data_5664 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5664 _Entry.Title ; Full 1H and 15N Chemical Shift Assignments for Oxytetracycline Acyl Carrier Protein ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-01-20 _Entry.Accession_date 2003-01-21 _Entry.Last_release_date 2003-08-08 _Entry.Original_release_date 2003-08-08 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _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 Stuart Findlow . C . 5664 2 Claire Winsor . . . 5664 3 Christopher Dempsey . E . 5664 4 John Crosby . . . 5664 5 Thomas Simpson . J . 5664 6 Matthew Crump . P . 5664 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5664 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 585 5664 '15N chemical shifts' 95 5664 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 . . 2003-08-08 2003-01-20 original author . 5664 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5664 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22744256 _Citation.DOI . _Citation.PubMed_ID 12859187 _Citation.Full_citation . _Citation.Title ; Solution Structure and Dynamics of Oxytetracycline Polyketide Synthase Acyl Carrier Protein from Streptomyces rimosus ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 42 _Citation.Journal_issue 28 _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 8423 _Citation.Page_last 8433 _Citation.Year 2003 _Citation.Details ; The paper reports a high resolution solution structure and dynamics of the oxytetracycline acyl carrier protein. Complete proton and nitrogen chemical shift assignments were achieved using 15N labelled ACP. ; 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 Stuart Findlow . C. . 5664 1 2 Claire Winsor . . . 5664 1 3 Thomas Simpson . J. . 5664 1 4 John Crosby . . . 5664 1 5 Matthew Crump . P. . 5664 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID NMR 5664 1 'solution structure' 5664 1 oxytetracycline 5664 1 'polyketide synthase' 5664 1 dynamics 5664 1 ACP 5664 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5664 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8163168 _Citation.Full_citation ; Kim ES, Bibb MJ, Butler MJ, Hopwood DA, Sherman DH. Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus. Gene. 1994 Apr 8;141(1):141-2. ; _Citation.Title 'Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Gene _Citation.Journal_name_full Gene _Citation.Journal_volume 141 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0378-1119 _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 141 _Citation.Page_last 142 _Citation.Year 1994 _Citation.Details ; The complete nucleotide sequences of the Streptomyces rimosus oxytetracycline (oxyTc) polyketide synthase (PKS)-encoding genes (otcY) has been determined, revealing three open reading frames. The deduced amino-acid sequences correspond to the presumed heterodimeric beta-ketoacyl synthase and acyl carrier protein found in other type-II (multicomponent) PKS systems that specify construction of acetate-derived polyketide antibiotics. ; 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 'E S' Kim E. S. . 5664 2 2 'M J' Bibb M. J. . 5664 2 3 'M J' Butler M. J. . 5664 2 4 'D A' Hopwood D. A. . 5664 2 5 'D H' Sherman D. H. . 5664 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_otc_ACP _Assembly.Sf_category assembly _Assembly.Sf_framecode system_otc_ACP _Assembly.Entry_ID 5664 _Assembly.ID 1 _Assembly.Name 'oxytetracycline acyl carrier protein' _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 reported' _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 5664 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 'otc ACP' 1 $otc_ACP . . . native . . . . . 5664 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes Swiss-prot P43677 . . . . . . 5664 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'oxytetracycline acyl carrier protein' system 5664 1 'otc ACP' abbreviation 5664 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'acyl carrier protein' 5664 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_otc_ACP _Entity.Sf_category entity _Entity.Sf_framecode otc_ACP _Entity.Entry_ID 5664 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Acyl Carrier Protein' _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 ; MTLLTLSDLLTLLRECAGEE ESIDLGGDVEDVAFDALGYD SLALLNTVGRIERDYGVQLG DDAVEKATTPRALIEMTNAS LTGASPSAGGAARDK ; _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 95 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 9916 _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 PDB 1NQ4 . "Solution Structure Of Oxytetracycline Acyl Carrier Protein" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 2 no EMBL CAA80986 . "polyketide acyl carrier protein [Streptomyces rimosus]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 3 no GB AAA03334 . "acyl-carrier protein [Streptomyces rimosus]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 4 no GB AAZ78327 . "OxyC [Streptomyces rimosus]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 5 no GB ELQ83294 . "phosphopantetheine-binding protein [Streptomyces rimosus subsp. rimosus ATCC 10970]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 6 no GB KEF12048 . "actinorhodin polyketide synthase acyl carrier protein [Streptomyces rimosus R6-500]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 7 no REF WP_003981021 . "MULTISPECIES: phosphopantetheine-binding protein [Streptomyces]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 8 no REF WP_030372734 . "MULTISPECIES: actinorhodin polyketide synthase acyl carrier protein [Streptomyces]" . . . . . 100.00 95 98.95 100.00 5.37e-57 . . . . 5664 1 9 no SP P43677 . "RecName: Full=Oxytetracycline polyketide synthase acyl carrier protein; Short=ACP [Streptomyces rimosus]" . . . . . 100.00 95 100.00 100.00 6.85e-58 . . . . 5664 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Acyl Carrier Protein' common 5664 1 ACP abbreviation 5664 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 . MET . 5664 1 2 . THR . 5664 1 3 . LEU . 5664 1 4 . LEU . 5664 1 5 . THR . 5664 1 6 . LEU . 5664 1 7 . SER . 5664 1 8 . ASP . 5664 1 9 . LEU . 5664 1 10 . LEU . 5664 1 11 . THR . 5664 1 12 . LEU . 5664 1 13 . LEU . 5664 1 14 . ARG . 5664 1 15 . GLU . 5664 1 16 . CYS . 5664 1 17 . ALA . 5664 1 18 . GLY . 5664 1 19 . GLU . 5664 1 20 . GLU . 5664 1 21 . GLU . 5664 1 22 . SER . 5664 1 23 . ILE . 5664 1 24 . ASP . 5664 1 25 . LEU . 5664 1 26 . GLY . 5664 1 27 . GLY . 5664 1 28 . ASP . 5664 1 29 . VAL . 5664 1 30 . GLU . 5664 1 31 . ASP . 5664 1 32 . VAL . 5664 1 33 . ALA . 5664 1 34 . PHE . 5664 1 35 . ASP . 5664 1 36 . ALA . 5664 1 37 . LEU . 5664 1 38 . GLY . 5664 1 39 . TYR . 5664 1 40 . ASP . 5664 1 41 . SER . 5664 1 42 . LEU . 5664 1 43 . ALA . 5664 1 44 . LEU . 5664 1 45 . LEU . 5664 1 46 . ASN . 5664 1 47 . THR . 5664 1 48 . VAL . 5664 1 49 . GLY . 5664 1 50 . ARG . 5664 1 51 . ILE . 5664 1 52 . GLU . 5664 1 53 . ARG . 5664 1 54 . ASP . 5664 1 55 . TYR . 5664 1 56 . GLY . 5664 1 57 . VAL . 5664 1 58 . GLN . 5664 1 59 . LEU . 5664 1 60 . GLY . 5664 1 61 . ASP . 5664 1 62 . ASP . 5664 1 63 . ALA . 5664 1 64 . VAL . 5664 1 65 . GLU . 