data_18052 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18052 _Entry.Title ; Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-11-11 _Entry.Accession_date 2011-11-11 _Entry.Last_release_date 2012-10-29 _Entry.Original_release_date 2012-10-29 _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 Na Sun . . . 18052 2 Rudolf Hartmann . . . 18052 3 Justin Lecher . . . 18052 4 Matthias Stoldt . . . 18052 5 Dieter Willbold . . . 18052 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' . 18052 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Institute for Structural Biochemistry (ICS-6) - Research Centre Juelich' . 18052 2 . 'Institute for Physical Biology - Heinrich-Heine-Universitaet' . 18052 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18052 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 217 18052 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 . . 2012-10-29 2011-11-11 original author . 18052 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18052 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23001756 _Citation.Full_citation . _Citation.Title 'Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Pept. Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 18 _Citation.Journal_issue 11 _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 691 _Citation.Page_last 695 _Citation.Year 2012 _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 Na Sun . . . 18052 1 2 Rudolf Hartmann . . . 18052 1 3 Justin Lecher . . . 18052 1 4 Matthias Stoldt . . . 18052 1 5 'Susanne Aileen' Funke . . . 18052 1 6 Lothar Gremer . . . 18052 1 7 Hans-Henning Ludwig . . . 18052 1 8 Hans-Ulrich Demuth . . . 18052 1 9 Martin Kleinschmi . . . 18052 1 10 Dieter Willbold . . . 18052 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18052 _Assembly.ID 1 _Assembly.Name MS2 _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass 4125.6626 _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 PyroAb 1 $PyroAb A . yes unfolded no no . . . 18052 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_PyroAb _Entity.Sf_category entity _Entity.Sf_framecode PyroAb _Entity.Entry_ID 18052 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Pyroglutamate_Abeta _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; XFRHDSGYEVHHQKLVFFAE DVGSNKGAIIGLMVGGVV ; _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 yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 38 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 4125.6626 _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) . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 2 no BMRB 15775 . APP_C99 . . . . . 97.37 122 100.00 100.00 2.57e-16 . . . . 18052 1 3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 4 no BMRB 17186 . Abeta . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 5 no BMRB 17764 . Abeta . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 6 no BMRB 17793 . Abeta(1-42) . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 7 no BMRB 17794 . Abeta(1-42) . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 8 no BMRB 17795 . Abeta(1-40) . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 9 no BMRB 17796 . Abeta40 . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 10 no BMRB 18127 . beta-amyloid . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 11 no BMRB 18128 . beta-amyloid . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 12 no BMRB 18129 . beta-amyloid . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 13 no BMRB 18131 . beta-amyloid . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 14 no BMRB 19009 . beta-amyloid_peptide . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 15 no BMRB 19309 . amyloid_peptide . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 16 no BMRB 19393 . Abeta . . . . . 97.37 39 97.30 97.30 1.12e-13 . . . . 18052 1 17 no BMRB 25218 . amyloid_peptide . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 18 no BMRB 25289 . amyloid_beta . . . . . 97.37 39 97.30 97.30 1.12e-13 . . . . 18052 1 19 no BMRB 25429 . entity . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 20 no BMRB 26508 . amyloid_B . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 21 no BMRB 26516 . amyloid_B . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 22 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 65.79 28 100.00 100.00 2.68e-08 . . . . 