data_17764 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17764 _Entry.Title ; A partially folded structure of amyloid-beta(1 40) in an aqueous environment ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-07-06 _Entry.Accession_date 2011-07-06 _Entry.Last_release_date 2011-08-19 _Entry.Original_release_date 2011-08-19 _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 'NMR, 20 STRUCTURES' _Entry.Details 'Folding mechanism of Abeta in aqueous environment' _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 Subramanian Vivekanandan . . . 17764 2 Jeffrey Brender . R. . 17764 3 Shirley Lee . Y. . 17764 4 Ayyalusamy Ramamoorthy . . . 17764 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID . 'PSI, Protein Structure Initiative' 'not applicable' . 17764 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'Amyloid-beta structure' . 17764 'in an aqueous environment' . 17764 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17764 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 254 17764 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2011-08-19 2011-07-06 original author . 17764 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LFM 'BMRB Entry Tracking System' 17764 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17764 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 21726530 _Citation.Full_citation . _Citation.Title 'A partially folded structure of amyloid-beta(1-40) in an aqueous environment.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Biophys. Res. Commun.' _Citation.Journal_name_full 'Biochemical and biophysical research communications' _Citation.Journal_volume 411 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 312 _Citation.Page_last 316 _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 Subramanian Vivekanandan . . . 17764 1 2 Jeffrey Brender . R. . 17764 1 3 Shirley Lee . Y. . 17764 1 4 Ayyalusamy Ramamoorthy . . . 17764 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17764 _Assembly.ID 1 _Assembly.Name Abeta _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 Abeta 1 $Abeta A . yes native no no . . . 17764 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Abeta _Entity.Sf_category entity _Entity.Sf_framecode Abeta _Entity.Entry_ID 17764 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Abeta _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _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 man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 4335.893 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 17764 1 3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 4 no BMRB 17186 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 5 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 1 6 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 1 7 no BMRB 17795 . Abeta(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 8 no BMRB 17796 . Abeta40 . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 9 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 92.50 38 100.00 100.00 2.74e-16 . . . . 17764 1 10 no BMRB 18127 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 11 no BMRB 18128 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 12 no BMRB 18129 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 13 no BMRB 18131 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 14 no BMRB 19009 . beta-amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 15 no BMRB 19309 . amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 16 no BMRB 19393 . Abeta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 17764 1 17 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 1 18 no BMRB 25289 . amyloid_beta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 17764 1 19 no BMRB 25429 . entity . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 1 20 no BMRB 26508 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 1 21 no BMRB 26516 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 65.00 26 100.00 100.00 2.06e-08 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 100.00 40 97.50 100.00 5.11e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17764 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17764 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.50 100.00 1.74e-18 . . . . 17764 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 1.14e-18 . . . . 17764 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 1.43e-18 . . . . 17764 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17764 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17764 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 3.56e-19 . . . . 17764 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 17764 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 17764 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.00 97 100.00 100.00 2.36e-17 . . . . 17764 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17764 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 75.00 30 100.00 100.00 1.09e-11 . . . . 17764 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 9.13e-19 . . . . 17764 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 1.74e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 4.05e-19 . . . . 17764 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17764 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17764 1 77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17764 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 9.42e-19 . . . . 17764 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 4.07e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17764 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17764 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 1.65e-18 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 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 . . . . 17764 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17764 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 1 ASP . 17764 1 2 2 ALA . 17764 1 3 3 GLU . 17764 1 4 4 PHE . 17764 1 5 5 ARG . 17764 1 6 6 HIS . 17764 1 7 7 ASP . 17764 1 8 8 SER . 17764 1 9 9 GLY . 17764 1 10 10 TYR . 17764 1 11 11 GLU . 17764 1 12 12 VAL . 17764 1 13 13 HIS . 17764 1 14 14 HIS . 17764 1 15 15 GLN . 17764 1 16 16 LYS . 17764 1 17 17 LEU . 17764 1 18 18 VAL . 17764 1 19 19 PHE . 17764 1 20 20 PHE . 17764 1 21 21 ALA . 17764 1 22 22 GLU . 17764 1 23 23 ASP . 17764 1 24 24 VAL . 17764 1 25 25 GLY . 17764 1 26 26 SER . 17764 1 27 27 ASN . 17764 1 28 28 LYS . 17764 1 29 29 GLY . 17764 1 30 30 ALA . 17764 1 31 31 ILE . 17764 1 32 32 ILE . 17764 1 33 33 GLY . 17764 1 34 34 LEU . 17764 1 35 35 MET . 17764 1 36 36 VAL . 17764 1 37 37 GLY . 17764 1 38 38 GLY . 17764 1 39 39 VAL . 17764 1 40 40 VAL . 