5664 1 66 . LYS . 5664 1 67 . ALA . 5664 1 68 . THR . 5664 1 69 . THR . 5664 1 70 . PRO . 5664 1 71 . ARG . 5664 1 72 . ALA . 5664 1 73 . LEU . 5664 1 74 . ILE . 5664 1 75 . GLU . 5664 1 76 . MET . 5664 1 77 . THR . 5664 1 78 . ASN . 5664 1 79 . ALA . 5664 1 80 . SER . 5664 1 81 . LEU . 5664 1 82 . THR . 5664 1 83 . GLY . 5664 1 84 . ALA . 5664 1 85 . SER . 5664 1 86 . PRO . 5664 1 87 . SER . 5664 1 88 . ALA . 5664 1 89 . GLY . 5664 1 90 . GLY . 5664 1 91 . ALA . 5664 1 92 . ALA . 5664 1 93 . ARG . 5664 1 94 . ASP . 5664 1 95 . LYS . 5664 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 . MET 1 1 5664 1 . THR 2 2 5664 1 . LEU 3 3 5664 1 . LEU 4 4 5664 1 . THR 5 5 5664 1 . LEU 6 6 5664 1 . SER 7 7 5664 1 . ASP 8 8 5664 1 . LEU 9 9 5664 1 . LEU 10 10 5664 1 . THR 11 11 5664 1 . LEU 12 12 5664 1 . LEU 13 13 5664 1 . ARG 14 14 5664 1 . GLU 15 15 5664 1 . CYS 16 16 5664 1 . ALA 17 17 5664 1 . GLY 18 18 5664 1 . GLU 19 19 5664 1 . GLU 20 20 5664 1 . GLU 21 21 5664 1 . SER 22 22 5664 1 . ILE 23 23 5664 1 . ASP 24 24 5664 1 . LEU 25 25 5664 1 . GLY 26 26 5664 1 . GLY 27 27 5664 1 . ASP 28 28 5664 1 . VAL 29 29 5664 1 . GLU 30 30 5664 1 . ASP 31 31 5664 1 . VAL 32 32 5664 1 . ALA 33 33 5664 1 . PHE 34 34 5664 1 . ASP 35 35 5664 1 . ALA 36 36 5664 1 . LEU 37 37 5664 1 . GLY 38 38 5664 1 . TYR 39 39 5664 1 . ASP 40 40 5664 1 . SER 41 41 5664 1 . LEU 42 42 5664 1 . ALA 43 43 5664 1 . LEU 44 44 5664 1 . LEU 45 45 5664 1 . ASN 46 46 5664 1 . THR 47 47 5664 1 . VAL 48 48 5664 1 . GLY 49 49 5664 1 . ARG 50 50 5664 1 . ILE 51 51 5664 1 . GLU 52 52 5664 1 . ARG 53 53 5664 1 . ASP 54 54 5664 1 . TYR 55 55 5664 1 . GLY 56 56 5664 1 . VAL 57 57 5664 1 . GLN 58 58 5664 1 . LEU 59 59 5664 1 . GLY 60 60 5664 1 . ASP 61 61 5664 1 . ASP 62 62 5664 1 . ALA 63 63 5664 1 . VAL 64 64 5664 1 . GLU 65 65 5664 1 . LYS 66 66 5664 1 . ALA 67 67 5664 1 . THR 68 68 5664 1 . THR 69 69 5664 1 . PRO 70 70 5664 1 . ARG 71 71 5664 1 . ALA 72 72 5664 1 . LEU 73 73 5664 1 . ILE 74 74 5664 1 . GLU 75 75 5664 1 . MET 76 76 5664 1 . THR 77 77 5664 1 . ASN 78 78 5664 1 . ALA 79 79 5664 1 . SER 80 80 5664 1 . LEU 81 81 5664 1 . THR 82 82 5664 1 . GLY 83 83 5664 1 . ALA 84 84 5664 1 . SER 85 85 5664 1 . PRO 86 86 5664 1 . SER 87 87 5664 1 . ALA 88 88 5664 1 . GLY 89 89 5664 1 . GLY 90 90 5664 1 . ALA 91 91 5664 1 . ALA 92 92 5664 1 . ARG 93 93 5664 1 . ASP 94 94 5664 1 . LYS 95 95 5664 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 5664 _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 $otc_ACP . 1927 . . 'Streptomyces rimosus' 'soil bacterium' . . Eubacteria . Streptomyces rimosus . . . . . . . . . . . . . . . . otcY1-3 . . . . 5664 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 5664 _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 $otc_ACP . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . . . . . . . pT-7 . . . . . . 5664 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5664 _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 'Acyl Carrier Protein' '[U-97% 15N]' . . 1 $otc_ACP . . 1 . . mM . . . . 5664 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 5664 _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 5.3 0.2 na 5664 1 temperature 298 0.5 K 5664 1 'ionic strength' 0.015 0.002 M 5664 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5664 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'NMR data processing' 5664 1 stop_ save_ save_Pipp _Software.Sf_category software _Software.Sf_framecode Pipp _Software.Entry_ID 5664 _Software.ID 2 _Software.Name Pipp _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'NMR data assignment' 5664 2 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 5664 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5664 _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 Varian INOVA . 600 . . . 5664 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 5664 _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 '1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 2 '1H-1H TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 3 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 4 '1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 5 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 6 HNHA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5664 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-1H TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5664 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNHA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 5664 _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 . . . . . . . . . 5664 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 5664 _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 '1H-1H NOESY' 1 $sample_1 . 5664 1 2 '1H-1H TOCSY' 1 $sample_1 . 5664 1 3 '1H-15N NOESY' 1 $sample_1 . 5664 1 4 '1H-15N TOCSY' 1 $sample_1 . 5664 1 5 '1H-15N HSQC' 1 $sample_1 . 5664 1 6 HNHA 1 $sample_1 . 5664 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 MET HA H 1 4.184 0.02 . 1 . . . . . . . . 5664 1 2 . 1 1 1 1 MET HB2 H 1 2.173 0.02 . 2 . . . . . . . . 5664 1 3 . 1 1 1 1 MET HG2 H 1 2.545 0.02 . 2 . . . . . . . . 5664 1 4 . 1 1 2 2 THR N N 15 121.402 0.05 . 1 . . . . . . . . 5664 1 5 . 1 1 2 2 THR H H 1 8.590 0.02 . 1 . . . . . . . . 5664 1 6 . 1 1 2 2 THR HA H 1 4.400 0.02 . 1 . . . . . . . . 5664 1 7 . 1 1 2 2 THR HB H 1 4.099 0.02 . 1 . . . . . . . . 5664 1 8 . 1 1 2 2 THR HG21 H 1 1.304 0.02 . 1 . . . . . . . . 5664 1 9 . 1 1 2 2 THR HG22 H 1 1.304 0.02 . 1 . . . . . . . . 5664 1 10 . 1 1 2 2 THR HG23 H 1 1.304 0.02 . 1 . . . . . . . . 5664 1 11 . 1 1 3 3 LEU N N 15 123.119 0.05 . 1 . . . . . . . . 5664 1 12 . 1 1 3 3 LEU H H 1 7.990 0.02 . 1 . . . . . . . . 5664 1 13 . 1 1 3 3 LEU HA H 1 4.305 0.02 . 1 . . . . . . . . 5664 1 14 . 1 1 3 3 LEU HB3 H 1 1.552 0.02 . 2 . . . . . . . . 5664 1 15 . 1 1 3 3 LEU HB2 H 1 1.493 0.02 . 2 . . . . . . . . 5664 1 16 . 1 1 3 3 LEU HG H 1 1.369 0.02 . 1 . . . . . . . . 5664 1 17 . 1 1 3 3 LEU HD11 H 1 0.776 0.02 . 2 . . . . . . . . 5664 1 18 . 1 1 3 3 LEU HD12 H 1 0.776 0.02 . 2 . . . . . . . . 5664 1 19 . 1 1 3 3 LEU HD13 H 1 0.776 0.02 . 2 . . . . . . . . 5664 1 20 . 1 1 3 3 LEU HD21 H 1 0.767 0.02 . 2 . . . . . . . . 5664 1 21 . 1 1 3 3 LEU HD22 H 1 0.767 0.02 . 2 . . . . . . . . 5664 1 22 . 1 1 3 3 LEU HD23 H 1 0.767 0.02 . 2 . . . . . . . . 5664 1 23 . 1 1 4 4 LEU N N 15 125.172 0.05 . 1 . . . . . . . . 5664 1 24 . 1 1 4 4 LEU H H 1 9.403 0.02 . 1 . . . . . . . . 5664 1 25 . 1 1 4 4 LEU HA H 1 4.430 0.02 . 1 . . . . . . . . 5664 1 26 . 1 1 4 4 LEU HB2 H 1 1.643 0.02 . 2 . . . . . . . . 5664 1 27 . 1 1 4 4 LEU HG H 1 1.451 0.02 . 1 . . . . . . . . 5664 1 28 . 1 1 4 4 LEU HD11 H 1 0.680 0.02 . 2 . . . . . . . . 5664 1 29 . 1 1 4 4 LEU HD12 H 1 0.680 0.02 . 2 . . . . . . . . 5664 1 30 . 1 1 4 4 LEU HD13 H 1 0.680 0.02 . 2 . . . . . . . . 5664 1 31 . 1 1 4 4 LEU HD21 H 1 0.721 0.02 . 2 . . . . . . . . 5664 1 32 . 1 1 4 4 LEU HD22 H 1 0.721 0.02 . 2 . . . . . . . . 5664 1 33 . 1 1 4 4 LEU HD23 H 1 0.721 0.02 . 2 . . . . . . . . 5664 1 34 . 1 1 5 5 THR N N 15 115.421 0.05 . 1 . . . . . . . . 5664 1 35 . 1 1 5 5 THR H H 1 7.607 0.02 . 