18052 1 23 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 65.79 28 100.00 100.00 2.68e-08 . . . . 18052 1 24 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 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 " . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 26 no PDB 1BA6 . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 97.37 40 97.30 97.30 2.84e-15 . . . . 18052 1 27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 68.42 26 100.00 100.00 2.19e-08 . . . . 18052 1 28 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 29 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 31 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 32 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 33 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 34 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 35 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 36 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 97.37 40 97.30 100.00 1.13e-15 . . . . 18052 1 38 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 97.37 122 100.00 100.00 2.57e-16 . . . . 18052 1 39 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 40 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 41 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 42 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 97.37 39 97.30 97.30 1.12e-13 . . . . 18052 1 43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 44 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 45 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 46 no PDB 3BAE . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" . . . . . 65.79 28 100.00 100.00 2.68e-08 . . . . 18052 1 47 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 48 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 65.79 28 100.00 100.00 2.68e-08 . . . . 18052 1 49 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 50 no PDB 4MVI . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 51 no PDB 4MVL . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 52 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 53 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 97.37 40 100.00 100.00 2.60e-16 . . . . 18052 1 54 no PDB 5AEF . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" . . . . . 68.42 28 100.00 100.00 4.19e-07 . . . . 18052 1 55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 97.37 52 97.30 100.00 4.76e-16 . . . . 18052 1 58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 97.37 696 100.00 100.00 1.52e-16 . . . . 18052 1 59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 97.37 751 100.00 100.00 1.64e-16 . . . . 18052 1 60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 97.37 751 100.00 100.00 1.64e-16 . . . . 18052 1 61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 1 62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 97.37 59 100.00 100.00 7.82e-17 . . . . 18052 1 63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 97.37 58 100.00 100.00 7.66e-17 . . . . 18052 1 64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 97.37 58 100.00 100.00 7.66e-17 . . . . 18052 1 65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 97.37 97 100.00 100.00 1.32e-16 . . . . 18052 1 66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 1 67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 76.32 30 100.00 100.00 5.42e-11 . . . . 18052 1 68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 97.37 412 100.00 100.00 5.42e-17 . . . . 18052 1 69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 97.37 264 100.00 100.00 7.71e-17 . . . . 18052 1 70 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 97.37 57 100.00 100.00 8.18e-17 . . . . 18052 1 71 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 97.37 57 100.00 100.00 8.18e-17 . . . . 18052 1 72 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 97.37 57 100.00 100.00 8.18e-17 . . . . 18052 1 73 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 97.37 57 100.00 100.00 8.18e-17 . . . . 18052 1 74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 97.37 82 100.00 100.00 9.64e-17 . . . . 18052 1 75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 1 76 no PRF 1403400A . "amyloid protein A4" . . . . . 97.37 751 100.00 100.00 1.64e-16 . . . . 18052 1 77 no PRF 1405204A . "amyloid protein" . . . . . 97.37 42 100.00 100.00 2.36e-16 . . . . 