data_17159 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17159 _Entry.Title ; Backbone assignment of the affibody-bound amyloid B-peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-08-31 _Entry.Accession_date 2010-08-31 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details 'Amyloid B-peptide bound to the N-terminally truncated Affibody ZAB3' _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 Joel Lindgren . . . 17159 2 Anna Wahlstrom . . . 17159 3 Jens Danielsson . . . 17159 4 Natalia Markova . . . 17159 5 Caroline Ekblad . . . 17159 6 Astrid Graslund . . . 17159 7 Lars Abrahmsen . . . 17159 8 Amelie Karlstrom . . . 17159 9 Sebastian Warmlander . . . 17159 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17159 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 70 17159 '15N chemical shifts' 35 17159 '1H chemical shifts' 35 17159 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 3 . . 2010-12-01 2010-08-31 update BMRB 'Update entry citation' 17159 2 . . 2010-10-05 2010-08-31 update BMRB 'Update entry citation' 17159 1 . . 2010-09-16 2010-08-31 original author 'original release' 17159 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17159 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 20886513 _Citation.Full_citation . _Citation.Title 'N-terminal engineering of amyloid--binding Affibody molecules yields improved chemical synthesis and higher binding affinity.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 19 _Citation.Journal_issue 12 _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 2319 _Citation.Page_last 2329 _Citation.Year 2010 _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 Joel Lindgren . . . 17159 1 2 Anna Wahlstrom . . . 17159 1 3 Jens Danielsson . . . 17159 1 4 Natalia Markova . . . 17159 1 5 Caroline Ekblad . . . 17159 1 6 Astrid Graslund . . . 17159 1 7 Lars Abrahmsen . . . 17159 1 8 'Amelie Eriksson' Karlstrom . . . 17159 1 9 'Sebastian K T S' Warmlander . . . 17159 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17159 _Assembly.ID 1 _Assembly.Name Affibody_Abeta _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _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 'Two affibody molecules bound to one Amyloid beta-peptide' _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-Peptide' 1 $Amyloid_beta-Peptide A . yes native no no . . . 17159 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Amyloid_beta-Peptide _Entity.Sf_category entity _Entity.Sf_framecode Amyloid_beta-Peptide _Entity.Entry_ID 17159 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Amyloid_beta-Peptide _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 40 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 17159 1 3 no BMRB 17186 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 4 no BMRB 17764 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 5 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 1 6 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 1 7 no BMRB 17795 . Abeta(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 8 no BMRB 17796 . Abeta40 . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 9 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 92.50 38 100.00 100.00 2.74e-16 . . . . 