1 . . . . . . . . 5664 1 36 . 1 1 5 5 THR HA H 1 4.697 0.02 . 1 . . . . . . . . 5664 1 37 . 1 1 5 5 THR HB H 1 4.530 0.02 . 1 . . . . . . . . 5664 1 38 . 1 1 5 5 THR HG21 H 1 1.214 0.02 . 1 . . . . . . . . 5664 1 39 . 1 1 5 5 THR HG22 H 1 1.214 0.02 . 1 . . . . . . . . 5664 1 40 . 1 1 5 5 THR HG23 H 1 1.214 0.02 . 1 . . . . . . . . 5664 1 41 . 1 1 6 6 LEU N N 15 122.648 0.05 . 1 . . . . . . . . 5664 1 42 . 1 1 6 6 LEU H H 1 8.964 0.02 . 1 . . . . . . . . 5664 1 43 . 1 1 6 6 LEU HA H 1 4.017 0.02 . 1 . . . . . . . . 5664 1 44 . 1 1 6 6 LEU HB2 H 1 1.880 0.02 . 2 . . . . . . . . 5664 1 45 . 1 1 6 6 LEU HG H 1 1.389 0.02 . 1 . . . . . . . . 5664 1 46 . 1 1 6 6 LEU HD11 H 1 0.792 0.02 . 2 . . . . . . . . 5664 1 47 . 1 1 6 6 LEU HD12 H 1 0.792 0.02 . 2 . . . . . . . . 5664 1 48 . 1 1 6 6 LEU HD13 H 1 0.792 0.02 . 2 . . . . . . . . 5664 1 49 . 1 1 6 6 LEU HD21 H 1 0.924 0.02 . 2 . . . . . . . . 5664 1 50 . 1 1 6 6 LEU HD22 H 1 0.924 0.02 . 2 . . . . . . . . 5664 1 51 . 1 1 6 6 LEU HD23 H 1 0.924 0.02 . 2 . . . . . . . . 5664 1 52 . 1 1 7 7 SER N N 15 112.478 0.05 . 1 . . . . . . . . 5664 1 53 . 1 1 7 7 SER H H 1 8.582 0.02 . 1 . . . . . . . . 5664 1 54 . 1 1 7 7 SER HA H 1 4.053 0.02 . 1 . . . . . . . . 5664 1 55 . 1 1 7 7 SER HB3 H 1 3.870 0.02 . 2 . . . . . . . . 5664 1 56 . 1 1 7 7 SER HB2 H 1 3.860 0.02 . 2 . . . . . . . . 5664 1 57 . 1 1 8 8 ASP N N 15 120.568 0.05 . 1 . . . . . . . . 5664 1 58 . 1 1 8 8 ASP H H 1 7.511 0.02 . 1 . . . . . . . . 5664 1 59 . 1 1 8 8 ASP HA H 1 4.491 0.02 . 1 . . . . . . . . 5664 1 60 . 1 1 8 8 ASP HB3 H 1 2.667 0.02 . 1 . . . . . . . . 5664 1 61 . 1 1 8 8 ASP HB2 H 1 2.812 0.02 . 1 . . . . . . . . 5664 1 62 . 1 1 9 9 LEU N N 15 121.456 0.05 . 1 . . . . . . . . 5664 1 63 . 1 1 9 9 LEU H H 1 8.504 0.02 . 1 . . . . . . . . 5664 1 64 . 1 1 9 9 LEU HA H 1 4.035 0.02 . 1 . . . . . . . . 5664 1 65 . 1 1 9 9 LEU HB3 H 1 2.178 0.02 . 1 . . . . . . . . 5664 1 66 . 1 1 9 9 LEU HB2 H 1 1.347 0.02 . 1 . . . . . . . . 5664 1 67 . 1 1 9 9 LEU HG H 1 1.602 0.02 . 1 . . . . . . . . 5664 1 68 . 1 1 9 9 LEU HD11 H 1 0.794 0.02 . 2 . . . . . . . . 5664 1 69 . 1 1 9 9 LEU HD12 H 1 0.794 0.02 . 2 . . . . . . . . 5664 1 70 . 1 1 9 9 LEU HD13 H 1 0.794 0.02 . 2 . . . . . . . . 5664 1 71 . 1 1 9 9 LEU HD21 H 1 1.038 0.02 . 2 . . . . . . . . 5664 1 72 . 1 1 9 9 LEU HD22 H 1 1.038 0.02 . 2 . . . . . . . . 5664 1 73 . 1 1 9 9 LEU HD23 H 1 1.038 0.02 . 2 . . . . . . . . 5664 1 74 . 1 1 10 10 LEU N N 15 118.044 0.05 . 1 . . . . . . . . 5664 1 75 . 1 1 10 10 LEU H H 1 8.756 0.02 . 1 . . . . . . . . 5664 1 76 . 1 1 10 10 LEU HA H 1 4.042 0.02 . 1 . . . . . . . . 5664 1 77 . 1 1 10 10 LEU HB2 H 1 1.968 0.02 . 2 . . . . . . . . 5664 1 78 . 1 1 10 10 LEU HG H 1 1.507 0.02 . 1 . . . . . . . . 5664 1 79 . 1 1 10 10 LEU HD11 H 1 0.854 0.02 . 2 . . . . . . . . 5664 1 80 . 1 1 10 10 LEU HD12 H 1 0.854 0.02 . 2 . . . . . . . . 5664 1 81 . 1 1 10 10 LEU HD13 H 1 0.854 0.02 . 2 . . . . . . . . 5664 1 82 . 1 1 10 10 LEU HD21 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 83 . 1 1 10 10 LEU HD22 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 84 . 1 1 10 10 LEU HD23 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 85 . 1 1 11 11 THR N N 15 117.151 0.05 . 1 . . . . . . . . 5664 1 86 . 1 1 11 11 THR H H 1 7.714 0.02 . 1 . . . . . . . . 5664 1 87 . 1 1 11 11 THR HA H 1 3.930 0.02 . 1 . . . . . . . . 5664 1 88 . 1 1 11 11 THR HB H 1 4.389 0.02 . 1 . . . . . . . . 5664 1 89 . 1 1 11 11 THR HG21 H 1 1.224 0.02 . 1 . . . . . . . . 5664 1 90 . 1 1 11 11 THR HG22 H 1 1.224 0.02 . 1 . . . . . . . . 5664 1 91 . 1 1 11 11 THR HG23 H 1 1.224 0.02 . 1 . . . . . . . . 5664 1 92 . 1 1 12 12 LEU N N 15 122.565 0.05 . 1 . . . . . . . . 5664 1 93 . 1 1 12 12 LEU H H 1 7.894 0.02 . 1 . . . . . . . . 5664 1 94 . 1 1 12 12 LEU HA H 1 4.040 0.02 . 1 . . . . . . . . 5664 1 95 . 1 1 12 12 LEU HB3 H 1 2.062 0.02 . 2 . . . . . . . . 5664 1 96 . 1 1 12 12 LEU HB2 H 1 2.020 0.02 . 2 . . . . . . . . 5664 1 97 . 1 1 12 12 LEU HG H 1 1.388 0.02 . 1 . . . . . . . . 5664 1 98 . 1 1 12 12 LEU HD11 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 99 . 1 1 12 12 LEU HD12 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 100 . 1 1 12 12 LEU HD13 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 101 . 1 1 12 12 LEU HD21 H 1 0.930 0.02 . 2 . . . . . . . . 5664 1 102 . 1 1 12 12 LEU HD22 H 1 0.930 0.02 . 2 . . . . . . . . 5664 1 103 . 1 1 12 12 LEU HD23 H 1 0.930 0.02 . 2 . . . . . . . . 5664 1 104 . 1 1 13 13 LEU N N 15 120.535 0.05 . 1 . . . . . . . . 5664 1 105 . 1 1 13 13 LEU H H 1 8.697 0.02 . 1 . . . . . . . . 5664 1 106 . 1 1 13 13 LEU HA H 1 3.812 0.02 . 1 . . . . . . . . 5664 1 107 . 1 1 13 13 LEU HB2 H 1 1.564 0.02 . 2 . . . . . . . . 5664 1 108 . 1 1 13 13 LEU HG H 1 1.372 0.02 . 1 . . . . . . . . 5664 1 109 . 1 1 13 13 LEU HD11 H 1 0.412 0.02 . 2 . . . . . . . . 5664 1 110 . 1 1 13 13 LEU HD12 H 1 0.412 0.02 . 2 . . . . . . . . 5664 1 111 . 1 1 13 13 LEU HD13 H 1 0.412 0.02 . 2 . . . . . . . . 5664 1 112 . 1 1 13 13 LEU HD21 H 1 0.614 0.02 . 2 . . . . . . . . 5664 1 113 . 1 1 13 13 LEU HD22 H 1 0.614 0.02 . 2 . . . . . . . . 5664 1 114 . 1 1 13 13 LEU HD23 H 1 0.614 0.02 . 2 . . . . . . . . 5664 1 115 . 1 1 14 14 ARG N N 15 117.212 0.05 . 1 . . . . . . . . 5664 1 116 . 1 1 14 14 ARG H H 1 7.692 0.02 . 1 . . . . . . . . 5664 1 117 . 1 1 14 14 ARG HA H 1 4.166 0.02 . 1 . . . . . . . . 5664 1 118 . 1 1 14 14 ARG HB3 H 1 1.877 0.02 . 2 . . . . . . . . 5664 1 119 . 1 1 14 14 ARG HB2 H 1 1.711 0.02 . 2 . . . . . . . . 5664 1 120 . 1 1 14 14 ARG HG2 H 1 1.990 0.02 . 2 . . . . . . . . 5664 1 121 . 1 1 14 14 ARG HD2 H 1 3.221 0.02 . 2 . . . . . . . . 5664 1 122 . 1 1 14 14 ARG HE H 1 7.420 0.02 . 1 . . . . . . . . 5664 1 123 . 1 1 15 15 GLU N N 15 118.448 0.05 . 1 . . . . . . . . 5664 1 124 . 1 1 15 15 GLU H H 1 8.060 0.02 . 1 . . . . . . . . 5664 1 125 . 1 1 15 15 GLU HA H 1 4.115 0.02 . 1 . . . . . . . . 5664 1 126 . 1 1 15 15 GLU HB3 H 1 2.260 0.02 . 2 . . . . . . . . 5664 1 127 . 1 1 15 15 GLU HB2 H 1 2.170 0.02 . 2 . . . . . . . . 5664 1 128 . 1 1 15 15 GLU HG3 H 1 2.670 0.02 . 2 . . . . . . . . 5664 1 129 . 1 1 15 15 GLU HG2 H 1 2.360 0.02 . 2 . . . . . . . . 5664 1 130 . 1 1 16 16 CYS N N 15 116.758 0.05 . 1 . . . . . . . . 5664 1 131 . 1 1 16 16 CYS H H 1 8.490 0.02 . 1 . . . . . . . . 5664 1 132 . 1 1 16 16 CYS HA H 1 4.299 0.02 . 1 . . . . . . . . 5664 1 133 . 1 1 16 16 CYS HB3 H 1 3.032 0.02 . 1 . . . . . . . . 5664 1 134 . 1 1 16 16 CYS HB2 H 1 2.760 0.02 . 1 . . . . . . . . 5664 1 135 . 1 1 17 17 ALA N N 15 121.861 0.05 . 1 . . . . . . . . 5664 1 136 . 1 1 17 17 ALA H H 1 8.202 0.02 . 1 . . . . . . . . 5664 1 137 . 1 1 17 17 ALA HA H 1 4.451 0.02 . 1 . . . . . . . . 5664 1 138 . 1 1 17 17 ALA HB1 H 1 1.627 0.02 . 1 . . . . . . . . 5664 1 139 . 1 1 17 17 ALA HB2 H 1 1.627 0.02 . 1 . . . . . . . . 5664 1 140 . 1 1 17 17 ALA HB3 H 1 1.627 0.02 . 1 . . . . . . . . 5664 1 141 . 1 1 18 18 GLY N N 15 107.512 0.05 . 1 . . . . . . . . 5664 1 142 . 1 1 18 18 GLY H H 1 7.977 0.02 . 1 . . . . . . . . 5664 1 143 . 1 1 18 18 GLY HA3 H 1 4.097 0.02 . 2 . . . . . . . . 5664 1 144 . 1 1 18 18 GLY HA2 H 1 3.930 0.02 . 