data_50428 ####################### # Entry information # ####################### save_entry_information_1 _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information_1 _Entry.ID 50428 _Entry.Title ; 1H, 13C, 15N solid-state MAS NMR assignments of influenza virus hemagglutinin stalk long alpha helix (LAH) antigen ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2020-08-06 _Entry.Accession_date 2020-08-06 _Entry.Last_release_date 2020-08-06 _Entry.Original_release_date 2020-08-06 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.14.0 _Entry.NMR_STAR_dict_location . _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solid-state _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_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 Kristaps Jaudzems . . . 0000-0003-3922-2447 50428 2 Anna Kirsteina . . . . 50428 3 Tobias Schubeis . . . . 50428 4 Andris Kazaks . . . . 50428 5 Kaspars Tars . . . . 50428 6 Anne Lesage . . . . 50428 7 Guido Pintacuda . . . . 50428 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 50428 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 232 50428 '15N chemical shifts' 48 50428 '1H chemical shifts' 164 50428 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 . . 2021-07-27 . original BMRB . 50428 stop_ save_ ############### # Citations # ############### save_citations_1 _Citation.Sf_category citations _Citation.Sf_framecode citations_1 _Citation.Entry_ID 50428 _Citation.ID 1 _Citation.Name . _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.PubMed_ID 33750007 _Citation.DOI . _Citation.Full_citation . _Citation.Title ; Structural Analysis of an Antigen Chemically Coupled on Virus-Like Particles in Vaccine Formulation ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Angew. Chem. Int. Ed. Engl.' _Citation.Journal_name_full 'Angewandte Chemie (International ed. in English)' _Citation.Journal_volume 60 _Citation.Journal_issue 23 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1521-3773 _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 12847 _Citation.Page_last 12851 _Citation.Year 2021 _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 Kristaps Jaudzems . . . . 50428 1 2 Anna Kirsteina . . . . 50428 1 3 Tobias Schubeis . . . . 50428 1 4 Gilles Casano . . . . 50428 1 5 Olivier Ouari . . . . 50428 1 6 Janis Bogans . . . . 50428 1 7 Andris Kazaks . . . . 50428 1 8 Kaspars Tars . . . . 50428 1 9 Anne Lesage . . . . 50428 1 10 Guido Pintacuda . . . . 50428 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly_1 _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly_1 _Assembly.Entry_ID 50428 _Assembly.ID 1 _Assembly.Name homotrimer _Assembly.BMRB_code . _Assembly.Number_of_components 3 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange no _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 'stalk protein, chain 1' 1 $entity_1 . . yes native no no . . . 50428 1 2 'stalk protein, chain 2' 1 $entity_1 . . no native no no . . . 50428 1 3 'stalk protein, chain 3' 1 $entity_1 . . no native no no . . . 50428 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 50428 _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 . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MEKRIENLNKKVDDGFLDIW TYNAELLVLLENERTLDYHD SNVKNLYEKVRSQLKNNA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 58 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . 50428 1 2 . GLU . 50428 1 3 . LYS . 50428 1 4 . ARG . 50428 1 5 . ILE . 50428 1 6 . GLU . 50428 1 7 . ASN . 50428 1 8 . LEU . 50428 1 9 . ASN . 50428 1 10 . LYS . 50428 1 11 . LYS . 50428 1 12 . VAL . 50428 1 13 . ASP . 50428 1 14 . ASP . 50428 1 15 . GLY . 50428 1 16 . PHE . 50428 1 17 . LEU . 50428 1 18 . ASP . 50428 1 19 . ILE . 50428 1 20 . TRP . 50428 1 21 . THR . 50428 1 22 . TYR . 50428 1 23 . ASN . 50428 1 24 . ALA . 50428 1 25 . GLU . 50428 1 26 . LEU . 50428 1 27 . LEU . 50428 1 28 . VAL . 50428 1 29 . LEU . 50428 1 30 . LEU . 50428 1 31 . GLU . 50428 1 32 . ASN . 50428 1 33 . GLU . 50428 1 34 . ARG . 50428 1 35 . THR . 50428 1 36 . LEU . 50428 1 37 . ASP . 50428 1 38 . TYR . 50428 1 39 . HIS . 50428 1 40 . ASP . 50428 1 41 . SER . 50428 1 42 . ASN . 50428 1 43 . VAL . 50428 1 44 . LYS . 50428 1 45 . ASN . 50428 1 46 . LEU . 50428 1 47 . TYR . 50428 1 48 . GLU . 50428 1 49 . LYS . 50428 1 50 . VAL . 50428 1 51 . ARG . 50428 1 52 . SER . 50428 1 53 . GLN . 50428 1 54 . LEU . 50428 1 55 . LYS . 50428 1 56 . ASN . 50428 1 57 . ASN . 50428 1 58 . ALA . 50428 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 50428 1 . GLU 2 2 50428 1 . LYS 3 3 50428 1 . ARG 4 4 50428 1 . ILE 5 5 50428 1 . GLU 6 6 50428 1 . ASN 7 7 50428 1 . LEU 8 8 50428 1 . ASN 9 9 50428 1 . LYS 10 10 50428 1 . LYS 11 11 50428 1 . VAL 12 12 50428 1 . ASP 13 13 50428 1 . ASP 14 14 50428 1 . GLY 15 15 50428 1 . PHE 16 16 50428 1 . LEU 17 17 50428 1 . ASP 18 18 50428 1 . ILE 19 19 50428 1 . TRP 20 20 50428 1 . THR 21 21 50428 1 . TYR 22 22 50428 1 . ASN 23 23 50428 1 . ALA 24 24 50428 1 . GLU 25 25 50428 1 . LEU 26 26 50428 1 . LEU 27 27 50428 1 . VAL 28 28 50428 1 . LEU 29 29 50428 1 . LEU 30 30 50428 1 . GLU 31 31 50428 1 . ASN 32 32 50428 1 . GLU 33 33 50428 1 . ARG 34 34 50428 1 . THR 35 35 50428 1 . LEU 36 36 50428 1 . ASP 37 37 50428 1 . TYR 38 38 50428 1 . HIS 39 39 50428 1 . ASP 40 40 50428 1 . SER 41 41 50428 1 . ASN 42 42 50428 1 . VAL 43 43 50428 1 . LYS 44 44 50428 1 . ASN 45 45 50428 1 . LEU 46 46 50428 1 . TYR 47 47 50428 1 . GLU 48 48 50428 1 . LYS 49 49 50428 1 . VAL 50 50 50428 1 . ARG 51 51 50428 1 . SER 52 52 50428 1 . GLN 53 53 50428 1 . LEU 54 54 50428 1 . LYS 55 55 50428 1 . ASN 56 56 50428 1 . ASN 57 57 50428 1 . ALA 58 58 50428 1 stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source_1 _Entity_natural_src_list.Entry_ID 50428 _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 . 