_shift_reference_label   $chemical_shift_reference
   _Assigned_chem_shift_list.Chem_shift_1H_err             .
   _Assigned_chem_shift_list.Chem_shift_13C_err            .
   _Assigned_chem_shift_list.Chem_shift_15N_err            .
   _Assigned_chem_shift_list.Chem_shift_31P_err            .
   _Assigned_chem_shift_list.Chem_shift_2H_err             .
   _Assigned_chem_shift_list.Chem_shift_19F_err            .
   _Assigned_chem_shift_list.Error_derivation_method       .
   _Assigned_chem_shift_list.Details                       .
   _Assigned_chem_shift_list.Text_data_format              .
   _Assigned_chem_shift_list.Text_data                     .

   loop_
      _Chem_shift_experiment.Experiment_ID
      _Chem_shift_experiment.Experiment_name
      _Chem_shift_experiment.Sample_ID
      _Chem_shift_experiment.Sample_label
      _Chem_shift_experiment.Sample_state
      _Chem_shift_experiment.Entry_ID
      _Chem_shift_experiment.Assigned_chem_shift_list_ID

      . . 1 $sample_1 . 4664 1 

   stop_

   loop_
      _Atom_chem_shift.ID
      _Atom_chem_shift.Assembly_atom_ID
      _Atom_chem_shift.Entity_assembly_ID
      _Atom_chem_shift.Entity_ID
      _Atom_chem_shift.Comp_index_ID
      _Atom_chem_shift.Seq_ID
      _Atom_chem_shift.Comp_ID
      _Atom_chem_shift.Atom_ID
      _Atom_chem_shift.Atom_type
      _Atom_chem_shift.Atom_isotope_number
      _Atom_chem_shift.Val
      _Atom_chem_shift.Val_err
      _Atom_chem_shift.Assign_fig_of_merit
      _Atom_chem_shift.Ambiguity_code
      _Atom_chem_shift.Occupancy
      _Atom_chem_shift.Resonance_ID
      _Atom_chem_shift.Auth_entity_assembly_ID
      _Atom_chem_shift.Auth_asym_ID
      _Atom_chem_shift.Auth_seq_ID
      _Atom_chem_shift.Auth_comp_ID
      _Atom_chem_shift.Auth_atom_ID
      _Atom_chem_shift.Details
      _Atom_chem_shift.Entry_ID
      _Atom_chem_shift.Assigned_chem_shift_list_ID

         1 . 1 1   4   4 PRO HA  H  1   4.12 0.03 . 1 . . . . . . . . 4664 1 
         2 . 1 1   4   4 PRO HB2 H  1   1.93 0.03 . 2 . . . . . . . . 4664 1 
         3 . 1 1   4   4 PRO HB3 H  1   1.54 0.03 . 2 . . . . . . . . 4664 1 
         4 . 1 1   4   4 PRO CA  C 13  64.12 0.50 . 1 . . . . . . . . 4664 1 
         5 . 1 1   4   4 PRO C   C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 
         6 . 1 1   4   4 PRO CB  C 13  33.08 0.50 . 1 . . . . . . . . 4664 1 
         7 . 1 1   5   5 ASP H   H  1   8.02 0.03 . 1 . . . . . . . . 4664 1 
         8 . 1 1   5   5 ASP HA  H  1   4.42 0.03 . 1 . . . . . . . . 4664 1 
         9 . 1 1   5   5 ASP HB2 H  1   2.67 0.03 . 2 . . . . . . . . 4664 1 
        10 . 1 1   5   5 ASP HB3 H  1   2.50 0.03 . 2 . . . . . . . . 4664 1 
        11 . 1 1   5   5 ASP CA  C 13  54.85 0.50 . 1 . . . . . . . . 4664 1 
        12 . 1 1   5   5 ASP C   C 13 178.28 0.50 . 1 . . . . . . . . 4664 1 
        13 . 1 1   5   5 ASP CB  C 13  42.58 0.50 . 1 . . . . . . . . 4664 1 
        14 . 1 1   5   5 ASP N   N 15 119.93 0.25 . 1 . . . . . . . . 4664 1 
        15 . 1 1   6   6 ARG H   H  1   8.53 0.03 . 1 . . . . . . . . 4664 1 
        16 . 1 1   6   6 ARG HA  H  1   4.04 0.03 . 1 . . . . . . . . 4664 1 
        17 . 1 1   6   6 ARG HB2 H  1   1.76 0.03 . 2 . . . . . . . . 4664 1 
        18 . 1 1   6   6 ARG HB3 H  1   1.72 0.03 . 2 . . . . . . . . 4664 1 
        19 . 1 1   6   6 ARG CA  C 13  59.37 0.50 . 1 . . . . . . . . 4664 1 
        20 . 1 1   6   6 ARG C   C 13 178.50 0.50 . 1 . . . . . . . . 4664 1 
        21 . 1 1   6   6 ARG CB  C 13  32.44 0.50 . 1 . . . . . . . . 4664 1 
        22 . 1 1   6   6 ARG N   N 15 125.15 0.25 . 1 . . . . . . . . 4664 1 
        23 . 1 1   7   7 SER H   H  1   8.32 0.03 . 1 . . . . . . . . 4664 1 
        24 . 1 1   7   7 SER HA  H  1   4.09 0.03 . 1 . . . . . . . . 4664 1 
        25 . 1 1   7   7 SER HB2 H  1   3.85 0.03 . 1 . . . . . . . . 4664 1 
        26 . 1 1   7   7 SER HB3 H  1   3.85 0.03 . 1 . . . . . . . . 4664 1 
        27 . 1 1   7   7 SER CA  C 13  62.36 0.50 . 1 . . . . . . . . 4664 1 
        28 . 1 1   7   7 SER C   C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 
        29 . 1 1   7   7 SER CB  C 13  63.83 0.50 . 1 . . . . . . . . 4664 1 
        30 . 1 1   7   7 SER N   N 15 115.20 0.25 . 1 . . . . . . . . 4664 1 
        31 . 1 1   8   8 GLU H   H  1   7.90 0.03 . 1 . . . . . . . . 4664 1 
        32 . 1 1   8   8 GLU HA  H  1   4.26 0.03 . 1 . . . . . . . . 4664 1 
        33 . 1 1   8   8 GLU HB2 H  1   2.22 0.03 . 2 . . . . . . . . 4664 1 
        34 . 1 1   8   8 GLU HB3 H  1   2.05 0.03 . 2 . . . . . . . . 4664 1 
        35 . 1 1   8   8 GLU CA  C 13  58.54 0.50 . 1 . . . . . . . . 4664 1 
        36 . 1 1   8   8 GLU C   C 13 178.00 0.50 . 1 . . . . . . . . 4664 1 
        37 . 1 1   8   8 GLU CB  C 13  31.09 0.50 . 1 . . . . . . . . 4664 1 
        38 . 1 1   8   8 GLU N   N 15 120.87 0.25 . 1 . . . . . . . . 4664 1 
        39 . 1 1   9   9 ILE H   H  1   7.39 0.03 . 1 . . . . . . . . 4664 1 
        40 . 1 1   9   9 ILE HA  H  1   4.25 0.03 . 1 . . . . . . . . 4664 1 
        41 . 1 1   9   9 ILE HB  H  1   2.04 0.03 . 1 . . . . . . . . 4664 1 
        42 . 1 1   9   9 ILE CA  C 13  63.47 0.50 . 1 . . . . . . . . 4664 1 
        43 . 1 1   9   9 ILE C   C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 
        44 . 1 1   9   9 ILE CB  C 13  40.54 0.50 . 1 . . . . . . . . 4664 1 
        45 . 1 1   9   9 ILE N   N 15 115.00 0.25 . 1 . . . . . . . . 4664 1 
        46 . 1 1  10  10 ALA H   H  1   7.37 0.03 . 1 . . . . . . . . 4664 1 
        47 . 1 1  10  10 ALA HA  H  1   4.08 0.03 . 1 . . . . . . . . 4664 1 
        48 . 1 1  10  10 ALA HB1 H  1   1.57 0.03 . 1 . . . . . . . . 4664 1 
        49 . 1 1  10  10 ALA HB2 H  1   1.57 0.03 . 1 . . . . . . . . 4664 1 
        50 . 1 1  10  10 ALA HB3 H  1   1.57 0.03 . 1 . . . . . . . . 4664 1 
        51 . 1 1  10  10 ALA CA  C 13  53.85 0.50 . 1 . . . . . . . . 4664 1 
        52 . 1 1  10  10 ALA C   C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 
        53 . 1 1  10  10 ALA CB  C 13  20.53 0.50 . 1 . . . . . . . . 4664 1 
        54 . 1 1  10  10 ALA N   N 15 120.68 0.25 . 1 . . . . . . . . 4664 1 
        55 . 1 1  11  11 GLY H   H  1   8.62 0.03 . 1 . . . . . . . . 4664 1 
        56 . 1 1  11  11 GLY HA2 H  1   4.60 0.03 . 2 . . . . . . . . 4664 1 
        57 . 1 1  11  11 GLY HA3 H  1   3.62 0.03 . 2 . . . . . . . . 4664 1 
        58 . 1 1  11  11 GLY CA  C 13  45.31 0.50 . 1 . . . . . . . . 4664 1 
        59 . 1 1  11  11 GLY C   C 13 174.70 0.50 . 1 . . . . . . . . 4664 1 
        60 . 1 1  11  11 GLY N   N 15 108.75 0.25 . 1 . . . . . . . . 4664 1 
        61 . 1 1  12  12 LYS H   H  1   8.64 0.03 . 1 . . . . . . . . 4664 1 
        62 . 1 1  12  12 LYS HA  H  1   4.76 0.03 . 1 . . . . . . . . 4664 1 
        63 . 1 1  12  12 LYS HB2 H  1   1.48 0.03 . 1 . . . . . . . . 4664 1 
        64 . 1 1  12  12 LYS HB3 H  1   1.48 0.03 . 1 . . . . . . . . 4664 1 
        65 . 1 1  12  12 LYS CA  C 13  58.23 0.50 . 1 . . . . . . . . 4664 1 
        66 . 1 1  12  12 LYS C   C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 
        67 . 1 1  12  12 LYS CB  C 13  34.78 0.50 . 1 . . . . . . . . 4664 1 
        68 . 1 1  12  12 LYS N   N 15 123.32 0.25 . 1 . . . . . . . . 4664 1 
        69 . 1 1  13  13 TRP H   H  1   9.36 0.03 . 1 . . . . . . . . 4664 1 
        70 . 1 1  13  13 TRP HA  H  1   4.55 0.03 . 1 . . . . . . . . 4664 1 
        71 . 1 1  13  13 TRP HB2 H  1   3.25 0.03 . 2 . . . . . . . . 4664 1 
        72 . 1 1  13  13 TRP HB3 H  1   2.68 0.03 . 2 . . . . . . . . 4664 1 
        73 . 1 1  13  13 TRP CA  C 13  57.69 0.50 . 1 . . . . . . . . 4664 1 
        74 . 1 1  13  13 TRP C   C 13 174.30 0.50 . 1 . . . . . . . . 4664 1 
        75 . 1 1  13  13 TRP CB  C 13  35.17 0.50 . 1 . . . . . . . . 4664 1 
        76 . 1 1  13  13 TRP N   N 15 126.94 0.25 . 1 . . . . . . . . 4664 1 
        77 . 1 1  14  14 TYR H   H  1   9.29 0.03 . 1 . . . . . . . . 4664 1 
        78 . 1 1  14  14 TYR HA  H  1   4.94 0.03 . 1 . . . . . . . . 4664 1 
        79 . 1 1  14  14 TYR HB2 H  1   2.85 0.03 . 2 . . . . . . . . 4664 1 
        80 . 1 1  14  14 TYR HB3 H  1   2.72 0.03 . 2 . . . . . . . . 4664 1 
        81 . 1 1  14  14 TYR CA  C 13  58.93 0.50 . 1 . . . . . . . . 4664 1 
        82 . 1 1  14  14 TYR C   C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 
        83 . 1 1  14  14 TYR CB  C 13  41.49 0.50 . 1 . . . . . . . . 4664 1 
        84 . 1 1  14  14 TYR N   N 15 119.21 0.25 . 1 . . . . . . . . 4664 1 
        85 . 1 1  15  15 VAL H   H  1   8.89 0.03 . 1 . . . . . . . . 4664 1 
        86 . 1 1  15  15 VAL HA  H  1   3.95 0.03 . 1 . . . . . . . . 4664 1 
        87 . 1 1  15  15 VAL HB  H  1   1.88 0.03 . 1 . . . . . . . . 4664 1 
        88 . 1 1  15  15 VAL CA  C 13  62.88 0.50 . 1 . . . . . . . . 4664 1 
        89 . 1 1  15  15 VAL C   C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 
        90 . 1 1  15  15 VAL CB  C 13  32.48 0.50 . 1 . . . . . . . . 4664 1 
        91 . 1 1  15  15 VAL N   N 15 125.01 0.25 . 1 . . . . . . . . 4664 1 
        92 . 1 1  16  16 VAL H   H  1   8.37 0.03 . 1 . . . . . . . . 4664 1 
        93 . 1 1  16  16 VAL HA  H  1   4.55 0.03 . 1 . . . . . . . . 4664 1 
        94 . 1 1  16  16 VAL HB  H  1   2.37 0.03 . 1 . . . . . . . . 4664 1 
        95 . 1 1  16  16 VAL CA  C 13  62.31 0.50 . 1 . . . . . . . . 4664 1 
        96 . 1 1  16  16 VAL C   C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 
        97 . 1 1  16  16 VAL CB  C 13  33.48 0.50 . 1 . . . . . . . . 4664 1 
        98 . 1 1  16  16 VAL N   N 15 115.31 0.25 . 1 . . . . . . . . 4664 1 
        99 . 1 1  17  17 ALA H   H  1   7.52 0.03 . 1 . . . . . . . . 4664 1 
       100 . 1 1  17  17 ALA HA  H  1   5.19 0.03 . 1 . . . . . . . . 4664 1 
       101 . 1 1  17  17 ALA HB1 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       102 . 1 1  17  17 ALA HB2 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       103 . 1 1  17  17 ALA HB3 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       104 . 1 1  17  17 ALA CA  C 13  53.12 0.50 . 1 . . . . . . . . 4664 1 
       105 . 1 1  17  17 ALA C   C 13 179.90 0.50 . 1 . . . . . . . . 4664 1 
       106 . 1 1  17  17 ALA CB  C 13  24.17 0.50 . 1 . . . . . . . . 4664 1 
       107 . 1 1  17  17 ALA N   N 15 123.65 0.25 . 1 . . . . . . . . 4664 1 
       108 . 1 1  18  18 LEU H   H  1   8.50 0.03 . 1 . . . . . . . . 4664 1 
       109 . 1 1  18  18 LEU HA  H  1   5.40 0.03 . 1 . . . . . . . . 4664 1 
       110 . 1 1  18  18 LEU CA  C 13  54.07 0.50 . 1 . . . . . . . . 4664 1 
