data_25218

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

save_entry_information
   _Entry.Sf_category                    entry_information
   _Entry.Sf_framecode                   entry_information
   _Entry.ID                             25218
   _Entry.Title                         
;
Chemical shifts of amyloid beta (1-42) peptide in aqueous solution
;
   _Entry.Type                           macromolecule
   _Entry.Version_type                   original
   _Entry.Submission_date                2014-09-11
   _Entry.Accession_date                 2014-09-11
   _Entry.Last_release_date              2015-03-17
   _Entry.Original_release_date          2015-03-17
   _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 Marielle Walti    . A. . 25218 
      2 Julien   Orts     . .  . 25218 
      3 Beat     Vogeli   . .  . 25218 
      4 Silvia   Campioni . .  . 25218 
      5 Roland   Riek     . .  . 25218 

   stop_

   loop_
      _Data_set.Type
      _Data_set.Count
      _Data_set.Entry_ID

      assigned_chemical_shifts 1 25218 

   stop_

   loop_
      _Datum.Type
      _Datum.Count
      _Datum.Entry_ID

      '13C chemical shifts'  78 25218 
      '15N chemical shifts'  42 25218 
      '1H chemical shifts'  242 25218 

   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 . . 2015-03-17 2014-09-11 original author . 25218 

   stop_

save_


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

save_entry_citation
   _Citation.Sf_category                  citations
   _Citation.Sf_framecode                 entry_citation
   _Citation.Entry_ID                     25218
   _Citation.ID                           1
   _Citation.Class                       'entry citation'
   _Citation.CAS_abstract_code            .
   _Citation.MEDLINE_UI_code              .
   _Citation.DOI                          .
   _Citation.PubMed_ID                    25676345
   _Citation.Full_citation                .
   _Citation.Title                       'Solution NMR Studies of Recombinant Abeta(1-42): From the Presence of a Micellar Entity to Residual Beta-Sheet Structure in the Soluble Species'
   _Citation.Status                       published
   _Citation.Type                         journal
   _Citation.Journal_abbrev               Chembiochem.
   _Citation.Journal_name_full            .
   _Citation.Journal_volume               16
   _Citation.Journal_issue                4
   _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                   659
   _Citation.Page_last                    669
   _Citation.Year                         2015
   _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 Marielle Walti    . A. . 25218 1 
      2 Julien   Orts     . .  . 25218 1 
      3 Beat     Vogeli   . .  . 25218 1 
      4 Silvia   Campioni . .  . 25218 1 
      5 Roland   Riek     . .  . 25218 1 

   stop_

save_


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

save_assembly
   _Assembly.Sf_category                       assembly
   _Assembly.Sf_framecode                      assembly
   _Assembly.Entry_ID                          25218
   _Assembly.ID                                1
   _Assembly.Name                             'amyloid beta'
   _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 entity 1 $entity A . yes native no no . . . 25218 1 