17159 1 10 no BMRB 18127 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 11 no BMRB 18128 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 12 no BMRB 18129 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 13 no BMRB 18131 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 14 no BMRB 19009 . beta-amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 15 no BMRB 19309 . amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 16 no BMRB 19393 . Abeta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 17159 1 17 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 1 18 no BMRB 25289 . amyloid_beta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 17159 1 19 no BMRB 25429 . entity . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 1 20 no BMRB 26508 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 1 21 no BMRB 26516 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 65.00 26 100.00 100.00 2.06e-08 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 100.00 40 97.50 100.00 5.11e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17159 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17159 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.50 100.00 1.74e-18 . . . . 17159 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 1.14e-18 . . . . 17159 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 1.43e-18 . . . . 17159 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17159 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17159 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 3.56e-19 . . . . 17159 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 17159 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 17159 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.00 97 100.00 100.00 2.36e-17 . . . . 17159 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17159 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 75.00 30 100.00 100.00 1.09e-11 . . . . 17159 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 9.13e-19 . . . . 17159 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 1.74e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 4.05e-19 . . . . 17159 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17159 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 17159 1 77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 17159 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 9.42e-19 . . . . 17159 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 4.07e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 17159 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17159 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 1.65e-18 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 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 . . . . 17159 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 17159 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 . 17159 1 2 . ALA . 17159 1 3 . GLU . 17159 1 4 . PHE . 17159 1 5 . ARG . 17159 1 6 . HIS . 17159 1 7 . ASP . 17159 1 8 . SER . 17159 1 9 . GLY . 17159 1 10 . TYR . 17159 1 11 . GLU . 17159 1 12 . VAL . 17159 1 13 . HIS . 17159 1 14 . HIS . 17159 1 15 . GLN . 17159 1 16 . LYS . 17159 1 17 . LEU . 17159 1 18 . VAL . 17159 1 19 . PHE . 17159 1 20 . PHE . 17159 1 21 . ALA . 17159 1 22 . GLU . 17159 1 23 . ASP . 17159 1 24 . VAL . 17159 1 25 . GLY . 17159 1 26 . SER . 17159 1 27 . ASN . 17159 1 28 . LYS . 17159 1 29 . GLY . 17159 1 30 . ALA . 17159 1 31 . ILE . 17159 1 32 . ILE . 