data_25218 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25218 _Entry.Title ; Chemical shifts of amyloid beta (1-42) peptide in aqueous solution ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-09-11 _Entry.Accession_date 2014-09-11 _Entry.Last_release_date 2015-03-17 _Entry.Original_release_date 2015-03-17 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Marielle Walti . A. . 25218 2 Julien Orts . . . 25218 3 Beat Vogeli . . . 25218 4 Silvia Campioni . . . 25218 5 Roland Riek . . . 25218 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25218 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 78 25218 '15N chemical shifts' 42 25218 '1H chemical shifts' 242 25218 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2015-03-17 2014-09-11 original author . 25218 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25218 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 25676345 _Citation.Full_citation . _Citation.Title 'Solution NMR Studies of Recombinant Abeta(1-42): From the Presence of a Micellar Entity to Residual Beta-Sheet Structure in the Soluble Species' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Chembiochem. _Citation.Journal_name_full . _Citation.Journal_volume 16 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 659 _Citation.Page_last 669 _Citation.Year 2015 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Marielle Walti . A. . 25218 1 2 Julien Orts . . . 25218 1 3 Beat Vogeli . . . 25218 1 4 Silvia Campioni . . . 25218 1 5 Roland Riek . . . 25218 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25218 _Assembly.ID 1 _Assembly.Name 'amyloid beta' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 entity 1 $entity A . yes native no no . . . 25218 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 25218 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name amyloid_peptide _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 42 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25218 1 3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 4 no BMRB 17186 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 5 no BMRB 17764 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 6 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 7 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 8 no BMRB 17795 . Abeta(1-40) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 9 no BMRB 17796 . Abeta40 . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 88.10 38 100.00 100.00 2.61e-16 . . . . 25218 1 11 no BMRB 18127 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 12 no BMRB 18128 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 13 no BMRB 18129 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 14 no BMRB 18131 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 15 no BMRB 19009 . beta-amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 16 no BMRB 19309 . amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 17 no BMRB 19393 . Abeta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25218 1 18 no BMRB 25289 . amyloid_beta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25218 1 19 no BMRB 25429 . entity . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 20 no BMRB 26508 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 21 no BMRB 26516 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 22 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25218 1 23 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25218 1 24 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 25 no PDB 1BA4 . "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 26 no PDB 1BA6 . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 95.24 40 97.50 97.50 1.43e-17 . . . . 25218 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 61.90 26 100.00 100.00 2.00e-08 . . . . 25218 1 28 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 29 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 31 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 32 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 33 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 34 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 35 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 36 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 95.24 40 97.50 100.00 4.61e-18 . . . . 25218 1 38 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25218 1 39 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 40 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 41 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 42 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25218 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 44 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 45 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 46 no PDB 3BAE . