data_5057 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5057 _Entry.Title ; 1H Chemical Shift Assignments for Alzheimer peptide Ab(1-40) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-06-14 _Entry.Accession_date 2001-06-14 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 Roland Riek . . . 5057 2 Peter Guntert . . . 5057 3 Heinz Dobeli . . . 5057 4 Beat Wipf . . . 5057 5 Kurt Wuthrich . . . 5057 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5057 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 212 5057 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 2 . . 2008-07-29 2001-06-14 update BMRB 'Updating non-standard residue' 5057 1 . . 2002-01-23 2001-06-14 original author . 5057 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5057 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21579731 _Citation.DOI . _Citation.PubMed_ID 11722581 _Citation.Full_citation . _Citation.Title ; NMR Studies in Aqueous Solution Fail to Identify Significant Conformational Differences between the Monomeric Forms of Two Alzheimer Peptides with Widely Different Plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 268 _Citation.Journal_issue 22 _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 5930 _Citation.Page_last 5936 _Citation.Year 2001 _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 Roland Riek . . . 5057 1 2 Peter Guntert . . . 5057 1 3 Heinz Dobeli . . . 5057 1 4 Beat Wipf . . . 5057 1 5 Kurt Wuthrich . . . 5057 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5057 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9636276 _Citation.Full_citation ; Dobeli H, Draeger N, Huber G, Jakob P, Schmidt D, Seilheimer B, Stuber D, Wipf B, Zulauf M. A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide. Biotechnology (N Y). 1995 Sep;13(9):988-93. ; _Citation.Title 'A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biotechnology (N.Y.)' _Citation.Journal_name_full 'Bio/technology (Nature Publishing Company)' _Citation.Journal_volume 13 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0733-222X _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 988 _Citation.Page_last 993 _Citation.Year 1995 _Citation.Details ; Senile plaques, a neuropathological hallmark of Alzheimer's disease, consist primarily of insoluble aggregates of beta-amyloid peptide (A beta). A 42-residue peptide (A beta 1-42) appears to be the predominant form. In contrast to A beta 1-40, A beta 1-42 is characterized by its extreme tendency to aggregate into fibers or precipitate. A tailored biotechnological method prevents aggregation of A beta 1-42 monomers during its production. The method is based on a protein tail fused to the amino terminus of A beta. This tail leads to a high expression in E. coli, and a histidine affinity tag facilitates purification. Selective cleavage of the fusion tail is performed with cyanogen bromide by immobilizing the fusion protein on a reversed phase chromatography column. Cleavage then occurs only at the methionine positioned at the designed site but not at the methionine contained in the membrane anchor sequence of A beta. Furthermore, immobilization prevents aggregation of cleaved A beta. Elution from the HPLC column and all succeeding purification steps are optimized to preserve A beta 1-42 as a monomer. Solutions of monomeric A beta 1-42 spontaneously aggregate into fibers within hours. This permits the investigation of the transition of monomers into fibers and the correlation of physico-chemical properties with biological activities. Mutations of A beta 1-42 at position 35 influence the aggregation properties. Wild-type A beta 1-42 with methionine at position 35 has similar properties as A beta with a methionine sulfoxide residue. The fiber formation tendency, however, is reduced when position 35 is occupied by a glutamine, serine, leucine, or a glutamic acid residue. ; 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 H. Dobeli H. . . 5057 2 2 N. Draeger N. . . 5057 2 3 G. Huber G. . . 5057 2 4 P. Jakob P. . . 5057 2 5 D. Schmidt D. . . 5057 2 6 B. Seilheimer B. . . 5057 2 7 D. Stuber D. . . 5057 2 8 B. Wipf B. . . 5057 2 9 M. Zulauf M. . . 5057 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Ab(1-40) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Ab(1-40) _Assembly.Entry_ID 5057 _Assembly.ID 1 _Assembly.Name 'Alzheimer peptide Ab(1-40) of man' _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5057 1 stop_ 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 Ab(1-40) 1 $Ab(1-40) . . . native . . . . . 