       111 . 1 1  18  18 LEU C   C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 
       112 . 1 1  18  18 LEU CB  C 13  50.03 0.50 . 1 . . . . . . . . 4664 1 
       113 . 1 1  18  18 LEU N   N 15 118.93 0.25 . 1 . . . . . . . . 4664 1 
       114 . 1 1  19  19 ALA H   H  1   8.26 0.03 . 1 . . . . . . . . 4664 1 
       115 . 1 1  19  19 ALA HA  H  1   5.35 0.03 . 1 . . . . . . . . 4664 1 
       116 . 1 1  19  19 ALA HB1 H  1   0.71 0.03 . 1 . . . . . . . . 4664 1 
       117 . 1 1  19  19 ALA HB2 H  1   0.71 0.03 . 1 . . . . . . . . 4664 1 
       118 . 1 1  19  19 ALA HB3 H  1   0.71 0.03 . 1 . . . . . . . . 4664 1 
       119 . 1 1  19  19 ALA CA  C 13  52.77 0.50 . 1 . . . . . . . . 4664 1 
       120 . 1 1  19  19 ALA C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       121 . 1 1  19  19 ALA CB  C 13  23.21 0.50 . 1 . . . . . . . . 4664 1 
       122 . 1 1  19  19 ALA N   N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 
       123 . 1 1  20  20 SER H   H  1   7.34 0.03 . 1 . . . . . . . . 4664 1 
       124 . 1 1  20  20 SER HA  H  1   3.77 0.03 . 1 . . . . . . . . 4664 1 
       125 . 1 1  20  20 SER HB2 H  1   3.53 0.03 . 1 . . . . . . . . 4664 1 
       126 . 1 1  20  20 SER HB3 H  1   3.53 0.03 . 1 . . . . . . . . 4664 1 
       127 . 1 1  20  20 SER CA  C 13  57.29 0.50 . 1 . . . . . . . . 4664 1 
       128 . 1 1  20  20 SER C   C 13 171.80 0.50 . 1 . . . . . . . . 4664 1 
       129 . 1 1  20  20 SER CB  C 13  64.27 0.50 . 1 . . . . . . . . 4664 1 
       130 . 1 1  20  20 SER N   N 15 114.76 0.25 . 1 . . . . . . . . 4664 1 
       131 . 1 1  21  21 ASN H   H  1   7.85 0.03 . 1 . . . . . . . . 4664 1 
       132 . 1 1  21  21 ASN HA  H  1   5.14 0.03 . 1 . . . . . . . . 4664 1 
       133 . 1 1  21  21 ASN HB2 H  1   3.40 0.03 . 2 . . . . . . . . 4664 1 
       134 . 1 1  21  21 ASN HB3 H  1   3.13 0.03 . 2 . . . . . . . . 4664 1 
       135 . 1 1  21  21 ASN CA  C 13  52.37 0.50 . 1 . . . . . . . . 4664 1 
       136 . 1 1  21  21 ASN C   C 13 177.60 0.50 . 1 . . . . . . . . 4664 1 
       137 . 1 1  21  21 ASN CB  C 13  40.33 0.50 . 1 . . . . . . . . 4664 1 
       138 . 1 1  21  21 ASN N   N 15 117.99 0.25 . 1 . . . . . . . . 4664 1 
       139 . 1 1  22  22 THR H   H  1   8.00 0.03 . 1 . . . . . . . . 4664 1 
       140 . 1 1  22  22 THR HA  H  1   4.33 0.03 . 1 . . . . . . . . 4664 1 
       141 . 1 1  22  22 THR CA  C 13  63.13 0.50 . 1 . . . . . . . . 4664 1 
       142 . 1 1  22  22 THR C   C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 
       143 . 1 1  22  22 THR CB  C 13  71.56 0.50 . 1 . . . . . . . . 4664 1 
       144 . 1 1  22  22 THR N   N 15 112.87 0.25 . 1 . . . . . . . . 4664 1 
       145 . 1 1  23  23 GLU H   H  1   8.89 0.03 . 1 . . . . . . . . 4664 1 
       146 . 1 1  23  23 GLU HA  H  1   4.68 0.03 . 1 . . . . . . . . 4664 1 
       147 . 1 1  23  23 GLU CA  C 13  61.30 0.50 . 1 . . . . . . . . 4664 1 
       148 . 1 1  23  23 GLU CB  C 13  30.31 0.50 . 1 . . . . . . . . 4664 1 
       149 . 1 1  23  23 GLU N   N 15 123.46 0.25 . 1 . . . . . . . . 4664 1 
       150 . 1 1  26  26 LEU CA  C 13  58.68 0.50 . 1 . . . . . . . . 4664 1 
       151 . 1 1  26  26 LEU C   C 13 180.30 0.50 . 1 . . . . . . . . 4664 1 
       152 . 1 1  26  26 LEU CB  C 13  41.91 0.50 . 1 . . . . . . . . 4664 1 
       153 . 1 1  27  27 ARG H   H  1   7.63 0.03 . 1 . . . . . . . . 4664 1 
       154 . 1 1  27  27 ARG HA  H  1   4.06 0.03 . 1 . . . . . . . . 4664 1 
       155 . 1 1  27  27 ARG HB2 H  1   1.74 0.03 . 1 . . . . . . . . 4664 1 
       156 . 1 1  27  27 ARG HB3 H  1   1.74 0.03 . 1 . . . . . . . . 4664 1 
       157 . 1 1  27  27 ARG CA  C 13  59.10 0.50 . 1 . . . . . . . . 4664 1 
       158 . 1 1  27  27 ARG C   C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 
       159 . 1 1  27  27 ARG CB  C 13  32.03 0.50 . 1 . . . . . . . . 4664 1 
       160 . 1 1  27  27 ARG N   N 15 117.67 0.25 . 1 . . . . . . . . 4664 1 
       161 . 1 1  28  28 GLU H   H  1   7.55 0.03 . 1 . . . . . . . . 4664 1 
       162 . 1 1  28  28 GLU HA  H  1   4.29 0.03 . 1 . . . . . . . . 4664 1 
       163 . 1 1  28  28 GLU CA  C 13  56.75 0.50 . 1 . . . . . . . . 4664 1 
       164 . 1 1  28  28 GLU C   C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 
       165 . 1 1  28  28 GLU CB  C 13  30.93 0.50 . 1 . . . . . . . . 4664 1 
       166 . 1 1  28  28 GLU N   N 15 116.73 0.25 . 1 . . . . . . . . 4664 1 
       167 . 1 1  29  29 LYS H   H  1   7.80 0.03 . 1 . . . . . . . . 4664 1 
       168 . 1 1  29  29 LYS CA  C 13  59.93 0.50 . 1 . . . . . . . . 4664 1 
       169 . 1 1  29  29 LYS C   C 13 178.80 0.50 . 1 . . . . . . . . 4664 1 
       170 . 1 1  29  29 LYS CB  C 13  31.45 0.50 . 1 . . . . . . . . 4664 1 
       171 . 1 1  29  29 LYS N   N 15 121.49 0.25 . 1 . . . . . . . . 4664 1 
       172 . 1 1  30  30 ASP H   H  1   8.29 0.03 . 1 . . . . . . . . 4664 1 
       173 . 1 1  30  30 ASP HA  H  1   4.30 0.03 . 1 . . . . . . . . 4664 1 
       174 . 1 1  30  30 ASP HB2 H  1   2.59 0.03 . 2 . . . . . . . . 4664 1 
       175 . 1 1  30  30 ASP HB3 H  1   2.53 0.03 . 2 . . . . . . . . 4664 1 
       176 . 1 1  30  30 ASP CA  C 13  57.11 0.50 . 1 . . . . . . . . 4664 1 
       177 . 1 1  30  30 ASP C   C 13 178.10 0.50 . 1 . . . . . . . . 4664 1 
       178 . 1 1  30  30 ASP CB  C 13  40.59 0.50 . 1 . . . . . . . . 4664 1 
       179 . 1 1  30  30 ASP N   N 15 119.60 0.25 . 1 . . . . . . . . 4664 1 
       180 . 1 1  31  31 LYS H   H  1   8.01 0.03 . 1 . . . . . . . . 4664 1 
       181 . 1 1  31  31 LYS HA  H  1   4.29 0.03 . 1 . . . . . . . . 4664 1 
       182 . 1 1  31  31 LYS HB2 H  1   1.88 0.03 . 1 . . . . . . . . 4664 1 
       183 . 1 1  31  31 LYS HB3 H  1   1.88 0.03 . 1 . . . . . . . . 4664 1 
       184 . 1 1  31  31 LYS CA  C 13  56.94 0.50 . 1 . . . . . . . . 4664 1 
       185 . 1 1  31  31 LYS C   C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 
       186 . 1 1  31  31 LYS CB  C 13  34.15 0.50 . 1 . . . . . . . . 4664 1 
       187 . 1 1  31  31 LYS N   N 15 118.77 0.25 . 1 . . . . . . . . 4664 1 
       188 . 1 1  32  32 MET H   H  1   7.13 0.03 . 1 . . . . . . . . 4664 1 
       189 . 1 1  32  32 MET HA  H  1   4.43 0.03 . 1 . . . . . . . . 4664 1 
       190 . 1 1  32  32 MET HB2 H  1   2.07 0.03 . 1 . . . . . . . . 4664 1 
       191 . 1 1  32  32 MET HB3 H  1   2.07 0.03 . 1 . . . . . . . . 4664 1 
       192 . 1 1  32  32 MET CA  C 13  57.92 0.50 . 1 . . . . . . . . 4664 1 
       193 . 1 1  32  32 MET C   C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 
       194 . 1 1  32  32 MET CB  C 13  33.55 0.50 . 1 . . . . . . . . 4664 1 
       195 . 1 1  32  32 MET N   N 15 121.09 0.25 . 1 . . . . . . . . 4664 1 
       196 . 1 1  33  33 LYS H   H  1   8.45 0.03 . 1 . . . . . . . . 4664 1 
       197 . 1 1  33  33 LYS HA  H  1   4.56 0.03 . 1 . . . . . . . . 4664 1 
       198 . 1 1  33  33 LYS HB2 H  1   1.59 0.03 . 1 . . . . . . . . 4664 1 
       199 . 1 1  33  33 LYS HB3 H  1   1.59 0.03 . 1 . . . . . . . . 4664 1 
       200 . 1 1  33  33 LYS CA  C 13  55.91 0.50 . 1 . . . . . . . . 4664 1 
       201 . 1 1  33  33 LYS C   C 13 174.00 0.50 . 1 . . . . . . . . 4664 1 
       202 . 1 1  33  33 LYS CB  C 13  39.29 0.50 . 1 . . . . . . . . 4664 1 
       203 . 1 1  33  33 LYS N   N 15 120.98 0.25 . 1 . . . . . . . . 4664 1 
       204 . 1 1  34  34 MET H   H  1   8.24 0.03 . 1 . . . . . . . . 4664 1 
       205 . 1 1  34  34 MET HA  H  1   4.31 0.03 . 1 . . . . . . . . 4664 1 
       206 . 1 1  34  34 MET CA  C 13  59.52 0.50 . 1 . . . . . . . . 4664 1 
       207 . 1 1  34  34 MET C   C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 
       208 . 1 1  34  34 MET CB  C 13  35.74 0.50 . 1 . . . . . . . . 4664 1 
       209 . 1 1  34  34 MET N   N 15 119.05 0.25 . 1 . . . . . . . . 4664 1 
       210 . 1 1  35  35 ALA H   H  1   7.33 0.03 . 1 . . . . . . . . 4664 1 
       211 . 1 1  35  35 ALA HA  H  1   5.19 0.03 . 1 . . . . . . . . 4664 1 
       212 . 1 1  35  35 ALA HB1 H  1   1.78 0.03 . 1 . . . . . . . . 4664 1 
       213 . 1 1  35  35 ALA HB2 H  1   1.78 0.03 . 1 . . . . . . . . 4664 1 
       214 . 1 1  35  35 ALA HB3 H  1   1.78 0.03 . 1 . . . . . . . . 4664 1 
       215 . 1 1  35  35 ALA CA  C 13  50.61 0.50 . 1 . . . . . . . . 4664 1 
       216 . 1 1  35  35 ALA C   C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 
       217 . 1 1  35  35 ALA CB  C 13  23.82 0.50 . 1 . . . . . . . . 4664 1 
       218 . 1 1  35  35 ALA N   N 15 126.73 0.25 . 1 . . . . . . . . 4664 1 
       219 . 1 1  36  36 MET H   H  1   8.80 0.03 . 1 . . . . . . . . 4664 1 
       220 . 1 1  36  36 MET HA  H  1   5.13 0.03 . 1 . . . . . . . . 4664 1 
       221 . 1 1  36  36 MET HB2 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       222 . 1 1  36  36 MET HB3 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       223 . 1 1  36  36 MET CA  C 13  56.14 0.50 . 1 . . . . . . . . 4664 1 
       224 . 1 1  36  36 MET C   C 13 173.50 0.50 . 1 . . . . . . . . 4664 1 
       225 . 1 1  36  36 MET CB  C 13  39.48 0.50 . 1 . . . . . . . . 4664 1 
       226 . 1 1  36  36 MET N   N 15 117.94 0.25 . 1 . . . . . . . . 4664 1 
       227 . 1 1  37  37 ALA H   H  1   8.89 0.03 . 1 . . . . . . . . 4664 1 
       228 . 1 1  37  37 ALA HA  H  1   5.32 0.03 . 1 . . . . . . . . 4664 1 
       229 . 1 1  37  37 ALA HB1 H  1   1.01 0.03 . 1 . . . . . . . . 4664 1 
       230 . 1 1  37  37 ALA HB2 H  1   1.01 0.03 . 1 . . . . . . . . 4664 1 
       231 . 1 1  37  37 ALA HB3 H  1   1.01 0.03 . 1 . . . . . . . . 4664 1 
       232 . 1 1  37  37 ALA CA  C 13  51.08 0.50 . 1 . . . . . . . . 4664 1 
       233 . 1 1  37  37 ALA C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
       234 . 1 1  37  37 ALA CB  C 13  24.27 0.50 . 1 . . . . . . . . 4664 1 
       235 . 1 1  37  37 ALA N   N 15 122.70 0.25 . 1 . . . . . . . . 4664 1 
       236 . 1 1  38  38 ARG H   H  1   9.14 0.03 . 1 . . . . . . . . 4664 1 
       237 . 1 1  38  38 ARG HA  H  1   5.02 0.03 . 1 . . . . . . . . 4664 1 
       238 . 1 1  38  38 ARG CA  C 13  55.29 0.50 . 1 . . . . . . . . 4664 1 
       239 . 1 1  38  38 ARG C   C 13 176.20 0.50 . 1 . . . . . . . . 4664 1 
       240 . 1 1  38  38 ARG CB  C 13  34.36 0.50 . 1 . . . . . . . . 4664 1 
       241 . 1 1  38  38 ARG N   N 15 121.44 0.25 . 1 . . . . . . . . 4664 1 
       242 . 1 1  39  39 ILE H   H  1   8.85 0.03 . 1 . . . . . . . . 4664 1 
       243 . 1 1  39  39 ILE HA  H  1   4.92 0.03 . 1 . . . . . . . . 4664 1 