   stop_

save_


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

save_entity
   _Entity.Sf_category                       entity
   _Entity.Sf_framecode                      entity
   _Entity.Entry_ID                          25218
   _Entity.ID                                1
   _Entity.BMRB_code                         .
   _Entity.Name                              amyloid_peptide
   _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
IA
;
   _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                42
   _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)                                                                                                              . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
       2 no BMRB        15775 .  APP_C99                                                                                                                          . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25218 1 
       3 no BMRB        17159 .  Amyloid_beta-Peptide                                                                                                             . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
       4 no BMRB        17186 .  Abeta                                                                                                                            . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
       5 no BMRB        17764 .  Abeta                                                                                                                            . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
       6 no BMRB        17793 .  Abeta(1-42)                                                                                                                      . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
       7 no BMRB        17794 .  Abeta(1-42)                                                                                                                      . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
       8 no BMRB        17795 .  Abeta(1-40)                                                                                                                      . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
       9 no BMRB        17796 .  Abeta40                                                                                                                          . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      10 no BMRB        18052 .  Pyroglutamate_Abeta                                                                                                              . . . . .  88.10  38 100.00 100.00 2.61e-16 . . . . 25218 1 
      11 no BMRB        18127 .  beta-amyloid                                                                                                                     . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      12 no BMRB        18128 .  beta-amyloid                                                                                                                     . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      13 no BMRB        18129 .  beta-amyloid                                                                                                                     . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      14 no BMRB        18131 .  beta-amyloid                                                                                                                     . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      15 no BMRB        19009 .  beta-amyloid_peptide                                                                                                             . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      16 no BMRB        19309 .  amyloid_peptide                                                                                                                  . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      17 no BMRB        19393 .  Abeta                                                                                                                            . . . . .  95.24  39  97.50  97.50 4.95e-16 . . . . 25218 1 
      18 no BMRB        25289 .  amyloid_beta                                                                                                                     . . . . .  95.24  39  97.50  97.50 4.95e-16 . . . . 25218 1 
      19 no BMRB        25429 .  entity                                                                                                                           . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      20 no BMRB        26508 .  amyloid_B                                                                                                                        . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      21 no BMRB        26516 .  amyloid_B                                                                                                                        . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      22 no PDB  1AMB          . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide"                                                                . . . . .  66.67  28 100.00 100.00 1.81e-10 . . . . 25218 1 
      23 no PDB  1AMC          . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide"                                                                . . . . .  66.67  28 100.00 100.00 1.81e-10 . . . . 25218 1 
      24 no PDB  1AML          . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)"                                                                      . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 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 " . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      26 no PDB  1BA6          . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . .  95.24  40  97.50  97.50 1.43e-17 . . . . 25218 1 
      27 no PDB  1HZ3          . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)"                                                                       . . . . .  61.90  26 100.00 100.00 2.00e-08 . . . . 25218 1 
      28 no PDB  1IYT          . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)"                                                      . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      29 no PDB  1Z0Q          . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)"                                                      . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      30 no PDB  2BEG          . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils"                                                                                 . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      31 no PDB  2G47          . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)"                                         . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      32 no PDB  2LFM          . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment"                                                    . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      33 no PDB  2LMN          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger"                                  . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      34 no PDB  2LMO          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger"                                  . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      35 no PDB  2LMP          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger"                                . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      36 no PDB  2LMQ          . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger"                                . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      37 no PDB  2LNQ          . "40-residue D23n Beta Amyloid Fibril"                                                                                             . . . . .  95.24  40  97.50 100.00 4.61e-18 . . . . 25218 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 6.42e-20 . . . . 25218 1 
      39 no PDB  2M4J          . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain"                                                           . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      40 no PDB  2M9R          . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside"            . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      41 no PDB  2M9S          . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside"            . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      42 no PDB  2MVX          . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation"                                                      . . . . .  95.24  39  97.50  97.50 4.95e-16 . . . . 25218 1 
      43 no PDB  2MXU          . "42-residue Beta Amyloid Fibril"                                                                                                  . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      44 no PDB  2OTK          . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein"                                                 . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 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 7.22e-20 . . . . 25218 1 
      46 no PDB  3BAE          . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)"                                      . . . . .  66.67  28 100.00 100.00 1.81e-10 . . . . 25218 1 
      47 no PDB  3IFN          . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex"                                                      . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      48 no PDB  4HIX          . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide"                                                          . . . . .  66.67  28 100.00 100.00 1.81e-10 . . . . 25218 1 
      49 no PDB  4M1C          . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)"                . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      50 no PDB  4MVI          . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)"          . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      51 no PDB  4MVL          . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40"           . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      52 no PDB  4NGE          . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)"                                             . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      53 no PDB  4ONG          . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40"                                                                           . . . . .  95.24  40 100.00 100.00 1.35e-18 . . . . 25218 1 
      54 no PDB  5AEF          . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril"                                                                        . . . . .  66.67  28 100.00 100.00 2.69e-08 . . . . 25218 1 
      55 no DBJ  BAA22264      . "amyloid precursor protein [Homo sapiens]"                                                                                        . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 
      56 no DBJ  BAA84580      . "amyloid precursor protein [Sus scrofa]"                                                                                          . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 
      57 no DBJ  BAB71958      . "amyloid precursor protein [Homo sapiens]"                                                                                        . . . . . 100.00  52  97.62 100.00 9.73e-20 . . . . 25218 1 
      58 no DBJ  BAD51938      . "amyloid beta A4 precursor protein [Macaca fascicularis]"                                                                         . . . . . 100.00 696 100.00 100.00 8.24e-20 . . . . 25218 1 
      59 no DBJ  BAE01907      . "unnamed protein product [Macaca fascicularis]"                                                                                   . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 
      60 no EMBL CAA30050      . "amyloid A4 protein [Homo sapiens]"                                                                                               . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 
      61 no EMBL CAA31830      . "A4 amyloid protein precursor [Homo sapiens]"                                                                                     . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 
      62 no EMBL CAA39589      . "amyloid precursor protein [Bos taurus]"                                                                                          . . . . . 100.00  59 100.00 100.00 1.94e-20 . . . . 25218 1 
      63 no EMBL CAA39590      . "amyloid precursor protein [Canis lupus familiaris]"                                                                              . . . . . 100.00  58 100.00 100.00 2.01e-20 . . . . 25218 1 
      64 no EMBL CAA39591      . "amyloid precursor protein [Cavia sp.]"                                                                                           . . . . . 100.00  58 100.00 100.00 2.01e-20 . . . . 25218 1 
      65 no GB   AAA35540      . "amyloid protein, partial [Homo sapiens]"                                                                                         . . . . .  95.24  97 100.00 100.00 1.03e-18 . . . . 25218 1 
      66 no GB   AAA36829      . "amyloid b-protein precursor [Macaca fascicularis]"                                                                               . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 
      67 no GB   AAA51564      . "amyloid beta protein, partial [Homo sapiens]"                                                                                    . . . . .  71.43  30 100.00 100.00 9.95e-12 . . . . 25218 1 
      68 no GB   AAA51722      . "amyloid beta-protein precursor, partial [Homo sapiens]"                                                                          . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25218 1 
      69 no GB   AAA51726      . "beta-amyloid A4, partial [Homo sapiens]"                                                                                         . . . . . 100.00 264 100.00 100.00 9.55e-20 . . . . 25218 1 
      70 no PIR  A60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - dog  (fragment)"                                                         . . . . . 100.00  57 100.00 100.00 2.12e-20 . . . . 25218 1 
      71 no PIR  D60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)"                                                       . . . . . 100.00  57 100.00 100.00 2.12e-20 . . . . 25218 1 
      72 no PIR  E60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)"                                                        . . . . . 100.00  57 100.00 100.00 2.12e-20 . . . . 25218 1 
      73 no PIR  G60045        . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)"                                                   . . . . . 100.00  57 100.00 100.00 2.12e-20 . . . . 25218 1 
      74 no PIR  PQ0438        . "Alzheimer's disease amyloid A4 protein precursor - rabbit  (fragment)"                                                           . . . . . 100.00  82 100.00 100.00 2.05e-20 . . . . 25218 1 
      75 no PRF  1303338A      . "amyloid A4 protein precursor"                                                                                                    . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 
      76 no PRF  1403400A      . "amyloid protein A4"                                                                                                              . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 
      77 no PRF  1405204A      . "amyloid protein"                                                                                                                 . . . . . 100.00  42 100.00 100.00 7.22e-20 . . . . 25218 1 
      78 no PRF  1507304A      . "beta amyloid peptide precursor"                                                                                                  . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25218 1 
      79 no PRF  1507304B      . "beta amyloid peptide precursor"                                                                                                  . . . . . 100.00 574 100.00 100.00 2.04e-19 . . . . 25218 1 
      80 no REF  NP_000475     . "amyloid beta A4 protein isoform a precursor [Homo sapiens]"                                                                      . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 
      81 no REF  NP_001006601  . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]"                                                      . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 
      82 no REF  NP_001013036  . "amyloid beta A4 protein precursor [Pan troglodytes]"                                                                             . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 
      83 no REF  NP_001070264  . "amyloid beta A4 protein precursor [Bos taurus]"                                                                                  . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 
      84 no REF  NP_001127014  . "amyloid beta A4 protein precursor [Pongo abelii]"                                                                                . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 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 9.34e-20 . . . . 25218 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 9.34e-20 . . . . 25218 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 9.34e-20 . . . . 25218 1 
      88 no SP   P86906        . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . .  95.24  40  97.50 100.00 5.31e-18 . . . . 25218 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 1.94e-20 . . . . 25218 1 
      90 no TPG  DAA33655      . "TPA: amyloid beta A4 protein [Bos taurus]"                                                                                       . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 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 . 25218 1 
       2 . ALA . 25218 1 
       3 . GLU . 25218 1 
       4 . PHE . 25218 1 
       5 . ARG . 25218 1 
       6 . HIS . 25218 1 
       7 . ASP . 25218 1 
       8 . SER . 25218 1 
       9 . GLY . 25218 1 
      10 . TYR . 25218 1 
      11 . GLU . 25218 1 
      12 . VAL . 25218 1 
      13 . HIS . 25218 1 
      14 . HIS . 25218 1 
      15 . GLN . 25218 1 
      16 . LYS . 25218 1 
      17 . LEU . 25218 1 
      18 . VAL . 25218 1 
      19 . PHE . 25218 1 
      20 . PHE . 25218 1 
      21 . ALA . 25218 1 
      22 . GLU . 25218 1 
      23 . ASP . 25218 1 
      24 . VAL . 25218 1 
      25 . GLY . 25218 1 
      26 . SER . 25218 1 
      27 . ASN . 25218 1 
      28 . LYS . 25218 1 
      29 . GLY . 25218 1 
      30 . ALA . 25218 1 
      31 . ILE . 25218 1 
      32 . ILE . 25218 1 
      33 . GLY . 25218 1 
      34 . LEU . 25218 1 
      35 . MET . 25218 1 
      36 . VAL . 25218 1 
      37 . GLY . 25218 1 
      38 . GLY . 25218 1 
      39 . VAL . 25218 1 
      40 . VAL . 25218 1 
      41 . ILE . 25218 1 
      42 . ALA . 25218 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 25218 1 
      . ALA  2  2 25218 1 
      . GLU  3  3 25218 1 
      . PHE  4  4 25218 1 
      . ARG  5  5 25218 1 
      . HIS  6  6 25218 1 
      . ASP  7  7 25218 1 
      . SER  8  8 25218 1 
      . GLY  9  9 25218 1 
      . TYR 10 10 25218 1 
      . GLU 11 11 25218 1 
      . VAL 12 12 25218 1 
      . HIS 13 13 25218 1 
      . HIS 14 14 25218 1 
      . GLN 15 15 25218 1 
      . LYS 16 16 25218 1 
      . LEU 17 17 25218 1 
      . VAL 18 18 25218 1 
      . PHE 19 19 25218 1 
      . PHE 20 20 25218 1 
      . ALA 21 21 25218 1 
      . GLU 22 22 25218 1 
      . ASP 23 23 25218 1 
      . VAL 24 24 25218 1 
      . GLY 25 25 25218 1 
      . SER 26 26 25218 1 
      . ASN 27 27 25218 1 
      . LYS 28 28 25218 1 
      . GLY 29 29 25218 1 
      . ALA 30 30 25218 1 
      . ILE 31 31 25218 1 
      . ILE 32 32 25218 1 
      . GLY 33 33 25218 1 
      . LEU 34 34 25218 1 
      . MET 35 35 25218 1 
      . VAL 36 36 25218 1 
      . GLY 37 37 25218 1 
      . GLY 38 38 25218 1 
      . VAL 39 39 25218 1 
      . VAL 40 40 25218 1 
      . ILE 41 41 25218 1 
      . ALA 42 42 25218 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       25218
   _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 $entity . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 25218 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       25218
   _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 $entity . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pRSET . . . . . . 25218 1 

   stop_

save_


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

save_sample_1
   _Sample.Sf_category                      sample
   _Sample.Sf_framecode                     sample_1
   _Sample.Entry_ID                         25218
   _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 amyloid_peptide '[U-13C; U-15N]'    . . 1 $entity . .   . 0.5 0.7 mM . . . . 25218 1 
      2 H2O             'natural abundance' . .  .  .      . . 90  .   .  %  . . . . 25218 1 
      3 D2O             'natural abundance' . .  .  .      . . 10  .   .  %  . . . . 25218 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       25218
   _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

       temperature     273   . K   25218 1 
       pH                7.4 . pH  25218 1 
       pressure          1   . atm 25218 1 
      'ionic strength'  20   . mM  25218 1 

   stop_

save_


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

save_ccpNMR
   _Software.Sf_category    software
   _Software.Sf_framecode   ccpNMR
   _Software.Entry_ID       25218
   _Software.ID             1
   _Software.Name           ccpNMR
   _Software.Version        .
   _Software.Details        .