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25218 1 47 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 48 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25218 1 49 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 50 no PDB 4MVI . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 51 no PDB 4MVL . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 52 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 53 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25218 1 54 no PDB 5AEF . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" . . . . . 66.67 28 100.00 100.00 2.69e-08 . . . . 25218 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.62 100.00 9.73e-20 . . . . 25218 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 8.24e-20 . . . . 25218 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 1.94e-20 . . . . 25218 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25218 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25218 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.24 97 100.00 100.00 1.03e-18 . . . . 25218 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 71.43 30 100.00 100.00 9.95e-12 . . . . 25218 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25218 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 9.55e-20 . . . . 25218 1 70 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25218 1 71 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25218 1 72 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25218 1 73 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25218 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 2.05e-20 . . . . 25218 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25218 1 77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25218 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25218 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 2.04e-19 . . . . 25218 1 80 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 81 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 85 no SP P05067 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 86 no SP P53601 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 87 no SP P79307 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25218 1 88 no SP P86906 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 95.24 40 97.50 100.00 5.31e-18 . . . . 25218 1 89 no SP Q28053 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 59 100.00 100.00 1.94e-20 . . . . 25218 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25218 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ASP . 25218 1 2 . ALA . 25218 1 3 . GLU . 25218 1 4 . PHE . 25218 1 5 . ARG . 25218 1 6 . HIS . 25218 1 7 . ASP . 25218 1 8 . SER . 25218 1 9 . GLY . 25218 1 10 . TYR . 25218 1 11 . GLU . 25218 1 12 . VAL . 25218 1 13 . HIS . 25218 1 14 . HIS . 25218 1 15 . GLN . 25218 1 16 . LYS . 25218 1 17 . LEU . 25218 1 18 . VAL . 25218 1 19 . PHE . 25218 1 20 . PHE . 25218 1 21 . ALA . 25218 1 22 . GLU . 25218 1 23 . ASP . 25218 1 24 . VAL . 25218 1 25 . GLY . 25218 1 26 . SER . 25218 1 27 . ASN . 25218 1 28 . LYS . 25218 1 29 . GLY . 25218 1 30 . ALA . 25218 1 31 . ILE . 25218 1 32 . ILE . 25218 1 33 . GLY . 25218 1 34 . LEU . 25218 1 35 . MET . 25218 1 36 . VAL . 25218 1 37 . GLY . 25218 1 38 . GLY . 25218 1 39 . VAL . 25218 1 40 . VAL . 25218 1 41 . ILE . 25218 1 42 . ALA . 25218 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ASP 1 1 25218 1 . ALA 2 2 25218 1 . GLU 3 3 25218 1 . PHE 4 4 25218 1 . ARG 5 5 25218 1 . HIS 6 6 25218 1 . ASP 7 7 25218 1 . SER 8 8 25218 1 . GLY 9 9 25218 1 . TYR 10 10 25218 1 . GLU 11 11 25218 1 . VAL 12 12 25218 1 . HIS 13 13 25218 1 . HIS 14 14 25218 1 . GLN 15 15 25218 1 . LYS 16 16 25218 1 . LEU 17 17 25218 1 . VAL 18 18 25218 1 . PHE 19 19 25218 1 . PHE 20 20 25218 1 . ALA 21 21 25218 1 . GLU 22 22 25218 1 . ASP 23 23 25218 1 . VAL 24 24 25218 1 . GLY 25 25 25218 1 . SER 26 26 25218 1 . ASN 27 27 25218 1 . LYS 28 28 25218 1 . GLY 29 29 25218 1 . ALA 30 30 25218 1 . ILE 31 31 25218 1 . ILE 32 32 25218 1 . GLY 33 33 25218 1 . LEU 34 34 25218 1 . MET 35 35 25218 1 . VAL 36 36 25218 1 . GLY 37 37 25218 1 . GLY 38 38 25218 1 . VAL 39 39 25218 1 . VAL 40 40 25218 1 . ILE 41 41 25218 1 . ALA 42 42 25218 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 25218 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 25218 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 25218 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pRSET . . . . . . 25218 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25218 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 amyloid_peptide '[U-13C; U-15N]' . . 