17159 1 33 . GLY . 17159 1 34 . LEU . 17159 1 35 . MET . 17159 1 36 . VAL . 17159 1 37 . GLY . 17159 1 38 . GLY . 17159 1 39 . VAL . 17159 1 40 . VAL . 17159 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 17159 1 . ALA 2 2 17159 1 . GLU 3 3 17159 1 . PHE 4 4 17159 1 . ARG 5 5 17159 1 . HIS 6 6 17159 1 . ASP 7 7 17159 1 . SER 8 8 17159 1 . GLY 9 9 17159 1 . TYR 10 10 17159 1 . GLU 11 11 17159 1 . VAL 12 12 17159 1 . HIS 13 13 17159 1 . HIS 14 14 17159 1 . GLN 15 15 17159 1 . LYS 16 16 17159 1 . LEU 17 17 17159 1 . VAL 18 18 17159 1 . PHE 19 19 17159 1 . PHE 20 20 17159 1 . ALA 21 21 17159 1 . GLU 22 22 17159 1 . ASP 23 23 17159 1 . VAL 24 24 17159 1 . GLY 25 25 17159 1 . SER 26 26 17159 1 . ASN 27 27 17159 1 . LYS 28 28 17159 1 . GLY 29 29 17159 1 . ALA 30 30 17159 1 . ILE 31 31 17159 1 . ILE 32 32 17159 1 . GLY 33 33 17159 1 . LEU 34 34 17159 1 . MET 35 35 17159 1 . VAL 36 36 17159 1 . GLY 37 37 17159 1 . GLY 38 38 17159 1 . VAL 39 39 17159 1 . VAL 40 40 17159 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 17159 _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-Peptide . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 17159 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 17159 _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-Peptide . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . NA . . . . . . 17159 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17159 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Amyloid beta peptide bound to the Affibody ZAB3 molecule' _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-Peptide' '[U-13C; U-15N]' . . 1 $Amyloid_beta-Peptide . . 0.29 . . mM 0.03 . . . 17159 1 2 'sodium phosphate' 'natural abundance' . . . . . . 10 . . mM 1 . . . 17159 1 3 DSS 'natural abundance' . . . . . . 0.1 . . mM 0.02 . . . 17159 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 17159 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 17159 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 17159 _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' 10 . mM 17159 1 pH 7.4 0.1 pH 17159 1 pressure 1 . atm 17159 1 temperature 298 1 K 17159 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 17159 _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' . . 17159 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17159 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 17159 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 17159 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17159 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 17159 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'equipped with a cryogenically cooled probehead' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 17159 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 'equipped with a cryogenically cooled probehead' . . 17159 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 17159 _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 . . . . . . . . . . . . . . . . 17159 1 2 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17159 1 3 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17159 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17159 1 5 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17159 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 17159 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0 internal indirect 0.25145 . . . . . . . . . 