2 . . . . . . . . 5664 1 145 . 1 1 19 19 GLU N N 15 119.332 0.05 . 1 . . . . . . . . 5664 1 146 . 1 1 19 19 GLU H H 1 8.260 0.02 . 1 . . . . . . . . 5664 1 147 . 1 1 19 19 GLU HA H 1 4.356 0.02 . 1 . . . . . . . . 5664 1 148 . 1 1 19 19 GLU HB3 H 1 2.123 0.02 . 1 . . . . . . . . 5664 1 149 . 1 1 19 19 GLU HB2 H 1 1.974 0.02 . 1 . . . . . . . . 5664 1 150 . 1 1 19 19 GLU HG2 H 1 2.306 0.02 . 2 . . . . . . . . 5664 1 151 . 1 1 20 20 GLU N N 15 121.441 0.05 . 1 . . . . . . . . 5664 1 152 . 1 1 20 20 GLU H H 1 8.526 0.02 . 1 . . . . . . . . 5664 1 153 . 1 1 20 20 GLU HA H 1 4.302 0.02 . 1 . . . . . . . . 5664 1 154 . 1 1 20 20 GLU HB3 H 1 2.120 0.02 . 2 . . . . . . . . 5664 1 155 . 1 1 20 20 GLU HB2 H 1 1.942 0.02 . 2 . . . . . . . . 5664 1 156 . 1 1 20 20 GLU HG2 H 1 2.299 0.02 . 2 . . . . . . . . 5664 1 157 . 1 1 21 21 GLU N N 15 120.986 0.05 . 1 . . . . . . . . 5664 1 158 . 1 1 21 21 GLU H H 1 8.308 0.02 . 1 . . . . . . . . 5664 1 159 . 1 1 21 21 GLU HA H 1 4.322 0.02 . 1 . . . . . . . . 5664 1 160 . 1 1 21 21 GLU HB3 H 1 2.073 0.02 . 2 . . . . . . . . 5664 1 161 . 1 1 21 21 GLU HB2 H 1 1.935 0.02 . 2 . . . . . . . . 5664 1 162 . 1 1 21 21 GLU HG2 H 1 2.299 0.02 . 2 . . . . . . . . 5664 1 163 . 1 1 22 22 SER N N 15 116.748 0.05 . 1 . . . . . . . . 5664 1 164 . 1 1 22 22 SER H H 1 8.347 0.02 . 1 . . . . . . . . 5664 1 165 . 1 1 22 22 SER HA H 1 4.439 0.02 . 1 . . . . . . . . 5664 1 166 . 1 1 22 22 SER HB2 H 1 3.838 0.02 . 2 . . . . . . . . 5664 1 167 . 1 1 23 23 ILE N N 15 122.237 0.05 . 1 . . . . . . . . 5664 1 168 . 1 1 23 23 ILE H H 1 7.958 0.02 . 1 . . . . . . . . 5664 1 169 . 1 1 23 23 ILE HA H 1 4.194 0.02 . 1 . . . . . . . . 5664 1 170 . 1 1 23 23 ILE HB H 1 1.840 0.02 . 1 . . . . . . . . 5664 1 171 . 1 1 23 23 ILE HG13 H 1 1.401 0.02 . 2 . . . . . . . . 5664 1 172 . 1 1 23 23 ILE HG12 H 1 1.154 0.02 . 2 . . . . . . . . 5664 1 173 . 1 1 23 23 ILE HD11 H 1 0.829 0.02 . 1 . . . . . . . . 5664 1 174 . 1 1 23 23 ILE HD12 H 1 0.829 0.02 . 1 . . . . . . . . 5664 1 175 . 1 1 23 23 ILE HD13 H 1 0.829 0.02 . 1 . . . . . . . . 5664 1 176 . 1 1 23 23 ILE HG21 H 1 0.877 0.02 . 1 . . . . . . . . 5664 1 177 . 1 1 23 23 ILE HG22 H 1 0.877 0.02 . 1 . . . . . . . . 5664 1 178 . 1 1 23 23 ILE HG23 H 1 0.877 0.02 . 1 . . . . . . . . 5664 1 179 . 1 1 24 24 ASP N N 15 124.778 0.05 . 1 . . . . . . . . 5664 1 180 . 1 1 24 24 ASP H H 1 8.410 0.02 . 1 . . . . . . . . 5664 1 181 . 1 1 24 24 ASP HA H 1 4.639 0.02 . 1 . . . . . . . . 5664 1 182 . 1 1 24 24 ASP HB3 H 1 2.756 0.02 . 1 . . . . . . . . 5664 1 183 . 1 1 24 24 ASP HB2 H 1 2.565 0.02 . 1 . . . . . . . . 5664 1 184 . 1 1 25 25 LEU N N 15 124.815 0.05 . 1 . . . . . . . . 5664 1 185 . 1 1 25 25 LEU H H 1 8.297 0.02 . 1 . . . . . . . . 5664 1 186 . 1 1 25 25 LEU HA H 1 4.352 0.02 . 1 . . . . . . . . 5664 1 187 . 1 1 25 25 LEU HB2 H 1 1.664 0.02 . 2 . . . . . . . . 5664 1 188 . 1 1 25 25 LEU HG H 1 1.720 0.02 . 1 . . . . . . . . 5664 1 189 . 1 1 25 25 LEU HD11 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 190 . 1 1 25 25 LEU HD12 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 191 . 1 1 25 25 LEU HD13 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 192 . 1 1 25 25 LEU HD21 H 1 0.959 0.02 . 2 . . . . . . . . 5664 1 193 . 1 1 25 25 LEU HD22 H 1 0.959 0.02 . 2 . . . . . . . . 5664 1 194 . 1 1 25 25 LEU HD23 H 1 0.959 0.02 . 2 . . . . . . . . 5664 1 195 . 1 1 26 26 GLY N N 15 108.268 0.05 . 1 . . . . . . . . 5664 1 196 . 1 1 26 26 GLY H H 1 8.297 0.02 . 1 . . . . . . . . 5664 1 197 . 1 1 26 26 GLY HA3 H 1 3.989 0.02 . 2 . . . . . . . . 5664 1 198 . 1 1 26 26 GLY HA2 H 1 3.897 0.02 . 2 . . . . . . . . 5664 1 199 . 1 1 27 27 GLY N N 15 107.010 0.05 . 1 . . . . . . . . 5664 1 200 . 1 1 27 27 GLY H H 1 8.041 0.02 . 1 . . . . . . . . 5664 1 201 . 1 1 27 27 GLY HA3 H 1 3.987 0.02 . 2 . . . . . . . . 5664 1 202 . 1 1 27 27 GLY HA2 H 1 3.820 0.02 . 2 . . . . . . . . 5664 1 203 . 1 1 28 28 ASP N N 15 121.033 0.05 . 1 . . . . . . . . 5664 1 204 . 1 1 28 28 ASP H H 1 8.477 0.02 . 1 . . . . . . . . 5664 1 205 . 1 1 28 28 ASP HA H 1 4.800 0.02 . 1 . . . . . . . . 5664 1 206 . 1 1 28 28 ASP HB3 H 1 2.814 0.02 . 2 . . . . . . . . 5664 1 207 . 1 1 28 28 ASP HB2 H 1 2.605 0.02 . 2 . . . . . . . . 5664 1 208 . 1 1 29 29 VAL N N 15 116.745 0.05 . 1 . . . . . . . . 5664 1 209 . 1 1 29 29 VAL H H 1 7.782 0.02 . 1 . . . . . . . . 5664 1 210 . 1 1 29 29 VAL HA H 1 4.331 0.02 . 1 . . . . . . . . 5664 1 211 . 1 1 29 29 VAL HB H 1 2.457 0.02 . 1 . . . . . . . . 5664 1 212 . 1 1 29 29 VAL HG11 H 1 0.864 0.02 . 2 . . . . . . . . 5664 1 213 . 1 1 29 29 VAL HG12 H 1 0.864 0.02 . 2 . . . . . . . . 5664 1 214 . 1 1 29 29 VAL HG13 H 1 0.864 0.02 . 2 . . . . . . . . 5664 1 215 . 1 1 30 30 GLU N N 15 119.221 0.05 . 1 . . . . . . . . 5664 1 216 . 1 1 30 30 GLU H H 1 8.358 0.02 . 1 . . . . . . . . 5664 1 217 . 1 1 30 30 GLU HA H 1 3.677 0.02 . 1 . . . . . . . . 5664 1 218 . 1 1 30 30 GLU HB3 H 1 2.040 0.02 . 1 . . . . . . . . 5664 1 219 . 1 1 30 30 GLU HB2 H 1 1.941 0.02 . 1 . . . . . . . . 5664 1 220 . 1 1 30 30 GLU HG3 H 1 2.370 0.02 . 2 . . . . . . . . 5664 1 221 . 1 1 30 30 GLU HG2 H 1 2.208 0.02 . 2 . . . . . . . . 5664 1 222 . 1 1 31 31 ASP N N 15 113.369 0.05 . 1 . . . . . . . . 5664 1 223 . 1 1 31 31 ASP H H 1 8.219 0.02 . 1 . . . . . . . . 5664 1 224 . 1 1 31 31 ASP HA H 1 5.030 0.02 . 1 . . . . . . . . 5664 1 225 . 1 1 31 31 ASP HB3 H 1 2.983 0.02 . 1 . . . . . . . . 5664 1 226 . 1 1 31 31 ASP HB2 H 1 2.303 0.02 . 1 . . . . . . . . 5664 1 227 . 1 1 32 32 VAL N N 15 124.370 0.05 . 1 . . . . . . . . 5664 1 228 . 1 1 32 32 VAL H H 1 7.323 0.02 . 1 . . . . . . . . 5664 1 229 . 1 1 32 32 VAL HA H 1 3.800 0.02 . 1 . . . . . . . . 5664 1 230 . 1 1 32 32 VAL HB H 1 1.899 0.02 . 1 . . . . . . . . 5664 1 231 . 1 1 32 32 VAL HG21 H 1 1.024 0.02 . 2 . . . . . . . . 5664 1 232 . 1 1 32 32 VAL HG22 H 1 1.024 0.02 . 2 . . . . . . . . 5664 1 233 . 1 1 32 32 VAL HG23 H 1 1.024 0.02 . 2 . . . . . . . . 5664 1 234 . 1 1 32 32 VAL HG11 H 1 0.874 0.02 . 2 . . . . . . . . 5664 1 235 . 1 1 32 32 VAL HG12 H 1 0.874 0.02 . 2 . . . . . . . . 5664 1 236 . 1 1 32 32 VAL HG13 H 1 0.874 0.02 . 2 . . . . . . . . 5664 1 237 . 1 1 33 33 ALA N N 15 125.327 0.05 . 1 . . . . . . . . 5664 1 238 . 1 1 33 33 ALA H H 1 8.070 0.02 . 1 . . . . . . . . 5664 1 239 . 1 1 33 33 ALA HA H 1 4.456 0.02 . 1 . . . . . . . . 5664 1 240 . 1 1 33 33 ALA HB1 H 1 1.525 0.02 . 1 . . . . . . . . 5664 1 241 . 1 1 33 33 ALA HB2 H 1 1.525 0.02 . 1 . . . . . . . . 5664 1 242 . 1 1 33 33 ALA HB3 H 1 1.525 0.02 . 1 . . . . . . . . 5664 1 243 . 1 1 34 34 PHE N N 15 118.816 0.05 . 1 . . . . . . . . 5664 1 244 . 1 1 34 34 PHE H H 1 8.008 0.02 . 1 . . . . . . . . 5664 1 245 . 1 1 34 34 PHE HA H 1 4.269 0.02 . 1 . . . . . . . . 5664 1 246 . 1 1 34 34 PHE HB3 H 1 3.394 0.02 . 1 . . . . . . . . 5664 1 247 . 1 1 34 34 PHE HB2 H 1 2.983 0.02 . 1 . . . . . . . . 5664 1 248 . 1 1 34 34 PHE HD1 H 1 7.240 0.02 . 1 . . . . . . . . 5664 1 249 . 1 1 34 34 PHE HE1 H 1 6.952 0.02 . 1 . . . . . . . . 5664 1 250 . 1 1 34 34 PHE HZ H 1 6.805 0.02 . 1 . . . . . . . . 5664 1 251 . 1 1 34 34 PHE HE2 H 1 6.952 0.02 . 1 . . . . . . . . 5664 1 252 . 