5057 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Ab(1-40) abbreviation 5057 1 'Alzheimer peptide Ab(1-40) of man' system 5057 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Ab(1-40) is associated with Alzheimer disease' 5057 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Ab(1-40) _Entity.Sf_category entity _Entity.Sf_framecode Ab(1-40) _Entity.Entry_ID 5057 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Ab _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 AEDVGSNKGAIIGLXVGGVV ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 40 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 97.50 97.50 8.35e-18 . . . . 5057 1 3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 4 no BMRB 17186 . Abeta . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 5 no BMRB 17764 . Abeta . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 6 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 7 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 8 no BMRB 17795 . Abeta(1-40) . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 9 no BMRB 17796 . Abeta40 . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 92.50 38 97.30 97.30 2.04e-15 . . . . 5057 1 11 no BMRB 18127 . beta-amyloid . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 12 no BMRB 18128 . beta-amyloid . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 13 no BMRB 18129 . beta-amyloid . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 14 no BMRB 18131 . beta-amyloid . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 15 no BMRB 19009 . beta-amyloid_peptide . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 16 no BMRB 19309 . amyloid_peptide . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 17 no BMRB 5400 . Abeta1-42 . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 18 no BMRB 6257 . Abeta . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 19 no BMRB 6554 . amyloid . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 20 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 70.00 28 100.00 100.00 1.71e-10 . . . . 5057 1 21 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 70.00 28 100.00 100.00 1.71e-10 . . . . 5057 1 22 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 23 no PDB 1BA4 . "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 24 no PDB 1BA6 . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 100.00 40 100.00 100.00 1.75e-17 . . . . 5057 1 25 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 62.50 26 100.00 100.00 1.09e-07 . . . . 5057 1 26 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 27 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 28 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 29 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 30 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 31 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 32 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 33 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 34 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 35 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 100.00 122 97.50 97.50 8.35e-18 . . . . 5057 1 36 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 37 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 38 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 39 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 40 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 41 no PDB 3BAE . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" . . . . . 70.00 28 100.00 100.00 1.71e-10 . . . . 5057 1 42 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 43 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 70.00 28 100.00 100.00 1.71e-10 . . . . 5057 1 44 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 45 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 46 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 100.00 40 97.50 97.50 1.14e-17 . . . . 5057 1 47 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 48 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 49 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 97.50 97.50 6.85e-18 . . . . 5057 1 50 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 97.50 97.50 9.04e-18 . . . . 5057 1 51 no DBJ BAG10647 . "amyloid beta A4 protein precursor [synthetic construct]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 52 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 97.50 97.50 8.53e-18 . . . . 