17159 1 H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . . . . . . . 17159 1 N 15 DSS 'methyl protons' . . . . ppm 0 internal indirect 0.10133 . . . . . . . . . 17159 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 17159 _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' . . . 17159 1 2 '3D HNCO' . . . 17159 1 3 '3D HN(CO)CA' . . . 17159 1 4 '3D HNCA' . . . 17159 1 5 '3D HCACO' . . . 17159 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 3 3 GLU H H 1 8.358 0.004 . 1 . . . . 3 E H . 17159 1 2 . 1 1 3 3 GLU C C 13 176.028 0.004 . 1 . . . . 3 E CO . 17159 1 3 . 1 1 3 3 GLU CA C 13 56.674 0.003 . 1 . . . . 3 E CA . 17159 1 4 . 1 1 3 3 GLU N N 15 120.146 0.009 . 1 . . . . 3 E N . 17159 1 5 . 1 1 4 4 PHE H H 1 8.180 0.000 . 1 . . . . 4 F H . 17159 1 6 . 1 1 4 4 PHE C C 13 175.254 0.021 . 1 . . . . 4 F CO . 17159 1 7 . 1 1 4 4 PHE CA C 13 57.638 0.008 . 1 . . . . 4 F CA . 17159 1 8 . 1 1 4 4 PHE N N 15 121.452 0.006 . 1 . . . . 4 F N . 17159 1 9 . 1 1 5 5 ARG H H 1 8.049 0.001 . 1 . . . . 5 R H . 17159 1 10 . 1 1 5 5 ARG C C 13 175.566 0.006 . 1 . . . . 5 R CO . 17159 1 11 . 1 1 5 5 ARG CA C 13 55.586 0.006 . 1 . . . . 5 R CA . 17159 1 12 . 1 1 5 5 ARG N N 15 123.404 0.033 . 1 . . . . 5 R N . 17159 1 13 . 1 1 7 7 ASP H H 1 8.266 0.001 . 1 . . . . 7 D H . 17159 1 14 . 1 1 7 7 ASP C C 13 175.053 0.021 . 1 . . . . 7 D CO . 17159 1 15 . 1 1 7 7 ASP CA C 13 54.177 0.006 . 1 . . . . 7 D CA . 17159 1 16 . 1 1 7 7 ASP N N 15 121.553 0.007 . 1 . . . . 7 D N . 17159 1 17 . 1 1 8 8 SER H H 1 8.279 0.002 . 1 . . . . 8 S H . 17159 1 18 . 1 1 8 8 SER C C 13 175.080 0.006 . 1 . . . . 8 S CO . 17159 1 19 . 1 1 8 8 SER CA C 13 58.971 0.003 . 1 . . . . 8 S CA . 17159 1 20 . 1 1 8 8 SER N N 15 116.252 0.008 . 1 . . . . 8 S N . 17159 1 21 . 1 1 9 9 GLY H H 1 8.422 0.004 . 1 . . . . 9 G H . 17159 1 22 . 1 1 9 9 GLY C C 13 173.923 0.014 . 1 . . . . 9 G CO . 17159 1 23 . 1 1 9 9 GLY CA C 13 45.368 0.052 . 1 . . . . 9 G CA . 17159 1 24 . 1 1 9 9 GLY N N 15 110.539 0.026 . 1 . . . . 9 G N . 17159 1 25 . 1 1 10 10 TYR H H 1 7.861 0.001 . 1 . . . . 10 Y H . 17159 1 26 . 1 1 10 10 TYR C C 13 175.618 0.007 . 1 . . . . 10 Y CO . 17159 1 27 . 1 1 10 10 TYR CA C 13 58.002 0.020 . 1 . . . . 10 Y CA . 17159 1 28 . 1 1 10 10 TYR N N 15 119.831 0.009 . 1 . . . . 10 Y N . 17159 1 29 . 1 1 11 11 GLU H H 1 8.276 0.001 . 1 . . . . 11 E H . 17159 1 30 . 1 1 11 11 GLU C C 13 176.039 0.025 . 1 . . . . 11 E CO . 17159 1 31 . 1 1 11 11 GLU CA C 13 56.484 0.001 . 1 . . . . 11 E CA . 17159 1 32 . 1 1 11 11 GLU N N 15 122.438 0.004 . 1 . . . . 11 E N . 17159 1 33 . 1 1 12 12 VAL H H 1 7.945 0.001 . 1 . . . . 12 V H . 17159 1 34 . 1 1 12 12 VAL C C 13 175.713 0.033 . 1 . . . . 12 V CO . 17159 1 35 . 1 1 12 12 VAL CA C 13 62.483 0.008 . 1 . . . . 12 V CA . 17159 1 36 . 1 1 12 12 VAL N N 15 120.612 0.024 . 1 . . . . 12 V N . 17159 1 37 . 1 1 13 13 HIS H H 1 8.187 0.007 . 1 . . . . 13 H H . 17159 1 38 . 1 1 13 13 HIS C C 13 174.969 0.006 . 1 . . . . 13 H CO . 17159 1 39 . 1 1 13 13 HIS CA C 13 55.944 0.006 . 1 . . . . 13 H CA . 17159 1 40 . 1 1 13 13 HIS N N 15 122.351 0.059 . 1 . . . . 13 H N . 17159 1 41 . 1 1 15 15 GLN H H 1 8.293 0.001 . 1 . . . . 15 Q H . 17159 1 42 . 1 1 15 15 GLN C C 13 175.214 0.003 . 1 . . . . 15 Q CO . 17159 1 43 . 1 1 15 15 GLN CA C 13 55.701 0.001 . 1 . . . . 15 Q CA . 