1 1 34 34 PHE HD2 H 1 7.240 0.02 . 1 . . . . . . . . 5664 1 253 . 1 1 35 35 ASP N N 15 116.044 0.05 . 1 . . . . . . . . 5664 1 254 . 1 1 35 35 ASP H H 1 8.773 0.02 . 1 . . . . . . . . 5664 1 255 . 1 1 35 35 ASP HA H 1 4.430 0.02 . 1 . . . . . . . . 5664 1 256 . 1 1 35 35 ASP HB3 H 1 2.757 0.02 . 2 . . . . . . . . 5664 1 257 . 1 1 35 35 ASP HB2 H 1 2.712 0.02 . 2 . . . . . . . . 5664 1 258 . 1 1 36 36 ALA N N 15 124.800 0.05 . 1 . . . . . . . . 5664 1 259 . 1 1 36 36 ALA H H 1 7.384 0.02 . 1 . . . . . . . . 5664 1 260 . 1 1 36 36 ALA HA H 1 4.245 0.02 . 1 . . . . . . . . 5664 1 261 . 1 1 36 36 ALA HB1 H 1 1.526 0.02 . 1 . . . . . . . . 5664 1 262 . 1 1 36 36 ALA HB2 H 1 1.526 0.02 . 1 . . . . . . . . 5664 1 263 . 1 1 36 36 ALA HB3 H 1 1.526 0.02 . 1 . . . . . . . . 5664 1 264 . 1 1 37 37 LEU N N 15 117.941 0.05 . 1 . . . . . . . . 5664 1 265 . 1 1 37 37 LEU H H 1 7.734 0.02 . 1 . . . . . . . . 5664 1 266 . 1 1 37 37 LEU HA H 1 4.259 0.02 . 1 . . . . . . . . 5664 1 267 . 1 1 37 37 LEU HB2 H 1 2.239 0.02 . 2 . . . . . . . . 5664 1 268 . 1 1 37 37 LEU HG H 1 1.784 0.02 . 1 . . . . . . . . 5664 1 269 . 1 1 37 37 LEU HD11 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 270 . 1 1 37 37 LEU HD12 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 271 . 1 1 37 37 LEU HD13 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 272 . 1 1 37 37 LEU HD21 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 273 . 1 1 37 37 LEU HD22 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 274 . 1 1 37 37 LEU HD23 H 1 0.848 0.02 . 2 . . . . . . . . 5664 1 275 . 1 1 38 38 GLY N N 15 103.580 0.05 . 1 . . . . . . . . 5664 1 276 . 1 1 38 38 GLY H H 1 7.473 0.02 . 1 . . . . . . . . 5664 1 277 . 1 1 38 38 GLY HA3 H 1 4.042 0.02 . 2 . . . . . . . . 5664 1 278 . 1 1 38 38 GLY HA2 H 1 3.523 0.02 . 2 . . . . . . . . 5664 1 279 . 1 1 39 39 TYR N N 15 120.533 0.05 . 1 . . . . . . . . 5664 1 280 . 1 1 39 39 TYR H H 1 7.724 0.02 . 1 . . . . . . . . 5664 1 281 . 1 1 39 39 TYR HA H 1 4.685 0.02 . 1 . . . . . . . . 5664 1 282 . 1 1 39 39 TYR HB3 H 1 2.730 0.02 . 2 . . . . . . . . 5664 1 283 . 1 1 39 39 TYR HB2 H 1 2.640 0.02 . 2 . . . . . . . . 5664 1 284 . 1 1 39 39 TYR HD1 H 1 6.920 0.02 . 3 . . . . . . . . 5664 1 285 . 1 1 39 39 TYR HE1 H 1 6.600 0.02 . 3 . . . . . . . . 5664 1 286 . 1 1 39 39 TYR HE2 H 1 6.602 0.02 . 3 . . . . . . . . 5664 1 287 . 1 1 39 39 TYR HD2 H 1 6.918 0.02 . 3 . . . . . . . . 5664 1 288 . 1 1 40 40 ASP N N 15 123.133 0.05 . 1 . . . . . . . . 5664 1 289 . 1 1 40 40 ASP H H 1 8.228 0.02 . 1 . . . . . . . . 5664 1 290 . 1 1 40 40 ASP HA H 1 4.620 0.02 . 1 . . . . . . . . 5664 1 291 . 1 1 40 40 ASP HB3 H 1 3.212 0.02 . 2 . . . . . . . . 5664 1 292 . 1 1 40 40 ASP HB2 H 1 2.768 0.02 . 2 . . . . . . . . 5664 1 293 . 1 1 41 41 SER N N 15 112.625 0.05 . 1 . . . . . . . . 5664 1 294 . 1 1 41 41 SER H H 1 8.280 0.02 . 1 . . . . . . . . 5664 1 295 . 1 1 41 41 SER HA H 1 4.027 0.02 . 1 . . . . . . . . 5664 1 296 . 1 1 41 41 SER HB3 H 1 3.920 0.02 . 2 . . . . . . . . 5664 1 297 . 1 1 41 41 SER HB2 H 1 3.870 0.02 . 2 . . . . . . . . 5664 1 298 . 1 1 42 42 LEU N N 15 123.631 0.05 . 1 . . . . . . . . 5664 1 299 . 1 1 42 42 LEU H H 1 7.644 0.02 . 1 . . . . . . . . 5664 1 300 . 1 1 42 42 LEU HA H 1 4.163 0.02 . 1 . . . . . . . . 5664 1 301 . 1 1 42 42 LEU HB2 H 1 1.719 0.02 . 2 . . . . . . . . 5664 1 302 . 1 1 42 42 LEU HG H 1 1.571 0.02 . 1 . . . . . . . . 5664 1 303 . 1 1 42 42 LEU HD11 H 1 0.893 0.02 . 2 . . . . . . . . 5664 1 304 . 1 1 42 42 LEU HD12 H 1 0.893 0.02 . 2 . . . . . . . . 5664 1 305 . 1 1 42 42 LEU HD13 H 1 0.893 0.02 . 2 . . . . . . . . 5664 1 306 . 1 1 42 42 LEU HD21 H 1 0.926 0.02 . 2 . . . . . . . . 5664 1 307 . 1 1 42 42 LEU HD22 H 1 0.926 0.02 . 2 . . . . . . . . 5664 1 308 . 1 1 42 42 LEU HD23 H 1 0.926 0.02 . 2 . . . . . . . . 5664 1 309 . 1 1 43 43 ALA N N 15 122.978 0.05 . 1 . . . . . . . . 5664 1 310 . 1 1 43 43 ALA H H 1 8.025 0.02 . 1 . . . . . . . . 5664 1 311 . 1 1 43 43 ALA HA H 1 4.155 0.02 . 1 . . . . . . . . 5664 1 312 . 1 1 43 43 ALA HB1 H 1 1.573 0.02 . 1 . . . . . . . . 5664 1 313 . 1 1 43 43 ALA HB2 H 1 1.573 0.02 . 1 . . . . . . . . 5664 1 314 . 1 1 43 43 ALA HB3 H 1 1.573 0.02 . 1 . . . . . . . . 5664 1 315 . 1 1 44 44 LEU N N 15 121.403 0.05 . 1 . . . . . . . . 5664 1 316 . 1 1 44 44 LEU H H 1 8.193 0.02 . 1 . . . . . . . . 5664 1 317 . 1 1 44 44 LEU HA H 1 3.666 0.02 . 1 . . . . . . . . 5664 1 318 . 1 1 44 44 LEU HB2 H 1 1.543 0.02 . 2 . . . . . . . . 5664 1 319 . 1 1 44 44 LEU HG H 1 1.361 0.02 . 1 . . . . . . . . 5664 1 320 . 1 1 44 44 LEU HD11 H 1 0.108 0.02 . 2 . . . . . . . . 5664 1 321 . 1 1 44 44 LEU HD12 H 1 0.108 0.02 . 2 . . . . . . . . 5664 1 322 . 1 1 44 44 LEU HD13 H 1 0.108 0.02 . 2 . . . . . . . . 5664 1 323 . 1 1 44 44 LEU HD21 H 1 0.187 0.02 . 2 . . . . . . . . 5664 1 324 . 1 1 44 44 LEU HD22 H 1 0.187 0.02 . 2 . . . . . . . . 5664 1 325 . 1 1 44 44 LEU HD23 H 1 0.187 0.02 . 2 . . . . . . . . 5664 1 326 . 1 1 45 45 LEU N N 15 122.278 0.05 . 1 . . . . . . . . 5664 1 327 . 1 1 45 45 LEU H H 1 8.495 0.02 . 1 . . . . . . . . 5664 1 328 . 1 1 45 45 LEU HA H 1 3.845 0.02 . 1 . . . . . . . . 5664 1 329 . 1 1 45 45 LEU HB2 H 1 1.791 0.02 . 2 . . . . . . . . 5664 1 330 . 1 1 45 45 LEU HG H 1 1.613 0.02 . 1 . . . . . . . . 5664 1 331 . 1 1 45 45 LEU HD11 H 1 0.810 0.02 . 2 . . . . . . . . 5664 1 332 . 1 1 45 45 LEU HD12 H 1 0.810 0.02 . 2 . . . . . . . . 5664 1 333 . 1 1 45 45 LEU HD13 H 1 0.810 0.02 . 2 . . . . . . . . 5664 1 334 . 1 1 45 45 LEU HD21 H 1 0.885 0.02 . 2 . . . . . . . . 5664 1 335 . 1 1 45 45 LEU HD22 H 1 0.885 0.02 . 2 . . . . . . . . 5664 1 336 . 1 1 45 45 LEU HD23 H 1 0.885 0.02 . 2 . . . . . . . . 5664 1 337 . 1 1 46 46 ASN N N 15 118.473 0.05 . 1 . . . . . . . . 5664 1 338 . 1 1 46 46 ASN H H 1 8.272 0.02 . 1 . . . . . . . . 5664 1 339 . 1 1 46 46 ASN HA H 1 4.472 0.02 . 1 . . . . . . . . 5664 1 340 . 1 1 46 46 ASN HB3 H 1 2.894 0.02 . 2 . . . . . . . . 5664 1 341 . 1 1 46 46 ASN HB2 H 1 2.814 0.02 . 2 . . . . . . . . 5664 1 342 . 1 1 46 46 ASN ND2 N 15 111.994 0.05 . 1 . . . . . . . . 5664 1 343 . 1 1 46 46 ASN HD21 H 1 6.835 0.02 . 2 . . . . . . . . 5664 1 344 . 1 1 46 46 ASN HD22 H 1 7.469 0.02 . 2 . . . . . . . . 5664 1 345 . 1 1 47 47 THR N N 15 120.904 0.05 . 1 . . . . . . . . 5664 1 346 . 1 1 47 47 THR H H 1 8.102 0.02 . 1 . . . . . . . . 5664 1 347 . 1 1 47 47 THR HA H 1 4.079 0.02 . 1 . . . . . . . . 5664 1 348 . 1 1 47 47 THR HB H 1 4.107 0.02 . 1 . . . . . . . . 5664 1 349 . 1 1 47 47 THR HG21 H 1 0.858 0.02 . 1 . . . . . . . . 5664 1 350 . 1 1 47 47 THR HG22 H 1 0.858 0.02 . 1 . . . . . . . . 5664 1 351 . 1 1 47 47 THR HG23 H 1 0.858 0.02 . 1 . . . . . . . . 5664 1 352 . 1 1 48 48 VAL N N 15 122.695 0.05 . 1 . . . . . . . . 5664 1 353 . 1 1 48 48 VAL H H 1 8.869 0.02 . 1 . . . . . . . . 5664 1 354 . 1 1 48 48 VAL HA H 1 3.349 0.02 . 1 . . . . . . . . 5664 1 355 . 1 1 48 48 VAL HB H 1 2.099 0.02 . 1 . . . . . . . . 5664 1 356 . 1 1 48 48 VAL HG11 H 1 0.804 0.02 . 2 . . . . . . . . 5664 1 357 . 1 1 48 48 VAL HG12 H 1 0.804 0.02 . 2 . . . . . . . . 5664 1 358 . 1 1 48 48 VAL HG13 H 1 0.804 0.02 . 2 . . . . . . . . 5664 1 359 . 