1 $entity . . . 0.5 0.7 mM . . . . 25218 1 2 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25218 1 3 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25218 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 25218 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID temperature 273 . K 25218 1 pH 7.4 . pH 25218 1 pressure 1 . atm 25218 1 'ionic strength' 20 . mM 25218 1 stop_ save_ ############################ # Computer software used # ############################ save_ccpNMR _Software.Sf_category software _Software.Sf_framecode ccpNMR _Software.Entry_ID 25218 _Software.ID 1 _Software.Name ccpNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 25218 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25218 1 'peak picking' 25218 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 25218 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 25218 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 . . . 25218 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 25218 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 3 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 4 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 5 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 6 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 8 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 9 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 10 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25218 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 25218 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 25218 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 25218 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 25218 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 25218 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D HNCA' . . . 25218 1 2 '3D HNCACB' . . . 25218 1 3 '3D HN(CO)CA' . . . 25218 1 4 '2D 1H-15N HSQC' . . . 25218 1 5 '2D 1H-1H TOCSY' . . . 25218 1 6 '2D 1H-1H NOESY' . . . 25218 1 7 '3D 1H-15N NOESY' . . . 25218 1 8 '3D 1H-15N TOCSY' . . . 25218 1 9 '3D 1H-13C NOESY aliphatic' . . . 25218 1 10 '3D HCCH-TOCSY' . . . 25218 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ASP CA C 13 53.036 0.400 . 1 . . . . 1 ASP CA . 25218 1 2 . 1 1 1 1 ASP CB C 13 38.622 0.400 . 1 . . . . 1 ASP CB . 25218 1 3 . 1 1 1 1 ASP N N 15 117.609 0.400 . 1 . . . . 1 ASP N . 25218 1 4 . 1 1 2 2 ALA H H 1 7.958 0.020 . 1 . . . . 2 ALA H . 25218 1 5 . 1 1 2 2 ALA HA H 1 4.161 0.020 . 1 . . . . 2 ALA HA . 25218 1 6 . 1 1 2 2 ALA HB1 H 1 1.267 0.020 . 1 . . . . 2 ALA HB1 . 25218 1 7 . 1 1 2 2 ALA HB2 H 1 1.267 0.020 . 1 . . . . 2 ALA HB2 . 25218 1 8 . 1 1 2 2 ALA HB3 H 1 1.267 0.020 . 1 . . . . 2 ALA HB3 . 25218 1 9 . 1 1 2 2 ALA CA C 13 52.400 0.400 . 1 . . . . 2 ALA CA . 25218 1 10 . 1 1 2 2 ALA CB C 13 19.112 0.400 . 1 . . . . 2 ALA CB . 25218 1 11 . 1 1 2 2 ALA N N 15 123.781 0.400 . 1 . . . . 2 ALA N . 25218 1 12 . 1 1 3 3 GLU H H 1 8.459 0.020 . 1 . . . . 3 GLU H . 25218 1 13 . 1 1 3 3 GLU HA H 1 4.073 0.020 . 1 . . . . 3 GLU HA . 25218 1 14 . 1 1 3 3 GLU HB2 H 1 1.801 0.020 . 2 . . . . 3 GLU HB2 . 25218 1 15 . 1 1 3 3 GLU HB3 H 1 2.002 0.020 . 2 . . . . 3 GLU HB3 . 25218 1 16 . 1 1 3 3 GLU HG2 H 1 2.108 0.020 . 2 . . . . 3 GLU HG2 . 25218 1 17 . 1 1 3 3 GLU HG3 H 1 2.108 0.020 . 2 . . . . 3 GLU HG3 . 25218 1 18 . 1 1 3 3 GLU CA C 13 56.497 0.400 . 1 . . . . 3 GLU CA . 25218 1 19 . 1 1 3 3 GLU CB C 13 30.199 0.400 . 1 . . . . 3 GLU CB . 25218 1 20 . 1 1 3 3 GLU N N 15 120.309 0.400 . 1 . . . . 3 GLU N . 25218 1 21 . 1 1 4 4 PHE H H 1 8.299 0.020 . 1 . . . . 4 PHE H . 25218 1 22 . 1 1 4 4 PHE HA H 1 4.438 0.020 . 1 . . . . 4 PHE HA . 25218 1 23 . 1 1 4 4 PHE HB2 H 1 2.895 0.020 . 2 . . . . 4 PHE HB2 . 25218 1 24 . 1 1 4 4 PHE HB3 H 1 2.895 0.020 . 2 . . . . 4 PHE HB3 . 25218 1 25 . 1 1 4 4 PHE CA C 13 57.630 0.400 . 1 . . . . 4 PHE CA . 25218 1 26 . 1 1 4 4 PHE CB C 13 39.487 0.400 . 1 . . . . 4 PHE CB . 25218 1 27 . 1 1 4 4 PHE N N 15 121.733 0.400 . 1 . . . . 4 PHE N . 25218 1 28 . 1 1 5 5 ARG H H 1 8.112 0.020 . 1 . . . . 5 ARG H . 25218 1 29 . 1 1 5 5 ARG HA H 1 4.162 0.020 . 1 . . . . 5 ARG HA . 25218 1 30 . 1 1 5 5 ARG HB2 H 1 1.620 0.020 . 2 . . . . 5 ARG HB2 . 25218 1 31 . 1 1 5 5 ARG HB3 H 1 1.511 0.020 . 2 . . . . 5 ARG HB3 . 25218 1 32 . 1 1 5 5 ARG HG2 H 1 1.380 0.020 . 2 . . . . 5 ARG HG2 . 25218 1 33 . 1 1 5 5 ARG HG3 H 1 1.380 0.020 . 2 . . . . 5 ARG HG3 . 25218 1 34 . 1 1 5 5 ARG HD2 H 1 3.011 0.020 . 2 . . . . 5 ARG HD2 . 25218 1 35 . 1 1 5 5 ARG HD3 H 1 3.011 0.020 . 2 . . . . 5 ARG HD3 . 25218 1 36 . 1 1 5 5 ARG CA C 13 55.312 0.400 . 1 . . . . 5 ARG CA . 25218 1 37 . 1 1 5 5 ARG CB C 13 31.109 0.400 . 