17764 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 17764 1 . ALA 2 2 17764 1 . GLU 3 3 17764 1 . PHE 4 4 17764 1 . ARG 5 5 17764 1 . HIS 6 6 17764 1 . ASP 7 7 17764 1 . SER 8 8 17764 1 . GLY 9 9 17764 1 . TYR 10 10 17764 1 . GLU 11 11 17764 1 . VAL 12 12 17764 1 . HIS 13 13 17764 1 . HIS 14 14 17764 1 . GLN 15 15 17764 1 . LYS 16 16 17764 1 . LEU 17 17 17764 1 . VAL 18 18 17764 1 . PHE 19 19 17764 1 . PHE 20 20 17764 1 . ALA 21 21 17764 1 . GLU 22 22 17764 1 . ASP 23 23 17764 1 . VAL 24 24 17764 1 . GLY 25 25 17764 1 . SER 26 26 17764 1 . ASN 27 27 17764 1 . LYS 28 28 17764 1 . GLY 29 29 17764 1 . ALA 30 30 17764 1 . ILE 31 31 17764 1 . ILE 32 32 17764 1 . GLY 33 33 17764 1 . LEU 34 34 17764 1 . MET 35 35 17764 1 . VAL 36 36 17764 1 . GLY 37 37 17764 1 . GLY 38 38 17764 1 . VAL 39 39 17764 1 . VAL 40 40 17764 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 17764 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Abeta . 9606 organism . 'Homo sapiens' humans . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 17764 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 17764 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Abeta . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . 'purchased from Anaspec' . . 17764 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17764 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '15C, 20 mM KPi, 50 mM NaCL, 77 uM Ab1-40' _Sample.Aggregate_sample_number . _Sample.Solvent_system '93% H2O/7% 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 'potassium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 17764 1 2 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 17764 1 3 Ab1-40 '[U-10% 13C; U-100% 15N]' . . 1 $Abeta . . 77 . . uM . . . . 17764 1 4 H2O 'natural abundance' . . . . . . 93 . . % . . . . 17764 1 5 D2O 'natural abundance' . . . . . . 7 . . % . . . . 17764 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 17764 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.07 . M 17764 1 pH 7.3 0.1 pH 17764 1 pressure 1 . atm 17764 1 temperature 288 . K 17764 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 17764 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 17764 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 17764 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 17764 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 17764 _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 . 900 . . . 17764 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 17764 _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-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17764 1 2 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17764 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 17764 _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 1.0 . . . . . . . . . 17764 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 17764 _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-1H TOCSY' . . . 17764 1 2 '2D 1H-1H NOESY' . . . 17764 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 4.035 0.002 . 1 . . . A 1 ASP HA . 17764 1 2 . 1 1 1 1 ASP HB2 H 1 2.540 0.002 . 2 . . . A 1 ASP HB2 . 17764 1 3 . 1 1 1 1 ASP HB3 H 1 2.668 0.000 . 2 . . . A 1 ASP HB3 . 17764 1 4 . 1 1 2 2 ALA H H 1 7.931 0.000 . 1 . . . A 2 ALA H . 17764 1 5 . 1 1 2 2 ALA HA H 1 4.140 0.003 . 1 . . . A 2 ALA HA . 17764 1 6 . 1 1 2 2 ALA HB1 H 1 1.203 0.003 . 1 . . . A 2 ALA HB1 . 17764 1 7 . 1 1 2 2 ALA HB2 H 1 1.203 0.003 . 1 . . . A 2 ALA HB2 . 17764 1 8 . 1 1 2 2 ALA HB3 H 1 1.203 0.003 . 1 . . . A 2 ALA HB3 . 17764 1 9 . 1 1 3 3 GLU H H 1 8.354 0.002 . 1 . . . A 3 GLU H . 17764 1 10 . 1 1 3 3 GLU HA H 1 4.019 0.003 . 1 . . . A 3 GLU HA . 17764 1 11 . 1 1 3 3 GLU HB2 H 1 1.769 0.000 . 2 . . . A 3 GLU HB2 . 