data_11435 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11435 _Entry.Title ; 1H, 13C, and 15N Chemical Shift Assignments for amyloid-beta-(1-40) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-03-16 _Entry.Accession_date 2011-03-16 _Entry.Last_release_date 2011-06-07 _Entry.Original_release_date 2011-06-07 _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 Takahiro Yamaguchi . . . 11435 2 Katsumi Matsuzaki . . . 11435 3 Masaru Hoshino . . . 11435 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 11435 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 107 11435 '15N chemical shifts' 39 11435 '1H chemical shifts' 206 11435 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 . . 2011-06-07 2011-03-16 original author . 11435 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 11435 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 21402073 _Citation.Full_citation . _Citation.Title 'Transient formation of intermediate conformational states of amyloid-beta peptide revealed by heteronuclear magnetic resonance spectroscopy' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full . _Citation.Journal_volume 585 _Citation.Journal_issue 7 _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 1097 _Citation.Page_last 1102 _Citation.Year 2011 _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 Takahiro Yamaguchi . . . 11435 1 2 Katsumi Matsuzaki . . . 11435 1 3 Masaru Hoshino . . . 11435 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11435 _Assembly.ID 1 _Assembly.Name Amyloid-beta-(1-40) _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 'Amyloid beta-(1-40)' 1 $Amyloid-beta-(1-40) A . yes 'intrinsically disordered' no yes . . . 11435 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Amyloid-beta-(1-40) _Entity.Sf_category entity _Entity.Sf_framecode Amyloid-beta-(1-40) _Entity.Entry_ID 11435 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Amyloid-beta-(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 2015-11-26 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 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 11435 1 2 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 3 no BMRB 17186 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 4 no BMRB 17764 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 5 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 1 6 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 1 7 no BMRB 17795 . Abeta(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 8 no BMRB 17796 . Abeta40 . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 9 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 92.50 38 100.00 100.00 2.74e-16 . . . . 11435 1 10 no BMRB 18127 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 11 no BMRB 18128 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 12 no BMRB 18129 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 13 no BMRB 18131 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 14 no BMRB 19009 . beta-amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 15 no BMRB 19309 . amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 16 no BMRB 19393 . Abeta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 11435 1 17 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 1 18 no BMRB 25289 . amyloid_beta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 11435 1 19 no BMRB 25429 . entity . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 1 20 no BMRB 26508 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 1 21 no BMRB 26516 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 65.00 26 100.00 100.00 2.06e-08 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 100.00 40 97.50 100.00 5.11e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 11435 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 11435 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.50 100.00 1.74e-18 . . . . 11435 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 1.14e-18 . . . . 11435 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 1.43e-18 . . . . 11435 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 11435 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 11435 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 3.56e-19 . . . . 11435 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 11435 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 11435 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.00 97 100.00 100.00 2.36e-17 . . . . 