data_30389 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 30389 _Entry.Title ; Solution structure of AGL55 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2017-12-24 _Entry.Accession_date 2017-12-24 _Entry.Last_release_date 2018-02-05 _Entry.Original_release_date 2018-02-05 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_experimental_methods.ID _Entry_experimental_methods.Method _Entry_experimental_methods.Subtype _Entry_experimental_methods.Entry_ID 1 'SOLUTION NMR' 'SOLUTION NMR' 30389 stop_ 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.ORCID _Entry_author.Entry_ID 1 C. Qiu C. . . . 30389 2 Y. Yuan Y. . . . 30389 3 F. Castellino F. J. . . 30389 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'PROTEIN BINDING' . 30389 'Plasminogen binding peptide' . 30389 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 30389 spectral_peak_list 1 30389 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 236 30389 '15N chemical shifts' 54 30389 '1H chemical shifts' 363 30389 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 . . 2019-01-11 . original BMRB . 30389 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 6BZJ . 30389 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 30389 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; The C-Domain Repeats in Plasminogen-binding Group A Streptococcal M-Protein are Essential Determinants for its Dimerization ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD 0353 _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 C. Qiu C. . . . 30389 1 2 Y. Yuan Y. . . . 30389 1 3 J. Zajicek J. . . . 30389 1 4 V. Ploplis V. A. . . 30389 1 5 S. Lee S. W. . . 30389 1 6 F. Castellino F. J. . . 30389 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 30389 _Assembly.ID 1 _Assembly.Name 'M 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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 entity_1 1 $entity_1 A A yes . . . . . . 30389 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 30389 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSAGLQEKERELEDLKDAEL KRLNEERHDHDKREAERKAL EDKLADKQEHLDGALRY ; _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 no _Entity.Nstd_chirality . _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 57 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID 1 _Entity.Fragment 'UNP residues 54-108' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6742.396 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID AGL55 na 30389 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 . GLY . 30389 1 2 . SER . 30389 1 3 . ALA . 30389 1 4 . GLY . 30389 1 5 . LEU . 30389 1 6 . GLN . 30389 1 7 . GLU . 30389 1 8 . LYS . 30389 1 9 . GLU . 30389 1 10 . ARG . 30389 1 11 . GLU . 30389 1 12 . LEU . 30389 1 13 . GLU . 30389 1 14 . ASP . 30389 1 15 . LEU . 30389 1 16 . LYS . 30389 1 17 . ASP . 30389 1 18 . ALA . 30389 1 19 . GLU . 30389 1 20 . LEU . 30389 1 21 . LYS . 30389 1 22 . ARG . 30389 1 23 . LEU . 30389 1 24 . ASN . 30389 1 25 . GLU . 30389 1 26 . GLU . 30389 1 27 . ARG . 30389 1 28 . HIS . 30389 1 29 . ASP . 30389 1 30 . HIS . 30389 1 31 . ASP . 30389 1 32 . LYS . 30389 1 33 . ARG . 30389 1 34 . GLU . 30389 1 35 . ALA . 30389 1 36 . GLU . 30389 1 37 . ARG . 30389 1 38 . LYS . 30389 1 39 . ALA . 30389 1 40 . LEU . 30389 1 41 . GLU . 30389 1 42 . ASP . 30389 1 43 . LYS . 30389 1 44 . LEU . 30389 1 45 . ALA . 30389 1 46 . ASP . 30389 1 47 . LYS . 30389 1 48 . GLN . 30389 1 49 . GLU . 30389 1 50 . HIS . 30389 1 51 . LEU . 30389 1 52 . ASP . 30389 1 53 . GLY . 30389 1 54 . ALA . 30389 1 55 . LEU . 30389 1 56 . ARG . 30389 1 57 . TYR . 30389 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 . GLY 1 1 30389 1 . SER 2 2 30389 1 . ALA 3 3 30389 1 . GLY 4 4 30389 1 . LEU 5 5 30389 1 . GLN 6 6 30389 1 . GLU 7 7 30389 1 . LYS 8 8 30389 1 . GLU 9 9 30389 1 . ARG 10 10 30389 1 . GLU 11 11 30389 1 . LEU 12 12 30389 1 . GLU 13 13 30389 1 . ASP 14 14 30389 1 . LEU 15 15 30389 1 . LYS 16 16 30389 1 . ASP 17 17 30389 1 . ALA 18 18 30389 1 . GLU 19 19 30389 1 . LEU 20 20 30389 1 . LYS 21 21 30389 1 . ARG 22 22 30389 1 . LEU 23 23 30389 1 . ASN 24 24 30389 1 . GLU 25 25 30389 1 . GLU 26 26 30389 1 . ARG 27 27 30389 1 . HIS 28 28 30389 1 . ASP 29 29 30389 1 . HIS 30 30 30389 1 . ASP 31 31 30389 1 . LYS 32 32 30389 1 . ARG 33 33 30389 1 . GLU 34 34 30389 1 . ALA 35 35 30389 1 . GLU 36 36 30389 1 . ARG 37 37 30389 1 . LYS 38 38 30389 1 . ALA 39 39 30389 1 . LEU 40 40 30389 1 . GLU 41 41 30389 1 . ASP 42 42 30389 1 . LYS 43 43 30389 1 . LEU 44 44 30389 1 . ALA 45 45 30389 1 . ASP 46 46 30389 1 . LYS 47 47 30389 1 . GLN 48 48 30389 1 . GLU 49 49 30389 1 . HIS 50 50 30389 1 . LEU 51 51 30389 1 . ASP 52 52 30389 1 . GLY 53 53 30389 1 . ALA 54 54 30389 1 . LEU 55 55 30389 1 . ARG 56 56 30389 1 . TYR 57 57 30389 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 30389 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity_1 . 1138874 organism . 'Streptococcus pyogenes NS88.2' 'Streptococcus pyogenes' . . Bacteria . Streptococcus pyogenes NS88.2 . . . . . . . . . . emm . 30389 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 30389 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity_1 . 'recombinant technology' 'Escherichia coli DH5[alpha]' . . 668369 . . . . . plasmid . . pET15b . . . 30389 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 30389 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '20 mM [U-99% 2H] BisTris-d19, 1 mM DSS, 1 mM sodium azide, 1 mM EDTA, 90% H2O/10% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 BisTris-d19 '[U-99% 2H]' . . 1 $entity_1 . . 20 . . mM . . . . 30389 1 2 DSS 'natural abundance' . . . . . . 1 . . mM . . . . 30389 1 3 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 30389 1 4 EDTA 'natural abundance' . . . . . . 1 . . mM . . . . 30389 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 30389 _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 'ionic strength' 20 . mM 30389 1 pH 6.7 . pH 30389 1 pressure 1 . atm 30389 1 temperature 298 . K 30389 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 30389 _Software.ID 1 _Software.Type . _Software.Name TOPSPIN _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 30389 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 30389 1 'data analysis' 30389 1 processing 30389 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 30389 _Software.ID 2 _Software.Type . _Software.Name SPARKY _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 30389 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 30389 2 'peak picking' 30389 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 30389 _Software.ID 3 _Software.Type . _Software.Name 'X-PLOR NIH' _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Schwieters, Kuszewski, Tjandra and Clore' . . 30389 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure calculation' 30389 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 30389 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AvanceII _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 30389 _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_1 Bruker AvanceII . 800 . . . 30389 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 30389 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 2 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 4 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 5 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 6 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 7 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 8 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 9 '3D NOESY-HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . 30389 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_1 _Chem_shift_reference.Entry_ID 30389 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.000 internal indirect 0.251449530 . . . . . 