5057 1 53 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 97.50 97.50 8.47e-18 . . . . 5057 1 54 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 97.50 97.50 2.03e-18 . . . . 5057 1 55 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 97.50 97.50 2.26e-18 . . . . 5057 1 56 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 97.50 97.50 2.26e-18 . . . . 5057 1 57 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.00 97 97.37 97.37 1.50e-16 . . . . 5057 1 58 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 97.50 97.50 9.25e-18 . . . . 5057 1 59 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 75.00 30 100.00 100.00 8.92e-12 . . . . 5057 1 60 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 97.50 97.50 5.76e-18 . . . . 5057 1 61 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 97.50 97.50 8.67e-18 . . . . 5057 1 62 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 100.00 57 97.50 97.50 2.14e-18 . . . . 5057 1 63 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 100.00 57 97.50 97.50 2.14e-18 . . . . 5057 1 64 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 100.00 57 97.50 97.50 2.14e-18 . . . . 5057 1 65 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 100.00 57 97.50 97.50 2.14e-18 . . . . 5057 1 66 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 97.50 97.50 2.88e-18 . . . . 5057 1 67 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 97.50 97.50 9.25e-18 . . . . 5057 1 68 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 97.50 97.50 8.53e-18 . . . . 5057 1 69 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 97.50 97.50 9.29e-18 . . . . 5057 1 70 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 97.50 97.50 5.82e-18 . . . . 5057 1 71 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 97.50 97.50 3.03e-17 . . . . 5057 1 72 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 73 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 74 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 97.50 97.50 7.63e-18 . . . . 5057 1 75 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 97.50 97.50 8.99e-18 . . . . 5057 1 76 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 97.50 97.50 1.07e-17 . . . . 5057 1 77 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 97.50 97.50 7.63e-18 . . . . 5057 1 78 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 97.50 97.50 7.63e-18 . . . . 5057 1 79 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 97.50 97.50 7.63e-18 . . . . 5057 1 80 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 97.50 97.50 2.03e-18 . . . . 5057 1 81 no SP Q28280 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 100.00 58 97.50 97.50 2.26e-18 . . . . 5057 1 82 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 97.50 97.50 8.99e-18 . . . . 5057 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Ab common 5057 1 Ab(1-40) abbreviation 5057 1 Ab(1-40) variant 5057 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 . 5057 1 2 . ALA . 5057 1 3 . GLU . 5057 1 4 . PHE . 5057 1 5 . ARG . 5057 1 6 . HIS . 5057 1 7 . ASP . 5057 1 8 . SER . 5057 1 9 . GLY . 5057 1 10 . TYR . 5057 1 11 . GLU . 5057 1 12 . VAL . 5057 1 13 . HIS . 5057 1 14 . HIS . 5057 1 15 . GLN . 5057 1 16 . LYS . 5057 1 17 . LEU . 5057 1 18 . VAL . 5057 1 19 . PHE . 5057 1 20 . PHE . 5057 1 21 . ALA . 5057 1 22 . GLU . 5057 1 23 . ASP . 5057 1 24 . VAL . 5057 1 25 . GLY . 5057 1 26 . SER . 5057 1 27 . ASN . 5057 1 28 . LYS . 5057 1 29 . GLY . 5057 1 30 . ALA . 5057 1 31 . ILE . 5057 1 32 . ILE . 5057 1 33 . GLY . 5057 1 34 . LEU . 5057 1 35 . SME . 5057 1 36 . VAL . 5057 1 37 . GLY . 5057 1 38 . GLY . 5057 1 39 . VAL . 5057 1 40 . VAL . 5057 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 5057 1 . ALA 2 2 5057 1 . GLU 3 3 5057 1 . PHE 4 4 5057 1 . ARG 5 5 5057 1 . HIS 6 6 5057 1 . ASP 7 7 5057 1 . SER 8 8 5057 1 . GLY 9 9 5057 1 . TYR 10 10 5057 1 . GLU 11 11 5057 1 . VAL 12 12 5057 1 . HIS 13 13 5057 1 . HIS 14 14 5057 1 . GLN 15 15 5057 1 . LYS 16 16 5057 1 . LEU 17 17 5057 1 . VAL 18 18 5057 1 . PHE 19 19 5057 1 . PHE 20 20 5057 1 . ALA 21 21 5057 1 . GLU 22 22 5057 1 . ASP 23 23 5057 1 . VAL 24 24 5057 1 . GLY 25 25 5057 1 . SER 26 26 5057 1 . ASN 27 27 5057 1 . LYS 28 28 5057 1 . GLY 29 29 5057 1 . ALA 30 30 5057 1 . ILE 31 31 5057 1 . ILE 32 32 5057 1 . GLY 33 33 5057 1 . LEU 34 34 5057 1 . SME 35 35 5057 1 . VAL 36 36 5057 1 . GLY 37 37 5057 1 . GLY 38 38 5057 1 . VAL 39 39 5057 1 . VAL 40 40 5057 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 5057 _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 $Ab(1-40) . