data_17795

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

save_entry_information
   _Entry.Sf_category                    entry_information
   _Entry.Sf_framecode                   entry_information
   _Entry.ID                             17795
   _Entry.Title                         
;
Backbone chemical shift assignments for A 40 with Met35 in its oxidised state
;
   _Entry.Type                           macromolecule
   _Entry.Version_type                   original
   _Entry.Submission_date                2011-07-20
   _Entry.Accession_date                 2011-07-20
   _Entry.Last_release_date              2011-08-26
   _Entry.Original_release_date          2011-08-26
   _Entry.Origination                    author
   _Entry.NMR_STAR_version               3.1.1.61
   _Entry.Original_NMR_STAR_version      3.1
   _Entry.Experimental_method            NMR
   _Entry.Experimental_method_subtype    solution
   _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 Michael Zagorski . . . 17795 

   stop_

   loop_
      _Data_set.Type
      _Data_set.Count
      _Data_set.Entry_ID

      assigned_chemical_shifts 1 17795 

   stop_

   loop_
      _Datum.Type
      _Datum.Count
      _Datum.Entry_ID

      '13C chemical shifts' 71 17795 
      '15N chemical shifts' 39 17795 
      '1H chemical shifts'  86 17795 

   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 . . 2011-08-26 2011-07-20 original author . 17795 

   stop_

   loop_
      _Related_entries.Database_name
      _Related_entries.Database_accession_code
      _Related_entries.Relationship
      _Related_entries.Entry_ID

      BMRB 17793 'Abeta(1-42) oxidised' 17795 
      BMRB 17794 'Abeta(1-42) reduced'  17795 
      BMRB 17796 'Abeta(1-40) reduced'  17795 

   stop_

save_


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

save_entry_citation
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 entry_citation
   _Citation.Entry_ID                     17795
   _Citation.ID                           1
   _Citation.Class                       'entry citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              .
   _Citation.DOI                          .
   _Citation.PubMed_ID                    14971932
   _Citation.Full_citation                .
   _Citation.Title                       'Solution NMR Studies of the Ab(1-40) and Ab(1-42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation'
   _Citation.Status                       published
   _Citation.Type                         journal
   _Citation.Journal_abbrev              'J. Am. Chem. Soc.'
   _Citation.Journal_name_full            .
   _Citation.Journal_volume               126
   _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                   1992
   _Citation.Page_last                    2005
   _Citation.Year                         2004
   _Citation.Details                      .

   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 Liming    Hou      . .  . 17795 1 
       2 Haiyan    Shao     . .  . 17795 1 
       3 Yongbo    Zhang    . .  . 17795 1 
       4 Hua       Li       . .  . 17795 1 
       5 Nanda     Menon    . K. . 17795 1 
       6 Elizabeth Neuhaus  . B. . 17795 1 
       7 John      Brewer   . M. . 17795 1 
       8 In-Ja     Byeon    . L. . 17795 1 
       9 Dale      Ray      . G. . 17795 1 
      10 Michael   Vitek    . P. . 17795 1 
      11 Iwashita  Takashi  . .  . 17795 1 
      12 Ronald    Makula   . A. . 17795 1 
      13 Alan      Przybyla . B. . 17795 1 
      14 Michael   Zagorski . G. . 17795 1 

   stop_

save_


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

save_assembly
   _Assembly.Sf_category                       assembly
   _Assembly.Sf_framecode                      assembly
   _Assembly.Entry_ID                          17795
   _Assembly.ID                                1
   _Assembly.Name                              Abeta(1-40)
   _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                       .
   _Assembly.Molecular_mass                    .
   _Assembly.Enzyme_commission_number          .
   _Assembly.Details                           .
   _Assembly.DB_query_date                     .
   _Assembly.DB_query_revised_last_date        .

   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 Abeta(1-40) 1 $Abeta(1-40) A . yes native no no . . . 17795 1 

   stop_

save_


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

save_Abeta(1-40)
   _Entity.Sf_category                       entity
   _Entity.Sf_framecode                      Abeta(1-40)
   _Entity.Entry_ID                          17795
   _Entity.ID                                1
   _Entity.BMRB_code                         .
   _Entity.Name                              Abeta(1-40)
   _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      
;
DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV

;
   _Entity.Target_identifier                 .
   _Entity.Polymer_author_defined_seq        .
   _Entity.Polymer_author_seq_details        .
   _Entity.Ambiguous_conformational_states   no
   _Entity.Ambiguous_chem_comp_sites         no
   _Entity.Nstd_monomer                      no
   _Entity.Nstd_chirality                    no
   _Entity.Nstd_linkage                      no
   _Entity.Nonpolymer_comp_ID                .
   _Entity.Nonpolymer_comp_label             .
   _Entity.Number_of_monomers                40
   _Entity.Number_of_nonpolymer_components   .
   _Entity.Paramagnetic                      no
   _Entity.Thiol_state                      'not present'
   _Entity.Src_method                        .
   _Entity.Parent_entity_ID                  .
   _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        2015-11-25

