data_18635 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18635 _Entry.Title ; Backbone resonance assignments of human beta-defensin 1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-08-02 _Entry.Accession_date 2012-08-02 _Entry.Last_release_date 2012-08-02 _Entry.Original_release_date 2012-08-02 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.1.32 _Entry.NMR_STAR_dict_location . _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_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 Viviane 'de Paula' . S. . . 18635 2 Natalia Gomes . S.F. . . 18635 3 Luize Lima . G. . . 18635 4 Catarina Miyamoto . A. . . 18635 5 Robson Monteiro . Q. . . 18635 6 Fabio Almeida . C.L. . . 18635 7 'Ana Paula' Valente . . . . 18635 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18635 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 61 18635 '15N chemical shifts' 33 18635 '1H chemical shifts' 103 18635 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 . . 2019-08-30 . original BMRB . 18635 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18634 'Backbone resonance assignments of human beta-defensin 6' 18635 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18635 _Citation.ID 1 _Citation.Name . _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24970887 _Citation.Full_citation . _Citation.Title ; Unique properties of human beta-defensin 6 (hBD6) and glycosaminoglycan complex: sandwich-like dimerization and competition with the chemokine receptor 2 (CCR2) binding site ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 289 _Citation.Journal_issue 33 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1083-351X _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 22969 _Citation.Page_last 22979 _Citation.Year 2014 _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 Viviane 'De Paula' V. S. . . 18635 1 2 Vitor Pomin V. H. . . 18635 1 3 'Ana Paula' Valente A. P. . . 18635 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18635 _Assembly.ID 1 _Assembly.Name HbD1 _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 HbD1 1 $HbD1 A . yes native no no . . . 18635 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 HbD1 1 CYS 5 5 SG . 1 HbD1 1 CYS 34 34 SG . HbD1 . 5 CYS SG . HbD1 . 34 CYS SG 18635 1 2 disulfide single . 1 HbD1 1 CYS 12 12 SG . 1 HbD1 1 CYS 27 27 SG . HbD1 . 12 CYS SG . HbD1 . 27 CYS SG 18635 1 3 disulfide single . 1 HbD1 1 CYS 17 17 SG . 1 HbD1 1 CYS 35 35 SG . HbD1 . 17 CYS SG . HbD1 . 