18052 1 78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 97.37 412 100.00 100.00 5.42e-17 . . . . 18052 1 79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 97.37 574 100.00 100.00 1.19e-16 . . . . 18052 1 80 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 81 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 1 84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 1 85 no SP P05067 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 86 no SP P53601 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 87 no SP P79307 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 97.37 770 100.00 100.00 1.68e-16 . . . . 18052 1 88 no SP P86906 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 97.37 40 97.30 100.00 1.08e-15 . . . . 18052 1 89 no SP Q28053 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 97.37 59 100.00 100.00 7.82e-17 . . . . 18052 1 90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 97.37 695 100.00 100.00 1.52e-16 . . . . 18052 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 . PCA . 18052 1 2 . PHE . 18052 1 3 . ARG . 18052 1 4 . HIS . 18052 1 5 . ASP . 18052 1 6 . SER . 18052 1 7 . GLY . 18052 1 8 . TYR . 18052 1 9 . GLU . 18052 1 10 . VAL . 18052 1 11 . HIS . 18052 1 12 . HIS . 18052 1 13 . GLN . 18052 1 14 . LYS . 18052 1 15 . LEU . 18052 1 16 . VAL . 18052 1 17 . PHE . 18052 1 18 . PHE . 18052 1 19 . ALA . 18052 1 20 . GLU . 18052 1 21 . ASP . 18052 1 22 . VAL . 18052 1 23 . GLY . 18052 1 24 . SER . 18052 1 25 . ASN . 18052 1 26 . LYS . 18052 1 27 . GLY . 18052 1 28 . ALA . 18052 1 29 . ILE . 18052 1 30 . ILE . 18052 1 31 . GLY . 18052 1 32 . LEU . 18052 1 33 . MET . 18052 1 34 . VAL . 18052 1 35 . GLY . 18052 1 36 . GLY . 18052 1 37 . VAL . 18052 1 38 . VAL . 18052 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 . PCA 1 1 18052 1 . PHE 2 2 18052 1 . ARG 3 3 18052 1 . HIS 4 4 18052 1 . ASP 5 5 18052 1 . SER 6 6 18052 1 . GLY 7 7 18052 1 . TYR 8 8 18052 1 . GLU 9 9 18052 1 . VAL 10 10 18052 1 . HIS 11 11 18052 1 . HIS 12 12 18052 1 . GLN 13 13 18052 1 . LYS 14 14 18052 1 . LEU 15 15 18052 1 . VAL 16 16 18052 1 . PHE 17 17 18052 1 . PHE 18 18 18052 1 . ALA 19 19 18052 1 . GLU 20 20 18052 1 . ASP 21 21 18052 1 . VAL 22 22 18052 1 . GLY 23 23 18052 1 . SER 24 24 18052 1 . ASN 25 25 18052 1 . LYS 26 26 18052 1 . GLY 27 27 18052 1 . ALA 28 28 18052 1 . ILE 29 29 18052 1 . ILE 30 30 18052 1 . GLY 31 31 18052 1 . LEU 32 32 18052 1 . MET 33 33 18052 1 . VAL 34 34 18052 1 . GLY 35 35 18052 1 . GLY 36 36 18052 1 . VAL 37 37 18052 1 . VAL 38 38 18052 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 18052 _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 $PyroAb . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18052 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 18052 _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 $PyroAb . 'chemical synthesis' Synthetic Synthetic . . . . . . . . . . . . . . . . . . . . . . . . . . . 18052 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_PCA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_PCA _Chem_comp.Entry_ID 18052 _Chem_comp.ID PCA _Chem_comp.Provenance . _Chem_comp.Name 'PYROGLUTAMIC ACID' _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code . _Chem_comp.PDB_code PCA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces PCC _Chem_comp.One_letter_code E _Chem_comp.Three_letter_code PCA _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID GLU _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C5 H7 N O3' _Chem_comp.Formula_weight 129.114 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Nov 14 12:08:48 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID C1CC(=O)NC1C(=O)O SMILES 'OpenEye OEToolkits' 1.5.0 18052 PCA C1CC(=O)N[C@@H]1C(=O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18052 PCA InChI=1S/C5H7NO3/c7-4-2-1-3(6-4)5(8)9/h3H,1-2H2,(H,6,7)(H,8,9)/t3-/m0/s1 InChI InChI 1.03 18052 PCA O=C(O)C1NC(=O)CC1 SMILES ACDLabs 10.04 18052 PCA OC(=O)[C@@H]1CCC(=O)N1 SMILES_CANONICAL CACTVS 3.341 18052 PCA OC(=O)[CH]1CCC(=O)N1 SMILES CACTVS 3.341 18052 PCA ODHCTXKNWHHXJC-VKHMYHEASA-N InChIKey InChI 1.03 18052 PCA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-5-oxopyrrolidine-2-carboxylic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18052 PCA 5-oxo-L-proline 'SYSTEMATIC NAME' ACDLabs 10.04 18052 PCA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 38.821 . 