1 1 49 49 GLY N N 15 105.656 0.05 . 1 . . . . . . . . 5664 1 360 . 1 1 49 49 GLY H H 1 7.915 0.02 . 1 . . . . . . . . 5664 1 361 . 1 1 49 49 GLY HA2 H 1 3.940 0.02 . 2 . . . . . . . . 5664 1 362 . 1 1 50 50 ARG N N 15 122.711 0.05 . 1 . . . . . . . . 5664 1 363 . 1 1 50 50 ARG H H 1 7.759 0.02 . 1 . . . . . . . . 5664 1 364 . 1 1 50 50 ARG HA H 1 4.077 0.02 . 1 . . . . . . . . 5664 1 365 . 1 1 50 50 ARG HB3 H 1 2.080 0.02 . 1 . . . . . . . . 5664 1 366 . 1 1 50 50 ARG HB2 H 1 1.922 0.02 . 1 . . . . . . . . 5664 1 367 . 1 1 50 50 ARG HG2 H 1 1.606 0.02 . 2 . . . . . . . . 5664 1 368 . 1 1 50 50 ARG HD3 H 1 3.165 0.02 . 2 . . . . . . . . 5664 1 369 . 1 1 50 50 ARG HD2 H 1 3.089 0.02 . 2 . . . . . . . . 5664 1 370 . 1 1 50 50 ARG HE H 1 8.030 0.02 . 1 . . . . . . . . 5664 1 371 . 1 1 51 51 ILE N N 15 121.333 0.05 . 1 . . . . . . . . 5664 1 372 . 1 1 51 51 ILE H H 1 8.609 0.02 . 1 . . . . . . . . 5664 1 373 . 1 1 51 51 ILE HA H 1 3.710 0.02 . 1 . . . . . . . . 5664 1 374 . 1 1 51 51 ILE HB H 1 2.080 0.02 . 1 . . . . . . . . 5664 1 375 . 1 1 51 51 ILE HG12 H 1 1.875 0.02 . 2 . . . . . . . . 5664 1 376 . 1 1 51 51 ILE HD11 H 1 0.621 0.02 . 1 . . . . . . . . 5664 1 377 . 1 1 51 51 ILE HD12 H 1 0.621 0.02 . 1 . . . . . . . . 5664 1 378 . 1 1 51 51 ILE HD13 H 1 0.621 0.02 . 1 . . . . . . . . 5664 1 379 . 1 1 51 51 ILE HG21 H 1 0.771 0.02 . 1 . . . . . . . . 5664 1 380 . 1 1 51 51 ILE HG22 H 1 0.771 0.02 . 1 . . . . . . . . 5664 1 381 . 1 1 51 51 ILE HG23 H 1 0.771 0.02 . 1 . . . . . . . . 5664 1 382 . 1 1 52 52 GLU N N 15 118.132 0.05 . 1 . . . . . . . . 5664 1 383 . 1 1 52 52 GLU H H 1 8.542 0.02 . 1 . . . . . . . . 5664 1 384 . 1 1 52 52 GLU HA H 1 4.111 0.02 . 1 . . . . . . . . 5664 1 385 . 1 1 52 52 GLU HB3 H 1 2.152 0.02 . 1 . . . . . . . . 5664 1 386 . 1 1 52 52 GLU HB2 H 1 1.897 0.02 . 1 . . . . . . . . 5664 1 387 . 1 1 52 52 GLU HG2 H 1 2.320 0.02 . 2 . . . . . . . . 5664 1 388 . 1 1 53 53 ARG N N 15 117.640 0.05 . 1 . . . . . . . . 5664 1 389 . 1 1 53 53 ARG H H 1 7.826 0.02 . 1 . . . . . . . . 5664 1 390 . 1 1 53 53 ARG HA H 1 4.115 0.02 . 1 . . . . . . . . 5664 1 391 . 1 1 53 53 ARG HB3 H 1 1.994 0.02 . 2 . . . . . . . . 5664 1 392 . 1 1 53 53 ARG HB2 H 1 1.956 0.02 . 2 . . . . . . . . 5664 1 393 . 1 1 53 53 ARG HG2 H 1 1.594 0.02 . 2 . . . . . . . . 5664 1 394 . 1 1 53 53 ARG HD2 H 1 3.209 0.02 . 2 . . . . . . . . 5664 1 395 . 1 1 53 53 ARG HE H 1 7.326 0.02 . 1 . . . . . . . . 5664 1 396 . 1 1 54 54 ASP N N 15 119.589 0.05 . 1 . . . . . . . . 5664 1 397 . 1 1 54 54 ASP H H 1 9.102 0.02 . 1 . . . . . . . . 5664 1 398 . 1 1 54 54 ASP HA H 1 4.377 0.02 . 1 . . . . . . . . 5664 1 399 . 1 1 54 54 ASP HB3 H 1 2.763 0.02 . 1 . . . . . . . . 5664 1 400 . 1 1 54 54 ASP HB2 H 1 2.329 0.02 . 1 . . . . . . . . 5664 1 401 . 1 1 55 55 TYR N N 15 115.770 0.05 . 1 . . . . . . . . 5664 1 402 . 1 1 55 55 TYR H H 1 8.938 0.02 . 1 . . . . . . . . 5664 1 403 . 1 1 55 55 TYR HA H 1 4.396 0.02 . 1 . . . . . . . . 5664 1 404 . 1 1 55 55 TYR HB3 H 1 3.157 0.02 . 2 . . . . . . . . 5664 1 405 . 1 1 55 55 TYR HB2 H 1 3.015 0.02 . 2 . . . . . . . . 5664 1 406 . 1 1 55 55 TYR HD1 H 1 7.400 0.02 . 1 . . . . . . . . 5664 1 407 . 1 1 55 55 TYR HE1 H 1 6.593 0.02 . 1 . . . . . . . . 5664 1 408 . 1 1 55 55 TYR HE2 H 1 6.588 0.02 . 1 . . . . . . . . 5664 1 409 . 1 1 55 55 TYR HD2 H 1 7.400 0.02 . 1 . . . . . . . . 5664 1 410 . 1 1 56 56 GLY N N 15 109.534 0.05 . 1 . . . . . . . . 5664 1 411 . 1 1 56 56 GLY H H 1 7.484 0.02 . 1 . . . . . . . . 5664 1 412 . 1 1 56 56 GLY HA3 H 1 3.983 0.02 . 2 . . . . . . . . 5664 1 413 . 1 1 56 56 GLY HA2 H 1 3.910 0.02 . 2 . . . . . . . . 5664 1 414 . 1 1 57 57 VAL N N 15 111.207 0.05 . 1 . . . . . . . . 5664 1 415 . 1 1 57 57 VAL H H 1 7.411 0.02 . 1 . . . . . . . . 5664 1 416 . 1 1 57 57 VAL HA H 1 4.636 0.02 . 1 . . . . . . . . 5664 1 417 . 1 1 57 57 VAL HB H 1 2.030 0.02 . 1 . . . . . . . . 5664 1 418 . 1 1 57 57 VAL HG21 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 419 . 1 1 57 57 VAL HG22 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 420 . 1 1 57 57 VAL HG23 H 1 0.890 0.02 . 2 . . . . . . . . 5664 1 421 . 1 1 57 57 VAL HG11 H 1 0.818 0.02 . 2 . . . . . . . . 5664 1 422 . 1 1 57 57 VAL HG12 H 1 0.818 0.02 . 2 . . . . . . . . 5664 1 423 . 1 1 57 57 VAL HG13 H 1 0.818 0.02 . 2 . . . . . . . . 5664 1 424 . 1 1 58 58 GLN N N 15 120.647 0.05 . 1 . . . . . . . . 5664 1 425 . 1 1 58 58 GLN H H 1 8.250 0.02 . 1 . . . . . . . . 5664 1 426 . 1 1 58 58 GLN HA H 1 4.522 0.02 . 1 . . . . . . . . 5664 1 427 . 1 1 58 58 GLN HB3 H 1 1.907 0.02 . 2 . . . . . . . . 5664 1 428 . 1 1 58 58 GLN HB2 H 1 2.020 0.02 . 2 . . . . . . . . 5664 1 429 . 1 1 58 58 GLN HG2 H 1 2.261 0.02 . 2 . . . . . . . . 5664 1 430 . 1 1 58 58 GLN NE2 N 15 115.600 0.05 . 1 . . . . . . . . 5664 1 431 . 1 1 58 58 GLN HE21 H 1 6.770 0.02 . 2 . . . . . . . . 5664 1 432 . 1 1 58 58 GLN HE22 H 1 7.540 0.02 . 2 . . . . . . . . 5664 1 433 . 1 1 59 59 LEU N N 15 124.345 0.05 . 1 . . . . . . . . 5664 1 434 . 1 1 59 59 LEU H H 1 9.115 0.02 . 1 . . . . . . . . 5664 1 435 . 1 1 59 59 LEU HA H 1 4.390 0.02 . 1 . . . . . . . . 5664 1 436 . 1 1 59 59 LEU HB2 H 1 1.672 0.02 . 2 . . . . . . . . 5664 1 437 . 1 1 59 59 LEU HG H 1 1.504 0.02 . 1 . . . . . . . . 5664 1 438 . 1 1 59 59 LEU HD11 H 1 0.789 0.02 . 2 . . . . . . . . 5664 1 439 . 1 1 59 59 LEU HD12 H 1 0.789 0.02 . 2 . . . . . . . . 5664 1 440 . 1 1 59 59 LEU HD13 H 1 0.789 0.02 . 2 . . . . . . . . 5664 1 441 . 1 1 59 59 LEU HD21 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 442 . 1 1 59 59 LEU HD22 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 443 . 1 1 59 59 LEU HD23 H 1 0.862 0.02 . 2 . . . . . . . . 5664 1 444 . 1 1 60 60 GLY N N 15 107.407 0.05 . 1 . . . . . . . . 5664 1 445 . 1 1 60 60 GLY H H 1 8.312 0.02 . 1 . . . . . . . . 5664 1 446 . 1 1 60 60 GLY HA3 H 1 4.293 0.02 . 2 . . . . . . . . 5664 1 447 . 1 1 60 60 GLY HA2 H 1 3.849 0.02 . 2 . . . . . . . . 5664 1 448 . 1 1 61 61 ASP N N 15 120.906 0.05 . 1 . . . . . . . . 5664 1 449 . 1 1 61 61 ASP H H 1 8.685 0.02 . 1 . . . . . . . . 5664 1 450 . 1 1 61 61 ASP HA H 1 4.352 0.02 . 1 . . . . . . . . 5664 1 451 . 1 1 61 61 ASP HB3 H 1 2.694 0.02 . 1 . . . . . . . . 5664 1 452 . 1 1 61 61 ASP HB2 H 1 2.588 0.02 . 1 . . . . . . . . 5664 1 453 . 1 1 62 62 ASP N N 15 117.595 0.05 . 1 . . . . . . . . 5664 1 454 . 1 1 62 62 ASP H H 1 8.582 0.02 . 1 . . . . . . . . 5664 1 455 . 1 1 62 62 ASP HA H 1 4.695 0.02 . 1 . . . . . . . . 5664 1 456 . 1 1 62 62 ASP HB3 H 1 2.871 0.02 . 1 . . . . . . . . 5664 1 457 . 1 1 62 62 ASP HB2 H 1 2.591 0.02 . 1 . . . . . . . . 5664 1 458 . 1 1 63 63 ALA N N 15 122.240 0.05 . 1 . . . . . . . . 5664 1 459 . 1 1 63 63 ALA H H 1 7.271 0.02 . 1 . . . . . . . . 5664 1 460 . 1 1 63 63 ALA HA H 1 3.801 0.02 . 1 . . . . . . . . 5664 1 461 . 1 1 63 63 ALA HB1 H 1 1.333 0.02 . 1 . . . . . . . . 5664 1 462 . 1 1 63 63 ALA HB2 H 1 1.333 0.02 . 1 . . . . . . . . 5664 1 463 . 1 1 63 63 ALA HB3 H 1 1.333 0.02 . 1 . . . . . . . . 5664 1 464 . 1 1 64 64 VAL N N 15 112.920 0.05 . 1 . . . . . . . . 5664 1 465 . 1 1 64 64 VAL H H 1 8.087 0.02 . 1 . . . . . . . . 5664 1 466 . 1 1 64 64 VAL HA H 1 3.487 0.02 . 