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

      CCPN . . 25218 1 

   stop_

   loop_
      _Task.Task
      _Task.Entry_ID
      _Task.Software_ID

      'chemical shift assignment' 25218 1 
      'peak picking'              25218 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         25218
   _NMR_spectrometer.ID               1
   _NMR_spectrometer.Details          .
   _NMR_spectrometer.Manufacturer     Bruker
   _NMR_spectrometer.Model            Avance
   _NMR_spectrometer.Serial_number    .
   _NMR_spectrometer.Field_strength   700

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       25218
   _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 Bruker Avance . 700 . . . 25218 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       25218
   _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 HNCA'                   no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       2 '3D HNCACB'                 no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       3 '3D HN(CO)CA'               no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       4 '2D 1H-15N HSQC'            no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       5 '2D 1H-1H TOCSY'            no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       6 '2D 1H-1H NOESY'            no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       7 '3D 1H-15N NOESY'           no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       8 '3D 1H-15N TOCSY'           no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
       9 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 
      10 '3D HCCH-TOCSY'             no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 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       25218
   _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 0.00 internal direct   1.000000000 . . . . . . . . . 25218 1 
      C 13 DSS 'methyl protons' . . . . ppm 0.00 na       indirect 0.251449530 . . . . . . . . . 25218 1 
      N 15 DSS 'methyl protons' . . . . ppm 0.00 na       indirect 0.101329118 . . . . . . . . . 25218 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                      25218
   _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 HNCA'                   . . . 25218 1 
       2 '3D HNCACB'                 . . . 25218 1 
       3 '3D HN(CO)CA'               . . . 25218 1 
       4 '2D 1H-15N HSQC'            . . . 25218 1 
       5 '2D 1H-1H TOCSY'            . . . 25218 1 
       6 '2D 1H-1H NOESY'            . . . 25218 1 
       7 '3D 1H-15N NOESY'           . . . 25218 1 
       8 '3D 1H-15N TOCSY'           . . . 25218 1 
       9 '3D 1H-13C NOESY aliphatic' . . . 25218 1 
      10 '3D HCCH-TOCSY'             . . . 25218 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 CA   C 13  53.036 0.400 . 1 . . . .  1 ASP CA   . 25218 1 
        2 . 1 1  1  1 ASP CB   C 13  38.622 0.400 . 1 . . . .  1 ASP CB   . 25218 1 
        3 . 1 1  1  1 ASP N    N 15 117.609 0.400 . 1 . . . .  1 ASP N    . 25218 1 
        4 . 1 1  2  2 ALA H    H  1   7.958 0.020 . 1 . . . .  2 ALA H    . 25218 1 
        5 . 1 1  2  2 ALA HA   H  1   4.161 0.020 . 1 . . . .  2 ALA HA   . 25218 1 
        6 . 1 1  2  2 ALA HB1  H  1   1.267 0.020 . 1 . . . .  2 ALA HB1  . 25218 1 
        7 . 1 1  2  2 ALA HB2  H  1   1.267 0.020 . 1 . . . .  2 ALA HB2  . 25218 1 
        8 . 1 1  2  2 ALA HB3  H  1   1.267 0.020 . 1 . . . .  2 ALA HB3  . 25218 1 
        9 . 1 1  2  2 ALA CA   C 13  52.400 0.400 . 1 . . . .  2 ALA CA   . 25218 1 
       10 . 1 1  2  2 ALA CB   C 13  19.112 0.400 . 1 . . . .  2 ALA CB   . 25218 1 
       11 . 1 1  2  2 ALA N    N 15 123.781 0.400 . 1 . . . .  2 ALA N    . 25218 1 
       12 . 1 1  3  3 GLU H    H  1   8.459 0.020 . 1 . . . .  3 GLU H    . 25218 1 
       13 . 1 1  3  3 GLU HA   H  1   4.073 0.020 . 1 . . . .  3 GLU HA   . 25218 1 
       14 . 1 1  3  3 GLU HB2  H  1   1.801 0.020 . 2 . . . .  3 GLU HB2  . 25218 1 
       15 . 1 1  3  3 GLU HB3  H  1   2.002 0.020 . 2 . . . .  3 GLU HB3  . 25218 1 
       16 . 1 1  3  3 GLU HG2  H  1   2.108 0.020 . 2 . . . .  3 GLU HG2  . 25218 1 
       17 . 1 1  3  3 GLU HG3  H  1   2.108 0.020 . 2 . . . .  3 GLU HG3  . 25218 1 
       18 . 1 1  3  3 GLU CA   C 13  56.497 0.400 . 1 . . . .  3 GLU CA   . 25218 1 
       19 . 1 1  3  3 GLU CB   C 13  30.199 0.400 . 1 . . . .  3 GLU CB   . 25218 1 
       20 . 1 1  3  3 GLU N    N 15 120.309 0.400 . 1 . . . .  3 GLU N    . 25218 1 
       21 . 1 1  4  4 PHE H    H  1   8.299 0.020 . 1 . . . .  4 PHE H    . 25218 1 
       22 . 1 1  4  4 PHE HA   H  1   4.438 0.020 . 1 . . . .  4 PHE HA   . 25218 1 
       23 . 1 1  4  4 PHE HB2  H  1   2.895 0.020 . 2 . . . .  4 PHE HB2  . 25218 1 
       24 . 1 1  4  4 PHE HB3  H  1   2.895 0.020 . 2 . . . .  4 PHE HB3  . 25218 1 
       25 . 1 1  4  4 PHE CA   C 13  57.630 0.400 . 1 . . . .  4 PHE CA   . 25218 1 
       26 . 1 1  4  4 PHE CB   C 13  39.487 0.400 . 1 . . . .  4 PHE CB   . 25218 1 
       27 . 1 1  4  4 PHE N    N 15 121.733 0.400 . 1 . . . .  4 PHE N    . 25218 1 
       28 . 1 1  5  5 ARG H    H  1   8.112 0.020 . 1 . . . .  5 ARG H    . 25218 1 
       29 . 1 1  5  5 ARG HA   H  1   4.162 0.020 . 1 . . . .  5 ARG HA   . 25218 1 
       30 . 1 1  5  5 ARG HB2  H  1   1.620 0.020 . 2 . . . .  5 ARG HB2  . 25218 1 
       31 . 1 1  5  5 ARG HB3  H  1   1.511 0.020 . 2 . . . .  5 ARG HB3  . 25218 1 
       32 . 1 1  5  5 ARG HG2  H  1   1.380 0.020 . 2 . . . .  5 ARG HG2  . 25218 1 
       33 . 1 1  5  5 ARG HG3  H  1   1.380 0.020 . 2 . . . .  5 ARG HG3  . 25218 1 