11435 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 11435 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 75.00 30 100.00 100.00 1.09e-11 . . . . 11435 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 9.13e-19 . . . . 11435 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 1.74e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 4.05e-19 . . . . 11435 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 11435 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 11435 1 77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 11435 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 9.42e-19 . . . . 11435 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 4.07e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 11435 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 11435 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 1.65e-18 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 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 . . . . 11435 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 11435 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 . 11435 1 2 . ALA . 11435 1 3 . GLU . 11435 1 4 . PHE . 11435 1 5 . ARG . 11435 1 6 . HIS . 11435 1 7 . ASP . 11435 1 8 . SER . 11435 1 9 . GLY . 11435 1 10 . TYR . 11435 1 11 . GLU . 11435 1 12 . VAL . 11435 1 13 . HIS . 11435 1 14 . HIS . 11435 1 15 . GLN . 11435 1 16 . LYS . 11435 1 17 . LEU . 11435 1 18 . VAL . 11435 1 19 . PHE . 11435 1 20 . PHE . 11435 1 21 . ALA . 11435 1 22 . GLU . 11435 1 23 . ASP . 11435 1 24 . VAL . 11435 1 25 . GLY . 11435 1 26 . SER . 11435 1 27 . ASN . 11435 1 28 . LYS . 11435 1 29 . GLY . 11435 1 30 . ALA . 11435 1 31 . ILE . 11435 1 32 . ILE . 11435 1 33 . GLY . 11435 1 34 . LEU . 11435 1 35 . MET . 11435 1 36 . VAL . 11435 1 37 . GLY . 11435 1 38 . GLY . 11435 1 39 . VAL . 11435 1 40 . VAL . 11435 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 11435 1 . ALA 2 2 11435 1 . GLU 3 3 11435 1 . PHE 4 4 11435 1 . ARG 5 5 11435 1 . HIS 6 6 11435 1 . ASP 7 7 11435 1 . SER 8 8 11435 1 . GLY 9 9 11435 1 . TYR 10 10 11435 1 . GLU 11 11 11435 1 . VAL 12 12 11435 1 . HIS 13 13 11435 1 . HIS 14 14 11435 1 . GLN 15 15 11435 1 . LYS 16 16 11435 1 . LEU 17 17 11435 1 . VAL 18 18 11435 1 . PHE 19 19 11435 1 . PHE 20 20 11435 1 . ALA 21 21 11435 1 . GLU 22 22 11435 1 . ASP 23 23 11435 1 . VAL 24 24 11435 1 . GLY 25 25 11435 1 . SER 26 26 11435 1 . ASN 27 27 11435 1 . LYS 28 28 11435 1 . GLY 29 29 11435 1 . ALA 30 30 11435 1 . ILE 31 31 11435 1 . ILE 32 32 11435 1 . GLY 33 33 11435 1 . LEU 34 34 11435 1 . MET 35 35 11435 1 . VAL 36 36 11435 1 . GLY 37 37 11435 1 . GLY 38 38 11435 1 . VAL 39 39 11435 1 . VAL 40 40 11435 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 11435 _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 $Amyloid-beta-(1-40) . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 11435 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 11435 _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 $Amyloid-beta-(1-40) . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET28a . . . . . . 11435 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11435 _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-beta-(1-40) [U-15N] . . 1 $Amyloid-beta-(1-40) . . 50 . . uM . . . . 11435 1 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 11435 1 3 'sodium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 11435 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 11435 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 11435 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 11435 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% 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-beta-(1-40) '[U-13C; U-15N]' . . 1 $Amyloid-beta-(1-40) . . 50 . . uM . . . . 11435 2 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 11435 2 3 'sodium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 11435 2 4 D2O 'natural abundance' . . . . . . 100 . . % . . . . 11435 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 11435 _Sample.ID 3 _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-beta-(1-40) '[U-13C; U-15N]' . . 1 $Amyloid-beta-(1-40) . . 150 . . uM . . . . 