1 . . . . . . . . 5664 1 467 . 1 1 64 64 VAL HB H 1 2.032 0.02 . 1 . . . . . . . . 5664 1 468 . 1 1 64 64 VAL HG21 H 1 0.891 0.02 . 2 . . . . . . . . 5664 1 469 . 1 1 64 64 VAL HG22 H 1 0.891 0.02 . 2 . . . . . . . . 5664 1 470 . 1 1 64 64 VAL HG23 H 1 0.891 0.02 . 2 . . . . . . . . 5664 1 471 . 1 1 64 64 VAL HG11 H 1 0.876 0.02 . 2 . . . . . . . . 5664 1 472 . 1 1 64 64 VAL HG12 H 1 0.876 0.02 . 2 . . . . . . . . 5664 1 473 . 1 1 64 64 VAL HG13 H 1 0.876 0.02 . 2 . . . . . . . . 5664 1 474 . 1 1 65 65 GLU N N 15 118.022 0.05 . 1 . . . . . . . . 5664 1 475 . 1 1 65 65 GLU H H 1 7.544 0.02 . 1 . . . . . . . . 5664 1 476 . 1 1 65 65 GLU HA H 1 4.028 0.02 . 1 . . . . . . . . 5664 1 477 . 1 1 65 65 GLU HB3 H 1 2.100 0.02 . 2 . . . . . . . . 5664 1 478 . 1 1 65 65 GLU HB2 H 1 2.062 0.02 . 2 . . . . . . . . 5664 1 479 . 1 1 65 65 GLU HG2 H 1 2.290 0.02 . 2 . . . . . . . . 5664 1 480 . 1 1 66 66 LYS N N 15 116.217 0.05 . 1 . . . . . . . . 5664 1 481 . 1 1 66 66 LYS H H 1 7.531 0.02 . 1 . . . . . . . . 5664 1 482 . 1 1 66 66 LYS HA H 1 4.224 0.02 . 1 . . . . . . . . 5664 1 483 . 1 1 66 66 LYS HB3 H 1 1.684 0.02 . 2 . . . . . . . . 5664 1 484 . 1 1 66 66 LYS HB2 H 1 1.900 0.02 . 2 . . . . . . . . 5664 1 485 . 1 1 66 66 LYS HG3 H 1 1.514 0.02 . 4 . . . . . . . . 5664 1 486 . 1 1 66 66 LYS HG2 H 1 1.386 0.02 . 4 . . . . . . . . 5664 1 487 . 1 1 66 66 LYS HD2 H 1 1.610 0.02 . 4 . . . . . . . . 5664 1 488 . 1 1 66 66 LYS HE2 H 1 2.898 0.02 . 2 . . . . . . . . 5664 1 489 . 1 1 67 67 ALA N N 15 124.801 0.05 . 1 . . . . . . . . 5664 1 490 . 1 1 67 67 ALA H H 1 7.929 0.02 . 1 . . . . . . . . 5664 1 491 . 1 1 67 67 ALA HA H 1 4.479 0.02 . 1 . . . . . . . . 5664 1 492 . 1 1 67 67 ALA HB1 H 1 1.321 0.02 . 1 . . . . . . . . 5664 1 493 . 1 1 67 67 ALA HB2 H 1 1.321 0.02 . 1 . . . . . . . . 5664 1 494 . 1 1 67 67 ALA HB3 H 1 1.321 0.02 . 1 . . . . . . . . 5664 1 495 . 1 1 68 68 THR N N 15 111.567 0.05 . 1 . . . . . . . . 5664 1 496 . 1 1 68 68 THR H H 1 7.944 0.02 . 1 . . . . . . . . 5664 1 497 . 1 1 68 68 THR HA H 1 4.360 0.02 . 1 . . . . . . . . 5664 1 498 . 1 1 68 68 THR HB H 1 4.370 0.02 . 1 . . . . . . . . 5664 1 499 . 1 1 68 68 THR HG21 H 1 1.301 0.02 . 1 . . . . . . . . 5664 1 500 . 1 1 68 68 THR HG22 H 1 1.301 0.02 . 1 . . . . . . . . 5664 1 501 . 1 1 68 68 THR HG23 H 1 1.301 0.02 . 1 . . . . . . . . 5664 1 502 . 1 1 69 69 THR N N 15 109.843 0.05 . 1 . . . . . . . . 5664 1 503 . 1 1 69 69 THR H H 1 7.233 0.02 . 1 . . . . . . . . 5664 1 504 . 1 1 69 69 THR HA H 1 4.297 0.02 . 1 . . . . . . . . 5664 1 505 . 1 1 69 69 THR HB H 1 4.298 0.02 . 1 . . . . . . . . 5664 1 506 . 1 1 69 69 THR HG21 H 1 0.874 0.02 . 1 . . . . . . . . 5664 1 507 . 1 1 69 69 THR HG22 H 1 0.874 0.02 . 1 . . . . . . . . 5664 1 508 . 1 1 69 69 THR HG23 H 1 0.874 0.02 . 1 . . . . . . . . 5664 1 509 . 1 1 70 70 PRO HA H 1 3.968 0.02 . 1 . . . . . . . . 5664 1 510 . 1 1 70 70 PRO HB3 H 1 2.380 0.02 . 2 . . . . . . . . 5664 1 511 . 1 1 70 70 PRO HB2 H 1 2.160 0.02 . 2 . . . . . . . . 5664 1 512 . 1 1 70 70 PRO HG2 H 1 1.850 0.02 . 2 . . . . . . . . 5664 1 513 . 1 1 70 70 PRO HD3 H 1 3.610 0.02 . 2 . . . . . . . . 5664 1 514 . 1 1 70 70 PRO HD2 H 1 3.550 0.02 . 2 . . . . . . . . 5664 1 515 . 1 1 71 71 ARG N N 15 116.203 0.05 . 1 . . . . . . . . 5664 1 516 . 1 1 71 71 ARG H H 1 8.704 0.02 . 1 . . . . . . . . 5664 1 517 . 1 1 71 71 ARG HA H 1 3.752 0.02 . 1 . . . . . . . . 5664 1 518 . 1 1 71 71 ARG HB3 H 1 1.356 0.02 . 1 . . . . . . . . 5664 1 519 . 1 1 71 71 ARG HB2 H 1 1.522 0.02 . 1 . . . . . . . . 5664 1 520 . 1 1 71 71 ARG HG2 H 1 1.797 0.02 . 2 . . . . . . . . 5664 1 521 . 1 1 71 71 ARG HD3 H 1 3.275 0.02 . 2 . . . . . . . . 5664 1 522 . 1 1 71 71 ARG HD2 H 1 2.953 0.02 . 2 . . . . . . . . 5664 1 523 . 1 1 71 71 ARG HE H 1 9.150 0.02 . 1 . . . . . . . . 5664 1 524 . 1 1 72 72 ALA N N 15 119.711 0.05 . 1 . . . . . . . . 5664 1 525 . 1 1 72 72 ALA H H 1 7.829 0.02 . 1 . . . . . . . . 5664 1 526 . 1 1 72 72 ALA HA H 1 4.173 0.02 . 1 . . . . . . . . 5664 1 527 . 1 1 72 72 ALA HB1 H 1 1.656 0.02 . 1 . . . . . . . . 5664 1 528 . 1 1 72 72 ALA HB2 H 1 1.656 0.02 . 1 . . . . . . . . 5664 1 529 . 1 1 72 72 ALA HB3 H 1 1.656 0.02 . 1 . . . . . . . . 5664 1 530 . 1 1 73 73 LEU N N 15 118.868 0.05 . 1 . . . . . . . . 5664 1 531 . 1 1 73 73 LEU H H 1 7.934 0.02 . 1 . . . . . . . . 5664 1 532 . 1 1 73 73 LEU HA H 1 4.302 0.02 . 1 . . . . . . . . 5664 1 533 . 1 1 73 73 LEU HB2 H 1 2.077 0.02 . 2 . . . . . . . . 5664 1 534 . 1 1 73 73 LEU HG H 1 1.507 0.02 . 1 . . . . . . . . 5664 1 535 . 1 1 73 73 LEU HD11 H 1 0.787 0.02 . 2 . . . . . . . . 5664 1 536 . 1 1 73 73 LEU HD12 H 1 0.787 0.02 . 2 . . . . . . . . 5664 1 537 . 1 1 73 73 LEU HD13 H 1 0.787 0.02 . 2 . . . . . . . . 5664 1 538 . 1 1 73 73 LEU HD21 H 1 0.852 0.02 . 2 . . . . . . . . 5664 1 539 . 1 1 73 73 LEU HD22 H 1 0.852 0.02 . 2 . . . . . . . . 5664 1 540 . 1 1 73 73 LEU HD23 H 1 0.852 0.02 . 2 . . . . . . . . 5664 1 541 . 1 1 74 74 ILE N N 15 123.998 0.05 . 1 . . . . . . . . 5664 1 542 . 1 1 74 74 ILE H H 1 8.817 0.02 . 1 . . . . . . . . 5664 1 543 . 1 1 74 74 ILE HA H 1 3.440 0.02 . 1 . . . . . . . . 5664 1 544 . 1 1 74 74 ILE HB H 1 1.888 0.02 . 1 . . . . . . . . 5664 1 545 . 1 1 74 74 ILE HG13 H 1 0.519 0.02 . 2 . . . . . . . . 5664 1 546 . 1 1 74 74 ILE HG12 H 1 1.754 0.02 . 2 . . . . . . . . 5664 1 547 . 1 1 74 74 ILE HD11 H 1 0.685 0.02 . 1 . . . . . . . . 5664 1 548 . 1 1 74 74 ILE HD12 H 1 0.685 0.02 . 1 . . . . . . . . 5664 1 549 . 1 1 74 74 ILE HD13 H 1 0.685 0.02 . 1 . . . . . . . . 5664 1 550 . 1 1 74 74 ILE HG21 H 1 0.790 0.02 . 1 . . . . . . . . 5664 1 551 . 1 1 74 74 ILE HG22 H 1 0.790 0.02 . 1 . . . . . . . . 5664 1 552 . 1 1 74 74 ILE HG23 H 1 0.790 0.02 . 1 . . . . . . . . 5664 1 553 . 1 1 75 75 GLU N N 15 118.422 0.05 . 1 . . . . . . . . 5664 1 554 . 1 1 75 75 GLU H H 1 8.638 0.02 . 1 . . . . . . . . 5664 1 555 . 1 1 75 75 GLU HA H 1 4.005 0.02 . 1 . . . . . . . . 5664 1 556 . 1 1 75 75 GLU HB3 H 1 2.061 0.02 . 2 . . . . . . . . 5664 1 557 . 1 1 75 75 GLU HB2 H 1 2.099 0.02 . 2 . . . . . . . . 5664 1 558 . 1 1 75 75 GLU HG3 H 1 2.500 0.02 . 2 . . . . . . . . 5664 1 559 . 1 1 75 75 GLU HG2 H 1 2.267 0.02 . 2 . . . . . . . . 5664 1 560 . 1 1 76 76 MET N N 15 118.033 0.05 . 1 . . . . . . . . 5664 1 561 . 1 1 76 76 MET H H 1 8.215 0.02 . 1 . . . . . . . . 5664 1 562 . 1 1 76 76 MET HA H 1 4.151 0.02 . 1 . . . . . . . . 5664 1 563 . 1 1 76 76 MET HB3 H 1 2.290 0.02 . 2 . . . . . . . . 5664 1 564 . 1 1 76 76 MET HB2 H 1 2.200 0.02 . 2 . . . . . . . . 5664 1 565 . 1 1 76 76 MET HG3 H 1 2.666 0.02 . 2 . . . . . . . . 5664 1 566 . 1 1 76 76 MET HG2 H 1 2.638 0.02 . 2 . . . . . . . . 5664 1 567 . 1 1 77 77 THR N N 15 118.804 0.05 . 1 . . . . . . . . 5664 1 568 . 1 1 77 77 THR H H 1 7.997 0.02 . 1 . . . . . . . . 5664 1 569 . 1 1 77 77 THR HA H 1 3.641 0.02 . 1 . . . . . . . . 5664 1 570 . 1 1 77 77 THR HB H 1 3.998 0.02 . 1 . . . . . . . . 5664 1 571 . 1 1 77 77 THR HG21 H 1 0.803 0.02 . 1 . . . . . . . . 5664 1 572 . 1 1 77 77 THR HG22 H 1 0.803 0.02 . 1 . . . . . . . . 5664 1 573 . 1 1 77 77 THR HG23 H 1 0.803 0.02 . 1 . . . . . . . . 5664 1 574 . 1 1 77 77 THR HG1 H 1 3.776 0.02 . 