1 . . . . 5 ARG CB . 25218 1 38 . 1 1 5 5 ARG N N 15 123.861 0.400 . 1 . . . . 5 ARG N . 25218 1 39 . 1 1 6 6 HIS H H 1 8.379 0.020 . 1 . . . . 6 HIS H . 25218 1 40 . 1 1 6 6 HIS HA H 1 4.401 0.020 . 1 . . . . 6 HIS HA . 25218 1 41 . 1 1 6 6 HIS HB2 H 1 2.923 0.020 . 2 . . . . 6 HIS HB2 . 25218 1 42 . 1 1 6 6 HIS HB3 H 1 2.923 0.020 . 2 . . . . 6 HIS HB3 . 25218 1 43 . 1 1 6 6 HIS CA C 13 56.478 0.400 . 1 . . . . 6 HIS CA . 25218 1 44 . 1 1 6 6 HIS CB C 13 30.743 0.400 . 1 . . . . 6 HIS CB . 25218 1 45 . 1 1 6 6 HIS N N 15 122.416 0.400 . 1 . . . . 6 HIS N . 25218 1 46 . 1 1 7 7 ASP H H 1 8.332 0.020 . 1 . . . . 7 ASP H . 25218 1 47 . 1 1 7 7 ASP HA H 1 4.509 0.020 . 1 . . . . 7 ASP HA . 25218 1 48 . 1 1 7 7 ASP HB2 H 1 2.558 0.020 . 2 . . . . 7 ASP HB2 . 25218 1 49 . 1 1 7 7 ASP HB3 H 1 2.558 0.020 . 2 . . . . 7 ASP HB3 . 25218 1 50 . 1 1 7 7 ASP CA C 13 53.908 0.400 . 1 . . . . 7 ASP CA . 25218 1 51 . 1 1 7 7 ASP CB C 13 40.970 0.400 . 1 . . . . 7 ASP CB . 25218 1 52 . 1 1 7 7 ASP N N 15 121.615 0.400 . 1 . . . . 7 ASP N . 25218 1 53 . 1 1 8 8 SER H H 1 8.406 0.020 . 1 . . . . 8 SER H . 25218 1 54 . 1 1 8 8 SER HA H 1 4.268 0.020 . 1 . . . . 8 SER HA . 25218 1 55 . 1 1 8 8 SER HB2 H 1 3.770 0.020 . 2 . . . . 8 SER HB2 . 25218 1 56 . 1 1 8 8 SER HB3 H 1 3.789 0.020 . 2 . . . . 8 SER HB3 . 25218 1 57 . 1 1 8 8 SER CA C 13 58.890 0.400 . 1 . . . . 8 SER CA . 25218 1 58 . 1 1 8 8 SER CB C 13 63.605 0.400 . 1 . . . . 8 SER CB . 25218 1 59 . 1 1 8 8 SER N N 15 116.526 0.400 . 1 . . . . 8 SER N . 25218 1 60 . 1 1 9 9 GLY H H 1 8.525 0.020 . 1 . . . . 9 GLY H . 25218 1 61 . 1 1 9 9 GLY HA3 H 1 3.781 0.020 . 2 . . . . 9 GLY HA3 . 25218 1 62 . 1 1 9 9 GLY CA C 13 45.087 0.400 . 1 . . . . 9 GLY CA . 25218 1 63 . 1 1 9 9 GLY N N 15 110.656 0.400 . 1 . . . . 9 GLY N . 25218 1 64 . 1 1 10 10 TYR H H 1 7.931 0.020 . 1 . . . . 10 TYR H . 25218 1 65 . 1 1 10 10 TYR HA H 1 4.413 0.020 . 1 . . . . 10 TYR HA . 25218 1 66 . 1 1 10 10 TYR HB2 H 1 2.919 0.020 . 2 . . . . 10 TYR HB2 . 25218 1 67 . 1 1 10 10 TYR HB3 H 1 2.842 0.020 . 2 . . . . 10 TYR HB3 . 25218 1 68 . 1 1 10 10 TYR CA C 13 58.005 0.400 . 1 . . . . 10 TYR CA . 25218 1 69 . 1 1 10 10 TYR CB C 13 38.722 0.400 . 1 . . . . 10 TYR CB . 25218 1 70 . 1 1 10 10 TYR N N 15 119.973 0.400 . 1 . . . . 10 TYR N . 25218 1 71 . 1 1 11 11 GLU H H 1 8.378 0.020 . 1 . . . . 11 GLU H . 25218 1 72 . 1 1 11 11 GLU HA H 1 4.087 0.020 . 1 . . . . 11 GLU HA . 25218 1 73 . 1 1 11 11 GLU HB2 H 1 1.721 0.020 . 2 . . . . 11 GLU HB2 . 25218 1 74 . 1 1 11 11 GLU HB3 H 1 1.721 0.020 . 2 . . . . 11 GLU HB3 . 25218 1 75 . 1 1 11 11 GLU HG2 H 1 2.075 0.020 . 2 . . . . 11 GLU HG2 . 25218 1 76 . 1 1 11 11 GLU HG3 H 1 2.075 0.020 . 2 . . . . 11 GLU HG3 . 25218 1 77 . 1 1 11 11 GLU CA C 13 56.468 0.400 . 1 . . . . 11 GLU CA . 25218 1 78 . 1 1 11 11 GLU CB C 13 30.260 0.400 . 1 . . . . 11 GLU CB . 25218 1 79 . 1 1 11 11 GLU N N 15 122.553 0.400 . 1 . . . . 11 GLU N . 25218 1 80 . 1 1 12 12 VAL H H 1 8.083 0.020 . 1 . . . . 12 VAL H . 25218 1 81 . 1 1 12 12 VAL HA H 1 3.825 0.020 . 1 . . . . 12 VAL HA . 25218 1 82 . 1 1 12 12 VAL HB H 1 1.830 0.020 . 1 . . . . 12 VAL HB . 25218 1 83 . 1 1 12 12 VAL HG11 H 1 0.669 0.020 . 2 . . . . 12 VAL HG11 . 25218 1 84 . 1 1 12 12 VAL HG12 H 1 0.669 0.020 . 2 . . . . 12 VAL HG12 . 25218 1 85 . 1 1 12 12 VAL HG13 H 1 0.669 0.020 . 2 . . . . 12 VAL HG13 . 25218 1 86 . 1 1 12 12 VAL HG21 H 1 0.757 0.020 . 2 . . . . 12 VAL HG21 . 25218 1 87 . 1 1 12 12 VAL HG22 H 1 0.757 0.020 . 2 . . . . 12 VAL HG22 . 25218 1 88 . 1 1 12 12 VAL HG23 H 1 0.757 0.020 . 2 . . . . 12 VAL HG23 . 25218 1 89 . 1 1 12 12 VAL CA C 13 62.786 0.400 . 1 . . . . 12 VAL CA . 25218 1 90 . 1 1 12 12 VAL CB C 13 32.485 0.400 . 1 . . . . 12 VAL CB . 25218 1 91 . 1 1 12 12 VAL N N 15 121.135 0.400 . 1 . . . . 12 VAL N . 25218 1 92 . 1 1 13 13 HIS H H 1 8.246 0.020 . 1 . . . . 13 HIS H . 25218 1 93 . 1 1 13 13 HIS HA H 1 4.475 0.020 . 1 . . . . 13 HIS HA . 25218 1 94 . 1 1 13 13 HIS HB2 H 1 2.903 0.020 . 2 . . . . 13 HIS HB2 . 25218 1 95 . 1 1 13 13 HIS HB3 H 1 2.910 0.020 . 2 . . . . 13 HIS HB3 . 25218 1 96 . 1 1 13 13 HIS CA C 13 56.193 0.400 . 1 . . . . 13 HIS CA . 25218 1 97 . 1 1 13 13 HIS CB C 13 30.727 0.400 . 1 . . . . 13 HIS CB . 25218 1 98 . 1 1 13 13 HIS N N 15 122.697 0.400 . 1 . . . . 13 HIS N . 25218 1 99 . 1 1 14 14 HIS H H 1 8.142 0.020 . 1 . . . . 14 HIS H . 25218 1 100 . 1 1 14 14 HIS HA H 1 4.426 0.020 . 1 . . . . 14 HIS HA . 25218 1 101 . 1 1 14 14 HIS HB2 H 1 2.899 0.020 . 2 . . . . 14 HIS HB2 . 25218 1 102 . 1 1 14 14 HIS HB3 H 1 2.972 0.020 . 2 . . . . 14 HIS HB3 . 25218 1 103 . 1 1 14 14 HIS CA C 13 56.489 0.400 . 1 . . . . 14 HIS CA . 25218 1 104 . 1 1 14 14 HIS CB C 13 30.697 0.400 . 