11435 3 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 11435 3 3 'sodium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 11435 3 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 11435 3 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 11435 3 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 11435 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.5 . pH 11435 1 temperature 277 . K 11435 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 11435 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 11435 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 11435 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 11435 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 11435 _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 DMX . 600 . . . 11435 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 11435 _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 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11435 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11435 1 3 '3D HNCACB' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11435 1 4 '3D HCCH-TOCSY' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11435 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 11435 _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 carbons' . . . . ppm 0.00 external direct 0.251449530 . . . . . . . . . 11435 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 external direct 1.000000000 . . . . . . . . . 11435 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 external indirect 0.101329118 . . . . . . . . . 11435 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 11435 _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 '2D 1H-15N HSQC' . . . 11435 1 2 '2D 1H-13C HSQC' . . . 11435 1 3 '3D HNCACB' . . . 11435 1 4 '3D HCCH-TOCSY' . . . 11435 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 HA H 1 4.23 0.01 . 1 . . . . 1 ASP HA . 11435 1 2 . 1 1 1 1 ASP HB2 H 1 2.72 0.01 . 2 . . . . 1 ASP HB2 . 11435 1 3 . 1 1 1 1 ASP HB3 H 1 2.84 0.01 . 2 . . . . 1 ASP HB3 . 11435 1 4 . 1 1 1 1 ASP CA C 13 53.7 0.1 . 1 . . . . 1 ASP CA . 11435 1 5 . 1 1 1 1 ASP CB C 13 40.0 0.1 . 1 . . . . 1 ASP CB . 11435 1 6 . 1 1 2 2 ALA H H 1 8.79 0.01 . 1 . . . . 2 ALA H . 11435 1 7 . 1 1 2 2 ALA HA H 1 4.31 0.01 . 1 . . . . 2 ALA HA . 11435 1 8 . 1 1 2 2 ALA HB1 H 1 1.37 0.01 . 1 . . . . 2 ALA MB . 11435 1 9 . 1 1 2 2 ALA HB2 H 1 1.37 0.01 . 1 . . . . 2 ALA MB . 11435 1 10 . 1 1 2 2 ALA HB3 H 1 1.37 0.01 . 1 . . . . 2 ALA MB . 11435 1 11 . 1 1 2 2 ALA CA C 13 52.7 0.1 . 1 . . . . 2 ALA CA . 11435 1 12 . 1 1 2 2 ALA CB C 13 19.1 0.1 . 1 . . . . 2 ALA CB . 11435 1 13 . 1 1 2 2 ALA N N 15 124.3 0.1 . 1 . . . . 2 ALA N . 11435 1 14 . 1 1 3 3 GLU H H 1 8.57 0.01 . 1 . . . . 3 GLU H . 11435 1 15 . 1 1 3 3 GLU HA H 1 4.18 0.01 . 1 . . . . 3 GLU HA . 11435 1 16 . 1 1 3 3 GLU HB2 H 1 1.92 0.01 . 5 . . . . 3 GLU HB2 . 11435 1 17 . 1 1 3 3 GLU HB3 H 1 2.04 0.01 . 5 . . . . 3 GLU HB3 . 11435 1 18 . 1 1 3 3 GLU HG2 H 1 2.14 0.01 . 5 . . . . 3 GLU HG2 . 11435 1 19 . 1 1 3 3 GLU HG3 H 1 2.22 0.01 . 5 . . . . 3 GLU HG3 . 11435 1 20 . 1 1 3 3 GLU CA C 13 56.6 0.1 . 1 . . . . 3 GLU CA . 11435 1 21 . 1 1 3 3 GLU CB C 13 30.2 0.1 . 1 . . . . 3 GLU CB . 11435 1 22 . 1 1 3 3 GLU CG C 13 36.2 0.1 . 5 . . . . 3 GLU CG . 11435 1 23 . 1 1 3 3 GLU N N 15 121.0 0.1 . 1 . . . . 3 GLU N . 11435 1 24 . 1 1 4 4 PHE H H 1 8.44 0.01 . 1 . . . . 4 PHE H . 11435 1 25 . 1 1 4 4 PHE HA H 1 4.59 0.01 . 1 . . . . 4 PHE HA . 11435 1 26 . 1 1 4 4 PHE HB2 H 1 3.02 0.01 . 2 . . . . 4 PHE HB2 . 11435 1 27 . 1 1 4 4 PHE CA C 13 57.6 0.1 . 1 . . . . 4 PHE CA . 11435 1 28 . 1 1 4 4 PHE CB C 13 39.5 0.1 . 1 . . . . 4 PHE CB . 11435 1 29 . 1 1 4 4 PHE N N 15 122.1 0.1 . 1 . . . . 4 PHE N . 11435 1 30 . 1 1 5 5 ARG H H 1 8.30 0.01 . 1 . . . . 5 ARG H . 11435 1 31 . 1 1 5 5 ARG HA H 1 4.24 0.01 . 1 . . . . 5 ARG HA . 11435 1 32 . 1 1 5 5 ARG HB2 H 1 1.64 0.01 . 2 . . . . 5 ARG HB2 . 11435 1 33 . 1 1 5 5 ARG HB3 H 1 1.73 0.01 . 2 . . . . 5 ARG HB3 . 11435 1 34 . 1 1 5 5 ARG HG2 H 1 1.48 0.01 . 2 . . . . 5 ARG HG2 . 11435 1 35 . 1 1 5 5 ARG HD2 H 1 3.12 0.01 . 2 . . . . 5 ARG HD2 . 11435 1 36 . 1 1 5 5 ARG CA C 13 55.7 0.1 . 1 . . . . 5 ARG CA . 11435 1 37 . 1 1 5 5 ARG CB C 13 31.0 0.1 . 1 . . . . 5 ARG CB . 11435 1 38 . 1 1 5 5 ARG CG C 13 27.0 0.1 . 1 . . . . 5 ARG CG . 11435 1 39 . 1 1 5 5 ARG CD C 13 43.2 0.1 . 1 . . . . 5 ARG CD . 11435 1 40 . 1 1 5 5 ARG N N 15 123.9 0.1 . 1 . . . . 5 ARG N . 11435 1 41 . 1 1 6 6 HIS H H 1 8.61 0.01 . 1 . . . . 6 HIS H . 11435 1 42 . 1 1 6 6 HIS HA H 1 4.59 0.01 . 1 . . . . 6 HIS HA . 11435 1 43 . 1 1 6 6 HIS HB2 H 1 3.08 0.01 . 5 . . . . 6 HIS HB2 . 11435 1 44 . 1 1 6 6 HIS HB3 H 1 3.16 0.01 . 5 . . . . 6 HIS HB3 . 11435 1 45 . 1 1 6 6 HIS CA C 13 55.9 0.1 . 1 . . . . 6 HIS CA . 11435 1 46 . 1 1 6 6 HIS CB C 13 30.0 0.1 . 1 . . . . 6 HIS CB . 11435 1 47 . 1 1 6 6 HIS N N 15 121.4 0.1 . 