35 CYS SG 18635 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HbD1 _Entity.Sf_category entity _Entity.Sf_framecode HbD1 _Entity.Entry_ID 18635 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name HbD1 _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 ; DHYNCVSSGGQCLYSACPIF TKIQGTCYRGKAKCCK ; _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 36 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _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 . ASP . 18635 1 2 . HIS . 18635 1 3 . TYR . 18635 1 4 . ASN . 18635 1 5 . CYS . 18635 1 6 . VAL . 18635 1 7 . SER . 18635 1 8 . SER . 18635 1 9 . GLY . 18635 1 10 . GLY . 18635 1 11 . GLN . 18635 1 12 . CYS . 18635 1 13 . LEU . 18635 1 14 . TYR . 18635 1 15 . SER . 18635 1 16 . ALA . 18635 1 17 . CYS . 18635 1 18 . PRO . 18635 1 19 . ILE . 18635 1 20 . PHE . 18635 1 21 . THR . 18635 1 22 . LYS . 18635 1 23 . ILE . 18635 1 24 . GLN . 18635 1 25 . GLY . 18635 1 26 . THR . 18635 1 27 . CYS . 18635 1 28 . TYR . 18635 1 29 . ARG . 18635 1 30 . GLY . 18635 1 31 . LYS . 18635 1 32 . ALA . 18635 1 33 . LYS . 18635 1 34 . CYS . 18635 1 35 . CYS . 18635 1 36 . LYS . 18635 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ASP 1 1 18635 1 . HIS 2 2 18635 1 . TYR 3 3 18635 1 . ASN 4 4 18635 1 . CYS 5 5 18635 1 . VAL 6 6 18635 1 . SER 7 7 18635 1 . SER 8 8 18635 1 . GLY 9 9 18635 1 . GLY 10 10 18635 1 . GLN 11 11 18635 1 . CYS 12 12 18635 1 . LEU 13 13 18635 1 . TYR 14 14 18635 1 . SER 15 15 18635 1 . ALA 16 16 18635 1 . CYS 17 17 18635 1 . PRO 18 18 18635 1 . ILE 19 19 18635 1 . PHE 20 20 18635 1 . THR 21 21 18635 1 . LYS 22 22 18635 1 . ILE 23 23 18635 1 . GLN 24 24 18635 1 . GLY 25 25 18635 1 . THR 26 26 18635 1 . CYS 27 27 18635 1 . TYR 28 28 18635 1 . ARG 29 29 18635 1 . GLY 30 30 18635 1 . LYS 31 31 18635 1 . ALA 32 32 18635 1 . LYS 33 33 18635 1 . CYS 34 34 18635 1 . CYS 35 35 18635 1 . LYS 36 36 18635 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 18635 _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 $HbD1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 18635 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 18635 _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 $HbD1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . pet32a . . . 18635 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18635 _Sample.ID 1 _Sample.Name . _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 HbD1 'natural abundance' . . 1 $HbD1 . . 0.5 . . mM . . . . 18635 1 2 'sodium phosphate' 'natural abundance' . . . . . . . 0.2 0.6 mM . . . . 18635 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18635 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18635 1 5 'phosphate buffer' 'natural abundance' . . . . . . 30 . . mM . . . . 18635 1 6 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 18635 1 7 'potassium chloride' 'natural abundance' . . . . . . 0.9 . . mM . . . . 