30389 1 H 1 DSS 'methyl protons' . . . . ppm 0.000 internal direct 1.0 . . . . . 30389 1 N 15 DSS 'methyl protons' . . . . ppm 0.000 internal indirect 0.101329118 . . . . . 30389 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 30389 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 30389 1 2 '3D HNCO' . . . 30389 1 3 '3D HNCA' . . . 30389 1 4 '3D HNCACB' . . . 30389 1 5 '3D CBCA(CO)NH' . . . 30389 1 6 '3D C(CO)NH' . . . 30389 1 7 '3D H(CCO)NH' . . . 30389 1 8 '3D HBHA(CO)NH' . . . 30389 1 9 '3D NOESY-HSQC' . . . 30389 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.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER HA H 1 4.507 0.02 1.000 1 . . . . A 2 SER HA . 30389 1 2 . 1 1 2 2 SER HB2 H 1 3.885 0.02 0.597 2 . . . . A 2 SER HB2 . 30389 1 3 . 1 1 2 2 SER HB3 H 1 3.885 0.02 0.838 2 . . . . A 2 SER HB3 . 30389 1 4 . 1 1 2 2 SER C C 13 174.310 0.20 1.000 1 . . . . A 2 SER C . 30389 1 5 . 1 1 2 2 SER CA C 13 58.330 0.20 1.000 1 . . . . A 2 SER CA . 30389 1 6 . 1 1 2 2 SER CB C 13 63.850 0.20 1.000 1 . . . . A 2 SER CB . 30389 1 7 . 1 1 3 3 ALA H H 1 8.554 0.02 1.000 1 . . . . A 3 ALA H . 30389 1 8 . 1 1 3 3 ALA HA H 1 4.372 0.02 1.000 1 . . . . A 3 ALA HA . 30389 1 9 . 1 1 3 3 ALA HB1 H 1 1.415 0.02 1.000 1 . . . . A 3 ALA HB1 . 30389 1 10 . 1 1 3 3 ALA HB2 H 1 1.415 0.02 1.000 1 . . . . A 3 ALA HB2 . 30389 1 11 . 1 1 3 3 ALA HB3 H 1 1.415 0.02 1.000 1 . . . . A 3 ALA HB3 . 30389 1 12 . 1 1 3 3 ALA C C 13 178.158 0.20 1.000 1 . . . . A 3 ALA C . 30389 1 13 . 1 1 3 3 ALA CA C 13 52.820 0.20 1.000 1 . . . . A 3 ALA CA . 30389 1 14 . 1 1 3 3 ALA CB C 13 19.290 0.20 1.000 1 . . . . A 3 ALA CB . 30389 1 15 . 1 1 3 3 ALA N N 15 126.172 0.20 1.000 1 . . . . A 3 ALA N . 30389 1 16 . 1 1 4 4 GLY H H 1 8.397 0.02 1.000 1 . . . . A 4 GLY H . 30389 1 17 . 1 1 4 4 GLY HA2 H 1 3.959 0.02 0.893 2 . . . . A 4 GLY HA2 . 30389 1 18 . 1 1 4 4 GLY HA3 H 1 3.959 0.02 0.391 2 . . . . A 4 GLY HA3 . 30389 1 19 . 1 1 4 4 GLY C C 13 174.264 0.20 1.000 1 . . . . A 4 GLY C . 30389 1 20 . 1 1 4 4 GLY CA C 13 45.310 0.20 0.734 1 . . . . A 4 GLY CA . 30389 1 21 . 1 1 4 4 GLY N N 15 108.146 0.20 1.000 1 . . . . A 4 GLY N . 30389 1 22 . 1 1 5 5 LEU H H 1 8.113 0.02 1.000 1 . . . . A 5 LEU H . 30389 1 23 . 1 1 5 5 LEU HA H 1 4.331 0.02 1.000 1 . . . . A 5 LEU HA . 30389 1 24 . 1 1 5 5 LEU HB2 H 1 1.847 0.02 0.522 2 . . . . A 5 LEU HB2 . 30389 1 25 . 1 1 5 5 LEU HB3 H 1 1.847 0.02 0.485 2 . . . . A 5 LEU HB3 . 30389 1 26 . 1 1 5 5 LEU HG H 1 1.630 0.02 0.453 1 . . . . A 5 LEU HG . 30389 1 27 . 1 1 5 5 LEU HD11 H 1 0.905 0.02 0.596 2 . . . . A 5 LEU HD11 . 30389 1 28 . 1 1 5 5 LEU HD12 H 1 0.905 0.02 0.596 2 . . . . A 5 LEU HD12 . 30389 1 29 . 1 1 5 5 LEU HD13 H 1 0.905 0.02 0.596 2 . . . . A 5 LEU HD13 . 30389 1 30 . 1 1 5 5 LEU HD21 H 1 0.905 0.02 0.498 2 . . . . A 5 LEU HD21 . 30389 1 31 . 1 1 5 5 LEU HD22 H 1 0.905 0.02 0.498 2 . . . . A 5 LEU HD22 . 30389 1 32 . 1 1 5 5 LEU HD23 H 1 0.905 0.02 0.498 2 . . . . A 5 LEU HD23 . 30389 1 33 . 1 1 5 5 LEU C C 13 177.735 0.20 1.000 1 . . . . A 5 LEU C . 30389 1 34 . 1 1 5 5 LEU CA C 13 55.430 0.20 1.000 1 . . . . A 5 LEU CA . 30389 1 35 . 1 1 5 5 LEU CB C 13 42.310 0.20 1.000 1 . . . . A 5 LEU CB . 30389 1 36 . 1 1 5 5 LEU CG C 13 27.100 0.20 1.000 1 . . . . A 5 LEU CG . 30389 1 37 . 1 1 5 5 LEU CD1 C 13 24.800 0.20 0.895 2 . . . . A 5 LEU CD1 . 30389 1 38 . 1 1 5 5 LEU CD2 C 13 23.640 0.20 0.882 2 . . . . A 5 LEU CD2 . 30389 1 39 . 1 1 5 5 LEU N N 15 121.675 0.20 1.000 1 . . . . A 5 LEU N . 30389 1 40 . 1 1 6 6 GLN H H 1 8.497 0.02 1.000 1 . . . . A 6 GLN H . 30389 1 41 . 1 1 6 6 GLN HA H 1 4.308 0.02 1.000 1 . . . . A 6 GLN HA . 30389 1 42 . 1 1 6 6 GLN HB2 H 1 2.145 0.02 0.224 2 . . . . A 6 GLN HB2 . 30389 1 43 . 1 1 6 6 GLN HB3 H 1 2.029 0.02 0.242 2 . . . . A 6 GLN HB3 . 30389 1 44 . 1 1 6 6 GLN HG2 H 1 2.385 0.02 0.630 2 . . . . A 6 GLN HG2 . 30389 1 45 . 1 1 6 6 GLN HG3 H 1 2.385 0.02 0.422 2 . . . . A 6 GLN HG3 . 30389 1 46 . 1 1 6 6 GLN C C 13 176.415 0.20 1.000 1 . . . . A 6 GLN C . 30389 1 47 . 1 1 6 6 GLN CA C 13 56.360 0.20 1.000 1 . . . . A 6 GLN CA . 30389 1 48 . 1 1 6 6 GLN CB C 13 29.220 0.20 1.000 1 . . . . A 6 GLN CB . 30389 1 49 . 1 1 6 6 GLN CG C 13 33.980 0.20 1.000 1 . . . . A 6 GLN CG . 30389 1 50 . 1 1 6 6 GLN N N 15 120.764 0.20 1.000 1 . . . . A 6 GLN N . 30389 1 51 . 1 1 7 7 GLU H H 1 8.475 0.02 1.000 1 . . . . A 7 GLU H . 30389 1 52 . 1 1 7 7 GLU HA H 1 4.214 0.02 1.000 1 . . . . A 7 GLU HA . 30389 1 53 . 1 1 7 7 GLU HB2 H 1 2.026 0.02 0.492 2 . . . . A 7 GLU HB2 . 30389 1 54 . 1 1 7 7 GLU HB3 H 1 2.026 0.02 0.577 2 . . . . A 7 GLU HB3 . 30389 1 55 . 1 1 7 7 GLU HG2 H 1 2.287 0.02 0.502 2 . . . . A 7 GLU HG2 . 30389 1 56 . 1 1 7 7 GLU HG3 H 1 2.287 0.02 0.461 2 . . . . A 7 GLU HG3 . 30389 1 57 . 1 1 7 7 GLU C C 13 177.074 0.20 1.000 1 . . . . A 7 GLU C . 30389 1 58 . 1 1 7 7 GLU CA C 13 57.520 0.20 1.000 1 . . . . A 7 GLU CA . 30389 1 59 . 1 1 7 7 GLU CB C 13 30.120 0.20 1.000 1 . . . . A 7 GLU CB . 30389 1 60 . 1 1 7 7 GLU CG C 13 36.390 0.20 1.000 1 . . . . A 7 GLU CG . 30389 1 61 . 1 1 7 7 GLU N N 15 121.999 0.20 1.000 1 . . . . A 7 GLU N . 30389 1 62 . 1 1 8 8 LYS H H 1 8.304 0.02 1.000 1 . . . . A 8 LYS H . 30389 1 63 . 1 1 8 8 LYS HA H 1 4.261 0.02 1.000 1 . . . . A 8 LYS HA . 30389 1 64 . 1 1 8 8 LYS HB2 H 1 1.843 0.02 0.310 2 . . . . A 8 LYS HB2 . 30389 1 65 . 1 1 8 8 LYS HB3 H 1 1.843 0.02 0.483 2 . . . . A 8 LYS HB3 . 30389 1 66 . 1 1 8 8 LYS HG2 H 1 1.459 0.02 0.476 2 . . . . A 8 LYS HG2 . 30389 1 67 . 1 1 8 8 LYS HG3 H 1 1.459 0.02 0.453 2 . . . . A 8 LYS HG3 . 30389 1 68 . 1 1 8 8 LYS HD2 H 1 1.704 0.02 0.487 2 . . . . A 8 LYS HD2 . 30389 1 69 . 1 1 8 8 LYS HD3 H 1 1.704 0.02 0.492 2 . . . . A 8 LYS HD3 . 30389 1 70 . 1 1 8 8 LYS C C 13 177.247 0.20 1.000 1 . . . . A 8 LYS C . 30389 1 71 . 1 1 8 8 LYS CA C 13 57.050 0.20 1.000 1 . . . . A 8 LYS CA . 30389 1 72 . 1 1 8 8 LYS CB C 13 32.730 0.20 1.000 1 . . . . A 8 LYS CB . 30389 1 73 . 1 1 8 8 LYS CG C 13 24.770 0.20 1.000 1 . . . . A 8 LYS CG . 30389 1 74 . 1 1 8 8 LYS CD C 13 29.030 0.20 1.000 1 . . . . A 8 LYS CD . 30389 1 75 . 1 1 8 8 LYS CE C 13 42.150 0.20 1.000 1 . . . . A 8 LYS CE . 30389 1 76 . 1 1 8 8 LYS N N 15 121.349 0.20 1.000 1 . . . . A 8 LYS N . 30389 1 77 . 1 1 9 9 GLU H H 1 8.392 0.02 1.000 1 . . . . A 9 GLU H . 30389 1 78 . 1 1 9 9 GLU HA H 1 4.165 0.02 1.000 1 . . . . A 9 GLU HA . 30389 1 79 . 1 1 9 9 GLU HB2 H 1 2.057 0.02 0.652 2 . . . . A 9 GLU HB2 . 30389 1 80 . 1 1 9 9 GLU HB3 H 1 2.057 0.02 0.490 2 . . . . A 9 GLU HB3 . 30389 1 81 . 1 1 9 9 GLU HG2 H 1 2.306 0.02 0.581 2 . . . . A 9 GLU HG2 . 30389 1 82 . 1 1 9 9 GLU HG3 H 1 2.306 0.02 0.340 2 . . . . A 9 GLU HG3 . 30389 1 83 . 1 1 9 9 GLU C C 13 177.315 0.20 1.000 1 . . . . A 9 GLU C . 30389 1 84 . 1 1 9 9 GLU CA C 13 57.870 0.20 0.781 1 . . . . A 9 GLU CA . 30389 1 85 . 1 1 9 9 GLU CB C 13 30.060 0.20 0.889 1 . . . . A 9 GLU CB . 30389 1 86 . 1 1 9 9 GLU CG C 13 36.550 0.20 1.000 1 . . . . A 9 GLU CG . 30389 1 87 . 1 1 9 9 GLU N N 15 121.072 0.20 1.000 1 . . . . A 9 GLU N . 30389 1 88 . 1 1 10 10 ARG H H 1 8.204 0.02 1.000 1 . . . . A 10 ARG H . 30389 1 89 . 1 1 10 10 ARG HA H 1 4.250 0.02 1.000 1 . . . . A 10 ARG HA . 30389 1 90 . 1 1 10 10 ARG HB2 H 1 1.873 0.02 0.495 2 . . . . A 10 ARG HB2 . 30389 1 91 . 1 1 10 10 ARG HB3 H 1 1.873 0.02 0.484 2 . . . . A 10 ARG HB3 . 30389 1 92 . 1 1 10 10 ARG HG2 H 1 1.669 0.02 0.497 2 . . . . A 10 ARG HG2 . 30389 1 93 . 1 1 10 10 ARG HG3 H 1 1.669 0.02 0.494 2 . . . . A 10 ARG HG3 . 30389 1 94 . 1 1 10 10 ARG HD2 H 1 3.219 0.02 0.464 2 . . . . A 10 ARG HD2 . 30389 1 95 . 1 1 10 10 ARG HD3 H 1 3.219 0.02 0.464 2 . . . . A 10 ARG HD3 . 30389 1 96 . 1 1 10 10 ARG C C 13 176.850 0.20 1.000 1 . . . . A 10 ARG C . 30389 1 97 . 