   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        11435 .  Amyloid-beta-(1-40)                                                                                                              . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
       2 no BMRB        15775 .  APP_C99                                                                                                                          . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 17795 1 
       3 no BMRB        17159 .  Amyloid_beta-Peptide                                                                                                             . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
       4 no BMRB        17186 .  Abeta                                                                                                                            . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
       5 no BMRB        17764 .  Abeta                                                                                                                            . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
       6 no BMRB        17793 .  Abeta(1-42)                                                                                                                      . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
       7 no BMRB        17794 .  Abeta(1-42)                                                                                                                      . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
       8 no BMRB        17796 .  Abeta40                                                                                                                          . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
       9 no BMRB        18052 .  Pyroglutamate_Abeta                                                                                                              . . . . .  92.50  38 100.00 100.00 2.74e-16 . . . . 17795 1 
      10 no BMRB        18127 .  beta-amyloid                                                                                                                     . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      11 no BMRB        18128 .  beta-amyloid                                                                                                                     . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      12 no BMRB        18129 .  beta-amyloid                                                                                                                     . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      13 no BMRB        18131 .  beta-amyloid                                                                                                                     . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      14 no BMRB        19009 .  beta-amyloid_peptide                                                                                                             . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      15 no BMRB        19309 .  amyloid_peptide                                                                                                                  . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      16 no BMRB        19393 .  Abeta                                                                                                                            . . . . . 100.00  39  97.50  97.50 5.36e-16 . . . . 17795 1 
      17 no BMRB        25218 .  amyloid_peptide                                                                                                                  . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      18 no BMRB        25289 .  amyloid_beta                                                                                                                     . . . . . 100.00  39  97.50  97.50 5.36e-16 . . . . 17795 1 
      19 no BMRB        25429 .  entity                                                                                                                           . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      20 no BMRB        26508 .  amyloid_B                                                                                                                        . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      21 no BMRB        26516 .  amyloid_B                                                                                                                        . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      22 no PDB  1AMB          . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide"                                                                . . . . .  70.00  28 100.00 100.00 2.11e-10 . . . . 17795 1 
      23 no PDB  1AMC          . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide"                                                                . . . . .  70.00  28 100.00 100.00 2.11e-10 . . . . 17795 1 
      24 no PDB  1AML          . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)"                                                                      . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      25 no PDB  1BA4          . "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      26 no PDB  1BA6          . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 100.00  40  97.50  97.50 1.67e-17 . . . . 17795 1 
      27 no PDB  1HZ3          . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)"                                                                       . . . . .  65.00  26 100.00 100.00 2.06e-08 . . . . 17795 1 
      28 no PDB  1IYT          . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)"                                                      . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      29 no PDB  1Z0Q          . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)"                                                      . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      30 no PDB  2BEG          . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils"                                                                                 . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      31 no PDB  2G47          . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)"                                         . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      32 no PDB  2LFM          . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment"                                                    . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      33 no PDB  2LMN          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger"                                  . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      34 no PDB  2LMO          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger"                                  . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      35 no PDB  2LMP          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger"                                . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      36 no PDB  2LMQ          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger"                                . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      37 no PDB  2LNQ          . "40-residue D23n Beta Amyloid Fibril"                                                                                             . . . . . 100.00  40  97.50 100.00 5.11e-18 . . . . 17795 1 
      38 no PDB  2LP1          . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)"                        . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 17795 1 
      39 no PDB  2M4J          . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain"                                                           . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      40 no PDB  2M9R          . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside"            . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      41 no PDB  2M9S          . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside"            . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      42 no PDB  2MVX          . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation"                                                      . . . . . 100.00  39  97.50  97.50 5.36e-16 . . . . 17795 1 
      43 no PDB  2MXU          . "42-residue Beta Amyloid Fibril"                                                                                                  . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      44 no PDB  2OTK          . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein"                                                 . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      45 no PDB  2WK3          . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)"                                         . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      46 no PDB  3BAE          . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)"                                      . . . . .  70.00  28 100.00 100.00 2.11e-10 . . . . 17795 1 
      47 no PDB  3IFN          . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex"                                                      . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      48 no PDB  4HIX          . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide"                                                          . . . . .  70.00  28 100.00 100.00 2.11e-10 . . . . 17795 1 
      49 no PDB  4M1C          . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)"                . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      50 no PDB  4MVI          . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)"          . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      51 no PDB  4MVL          . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40"           . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      52 no PDB  4NGE          . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)"                                             . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      53 no PDB  4ONG          . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40"                                                                           . . . . . 100.00  40 100.00 100.00 1.49e-18 . . . . 17795 1 
      54 no PDB  5AEF          . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril"                                                                        . . . . .  65.00  28 100.00 100.00 3.73e-07 . . . . 17795 1 
      55 no DBJ  BAA22264      . "amyloid precursor protein [Homo sapiens]"                                                                                        . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      56 no DBJ  BAA84580      . "amyloid precursor protein [Sus scrofa]"                                                                                          . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      57 no DBJ  BAB71958      . "amyloid precursor protein [Homo sapiens]"                                                                                        . . . . . 100.00  52  97.50 100.00 1.74e-18 . . . . 17795 1 
      58 no DBJ  BAD51938      . "amyloid beta A4 precursor protein [Macaca fascicularis]"                                                                         . . . . . 100.00 696 100.00 100.00 1.14e-18 . . . . 17795 1 
      59 no DBJ  BAE01907      . "unnamed protein product [Macaca fascicularis]"                                                                                   . . . . . 100.00 751 100.00 100.00 1.43e-18 . . . . 17795 1 
      60 no EMBL CAA30050      . "amyloid A4 protein [Homo sapiens]"                                                                                               . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17795 1 
      61 no EMBL CAA31830      . "A4 amyloid protein precursor [Homo sapiens]"                                                                                     . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17795 1 
      62 no EMBL CAA39589      . "amyloid precursor protein [Bos taurus]"                                                                                          . . . . . 100.00  59 100.00 100.00 3.56e-19 . . . . 17795 1 
      63 no EMBL CAA39590      . "amyloid precursor protein [Canis lupus familiaris]"                                                                              . . . . . 100.00  58 100.00 100.00 3.68e-19 . . . . 17795 1 
      64 no EMBL CAA39591      . "amyloid precursor protein [Cavia sp.]"                                                                                           . . . . . 100.00  58 100.00 100.00 3.68e-19 . . . . 17795 1 
      65 no GB   AAA35540      . "amyloid protein, partial [Homo sapiens]"                                                                                         . . . . .  95.00  97 100.00 100.00 2.36e-17 . . . . 17795 1 
      66 no GB   AAA36829      . "amyloid b-protein precursor [Macaca fascicularis]"                                                                               . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17795 1 
      67 no GB   AAA51564      . "amyloid beta protein, partial [Homo sapiens]"                                                                                    . . . . .  75.00  30 100.00 100.00 1.09e-11 . . . . 17795 1 
      68 no GB   AAA51722      . "amyloid beta-protein precursor, partial [Homo sapiens]"                                                                          . . . . . 100.00 412 100.00 100.00 9.13e-19 . . . . 17795 1 
      69 no GB   AAA51726      . "beta-amyloid A4, partial [Homo sapiens]"                                                                                         . . . . . 100.00 264 100.00 100.00 1.74e-18 . . . . 17795 1 
      70 no PIR  A60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - dog  (fragment)"                                                         . . . . . 100.00  57 100.00 100.00 4.01e-19 . . . . 17795 1 
      71 no PIR  D60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)"                                                       . . . . . 100.00  57 100.00 100.00 4.01e-19 . . . . 17795 1 
      72 no PIR  E60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)"                                                        . . . . . 100.00  57 100.00 100.00 4.01e-19 . . . . 17795 1 
      73 no PIR  G60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)"                                                   . . . . . 100.00  57 100.00 100.00 4.01e-19 . . . . 17795 1 
      74 no PIR  PQ0438        . "Alzheimer's disease amyloid A4 protein precursor - rabbit  (fragment)"                                                           . . . . . 100.00  82 100.00 100.00 4.05e-19 . . . . 17795 1 
      75 no PRF  1303338A      . "amyloid A4 protein precursor"                                                                                                    . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17795 1 
      76 no PRF  1403400A      . "amyloid protein A4"                                                                                                              . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17795 1 
      77 no PRF  1405204A      . "amyloid protein"                                                                                                                 . . . . . 100.00  42 100.00 100.00 1.28e-18 . . . . 17795 1 
      78 no PRF  1507304A      . "beta amyloid peptide precursor"                                                                                                  . . . . . 100.00 412 100.00 100.00 9.42e-19 . . . . 17795 1 
      79 no PRF  1507304B      . "beta amyloid peptide precursor"                                                                                                  . . . . . 100.00 574 100.00 100.00 4.07e-18 . . . . 17795 1 
      80 no REF  NP_000475     . "amyloid beta A4 protein isoform a precursor [Homo sapiens]"                                                                      . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      81 no REF  NP_001006601  . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]"                                                      . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      82 no REF  NP_001013036  . "amyloid beta A4 protein precursor [Pan troglodytes]"                                                                             . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      83 no REF  NP_001070264  . "amyloid beta A4 protein precursor [Bos taurus]"                                                                                  . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17795 1 
      84 no REF  NP_001127014  . "amyloid beta A4 protein precursor [Pongo abelii]"                                                                                . . . . . 100.00 695 100.00 100.00 1.65e-18 . . . . 17795 1 
      85 no SP   P05067        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      86 no SP   P53601        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      87 no SP   P79307        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17795 1 
      88 no SP   P86906        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00  40  97.50 100.00 5.51e-18 . . . . 17795 1 
      89 no SP   Q28053        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00  59 100.00 100.00 3.56e-19 . . . . 17795 1 
      90 no TPG  DAA33655      . "TPA: amyloid beta A4 protein [Bos taurus]"                                                                                       . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17795 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 . ASP . 17795 1 
       2 . ALA . 17795 1 
       3 . GLU . 17795 1 
       4 . PHE . 17795 1 
       5 . ARG . 17795 1 
       6 . HIS . 17795 1 
       7 . ASP . 17795 1 
       8 . SER . 17795 1 
       9 . GLY . 17795 1 
      10 . TYR . 17795 1 
      11 . GLU . 17795 1 
      12 . VAL . 17795 1 
      13 . HIS . 17795 1 
      14 . HIS . 17795 1 
      15 . GLN . 17795 1 
      16 . LYS . 17795 1 
      17 . LEU . 17795 1 
      18 . VAL . 17795 1 
      19 . PHE . 17795 1 
      20 . PHE . 17795 1 
      21 . ALA . 17795 1 
      22 . GLU . 17795 1 
      23 . ASP . 17795 1 
      24 . VAL . 17795 1 
      25 . GLY . 17795 1 
      26 . SER . 17795 1 
      27 . ASN . 17795 1 
      28 . LYS . 17795 1 
      29 . GLY . 17795 1 
      30 . ALA . 17795 1 
      31 . ILE . 17795 1 
      32 . ILE . 17795 1 
      33 . GLY . 17795 1 
      34 . LEU . 17795 1 
      35 . MET . 17795 1 
      36 . VAL . 17795 1 
      37 . GLY . 17795 1 
      38 . GLY . 17795 1 
      39 . VAL . 17795 1 
      40 . VAL . 17795 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