18635 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 18635 _Sample_condition_list.ID 1 _Sample_condition_list.Name . _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 . M 18635 1 pH 7.4 . pH 18635 1 pressure 1 . atm 18635 1 temperature 298 . K 18635 1 stop_ save_ ############################ # Computer software used # ############################ save_cara _Software.Sf_category software _Software.Sf_framecode cara _Software.Entry_ID 18635 _Software.ID 1 _Software.Type . _Software.Name CARA _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Keller and Wuthrich' . . 18635 1 stop_ loop_ _Task.Software_module _Task.Task _Task.Entry_ID _Task.Software_ID . 'chemical shift assignment' 18635 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 18635 _NMR_spectrometer.ID 1 _NMR_spectrometer.Name . _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _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 18635 _NMR_spectrometer_list.ID 1 _NMR_spectrometer_list.Name . loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 800 . . . 18635 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 18635 _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 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18635 1 2 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18635 1 3 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18635 1 4 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18635 1 5 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18635 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18635 _Chem_shift_reference.ID 1 _Chem_shift_reference.Name . _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 0.00 na indirect 0.251449530 . . . . . 18635 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . 18635 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . 18635 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18635 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name . _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 $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D HNCACB' . . . 18635 1 3 '3D CBCA(CO)NH' . . . 18635 1 4 '3D HBHA(CO)NH' . . . 18635 1 5 '2D 1H-15N HSQC' . . . 18635 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 1 1 ASP H H 1 8.518 0.020 . 1 . . . . . 1 ASP H . 18635 1 2 . 1 1 1 1 ASP CA C 13 56.582 0.3 . 1 . . . . . 1 ASP CA . 18635 1 3 . 1 1 1 1 ASP N N 15 120.935 0.3 . 1 . . . . . 1 ASP N . 18635 1 4 . 1 1 2 2 HIS H H 1 7.999 0.020 . 1 . . . . . 2 HIS H . 18635 1 5 . 1 1 2 2 HIS HA H 1 4.067 0.020 . 1 . . . . . 2 HIS HA . 18635 1 6 . 1 1 2 2 HIS HB2 H 1 2.954 0.020 . 2 . . . . . 2 HIS HB2 . 18635 1 7 . 1 1 2 2 HIS HB3 H 1 2.447 0.020 . 2 . . . . . 2 HIS HB3 . 18635 1 8 . 1 1 2 2 HIS CA C 13 52.790 0.3 . 1 . . . . . 2 HIS CA . 18635 1 9 . 