       34 . 1 1  5  5 ARG HD2  H  1   3.011 0.020 . 2 . . . .  5 ARG HD2  . 25218 1 
       35 . 1 1  5  5 ARG HD3  H  1   3.011 0.020 . 2 . . . .  5 ARG HD3  . 25218 1 
       36 . 1 1  5  5 ARG CA   C 13  55.312 0.400 . 1 . . . .  5 ARG CA   . 25218 1 
       37 . 1 1  5  5 ARG CB   C 13  31.109 0.400 . 1 . . . .  5 ARG CB   . 25218 1 
       38 . 1 1  5  5 ARG N    N 15 123.861 0.400 . 1 . . . .  5 ARG N    . 25218 1 
       39 . 1 1  6  6 HIS H    H  1   8.379 0.020 . 1 . . . .  6 HIS H    . 25218 1 
       40 . 1 1  6  6 HIS HA   H  1   4.401 0.020 . 1 . . . .  6 HIS HA   . 25218 1 
       41 . 1 1  6  6 HIS HB2  H  1   2.923 0.020 . 2 . . . .  6 HIS HB2  . 25218 1 
       42 . 1 1  6  6 HIS HB3  H  1   2.923 0.020 . 2 . . . .  6 HIS HB3  . 25218 1 
       43 . 1 1  6  6 HIS CA   C 13  56.478 0.400 . 1 . . . .  6 HIS CA   . 25218 1 
       44 . 1 1  6  6 HIS CB   C 13  30.743 0.400 . 1 . . . .  6 HIS CB   . 25218 1 
       45 . 1 1  6  6 HIS N    N 15 122.416 0.400 . 1 . . . .  6 HIS N    . 25218 1 
       46 . 1 1  7  7 ASP H    H  1   8.332 0.020 . 1 . . . .  7 ASP H    . 25218 1 
       47 . 1 1  7  7 ASP HA   H  1   4.509 0.020 . 1 . . . .  7 ASP HA   . 25218 1 
       48 . 1 1  7  7 ASP HB2  H  1   2.558 0.020 . 2 . . . .  7 ASP HB2  . 25218 1 
       49 . 1 1  7  7 ASP HB3  H  1   2.558 0.020 . 2 . . . .  7 ASP HB3  . 25218 1 
       50 . 1 1  7  7 ASP CA   C 13  53.908 0.400 . 1 . . . .  7 ASP CA   . 25218 1 
       51 . 1 1  7  7 ASP CB   C 13  40.970 0.400 . 1 . . . .  7 ASP CB   . 25218 1 
       52 . 1 1  7  7 ASP N    N 15 121.615 0.400 . 1 . . . .  7 ASP N    . 25218 1 
       53 . 1 1  8  8 SER H    H  1   8.406 0.020 . 1 . . . .  8 SER H    . 25218 1 
       54 . 1 1  8  8 SER HA   H  1   4.268 0.020 . 1 . . . .  8 SER HA   . 25218 1 
       55 . 1 1  8  8 SER HB2  H  1   3.770 0.020 . 2 . . . .  8 SER HB2  . 25218 1 
       56 . 1 1  8  8 SER HB3  H  1   3.789 0.020 . 2 . . . .  8 SER HB3  . 25218 1 
       57 . 1 1  8  8 SER CA   C 13  58.890 0.400 . 1 . . . .  8 SER CA   . 25218 1 
       58 . 1 1  8  8 SER CB   C 13  63.605 0.400 . 1 . . . .  8 SER CB   . 25218 1 
       59 . 1 1  8  8 SER N    N 15 116.526 0.400 . 1 . . . .  8 SER N    . 25218 1 
       60 . 1 1  9  9 GLY H    H  1   8.525 0.020 . 1 . . . .  9 GLY H    . 25218 1 
       61 . 1 1  9  9 GLY HA3  H  1   3.781 0.020 . 2 . . . .  9 GLY HA3  . 25218 1 
       62 . 1 1  9  9 GLY CA   C 13  45.087 0.400 . 1 . . . .  9 GLY CA   . 25218 1 
       63 . 1 1  9  9 GLY N    N 15 110.656 0.400 . 1 . . . .  9 GLY N    . 25218 1 
       64 . 1 1 10 10 TYR H    H  1   7.931 0.020 . 1 . . . . 10 TYR H    . 25218 1 
       65 . 1 1 10 10 TYR HA   H  1   4.413 0.020 . 1 . . . . 10 TYR HA   . 25218 1 
       66 . 1 1 10 10 TYR HB2  H  1   2.919 0.020 . 2 . . . . 10 TYR HB2  . 25218 1 
       67 . 1 1 10 10 TYR HB3  H  1   2.842 0.020 . 2 . . . . 10 TYR HB3  . 25218 1 
       68 . 1 1 10 10 TYR CA   C 13  58.005 0.400 . 1 . . . . 10 TYR CA   . 25218 1 
       69 . 1 1 10 10 TYR CB   C 13  38.722 0.400 . 1 . . . . 10 TYR CB   . 25218 1 
       70 . 1 1 10 10 TYR N    N 15 119.973 0.400 . 1 . . . . 10 TYR N    . 25218 1 
       71 . 1 1 11 11 GLU H    H  1   8.378 0.020 . 1 . . . . 11 GLU H    . 25218 1 
       72 . 1 1 11 11 GLU HA   H  1   4.087 0.020 . 1 . . . . 11 GLU HA   . 25218 1 
       73 . 1 1 11 11 GLU HB2  H  1   1.721 0.020 . 2 . . . . 11 GLU HB2  . 25218 1 
       74 . 1 1 11 11 GLU HB3  H  1   1.721 0.020 . 2 . . . . 11 GLU HB3  . 25218 1 
       75 . 1 1 11 11 GLU HG2  H  1   2.075 0.020 . 2 . . . . 11 GLU HG2  . 25218 1 
       76 . 1 1 11 11 GLU HG3  H  1   2.075 0.020 . 2 . . . . 11 GLU HG3  . 25218 1 
       77 . 1 1 11 11 GLU CA   C 13  56.468 0.400 . 1 . . . . 11 GLU CA   . 25218 1 
       78 . 1 1 11 11 GLU CB   C 13  30.260 0.400 . 1 . . . . 11 GLU CB   . 25218 1 
       79 . 1 1 11 11 GLU N    N 15 122.553 0.400 . 1 . . . . 11 GLU N    . 25218 1 
       80 . 1 1 12 12 VAL H    H  1   8.083 0.020 . 1 . . . . 12 VAL H    . 25218 1 
       81 . 1 1 12 12 VAL HA   H  1   3.825 0.020 . 1 . . . . 12 VAL HA   . 25218 1 
       82 . 1 1 12 12 VAL HB   H  1   1.830 0.020 . 1 . . . . 12 VAL HB   . 25218 1 
       83 . 1 1 12 12 VAL HG11 H  1   0.669 0.020 . 2 . . . . 12 VAL HG11 . 25218 1 
       84 . 1 1 12 12 VAL HG12 H  1   0.669 0.020 . 2 . . . . 12 VAL HG12 . 25218 1 
       85 . 1 1 12 12 VAL HG13 H  1   0.669 0.020 . 2 . . . . 12 VAL HG13 . 25218 1 
       86 . 1 1 12 12 VAL HG21 H  1   0.757 0.020 . 2 . . . . 12 VAL HG21 . 25218 1 
       87 . 1 1 12 12 VAL HG22 H  1   0.757 0.020 . 2 . . . . 12 VAL HG22 . 25218 1 
       88 . 1 1 12 12 VAL HG23 H  1   0.757 0.020 . 2 . . . . 12 VAL HG23 . 25218 1 
       89 . 1 1 12 12 VAL CA   C 13  62.786 0.400 . 1 . . . . 12 VAL CA   . 25218 1 
       90 . 1 1 12 12 VAL CB   C 13  32.485 0.400 . 1 . . . . 12 VAL CB   . 25218 1 
       91 . 1 1 12 12 VAL N    N 15 121.135 0.400 . 1 . . . . 12 VAL N    . 25218 1 
       92 . 1 1 13 13 HIS H    H  1   8.246 0.020 . 1 . . . . 13 HIS H    . 25218 1 
       93 . 1 1 13 13 HIS HA   H  1   4.475 0.020 . 1 . . . . 13 HIS HA   . 25218 1 
       94 . 1 1 13 13 HIS HB2  H  1   2.903 0.020 . 2 . . . . 13 HIS HB2  . 25218 1 
       95 . 1 1 13 13 HIS HB3  H  1   2.910 0.020 . 2 . . . . 13 HIS HB3  . 25218 1 
       96 . 1 1 13 13 HIS CA   C 13  56.193 0.400 . 1 . . . . 13 HIS CA   . 25218 1 
       97 . 1 1 13 13 HIS CB   C 13  30.727 0.400 . 1 . . . . 13 HIS CB   . 25218 1 
       98 . 1 1 13 13 HIS N    N 15 122.697 0.400 . 1 . . . . 13 HIS N    . 25218 1 
       99 . 1 1 14 14 HIS H    H  1   8.142 0.020 . 1 . . . . 14 HIS H    . 25218 1 