57.719 . 67.990 . 0.713 0.531 -0.633 1 . 18052 PCA CA . CA . . C . . S 0 . . . . no no . . . . 38.455 . 58.883 . 67.183 . -0.328 0.539 0.400 2 . 18052 PCA CB . CB . . C . . N 0 . . . . no no . . . . 37.375 . 59.639 . 67.947 . -1.455 -0.368 -0.140 3 . 18052 PCA CG . CG . . C . . N 0 . . . . no no . . . . 37.746 . 59.312 . 69.375 . -1.232 -0.272 -1.667 4 . 18052 PCA CD . CD . . C . . N 0 . . . . no no . . . . 38.398 . 57.930 . 69.250 . 0.231 0.082 -1.807 5 . 18052 PCA OE . OE . . O . . N 0 . . . . no no . . . . 38.575 . 57.133 . 70.197 . 0.876 -0.019 -2.829 6 . 18052 PCA C . C . . C . . N 0 . . . . no no . . . . 39.640 . 59.813 . 66.967 . 0.214 -0.015 1.691 7 . 18052 PCA O . O . . O . . N 0 . . . . no no . . . . 40.560 . 59.863 . 67.790 . 1.122 -0.812 1.672 8 . 18052 PCA OXT . OXT . . O . . N 0 . . . . no yes . . . . 39.626 . 60.540 . 65.853 . -0.311 0.374 2.863 9 . 18052 PCA H . H . . H . . N 0 . . . . no no . . . . 39.309 . 56.868 . 67.709 . 1.631 0.810 -0.489 10 . 18052 PCA HA . HA . . H . . N 0 . . . . no no . . . . 38.103 . 58.540 . 66.181 . -0.700 1.552 0.552 11 . 18052 PCA HB2 . HB2 . . H . . N 0 . . . . no no . . . . 37.293 . 60.725 . 67.710 . -1.331 -1.393 0.208 12 . 18052 PCA HB3 . HB3 . . H . . N 0 . . . . no no . . . . 36.325 . 59.396 . 67.657 . -2.435 0.019 0.136 13 . 18052 PCA HG2 . HG2 . . H . . N 0 . . . . no no . . . . 38.375 . 60.080 . 69.881 . -1.439 -1.230 -2.144 14 . 18052 PCA HG3 . HG3 . . H . . N 0 . . . . no no . . . . 36.900 . 59.365 . 70.100 . -1.857 0.511 -2.095 15 . 18052 PCA HXT . HXT . . H . . N 0 . . . . no yes . . . . 40.365 . 61.120 . 65.718 . 0.036 0.018 3.692 16 . 18052 PCA stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 18052 PCA 2 . SING N CD no N 2 . 18052 PCA 3 . SING N H no N 3 . 18052 PCA 4 . SING CA CB no N 4 . 18052 PCA 5 . SING CA C no N 5 . 18052 PCA 6 . SING CA HA no N 6 . 18052 PCA 7 . SING CB CG no N 7 . 18052 PCA 8 . SING CB HB2 no N 8 . 18052 PCA 9 . SING CB HB3 no N 9 . 18052 PCA 10 . SING CG CD no N 10 . 18052 PCA 11 . SING CG HG2 no N 11 . 18052 PCA 12 . SING CG HG3 no N 12 . 18052 PCA 13 . DOUB CD OE no N 13 . 18052 PCA 14 . DOUB C O no N 14 . 18052 PCA 15 . SING C OXT no N 15 . 18052 PCA 16 . SING OXT HXT no N 16 . 18052 PCA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_1 _Sample.Sf_category sample _Sample.Sf_framecode 1 _Sample.Entry_ID 18052 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system trifluoroethanol/water _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 'Pyroglutamate Abeta' 'natural abundance' . . 1 $PyroAb . . 0.1 . . mM . . . . 18052 1 2 Trifluoroethanol 'natural abundance' . . . . . . 40 . . % . . . . 18052 1 3 H2O 'natural abundance' . . . . . . 60 . . % . . . . 18052 1 stop_ save_ ####################### # Sample conditions # ####################### save_Standard _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Standard _Sample_condition_list.Entry_ID 18052 _Sample_condition_list.ID 1 _Sample_condition_list.Details '40% TFE in water' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.050 . M 18052 1 pH 2.800 . pH 18052 1 pressure 1.000 . atm 18052 1 temperature 298.000 . K 18052 1 stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Software.Sf_category software _Software.Sf_framecode CcpNmr_Analysis _Software.Entry_ID 18052 _Software.ID 1 _Software.Name ANALYSIS _Software.Version 2.1 _Software.Details 'The CCPN NMR assignment and data analysis application' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk 18052 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignment 18052 1 stop_ save_ save_NmrPipe _Software.Sf_category software _Software.Sf_framecode NmrPipe _Software.Entry_ID 18052 _Software.ID 2 _Software.Name NMRPipe _Software.Version 5.99.2011.242.16.23 _Software.Details 'NMRPipe Spectral Processing and Analysis System' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID NIH 'Laboratory of Chemical Physics, NIDDK, NIH, USA' http://spin.niddk.nih.gov/NMRPipe/ 18052 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID conversion 18052 2 processing 18052 2 stop_ save_ save_VnmrJ _Software.Sf_category software _Software.Sf_framecode VnmrJ _Software.Entry_ID 18052 _Software.ID 3 _Software.Name VnmrJ _Software.Version 2.3A _Software.Details 'NMR acquisition and processing software' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Agilent Technologies (formerly Varian)' 'Lake Forest, CA, USA' http://www.varianinc.com/cgi-bin/nav?products/nmr/software/vnmrj 18052 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data recording' 18052 3 'spectrometer operation' 18052 3 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 18052 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18052 _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 Varian VNMRS . 