1 1 2 2 HIS N N 15 122.278 0.3 . 1 . . . . . 2 HIS N . 18635 1 10 . 1 1 3 3 TYR H H 1 8.332 0.020 . 1 . . . . . 3 TYR H . 18635 1 11 . 1 1 3 3 TYR CA C 13 55.440 0.3 . 1 . . . . . 3 TYR CA . 18635 1 12 . 1 1 3 3 TYR N N 15 118.171 0.3 . 1 . . . . . 3 TYR N . 18635 1 13 . 1 1 4 4 ASN HA H 1 4.286 0.020 . 1 . . . . . 4 ASN HA . 18635 1 14 . 1 1 4 4 ASN HB2 H 1 2.179 0.020 . 1 . . . . . 4 ASN HB2 . 18635 1 15 . 1 1 4 4 ASN CA C 13 55.531 0.3 . 1 . . . . . 4 ASN CA . 18635 1 16 . 1 1 4 4 ASN CB C 13 37.429 0.3 . 1 . . . . . 4 ASN CB . 18635 1 17 . 1 1 5 5 CYS H H 1 8.103 0.020 . 1 . . . . . 5 CYS H . 18635 1 18 . 1 1 5 5 CYS HA H 1 4.063 0.020 . 1 . . . . . 5 CYS HA . 18635 1 19 . 1 1 5 5 CYS HB2 H 1 2.939 0.020 . 1 . . . . . 5 CYS HB2 . 18635 1 20 . 1 1 5 5 CYS CA C 13 59.050 0.3 . 1 . . . . . 5 CYS CA . 18635 1 21 . 1 1 5 5 CYS N N 15 118.853 0.3 . 1 . . . . . 5 CYS N . 18635 1 22 . 1 1 6 6 VAL H H 1 8.175 0.020 . 1 . . . . . 6 VAL H . 18635 1 23 . 1 1 6 6 VAL CA C 13 65.035 0.3 . 1 . . . . . 6 VAL CA . 18635 1 24 . 1 1 6 6 VAL CB C 13 31.271 0.3 . 1 . . . . . 6 VAL CB . 18635 1 25 . 1 1 6 6 VAL N N 15 117.393 0.3 . 1 . . . . . 6 VAL N . 18635 1 26 . 1 1 7 7 SER H H 1 8.475 0.020 . 1 . . . . . 7 SER H . 18635 1 27 . 1 1 7 7 SER HA H 1 4.206 0.020 . 1 . . . . . 7 SER HA . 18635 1 28 . 1 1 7 7 SER HB2 H 1 3.719 0.020 . 1 . . . . . 7 SER HB2 . 18635 1 29 . 1 1 7 7 SER CA C 13 61.152 0.3 . 1 . . . . . 7 SER CA . 18635 1 30 . 1 1 7 7 SER CB C 13 62.421 0.3 . 1 . . . . . 7 SER CB . 18635 1 31 . 1 1 7 7 SER N N 15 117.296 0.3 . 1 . . . . . 7 SER N . 18635 1 32 . 1 1 8 8 SER H H 1 7.306 0.020 . 1 . . . . . 8 SER H . 18635 1 33 . 1 1 8 8 SER HA H 1 4.603 0.020 . 1 . . . . . 8 SER HA . 18635 1 34 . 1 1 8 8 SER HB2 H 1 3.977 0.020 . 1 . . . . . 8 SER HB2 . 18635 1 35 . 1 1 8 8 SER CA C 13 57.862 0.3 . 1 . . . . . 8 SER CA . 18635 1 36 . 1 1 8 8 SER CB C 13 63.529 0.3 . 1 . . . . . 8 SER CB . 18635 1 37 . 1 1 8 8 SER N N 15 114.084 0.3 . 1 . . . . . 8 SER N . 18635 1 38 . 1 1 9 9 GLY H H 1 7.772 0.020 . 1 . . . . . 9 GLY H . 18635 1 39 . 1 1 9 9 GLY HA2 H 1 4.325 0.020 . 2 . . . . . 9 GLY HA2 . 18635 1 40 . 1 1 9 9 GLY HA3 H 1 3.809 0.020 . 2 . . . . . 9 GLY HA3 . 18635 1 41 . 1 1 9 9 GLY CA C 13 44.976 0.3 . 1 . . . . . 9 GLY CA . 18635 1 42 . 1 1 9 9 GLY N N 15 107.971 0.3 . 1 . . . . . 9 GLY N . 18635 1 43 . 1 1 10 10 GLY H H 1 8.132 0.020 . 1 . . . . . 10 GLY H . 18635 1 44 . 1 1 10 10 GLY HA2 H 1 4.544 0.020 . 2 . . . . . 10 GLY HA2 . 18635 1 45 . 1 1 10 10 GLY HA3 H 1 3.282 0.020 . 2 . . . . . 10 GLY HA3 . 18635 1 46 . 1 1 10 10 GLY CA C 13 44.062 0.3 . 1 . . . . . 10 GLY CA . 18635 1 47 . 1 1 10 10 GLY N N 15 107.972 0.3 . 1 . . . . . 10 GLY N . 18635 1 48 . 1 1 11 11 GLN H H 1 8.139 0.020 . 