data_25429 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25429 _Entry.Title ; 42-Residue Beta Amyloid Fibril ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2015-01-14 _Entry.Accession_date 2015-01-14 _Entry.Last_release_date 2015-05-04 _Entry.Original_release_date 2015-05-04 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.77 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLID-STATE _Entry.Details 'Amyloid Beta 42 Structural Model' _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 Yiling Xiao . . . 25429 2 Buyong Ma . . . 25429 3 Dan McElheny . . . 25429 4 Sudhakar Parthasarathy . . . 25429 5 Fei Long . . . 25429 6 Minako Hoshi . . . 25429 7 Ruth Nussinov . . . 25429 8 Yoshitaka Ishii . . . 25429 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 1 'not applicable' 'not applicable' . 25429 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'Amyloid Fibril' . 25429 'Protein Fibril' . 25429 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25429 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 78 25429 '15N chemical shifts' 25 25429 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2015-05-04 . original BMRB . 25429 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2MXU 'BMRB Entry Tracking System' 25429 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25429 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; A (1-42) Fibril Structure Illuminates Self-recognition and Replication Machinery of Amyloid in Alzheimer's ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'Nat. Struct. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _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 Yiling Xiao . . . 25429 1 2 Buyong Ma . . . 25429 1 3 Dan McElheny . . . 25429 1 4 Sudhakar Parthasarathy . . . 25429 1 5 Fei Long . . . 25429 1 6 Minako Hoshi . . . 25429 1 7 Ruth Nussinov . . . 25429 1 8 Yoshitaka Ishii . . . 25429 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25429 _Assembly.ID 1 _Assembly.Name '42-Residue Beta Amyloid Fibril' _Assembly.BMRB_code . _Assembly.Number_of_components 12 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 entity_1 1 $entity A . yes native no no . . . 25429 1 2 entity_2 1 $entity B . yes native no no . . . 25429 1 3 entity_3 1 $entity C . yes native no no . . . 25429 1 4 entity_4 1 $entity D . yes native no no . . . 25429 1 5 entity_5 1 $entity E . yes native no no . . . 25429 1 6 entity_6 1 $entity F . yes native no no . . . 25429 1 7 entity_7 1 $entity G . yes native no no . . . 25429 1 8 entity_8 1 $entity H . yes native no no . . . 25429 1 9 entity_9 1 $entity I . yes native no no . . . 25429 1 10 entity_10 1 $entity J . yes native no no . . . 25429 1 11 entity_11 1 $entity K . yes native no no . . . 25429 1 12 entity_12 1 $entity L . yes native no no . . . 25429 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 25429 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID ABCDEFGHIJKL _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 42 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3339.934 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25429 1 3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 4 no BMRB 17186 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 5 no BMRB 17764 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 6 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 7 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 8 no BMRB 17795 . Abeta(1-40) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 9 no BMRB 17796 . Abeta40 . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 88.10 38 100.00 100.00 2.61e-16 . . . . 