       244 . 1 1  39  39 ILE HB  H  1   1.44 0.03 . 1 . . . . . . . . 4664 1 
       245 . 1 1  39  39 ILE CA  C 13  60.11 0.50 . 1 . . . . . . . . 4664 1 
       246 . 1 1  39  39 ILE C   C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 
       247 . 1 1  39  39 ILE CB  C 13  41.27 0.50 . 1 . . . . . . . . 4664 1 
       248 . 1 1  39  39 ILE N   N 15 126.21 0.25 . 1 . . . . . . . . 4664 1 
       249 . 1 1  40  40 SER H   H  1   8.66 0.03 . 1 . . . . . . . . 4664 1 
       250 . 1 1  40  40 SER HA  H  1   4.55 0.03 . 1 . . . . . . . . 4664 1 
       251 . 1 1  40  40 SER HB2 H  1   3.69 0.03 . 2 . . . . . . . . 4664 1 
       252 . 1 1  40  40 SER HB3 H  1   3.57 0.03 . 2 . . . . . . . . 4664 1 
       253 . 1 1  40  40 SER CA  C 13  57.95 0.50 . 1 . . . . . . . . 4664 1 
       254 . 1 1  40  40 SER C   C 13 173.00 0.50 . 1 . . . . . . . . 4664 1 
       255 . 1 1  40  40 SER CB  C 13  66.30 0.50 . 1 . . . . . . . . 4664 1 
       256 . 1 1  40  40 SER N   N 15 121.80 0.25 . 1 . . . . . . . . 4664 1 
       257 . 1 1  41  41 PHE H   H  1   8.96 0.03 . 1 . . . . . . . . 4664 1 
       258 . 1 1  41  41 PHE HA  H  1   4.62 0.03 . 1 . . . . . . . . 4664 1 
       259 . 1 1  41  41 PHE HB2 H  1   3.17 0.03 . 2 . . . . . . . . 4664 1 
       260 . 1 1  41  41 PHE HB3 H  1   2.80 0.03 . 2 . . . . . . . . 4664 1 
       261 . 1 1  41  41 PHE CA  C 13  59.92 0.50 . 1 . . . . . . . . 4664 1 
       262 . 1 1  41  41 PHE C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       263 . 1 1  41  41 PHE CB  C 13  40.97 0.50 . 1 . . . . . . . . 4664 1 
       264 . 1 1  41  41 PHE N   N 15 123.14 0.25 . 1 . . . . . . . . 4664 1 
       265 . 1 1  42  42 LEU H   H  1   8.42 0.03 . 1 . . . . . . . . 4664 1 
       266 . 1 1  42  42 LEU HA  H  1   4.53 0.03 . 1 . . . . . . . . 4664 1 
       267 . 1 1  42  42 LEU HB2 H  1   1.55 0.03 . 2 . . . . . . . . 4664 1 
       268 . 1 1  42  42 LEU HB3 H  1   1.38 0.03 . 2 . . . . . . . . 4664 1 
       269 . 1 1  42  42 LEU CA  C 13  55.45 0.50 . 1 . . . . . . . . 4664 1 
       270 . 1 1  42  42 LEU C   C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 
       271 . 1 1  42  42 LEU CB  C 13  43.86 0.50 . 1 . . . . . . . . 4664 1 
       272 . 1 1  42  42 LEU N   N 15 126.05 0.25 . 1 . . . . . . . . 4664 1 
       273 . 1 1  43  43 GLY H   H  1   8.25 0.03 . 1 . . . . . . . . 4664 1 
       274 . 1 1  43  43 GLY HA2 H  1   4.03 0.03 . 1 . . . . . . . . 4664 1 
       275 . 1 1  43  43 GLY HA3 H  1   4.03 0.03 . 1 . . . . . . . . 4664 1 
       276 . 1 1  43  43 GLY CA  C 13  45.94 0.50 . 1 . . . . . . . . 4664 1 
       277 . 1 1  43  43 GLY C   C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 
       278 . 1 1  43  43 GLY N   N 15 109.65 0.25 . 1 . . . . . . . . 4664 1 
       279 . 1 1  44  44 GLU H   H  1   8.81 0.03 . 1 . . . . . . . . 4664 1 
       280 . 1 1  44  44 GLU HA  H  1   4.06 0.03 . 1 . . . . . . . . 4664 1 
       281 . 1 1  44  44 GLU HB2 H  1   1.93 0.03 . 1 . . . . . . . . 4664 1 
       282 . 1 1  44  44 GLU HB3 H  1   1.93 0.03 . 1 . . . . . . . . 4664 1 
       283 . 1 1  44  44 GLU CA  C 13  59.55 0.50 . 1 . . . . . . . . 4664 1 
       284 . 1 1  44  44 GLU C   C 13 178.30 0.50 . 1 . . . . . . . . 4664 1 
       285 . 1 1  44  44 GLU CB  C 13  30.86 0.50 . 1 . . . . . . . . 4664 1 
       286 . 1 1  44  44 GLU N   N 15 121.22 0.25 . 1 . . . . . . . . 4664 1 
       287 . 1 1  45  45 ASP H   H  1   8.38 0.03 . 1 . . . . . . . . 4664 1 
       288 . 1 1  45  45 ASP HA  H  1   4.82 0.03 . 1 . . . . . . . . 4664 1 
       289 . 1 1  45  45 ASP HB2 H  1   2.95 0.03 . 2 . . . . . . . . 4664 1 
       290 . 1 1  45  45 ASP HB3 H  1   2.74 0.03 . 2 . . . . . . . . 4664 1 
       291 . 1 1  45  45 ASP CA  C 13  54.91 0.50 . 1 . . . . . . . . 4664 1 
       292 . 1 1  45  45 ASP C   C 13 175.60 0.50 . 1 . . . . . . . . 4664 1 
       293 . 1 1  45  45 ASP CB  C 13  42.81 0.50 . 1 . . . . . . . . 4664 1 
       294 . 1 1  45  45 ASP N   N 15 115.82 0.25 . 1 . . . . . . . . 4664 1 
       295 . 1 1  46  46 GLU H   H  1   7.38 0.03 . 1 . . . . . . . . 4664 1 
       296 . 1 1  46  46 GLU HA  H  1   5.46 0.03 . 1 . . . . . . . . 4664 1 
       297 . 1 1  46  46 GLU HB2 H  1   1.94 0.03 . 1 . . . . . . . . 4664 1 
       298 . 1 1  46  46 GLU HB3 H  1   1.94 0.03 . 1 . . . . . . . . 4664 1 
       299 . 1 1  46  46 GLU CA  C 13  56.45 0.50 . 1 . . . . . . . . 4664 1 
       300 . 1 1  46  46 GLU C   C 13 176.04 0.50 . 1 . . . . . . . . 4664 1 
       301 . 1 1  46  46 GLU CB  C 13  34.83 0.50 . 1 . . . . . . . . 4664 1 
       302 . 1 1  46  46 GLU N   N 15 118.62 0.25 . 1 . . . . . . . . 4664 1 
       303 . 1 1  47  47 LEU H   H  1   9.04 0.03 . 1 . . . . . . . . 4664 1 
       304 . 1 1  47  47 LEU HA  H  1   4.80 0.03 . 1 . . . . . . . . 4664 1 
       305 . 1 1  47  47 LEU CA  C 13  55.06 0.50 . 1 . . . . . . . . 4664 1 
       306 . 1 1  47  47 LEU C   C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 
       307 . 1 1  47  47 LEU N   N 15 125.22 0.25 . 1 . . . . . . . . 4664 1 
       308 . 1 1  48  48 LYS H   H  1   8.93 0.03 . 1 . . . . . . . . 4664 1 
       309 . 1 1  48  48 LYS HA  H  1   4.88 0.03 . 1 . . . . . . . . 4664 1 
       310 . 1 1  48  48 LYS CA  C 13  56.17 0.50 . 1 . . . . . . . . 4664 1 
       311 . 1 1  48  48 LYS C   C 13 175.40 0.50 . 1 . . . . . . . . 4664 1 
       312 . 1 1  48  48 LYS CB  C 13  35.63 0.50 . 1 . . . . . . . . 4664 1 
       313 . 1 1  48  48 LYS N   N 15 125.15 0.25 . 1 . . . . . . . . 4664 1 
       314 . 1 1  49  49 VAL H   H  1   8.80 0.03 . 1 . . . . . . . . 4664 1 
       315 . 1 1  49  49 VAL HA  H  1   4.43 0.03 . 1 . . . . . . . . 4664 1 
       316 . 1 1  49  49 VAL HB  H  1   1.57 0.03 . 1 . . . . . . . . 4664 1 
       317 . 1 1  49  49 VAL CA  C 13  61.58 0.50 . 1 . . . . . . . . 4664 1 
       318 . 1 1  49  49 VAL C   C 13 174.70 0.50 . 1 . . . . . . . . 4664 1 
       319 . 1 1  49  49 VAL CB  C 13  35.39 0.50 . 1 . . . . . . . . 4664 1 
       320 . 1 1  49  49 VAL N   N 15 127.46 0.25 . 1 . . . . . . . . 4664 1 
       321 . 1 1  50  50 SER H   H  1   8.26 0.03 . 1 . . . . . . . . 4664 1 
       322 . 1 1  50  50 SER HA  H  1   4.76 0.03 . 1 . . . . . . . . 4664 1 
       323 . 1 1  50  50 SER HB2 H  1   3.83 0.03 . 2 . . . . . . . . 4664 1 
       324 . 1 1  50  50 SER HB3 H  1   3.41 0.03 . 2 . . . . . . . . 4664 1 
       325 . 1 1  50  50 SER CA  C 13  57.17 0.50 . 1 . . . . . . . . 4664 1 
       326 . 1 1  50  50 SER C   C 13 173.80 0.50 . 1 . . . . . . . . 4664 1 
       327 . 1 1  50  50 SER CB  C 13  64.99 0.50 . 1 . . . . . . . . 4664 1 
       328 . 1 1  50  50 SER N   N 15 121.67 0.25 . 1 . . . . . . . . 4664 1 
       329 . 1 1  51  51 TYR H   H  1   8.90 0.03 . 1 . . . . . . . . 4664 1 
       330 . 1 1  51  51 TYR HA  H  1   4.77 0.03 . 1 . . . . . . . . 4664 1 
       331 . 1 1  51  51 TYR HB2 H  1   3.18 0.03 . 2 . . . . . . . . 4664 1 
       332 . 1 1  51  51 TYR HB3 H  1   3.13 0.03 . 2 . . . . . . . . 4664 1 
       333 . 1 1  51  51 TYR CA  C 13  58.11 0.50 . 1 . . . . . . . . 4664 1 
       334 . 1 1  51  51 TYR C   C 13 177.90 0.50 . 1 . . . . . . . . 4664 1 
       335 . 1 1  51  51 TYR CB  C 13  42.42 0.50 . 1 . . . . . . . . 4664 1 
       336 . 1 1  51  51 TYR N   N 15 123.02 0.25 . 1 . . . . . . . . 4664 1 
       337 . 1 1  52  52 ALA H   H  1   8.50 0.03 . 1 . . . . . . . . 4664 1 
       338 . 1 1  52  52 ALA HA  H  1   4.81 0.03 . 1 . . . . . . . . 4664 1 
       339 . 1 1  52  52 ALA HB1 H  1   0.87 0.03 . 1 . . . . . . . . 4664 1 
       340 . 1 1  52  52 ALA HB2 H  1   0.87 0.03 . 1 . . . . . . . . 4664 1 
       341 . 1 1  52  52 ALA HB3 H  1   0.87 0.03 . 1 . . . . . . . . 4664 1 
       342 . 1 1  52  52 ALA CA  C 13  52.98 0.50 . 1 . . . . . . . . 4664 1 
       343 . 1 1  52  52 ALA C   C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 
       344 . 1 1  52  52 ALA CB  C 13  21.87 0.50 . 1 . . . . . . . . 4664 1 
       345 . 1 1  52  52 ALA N   N 15 124.49 0.25 . 1 . . . . . . . . 4664 1 
       346 . 1 1  53  53 VAL H   H  1   9.06 0.03 . 1 . . . . . . . . 4664 1 
       347 . 1 1  53  53 VAL HA  H  1   4.64 0.03 . 1 . . . . . . . . 4664 1 
       348 . 1 1  53  53 VAL HB  H  1   1.73 0.03 . 1 . . . . . . . . 4664 1 
       349 . 1 1  53  53 VAL CA  C 13  59.29 0.50 . 1 . . . . . . . . 4664 1 
       350 . 1 1  53  53 VAL CB  C 13  36.71 0.50 . 1 . . . . . . . . 4664 1 
       351 . 1 1  53  53 VAL N   N 15 125.02 0.25 . 1 . . . . . . . . 4664 1 
       352 . 1 1  56  56 PRO CA  C 13  66.40 0.50 . 1 . . . . . . . . 4664 1 
       353 . 1 1  56  56 PRO C   C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 
       354 . 1 1  56  56 PRO CB  C 13  32.43 0.50 . 1 . . . . . . . . 4664 1 
       355 . 1 1  57  57 ASN H   H  1   8.25 0.03 . 1 . . . . . . . . 4664 1 
       356 . 1 1  57  57 ASN HA  H  1   4.65 0.03 . 1 . . . . . . . . 4664 1 
       357 . 1 1  57  57 ASN HB2 H  1   2.79 0.03 . 1 . . . . . . . . 4664 1 
       358 . 1 1  57  57 ASN HB3 H  1   2.79 0.03 . 1 . . . . . . . . 4664 1 
       359 . 1 1  57  57 ASN CA  C 13  53.91 0.50 . 1 . . . . . . . . 4664 1 
       360 . 1 1  57  57 ASN C   C 13 175.90 0.50 . 1 . . . . . . . . 4664 1 
       361 . 1 1  57  57 ASN CB  C 13  39.21 0.50 . 1 . . . . . . . . 4664 1 
       362 . 1 1  57  57 ASN N   N 15 114.85 0.25 . 1 . . . . . . . . 4664 1 
       363 . 1 1  58  58 GLY H   H  1   7.70 0.03 . 1 . . . . . . . . 4664 1 
       364 . 1 1  58  58 GLY HA2 H  1   4.06 0.03 . 2 . . . . . . . . 4664 1 
       365 . 1 1  58  58 GLY HA3 H  1   3.94 0.03 . 2 . . . . . . . . 4664 1 
       366 . 1 1  58  58 GLY CA  C 13  47.03 0.50 . 1 . . . . . . . . 4664 1 
       367 . 1 1  58  58 GLY N   N 15 107.32 0.25 . 1 . . . . . . . . 4664 1 
       368 . 1 1  61  61 LYS HA  H  1   5.40 0.03 . 1 . . . . . . . . 4664 1 
       369 . 1 1  61  61 LYS CA  C 13  56.14 0.50 . 1 . . . . . . . . 4664 1 
       370 . 1 1  61  61 LYS C   C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 
       371 . 1 1  61  61 LYS CB  C 13  36.25 0.50 . 1 . . . . . . . . 4664 1 
       372 . 1 1  62  62 TRP H   H  1   7.95 0.03 . 1 . . . . . . . . 4664 1 
       373 . 1 1  62  62 TRP HA  H  1   4.78 0.03 . 1 . . . . . . . . 4664 1 
       374 . 1 1  62  62 TRP HB2 H  1   3.15 0.03 . 1 . . . . . . . . 4664 1 
       375 . 1 1  62  62 TRP HB3 H  1   3.15 0.03 . 1 . . . . . . . . 4664 1 
       376 . 1 1  62  62 TRP CA  C 13  57.88 0.50 . 1 . . . . . . . . 4664 1 
       377 . 1 1  62  62 TRP C   C 13 172.80 0.50 . 1 . . . . . . . . 4664 1 
       378 . 1 1  62  62 TRP CB  C 13  31.69 0.50 . 1 . . . . . . . . 4664 1 