1 1 10 10 ARG CA C 13 57.040 0.20 1.000 1 . . . . A 10 ARG CA . 30389 1 98 . 1 1 10 10 ARG CB C 13 30.590 0.20 0.870 1 . . . . A 10 ARG CB . 30389 1 99 . 1 1 10 10 ARG CG C 13 27.120 0.20 0.572 1 . . . . A 10 ARG CG . 30389 1 100 . 1 1 10 10 ARG CD C 13 43.330 0.20 0.406 1 . . . . A 10 ARG CD . 30389 1 101 . 1 1 10 10 ARG N N 15 120.952 0.20 1.000 1 . . . . A 10 ARG N . 30389 1 102 . 1 1 11 11 GLU H H 1 8.322 0.02 1.000 1 . . . . A 11 GLU H . 30389 1 103 . 1 1 11 11 GLU HA H 1 4.205 0.02 0.752 1 . . . . A 11 GLU HA . 30389 1 104 . 1 1 11 11 GLU HB2 H 1 2.070 0.02 0.475 2 . . . . A 11 GLU HB2 . 30389 1 105 . 1 1 11 11 GLU HB3 H 1 2.070 0.02 0.544 2 . . . . A 11 GLU HB3 . 30389 1 106 . 1 1 11 11 GLU HG2 H 1 2.308 0.02 0.486 2 . . . . A 11 GLU HG2 . 30389 1 107 . 1 1 11 11 GLU HG3 H 1 2.308 0.02 0.439 2 . . . . A 11 GLU HG3 . 30389 1 108 . 1 1 11 11 GLU C C 13 177.428 0.20 1.000 1 . . . . A 11 GLU C . 30389 1 109 . 1 1 11 11 GLU CA C 13 57.700 0.20 1.000 1 . . . . A 11 GLU CA . 30389 1 110 . 1 1 11 11 GLU CB C 13 30.040 0.20 1.000 1 . . . . A 11 GLU CB . 30389 1 111 . 1 1 11 11 GLU CG C 13 36.410 0.20 1.000 1 . . . . A 11 GLU CG . 30389 1 112 . 1 1 11 11 GLU N N 15 121.030 0.20 1.000 1 . . . . A 11 GLU N . 30389 1 113 . 1 1 12 12 LEU H H 1 8.128 0.02 1.000 1 . . . . A 12 LEU H . 30389 1 114 . 1 1 12 12 LEU HA H 1 4.253 0.02 1.000 1 . . . . A 12 LEU HA . 30389 1 115 . 1 1 12 12 LEU HB2 H 1 1.755 0.02 0.522 2 . . . . A 12 LEU HB2 . 30389 1 116 . 1 1 12 12 LEU HB3 H 1 1.755 0.02 0.505 2 . . . . A 12 LEU HB3 . 30389 1 117 . 1 1 12 12 LEU HG H 1 1.618 0.02 0.480 1 . . . . A 12 LEU HG . 30389 1 118 . 1 1 12 12 LEU HD11 H 1 0.921 0.02 0.560 2 . . . . A 12 LEU HD11 . 30389 1 119 . 1 1 12 12 LEU HD12 H 1 0.921 0.02 0.560 2 . . . . A 12 LEU HD12 . 30389 1 120 . 1 1 12 12 LEU HD13 H 1 0.921 0.02 0.560 2 . . . . A 12 LEU HD13 . 30389 1 121 . 1 1 12 12 LEU HD21 H 1 0.921 0.02 0.539 2 . . . . A 12 LEU HD21 . 30389 1 122 . 1 1 12 12 LEU HD22 H 1 0.921 0.02 0.539 2 . . . . A 12 LEU HD22 . 30389 1 123 . 1 1 12 12 LEU HD23 H 1 0.921 0.02 0.539 2 . . . . A 12 LEU HD23 . 30389 1 124 . 1 1 12 12 LEU C C 13 178.392 0.20 1.000 1 . . . . A 12 LEU C . 30389 1 125 . 1 1 12 12 LEU CA C 13 56.340 0.20 1.000 1 . . . . A 12 LEU CA . 30389 1 126 . 1 1 12 12 LEU CB C 13 42.060 0.20 1.000 1 . . . . A 12 LEU CB . 30389 1 127 . 1 1 12 12 LEU CG C 13 27.110 0.20 1.000 1 . . . . A 12 LEU CG . 30389 1 128 . 1 1 12 12 LEU CD1 C 13 24.930 0.20 0.874 2 . . . . A 12 LEU CD1 . 30389 1 129 . 1 1 12 12 LEU CD2 C 13 23.690 0.20 0.880 2 . . . . A 12 LEU CD2 . 30389 1 130 . 1 1 12 12 LEU N N 15 121.244 0.20 1.000 1 . . . . A 12 LEU N . 30389 1 131 . 1 1 13 13 GLU H H 1 8.249 0.02 1.000 1 . . . . A 13 GLU H . 30389 1 132 . 1 1 13 13 GLU HA H 1 4.164 0.02 1.000 1 . . . . A 13 GLU HA . 30389 1 133 . 1 1 13 13 GLU HB2 H 1 2.048 0.02 0.479 2 . . . . A 13 GLU HB2 . 30389 1 134 . 1 1 13 13 GLU HB3 H 1 2.048 0.02 0.553 2 . . . . A 13 GLU HB3 . 30389 1 135 . 1 1 13 13 GLU HG2 H 1 2.304 0.02 0.493 2 . . . . A 13 GLU HG2 . 30389 1 136 . 1 1 13 13 GLU HG3 H 1 2.304 0.02 0.447 2 . . . . A 13 GLU HG3 . 30389 1 137 . 1 1 13 13 GLU C C 13 177.162 0.20 1.000 1 . . . . A 13 GLU C . 30389 1 138 . 1 1 13 13 GLU CA C 13 57.790 0.20 1.000 1 . . . . A 13 GLU CA . 30389 1 139 . 1 1 13 13 GLU CB C 13 30.130 0.20 1.000 1 . . . . A 13 GLU CB . 30389 1 140 . 1 1 13 13 GLU CG C 13 36.280 0.20 1.000 1 . . . . A 13 GLU CG . 30389 1 141 . 1 1 13 13 GLU N N 15 121.031 0.20 1.000 1 . . . . A 13 GLU N . 30389 1 142 . 1 1 14 14 ASP H H 1 8.365 0.02 1.000 1 . . . . A 14 ASP H . 30389 1 143 . 1 1 14 14 ASP HA H 1 4.548 0.02 1.000 1 . . . . A 14 ASP HA . 30389 1 144 . 1 1 14 14 ASP HB2 H 1 2.724 0.02 0.870 2 . . . . A 14 ASP HB2 . 30389 1 145 . 1 1 14 14 ASP HB3 H 1 2.724 0.02 0.365 2 . . . . A 14 ASP HB3 . 30389 1 146 . 1 1 14 14 ASP C C 13 177.568 0.20 1.000 1 . . . . A 14 ASP C . 30389 1 147 . 1 1 14 14 ASP CA C 13 55.970 0.20 1.000 1 . . . . A 14 ASP CA . 30389 1 148 . 1 1 14 14 ASP CB C 13 40.780 0.20 1.000 1 . . . . A 14 ASP CB . 30389 1 149 . 1 1 14 14 ASP N N 15 120.919 0.20 1.000 1 . . . . A 14 ASP N . 30389 1 150 . 1 1 15 15 LEU H H 1 8.085 0.02 1.000 1 . . . . A 15 LEU H . 30389 1 151 . 1 1 15 15 LEU HA H 1 4.251 0.02 0.660 1 . . . . A 15 LEU HA . 30389 1 152 . 1 1 15 15 LEU HB2 H 1 1.774 0.02 0.318 2 . . . . A 15 LEU HB2 . 30389 1 153 . 1 1 15 15 LEU HB3 H 1 1.774 0.02 0.582 2 . . . . A 15 LEU HB3 . 30389 1 154 . 1 1 15 15 LEU HG H 1 1.638 0.02 0.459 1 . . . . A 15 LEU HG . 30389 1 155 . 1 1 15 15 LEU HD11 H 1 0.919 0.02 0.564 2 . . . . A 15 LEU HD11 . 30389 1 156 . 1 1 15 15 LEU HD12 H 1 0.919 0.02 0.564 2 . . . . A 15 LEU HD12 . 30389 1 157 . 1 1 15 15 LEU HD13 H 1 0.919 0.02 0.564 2 . . . . A 15 LEU HD13 . 30389 1 158 . 1 1 15 15 LEU HD21 H 1 0.919 0.02 0.527 2 . . . . A 15 LEU HD21 . 30389 1 159 . 1 1 15 15 LEU HD22 H 1 0.919 0.02 0.527 2 . . . . A 15 LEU HD22 . 30389 1 160 . 1 1 15 15 LEU HD23 H 1 0.919 0.02 0.527 2 . . . . A 15 LEU HD23 . 30389 1 161 . 1 1 15 15 LEU C C 13 178.668 0.20 1.000 1 . . . . A 15 LEU C . 30389 1 162 . 1 1 15 15 LEU CA C 13 56.720 0.20 1.000 1 . . . . A 15 LEU CA . 30389 1 163 . 1 1 15 15 LEU CB C 13 42.090 0.20 1.000 1 . . . . A 15 LEU CB . 30389 1 164 . 1 1 15 15 LEU CG C 13 27.050 0.20 1.000 1 . . . . A 15 LEU CG . 30389 1 165 . 1 1 15 15 LEU CD1 C 13 25.130 0.20 0.873 2 . . . . A 15 LEU CD1 . 30389 1 166 . 1 1 15 15 LEU CD2 C 13 23.700 0.20 0.867 2 . . . . A 15 LEU CD2 . 30389 1 167 . 1 1 15 15 LEU N N 15 122.546 0.20 1.000 1 . . . . A 15 LEU N . 30389 1 168 . 1 1 16 16 LYS H H 1 8.167 0.02 1.000 1 . . . . A 16 LYS H . 30389 1 169 . 1 1 16 16 LYS HA H 1 4.186 0.02 1.000 1 . . . . A 16 LYS HA . 30389 1 170 . 1 1 16 16 LYS HB2 H 1 1.910 0.02 0.483 2 . . . . A 16 LYS HB2 . 30389 1 171 . 1 1 16 16 LYS HB3 H 1 1.910 0.02 0.520 2 . . . . A 16 LYS HB3 . 30389 1 172 . 1 1 16 16 LYS HG2 H 1 1.485 0.02 0.435 2 . . . . A 16 LYS HG2 . 30389 1 173 . 1 1 16 16 LYS HG3 H 1 1.485 0.02 0.499 2 . . . . A 16 LYS HG3 . 30389 1 174 . 1 1 16 16 LYS HD2 H 1 1.757 0.02 0.366 2 . . . . A 16 LYS HD2 . 30389 1 175 . 1 1 16 16 LYS HD3 H 1 1.757 0.02 0.339 2 . . . . A 16 LYS HD3 . 30389 1 176 . 1 1 16 16 LYS HE2 H 1 2.968 0.02 0.366 2 . . . . A 16 LYS HE2 . 30389 1 177 . 1 1 16 16 LYS HE3 H 1 2.968 0.02 0.339 2 . . . . A 16 LYS HE3 . 30389 1 178 . 1 1 16 16 LYS C C 13 178.045 0.20 1.000 1 . . . . A 16 LYS C . 30389 1 179 . 1 1 16 16 LYS CA C 13 58.040 0.20 1.000 1 . . . . A 16 LYS CA . 30389 1 180 . 1 1 16 16 LYS CB C 13 32.320 0.20 1.000 1 . . . . A 16 LYS CB . 30389 1 181 . 1 1 16 16 LYS CG C 13 24.920 0.20 1.000 1 . . . . A 16 LYS CG . 30389 1 182 . 1 1 16 16 LYS CD C 13 29.160 0.20 1.000 1 . . . . A 16 LYS CD . 30389 1 183 . 1 1 16 16 LYS CE C 13 42.140 0.20 1.000 1 . . . . A 16 LYS CE . 30389 1 184 . 1 1 16 16 LYS N N 15 120.882 0.20 1.000 1 . . . . A 16 LYS N . 30389 1 185 . 1 1 17 17 ASP H H 1 8.236 0.02 1.000 1 . . . . A 17 ASP H . 30389 1 186 . 1 1 17 17 ASP HA H 1 4.496 0.02 1.000 1 . . . . A 17 ASP HA . 30389 1 187 . 1 1 17 17 ASP HB2 H 1 2.735 0.02 0.835 2 . . . . A 17 ASP HB2 . 30389 1 188 . 1 1 17 17 ASP HB3 H 1 2.735 0.02 0.432 2 . . . . A 17 ASP HB3 . 30389 1 189 . 1 1 17 17 ASP C C 13 177.664 0.20 1.000 1 . . . . A 17 ASP C . 30389 1 190 . 1 1 17 17 ASP CA C 13 56.260 0.20 1.000 1 . . . . A 17 ASP CA . 30389 1 191 . 1 1 17 17 ASP CB C 13 41.160 0.20 1.000 1 . . . . A 17 ASP CB . 30389 1 192 . 1 1 17 17 ASP N N 15 120.271 0.20 1.000 1 . . . . A 17 ASP N . 30389 1 193 . 1 1 18 18 ALA H H 1 8.162 0.02 1.000 1 . . . . A 18 ALA H . 30389 1 194 . 1 1 18 18 ALA HA H 1 4.142 0.02 0.596 1 . . . . A 18 ALA HA . 30389 1 195 . 1 1 18 18 ALA HB1 H 1 1.497 0.02 0.437 1 . . . . A 18 ALA HB1 . 30389 1 196 . 1 1 18 18 ALA HB2 H 1 1.497 0.02 0.437 1 . . . . A 18 ALA HB2 . 30389 1 197 . 