17764 1 12 . 1 1 3 3 GLU HB3 H 1 1.719 0.000 . 2 . . . A 3 GLU HB3 . 17764 1 13 . 1 1 3 3 GLU HG2 H 1 2.058 0.000 . 2 . . . A 3 GLU HG2 . 17764 1 14 . 1 1 3 3 GLU HG3 H 1 1.965 0.002 . 2 . . . A 3 GLU HG3 . 17764 1 15 . 1 1 4 4 PHE H H 1 8.209 0.002 . 1 . . . A 4 PHE H . 17764 1 16 . 1 1 4 4 PHE HA H 1 4.403 0.003 . 1 . . . A 4 PHE HA . 17764 1 17 . 1 1 4 4 PHE HB2 H 1 2.851 0.002 . 2 . . . A 4 PHE HB2 . 17764 1 18 . 1 1 4 4 PHE HB3 H 1 2.851 0.002 . 2 . . . A 4 PHE HB3 . 17764 1 19 . 1 1 4 4 PHE HD1 H 1 7.099 0.002 . 2 . . . A 4 PHE HD1 . 17764 1 20 . 1 1 4 4 PHE HD2 H 1 7.099 0.002 . 2 . . . A 4 PHE HD2 . 17764 1 21 . 1 1 4 4 PHE HE1 H 1 7.012 0.002 . 2 . . . A 4 PHE HE1 . 17764 1 22 . 1 1 4 4 PHE HE2 H 1 7.012 0.002 . 2 . . . A 4 PHE HE2 . 17764 1 23 . 1 1 5 5 ARG H H 1 8.067 0.002 . 1 . . . A 5 ARG H . 17764 1 24 . 1 1 5 5 ARG HA H 1 4.095 0.003 . 1 . . . A 5 ARG HA . 17764 1 25 . 1 1 5 5 ARG HB2 H 1 1.328 0.005 . 2 . . . A 5 ARG HB2 . 17764 1 26 . 1 1 5 5 ARG HB3 H 1 1.328 0.005 . 2 . . . A 5 ARG HB3 . 17764 1 27 . 1 1 5 5 ARG HG2 H 1 1.576 0.002 . 2 . . . A 5 ARG HG2 . 17764 1 28 . 1 1 5 5 ARG HG3 H 1 1.469 0.002 . 2 . . . A 5 ARG HG3 . 17764 1 29 . 1 1 5 5 ARG HD2 H 1 2.965 0.004 . 2 . . . A 5 ARG HD2 . 17764 1 30 . 1 1 5 5 ARG HD3 H 1 2.965 0.004 . 2 . . . A 5 ARG HD3 . 17764 1 31 . 1 1 6 6 HIS HA H 1 4.396 0.004 . 1 . . . A 6 HIS HA . 17764 1 32 . 1 1 6 6 HIS HB2 H 1 2.973 0.003 . 2 . . . A 6 HIS HB2 . 17764 1 33 . 1 1 6 6 HIS HB3 H 1 2.903 0.003 . 2 . . . A 6 HIS HB3 . 17764 1 34 . 1 1 6 6 HIS HD1 H 1 6.645 0.000 . 1 . . . A 6 HIS HD1 . 17764 1 35 . 1 1 6 6 HIS HD2 H 1 6.923 0.001 . 1 . . . A 6 HIS HD2 . 17764 1 36 . 1 1 7 7 ASP H H 1 8.281 0.002 . 1 . . . A 7 ASP H . 17764 1 37 . 1 1 7 7 ASP HA H 1 4.463 0.004 . 1 . . . A 7 ASP HA . 17764 1 38 . 1 1 7 7 ASP HB2 H 1 2.516 0.001 . 2 . . . A 7 ASP HB2 . 17764 1 39 . 1 1 7 7 ASP HB3 H 1 2.516 0.001 . 2 . . . A 7 ASP HB3 . 17764 1 40 . 1 1 8 8 SER H H 1 8.333 0.003 . 1 . . . A 8 SER H . 17764 1 41 . 1 1 8 8 SER HA H 1 4.223 0.004 . 1 . . . A 8 SER HA . 17764 1 42 . 1 1 8 8 SER HB2 H 1 3.754 0.003 . 2 . . . A 8 SER HB2 . 17764 1 43 . 1 1 8 8 SER HB3 H 1 3.713 0.003 . 2 . . . A 8 SER HB3 . 17764 1 44 . 1 1 9 9 GLY H H 1 8.445 0.001 . 1 . . . A 9 GLY H . 17764 1 45 . 1 1 9 9 GLY HA2 H 1 3.782 0.005 . 2 . . . A 9 GLY HA2 . 17764 1 46 . 1 1 9 9 GLY HA3 H 1 3.721 0.003 . 2 . . . A 9 GLY HA3 . 17764 1 47 . 1 1 10 10 TYR H H 1 7.860 0.002 . 1 . . . A 10 TYR H . 17764 1 48 . 1 1 10 10 TYR HA H 1 4.344 0.004 . 1 . . . A 10 TYR HA . 17764 1 49 . 1 1 10 10 TYR HB2 H 1 2.862 0.002 . 2 . . . A 10 TYR HB2 . 17764 1 50 . 1 1 10 10 TYR HB3 H 1 2.791 0.002 . 2 . . . A 10 TYR HB3 . 17764 1 51 . 1 1 10 10 TYR HD1 H 1 6.893 0.001 . 3 . . . A 10 TYR HD1 . 17764 1 52 . 1 1 10 10 TYR HD2 H 1 6.893 0.001 . 3 . . . A 10 TYR HD2 . 17764 1 53 . 1 1 10 10 TYR HE1 H 1 6.612 0.001 . 3 . . . A 10 TYR HE1 . 17764 1 54 . 1 1 10 10 TYR HE2 H 1 6.612 0.001 . 3 . . . A 10 TYR HE2 . 17764 1 55 . 1 1 11 11 GLU H H 1 8.283 0.001 . 1 . . . A 11 GLU H . 17764 1 56 . 1 1 11 11 GLU HA H 1 4.037 0.004 . 1 . . . A 11 GLU HA . 17764 1 57 . 1 1 11 11 GLU HB2 H 1 1.697 0.005 . 2 . . . A 11 GLU HB2 . 17764 1 58 . 1 1 11 11 GLU HB3 H 1 1.773 0.002 . 2 . . . A 11 GLU HB3 . 17764 1 59 . 1 1 11 11 GLU HG2 H 1 2.046 0.002 . 2 . . . A 11 GLU HG2 . 17764 1 60 . 1 1 11 11 GLU HG3 H 1 1.995 0.001 . 2 . . . A 11 GLU HG3 . 17764 1 61 . 1 1 12 12 VAL H H 1 7.970 0.001 . 1 . . . A 12 VAL H . 17764 1 62 . 1 1 12 12 VAL HA H 1 3.775 0.002 . 