      . ASP  1  1 17795 1 
      . ALA  2  2 17795 1 
      . GLU  3  3 17795 1 
      . PHE  4  4 17795 1 
      . ARG  5  5 17795 1 
      . HIS  6  6 17795 1 
      . ASP  7  7 17795 1 
      . SER  8  8 17795 1 
      . GLY  9  9 17795 1 
      . TYR 10 10 17795 1 
      . GLU 11 11 17795 1 
      . VAL 12 12 17795 1 
      . HIS 13 13 17795 1 
      . HIS 14 14 17795 1 
      . GLN 15 15 17795 1 
      . LYS 16 16 17795 1 
      . LEU 17 17 17795 1 
      . VAL 18 18 17795 1 
      . PHE 19 19 17795 1 
      . PHE 20 20 17795 1 
      . ALA 21 21 17795 1 
      . GLU 22 22 17795 1 
      . ASP 23 23 17795 1 
      . VAL 24 24 17795 1 
      . GLY 25 25 17795 1 
      . SER 26 26 17795 1 
      . ASN 27 27 17795 1 
      . LYS 28 28 17795 1 
      . GLY 29 29 17795 1 
      . ALA 30 30 17795 1 
      . ILE 31 31 17795 1 
      . ILE 32 32 17795 1 
      . GLY 33 33 17795 1 
      . LEU 34 34 17795 1 
      . MET 35 35 17795 1 
      . VAL 36 36 17795 1 
      . GLY 37 37 17795 1 
      . GLY 38 38 17795 1 
      . VAL 39 39 17795 1 
      . VAL 40 40 17795 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       17795
   _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 $Abeta(1-40) . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 17795 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       17795
   _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 $Abeta(1-40) . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 17795 1 