1 . . . . 6 HIS N . 11435 1 48 . 1 1 7 7 ASP H H 1 8.53 0.01 . 1 . . . . 7 ASP H . 11435 1 49 . 1 1 7 7 ASP HA H 1 4.65 0.01 . 1 . . . . 7 ASP HA . 11435 1 50 . 1 1 7 7 ASP HB2 H 1 2.70 0.01 . 5 . . . . 7 ASP HB2 . 11435 1 51 . 1 1 7 7 ASP CA C 13 54.1 0.1 . 1 . . . . 7 ASP CA . 11435 1 52 . 1 1 7 7 ASP CB C 13 41.2 0.1 . 1 . . . . 7 ASP CB . 11435 1 53 . 1 1 7 7 ASP N N 15 122.1 0.1 . 1 . . . . 7 ASP N . 11435 1 54 . 1 1 8 8 SER H H 1 8.60 0.01 . 1 . . . . 8 SER H . 11435 1 55 . 1 1 8 8 SER HA H 1 4.40 0.01 . 1 . . . . 8 SER HA . 11435 1 56 . 1 1 8 8 SER HB2 H 1 3.90 0.01 . 5 . . . . 8 SER HB2 . 11435 1 57 . 1 1 8 8 SER CA C 13 59.2 0.1 . 1 . . . . 8 SER CA . 11435 1 58 . 1 1 8 8 SER CB C 13 63.6 0.1 . 1 . . . . 8 SER CB . 11435 1 59 . 1 1 8 8 SER N N 15 117.1 0.1 . 1 . . . . 8 SER N . 11435 1 60 . 1 1 9 9 GLY H H 1 8.68 0.01 . 1 . . . . 9 GLY H . 11435 1 61 . 1 1 9 9 GLY HA2 H 1 3.93 0.01 . 2 . . . . 9 GLY HA2 . 11435 1 62 . 1 1 9 9 GLY CA C 13 45.4 0.1 . 1 . . . . 9 GLY CA . 11435 1 63 . 1 1 9 9 GLY N N 15 111.2 0.1 . 1 . . . . 9 GLY N . 11435 1 64 . 1 1 10 10 TYR H H 1 8.07 0.01 . 1 . . . . 10 TYR H . 11435 1 65 . 1 1 10 10 TYR HA H 1 4.51 0.01 . 1 . . . . 10 TYR HA . 11435 1 66 . 1 1 10 10 TYR HB2 H 1 2.97 0.01 . 2 . . . . 10 TYR HB2 . 11435 1 67 . 1 1 10 10 TYR HB3 H 1 3.01 0.01 . 2 . . . . 10 TYR HB3 . 11435 1 68 . 1 1 10 10 TYR CA C 13 58.4 0.1 . 1 . . . . 10 TYR CA . 11435 1 69 . 1 1 10 10 TYR CB C 13 38.8 0.1 . 1 . . . . 10 TYR CB . 11435 1 70 . 1 1 10 10 TYR N N 15 120.6 0.1 . 1 . . . . 10 TYR N . 11435 1 71 . 1 1 11 11 GLU H H 1 8.49 0.01 . 1 . . . . 11 GLU H . 11435 1 72 . 1 1 11 11 GLU HA H 1 4.21 0.01 . 1 . . . . 11 GLU HA . 11435 1 73 . 1 1 11 11 GLU HB2 H 1 1.92 0.01 . 5 . . . . 11 GLU HB2 . 11435 1 74 . 1 1 11 11 GLU HB3 H 1 2.04 0.01 . 5 . . . . 11 GLU HB3 . 11435 1 75 . 1 1 11 11 GLU HG2 H 1 2.14 0.01 . 5 . . . . 11 GLU HG2 . 11435 1 76 . 1 1 11 11 GLU HG3 H 1 2.22 0.01 . 5 . . . . 11 GLU HG3 . 11435 1 77 . 1 1 11 11 GLU CA C 13 56.5 0.1 . 1 . . . . 11 GLU CA . 11435 1 78 . 1 1 11 11 GLU CB C 13 30.3 0.1 . 1 . . . . 11 GLU CB . 11435 1 79 . 1 1 11 11 GLU CG C 13 36.2 0.1 . 5 . . . . 11 GLU CG . 11435 1 80 . 1 1 11 11 GLU N N 15 123.0 0.1 . 1 . . . . 11 GLU N . 11435 1 81 . 1 1 12 12 VAL H H 1 8.21 0.01 . 1 . . . . 12 VAL H . 11435 1 82 . 1 1 12 12 VAL HA H 1 3.93 0.01 . 1 . . . . 12 VAL HA . 11435 1 83 . 1 1 12 12 VAL HB H 1 1.93 0.01 . 1 . . . . 12 VAL HB . 11435 1 84 . 1 1 12 12 VAL HG11 H 1 0.77 0.01 . 2 . . . . 12 VAL MG1 . 11435 1 85 . 1 1 12 12 VAL HG12 H 1 0.77 0.01 . 2 . . . . 12 VAL MG1 . 11435 1 86 . 1 1 12 12 VAL HG13 H 1 0.77 0.01 . 2 . . . . 12 VAL MG1 . 11435 1 87 . 1 1 12 12 VAL HG21 H 1 0.88 0.01 . 2 . . . . 12 VAL MG2 . 11435 1 88 . 1 1 12 12 VAL HG22 H 1 0.88 0.01 . 2 . . . . 12 VAL MG2 . 11435 1 89 . 1 1 12 12 VAL HG23 H 1 0.88 0.01 . 2 . . . . 12 VAL MG2 . 11435 1 90 . 1 1 12 12 VAL CA C 13 62.8 0.1 . 1 . . . . 12 VAL CA . 11435 1 91 . 1 1 12 12 VAL CB C 13 32.5 0.1 . 1 . . . . 12 VAL CB . 11435 1 92 . 1 1 12 12 VAL CG1 C 13 20.8 0.1 . 2 . . . . 12 VAL CG1 . 11435 1 93 . 1 1 12 12 VAL N N 15 121.8 0.1 . 1 . . . . 12 VAL N . 11435 1 94 . 1 1 13 13 HIS H H 1 8.49 0.01 . 1 . . . . 13 HIS H . 11435 1 95 . 1 1 13 13 HIS HA H 1 4.66 0.01 . 1 . . . . 13 HIS HA . 11435 1 96 . 1 1 13 13 HIS HB2 H 1 3.05 0.01 . 2 . . . . 13 HIS HB2 . 11435 1 97 . 1 1 13 13 HIS HB3 H 1 3.12 0.01 . 2 . . . . 13 HIS HB3 . 11435 1 98 . 1 1 13 13 HIS CA C 13 55.7 0.1 . 1 . . . . 13 HIS CA . 11435 1 99 . 1 1 13 13 HIS CB C 13 29.9 0.1 . 1 . . . . 13 HIS CB . 11435 1 100 . 1 1 13 13 HIS N N 15 122.7 0.1 . 1 . . . . 13 HIS N . 11435 1 101 . 1 1 14 14 HIS H H 1 8.53 0.01 . 1 . . . . 14 HIS H . 11435 1 102 . 1 1 14 14 HIS HA H 1 4.60 0.01 . 1 . . . . 14 HIS HA . 11435 1 103 . 1 1 14 14 HIS HB2 H 1 3.08 0.01 . 5 . . . . 14 HIS HB2 . 11435 1 104 . 1 1 14 14 HIS HB3 H 1 3.16 0.01 . 5 . . . . 14 HIS HB3 . 11435 1 105 . 1 1 14 14 HIS CA C 13 55.9 0.1 . 1 . . . . 14 HIS CA . 11435 1 106 . 1 1 14 14 HIS CB C 13 29.9 0.1 . 1 . . . . 14 HIS CB . 11435 1 107 . 1 1 14 14 HIS N N 15 121.3 0.1 . 1 . . . . 14 HIS N . 11435 1 108 . 1 1 15 15 GLN H H 1 8.62 0.01 . 1 . . . . 15 GLN H . 11435 1 109 . 1 1 15 15 GLN HA H 1 4.29 0.01 . 1 . . . . 15 GLN HA . 11435 1 110 . 1 1 15 15 GLN HB2 H 1 1.98 0.01 . 2 . . . . 15 GLN HB2 . 11435 1 111 . 1 1 15 15 GLN HB3 H 1 2.06 0.01 . 2 . . . . 15 GLN HB3 . 11435 1 112 . 1 1 15 15 GLN HG2 H 1 2.35 0.01 . 2 . . . . 15 GLN HG2 . 11435 1 113 . 1 1 15 15 GLN CA C 13 55.9 0.1 . 1 . . . . 15 GLN CA . 11435 1 114 . 