17159 1 44 . 1 1 15 15 GLN N N 15 120.993 0.057 . 1 . . . . 15 Q N . 17159 1 45 . 1 1 16 16 LYS H H 1 8.371 0.001 . 1 . . . . 16 K H . 17159 1 46 . 1 1 16 16 LYS C C 13 175.207 0.005 . 1 . . . . 16 K CO . 17159 1 47 . 1 1 16 16 LYS CA C 13 56.383 0.017 . 1 . . . . 16 K CA . 17159 1 48 . 1 1 16 16 LYS N N 15 123.503 0.018 . 1 . . . . 16 K N . 17159 1 49 . 1 1 17 17 LEU H H 1 8.292 0.000 . 1 . . . . 17 L H . 17159 1 50 . 1 1 17 17 LEU C C 13 175.945 0.015 . 1 . . . . 17 L CO . 17159 1 51 . 1 1 17 17 LEU CA C 13 54.487 0.005 . 1 . . . . 17 L CA . 17159 1 52 . 1 1 17 17 LEU N N 15 124.409 0.030 . 1 . . . . 17 L N . 17159 1 53 . 1 1 18 18 VAL H H 1 8.350 0.001 . 1 . . . . 18 V H . 17159 1 54 . 1 1 18 18 VAL C C 13 174.868 0.000 . 1 . . . . 18 V CO . 17159 1 55 . 1 1 18 18 VAL CA C 13 61.284 0.022 . 1 . . . . 18 V CA . 17159 1 56 . 1 1 18 18 VAL N N 15 123.212 0.024 . 1 . . . . 18 V N . 17159 1 57 . 1 1 19 19 PHE H H 1 9.314 0.003 . 1 . . . . 19 F H . 17159 1 58 . 1 1 19 19 PHE C C 13 174.551 0.002 . 1 . . . . 19 F CO . 17159 1 59 . 1 1 19 19 PHE CA C 13 59.134 0.007 . 1 . . . . 19 F CA . 17159 1 60 . 1 1 19 19 PHE N N 15 127.548 0.050 . 1 . . . . 19 F N . 17159 1 61 . 1 1 20 20 PHE H H 1 8.659 0.004 . 1 . . . . 20 F H . 17159 1 62 . 1 1 20 20 PHE C C 13 171.764 0.016 . 1 . . . . 20 F CO . 17159 1 63 . 1 1 20 20 PHE CA C 13 55.382 0.003 . 1 . . . . 20 F CA . 17159 1 64 . 1 1 20 20 PHE N N 15 116.606 0.028 . 1 . . . . 20 F N . 17159 1 65 . 1 1 21 21 ALA H H 1 8.529 0.002 . 1 . . . . 21 A H . 17159 1 66 . 1 1 21 21 ALA C C 13 175.265 0.031 . 1 . . . . 21 A CO . 17159 1 67 . 1 1 21 21 ALA CA C 13 49.588 0.016 . 1 . . . . 21 A CA . 17159 1 68 . 1 1 21 21 ALA N N 15 119.144 0.065 . 1 . . . . 21 A N . 17159 1 69 . 1 1 22 22 GLU H H 1 9.360 0.002 . 1 . . . . 22 E H . 17159 1 70 . 1 1 22 22 GLU C C 13 175.224 0.010 . 1 . . . . 22 E CO . 17159 1 71 . 1 1 22 22 GLU CA C 13 54.246 0.003 . 1 . . . . 22 E CA . 17159 1 72 . 1 1 22 22 GLU N N 15 123.515 0.045 . 1 . . . . 22 E N . 17159 1 73 . 1 1 23 23 ASP H H 1 8.748 0.002 . 1 . . . . 23 D H . 17159 1 74 . 1 1 23 23 ASP C C 13 176.651 0.021 . 1 . . . . 23 D CO . 17159 1 75 . 1 1 23 23 ASP CA C 13 54.227 0.007 . 1 . . . . 23 D CA . 17159 1 76 . 1 1 23 23 ASP N N 15 126.602 0.027 . 1 . . . . 23 D N . 17159 1 77 . 1 1 24 24 VAL H H 1 8.420 0.002 . 1 . . . . 24 V H . 17159 1 78 . 1 1 24 24 VAL C C 13 177.062 0.006 . 1 . . . . 24 V CO . 17159 1 79 . 1 1 24 24 VAL CA C 13 62.281 0.016 . 1 . . . . 24 V CA . 17159 1 80 . 1 1 24 24 VAL N N 15 122.764 0.025 . 1 . . . . 24 V N . 17159 1 81 . 1 1 25 25 GLY H H 1 8.434 0.002 . 1 . . . . 25 G H . 17159 1 82 . 1 1 25 25 GLY C C 13 174.082 0.029 . 1 . . . . 25 G CO . 17159 1 83 . 1 1 25 25 GLY CA C 13 45.234 0.012 . 1 . . . . 25 G CA . 17159 1 84 . 1 1 25 25 GLY N N 15 110.653 0.030 . 1 . . . . 25 G N . 17159 1 85 . 1 1 26 26 SER H H 1 8.409 0.004 . 1 . . . . 26 S H . 17159 1 86 . 1 1 26 26 SER C C 13 174.709 0.000 . 1 . . . . 26 S CO . 17159 1 87 . 1 1 26 26 SER CA C 13 58.476 0.000 . 1 . . . . 26 S CA . 17159 1 88 . 1 1 26 26 SER N N 15 113.230 0.039 . 1 . . . . 26 S N . 17159 1 89 . 1 1 28 28 LYS H H 1 7.853 0.000 . 1 . . . . 28 K H . 17159 1 90 . 1 1 28 28 LYS C C 13 176.822 0.006 . 1 . . . . 28 K CO . 17159 1 91 . 1 1 28 28 LYS CA C 13 56.203 0.001 . 1 . . . . 28 K CA . 17159 1 92 . 1 1 28 28 LYS N N 15 117.651 0.011 . 1 . . . . 