       379 . 1 1  62  62 TRP N   N 15 122.97 0.25 . 1 . . . . . . . . 4664 1 
       380 . 1 1  63  63 GLU H   H  1   8.29 0.03 . 1 . . . . . . . . 4664 1 
       381 . 1 1  63  63 GLU HA  H  1   5.53 0.03 . 1 . . . . . . . . 4664 1 
       382 . 1 1  63  63 GLU HB2 H  1   1.77 0.03 . 1 . . . . . . . . 4664 1 
       383 . 1 1  63  63 GLU HB3 H  1   1.77 0.03 . 1 . . . . . . . . 4664 1 
       384 . 1 1  63  63 GLU CA  C 13  55.17 0.50 . 1 . . . . . . . . 4664 1 
       385 . 1 1  63  63 GLU C   C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 
       386 . 1 1  63  63 GLU CB  C 13  35.01 0.50 . 1 . . . . . . . . 4664 1 
       387 . 1 1  63  63 GLU N   N 15 118.12 0.25 . 1 . . . . . . . . 4664 1 
       388 . 1 1  64  64 THR H   H  1   8.93 0.03 . 1 . . . . . . . . 4664 1 
       389 . 1 1  64  64 THR HA  H  1   4.46 0.03 . 1 . . . . . . . . 4664 1 
       390 . 1 1  64  64 THR HB  H  1   3.78 0.03 . 1 . . . . . . . . 4664 1 
       391 . 1 1  64  64 THR CA  C 13  63.05 0.50 . 1 . . . . . . . . 4664 1 
       392 . 1 1  64  64 THR C   C 13 172.80 0.50 . 1 . . . . . . . . 4664 1 
       393 . 1 1  64  64 THR CB  C 13  73.12 0.50 . 1 . . . . . . . . 4664 1 
       394 . 1 1  64  64 THR N   N 15 118.91 0.25 . 1 . . . . . . . . 4664 1 
       395 . 1 1  65  65 THR H   H  1   8.36 0.03 . 1 . . . . . . . . 4664 1 
       396 . 1 1  65  65 THR HA  H  1   5.13 0.03 . 1 . . . . . . . . 4664 1 
       397 . 1 1  65  65 THR HB  H  1   3.91 0.03 . 1 . . . . . . . . 4664 1 
       398 . 1 1  65  65 THR CA  C 13  62.69 0.50 . 1 . . . . . . . . 4664 1 
       399 . 1 1  65  65 THR C   C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 
       400 . 1 1  65  65 THR CB  C 13  70.91 0.50 . 1 . . . . . . . . 4664 1 
       401 . 1 1  65  65 THR N   N 15 120.74 0.25 . 1 . . . . . . . . 4664 1 
       402 . 1 1  66  66 PHE H   H  1   8.24 0.03 . 1 . . . . . . . . 4664 1 
       403 . 1 1  66  66 PHE HA  H  1   4.68 0.03 . 1 . . . . . . . . 4664 1 
       404 . 1 1  66  66 PHE CA  C 13  62.43 0.50 . 1 . . . . . . . . 4664 1 
       405 . 1 1  66  66 PHE C   C 13 175.30 0.50 . 1 . . . . . . . . 4664 1 
       406 . 1 1  66  66 PHE CB  C 13  33.11 0.50 . 1 . . . . . . . . 4664 1 
       407 . 1 1  66  66 PHE N   N 15 125.19 0.25 . 1 . . . . . . . . 4664 1 
       408 . 1 1  67  67 LYS H   H  1   8.82 0.03 . 1 . . . . . . . . 4664 1 
       409 . 1 1  67  67 LYS HA  H  1   5.41 0.03 . 1 . . . . . . . . 4664 1 
       410 . 1 1  67  67 LYS HB2 H  1   1.99 0.03 . 2 . . . . . . . . 4664 1 
       411 . 1 1  67  67 LYS HB3 H  1   1.83 0.03 . 2 . . . . . . . . 4664 1 
       412 . 1 1  67  67 LYS CA  C 13  55.52 0.50 . 1 . . . . . . . . 4664 1 
       413 . 1 1  67  67 LYS C   C 13 177.60 0.50 . 1 . . . . . . . . 4664 1 
       414 . 1 1  67  67 LYS CB  C 13  37.22 0.50 . 1 . . . . . . . . 4664 1 
       415 . 1 1  67  67 LYS N   N 15 120.68 0.25 . 1 . . . . . . . . 4664 1 
       416 . 1 1  68  68 LYS H   H  1   8.83 0.03 . 1 . . . . . . . . 4664 1 
       417 . 1 1  68  68 LYS CA  C 13  58.56 0.50 . 1 . . . . . . . . 4664 1 
       418 . 1 1  68  68 LYS C   C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 
       419 . 1 1  68  68 LYS CB  C 13  35.23 0.50 . 1 . . . . . . . . 4664 1 
       420 . 1 1  68  68 LYS N   N 15 129.88 0.25 . 1 . . . . . . . . 4664 1 
       421 . 1 1  69  69 THR H   H  1   8.62 0.03 . 1 . . . . . . . . 4664 1 
       422 . 1 1  69  69 THR HA  H  1   4.62 0.03 . 1 . . . . . . . . 4664 1 
       423 . 1 1  69  69 THR HB  H  1   4.44 0.03 . 1 . . . . . . . . 4664 1 
       424 . 1 1  69  69 THR CA  C 13  61.84 0.50 . 1 . . . . . . . . 4664 1 
       425 . 1 1  69  69 THR C   C 13 175.70 0.50 . 1 . . . . . . . . 4664 1 
       426 . 1 1  69  69 THR CB  C 13  70.62 0.50 . 1 . . . . . . . . 4664 1 
       427 . 1 1  69  69 THR N   N 15 119.35 0.25 . 1 . . . . . . . . 4664 1 
       428 . 1 1  70  70 SER H   H  1   8.24 0.03 . 1 . . . . . . . . 4664 1 
       429 . 1 1  70  70 SER HA  H  1   4.35 0.03 . 1 . . . . . . . . 4664 1 
       430 . 1 1  70  70 SER HB2 H  1   3.98 0.03 . 2 . . . . . . . . 4664 1 
       431 . 1 1  70  70 SER HB3 H  1   3.79 0.03 . 2 . . . . . . . . 4664 1 
       432 . 1 1  70  70 SER CA  C 13  59.21 0.50 . 1 . . . . . . . . 4664 1 
       433 . 1 1  70  70 SER C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       434 . 1 1  70  70 SER CB  C 13  64.34 0.50 . 1 . . . . . . . . 4664 1 
       435 . 1 1  70  70 SER N   N 15 112.71 0.25 . 1 . . . . . . . . 4664 1 
       436 . 1 1  71  71 ASP H   H  1   7.86 0.03 . 1 . . . . . . . . 4664 1 
       437 . 1 1  71  71 ASP HA  H  1   4.29 0.03 . 1 . . . . . . . . 4664 1 
       438 . 1 1  71  71 ASP HB2 H  1   2.61 0.03 . 2 . . . . . . . . 4664 1 
       439 . 1 1  71  71 ASP HB3 H  1   2.03 0.03 . 2 . . . . . . . . 4664 1 
       440 . 1 1  71  71 ASP CA  C 13  56.09 0.50 . 1 . . . . . . . . 4664 1 
       441 . 1 1  71  71 ASP C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
       442 . 1 1  71  71 ASP CB  C 13  43.09 0.50 . 1 . . . . . . . . 4664 1 
       443 . 1 1  71  71 ASP N   N 15 121.92 0.25 . 1 . . . . . . . . 4664 1 
       444 . 1 1  72  72 ASP H   H  1   8.37 0.03 . 1 . . . . . . . . 4664 1 
       445 . 1 1  72  72 ASP HA  H  1   4.37 0.03 . 1 . . . . . . . . 4664 1 
       446 . 1 1  72  72 ASP HB2 H  1   2.53 0.03 . 2 . . . . . . . . 4664 1 
       447 . 1 1  72  72 ASP HB3 H  1   2.45 0.03 . 2 . . . . . . . . 4664 1 
       448 . 1 1  72  72 ASP CA  C 13  56.13 0.50 . 1 . . . . . . . . 4664 1 
       449 . 1 1  72  72 ASP C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       450 . 1 1  72  72 ASP CB  C 13  42.11 0.50 . 1 . . . . . . . . 4664 1 
       451 . 1 1  72  72 ASP N   N 15 121.54 0.25 . 1 . . . . . . . . 4664 1 
       452 . 1 1  73  73 GLY H   H  1   8.08 0.03 . 1 . . . . . . . . 4664 1 
       453 . 1 1  73  73 GLY HA2 H  1   3.96 0.03 . 2 . . . . . . . . 4664 1 
       454 . 1 1  73  73 GLY HA3 H  1   3.69 0.03 . 2 . . . . . . . . 4664 1 
       455 . 1 1  73  73 GLY CA  C 13  45.47 0.50 . 1 . . . . . . . . 4664 1 
       456 . 1 1  73  73 GLY C   C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 
       457 . 1 1  73  73 GLY N   N 15 109.82 0.25 . 1 . . . . . . . . 4664 1 
       458 . 1 1  74  74 GLU H   H  1   8.70 0.03 . 1 . . . . . . . . 4664 1 
       459 . 1 1  74  74 GLU HA  H  1   4.60 0.03 . 1 . . . . . . . . 4664 1 
       460 . 1 1  74  74 GLU CA  C 13  55.66 0.50 . 1 . . . . . . . . 4664 1 
       461 . 1 1  74  74 GLU C   C 13 174.50 0.50 . 1 . . . . . . . . 4664 1 
       462 . 1 1  74  74 GLU CB  C 13  30.98 0.50 . 1 . . . . . . . . 4664 1 
       463 . 1 1  74  74 GLU N   N 15 124.18 0.25 . 1 . . . . . . . . 4664 1 
       464 . 1 1  75  75 VAL H   H  1   7.80 0.03 . 1 . . . . . . . . 4664 1 
       465 . 1 1  75  75 VAL HA  H  1   4.91 0.03 . 1 . . . . . . . . 4664 1 
       466 . 1 1  75  75 VAL HB  H  1   1.96 0.03 . 1 . . . . . . . . 4664 1 
       467 . 1 1  75  75 VAL CA  C 13  62.42 0.50 . 1 . . . . . . . . 4664 1 
       468 . 1 1  75  75 VAL C   C 13 175.10 0.50 . 1 . . . . . . . . 4664 1 
       469 . 1 1  75  75 VAL CB  C 13  34.24 0.50 . 1 . . . . . . . . 4664 1 
       470 . 1 1  75  75 VAL N   N 15 124.50 0.25 . 1 . . . . . . . . 4664 1 
       471 . 1 1  76  76 TYR H   H  1   9.19 0.03 . 1 . . . . . . . . 4664 1 
       472 . 1 1  76  76 TYR HA  H  1   5.15 0.03 . 1 . . . . . . . . 4664 1 
       473 . 1 1  76  76 TYR HB2 H  1   2.64 0.03 . 1 . . . . . . . . 4664 1 
       474 . 1 1  76  76 TYR HB3 H  1   2.64 0.03 . 1 . . . . . . . . 4664 1 
       475 . 1 1  76  76 TYR CA  C 13  57.72 0.50 . 1 . . . . . . . . 4664 1 
       476 . 1 1  76  76 TYR C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       477 . 1 1  76  76 TYR CB  C 13  43.27 0.50 . 1 . . . . . . . . 4664 1 
       478 . 1 1  76  76 TYR N   N 15 125.39 0.25 . 1 . . . . . . . . 4664 1 
       479 . 1 1  77  77 TYR H   H  1   9.38 0.03 . 1 . . . . . . . . 4664 1 
       480 . 1 1  77  77 TYR HA  H  1   5.79 0.03 . 1 . . . . . . . . 4664 1 
       481 . 1 1  77  77 TYR HB2 H  1   2.90 0.03 . 2 . . . . . . . . 4664 1 
       482 . 1 1  77  77 TYR HB3 H  1   2.88 0.03 . 2 . . . . . . . . 4664 1 
       483 . 1 1  77  77 TYR CA  C 13  58.01 0.50 . 1 . . . . . . . . 4664 1 
       484 . 1 1  77  77 TYR C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       485 . 1 1  77  77 TYR CB  C 13  44.71 0.50 . 1 . . . . . . . . 4664 1 
       486 . 1 1  77  77 TYR N   N 15 121.32 0.25 . 1 . . . . . . . . 4664 1 
       487 . 1 1  78  78 SER H   H  1   8.46 0.03 . 1 . . . . . . . . 4664 1 
       488 . 1 1  78  78 SER HA  H  1   4.74 0.03 . 1 . . . . . . . . 4664 1 
       489 . 1 1  78  78 SER HB2 H  1   3.09 0.03 . 2 . . . . . . . . 4664 1 
       490 . 1 1  78  78 SER HB3 H  1   2.66 0.03 . 2 . . . . . . . . 4664 1 
       491 . 1 1  78  78 SER CA  C 13  55.65 0.50 . 1 . . . . . . . . 4664 1 
       492 . 1 1  78  78 SER C   C 13 175.10 0.50 . 1 . . . . . . . . 4664 1 
       493 . 1 1  78  78 SER CB  C 13  64.41 0.50 . 1 . . . . . . . . 4664 1 
       494 . 1 1  78  78 SER N   N 15 125.58 0.25 . 1 . . . . . . . . 4664 1 
       495 . 1 1  79  79 GLU H   H  1   8.60 0.03 . 1 . . . . . . . . 4664 1 
       496 . 1 1  79  79 GLU HA  H  1   3.87 0.03 . 1 . . . . . . . . 4664 1 
       497 . 1 1  79  79 GLU HB2 H  1   2.06 0.03 . 1 . . . . . . . . 4664 1 
       498 . 1 1  79  79 GLU HB3 H  1   2.06 0.03 . 1 . . . . . . . . 4664 1 
       499 . 1 1  79  79 GLU CA  C 13  59.61 0.50 . 1 . . . . . . . . 4664 1 
       500 . 1 1  79  79 GLU C   C 13 179.60 0.50 . 1 . . . . . . . . 4664 1 
       501 . 1 1  79  79 GLU CB  C 13  30.58 0.50 . 1 . . . . . . . . 4664 1 
       502 . 1 1  79  79 GLU N   N 15 130.88 0.25 . 1 . . . . . . . . 4664 1 
       503 . 1 1  80  80 GLU H   H  1   8.42 0.03 . 1 . . . . . . . . 4664 1 
       504 . 1 1  80  80 GLU HA  H  1   3.91 0.03 . 1 . . . . . . . . 4664 1 
       505 . 1 1  80  80 GLU HB2 H  1   1.96 0.03 . 2 . . . . . . . . 4664 1 
       506 . 1 1  80  80 GLU HB3 H  1   1.86 0.03 . 2 . . . . . . . . 4664 1 
       507 . 1 1  80  80 GLU CA  C 13  60.16 0.50 . 1 . . . . . . . . 4664 1 
       508 . 1 1  80  80 GLU C   C 13 178.60 0.50 . 1 . . . . . . . . 4664 1 
       509 . 1 1  80  80 GLU CB  C 13  30.45 0.50 . 1 . . . . . . . . 4664 1 
       510 . 1 1  80  80 GLU N   N 15 119.71 0.25 . 1 . . . . . . . . 4664 1 
       511 . 1 1  81  81 ALA H   H  1   7.28 0.03 . 1 . . . . . . . . 4664 1 
       512 . 1 1  81  81 ALA HA  H  1   4.28 0.03 . 1 . . . . . . . . 4664 1 