1 . . . A 12 VAL HA . 17764 1 63 . 1 1 12 12 VAL HB H 1 1.774 0.002 . 1 . . . A 12 VAL HB . 17764 1 64 . 1 1 12 12 VAL HG11 H 1 0.707 0.002 . 2 . . . A 12 VAL HG11 . 17764 1 65 . 1 1 12 12 VAL HG12 H 1 0.707 0.002 . 2 . . . A 12 VAL HG12 . 17764 1 66 . 1 1 12 12 VAL HG13 H 1 0.707 0.002 . 2 . . . A 12 VAL HG13 . 17764 1 67 . 1 1 12 12 VAL HG21 H 1 0.611 0.002 . 2 . . . A 12 VAL HG21 . 17764 1 68 . 1 1 12 12 VAL HG22 H 1 0.611 0.002 . 2 . . . A 12 VAL HG22 . 17764 1 69 . 1 1 12 12 VAL HG23 H 1 0.611 0.002 . 2 . . . A 12 VAL HG23 . 17764 1 70 . 1 1 13 13 HIS H H 1 7.760 0.002 . 1 . . . A 13 HIS H . 17764 1 71 . 1 1 13 13 HIS HA H 1 4.457 0.002 . 1 . . . A 13 HIS HA . 17764 1 72 . 1 1 13 13 HIS HB2 H 1 2.920 0.002 . 2 . . . A 13 HIS HB2 . 17764 1 73 . 1 1 13 13 HIS HB3 H 1 2.866 0.003 . 2 . . . A 13 HIS HB3 . 17764 1 74 . 1 1 13 13 HIS HD1 H 1 6.610 0.000 . 1 . . . A 13 HIS HD1 . 17764 1 75 . 1 1 13 13 HIS HD2 H 1 6.849 0.001 . 1 . . . A 13 HIS HD2 . 17764 1 76 . 1 1 14 14 HIS H H 1 6.860 0.003 . 1 . . . A 14 HIS H . 17764 1 77 . 1 1 14 14 HIS HA H 1 4.396 0.003 . 1 . . . A 14 HIS HA . 17764 1 78 . 1 1 14 14 HIS HB2 H 1 2.964 0.002 . 2 . . . A 14 HIS HB2 . 17764 1 79 . 1 1 14 14 HIS HB3 H 1 2.861 0.002 . 2 . . . A 14 HIS HB3 . 17764 1 80 . 1 1 15 15 GLN H H 1 8.336 0.002 . 1 . . . A 15 GLN H . 17764 1 81 . 1 1 15 15 GLN HA H 1 4.110 0.003 . 1 . . . A 15 GLN HA . 17764 1 82 . 1 1 15 15 GLN HB2 H 1 1.905 0.002 . 2 . . . A 15 GLN HB2 . 17764 1 83 . 1 1 15 15 GLN HB3 H 1 1.819 0.002 . 2 . . . A 15 GLN HB3 . 17764 1 84 . 1 1 15 15 GLN HG2 H 1 2.173 0.002 . 2 . . . A 15 GLN HG2 . 17764 1 85 . 1 1 15 15 GLN HG3 H 1 2.173 0.002 . 2 . . . A 15 GLN HG3 . 17764 1 86 . 1 1 15 15 GLN HE21 H 1 7.475 0.000 . 2 . . . A 15 GLN HE21 . 17764 1 87 . 1 1 15 15 GLN HE22 H 1 6.795 0.001 . 2 . . . A 15 GLN HE22 . 17764 1 88 . 1 1 16 16 LYS H H 1 8.317 0.002 . 1 . . . A 16 LYS H . 17764 1 89 . 1 1 16 16 LYS HA H 1 4.116 0.003 . 1 . . . A 16 LYS HA . 17764 1 90 . 1 1 16 16 LYS HB2 H 1 1.644 0.005 . 2 . . . A 16 LYS HB2 . 17764 1 91 . 1 1 16 16 LYS HB3 H 1 1.584 0.002 . 2 . . . A 16 LYS HB3 . 17764 1 92 . 1 1 16 16 LYS HG2 H 1 1.284 0.003 . 2 . . . A 16 LYS HG2 . 17764 1 93 . 1 1 16 16 LYS HG3 H 1 1.214 0.005 . 2 . . . A 16 LYS HG3 . 17764 1 94 . 1 1 16 16 LYS HD2 H 1 1.514 0.004 . 2 . . . A 16 LYS HD2 . 17764 1 95 . 1 1 16 16 LYS HD3 H 1 1.514 0.004 . 2 . . . A 16 LYS HD3 . 17764 1 96 . 1 1 16 16 LYS HE2 H 1 2.813 0.002 . 2 . . . A 16 LYS HE2 . 17764 1 97 . 1 1 16 16 LYS HE3 H 1 2.813 0.002 . 2 . . . A 16 LYS HE3 . 17764 1 98 . 1 1 17 17 LEU H H 1 8.169 0.003 . 1 . . . A 17 LEU H . 17764 1 99 . 1 1 17 17 LEU HA H 1 4.169 0.003 . 1 . . . A 17 LEU HA . 17764 1 100 . 1 1 17 17 LEU HB2 H 1 1.443 0.002 . 2 . . . A 17 LEU HB2 . 17764 1 101 . 1 1 17 17 LEU HB3 H 1 1.398 0.002 . 2 . . . A 17 LEU HB3 . 17764 1 102 . 1 1 17 17 LEU HG H 1 1.281 0.004 . 1 . . . A 17 LEU HG . 17764 1 103 . 1 1 17 17 LEU HD11 H 1 0.682 0.003 . 2 . . . A 17 LEU HD11 . 17764 1 104 . 1 1 17 17 LEU HD12 H 1 0.682 0.003 . 2 . . . A 17 LEU HD12 . 17764 1 105 . 1 1 17 17 LEU HD13 H 1 0.682 0.003 . 2 . . . A 17 LEU HD13 . 17764 1 106 . 1 1 17 17 LEU HD21 H 1 0.749 0.003 . 2 . . . A 17 LEU HD21 . 17764 1 107 . 1 1 17 17 LEU HD22 H 1 0.749 0.003 . 2 . . . A 17 LEU HD22 . 17764 1 108 . 1 1 17 17 LEU HD23 H 1 0.749 0.003 . 2 . . . A 17 LEU HD23 . 17764 1 109 . 1 1 18 18 VAL H H 1 7.902 0.002 . 1 . . . A 18 VAL H . 17764 1 110 . 1 1 18 18 VAL HA H 1 3.871 0.002 . 1 . . . A 18 VAL HA . 17764 1 111 . 