1 1 15 15 GLN CB C 13 29.5 0.1 . 1 . . . . 15 GLN CB . 11435 1 115 . 1 1 15 15 GLN CG C 13 33.7 0.1 . 1 . . . . 15 GLN CG . 11435 1 116 . 1 1 15 15 GLN N N 15 122.1 0.1 . 1 . . . . 15 GLN N . 11435 1 117 . 1 1 16 16 LYS H H 1 8.58 0.01 . 1 . . . . 16 LYS H . 11435 1 118 . 1 1 16 16 LYS HA H 1 4.29 0.01 . 1 . . . . 16 LYS HA . 11435 1 119 . 1 1 16 16 LYS HB2 H 1 1.78 0.01 . 2 . . . . 16 LYS HB2 . 11435 1 120 . 1 1 16 16 LYS HG2 H 1 1.40 0.01 . 5 . . . . 16 LYS HG2 . 11435 1 121 . 1 1 16 16 LYS HG3 H 1 1.46 0.01 . 5 . . . . 16 LYS HG3 . 11435 1 122 . 1 1 16 16 LYS HD2 H 1 1.68 0.01 . 5 . . . . 16 LYS HD2 . 11435 1 123 . 1 1 16 16 LYS HD3 H 1 1.78 0.01 . 5 . . . . 16 LYS HD3 . 11435 1 124 . 1 1 16 16 LYS HE2 H 1 2.98 0.01 . 5 . . . . 16 LYS HE2 . 11435 1 125 . 1 1 16 16 LYS CA C 13 56.4 0.1 . 1 . . . . 16 LYS CA . 11435 1 126 . 1 1 16 16 LYS CB C 13 33.0 0.1 . 1 . . . . 16 LYS CB . 11435 1 127 . 1 1 16 16 LYS CG C 13 24.8 0.1 . 5 . . . . 16 LYS CG . 11435 1 128 . 1 1 16 16 LYS CD C 13 29.1 0.1 . 5 . . . . 16 LYS CD . 11435 1 129 . 1 1 16 16 LYS CE C 13 42.0 0.1 . 5 . . . . 16 LYS CE . 11435 1 130 . 1 1 16 16 LYS N N 15 123.9 0.1 . 1 . . . . 16 LYS N . 11435 1 131 . 1 1 17 17 LEU H H 1 8.43 0.01 . 1 . . . . 17 LEU H . 11435 1 132 . 1 1 17 17 LEU HA H 1 4.34 0.01 . 1 . . . . 17 LEU HA . 11435 1 133 . 1 1 17 17 LEU HB2 H 1 1.44 0.01 . 5 . . . . 17 LEU HB2 . 11435 1 134 . 1 1 17 17 LEU HG H 1 1.60 0.01 . 5 . . . . 17 LEU HG . 11435 1 135 . 1 1 17 17 LEU HD11 H 1 0.86 0.01 . 5 . . . . 17 LEU MD1 . 11435 1 136 . 1 1 17 17 LEU HD12 H 1 0.86 0.01 . 5 . . . . 17 LEU MD1 . 11435 1 137 . 1 1 17 17 LEU HD13 H 1 0.86 0.01 . 5 . . . . 17 LEU MD1 . 11435 1 138 . 1 1 17 17 LEU HD21 H 1 0.92 0.01 . 5 . . . . 17 LEU MD2 . 11435 1 139 . 1 1 17 17 LEU HD22 H 1 0.92 0.01 . 5 . . . . 17 LEU MD2 . 11435 1 140 . 1 1 17 17 LEU HD23 H 1 0.92 0.01 . 5 . . . . 17 LEU MD2 . 11435 1 141 . 1 1 17 17 LEU CA C 13 55.1 0.1 . 1 . . . . 17 LEU CA . 11435 1 142 . 1 1 17 17 LEU CB C 13 42.3 0.1 . 1 . . . . 17 LEU CB . 11435 1 143 . 1 1 17 17 LEU CG C 13 26.9 0.1 . 1 . . . . 17 LEU CG . 11435 1 144 . 1 1 17 17 LEU CD1 C 13 23.6 0.1 . 5 . . . . 17 LEU CD1 . 11435 1 145 . 1 1 17 17 LEU CD2 C 13 24.8 0.1 . 5 . . . . 17 LEU CD2 . 11435 1 146 . 1 1 17 17 LEU N N 15 124.6 0.1 . 1 . . . . 17 LEU N . 11435 1 147 . 1 1 18 18 VAL H H 1 8.16 0.01 . 1 . . . . 18 VAL H . 11435 1 148 . 1 1 18 18 VAL HA H 1 4.04 0.01 . 1 . . . . 18 VAL HA . 11435 1 149 . 1 1 18 18 VAL HB H 1 1.90 0.01 . 1 . . . . 18 VAL HB . 11435 1 150 . 1 1 18 18 VAL HG11 H 1 0.75 0.01 . 2 . . . . 18 VAL MG1 . 11435 1 151 . 1 1 18 18 VAL HG12 H 1 0.75 0.01 . 2 . . . . 18 VAL MG1 . 11435 1 152 . 1 1 18 18 VAL HG13 H 1 0.75 0.01 . 2 . . . . 18 VAL MG1 . 11435 1 153 . 1 1 18 18 VAL HG21 H 1 0.84 0.01 . 2 . . . . 18 VAL MG2 . 11435 1 154 . 1 1 18 18 VAL HG22 H 1 0.84 0.01 . 2 . . . . 18 VAL MG2 . 11435 1 155 . 1 1 18 18 VAL HG23 H 1 0.84 0.01 . 2 . . . . 18 VAL MG2 . 11435 1 156 . 1 1 18 18 VAL CA C 13 62.0 0.1 . 1 . . . . 18 VAL CA . 11435 1 157 . 1 1 18 18 VAL CB C 13 33.1 0.1 . 1 . . . . 18 VAL CB . 11435 1 158 . 1 1 18 18 VAL CG1 C 13 21.2 0.1 . 2 . . . . 18 VAL CG1 . 11435 1 159 . 1 1 18 18 VAL CG2 C 13 20.6 0.1 . 2 . . . . 18 VAL CG2 . 11435 1 160 . 1 1 18 18 VAL N N 15 122.1 0.1 . 1 . . . . 18 VAL N . 11435 1 161 . 1 1 19 19 PHE H H 1 8.42 0.01 . 1 . . . . 19 PHE H . 11435 1 162 . 1 1 19 19 PHE HA H 1 4.60 0.01 . 1 . . . . 19 PHE HA . 11435 1 163 . 1 1 19 19 PHE HB2 H 1 2.92 0.01 . 5 . . . . 19 PHE HB2 . 11435 1 164 . 1 1 19 19 PHE HB3 H 1 3.07 0.01 . 5 . . . . 19 PHE HB3 . 11435 1 165 . 1 1 19 19 PHE CA C 13 57.5 0.1 . 1 . . . . 19 PHE CA . 11435 1 166 . 1 1 19 19 PHE CB C 13 40.2 0.1 . 1 . . . . 19 PHE CB . 11435 1 167 . 1 1 19 19 PHE N N 15 125.0 0.1 . 1 . . . . 19 PHE N . 11435 1 168 . 1 1 20 20 PHE H H 1 8.36 0.01 . 1 . . . . 20 PHE H . 11435 1 169 . 1 1 20 20 PHE HA H 1 4.58 0.01 . 1 . . . . 20 PHE HA . 11435 1 170 . 1 1 20 20 PHE HB2 H 1 2.92 0.01 . 5 . . . . 20 PHE HB2 . 11435 1 171 . 1 1 20 20 PHE HB3 H 1 3.07 0.01 . 5 . . . . 20 PHE HB3 . 11435 1 172 . 1 1 20 20 PHE CA C 13 57.4 0.1 . 1 . . . . 20 PHE CA . 11435 1 173 . 1 1 20 20 PHE CB C 13 40.1 0.1 . 1 . . . . 20 PHE CB . 11435 1 174 . 1 1 20 20 PHE N N 15 123.5 0.1 . 1 . . . . 20 PHE N . 11435 1 175 . 1 1 21 21 ALA H H 1 8.38 0.01 . 1 . . . . 21 ALA H . 11435 1 176 . 1 1 21 21 ALA HA H 1 4.23 0.01 . 1 . . . . 21 ALA HA . 11435 1 177 . 1 1 21 21 ALA HB1 H 1 1.37 0.01 . 1 . . . . 21 ALA MB . 11435 1 178 . 1 1 21 21 ALA HB2 H 1 1.37 0.01 . 1 . . . . 21 ALA MB . 