1 . . . . . . . . 5664 1 575 . 1 1 78 78 ASN N N 15 120.076 0.05 . 1 . . . . . . . . 5664 1 576 . 1 1 78 78 ASN H H 1 8.536 0.02 . 1 . . . . . . . . 5664 1 577 . 1 1 78 78 ASN HA H 1 4.639 0.02 . 1 . . . . . . . . 5664 1 578 . 1 1 78 78 ASN HB2 H 1 2.777 0.02 . 2 . . . . . . . . 5664 1 579 . 1 1 78 78 ASN ND2 N 15 109.586 0.05 . 1 . . . . . . . . 5664 1 580 . 1 1 78 78 ASN HD21 H 1 7.321 0.02 . 2 . . . . . . . . 5664 1 581 . 1 1 78 78 ASN HD22 H 1 7.392 0.02 . 2 . . . . . . . . 5664 1 582 . 1 1 79 79 ALA N N 15 124.386 0.05 . 1 . . . . . . . . 5664 1 583 . 1 1 79 79 ALA H H 1 8.289 0.02 . 1 . . . . . . . . 5664 1 584 . 1 1 79 79 ALA HA H 1 4.171 0.02 . 1 . . . . . . . . 5664 1 585 . 1 1 79 79 ALA HB1 H 1 1.483 0.02 . 1 . . . . . . . . 5664 1 586 . 1 1 79 79 ALA HB2 H 1 1.483 0.02 . 1 . . . . . . . . 5664 1 587 . 1 1 79 79 ALA HB3 H 1 1.483 0.02 . 1 . . . . . . . . 5664 1 588 . 1 1 80 80 SER N N 15 113.733 0.05 . 1 . . . . . . . . 5664 1 589 . 1 1 80 80 SER H H 1 7.448 0.02 . 1 . . . . . . . . 5664 1 590 . 1 1 80 80 SER HA H 1 4.348 0.02 . 1 . . . . . . . . 5664 1 591 . 1 1 80 80 SER HB3 H 1 3.994 0.02 . 2 . . . . . . . . 5664 1 592 . 1 1 80 80 SER HB2 H 1 3.990 0.02 . 2 . . . . . . . . 5664 1 593 . 1 1 81 81 LEU N N 15 121.405 0.05 . 1 . . . . . . . . 5664 1 594 . 1 1 81 81 LEU H H 1 7.968 0.02 . 1 . . . . . . . . 5664 1 595 . 1 1 81 81 LEU HA H 1 4.206 0.02 . 1 . . . . . . . . 5664 1 596 . 1 1 81 81 LEU HB3 H 1 1.609 0.02 . 1 . . . . . . . . 5664 1 597 . 1 1 81 81 LEU HB2 H 1 1.945 0.02 . 1 . . . . . . . . 5664 1 598 . 1 1 81 81 LEU HG H 1 1.767 0.02 . 1 . . . . . . . . 5664 1 599 . 1 1 81 81 LEU HD11 H 1 1.028 0.02 . 2 . . . . . . . . 5664 1 600 . 1 1 81 81 LEU HD12 H 1 1.028 0.02 . 2 . . . . . . . . 5664 1 601 . 1 1 81 81 LEU HD13 H 1 1.028 0.02 . 2 . . . . . . . . 5664 1 602 . 1 1 81 81 LEU HD21 H 1 1.099 0.02 . 2 . . . . . . . . 5664 1 603 . 1 1 81 81 LEU HD22 H 1 1.099 0.02 . 2 . . . . . . . . 5664 1 604 . 1 1 81 81 LEU HD23 H 1 1.099 0.02 . 2 . . . . . . . . 5664 1 605 . 1 1 82 82 THR N N 15 108.991 0.05 . 1 . . . . . . . . 5664 1 606 . 1 1 82 82 THR H H 1 7.953 0.02 . 1 . . . . . . . . 5664 1 607 . 1 1 82 82 THR HA H 1 4.251 0.02 . 1 . . . . . . . . 5664 1 608 . 1 1 82 82 THR HB H 1 4.312 0.02 . 1 . . . . . . . . 5664 1 609 . 1 1 82 82 THR HG21 H 1 1.282 0.02 . 1 . . . . . . . . 5664 1 610 . 1 1 82 82 THR HG22 H 1 1.282 0.02 . 1 . . . . . . . . 5664 1 611 . 1 1 82 82 THR HG23 H 1 1.282 0.02 . 1 . . . . . . . . 5664 1 612 . 1 1 83 83 GLY N N 15 110.379 0.05 . 1 . . . . . . . . 5664 1 613 . 1 1 83 83 GLY H H 1 7.851 0.02 . 1 . . . . . . . . 5664 1 614 . 1 1 83 83 GLY HA2 H 1 3.999 0.02 . 2 . . . . . . . . 5664 1 615 . 1 1 84 84 ALA N N 15 123.117 0.05 . 1 . . . . . . . . 5664 1 616 . 1 1 84 84 ALA H H 1 7.951 0.02 . 1 . . . . . . . . 5664 1 617 . 1 1 84 84 ALA HA H 1 4.384 0.02 . 1 . . . . . . . . 5664 1 618 . 1 1 84 84 ALA HB1 H 1 1.385 0.02 . 1 . . . . . . . . 5664 1 619 . 1 1 84 84 ALA HB2 H 1 1.385 0.02 . 1 . . . . . . . . 5664 1 620 . 1 1 84 84 ALA HB3 H 1 1.385 0.02 . 1 . . . . . . . . 5664 1 621 . 1 1 85 85 SER N N 15 116.297 0.05 . 1 . . . . . . . . 5664 1 622 . 1 1 85 85 SER H H 1 8.215 0.02 . 1 . . . . . . . . 5664 1 623 . 1 1 85 85 SER HA H 1 4.550 0.02 . 1 . . . . . . . . 5664 1 624 . 1 1 85 85 SER HB2 H 1 3.854 0.02 . 2 . . . . . . . . 5664 1 625 . 1 1 86 86 PRO HA H 1 4.490 0.02 . 1 . . . . . . . . 5664 1 626 . 1 1 86 86 PRO HB3 H 1 2.320 0.02 . 2 . . . . . . . . 5664 1 627 . 1 1 86 86 PRO HB2 H 1 1.961 0.02 . 2 . . . . . . . . 5664 1 628 . 1 1 86 86 PRO HG2 H 1 2.050 0.02 . 2 . . . . . . . . 5664 1 629 . 1 1 86 86 PRO HD3 H 1 3.850 0.02 . 2 . . . . . . . . 5664 1 630 . 1 1 86 86 PRO HD2 H 1 3.760 0.02 . 2 . . . . . . . . 5664 1 631 . 1 1 87 87 SER N N 15 115.537 0.05 . 1 . . . . . . . . 5664 1 632 . 1 1 87 87 SER H H 1 8.325 0.02 . 1 . . . . . . . . 5664 1 633 . 1 1 87 87 SER HA H 1 4.430 0.02 . 1 . . . . . . . . 5664 1 634 . 1 1 87 87 SER HB3 H 1 3.900 0.02 . 2 . . . . . . . . 5664 1 635 . 1 1 87 87 SER HB2 H 1 3.860 0.02 . 2 . . . . . . . . 5664 1 636 . 1 1 88 88 ALA N N 15 126.126 0.05 . 1 . . . . . . . . 5664 1 637 . 1 1 88 88 ALA H H 1 8.296 0.02 . 1 . . . . . . . . 5664 1 638 . 1 1 88 88 ALA HA H 1 4.369 0.02 . 1 . . . . . . . . 5664 1 639 . 1 1 88 88 ALA HB1 H 1 1.405 0.02 . 1 . . . . . . . . 5664 1 640 . 1 1 88 88 ALA HB2 H 1 1.405 0.02 . 1 . . . . . . . . 5664 1 641 . 1 1 88 88 ALA HB3 H 1 1.405 0.02 . 1 . . . . . . . . 5664 1 642 . 1 1 89 89 GLY N N 15 107.937 0.05 . 1 . . . . . . . . 5664 1 643 . 1 1 89 89 GLY H H 1 8.340 0.02 . 1 . . . . . . . . 5664 1 644 . 1 1 89 89 GLY HA2 H 1 3.949 0.02 . 2 . . . . . . . . 5664 1 645 . 1 1 90 90 GLY N N 15 108.710 0.05 . 1 . . . . . . . . 5664 1 646 . 1 1 90 90 GLY H H 1 8.212 0.02 . 1 . . . . . . . . 5664 1 647 . 1 1 90 90 GLY HA2 H 1 3.947 0.02 . 2 . . . . . . . . 5664 1 648 . 1 1 91 91 ALA N N 15 123.894 0.05 . 1 . . . . . . . . 5664 1 649 . 1 1 91 91 ALA H H 1 8.161 0.02 . 1 . . . . . . . . 5664 1 650 . 1 1 91 91 ALA HA H 1 4.315 0.02 . 1 . . . . . . . . 5664 1 651 . 1 1 91 91 ALA HB1 H 1 1.365 0.02 . 1 . . . . . . . . 5664 1 652 . 1 1 91 91 ALA HB2 H 1 1.365 0.02 . 1 . . . . . . . . 5664 1 653 . 1 1 91 91 ALA HB3 H 1 1.365 0.02 . 1 . . . . . . . . 5664 1 654 . 1 1 92 92 ALA N N 15 123.520 0.05 . 1 . . . . . . . . 5664 1 655 . 1 1 92 92 ALA H H 1 8.262 0.02 . 1 . . . . . . . . 5664 1 656 . 1 1 92 92 ALA HA H 1 4.281 0.02 . 1 . . . . . . . . 5664 1 657 . 1 1 92 92 ALA HB1 H 1 1.388 0.02 . 1 . . . . . . . . 5664 1 658 . 1 1 92 92 ALA HB2 H 1 1.388 0.02 . 1 . . . . . . . . 5664 1 659 . 1 1 92 92 ALA HB3 H 1 1.388 0.02 . 1 . . . . . . . . 5664 1 660 . 1 1 93 93 ARG N N 15 120.136 0.05 . 1 . . . . . . . . 5664 1 661 . 1 1 93 93 ARG H H 1 8.251 0.02 . 1 . . . . . . . . 5664 1 662 . 1 1 93 93 ARG HA H 1 4.344 0.02 . 1 . . . . . . . . 5664 1 663 . 1 1 93 93 ARG HB3 H 1 1.873 0.02 . 2 . . . . . . . . 5664 1 664 . 1 1 93 93 ARG HB2 H 1 1.754 0.02 . 2 . . . . . . . . 5664 1 665 . 1 1 93 93 ARG HG2 H 1 1.626 0.02 . 2 . . . . . . . . 5664 1 666 . 1 1 93 93 ARG HD2 H 1 3.199 0.02 . 2 . . . . . . . . 5664 1 667 . 1 1 93 93 ARG HE H 1 7.230 0.02 . 1 . . . . . . . . 5664 1 668 . 1 1 94 94 ASP N N 15 121.407 0.05 . 1 . . . . . . . . 5664 1 669 . 1 1 94 94 ASP H H 1 8.357 0.02 . 1 . . . . . . . . 5664 1 670 . 1 1 94 94 ASP HA H 1 4.571 0.02 . 1 . . . . . . . . 5664 1 671 . 1 1 94 94 ASP HB3 H 1 2.706 0.02 . 2 . . . . . . . . 5664 1 672 . 1 1 94 94 ASP HB2 H 1 2.614 0.02 . 2 . . . . . . . . 5664 1 673 . 1 1 95 95 LYS N N 15 125.439 0.05 . 1 . . . . . . . . 5664 1 674 . 1 1 95 95 LYS H H 1 7.764 0.02 . 1 . . . . . . . . 5664 1 675 . 1 1 95 95 LYS HA H 1 4.133 0.02 . 1 . . . . . . . . 5664 1 676 . 1 1 95 95 LYS HB3 H 1 1.801 0.02 . 2 . . . . . . . . 5664 1 677 . 1 1 95 95 LYS HB2 H 1 1.722 0.02 . 2 . . . . . . . . 5664 1 678 . 1 1 95 95 LYS HG2 H 1 1.377 0.02 . 4 . . . . . . . . 5664 1 679 . 1 1 95 95 LYS HD2 H 1 1.682 0.02 . 4 . . . . . . . . 5664 1 680 . 1 1 95 95 LYS HE2 H 1 3.000 0.02 . 2 . . . . . . . . 5664 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 487 5664 1 1 486 5664 1 1 485 5664 1 2 679 5664 1 2 678 5664 1 stop_ save_