11309 virus . 'Influenza virus' 'Influenza virus' . . Viruses . Influenza 'Influenza virus' . . . . . . . . . . . . . 50428 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source_1 _Entity_experimental_src_list.Entry_ID 50428 _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' . . . Escherichia coli . . . plasmid . . pETDuet-1 . . . 50428 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 50428 _Sample.ID 1 _Sample.Name sample1 _Sample.Type microcrystalline _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number 1 _Sample.Solvent_system none _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 'stalk protein' '[U-100% 13C; U-100% 15N]' . . 1 $entity_1 . . 500 . . mg/mL 200 . . . 50428 1 2 'ammonium sulfate' 'natural abundance' . . . . . . saturated . . na . . . . 50428 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 50428 _Sample_condition_list.ID 1 _Sample_condition_list.Name sample_conditions1 _Sample_condition_list.Details '3.2 mm rotor' 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 8 . pH 50428 1 pressure 1 . atm 50428 1 temperature 283 5 K 50428 1 'temperature controller setting' 273 0.1 K 50428 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 50428 _Sample_condition_list.ID 2 _Sample_condition_list.Name sample_conditions2 _Sample_condition_list.Details '0.7 mm rotor' 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 8 . pH 50428 2 pressure 1 . atm 50428 2 temperature 283 5 K 50428 2 'temperature controller setting' 265 0.1 K 50428 2 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 50428 _Software.ID 1 _Software.Type . _Software.Name TOPSPIN _Software.Version 3.5.7 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID collection . 50428 1 processing . 50428 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 50428 _Software.ID 2 _Software.Type . _Software.Name CARA _Software.Version 1.9.1 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Software_module _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' . 50428 2 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 50428 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name '800 MHz' _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model 'AVANCE III HD' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 50428 _NMR_spectrometer.ID 2 _NMR_spectrometer.Name '1000 MHz' _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model 'AVANCE III' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 1000 save_ ############################# # NMR applied experiments # ############################# save_experiment_list_1 _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list_1 _Experiment_list.Entry_ID 50428 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NUS_flag _Experiment.Interleaved_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.Details _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '3D NCOCX' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 2 '3D NCACX' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 3 '3D CONCA' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 4 '3D CANCO' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 5 '2D DARR' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 6 '2D RFDR' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 7 '2D C(HH)C' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 8 '3D N(HH)C' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 9 '2D NCO' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 10 '2D NCA' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $NMR_spectrometer_1 . . . . . . . . . . . . . . . . . 50428 1 11 '3D (H)NCAH' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $NMR_spectrometer_2 . . . . . . . . . . . . . . . . . 50428 1 12 '3D (H)CBCAH' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $NMR_spectrometer_2 . . . . . . . . . . . . . . . . . 50428 1 13 '3D (H)COCAH' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $NMR_spectrometer_2 . . . . . . . . . . . . . . . . . 50428 1 14 '3D (H)CCH-TOCSY' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $NMR_spectrometer_2 . . . . . . . . . . . . . . . . . 50428 1 15 '2D 1H-13C CP-HSQC' no . . . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $NMR_spectrometer_2 . . . . . . . . . . . . . . . . . 50428 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 50428 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name water _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 water protons . . . . ppm 5 internal indirect 0.25144953 . . . . . 50428 1 H 1 water protons . . . . ppm 5 internal direct 1 . . . . . 50428 1 N 15 water protons . . . . ppm 5 internal indirect 0.101329118 . . . . . 50428 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 50428 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name chemical_shifts _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_2 _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 0.1 _Assigned_chem_shift_list.Chem_shift_13C_err 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D NCOCX' . . . 50428 1 2 '3D NCACX' . . . 50428 1 3 '3D CONCA' . . . 50428 1 4 '3D CANCO' . . . 50428 1 5 '2D DARR' . . . 50428 1 6 '2D RFDR' . . . 50428 1 9 '2D NCO' . . . 50428 1 10 '2D NCA' . . . 50428 1 11 '3D (H)NCAH' . . . 50428 1 12 '3D (H)CBCAH' . . . 50428 1 13 '3D (H)COCAH' . . . 50428 1 14 '3D (H)CCH-TOCSY' . . . 50428 1 15 '2D 1H-13C CP-HSQC' . . . 