1 . . . . 14 HIS CB . 25218 1 105 . 1 1 14 14 HIS N N 15 121.248 0.400 . 1 . . . . 14 HIS N . 25218 1 106 . 1 1 15 15 GLN H H 1 8.376 0.020 . 1 . . . . 15 GLN H . 25218 1 107 . 1 1 15 15 GLN HA H 1 4.150 0.020 . 1 . . . . 15 GLN HA . 25218 1 108 . 1 1 15 15 GLN HB2 H 1 1.861 0.020 . 2 . . . . 15 GLN HB2 . 25218 1 109 . 1 1 15 15 GLN HB3 H 1 1.950 0.020 . 2 . . . . 15 GLN HB3 . 25218 1 110 . 1 1 15 15 GLN HG2 H 1 2.215 0.020 . 2 . . . . 15 GLN HG2 . 25218 1 111 . 1 1 15 15 GLN HG3 H 1 2.215 0.020 . 2 . . . . 15 GLN HG3 . 25218 1 112 . 1 1 15 15 GLN CA C 13 55.883 0.400 . 1 . . . . 15 GLN CA . 25218 1 113 . 1 1 15 15 GLN CB C 13 29.386 0.400 . 1 . . . . 15 GLN CB . 25218 1 114 . 1 1 15 15 GLN N N 15 121.474 0.400 . 1 . . . . 15 GLN N . 25218 1 115 . 1 1 16 16 LYS H H 1 8.381 0.020 . 1 . . . . 16 LYS H . 25218 1 116 . 1 1 16 16 LYS HA H 1 4.157 0.020 . 1 . . . . 16 LYS HA . 25218 1 117 . 1 1 16 16 LYS HB2 H 1 1.653 0.020 . 2 . . . . 16 LYS HB2 . 25218 1 118 . 1 1 16 16 LYS HB3 H 1 1.690 0.020 . 2 . . . . 16 LYS HB3 . 25218 1 119 . 1 1 16 16 LYS HG2 H 1 1.277 0.020 . 2 . . . . 16 LYS HG2 . 25218 1 120 . 1 1 16 16 LYS HG3 H 1 1.340 0.020 . 2 . . . . 16 LYS HG3 . 25218 1 121 . 1 1 16 16 LYS CA C 13 56.177 0.400 . 1 . . . . 16 LYS CA . 25218 1 122 . 1 1 16 16 LYS CB C 13 32.691 0.400 . 1 . . . . 16 LYS CB . 25218 1 123 . 1 1 16 16 LYS N N 15 122.806 0.400 . 1 . . . . 16 LYS N . 25218 1 124 . 1 1 17 17 LEU H H 1 8.257 0.020 . 1 . . . . 17 LEU H . 25218 1 125 . 1 1 17 17 LEU HA H 1 4.215 0.020 . 1 . . . . 17 LEU HA . 25218 1 126 . 1 1 17 17 LEU HB2 H 1 1.496 0.020 . 2 . . . . 17 LEU HB2 . 25218 1 127 . 1 1 17 17 LEU HB3 H 1 1.496 0.020 . 2 . . . . 17 LEU HB3 . 25218 1 128 . 1 1 17 17 LEU HG H 1 1.338 0.020 . 1 . . . . 17 LEU HG . 25218 1 129 . 1 1 17 17 LEU HD11 H 1 0.811 0.020 . 2 . . . . 17 LEU HD11 . 25218 1 130 . 1 1 17 17 LEU HD12 H 1 0.811 0.020 . 2 . . . . 17 LEU HD12 . 25218 1 131 . 1 1 17 17 LEU HD13 H 1 0.811 0.020 . 2 . . . . 17 LEU HD13 . 25218 1 132 . 1 1 17 17 LEU HD21 H 1 0.744 0.020 . 2 . . . . 17 LEU HD21 . 25218 1 133 . 1 1 17 17 LEU HD22 H 1 0.744 0.020 . 2 . . . . 17 LEU HD22 . 25218 1 134 . 1 1 17 17 LEU HD23 H 1 0.744 0.020 . 2 . . . . 17 LEU HD23 . 25218 1 135 . 1 1 17 17 LEU CA C 13 55.129 0.400 . 1 . . . . 17 LEU CA . 25218 1 136 . 1 1 17 17 LEU CB C 13 42.348 0.400 . 1 . . . . 17 LEU CB . 25218 1 137 . 1 1 17 17 LEU N N 15 123.881 0.400 . 1 . . . . 17 LEU N . 25218 1 138 . 1 1 18 18 VAL H H 1 8.002 0.020 . 1 . . . . 18 VAL H . 25218 1 139 . 1 1 18 18 VAL HA H 1 3.920 0.020 . 1 . . . . 18 VAL HA . 25218 1 140 . 1 1 18 18 VAL HB H 1 1.795 0.020 . 1 . . . . 18 VAL HB . 25218 1 141 . 1 1 18 18 VAL HG11 H 1 0.643 0.020 . 2 . . . . 18 VAL HG11 . 25218 1 142 . 1 1 18 18 VAL HG12 H 1 0.643 0.020 . 2 . . . . 18 VAL HG12 . 25218 1 143 . 1 1 18 18 VAL HG13 H 1 0.643 0.020 . 2 . . . . 18 VAL HG13 . 25218 1 144 . 1 1 18 18 VAL HG21 H 1 0.734 0.020 . 2 . . . . 18 VAL HG21 . 25218 1 145 . 1 1 18 18 VAL HG22 H 1 0.734 0.020 . 2 . . . . 18 VAL HG22 . 25218 1 146 . 1 1 18 18 VAL HG23 H 1 0.734 0.020 . 2 . . . . 18 VAL HG23 . 25218 1 147 . 1 1 18 18 VAL CA C 13 61.860 0.400 . 1 . . . . 18 VAL CA . 25218 1 148 . 1 1 18 18 VAL CB C 13 33.008 0.400 . 1 . . . . 18 VAL CB . 25218 1 149 . 1 1 18 18 VAL N N 15 121.466 0.400 . 1 . . . . 18 VAL N . 25218 1 150 . 1 1 19 19 PHE H H 1 8.266 0.020 . 1 . . . . 19 PHE H . 25218 1 151 . 1 1 19 19 PHE HA H 1 4.471 0.020 . 1 . . . . 19 PHE HA . 25218 1 152 . 1 1 19 19 PHE HB2 H 1 2.874 0.020 . 2 . . . . 19 PHE HB2 . 25218 1 153 . 1 1 19 19 PHE HB3 H 1 2.817 0.020 . 2 . . . . 19 PHE HB3 . 25218 1 154 . 1 1 19 19 PHE CA C 13 57.284 0.400 . 1 . . . . 19 PHE CA . 25218 1 155 . 1 1 19 19 PHE CB C 13 40.024 0.400 . 1 . . . . 19 PHE CB . 25218 1 156 . 1 1 19 19 PHE N N 15 124.337 0.400 . 1 . . . . 19 PHE N . 25218 1 157 . 1 1 20 20 PHE H H 1 8.240 0.020 . 1 . . . . 20 PHE H . 25218 1 158 . 1 1 20 20 PHE HA H 1 4.467 0.020 . 1 . . . . 20 PHE HA . 25218 1 159 . 1 1 20 20 PHE HB2 H 1 2.969 0.020 . 2 . . . . 20 PHE HB2 . 25218 1 160 . 1 1 20 20 PHE HB3 H 1 2.822 0.020 . 2 . . . . 20 PHE HB3 . 25218 1 161 . 1 1 20 20 PHE CA C 13 57.240 0.400 . 1 . . . . 20 PHE CA . 25218 1 162 . 1 1 20 20 PHE CB C 13 40.030 0.400 . 1 . . . . 20 PHE CB . 25218 1 163 . 1 1 20 20 PHE N N 15 122.962 0.400 . 1 . . . . 20 PHE N . 25218 1 164 . 1 1 21 21 ALA H H 1 8.250 0.020 . 1 . . . . 21 ALA H . 25218 1 165 . 1 1 21 21 ALA HA H 1 4.114 0.020 . 1 . . . . 21 ALA HA . 25218 1 166 . 1 1 21 21 ALA HB1 H 1 1.262 0.020 . 1 . . . . 21 ALA HB1 . 25218 1 167 . 1 1 21 21 ALA HB2 H 1 1.262 0.020 . 1 . . . . 21 ALA HB2 . 25218 1 168 . 1 1 21 21 ALA HB3 H 1 1.262 0.020 . 1 . . . . 21 ALA HB3 . 25218 1 169 . 