11435 1 179 . 1 1 21 21 ALA HB3 H 1 1.37 0.01 . 1 . . . . 21 ALA MB . 11435 1 180 . 1 1 21 21 ALA CA C 13 52.4 0.1 . 1 . . . . 21 ALA CA . 11435 1 181 . 1 1 21 21 ALA CB C 13 19.4 0.1 . 1 . . . . 21 ALA CB . 11435 1 182 . 1 1 21 21 ALA N N 15 126.7 0.1 . 1 . . . . 21 ALA N . 11435 1 183 . 1 1 22 22 GLU H H 1 8.50 0.01 . 1 . . . . 22 GLU H . 11435 1 184 . 1 1 22 22 GLU HA H 1 4.21 0.01 . 1 . . . . 22 GLU HA . 11435 1 185 . 1 1 22 22 GLU HB2 H 1 1.92 0.01 . 5 . . . . 22 GLU HB2 . 11435 1 186 . 1 1 22 22 GLU HB3 H 1 2.04 0.01 . 5 . . . . 22 GLU HB3 . 11435 1 187 . 1 1 22 22 GLU HG2 H 1 2.14 0.01 . 5 . . . . 22 GLU HG2 . 11435 1 188 . 1 1 22 22 GLU HG3 H 1 2.22 0.01 . 5 . . . . 22 GLU HG3 . 11435 1 189 . 1 1 22 22 GLU CA C 13 56.6 0.1 . 1 . . . . 22 GLU CA . 11435 1 190 . 1 1 22 22 GLU CB C 13 30.3 0.1 . 1 . . . . 22 GLU CB . 11435 1 191 . 1 1 22 22 GLU CG C 13 36.2 0.1 . 5 . . . . 22 GLU CG . 11435 1 192 . 1 1 22 22 GLU N N 15 120.4 0.1 . 1 . . . . 22 GLU N . 11435 1 193 . 1 1 23 23 ASP H H 1 8.56 0.01 . 1 . . . . 23 ASP H . 11435 1 194 . 1 1 23 23 ASP HA H 1 4.66 0.01 . 1 . . . . 23 ASP HA . 11435 1 195 . 1 1 23 23 ASP HB2 H 1 2.70 0.01 . 5 . . . . 23 ASP HB2 . 11435 1 196 . 1 1 23 23 ASP CA C 13 54.2 0.1 . 1 . . . . 23 ASP CA . 11435 1 197 . 1 1 23 23 ASP CB C 13 41.1 0.1 . 1 . . . . 23 ASP CB . 11435 1 198 . 1 1 23 23 ASP N N 15 122.2 0.1 . 1 . . . . 23 ASP N . 11435 1 199 . 1 1 24 24 VAL H H 1 8.30 0.01 . 1 . . . . 24 VAL H . 11435 1 200 . 1 1 24 24 VAL HA H 1 4.15 0.01 . 1 . . . . 24 VAL HA . 11435 1 201 . 1 1 24 24 VAL HB H 1 2.19 0.01 . 1 . . . . 24 VAL HB . 11435 1 202 . 1 1 24 24 VAL HG11 H 1 0.95 0.01 . 5 . . . . 24 VAL MG1 . 11435 1 203 . 1 1 24 24 VAL HG12 H 1 0.95 0.01 . 5 . . . . 24 VAL MG1 . 11435 1 204 . 1 1 24 24 VAL HG13 H 1 0.95 0.01 . 5 . . . . 24 VAL MG1 . 11435 1 205 . 1 1 24 24 VAL CA C 13 62.8 0.1 . 1 . . . . 24 VAL CA . 11435 1 206 . 1 1 24 24 VAL CB C 13 32.3 0.1 . 1 . . . . 24 VAL CB . 11435 1 207 . 1 1 24 24 VAL CG1 C 13 20.8 0.1 . 5 . . . . 24 VAL CG1 . 11435 1 208 . 1 1 24 24 VAL N N 15 121.1 0.1 . 1 . . . . 24 VAL N . 11435 1 209 . 1 1 25 25 GLY H H 1 8.68 0.01 . 1 . . . . 25 GLY H . 11435 1 210 . 1 1 25 25 GLY HA2 H 1 3.99 0.01 . 2 . . . . 25 GLY HA2 . 11435 1 211 . 1 1 25 25 GLY CA C 13 45.5 0.1 . 1 . . . . 25 GLY CA . 11435 1 212 . 1 1 25 25 GLY N N 15 112.3 0.1 . 1 . . . . 25 GLY N . 11435 1 213 . 1 1 26 26 SER H H 1 8.30 0.01 . 1 . . . . 26 SER H . 11435 1 214 . 1 1 26 26 SER HA H 1 4.43 0.01 . 1 . . . . 26 SER HA . 11435 1 215 . 1 1 26 26 SER HB2 H 1 3.90 0.01 . 5 . . . . 26 SER HB2 . 11435 1 216 . 1 1 26 26 SER CA C 13 58.6 0.1 . 1 . . . . 26 SER CA . 11435 1 217 . 1 1 26 26 SER CB C 13 63.7 0.1 . 1 . . . . 26 SER CB . 11435 1 218 . 1 1 26 26 SER N N 15 116.0 0.1 . 1 . . . . 26 SER N . 11435 1 219 . 1 1 27 27 ASN H H 1 8.62 0.01 . 1 . . . . 27 ASN H . 11435 1 220 . 1 1 27 27 ASN HA H 1 4.75 0.01 . 1 . . . . 27 ASN HA . 11435 1 221 . 1 1 27 27 ASN HB2 H 1 2.81 0.01 . 2 . . . . 27 ASN HB2 . 11435 1 222 . 1 1 27 27 ASN HB3 H 1 2.87 0.01 . 2 . . . . 27 ASN HB3 . 11435 1 223 . 1 1 27 27 ASN CA C 13 53.3 0.1 . 1 . . . . 27 ASN CA . 11435 1 224 . 1 1 27 27 ASN CB C 13 38.5 0.1 . 1 . . . . 27 ASN CB . 11435 1 225 . 1 1 27 27 ASN N N 15 121.0 0.1 . 1 . . . . 27 ASN N . 11435 1 226 . 1 1 28 28 LYS H H 1 8.49 0.01 . 1 . . . . 28 LYS H . 11435 1 227 . 1 1 28 28 LYS HA H 1 4.28 0.01 . 1 . . . . 28 LYS HA . 11435 1 228 . 1 1 28 28 LYS HB2 H 1 1.89 0.01 . 2 . . . . 28 LYS HB2 . 11435 1 229 . 1 1 28 28 LYS HG2 H 1 1.40 0.01 . 5 . . . . 28 LYS HG2 . 11435 1 230 . 1 1 28 28 LYS HG3 H 1 1.46 0.01 . 5 . . . . 28 LYS HG3 . 11435 1 231 . 1 1 28 28 LYS HD2 H 1 1.68 0.01 . 5 . . . . 28 LYS HD2 . 11435 1 232 . 1 1 28 28 LYS HD3 H 1 1.78 0.01 . 5 . . . . 28 LYS HD3 . 11435 1 233 . 1 1 28 28 LYS HE2 H 1 2.98 0.01 . 5 . . . . 28 LYS HE2 . 11435 1 234 . 1 1 28 28 LYS CA C 13 56.8 0.1 . 1 . . . . 28 LYS CA . 11435 1 235 . 1 1 28 28 LYS CB C 13 32.5 0.1 . 1 . . . . 28 LYS CB . 11435 1 236 . 1 1 28 28 LYS CG C 13 24.8 0.1 . 5 . . . . 28 LYS CG . 11435 1 237 . 1 1 28 28 LYS CD C 13 32.8 0.1 . 5 . . . . 28 LYS CD . 11435 1 238 . 1 1 28 28 LYS CE C 13 42.0 0.1 . 5 . . . . 28 LYS CE . 11435 1 239 . 1 1 28 28 LYS N N 15 122.2 0.1 . 1 . . . . 28 LYS N . 11435 1 240 . 1 1 29 29 GLY H H 1 8.56 0.01 . 1 . . . . 29 GLY H . 11435 1 241 . 1 1 29 29 GLY HA2 H 1 3.94 0.01 . 2 . . . . 29 GLY HA2 . 11435 1 242 . 1 1 29 29 GLY CA C 13 45.2 0.1 . 1 . . . . 29 GLY CA . 11435 1 243 . 1 1 29 29 GLY N N 15 110.0 0.1 . 1 . . . . 29 GLY N . 11435 1 244 . 