   stop_

save_


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

save_sample_1
   _Sample.Sf_category                      sample
   _Sample.Sf_framecode                     sample_1
   _Sample.Entry_ID                         17795
   _Sample.ID                               1
   _Sample.Type                             solution
   _Sample.Sub_type                         .
   _Sample.Details                          .
   _Sample.Aggregate_sample_number          .
   _Sample.Solvent_system                  '90% H2O/10% D2O'
   _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 Abeta(1-40) '[U-95% 15N]'       . . 1 $Abeta(1-40) . .   . 0.2 0.3 mM . . . . 17795 1 
      2 H2O         'natural abundance' . .  .  .           . . 90  .   .  %  . . . . 17795 1 
      3 D2O         'natural abundance' . .  .  .           . . 10  .   .  %  . . . . 17795 1 

   stop_

save_


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

save_sample_conditions_1
   _Sample_condition_list.Sf_category    sample_conditions
   _Sample_condition_list.Sf_framecode   sample_conditions_1
   _Sample_condition_list.Entry_ID       17795
   _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

      'ionic strength'   0.01 . M   17795 1 
       pH                7.2  . pH  17795 1 
       pressure          1    . atm 17795 1 
       temperature     273    . K   17795 1 

   stop_

save_


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

save_SPARKY
   _Software.Sf_category    software
   _Software.Sf_framecode   SPARKY
   _Software.Entry_ID       17795
   _Software.ID             1
   _Software.Name           SPARKY
   _Software.Version        .
   _Software.Details        .

   loop_
      _Vendor.Name
      _Vendor.Address
      _Vendor.Electronic_address
      _Vendor.Entry_ID
      _Vendor.Software_ID

      Goddard . . 17795 1 

   stop_

   loop_
      _Task.Task
      _Task.Entry_ID
      _Task.Software_ID

      collection 17795 1 

   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         17795
   _NMR_spectrometer.ID               1
   _NMR_spectrometer.Details          .
   _NMR_spectrometer.Manufacturer     Varian
   _NMR_spectrometer.Model            INOVA
   _NMR_spectrometer.Serial_number    .
   _NMR_spectrometer.Field_strength   600

save_


save_spectrometer_2
   _NMR_spectrometer.Sf_category      NMR_spectrometer
   _NMR_spectrometer.Sf_framecode     spectrometer_2
   _NMR_spectrometer.Entry_ID         17795
   _NMR_spectrometer.ID               2
   _NMR_spectrometer.Details          .
   _NMR_spectrometer.Manufacturer     Bruker
   _NMR_spectrometer.Model            DRX
   _NMR_spectrometer.Serial_number    .
   _NMR_spectrometer.Field_strength   800

save_


save_NMR_spectrometer_list
   _NMR_spectrometer_list.Sf_category    NMR_spectrometer_list
   _NMR_spectrometer_list.Sf_framecode   NMR_spectrometer_list
   _NMR_spectrometer_list.Entry_ID       17795
   _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 INOVA . 600 . . . 17795 1 
      2 spectrometer_2 Bruker DRX   . 800 . . . 17795 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       17795
   _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 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 17795 1 
      2 '3D HNHA'   no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 17795 1 

   stop_

save_


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

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

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

save_chemical_shift_reference_1
   _Chem_shift_reference.Sf_category    chem_shift_reference
   _Chem_shift_reference.Sf_framecode   chemical_shift_reference_1
   _Chem_shift_reference.Entry_ID       17795
   _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