50428 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 2 $software_2 . . 50428 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_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 5 5 ILE HA H 1 3.194 0.100 . 1 . . . . . 5 ILE HA . 50428 1 2 . 1 . 1 5 5 ILE HB H 1 1.504 0.100 . 1 . . . . . 5 ILE HB . 50428 1 3 . 1 . 1 5 5 ILE HG12 H 1 1.072 0.100 . 1 . . . . . 5 ILE HG12 . 50428 1 4 . 1 . 1 5 5 ILE HG13 H 1 1.072 0.100 . 1 . . . . . 5 ILE HG13 . 50428 1 5 . 1 . 1 5 5 ILE HG21 H 1 0.372 0.100 . 1 . . . . . 5 ILE HG2 . 50428 1 6 . 1 . 1 5 5 ILE HG22 H 1 0.372 0.100 . 1 . . . . . 5 ILE HG2 . 50428 1 7 . 1 . 1 5 5 ILE HG23 H 1 0.372 0.100 . 1 . . . . . 5 ILE HG2 . 50428 1 8 . 1 . 1 5 5 ILE HD11 H 1 0.309 0.100 . 1 . . . . . 5 ILE HD1 . 50428 1 9 . 1 . 1 5 5 ILE HD12 H 1 0.309 0.100 . 1 . . . . . 5 ILE HD1 . 50428 1 10 . 1 . 1 5 5 ILE HD13 H 1 0.309 0.100 . 1 . . . . . 5 ILE HD1 . 50428 1 11 . 1 . 1 5 5 ILE C C 13 177.537 0.3 . 1 . . . . . 5 ILE C . 50428 1 12 . 1 . 1 5 5 ILE CA C 13 63.566 0.3 . 1 . . . . . 5 ILE CA . 50428 1 13 . 1 . 1 5 5 ILE CB C 13 36.786 0.3 . 1 . . . . . 5 ILE CB . 50428 1 14 . 1 . 1 5 5 ILE CG1 C 13 28.910 0.3 . 1 . . . . . 5 ILE CG1 . 50428 1 15 . 1 . 1 5 5 ILE CG2 C 13 17.278 0.3 . 1 . . . . . 5 ILE CG2 . 50428 1 16 . 1 . 1 5 5 ILE CD1 C 13 12.757 0.3 . 1 . . . . . 5 ILE CD1 . 50428 1 17 . 1 . 1 5 5 ILE N N 15 120.095 0.3 . 1 . . . . . 5 ILE N . 50428 1 18 . 1 . 1 6 6 GLU HA H 1 3.521 0.100 . 1 . . . . . 6 GLU HA . 50428 1 19 . 1 . 1 6 6 GLU HB2 H 1 1.589 0.100 . 1 . . . . . 6 GLU HB2 . 50428 1 20 . 1 . 1 6 6 GLU HB3 H 1 1.589 0.100 . 1 . . . . . 6 GLU HB3 . 50428 1 21 . 1 . 1 6 6 GLU HG2 H 1 1.835 0.100 . 1 . . . . . 6 GLU HG2 . 50428 1 22 . 1 . 1 6 6 GLU HG3 H 1 1.835 0.100 . 1 . . . . . 6 GLU HG3 . 50428 1 23 . 1 . 1 6 6 GLU C C 13 179.233 0.3 . 1 . . . . . 6 GLU C . 50428 1 24 . 1 . 1 6 6 GLU CA C 13 59.143 0.3 . 1 . . . . . 6 GLU CA . 50428 1 25 . 1 . 1 6 6 GLU CB C 13 28.763 0.3 . 1 . . . . . 6 GLU CB . 50428 1 26 . 1 . 1 6 6 GLU CG C 13 35.860 0.3 . 1 . . . . . 6 GLU CG . 50428 1 27 . 1 . 1 6 6 GLU CD C 13 182.664 0.3 . 1 . . . . . 6 GLU CD . 50428 1 28 . 1 . 1 6 6 GLU N N 15 122.295 0.3 . 1 . . . . . 6 GLU N . 50428 1 29 . 1 . 1 7 7 ASN HA H 1 3.996 0.100 . 1 . . . . . 7 ASN HA . 50428 1 30 . 1 . 1 7 7 ASN HB2 H 1 2.325 0.100 . 1 . . . . . 7 ASN HB2 . 50428 1 31 . 1 . 1 7 7 ASN HB3 H 1 2.325 0.100 . 1 . . . . . 7 ASN HB3 . 50428 1 32 . 1 . 1 7 7 ASN C C 13 177.545 0.3 . 1 . . . . . 7 ASN C . 50428 1 33 . 1 . 1 7 7 ASN CA C 13 55.264 0.3 . 1 . . . . . 7 ASN CA . 50428 1 34 . 1 . 1 7 7 ASN CB C 13 37.255 0.3 . 1 . . . . . 7 ASN CB . 50428 1 35 . 1 . 1 7 7 ASN CG C 13 175.140 0.3 . 1 . . . . . 7 ASN CG . 50428 1 36 . 1 . 1 7 7 ASN N N 15 117.407 0.3 . 1 . . . . . 7 ASN N . 50428 1 37 . 1 . 1 8 8 LEU H H 1 8.223 0.100 . 1 . . . . . 8 LEU H . 50428 1 38 . 1 . 1 8 8 LEU HA H 1 3.758 0.100 . 1 . . . . . 8 LEU HA . 50428 1 39 . 1 . 1 8 8 LEU HB2 H 1 1.178 0.100 . 1 . . . . . 8 LEU HB2 . 50428 1 40 . 1 . 1 8 8 LEU HB3 H 1 1.178 0.100 . 1 . . . . . 8 LEU HB3 . 50428 1 41 . 1 . 1 8 8 LEU HG H 1 1.098 0.100 . 1 . . . . . 8 LEU HG . 50428 1 42 . 1 . 1 8 8 LEU HD11 H 1 0.487 0.100 . 1 . . . . . 8 LEU HD1 . 50428 1 43 . 1 . 1 8 8 LEU HD12 H 1 0.487 0.100 . 1 . . . . . 8 LEU HD1 . 50428 1 44 . 1 . 1 8 8 LEU HD13 H 1 0.487 0.100 . 1 . . . . . 8 LEU HD1 . 50428 1 45 . 1 . 1 8 8 LEU HD21 H 1 0.305 0.100 . 1 . . . . . 8 LEU HD2 . 50428 1 46 . 1 . 1 8 8 LEU HD22 H 1 0.305 0.100 . 1 . . . . . 8 LEU HD2 . 50428 1 47 . 1 . 1 8 8 LEU HD23 H 1 0.305 0.100 . 1 . . . . . 8 LEU HD2 . 50428 1 48 . 1 . 1 8 8 LEU C C 13 177.449 0.3 . 1 . . . . . 8 LEU C . 50428 1 49 . 1 . 1 8 8 LEU CA C 13 57.190 0.3 . 1 . . . . . 8 LEU CA . 50428 1 50 . 1 . 1 8 8 LEU CB C 13 40.737 0.3 . 1 . . . . . 8 LEU CB . 50428 1 51 . 1 . 1 8 8 LEU CG C 13 27.006 0.3 . 1 . . . . . 8 LEU CG . 50428 1 52 . 1 . 1 8 8 LEU CD1 C 13 23.374 0.3 . 1 . . . . . 8 LEU CD1 . 50428 1 53 . 1 . 1 8 8 LEU CD2 C 13 25.679 0.3 . 1 . . . . . 8 LEU CD2 . 50428 1 54 . 1 . 1 8 8 LEU N N 15 123.342 0.3 . 1 . . . . . 8 LEU N . 50428 1 55 . 1 . 1 9 9 ASN HA H 1 3.605 0.100 . 1 . . . . . 9 ASN HA . 50428 1 56 . 1 . 1 9 9 ASN HB2 H 1 2.253 0.100 . 1 . . . . . 9 ASN HB2 . 50428 1 57 . 1 . 1 9 9 ASN HB3 H 1 2.253 0.100 . 1 . . . . . 9 ASN HB3 . 50428 1 58 . 1 . 1 9 9 ASN C C 13 175.911 0.3 . 1 . . . . . 9 ASN C . 50428 1 59 . 1 . 1 9 9 ASN CA C 13 57.095 0.3 . 1 . . . . . 9 ASN CA . 50428 1 60 . 1 . 1 9 9 ASN CB C 13 39.351 0.3 . 1 . . . . . 9 ASN CB . 50428 1 61 . 1 . 1 9 9 ASN N N 15 117.511 0.3 . 1 . . . . . 9 ASN N . 50428 1 62 . 1 . 1 10 10 LYS HA H 1 3.583 0.100 . 1 . . . . . 10 LYS HA . 50428 1 63 . 1 . 1 10 10 LYS HB2 H 1 1.431 0.100 . 1 . . . . . 10 LYS HB2 . 50428 1 64 . 1 . 1 10 10 LYS HB3 H 1 1.431 0.100 . 1 . . . . . 10 LYS HB3 . 50428 1 65 . 1 . 1 10 10 LYS C C 13 177.109 0.3 . 1 . . . . . 10 LYS C . 50428 1 66 . 1 . 1 10 10 LYS CA C 13 59.063 0.3 . 1 . . . . . 10 LYS CA . 50428 1 67 . 1 . 1 10 10 LYS CB C 13 31.963 0.3 . 1 . . . . . 10 LYS CB . 50428 1 68 . 1 . 1 10 10 LYS CG C 13 24.696 0.3 . 1 . . . . . 10 LYS CG . 50428 1 69 . 1 . 1 10 10 LYS CD C 13 28.886 0.3 . 1 . . . . . 10 LYS CD . 50428 1 70 . 1 . 1 10 10 LYS CE C 13 41.656 0.3 . 1 . . . . . 10 LYS CE . 50428 1 71 . 1 . 1 10 10 LYS N N 15 117.302 0.3 . 1 . . . . . 10 LYS N . 50428 1 72 . 1 . 1 11 11 LYS HA H 1 3.612 0.100 . 1 . . . . . 11 LYS HA . 50428 1 73 . 1 . 1 11 11 LYS HB2 H 1 1.443 0.100 . 1 . . . . . 11 LYS HB2 . 50428 1 74 . 1 . 1 11 11 LYS HB3 H 1 1.443 0.100 . 1 . . . . . 11 LYS HB3 . 50428 1 75 . 1 . 1 11 11 LYS C C 13 179.742 0.3 . 