1 . . . . . 11 GLN H . 18635 1 49 . 1 1 11 11 GLN HA H 1 4.574 0.020 . 1 . . . . . 11 GLN HA . 18635 1 50 . 1 1 11 11 GLN HB2 H 1 1.901 0.020 . 2 . . . . . 11 GLN HB2 . 18635 1 51 . 1 1 11 11 GLN HB3 H 1 1.692 0.020 . 2 . . . . . 11 GLN HB3 . 18635 1 52 . 1 1 11 11 GLN CA C 13 53.795 0.3 . 1 . . . . . 11 GLN CA . 18635 1 53 . 1 1 11 11 GLN CB C 13 32.442 0.3 . 1 . . . . . 11 GLN CB . 18635 1 54 . 1 1 11 11 GLN N N 15 114.512 0.3 . 1 . . . . . 11 GLN N . 18635 1 55 . 1 1 12 12 CYS H H 1 8.721 0.020 . 1 . . . . . 12 CYS H . 18635 1 56 . 1 1 12 12 CYS HA H 1 5.398 0.020 . 1 . . . . . 12 CYS HA . 18635 1 57 . 1 1 12 12 CYS HB2 H 1 2.855 0.020 . 2 . . . . . 12 CYS HB2 . 18635 1 58 . 1 1 12 12 CYS HB3 H 1 2.229 0.020 . 2 . . . . . 12 CYS HB3 . 18635 1 59 . 1 1 12 12 CYS CA C 13 52.950 0.3 . 1 . . . . . 12 CYS CA . 18635 1 60 . 1 1 12 12 CYS CB C 13 38.917 0.3 . 1 . . . . . 12 CYS CB . 18635 1 61 . 1 1 12 12 CYS N N 15 122.473 0.3 . 1 . . . . . 12 CYS N . 18635 1 62 . 1 1 13 13 LEU H H 1 9.308 0.020 . 1 . . . . . 13 LEU H . 18635 1 63 . 1 1 13 13 LEU HA H 1 4.822 0.020 . 1 . . . . . 13 LEU HA . 18635 1 64 . 1 1 13 13 LEU HB2 H 1 1.583 0.020 . 1 . . . . . 13 LEU HB2 . 18635 1 65 . 1 1 13 13 LEU CA C 13 53.337 0.3 . 1 . . . . . 13 LEU CA . 18635 1 66 . 1 1 13 13 LEU CB C 13 45.537 0.3 . 1 . . . . . 13 LEU CB . 18635 1 67 . 1 1 13 13 LEU N N 15 126.302 0.3 . 1 . . . . . 13 LEU N . 18635 1 68 . 1 1 14 14 TYR H H 1 9.050 0.020 . 1 . . . . . 14 TYR H . 18635 1 69 . 1 1 14 14 TYR HA H 1 4.623 0.020 . 1 . . . . . 14 TYR HA . 18635 1 70 . 1 1 14 14 TYR HB2 H 1 3.242 0.020 . 2 . . . . . 14 TYR HB2 . 18635 1 71 . 1 1 14 14 TYR HB3 H 1 2.805 0.020 . 2 . . . . . 14 TYR HB3 . 18635 1 72 . 1 1 14 14 TYR CA C 13 59.382 0.3 . 1 . . . . . 14 TYR CA . 18635 1 73 . 1 1 14 14 TYR CB C 13 37.553 0.3 . 1 . . . . . 14 TYR CB . 18635 1 74 . 1 1 14 14 TYR N N 15 121.091 0.3 . 1 . . . . . 14 TYR N . 18635 1 75 . 1 1 15 15 SER H H 1 7.549 0.020 . 1 . . . . . 15 SER H . 18635 1 76 . 1 1 15 15 SER HA H 1 4.196 0.020 . 1 . . . . . 15 SER HA . 18635 1 77 . 1 1 15 15 SER HB2 H 1 3.888 0.020 . 1 . . . . . 15 SER HB2 . 18635 1 78 . 1 1 15 15 SER CA C 13 57.633 0.3 . 1 . . . . . 15 SER CA . 18635 1 79 . 1 1 15 15 SER CB C 13 64.168 0.3 . 1 . . . . . 15 SER CB . 18635 1 80 . 1 1 15 15 SER N N 15 112.994 0.3 . 1 . . . . . 15 SER N . 18635 1 81 . 1 1 16 16 ALA H H 1 8.090 0.020 . 1 . . . . . 16 ALA H . 18635 1 82 . 1 1 16 16 ALA HA H 1 4.146 0.020 . 1 . . . . . 16 ALA HA . 18635 1 83 . 1 1 16 16 ALA HB1 H 1 1.305 0.020 . 1 . . . . . 16 ALA HB . 18635 1 84 . 1 1 16 16 ALA HB2 H 1 1.305 0.020 . 1 . . . . . 16 ALA HB . 18635 1 85 . 1 1 16 16 ALA HB3 H 1 1.305 0.020 . 1 . . . . . 16 ALA HB . 18635 1 86 . 