1 1 18 18 ALA HB3 H 1 1.497 0.02 0.437 1 . . . . A 18 ALA HB3 . 30389 1 198 . 1 1 18 18 ALA C C 13 180.100 0.20 0.052 1 . . . . A 18 ALA C . 30389 1 199 . 1 1 18 18 ALA CA C 13 54.480 0.20 0.052 1 . . . . A 18 ALA CA . 30389 1 200 . 1 1 18 18 ALA CB C 13 18.530 0.20 0.449 1 . . . . A 18 ALA CB . 30389 1 201 . 1 1 18 18 ALA N N 15 122.807 0.20 1.000 1 . . . . A 18 ALA N . 30389 1 202 . 1 1 19 19 GLU H H 1 8.149 0.02 0.052 1 . . . . A 19 GLU H . 30389 1 203 . 1 1 19 19 GLU HA H 1 4.200 0.02 0.571 1 . . . . A 19 GLU HA . 30389 1 204 . 1 1 19 19 GLU HB2 H 1 2.112 0.02 0.524 2 . . . . A 19 GLU HB2 . 30389 1 205 . 1 1 19 19 GLU HB3 H 1 2.112 0.02 0.463 2 . . . . A 19 GLU HB3 . 30389 1 206 . 1 1 19 19 GLU HG2 H 1 2.304 0.02 0.250 2 . . . . A 19 GLU HG2 . 30389 1 207 . 1 1 19 19 GLU HG3 H 1 2.304 0.02 0.423 2 . . . . A 19 GLU HG3 . 30389 1 208 . 1 1 19 19 GLU C C 13 178.100 0.20 0.526 1 . . . . A 19 GLU C . 30389 1 209 . 1 1 19 19 GLU CA C 13 58.410 0.20 0.718 1 . . . . A 19 GLU CA . 30389 1 210 . 1 1 19 19 GLU CB C 13 29.680 0.20 1.000 1 . . . . A 19 GLU CB . 30389 1 211 . 1 1 19 19 GLU CG C 13 36.150 0.20 1.000 1 . . . . A 19 GLU CG . 30389 1 212 . 1 1 19 19 GLU N N 15 119.239 0.20 0.052 1 . . . . A 19 GLU N . 30389 1 213 . 1 1 20 20 LEU H H 1 7.975 0.02 0.526 1 . . . . A 20 LEU H . 30389 1 214 . 1 1 20 20 LEU HA H 1 4.144 0.02 1.000 1 . . . . A 20 LEU HA . 30389 1 215 . 1 1 20 20 LEU HB2 H 1 1.800 0.02 0.491 2 . . . . A 20 LEU HB2 . 30389 1 216 . 1 1 20 20 LEU HB3 H 1 1.800 0.02 0.549 2 . . . . A 20 LEU HB3 . 30389 1 217 . 1 1 20 20 LEU HG H 1 1.669 0.02 0.504 1 . . . . A 20 LEU HG . 30389 1 218 . 1 1 20 20 LEU HD11 H 1 0.938 0.02 0.491 2 . . . . A 20 LEU HD11 . 30389 1 219 . 1 1 20 20 LEU HD12 H 1 0.938 0.02 0.549 2 . . . . A 20 LEU HD12 . 30389 1 220 . 1 1 20 20 LEU HD13 H 1 0.938 0.02 0.491 2 . . . . A 20 LEU HD13 . 30389 1 221 . 1 1 20 20 LEU HD21 H 1 0.938 0.02 0.549 2 . . . . A 20 LEU HD21 . 30389 1 222 . 1 1 20 20 LEU HD22 H 1 0.938 0.02 0.491 2 . . . . A 20 LEU HD22 . 30389 1 223 . 1 1 20 20 LEU HD23 H 1 0.938 0.02 0.549 2 . . . . A 20 LEU HD23 . 30389 1 224 . 1 1 20 20 LEU C C 13 179.059 0.20 1.000 1 . . . . A 20 LEU C . 30389 1 225 . 1 1 20 20 LEU CA C 13 57.320 0.20 1.000 1 . . . . A 20 LEU CA . 30389 1 226 . 1 1 20 20 LEU CB C 13 41.730 0.20 1.000 1 . . . . A 20 LEU CB . 30389 1 227 . 1 1 20 20 LEU CG C 13 27.050 0.20 0.406 1 . . . . A 20 LEU CG . 30389 1 228 . 1 1 20 20 LEU CD1 C 13 24.860 0.20 0.521 2 . . . . A 20 LEU CD1 . 30389 1 229 . 1 1 20 20 LEU CD2 C 13 23.910 0.20 0.417 2 . . . . A 20 LEU CD2 . 30389 1 230 . 1 1 20 20 LEU N N 15 120.695 0.20 0.526 1 . . . . A 20 LEU N . 30389 1 231 . 1 1 21 21 LYS H H 1 8.015 0.02 1.000 1 . . . . A 21 LYS H . 30389 1 232 . 1 1 21 21 LYS HA H 1 4.114 0.02 1.000 1 . . . . A 21 LYS HA . 30389 1 233 . 1 1 21 21 LYS HB2 H 1 1.887 0.02 0.464 2 . . . . A 21 LYS HB2 . 30389 1 234 . 1 1 21 21 LYS HB3 H 1 1.887 0.02 0.460 2 . . . . A 21 LYS HB3 . 30389 1 235 . 1 1 21 21 LYS HG2 H 1 1.411 0.02 0.514 2 . . . . A 21 LYS HG2 . 30389 1 236 . 1 1 21 21 LYS HG3 H 1 1.411 0.02 0.477 2 . . . . A 21 LYS HG3 . 30389 1 237 . 1 1 21 21 LYS HD2 H 1 1.543 0.02 0.475 2 . . . . A 21 LYS HD2 . 30389 1 238 . 1 1 21 21 LYS HD3 H 1 1.543 0.02 0.482 2 . . . . A 21 LYS HD3 . 30389 1 239 . 1 1 21 21 LYS HE2 H 1 2.987 0.02 0.475 2 . . . . A 21 LYS HE2 . 30389 1 240 . 1 1 21 21 LYS HE3 H 1 2.987 0.02 0.482 2 . . . . A 21 LYS HE3 . 30389 1 241 . 1 1 21 21 LYS C C 13 178.312 0.20 1.000 1 . . . . A 21 LYS C . 30389 1 242 . 1 1 21 21 LYS CA C 13 58.770 0.20 1.000 1 . . . . A 21 LYS CA . 30389 1 243 . 1 1 21 21 LYS CB C 13 32.640 0.20 1.000 1 . . . . A 21 LYS CB . 30389 1 244 . 1 1 21 21 LYS CG C 13 25.440 0.20 1.000 1 . . . . A 21 LYS CG . 30389 1 245 . 1 1 21 21 LYS CD C 13 29.410 0.20 1.000 1 . . . . A 21 LYS CD . 30389 1 246 . 1 1 21 21 LYS CE C 13 42.250 0.20 1.000 1 . . . . A 21 LYS CE . 30389 1 247 . 1 1 21 21 LYS N N 15 119.562 0.20 1.000 1 . . . . A 21 LYS N . 30389 1 248 . 1 1 22 22 ARG H H 1 7.887 0.02 1.000 1 . . . . A 22 ARG H . 30389 1 249 . 1 1 22 22 ARG HA H 1 4.165 0.02 1.000 1 . . . . A 22 ARG HA . 30389 1 250 . 1 1 22 22 ARG HB2 H 1 1.920 0.02 0.639 2 . . . . A 22 ARG HB2 . 30389 1 251 . 1 1 22 22 ARG HB3 H 1 1.920 0.02 0.379 2 . . . . A 22 ARG HB3 . 30389 1 252 . 1 1 22 22 ARG HG2 H 1 1.618 0.02 0.520 2 . . . . A 22 ARG HG2 . 30389 1 253 . 1 1 22 22 ARG HG3 H 1 1.618 0.02 0.470 2 . . . . A 22 ARG HG3 . 30389 1 254 . 1 1 22 22 ARG HD2 H 1 3.224 0.02 0.726 2 . . . . A 22 ARG HD2 . 30389 1 255 . 1 1 22 22 ARG HD3 H 1 3.224 0.02 0.299 2 . . . . A 22 ARG HD3 . 30389 1 256 . 1 1 22 22 ARG C C 13 178.150 0.20 1.000 1 . . . . A 22 ARG C . 30389 1 257 . 1 1 22 22 ARG CA C 13 58.280 0.20 1.000 1 . . . . A 22 ARG CA . 30389 1 258 . 1 1 22 22 ARG CB C 13 30.250 0.20 1.000 1 . . . . A 22 ARG CB . 30389 1 259 . 1 1 22 22 ARG CG C 13 27.380 0.20 1.000 1 . . . . A 22 ARG CG . 30389 1 260 . 1 1 22 22 ARG CD C 13 43.380 0.20 0.884 1 . . . . A 22 ARG CD . 30389 1 261 . 1 1 22 22 ARG N N 15 120.110 0.20 1.000 1 . . . . A 22 ARG N . 30389 1 262 . 1 1 23 23 LEU H H 1 8.197 0.02 1.000 1 . . . . A 23 LEU H . 30389 1 263 . 1 1 23 23 LEU HA H 1 4.163 0.02 1.000 1 . . . . A 23 LEU HA . 30389 1 264 . 1 1 23 23 LEU HB2 H 1 1.791 0.02 0.506 2 . . . . A 23 LEU HB2 . 30389 1 265 . 1 1 23 23 LEU HB3 H 1 1.791 0.02 0.538 2 . . . . A 23 LEU HB3 . 30389 1 266 . 1 1 23 23 LEU HG H 1 1.602 0.02 0.508 1 . . . . A 23 LEU HG . 30389 1 267 . 1 1 23 23 LEU HD11 H 1 0.905 0.02 0.616 2 . . . . A 23 LEU HD11 . 30389 1 268 . 1 1 23 23 LEU HD12 H 1 0.905 0.02 0.616 2 . . . . A 23 LEU HD12 . 30389 1 269 . 1 1 23 23 LEU HD13 H 1 0.905 0.02 0.616 2 . . . . A 23 LEU HD13 . 30389 1 270 . 1 1 23 23 LEU HD21 H 1 0.905 0.02 0.507 2 . . . . A 23 LEU HD21 . 30389 1 271 . 1 1 23 23 LEU HD22 H 1 0.905 0.02 0.507 2 . . . . A 23 LEU HD22 . 30389 1 272 . 1 1 23 23 LEU HD23 H 1 0.905 0.02 0.507 2 . . . . A 23 LEU HD23 . 30389 1 273 . 1 1 23 23 LEU C C 13 178.905 0.20 1.000 1 . . . . A 23 LEU C . 30389 1 274 . 1 1 23 23 LEU CA C 13 57.090 0.20 1.000 1 . . . . A 23 LEU CA . 30389 1 275 . 1 1 23 23 LEU CB C 13 42.080 0.20 1.000 1 . . . . A 23 LEU CB . 30389 1 276 . 1 1 23 23 LEU CG C 13 27.050 0.20 0.398 1 . . . . A 23 LEU CG . 30389 1 277 . 1 1 23 23 LEU CD1 C 13 25.070 0.20 0.527 2 . . . . A 23 LEU CD1 . 30389 1 278 . 1 1 23 23 LEU CD2 C 13 23.770 0.20 0.421 2 . . . . A 23 LEU CD2 . 30389 1 279 . 1 1 23 23 LEU N N 15 120.689 0.20 1.000 1 . . . . A 23 LEU N . 30389 1 280 . 1 1 24 24 ASN H H 1 8.249 0.02 1.000 1 . . . . A 24 ASN H . 30389 1 281 . 1 1 24 24 ASN HA H 1 4.569 0.02 0.839 1 . . . . A 24 ASN HA . 30389 1 282 . 1 1 24 24 ASN HB2 H 1 2.857 0.02 0.672 2 . . . . A 24 ASN HB2 . 30389 1 283 . 1 1 24 24 ASN HB3 H 1 2.857 0.02 0.657 2 . . . . A 24 ASN HB3 . 30389 1 284 . 1 1 24 24 ASN C C 13 176.800 0.20 0.517 1 . . . . A 24 ASN C . 30389 1 285 . 1 1 24 24 ASN CA C 13 54.970 0.20 1.000 1 . . . . A 24 ASN CA . 30389 1 286 . 1 1 24 24 ASN CB C 13 38.610 0.20 0.734 1 . . . . A 24 ASN CB . 30389 1 287 . 1 1 24 24 ASN N N 15 117.970 0.20 1.000 1 . . . . A 24 ASN N . 30389 1 288 . 1 1 25 25 GLU H H 1 8.173 0.02 0.517 1 . . . . A 25 GLU H . 30389 1 289 . 1 1 25 25 GLU HA H 1 4.188 0.02 1.000 1 . . . . A 25 GLU HA . 30389 1 290 . 1 1 25 25 GLU HB2 H 1 2.107 0.02 0.630 2 . . . . A 25 GLU HB2 . 30389 1 291 . 1 1 25 25 GLU HB3 H 1 2.107 0.02 0.525 2 . . . . A 25 GLU HB3 . 30389 1 292 . 1 1 25 25 GLU HG2 H 1 2.403 0.02 0.471 2 . . . . A 25 GLU HG2 . 30389 1 293 . 1 1 25 25 GLU HG3 H 1 2.319 0.02 0.636 2 . . . . A 25 GLU HG3 . 30389 1 294 . 1 1 25 25 GLU C C 13 177.800 0.20 1.000 1 . . . . A 25 GLU C . 30389 1 295 . 1 1 25 25 GLU CA C 13 58.160 0.20 1.000 1 . . . . A 25 GLU CA . 30389 1 296 . 1 1 25 25 GLU CB C 13 30.180 0.20 0.693 1 . . . . A 25 GLU CB . 30389 1 297 . 