28 K N . 17159 1 93 . 1 1 29 29 GLY H H 1 8.138 0.001 . 1 . . . . 29 G H . 17159 1 94 . 1 1 29 29 GLY C C 13 172.297 0.003 . 1 . . . . 29 G CO . 17159 1 95 . 1 1 29 29 GLY CA C 13 45.159 0.001 . 1 . . . . 29 G CA . 17159 1 96 . 1 1 29 29 GLY N N 15 108.726 0.047 . 1 . . . . 29 G N . 17159 1 97 . 1 1 30 30 ALA H H 1 7.906 0.002 . 1 . . . . 30 A H . 17159 1 98 . 1 1 30 30 ALA C C 13 175.950 0.001 . 1 . . . . 30 A CO . 17159 1 99 . 1 1 30 30 ALA CA C 13 51.226 0.014 . 1 . . . . 30 A CA . 17159 1 100 . 1 1 30 30 ALA N N 15 121.726 0.014 . 1 . . . . 30 A N . 17159 1 101 . 1 1 31 31 ILE H H 1 8.607 0.002 . 1 . . . . 31 I H . 17159 1 102 . 1 1 31 31 ILE C C 13 174.248 0.009 . 1 . . . . 31 I CO . 17159 1 103 . 1 1 31 31 ILE CA C 13 59.627 0.005 . 1 . . . . 31 I CA . 17159 1 104 . 1 1 31 31 ILE N N 15 117.522 0.039 . 1 . . . . 31 I N . 17159 1 105 . 1 1 32 32 ILE H H 1 8.370 0.003 . 1 . . . . 32 I H . 17159 1 106 . 1 1 32 32 ILE C C 13 175.202 0.000 . 1 . . . . 32 I CO . 17159 1 107 . 1 1 32 32 ILE CA C 13 57.213 0.003 . 1 . . . . 32 I CA . 17159 1 108 . 1 1 32 32 ILE N N 15 123.855 0.061 . 1 . . . . 32 I N . 17159 1 109 . 1 1 33 33 GLY H H 1 7.595 0.003 . 1 . . . . 33 G H . 17159 1 110 . 1 1 33 33 GLY C C 13 169.339 0.018 . 1 . . . . 33 G CO . 17159 1 111 . 1 1 33 33 GLY CA C 13 44.356 0.002 . 1 . . . . 33 G CA . 17159 1 112 . 1 1 33 33 GLY N N 15 112.877 0.032 . 1 . . . . 33 G N . 17159 1 113 . 1 1 34 34 LEU H H 1 8.455 0.001 . 1 . . . . 34 L H . 17159 1 114 . 1 1 34 34 LEU C C 13 174.486 0.000 . 1 . . . . 34 L CO . 17159 1 115 . 1 1 34 34 LEU CA C 13 53.585 0.001 . 1 . . . . 34 L CA . 17159 1 116 . 1 1 34 34 LEU N N 15 116.284 0.019 . 1 . . . . 34 L N . 17159 1 117 . 1 1 35 35 MET H H 1 9.280 0.002 . 1 . . . . 35 M H . 17159 1 118 . 1 1 35 35 MET C C 13 175.119 0.003 . 1 . . . . 35 M CO . 17159 1 119 . 1 1 35 35 MET CA C 13 53.772 0.047 . 1 . . . . 35 M CA . 17159 1 120 . 1 1 35 35 MET N N 15 122.834 0.014 . 1 . . . . 35 M N . 17159 1 121 . 1 1 36 36 VAL H H 1 8.960 0.003 . 1 . . . . 36 V H . 17159 1 122 . 1 1 36 36 VAL C C 13 176.553 0.002 . 1 . . . . 36 V CO . 17159 1 123 . 1 1 36 36 VAL CA C 13 61.502 0.007 . 1 . . . . 36 V CA . 17159 1 124 . 1 1 36 36 VAL N N 15 127.341 0.017 . 1 . . . . 36 V N . 17159 1 125 . 1 1 37 37 GLY H H 1 8.771 0.002 . 1 . . . . 37 G H . 17159 1 126 . 1 1 37 37 GLY C C 13 173.834 0.006 . 1 . . . . 37 G CO . 17159 1 127 . 1 1 37 37 GLY CA C 13 45.444 0.004 . 1 . . . . 37 G CA . 17159 1 128 . 1 1 37 37 GLY N N 15 115.386 0.016 . 1 . . . . 37 G N . 17159 1 129 . 1 1 38 38 GLY H H 1 8.098 0.001 . 1 . . . . 38 G H . 17159 1 130 . 1 1 38 38 GLY C C 13 173.289 0.005 . 1 . . . . 38 G CO . 17159 1 131 . 1 1 38 38 GLY CA C 13 44.794 0.002 . 1 . . . . 38 G CA . 17159 1 132 . 1 1 38 38 GLY N N 15 107.275 0.005 . 1 . . . . 38 G N . 17159 1 133 . 1 1 39 39 VAL H H 1 7.924 0.001 . 1 . . . . 39 V H . 17159 1 134 . 1 1 39 39 VAL C C 13 175.162 0.003 . 1 . . . . 39 V CO . 17159 1 135 . 1 1 39 39 VAL CA C 13 62.117 0.006 . 1 . . . . 39 V CA . 17159 1 136 . 1 1 39 39 VAL N N 15 118.453 0.015 . 1 . . . . 39 V N . 17159 1 137 . 1 1 40 40 VAL H H 1 7.611 0.002 . 1 . . . . 40 V H . 17159 1 138 . 1 1 40 40 VAL C C 13 180.725 0.006 . 1 . . . . 40 V CO . 17159 1 139 . 1 1 40 40 VAL CA C 13 63.745 0.006 . 1 . . . . 40 V CA . 17159 1 140 . 1 1 40 40 VAL N N 15 127.502 0.011 . 1 . . . . 40 V N . 17159 1 stop_ save_