1 1 16 16 ALA CA C 13 52.260 0.3 . 1 . . . . . 16 ALA CA . 18635 1 87 . 1 1 16 16 ALA CB C 13 18.922 0.3 . 1 . . . . . 16 ALA CB . 18635 1 88 . 1 1 16 16 ALA N N 15 119.748 0.3 . 1 . . . . . 16 ALA N . 18635 1 89 . 1 1 17 17 CYS H H 1 8.601 0.020 . 1 . . . . . 17 CYS H . 18635 1 90 . 1 1 17 17 CYS CA C 13 51.373 0.3 . 1 . . . . . 17 CYS CA . 18635 1 91 . 1 1 17 17 CYS N N 15 119.453 0.3 . 1 . . . . . 17 CYS N . 18635 1 92 . 1 1 18 18 PRO HA H 1 4.435 0.020 . 1 . . . . . 18 PRO HA . 18635 1 93 . 1 1 18 18 PRO HB2 H 1 2.249 0.020 . 2 . . . . . 18 PRO HB2 . 18635 1 94 . 1 1 18 18 PRO HB3 H 1 1.891 0.020 . 2 . . . . . 18 PRO HB3 . 18635 1 95 . 1 1 18 18 PRO CA C 13 63.163 0.3 . 1 . . . . . 18 PRO CA . 18635 1 96 . 1 1 18 18 PRO CB C 13 31.658 0.3 . 1 . . . . . 18 PRO CB . 18635 1 97 . 1 1 19 19 ILE H H 1 8.335 0.020 . 1 . . . . . 19 ILE H . 18635 1 98 . 1 1 19 19 ILE CA C 13 54.526 0.3 . 1 . . . . . 19 ILE CA . 18635 1 99 . 1 1 19 19 ILE CB C 13 40.640 0.3 . 1 . . . . . 19 ILE CB . 18635 1 100 . 1 1 19 19 ILE N N 15 119.884 0.3 . 1 . . . . . 19 ILE N . 18635 1 101 . 1 1 20 20 PHE HA H 1 4.464 0.020 . 1 . . . . . 20 PHE HA . 18635 1 102 . 1 1 20 20 PHE HB2 H 1 3.421 0.020 . 1 . . . . . 20 PHE HB2 . 18635 1 103 . 1 1 20 20 PHE CA C 13 58.367 0.3 . 1 . . . . . 20 PHE CA . 18635 1 104 . 1 1 20 20 PHE CB C 13 36.361 0.3 . 1 . . . . . 20 PHE CB . 18635 1 105 . 1 1 21 21 THR H H 1 8.039 0.020 . 1 . . . . . 21 THR H . 18635 1 106 . 1 1 21 21 THR HA H 1 4.812 0.020 . 1 . . . . . 21 THR HA . 18635 1 107 . 1 1 21 21 THR HB H 1 3.809 0.020 . 1 . . . . . 21 THR HB . 18635 1 108 . 1 1 21 21 THR CA C 13 60.512 0.3 . 1 . . . . . 21 THR CA . 18635 1 109 . 1 1 21 21 THR CB C 13 72.472 0.3 . 1 . . . . . 21 THR CB . 18635 1 110 . 1 1 21 21 THR N N 15 110.619 0.3 . 1 . . . . . 21 THR N . 18635 1 111 . 1 1 22 22 LYS H H 1 9.175 0.020 . 1 . . . . . 22 LYS H . 18635 1 112 . 1 1 22 22 LYS HA H 1 4.723 0.020 . 1 . . . . . 22 LYS HA . 18635 1 113 . 1 1 22 22 LYS HB2 H 1 1.741 0.020 . 1 . . . . . 22 LYS HB2 . 18635 1 114 . 1 1 22 22 LYS CA C 13 54.206 0.3 . 1 . . . . . 22 LYS CA . 18635 1 115 . 1 1 22 22 LYS CB C 13 35.956 0.3 . 1 . . . . . 22 LYS CB . 18635 1 116 . 1 1 22 22 LYS N N 15 118.950 0.3 . 1 . . . . . 22 LYS N . 18635 1 117 . 1 1 23 23 ILE H H 1 8.360 0.020 . 1 . . . . . 23 ILE H . 18635 1 118 . 1 1 23 23 ILE HA H 1 4.266 0.020 . 1 . . . . . 23 ILE HA . 18635 1 119 . 1 1 23 23 ILE CA C 13 62.842 0.3 . 1 . . . . . 23 ILE CA . 18635 1 120 . 1 1 23 23 ILE CB C 13 38.191 0.3 . 1 . . . . . 23 ILE CB . 18635 1 121 . 1 1 23 23 ILE N N 15 121.344 0.3 . 1 . . . . . 23 ILE N . 18635 1 122 . 1 1 24 24 GLN H H 1 9.321 0.020 . 1 . . . . . 24 GLN H . 18635 1 123 . 1 1 24 24 GLN HA H 1 4.355 0.020 . 1 . . . . . 