1 1 21 21 ALA CA C 13 52.257 0.400 . 1 . . . . 21 ALA CA . 25218 1 170 . 1 1 21 21 ALA CB C 13 19.266 0.400 . 1 . . . . 21 ALA CB . 25218 1 171 . 1 1 21 21 ALA N N 15 126.210 0.400 . 1 . . . . 21 ALA N . 25218 1 172 . 1 1 22 22 GLU H H 1 8.365 0.020 . 1 . . . . 22 GLU H . 25218 1 173 . 1 1 22 22 GLU HA H 1 4.090 0.020 . 1 . . . . 22 GLU HA . 25218 1 174 . 1 1 22 22 GLU HB2 H 1 1.931 0.020 . 2 . . . . 22 GLU HB2 . 25218 1 175 . 1 1 22 22 GLU HB3 H 1 1.814 0.020 . 2 . . . . 22 GLU HB3 . 25218 1 176 . 1 1 22 22 GLU HG2 H 1 2.167 0.020 . 2 . . . . 22 GLU HG2 . 25218 1 177 . 1 1 22 22 GLU HG3 H 1 2.167 0.020 . 2 . . . . 22 GLU HG3 . 25218 1 178 . 1 1 22 22 GLU CA C 13 56.482 0.400 . 1 . . . . 22 GLU CA . 25218 1 179 . 1 1 22 22 GLU CB C 13 30.240 0.400 . 1 . . . . 22 GLU CB . 25218 1 180 . 1 1 22 22 GLU N N 15 119.907 0.400 . 1 . . . . 22 GLU N . 25218 1 181 . 1 1 23 23 ASP H H 1 8.430 0.020 . 1 . . . . 23 ASP H . 25218 1 182 . 1 1 23 23 ASP HA H 1 4.534 0.020 . 1 . . . . 23 ASP HA . 25218 1 183 . 1 1 23 23 ASP HB2 H 1 2.533 0.020 . 2 . . . . 23 ASP HB2 . 25218 1 184 . 1 1 23 23 ASP HB3 H 1 2.641 0.020 . 2 . . . . 23 ASP HB3 . 25218 1 185 . 1 1 23 23 ASP CA C 13 54.008 0.400 . 1 . . . . 23 ASP CA . 25218 1 186 . 1 1 23 23 ASP CB C 13 40.949 0.400 . 1 . . . . 23 ASP CB . 25218 1 187 . 1 1 23 23 ASP N N 15 121.769 0.400 . 1 . . . . 23 ASP N . 25218 1 188 . 1 1 24 24 VAL H H 1 8.168 0.020 . 1 . . . . 24 VAL H . 25218 1 189 . 1 1 24 24 VAL HA H 1 4.027 0.020 . 1 . . . . 24 VAL HA . 25218 1 190 . 1 1 24 24 VAL HB H 1 2.084 0.020 . 1 . . . . 24 VAL HB . 25218 1 191 . 1 1 24 24 VAL HG11 H 1 0.850 0.020 . 2 . . . . 24 VAL HG1 . 25218 1 192 . 1 1 24 24 VAL HG12 H 1 0.850 0.020 . 2 . . . . 24 VAL HG1 . 25218 1 193 . 1 1 24 24 VAL HG13 H 1 0.850 0.020 . 2 . . . . 24 VAL HG1 . 25218 1 194 . 1 1 24 24 VAL HG21 H 1 0.850 0.020 . 2 . . . . 24 VAL HG2 . 25218 1 195 . 1 1 24 24 VAL HG22 H 1 0.850 0.020 . 2 . . . . 24 VAL HG2 . 25218 1 196 . 1 1 24 24 VAL HG23 H 1 0.850 0.020 . 2 . . . . 24 VAL HG2 . 25218 1 197 . 1 1 24 24 VAL CA C 13 62.644 0.400 . 1 . . . . 24 VAL CA . 25218 1 198 . 1 1 24 24 VAL CB C 13 32.069 0.400 . 1 . . . . 24 VAL CB . 25218 1 199 . 1 1 24 24 VAL N N 15 120.648 0.400 . 1 . . . . 24 VAL N . 25218 1 200 . 1 1 25 25 GLY H H 1 8.555 0.020 . 1 . . . . 25 GLY H . 25218 1 201 . 1 1 25 25 GLY HA2 H 1 3.866 0.020 . 2 . . . . 25 GLY HA2 . 25218 1 202 . 1 1 25 25 GLY HA3 H 1 3.866 0.020 . 2 . . . . 25 GLY HA3 . 25218 1 203 . 1 1 25 25 GLY CA C 13 45.241 0.400 . 1 . . . . 25 GLY CA . 25218 1 204 . 1 1 25 25 GLY N N 15 111.702 0.400 . 1 . . . . 25 GLY N . 25218 1 205 . 1 1 26 26 SER H H 1 8.148 0.020 . 1 . . . . 26 SER H . 25218 1 206 . 1 1 26 26 SER HA H 1 4.312 0.020 . 1 . . . . 26 SER HA . 25218 1 207 . 1 1 26 26 SER HB2 H 1 3.786 0.020 . 2 . . . . 26 SER HB2 . 25218 1 208 . 1 1 26 26 SER HB3 H 1 3.786 0.020 . 2 . . . . 26 SER HB3 . 25218 1 209 . 1 1 26 26 SER CA C 13 58.441 0.400 . 1 . . . . 26 SER CA . 25218 1 210 . 1 1 26 26 SER CB C 13 63.557 0.400 . 1 . . . . 26 SER CB . 25218 1 211 . 1 1 26 26 SER N N 15 115.416 0.400 . 1 . . . . 26 SER N . 25218 1 212 . 1 1 27 27 ASN H H 1 8.481 0.020 . 1 . . . . 27 ASN H . 25218 1 213 . 1 1 27 27 ASN HA H 1 4.308 0.020 . 1 . . . . 27 ASN HA . 25218 1 214 . 1 1 27 27 ASN HB2 H 1 2.764 0.020 . 2 . . . . 27 ASN HB2 . 25218 1 215 . 1 1 27 27 ASN HB3 H 1 2.705 0.020 . 2 . . . . 27 ASN HB3 . 25218 1 216 . 1 1 27 27 ASN CA C 13 53.166 0.400 . 1 . . . . 27 ASN CA . 25218 1 217 . 1 1 27 27 ASN CB C 13 38.418 0.400 . 1 . . . . 27 ASN CB . 25218 1 218 . 1 1 27 27 ASN N N 15 120.661 0.400 . 1 . . . . 27 ASN N . 25218 1 219 . 1 1 28 28 LYS H H 1 8.360 0.020 . 1 . . . . 28 LYS H . 25218 1 220 . 1 1 28 28 LYS HA H 1 4.161 0.020 . 1 . . . . 28 LYS HA . 25218 1 221 . 1 1 28 28 LYS HB2 H 1 1.779 0.020 . 2 . . . . 28 LYS HB2 . 25218 1 222 . 1 1 28 28 LYS HB3 H 1 1.669 0.020 . 2 . . . . 28 LYS HB3 . 25218 1 223 . 1 1 28 28 LYS HG2 H 1 1.334 0.020 . 2 . . . . 28 LYS HG2 . 25218 1 224 . 1 1 28 28 LYS HG3 H 1 1.334 0.020 . 2 . . . . 28 LYS HG3 . 25218 1 225 . 1 1 28 28 LYS HD2 H 1 1.311 0.020 . 2 . . . . 28 LYS HD2 . 25218 1 226 . 1 1 28 28 LYS HD3 H 1 1.311 0.020 . 2 . . . . 28 LYS HD3 . 25218 1 227 . 1 1 28 28 LYS CA C 13 56.456 0.400 . 1 . . . . 28 LYS CA . 25218 1 228 . 1 1 28 28 LYS CB C 13 32.523 0.400 . 1 . . . . 28 LYS CB . 25218 1 229 . 1 1 28 28 LYS N N 15 121.692 0.400 . 1 . . . . 28 LYS N . 25218 1 230 . 1 1 29 29 GLY H H 1 8.424 0.020 . 1 . . . . 29 GLY H . 25218 1 231 . 1 1 29 29 GLY HA2 H 1 3.819 0.020 . 2 . . . . 29 GLY HA2 . 25218 1 232 . 1 1 29 29 GLY HA3 H 1 3.819 0.020 . 2 . . . . 29 GLY HA3 . 25218 1 233 . 1 1 29 29 GLY CA C 13 45.034 0.400 . 1 . . . . 29 GLY CA . 25218 1 234 . 