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5057 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 5057 _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 $Ab(1-40) . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . 'Ab is expressed and purified on the basis of ref_1.' . . 5057 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_SME _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_SME _Chem_comp.Entry_ID 5057 _Chem_comp.ID SME _Chem_comp.Provenance . _Chem_comp.Name 'METHIONINE SULFOXIDE' _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code SME _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 . _Chem_comp.One_letter_code M _Chem_comp.Three_letter_code SME _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 MET _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 H11 N O3 S' _Chem_comp.Formula_weight 165.211 _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 1BA6 _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 Wed Jul 20 15:14:56 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 CS(=O)CCC(C(=O)O)N SMILES 'OpenEye OEToolkits' 1.5.0 5057 SME C[S@@](=O)CC[C@@H](C(=O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5057 SME C[S](=O)CC[CH](N)C(O)=O SMILES CACTVS 3.341 5057 SME C[S@@](=O)CC[C@H](N)C(O)=O SMILES_CANONICAL CACTVS 3.341 5057 SME InChI=1S/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-,10+/m0/s1 InChI InChI 1.03 5057 SME O=C(O)C(N)CCS(=O)C SMILES ACDLabs 10.04 5057 SME QEFRNWWLZKMPFJ-ZXPFJRLXSA-N InChIKey InChI 1.03 5057 SME 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)-2-amino-4-[(R)-methylsulfinyl]butanoic acid' 'SYSTEMATIC NAME' ACDLabs 10.04 5057 SME '(2S)-2-amino-4-[(R)-methylsulfinyl]butanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5057 SME 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 . . . . 7.763 . -0.195 . -10.134 . -1.797 -0.400 -1.472 1 . 5057 SME CA . CA . . C . . S 0 . . . . no no . . . . 6.958 . 0.781 . -10.922 . -0.566 0.400 -1.524 2 . 5057 SME CB . CB . . C . . N 0 . . . . no no . . . . 5.987 . -0.007 . -11.847 . 0.285 0.107 -0.288 3 . 5057 SME CG . CG . . C . . N 0 . . . . no no . . . . 5.729 . 0.796 . -13.133 . -0.504 0.467 0.972 4 . 5057 SME S . S . . S . . R 0 . . . . no no . . . . 4.691 . -0.181 . -14.233 . 0.506 0.120 2.438 5 . 5057 SME OE . OE . . O . . N 0 . . . . no no . . . . 5.421 . -1.423 . -14.572 . 0.742 -1.277 2.530 6 . 5057 SME CE . CE . . C . . N 0 . . . . no no . . . . 4.760 . 0.909 . -15.665 . -0.648 0.626 3.743 7 . 5057 SME C . C . . C . . N 0 . . . . no no . . . . 6.186 . 1.682 . -9.946 . 0.210 0.046 -2.765 8 . 5057 SME O . O . . O . . N 0 . . . . no no . . . . 5.088 . 2.131 . -10.217 . 0.137 -1.067 -3.227 9 . 5057 SME OXT . OXT . . O . . N 0 . . . . no yes . . . . 6.817 . 1.912 . -8.824 . 0.985 0.968 -3.358 10 . 5057 SME H . H . . H . . N 0 . . . . no no . . . . 7.570 . -0.314 . -9.184 . -2.230 -0.208 -0.581 11 . 5057 SME H2 . H2 . . H . . N 0 . . . . no yes . . . . 8.248 . -0.869 . -10.726 . -1.512 -1.368 -1.453 12 . 5057 SME HA . HA . . H . . N 0 . . . . no no . . . . 7.644 . 1.398 . -11.474 . -0.823 1.459 -1.546 13 . 5057 SME HB2 . HB2 . . H . . N 0 . . . . no no . . . . 5.051 . -0.194 . -11.341 . 1.198 0.702 -0.326 14 . 5057 SME HB3 . HB3 . . H . . N 0 . . . . no no . . . . 6.421 . -0.960 . -12.111 . 0.542 -0.951 -0.266 15 . 5057 SME HG2 . HG2 . . H . . N 0 . . . . no no . . . . 6.662 . 1.016 . -13.632 . -1.417 -0.127 1.011 16 . 5057 SME HG3 . HG3 . . H . . N 0 . . . . no no . . . . 5.223 . 1.722 . -12.902 . -0.761 1.526 0.950 17 . 5057 SME HE1 . HE1 . . H . . N 0 . . . . no no . . . . 4.397 . 1.889 . -15.391 . -0.182 0.477 4.717 18 . 5057 SME HE2 . HE2 . . H . . N 0 . . . . no no . . . . 4.143 . 0.505 . -16.454 . -0.899 1.679 3.617 19 . 5057 SME HE3 . HE3 . . H . . N 0 . . . . no no . . . . 5.780 . 0.986 . -16.011 . -1.555 0.025 3.678 20 . 5057 SME HXT . HXT . . H . . N 0 . . . . no yes . . . . 6.339 . 2.469 . -8.220 . 1.484 0.741 -4.154 21 . 5057 SME 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 . 5057 SME 2 . SING N H no N 2 . 5057 SME 3 . SING N H2 no N 3 . 5057 SME 4 . SING CA CB no N 4 . 5057 SME 5 . SING CA C no N 5 . 5057 SME 6 . SING CA HA no N 6 . 5057 SME 7 . SING CB CG no N 7 . 5057 SME 8 . SING CB HB2 no N 8 . 5057 SME 9 . SING CB HB3 no N 9 . 5057 SME 10 . SING CG S no N 10 . 5057 SME 11 . SING CG HG2 no N 11 . 