24 GLN HA . 18635 1 124 . 1 1 24 24 GLN HB2 H 1 1.643 0.020 . 1 . . . . . 24 GLN HB2 . 18635 1 125 . 1 1 24 24 GLN CA C 13 54.530 0.3 . 1 . . . . . 24 GLN CA . 18635 1 126 . 1 1 24 24 GLN CB C 13 29.461 0.3 . 1 . . . . . 24 GLN CB . 18635 1 127 . 1 1 24 24 GLN N N 15 129.047 0.3 . 1 . . . . . 24 GLN N . 18635 1 128 . 1 1 25 25 GLY H H 1 8.485 0.020 . 1 . . . . . 25 GLY H . 18635 1 129 . 1 1 25 25 GLY HA2 H 1 3.997 0.020 . 1 . . . . . 25 GLY HA2 . 18635 1 130 . 1 1 25 25 GLY CA C 13 45.205 0.3 . 1 . . . . . 25 GLY CA . 18635 1 131 . 1 1 25 25 GLY N N 15 109.373 0.3 . 1 . . . . . 25 GLY N . 18635 1 132 . 1 1 26 26 THR H H 1 8.075 0.020 . 1 . . . . . 26 THR H . 18635 1 133 . 1 1 26 26 THR HA H 1 4.415 0.020 . 1 . . . . . 26 THR HA . 18635 1 134 . 1 1 26 26 THR HB H 1 4.256 0.020 . 1 . . . . . 26 THR HB . 18635 1 135 . 1 1 26 26 THR CA C 13 61.371 0.3 . 1 . . . . . 26 THR CA . 18635 1 136 . 1 1 26 26 THR CB C 13 69.704 0.3 . 1 . . . . . 26 THR CB . 18635 1 137 . 1 1 26 26 THR N N 15 112.702 0.3 . 1 . . . . . 26 THR N . 18635 1 138 . 1 1 27 27 CYS H H 1 8.475 0.020 . 1 . . . . . 27 CYS H . 18635 1 139 . 1 1 27 27 CYS HA H 1 4.574 0.020 . 1 . . . . . 27 CYS HA . 18635 1 140 . 1 1 27 27 CYS HB2 H 1 2.646 0.020 . 1 . . . . . 27 CYS HB2 . 18635 1 141 . 1 1 27 27 CYS CA C 13 54.389 0.3 . 1 . . . . . 27 CYS CA . 18635 1 142 . 1 1 27 27 CYS CB C 13 40.959 0.3 . 1 . . . . . 27 CYS CB . 18635 1 143 . 1 1 27 27 CYS N N 15 122.298 0.3 . 1 . . . . . 27 CYS N . 18635 1 144 . 1 1 28 28 TYR H H 1 8.303 0.020 . 1 . . . . . 28 TYR H . 18635 1 145 . 1 1 28 28 TYR HA H 1 4.544 0.020 . 1 . . . . . 28 TYR HA . 18635 1 146 . 1 1 28 28 TYR HB2 H 1 2.646 0.020 . 1 . . . . . 28 TYR HB2 . 18635 1 147 . 1 1 28 28 TYR CA C 13 54.572 0.3 . 1 . . . . . 28 TYR CA . 18635 1 148 . 1 1 28 28 TYR CB C 13 40.496 0.3 . 1 . . . . . 28 TYR CB . 18635 1 149 . 1 1 28 28 TYR N N 15 120.721 0.3 . 1 . . . . . 28 TYR N . 18635 1 150 . 1 1 29 29 ARG H H 1 8.124 0.020 . 1 . . . . . 29 ARG H . 18635 1 151 . 1 1 29 29 ARG HA H 1 3.928 0.020 . 1 . . . . . 29 ARG HA . 18635 1 152 . 1 1 29 29 ARG HB2 H 1 2.050 0.020 . 1 . . . . . 29 ARG HB2 . 18635 1 153 . 1 1 29 29 ARG CA C 13 56.354 0.3 . 1 . . . . . 29 ARG CA . 18635 1 154 . 1 1 29 29 ARG N N 15 120.572 0.3 . 1 . . . . . 29 ARG N . 18635 1 155 . 1 1 30 30 GLY H H 1 8.403 0.020 . 1 . . . . . 30 GLY H . 18635 1 156 . 1 1 30 30 GLY HA2 H 1 4.295 0.020 . 2 . . . . . 30 GLY HA2 . 18635 1 157 . 1 1 30 30 GLY HA3 H 1 3.441 0.020 . 2 . . . . . 30 GLY HA3 . 18635 1 158 . 1 1 30 30 GLY CA C 13 44.748 0.3 . 1 . . . . . 30 GLY CA . 18635 1 159 . 1 1 30 30 GLY N N 15 104.897 0.3 . 1 . . . . . 30 GLY N . 18635 1 160 . 1 1 31 31 LYS H H 1 7.628 0.020 . 1 . . . . . 31 LYS H . 