       513 . 1 1  81  81 ALA HB1 H  1   1.30 0.03 . 1 . . . . . . . . 4664 1 
       514 . 1 1  81  81 ALA HB2 H  1   1.30 0.03 . 1 . . . . . . . . 4664 1 
       515 . 1 1  81  81 ALA HB3 H  1   1.30 0.03 . 1 . . . . . . . . 4664 1 
       516 . 1 1  81  81 ALA CA  C 13  52.38 0.50 . 1 . . . . . . . . 4664 1 
       517 . 1 1  81  81 ALA C   C 13 177.10 0.50 . 1 . . . . . . . . 4664 1 
       518 . 1 1  81  81 ALA CB  C 13  20.75 0.50 . 1 . . . . . . . . 4664 1 
       519 . 1 1  81  81 ALA N   N 15 118.49 0.25 . 1 . . . . . . . . 4664 1 
       520 . 1 1  82  82 LYS H   H  1   7.74 0.03 . 1 . . . . . . . . 4664 1 
       521 . 1 1  82  82 LYS HA  H  1   3.82 0.03 . 1 . . . . . . . . 4664 1 
       522 . 1 1  82  82 LYS CA  C 13  57.08 0.50 . 1 . . . . . . . . 4664 1 
       523 . 1 1  82  82 LYS C   C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 
       524 . 1 1  82  82 LYS CB  C 13  30.54 0.50 . 1 . . . . . . . . 4664 1 
       525 . 1 1  82  82 LYS N   N 15 119.08 0.25 . 1 . . . . . . . . 4664 1 
       526 . 1 1  83  83 LYS H   H  1   7.07 0.03 . 1 . . . . . . . . 4664 1 
       527 . 1 1  83  83 LYS HA  H  1   5.38 0.03 . 1 . . . . . . . . 4664 1 
       528 . 1 1  83  83 LYS CA  C 13  55.50 0.50 . 1 . . . . . . . . 4664 1 
       529 . 1 1  83  83 LYS CB  C 13  40.04 0.50 . 1 . . . . . . . . 4664 1 
       530 . 1 1  83  83 LYS N   N 15 119.10 0.25 . 1 . . . . . . . . 4664 1 
       531 . 1 1  86  86 GLU CA  C 13  54.75 0.50 . 1 . . . . . . . . 4664 1 
       532 . 1 1  86  86 GLU C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       533 . 1 1  86  86 GLU CB  C 13  34.32 0.50 . 1 . . . . . . . . 4664 1 
       534 . 1 1  87  87 VAL H   H  1   8.69 0.03 . 1 . . . . . . . . 4664 1 
       535 . 1 1  87  87 VAL HA  H  1   4.14 0.03 . 1 . . . . . . . . 4664 1 
       536 . 1 1  87  87 VAL HB  H  1   2.20 0.03 . 1 . . . . . . . . 4664 1 
       537 . 1 1  87  87 VAL CA  C 13  63.37 0.50 . 1 . . . . . . . . 4664 1 
       538 . 1 1  87  87 VAL C   C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 
       539 . 1 1  87  87 VAL CB  C 13  31.97 0.50 . 1 . . . . . . . . 4664 1 
       540 . 1 1  87  87 VAL N   N 15 126.00 0.25 . 1 . . . . . . . . 4664 1 
       541 . 1 1  88  88 LEU H   H  1   8.93 0.03 . 1 . . . . . . . . 4664 1 
       542 . 1 1  88  88 LEU CA  C 13  56.94 0.50 . 1 . . . . . . . . 4664 1 
       543 . 1 1  88  88 LEU C   C 13 178.20 0.50 . 1 . . . . . . . . 4664 1 
       544 . 1 1  88  88 LEU CB  C 13  44.10 0.50 . 1 . . . . . . . . 4664 1 
       545 . 1 1  88  88 LEU N   N 15 128.80 0.25 . 1 . . . . . . . . 4664 1 
       546 . 1 1  89  89 ASP H   H  1   7.02 0.03 . 1 . . . . . . . . 4664 1 
       547 . 1 1  89  89 ASP HA  H  1   4.70 0.03 . 1 . . . . . . . . 4664 1 
       548 . 1 1  89  89 ASP HB2 H  1   2.73 0.03 . 1 . . . . . . . . 4664 1 
       549 . 1 1  89  89 ASP HB3 H  1   2.73 0.03 . 1 . . . . . . . . 4664 1 
       550 . 1 1  89  89 ASP CA  C 13  55.88 0.50 . 1 . . . . . . . . 4664 1 
       551 . 1 1  89  89 ASP C   C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 
       552 . 1 1  89  89 ASP CB  C 13  46.51 0.50 . 1 . . . . . . . . 4664 1 
       553 . 1 1  89  89 ASP N   N 15 114.58 0.25 . 1 . . . . . . . . 4664 1 
       554 . 1 1  90  90 THR H   H  1   7.99 0.03 . 1 . . . . . . . . 4664 1 
       555 . 1 1  90  90 THR HA  H  1   3.75 0.03 . 1 . . . . . . . . 4664 1 
       556 . 1 1  90  90 THR HB  H  1   3.83 0.03 . 1 . . . . . . . . 4664 1 
       557 . 1 1  90  90 THR CA  C 13  61.49 0.50 . 1 . . . . . . . . 4664 1 
       558 . 1 1  90  90 THR C   C 13 179.86 0.50 . 1 . . . . . . . . 4664 1 
       559 . 1 1  90  90 THR CB  C 13  69.15 0.50 . 1 . . . . . . . . 4664 1 
       560 . 1 1  90  90 THR N   N 15 120.53 0.25 . 1 . . . . . . . . 4664 1 
       561 . 1 1  91  91 ASP H   H  1   6.70 0.03 . 1 . . . . . . . . 4664 1 
       562 . 1 1  91  91 ASP HA  H  1   4.76 0.03 . 1 . . . . . . . . 4664 1 
       563 . 1 1  91  91 ASP CA  C 13  53.80 0.50 . 1 . . . . . . . . 4664 1 
       564 . 1 1  91  91 ASP C   C 13 177.70 0.50 . 1 . . . . . . . . 4664 1 
       565 . 1 1  91  91 ASP CB  C 13  41.90 0.50 . 1 . . . . . . . . 4664 1 
       566 . 1 1  91  91 ASP N   N 15 123.00 0.25 . 1 . . . . . . . . 4664 1 
       567 . 1 1  92  92 TYR H   H  1   9.30 0.03 . 1 . . . . . . . . 4664 1 
       568 . 1 1  92  92 TYR CA  C 13  62.08 0.50 . 1 . . . . . . . . 4664 1 
       569 . 1 1  92  92 TYR C   C 13 174.90 0.50 . 1 . . . . . . . . 4664 1 
       570 . 1 1  92  92 TYR CB  C 13  36.77 0.50 . 1 . . . . . . . . 4664 1 
       571 . 1 1  92  92 TYR N   N 15 115.90 0.25 . 1 . . . . . . . . 4664 1 
       572 . 1 1  93  93 LYS H   H  1   7.99 0.03 . 1 . . . . . . . . 4664 1 
       573 . 1 1  93  93 LYS HA  H  1   4.59 0.03 . 1 . . . . . . . . 4664 1 
       574 . 1 1  93  93 LYS HB2 H  1   1.62 0.03 . 1 . . . . . . . . 4664 1 
       575 . 1 1  93  93 LYS HB3 H  1   1.62 0.03 . 1 . . . . . . . . 4664 1 
       576 . 1 1  93  93 LYS CA  C 13  59.30 0.50 . 1 . . . . . . . . 4664 1 
       577 . 1 1  93  93 LYS C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
       578 . 1 1  93  93 LYS CB  C 13  37.84 0.50 . 1 . . . . . . . . 4664 1 
       579 . 1 1  93  93 LYS N   N 15 113.37 0.25 . 1 . . . . . . . . 4664 1 
       580 . 1 1  94  94 SER H   H  1  11.29 0.03 . 1 . . . . . . . . 4664 1 
       581 . 1 1  94  94 SER HA  H  1   4.78 0.03 . 1 . . . . . . . . 4664 1 
       582 . 1 1  94  94 SER HB2 H  1   4.17 0.03 . 2 . . . . . . . . 4664 1 
       583 . 1 1  94  94 SER HB3 H  1   3.81 0.03 . 2 . . . . . . . . 4664 1 
       584 . 1 1  94  94 SER CA  C 13  61.05 0.50 . 1 . . . . . . . . 4664 1 
       585 . 1 1  94  94 SER C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       586 . 1 1  94  94 SER CB  C 13  68.64 0.50 . 1 . . . . . . . . 4664 1 
       587 . 1 1  94  94 SER N   N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 
       588 . 1 1  95  95 TYR H   H  1   8.40 0.03 . 1 . . . . . . . . 4664 1 
       589 . 1 1  95  95 TYR HA  H  1   6.08 0.03 . 1 . . . . . . . . 4664 1 
       590 . 1 1  95  95 TYR HB2 H  1   3.22 0.03 . 2 . . . . . . . . 4664 1 
       591 . 1 1  95  95 TYR HB3 H  1   3.08 0.03 . 2 . . . . . . . . 4664 1 
       592 . 1 1  95  95 TYR CA  C 13  58.52 0.50 . 1 . . . . . . . . 4664 1 
       593 . 1 1  95  95 TYR C   C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 
       594 . 1 1  95  95 TYR CB  C 13  42.75 0.50 . 1 . . . . . . . . 4664 1 
       595 . 1 1  95  95 TYR N   N 15 123.50 0.25 . 1 . . . . . . . . 4664 1 
       596 . 1 1  96  96 ALA H   H  1   9.01 0.03 . 1 . . . . . . . . 4664 1 
       597 . 1 1  96  96 ALA HA  H  1   4.53 0.03 . 1 . . . . . . . . 4664 1 
       598 . 1 1  96  96 ALA HB1 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       599 . 1 1  96  96 ALA HB2 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       600 . 1 1  96  96 ALA HB3 H  1   0.90 0.03 . 1 . . . . . . . . 4664 1 
       601 . 1 1  96  96 ALA CA  C 13  53.37 0.50 . 1 . . . . . . . . 4664 1 
       602 . 1 1  96  96 ALA C   C 13 175.70 0.50 . 1 . . . . . . . . 4664 1 
       603 . 1 1  96  96 ALA CB  C 13  24.23 0.50 . 1 . . . . . . . . 4664 1 
       604 . 1 1  96  96 ALA N   N 15 121.67 0.25 . 1 . . . . . . . . 4664 1 
       605 . 1 1  97  97 VAL H   H  1   9.26 0.03 . 1 . . . . . . . . 4664 1 
       606 . 1 1  97  97 VAL HA  H  1   4.95 0.03 . 1 . . . . . . . . 4664 1 
       607 . 1 1  97  97 VAL HB  H  1   2.09 0.03 . 1 . . . . . . . . 4664 1 
       608 . 1 1  97  97 VAL CA  C 13  63.45 0.50 . 1 . . . . . . . . 4664 1 
       609 . 1 1  97  97 VAL C   C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 
       610 . 1 1  97  97 VAL CB  C 13  33.48 0.50 . 1 . . . . . . . . 4664 1 
       611 . 1 1  97  97 VAL N   N 15 122.55 0.25 . 1 . . . . . . . . 4664 1 
       612 . 1 1  98  98 ILE H   H  1   9.50 0.03 . 1 . . . . . . . . 4664 1 
       613 . 1 1  98  98 ILE HA  H  1   5.07 0.03 . 1 . . . . . . . . 4664 1 
       614 . 1 1  98  98 ILE HB  H  1   1.91 0.03 . 1 . . . . . . . . 4664 1 
       615 . 1 1  98  98 ILE CA  C 13  58.91 0.50 . 1 . . . . . . . . 4664 1 
       616 . 1 1  98  98 ILE C   C 13 175.20 0.50 . 1 . . . . . . . . 4664 1 
       617 . 1 1  98  98 ILE CB  C 13  42.54 0.50 . 1 . . . . . . . . 4664 1 
       618 . 1 1  98  98 ILE N   N 15 131.11 0.25 . 1 . . . . . . . . 4664 1 
       619 . 1 1  99  99 TYR H   H  1   9.47 0.03 . 1 . . . . . . . . 4664 1 
       620 . 1 1  99  99 TYR HA  H  1   5.19 0.03 . 1 . . . . . . . . 4664 1 
       621 . 1 1  99  99 TYR HB2 H  1   2.59 0.03 . 1 . . . . . . . . 4664 1 
       622 . 1 1  99  99 TYR HB3 H  1   2.59 0.03 . 1 . . . . . . . . 4664 1 
       623 . 1 1  99  99 TYR CA  C 13  57.79 0.50 . 1 . . . . . . . . 4664 1 
       624 . 1 1  99  99 TYR C   C 13 174.80 0.50 . 1 . . . . . . . . 4664 1 
       625 . 1 1  99  99 TYR CB  C 13  42.17 0.50 . 1 . . . . . . . . 4664 1 
       626 . 1 1  99  99 TYR N   N 15 128.87 0.25 . 1 . . . . . . . . 4664 1 
       627 . 1 1 100 100 ALA H   H  1   9.53 0.03 . 1 . . . . . . . . 4664 1 
       628 . 1 1 100 100 ALA HA  H  1   5.63 0.03 . 1 . . . . . . . . 4664 1 
       629 . 1 1 100 100 ALA HB1 H  1   1.42 0.03 . 1 . . . . . . . . 4664 1 
       630 . 1 1 100 100 ALA HB2 H  1   1.42 0.03 . 1 . . . . . . . . 4664 1 
       631 . 1 1 100 100 ALA HB3 H  1   1.42 0.03 . 1 . . . . . . . . 4664 1 
       632 . 1 1 100 100 ALA CA  C 13  51.41 0.50 . 1 . . . . . . . . 4664 1 
       633 . 1 1 100 100 ALA C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
       634 . 1 1 100 100 ALA CB  C 13  24.85 0.50 . 1 . . . . . . . . 4664 1 
       635 . 1 1 100 100 ALA N   N 15 135.26 0.25 . 1 . . . . . . . . 4664 1 
       636 . 1 1 101 101 THR H   H  1   9.35 0.03 . 1 . . . . . . . . 4664 1 
       637 . 1 1 101 101 THR HA  H  1   5.33 0.03 . 1 . . . . . . . . 4664 1 
       638 . 1 1 101 101 THR HB  H  1   3.94 0.03 . 1 . . . . . . . . 4664 1 
       639 . 1 1 101 101 THR CA  C 13  62.05 0.50 . 1 . . . . . . . . 4664 1 
       640 . 1 1 101 101 THR C   C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 
       641 . 1 1 101 101 THR CB  C 13  73.12 0.50 . 1 . . . . . . . . 4664 1 
       642 . 1 1 101 101 THR N   N 15 117.35 0.25 . 1 . . . . . . . . 4664 1 
       643 . 1 1 102 102 ARG H   H  1   8.91 0.03 . 1 . . . . . . . . 4664 1 
       644 . 1 1 102 102 ARG HA  H  1   5.17 0.03 . 1 . . . . . . . . 4664 1 
       645 . 1 1 102 102 ARG CA  C 13  55.38 0.50 . 1 . . . . . . . . 4664 1 
       646 . 1 1 102 102 ARG C   C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 