1 1 29 29 GLY N N 15 109.500 0.400 . 1 . . . . 29 GLY N . 25218 1 235 . 1 1 30 30 ALA H H 1 8.031 0.020 . 1 . . . . 30 ALA H . 25218 1 236 . 1 1 30 30 ALA HA H 1 4.194 0.020 . 1 . . . . 30 ALA HA . 25218 1 237 . 1 1 30 30 ALA HB1 H 1 1.262 0.020 . 1 . . . . 30 ALA HB1 . 25218 1 238 . 1 1 30 30 ALA HB2 H 1 1.262 0.020 . 1 . . . . 30 ALA HB2 . 25218 1 239 . 1 1 30 30 ALA HB3 H 1 1.262 0.020 . 1 . . . . 30 ALA HB3 . 25218 1 240 . 1 1 30 30 ALA CA C 13 52.379 0.400 . 1 . . . . 30 ALA CA . 25218 1 241 . 1 1 30 30 ALA CB C 13 19.339 0.400 . 1 . . . . 30 ALA CB . 25218 1 242 . 1 1 30 30 ALA N N 15 123.448 0.400 . 1 . . . . 30 ALA N . 25218 1 243 . 1 1 31 31 ILE H H 1 8.183 0.020 . 1 . . . . 31 ILE H . 25218 1 244 . 1 1 31 31 ILE HA H 1 4.045 0.020 . 1 . . . . 31 ILE HA . 25218 1 245 . 1 1 31 31 ILE HB H 1 1.756 0.020 . 1 . . . . 31 ILE HB . 25218 1 246 . 1 1 31 31 ILE HG12 H 1 1.400 0.020 . 2 . . . . 31 ILE HG12 . 25218 1 247 . 1 1 31 31 ILE HG13 H 1 1.095 0.020 . 2 . . . . 31 ILE HG13 . 25218 1 248 . 1 1 31 31 ILE HG21 H 1 0.814 0.020 . 1 . . . . 31 ILE HG21 . 25218 1 249 . 1 1 31 31 ILE HG22 H 1 0.814 0.020 . 1 . . . . 31 ILE HG22 . 25218 1 250 . 1 1 31 31 ILE HG23 H 1 0.814 0.020 . 1 . . . . 31 ILE HG23 . 25218 1 251 . 1 1 31 31 ILE HD11 H 1 0.771 0.020 . 1 . . . . 31 ILE HD11 . 25218 1 252 . 1 1 31 31 ILE HD12 H 1 0.771 0.020 . 1 . . . . 31 ILE HD12 . 25218 1 253 . 1 1 31 31 ILE HD13 H 1 0.771 0.020 . 1 . . . . 31 ILE HD13 . 25218 1 254 . 1 1 31 31 ILE CA C 13 60.988 0.400 . 1 . . . . 31 ILE CA . 25218 1 255 . 1 1 31 31 ILE CB C 13 38.310 0.400 . 1 . . . . 31 ILE CB . 25218 1 256 . 1 1 31 31 ILE N N 15 120.685 0.400 . 1 . . . . 31 ILE N . 25218 1 257 . 1 1 32 32 ILE H H 1 8.331 0.020 . 1 . . . . 32 ILE H . 25218 1 258 . 1 1 32 32 ILE HA H 1 4.045 0.020 . 1 . . . . 32 ILE HA . 25218 1 259 . 1 1 32 32 ILE HB H 1 1.756 0.020 . 1 . . . . 32 ILE HB . 25218 1 260 . 1 1 32 32 ILE HG12 H 1 1.395 0.020 . 2 . . . . 32 ILE HG12 . 25218 1 261 . 1 1 32 32 ILE HG13 H 1 1.395 0.020 . 2 . . . . 32 ILE HG13 . 25218 1 262 . 1 1 32 32 ILE HG21 H 1 1.102 0.020 . 1 . . . . 32 ILE HG21 . 25218 1 263 . 1 1 32 32 ILE HG22 H 1 1.102 0.020 . 1 . . . . 32 ILE HG22 . 25218 1 264 . 1 1 32 32 ILE HG23 H 1 1.102 0.020 . 1 . . . . 32 ILE HG23 . 25218 1 265 . 1 1 32 32 ILE HD11 H 1 0.772 0.020 . 1 . . . . 32 ILE HD11 . 25218 1 266 . 1 1 32 32 ILE HD12 H 1 0.772 0.020 . 1 . . . . 32 ILE HD12 . 25218 1 267 . 1 1 32 32 ILE HD13 H 1 0.772 0.020 . 1 . . . . 32 ILE HD13 . 25218 1 268 . 1 1 32 32 ILE CA C 13 61.005 0.400 . 1 . . . . 32 ILE CA . 25218 1 269 . 1 1 32 32 ILE CB C 13 38.319 0.400 . 1 . . . . 32 ILE CB . 25218 1 270 . 1 1 32 32 ILE N N 15 126.300 0.400 . 1 . . . . 32 ILE N . 25218 1 271 . 1 1 33 33 GLY H H 1 8.488 0.020 . 1 . . . . 33 GLY H . 25218 1 272 . 1 1 33 33 GLY HA2 H 1 3.824 0.020 . 2 . . . . 33 GLY HA2 . 25218 1 273 . 1 1 33 33 GLY HA3 H 1 3.824 0.020 . 2 . . . . 33 GLY HA3 . 25218 1 274 . 1 1 33 33 GLY CA C 13 45.022 0.400 . 1 . . . . 33 GLY CA . 25218 1 275 . 1 1 33 33 GLY N N 15 113.019 0.400 . 1 . . . . 33 GLY N . 25218 1 276 . 1 1 34 34 LEU H H 1 8.062 0.020 . 1 . . . . 34 LEU H . 25218 1 277 . 1 1 34 34 LEU HA H 1 4.244 0.020 . 1 . . . . 34 LEU HA . 25218 1 278 . 1 1 34 34 LEU HB2 H 1 1.503 0.020 . 2 . . . . 34 LEU HB2 . 25218 1 279 . 1 1 34 34 LEU HB3 H 1 1.492 0.020 . 2 . . . . 34 LEU HB3 . 25218 1 280 . 1 1 34 34 LEU HD11 H 1 0.816 0.020 . 2 . . . . 34 LEU HD11 . 25218 1 281 . 1 1 34 34 LEU HD12 H 1 0.816 0.020 . 2 . . . . 34 LEU HD12 . 25218 1 282 . 1 1 34 34 LEU HD13 H 1 0.816 0.020 . 2 . . . . 34 LEU HD13 . 25218 1 283 . 1 1 34 34 LEU HD21 H 1 0.761 0.020 . 2 . . . . 34 LEU HD21 . 25218 1 284 . 1 1 34 34 LEU HD22 H 1 0.761 0.020 . 2 . . . . 34 LEU HD22 . 25218 1 285 . 1 1 34 34 LEU HD23 H 1 0.761 0.020 . 2 . . . . 34 LEU HD23 . 25218 1 286 . 1 1 34 34 LEU CA C 13 54.906 0.400 . 1 . . . . 34 LEU CA . 25218 1 287 . 1 1 34 34 LEU CB C 13 42.510 0.400 . 1 . . . . 34 LEU CB . 25218 1 288 . 1 1 34 34 LEU N N 15 121.624 0.400 . 1 . . . . 34 LEU N . 25218 1 289 . 1 1 35 35 MET H H 1 8.434 0.020 . 1 . . . . 35 MET H . 25218 1 290 . 1 1 35 35 MET HA H 1 4.522 0.020 . 1 . . . . 35 MET HA . 25218 1 291 . 1 1 35 35 MET HB2 H 1 1.900 0.020 . 2 . . . . 35 MET HB2 . 25218 1 292 . 1 1 35 35 MET HB3 H 1 1.900 0.020 . 2 . . . . 35 MET HB3 . 25218 1 293 . 1 1 35 35 MET HG2 H 1 2.351 0.020 . 2 . . . . 35 MET HG2 . 25218 1 294 . 1 1 35 35 MET HG3 H 1 2.443 0.020 . 2 . . . . 35 MET HG3 . 25218 1 295 . 1 1 35 35 MET CA C 13 54.987 0.400 . 1 . . . . 35 MET CA . 25218 1 296 . 1 1 35 35 MET CB C 13 33.026 0.400 . 1 . . . . 35 MET CB . 25218 1 297 . 1 1 35 35 MET N N 15 121.961 0.400 . 1 . . . . 35 MET N . 25218 1 298 . 1 1 36 36 VAL H H 1 8.340 0.020 . 