1 . . . . . 11 LYS C . 50428 1 76 . 1 . 1 11 11 LYS CA C 13 59.073 0.3 . 1 . . . . . 11 LYS CA . 50428 1 77 . 1 . 1 11 11 LYS CB C 13 31.811 0.3 . 1 . . . . . 11 LYS CB . 50428 1 78 . 1 . 1 11 11 LYS CG C 13 24.811 0.3 . 1 . . . . . 11 LYS CG . 50428 1 79 . 1 . 1 11 11 LYS CD C 13 29.930 0.3 . 1 . . . . . 11 LYS CD . 50428 1 80 . 1 . 1 11 11 LYS CE C 13 41.592 0.3 . 1 . . . . . 11 LYS CE . 50428 1 81 . 1 . 1 11 11 LYS N N 15 119.327 0.3 . 1 . . . . . 11 LYS N . 50428 1 82 . 1 . 1 12 12 VAL H H 1 8.467 0.100 . 1 . . . . . 12 VAL H . 50428 1 83 . 1 . 1 12 12 VAL HA H 1 2.928 0.100 . 1 . . . . . 12 VAL HA . 50428 1 84 . 1 . 1 12 12 VAL HB H 1 1.616 0.100 . 1 . . . . . 12 VAL HB . 50428 1 85 . 1 . 1 12 12 VAL HG11 H 1 -0.083 0.100 . 1 . . . . . 12 VAL HG1 . 50428 1 86 . 1 . 1 12 12 VAL HG12 H 1 -0.083 0.100 . 1 . . . . . 12 VAL HG1 . 50428 1 87 . 1 . 1 12 12 VAL HG13 H 1 -0.083 0.100 . 1 . . . . . 12 VAL HG1 . 50428 1 88 . 1 . 1 12 12 VAL HG21 H 1 0.294 0.100 . 1 . . . . . 12 VAL HG2 . 50428 1 89 . 1 . 1 12 12 VAL HG22 H 1 0.294 0.100 . 1 . . . . . 12 VAL HG2 . 50428 1 90 . 1 . 1 12 12 VAL HG23 H 1 0.294 0.100 . 1 . . . . . 12 VAL HG2 . 50428 1 91 . 1 . 1 12 12 VAL C C 13 175.780 0.3 . 1 . . . . . 12 VAL C . 50428 1 92 . 1 . 1 12 12 VAL CA C 13 66.591 0.3 . 1 . . . . . 12 VAL CA . 50428 1 93 . 1 . 1 12 12 VAL CB C 13 31.123 0.3 . 1 . . . . . 12 VAL CB . 50428 1 94 . 1 . 1 12 12 VAL CG1 C 13 21.793 0.3 . 1 . . . . . 12 VAL CG1 . 50428 1 95 . 1 . 1 12 12 VAL CG2 C 13 24.355 0.3 . 1 . . . . . 12 VAL CG2 . 50428 1 96 . 1 . 1 12 12 VAL N N 15 120.130 0.3 . 1 . . . . . 12 VAL N . 50428 1 97 . 1 . 1 13 13 ASP HA H 1 3.943 0.100 . 1 . . . . . 13 ASP HA . 50428 1 98 . 1 . 1 13 13 ASP HB2 H 1 2.302 0.100 . 1 . . . . . 13 ASP HB2 . 50428 1 99 . 1 . 1 13 13 ASP HB3 H 1 2.302 0.100 . 1 . . . . . 13 ASP HB3 . 50428 1 100 . 1 . 1 13 13 ASP C C 13 178.980 0.3 . 1 . . . . . 13 ASP C . 50428 1 101 . 1 . 1 13 13 ASP CA C 13 57.591 0.3 . 1 . . . . . 13 ASP CA . 50428 1 102 . 1 . 1 13 13 ASP CB C 13 39.578 0.3 . 1 . . . . . 13 ASP CB . 50428 1 103 . 1 . 1 13 13 ASP N N 15 119.676 0.3 . 1 . . . . . 13 ASP N . 50428 1 104 . 1 . 1 14 14 ASP HA H 1 3.891 0.100 . 1 . . . . . 14 ASP HA . 50428 1 105 . 1 . 1 14 14 ASP HB2 H 1 2.239 0.100 . 1 . . . . . 14 ASP HB2 . 50428 1 106 . 1 . 1 14 14 ASP HB3 H 1 2.239 0.100 . 1 . . . . . 14 ASP HB3 . 50428 1 107 . 1 . 1 14 14 ASP C C 13 178.196 0.3 . 1 . . . . . 14 ASP C . 50428 1 108 . 1 . 1 14 14 ASP CA C 13 56.658 0.3 . 1 . . . . . 14 ASP CA . 50428 1 109 . 1 . 1 14 14 ASP CB C 13 39.535 0.3 . 1 . . . . . 14 ASP CB . 50428 1 110 . 1 . 1 14 14 ASP N N 15 120.060 0.3 . 1 . . . . . 14 ASP N . 50428 1 111 . 1 . 1 15 15 GLY H H 1 8.402 0.100 . 1 . . . . . 15 GLY H . 50428 1 112 . 1 . 1 15 15 GLY HA2 H 1 2.983 0.100 . 2 . . . . . 15 GLY HA2 . 50428 1 113 . 1 . 1 15 15 GLY HA3 H 1 3.312 0.100 . 2 . . . . . 15 GLY HA3 . 50428 1 114 . 1 . 1 15 15 GLY C C 13 177.158 0.3 . 1 . . . . . 15 GLY C . 50428 1 115 . 1 . 1 15 15 GLY CA C 13 46.829 0.3 . 1 . . . . . 15 GLY CA . 50428 1 116 . 1 . 1 15 15 GLY N N 15 108.469 0.3 . 1 . . . . . 15 GLY N . 50428 1 117 . 1 . 1 16 16 PHE HA H 1 4.294 0.100 . 1 . . . . . 16 PHE HA . 50428 1 118 . 1 . 1 16 16 PHE HB2 H 1 2.873 0.100 . 2 . . . . . 16 PHE HB2 . 50428 1 119 . 1 . 1 16 16 PHE HB3 H 1 3.130 0.100 . 2 . . . . . 16 PHE HB3 . 50428 1 120 . 1 . 1 16 16 PHE C C 13 177.977 0.3 . 1 . . . . . 16 PHE C . 50428 1 121 . 1 . 1 16 16 PHE CA C 13 57.765 0.3 . 1 . . . . . 16 PHE CA . 50428 1 122 . 1 . 1 16 16 PHE CB C 13 36.156 0.3 . 1 . . . . . 16 PHE CB . 50428 1 123 . 1 . 1 16 16 PHE CG C 13 140.147 0.3 . 1 . . . . . 16 PHE CG . 50428 1 124 . 1 . 1 16 16 PHE CD1 C 13 130.195 0.3 . 1 . . . . . 16 PHE CD1 . 50428 1 125 . 1 . 1 16 16 PHE CE1 C 13 128.454 0.3 . 1 . . . . . 16 PHE CE1 . 50428 1 126 . 1 . 1 16 16 PHE CZ C 13 128.745 0.3 . 1 . . . . . 16 PHE CZ . 50428 1 127 . 1 . 1 16 16 PHE N N 15 121.142 0.3 . 1 . . . . . 16 PHE N . 50428 1 128 . 1 . 1 17 17 LEU HA H 1 3.912 0.100 . 1 . . . . . 17 LEU HA . 50428 1 129 . 1 . 1 17 17 LEU HB2 H 1 1.297 0.100 . 2 . . . . . 17 LEU HB2 . 50428 1 130 . 1 . 1 17 17 LEU HB3 H 1 1.576 0.100 . 2 . . . . . 17 LEU HB3 . 50428 1 131 . 1 . 1 17 17 LEU HG H 1 1.218 0.100 . 1 . . . . . 17 LEU HG . 50428 1 132 . 1 . 1 17 17 LEU HD11 H 1 0.382 0.100 . 1 . . . . . 17 LEU HD1 . 50428 1 133 . 1 . 1 17 17 LEU HD12 H 1 0.382 0.100 . 1 . . . . . 17 LEU HD1 . 50428 1 134 . 1 . 1 17 17 LEU HD13 H 1 0.382 0.100 . 1 . . . . . 17 LEU HD1 . 50428 1 135 . 1 . 1 17 17 LEU HD21 H 1 0.289 0.100 . 1 . . . . . 17 LEU HD2 . 50428 1 136 . 1 . 1 17 17 LEU HD22 H 1 0.289 0.100 . 1 . . . . . 17 LEU HD2 . 50428 1 137 . 1 . 1 17 17 LEU HD23 H 1 0.289 0.100 . 1 . . . . . 17 LEU HD2 . 50428 1 138 . 1 . 1 17 17 LEU C C 13 180.251 0.3 . 1 . . . . . 17 LEU C . 50428 1 139 . 1 . 1 17 17 LEU CA C 13 58.231 0.3 . 1 . . . . . 17 LEU CA . 50428 1 140 . 1 . 1 17 17 LEU CB C 13 40.597 0.3 . 1 . . . . . 17 LEU CB . 50428 1 141 . 1 . 1 17 17 LEU CG C 13 26.844 0.3 . 1 . . . . . 17 LEU CG . 50428 1 142 . 1 . 1 17 17 LEU CD1 C 13 22.765 0.3 . 1 . . . . . 17 LEU CD1 . 50428 1 143 . 1 . 1 17 17 LEU CD2 C 13 25.252 0.3 . 1 . . . . . 17 LEU CD2 . 50428 1 144 . 1 . 1 17 17 LEU N N 15 120.828 0.3 . 1 . . . . . 17 LEU N . 50428 1 145 . 1 . 1 18 18 ASP H H 1 8.714 0.100 . 1 . . . . . 18 ASP H . 50428 1 146 . 1 . 1 18 18 ASP HA H 1 3.985 0.100 . 1 . . . . . 18 ASP HA . 50428 1 147 . 1 . 1 18 18 ASP HB2 H 1 2.200 0.100 . 1 . . . . . 18 ASP HB2 . 50428 1 148 . 1 . 1 18 18 ASP HB3 H 1 2.200 0.100 . 1 . . . . . 18 ASP HB3 . 50428 1 149 . 1 . 1 18 18 ASP C C 13 179.471 0.3 . 