       647 . 1 1 102 102 ARG CB  C 13  36.22 0.50 . 1 . . . . . . . . 4664 1 
       648 . 1 1 102 102 ARG N   N 15 126.75 0.25 . 1 . . . . . . . . 4664 1 
       649 . 1 1 103 103 VAL H   H  1   7.74 0.03 . 1 . . . . . . . . 4664 1 
       650 . 1 1 103 103 VAL HA  H  1   4.68 0.03 . 1 . . . . . . . . 4664 1 
       651 . 1 1 103 103 VAL CA  C 13  62.43 0.50 . 1 . . . . . . . . 4664 1 
       652 . 1 1 103 103 VAL C   C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 
       653 . 1 1 103 103 VAL CB  C 13  33.31 0.50 . 1 . . . . . . . . 4664 1 
       654 . 1 1 103 103 VAL N   N 15 123.16 0.25 . 1 . . . . . . . . 4664 1 
       655 . 1 1 104 104 LYS H   H  1   8.88 0.03 . 1 . . . . . . . . 4664 1 
       656 . 1 1 104 104 LYS HA  H  1   4.33 0.03 . 1 . . . . . . . . 4664 1 
       657 . 1 1 104 104 LYS HB2 H  1   1.41 0.03 . 1 . . . . . . . . 4664 1 
       658 . 1 1 104 104 LYS HB3 H  1   1.41 0.03 . 1 . . . . . . . . 4664 1 
       659 . 1 1 104 104 LYS CA  C 13  55.97 0.50 . 1 . . . . . . . . 4664 1 
       660 . 1 1 104 104 LYS CB  C 13  36.55 0.50 . 1 . . . . . . . . 4664 1 
       661 . 1 1 104 104 LYS N   N 15 130.93 0.25 . 1 . . . . . . . . 4664 1 
       662 . 1 1 105 105 ASP H   H  1   9.39 0.03 . 1 . . . . . . . . 4664 1 
       663 . 1 1 105 105 ASP HA  H  1   4.66 0.03 . 1 . . . . . . . . 4664 1 
       664 . 1 1 105 105 ASP CA  C 13  56.45 0.50 . 1 . . . . . . . . 4664 1 
       665 . 1 1 105 105 ASP C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       666 . 1 1 105 105 ASP CB  C 13  40.53 0.50 . 1 . . . . . . . . 4664 1 
       667 . 1 1 105 105 ASP N   N 15 130.04 0.25 . 1 . . . . . . . . 4664 1 
       668 . 1 1 106 106 GLY H   H  1   8.24 0.03 . 1 . . . . . . . . 4664 1 
       669 . 1 1 106 106 GLY HA2 H  1   4.02 0.03 . 2 . . . . . . . . 4664 1 
       670 . 1 1 106 106 GLY HA3 H  1   3.45 0.03 . 2 . . . . . . . . 4664 1 
       671 . 1 1 106 106 GLY CA  C 13  46.34 0.50 . 1 . . . . . . . . 4664 1 
       672 . 1 1 106 106 GLY C   C 13 174.60 0.50 . 1 . . . . . . . . 4664 1 
       673 . 1 1 106 106 GLY N   N 15 103.63 0.25 . 1 . . . . . . . . 4664 1 
       674 . 1 1 107 107 ARG H   H  1   7.78 0.03 . 1 . . . . . . . . 4664 1 
       675 . 1 1 107 107 ARG HA  H  1   4.58 0.03 . 1 . . . . . . . . 4664 1 
       676 . 1 1 107 107 ARG HB2 H  1   1.73 0.03 . 1 . . . . . . . . 4664 1 
       677 . 1 1 107 107 ARG HB3 H  1   1.73 0.03 . 1 . . . . . . . . 4664 1 
       678 . 1 1 107 107 ARG CA  C 13  55.40 0.50 . 1 . . . . . . . . 4664 1 
       679 . 1 1 107 107 ARG C   C 13 175.60 0.50 . 1 . . . . . . . . 4664 1 
       680 . 1 1 107 107 ARG CB  C 13  33.35 0.50 . 1 . . . . . . . . 4664 1 
       681 . 1 1 107 107 ARG N   N 15 122.00 0.25 . 1 . . . . . . . . 4664 1 
       682 . 1 1 108 108 THR H   H  1   8.56 0.03 . 1 . . . . . . . . 4664 1 
       683 . 1 1 108 108 THR HA  H  1   4.40 0.03 . 1 . . . . . . . . 4664 1 
       684 . 1 1 108 108 THR HB  H  1   3.86 0.03 . 1 . . . . . . . . 4664 1 
       685 . 1 1 108 108 THR CA  C 13  64.18 0.50 . 1 . . . . . . . . 4664 1 
       686 . 1 1 108 108 THR C   C 13 174.40 0.50 . 1 . . . . . . . . 4664 1 
       687 . 1 1 108 108 THR CB  C 13  69.73 0.50 . 1 . . . . . . . . 4664 1 
       688 . 1 1 108 108 THR N   N 15 119.62 0.25 . 1 . . . . . . . . 4664 1 
       689 . 1 1 109 109 LEU H   H  1   9.13 0.03 . 1 . . . . . . . . 4664 1 
       690 . 1 1 109 109 LEU HA  H  1   4.63 0.03 . 1 . . . . . . . . 4664 1 
       691 . 1 1 109 109 LEU CA  C 13  54.27 0.50 . 1 . . . . . . . . 4664 1 
       692 . 1 1 109 109 LEU C   C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 
       693 . 1 1 109 109 LEU N   N 15 129.73 0.25 . 1 . . . . . . . . 4664 1 
       694 . 1 1 110 110 HIS H   H  1   8.39 0.03 . 1 . . . . . . . . 4664 1 
       695 . 1 1 110 110 HIS HA  H  1   5.94 0.03 . 1 . . . . . . . . 4664 1 
       696 . 1 1 110 110 HIS HB2 H  1   2.96 0.03 . 2 . . . . . . . . 4664 1 
       697 . 1 1 110 110 HIS HB3 H  1   2.89 0.03 . 2 . . . . . . . . 4664 1 
       698 . 1 1 110 110 HIS CA  C 13  55.28 0.50 . 1 . . . . . . . . 4664 1 
       699 . 1 1 110 110 HIS C   C 13 176.10 0.50 . 1 . . . . . . . . 4664 1 
       700 . 1 1 110 110 HIS CB  C 13  34.39 0.50 . 1 . . . . . . . . 4664 1 
       701 . 1 1 110 110 HIS N   N 15 116.91 0.25 . 1 . . . . . . . . 4664 1 
       702 . 1 1 111 111 MET H   H  1   9.01 0.03 . 1 . . . . . . . . 4664 1 
       703 . 1 1 111 111 MET HA  H  1   4.49 0.03 . 1 . . . . . . . . 4664 1 
       704 . 1 1 111 111 MET HB2 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       705 . 1 1 111 111 MET HB3 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       706 . 1 1 111 111 MET CA  C 13  56.25 0.50 . 1 . . . . . . . . 4664 1 
       707 . 1 1 111 111 MET C   C 13 174.90 0.50 . 1 . . . . . . . . 4664 1 
       708 . 1 1 111 111 MET CB  C 13  37.58 0.50 . 1 . . . . . . . . 4664 1 
       709 . 1 1 111 111 MET N   N 15 124.18 0.25 . 1 . . . . . . . . 4664 1 
       710 . 1 1 112 112 MET H   H  1   9.06 0.03 . 1 . . . . . . . . 4664 1 
       711 . 1 1 112 112 MET HA  H  1   5.58 0.03 . 1 . . . . . . . . 4664 1 
       712 . 1 1 112 112 MET HB2 H  1   2.05 0.03 . 1 . . . . . . . . 4664 1 
       713 . 1 1 112 112 MET HB3 H  1   2.05 0.03 . 1 . . . . . . . . 4664 1 
       714 . 1 1 112 112 MET CA  C 13  55.32 0.50 . 1 . . . . . . . . 4664 1 
       715 . 1 1 112 112 MET C   C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 
       716 . 1 1 112 112 MET CB  C 13  37.15 0.50 . 1 . . . . . . . . 4664 1 
       717 . 1 1 112 112 MET N   N 15 123.86 0.25 . 1 . . . . . . . . 4664 1 
       718 . 1 1 113 113 ARG H   H  1   9.37 0.03 . 1 . . . . . . . . 4664 1 
       719 . 1 1 113 113 ARG HA  H  1   5.00 0.03 . 1 . . . . . . . . 4664 1 
       720 . 1 1 113 113 ARG CA  C 13  55.67 0.50 . 1 . . . . . . . . 4664 1 
       721 . 1 1 113 113 ARG C   C 13 175.00 0.50 . 1 . . . . . . . . 4664 1 
       722 . 1 1 113 113 ARG CB  C 13  38.27 0.50 . 1 . . . . . . . . 4664 1 
       723 . 1 1 113 113 ARG N   N 15 120.04 0.25 . 1 . . . . . . . . 4664 1 
       724 . 1 1 114 114 LEU H   H  1   7.96 0.03 . 1 . . . . . . . . 4664 1 
       725 . 1 1 114 114 LEU HA  H  1   4.99 0.03 . 1 . . . . . . . . 4664 1 
       726 . 1 1 114 114 LEU HB2 H  1   2.24 0.03 . 1 . . . . . . . . 4664 1 
       727 . 1 1 114 114 LEU HB3 H  1   2.24 0.03 . 1 . . . . . . . . 4664 1 
       728 . 1 1 114 114 LEU CA  C 13  54.25 0.50 . 1 . . . . . . . . 4664 1 
       729 . 1 1 114 114 LEU C   C 13 175.33 0.50 . 1 . . . . . . . . 4664 1 
       730 . 1 1 114 114 LEU CB  C 13  43.89 0.50 . 1 . . . . . . . . 4664 1 
       731 . 1 1 114 114 LEU N   N 15 125.31 0.25 . 1 . . . . . . . . 4664 1 
       732 . 1 1 115 115 TYR H   H  1   9.54 0.03 . 1 . . . . . . . . 4664 1 
       733 . 1 1 115 115 TYR CA  C 13  58.11 0.50 . 1 . . . . . . . . 4664 1 
       734 . 1 1 115 115 TYR C   C 13 177.70 0.50 . 1 . . . . . . . . 4664 1 
       735 . 1 1 115 115 TYR N   N 15 126.76 0.25 . 1 . . . . . . . . 4664 1 
       736 . 1 1 116 116 SER H   H  1   9.85 0.03 . 1 . . . . . . . . 4664 1 
       737 . 1 1 116 116 SER HA  H  1   5.73 0.03 . 1 . . . . . . . . 4664 1 
       738 . 1 1 116 116 SER HB2 H  1   3.89 0.03 . 2 . . . . . . . . 4664 1 
       739 . 1 1 116 116 SER HB3 H  1   3.59 0.03 . 2 . . . . . . . . 4664 1 
       740 . 1 1 116 116 SER CA  C 13  56.55 0.50 . 1 . . . . . . . . 4664 1 
       741 . 1 1 116 116 SER C   C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 
       742 . 1 1 116 116 SER CB  C 13  67.66 0.50 . 1 . . . . . . . . 4664 1 
       743 . 1 1 116 116 SER N   N 15 113.93 0.25 . 1 . . . . . . . . 4664 1 
       744 . 1 1 117 117 ARG H   H  1   8.25 0.03 . 1 . . . . . . . . 4664 1 
       745 . 1 1 117 117 ARG HA  H  1   3.60 0.03 . 1 . . . . . . . . 4664 1 
       746 . 1 1 117 117 ARG HB2 H  1   1.79 0.03 . 2 . . . . . . . . 4664 1 
       747 . 1 1 117 117 ARG HB3 H  1   1.28 0.03 . 2 . . . . . . . . 4664 1 
       748 . 1 1 117 117 ARG CA  C 13  58.08 0.50 . 1 . . . . . . . . 4664 1 
       749 . 1 1 117 117 ARG C   C 13 176.40 0.50 . 1 . . . . . . . . 4664 1 
       750 . 1 1 117 117 ARG CB  C 13  32.45 0.50 . 1 . . . . . . . . 4664 1 
       751 . 1 1 117 117 ARG N   N 15 131.38 0.25 . 1 . . . . . . . . 4664 1 
       752 . 1 1 118 118 SER H   H  1   7.87 0.03 . 1 . . . . . . . . 4664 1 
       753 . 1 1 118 118 SER HA  H  1   4.90 0.03 . 1 . . . . . . . . 4664 1 
       754 . 1 1 118 118 SER HB2 H  1   3.88 0.03 . 2 . . . . . . . . 4664 1 
       755 . 1 1 118 118 SER HB3 H  1   3.59 0.03 . 2 . . . . . . . . 4664 1 
       756 . 1 1 118 118 SER CA  C 13  54.79 0.50 . 1 . . . . . . . . 4664 1 
       757 . 1 1 118 118 SER CB  C 13  65.77 0.50 . 1 . . . . . . . . 4664 1 
       758 . 1 1 118 118 SER N   N 15 111.94 0.25 . 1 . . . . . . . . 4664 1 
       759 . 1 1 119 119 PRO HA  H  1   4.01 0.03 . 1 . . . . . . . . 4664 1 
       760 . 1 1 119 119 PRO HB2 H  1   2.23 0.03 . 2 . . . . . . . . 4664 1 
       761 . 1 1 119 119 PRO HB3 H  1   1.94 0.03 . 2 . . . . . . . . 4664 1 
       762 . 1 1 119 119 PRO CA  C 13  64.97 0.50 . 1 . . . . . . . . 4664 1 
       763 . 1 1 119 119 PRO C   C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 
       764 . 1 1 119 119 PRO CB  C 13  32.43 0.50 . 1 . . . . . . . . 4664 1 
       765 . 1 1 120 120 GLU H   H  1   7.30 0.03 . 1 . . . . . . . . 4664 1 
       766 . 1 1 120 120 GLU HA  H  1   4.17 0.03 . 1 . . . . . . . . 4664 1 
       767 . 1 1 120 120 GLU HB2 H  1   1.74 0.03 . 2 . . . . . . . . 4664 1 
       768 . 1 1 120 120 GLU HB3 H  1   1.69 0.03 . 2 . . . . . . . . 4664 1 
       769 . 1 1 120 120 GLU CA  C 13  55.88 0.50 . 1 . . . . . . . . 4664 1 
       770 . 1 1 120 120 GLU C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       771 . 1 1 120 120 GLU CB  C 13  29.71 0.50 . 1 . . . . . . . . 4664 1 
       772 . 1 1 120 120 GLU N   N 15 118.13 0.25 . 1 . . . . . . . . 4664 1 
       773 . 1 1 121 121 VAL H   H  1   7.81 0.03 . 1 . . . . . . . . 4664 1 
       774 . 1 1 121 121 VAL HA  H  1   4.07 0.03 . 1 . . . . . . . . 4664 1 
       775 . 1 1 121 121 VAL HB  H  1   1.76 0.03 . 1 . . . . . . . . 4664 1 
       776 . 1 1 121 121 VAL CA  C 13  61.71 0.50 . 1 . . . . . . . . 4664 1 
       777 . 1 1 121 121 VAL C   C 13 175.50 0.50 . 1 . . . . . . . . 4664 1 
       778 . 1 1 121 121 VAL CB  C 13  34.22 0.50 . 1 . . . . . . . . 4664 1 
       779 . 1 1 121 121 VAL N   N 15 125.71 0.25 . 1 . . . . . . . . 4664 1 
       780 . 1 1 122 122 SER H   H  1   8.57 0.03 . 1 . . . . . . . . 4664 1 