1 1 30 30 ALA H H 1 8.16 0.01 . 1 . . . . 30 ALA H . 11435 1 245 . 1 1 30 30 ALA HA H 1 4.32 0.01 . 1 . . . . 30 ALA HA . 11435 1 246 . 1 1 30 30 ALA HB1 H 1 1.36 0.01 . 1 . . . . 30 ALA MB . 11435 1 247 . 1 1 30 30 ALA HB2 H 1 1.36 0.01 . 1 . . . . 30 ALA MB . 11435 1 248 . 1 1 30 30 ALA HB3 H 1 1.36 0.01 . 1 . . . . 30 ALA MB . 11435 1 249 . 1 1 30 30 ALA CA C 13 52.5 0.1 . 1 . . . . 30 ALA CA . 11435 1 250 . 1 1 30 30 ALA CB C 13 19.3 0.1 . 1 . . . . 30 ALA CB . 11435 1 251 . 1 1 30 30 ALA N N 15 124.0 0.1 . 1 . . . . 30 ALA N . 11435 1 252 . 1 1 31 31 ILE H H 1 8.33 0.01 . 1 . . . . 31 ILE H . 11435 1 253 . 1 1 31 31 ILE HA H 1 4.16 0.01 . 1 . . . . 31 ILE HA . 11435 1 254 . 1 1 31 31 ILE HB H 1 1.86 0.01 . 5 . . . . 31 ILE HB . 11435 1 255 . 1 1 31 31 ILE HG12 H 1 1.20 0.01 . 5 . . . . 31 ILE HG12 . 11435 1 256 . 1 1 31 31 ILE HG13 H 1 1.51 0.01 . 5 . . . . 31 ILE HG13 . 11435 1 257 . 1 1 31 31 ILE HG21 H 1 0.92 0.01 . 5 . . . . 31 ILE MG . 11435 1 258 . 1 1 31 31 ILE HG22 H 1 0.92 0.01 . 5 . . . . 31 ILE MG . 11435 1 259 . 1 1 31 31 ILE HG23 H 1 0.92 0.01 . 5 . . . . 31 ILE MG . 11435 1 260 . 1 1 31 31 ILE HD11 H 1 0.87 0.01 . 5 . . . . 31 ILE MD . 11435 1 261 . 1 1 31 31 ILE HD12 H 1 0.87 0.01 . 5 . . . . 31 ILE MD . 11435 1 262 . 1 1 31 31 ILE HD13 H 1 0.87 0.01 . 5 . . . . 31 ILE MD . 11435 1 263 . 1 1 31 31 ILE CA C 13 61.1 0.1 . 1 . . . . 31 ILE CA . 11435 1 264 . 1 1 31 31 ILE CB C 13 38.4 0.1 . 1 . . . . 31 ILE CB . 11435 1 265 . 1 1 31 31 ILE CG1 C 13 27.3 0.1 . 5 . . . . 31 ILE CG1 . 11435 1 266 . 1 1 31 31 ILE CG2 C 13 17.4 0.1 . 5 . . . . 31 ILE CG2 . 11435 1 267 . 1 1 31 31 ILE CD1 C 13 12.6 0.1 . 5 . . . . 31 ILE CD1 . 11435 1 268 . 1 1 31 31 ILE N N 15 121.3 0.1 . 1 . . . . 31 ILE N . 11435 1 269 . 1 1 32 32 ILE H H 1 8.43 0.01 . 1 . . . . 32 ILE H . 11435 1 270 . 1 1 32 32 ILE HA H 1 4.17 0.01 . 1 . . . . 32 ILE HA . 11435 1 271 . 1 1 32 32 ILE HB H 1 1.86 0.01 . 5 . . . . 32 ILE HB . 11435 1 272 . 1 1 32 32 ILE HG12 H 1 1.20 0.01 . 5 . . . . 32 ILE HG12 . 11435 1 273 . 1 1 32 32 ILE HG13 H 1 1.51 0.01 . 5 . . . . 32 ILE HG13 . 11435 1 274 . 1 1 32 32 ILE HG21 H 1 0.92 0.01 . 5 . . . . 32 ILE MG . 11435 1 275 . 1 1 32 32 ILE HG22 H 1 0.92 0.01 . 5 . . . . 32 ILE MG . 11435 1 276 . 1 1 32 32 ILE HG23 H 1 0.92 0.01 . 5 . . . . 32 ILE MG . 11435 1 277 . 1 1 32 32 ILE HD11 H 1 0.87 0.01 . 5 . . . . 32 ILE MD . 11435 1 278 . 1 1 32 32 ILE HD12 H 1 0.87 0.01 . 5 . . . . 32 ILE MD . 11435 1 279 . 1 1 32 32 ILE HD13 H 1 0.87 0.01 . 5 . . . . 32 ILE MD . 11435 1 280 . 1 1 32 32 ILE CA C 13 61.2 0.1 . 1 . . . . 32 ILE CA . 11435 1 281 . 1 1 32 32 ILE CB C 13 38.4 0.1 . 1 . . . . 32 ILE CB . 11435 1 282 . 1 1 32 32 ILE CG1 C 13 27.3 0.1 . 5 . . . . 32 ILE CG1 . 11435 1 283 . 1 1 32 32 ILE CG2 C 13 17.4 0.1 . 5 . . . . 32 ILE CG2 . 11435 1 284 . 1 1 32 32 ILE CD1 C 13 12.6 0.1 . 5 . . . . 32 ILE CD1 . 11435 1 285 . 1 1 32 32 ILE N N 15 126.8 0.1 . 1 . . . . 32 ILE N . 11435 1 286 . 1 1 33 33 GLY H H 1 8.62 0.01 . 1 . . . . 33 GLY H . 11435 1 287 . 1 1 33 33 GLY HA2 H 1 3.95 0.01 . 2 . . . . 33 GLY HA2 . 11435 1 288 . 1 1 33 33 GLY CA C 13 45.2 0.1 . 1 . . . . 33 GLY CA . 11435 1 289 . 1 1 33 33 GLY N N 15 113.6 0.1 . 1 . . . . 33 GLY N . 11435 1 290 . 1 1 34 34 LEU H H 1 8.19 0.01 . 1 . . . . 34 LEU H . 11435 1 291 . 1 1 34 34 LEU HA H 1 4.35 0.01 . 1 . . . . 34 LEU HA . 11435 1 292 . 1 1 34 34 LEU HB2 H 1 1.44 0.01 . 5 . . . . 34 LEU HB2 . 11435 1 293 . 1 1 34 34 LEU HG H 1 1.60 0.01 . 5 . . . . 34 LEU HG . 11435 1 294 . 1 1 34 34 LEU HD11 H 1 0.86 0.01 . 5 . . . . 34 LEU MD1 . 11435 1 295 . 1 1 34 34 LEU HD12 H 1 0.86 0.01 . 5 . . . . 34 LEU MD1 . 11435 1 296 . 1 1 34 34 LEU HD13 H 1 0.86 0.01 . 5 . . . . 34 LEU MD1 . 11435 1 297 . 1 1 34 34 LEU HD21 H 1 0.92 0.01 . 5 . . . . 34 LEU MD2 . 11435 1 298 . 1 1 34 34 LEU HD22 H 1 0.92 0.01 . 5 . . . . 34 LEU MD2 . 11435 1 299 . 1 1 34 34 LEU HD23 H 1 0.92 0.01 . 5 . . . . 34 LEU MD2 . 11435 1 300 . 1 1 34 34 LEU CA C 13 55.2 0.1 . 1 . . . . 34 LEU CA . 11435 1 301 . 1 1 34 34 LEU CB C 13 42.5 0.1 . 1 . . . . 34 LEU CB . 11435 1 302 . 1 1 34 34 LEU CG C 13 26.9 0.1 . 1 . . . . 34 LEU CG . 11435 1 303 . 1 1 34 34 LEU CD1 C 13 23.6 0.1 . 5 . . . . 34 LEU CD1 . 11435 1 304 . 1 1 34 34 LEU CD2 C 13 24.8 0.1 . 5 . . . . 34 LEU CD2 . 11435 1 305 . 1 1 34 34 LEU N N 15 122.1 0.1 . 1 . . . . 34 LEU N . 11435 1 306 . 1 1 35 35 MET H H 1 8.59 0.01 . 1 . . . . 35 MET H . 11435 1 307 . 1 1 35 35 MET HA H 1 4.54 0.01 . 1 . . . . 35 MET HA . 11435 1 308 . 1 1 35 35 MET HB2 H 1 2.03 0.01 . 2 . . . . 