1 1 18 18 VAL HB H 1 1.742 0.003 . 1 . . . A 18 VAL HB . 17764 1 112 . 1 1 18 18 VAL HG11 H 1 0.673 0.003 . 2 . . . A 18 VAL HG11 . 17764 1 113 . 1 1 18 18 VAL HG12 H 1 0.673 0.003 . 2 . . . A 18 VAL HG12 . 17764 1 114 . 1 1 18 18 VAL HG13 H 1 0.673 0.003 . 2 . . . A 18 VAL HG13 . 17764 1 115 . 1 1 18 18 VAL HG21 H 1 0.587 0.002 . 2 . . . A 18 VAL HG21 . 17764 1 116 . 1 1 18 18 VAL HG22 H 1 0.587 0.002 . 2 . . . A 18 VAL HG22 . 17764 1 117 . 1 1 18 18 VAL HG23 H 1 0.587 0.002 . 2 . . . A 18 VAL HG23 . 17764 1 118 . 1 1 19 19 PHE H H 1 8.160 0.001 . 1 . . . A 19 PHE H . 17764 1 119 . 1 1 19 19 PHE HA H 1 4.418 0.001 . 1 . . . A 19 PHE HA . 17764 1 120 . 1 1 19 19 PHE HB2 H 1 2.821 0.006 . 2 . . . A 19 PHE HB2 . 17764 1 121 . 1 1 19 19 PHE HB3 H 1 2.749 0.002 . 2 . . . A 19 PHE HB3 . 17764 1 122 . 1 1 19 19 PHE HD1 H 1 7.005 0.002 . 2 . . . A 19 PHE HD1 . 17764 1 123 . 1 1 19 19 PHE HD2 H 1 7.005 0.002 . 2 . . . A 19 PHE HD2 . 17764 1 124 . 1 1 19 19 PHE HE1 H 1 7.144 0.001 . 2 . . . A 19 PHE HE1 . 17764 1 125 . 1 1 19 19 PHE HE2 H 1 7.144 0.001 . 2 . . . A 19 PHE HE2 . 17764 1 126 . 1 1 19 19 PHE HZ H 1 7.114 0.002 . 1 . . . A 19 PHE HZ . 17764 1 127 . 1 1 20 20 PHE H H 1 8.132 0.002 . 1 . . . A 20 PHE H . 17764 1 128 . 1 1 20 20 PHE HA H 1 4.422 0.003 . 1 . . . A 20 PHE HA . 17764 1 129 . 1 1 20 20 PHE HB2 H 1 2.926 0.001 . 2 . . . A 20 PHE HB2 . 17764 1 130 . 1 1 20 20 PHE HB3 H 1 2.773 0.001 . 2 . . . A 20 PHE HB3 . 17764 1 131 . 1 1 20 20 PHE HD1 H 1 7.076 0.002 . 2 . . . A 20 PHE HD1 . 17764 1 132 . 1 1 20 20 PHE HD2 H 1 7.076 0.002 . 2 . . . A 20 PHE HD2 . 17764 1 133 . 1 1 20 20 PHE HE1 H 1 7.161 0.003 . 2 . . . A 20 PHE HE1 . 17764 1 134 . 1 1 20 20 PHE HE2 H 1 7.161 0.003 . 2 . . . A 20 PHE HE2 . 17764 1 135 . 1 1 21 21 ALA H H 1 8.154 0.001 . 1 . . . A 21 ALA H . 17764 1 136 . 1 1 21 21 ALA HA H 1 4.061 0.003 . 1 . . . A 21 ALA HA . 17764 1 137 . 1 1 21 21 ALA HB1 H 1 1.206 0.002 . 1 . . . A 21 ALA HB1 . 17764 1 138 . 1 1 21 21 ALA HB2 H 1 1.206 0.002 . 1 . . . A 21 ALA HB2 . 17764 1 139 . 1 1 21 21 ALA HB3 H 1 1.206 0.002 . 1 . . . A 21 ALA HB3 . 17764 1 140 . 1 1 22 22 GLU H H 1 8.269 0.003 . 1 . . . A 22 GLU H . 17764 1 141 . 1 1 22 22 GLU HA H 1 4.048 0.003 . 1 . . . A 22 GLU HA . 17764 1 142 . 1 1 22 22 GLU HB2 H 1 1.762 0.004 . 2 . . . A 22 GLU HB2 . 17764 1 143 . 1 1 22 22 GLU HB3 H 1 1.880 0.002 . 2 . . . A 22 GLU HB3 . 17764 1 144 . 1 1 22 22 GLU HG2 H 1 2.108 0.010 . 2 . . . A 22 GLU HG2 . 17764 1 145 . 1 1 22 22 GLU HG3 H 1 2.108 0.010 . 2 . . . A 22 GLU HG3 . 17764 1 146 . 1 1 23 23 ASP H H 1 8.325 0.001 . 1 . . . A 23 ASP H . 17764 1 147 . 1 1 23 23 ASP HA H 1 4.487 0.002 . 1 . . . A 23 ASP HA . 17764 1 148 . 1 1 23 23 ASP HB2 H 1 2.584 0.003 . 2 . . . A 23 ASP HB2 . 17764 1 149 . 1 1 23 23 ASP HB3 H 1 2.480 0.004 . 2 . . . A 23 ASP HB3 . 17764 1 150 . 1 1 24 24 VAL H H 1 8.053 0.001 . 1 . . . A 24 VAL H . 17764 1 151 . 1 1 24 24 VAL HA H 1 3.972 0.002 . 1 . . . A 24 VAL HA . 17764 1 152 . 1 1 24 24 VAL HB H 1 2.025 0.003 . 1 . . . A 24 VAL HB . 17764 1 153 . 1 1 24 24 VAL HG11 H 1 0.795 0.003 . 2 . . . A 24 VAL HG11 . 17764 1 154 . 1 1 24 24 VAL HG12 H 1 0.795 0.003 . 2 . . . A 24 VAL HG12 . 17764 1 155 . 1 1 24 24 VAL HG13 H 1 0.795 0.003 . 2 . . . A 24 VAL HG13 . 17764 1 156 . 1 1 24 24 VAL HG21 H 1 0.795 0.003 . 2 . . . A 24 VAL HG21 . 17764 1 157 . 1 1 24 24 VAL HG22 H 1 0.795 0.003 . 2 . . . A 24 VAL HG22 . 17764 1 158 . 1 1 24 24 VAL HG23 H 1 0.795 0.003 . 2 . . . A 24 VAL HG23 . 17764 1 159 . 