       781 . 1 1 122 122 SER HA  H  1   4.68 0.03 . 1 . . . . . . . . 4664 1 
       782 . 1 1 122 122 SER HB2 H  1   4.20 0.03 . 2 . . . . . . . . 4664 1 
       783 . 1 1 122 122 SER HB3 H  1   3.88 0.03 . 2 . . . . . . . . 4664 1 
       784 . 1 1 122 122 SER CA  C 13  57.23 0.50 . 1 . . . . . . . . 4664 1 
       785 . 1 1 122 122 SER CB  C 13  64.40 0.50 . 1 . . . . . . . . 4664 1 
       786 . 1 1 122 122 SER N   N 15 125.18 0.25 . 1 . . . . . . . . 4664 1 
       787 . 1 1 123 123 PRO HA  H  1   4.26 0.03 . 1 . . . . . . . . 4664 1 
       788 . 1 1 123 123 PRO HB2 H  1   2.29 0.03 . 2 . . . . . . . . 4664 1 
       789 . 1 1 123 123 PRO HB3 H  1   1.87 0.03 . 2 . . . . . . . . 4664 1 
       790 . 1 1 123 123 PRO CA  C 13  65.91 0.50 . 1 . . . . . . . . 4664 1 
       791 . 1 1 123 123 PRO C   C 13 180.40 0.50 . 1 . . . . . . . . 4664 1 
       792 . 1 1 123 123 PRO CB  C 13  32.57 0.50 . 1 . . . . . . . . 4664 1 
       793 . 1 1 124 124 ALA H   H  1   7.93 0.03 . 1 . . . . . . . . 4664 1 
       794 . 1 1 124 124 ALA HA  H  1   4.01 0.03 . 1 . . . . . . . . 4664 1 
       795 . 1 1 124 124 ALA HB1 H  1   1.23 0.03 . 1 . . . . . . . . 4664 1 
       796 . 1 1 124 124 ALA HB2 H  1   1.23 0.03 . 1 . . . . . . . . 4664 1 
       797 . 1 1 124 124 ALA HB3 H  1   1.23 0.03 . 1 . . . . . . . . 4664 1 
       798 . 1 1 124 124 ALA CA  C 13  55.92 0.50 . 1 . . . . . . . . 4664 1 
       799 . 1 1 124 124 ALA C   C 13 180.90 0.50 . 1 . . . . . . . . 4664 1 
       800 . 1 1 124 124 ALA CB  C 13  19.15 0.50 . 1 . . . . . . . . 4664 1 
       801 . 1 1 124 124 ALA N   N 15 120.88 0.25 . 1 . . . . . . . . 4664 1 
       802 . 1 1 125 125 ALA H   H  1   7.41 0.03 . 1 . . . . . . . . 4664 1 
       803 . 1 1 125 125 ALA HA  H  1   3.37 0.03 . 1 . . . . . . . . 4664 1 
       804 . 1 1 125 125 ALA HB1 H  1   1.08 0.03 . 1 . . . . . . . . 4664 1 
       805 . 1 1 125 125 ALA HB2 H  1   1.08 0.03 . 1 . . . . . . . . 4664 1 
       806 . 1 1 125 125 ALA HB3 H  1   1.08 0.03 . 1 . . . . . . . . 4664 1 
       807 . 1 1 125 125 ALA CA  C 13  55.59 0.50 . 1 . . . . . . . . 4664 1 
       808 . 1 1 125 125 ALA C   C 13 180.20 0.50 . 1 . . . . . . . . 4664 1 
       809 . 1 1 125 125 ALA CB  C 13  19.36 0.50 . 1 . . . . . . . . 4664 1 
       810 . 1 1 125 125 ALA N   N 15 121.76 0.25 . 1 . . . . . . . . 4664 1 
       811 . 1 1 126 126 THR H   H  1   7.73 0.03 . 1 . . . . . . . . 4664 1 
       812 . 1 1 126 126 THR HA  H  1   4.08 0.03 . 1 . . . . . . . . 4664 1 
       813 . 1 1 126 126 THR HB  H  1   3.52 0.03 . 1 . . . . . . . . 4664 1 
       814 . 1 1 126 126 THR CA  C 13  67.66 0.50 . 1 . . . . . . . . 4664 1 
       815 . 1 1 126 126 THR C   C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 
       816 . 1 1 126 126 THR CB  C 13  68.88 0.50 . 1 . . . . . . . . 4664 1 
       817 . 1 1 126 126 THR N   N 15 113.98 0.25 . 1 . . . . . . . . 4664 1 
       818 . 1 1 127 127 ALA H   H  1   7.80 0.03 . 1 . . . . . . . . 4664 1 
       819 . 1 1 127 127 ALA HA  H  1   4.01 0.03 . 1 . . . . . . . . 4664 1 
       820 . 1 1 127 127 ALA HB1 H  1   1.36 0.03 . 1 . . . . . . . . 4664 1 
       821 . 1 1 127 127 ALA HB2 H  1   1.36 0.03 . 1 . . . . . . . . 4664 1 
       822 . 1 1 127 127 ALA HB3 H  1   1.36 0.03 . 1 . . . . . . . . 4664 1 
       823 . 1 1 127 127 ALA CA  C 13  56.33 0.50 . 1 . . . . . . . . 4664 1 
       824 . 1 1 127 127 ALA C   C 13 172.36 0.50 . 1 . . . . . . . . 4664 1 
       825 . 1 1 127 127 ALA CB  C 13  18.76 0.50 . 1 . . . . . . . . 4664 1 
       826 . 1 1 127 127 ALA N   N 15 123.92 0.25 . 1 . . . . . . . . 4664 1 
       827 . 1 1 128 128 ILE H   H  1   7.55 0.03 . 1 . . . . . . . . 4664 1 
       828 . 1 1 128 128 ILE HA  H  1   3.67 0.03 . 1 . . . . . . . . 4664 1 
       829 . 1 1 128 128 ILE HB  H  1   1.62 0.03 . 1 . . . . . . . . 4664 1 
       830 . 1 1 128 128 ILE CA  C 13  65.67 0.50 . 1 . . . . . . . . 4664 1 
       831 . 1 1 128 128 ILE C   C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 
       832 . 1 1 128 128 ILE CB  C 13  39.51 0.50 . 1 . . . . . . . . 4664 1 
       833 . 1 1 128 128 ILE N   N 15 121.69 0.25 . 1 . . . . . . . . 4664 1 
       834 . 1 1 129 129 PHE H   H  1   8.16 0.03 . 1 . . . . . . . . 4664 1 
       835 . 1 1 129 129 PHE HA  H  1   3.94 0.03 . 1 . . . . . . . . 4664 1 
       836 . 1 1 129 129 PHE HB2 H  1   3.20 0.03 . 2 . . . . . . . . 4664 1 
       837 . 1 1 129 129 PHE HB3 H  1   3.13 0.03 . 2 . . . . . . . . 4664 1 
       838 . 1 1 129 129 PHE CA  C 13  63.35 0.50 . 1 . . . . . . . . 4664 1 
       839 . 1 1 129 129 PHE C   C 13 177.10 0.50 . 1 . . . . . . . . 4664 1 
       840 . 1 1 129 129 PHE CB  C 13  41.12 0.50 . 1 . . . . . . . . 4664 1 
       841 . 1 1 129 129 PHE N   N 15 120.96 0.25 . 1 . . . . . . . . 4664 1 
       842 . 1 1 130 130 ARG H   H  1   8.55 0.03 . 1 . . . . . . . . 4664 1 
       843 . 1 1 130 130 ARG HA  H  1   3.48 0.03 . 1 . . . . . . . . 4664 1 
       844 . 1 1 130 130 ARG HB2 H  1   1.88 0.03 . 2 . . . . . . . . 4664 1 
       845 . 1 1 130 130 ARG HB3 H  1   1.75 0.03 . 2 . . . . . . . . 4664 1 
       846 . 1 1 130 130 ARG CA  C 13  61.04 0.50 . 1 . . . . . . . . 4664 1 
       847 . 1 1 130 130 ARG C   C 13 180.40 0.50 . 1 . . . . . . . . 4664 1 
       848 . 1 1 130 130 ARG CB  C 13  30.75 0.50 . 1 . . . . . . . . 4664 1 
       849 . 1 1 130 130 ARG N   N 15 117.06 0.25 . 1 . . . . . . . . 4664 1 
       850 . 1 1 131 131 LYS H   H  1   7.92 0.03 . 1 . . . . . . . . 4664 1 
       851 . 1 1 131 131 LYS HA  H  1   3.95 0.03 . 1 . . . . . . . . 4664 1 
       852 . 1 1 131 131 LYS HB2 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       853 . 1 1 131 131 LYS HB3 H  1   1.83 0.03 . 1 . . . . . . . . 4664 1 
       854 . 1 1 131 131 LYS CA  C 13  60.41 0.50 . 1 . . . . . . . . 4664 1 
       855 . 1 1 131 131 LYS C   C 13 180.30 0.50 . 1 . . . . . . . . 4664 1 
       856 . 1 1 131 131 LYS CB  C 13  33.42 0.50 . 1 . . . . . . . . 4664 1 
       857 . 1 1 131 131 LYS N   N 15 122.91 0.25 . 1 . . . . . . . . 4664 1 
       858 . 1 1 132 132 LEU H   H  1   8.35 0.03 . 1 . . . . . . . . 4664 1 
       859 . 1 1 132 132 LEU HA  H  1   3.86 0.03 . 1 . . . . . . . . 4664 1 
       860 . 1 1 132 132 LEU HB2 H  1   1.63 0.03 . 1 . . . . . . . . 4664 1 
       861 . 1 1 132 132 LEU HB3 H  1   1.63 0.03 . 1 . . . . . . . . 4664 1 
       862 . 1 1 132 132 LEU CA  C 13  58.58 0.50 . 1 . . . . . . . . 4664 1 
       863 . 1 1 132 132 LEU C   C 13 180.60 0.50 . 1 . . . . . . . . 4664 1 
       864 . 1 1 132 132 LEU CB  C 13  42.45 0.50 . 1 . . . . . . . . 4664 1 
       865 . 1 1 132 132 LEU N   N 15 120.95 0.25 . 1 . . . . . . . . 4664 1 
       866 . 1 1 133 133 ALA H   H  1   8.66 0.03 . 1 . . . . . . . . 4664 1 
       867 . 1 1 133 133 ALA HA  H  1   3.89 0.03 . 1 . . . . . . . . 4664 1 
       868 . 1 1 133 133 ALA HB1 H  1   0.79 0.03 . 1 . . . . . . . . 4664 1 
       869 . 1 1 133 133 ALA HB2 H  1   0.79 0.03 . 1 . . . . . . . . 4664 1 
       870 . 1 1 133 133 ALA HB3 H  1   0.79 0.03 . 1 . . . . . . . . 4664 1 
       871 . 1 1 133 133 ALA CA  C 13  56.04 0.50 . 1 . . . . . . . . 4664 1 
       872 . 1 1 133 133 ALA C   C 13 171.89 0.50 . 1 . . . . . . . . 4664 1 
       873 . 1 1 133 133 ALA CB  C 13  16.93 0.50 . 1 . . . . . . . . 4664 1 
       874 . 1 1 133 133 ALA N   N 15 123.18 0.25 . 1 . . . . . . . . 4664 1 
       875 . 1 1 134 134 GLY H   H  1   8.03 0.03 . 1 . . . . . . . . 4664 1 
       876 . 1 1 134 134 GLY HA2 H  1   3.81 0.03 . 1 . . . . . . . . 4664 1 
       877 . 1 1 134 134 GLY HA3 H  1   3.81 0.03 . 1 . . . . . . . . 4664 1 
       878 . 1 1 134 134 GLY CA  C 13  48.08 0.50 . 1 . . . . . . . . 4664 1 
       879 . 1 1 134 134 GLY C   C 13 179.20 0.50 . 1 . . . . . . . . 4664 1 
       880 . 1 1 134 134 GLY N   N 15 108.18 0.25 . 1 . . . . . . . . 4664 1 
       881 . 1 1 135 135 GLU H   H  1   7.63 0.03 . 1 . . . . . . . . 4664 1 
       882 . 1 1 135 135 GLU HA  H  1   3.98 0.03 . 1 . . . . . . . . 4664 1 
       883 . 1 1 135 135 GLU HB2 H  1   1.95 0.03 . 1 . . . . . . . . 4664 1 
       884 . 1 1 135 135 GLU HB3 H  1   1.95 0.03 . 1 . . . . . . . . 4664 1 
       885 . 1 1 135 135 GLU CA  C 13  59.38 0.50 . 1 . . . . . . . . 4664 1 
       886 . 1 1 135 135 GLU C   C 13 178.40 0.50 . 1 . . . . . . . . 4664 1 
       887 . 1 1 135 135 GLU CB  C 13  30.51 0.50 . 1 . . . . . . . . 4664 1 
       888 . 1 1 135 135 GLU N   N 15 122.63 0.25 . 1 . . . . . . . . 4664 1 
       889 . 1 1 136 136 ARG H   H  1   7.03 0.03 . 1 . . . . . . . . 4664 1 
       890 . 1 1 136 136 ARG HA  H  1   4.05 0.03 . 1 . . . . . . . . 4664 1 
       891 . 1 1 136 136 ARG HB2 H  1   1.30 0.03 . 1 . . . . . . . . 4664 1 
       892 . 1 1 136 136 ARG HB3 H  1   1.30 0.03 . 1 . . . . . . . . 4664 1 
       893 . 1 1 136 136 ARG CA  C 13  55.78 0.50 . 1 . . . . . . . . 4664 1 
       894 . 1 1 136 136 ARG C   C 13 174.50 0.50 . 1 . . . . . . . . 4664 1 
       895 . 1 1 136 136 ARG CB  C 13  29.48 0.50 . 1 . . . . . . . . 4664 1 
       896 . 1 1 136 136 ARG N   N 15 118.75 0.25 . 1 . . . . . . . . 4664 1 
       897 . 1 1 137 137 ASN H   H  1   7.47 0.03 . 1 . . . . . . . . 4664 1 
       898 . 1 1 137 137 ASN HA  H  1   4.06 0.03 . 1 . . . . . . . . 4664 1 
       899 . 1 1 137 137 ASN HB2 H  1   2.79 0.03 . 2 . . . . . . . . 4664 1 
       900 . 1 1 137 137 ASN HB3 H  1   2.72 0.03 . 2 . . . . . . . . 4664 1 
       901 . 1 1 137 137 ASN CA  C 13  55.79 0.50 . 1 . . . . . . . . 4664 1 
       902 . 1 1 137 137 ASN C   C 13 175.20 0.50 . 1 . . . . . . . . 4664 1 
       903 . 1 1 137 137 ASN CB  C 13  37.14 0.50 . 1 . . . . . . . . 4664 1 
       904 . 1 1 137 137 ASN N   N 15 110.33 0.25 . 1 . . . . . . . . 4664 1 
       905 . 1 1 138 138 TYR H   H  1   7.92 0.03 . 1 . . . . . . . . 4664 1 
       906 . 1 1 138 138 TYR HA  H  1   5.22 0.03 . 1 . . . . . . . . 4664 1 
       907 . 1 1 138 138 TYR HB2 H  1   2.50 0.03 . 2 . . . . . . . . 4664 1 
       908 . 1 1 138 138 TYR HB3 H  1   2.45 0.03 . 2 . . . . . . . . 4664 1 
       909 . 1 1 138 138 TYR CA  C 13  57.67 0.50 . 1 . . . . . . . . 4664 1 
       910 . 1 1 138 138 TYR C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       911 . 1 1 138 138 TYR CB  C 13  37.57 0.50 . 1 . . . . . . . . 4664 1 
       912 . 1 1 138 138 TYR N   N 15 119.40 0.25 . 1 . . . . . . . . 4664 1 
       913 . 1 1 139 139 THR H   H  1   7.64 0.03 . 1 . . . . . . . . 4664 1 
       914 . 1 1 139 139 THR HA  H  1   4.34 0.03 . 1 . . . . . . . . 4664 1 
       915 . 1 1 139 139 THR HB  H  1   4.63 0.03 . 1 . . . . . . . . 4664 1 