      C 13 DSS 'methyl protons' . . . . ppm 0.00 n/a      indirect 0.251449530 . . . . . . . . . 17795 1 
      H  1 DSS 'methyl protons' . . . . ppm 0.00 internal direct   1.000000000 . . . . . . . . . 17795 1 
      N 15 DSS 'methyl protons' . . . . ppm 0.00 n/a      indirect 0.101329118 . . . . . . . . . 17795 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_assigned_chem_shift_list_1
   _Assigned_chem_shift_list.Sf_category                   assigned_chemical_shifts
   _Assigned_chem_shift_list.Sf_framecode                  assigned_chem_shift_list_1
   _Assigned_chem_shift_list.Entry_ID                      17795
   _Assigned_chem_shift_list.ID                            1
   _Assigned_chem_shift_list.Sample_condition_list_ID      1
   _Assigned_chem_shift_list.Sample_condition_list_label  $sample_conditions_1
   _Assigned_chem_shift_list.Chem_shift_reference_ID       1
   _Assigned_chem_shift_list.Chem_shift_reference_label   $chemical_shift_reference_1
   _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 '3D HNCACB' . . . 17795 1 
      2 '3D HNHA'   . . . 17795 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  1  1 ASP H   H  1   8.65 . . 1 . . . .  1 ASP H   . 17795 1 
        2 . 1 1  1  1 ASP HA  H  1   4.66 . . 1 . . . .  1 ASP HA  . 17795 1 
        3 . 1 1  1  1 ASP CB  C 13  42.18 . . 1 . . . .  1 ASP CB  . 17795 1 
        4 . 1 1  2  2 ALA H   H  1   8.15 . . 1 . . . .  2 ALA H   . 17795 1 
        5 . 1 1  2  2 ALA HA  H  1   4.31 . . 1 . . . .  2 ALA HA  . 17795 1 
        6 . 1 1  2  2 ALA CA  C 13  52.78 . . 1 . . . .  2 ALA CA  . 17795 1 
        7 . 1 1  2  2 ALA CB  C 13  19.08 . . 1 . . . .  2 ALA CB  . 17795 1 
        8 . 1 1  2  2 ALA N   N 15 123.30 . . 1 . . . .  2 ALA N   . 17795 1 
        9 . 1 1  3  3 GLU H   H  1   8.58 . . 1 . . . .  3 GLU H   . 17795 1 
       10 . 1 1  3  3 GLU HA  H  1   4.18 . . 1 . . . .  3 GLU HA  . 17795 1 
       11 . 1 1  3  3 GLU CA  C 13  56.55 . . 1 . . . .  3 GLU CA  . 17795 1 
       12 . 1 1  3  3 GLU CB  C 13  30.17 . . 1 . . . .  3 GLU CB  . 17795 1 
       13 . 1 1  3  3 GLU N   N 15 120.40 . . 1 . . . .  3 GLU N   . 17795 1 
       14 . 1 1  4  4 PHE H   H  1   8.43 . . 1 . . . .  4 PHE H   . 17795 1 
       15 . 1 1  4  4 PHE HA  H  1   4.55 . . 1 . . . .  4 PHE HA  . 17795 1 
       16 . 1 1  4  4 PHE CA  C 13  57.75 . . 1 . . . .  4 PHE CA  . 17795 1 
       17 . 1 1  4  4 PHE CB  C 13  39.46 . . 1 . . . .  4 PHE CB  . 17795 1 
       18 . 1 1  4  4 PHE N   N 15 121.90 . . 1 . . . .  4 PHE N   . 17795 1 
       19 . 1 1  5  5 ARG H   H  1   8.24 . . 1 . . . .  5 ARG H   . 17795 1 
       20 . 1 1  5  5 ARG HA  H  1   4.29 . . 1 . . . .  5 ARG HA  . 17795 1 
       21 . 1 1  5  5 ARG CA  C 13  55.32 . . 1 . . . .  5 ARG CA  . 17795 1 
       22 . 1 1  5  5 ARG CB  C 13  31.13 . . 1 . . . .  5 ARG CB  . 17795 1 
       23 . 1 1  5  5 ARG N   N 15 124.00 . . 1 . . . .  5 ARG N   . 17795 1 
       24 . 1 1  6  6 HIS H   H  1   8.05 . . 1 . . . .  6 HIS H   . 17795 1 
       25 . 1 1  6  6 HIS HA  H  1   4.52 . . 1 . . . .  6 HIS HA  . 17795 1 
       26 . 1 1  6  6 HIS CB  C 13  30.78 . . 1 . . . .  6 HIS CB  . 17795 1 
       27 . 1 1  6  6 HIS N   N 15 123.10 . . 1 . . . .  6 HIS N   . 17795 1 
       28 . 1 1  7  7 ASP H   H  1   8.45 . . 1 . . . .  7 ASP H   . 17795 1 
       29 . 1 1  7  7 ASP HA  H  1   4.62 . . 1 . . . .  7 ASP HA  . 17795 1 
       30 . 1 1  7  7 ASP CA  C 13  53.96 . . 1 . . . .  7 ASP CA  . 17795 1 
       31 . 1 1  7  7 ASP CB  C 13  40.99 . . 1 . . . .  7 ASP CB  . 17795 1 
       32 . 1 1  7  7 ASP N   N 15 121.80 . . 1 . . . .  7 ASP N   . 17795 1 
       33 . 1 1  8  8 SER H   H  1   8.48 . . 1 . . . .  8 SER H   . 17795 1 
       34 . 1 1  8  8 SER HA  H  1   4.36 . . 1 . . . .  8 SER HA  . 17795 1 
       35 . 1 1  8  8 SER CA  C 13  59.06 . . 1 . . . .  8 SER CA  . 17795 1 
       36 . 1 1  8  8 SER CB  C 13  63.60 . . 1 . . . .  8 SER CB  . 17795 1 
       37 . 1 1  8  8 SER N   N 15 116.70 . . 1 . . . .  8 SER N   . 17795 1 
       38 . 1 1  9  9 GLY H   H  1   8.60 . . 1 . . . .  9 GLY H   . 17795 1 