1 1 25 25 GLY H H 1 8.451 0.001 . 1 . . . A 25 GLY H . 17764 1 160 . 1 1 25 25 GLY HA2 H 1 3.817 0.003 . 2 . . . A 25 GLY HA2 . 17764 1 161 . 1 1 25 25 GLY HA3 H 1 3.817 0.003 . 2 . . . A 25 GLY HA3 . 17764 1 162 . 1 1 26 26 SER H H 1 8.065 0.003 . 1 . . . A 26 SER H . 17764 1 163 . 1 1 26 26 SER HA H 1 4.271 0.008 . 1 . . . A 26 SER HA . 17764 1 164 . 1 1 26 26 SER HB2 H 1 3.752 0.006 . 2 . . . A 26 SER HB2 . 17764 1 165 . 1 1 26 26 SER HB3 H 1 3.706 0.005 . 2 . . . A 26 SER HB3 . 17764 1 166 . 1 1 27 27 ASN H H 1 8.391 0.001 . 1 . . . A 27 ASN H . 17764 1 167 . 1 1 27 27 ASN HA H 1 4.575 0.003 . 1 . . . A 27 ASN HA . 17764 1 168 . 1 1 27 27 ASN HB2 H 1 2.712 0.002 . 2 . . . A 27 ASN HB2 . 17764 1 169 . 1 1 27 27 ASN HB3 H 1 2.645 0.003 . 2 . . . A 27 ASN HB3 . 17764 1 170 . 1 1 27 27 ASN HD21 H 1 6.834 0.001 . 2 . . . A 27 ASN HD21 . 17764 1 171 . 1 1 27 27 ASN HD22 H 1 7.545 0.001 . 2 . . . A 27 ASN HD22 . 17764 1 172 . 1 1 28 28 LYS H H 1 8.252 0.002 . 1 . . . A 28 LYS H . 17764 1 173 . 1 1 28 28 LYS HA H 1 4.110 0.004 . 1 . . . A 28 LYS HA . 17764 1 174 . 1 1 28 28 LYS HB2 H 1 1.724 0.005 . 2 . . . A 28 LYS HB2 . 17764 1 175 . 1 1 28 28 LYS HB3 H 1 1.613 0.002 . 2 . . . A 28 LYS HB3 . 17764 1 176 . 1 1 28 28 LYS HG2 H 1 1.316 0.008 . 2 . . . A 28 LYS HG2 . 17764 1 177 . 1 1 28 28 LYS HG3 H 1 1.316 0.008 . 2 . . . A 28 LYS HG3 . 17764 1 178 . 1 1 29 29 GLY H H 1 8.326 0.001 . 1 . . . A 29 GLY H . 17764 1 179 . 1 1 29 29 GLY HA2 H 1 3.763 0.002 . 2 . . . A 29 GLY HA2 . 17764 1 180 . 1 1 29 29 GLY HA3 H 1 3.763 0.002 . 2 . . . A 29 GLY HA3 . 17764 1 181 . 1 1 30 30 ALA H H 1 7.939 0.003 . 1 . . . A 30 ALA H . 17764 1 182 . 1 1 30 30 ALA HA H 1 4.155 0.003 . 1 . . . A 30 ALA HA . 17764 1 183 . 1 1 30 30 ALA HB1 H 1 1.209 0.002 . 1 . . . A 30 ALA HB1 . 17764 1 184 . 1 1 30 30 ALA HB2 H 1 1.209 0.002 . 1 . . . A 30 ALA HB2 . 17764 1 185 . 1 1 30 30 ALA HB3 H 1 1.209 0.002 . 1 . . . A 30 ALA HB3 . 17764 1 186 . 1 1 31 31 ILE H H 1 8.076 0.002 . 1 . . . A 31 ILE H . 17764 1 187 . 1 1 31 31 ILE HA H 1 3.995 0.002 . 1 . . . A 31 ILE HA . 17764 1 188 . 1 1 31 31 ILE HB H 1 1.703 0.001 . 1 . . . A 31 ILE HB . 17764 1 189 . 1 1 31 31 ILE HG12 H 1 1.339 0.003 . 2 . . . A 31 ILE HG12 . 17764 1 190 . 1 1 31 31 ILE HG13 H 1 1.039 0.003 . 2 . . . A 31 ILE HG13 . 17764 1 191 . 1 1 31 31 ILE HD11 H 1 0.709 0.000 . 1 . . . A 31 ILE HD11 . 17764 1 192 . 1 1 31 31 ILE HD12 H 1 0.709 0.000 . 1 . . . A 31 ILE HD12 . 17764 1 193 . 1 1 31 31 ILE HD13 H 1 0.709 0.000 . 1 . . . A 31 ILE HD13 . 17764 1 194 . 1 1 32 32 ILE H H 1 8.177 0.005 . 1 . . . A 32 ILE H . 17764 1 195 . 1 1 32 32 ILE HA H 1 3.999 0.002 . 1 . . . A 32 ILE HA . 17764 1 196 . 1 1 32 32 ILE HB H 1 1.705 0.002 . 1 . . . A 32 ILE HB . 17764 1 197 . 1 1 32 32 ILE HG21 H 1 1.047 0.004 . 1 . . . A 32 ILE HG21 . 17764 1 198 . 1 1 32 32 ILE HG22 H 1 1.047 0.004 . 1 . . . A 32 ILE HG22 . 17764 1 199 . 1 1 32 32 ILE HG23 H 1 1.047 0.004 . 1 . . . A 32 ILE HG23 . 17764 1 200 . 1 1 32 32 ILE HD11 H 1 0.703 0.003 . 1 . . . A 32 ILE HD11 . 17764 1 201 . 1 1 32 32 ILE HD12 H 1 0.703 0.003 . 1 . . . A 32 ILE HD12 . 17764 1 202 . 1 1 32 32 ILE HD13 H 1 0.703 0.003 . 1 . . . A 32 ILE HD13 . 17764 1 203 . 1 1 33 33 GLY H H 1 8.369 0.001 . 1 . . . A 33 GLY H . 17764 1 204 . 1 1 33 33 GLY HA2 H 1 3.765 0.002 . 2 . . . A 33 GLY HA2 . 17764 1 205 . 1 1 33 33 GLY HA3 H 1 3.765 0.002 . 2 . . . A 33 GLY HA3 . 17764 1 206 . 1 1 34 34 LEU H H 1 7.953 0.002 . 1 . . . A 34 LEU H . 17764 1 207 . 1 1 34 34 LEU HA H 1 4.183 0.003 . 