1 1 25 25 GLU CG C 13 36.470 0.20 1.000 1 . . . . A 25 GLU CG . 30389 1 298 . 1 1 25 25 GLU N N 15 120.990 0.20 0.517 1 . . . . A 25 GLU N . 30389 1 299 . 1 1 26 26 GLU H H 1 8.292 0.02 1.000 1 . . . . A 26 GLU H . 30389 1 300 . 1 1 26 26 GLU HA H 1 4.196 0.02 0.544 1 . . . . A 26 GLU HA . 30389 1 301 . 1 1 26 26 GLU HB2 H 1 2.069 0.02 0.527 2 . . . . A 26 GLU HB2 . 30389 1 302 . 1 1 26 26 GLU HB3 H 1 2.069 0.02 0.349 2 . . . . A 26 GLU HB3 . 30389 1 303 . 1 1 26 26 GLU HG2 H 1 2.399 0.02 0.720 2 . . . . A 26 GLU HG2 . 30389 1 304 . 1 1 26 26 GLU HG3 H 1 2.241 0.02 0.570 2 . . . . A 26 GLU HG3 . 30389 1 305 . 1 1 26 26 GLU C C 13 177.800 0.20 0.500 1 . . . . A 26 GLU C . 30389 1 306 . 1 1 26 26 GLU CA C 13 58.000 0.20 0.705 1 . . . . A 26 GLU CA . 30389 1 307 . 1 1 26 26 GLU CB C 13 29.990 0.20 1.000 1 . . . . A 26 GLU CB . 30389 1 308 . 1 1 26 26 GLU CG C 13 36.540 0.20 1.000 1 . . . . A 26 GLU CG . 30389 1 309 . 1 1 26 26 GLU N N 15 120.868 0.20 1.000 1 . . . . A 26 GLU N . 30389 1 310 . 1 1 27 27 ARG H H 1 8.131 0.02 0.500 1 . . . . A 27 ARG H . 30389 1 311 . 1 1 27 27 ARG HA H 1 4.228 0.02 1.000 1 . . . . A 27 ARG HA . 30389 1 312 . 1 1 27 27 ARG HB2 H 1 1.874 0.02 0.467 2 . . . . A 27 ARG HB2 . 30389 1 313 . 1 1 27 27 ARG HB3 H 1 1.874 0.02 0.489 2 . . . . A 27 ARG HB3 . 30389 1 314 . 1 1 27 27 ARG HG2 H 1 1.653 0.02 0.468 2 . . . . A 27 ARG HG2 . 30389 1 315 . 1 1 27 27 ARG HG3 H 1 1.653 0.02 0.504 2 . . . . A 27 ARG HG3 . 30389 1 316 . 1 1 27 27 ARG HD2 H 1 3.196 0.02 0.467 2 . . . . A 27 ARG HD2 . 30389 1 317 . 1 1 27 27 ARG HD3 H 1 3.196 0.02 0.489 2 . . . . A 27 ARG HD3 . 30389 1 318 . 1 1 27 27 ARG C C 13 177.166 0.20 1.000 1 . . . . A 27 ARG C . 30389 1 319 . 1 1 27 27 ARG CA C 13 57.500 0.20 1.000 1 . . . . A 27 ARG CA . 30389 1 320 . 1 1 27 27 ARG CB C 13 30.400 0.20 1.000 1 . . . . A 27 ARG CB . 30389 1 321 . 1 1 27 27 ARG CG C 13 27.240 0.20 1.000 1 . . . . A 27 ARG CG . 30389 1 322 . 1 1 27 27 ARG CD C 13 43.390 0.20 1.000 1 . . . . A 27 ARG CD . 30389 1 323 . 1 1 27 27 ARG N N 15 120.674 0.20 0.500 1 . . . . A 27 ARG N . 30389 1 324 . 1 1 28 28 HIS H H 1 8.307 0.02 1.000 1 . . . . A 28 HIS H . 30389 1 325 . 1 1 28 28 HIS HA H 1 4.594 0.02 1.000 1 . . . . A 28 HIS HA . 30389 1 326 . 1 1 28 28 HIS HB2 H 1 3.257 0.02 0.722 2 . . . . A 28 HIS HB2 . 30389 1 327 . 1 1 28 28 HIS HB3 H 1 3.257 0.02 0.861 2 . . . . A 28 HIS HB3 . 30389 1 328 . 1 1 28 28 HIS C C 13 176.006 0.20 1.000 1 . . . . A 28 HIS C . 30389 1 329 . 1 1 28 28 HIS CA C 13 57.230 0.20 1.000 1 . . . . A 28 HIS CA . 30389 1 330 . 1 1 28 28 HIS CB C 13 29.430 0.20 1.000 1 . . . . A 28 HIS CB . 30389 1 331 . 1 1 28 28 HIS N N 15 118.902 0.20 1.000 1 . . . . A 28 HIS N . 30389 1 332 . 1 1 29 29 ASP H H 1 8.385 0.02 1.000 1 . . . . A 29 ASP H . 30389 1 333 . 1 1 29 29 ASP HA H 1 4.517 0.02 1.000 1 . . . . A 29 ASP HA . 30389 1 334 . 1 1 29 29 ASP HB2 H 1 2.705 0.02 0.828 2 . . . . A 29 ASP HB2 . 30389 1 335 . 1 1 29 29 ASP HB3 H 1 2.705 0.02 0.362 2 . . . . A 29 ASP HB3 . 30389 1 336 . 1 1 29 29 ASP C C 13 177.118 0.20 1.000 1 . . . . A 29 ASP C . 30389 1 337 . 1 1 29 29 ASP CA C 13 55.660 0.20 1.000 1 . . . . A 29 ASP CA . 30389 1 338 . 1 1 29 29 ASP CB C 13 40.930 0.20 1.000 1 . . . . A 29 ASP CB . 30389 1 339 . 1 1 29 29 ASP N N 15 120.486 0.20 1.000 1 . . . . A 29 ASP N . 30389 1 340 . 1 1 30 30 HIS H H 1 8.368 0.02 1.000 1 . . . . A 30 HIS H . 30389 1 341 . 1 1 30 30 HIS HA H 1 4.404 0.02 1.000 1 . . . . A 30 HIS HA . 30389 1 342 . 1 1 30 30 HIS HB2 H 1 3.288 0.02 0.766 2 . . . . A 30 HIS HB2 . 30389 1 343 . 1 1 30 30 HIS HB3 H 1 3.288 0.02 0.848 2 . . . . A 30 HIS HB3 . 30389 1 344 . 1 1 30 30 HIS C C 13 176.155 0.20 1.000 1 . . . . A 30 HIS C . 30389 1 345 . 1 1 30 30 HIS CA C 13 58.160 0.20 1.000 1 . . . . A 30 HIS CA . 30389 1 346 . 1 1 30 30 HIS CB C 13 29.570 0.20 1.000 1 . . . . A 30 HIS CB . 30389 1 347 . 1 1 30 30 HIS N N 15 119.181 0.20 1.000 1 . . . . A 30 HIS N . 30389 1 348 . 1 1 31 31 ASP H H 1 8.458 0.02 1.000 1 . . . . A 31 ASP H . 30389 1 349 . 1 1 31 31 ASP HA H 1 4.452 0.02 1.000 1 . . . . A 31 ASP HA . 30389 1 350 . 1 1 31 31 ASP HB2 H 1 2.740 0.02 0.607 2 . . . . A 31 ASP HB2 . 30389 1 351 . 1 1 31 31 ASP HB3 H 1 2.740 0.02 0.547 2 . . . . A 31 ASP HB3 . 30389 1 352 . 1 1 31 31 ASP C C 13 177.925 0.20 1.000 1 . . . . A 31 ASP C . 30389 1 353 . 1 1 31 31 ASP CA C 13 56.020 0.20 1.000 1 . . . . A 31 ASP CA . 30389 1 354 . 1 1 31 31 ASP CB C 13 40.460 0.20 1.000 1 . . . . A 31 ASP CB . 30389 1 355 . 1 1 31 31 ASP N N 15 120.440 0.20 1.000 1 . . . . A 31 ASP N . 30389 1 356 . 1 1 32 32 LYS H H 1 8.207 0.02 1.000 1 . . . . A 32 LYS H . 30389 1 357 . 1 1 32 32 LYS HA H 1 4.171 0.02 1.000 1 . . . . A 32 LYS HA . 30389 1 358 . 1 1 32 32 LYS HB2 H 1 1.867 0.02 0.421 2 . . . . A 32 LYS HB2 . 30389 1 359 . 1 1 32 32 LYS HB3 H 1 1.867 0.02 0.497 2 . . . . A 32 LYS HB3 . 30389 1 360 . 1 1 32 32 LYS HG2 H 1 1.437 0.02 0.896 2 . . . . A 32 LYS HG2 . 30389 1 361 . 1 1 32 32 LYS HG3 H 1 1.437 0.02 0.419 2 . . . . A 32 LYS HG3 . 30389 1 362 . 1 1 32 32 LYS C C 13 177.952 0.20 1.000 1 . . . . A 32 LYS C . 30389 1 363 . 1 1 32 32 LYS CA C 13 58.280 0.20 1.000 1 . . . . A 32 LYS CA . 30389 1 364 . 1 1 32 32 LYS CB C 13 32.590 0.20 1.000 1 . . . . A 32 LYS CB . 30389 1 365 . 1 1 32 32 LYS CG C 13 24.930 0.20 0.590 1 . . . . A 32 LYS CG . 30389 1 366 . 1 1 32 32 LYS N N 15 122.388 0.20 1.000 1 . . . . A 32 LYS N . 30389 1 367 . 1 1 33 33 ARG H H 1 8.178 0.02 1.000 1 . . . . A 33 ARG H . 30389 1 368 . 1 1 33 33 ARG HA H 1 4.185 0.02 1.000 1 . . . . A 33 ARG HA . 30389 1 369 . 1 1 33 33 ARG HB2 H 1 1.897 0.02 0.377 2 . . . . A 33 ARG HB2 . 30389 1 370 . 1 1 33 33 ARG HB3 H 1 1.897 0.02 0.467 2 . . . . A 33 ARG HB3 . 30389 1 371 . 1 1 33 33 ARG HG2 H 1 1.691 0.02 0.460 2 . . . . A 33 ARG HG2 . 30389 1 372 . 1 1 33 33 ARG HG3 H 1 1.691 0.02 0.456 2 . . . . A 33 ARG HG3 . 30389 1 373 . 1 1 33 33 ARG HD2 H 1 3.208 0.02 0.377 2 . . . . A 33 ARG HD2 . 30389 1 374 . 1 1 33 33 ARG HD3 H 1 3.208 0.02 0.467 2 . . . . A 33 ARG HD3 . 30389 1 375 . 1 1 33 33 ARG C C 13 178.647 0.20 1.000 1 . . . . A 33 ARG C . 30389 1 376 . 1 1 33 33 ARG CA C 13 58.150 0.20 1.000 1 . . . . A 33 ARG CA . 30389 1 377 . 1 1 33 33 ARG CB C 13 30.200 0.20 0.881 1 . . . . A 33 ARG CB . 30389 1 378 . 1 1 33 33 ARG CG C 13 27.650 0.20 1.000 1 . . . . A 33 ARG CG . 30389 1 379 . 1 1 33 33 ARG CD C 13 43.440 0.20 0.881 1 . . . . A 33 ARG CD . 30389 1 380 . 1 1 33 33 ARG N N 15 120.121 0.20 1.000 1 . . . . A 33 ARG N . 30389 1 381 . 1 1 34 34 GLU H H 1 8.285 0.02 1.000 1 . . . . A 34 GLU H . 30389 1 382 . 1 1 34 34 GLU HA H 1 4.162 0.02 0.686 1 . . . . A 34 GLU HA . 30389 1 383 . 1 1 34 34 GLU HB2 H 1 2.016 0.02 0.614 2 . . . . A 34 GLU HB2 . 30389 1 384 . 1 1 34 34 GLU HB3 H 1 2.016 0.02 0.479 2 . . . . A 34 GLU HB3 . 30389 1 385 . 1 1 34 34 GLU HG2 H 1 2.210 0.02 0.773 2 . . . . A 34 GLU HG2 . 30389 1 386 . 1 1 34 34 GLU HG3 H 1 2.210 0.02 0.401 2 . . . . A 34 GLU HG3 . 30389 1 387 . 1 1 34 34 GLU C C 13 177.850 0.20 1.000 1 . . . . A 34 GLU C . 30389 1 388 . 1 1 34 34 GLU CA C 13 58.180 0.20 1.000 1 . . . . A 34 GLU CA . 30389 1 389 . 1 1 34 34 GLU CB C 13 29.720 0.20 0.866 1 . . . . A 34 GLU CB . 30389 1 390 . 1 1 34 34 GLU CG C 13 36.190 0.20 1.000 1 . . . . A 34 GLU CG . 30389 1 391 . 1 1 34 34 GLU N N 15 120.696 0.20 1.000 1 . . . . A 34 GLU N . 30389 1 392 . 1 1 35 35 ALA H H 1 8.094 0.02 1.000 1 . . . . A 35 ALA H . 30389 1 393 . 1 1 35 35 ALA C C 13 180.053 0.20 1.000 1 . . . . A 35 ALA C . 30389 1 394 . 1 1 35 35 ALA CA C 13 54.290 0.20 1.000 1 . . . . A 35 ALA CA . 30389 1 395 . 1 1 35 35 ALA CB C 13 18.420 0.20 1.000 1 . . . . A 35 ALA CB . 30389 1 396 . 1 1 35 35 ALA N N 15 122.701 0.20 1.000 1 . . . . A 35 ALA N . 30389 1 397 . 1 1 36 36 GLU HA H 1 4.122 0.02 1.000 1 . . . . A 36 GLU HA . 