       39 . 1 1  9  9 GLY HA2 H  1   3.83 . . 2 . . . .  9 GLY HA1 . 17795 1 
       40 . 1 1  9  9 GLY HA3 H  1   3.90 . . 2 . . . .  9 GLY HA2 . 17795 1 
       41 . 1 1  9  9 GLY CA  C 13  45.26 . . 1 . . . .  9 GLY CA  . 17795 1 
       42 . 1 1  9  9 GLY N   N 15 110.80 . . 1 . . . .  9 GLY N   . 17795 1 
       43 . 1 1 10 10 TYR H   H  1   8.02 . . 1 . . . . 10 TYR H   . 17795 1 
       44 . 1 1 10 10 TYR HA  H  1   4.52 . . 1 . . . . 10 TYR HA  . 17795 1 
       45 . 1 1 10 10 TYR CA  C 13  58.10 . . 1 . . . . 10 TYR CA  . 17795 1 
       46 . 1 1 10 10 TYR CB  C 13  38.72 . . 1 . . . . 10 TYR CB  . 17795 1 
       47 . 1 1 10 10 TYR N   N 15 120.10 . . 1 . . . . 10 TYR N   . 17795 1 
       48 . 1 1 11 11 GLU H   H  1   8.51 . . 1 . . . . 11 GLU H   . 17795 1 
       49 . 1 1 11 11 GLU HA  H  1   4.19 . . 1 . . . . 11 GLU HA  . 17795 1 
       50 . 1 1 11 11 GLU CA  C 13  56.42 . . 1 . . . . 11 GLU CA  . 17795 1 
       51 . 1 1 11 11 GLU CB  C 13  30.27 . . 1 . . . . 11 GLU CB  . 17795 1 
       52 . 1 1 11 11 GLU N   N 15 122.70 . . 1 . . . . 11 GLU N   . 17795 1 
       53 . 1 1 12 12 VAL H   H  1   8.21 . . 1 . . . . 12 VAL H   . 17795 1 
       54 . 1 1 12 12 VAL HA  H  1   3.93 . . 1 . . . . 12 VAL HA  . 17795 1 
       55 . 1 1 12 12 VAL CA  C 13  62.76 . . 1 . . . . 12 VAL CA  . 17795 1 
       56 . 1 1 12 12 VAL CB  C 13  32.46 . . 1 . . . . 12 VAL CB  . 17795 1 
       57 . 1 1 12 12 VAL N   N 15 121.20 . . 1 . . . . 12 VAL N   . 17795 1 
       58 . 1 1 13 13 HIS H   H  1   8.35 . . 1 . . . . 13 HIS H   . 17795 1 
       59 . 1 1 13 13 HIS HA  H  1   4.58 . . 1 . . . . 13 HIS HA  . 17795 1 
       60 . 1 1 13 13 HIS CA  C 13  56.31 . . 1 . . . . 13 HIS CA  . 17795 1 
       61 . 1 1 13 13 HIS CB  C 13  30.86 . . 1 . . . . 13 HIS CB  . 17795 1 
       62 . 1 1 13 13 HIS N   N 15 122.70 . . 1 . . . . 13 HIS N   . 17795 1 
       63 . 1 1 14 14 HIS H   H  1   8.02 . . 1 . . . . 14 HIS H   . 17795 1 
       64 . 1 1 14 14 HIS HA  H  1   4.54 . . 1 . . . . 14 HIS HA  . 17795 1 
       65 . 1 1 14 14 HIS CB  C 13  30.74 . . 1 . . . . 14 HIS CB  . 17795 1 
       66 . 1 1 14 14 HIS N   N 15 121.40 . . 1 . . . . 14 HIS N   . 17795 1 
       67 . 1 1 15 15 GLN H   H  1   8.55 . . 1 . . . . 15 GLN H   . 17795 1 
       68 . 1 1 15 15 GLN HA  H  1   4.27 . . 1 . . . . 15 GLN HA  . 17795 1 
       69 . 1 1 15 15 GLN CA  C 13  56.11 . . 1 . . . . 15 GLN CA  . 17795 1 
       70 . 1 1 15 15 GLN CB  C 13  29.28 . . 1 . . . . 15 GLN CB  . 17795 1 
       71 . 1 1 15 15 GLN N   N 15 121.50 . . 1 . . . . 15 GLN N   . 17795 1 
       72 . 1 1 16 16 LYS H   H  1   8.52 . . 1 . . . . 16 LYS H   . 17795 1 
       73 . 1 1 16 16 LYS HA  H  1   4.26 . . 1 . . . . 16 LYS HA  . 17795 1 
       74 . 1 1 16 16 LYS CA  C 13  56.42 . . 1 . . . . 16 LYS CA  . 17795 1 
       75 . 1 1 16 16 LYS CB  C 13  32.79 . . 1 . . . . 16 LYS CB  . 17795 1 
       76 . 1 1 16 16 LYS N   N 15 123.00 . . 1 . . . . 16 LYS N   . 17795 1 
       77 . 1 1 17 17 LEU H   H  1   8.38 . . 1 . . . . 17 LEU H   . 17795 1 
       78 . 1 1 17 17 LEU HA  H  1   4.33 . . 1 . . . . 17 LEU HA  . 17795 1 
       79 . 1 1 17 17 LEU CA  C 13  55.06 . . 1 . . . . 17 LEU CA  . 17795 1 
       80 . 1 1 17 17 LEU CB  C 13  42.27 . . 1 . . . . 17 LEU CB  . 17795 1 
       81 . 1 1 17 17 LEU N   N 15 123.90 . . 1 . . . . 17 LEU N   . 17795 1 
       82 . 1 1 18 18 VAL H   H  1   8.13 . . 1 . . . . 18 VAL H   . 17795 1 
       83 . 1 1 18 18 VAL HA  H  1   4.03 . . 1 . . . . 18 VAL HA  . 17795 1 
       84 . 1 1 18 18 VAL CA  C 13  61.93 . . 1 . . . . 18 VAL CA  . 17795 1 
       85 . 1 1 18 18 VAL CB  C 13  32.98 . . 1 . . . . 18 VAL CB  . 17795 1 
       86 . 1 1 18 18 VAL N   N 15 121.60 . . 1 . . . . 18 VAL N   . 17795 1 
       87 . 1 1 19 19 PHE H   H  1   8.39 . . 1 . . . . 19 PHE H   . 17795 1 
       88 . 1 1 19 19 PHE HA  H  1   4.58 . . 1 . . . . 19 PHE HA  . 17795 1 
       89 . 1 1 19 19 PHE CA  C 13  57.36 . . 1 . . . . 19 PHE CA  . 17795 1 
       90 . 1 1 19 19 PHE CB  C 13  40.10 . . 1 . . . . 19 PHE CB  . 17795 1 
       91 . 1 1 19 19 PHE N   N 15 124.60 . . 1 . . . . 19 PHE N   . 17795 1 