900 . . . 18052 1 stop_ save_ save_900_CP _NMR_spectrometer_probe.Sf_category NMR_spectrometer_probe _NMR_spectrometer_probe.Sf_framecode 900_CP _NMR_spectrometer_probe.Entry_ID 18052 _NMR_spectrometer_probe.ID 1 _NMR_spectrometer_probe.Details . _NMR_spectrometer_probe.Manufacturer Varian _NMR_spectrometer_probe.Model '900MHz Z-axis PFG triple resonance cold probe' _NMR_spectrometer_probe.Serial_number . _NMR_spectrometer_probe.Diameter 5.0 _NMR_spectrometer_probe.Rotor_length . _NMR_spectrometer_probe.Rotor_composition . _NMR_spectrometer_probe.Internal_volume . _NMR_spectrometer_probe.Spacer_present . loop_ _NMR_probe.Type _NMR_probe.Entry_ID _NMR_probe.NMR_spectrometer_probe_ID liquid 18052 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 18052 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $1 isotropic . . 1 $Standard . . . 1 $spectrometer_1 1 $900_CP . . . . . . . . . . . . . . 18052 1 2 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $1 isotropic . . 1 $Standard . . . 1 $spectrometer_1 1 $900_CP . . . . . . . . . . . . . . 18052 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 18052 _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 0.0 external direct 1.0 'capilary in NMR tube' . . . . . . . . 18052 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 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list _Assigned_chem_shift_list.Entry_ID 18052 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Standard _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-1H TOCSY' 1 $1 isotropic 18052 1 2 '2D 1H-1H NOESY' 1 $1 isotropic 18052 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 PCA H H 1 7.759 0.03 . 1 . . . . 139 . . . 18052 1 2 . 1 1 1 1 PCA HA H 1 4.224 0.003 . 1 . . . . 140 . . . 18052 1 3 . 1 1 1 1 PCA HB2 H 1 2.147 0.03 . 2 . . . . 155 . . . 18052 1 4 . 1 1 1 1 PCA HB3 H 1 1.712 0.03 . 2 . . . . 154 . . . 18052 1 5 . 1 1 1 1 PCA HG2 H 1 2.429 0.004 . 2 . . . . 157 . . . 18052 1 6 . 1 1 1 1 PCA HG3 H 1 2.276 0.003 . 2 . . . . 156 . . . 18052 1 7 . 1 1 2 2 PHE H H 1 7.947 0.003 . 1 . . . . 2 PHE H . 18052 1 8 . 1 1 2 2 PHE HA H 1 4.713 0.015 . 1 . . . . 2 PHE HA . 18052 1 9 . 1 1 2 2 PHE HB2 H 1 2.978 0.002 . 2 . . . . 2 PHE HB2 . 18052 1 10 . 1 1 2 2 PHE HB3 H 1 3.229 0.004 . 2 . . . . 2 PHE HB3 . 18052 1 11 . 1 1 2 2 PHE HD1 H 1 7.254 0.001 . 3 . . . . 2 PHE HD1 . 18052 1 12 . 1 1 2 2 PHE HD2 H 1 7.254 0.001 . 3 . . . . 2 PHE HD2 . 18052 1 13 . 1 1 2 2 PHE HE1 H 1 7.334 0.003 . 3 . . . . 2 PHE HE1 . 18052 1 14 . 1 1 2 2 PHE HE2 H 1 7.334 0.003 . 3 . . . . 2 PHE HE2 . 18052 1 15 . 1 1 3 3 ARG H H 1 8.281 0.003 . 1 . . . . 3 ARG H . 18052 1 16 . 1 1 3 3 ARG HA H 1 4.310 0.007 . 1 . . . . 3 ARG HA . 18052 1 17 . 1 1 3 3 ARG HB2 H 1 1.762 0.005 . 2 . . . . 3 ARG HB2 . 18052 1 18 . 1 1 3 3 ARG HB3 H 1 1.843 0.004 . 2 . . . . 3 ARG HB3 . 18052 1 19 . 1 1 3 3 ARG HG2 H 1 1.577 0.003 . 2 . . . . 3 ARG HG2 . 18052 1 20 . 1 1 3 3 ARG HG3 H 1 1.626 0.002 . 2 . . . . 3 ARG HG3 . 18052 1 21 . 1 1 3 3 ARG HD3 H 1 3.200 0.002 . 1 . . . . 3 ARG HD3 . 18052 1 22 . 1 1 3 3 ARG HE H 1 7.340 0.002 . 1 . . . . 3 ARG HE . 18052 1 23 . 1 1 4 4 HIS H H 1 8.568 0.007 . 1 . . . . 4 HIS H . 18052 1 24 . 1 1 4 4 HIS HA H 1 4.724 0.013 . 1 . . . . 4 HIS HA . 18052 1 25 . 1 1 4 4 HIS HB2 H 1 3.204 0.004 . 2 . . . . 4 HIS HB2 . 18052 1 26 . 1 1 4 4 HIS HB3 H 1 3.299 0.002 . 2 . . . . 4 HIS HB3 . 18052 1 27 . 1 1 4 4 HIS HD2 H 1 7.258 0.03 . 1 . . . . 4 HIS HD2 . 18052 1 28 . 1 1 4 4 HIS HE1 H 1 8.569 0.03 . 1 . . . . 4 HIS HE1 . 18052 1 29 . 1 1 5 5 ASP H H 1 8.453 0.001 . 1 . . . . 5 ASP H . 18052 1 30 . 1 1 5 5 ASP HA H 1 4.814 0.005 . 1 . . . . 5 ASP HA . 18052 1 31 . 1 1 5 5 ASP HB2 H 1 2.917 0.002 . 1 . . . . 5 ASP HB2 . 18052 1 32 . 1 1 6 6 SER H H 1 8.452 0.004 . 1 . . . . 6 SER H . 18052 1 33 . 1 1 6 6 SER HA H 1 4.444 0.001 . 1 . . . . 6 SER HA . 18052 1 34 . 1 1 6 6 SER HB2 H 1 4.014 0.008 . 2 . . . . 6 SER HB2 . 18052 1 35 . 1 1 6 6 SER HB3 H 1 4.025 0.002 . 