30389 1 398 . 1 1 36 36 GLU HB2 H 1 2.079 0.02 0.471 2 . . . . A 36 GLU HB2 . 30389 1 399 . 1 1 36 36 GLU HB3 H 1 2.079 0.02 0.520 2 . . . . A 36 GLU HB3 . 30389 1 400 . 1 1 36 36 GLU HG2 H 1 2.429 0.02 0.470 2 . . . . A 36 GLU HG2 . 30389 1 401 . 1 1 36 36 GLU HG3 H 1 2.253 0.02 0.458 2 . . . . A 36 GLU HG3 . 30389 1 402 . 1 1 36 36 GLU C C 13 178.100 0.20 1.000 1 . . . . A 36 GLU C . 30389 1 403 . 1 1 36 36 GLU CA C 13 58.280 0.20 1.000 1 . . . . A 36 GLU CA . 30389 1 404 . 1 1 36 36 GLU CB C 13 29.860 0.20 1.000 1 . . . . A 36 GLU CB . 30389 1 405 . 1 1 36 36 GLU CG C 13 36.540 0.20 0.898 1 . . . . A 36 GLU CG . 30389 1 406 . 1 1 37 37 ARG H H 1 8.056 0.02 1.000 1 . . . . A 37 ARG H . 30389 1 407 . 1 1 37 37 ARG HA H 1 4.167 0.02 1.000 1 . . . . A 37 ARG HA . 30389 1 408 . 1 1 37 37 ARG HB2 H 1 1.926 0.02 0.505 2 . . . . A 37 ARG HB2 . 30389 1 409 . 1 1 37 37 ARG HB3 H 1 1.926 0.02 0.805 2 . . . . A 37 ARG HB3 . 30389 1 410 . 1 1 37 37 ARG HG2 H 1 1.624 0.02 0.303 2 . . . . A 37 ARG HG2 . 30389 1 411 . 1 1 37 37 ARG HG3 H 1 1.624 0.02 0.300 2 . . . . A 37 ARG HG3 . 30389 1 412 . 1 1 37 37 ARG HD2 H 1 3.225 0.02 0.717 2 . . . . A 37 ARG HD2 . 30389 1 413 . 1 1 37 37 ARG HD3 H 1 3.225 0.02 0.298 2 . . . . A 37 ARG HD3 . 30389 1 414 . 1 1 37 37 ARG C C 13 178.100 0.20 1.000 1 . . . . A 37 ARG C . 30389 1 415 . 1 1 37 37 ARG CA C 13 58.200 0.20 1.000 1 . . . . A 37 ARG CA . 30389 1 416 . 1 1 37 37 ARG CB C 13 30.160 0.20 0.790 1 . . . . A 37 ARG CB . 30389 1 417 . 1 1 37 37 ARG CG C 13 27.340 0.20 0.824 1 . . . . A 37 ARG CG . 30389 1 418 . 1 1 37 37 ARG CD C 13 43.370 0.20 0.723 1 . . . . A 37 ARG CD . 30389 1 419 . 1 1 37 37 ARG N N 15 121.090 0.20 1.000 1 . . . . A 37 ARG N . 30389 1 420 . 1 1 38 38 LYS H H 1 8.201 0.02 1.000 1 . . . . A 38 LYS H . 30389 1 421 . 1 1 38 38 LYS HA H 1 4.113 0.02 1.000 1 . . . . A 38 LYS HA . 30389 1 422 . 1 1 38 38 LYS HB2 H 1 1.860 0.02 0.468 2 . . . . A 38 LYS HB2 . 30389 1 423 . 1 1 38 38 LYS HB3 H 1 1.860 0.02 0.483 2 . . . . A 38 LYS HB3 . 30389 1 424 . 1 1 38 38 LYS HG2 H 1 1.471 0.02 0.452 2 . . . . A 38 LYS HG2 . 30389 1 425 . 1 1 38 38 LYS HG3 H 1 1.471 0.02 0.492 2 . . . . A 38 LYS HG3 . 30389 1 426 . 1 1 38 38 LYS HE2 H 1 2.998 0.02 0.468 2 . . . . A 38 LYS HE2 . 30389 1 427 . 1 1 38 38 LYS HE3 H 1 2.998 0.02 0.483 2 . . . . A 38 LYS HE3 . 30389 1 428 . 1 1 38 38 LYS C C 13 177.514 0.20 1.000 1 . . . . A 38 LYS C . 30389 1 429 . 1 1 38 38 LYS CA C 13 58.000 0.20 1.000 1 . . . . A 38 LYS CA . 30389 1 430 . 1 1 38 38 LYS CB C 13 32.580 0.20 1.000 1 . . . . A 38 LYS CB . 30389 1 431 . 1 1 38 38 LYS CG C 13 25.100 0.20 1.000 1 . . . . A 38 LYS CG . 30389 1 432 . 1 1 38 38 LYS CD C 13 29.030 0.20 1.000 1 . . . . A 38 LYS CD . 30389 1 433 . 1 1 38 38 LYS CE C 13 42.030 0.20 1.000 1 . . . . A 38 LYS CE . 30389 1 434 . 1 1 38 38 LYS N N 15 120.813 0.20 1.000 1 . . . . A 38 LYS N . 30389 1 435 . 1 1 39 39 ALA H H 1 7.971 0.02 1.000 1 . . . . A 39 ALA H . 30389 1 436 . 1 1 39 39 ALA HA H 1 4.240 0.02 1.000 1 . . . . A 39 ALA HA . 30389 1 437 . 1 1 39 39 ALA HB1 H 1 1.467 0.02 1.000 1 . . . . A 39 ALA HB1 . 30389 1 438 . 1 1 39 39 ALA HB2 H 1 1.467 0.02 1.000 1 . . . . A 39 ALA HB2 . 30389 1 439 . 1 1 39 39 ALA HB3 H 1 1.467 0.02 1.000 1 . . . . A 39 ALA HB3 . 30389 1 440 . 1 1 39 39 ALA C C 13 179.319 0.20 1.000 1 . . . . A 39 ALA C . 30389 1 441 . 1 1 39 39 ALA CA C 13 53.880 0.20 1.000 1 . . . . A 39 ALA CA . 30389 1 442 . 1 1 39 39 ALA CB C 13 18.560 0.20 1.000 1 . . . . A 39 ALA CB . 30389 1 443 . 1 1 39 39 ALA N N 15 121.968 0.20 1.000 1 . . . . A 39 ALA N . 30389 1 444 . 1 1 40 40 LEU H H 1 7.831 0.02 1.000 1 . . . . A 40 LEU H . 30389 1 445 . 1 1 40 40 LEU HA H 1 4.235 0.02 1.000 1 . . . . A 40 LEU HA . 30389 1 446 . 1 1 40 40 LEU HB2 H 1 1.728 0.02 0.451 2 . . . . A 40 LEU HB2 . 30389 1 447 . 1 1 40 40 LEU HB3 H 1 1.728 0.02 0.534 2 . . . . A 40 LEU HB3 . 30389 1 448 . 1 1 40 40 LEU HD11 H 1 0.925 0.02 0.565 2 . . . . A 40 LEU HD11 . 30389 1 449 . 1 1 40 40 LEU HD12 H 1 0.925 0.02 0.565 2 . . . . A 40 LEU HD12 . 30389 1 450 . 1 1 40 40 LEU HD13 H 1 0.925 0.02 0.565 2 . . . . A 40 LEU HD13 . 30389 1 451 . 1 1 40 40 LEU HD21 H 1 0.925 0.02 0.527 2 . . . . A 40 LEU HD21 . 30389 1 452 . 1 1 40 40 LEU HD22 H 1 0.925 0.02 0.527 2 . . . . A 40 LEU HD22 . 30389 1 453 . 1 1 40 40 LEU HD23 H 1 0.925 0.02 0.527 2 . . . . A 40 LEU HD23 . 30389 1 454 . 1 1 40 40 LEU C C 13 178.469 0.20 1.000 1 . . . . A 40 LEU C . 30389 1 455 . 1 1 40 40 LEU CA C 13 56.700 0.20 1.000 1 . . . . A 40 LEU CA . 30389 1 456 . 1 1 40 40 LEU CB C 13 42.160 0.20 1.000 1 . . . . A 40 LEU CB . 30389 1 457 . 1 1 40 40 LEU CG C 13 26.970 0.20 1.000 1 . . . . A 40 LEU CG . 30389 1 458 . 1 1 40 40 LEU CD1 C 13 23.800 0.20 0.716 2 . . . . A 40 LEU CD1 . 30389 1 459 . 1 1 40 40 LEU CD2 C 13 24.780 0.20 0.716 2 . . . . A 40 LEU CD2 . 30389 1 460 . 1 1 40 40 LEU N N 15 119.475 0.20 1.000 1 . . . . A 40 LEU N . 30389 1 461 . 1 1 41 41 GLU H H 1 8.141 0.02 1.000 1 . . . . A 41 GLU H . 30389 1 462 . 1 1 41 41 GLU HA H 1 4.121 0.02 0.844 1 . . . . A 41 GLU HA . 30389 1 463 . 1 1 41 41 GLU HB2 H 1 2.079 0.02 0.471 2 . . . . A 41 GLU HB2 . 30389 1 464 . 1 1 41 41 GLU HB3 H 1 2.079 0.02 0.520 2 . . . . A 41 GLU HB3 . 30389 1 465 . 1 1 41 41 GLU HG2 H 1 2.393 0.02 0.470 2 . . . . A 41 GLU HG2 . 30389 1 466 . 1 1 41 41 GLU HG3 H 1 2.253 0.02 0.458 2 . . . . A 41 GLU HG3 . 30389 1 467 . 1 1 41 41 GLU C C 13 177.802 0.20 1.000 1 . . . . A 41 GLU C . 30389 1 468 . 1 1 41 41 GLU CA C 13 58.020 0.20 1.000 1 . . . . A 41 GLU CA . 30389 1 469 . 1 1 41 41 GLU CB C 13 30.040 0.20 1.000 1 . . . . A 41 GLU CB . 30389 1 470 . 1 1 41 41 GLU CG C 13 36.570 0.20 0.850 1 . . . . A 41 GLU CG . 30389 1 471 . 1 1 41 41 GLU N N 15 120.044 0.20 1.000 1 . . . . A 41 GLU N . 30389 1 472 . 1 1 42 42 ASP H H 1 8.319 0.02 1.000 1 . . . . A 42 ASP H . 30389 1 473 . 1 1 42 42 ASP HA H 1 4.536 0.02 0.897 1 . . . . A 42 ASP HA . 30389 1 474 . 1 1 42 42 ASP HB2 H 1 2.703 0.02 0.814 2 . . . . A 42 ASP HB2 . 30389 1 475 . 1 1 42 42 ASP HB3 H 1 2.703 0.02 0.356 2 . . . . A 42 ASP HB3 . 30389 1 476 . 1 1 42 42 ASP C C 13 177.156 0.20 0.508 1 . . . . A 42 ASP C . 30389 1 477 . 1 1 42 42 ASP CA C 13 55.970 0.20 0.850 1 . . . . A 42 ASP CA . 30389 1 478 . 1 1 42 42 ASP CB C 13 40.770 0.20 1.000 1 . . . . A 42 ASP CB . 30389 1 479 . 1 1 42 42 ASP N N 15 120.591 0.20 1.000 1 . . . . A 42 ASP N . 30389 1 480 . 1 1 43 43 LYS H H 1 7.978 0.02 0.508 1 . . . . A 43 LYS H . 30389 1 481 . 1 1 43 43 LYS HA H 1 4.273 0.02 0.867 1 . . . . A 43 LYS HA . 30389 1 482 . 1 1 43 43 LYS HB2 H 1 1.900 0.02 0.447 2 . . . . A 43 LYS HB2 . 30389 1 483 . 1 1 43 43 LYS HB3 H 1 1.900 0.02 0.544 2 . . . . A 43 LYS HB3 . 30389 1 484 . 1 1 43 43 LYS HG2 H 1 1.480 0.02 0.447 2 . . . . A 43 LYS HG2 . 30389 1 485 . 1 1 43 43 LYS HG3 H 1 1.480 0.02 0.544 2 . . . . A 43 LYS HG3 . 30389 1 486 . 1 1 43 43 LYS HE2 H 1 2.955 0.02 0.447 2 . . . . A 43 LYS HE2 . 30389 1 487 . 1 1 43 43 LYS HE3 H 1 2.955 0.02 0.544 2 . . . . A 43 LYS HE3 . 30389 1 488 . 1 1 43 43 LYS C C 13 177.483 0.20 1.000 1 . . . . A 43 LYS C . 30389 1 489 . 1 1 43 43 LYS CA C 13 57.200 0.20 1.000 1 . . . . A 43 LYS CA . 30389 1 490 . 1 1 43 43 LYS CB C 13 32.620 0.20 1.000 1 . . . . A 43 LYS CB . 30389 1 491 . 1 1 43 43 LYS CG C 13 24.930 0.20 1.000 1 . . . . A 43 LYS CG . 30389 1 492 . 1 1 43 43 LYS CD C 13 29.220 0.20 1.000 1 . . . . A 43 LYS CD . 30389 1 493 . 1 1 43 43 LYS CE C 13 40.940 0.20 1.000 1 . . . . A 43 LYS CE . 30389 1 494 . 1 1 43 43 LYS N N 15 120.750 0.20 0.508 1 . . . . A 43 LYS N . 30389 1 495 . 1 1 44 44 LEU H H 1 8.081 0.02 1.000 1 . . . . A 44 LEU H . 30389 1 496 . 1 1 44 44 LEU HA H 1 4.269 0.02 1.000 1 . . . . A 44 LEU HA . 30389 1 497 . 1 1 44 44 LEU HB2 H 1 1.746 0.02 0.525 2 . . . . A 44 LEU HB2 . 30389 1 498 . 