5057 SME 12 . SING CG HG3 no N 12 . 5057 SME 13 . DOUB S OE no N 13 . 5057 SME 14 . SING S CE no N 14 . 5057 SME 15 . SING CE HE1 no N 15 . 5057 SME 16 . SING CE HE2 no N 16 . 5057 SME 17 . SING CE HE3 no N 17 . 5057 SME 18 . DOUB C O no N 18 . 5057 SME 19 . SING C OXT no N 19 . 5057 SME 20 . SING OXT HXT no N 20 . 5057 SME stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5057 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 Ab . . . 1 $Ab(1-40) . . . . 1 mM . . . . 5057 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5057 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.4 0.1 n/a 5057 1 temperature 281 1 K 5057 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5057 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5057 _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 NMR_spectrometer Bruker DRX . 750 . . . 5057 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 5057 _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 . . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5057 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5057 _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 internal direct 1.0 . . . . . . . . . 5057 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5057 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 $sample_1 . 5057 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ASP HA H 1 4.50 0.01 . 1 . . . . . . . . 5057 1 2 . 1 1 1 1 ASP HB2 H 1 2.55 0.01 . 2 . . . . . . . . 5057 1 3 . 1 1 1 1 ASP HB3 H 1 2.69 0.01 . 2 . . . . . . . . 5057 1 4 . 1 1 2 2 ALA H H 1 7.88 0.01 . 1 . . . . . . . . 5057 1 5 . 1 1 2 2 ALA HA H 1 4.09 0.01 . 1 . . . . . . . . 5057 1 6 . 1 1 2 2 ALA HB1 H 1 1.21 0.01 . 1 . . . . . . . . 5057 1 7 . 1 1 2 2 ALA HB2 H 1 1.21 0.01 . 1 . . . . . . . . 5057 1 8 . 1 1 2 2 ALA HB3 H 1 1.21 0.01 . 1 . . . . . . . . 5057 1 9 . 1 1 3 3 GLU H H 1 8.35 0.01 . 1 . . . . . . . . 5057 1 10 . 1 1 3 3 GLU HA H 1 4.01 0.01 . 1 . . . . . . . . 5057 1 11 . 1 1 3 3 GLU HB2 H 1 1.71 0.01 . 2 . . . . . . . . 5057 1 12 . 1 1 3 3 GLU HB3 H 1 1.76 0.01 . 2 . . . . . . . . 5057 1 13 . 1 1 3 3 GLU HG2 H 1 1.97 0.01 . 2 . . . . . . . . 5057 1 14 . 1 1 3 3 GLU HG3 H 1 2.05 0.01 . 2 . . . . . . . . 5057 1 15 . 1 1 4 4 PHE H H 1 8.23 0.01 . 1 . . . . . . . . 5057 1 16 . 1 1 4 4 PHE HA H 1 4.39 0.01 . 1 . . . . . . . . 5057 1 17 . 1 1 4 4 PHE HB2 H 1 2.84 0.01 . 1 . . . . . . . . 5057 1 18 . 1 1 4 4 PHE HB3 H 1 2.84 0.01 . 1 . . . . . . . . 5057 1 19 . 1 1 4 4 PHE HD1 H 1 7.00 0.01 . 1 . . . . . . . . 5057 1 20 . 1 1 4 4 PHE HD2 H 1 7.00 0.01 . 1 . . . . . . . . 5057 1 21 . 1 1 4 4 PHE HE1 H 1 7.09 0.01 . 1 . . . . . . . . 5057 1 22 . 1 1 4 4 PHE HE2 H 1 7.09 0.01 . 1 . . . . . . . . 5057 1 23 . 1 1 4 4 PHE HZ H 1 7.10 0.01 . 1 . . . . . . . . 5057 1 24 . 1 1 5 5 ARG H H 1 8.08 0.01 . 1 . . . . . . . . 5057 1 25 . 1 1 5 5 ARG HA H 1 4.08 0.01 . 1 . . . . . . . . 5057 1 26 . 1 1 5 5 ARG HB2 H 1 1.46 0.01 . 2 . . . . . . . . 5057 1 27 . 1 1 5 5 ARG HB3 H 1 1.57 0.01 . 2 . . . . . . . . 5057 1 28 . 1 1 5 5 ARG HG2 H 1 1.33 0.01 . 1 . . . . . . . . 5057 1 29 . 1 1 5 5 ARG HG3 H 1 1.33 0.01 . 1 . . . . . . . . 5057 1 30 . 1 1 5 5 ARG HD2 H 1 2.95 0.01 . 1 . . . . . . . . 5057 1 31 . 1 1 5 5 ARG HD3 H 1 2.95 0.01 . 1 . . . . . . . . 5057 1 32 . 1 1 7 7 ASP H H 1 8.30 0.01 . 1 . . . . . . . . 5057 1 33 . 1 1 7 7 ASP HA H 1 4.46 0.01 . 1 . . . . . . . . 5057 1 34 . 1 1 7 7 ASP HB2 H 1 2.51 0.01 . 1 . . . . . . . . 5057 1 35 . 1 1 7 7 ASP HB3 H 1 2.51 0.01 . 1 . . . . . . . . 5057 1 36 . 1 1 8 8 SER H H 1 8.35 0.01 . 1 . . . . . . . . 5057 1 37 . 1 1 8 8 SER HA H 1 4.21 0.01 . 1 . . . . . . . . 5057 1 38 . 1 1 8 8 SER HB2 H 1 3.75 0.01 . 2 . . . . . . . . 5057 1 39 . 1 1 8 8 SER HB3 H 1 3.70 0.01 . 2 . . . . . . . . 5057 1 40 . 1 1 9 9 GLY H H 1 8.45 0.01 . 1 . . . . . . . . 5057 1 41 . 1 1 9 9 GLY HA2 H 1 3.77 0.01 . 2 . . . . . . . . 5057 1 42 . 1 1 9 9 GLY HA3 H 1 3.71 0.01 . 2 . . . . . . . . 5057 1 43 . 1 1 10 10 TYR H H 1 7.86 0.01 . 1 . . . . . . . . 5057 1 44 . 1 1 10 10 TYR HA H 1 4.33 0.01 . 1 . . . . . . . . 5057 1 45 . 1 1 10 10 TYR HB2 H 1 2.85 0.01 . 2 . . . . . . . . 5057 1 46 . 1 1 10 10 TYR HB3 H 1 2.79 0.01 . 2 . . . . . . . . 5057 1 47 . 1 1 10 10 TYR HD1 H 1 6.88 0.01 . 1 . . . . . . . . 5057 1 48 . 1 1 10 10 TYR HD2 H 1 6.88 0.01 . 1 . . . . . . . . 5057 1 49 . 1 1 10 10 TYR HE1 H 1 6.59 0.01 . 1 . . . . . . . . 5057 1 50 . 1 1 10 10 TYR HE2 H 1 6.59 0.01 . 1 . . . . . . . . 5057 1 51 . 1 1 11 11 GLU H H 1 8.28 0.01 . 1 . . . . . . . . 