      100 . 1 1 14 14 HIS HA   H  1   4.426 0.020 . 1 . . . . 14 HIS HA   . 25218 1 
      101 . 1 1 14 14 HIS HB2  H  1   2.899 0.020 . 2 . . . . 14 HIS HB2  . 25218 1 
      102 . 1 1 14 14 HIS HB3  H  1   2.972 0.020 . 2 . . . . 14 HIS HB3  . 25218 1 
      103 . 1 1 14 14 HIS CA   C 13  56.489 0.400 . 1 . . . . 14 HIS CA   . 25218 1 
      104 . 1 1 14 14 HIS CB   C 13  30.697 0.400 . 1 . . . . 14 HIS CB   . 25218 1 
      105 . 1 1 14 14 HIS N    N 15 121.248 0.400 . 1 . . . . 14 HIS N    . 25218 1 
      106 . 1 1 15 15 GLN H    H  1   8.376 0.020 . 1 . . . . 15 GLN H    . 25218 1 
      107 . 1 1 15 15 GLN HA   H  1   4.150 0.020 . 1 . . . . 15 GLN HA   . 25218 1 
      108 . 1 1 15 15 GLN HB2  H  1   1.861 0.020 . 2 . . . . 15 GLN HB2  . 25218 1 
      109 . 1 1 15 15 GLN HB3  H  1   1.950 0.020 . 2 . . . . 15 GLN HB3  . 25218 1 
      110 . 1 1 15 15 GLN HG2  H  1   2.215 0.020 . 2 . . . . 15 GLN HG2  . 25218 1 
      111 . 1 1 15 15 GLN HG3  H  1   2.215 0.020 . 2 . . . . 15 GLN HG3  . 25218 1 
      112 . 1 1 15 15 GLN CA   C 13  55.883 0.400 . 1 . . . . 15 GLN CA   . 25218 1 
      113 . 1 1 15 15 GLN CB   C 13  29.386 0.400 . 1 . . . . 15 GLN CB   . 25218 1 
      114 . 1 1 15 15 GLN N    N 15 121.474 0.400 . 1 . . . . 15 GLN N    . 25218 1 
      115 . 1 1 16 16 LYS H    H  1   8.381 0.020 . 1 . . . . 16 LYS H    . 25218 1 
      116 . 1 1 16 16 LYS HA   H  1   4.157 0.020 . 1 . . . . 16 LYS HA   . 25218 1 
      117 . 1 1 16 16 LYS HB2  H  1   1.653 0.020 . 2 . . . . 16 LYS HB2  . 25218 1 
      118 . 1 1 16 16 LYS HB3  H  1   1.690 0.020 . 2 . . . . 16 LYS HB3  . 25218 1 
      119 . 1 1 16 16 LYS HG2  H  1   1.277 0.020 . 2 . . . . 16 LYS HG2  . 25218 1 
      120 . 1 1 16 16 LYS HG3  H  1   1.340 0.020 . 2 . . . . 16 LYS HG3  . 25218 1 
      121 . 1 1 16 16 LYS CA   C 13  56.177 0.400 . 1 . . . . 16 LYS CA   . 25218 1 
      122 . 1 1 16 16 LYS CB   C 13  32.691 0.400 . 1 . . . . 16 LYS CB   . 25218 1 
      123 . 1 1 16 16 LYS N    N 15 122.806 0.400 . 1 . . . . 16 LYS N    . 25218 1 
      124 . 1 1 17 17 LEU H    H  1   8.257 0.020 . 1 . . . . 17 LEU H    . 25218 1 
      125 . 1 1 17 17 LEU HA   H  1   4.215 0.020 . 1 . . . . 17 LEU HA   . 25218 1 
      126 . 1 1 17 17 LEU HB2  H  1   1.496 0.020 . 2 . . . . 17 LEU HB2  . 25218 1 
      127 . 1 1 17 17 LEU HB3  H  1   1.496 0.020 . 2 . . . . 17 LEU HB3  . 25218 1 
      128 . 1 1 17 17 LEU HG   H  1   1.338 0.020 . 1 . . . . 17 LEU HG   . 25218 1 
      129 . 1 1 17 17 LEU HD11 H  1   0.811 0.020 . 2 . . . . 17 LEU HD11 . 25218 1 
      130 . 1 1 17 17 LEU HD12 H  1   0.811 0.020 . 2 . . . . 17 LEU HD12 . 25218 1 
      131 . 1 1 17 17 LEU HD13 H  1   0.811 0.020 . 2 . . . . 17 LEU HD13 . 25218 1 
      132 . 1 1 17 17 LEU HD21 H  1   0.744 0.020 . 2 . . . . 17 LEU HD21 . 25218 1 
      133 . 1 1 17 17 LEU HD22 H  1   0.744 0.020 . 2 . . . . 17 LEU HD22 . 25218 1 
      134 . 1 1 17 17 LEU HD23 H  1   0.744 0.020 . 2 . . . . 17 LEU HD23 . 25218 1 
      135 . 1 1 17 17 LEU CA   C 13  55.129 0.400 . 1 . . . . 17 LEU CA   . 25218 1 
      136 . 1 1 17 17 LEU CB   C 13  42.348 0.400 . 1 . . . . 17 LEU CB   . 25218 1 
      137 . 1 1 17 17 LEU N    N 15 123.881 0.400 . 1 . . . . 17 LEU N    . 25218 1 
      138 . 1 1 18 18 VAL H    H  1   8.002 0.020 . 1 . . . . 18 VAL H    . 25218 1 
      139 . 1 1 18 18 VAL HA   H  1   3.920 0.020 . 1 . . . . 18 VAL HA   . 25218 1 
      140 . 1 1 18 18 VAL HB   H  1   1.795 0.020 . 1 . . . . 18 VAL HB   . 25218 1 
      141 . 1 1 18 18 VAL HG11 H  1   0.643 0.020 . 2 . . . . 18 VAL HG11 . 25218 1 
      142 . 1 1 18 18 VAL HG12 H  1   0.643 0.020 . 2 . . . . 18 VAL HG12 . 25218 1 
      143 . 1 1 18 18 VAL HG13 H  1   0.643 0.020 . 2 . . . . 18 VAL HG13 . 25218 1 
      144 . 1 1 18 18 VAL HG21 H  1   0.734 0.020 . 2 . . . . 18 VAL HG21 . 25218 1 
      145 . 1 1 18 18 VAL HG22 H  1   0.734 0.020 . 2 . . . . 18 VAL HG22 . 25218 1 
      146 . 1 1 18 18 VAL HG23 H  1   0.734 0.020 . 2 . . . . 18 VAL HG23 . 25218 1 
      147 . 1 1 18 18 VAL CA   C 13  61.860 0.400 . 1 . . . . 18 VAL CA   . 25218 1 
      148 . 1 1 18 18 VAL CB   C 13  33.008 0.400 . 1 . . . . 18 VAL CB   . 25218 1 
      149 . 1 1 18 18 VAL N    N 15 121.466 0.400 . 1 . . . . 18 VAL N    . 25218 1 
      150 . 1 1 19 19 PHE H    H  1   8.266 0.020 . 1 . . . . 19 PHE H    . 25218 1 
      151 . 1 1 19 19 PHE HA   H  1   4.471 0.020 . 1 . . . . 19 PHE HA   . 25218 1 
      152 . 1 1 19 19 PHE HB2  H  1   2.874 0.020 . 2 . . . . 19 PHE HB2  . 25218 1 
      153 . 1 1 19 19 PHE HB3  H  1   2.817 0.020 . 2 . . . . 19 PHE HB3  . 25218 1 
      154 . 1 1 19 19 PHE CA   C 13  57.284 0.400 . 1 . . . . 19 PHE CA   . 25218 1 
      155 . 1 1 19 19 PHE CB   C 13  40.024 0.400 . 1 . . . . 19 PHE CB   . 25218 1 
      156 . 1 1 19 19 PHE N    N 15 124.337 0.400 . 1 . . . . 19 PHE N    . 25218 1 
      157 . 1 1 20 20 PHE H    H  1   8.240 0.020 . 1 . . . . 20 PHE H    . 25218 1 
      158 . 1 1 20 20 PHE HA   H  1   4.467 0.020 . 1 . . . . 20 PHE HA   . 25218 1 
      159 . 1 1 20 20 PHE HB2  H  1   2.969 0.020 . 2 . . . . 20 PHE HB2  . 25218 1 
      160 . 1 1 20 20 PHE HB3  H  1   2.822 0.020 . 2 . . . . 20 PHE HB3  . 25218 1 
      161 . 1 1 20 20 PHE CA   C 13  57.240 0.400 . 1 . . . . 20 PHE CA   . 25218 1 
      162 . 1 1 20 20 PHE CB   C 13  40.030 0.400 . 1 . . . . 20 PHE CB   . 25218 1 
      163 . 1 1 20 20 PHE N    N 15 122.962 0.400 . 1 . . . . 20 PHE N    . 25218 1 
      164 . 1 1 21 21 ALA H    H  1   8.250 0.020 . 1 . . . . 21 ALA H    . 25218 1 
      165 . 1 1 21 21 ALA HA   H  1   4.114 0.020 . 1 . . . . 21 ALA HA   . 25218 1 