2 . . . . 6 SER HB3 . 18052 1 36 . 1 1 7 7 GLY H H 1 8.577 0.003 . 1 . . . . 7 GLY H . 18052 1 37 . 1 1 7 7 GLY HA2 H 1 3.932 0.003 . 1 . . . . 7 GLY HA2 . 18052 1 38 . 1 1 8 8 TYR H H 1 8.066 0.002 . 1 . . . . 8 TYR H . 18052 1 39 . 1 1 8 8 TYR HA H 1 4.352 0.002 . 1 . . . . 8 TYR HA . 18052 1 40 . 1 1 8 8 TYR HB2 H 1 3.166 0.003 . 2 . . . . 8 TYR HB2 . 18052 1 41 . 1 1 8 8 TYR HB3 H 1 3.101 0.005 . 2 . . . . 8 TYR HB3 . 18052 1 42 . 1 1 8 8 TYR HD1 H 1 7.089 0.001 . 3 . . . . 8 TYR HD1 . 18052 1 43 . 1 1 8 8 TYR HD2 H 1 7.089 0.001 . 3 . . . . 8 TYR HD2 . 18052 1 44 . 1 1 8 8 TYR HE1 H 1 6.767 0.002 . 3 . . . . 8 TYR HE1 . 18052 1 45 . 1 1 8 8 TYR HE2 H 1 6.767 0.002 . 3 . . . . 8 TYR HE2 . 18052 1 46 . 1 1 9 9 GLU H H 1 8.308 0.003 . 1 . . . . 9 GLU H . 18052 1 47 . 1 1 9 9 GLU HA H 1 4.150 0.001 . 1 . . . . 9 GLU HA . 18052 1 48 . 1 1 9 9 GLU HB2 H 1 2.206 0.004 . 1 . . . . 9 GLU HB2 . 18052 1 49 . 1 1 9 9 GLU HG3 H 1 2.537 0.004 . 1 . . . . 9 GLU HG3 . 18052 1 50 . 1 1 10 10 VAL H H 1 8.127 0.004 . 1 . . . . 10 VAL H . 18052 1 51 . 1 1 10 10 VAL HA H 1 3.837 0.001 . 1 . . . . 10 VAL HA . 18052 1 52 . 1 1 10 10 VAL HB H 1 2.083 0.002 . 1 . . . . 10 VAL HB . 18052 1 53 . 1 1 10 10 VAL HG11 H 1 1.031 0.002 . 2 . . . . 10 VAL HG11 . 18052 1 54 . 1 1 10 10 VAL HG12 H 1 1.031 0.002 . 2 . . . . 10 VAL HG12 . 18052 1 55 . 1 1 10 10 VAL HG13 H 1 1.031 0.002 . 2 . . . . 10 VAL HG13 . 18052 1 56 . 1 1 10 10 VAL HG21 H 1 0.907 0.006 . 2 . . . . 10 VAL HG21 . 18052 1 57 . 1 1 10 10 VAL HG22 H 1 0.907 0.006 . 2 . . . . 10 VAL HG22 . 18052 1 58 . 1 1 10 10 VAL HG23 H 1 0.907 0.006 . 2 . . . . 10 VAL HG23 . 18052 1 59 . 1 1 11 11 HIS H H 1 8.109 0.003 . 1 . . . . 11 HIS H . 18052 1 60 . 1 1 11 11 HIS HA H 1 4.427 0.002 . 1 . . . . 11 HIS HA . 18052 1 61 . 1 1 11 11 HIS HB2 H 1 3.270 0.003 . 1 . . . . 11 HIS HB2 . 18052 1 62 . 1 1 11 11 HIS HD2 H 1 7.274 0.001 . 1 . . . . 11 HIS HD2 . 18052 1 63 . 1 1 11 11 HIS HE1 H 1 8.598 0.001 . 1 . . . . 11 HIS HE1 . 18052 1 64 . 1 1 12 12 HIS H H 1 8.485 0.002 . 1 . . . . 12 HIS H . 18052 1 65 . 1 1 12 12 HIS HA H 1 4.323 0.005 . 1 . . . . 12 HIS HA . 18052 1 66 . 1 1 12 12 HIS HB2 H 1 3.298 0.005 . 2 . . . . 12 HIS HB2 . 18052 1 67 . 1 1 12 12 HIS HB3 H 1 3.074 0.001 . 2 . . . . 12 HIS HB3 . 18052 1 68 . 1 1 12 12 HIS HD2 H 1 7.221 0.001 . 1 . . . . 12 HIS HD2 . 18052 1 69 . 1 1 12 12 HIS HE1 H 1 8.465 0.001 . 1 . . . . 12 HIS HE1 . 18052 1 70 . 1 1 13 13 GLN H H 1 8.346 0.002 . 1 . . . . 13 GLN H . 18052 1 71 . 1 1 13 13 GLN HA H 1 4.012 0.002 . 1 . . . . 13 GLN HA . 18052 1 72 . 1 1 13 13 GLN HB2 H 1 2.211 0.003 . 2 . . . . 13 GLN HB2 . 18052 1 73 . 1 1 13 13 GLN HB3 H 1 2.141 0.007 . 2 . . . . 13 GLN HB3 . 18052 1 74 . 1 1 13 13 GLN HG3 H 1 2.374 0.002 . 1 . . . . 13 GLN HG3 . 18052 1 75 . 1 1 13 13 GLN HE21 H 1 6.626 0.002 . 1 . . . . 13 GLN HE21 . 18052 1 76 . 1 1 13 13 GLN HE22 H 1 6.871 0.001 . 1 . . . . 13 GLN HE22 . 18052 1 77 . 1 1 14 14 LYS H H 1 8.079 0.002 . 1 . . . . 14 LYS H . 18052 1 78 . 1 1 14 14 LYS HA H 1 4.127 0.002 . 1 . . . . 14 LYS HA . 18052 1 79 . 1 1 15 15 LEU H H 1 7.687 0.003 . 1 . . . . 15 LEU H . 18052 1 80 . 1 1 15 15 LEU HA H 1 4.249 0.006 . 1 . . . . 15 LEU HA . 18052 1 81 . 1 1 15 15 LEU HB3 H 1 1.754 0.002 . 1 . . . . 15 LEU HB3 . 18052 1 82 . 1 1 15 15 LEU HG H 1 1.691 0.002 . 1 . . . . 15 LEU HG . 18052 1 83 . 1 1 15 15 LEU HD11 H 1 0.887 0.002 . 2 . . . . 15 LEU HD11 . 18052 1 84 . 1 1 15 15 LEU HD12 H 1 0.887 0.002 . 2 . . . . 15 LEU HD12 . 18052 1 85 . 1 1 15 15 LEU HD13 H 1 0.887 0.002 . 2 . . . . 15 LEU HD13 . 18052 1 86 . 1 1 15 15 LEU HD21 H 1 0.924 0.002 . 2 . . . . 15 LEU HD21 . 18052 1 87 . 1 1 15 15 LEU HD22 H 1 0.924 0.002 . 2 . . . . 15 LEU HD22 . 18052 1 88 . 1 1 15 15 LEU HD23 H 1 0.924 0.002 . 2 . . . . 15 LEU HD23 . 18052 1 89 . 1 1 16 16 VAL H H 1 7.777 0.004 . 1 . . . . 16 VAL H . 18052 1 90 . 1 1 16 16 VAL HA H 1 3.672 0.002 . 1 . . . . 16 VAL HA . 18052 1 91 . 1 1 16 16 VAL HB H 1 2.042 0.005 . 1 . . . . 16 VAL HB . 18052 1 92 . 1 1 16 16 VAL HG21 H 1 0.862 0.003 . 1 . . . . 16 VAL HG21 . 18052 1 93 . 1 1 16 16 VAL HG22 H 1 0.862 0.003 . 1 . . . . 16 VAL HG22 . 18052 1 94 . 1 1 16 16 VAL HG23 H 1 0.862 0.003 . 1 . . . . 16 VAL HG23 . 18052 1 95 . 1 1 17 17 PHE H H 1 8.019 0.002 . 1 . . . . 17 PHE H . 18052 1 96 . 1 1 17 17 PHE HA H 1 4.398 0.002 . 1 . . . . 17 PHE HA . 18052 1 97 . 1 1 17 17 PHE HB2 H 1 3.200 0.004 . 