1 . . . . . 18 ASP C . 50428 1 150 . 1 . 1 18 18 ASP CA C 13 57.397 0.3 . 1 . . . . . 18 ASP CA . 50428 1 151 . 1 . 1 18 18 ASP CB C 13 40.162 0.3 . 1 . . . . . 18 ASP CB . 50428 1 152 . 1 . 1 18 18 ASP N N 15 121.631 0.3 . 1 . . . . . 18 ASP N . 50428 1 153 . 1 . 1 19 19 ILE H H 1 8.166 0.100 . 1 . . . . . 19 ILE H . 50428 1 154 . 1 . 1 19 19 ILE HA H 1 2.919 0.100 . 1 . . . . . 19 ILE HA . 50428 1 155 . 1 . 1 19 19 ILE HB H 1 1.118 0.100 . 1 . . . . . 19 ILE HB . 50428 1 156 . 1 . 1 19 19 ILE HG12 H 1 -0.572 0.100 . 2 . . . . . 19 ILE HG12 . 50428 1 157 . 1 . 1 19 19 ILE HG13 H 1 1.204 0.100 . 2 . . . . . 19 ILE HG13 . 50428 1 158 . 1 . 1 19 19 ILE HG21 H 1 -0.534 0.100 . 1 . . . . . 19 ILE HG2 . 50428 1 159 . 1 . 1 19 19 ILE HG22 H 1 -0.534 0.100 . 1 . . . . . 19 ILE HG2 . 50428 1 160 . 1 . 1 19 19 ILE HG23 H 1 -0.534 0.100 . 1 . . . . . 19 ILE HG2 . 50428 1 161 . 1 . 1 19 19 ILE HD11 H 1 0.077 0.100 . 1 . . . . . 19 ILE HD1 . 50428 1 162 . 1 . 1 19 19 ILE HD12 H 1 0.077 0.100 . 1 . . . . . 19 ILE HD1 . 50428 1 163 . 1 . 1 19 19 ILE HD13 H 1 0.077 0.100 . 1 . . . . . 19 ILE HD1 . 50428 1 164 . 1 . 1 19 19 ILE C C 13 177.294 0.3 . 1 . . . . . 19 ILE C . 50428 1 165 . 1 . 1 19 19 ILE CA C 13 64.675 0.3 . 1 . . . . . 19 ILE CA . 50428 1 166 . 1 . 1 19 19 ILE CB C 13 37.801 0.3 . 1 . . . . . 19 ILE CB . 50428 1 167 . 1 . 1 19 19 ILE CG1 C 13 30.686 0.3 . 1 . . . . . 19 ILE CG1 . 50428 1 168 . 1 . 1 19 19 ILE CG2 C 13 16.541 0.3 . 1 . . . . . 19 ILE CG2 . 50428 1 169 . 1 . 1 19 19 ILE CD1 C 13 15.266 0.3 . 1 . . . . . 19 ILE CD1 . 50428 1 170 . 1 . 1 19 19 ILE N N 15 121.914 0.3 . 1 . . . . . 19 ILE N . 50428 1 171 . 1 . 1 20 20 TRP H H 1 8.961 0.100 . 1 . . . . . 20 TRP H . 50428 1 172 . 1 . 1 20 20 TRP HA H 1 3.693 0.100 . 1 . . . . . 20 TRP HA . 50428 1 173 . 1 . 1 20 20 TRP HB2 H 1 2.466 0.100 . 2 . . . . . 20 TRP HB2 . 50428 1 174 . 1 . 1 20 20 TRP HB3 H 1 2.694 0.100 . 2 . . . . . 20 TRP HB3 . 50428 1 175 . 1 . 1 20 20 TRP C C 13 177.871 0.3 . 1 . . . . . 20 TRP C . 50428 1 176 . 1 . 1 20 20 TRP CA C 13 61.454 0.3 . 1 . . . . . 20 TRP CA . 50428 1 177 . 1 . 1 20 20 TRP CB C 13 28.023 0.3 . 1 . . . . . 20 TRP CB . 50428 1 178 . 1 . 1 20 20 TRP CG C 13 111.413 0.3 . 1 . . . . . 20 TRP CG . 50428 1 179 . 1 . 1 20 20 TRP CD1 C 13 128.622 0.3 . 1 . . . . . 20 TRP CD1 . 50428 1 180 . 1 . 1 20 20 TRP CD2 C 13 128.224 0.3 . 1 . . . . . 20 TRP CD2 . 50428 1 181 . 1 . 1 20 20 TRP CE2 C 13 138.757 0.3 . 1 . . . . . 20 TRP CE2 . 50428 1 182 . 1 . 1 20 20 TRP CE3 C 13 117.673 0.3 . 1 . . . . . 20 TRP CE3 . 50428 1 183 . 1 . 1 20 20 TRP CZ2 C 13 114.860 0.3 . 1 . . . . . 20 TRP CZ2 . 50428 1 184 . 1 . 1 20 20 TRP CZ3 C 13 120.580 0.3 . 1 . . . . . 20 TRP CZ3 . 50428 1 185 . 1 . 1 20 20 TRP CH2 C 13 123.486 0.3 . 1 . . . . . 20 TRP CH2 . 50428 1 186 . 1 . 1 20 20 TRP N N 15 120.374 0.3 . 1 . . . . . 20 TRP N . 50428 1 187 . 1 . 1 20 20 TRP NE1 N 15 130.400 0.3 . 1 . . . . . 20 TRP NE1 . 50428 1 188 . 1 . 1 21 21 THR H H 1 8.940 0.100 . 1 . . . . . 21 THR H . 50428 1 189 . 1 . 1 21 21 THR HA H 1 3.384 0.100 . 1 . . . . . 21 THR HA . 50428 1 190 . 1 . 1 21 21 THR HB H 1 3.936 0.100 . 1 . . . . . 21 THR HB . 50428 1 191 . 1 . 1 21 21 THR HG21 H 1 0.753 0.100 . 1 . . . . . 21 THR HG2 . 50428 1 192 . 1 . 1 21 21 THR HG22 H 1 0.753 0.100 . 1 . . . . . 21 THR HG2 . 50428 1 193 . 1 . 1 21 21 THR HG23 H 1 0.753 0.100 . 1 . . . . . 21 THR HG2 . 50428 1 194 . 1 . 1 21 21 THR C C 13 175.367 0.3 . 1 . . . . . 21 THR C . 50428 1 195 . 1 . 1 21 21 THR CA C 13 67.172 0.3 . 1 . . . . . 21 THR CA . 50428 1 196 . 1 . 1 21 21 THR CB C 13 68.249 0.3 . 1 . . . . . 21 THR CB . 50428 1 197 . 1 . 1 21 21 THR CG2 C 13 20.676 0.3 . 1 . . . . . 21 THR CG2 . 50428 1 198 . 1 . 1 21 21 THR N N 15 116.746 0.3 . 1 . . . . . 21 THR N . 50428 1 199 . 1 . 1 22 22 TYR H H 1 7.833 0.100 . 1 . . . . . 22 TYR H . 50428 1 200 . 1 . 1 22 22 TYR HA H 1 3.517 0.100 . 1 . . . . . 22 TYR HA . 50428 1 201 . 1 . 1 22 22 TYR HB2 H 1 2.412 0.100 . 1 . . . . . 22 TYR HB2 . 50428 1 202 . 1 . 1 22 22 TYR C C 13 176.002 0.3 . 1 . . . . . 22 TYR C . 50428 1 203 . 1 . 1 22 22 TYR CA C 13 61.724 0.3 . 1 . . . . . 22 TYR CA . 50428 1 204 . 1 . 1 22 22 TYR CB C 13 38.262 0.3 . 1 . . . . . 22 TYR CB . 50428 1 205 . 1 . 1 22 22 TYR CG C 13 127.230 0.3 . 1 . . . . . 22 TYR CG . 50428 1 206 . 1 . 1 22 22 TYR CD1 C 13 132.385 0.3 . 1 . . . . . 22 TYR CD1 . 50428 1 207 . 1 . 1 22 22 TYR CE1 C 13 117.513 0.3 . 1 . . . . . 22 TYR CE1 . 50428 1 208 . 1 . 1 22 22 TYR CZ C 13 158.669 0.3 . 1 . . . . . 22 TYR CZ . 50428 1 209 . 1 . 1 22 22 TYR N N 15 122.687 0.3 . 1 . . . . . 22 TYR N . 50428 1 210 . 1 . 1 23 23 ASN HA H 1 3.669 0.100 . 1 . . . . . 23 ASN HA . 50428 1 211 . 1 . 1 23 23 ASN HB2 H 1 1.795 0.100 . 2 . . . . . 23 ASN HB2 . 50428 1 212 . 1 . 1 23 23 ASN HB3 H 1 2.239 0.100 . 2 . . . . . 23 ASN HB3 . 50428 1 213 . 1 . 1 23 23 ASN C C 13 177.759 0.3 . 1 . . . . . 23 ASN C . 50428 1 214 . 1 . 1 23 23 ASN CA C 13 55.208 0.3 . 1 . . . . . 23 ASN CA . 50428 1 215 . 1 . 1 23 23 ASN CB C 13 36.589 0.3 . 1 . . . . . 23 ASN CB . 50428 1 216 . 1 . 1 23 23 ASN N N 15 116.091 0.3 . 1 . . . . . 23 ASN N . 50428 1 217 . 1 . 1 24 24 ALA H H 1 8.569 0.100 . 1 . . . . . 24 ALA H . 50428 1 218 . 1 . 1 24 24 ALA HA H 1 3.430 0.100 . 1 . . . . . 24 ALA HA . 50428 1 219 . 1 . 1 24 24 ALA HB1 H 1 1.066 0.100 . 1 . . . . . 24 ALA HB . 50428 1 220 . 1 . 1 24 24 ALA HB2 H 1 1.066 0.100 . 1 . . . . . 24 ALA HB . 50428 1 221 . 1 . 1 24 24 ALA HB3 H 1 1.066 0.100 . 1 . . . . . 24 ALA HB . 50428 1 222 . 1 . 1 24 24 ALA C C 13 178.372 0.3 . 1 . . . . . 24 ALA C . 