1 . . . . 36 VAL H . 25218 1 299 . 1 1 36 36 VAL HA H 1 4.028 0.020 . 1 . . . . 36 VAL HA . 25218 1 300 . 1 1 36 36 VAL HB H 1 1.936 0.020 . 1 . . . . 36 VAL HB . 25218 1 301 . 1 1 36 36 VAL HG11 H 1 0.837 0.020 . 2 . . . . 36 VAL HG1 . 25218 1 302 . 1 1 36 36 VAL HG12 H 1 0.837 0.020 . 2 . . . . 36 VAL HG1 . 25218 1 303 . 1 1 36 36 VAL HG13 H 1 0.837 0.020 . 2 . . . . 36 VAL HG1 . 25218 1 304 . 1 1 36 36 VAL HG21 H 1 0.837 0.020 . 2 . . . . 36 VAL HG2 . 25218 1 305 . 1 1 36 36 VAL HG22 H 1 0.837 0.020 . 2 . . . . 36 VAL HG2 . 25218 1 306 . 1 1 36 36 VAL HG23 H 1 0.837 0.020 . 2 . . . . 36 VAL HG2 . 25218 1 307 . 1 1 36 36 VAL CA C 13 62.497 0.400 . 1 . . . . 36 VAL CA . 25218 1 308 . 1 1 36 36 VAL CB C 13 33.022 0.400 . 1 . . . . 36 VAL CB . 25218 1 309 . 1 1 36 36 VAL N N 15 122.813 0.400 . 1 . . . . 36 VAL N . 25218 1 310 . 1 1 37 37 GLY H H 1 8.758 0.020 . 1 . . . . 37 GLY H . 25218 1 311 . 1 1 37 37 GLY HA2 H 1 3.856 0.020 . 2 . . . . 37 GLY HA2 . 25218 1 312 . 1 1 37 37 GLY HA3 H 1 3.856 0.020 . 2 . . . . 37 GLY HA3 . 25218 1 313 . 1 1 37 37 GLY CA C 13 45.249 0.400 . 1 . . . . 37 GLY CA . 25218 1 314 . 1 1 37 37 GLY N N 15 114.223 0.400 . 1 . . . . 37 GLY N . 25218 1 315 . 1 1 38 38 GLY H H 1 8.326 0.020 . 1 . . . . 38 GLY H . 25218 1 316 . 1 1 38 38 GLY HA2 H 1 3.850 0.020 . 2 . . . . 38 GLY HA2 . 25218 1 317 . 1 1 38 38 GLY HA3 H 1 3.850 0.020 . 2 . . . . 38 GLY HA3 . 25218 1 318 . 1 1 38 38 GLY CA C 13 45.077 0.400 . 1 . . . . 38 GLY CA . 25218 1 319 . 1 1 38 38 GLY N N 15 107.850 0.400 . 1 . . . . 38 GLY N . 25218 1 320 . 1 1 39 39 VAL H H 1 7.923 0.020 . 1 . . . . 39 VAL H . 25218 1 321 . 1 1 39 39 VAL HA H 1 4.054 0.020 . 1 . . . . 39 VAL HA . 25218 1 322 . 1 1 39 39 VAL HB H 1 1.933 0.020 . 1 . . . . 39 VAL HB . 25218 1 323 . 1 1 39 39 VAL HG11 H 1 0.818 0.020 . 2 . . . . 39 VAL HG1 . 25218 1 324 . 1 1 39 39 VAL HG12 H 1 0.818 0.020 . 2 . . . . 39 VAL HG1 . 25218 1 325 . 1 1 39 39 VAL HG13 H 1 0.818 0.020 . 2 . . . . 39 VAL HG1 . 25218 1 326 . 1 1 39 39 VAL HG21 H 1 0.818 0.020 . 2 . . . . 39 VAL HG2 . 25218 1 327 . 1 1 39 39 VAL HG22 H 1 0.818 0.020 . 2 . . . . 39 VAL HG2 . 25218 1 328 . 1 1 39 39 VAL HG23 H 1 0.818 0.020 . 2 . . . . 39 VAL HG2 . 25218 1 329 . 1 1 39 39 VAL CA C 13 61.855 0.400 . 1 . . . . 39 VAL CA . 25218 1 330 . 1 1 39 39 VAL CB C 13 33.112 0.400 . 1 . . . . 39 VAL CB . 25218 1 331 . 1 1 39 39 VAL N N 15 119.768 0.400 . 1 . . . . 39 VAL N . 25218 1 332 . 1 1 40 40 VAL H H 1 8.416 0.020 . 1 . . . . 40 VAL H . 25218 1 333 . 1 1 40 40 VAL HA H 1 4.042 0.020 . 1 . . . . 40 VAL HA . 25218 1 334 . 1 1 40 40 VAL HB H 1 1.888 0.020 . 1 . . . . 40 VAL HB . 25218 1 335 . 1 1 40 40 VAL HG11 H 1 0.824 0.020 . 2 . . . . 40 VAL HG1 . 25218 1 336 . 1 1 40 40 VAL HG12 H 1 0.824 0.020 . 2 . . . . 40 VAL HG1 . 25218 1 337 . 1 1 40 40 VAL HG13 H 1 0.824 0.020 . 2 . . . . 40 VAL HG1 . 25218 1 338 . 1 1 40 40 VAL HG21 H 1 0.824 0.020 . 2 . . . . 40 VAL HG2 . 25218 1 339 . 1 1 40 40 VAL HG22 H 1 0.824 0.020 . 2 . . . . 40 VAL HG2 . 25218 1 340 . 1 1 40 40 VAL HG23 H 1 0.824 0.020 . 2 . . . . 40 VAL HG2 . 25218 1 341 . 1 1 40 40 VAL CA C 13 62.473 0.400 . 1 . . . . 40 VAL CA . 25218 1 342 . 1 1 40 40 VAL CB C 13 32.512 0.400 . 1 . . . . 40 VAL CB . 25218 1 343 . 1 1 40 40 VAL N N 15 126.149 0.400 . 1 . . . . 40 VAL N . 25218 1 344 . 1 1 41 41 ILE H H 1 8.462 0.020 . 1 . . . . 41 ILE H . 25218 1 345 . 1 1 41 41 ILE HA H 1 4.023 0.020 . 1 . . . . 41 ILE HA . 25218 1 346 . 1 1 41 41 ILE HB H 1 1.777 0.020 . 1 . . . . 41 ILE HB . 25218 1 347 . 1 1 41 41 ILE HG12 H 1 1.385 0.020 . 2 . . . . 41 ILE HG12 . 25218 1 348 . 1 1 41 41 ILE HG13 H 1 1.100 0.020 . 2 . . . . 41 ILE HG13 . 25218 1 349 . 1 1 41 41 ILE HD11 H 1 0.782 0.020 . 1 . . . . 41 ILE HD11 . 25218 1 350 . 1 1 41 41 ILE HD12 H 1 0.782 0.020 . 1 . . . . 41 ILE HD12 . 25218 1 351 . 1 1 41 41 ILE HD13 H 1 0.782 0.020 . 1 . . . . 41 ILE HD13 . 25218 1 352 . 1 1 41 41 ILE CA C 13 60.700 0.400 . 1 . . . . 41 ILE CA . 25218 1 353 . 1 1 41 41 ILE CB C 13 38.287 0.400 . 1 . . . . 41 ILE CB . 25218 1 354 . 1 1 41 41 ILE N N 15 127.666 0.400 . 1 . . . . 41 ILE N . 25218 1 355 . 1 1 42 42 ALA H H 1 8.045 0.020 . 1 . . . . 42 ALA H . 25218 1 356 . 1 1 42 42 ALA HA H 1 4.037 0.020 . 1 . . . . 42 ALA HA . 25218 1 357 . 1 1 42 42 ALA HB1 H 1 1.231 0.020 . 1 . . . . 42 ALA HB1 . 25218 1 358 . 1 1 42 42 ALA HB2 H 1 1.231 0.020 . 1 . . . . 42 ALA HB2 . 25218 1 359 . 1 1 42 42 ALA HB3 H 1 1.231 0.020 . 1 . . . . 42 ALA HB3 . 25218 1 360 . 1 1 42 42 ALA CA C 13 53.735 0.400 . 1 . . . . 42 ALA CA . 25218 1 361 . 1 1 42 42 ALA CB C 13 20.211 0.400 . 1 . . . . 42 ALA CB . 25218 1 362 . 1 1 42 42 ALA N N 15 134.150 0.400 . 1 . . . . 42 ALA N . 25218 1 stop_ save_