1 . . . . 17 PHE HB2 . 18052 1 98 . 1 1 17 17 PHE HD1 H 1 7.178 0.002 . 3 . . . . 17 PHE HD1 . 18052 1 99 . 1 1 17 17 PHE HD2 H 1 7.178 0.002 . 3 . . . . 17 PHE HD2 . 18052 1 100 . 1 1 17 17 PHE HE1 H 1 7.285 0.002 . 3 . . . . 17 PHE HE1 . 18052 1 101 . 1 1 17 17 PHE HE2 H 1 7.285 0.002 . 3 . . . . 17 PHE HE2 . 18052 1 102 . 1 1 18 18 PHE H H 1 8.329 0.004 . 1 . . . . 18 PHE H . 18052 1 103 . 1 1 18 18 PHE HA H 1 4.309 0.004 . 1 . . . . 18 PHE HA . 18052 1 104 . 1 1 18 18 PHE HB2 H 1 3.285 0.011 . 1 . . . . 18 PHE HB2 . 18052 1 105 . 1 1 18 18 PHE HD1 H 1 7.273 0.002 . 3 . . . . 18 PHE HD1 . 18052 1 106 . 1 1 18 18 PHE HD2 H 1 7.273 0.002 . 3 . . . . 18 PHE HD2 . 18052 1 107 . 1 1 18 18 PHE HE1 H 1 7.297 0.003 . 3 . . . . 18 PHE HE1 . 18052 1 108 . 1 1 18 18 PHE HE2 H 1 7.297 0.003 . 3 . . . . 18 PHE HE2 . 18052 1 109 . 1 1 18 18 PHE HZ H 1 7.244 0.03 . 1 . . . . 18 PHE HZ . 18052 1 110 . 1 1 19 19 ALA H H 1 8.582 0.005 . 1 . . . . 19 ALA H . 18052 1 111 . 1 1 19 19 ALA HA H 1 3.998 0.005 . 1 . . . . 19 ALA HA . 18052 1 112 . 1 1 19 19 ALA HB1 H 1 1.533 0.002 . 1 . . . . 19 ALA HB1 . 18052 1 113 . 1 1 19 19 ALA HB2 H 1 1.533 0.002 . 1 . . . . 19 ALA HB2 . 18052 1 114 . 1 1 19 19 ALA HB3 H 1 1.533 0.002 . 1 . . . . 19 ALA HB3 . 18052 1 115 . 1 1 20 20 GLU H H 1 8.326 0.003 . 1 . . . . 20 GLU H . 18052 1 116 . 1 1 20 20 GLU HA H 1 4.169 0.002 . 1 . . . . 20 GLU HA . 18052 1 117 . 1 1 20 20 GLU HB2 H 1 2.185 0.004 . 2 . . . . 20 GLU HB2 . 18052 1 118 . 1 1 20 20 GLU HB3 H 1 2.118 0.006 . 2 . . . . 20 GLU HB3 . 18052 1 119 . 1 1 20 20 GLU HG2 H 1 2.645 0.001 . 2 . . . . 20 GLU HG2 . 18052 1 120 . 1 1 20 20 GLU HG3 H 1 2.491 0.001 . 2 . . . . 20 GLU HG3 . 18052 1 121 . 1 1 21 21 ASP H H 1 8.210 0.003 . 1 . . . . 21 ASP H . 18052 1 122 . 1 1 21 21 ASP HA H 1 4.572 0.001 . 1 . . . . 21 ASP HA . 18052 1 123 . 1 1 21 21 ASP HB2 H 1 2.779 0.005 . 2 . . . . 21 ASP HB2 . 18052 1 124 . 1 1 21 21 ASP HB3 H 1 2.809 0.002 . 2 . . . . 21 ASP HB3 . 18052 1 125 . 1 1 22 22 VAL H H 1 8.091 0.005 . 1 . . . . 22 VAL H . 18052 1 126 . 1 1 22 22 VAL HA H 1 3.822 0.002 . 1 . . . . 22 VAL HA . 18052 1 127 . 1 1 22 22 VAL HB H 1 1.949 0.002 . 1 . . . . 22 VAL HB . 18052 1 128 . 1 1 22 22 VAL HG11 H 1 0.832 0.002 . 2 . . . . 22 VAL HG11 . 18052 1 129 . 1 1 22 22 VAL HG12 H 1 0.832 0.002 . 2 . . . . 22 VAL HG12 . 18052 1 130 . 1 1 22 22 VAL HG13 H 1 0.832 0.002 . 2 . . . . 22 VAL HG13 . 18052 1 131 . 1 1 22 22 VAL HG21 H 1 0.753 0.003 . 2 . . . . 22 VAL HG21 . 18052 1 132 . 1 1 22 22 VAL HG22 H 1 0.753 0.003 . 2 . . . . 22 VAL HG22 . 18052 1 133 . 1 1 22 22 VAL HG23 H 1 0.753 0.003 . 2 . . . . 22 VAL HG23 . 18052 1 134 . 1 1 23 23 GLY H H 1 8.165 0.002 . 1 . . . . 23 GLY H . 18052 1 135 . 1 1 23 23 GLY HA2 H 1 3.896 0.002 . 1 . . . . 23 GLY HA2 . 18052 1 136 . 1 1 24 24 SER H H 1 7.913 0.003 . 1 . . . . 24 SER H . 18052 1 137 . 1 1 24 24 SER HA H 1 4.447 0.001 . 1 . . . . 24 SER HA . 18052 1 138 . 1 1 24 24 SER HB2 H 1 4.022 0.002 . 2 . . . . 24 SER HB2 . 18052 1 139 . 1 1 24 24 SER HB3 H 1 3.974 0.005 . 2 . . . . 24 SER HB3 . 18052 1 140 . 1 1 25 25 ASN H H 1 8.094 0.003 . 1 . . . . 25 ASN H . 18052 1 141 . 1 1 25 25 ASN HA H 1 4.821 0.03 . 1 . . . . 25 ASN HA . 18052 1 142 . 1 1 25 25 ASN HB2 H 1 2.960 0.002 . 2 . . . . 25 ASN HB2 . 18052 1 143 . 1 1 25 25 ASN HB3 H 1 2.848 0.003 . 2 . . . . 25 ASN HB3 . 18052 1 144 . 1 1 25 25 ASN HD21 H 1 6.729 0.002 . 1 . . . . 25 ASN HD21 . 18052 1 145 . 1 1 25 25 ASN HD22 H 1 7.485 0.003 . 1 . . . . 25 ASN HD22 . 18052 1 146 . 1 1 26 26 LYS H H 1 8.251 0.003 . 1 . . . . 26 LYS H . 18052 1 147 . 1 1 26 26 LYS HA H 1 4.141 0.002 . 1 . . . . 26 LYS HA . 18052 1 148 . 1 1 26 26 LYS HB2 H 1 1.899 0.004 . 1 . . . . 26 LYS HB2 . 18052 1 149 . 1 1 26 26 LYS HG2 H 1 1.485 0.005 . 2 . . . . 26 LYS HG2 . 18052 1 150 . 1 1 26 26 LYS HG3 H 1 1.562 0.003 . 2 . . . . 26 LYS HG3 . 18052 1 151 . 1 1 27 27 GLY H H 1 8.361 0.003 . 1 . . . . 27 GLY H . 18052 1 152 . 1 1 27 27 GLY HA2 H 1 3.901 0.003 . 2 . . . . 27 GLY HA2 . 18052 1 153 . 1 1 27 27 GLY HA3 H 1 3.871 0.004 . 2 . . . . 27 GLY HA3 . 18052 1 154 . 1 1 28 28 ALA H H 1 7.801 0.002 . 1 . . . . 28 ALA H . 18052 1 155 . 1 1 28 28 ALA HA H 1 4.241 0.002 . 1 . . . . 28 ALA HA . 18052 1 156 . 1 1 28 28 ALA HB1 H 1 1.507 0.002 . 1 . . . . 28 ALA HB1 . 18052 1 157 . 1 1 28 28 ALA HB2 H 1 1.507 0.002 . 1 . . . . 28 ALA HB2 . 18052 1 158 . 