50428 1 223 . 1 . 1 24 24 ALA CA C 13 55.183 0.3 . 1 . . . . . 24 ALA CA . 50428 1 224 . 1 . 1 24 24 ALA CB C 13 18.175 0.3 . 1 . . . . . 24 ALA CB . 50428 1 225 . 1 . 1 24 24 ALA N N 15 122.923 0.3 . 1 . . . . . 24 ALA N . 50428 1 226 . 1 . 1 25 25 GLU HA H 1 3.593 0.100 . 1 . . . . . 25 GLU HA . 50428 1 227 . 1 . 1 25 25 GLU HB2 H 1 1.616 0.100 . 1 . . . . . 25 GLU HB2 . 50428 1 228 . 1 . 1 25 25 GLU HB3 H 1 1.616 0.100 . 1 . . . . . 25 GLU HB3 . 50428 1 229 . 1 . 1 25 25 GLU HG2 H 1 1.855 0.100 . 1 . . . . . 25 GLU HG2 . 50428 1 230 . 1 . 1 25 25 GLU HG3 H 1 1.855 0.100 . 1 . . . . . 25 GLU HG3 . 50428 1 231 . 1 . 1 25 25 GLU C C 13 179.169 0.3 . 1 . . . . . 25 GLU C . 50428 1 232 . 1 . 1 25 25 GLU CA C 13 58.770 0.3 . 1 . . . . . 25 GLU CA . 50428 1 233 . 1 . 1 25 25 GLU CB C 13 28.987 0.3 . 1 . . . . . 25 GLU CB . 50428 1 234 . 1 . 1 25 25 GLU CG C 13 36.129 0.3 . 1 . . . . . 25 GLU CG . 50428 1 235 . 1 . 1 25 25 GLU CD C 13 183.024 0.3 . 1 . . . . . 25 GLU CD . 50428 1 236 . 1 . 1 25 25 GLU N N 15 117.861 0.3 . 1 . . . . . 25 GLU N . 50428 1 237 . 1 . 1 26 26 LEU C C 13 177.563 0.3 . 1 . . . . . 26 LEU C . 50428 1 238 . 1 . 1 26 26 LEU CA C 13 57.311 0.3 . 1 . . . . . 26 LEU CA . 50428 1 239 . 1 . 1 26 26 LEU CB C 13 41.062 0.3 . 1 . . . . . 26 LEU CB . 50428 1 240 . 1 . 1 26 26 LEU CG C 13 26.900 0.3 . 1 . . . . . 26 LEU CG . 50428 1 241 . 1 . 1 26 26 LEU CD1 C 13 21.903 0.3 . 1 . . . . . 26 LEU CD1 . 50428 1 242 . 1 . 1 26 26 LEU CD2 C 13 23.324 0.3 . 1 . . . . . 26 LEU CD2 . 50428 1 243 . 1 . 1 26 26 LEU N N 15 118.140 0.3 . 1 . . . . . 26 LEU N . 50428 1 244 . 1 . 1 27 27 LEU HB2 H 1 1.032 0.100 . 1 . . . . . 27 LEU HB2 . 50428 1 245 . 1 . 1 27 27 LEU HB3 H 1 1.032 0.100 . 1 . . . . . 27 LEU HB3 . 50428 1 246 . 1 . 1 27 27 LEU C C 13 178.264 0.3 . 1 . . . . . 27 LEU C . 50428 1 247 . 1 . 1 27 27 LEU CA C 13 58.126 0.3 . 1 . . . . . 27 LEU CA . 50428 1 248 . 1 . 1 27 27 LEU CB C 13 41.415 0.3 . 1 . . . . . 27 LEU CB . 50428 1 249 . 1 . 1 27 27 LEU CG C 13 26.200 0.3 . 1 . . . . . 27 LEU CG . 50428 1 250 . 1 . 1 27 27 LEU CD1 C 13 23.040 0.3 . 1 . . . . . 27 LEU CD1 . 50428 1 251 . 1 . 1 27 27 LEU CD2 C 13 25.037 0.3 . 1 . . . . . 27 LEU CD2 . 50428 1 252 . 1 . 1 27 27 LEU N N 15 120.828 0.3 . 1 . . . . . 27 LEU N . 50428 1 253 . 1 . 1 28 28 VAL H H 1 8.193 0.100 . 1 . . . . . 28 VAL H . 50428 1 254 . 1 . 1 28 28 VAL C C 13 178.226 0.3 . 1 . . . . . 28 VAL C . 50428 1 255 . 1 . 1 28 28 VAL CA C 13 65.618 0.3 . 1 . . . . . 28 VAL CA . 50428 1 256 . 1 . 1 28 28 VAL CB C 13 31.238 0.3 . 1 . . . . . 28 VAL CB . 50428 1 257 . 1 . 1 28 28 VAL CG1 C 13 21.024 0.3 . 1 . . . . . 28 VAL CG1 . 50428 1 258 . 1 . 1 28 28 VAL CG2 C 13 22.874 0.3 . 1 . . . . . 28 VAL CG2 . 50428 1 259 . 1 . 1 28 28 VAL N N 15 115.615 0.3 . 1 . . . . . 28 VAL N . 50428 1 260 . 1 . 1 29 29 LEU CA C 13 58.020 0.3 . 1 . . . . . 29 LEU CA . 50428 1 261 . 1 . 1 29 29 LEU CB C 13 41.000 0.3 . 1 . . . . . 29 LEU CB . 50428 1 262 . 1 . 1 31 31 GLU CB C 13 29.370 0.3 . 1 . . . . . 31 GLU CB . 50428 1 263 . 1 . 1 31 31 GLU CG C 13 36.370 0.3 . 1 . . . . . 31 GLU CG . 50428 1 264 . 1 . 1 32 32 ASN C C 13 177.673 0.3 . 1 . . . . . 32 ASN C . 50428 1 265 . 1 . 1 32 32 ASN CA C 13 55.801 0.3 . 1 . . . . . 32 ASN CA . 50428 1 266 . 1 . 1 32 32 ASN CB C 13 38.107 0.3 . 1 . . . . . 32 ASN CB . 50428 1 267 . 1 . 1 32 32 ASN CG C 13 175.544 0.3 . 1 . . . . . 32 ASN CG . 50428 1 268 . 1 . 1 32 32 ASN N N 15 120.584 0.3 . 1 . . . . . 32 ASN N . 50428 1 269 . 1 . 1 32 32 ASN ND2 N 15 112.542 0.3 . 1 . . . . . 32 ASN ND2 . 50428 1 270 . 1 . 1 33 33 GLU HA H 1 3.839 0.100 . 1 . . . . . 33 GLU HA . 50428 1 271 . 1 . 1 33 33 GLU C C 13 176.472 0.3 . 1 . . . . . 33 GLU C . 50428 1 272 . 1 . 1 33 33 GLU CA C 13 56.176 0.3 . 1 . . . . . 33 GLU CA . 50428 1 273 . 1 . 1 33 33 GLU CB C 13 29.697 0.3 . 1 . . . . . 33 GLU CB . 50428 1 274 . 1 . 1 33 33 GLU CG C 13 34.869 0.3 . 1 . . . . . 33 GLU CG . 50428 1 275 . 1 . 1 33 33 GLU CD C 13 183.740 0.3 . 1 . . . . . 33 GLU CD . 50428 1 276 . 1 . 1 33 33 GLU N N 15 115.661 0.3 . 1 . . . . . 33 GLU N . 50428 1 277 . 1 . 1 34 34 ARG H H 1 7.926 0.100 . 1 . . . . . 34 ARG H . 50428 1 278 . 1 . 1 34 34 ARG HA H 1 3.728 0.100 . 1 . . . . . 34 ARG HA . 50428 1 279 . 1 . 1 34 34 ARG HB2 H 1 1.125 0.100 . 1 . . . . . 34 ARG HB2 . 50428 1 280 . 1 . 1 34 34 ARG HB3 H 1 1.125 0.100 . 1 . . . . . 34 ARG HB3 . 50428 1 281 . 1 . 1 34 34 ARG C C 13 174.954 0.3 . 1 . . . . . 34 ARG C . 50428 1 282 . 1 . 1 34 34 ARG CA C 13 56.523 0.3 . 1 . . . . . 34 ARG CA . 50428 1 283 . 1 . 1 34 34 ARG CB C 13 27.120 0.3 . 1 . . . . . 34 ARG CB . 50428 1 284 . 1 . 1 34 34 ARG CG C 13 25.527 0.3 . 1 . . . . . 34 ARG CG . 50428 1 285 . 1 . 1 34 34 ARG CD C 13 42.189 0.3 . 1 . . . . . 34 ARG CD . 50428 1 286 . 1 . 1 34 34 ARG CZ C 13 158.966 0.3 . 1 . . . . . 34 ARG CZ . 50428 1 287 . 1 . 1 34 34 ARG N N 15 111.866 0.3 . 1 . . . . . 34 ARG N . 50428 1 288 . 1 . 1 35 35 THR HA H 1 3.210 0.100 . 1 . . . . . 35 THR HA . 50428 1 289 . 1 . 1 35 35 THR HB H 1 3.204 0.100 . 1 . . . . . 35 THR HB . 50428 1 290 . 1 . 1 35 35 THR HG21 H 1 0.674 0.100 . 1 . . . . . 35 THR HG2 . 50428 1 291 . 1 . 1 35 35 THR HG22 H 1 0.674 0.100 . 1 . . . . . 35 THR HG2 . 50428 1 292 . 1 . 1 35 35 THR HG23 H 1 0.674 0.100 . 1 . . . . . 35 THR HG2 . 50428 1 293 . 1 . 1 35 35 THR C C 13 176.098 0.3 . 1 . . . . . 35 THR C . 50428 1 294 . 1 . 1 35 35 THR CA C 13 65.703 0.3 . 1 . . . . . 35 THR CA . 50428 1 295 . 1 . 1 35 35 THR CB C 13 69.033 0.3 . 1 . . . . . 35 THR CB . 50428 1 296 . 1 . 1 35 35 THR CG2 C 13 23.833 0.3 . 1 . . . . . 35 THR CG2 . 50428 1 297 . 