1 1 44 44 LEU HB3 H 1 1.746 0.02 0.510 2 . . . . A 44 LEU HB3 . 30389 1 499 . 1 1 44 44 LEU HG H 1 1.603 0.02 0.472 1 . . . . A 44 LEU HG . 30389 1 500 . 1 1 44 44 LEU HD11 H 1 0.909 0.02 0.580 2 . . . . A 44 LEU HD11 . 30389 1 501 . 1 1 44 44 LEU HD12 H 1 0.909 0.02 0.580 2 . . . . A 44 LEU HD12 . 30389 1 502 . 1 1 44 44 LEU HD13 H 1 0.909 0.02 0.580 2 . . . . A 44 LEU HD13 . 30389 1 503 . 1 1 44 44 LEU HD21 H 1 0.909 0.02 0.443 2 . . . . A 44 LEU HD21 . 30389 1 504 . 1 1 44 44 LEU HD22 H 1 0.909 0.02 0.443 2 . . . . A 44 LEU HD22 . 30389 1 505 . 1 1 44 44 LEU HD23 H 1 0.909 0.02 0.443 2 . . . . A 44 LEU HD23 . 30389 1 506 . 1 1 44 44 LEU C C 13 177.737 0.20 1.000 1 . . . . A 44 LEU C . 30389 1 507 . 1 1 44 44 LEU CA C 13 55.710 0.20 1.000 1 . . . . A 44 LEU CA . 30389 1 508 . 1 1 44 44 LEU CB C 13 42.020 0.20 1.000 1 . . . . A 44 LEU CB . 30389 1 509 . 1 1 44 44 LEU CG C 13 26.990 0.20 1.000 1 . . . . A 44 LEU CG . 30389 1 510 . 1 1 44 44 LEU CD1 C 13 25.120 0.20 1.000 2 . . . . A 44 LEU CD1 . 30389 1 511 . 1 1 44 44 LEU CD2 C 13 23.410 0.20 1.000 2 . . . . A 44 LEU CD2 . 30389 1 512 . 1 1 44 44 LEU N N 15 121.225 0.20 1.000 1 . . . . A 44 LEU N . 30389 1 513 . 1 1 45 45 ALA H H 1 7.976 0.02 1.000 1 . . . . A 45 ALA H . 30389 1 514 . 1 1 45 45 ALA HA H 1 4.257 0.02 1.000 1 . . . . A 45 ALA HA . 30389 1 515 . 1 1 45 45 ALA HB1 H 1 1.435 0.02 1.000 1 . . . . A 45 ALA HB1 . 30389 1 516 . 1 1 45 45 ALA HB2 H 1 1.435 0.02 1.000 1 . . . . A 45 ALA HB2 . 30389 1 517 . 1 1 45 45 ALA HB3 H 1 1.435 0.02 1.000 1 . . . . A 45 ALA HB3 . 30389 1 518 . 1 1 45 45 ALA C C 13 177.763 0.20 1.000 1 . . . . A 45 ALA C . 30389 1 519 . 1 1 45 45 ALA CA C 13 52.920 0.20 1.000 1 . . . . A 45 ALA CA . 30389 1 520 . 1 1 45 45 ALA CB C 13 19.180 0.20 1.000 1 . . . . A 45 ALA CB . 30389 1 521 . 1 1 45 45 ALA N N 15 123.162 0.20 1.000 1 . . . . A 45 ALA N . 30389 1 522 . 1 1 46 46 ASP H H 1 8.113 0.02 1.000 1 . . . . A 46 ASP H . 30389 1 523 . 1 1 46 46 ASP HA H 1 4.559 0.02 0.724 1 . . . . A 46 ASP HA . 30389 1 524 . 1 1 46 46 ASP HB2 H 1 2.700 0.02 0.815 2 . . . . A 46 ASP HB2 . 30389 1 525 . 1 1 46 46 ASP HB3 H 1 2.700 0.02 0.847 2 . . . . A 46 ASP HB3 . 30389 1 526 . 1 1 46 46 ASP C C 13 176.462 0.20 1.000 1 . . . . A 46 ASP C . 30389 1 527 . 1 1 46 46 ASP CA C 13 55.230 0.20 1.000 1 . . . . A 46 ASP CA . 30389 1 528 . 1 1 46 46 ASP CB C 13 41.100 0.20 1.000 1 . . . . A 46 ASP CB . 30389 1 529 . 1 1 46 46 ASP N N 15 118.985 0.20 1.000 1 . . . . A 46 ASP N . 30389 1 530 . 1 1 47 47 LYS H H 1 8.157 0.02 1.000 1 . . . . A 47 LYS H . 30389 1 531 . 1 1 47 47 LYS HA H 1 4.295 0.02 0.511 1 . . . . A 47 LYS HA . 30389 1 532 . 1 1 47 47 LYS HB2 H 1 1.888 0.02 0.529 2 . . . . A 47 LYS HB2 . 30389 1 533 . 1 1 47 47 LYS HB3 H 1 1.888 0.02 0.419 2 . . . . A 47 LYS HB3 . 30389 1 534 . 1 1 47 47 LYS HG2 H 1 1.436 0.02 0.751 2 . . . . A 47 LYS HG2 . 30389 1 535 . 1 1 47 47 LYS HG3 H 1 1.436 0.02 0.465 2 . . . . A 47 LYS HG3 . 30389 1 536 . 1 1 47 47 LYS HD2 H 1 1.789 0.02 0.475 2 . . . . A 47 LYS HD2 . 30389 1 537 . 1 1 47 47 LYS HD3 H 1 1.789 0.02 0.477 2 . . . . A 47 LYS HD3 . 30389 1 538 . 1 1 47 47 LYS HE2 H 1 2.969 0.02 0.475 2 . . . . A 47 LYS HE2 . 30389 1 539 . 1 1 47 47 LYS HE3 H 1 2.969 0.02 0.477 2 . . . . A 47 LYS HE3 . 30389 1 540 . 1 1 47 47 LYS C C 13 176.700 0.20 0.500 1 . . . . A 47 LYS C . 30389 1 541 . 1 1 47 47 LYS CA C 13 56.420 0.20 0.711 1 . . . . A 47 LYS CA . 30389 1 542 . 1 1 47 47 LYS CB C 13 32.720 0.20 1.000 1 . . . . A 47 LYS CB . 30389 1 543 . 1 1 47 47 LYS CG C 13 24.720 0.20 1.000 1 . . . . A 47 LYS CG . 30389 1 544 . 1 1 47 47 LYS CD C 13 29.240 0.20 1.000 1 . . . . A 47 LYS CD . 30389 1 545 . 1 1 47 47 LYS N N 15 121.026 0.20 1.000 1 . . . . A 47 LYS N . 30389 1 546 . 1 1 48 48 GLN H H 1 8.315 0.02 0.500 1 . . . . A 48 GLN H . 30389 1 547 . 1 1 48 48 GLN HA H 1 4.269 0.02 1.000 1 . . . . A 48 GLN HA . 30389 1 548 . 1 1 48 48 GLN HB2 H 1 2.020 0.02 0.594 2 . . . . A 48 GLN HB2 . 30389 1 549 . 1 1 48 48 GLN HB3 H 1 2.020 0.02 0.494 2 . . . . A 48 GLN HB3 . 30389 1 550 . 1 1 48 48 GLN HG2 H 1 2.341 0.02 0.502 2 . . . . A 48 GLN HG2 . 30389 1 551 . 1 1 48 48 GLN HG3 H 1 2.341 0.02 0.517 2 . . . . A 48 GLN HG3 . 30389 1 552 . 1 1 48 48 GLN C C 13 175.959 0.20 1.000 1 . . . . A 48 GLN C . 30389 1 553 . 1 1 48 48 GLN CA C 13 55.960 0.20 1.000 1 . . . . A 48 GLN CA . 30389 1 554 . 1 1 48 48 GLN CB C 13 29.430 0.20 1.000 1 . . . . A 48 GLN CB . 30389 1 555 . 1 1 48 48 GLN CG C 13 33.920 0.20 1.000 1 . . . . A 48 GLN CG . 30389 1 556 . 1 1 48 48 GLN N N 15 120.539 0.20 0.500 1 . . . . A 48 GLN N . 30389 1 557 . 1 1 49 49 GLU H H 1 8.394 0.02 1.000 1 . . . . A 49 GLU H . 30389 1 558 . 1 1 49 49 GLU HA H 1 4.207 0.02 1.000 1 . . . . A 49 GLU HA . 30389 1 559 . 1 1 49 49 GLU HB2 H 1 1.910 0.02 0.505 2 . . . . A 49 GLU HB2 . 30389 1 560 . 1 1 49 49 GLU HB3 H 1 1.910 0.02 0.642 2 . . . . A 49 GLU HB3 . 30389 1 561 . 1 1 49 49 GLU HG2 H 1 2.185 0.02 0.642 2 . . . . A 49 GLU HG2 . 30389 1 562 . 1 1 49 49 GLU HG3 H 1 2.185 0.02 0.400 2 . . . . A 49 GLU HG3 . 30389 1 563 . 1 1 49 49 GLU C C 13 176.207 0.20 1.000 1 . . . . A 49 GLU C . 30389 1 564 . 1 1 49 49 GLU CA C 13 56.770 0.20 1.000 1 . . . . A 49 GLU CA . 30389 1 565 . 1 1 49 49 GLU CB C 13 30.510 0.20 1.000 1 . . . . A 49 GLU CB . 30389 1 566 . 1 1 49 49 GLU CG C 13 36.270 0.20 1.000 1 . . . . A 49 GLU CG . 30389 1 567 . 1 1 49 49 GLU N N 15 121.457 0.20 1.000 1 . . . . A 49 GLU N . 30389 1 568 . 1 1 50 50 HIS H H 1 8.480 0.02 1.000 1 . . . . A 50 HIS H . 30389 1 569 . 1 1 50 50 HIS HA H 1 4.679 0.02 1.000 1 . . . . A 50 HIS HA . 30389 1 570 . 1 1 50 50 HIS HB2 H 1 3.195 0.02 1.000 2 . . . . A 50 HIS HB2 . 30389 1 571 . 1 1 50 50 HIS HB3 H 1 3.136 0.02 1.000 2 . . . . A 50 HIS HB3 . 30389 1 572 . 1 1 50 50 HIS C C 13 174.654 0.20 1.000 1 . . . . A 50 HIS C . 30389 1 573 . 1 1 50 50 HIS CA C 13 55.370 0.20 1.000 1 . . . . A 50 HIS CA . 30389 1 574 . 1 1 50 50 HIS CB C 13 29.510 0.20 1.000 1 . . . . A 50 HIS CB . 30389 1 575 . 1 1 50 50 HIS N N 15 119.512 0.20 1.000 1 . . . . A 50 HIS N . 30389 1 576 . 1 1 51 51 LEU H H 1 8.303 0.02 1.000 1 . . . . A 51 LEU H . 30389 1 577 . 1 1 51 51 LEU HA H 1 4.357 0.02 1.000 1 . . . . A 51 LEU HA . 30389 1 578 . 1 1 51 51 LEU HB2 H 1 1.813 0.02 0.497 2 . . . . A 51 LEU HB2 . 30389 1 579 . 1 1 51 51 LEU HB3 H 1 1.813 0.02 0.481 2 . . . . A 51 LEU HB3 . 30389 1 580 . 1 1 51 51 LEU HG H 1 1.588 0.02 0.451 1 . . . . A 51 LEU HG . 30389 1 581 . 1 1 51 51 LEU HD11 H 1 0.871 0.02 0.482 2 . . . . A 51 LEU HD11 . 30389 1 582 . 1 1 51 51 LEU HD12 H 1 0.871 0.02 0.482 2 . . . . A 51 LEU HD12 . 30389 1 583 . 1 1 51 51 LEU HD13 H 1 0.871 0.02 0.482 2 . . . . A 51 LEU HD13 . 30389 1 584 . 1 1 51 51 LEU HD21 H 1 0.871 0.02 0.715 2 . . . . A 51 LEU HD21 . 30389 1 585 . 1 1 51 51 LEU HD22 H 1 0.871 0.02 0.715 2 . . . . A 51 LEU HD22 . 30389 1 586 . 1 1 51 51 LEU HD23 H 1 0.871 0.02 0.715 2 . . . . A 51 LEU HD23 . 30389 1 587 . 1 1 51 51 LEU C C 13 177.093 0.20 1.000 1 . . . . A 51 LEU C . 30389 1 588 . 1 1 51 51 LEU CA C 13 55.120 0.20 1.000 1 . . . . A 51 LEU CA . 30389 1 589 . 1 1 51 51 LEU CB C 13 42.300 0.20 1.000 1 . . . . A 51 LEU CB . 30389 1 590 . 1 1 51 51 LEU CG C 13 26.980 0.20 1.000 1 . . . . A 51 LEU CG . 30389 1 591 . 1 1 51 51 LEU CD1 C 13 24.830 0.20 1.000 2 . . . . A 51 LEU CD1 . 30389 1 592 . 1 1 51 51 LEU CD2 C 13 23.420 0.20 1.000 2 . . . . A 51 LEU CD2 . 30389 1 593 . 1 1 51 51 LEU N N 15 123.849 0.20 1.000 1 . . . . A 51 LEU N . 30389 1 594 . 1 1 52 52 ASP H H 1 8.420 0.02 1.000 1 . . . . A 52 ASP H . 30389 1 595 . 1 1 52 52 ASP HA H 1 4.560 0.02 1.000 1 . . . . A 52 ASP HA . 30389 1 596 . 1 1 52 52 ASP HB2 H 1 2.681 0.02 0.898 2 . . . . A 52 ASP HB2 . 30389 1 597 . 1 1 52 52 ASP HB3 H 1 2.681 0.02 0.387 2 . . . . A 52 ASP HB3 . 30389 1 598 . 