      166 . 1 1 21 21 ALA HB1  H  1   1.262 0.020 . 1 . . . . 21 ALA HB1  . 25218 1 
      167 . 1 1 21 21 ALA HB2  H  1   1.262 0.020 . 1 . . . . 21 ALA HB2  . 25218 1 
      168 . 1 1 21 21 ALA HB3  H  1   1.262 0.020 . 1 . . . . 21 ALA HB3  . 25218 1 
      169 . 1 1 21 21 ALA CA   C 13  52.257 0.400 . 1 . . . . 21 ALA CA   . 25218 1 
      170 . 1 1 21 21 ALA CB   C 13  19.266 0.400 . 1 . . . . 21 ALA CB   . 25218 1 
      171 . 1 1 21 21 ALA N    N 15 126.210 0.400 . 1 . . . . 21 ALA N    . 25218 1 
      172 . 1 1 22 22 GLU H    H  1   8.365 0.020 . 1 . . . . 22 GLU H    . 25218 1 
      173 . 1 1 22 22 GLU HA   H  1   4.090 0.020 . 1 . . . . 22 GLU HA   . 25218 1 
      174 . 1 1 22 22 GLU HB2  H  1   1.931 0.020 . 2 . . . . 22 GLU HB2  . 25218 1 
      175 . 1 1 22 22 GLU HB3  H  1   1.814 0.020 . 2 . . . . 22 GLU HB3  . 25218 1 
      176 . 1 1 22 22 GLU HG2  H  1   2.167 0.020 . 2 . . . . 22 GLU HG2  . 25218 1 
      177 . 1 1 22 22 GLU HG3  H  1   2.167 0.020 . 2 . . . . 22 GLU HG3  . 25218 1 
      178 . 1 1 22 22 GLU CA   C 13  56.482 0.400 . 1 . . . . 22 GLU CA   . 25218 1 
      179 . 1 1 22 22 GLU CB   C 13  30.240 0.400 . 1 . . . . 22 GLU CB   . 25218 1 
      180 . 1 1 22 22 GLU N    N 15 119.907 0.400 . 1 . . . . 22 GLU N    . 25218 1 
      181 . 1 1 23 23 ASP H    H  1   8.430 0.020 . 1 . . . . 23 ASP H    . 25218 1 
      182 . 1 1 23 23 ASP HA   H  1   4.534 0.020 . 1 . . . . 23 ASP HA   . 25218 1 
      183 . 1 1 23 23 ASP HB2  H  1   2.533 0.020 . 2 . . . . 23 ASP HB2  . 25218 1 
      184 . 1 1 23 23 ASP HB3  H  1   2.641 0.020 . 2 . . . . 23 ASP HB3  . 25218 1 
      185 . 1 1 23 23 ASP CA   C 13  54.008 0.400 . 1 . . . . 23 ASP CA   . 25218 1 
      186 . 1 1 23 23 ASP CB   C 13  40.949 0.400 . 1 . . . . 23 ASP CB   . 25218 1 
      187 . 1 1 23 23 ASP N    N 15 121.769 0.400 . 1 . . . . 23 ASP N    . 25218 1 
      188 . 1 1 24 24 VAL H    H  1   8.168 0.020 . 1 . . . . 24 VAL H    . 25218 1 
      189 . 1 1 24 24 VAL HA   H  1   4.027 0.020 . 1 . . . . 24 VAL HA   . 25218 1 
      190 . 1 1 24 24 VAL HB   H  1   2.084 0.020 . 1 . . . . 24 VAL HB   . 25218 1 
      191 . 1 1 24 24 VAL HG11 H  1   0.850 0.020 . 2 . . . . 24 VAL HG1  . 25218 1 
      192 . 1 1 24 24 VAL HG12 H  1   0.850 0.020 . 2 . . . . 24 VAL HG1  . 25218 1 
      193 . 1 1 24 24 VAL HG13 H  1   0.850 0.020 . 2 . . . . 24 VAL HG1  . 25218 1 
      194 . 1 1 24 24 VAL HG21 H  1   0.850 0.020 . 2 . . . . 24 VAL HG2  . 25218 1 
      195 . 1 1 24 24 VAL HG22 H  1   0.850 0.020 . 2 . . . . 24 VAL HG2  . 25218 1 
      196 . 1 1 24 24 VAL HG23 H  1   0.850 0.020 . 2 . . . . 24 VAL HG2  . 25218 1 
      197 . 1 1 24 24 VAL CA   C 13  62.644 0.400 . 1 . . . . 24 VAL CA   . 25218 1 
      198 . 1 1 24 24 VAL CB   C 13  32.069 0.400 . 1 . . . . 24 VAL CB   . 25218 1 
      199 . 1 1 24 24 VAL N    N 15 120.648 0.400 . 1 . . . . 24 VAL N    . 25218 1 
      200 . 1 1 25 25 GLY H    H  1   8.555 0.020 . 1 . . . . 25 GLY H    . 25218 1 
      201 . 1 1 25 25 GLY HA2  H  1   3.866 0.020 . 2 . . . . 25 GLY HA2  . 25218 1 
      202 . 1 1 25 25 GLY HA3  H  1   3.866 0.020 . 2 . . . . 25 GLY HA3  . 25218 1 
      203 . 1 1 25 25 GLY CA   C 13  45.241 0.400 . 1 . . . . 25 GLY CA   . 25218 1 
      204 . 1 1 25 25 GLY N    N 15 111.702 0.400 . 1 . . . . 25 GLY N    . 25218 1 
      205 . 1 1 26 26 SER H    H  1   8.148 0.020 . 1 . . . . 26 SER H    . 25218 1 
      206 . 1 1 26 26 SER HA   H  1   4.312 0.020 . 1 . . . . 26 SER HA   . 25218 1 
      207 . 1 1 26 26 SER HB2  H  1   3.786 0.020 . 2 . . . . 26 SER HB2  . 25218 1 
      208 . 1 1 26 26 SER HB3  H  1   3.786 0.020 . 2 . . . . 26 SER HB3  . 25218 1 
      209 . 1 1 26 26 SER CA   C 13  58.441 0.400 . 1 . . . . 26 SER CA   . 25218 1 
      210 . 1 1 26 26 SER CB   C 13  63.557 0.400 . 1 . . . . 26 SER CB   . 25218 1 
      211 . 1 1 26 26 SER N    N 15 115.416 0.400 . 1 . . . . 26 SER N    . 25218 1 
      212 . 1 1 27 27 ASN H    H  1   8.481 0.020 . 1 . . . . 27 ASN H    . 25218 1 
      213 . 1 1 27 27 ASN HA   H  1   4.308 0.020 . 1 . . . . 27 ASN HA   . 25218 1 
      214 . 1 1 27 27 ASN HB2  H  1   2.764 0.020 . 2 . . . . 27 ASN HB2  . 25218 1 
      215 . 1 1 27 27 ASN HB3  H  1   2.705 0.020 . 2 . . . . 27 ASN HB3  . 25218 1 
      216 . 1 1 27 27 ASN CA   C 13  53.166 0.400 . 1 . . . . 27 ASN CA   . 25218 1 
      217 . 1 1 27 27 ASN CB   C 13  38.418 0.400 . 1 . . . . 27 ASN CB   . 25218 1 
      218 . 1 1 27 27 ASN N    N 15 120.661 0.400 . 1 . . . . 27 ASN N    . 25218 1 
      219 . 1 1 28 28 LYS H    H  1   8.360 0.020 . 1 . . . . 28 LYS H    . 25218 1 
      220 . 1 1 28 28 LYS HA   H  1   4.161 0.020 . 1 . . . . 28 LYS HA   . 25218 1 
      221 . 1 1 28 28 LYS HB2  H  1   1.779 0.020 . 2 . . . . 28 LYS HB2  . 25218 1 
      222 . 1 1 28 28 LYS HB3  H  1   1.669 0.020 . 2 . . . . 28 LYS HB3  . 25218 1 
      223 . 1 1 28 28 LYS HG2  H  1   1.334 0.020 . 2 . . . . 28 LYS HG2  . 25218 1 
      224 . 1 1 28 28 LYS HG3  H  1   1.334 0.020 . 2 . . . . 28 LYS HG3  . 25218 1 
      225 . 1 1 28 28 LYS HD2  H  1   1.311 0.020 . 2 . . . . 28 LYS HD2  . 25218 1 
      226 . 1 1 28 28 LYS HD3  H  1   1.311 0.020 . 2 . . . . 28 LYS HD3  . 25218 1 
      227 . 1 1 28 28 LYS CA   C 13  56.456 0.400 . 1 . . . . 28 LYS CA   . 25218 1 
      228 . 1 1 28 28 LYS CB   C 13  32.523 0.400 . 1 . . . . 28 LYS CB   . 25218 1 
      229 . 1 1 28 28 LYS N    N 15 121.692 0.400 . 1 . . . . 28 LYS N    . 25218 1 
      230 . 1 1 29 29 GLY H    H  1   8.424 0.020 . 1 . . . . 29 GLY H    . 25218 1 
      231 . 1 1 29 29 GLY HA2  H  1   3.819 0.020 . 2 . . . . 29 GLY HA2  . 25218 1 