25429 1 11 no BMRB 18127 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 12 no BMRB 18128 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 13 no BMRB 18129 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 14 no BMRB 18131 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 15 no BMRB 19009 . beta-amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 16 no BMRB 19309 . amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 17 no BMRB 19393 . Abeta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1 18 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 19 no BMRB 25289 . amyloid_beta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1 20 no BMRB 26508 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 21 no BMRB 26516 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 22 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1 23 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1 24 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 25 no PDB 1BA4 . "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 26 no PDB 1BA6 . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 95.24 40 97.50 97.50 1.43e-17 . . . . 25429 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 61.90 26 100.00 100.00 2.00e-08 . . . . 25429 1 28 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 29 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 31 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 32 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 33 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 34 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 35 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 36 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 95.24 40 97.50 100.00 4.61e-18 . . . . 25429 1 38 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25429 1 39 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 40 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 41 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 42 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 44 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 45 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 46 no PDB 3BAE . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1 47 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 48 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1 49 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 50 no PDB 4MVI . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 51 no PDB 4MVL . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 52 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 53 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1 54 no PDB 5AEF . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" . . . . . 66.67 28 100.00 100.00 2.69e-08 . . . . 25429 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.62 100.00 9.73e-20 . . . . 25429 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 8.24e-20 . . . . 25429 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 1.94e-20 . . . . 25429 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25429 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25429 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.24 97 100.00 100.00 1.03e-18 . . . . 25429 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 71.43 30 100.00 100.00 9.95e-12 . . . . 25429 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25429 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 9.55e-20 . . . . 25429 1 70 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1 71 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1 72 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1 73 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 2.05e-20 . . . . 25429 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1 77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25429 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 2.04e-19 . . . . 25429 1 80 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 81 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1 85 no SP P05067 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 86 no SP P53601 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 87 no SP P79307 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1 88 no SP P86906 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 95.24 40 97.50 100.00 5.31e-18 . . . . 