18635 1 161 . 1 1 31 31 LYS HA H 1 4.305 0.020 . 1 . . . . . 31 LYS HA . 18635 1 162 . 1 1 31 31 LYS HB2 H 1 2.169 0.020 . 1 . . . . . 31 LYS HB2 . 18635 1 163 . 1 1 31 31 LYS CA C 13 57.999 0.3 . 1 . . . . . 31 LYS CA . 18635 1 164 . 1 1 31 31 LYS CB C 13 33.081 0.3 . 1 . . . . . 31 LYS CB . 18635 1 165 . 1 1 31 31 LYS N N 15 119.359 0.3 . 1 . . . . . 31 LYS N . 18635 1 166 . 1 1 32 32 ALA H H 1 8.189 0.020 . 1 . . . . . 32 ALA H . 18635 1 167 . 1 1 32 32 ALA HA H 1 4.564 0.020 . 1 . . . . . 32 ALA HA . 18635 1 168 . 1 1 32 32 ALA HB1 H 1 0.450 0.020 . 1 . . . . . 32 ALA HB . 18635 1 169 . 1 1 32 32 ALA HB2 H 1 0.450 0.020 . 1 . . . . . 32 ALA HB . 18635 1 170 . 1 1 32 32 ALA HB3 H 1 0.450 0.020 . 1 . . . . . 32 ALA HB . 18635 1 171 . 1 1 32 32 ALA CA C 13 49.180 0.3 . 1 . . . . . 32 ALA CA . 18635 1 172 . 1 1 32 32 ALA CB C 13 20.731 0.3 . 1 . . . . . 32 ALA CB . 18635 1 173 . 1 1 32 32 ALA N N 15 119.184 0.3 . 1 . . . . . 32 ALA N . 18635 1 174 . 1 1 33 33 LYS H H 1 8.607 0.020 . 1 . . . . . 33 LYS H . 18635 1 175 . 1 1 33 33 LYS HA H 1 4.365 0.020 . 1 . . . . . 33 LYS HA . 18635 1 176 . 1 1 33 33 LYS HB2 H 1 1.752 0.020 . 2 . . . . . 33 LYS HB2 . 18635 1 177 . 1 1 33 33 LYS HB3 H 1 1.613 0.020 . 2 . . . . . 33 LYS HB3 . 18635 1 178 . 1 1 33 33 LYS CA C 13 55.211 0.3 . 1 . . . . . 33 LYS CA . 18635 1 179 . 1 1 33 33 LYS N N 15 120.059 0.3 . 1 . . . . . 33 LYS N . 18635 1 180 . 1 1 34 34 CYS H H 1 7.903 0.020 . 1 . . . . . 34 CYS H . 18635 1 181 . 1 1 34 34 CYS HA H 1 5.041 0.020 . 1 . . . . . 34 CYS HA . 18635 1 182 . 1 1 34 34 CYS HB2 H 1 2.676 0.020 . 2 . . . . . 34 CYS HB2 . 18635 1 183 . 1 1 34 34 CYS HB3 H 1 2.288 0.020 . 2 . . . . . 34 CYS HB3 . 18635 1 184 . 1 1 34 34 CYS CA C 13 54.800 0.3 . 1 . . . . . 34 CYS CA . 18635 1 185 . 1 1 34 34 CYS CB C 13 39.575 0.3 . 1 . . . . . 34 CYS CB . 18635 1 186 . 1 1 34 34 CYS N N 15 119.437 0.3 . 1 . . . . . 34 CYS N . 18635 1 187 . 1 1 35 35 CYS H H 1 9.208 0.020 . 1 . . . . . 35 CYS H . 18635 1 188 . 1 1 35 35 CYS HA H 1 5.269 0.020 . 1 . . . . . 35 CYS HA . 18635 1 189 . 1 1 35 35 CYS HB2 H 1 2.994 0.020 . 2 . . . . . 35 CYS HB2 . 18635 1 190 . 1 1 35 35 CYS HB3 H 1 2.567 0.020 . 2 . . . . . 35 CYS HB3 . 18635 1 191 . 1 1 35 35 CYS CA C 13 53.380 0.3 . 1 . . . . . 35 CYS CA . 18635 1 192 . 1 1 35 35 CYS CB C 13 40.214 0.3 . 1 . . . . . 35 CYS CB . 18635 1 193 . 1 1 35 35 CYS N N 15 128.490 0.3 . 1 . . . . . 35 CYS N . 18635 1 194 . 1 1 36 36 LYS H H 1 9.214 0.020 . 1 . . . . . 36 LYS H . 18635 1 195 . 1 1 36 36 LYS CA C 13 58.540 0.3 . 1 . . . . . 36 LYS CA . 18635 1 196 . 1 1 36 36 LYS CB C 13 36.169 0.3 . 1 . . . . . 36 LYS CB . 18635 1 197 . 1 1 36 36 LYS N N 15 129.882 0.3 . 1 . . . . . 36 LYS N . 18635 1 stop_ save_