5057 1 52 . 1 1 11 11 GLU HA H 1 4.03 0.01 . 1 . . . . . . . . 5057 1 53 . 1 1 11 11 GLU HB2 H 1 1.69 0.01 . 1 . . . . . . . . 5057 1 54 . 1 1 11 11 GLU HB3 H 1 1.69 0.01 . 1 . . . . . . . . 5057 1 55 . 1 1 11 11 GLU HG2 H 1 2.04 0.01 . 1 . . . . . . . . 5057 1 56 . 1 1 11 11 GLU HG3 H 1 2.04 0.01 . 1 . . . . . . . . 5057 1 57 . 1 1 12 12 VAL H H 1 7.97 0.01 . 1 . . . . . . . . 5057 1 58 . 1 1 12 12 VAL HA H 1 3.75 0.01 . 1 . . . . . . . . 5057 1 59 . 1 1 12 12 VAL HB H 1 1.76 0.01 . 1 . . . . . . . . 5057 1 60 . 1 1 12 12 VAL HG11 H 1 0.70 0.01 . 2 . . . . . . . . 5057 1 61 . 1 1 12 12 VAL HG12 H 1 0.70 0.01 . 2 . . . . . . . . 5057 1 62 . 1 1 12 12 VAL HG13 H 1 0.70 0.01 . 2 . . . . . . . . 5057 1 63 . 1 1 12 12 VAL HG21 H 1 0.59 0.01 . 2 . . . . . . . . 5057 1 64 . 1 1 12 12 VAL HG22 H 1 0.59 0.01 . 2 . . . . . . . . 5057 1 65 . 1 1 12 12 VAL HG23 H 1 0.59 0.01 . 2 . . . . . . . . 5057 1 66 . 1 1 13 13 HIS H H 1 8.22 0.01 . 1 . . . . . . . . 5057 1 67 . 1 1 13 13 HIS HA H 1 4.44 0.01 . 1 . . . . . . . . 5057 1 68 . 1 1 13 13 HIS HB2 H 1 2.91 0.01 . 2 . . . . . . . . 5057 1 69 . 1 1 13 13 HIS HB3 H 1 2.85 0.01 . 2 . . . . . . . . 5057 1 70 . 1 1 13 13 HIS HD1 H 1 6.86 0.01 . 1 . . . . . . . . 5057 1 71 . 1 1 14 14 HIS H H 1 8.29 0.01 . 1 . . . . . . . . 5057 1 72 . 1 1 14 14 HIS HA H 1 4.40 0.01 . 1 . . . . . . . . 5057 1 73 . 1 1 14 14 HIS HB2 H 1 2.96 0.01 . 2 . . . . . . . . 5057 1 74 . 1 1 14 14 HIS HB3 H 1 2.90 0.01 . 2 . . . . . . . . 5057 1 75 . 1 1 14 14 HIS HD1 H 1 6.87 0.01 . 1 . . . . . . . . 5057 1 76 . 1 1 15 15 GLN H H 1 8.35 0.01 . 1 . . . . . . . . 5057 1 77 . 1 1 15 15 GLN HA H 1 4.11 0.01 . 1 . . . . . . . . 5057 1 78 . 1 1 15 15 GLN HB2 H 1 1.81 0.01 . 2 . . . . . . . . 5057 1 79 . 1 1 15 15 GLN HB3 H 1 1.89 0.01 . 2 . . . . . . . . 5057 1 80 . 1 1 15 15 GLN HG2 H 1 2.17 0.01 . 1 . . . . . . . . 5057 1 81 . 1 1 15 15 GLN HG3 H 1 2.17 0.01 . 1 . . . . . . . . 5057 1 82 . 1 1 15 15 GLN HE21 H 1 6.80 0.01 . 2 . . . . . . . . 5057 1 83 . 1 1 15 15 GLN HE22 H 1 7.48 0.01 . 2 . . . . . . . . 5057 1 84 . 1 1 16 16 LYS H H 1 8.33 0.01 . 1 . . . . . . . . 5057 1 85 . 1 1 16 16 LYS HA H 1 4.11 0.01 . 1 . . . . . . . . 5057 1 86 . 1 1 16 16 LYS HB2 H 1 1.63 0.01 . 2 . . . . . . . . 5057 1 87 . 1 1 16 16 LYS HB3 H 1 1.58 0.01 . 2 . . . . . . . . 5057 1 88 . 1 1 16 16 LYS HG2 H 1 1.27 0.01 . 2 . . . . . . . . 5057 1 89 . 1 1 16 16 LYS HG3 H 1 1.20 0.01 . 2 . . . . . . . . 5057 1 90 . 1 1 16 16 LYS HD2 H 1 1.50 0.01 . 1 . . . . . . . . 5057 1 91 . 1 1 16 16 LYS HD3 H 1 1.50 0.01 . 1 . . . . . . . . 5057 1 92 . 1 1 16 16 LYS HE2 H 1 2.80 0.01 . 1 . . . . . . . . 5057 1 93 . 1 1 16 16 LYS HE3 H 1 2.80 0.01 . 1 . . . . . . . . 5057 1 94 . 1 1 17 17 LEU H H 1 8.19 0.01 . 1 . . . . . . . . 5057 1 95 . 1 1 17 17 LEU HA H 1 4.17 0.01 . 1 . . . . . . . . 5057 1 96 . 1 1 17 17 LEU HB2 H 1 1.43 0.01 . 1 . . . . . . . . 5057 1 97 . 1 1 17 17 LEU HB3 H 1 1.43 0.01 . 1 . . . . . . . . 5057 1 98 . 1 1 17 17 LEU HG H 1 1.27 0.01 . 1 . . . . . . . . 5057 1 99 . 1 1 17 17 LEU HD11 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 100 . 1 1 17 17 LEU HD12 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 101 . 1 1 17 17 LEU HD13 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 102 . 1 1 17 17 LEU HD21 H 1 0.74 0.01 . 2 . . . . . . . . 5057 1 103 . 1 1 17 17 LEU HD22 H 1 0.74 0.01 . 2 . . . . . . . . 5057 1 104 . 1 1 17 17 LEU HD23 H 1 0.74 0.01 . 2 . . . . . . . . 5057 1 105 . 1 1 18 18 VAL H H 1 7.92 0.01 . 1 . . . . . . . . 5057 1 106 . 1 1 18 18 VAL HA H 1 3.86 0.01 . 1 . . . . . . . . 5057 1 107 . 1 1 18 18 VAL HB H 1 1.73 0.01 . 1 . . . . . . . . 5057 1 108 . 1 1 18 18 VAL HG11 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 109 . 1 1 18 18 VAL HG12 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 110 . 1 1 18 18 VAL HG13 H 1 0.67 0.01 . 2 . . . . . . . . 5057 1 111 . 1 1 18 18 VAL HG21 H 1 0.58 0.01 . 2 . . . . . . . . 5057 1 112 . 1 1 18 18 VAL HG22 H 1 0.58 0.01 . 2 . . . . . . . . 5057 1 113 . 1 1 18 18 VAL HG23 H 1 0.58 0.01 . 2 . . . . . . . . 5057 1 114 . 1 1 19 19 PHE H H 1 8.18 0.01 . 1 . . . . . . . . 5057 1 115 . 1 1 19 19 PHE HA H 1 4.41 0.01 . 1 . . . . . . . . 5057 1 116 . 1 1 19 19 PHE HB2 H 1 2.81 0.01 . 2 . . . . . . . . 5057 1 117 . 1 1 19 19 PHE HB3 H 1 2.74 0.01 . 2 . . . . . . . . 5057 1 118 . 1 1 19 19 PHE HD1 H 1 6.99 0.01 . 1 . . . . . . . . 5057 1 119 . 1 1 19 19 PHE HD2 H 1 6.99 0.01 . 1 . . . . . . . . 5057 1 120 . 1 1 19 19 PHE HE1 H 1 7.14 0.01 . 