1 . 1 35 35 THR N N 15 119.045 0.3 . 1 . . . . . 35 THR N . 50428 1 298 . 1 . 1 36 36 LEU HA H 1 4.091 0.100 . 1 . . . . . 36 LEU HA . 50428 1 299 . 1 . 1 36 36 LEU HB2 H 1 0.920 0.100 . 1 . . . . . 36 LEU HB2 . 50428 1 300 . 1 . 1 36 36 LEU HB3 H 1 0.920 0.100 . 1 . . . . . 36 LEU HB3 . 50428 1 301 . 1 . 1 36 36 LEU C C 13 174.806 0.3 . 1 . . . . . 36 LEU C . 50428 1 302 . 1 . 1 36 36 LEU CA C 13 51.125 0.3 . 1 . . . . . 36 LEU CA . 50428 1 303 . 1 . 1 36 36 LEU CB C 13 43.906 0.3 . 1 . . . . . 36 LEU CB . 50428 1 304 . 1 . 1 36 36 LEU CG C 13 26.943 0.3 . 1 . . . . . 36 LEU CG . 50428 1 305 . 1 . 1 36 36 LEU CD1 C 13 22.431 0.3 . 1 . . . . . 36 LEU CD1 . 50428 1 306 . 1 . 1 36 36 LEU CD2 C 13 25.654 0.3 . 1 . . . . . 36 LEU CD2 . 50428 1 307 . 1 . 1 36 36 LEU N N 15 112.868 0.3 . 1 . . . . . 36 LEU N . 50428 1 308 . 1 . 1 37 37 ASP HA H 1 4.133 0.100 . 1 . . . . . 37 ASP HA . 50428 1 309 . 1 . 1 37 37 ASP HB2 H 1 1.748 0.100 . 2 . . . . . 37 ASP HB2 . 50428 1 310 . 1 . 1 37 37 ASP HB3 H 1 2.624 0.100 . 2 . . . . . 37 ASP HB3 . 50428 1 311 . 1 . 1 37 37 ASP C C 13 175.896 0.3 . 1 . . . . . 37 ASP C . 50428 1 312 . 1 . 1 37 37 ASP CA C 13 52.194 0.3 . 1 . . . . . 37 ASP CA . 50428 1 313 . 1 . 1 37 37 ASP CB C 13 41.312 0.3 . 1 . . . . . 37 ASP CB . 50428 1 314 . 1 . 1 37 37 ASP CG C 13 179.282 0.3 . 1 . . . . . 37 ASP CG . 50428 1 315 . 1 . 1 37 37 ASP N N 15 121.422 0.3 . 1 . . . . . 37 ASP N . 50428 1 316 . 1 . 1 38 38 TYR HA H 1 3.712 0.100 . 1 . . . . . 38 TYR HA . 50428 1 317 . 1 . 1 38 38 TYR CA C 13 59.471 0.3 . 1 . . . . . 38 TYR CA . 50428 1 318 . 1 . 1 38 38 TYR CB C 13 37.801 0.3 . 1 . . . . . 38 TYR CB . 50428 1 319 . 1 . 1 38 38 TYR CG C 13 129.879 0.3 . 1 . . . . . 38 TYR CG . 50428 1 320 . 1 . 1 38 38 TYR CD1 C 13 132.439 0.3 . 1 . . . . . 38 TYR CD1 . 50428 1 321 . 1 . 1 38 38 TYR CE1 C 13 117.824 0.3 . 1 . . . . . 38 TYR CE1 . 50428 1 322 . 1 . 1 38 38 TYR N N 15 126.030 0.3 . 1 . . . . . 38 TYR N . 50428 1 323 . 1 . 1 39 39 HIS CA C 13 56.304 0.3 . 1 . . . . . 39 HIS CA . 50428 1 324 . 1 . 1 39 39 HIS CB C 13 28.537 0.3 . 1 . . . . . 39 HIS CB . 50428 1 325 . 1 . 1 39 39 HIS CG C 13 133.425 0.3 . 1 . . . . . 39 HIS CG . 50428 1 326 . 1 . 1 39 39 HIS CD2 C 13 119.596 0.3 . 1 . . . . . 39 HIS CD2 . 50428 1 327 . 1 . 1 39 39 HIS CE1 C 13 136.954 0.3 . 1 . . . . . 39 HIS CE1 . 50428 1 328 . 1 . 1 40 40 ASP HA H 1 4.101 0.100 . 1 . . . . . 40 ASP HA . 50428 1 329 . 1 . 1 40 40 ASP HB2 H 1 2.200 0.100 . 1 . . . . . 40 ASP HB2 . 50428 1 330 . 1 . 1 40 40 ASP HB3 H 1 2.200 0.100 . 1 . . . . . 40 ASP HB3 . 50428 1 331 . 1 . 1 40 40 ASP C C 13 177.586 0.3 . 1 . . . . . 40 ASP C . 50428 1 332 . 1 . 1 40 40 ASP CA C 13 53.316 0.3 . 1 . . . . . 40 ASP CA . 50428 1 333 . 1 . 1 40 40 ASP CB C 13 42.053 0.3 . 1 . . . . . 40 ASP CB . 50428 1 334 . 1 . 1 40 40 ASP CG C 13 179.375 0.3 . 1 . . . . . 40 ASP CG . 50428 1 335 . 1 . 1 40 40 ASP N N 15 120.724 0.3 . 1 . . . . . 40 ASP N . 50428 1 336 . 1 . 1 41 41 SER HA H 1 3.457 0.100 . 1 . . . . . 41 SER HA . 50428 1 337 . 1 . 1 41 41 SER C C 13 176.011 0.3 . 1 . . . . . 41 SER C . 50428 1 338 . 1 . 1 41 41 SER CA C 13 61.872 0.3 . 1 . . . . . 41 SER CA . 50428 1 339 . 1 . 1 41 41 SER CB C 13 62.212 0.3 . 1 . . . . . 41 SER CB . 50428 1 340 . 1 . 1 41 41 SER N N 15 123.737 0.3 . 1 . . . . . 41 SER N . 50428 1 341 . 1 . 1 42 42 ASN H H 1 9.144 0.100 . 1 . . . . . 42 ASN H . 50428 1 342 . 1 . 1 42 42 ASN HA H 1 3.986 0.100 . 1 . . . . . 42 ASN HA . 50428 1 343 . 1 . 1 42 42 ASN HB2 H 1 2.399 0.100 . 1 . . . . . 42 ASN HB2 . 50428 1 344 . 1 . 1 42 42 ASN HB3 H 1 2.399 0.100 . 1 . . . . . 42 ASN HB3 . 50428 1 345 . 1 . 1 42 42 ASN C C 13 177.640 0.3 . 1 . . . . . 42 ASN C . 50428 1 346 . 1 . 1 42 42 ASN CA C 13 55.809 0.3 . 1 . . . . . 42 ASN CA . 50428 1 347 . 1 . 1 42 42 ASN CB C 13 38.136 0.3 . 1 . . . . . 42 ASN CB . 50428 1 348 . 1 . 1 42 42 ASN CG C 13 175.924 0.3 . 1 . . . . . 42 ASN CG . 50428 1 349 . 1 . 1 42 42 ASN N N 15 118.489 0.3 . 1 . . . . . 42 ASN N . 50428 1 350 . 1 . 1 43 43 VAL H H 1 7.725 0.100 . 1 . . . . . 43 VAL H . 50428 1 351 . 1 . 1 43 43 VAL HA H 1 3.137 0.100 . 1 . . . . . 43 VAL HA . 50428 1 352 . 1 . 1 43 43 VAL HB H 1 2.040 0.100 . 1 . . . . . 43 VAL HB . 50428 1 353 . 1 . 1 43 43 VAL HG11 H 1 0.415 0.100 . 1 . . . . . 43 VAL HG1 . 50428 1 354 . 1 . 1 43 43 VAL HG12 H 1 0.415 0.100 . 1 . . . . . 43 VAL HG1 . 50428 1 355 . 1 . 1 43 43 VAL HG13 H 1 0.415 0.100 . 1 . . . . . 43 VAL HG1 . 50428 1 356 . 1 . 1 43 43 VAL HG21 H 1 0.647 0.100 . 1 . . . . . 43 VAL HG2 . 50428 1 357 . 1 . 1 43 43 VAL HG22 H 1 0.647 0.100 . 1 . . . . . 43 VAL HG2 . 50428 1 358 . 1 . 1 43 43 VAL HG23 H 1 0.647 0.100 . 1 . . . . . 43 VAL HG2 . 50428 1 359 . 1 . 1 43 43 VAL C C 13 177.966 0.3 . 1 . . . . . 43 VAL C . 50428 1 360 . 1 . 1 43 43 VAL CA C 13 65.679 0.3 . 1 . . . . . 43 VAL CA . 50428 1 361 . 1 . 1 43 43 VAL CB C 13 31.098 0.3 . 1 . . . . . 43 VAL CB . 50428 1 362 . 1 . 1 43 43 VAL CG1 C 13 21.536 0.3 . 1 . . . . . 43 VAL CG1 . 50428 1 363 . 1 . 1 43 43 VAL CG2 C 13 24.850 0.3 . 1 . . . . . 43 VAL CG2 . 50428 1 364 . 1 . 1 43 43 VAL N N 15 122.923 0.3 . 1 . . . . . 43 VAL N . 50428 1 365 . 1 . 1 44 44 LYS HA H 1 3.432 0.100 . 1 . . . . . 44 LYS HA . 50428 1 366 . 1 . 1 44 44 LYS C C 13 179.007 0.3 . 1 . . . . . 44 LYS C . 50428 1 367 . 1 . 1 44 44 LYS CA C 13 59.490 0.3 . 1 . . . . . 44 LYS CA . 50428 1 368 . 1 . 1 44 44 LYS CB C 13 31.214 0.3 . 1 . . . . . 44 LYS CB . 50428 1 369 . 1 . 1 44 44 LYS CG C 13 24.462 0.3 . 1 . . . . . 44 LYS CG . 50428 1 370 . 1 . 1 44 44 LYS CD C 13 29.258 0.3 . 1 . . . . . 44 LYS CD . 