       92 . 1 1 20 20 PHE H   H  1   8.39 . . 1 . . . . 20 PHE H   . 17795 1 
       93 . 1 1 20 20 PHE HA  H  1   4.58 . . 1 . . . . 20 PHE HA  . 17795 1 
       94 . 1 1 20 20 PHE CA  C 13  57.28 . . 1 . . . . 20 PHE CA  . 17795 1 
       95 . 1 1 20 20 PHE CB  C 13  40.00 . . 1 . . . . 20 PHE CB  . 17795 1 
       96 . 1 1 20 20 PHE N   N 15 123.20 . . 1 . . . . 20 PHE N   . 17795 1 
       97 . 1 1 21 21 ALA H   H  1   8.36 . . 1 . . . . 21 ALA H   . 17795 1 
       98 . 1 1 21 21 ALA HA  H  1   4.22 . . 1 . . . . 21 ALA HA  . 17795 1 
       99 . 1 1 21 21 ALA CA  C 13  52.29 . . 1 . . . . 21 ALA CA  . 17795 1 
      100 . 1 1 21 21 ALA CB  C 13  19.30 . . 1 . . . . 21 ALA CB  . 17795 1 
      101 . 1 1 21 21 ALA N   N 15 126.30 . . 1 . . . . 21 ALA N   . 17795 1 
      102 . 1 1 22 22 GLU H   H  1   8.49 . . 1 . . . . 22 GLU H   . 17795 1 
      103 . 1 1 22 22 GLU HA  H  1   4.20 . . 1 . . . . 22 GLU HA  . 17795 1 
      104 . 1 1 22 22 GLU CA  C 13  56.51 . . 1 . . . . 22 GLU CA  . 17795 1 
      105 . 1 1 22 22 GLU CB  C 13  30.25 . . 1 . . . . 22 GLU CB  . 17795 1 
      106 . 1 1 22 22 GLU N   N 15 120.10 . . 1 . . . . 22 GLU N   . 17795 1 
      107 . 1 1 23 23 ASP H   H  1   8.56 . . 1 . . . . 23 ASP H   . 17795 1 
      108 . 1 1 23 23 ASP HA  H  1   4.65 . . 1 . . . . 23 ASP HA  . 17795 1 
      109 . 1 1 23 23 ASP CA  C 13  54.03 . . 1 . . . . 23 ASP CA  . 17795 1 
      110 . 1 1 23 23 ASP CB  C 13  40.98 . . 1 . . . . 23 ASP CB  . 17795 1 
      111 . 1 1 23 23 ASP N   N 15 121.90 . . 1 . . . . 23 ASP N   . 17795 1 
      112 . 1 1 24 24 VAL H   H  1   8.30 . . 1 . . . . 24 VAL H   . 17795 1 
      113 . 1 1 24 24 VAL HA  H  1   4.14 . . 1 . . . . 24 VAL HA  . 17795 1 
      114 . 1 1 24 24 VAL CA  C 13  62.72 . . 1 . . . . 24 VAL CA  . 17795 1 
      115 . 1 1 24 24 VAL CB  C 13  32.17 . . 1 . . . . 24 VAL CB  . 17795 1 
      116 . 1 1 24 24 VAL N   N 15 120.80 . . 1 . . . . 24 VAL N   . 17795 1 
      117 . 1 1 25 25 GLY H   H  1   8.68 . . 1 . . . . 25 GLY H   . 17795 1 
      118 . 1 1 25 25 GLY HA2 H  1   3.99 . . 2 . . . . 25 GLY HA1 . 17795 1 
      119 . 1 1 25 25 GLY HA3 H  1   3.99 . . 2 . . . . 25 GLY HA2 . 17795 1 
      120 . 1 1 25 25 GLY CA  C 13  45.40 . . 1 . . . . 25 GLY CA  . 17795 1 
      121 . 1 1 25 25 GLY N   N 15 111.90 . . 1 . . . . 25 GLY N   . 17795 1 
      122 . 1 1 26 26 SER H   H  1   8.26 . . 1 . . . . 26 SER H   . 17795 1 
      123 . 1 1 26 26 SER HA  H  1   4.44 . . 1 . . . . 26 SER HA  . 17795 1 
      124 . 1 1 26 26 SER CA  C 13  58.54 . . 1 . . . . 26 SER CA  . 17795 1 
      125 . 1 1 26 26 SER CB  C 13  63.69 . . 1 . . . . 26 SER CB  . 17795 1 
      126 . 1 1 26 26 SER N   N 15 115.60 . . 1 . . . . 26 SER N   . 17795 1 
      127 . 1 1 27 27 ASN H   H  1   8.60 . . 1 . . . . 27 ASN H   . 17795 1 
      128 . 1 1 27 27 ASN HA  H  1   4.75 . . 1 . . . . 27 ASN HA  . 17795 1 
      129 . 1 1 27 27 ASN CA  C 13  53.16 . . 1 . . . . 27 ASN CA  . 17795 1 
      130 . 1 1 27 27 ASN CB  C 13  38.38 . . 1 . . . . 27 ASN CB  . 17795 1 
      131 . 1 1 27 27 ASN N   N 15 120.70 . . 1 . . . . 27 ASN N   . 17795 1 
      132 . 1 1 28 28 LYS H   H  1   8.49 . . 1 . . . . 28 LYS H   . 17795 1 
      133 . 1 1 28 28 LYS HA  H  1   4.27 . . 1 . . . . 28 LYS HA  . 17795 1 
      134 . 1 1 28 28 LYS CA  C 13  56.70 . . 1 . . . . 28 LYS CA  . 17795 1 
      135 . 1 1 28 28 LYS CB  C 13  32.40 . . 1 . . . . 28 LYS CB  . 17795 1 
      136 . 1 1 28 28 LYS N   N 15 121.90 . . 1 . . . . 28 LYS N   . 17795 1 
      137 . 1 1 29 29 GLY H   H  1   8.54 . . 1 . . . . 29 GLY H   . 17795 1 
      138 . 1 1 29 29 GLY HA2 H  1   3.93 . . 2 . . . . 29 GLY HA1 . 17795 1 
      139 . 1 1 29 29 GLY HA3 H  1   3.93 . . 2 . . . . 29 GLY HA2 . 17795 1 
      140 . 1 1 29 29 GLY CA  C 13  45.04 . . 1 . . . . 29 GLY CA  . 17795 1 
      141 . 1 1 29 29 GLY N   N 15 109.70 . . 1 . . . . 29 GLY N   . 17795 1 
      142 . 1 1 30 30 ALA H   H  1   8.15 . . 1 . . . . 30 ALA H   . 17795 1 
      143 . 1 1 30 30 ALA HA  H  1   4.31 . . 1 . . . . 30 ALA HA  . 17795 1 
      144 . 1 1 30 30 ALA CA  C 13  52.35 . . 1 . . . . 30 ALA CA  . 17795 1 