      232 . 1 1 29 29 GLY HA3  H  1   3.819 0.020 . 2 . . . . 29 GLY HA3  . 25218 1 
      233 . 1 1 29 29 GLY CA   C 13  45.034 0.400 . 1 . . . . 29 GLY CA   . 25218 1 
      234 . 1 1 29 29 GLY N    N 15 109.500 0.400 . 1 . . . . 29 GLY N    . 25218 1 
      235 . 1 1 30 30 ALA H    H  1   8.031 0.020 . 1 . . . . 30 ALA H    . 25218 1 
      236 . 1 1 30 30 ALA HA   H  1   4.194 0.020 . 1 . . . . 30 ALA HA   . 25218 1 
      237 . 1 1 30 30 ALA HB1  H  1   1.262 0.020 . 1 . . . . 30 ALA HB1  . 25218 1 
      238 . 1 1 30 30 ALA HB2  H  1   1.262 0.020 . 1 . . . . 30 ALA HB2  . 25218 1 
      239 . 1 1 30 30 ALA HB3  H  1   1.262 0.020 . 1 . . . . 30 ALA HB3  . 25218 1 
      240 . 1 1 30 30 ALA CA   C 13  52.379 0.400 . 1 . . . . 30 ALA CA   . 25218 1 
      241 . 1 1 30 30 ALA CB   C 13  19.339 0.400 . 1 . . . . 30 ALA CB   . 25218 1 
      242 . 1 1 30 30 ALA N    N 15 123.448 0.400 . 1 . . . . 30 ALA N    . 25218 1 
      243 . 1 1 31 31 ILE H    H  1   8.183 0.020 . 1 . . . . 31 ILE H    . 25218 1 
      244 . 1 1 31 31 ILE HA   H  1   4.045 0.020 . 1 . . . . 31 ILE HA   . 25218 1 
      245 . 1 1 31 31 ILE HB   H  1   1.756 0.020 . 1 . . . . 31 ILE HB   . 25218 1 
      246 . 1 1 31 31 ILE HG12 H  1   1.400 0.020 . 2 . . . . 31 ILE HG12 . 25218 1 
      247 . 1 1 31 31 ILE HG13 H  1   1.095 0.020 . 2 . . . . 31 ILE HG13 . 25218 1 
      248 . 1 1 31 31 ILE HG21 H  1   0.814 0.020 . 1 . . . . 31 ILE HG21 . 25218 1 
      249 . 1 1 31 31 ILE HG22 H  1   0.814 0.020 . 1 . . . . 31 ILE HG22 . 25218 1 
      250 . 1 1 31 31 ILE HG23 H  1   0.814 0.020 . 1 . . . . 31 ILE HG23 . 25218 1 
      251 . 1 1 31 31 ILE HD11 H  1   0.771 0.020 . 1 . . . . 31 ILE HD11 . 25218 1 
      252 . 1 1 31 31 ILE HD12 H  1   0.771 0.020 . 1 . . . . 31 ILE HD12 . 25218 1 
      253 . 1 1 31 31 ILE HD13 H  1   0.771 0.020 . 1 . . . . 31 ILE HD13 . 25218 1 
      254 . 1 1 31 31 ILE CA   C 13  60.988 0.400 . 1 . . . . 31 ILE CA   . 25218 1 
      255 . 1 1 31 31 ILE CB   C 13  38.310 0.400 . 1 . . . . 31 ILE CB   . 25218 1 
      256 . 1 1 31 31 ILE N    N 15 120.685 0.400 . 1 . . . . 31 ILE N    . 25218 1 
      257 . 1 1 32 32 ILE H    H  1   8.331 0.020 . 1 . . . . 32 ILE H    . 25218 1 
      258 . 1 1 32 32 ILE HA   H  1   4.045 0.020 . 1 . . . . 32 ILE HA   . 25218 1 
      259 . 1 1 32 32 ILE HB   H  1   1.756 0.020 . 1 . . . . 32 ILE HB   . 25218 1 
      260 . 1 1 32 32 ILE HG12 H  1   1.395 0.020 . 2 . . . . 32 ILE HG12 . 25218 1 
      261 . 1 1 32 32 ILE HG13 H  1   1.395 0.020 . 2 . . . . 32 ILE HG13 . 25218 1 
      262 . 1 1 32 32 ILE HG21 H  1   1.102 0.020 . 1 . . . . 32 ILE HG21 . 25218 1 
      263 . 1 1 32 32 ILE HG22 H  1   1.102 0.020 . 1 . . . . 32 ILE HG22 . 25218 1 
      264 . 1 1 32 32 ILE HG23 H  1   1.102 0.020 . 1 . . . . 32 ILE HG23 . 25218 1 
      265 . 1 1 32 32 ILE HD11 H  1   0.772 0.020 . 1 . . . . 32 ILE HD11 . 25218 1 
      266 . 1 1 32 32 ILE HD12 H  1   0.772 0.020 . 1 . . . . 32 ILE HD12 . 25218 1 
      267 . 1 1 32 32 ILE HD13 H  1   0.772 0.020 . 1 . . . . 32 ILE HD13 . 25218 1 
      268 . 1 1 32 32 ILE CA   C 13  61.005 0.400 . 1 . . . . 32 ILE CA   . 25218 1 
      269 . 1 1 32 32 ILE CB   C 13  38.319 0.400 . 1 . . . . 32 ILE CB   . 25218 1 
      270 . 1 1 32 32 ILE N    N 15 126.300 0.400 . 1 . . . . 32 ILE N    . 25218 1 
      271 . 1 1 33 33 GLY H    H  1   8.488 0.020 . 1 . . . . 33 GLY H    . 25218 1 
      272 . 1 1 33 33 GLY HA2  H  1   3.824 0.020 . 2 . . . . 33 GLY HA2  . 25218 1 
      273 . 1 1 33 33 GLY HA3  H  1   3.824 0.020 . 2 . . . . 33 GLY HA3  . 25218 1 
      274 . 1 1 33 33 GLY CA   C 13  45.022 0.400 . 1 . . . . 33 GLY CA   . 25218 1 
      275 . 1 1 33 33 GLY N    N 15 113.019 0.400 . 1 . . . . 33 GLY N    . 25218 1 
      276 . 1 1 34 34 LEU H    H  1   8.062 0.020 . 1 . . . . 34 LEU H    . 25218 1 
      277 . 1 1 34 34 LEU HA   H  1   4.244 0.020 . 1 . . . . 34 LEU HA   . 25218 1 
      278 . 1 1 34 34 LEU HB2  H  1   1.503 0.020 . 2 . . . . 34 LEU HB2  . 25218 1 
      279 . 1 1 34 34 LEU HB3  H  1   1.492 0.020 . 2 . . . . 34 LEU HB3  . 25218 1 
      280 . 1 1 34 34 LEU HD11 H  1   0.816 0.020 . 2 . . . . 34 LEU HD11 . 25218 1 
      281 . 1 1 34 34 LEU HD12 H  1   0.816 0.020 . 2 . . . . 34 LEU HD12 . 25218 1 
      282 . 1 1 34 34 LEU HD13 H  1   0.816 0.020 . 2 . . . . 34 LEU HD13 . 25218 1 
      283 . 1 1 34 34 LEU HD21 H  1   0.761 0.020 . 2 . . . . 34 LEU HD21 . 25218 1 
      284 . 1 1 34 34 LEU HD22 H  1   0.761 0.020 . 2 . . . . 34 LEU HD22 . 25218 1 
      285 . 1 1 34 34 LEU HD23 H  1   0.761 0.020 . 2 . . . . 34 LEU HD23 . 25218 1 
      286 . 1 1 34 34 LEU CA   C 13  54.906 0.400 . 1 . . . . 34 LEU CA   . 25218 1 
      287 . 1 1 34 34 LEU CB   C 13  42.510 0.400 . 1 . . . . 34 LEU CB   . 25218 1 
      288 . 1 1 34 34 LEU N    N 15 121.624 0.400 . 1 . . . . 34 LEU N    . 25218 1 
      289 . 1 1 35 35 MET H    H  1   8.434 0.020 . 1 . . . . 35 MET H    . 25218 1 
      290 . 1 1 35 35 MET HA   H  1   4.522 0.020 . 1 . . . . 35 MET HA   . 25218 1 
      291 . 1 1 35 35 MET HB2  H  1   1.900 0.020 . 2 . . . . 35 MET HB2  . 25218 1 
      292 . 1 1 35 35 MET HB3  H  1   1.900 0.020 . 2 . . . . 35 MET HB3  . 25218 1 
      293 . 1 1 35 35 MET HG2  H  1   2.351 0.020 . 2 . . . . 35 MET HG2  . 25218 1 
      294 . 1 1 35 35 MET HG3  H  1   2.443 0.020 . 2 . . . . 35 MET HG3  . 25218 1 
      295 . 1 1 35 35 MET CA   C 13  54.987 0.400 . 1 . . . . 35 MET CA   . 25218 1 
      296 . 1 1 35 35 MET CB   C 13  33.026 0.400 . 1 . . . . 35 MET CB   . 25218 1 