35 MET HB2 . 11435 1 309 . 1 1 35 35 MET HG2 H 1 2.51 0.01 . 2 . . . . 35 MET HG2 . 11435 1 310 . 1 1 35 35 MET HG3 H 1 2.59 0.01 . 2 . . . . 35 MET HG3 . 11435 1 311 . 1 1 35 35 MET CA C 13 55.3 0.1 . 1 . . . . 35 MET CA . 11435 1 312 . 1 1 35 35 MET CB C 13 32.6 0.1 . 1 . . . . 35 MET CB . 11435 1 313 . 1 1 35 35 MET CG C 13 31.9 0.1 . 1 . . . . 35 MET CG . 11435 1 314 . 1 1 35 35 MET N N 15 122.4 0.1 . 1 . . . . 35 MET N . 11435 1 315 . 1 1 36 36 VAL H H 1 8.39 0.01 . 1 . . . . 36 VAL H . 11435 1 316 . 1 1 36 36 VAL HA H 1 4.13 0.01 . 1 . . . . 36 VAL HA . 11435 1 317 . 1 1 36 36 VAL HB H 1 2.08 0.01 . 1 . . . . 36 VAL HB . 11435 1 318 . 1 1 36 36 VAL HG11 H 1 0.95 0.01 . 5 . . . . 36 VAL MG1 . 11435 1 319 . 1 1 36 36 VAL HG12 H 1 0.95 0.01 . 5 . . . . 36 VAL MG1 . 11435 1 320 . 1 1 36 36 VAL HG13 H 1 0.95 0.01 . 5 . . . . 36 VAL MG1 . 11435 1 321 . 1 1 36 36 VAL CA C 13 62.7 0.1 . 1 . . . . 36 VAL CA . 11435 1 322 . 1 1 36 36 VAL CB C 13 32.7 0.1 . 1 . . . . 36 VAL CB . 11435 1 323 . 1 1 36 36 VAL CG1 C 13 20.8 0.1 . 5 . . . . 36 VAL CG1 . 11435 1 324 . 1 1 36 36 VAL N N 15 123.0 0.1 . 1 . . . . 36 VAL N . 11435 1 325 . 1 1 37 37 GLY H H 1 8.75 0.01 . 1 . . . . 37 GLY H . 11435 1 326 . 1 1 37 37 GLY HA2 H 1 4.00 0.01 . 2 . . . . 37 GLY HA2 . 11435 1 327 . 1 1 37 37 GLY CA C 13 45.2 0.1 . 1 . . . . 37 GLY CA . 11435 1 328 . 1 1 37 37 GLY N N 15 113.7 0.1 . 1 . . . . 37 GLY N . 11435 1 329 . 1 1 38 38 GLY H H 1 8.39 0.01 . 1 . . . . 38 GLY H . 11435 1 330 . 1 1 38 38 GLY HA2 H 1 3.98 0.01 . 2 . . . . 38 GLY HA2 . 11435 1 331 . 1 1 38 38 GLY CA C 13 45.1 0.1 . 1 . . . . 38 GLY CA . 11435 1 332 . 1 1 38 38 GLY N N 15 109.1 0.1 . 1 . . . . 38 GLY N . 11435 1 333 . 1 1 39 39 VAL H H 1 8.22 0.01 . 1 . . . . 39 VAL H . 11435 1 334 . 1 1 39 39 VAL HA H 1 4.19 0.01 . 1 . . . . 39 VAL HA . 11435 1 335 . 1 1 39 39 VAL HB H 1 2.09 0.01 . 1 . . . . 39 VAL HB . 11435 1 336 . 1 1 39 39 VAL HG11 H 1 0.94 0.01 . 2 . . . . 39 VAL MG1 . 11435 1 337 . 1 1 39 39 VAL HG12 H 1 0.94 0.01 . 2 . . . . 39 VAL MG1 . 11435 1 338 . 1 1 39 39 VAL HG13 H 1 0.94 0.01 . 2 . . . . 39 VAL MG1 . 11435 1 339 . 1 1 39 39 VAL CA C 13 62.5 0.1 . 1 . . . . 39 VAL CA . 11435 1 340 . 1 1 39 39 VAL CB C 13 32.9 0.1 . 1 . . . . 39 VAL CB . 11435 1 341 . 1 1 39 39 VAL CG1 C 13 20.9 0.1 . 2 . . . . 39 VAL CG1 . 11435 1 342 . 1 1 39 39 VAL N N 15 120.3 0.1 . 1 . . . . 39 VAL N . 11435 1 343 . 1 1 40 40 VAL H H 1 7.97 0.01 . 1 . . . . 40 VAL H . 11435 1 344 . 1 1 40 40 VAL HB H 1 2.05 0.01 . 1 . . . . 40 VAL HB . 11435 1 345 . 1 1 40 40 VAL HG11 H 1 0.90 0.01 . 2 . . . . 40 VAL MG1 . 11435 1 346 . 1 1 40 40 VAL HG12 H 1 0.90 0.01 . 2 . . . . 40 VAL MG1 . 11435 1 347 . 1 1 40 40 VAL HG13 H 1 0.90 0.01 . 2 . . . . 40 VAL MG1 . 11435 1 348 . 1 1 40 40 VAL CA C 13 63.8 0.1 . 1 . . . . 40 VAL CA . 11435 1 349 . 1 1 40 40 VAL CB C 13 33.2 0.1 . 1 . . . . 40 VAL CB . 11435 1 350 . 1 1 40 40 VAL CG1 C 13 21.6 0.1 . 2 . . . . 40 VAL CG1 . 11435 1 351 . 1 1 40 40 VAL CG2 C 13 20.2 0.1 . 2 . . . . 40 VAL CG2 . 11435 1 352 . 1 1 40 40 VAL N N 15 128.9 0.1 . 1 . . . . 40 VAL N . 11435 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 16 11435 1 1 17 11435 1 1 73 11435 1 1 74 11435 1 1 185 11435 1 1 186 11435 1 2 18 11435 1 2 19 11435 1 2 75 11435 1 2 76 11435 1 2 187 11435 1 2 188 11435 1 3 22 11435 1 3 79 11435 1 3 191 11435 1 4 43 11435 1 4 44 11435 1 4 103 11435 1 4 104 11435 1 5 50 11435 1 5 195 11435 1 6 56 11435 1 6 215 11435 1 7 120 11435 1 7 121 11435 1 7 229 11435 1 7 230 11435 1 8 122 11435 1 8 123 11435 1 8 231 11435 1 8 232 11435 1 9 124 11435 1 9 233 11435 1 10 127 11435 1 10 236 11435 1 11 128 11435 1 11 237 11435 1 12 129 11435 1 12 238 11435 1 13 133 11435 1 13 292 11435 1 14 134 11435 1 14 293 11435 1 15 135 11435 1 15 136 11435 1 15 137 11435 1 15 294 11435 1 15 295 11435 1 15 296 11435 1 16 138 11435 1 16 139 11435 1 16 140 11435 1 16 297 11435 1 16 298 11435 1 16 299 11435 1 17 144 11435 1 17 303 11435 1 18 145 11435 1 18 304 11435 1 19 163 11435 1 19 164 11435 1 19 170 11435 1 19 171 11435 1 21 202 11435 1 21 203 11435 1 21 204 11435 1 21 318 11435 1 21 319 11435 1 21 320 11435 1 22 207 11435 1 22 323 11435 1 23 254 11435 1 23 271 11435 1 24 255 11435 1 24 256 11435 1 24 272 11435 1 24 273 11435 1 25 257 11435 1 25 258 11435 1 25 259 11435 1 25 274 11435 1 25 275 11435 1 25 276 11435 1 26 260 11435 1 26 261 11435 1 26 262 11435 1 26 277 11435 1 26 278 11435 1 26 279 11435 1 27 265 11435 1 27 282 11435 1 28 266 11435 1 28 283 11435 1 29 267 11435 1 29 284 11435 1 stop_ save_