25429 1 89 no SP Q28053 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 59 100.00 100.00 1.94e-20 . . . . 25429 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 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 . 25429 1 2 . ALA . 25429 1 3 . GLU . 25429 1 4 . PHE . 25429 1 5 . ARG . 25429 1 6 . HIS . 25429 1 7 . ASP . 25429 1 8 . SER . 25429 1 9 . GLY . 25429 1 10 . TYR . 25429 1 11 . GLU . 25429 1 12 . VAL . 25429 1 13 . HIS . 25429 1 14 . HIS . 25429 1 15 . GLN . 25429 1 16 . LYS . 25429 1 17 . LEU . 25429 1 18 . VAL . 25429 1 19 . PHE . 25429 1 20 . PHE . 25429 1 21 . ALA . 25429 1 22 . GLU . 25429 1 23 . ASP . 25429 1 24 . VAL . 25429 1 25 . GLY . 25429 1 26 . SER . 25429 1 27 . ASN . 25429 1 28 . LYS . 25429 1 29 . GLY . 25429 1 30 . ALA . 25429 1 31 . ILE . 25429 1 32 . ILE . 25429 1 33 . GLY . 25429 1 34 . LEU . 25429 1 35 . MET . 25429 1 36 . VAL . 25429 1 37 . GLY . 25429 1 38 . GLY . 25429 1 39 . VAL . 25429 1 40 . VAL . 25429 1 41 . ILE . 25429 1 42 . ALA . 25429 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 25429 1 . ALA 2 2 25429 1 . GLU 3 3 25429 1 . PHE 4 4 25429 1 . ARG 5 5 25429 1 . HIS 6 6 25429 1 . ASP 7 7 25429 1 . SER 8 8 25429 1 . GLY 9 9 25429 1 . TYR 10 10 25429 1 . GLU 11 11 25429 1 . VAL 12 12 25429 1 . HIS 13 13 25429 1 . HIS 14 14 25429 1 . GLN 15 15 25429 1 . LYS 16 16 25429 1 . LEU 17 17 25429 1 . VAL 18 18 25429 1 . PHE 19 19 25429 1 . PHE 20 20 25429 1 . ALA 21 21 25429 1 . GLU 22 22 25429 1 . ASP 23 23 25429 1 . VAL 24 24 25429 1 . GLY 25 25 25429 1 . SER 26 26 25429 1 . ASN 27 27 25429 1 . LYS 28 28 25429 1 . GLY 29 29 25429 1 . ALA 30 30 25429 1 . ILE 31 31 25429 1 . ILE 32 32 25429 1 . GLY 33 33 25429 1 . LEU 34 34 25429 1 . MET 35 35 25429 1 . VAL 36 36 25429 1 . GLY 37 37 25429 1 . GLY 38 38 25429 1 . VAL 39 39 25429 1 . VAL 40 40 25429 1 . ILE 41 41 25429 1 . ALA 42 42 25429 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 25429 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25429 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 25429 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity . 'chemical synthesis' . . . . . . . . . . . . . . . ; hemically synthesized by an Applied Biosystems model 433A automated peptide synthesizer with Fmoc protected 13C- and 15N-labeled amino acids at selected sites ; 25429 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25429 _Sample.ID 1 _Sample.Type solid _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 AB42 '[U-100% 13C; U-100% 15N]' . . 1 $entity . . 50 . . uM . . . . 25429 1 2 'sodium phosphate' 'natural abundance' . . . . . . 10 . . mM . . . . 25429 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25429 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25429 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 25429 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.4 0.1 pH 25429 1 pressure 1 . atm 25429 1 temperature 283 1 K 25429 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 25429 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details 'The Fold was initially determined within CYANA 2.1, Further annealing was done within AMBER12 however.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25429 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 25429 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 25429 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UnityPlus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 400 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 25429 _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 . 400 . . . 25429 1 2 spectrometer_2 Varian UnityPlus . 400 . . . 