      145 . 1 1 30 30 ALA CB  C 13  19.18 . . 1 . . . . 30 ALA CB  . 17795 1 
      146 . 1 1 30 30 ALA N   N 15 123.70 . . 1 . . . . 30 ALA N   . 17795 1 
      147 . 1 1 31 31 ILE H   H  1   8.33 . . 1 . . . . 31 ILE H   . 17795 1 
      148 . 1 1 31 31 ILE HA  H  1   4.15 . . 1 . . . . 31 ILE HA  . 17795 1 
      149 . 1 1 31 31 ILE CA  C 13  60.99 . . 1 . . . . 31 ILE CA  . 17795 1 
      150 . 1 1 31 31 ILE CB  C 13  38.29 . . 1 . . . . 31 ILE CB  . 17795 1 
      151 . 1 1 31 31 ILE N   N 15 120.90 . . 1 . . . . 31 ILE N   . 17795 1 
      152 . 1 1 32 32 ILE H   H  1   8.44 . . 1 . . . . 32 ILE H   . 17795 1 
      153 . 1 1 32 32 ILE HA  H  1   4.16 . . 1 . . . . 32 ILE HA  . 17795 1 
      154 . 1 1 32 32 ILE CA  C 13  61.08 . . 1 . . . . 32 ILE CA  . 17795 1 
      155 . 1 1 32 32 ILE CB  C 13  38.37 . . 1 . . . . 32 ILE CB  . 17795 1 
      156 . 1 1 32 32 ILE N   N 15 126.50 . . 1 . . . . 32 ILE N   . 17795 1 
      157 . 1 1 33 33 GLY H   H  1   8.62 . . 1 . . . . 33 GLY H   . 17795 1 
      158 . 1 1 33 33 GLY HA2 H  1   3.92 . . 2 . . . . 33 GLY HA1 . 17795 1 
      159 . 1 1 33 33 GLY HA3 H  1   3.96 . . 2 . . . . 33 GLY HA2 . 17795 1 
      160 . 1 1 33 33 GLY CA  C 13  45.01 . . 1 . . . . 33 GLY CA  . 17795 1 
      161 . 1 1 33 33 GLY N   N 15 113.40 . . 1 . . . . 33 GLY N   . 17795 1 
      162 . 1 1 34 34 LEU H   H  1   8.21 . . 1 . . . . 34 LEU H   . 17795 1 
      163 . 1 1 34 34 LEU HA  H  1   4.35 . . 1 . . . . 34 LEU HA  . 17795 1 
      164 . 1 1 34 34 LEU CA  C 13  55.06 . . 1 . . . . 34 LEU CA  . 17795 1 
      165 . 1 1 34 34 LEU CB  C 13  42.47 . . 1 . . . . 34 LEU CB  . 17795 1 
      166 . 1 1 34 34 LEU N   N 15 121.70 . . 1 . . . . 34 LEU N   . 17795 1 
      167 . 1 1 35 35 MET H   H  1   8.74 . . 1 . . . . 35 MET H   . 17795 1 
      168 . 1 1 35 35 MET HA  H  1   4.57 . . 1 . . . . 35 MET HA  . 17795 1 
      169 . 1 1 35 35 MET CA  C 13  54.94 . . 1 . . . . 35 MET CA  . 17795 1 
      170 . 1 1 35 35 MET CB  C 13  26.64 . . 1 . . . . 35 MET CB  . 17795 1 
      171 . 1 1 35 35 MET N   N 15 121.50 . . 1 . . . . 35 MET N   . 17795 1 
      172 . 1 1 36 36 VAL H   H  1   8.52 . . 1 . . . . 36 VAL H   . 17795 1 
      173 . 1 1 36 36 VAL HA  H  1   4.14 . . 1 . . . . 36 VAL HA  . 17795 1 
      174 . 1 1 36 36 VAL CA  C 13  62.55 . . 1 . . . . 36 VAL CA  . 17795 1 
      175 . 1 1 36 36 VAL CB  C 13  32.69 . . 1 . . . . 36 VAL CB  . 17795 1 
      176 . 1 1 36 36 VAL N   N 15 122.70 . . 1 . . . . 36 VAL N   . 17795 1 
      177 . 1 1 37 37 GLY H   H  1   8.76 . . 1 . . . . 37 GLY H   . 17795 1 
      178 . 1 1 37 37 GLY HA2 H  1   3.97 . . 2 . . . . 37 GLY HA1 . 17795 1 
      179 . 1 1 37 37 GLY HA3 H  1   4.02 . . 2 . . . . 37 GLY HA2 . 17795 1 
      180 . 1 1 37 37 GLY CA  C 13  45.07 . . 1 . . . . 37 GLY CA  . 17795 1 
      181 . 1 1 37 37 GLY N   N 15 113.20 . . 1 . . . . 37 GLY N   . 17795 1 
      182 . 1 1 38 38 GLY H   H  1   8.41 . . 1 . . . . 38 GLY H   . 17795 1 
      183 . 1 1 38 38 GLY HA2 H  1   3.94 . . 2 . . . . 38 GLY HA1 . 17795 1 
      184 . 1 1 38 38 GLY HA3 H  1   4.03 . . 2 . . . . 38 GLY HA2 . 17795 1 
      185 . 1 1 38 38 GLY CA  C 13  44.98 . . 1 . . . . 38 GLY CA  . 17795 1 
      186 . 1 1 38 38 GLY N   N 15 108.90 . . 1 . . . . 38 GLY N   . 17795 1 
      187 . 1 1 39 39 VAL H   H  1   8.23 . . 1 . . . . 39 VAL H   . 17795 1 
      188 . 1 1 39 39 VAL HA  H  1   4.19 . . 1 . . . . 39 VAL HA  . 17795 1 
      189 . 1 1 39 39 VAL CA  C 13  62.48 . . 1 . . . . 39 VAL CA  . 17795 1 
      190 . 1 1 39 39 VAL CB  C 13  33.73 . . 1 . . . . 39 VAL CB  . 17795 1 
      191 . 1 1 39 39 VAL N   N 15 120.10 . . 1 . . . . 39 VAL N   . 17795 1 
      192 . 1 1 40 40 VAL H   H  1   7.96 . . 1 . . . . 40 VAL H   . 17795 1 
      193 . 1 1 40 40 VAL HA  H  1   4.05 . . 1 . . . . 40 VAL HA  . 17795 1 
      194 . 1 1 40 40 VAL CA  C 13  63.74 . . 1 . . . . 40 VAL CA  . 17795 1 
      195 . 1 1 40 40 VAL CB  C 13  33.10 . . 1 . . . . 40 VAL CB  . 17795 1 
      196 . 1 1 40 40 VAL N   N 15 128.50 . . 1 . . . . 40 VAL N   . 17795 1 

   stop_

save_