1 . . . . . . . . 5057 1 121 . 1 1 19 19 PHE HE2 H 1 7.14 0.01 . 1 . . . . . . . . 5057 1 122 . 1 1 19 19 PHE HZ H 1 7.11 0.01 . 1 . . . . . . . . 5057 1 123 . 1 1 20 20 PHE H H 1 8.14 0.01 . 1 . . . . . . . . 5057 1 124 . 1 1 20 20 PHE HA H 1 4.40 0.01 . 1 . . . . . . . . 5057 1 125 . 1 1 20 20 PHE HB2 H 1 2.91 0.01 . 2 . . . . . . . . 5057 1 126 . 1 1 20 20 PHE HB3 H 1 2.76 0.01 . 2 . . . . . . . . 5057 1 127 . 1 1 20 20 PHE HD1 H 1 7.06 0.01 . 1 . . . . . . . . 5057 1 128 . 1 1 20 20 PHE HD2 H 1 7.06 0.01 . 1 . . . . . . . . 5057 1 129 . 1 1 20 20 PHE HE1 H 1 7.15 0.01 . 1 . . . . . . . . 5057 1 130 . 1 1 20 20 PHE HE2 H 1 7.15 0.01 . 1 . . . . . . . . 5057 1 131 . 1 1 20 20 PHE HZ H 1 7.11 0.01 . 1 . . . . . . . . 5057 1 132 . 1 1 21 21 ALA H H 1 8.16 0.01 . 1 . . . . . . . . 5057 1 133 . 1 1 21 21 ALA HA H 1 4.05 0.01 . 1 . . . . . . . . 5057 1 134 . 1 1 21 21 ALA HB1 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 135 . 1 1 21 21 ALA HB2 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 136 . 1 1 21 21 ALA HB3 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 137 . 1 1 22 22 GLU H H 1 8.28 0.01 . 1 . . . . . . . . 5057 1 138 . 1 1 22 22 GLU HA H 1 4.04 0.01 . 1 . . . . . . . . 5057 1 139 . 1 1 22 22 GLU HB2 H 1 1.75 0.01 . 2 . . . . . . . . 5057 1 140 . 1 1 22 22 GLU HB3 H 1 1.87 0.01 . 2 . . . . . . . . 5057 1 141 . 1 1 22 22 GLU HG2 H 1 2.10 0.01 . 1 . . . . . . . . 5057 1 142 . 1 1 22 22 GLU HG3 H 1 2.10 0.01 . 1 . . . . . . . . 5057 1 143 . 1 1 23 23 ASP H H 1 8.34 0.01 . 1 . . . . . . . . 5057 1 144 . 1 1 23 23 ASP HA H 1 4.47 0.01 . 1 . . . . . . . . 5057 1 145 . 1 1 23 23 ASP HB2 H 1 2.57 0.01 . 2 . . . . . . . . 5057 1 146 . 1 1 23 23 ASP HB3 H 1 2.46 0.01 . 2 . . . . . . . . 5057 1 147 . 1 1 24 24 VAL H H 1 8.07 0.01 . 1 . . . . . . . . 5057 1 148 . 1 1 24 24 VAL HA H 1 3.96 0.01 . 1 . . . . . . . . 5057 1 149 . 1 1 24 24 VAL HB H 1 2.02 0.01 . 1 . . . . . . . . 5057 1 150 . 1 1 24 24 VAL HG11 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 151 . 1 1 24 24 VAL HG12 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 152 . 1 1 24 24 VAL HG13 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 153 . 1 1 24 24 VAL HG21 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 154 . 1 1 24 24 VAL HG22 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 155 . 1 1 24 24 VAL HG23 H 1 0.79 0.01 . 1 . . . . . . . . 5057 1 156 . 1 1 25 25 GLY H H 1 8.46 0.01 . 1 . . . . . . . . 5057 1 157 . 1 1 25 25 GLY HA2 H 1 3.81 0.01 . 1 . . . . . . . . 5057 1 158 . 1 1 25 25 GLY HA3 H 1 3.81 0.01 . 1 . . . . . . . . 5057 1 159 . 1 1 26 26 SER H H 1 8.05 0.01 . 1 . . . . . . . . 5057 1 160 . 1 1 26 26 SER HA H 1 4.25 0.01 . 1 . . . . . . . . 5057 1 161 . 1 1 26 26 SER HB2 H 1 3.74 0.01 . 2 . . . . . . . . 5057 1 162 . 1 1 26 26 SER HB3 H 1 3.70 0.01 . 2 . . . . . . . . 5057 1 163 . 1 1 27 27 ASN H H 1 8.39 0.01 . 1 . . . . . . . . 5057 1 164 . 1 1 27 27 ASN HA H 1 4.57 0.01 . 1 . . . . . . . . 5057 1 165 . 1 1 27 27 ASN HB2 H 1 2.71 0.01 . 2 . . . . . . . . 5057 1 166 . 1 1 27 27 ASN HB3 H 1 2.63 0.01 . 2 . . . . . . . . 5057 1 167 . 1 1 27 27 ASN HD21 H 1 6.83 0.01 . 2 . . . . . . . . 5057 1 168 . 1 1 27 27 ASN HD22 H 1 7.55 0.01 . 2 . . . . . . . . 5057 1 169 . 1 1 28 28 LYS H H 1 8.26 0.01 . 1 . . . . . . . . 5057 1 170 . 1 1 28 28 LYS HA H 1 4.10 0.01 . 1 . . . . . . . . 5057 1 171 . 1 1 28 28 LYS HB2 H 1 1.60 0.01 . 2 . . . . . . . . 5057 1 172 . 1 1 28 28 LYS HB3 H 1 1.72 0.01 . 2 . . . . . . . . 5057 1 173 . 1 1 28 28 LYS HG2 H 1 1.30 0.01 . 2 . . . . . . . . 5057 1 174 . 1 1 28 28 LYS HG3 H 1 1.24 0.01 . 2 . . . . . . . . 5057 1 175 . 1 1 28 28 LYS HD2 H 1 1.50 0.01 . 2 . . . . . . . . 5057 1 176 . 1 1 28 28 LYS HE2 H 1 2.81 0.01 . 1 . . . . . . . . 5057 1 177 . 1 1 28 28 LYS HE3 H 1 2.81 0.01 . 1 . . . . . . . . 5057 1 178 . 1 1 29 29 GLY H H 1 8.33 0.01 . 1 . . . . . . . . 5057 1 179 . 1 1 29 29 GLY HA2 H 1 3.75 0.01 . 1 . . . . . . . . 5057 1 180 . 1 1 29 29 GLY HA3 H 1 3.75 0.01 . 1 . . . . . . . . 5057 1 181 . 1 1 30 30 ALA H H 1 7.95 0.01 . 1 . . . . . . . . 5057 1 182 . 1 1 30 30 ALA HA H 1 4.13 0.01 . 1 . . . . . . . . 5057 1 183 . 1 1 30 30 ALA HB1 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 184 . 1 1 30 30 ALA HB2 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 185 . 1 1 30 30 ALA HB3 H 1 1.20 0.01 . 1 . . . . . . . . 5057 1 186 . 1 1 31 31 ILE H H 1 8.10 0.01 . 1 . . . . . . . . 5057 1 187 . 1 1 31 31 ILE HA H 1 3.98 0.01 . 1 . . . . . . . . 5057 1 188 . 