25429 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 25429 _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 13C-13C DARR (50 ms)' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1 2 '2D 13C-13C DARR (200 ms)' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1 3 '2D 13C-15N correlation' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1 4 '1D 13C-13C fpRFDR-CT' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1 5 '1D 13C-15N REDOR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 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 25429 _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 TMS 'methyl carbon' . . . . ppm 0 external direct 1 . . . . . . . . . 25429 1 N 15 TMS 'methyl carbon' . . . . ppm 0 external indirect 1 . . . . . . . . . 25429 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 25429 _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 1 _Assigned_chem_shift_list.Chem_shift_13C_err 1 _Assigned_chem_shift_list.Chem_shift_15N_err 1 _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 13C-13C DARR (50 ms)' . . . 25429 1 3 '2D 13C-15N correlation' . . . 25429 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 2 2 ALA C C 13 173.600 1 . 1 . . . . 2 ALA C . 25429 1 2 . 1 1 2 2 ALA CA C 13 50.500 1 . 1 . . . . 2 ALA CA . 25429 1 3 . 1 1 2 2 ALA CB C 13 17.600 1 . 1 . . . . 2 ALA CB . 25429 1 4 . 1 1 4 4 PHE C C 13 173.000 1 . 1 . . . . 4 PHE C . 25429 1 5 . 1 1 4 4 PHE CA C 13 55.000 1 . 1 . . . . 4 PHE CA . 25429 1 6 . 1 1 4 4 PHE CB C 13 40.000 1 . 1 . . . . 4 PHE CB . 25429 1 7 . 1 1 4 4 PHE N N 15 123.600 1 . 1 . . . . 4 PHE N . 25429 1 8 . 1 1 9 9 GLY C C 13 170.500 1 . 1 . . . . 9 GLY C . 25429 1 9 . 1 1 9 9 GLY CA C 13 43.300 1 . 1 . . . . 9 GLY CA . 25429 1 10 . 1 1 9 9 GLY N N 15 109.120 1 . 1 . . . . 9 GLY N . 25429 1 11 . 1 1 12 12 VAL C C 13 172.300 1 . 1 . . . A 12 VAL C . 25429 1 12 . 1 1 12 12 VAL CA C 13 59.000 1 . 1 . . . A 12 VAL CA . 25429 1 13 . 1 1 12 12 VAL CB C 13 33.600 1 . 1 . . . A 12 VAL CB . 25429 1 14 . 1 1 12 12 VAL N N 15 125.300 1 . 1 . . . A 12 VAL N . 25429 1 15 . 1 1 13 13 HIS C C 13 171.900 1 . 1 . . . A 13 HIS C . 25429 1 16 . 1 1 13 13 HIS CA C 13 52.400 1 . 1 . . . A 13 HIS CA . 25429 1 17 . 1 1 13 13 HIS CB C 13 30.000 1 . 1 . . . A 13 HIS CB . 25429 1 18 . 1 1 17 17 LEU C C 13 172.900 1 . 1 . . . A 17 LEU C . 25429 1 19 . 1 1 17 17 LEU CA C 13 52.900 1 . 1 . . . A 17 LEU CA . 25429 1 20 . 1 1 17 17 LEU CB C 13 43.200 1 . 1 . . . A 17 LEU CB . 25429 1 21 . 1 1 17 17 LEU N N 15 132.300 1 . 1 . . . A 17 LEU N . 25429 1 22 . 1 1 18 18 VAL C C 13 171.900 1 . 1 . . . A 18 VAL C . 25429 1 23 . 1 1 18 18 VAL CA C 13 57.600 1 . 1 . . . A 18 VAL CA . 25429 1 24 . 1 1 18 18 VAL CB C 13 33.500 1 . 1 . . . A 18 VAL CB . 25429 1 25 . 1 1 18 18 VAL N N 15 125.200 1 . 1 . . . A 18 VAL N . 25429 1 26 . 1 1 19 19 PHE C C 13 172.900 1 . 1 . . . A 19 PHE C . 25429 1 27 . 1 1 19 19 PHE CA C 13 58.800 1 . 1 . . . A 19 PHE CA . 25429 1 28 . 1 1 19 19 PHE CB C 13 39.100 1 . 1 . . . A 19 PHE CB . 25429 1 29 . 1 1 19 19 PHE N N 15 130.200 1 . 1 . . . A 19 PHE N . 25429 1 30 . 1 1 20 20 PHE C C 13 172.600 1 . 1 . . . A 20 PHE C . 25429 1 31 . 1 1 20 20 PHE CA C 13 55.200 1 . 1 . . . A 20 PHE CA . 25429 1 32 . 1 1 20 20 PHE CB C 13 38.500 1 . 1 . . . A 20 PHE CB . 25429 1 33 . 1 1 20 20 PHE N N 15 117.900 1 . 1 . . . A 20 PHE N . 25429 1 34 . 1 1 21 21 ALA C C 13 175.300 1 . 1 . . . A 21 ALA C . 25429 1 35 . 1 1 21 21 ALA CA C 13 51.200 1 . 1 . . . A 21 ALA CA . 25429 1 36 . 1 1 21 21 ALA CB C 13 18.800 1 . 1 . . . A 21 ALA CB . 25429 1 37 . 1 1 21 21 ALA N N 15 124.150 1 . 1 . . . A 21 ALA N . 25429 1 38 . 1 1 23 23 ASP C C 13 173.600 1 . 1 . . . A 23 ASP C . 25429 1 39 . 1 1 23 23 ASP CA C 13 53.800 1 . 1 . . . A 23 ASP CA . 25429 1 40 . 1 1 23 23 ASP CB C 13 39.600 1 . 1 . . . A 23 ASP CB . 25429 1 41 . 1 1 23 23 ASP N N 15 122.150 1 . 1 . . . A 23 ASP N . 25429 1 42 . 1 1 24 24 VAL C C 13 175.000 1 . 1 . . . A 24 VAL C . 25429 1 43 . 1 1 24 24 VAL CA C 13 57.600 1 . 1 . . . A 24 VAL CA . 25429 1 44 . 1 1 24 24 VAL CB C 13 34.100 1 . 1 . . . A 24 VAL CB . 25429 1 45 . 1 1 24 24 VAL N N 15 118.550 1 . 