       916 . 1 1 139 139 THR CA  C 13  61.40 0.50 . 1 . . . . . . . . 4664 1 
       917 . 1 1 139 139 THR C   C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 
       918 . 1 1 139 139 THR CB  C 13  71.19 0.50 . 1 . . . . . . . . 4664 1 
       919 . 1 1 139 139 THR N   N 15 115.69 0.25 . 1 . . . . . . . . 4664 1 
       920 . 1 1 140 140 ASP H   H  1   8.52 0.03 . 1 . . . . . . . . 4664 1 
       921 . 1 1 140 140 ASP HA  H  1   4.18 0.03 . 1 . . . . . . . . 4664 1 
       922 . 1 1 140 140 ASP HB2 H  1   2.61 0.03 . 1 . . . . . . . . 4664 1 
       923 . 1 1 140 140 ASP HB3 H  1   2.61 0.03 . 1 . . . . . . . . 4664 1 
       924 . 1 1 140 140 ASP CA  C 13  59.04 0.50 . 1 . . . . . . . . 4664 1 
       925 . 1 1 140 140 ASP C   C 13 179.40 0.50 . 1 . . . . . . . . 4664 1 
       926 . 1 1 140 140 ASP CB  C 13  41.89 0.50 . 1 . . . . . . . . 4664 1 
       927 . 1 1 140 140 ASP N   N 15 118.66 0.25 . 1 . . . . . . . . 4664 1 
       928 . 1 1 141 141 GLU H   H  1   8.41 0.03 . 1 . . . . . . . . 4664 1 
       929 . 1 1 141 141 GLU HA  H  1   4.19 0.03 . 1 . . . . . . . . 4664 1 
       930 . 1 1 141 141 GLU HB2 H  1   2.03 0.03 . 2 . . . . . . . . 4664 1 
       931 . 1 1 141 141 GLU HB3 H  1   1.97 0.03 . 2 . . . . . . . . 4664 1 
       932 . 1 1 141 141 GLU CA  C 13  59.08 0.50 . 1 . . . . . . . . 4664 1 
       933 . 1 1 141 141 GLU C   C 13 177.20 0.50 . 1 . . . . . . . . 4664 1 
       934 . 1 1 141 141 GLU CB  C 13  30.12 0.50 . 1 . . . . . . . . 4664 1 
       935 . 1 1 141 141 GLU N   N 15 117.55 0.25 . 1 . . . . . . . . 4664 1 
       936 . 1 1 142 142 MET H   H  1   7.87 0.03 . 1 . . . . . . . . 4664 1 
       937 . 1 1 142 142 MET HA  H  1   4.42 0.03 . 1 . . . . . . . . 4664 1 
       938 . 1 1 142 142 MET CA  C 13  56.95 0.50 . 1 . . . . . . . . 4664 1 
       939 . 1 1 142 142 MET C   C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 
       940 . 1 1 142 142 MET CB  C 13  33.63 0.50 . 1 . . . . . . . . 4664 1 
       941 . 1 1 142 142 MET N   N 15 118.24 0.25 . 1 . . . . . . . . 4664 1 
       942 . 1 1 143 143 VAL H   H  1   7.03 0.03 . 1 . . . . . . . . 4664 1 
       943 . 1 1 143 143 VAL HA  H  1   4.71 0.03 . 1 . . . . . . . . 4664 1 
       944 . 1 1 143 143 VAL HB  H  1   2.04 0.03 . 1 . . . . . . . . 4664 1 
       945 . 1 1 143 143 VAL CA  C 13  62.32 0.50 . 1 . . . . . . . . 4664 1 
       946 . 1 1 143 143 VAL C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
       947 . 1 1 143 143 VAL CB  C 13  34.49 0.50 . 1 . . . . . . . . 4664 1 
       948 . 1 1 143 143 VAL N   N 15 117.58 0.25 . 1 . . . . . . . . 4664 1 
       949 . 1 1 144 144 ALA H   H  1   9.52 0.03 . 1 . . . . . . . . 4664 1 
       950 . 1 1 144 144 ALA HA  H  1   4.74 0.03 . 1 . . . . . . . . 4664 1 
       951 . 1 1 144 144 ALA HB1 H  1   1.21 0.03 . 1 . . . . . . . . 4664 1 
       952 . 1 1 144 144 ALA HB2 H  1   1.21 0.03 . 1 . . . . . . . . 4664 1 
       953 . 1 1 144 144 ALA HB3 H  1   1.21 0.03 . 1 . . . . . . . . 4664 1 
       954 . 1 1 144 144 ALA CA  C 13  51.49 0.50 . 1 . . . . . . . . 4664 1 
       955 . 1 1 144 144 ALA C   C 13 176.80 0.50 . 1 . . . . . . . . 4664 1 
       956 . 1 1 144 144 ALA CB  C 13  22.72 0.50 . 1 . . . . . . . . 4664 1 
       957 . 1 1 144 144 ALA N   N 15 131.82 0.25 . 1 . . . . . . . . 4664 1 
       958 . 1 1 145 145 MET H   H  1   8.53 0.03 . 1 . . . . . . . . 4664 1 
       959 . 1 1 145 145 MET HA  H  1   4.85 0.03 . 1 . . . . . . . . 4664 1 
       960 . 1 1 145 145 MET HB2 H  1   1.99 0.03 . 2 . . . . . . . . 4664 1 
       961 . 1 1 145 145 MET HB3 H  1   1.93 0.03 . 2 . . . . . . . . 4664 1 
       962 . 1 1 145 145 MET CA  C 13  54.06 0.50 . 1 . . . . . . . . 4664 1 
       963 . 1 1 145 145 MET C   C 13 177.90 0.50 . 1 . . . . . . . . 4664 1 
       964 . 1 1 145 145 MET CB  C 13  30.13 0.50 . 1 . . . . . . . . 4664 1 
       965 . 1 1 145 145 MET N   N 15 123.10 0.25 . 1 . . . . . . . . 4664 1 
       966 . 1 1 146 146 LEU H   H  1   7.81 0.03 . 1 . . . . . . . . 4664 1 
       967 . 1 1 146 146 LEU CB  C 13  42.96 0.50 . 1 . . . . . . . . 4664 1 
       968 . 1 1 146 146 LEU N   N 15 126.17 0.25 . 1 . . . . . . . . 4664 1 
       969 . 1 1 147 147 PRO HA  H  1   4.49 0.03 . 1 . . . . . . . . 4664 1 
       970 . 1 1 147 147 PRO HB2 H  1   2.31 0.03 . 2 . . . . . . . . 4664 1 
       971 . 1 1 147 147 PRO HB3 H  1   1.84 0.03 . 2 . . . . . . . . 4664 1 
       972 . 1 1 147 147 PRO CA  C 13  63.23 0.50 . 1 . . . . . . . . 4664 1 
       973 . 1 1 147 147 PRO C   C 13 177.30 0.50 . 1 . . . . . . . . 4664 1 
       974 . 1 1 147 147 PRO CB  C 13  33.73 0.50 . 1 . . . . . . . . 4664 1 
       975 . 1 1 148 148 ARG H   H  1   8.43 0.03 . 1 . . . . . . . . 4664 1 
       976 . 1 1 148 148 ARG HA  H  1   4.18 0.03 . 1 . . . . . . . . 4664 1 
       977 . 1 1 148 148 ARG HB2 H  1   1.74 0.03 . 2 . . . . . . . . 4664 1 
       978 . 1 1 148 148 ARG HB3 H  1   1.68 0.03 . 2 . . . . . . . . 4664 1 
       979 . 1 1 148 148 ARG CA  C 13  58.35 0.50 . 1 . . . . . . . . 4664 1 
       980 . 1 1 148 148 ARG C   C 13 176.50 0.50 . 1 . . . . . . . . 4664 1 
       981 . 1 1 148 148 ARG CB  C 13  32.54 0.50 . 1 . . . . . . . . 4664 1 
       982 . 1 1 148 148 ARG N   N 15 121.39 0.25 . 1 . . . . . . . . 4664 1 
       983 . 1 1 149 149 GLN H   H  1   7.66 0.03 . 1 . . . . . . . . 4664 1 
       984 . 1 1 149 149 GLN HA  H  1   4.61 0.03 . 1 . . . . . . . . 4664 1 
       985 . 1 1 149 149 GLN HB2 H  1   2.06 0.03 . 1 . . . . . . . . 4664 1 
       986 . 1 1 149 149 GLN HB3 H  1   2.06 0.03 . 1 . . . . . . . . 4664 1 
       987 . 1 1 149 149 GLN CA  C 13  55.72 0.50 . 1 . . . . . . . . 4664 1 
       988 . 1 1 149 149 GLN C   C 13 175.30 0.50 . 1 . . . . . . . . 4664 1 
       989 . 1 1 149 149 GLN CB  C 13  29.67 0.50 . 1 . . . . . . . . 4664 1 
       990 . 1 1 149 149 GLN N   N 15 115.79 0.25 . 1 . . . . . . . . 4664 1 
       991 . 1 1 150 150 GLU H   H  1   8.47 0.03 . 1 . . . . . . . . 4664 1 
       992 . 1 1 150 150 GLU HA  H  1   4.38 0.03 . 1 . . . . . . . . 4664 1 
       993 . 1 1 150 150 GLU HB2 H  1   2.12 0.03 . 2 . . . . . . . . 4664 1 
       994 . 1 1 150 150 GLU HB3 H  1   1.63 0.03 . 2 . . . . . . . . 4664 1 
       995 . 1 1 150 150 GLU CA  C 13  56.22 0.50 . 1 . . . . . . . . 4664 1 
       996 . 1 1 150 150 GLU C   C 13 176.70 0.50 . 1 . . . . . . . . 4664 1 
       997 . 1 1 150 150 GLU CB  C 13  32.42 0.50 . 1 . . . . . . . . 4664 1 
       998 . 1 1 150 150 GLU N   N 15 118.54 0.25 . 1 . . . . . . . . 4664 1 
       999 . 1 1 151 151 GLU H   H  1   7.92 0.03 . 1 . . . . . . . . 4664 1 
      1000 . 1 1 151 151 GLU HA  H  1   4.17 0.03 . 1 . . . . . . . . 4664 1 
      1001 . 1 1 151 151 GLU HB2 H  1   1.99 0.03 . 1 . . . . . . . . 4664 1 
      1002 . 1 1 151 151 GLU HB3 H  1   1.99 0.03 . 1 . . . . . . . . 4664 1 
      1003 . 1 1 151 151 GLU CA  C 13  59.47 0.50 . 1 . . . . . . . . 4664 1 
      1004 . 1 1 151 151 GLU C   C 13 177.00 0.50 . 1 . . . . . . . . 4664 1 
      1005 . 1 1 151 151 GLU CB  C 13  32.29 0.50 . 1 . . . . . . . . 4664 1 
      1006 . 1 1 151 151 GLU N   N 15 119.93 0.25 . 1 . . . . . . . . 4664 1 
      1007 . 1 1 152 152 CYS H   H  1   9.52 0.03 . 1 . . . . . . . . 4664 1 
      1008 . 1 1 152 152 CYS HA  H  1   5.07 0.03 . 1 . . . . . . . . 4664 1 
      1009 . 1 1 152 152 CYS HB2 H  1   3.01 0.03 . 1 . . . . . . . . 4664 1 
      1010 . 1 1 152 152 CYS HB3 H  1   3.01 0.03 . 1 . . . . . . . . 4664 1 
      1011 . 1 1 152 152 CYS CA  C 13  53.99 0.50 . 1 . . . . . . . . 4664 1 
      1012 . 1 1 152 152 CYS C   C 13 173.80 0.50 . 1 . . . . . . . . 4664 1 
      1013 . 1 1 152 152 CYS CB  C 13  35.04 0.50 . 1 . . . . . . . . 4664 1 
      1014 . 1 1 152 152 CYS N   N 15 122.88 0.25 . 1 . . . . . . . . 4664 1 
      1015 . 1 1 153 153 THR H   H  1   8.40 0.03 . 1 . . . . . . . . 4664 1 
      1016 . 1 1 153 153 THR HA  H  1   4.80 0.03 . 1 . . . . . . . . 4664 1 
      1017 . 1 1 153 153 THR HB  H  1   4.03 0.03 . 1 . . . . . . . . 4664 1 
      1018 . 1 1 153 153 THR CA  C 13  59.86 0.50 . 1 . . . . . . . . 4664 1 
      1019 . 1 1 153 153 THR C   C 13 173.90 0.50 . 1 . . . . . . . . 4664 1 
      1020 . 1 1 153 153 THR CB  C 13  72.48 0.50 . 1 . . . . . . . . 4664 1 
      1021 . 1 1 153 153 THR N   N 15 118.84 0.25 . 1 . . . . . . . . 4664 1 
      1022 . 1 1 154 154 VAL H   H  1   6.85 0.03 . 1 . . . . . . . . 4664 1 
      1023 . 1 1 154 154 VAL HA  H  1   4.04 0.03 . 1 . . . . . . . . 4664 1 
      1024 . 1 1 154 154 VAL HB  H  1   1.91 0.03 . 1 . . . . . . . . 4664 1 
      1025 . 1 1 154 154 VAL CA  C 13  62.03 0.50 . 1 . . . . . . . . 4664 1 
      1026 . 1 1 154 154 VAL C   C 13 176.60 0.50 . 1 . . . . . . . . 4664 1 
      1027 . 1 1 154 154 VAL CB  C 13  33.32 0.50 . 1 . . . . . . . . 4664 1 
      1028 . 1 1 154 154 VAL N   N 15 115.82 0.25 . 1 . . . . . . . . 4664 1 
      1029 . 1 1 155 155 ASP H   H  1   8.29 0.03 . 1 . . . . . . . . 4664 1 
      1030 . 1 1 155 155 ASP HA  H  1   4.42 0.03 . 1 . . . . . . . . 4664 1 
      1031 . 1 1 155 155 ASP HB2 H  1   2.59 0.03 . 2 . . . . . . . . 4664 1 
      1032 . 1 1 155 155 ASP HB3 H  1   2.34 0.03 . 2 . . . . . . . . 4664 1 
      1033 . 1 1 155 155 ASP CA  C 13  55.77 0.50 . 1 . . . . . . . . 4664 1 
      1034 . 1 1 155 155 ASP C   C 13 176.90 0.50 . 1 . . . . . . . . 4664 1 
      1035 . 1 1 155 155 ASP CB  C 13  42.40 0.50 . 1 . . . . . . . . 4664 1 
      1036 . 1 1 155 155 ASP N   N 15 124.82 0.25 . 1 . . . . . . . . 4664 1 
      1037 . 1 1 156 156 GLU H   H  1   8.35 0.03 . 1 . . . . . . . . 4664 1 
      1038 . 1 1 156 156 GLU HA  H  1   4.11 0.03 . 1 . . . . . . . . 4664 1 
      1039 . 1 1 156 156 GLU HB2 H  1   1.93 0.03 . 2 . . . . . . . . 4664 1 
      1040 . 1 1 156 156 GLU HB3 H  1   1.73 0.03 . 2 . . . . . . . . 4664 1 
      1041 . 1 1 156 156 GLU CA  C 13  57.49 0.50 . 1 . . . . . . . . 4664 1 
      1042 . 1 1 156 156 GLU C   C 13 176.45 0.50 . 1 . . . . . . . . 4664 1 
      1043 . 1 1 156 156 GLU CB  C 13  31.50 0.50 . 1 . . . . . . . . 4664 1 
      1044 . 1 1 156 156 GLU N   N 15 121.83 0.25 . 1 . . . . . . . . 4664 1 
      1045 . 1 1 157 157 VAL H   H  1   7.52 0.03 . 1 . . . . . . . . 4664 1 
      1046 . 1 1 157 157 VAL HA  H  1   3.88 0.03 . 1 . . . . . . . . 4664 1 
      1047 . 1 1 157 157 VAL HB  H  1   1.94 0.03 . 1 . . . . . . . . 4664 1 
      1048 . 1 1 157 157 VAL CA  C 13  64.39 0.50 . 1 . . . . . . . . 4664 1 
      1049 . 1 1 157 157 VAL CB  C 13  34.33 0.50 . 1 . . . . . . . . 4664 1 
      1050 . 1 1 157 157 VAL N   N 15 124.69 0.25 . 1 . . . . . . . . 4664 1 

   stop_

save_