1 . . . A 34 LEU HA . 17764 1 208 . 1 1 34 34 LEU HB2 H 1 1.438 0.001 . 2 . . . A 34 LEU HB2 . 17764 1 209 . 1 1 34 34 LEU HB3 H 1 1.438 0.001 . 2 . . . A 34 LEU HB3 . 17764 1 210 . 1 1 34 34 LEU HD11 H 1 0.765 0.004 . 2 . . . A 34 LEU HD11 . 17764 1 211 . 1 1 34 34 LEU HD12 H 1 0.765 0.004 . 2 . . . A 34 LEU HD12 . 17764 1 212 . 1 1 34 34 LEU HD13 H 1 0.765 0.004 . 2 . . . A 34 LEU HD13 . 17764 1 213 . 1 1 34 34 LEU HD21 H 1 0.713 0.003 . 2 . . . A 34 LEU HD21 . 17764 1 214 . 1 1 34 34 LEU HD22 H 1 0.713 0.003 . 2 . . . A 34 LEU HD22 . 17764 1 215 . 1 1 34 34 LEU HD23 H 1 0.713 0.003 . 2 . . . A 34 LEU HD23 . 17764 1 216 . 1 1 35 35 MET H H 1 8.350 0.003 . 1 . . . A 35 MET H . 17764 1 217 . 1 1 35 35 MET HA H 1 4.367 0.001 . 1 . . . A 35 MET HA . 17764 1 218 . 1 1 35 35 MET HB2 H 1 1.918 0.003 . 2 . . . A 35 MET HB2 . 17764 1 219 . 1 1 35 35 MET HB3 H 1 1.859 0.003 . 2 . . . A 35 MET HB3 . 17764 1 220 . 1 1 35 35 MET HG2 H 1 2.431 0.002 . 2 . . . A 35 MET HG2 . 17764 1 221 . 1 1 35 35 MET HG3 H 1 2.354 0.002 . 2 . . . A 35 MET HG3 . 17764 1 222 . 1 1 36 36 VAL H H 1 8.135 0.002 . 1 . . . A 36 VAL H . 17764 1 223 . 1 1 36 36 VAL HA H 1 3.969 0.002 . 1 . . . A 36 VAL HA . 17764 1 224 . 1 1 36 36 VAL HB H 1 1.924 0.003 . 1 . . . A 36 VAL HB . 17764 1 225 . 1 1 36 36 VAL HG11 H 1 0.786 0.002 . 2 . . . A 36 VAL HG11 . 17764 1 226 . 1 1 36 36 VAL HG12 H 1 0.786 0.002 . 2 . . . A 36 VAL HG12 . 17764 1 227 . 1 1 36 36 VAL HG13 H 1 0.786 0.002 . 2 . . . A 36 VAL HG13 . 17764 1 228 . 1 1 36 36 VAL HG21 H 1 0.786 0.002 . 2 . . . A 36 VAL HG21 . 17764 1 229 . 1 1 36 36 VAL HG22 H 1 0.786 0.002 . 2 . . . A 36 VAL HG22 . 17764 1 230 . 1 1 36 36 VAL HG23 H 1 0.786 0.002 . 2 . . . A 36 VAL HG23 . 17764 1 231 . 1 1 37 37 GLY H H 1 8.496 0.001 . 1 . . . A 37 GLY H . 17764 1 232 . 1 1 37 37 GLY HA2 H 1 3.826 0.004 . 2 . . . A 37 GLY HA2 . 17764 1 233 . 1 1 37 37 GLY HA3 H 1 3.826 0.004 . 2 . . . A 37 GLY HA3 . 17764 1 234 . 1 1 38 38 GLY H H 1 8.166 0.002 . 1 . . . A 38 GLY H . 17764 1 235 . 1 1 38 38 GLY HA2 H 1 3.855 0.002 . 2 . . . A 38 GLY HA2 . 17764 1 236 . 1 1 38 38 GLY HA3 H 1 3.789 0.003 . 2 . . . A 38 GLY HA3 . 17764 1 237 . 1 1 39 39 VAL H H 1 7.981 0.004 . 1 . . . A 39 VAL H . 17764 1 238 . 1 1 39 39 VAL HA H 1 4.015 0.001 . 1 . . . A 39 VAL HA . 17764 1 239 . 1 1 39 39 VAL HB H 1 1.927 0.003 . 1 . . . A 39 VAL HB . 17764 1 240 . 1 1 39 39 VAL HG11 H 1 0.776 0.003 . 2 . . . A 39 VAL HG11 . 17764 1 241 . 1 1 39 39 VAL HG12 H 1 0.776 0.003 . 2 . . . A 39 VAL HG12 . 17764 1 242 . 1 1 39 39 VAL HG13 H 1 0.776 0.003 . 2 . . . A 39 VAL HG13 . 17764 1 243 . 1 1 39 39 VAL HG21 H 1 0.776 0.003 . 2 . . . A 39 VAL HG21 . 17764 1 244 . 1 1 39 39 VAL HG22 H 1 0.776 0.003 . 2 . . . A 39 VAL HG22 . 17764 1 245 . 1 1 39 39 VAL HG23 H 1 0.776 0.003 . 2 . . . A 39 VAL HG23 . 17764 1 246 . 1 1 40 40 VAL H H 1 7.718 0.001 . 1 . . . A 40 VAL H . 17764 1 247 . 1 1 40 40 VAL HA H 1 3.890 0.000 . 1 . . . A 40 VAL HA . 17764 1 248 . 1 1 40 40 VAL HB H 1 1.898 0.003 . 1 . . . A 40 VAL HB . 17764 1 249 . 1 1 40 40 VAL HG11 H 1 0.738 0.006 . 2 . . . A 40 VAL HG11 . 17764 1 250 . 1 1 40 40 VAL HG12 H 1 0.738 0.006 . 2 . . . A 40 VAL HG12 . 17764 1 251 . 1 1 40 40 VAL HG13 H 1 0.738 0.006 . 2 . . . A 40 VAL HG13 . 17764 1 252 . 1 1 40 40 VAL HG21 H 1 0.738 0.006 . 2 . . . A 40 VAL HG21 . 17764 1 253 . 1 1 40 40 VAL HG22 H 1 0.738 0.006 . 2 . . . A 40 VAL HG22 . 17764 1 254 . 1 1 40 40 VAL HG23 H 1 0.738 0.006 . 2 . . . A 40 VAL HG23 . 17764 1 stop_ save_