1 . . . A 24 VAL N . 25429 1 46 . 1 1 25 25 GLY C C 13 172.200 1 . 1 . . . A 25 GLY C . 25429 1 47 . 1 1 25 25 GLY CA C 13 46.500 1 . 1 . . . A 25 GLY CA . 25429 1 48 . 1 1 25 25 GLY N N 15 115.540 1 . 1 . . . A 25 GLY N . 25429 1 49 . 1 1 26 26 SER C C 13 170.300 1 . 1 . . . A 26 SER C . 25429 1 50 . 1 1 26 26 SER CA C 13 54.400 1 . 1 . . . A 26 SER CA . 25429 1 51 . 1 1 26 26 SER CB C 13 63.800 1 . 1 . . . A 26 SER CB . 25429 1 52 . 1 1 26 26 SER N N 15 115.000 1 . 1 . . . A 26 SER N . 25429 1 53 . 1 1 28 28 LYS C C 13 173.200 1 . 1 . . . A 28 LYS C . 25429 1 54 . 1 1 28 28 LYS CA C 13 52.600 1 . 1 . . . A 28 LYS CA . 25429 1 55 . 1 1 28 28 LYS CB C 13 33.300 1 . 1 . . . A 28 LYS CB . 25429 1 56 . 1 1 28 28 LYS N N 15 129.300 1 . 1 . . . A 28 LYS N . 25429 1 57 . 1 1 29 29 GLY C C 13 169.400 1 . 1 . . . A 29 GLY C . 25429 1 58 . 1 1 29 29 GLY CA C 13 46.600 1 . 1 . . . A 29 GLY CA . 25429 1 59 . 1 1 29 29 GLY N N 15 113.600 1 . 1 . . . A 29 GLY N . 25429 1 60 . 1 1 30 30 ALA C C 13 173.900 1 . 1 . . . A 30 ALA C . 25429 1 61 . 1 1 30 30 ALA CA C 13 49.000 1 . 1 . . . A 30 ALA CA . 25429 1 62 . 1 1 30 30 ALA CB C 13 20.000 1 . 1 . . . A 30 ALA CB . 25429 1 63 . 1 1 30 30 ALA N N 15 126.000 1 . 1 . . . A 30 ALA N . 25429 1 64 . 1 1 31 31 ILE C C 13 171.900 1 . 1 . . . A 31 ILE C . 25429 1 65 . 1 1 31 31 ILE CA C 13 58.200 1 . 1 . . . A 31 ILE CA . 25429 1 66 . 1 1 31 31 ILE CB C 13 42.600 1 . 1 . . . A 31 ILE CB . 25429 1 67 . 1 1 31 31 ILE N N 15 121.700 1 . 1 . . . A 31 ILE N . 25429 1 68 . 1 1 32 32 ILE C C 13 172.300 1 . 1 . . . A 32 ILE C . 25429 1 69 . 1 1 32 32 ILE CA C 13 58.300 1 . 1 . . . A 32 ILE CA . 25429 1 70 . 1 1 32 32 ILE CB C 13 39.500 1 . 1 . . . A 32 ILE CB . 25429 1 71 . 1 1 32 32 ILE N N 15 126.520 1 . 1 . . . A 32 ILE N . 25429 1 72 . 1 1 33 33 GLY C C 13 170.600 1 . 1 . . . A 33 GLY C . 25429 1 73 . 1 1 33 33 GLY CA C 13 44.400 1 . 1 . . . A 33 GLY CA . 25429 1 74 . 1 1 33 33 GLY N N 15 111.280 1 . 1 . . . A 33 GLY N . 25429 1 75 . 1 1 34 34 LEU C C 13 176.600 1 . 1 . . . A 34 LEU C . 25429 1 76 . 1 1 34 34 LEU CA C 13 55.400 1 . 1 . . . A 34 LEU CA . 25429 1 77 . 1 1 34 34 LEU CB C 13 40.100 1 . 1 . . . A 34 LEU CB . 25429 1 78 . 1 1 34 34 LEU N N 15 111.460 1 . 1 . . . A 34 LEU N . 25429 1 79 . 1 1 36 36 VAL C C 13 173.200 1 . 1 . . . A 36 VAL C . 25429 1 80 . 1 1 36 36 VAL CA C 13 58.900 1 . 1 . . . A 36 VAL CA . 25429 1 81 . 1 1 36 36 VAL CB C 13 32.800 1 . 1 . . . A 36 VAL CB . 25429 1 82 . 1 1 36 36 VAL N N 15 124.360 1 . 1 . . . A 36 VAL N . 25429 1 83 . 1 1 37 37 GLY C C 13 170.500 1 . 1 . . . A 37 GLY C . 25429 1 84 . 1 1 37 37 GLY CA C 13 43.600 1 . 1 . . . A 37 GLY CA . 25429 1 85 . 1 1 37 37 GLY N N 15 116.240 1 . 1 . . . A 37 GLY N . 25429 1 86 . 1 1 38 38 GLY C C 13 171.500 1 . 1 . . . A 38 GLY C . 25429 1 87 . 1 1 38 38 GLY CA C 13 46.800 1 . 1 . . . A 38 GLY CA . 25429 1 88 . 1 1 38 38 GLY N N 15 113.600 1 . 1 . . . A 38 GLY N . 25429 1 89 . 1 1 39 39 VAL C C 13 171.900 1 . 1 . . . A 39 VAL C . 25429 1 90 . 1 1 39 39 VAL CA C 13 58.300 1 . 1 . . . A 39 VAL CA . 25429 1 91 . 1 1 39 39 VAL CB C 13 34.000 1 . 1 . . . A 39 VAL CB . 25429 1 92 . 1 1 39 39 VAL N N 15 120.300 1 . 1 . . . A 39 VAL N . 25429 1 93 . 1 1 40 40 VAL C C 13 171.800 1 . 1 . . . A 40 VAL C . 25429 1 94 . 1 1 40 40 VAL CA C 13 59.100 1 . 1 . . . A 40 VAL CA . 25429 1 95 . 1 1 40 40 VAL CB C 13 33.300 1 . 1 . . . A 40 VAL CB . 25429 1 96 . 1 1 40 40 VAL N N 15 127.600 1 . 1 . . . A 40 VAL N . 25429 1 97 . 1 1 41 41 ILE C C 13 171.200 1 . 1 . . . A 41 ILE C . 25429 1 98 . 1 1 41 41 ILE CA C 13 58.300 1 . 1 . . . A 41 ILE CA . 25429 1 99 . 1 1 41 41 ILE CB C 13 37.800 1 . 1 . . . A 41 ILE CB . 25429 1 100 . 1 1 41 41 ILE N N 15 128.600 1 . 1 . . . A 41 ILE N . 25429 1 101 . 1 1 42 42 ALA C C 13 180.000 1 . 1 . . . A 42 ALA C . 25429 1 102 . 1 1 42 42 ALA CA C 13 50.800 1 . 1 . . . A 42 ALA CA . 25429 1 103 . 1 1 42 42 ALA CB C 13 19.300 1 . 1 . . . A 42 ALA CB . 25429 1 stop_ save_