      297 . 1 1 35 35 MET N    N 15 121.961 0.400 . 1 . . . . 35 MET N    . 25218 1 
      298 . 1 1 36 36 VAL H    H  1   8.340 0.020 . 1 . . . . 36 VAL H    . 25218 1 
      299 . 1 1 36 36 VAL HA   H  1   4.028 0.020 . 1 . . . . 36 VAL HA   . 25218 1 
      300 . 1 1 36 36 VAL HB   H  1   1.936 0.020 . 1 . . . . 36 VAL HB   . 25218 1 
      301 . 1 1 36 36 VAL HG11 H  1   0.837 0.020 . 2 . . . . 36 VAL HG1  . 25218 1 
      302 . 1 1 36 36 VAL HG12 H  1   0.837 0.020 . 2 . . . . 36 VAL HG1  . 25218 1 
      303 . 1 1 36 36 VAL HG13 H  1   0.837 0.020 . 2 . . . . 36 VAL HG1  . 25218 1 
      304 . 1 1 36 36 VAL HG21 H  1   0.837 0.020 . 2 . . . . 36 VAL HG2  . 25218 1 
      305 . 1 1 36 36 VAL HG22 H  1   0.837 0.020 . 2 . . . . 36 VAL HG2  . 25218 1 
      306 . 1 1 36 36 VAL HG23 H  1   0.837 0.020 . 2 . . . . 36 VAL HG2  . 25218 1 
      307 . 1 1 36 36 VAL CA   C 13  62.497 0.400 . 1 . . . . 36 VAL CA   . 25218 1 
      308 . 1 1 36 36 VAL CB   C 13  33.022 0.400 . 1 . . . . 36 VAL CB   . 25218 1 
      309 . 1 1 36 36 VAL N    N 15 122.813 0.400 . 1 . . . . 36 VAL N    . 25218 1 
      310 . 1 1 37 37 GLY H    H  1   8.758 0.020 . 1 . . . . 37 GLY H    . 25218 1 
      311 . 1 1 37 37 GLY HA2  H  1   3.856 0.020 . 2 . . . . 37 GLY HA2  . 25218 1 
      312 . 1 1 37 37 GLY HA3  H  1   3.856 0.020 . 2 . . . . 37 GLY HA3  . 25218 1 
      313 . 1 1 37 37 GLY CA   C 13  45.249 0.400 . 1 . . . . 37 GLY CA   . 25218 1 
      314 . 1 1 37 37 GLY N    N 15 114.223 0.400 . 1 . . . . 37 GLY N    . 25218 1 
      315 . 1 1 38 38 GLY H    H  1   8.326 0.020 . 1 . . . . 38 GLY H    . 25218 1 
      316 . 1 1 38 38 GLY HA2  H  1   3.850 0.020 . 2 . . . . 38 GLY HA2  . 25218 1 
      317 . 1 1 38 38 GLY HA3  H  1   3.850 0.020 . 2 . . . . 38 GLY HA3  . 25218 1 
      318 . 1 1 38 38 GLY CA   C 13  45.077 0.400 . 1 . . . . 38 GLY CA   . 25218 1 
      319 . 1 1 38 38 GLY N    N 15 107.850 0.400 . 1 . . . . 38 GLY N    . 25218 1 
      320 . 1 1 39 39 VAL H    H  1   7.923 0.020 . 1 . . . . 39 VAL H    . 25218 1 
      321 . 1 1 39 39 VAL HA   H  1   4.054 0.020 . 1 . . . . 39 VAL HA   . 25218 1 
      322 . 1 1 39 39 VAL HB   H  1   1.933 0.020 . 1 . . . . 39 VAL HB   . 25218 1 
      323 . 1 1 39 39 VAL HG11 H  1   0.818 0.020 . 2 . . . . 39 VAL HG1  . 25218 1 
      324 . 1 1 39 39 VAL HG12 H  1   0.818 0.020 . 2 . . . . 39 VAL HG1  . 25218 1 
      325 . 1 1 39 39 VAL HG13 H  1   0.818 0.020 . 2 . . . . 39 VAL HG1  . 25218 1 
      326 . 1 1 39 39 VAL HG21 H  1   0.818 0.020 . 2 . . . . 39 VAL HG2  . 25218 1 
      327 . 1 1 39 39 VAL HG22 H  1   0.818 0.020 . 2 . . . . 39 VAL HG2  . 25218 1 
      328 . 1 1 39 39 VAL HG23 H  1   0.818 0.020 . 2 . . . . 39 VAL HG2  . 25218 1 
      329 . 1 1 39 39 VAL CA   C 13  61.855 0.400 . 1 . . . . 39 VAL CA   . 25218 1 
      330 . 1 1 39 39 VAL CB   C 13  33.112 0.400 . 1 . . . . 39 VAL CB   . 25218 1 
      331 . 1 1 39 39 VAL N    N 15 119.768 0.400 . 1 . . . . 39 VAL N    . 25218 1 
      332 . 1 1 40 40 VAL H    H  1   8.416 0.020 . 1 . . . . 40 VAL H    . 25218 1 
      333 . 1 1 40 40 VAL HA   H  1   4.042 0.020 . 1 . . . . 40 VAL HA   . 25218 1 
      334 . 1 1 40 40 VAL HB   H  1   1.888 0.020 . 1 . . . . 40 VAL HB   . 25218 1 
      335 . 1 1 40 40 VAL HG11 H  1   0.824 0.020 . 2 . . . . 40 VAL HG1  . 25218 1 
      336 . 1 1 40 40 VAL HG12 H  1   0.824 0.020 . 2 . . . . 40 VAL HG1  . 25218 1 
      337 . 1 1 40 40 VAL HG13 H  1   0.824 0.020 . 2 . . . . 40 VAL HG1  . 25218 1 
      338 . 1 1 40 40 VAL HG21 H  1   0.824 0.020 . 2 . . . . 40 VAL HG2  . 25218 1 
      339 . 1 1 40 40 VAL HG22 H  1   0.824 0.020 . 2 . . . . 40 VAL HG2  . 25218 1 
      340 . 1 1 40 40 VAL HG23 H  1   0.824 0.020 . 2 . . . . 40 VAL HG2  . 25218 1 
      341 . 1 1 40 40 VAL CA   C 13  62.473 0.400 . 1 . . . . 40 VAL CA   . 25218 1 
      342 . 1 1 40 40 VAL CB   C 13  32.512 0.400 . 1 . . . . 40 VAL CB   . 25218 1 
      343 . 1 1 40 40 VAL N    N 15 126.149 0.400 . 1 . . . . 40 VAL N    . 25218 1 
      344 . 1 1 41 41 ILE H    H  1   8.462 0.020 . 1 . . . . 41 ILE H    . 25218 1 
      345 . 1 1 41 41 ILE HA   H  1   4.023 0.020 . 1 . . . . 41 ILE HA   . 25218 1 
      346 . 1 1 41 41 ILE HB   H  1   1.777 0.020 . 1 . . . . 41 ILE HB   . 25218 1 
      347 . 1 1 41 41 ILE HG12 H  1   1.385 0.020 . 2 . . . . 41 ILE HG12 . 25218 1 
      348 . 1 1 41 41 ILE HG13 H  1   1.100 0.020 . 2 . . . . 41 ILE HG13 . 25218 1 
      349 . 1 1 41 41 ILE HD11 H  1   0.782 0.020 . 1 . . . . 41 ILE HD11 . 25218 1 
      350 . 1 1 41 41 ILE HD12 H  1   0.782 0.020 . 1 . . . . 41 ILE HD12 . 25218 1 
      351 . 1 1 41 41 ILE HD13 H  1   0.782 0.020 . 1 . . . . 41 ILE HD13 . 25218 1 
      352 . 1 1 41 41 ILE CA   C 13  60.700 0.400 . 1 . . . . 41 ILE CA   . 25218 1 
      353 . 1 1 41 41 ILE CB   C 13  38.287 0.400 . 1 . . . . 41 ILE CB   . 25218 1 
      354 . 1 1 41 41 ILE N    N 15 127.666 0.400 . 1 . . . . 41 ILE N    . 25218 1 
      355 . 1 1 42 42 ALA H    H  1   8.045 0.020 . 1 . . . . 42 ALA H    . 25218 1 
      356 . 1 1 42 42 ALA HA   H  1   4.037 0.020 . 1 . . . . 42 ALA HA   . 25218 1 
      357 . 1 1 42 42 ALA HB1  H  1   1.231 0.020 . 1 . . . . 42 ALA HB1  . 25218 1 
      358 . 1 1 42 42 ALA HB2  H  1   1.231 0.020 . 1 . . . . 42 ALA HB2  . 25218 1 
      359 . 1 1 42 42 ALA HB3  H  1   1.231 0.020 . 1 . . . . 42 ALA HB3  . 25218 1 
      360 . 1 1 42 42 ALA CA   C 13  53.735 0.400 . 1 . . . . 42 ALA CA   . 25218 1 
      361 . 1 1 42 42 ALA CB   C 13  20.211 0.400 . 1 . . . . 42 ALA CB   . 25218 1 
      362 . 1 1 42 42 ALA N    N 15 134.150 0.400 . 1 . . . . 42 ALA N    . 25218 1 

   stop_

save_