50428 1 371 . 1 . 1 44 44 LYS CE C 13 41.365 0.3 . 1 . . . . . 44 LYS CE . 50428 1 372 . 1 . 1 44 44 LYS N N 15 120.326 0.3 . 1 . . . . . 44 LYS N . 50428 1 373 . 1 . 1 45 45 ASN HA H 1 3.959 0.100 . 1 . . . . . 45 ASN HA . 50428 1 374 . 1 . 1 45 45 ASN C C 13 175.432 0.3 . 1 . . . . . 45 ASN C . 50428 1 375 . 1 . 1 45 45 ASN CA C 13 55.806 0.3 . 1 . . . . . 45 ASN CA . 50428 1 376 . 1 . 1 45 45 ASN CB C 13 37.955 0.3 . 1 . . . . . 45 ASN CB . 50428 1 377 . 1 . 1 45 45 ASN N N 15 115.067 0.3 . 1 . . . . . 45 ASN N . 50428 1 378 . 1 . 1 47 47 TYR C C 13 178.505 0.3 . 1 . . . . . 47 TYR C . 50428 1 379 . 1 . 1 47 47 TYR CA C 13 61.896 0.3 . 1 . . . . . 47 TYR CA . 50428 1 380 . 1 . 1 47 47 TYR CB C 13 38.469 0.3 . 1 . . . . . 47 TYR CB . 50428 1 381 . 1 . 1 47 47 TYR CG C 13 127.287 0.3 . 1 . . . . . 47 TYR CG . 50428 1 382 . 1 . 1 47 47 TYR CD1 C 13 132.387 0.3 . 1 . . . . . 47 TYR CD1 . 50428 1 383 . 1 . 1 47 47 TYR CE1 C 13 117.700 0.3 . 1 . . . . . 47 TYR CE1 . 50428 1 384 . 1 . 1 47 47 TYR N N 15 117.407 0.3 . 1 . . . . . 47 TYR N . 50428 1 385 . 1 . 1 48 48 GLU C C 13 179.219 0.3 . 1 . . . . . 48 GLU C . 50428 1 386 . 1 . 1 48 48 GLU CA C 13 58.794 0.3 . 1 . . . . . 48 GLU CA . 50428 1 387 . 1 . 1 48 48 GLU CB C 13 28.807 0.3 . 1 . . . . . 48 GLU CB . 50428 1 388 . 1 . 1 48 48 GLU CG C 13 36.442 0.3 . 1 . . . . . 48 GLU CG . 50428 1 389 . 1 . 1 48 48 GLU CD C 13 182.976 0.3 . 1 . . . . . 48 GLU CD . 50428 1 390 . 1 . 1 48 48 GLU N N 15 117.432 0.3 . 1 . . . . . 48 GLU N . 50428 1 391 . 1 . 1 49 49 LYS HA H 1 3.459 0.100 . 1 . . . . . 49 LYS HA . 50428 1 392 . 1 . 1 49 49 LYS C C 13 178.233 0.3 . 1 . . . . . 49 LYS C . 50428 1 393 . 1 . 1 49 49 LYS CA C 13 59.126 0.3 . 1 . . . . . 49 LYS CA . 50428 1 394 . 1 . 1 49 49 LYS CB C 13 31.270 0.3 . 1 . . . . . 49 LYS CB . 50428 1 395 . 1 . 1 49 49 LYS CG C 13 24.918 0.3 . 1 . . . . . 49 LYS CG . 50428 1 396 . 1 . 1 49 49 LYS CD C 13 29.583 0.3 . 1 . . . . . 49 LYS CD . 50428 1 397 . 1 . 1 49 49 LYS CE C 13 41.561 0.3 . 1 . . . . . 49 LYS CE . 50428 1 398 . 1 . 1 49 49 LYS N N 15 120.130 0.3 . 1 . . . . . 49 LYS N . 50428 1 399 . 1 . 1 50 50 VAL H H 1 8.306 0.100 . 1 . . . . . 50 VAL H . 50428 1 400 . 1 . 1 50 50 VAL HA H 1 2.854 0.100 . 1 . . . . . 50 VAL HA . 50428 1 401 . 1 . 1 50 50 VAL HB H 1 1.656 0.100 . 1 . . . . . 50 VAL HB . 50428 1 402 . 1 . 1 50 50 VAL HG11 H 1 0.493 0.100 . 1 . . . . . 50 VAL HG1 . 50428 1 403 . 1 . 1 50 50 VAL HG12 H 1 0.493 0.100 . 1 . . . . . 50 VAL HG1 . 50428 1 404 . 1 . 1 50 50 VAL HG13 H 1 0.493 0.100 . 1 . . . . . 50 VAL HG1 . 50428 1 405 . 1 . 1 50 50 VAL HG21 H 1 0.581 0.100 . 1 . . . . . 50 VAL HG2 . 50428 1 406 . 1 . 1 50 50 VAL HG22 H 1 0.581 0.100 . 1 . . . . . 50 VAL HG2 . 50428 1 407 . 1 . 1 50 50 VAL HG23 H 1 0.581 0.100 . 1 . . . . . 50 VAL HG2 . 50428 1 408 . 1 . 1 50 50 VAL C C 13 177.189 0.3 . 1 . . . . . 50 VAL C . 50428 1 409 . 1 . 1 50 50 VAL CA C 13 65.598 0.3 . 1 . . . . . 50 VAL CA . 50428 1 410 . 1 . 1 50 50 VAL CB C 13 31.151 0.3 . 1 . . . . . 50 VAL CB . 50428 1 411 . 1 . 1 50 50 VAL CG1 C 13 22.212 0.3 . 1 . . . . . 50 VAL CG1 . 50428 1 412 . 1 . 1 50 50 VAL CG2 C 13 22.845 0.3 . 1 . . . . . 50 VAL CG2 . 50428 1 413 . 1 . 1 50 50 VAL N N 15 117.197 0.3 . 1 . . . . . 50 VAL N . 50428 1 414 . 1 . 1 51 51 ARG C C 13 179.044 0.3 . 1 . . . . . 51 ARG C . 50428 1 415 . 1 . 1 51 51 ARG CA C 13 59.099 0.3 . 1 . . . . . 51 ARG CA . 50428 1 416 . 1 . 1 51 51 ARG CB C 13 29.989 0.3 . 1 . . . . . 51 ARG CB . 50428 1 417 . 1 . 1 51 51 ARG CG C 13 27.112 0.3 . 1 . . . . . 51 ARG CG . 50428 1 418 . 1 . 1 51 51 ARG CD C 13 43.197 0.3 . 1 . . . . . 51 ARG CD . 50428 1 419 . 1 . 1 51 51 ARG N N 15 118.072 0.3 . 1 . . . . . 51 ARG N . 50428 1 420 . 1 . 1 52 52 SER HA H 1 3.488 0.100 . 1 . . . . . 52 SER HA . 50428 1 421 . 1 . 1 52 52 SER C C 13 176.342 0.3 . 1 . . . . . 52 SER C . 50428 1 422 . 1 . 1 52 52 SER CA C 13 60.992 0.3 . 1 . . . . . 52 SER CA . 50428 1 423 . 1 . 1 52 52 SER CB C 13 62.512 0.3 . 1 . . . . . 52 SER CB . 50428 1 424 . 1 . 1 52 52 SER N N 15 113.008 0.3 . 1 . . . . . 52 SER N . 50428 1 425 . 1 . 1 53 53 GLN C C 13 178.549 0.3 . 1 . . . . . 53 GLN C . 50428 1 426 . 1 . 1 53 53 GLN CA C 13 56.786 0.3 . 1 . . . . . 53 GLN CA . 50428 1 427 . 1 . 1 53 53 GLN CB C 13 25.978 0.3 . 1 . . . . . 53 GLN CB . 50428 1 428 . 1 . 1 53 53 GLN CG C 13 30.187 0.3 . 1 . . . . . 53 GLN CG . 50428 1 429 . 1 . 1 53 53 GLN CD C 13 178.704 0.3 . 1 . . . . . 53 GLN CD . 50428 1 430 . 1 . 1 53 53 GLN N N 15 119.111 0.3 . 1 . . . . . 53 GLN N . 50428 1 431 . 1 . 1 53 53 GLN NE2 N 15 109.400 0.3 . 1 . . . . . 53 GLN NE2 . 50428 1 432 . 1 . 1 54 54 LEU CD2 C 13 23.090 0.3 . 1 . . . . . 54 LEU CD2 . 50428 1 433 . 1 . 1 56 56 ASN CA C 13 53.815 0.3 . 1 . . . . . 56 ASN CA . 50428 1 434 . 1 . 1 56 56 ASN CB C 13 38.526 0.3 . 1 . . . . . 56 ASN CB . 50428 1 435 . 1 . 1 57 57 ASN CA C 13 52.996 0.3 . 1 . . . . . 57 ASN CA . 50428 1 436 . 1 . 1 57 57 ASN CB C 13 39.376 0.3 . 1 . . . . . 57 ASN CB . 50428 1 437 . 1 . 1 58 58 ALA HA H 1 3.574 0.100 . 1 . . . . . 58 ALA HA . 50428 1 438 . 1 . 1 58 58 ALA HB1 H 1 0.912 0.100 . 1 . . . . . 58 ALA HB . 50428 1 439 . 1 . 1 58 58 ALA HB2 H 1 0.912 0.100 . 1 . . . . . 58 ALA HB . 50428 1 440 . 1 . 1 58 58 ALA HB3 H 1 0.912 0.100 . 1 . . . . . 58 ALA HB . 50428 1 441 . 1 . 1 58 58 ALA C C 13 182.118 0.3 . 1 . . . . . 58 ALA C . 50428 1 442 . 1 . 1 58 58 ALA CA C 13 53.789 0.3 . 1 . . . . . 58 ALA CA . 50428 1 443 . 1 . 1 58 58 ALA CB C 13 19.528 0.3 . 1 . . . . . 58 ALA CB . 50428 1 444 . 1 . 1 58 58 ALA N N 15 127.881 0.3 . 1 . . . . . 58 ALA N . 50428 1 stop_ save_