1 1 52 52 ASP C C 13 176.895 0.20 1.000 1 . . . . A 52 ASP C . 30389 1 599 . 1 1 52 52 ASP CA C 13 55.020 0.20 0.625 1 . . . . A 52 ASP CA . 30389 1 600 . 1 1 52 52 ASP CB C 13 41.260 0.20 1.000 1 . . . . A 52 ASP CB . 30389 1 601 . 1 1 52 52 ASP N N 15 121.139 0.20 1.000 1 . . . . A 52 ASP N . 30389 1 602 . 1 1 53 53 GLY H H 1 8.351 0.02 1.000 1 . . . . A 53 GLY H . 30389 1 603 . 1 1 53 53 GLY HA2 H 1 3.925 0.02 0.837 2 . . . . A 53 GLY HA2 . 30389 1 604 . 1 1 53 53 GLY HA3 H 1 3.925 0.02 0.853 2 . . . . A 53 GLY HA3 . 30389 1 605 . 1 1 53 53 GLY C C 13 174.095 0.20 1.000 1 . . . . A 53 GLY C . 30389 1 606 . 1 1 53 53 GLY CA C 13 45.640 0.20 1.000 1 . . . . A 53 GLY CA . 30389 1 607 . 1 1 53 53 GLY N N 15 109.633 0.20 1.000 1 . . . . A 53 GLY N . 30389 1 608 . 1 1 54 54 ALA H H 1 8.071 0.02 1.000 1 . . . . A 54 ALA H . 30389 1 609 . 1 1 54 54 ALA HA H 1 4.283 0.02 0.718 1 . . . . A 54 ALA HA . 30389 1 610 . 1 1 54 54 ALA HB1 H 1 1.374 0.02 1.000 1 . . . . A 54 ALA HB1 . 30389 1 611 . 1 1 54 54 ALA HB2 H 1 1.374 0.02 1.000 1 . . . . A 54 ALA HB2 . 30389 1 612 . 1 1 54 54 ALA HB3 H 1 1.374 0.02 1.000 1 . . . . A 54 ALA HB3 . 30389 1 613 . 1 1 54 54 ALA C C 13 177.632 0.20 1.000 1 . . . . A 54 ALA C . 30389 1 614 . 1 1 54 54 ALA CA C 13 52.550 0.20 1.000 1 . . . . A 54 ALA CA . 30389 1 615 . 1 1 54 54 ALA CB C 13 19.350 0.20 1.000 1 . . . . A 54 ALA CB . 30389 1 616 . 1 1 54 54 ALA N N 15 123.267 0.20 1.000 1 . . . . A 54 ALA N . 30389 1 617 . 1 1 55 55 LEU H H 1 8.083 0.02 1.000 1 . . . . A 55 LEU H . 30389 1 618 . 1 1 55 55 LEU HA H 1 4.277 0.02 1.000 1 . . . . A 55 LEU HA . 30389 1 619 . 1 1 55 55 LEU HB2 H 1 1.611 0.02 0.426 2 . . . . A 55 LEU HB2 . 30389 1 620 . 1 1 55 55 LEU HB3 H 1 1.611 0.02 0.549 2 . . . . A 55 LEU HB3 . 30389 1 621 . 1 1 55 55 LEU HG H 1 1.469 0.02 0.441 1 . . . . A 55 LEU HG . 30389 1 622 . 1 1 55 55 LEU HD11 H 1 0.888 0.02 0.468 2 . . . . A 55 LEU HD11 . 30389 1 623 . 1 1 55 55 LEU HD12 H 1 0.888 0.02 0.468 2 . . . . A 55 LEU HD12 . 30389 1 624 . 1 1 55 55 LEU HD13 H 1 0.888 0.02 0.468 2 . . . . A 55 LEU HD13 . 30389 1 625 . 1 1 55 55 LEU HD21 H 1 0.888 0.02 0.659 2 . . . . A 55 LEU HD21 . 30389 1 626 . 1 1 55 55 LEU HD22 H 1 0.888 0.02 0.659 2 . . . . A 55 LEU HD22 . 30389 1 627 . 1 1 55 55 LEU HD23 H 1 0.888 0.02 0.659 2 . . . . A 55 LEU HD23 . 30389 1 628 . 1 1 55 55 LEU C C 13 176.857 0.20 1.000 1 . . . . A 55 LEU C . 30389 1 629 . 1 1 55 55 LEU CA C 13 55.080 0.20 1.000 1 . . . . A 55 LEU CA . 30389 1 630 . 1 1 55 55 LEU CB C 13 42.160 0.20 1.000 1 . . . . A 55 LEU CB . 30389 1 631 . 1 1 55 55 LEU CG C 13 27.000 0.20 1.000 1 . . . . A 55 LEU CG . 30389 1 632 . 1 1 55 55 LEU CD1 C 13 23.630 0.20 0.689 2 . . . . A 55 LEU CD1 . 30389 1 633 . 1 1 55 55 LEU CD2 C 13 24.820 0.20 0.683 2 . . . . A 55 LEU CD2 . 30389 1 634 . 1 1 55 55 LEU N N 15 120.725 0.20 1.000 1 . . . . A 55 LEU N . 30389 1 635 . 1 1 56 56 ARG H H 1 8.083 0.02 1.000 1 . . . . A 56 ARG H . 30389 1 636 . 1 1 56 56 ARG HA H 1 4.312 0.02 1.000 1 . . . . A 56 ARG HA . 30389 1 637 . 1 1 56 56 ARG HB2 H 1 1.786 0.02 0.325 2 . . . . A 56 ARG HB2 . 30389 1 638 . 1 1 56 56 ARG HB3 H 1 1.786 0.02 0.543 2 . . . . A 56 ARG HB3 . 30389 1 639 . 1 1 56 56 ARG HG2 H 1 1.642 0.02 0.412 2 . . . . A 56 ARG HG2 . 30389 1 640 . 1 1 56 56 ARG HG3 H 1 1.527 0.02 0.382 2 . . . . A 56 ARG HG3 . 30389 1 641 . 1 1 56 56 ARG HD2 H 1 3.145 0.02 0.540 2 . . . . A 56 ARG HD2 . 30389 1 642 . 1 1 56 56 ARG HD3 H 1 3.145 0.02 0.750 2 . . . . A 56 ARG HD3 . 30389 1 643 . 1 1 56 56 ARG C C 13 174.729 0.20 1.000 1 . . . . A 56 ARG C . 30389 1 644 . 1 1 56 56 ARG CA C 13 55.580 0.20 1.000 1 . . . . A 56 ARG CA . 30389 1 645 . 1 1 56 56 ARG CB C 13 31.070 0.20 1.000 1 . . . . A 56 ARG CB . 30389 1 646 . 1 1 56 56 ARG CG C 13 27.020 0.20 1.000 1 . . . . A 56 ARG CG . 30389 1 647 . 1 1 56 56 ARG CD C 13 43.260 0.20 1.000 1 . . . . A 56 ARG CD . 30389 1 648 . 1 1 56 56 ARG N N 15 121.877 0.20 1.000 1 . . . . A 56 ARG N . 30389 1 649 . 1 1 57 57 TYR H H 1 7.698 0.02 1.000 1 . . . . A 57 TYR H . 30389 1 650 . 1 1 57 57 TYR C C 13 180.400 0.20 1.000 1 . . . . A 57 TYR C . 30389 1 651 . 1 1 57 57 TYR CA C 13 59.050 0.02 1.000 1 . . . . A 57 TYR CA . 30389 1 652 . 1 1 57 57 TYR CB C 13 39.560 0.20 1.000 1 . . . . A 57 TYR CB . 30389 1 653 . 1 1 57 57 TYR N N 15 126.059 0.20 1.000 1 . . . . A 57 TYR N . 30389 1 stop_ save_ ######################### # Spectral peak lists # ######################### save_spectral_peak_list_1 _Spectral_peak_list.Sf_category spectral_peak_list _Spectral_peak_list.Sf_framecode spectral_peak_list_1 _Spectral_peak_list.Entry_ID 30389 _Spectral_peak_list.ID 1 _Spectral_peak_list.Sample_ID 1 _Spectral_peak_list.Sample_label $sample_1 _Spectral_peak_list.Sample_condition_list_ID 1 _Spectral_peak_list.Sample_condition_list_label $sample_conditions_1 _Spectral_peak_list.Experiment_ID 1 _Spectral_peak_list.Experiment_name '2D 1H-15N HSQC' _Spectral_peak_list.Experiment_class . _Spectral_peak_list.Experiment_type . _Spectral_peak_list.Number_of_spectral_dimensions 2 _Spectral_peak_list.Chemical_shift_list . _Spectral_peak_list.Assigned_chem_shift_list_ID 1 _Spectral_peak_list.Assigned_chem_shift_list_label $assigned_chemical_shifts_1 _Spectral_peak_list.Details . _Spectral_peak_list.Text_data_format text _Spectral_peak_list.Text_data ; Assignment w1 w2 Data Height Ala3N-HN 126.172 8.554 21564268 Gly4N-HN 108.146 8.397 41994312 Leu5N-HN 121.675 8.113 80711592 Gln6N-HN 120.764 8.497 70053168 Glu7N-HN 121.999 8.475 76176688 Lys8N-HN 121.349 8.304 75106288 Glu9N-HN 121.072 8.392 53551288 Arg10N-HN 120.952 8.204 77580696 Glu11N-HN 121.034 8.322 59494436 Leu12N-HN 121.244 8.128 63015808 Glu13N-HN 121.031 8.249 68071520 Asp14N-HN 120.919 8.365 61712472 Leu15N-HN 122.546 8.085 62204120 Lys16N-HN 120.882 8.167 101038376 Asp17N-HN 120.271 8.236 58242896 Ala18N-HN 122.807 8.162 58797848 Glu19N-HN 119.239 8.149 75165072 Leu20N-HN 120.695 7.975 105212608 Lys21N-HN 119.562 8.015 53045388 Arg22N-HN 120.110 7.887 56047048 Leu23N-HN 120.689 8.197 66282568 Asn24N-HN 117.970 8.249 48785976 Glu25N-HN 121.008 8.173 43693944 Glu26N-HN 120.828 8.292 53233780 Arg27N-HN 120.674 8.131 48589412 His28N-HN 118.902 8.307 13742920 Asp29N-HN 120.486 8.385 20393160 His30N-HN 119.181 8.368 13966728 Asp31N-HN 120.440 8.458 36045592 Lys32N-HN 122.388 8.207 48843604 Arg33N-HN 120.121 8.178 46855576 Glu34N-HN 120.696 8.285 65593828 Ala35N-HN 122.830 8.099 59653768 Arg37N-HN 121.086 8.056 56775972 Lys38N-HN 120.813 8.201 74017848 Ala39N-HN 121.968 7.971 55256732 Leu40N-HN 119.475 7.831 54737608 Glu41N-HN 120.044 8.141 59642472 Asp42N-HN 120.591 8.319 85736128 Lys43N-HN 120.750 7.978 83365776 Leu44N-HN 121.225 8.081 49502232 Ala45N-HN 123.162 7.976 77073264 Asp46N-HN 118.985 8.113 69576368 Lys47N-HN 121.026 8.157 79722528 Gln48N-HN 120.539 8.315 101696408 Glu49N-HN 121.457 8.394 61354988 His50N-HN 119.512 8.480 32020424 Leu51N-HN 123.849 8.303 50313956 Asp52N-HN 121.139 8.420 74158096 Gly53N-HN 109.633 8.351 57840744 Ala54N-HN 123.267 8.071 88508312 Leu55N-HN 120.725 8.083 81989960 Arg56N-HN 121.877 8.083 70918072 Tyr57N-HN 126.059 7.698 82243352 ; loop_ _Spectral_dim.ID _Spectral_dim.Axis_code _Spectral_dim.Spectrometer_frequency _Spectral_dim.Atom_type _Spectral_dim.Atom_isotope_number _Spectral_dim.Spectral_region _Spectral_dim.Magnetization_linkage_ID _Spectral_dim.Under_sampling_type _Spectral_dim.Sweep_width _Spectral_dim.Sweep_width_units _Spectral_dim.Value_first_point _Spectral_dim.Absolute_peak_positions _Spectral_dim.Acquisition _Spectral_dim.Center_frequency_offset _Spectral_dim.Encoding_code _Spectral_dim.Encoded_reduced_dimension_ID _Spectral_dim.Entry_ID _Spectral_dim.Spectral_peak_list_ID 1 . . H 1 HN 2 . 11 ppm . . . 4.688 . . 30389 1 2 . . N 15 N 1 . 22 ppm . . . 117.8 . . 30389 1 stop_ save_