1 1 31 31 ILE HB H 1 1.69 0.01 . 1 . . . . . . . . 5057 1 189 . 1 1 31 31 ILE HG21 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 190 . 1 1 31 31 ILE HG22 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 191 . 1 1 31 31 ILE HG23 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 192 . 1 1 31 31 ILE HG12 H 1 1.03 0.01 . 2 . . . . . . . . 5057 1 193 . 1 1 31 31 ILE HG13 H 1 1.33 0.01 . 2 . . . . . . . . 5057 1 194 . 1 1 31 31 ILE HD11 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 195 . 1 1 31 31 ILE HD12 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 196 . 1 1 31 31 ILE HD13 H 1 0.70 0.01 . 1 . . . . . . . . 5057 1 197 . 1 1 32 32 ILE H H 1 8.21 0.01 . 1 . . . . . . . . 5057 1 198 . 1 1 32 32 ILE HA H 1 3.99 0.01 . 1 . . . . . . . . 5057 1 199 . 1 1 32 32 ILE HB H 1 1.69 0.01 . 1 . . . . . . . . 5057 1 200 . 1 1 32 32 ILE HG12 H 1 1.04 0.01 . 2 . . . . . . . . 5057 1 201 . 1 1 32 32 ILE HG13 H 1 1.33 0.01 . 2 . . . . . . . . 5057 1 202 . 1 1 32 32 ILE HD11 H 1 0.75 0.01 . 1 . . . . . . . . 5057 1 203 . 1 1 32 32 ILE HD12 H 1 0.75 0.01 . 1 . . . . . . . . 5057 1 204 . 1 1 32 32 ILE HD13 H 1 0.75 0.01 . 1 . . . . . . . . 5057 1 205 . 1 1 33 33 GLY H H 1 8.39 0.01 . 1 . . . . . . . . 5057 1 206 . 1 1 33 33 GLY HA2 H 1 3.80 0.01 . 2 . . . . . . . . 5057 1 207 . 1 1 33 33 GLY HA3 H 1 3.75 0.01 . 2 . . . . . . . . 5057 1 208 . 1 1 34 34 LEU H H 1 7.99 0.01 . 1 . . . . . . . . 5057 1 209 . 1 1 34 34 LEU HA H 1 4.17 0.01 . 1 . . . . . . . . 5057 1 210 . 1 1 34 34 LEU HB2 H 1 1.44 0.01 . 1 . . . . . . . . 5057 1 211 . 1 1 34 34 LEU HB3 H 1 1.44 0.01 . 1 . . . . . . . . 5057 1 212 . 1 1 34 34 LEU HG H 1 1.44 0.01 . 1 . . . . . . . . 5057 1 213 . 1 1 34 34 LEU HD11 H 1 0.71 0.01 . 2 . . . . . . . . 5057 1 214 . 1 1 34 34 LEU HD12 H 1 0.71 0.01 . 2 . . . . . . . . 5057 1 215 . 1 1 34 34 LEU HD13 H 1 0.71 0.01 . 2 . . . . . . . . 5057 1 216 . 1 1 34 34 LEU HD21 H 1 0.76 0.01 . 2 . . . . . . . . 5057 1 217 . 1 1 34 34 LEU HD22 H 1 0.76 0.01 . 2 . . . . . . . . 5057 1 218 . 1 1 34 34 LEU HD23 H 1 0.76 0.01 . 2 . . . . . . . . 5057 1 219 . 1 1 35 35 SME H H 1 8.54 0.01 . 1 . . . . . . . . 5057 1 220 . 1 1 35 35 SME HA H 1 4.42 0.01 . 1 . . . . . . . . 5057 1 221 . 1 1 35 35 SME HB2 H 1 2.08 0.01 . 2 . . . . . . . . 5057 1 222 . 1 1 35 35 SME HB3 H 1 2.00 0.01 . 2 . . . . . . . . 5057 1 223 . 1 1 35 35 SME HG2 H 1 2.79 0.01 . 2 . . . . . . . . 5057 1 224 . 1 1 35 35 SME HG3 H 1 2.79 0.01 . 2 . . . . . . . . 5057 1 225 . 1 1 36 36 VAL H H 1 8.29 0.01 . 1 . . . . . . . . 5057 1 226 . 1 1 36 36 VAL HA H 1 3.97 0.01 . 1 . . . . . . . . 5057 1 227 . 1 1 36 36 VAL HB H 1 1.92 0.01 . 1 . . . . . . . . 5057 1 228 . 1 1 36 36 VAL HG21 H 1 0.78 0.01 . 2 . . . . . . . . 5057 1 229 . 1 1 36 36 VAL HG22 H 1 0.78 0.01 . 2 . . . . . . . . 5057 1 230 . 1 1 36 36 VAL HG23 H 1 0.78 0.01 . 2 . . . . . . . . 5057 1 231 . 1 1 37 37 GLY H H 1 8.53 0.01 . 1 . . . . . . . . 5057 1 232 . 1 1 37 37 GLY HA2 H 1 3.82 0.01 . 1 . . . . . . . . 5057 1 233 . 1 1 37 37 GLY HA3 H 1 3.82 0.01 . 1 . . . . . . . . 5057 1 234 . 1 1 38 38 GLY H H 1 8.20 0.01 . 1 . . . . . . . . 5057 1 235 . 1 1 38 38 GLY HA2 H 1 3.85 0.01 . 2 . . . . . . . . 5057 1 236 . 1 1 38 38 GLY HA3 H 1 3.77 0.01 . 2 . . . . . . . . 5057 1 237 . 1 1 39 39 VAL H H 1 8.01 0.01 . 1 . . . . . . . . 5057 1 238 . 1 1 39 39 VAL HA H 1 4.00 0.01 . 1 . . . . . . . . 5057 1 239 . 1 1 39 39 VAL HB H 1 1.91 0.01 . 1 . . . . . . . . 5057 1 240 . 1 1 39 39 VAL HG11 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 241 . 1 1 39 39 VAL HG12 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 242 . 1 1 39 39 VAL HG13 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 243 . 1 1 39 39 VAL HG21 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 244 . 1 1 39 39 VAL HG22 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 245 . 1 1 39 39 VAL HG23 H 1 0.77 0.01 . 1 . . . . . . . . 5057 1 246 . 1 1 40 40 VAL H H 1 7.73 0.01 . 1 . . . . . . . . 5057 1 247 . 1 1 40 40 VAL HA H 1 4.01 0.01 . 1 . . . . . . . . 5057 1 248 . 1 1 40 40 VAL HB H 1 1.91 0.01 . 1 . . . . . . . . 5057 1 249 . 1 1 40 40 VAL HG11 H 1 0.77 0.01 . 2 . . . . . . . . 5057 1 250 . 1 1 40 40 VAL HG12 H 1 0.77 0.01 . 2 . . . . . . . . 5057 1 251 . 1 1 40 40 VAL HG13 H 1 0.77 0.01 . 2 . . . . . . . . 5057 1 252 . 1 1 40 40 VAL HG21 H 1 0.75 0.01 . 2 . . . . . . . . 5057 1 253 . 1 1 40 40 VAL HG22 H 1 0.75 0.01 . 2 . . . . . . . . 5057 1 254 . 1 1 40 40 VAL HG23 H 1 0.75 0.01 . 2 . . . . . . . . 5057 1 stop_ save_