1 1 28 28 ALA HB3 H 1 1.507 0.002 . 1 . . . . 28 ALA HB3 . 18052 1 159 . 1 1 29 29 ILE H H 1 7.676 0.003 . 1 . . . . 29 ILE H . 18052 1 160 . 1 1 29 29 ILE HA H 1 3.926 0.003 . 1 . . . . 29 ILE HA . 18052 1 161 . 1 1 29 29 ILE HB H 1 2.019 0.002 . 1 . . . . 29 ILE HB . 18052 1 162 . 1 1 29 29 ILE HG12 H 1 0.979 0.002 . 2 . . . . 29 ILE HG12 . 18052 1 163 . 1 1 29 29 ILE HG13 H 1 1.284 0.03 . 2 . . . . 29 ILE HG13 . 18052 1 164 . 1 1 29 29 ILE HD11 H 1 0.902 0.002 . 1 . . . . 29 ILE HD11 . 18052 1 165 . 1 1 29 29 ILE HD12 H 1 0.902 0.002 . 1 . . . . 29 ILE HD12 . 18052 1 166 . 1 1 29 29 ILE HD13 H 1 0.902 0.002 . 1 . . . . 29 ILE HD13 . 18052 1 167 . 1 1 30 30 ILE H H 1 7.897 0.005 . 1 . . . . 30 ILE H . 18052 1 168 . 1 1 30 30 ILE HA H 1 3.868 0.003 . 1 . . . . 30 ILE HA . 18052 1 169 . 1 1 30 30 ILE HB H 1 1.947 0.003 . 1 . . . . 30 ILE HB . 18052 1 170 . 1 1 30 30 ILE HG12 H 1 1.265 0.002 . 2 . . . . 30 ILE HG12 . 18052 1 171 . 1 1 30 30 ILE HG13 H 1 0.941 0.002 . 2 . . . . 30 ILE HG13 . 18052 1 172 . 1 1 31 31 GLY H H 1 7.991 0.001 . 1 . . . . 31 GLY H . 18052 1 173 . 1 1 31 31 GLY HA2 H 1 3.823 0.003 . 2 . . . . 31 GLY HA2 . 18052 1 174 . 1 1 31 31 GLY HA3 H 1 3.859 0.004 . 2 . . . . 31 GLY HA3 . 18052 1 175 . 1 1 32 32 LEU H H 1 7.847 0.003 . 1 . . . . 32 LEU H . 18052 1 176 . 1 1 32 32 LEU HA H 1 4.227 0.002 . 1 . . . . 32 LEU HA . 18052 1 177 . 1 1 32 32 LEU HB2 H 1 1.980 0.002 . 2 . . . . 32 LEU HB2 . 18052 1 178 . 1 1 32 32 LEU HB3 H 1 1.830 0.003 . 2 . . . . 32 LEU HB3 . 18052 1 179 . 1 1 32 32 LEU HG H 1 1.594 0.002 . 1 . . . . 32 LEU HG . 18052 1 180 . 1 1 32 32 LEU HD11 H 1 0.910 0.03 . 2 . . . . 32 LEU HD11 . 18052 1 181 . 1 1 32 32 LEU HD12 H 1 0.910 0.03 . 2 . . . . 32 LEU HD12 . 18052 1 182 . 1 1 32 32 LEU HD13 H 1 0.910 0.03 . 2 . . . . 32 LEU HD13 . 18052 1 183 . 1 1 32 32 LEU HD21 H 1 0.881 0.002 . 2 . . . . 32 LEU HD21 . 18052 1 184 . 1 1 32 32 LEU HD22 H 1 0.881 0.002 . 2 . . . . 32 LEU HD22 . 18052 1 185 . 1 1 32 32 LEU HD23 H 1 0.881 0.002 . 2 . . . . 32 LEU HD23 . 18052 1 186 . 1 1 33 33 MET H H 1 8.168 0.004 . 1 . . . . 33 MET H . 18052 1 187 . 1 1 33 33 MET HA H 1 4.342 0.004 . 1 . . . . 33 MET HA . 18052 1 188 . 1 1 33 33 MET HB2 H 1 2.168 0.002 . 2 . . . . 33 MET HB2 . 18052 1 189 . 1 1 33 33 MET HB3 H 1 2.310 0.003 . 2 . . . . 33 MET HB3 . 18052 1 190 . 1 1 33 33 MET HG2 H 1 2.743 0.003 . 2 . . . . 33 MET HG2 . 18052 1 191 . 1 1 33 33 MET HG3 H 1 2.545 0.003 . 2 . . . . 33 MET HG3 . 18052 1 192 . 1 1 34 34 VAL H H 1 8.455 0.005 . 1 . . . . 34 VAL H . 18052 1 193 . 1 1 34 34 VAL HA H 1 4.028 0.002 . 1 . . . . 34 VAL HA . 18052 1 194 . 1 1 34 34 VAL HB H 1 2.238 0.002 . 1 . . . . 34 VAL HB . 18052 1 195 . 1 1 34 34 VAL HG11 H 1 1.050 0.003 . 2 . . . . 34 VAL HG11 . 18052 1 196 . 1 1 34 34 VAL HG12 H 1 1.050 0.003 . 2 . . . . 34 VAL HG12 . 18052 1 197 . 1 1 34 34 VAL HG13 H 1 1.050 0.003 . 2 . . . . 34 VAL HG13 . 18052 1 198 . 1 1 34 34 VAL HG21 H 1 0.982 0.002 . 2 . . . . 34 VAL HG21 . 18052 1 199 . 1 1 34 34 VAL HG22 H 1 0.982 0.002 . 2 . . . . 34 VAL HG22 . 18052 1 200 . 1 1 34 34 VAL HG23 H 1 0.982 0.002 . 2 . . . . 34 VAL HG23 . 18052 1 201 . 1 1 35 35 GLY H H 1 8.035 0.003 . 1 . . . . 35 GLY H . 18052 1 202 . 1 1 35 35 GLY HA2 H 1 3.919 0.006 . 2 . . . . 35 GLY HA2 . 18052 1 203 . 1 1 35 35 GLY HA3 H 1 4.082 0.003 . 2 . . . . 35 GLY HA3 . 18052 1 204 . 1 1 36 36 GLY H H 1 7.945 0.002 . 1 . . . . 36 GLY H . 18052 1 205 . 1 1 36 36 GLY HA2 H 1 4.010 0.002 . 1 . . . . 36 GLY HA2 . 18052 1 206 . 1 1 37 37 VAL H H 1 7.883 0.003 . 1 . . . . 37 VAL H . 18052 1 207 . 1 1 37 37 VAL HA H 1 4.118 0.001 . 1 . . . . 37 VAL HA . 18052 1 208 . 1 1 37 37 VAL HB H 1 2.135 0.003 . 1 . . . . 37 VAL HB . 18052 1 209 . 1 1 37 37 VAL HG21 H 1 0.981 0.002 . 1 . . . . 37 VAL HG21 . 18052 1 210 . 1 1 37 37 VAL HG22 H 1 0.981 0.002 . 1 . . . . 37 VAL HG22 . 18052 1 211 . 1 1 37 37 VAL HG23 H 1 0.981 0.002 . 1 . . . . 37 VAL HG23 . 18052 1 212 . 1 1 38 38 VAL H H 1 7.566 0.003 . 1 . . . . 38 VAL H . 18052 1 213 . 1 1 38 38 VAL HA H 1 4.319 0.004 . 1 . . . . 38 VAL HA . 18052 1 214 . 1 1 38 38 VAL HB H 1 2.155 0.007 . 1 . . . . 38 VAL HB . 18052 1 215 . 1 1 38 38 VAL HG21 H 1 0.947 0.006 . 1 . . . . 38 VAL HG21 . 18052 1 216 . 1 1 38 38 VAL HG22 H 1 0.947 0.006 . 1 . . . . 38 VAL HG22 . 18052 1 217 . 1 1 38 38 VAL HG23 H 1 0.947 0.006 . 1 . . . . 38 VAL HG23 . 18052 1 stop_ save_