data_5052 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5052 _Entry.Title ; 1H Assigned Chemical Shifts for Neurotoxin II ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-06-12 _Entry.Accession_date 2001-06-12 _Entry.Last_release_date 2001-06-12 _Entry.Original_release_date 2001-06-12 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 Yuan Cheng . . . . 5052 2 Wanyu Wang . . . . 5052 3 Jinfeng Wang . . . . 5052 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5052 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 373 5052 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2001-06-18 . original author 'Original release' 5052 1 . . 2003-02-18 . update BMRB 'Links to related BMRB entries inserted' 5052 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5690 'Chemical shifts by different group' 5052 PDB 1JE9 'BMRB Entry Tracking System' 5052 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5052 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; 1H Assigned Chemical Shifts for Neurotoxin II ; _Citation.Status published _Citation.Type 'BMRB only' _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Yuan Cheng . . . . 5052 1 2 Wanyu Wang . . . . 5052 1 3 Jinfeng Wang . . . . 5052 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_neurotoxin_II _Assembly.Sf_category assembly _Assembly.Sf_framecode system_neurotoxin_II _Assembly.Entry_ID 5052 _Assembly.ID 1 _Assembly.Name 'neurotoxin II' _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 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5052 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'neurotoxin II monomer' 1 $nt2 . . . native . . . . . 5052 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 . 1 CYS 3 3 SG . 1 . 1 CYS 23 23 SG . . . . . . . . . . . . 5052 1 2 disulfide single . 1 . 1 CYS 17 17 SG . 1 . 1 CYS 40 40 SG . . . . . . . . . . . . 5052 1 3 disulfide single . 1 . 1 CYS 42 42 SG . 1 . 1 CYS 53 53 SG . . . . . . . . . . . . 5052 1 4 disulfide single . 1 . 1 CYS 54 54 SG . 1 . 1 CYS 59 59 SG . . . . . . . . . . . . 5052 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'neurotoxin II' abbreviation 5052 1 'neurotoxin II' system 5052 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_nt2 _Entity.Sf_category entity _Entity.Sf_framecode nt2 _Entity.Entry_ID 5052 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'cobrotoxin, neurotoxin' _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 ; LECHNQQSSQAPTTKTCSGE TNCYKKWWSDHRGTIIERGC GCPKVKPGVNLNCCRTDRCN N ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 61 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 5690 . 'neurotoxin II' . . . . . 100.00 61 98.36 98.36 2.77e-27 . . . . 5052 1 2 no PDB 1JE9 . 'Nmr Solution Structure Of Nt2' . . . . . 100.00 61 100.00 100.00 6.02e-28 . . . . 5052 1 3 no PDB 1NOR . 'Two-Dimensional 1h-Nmr Study Of The Spatial Structure Of Neurotoxin Ii From Naja Oxiana' . . . . . 100.00 61 98.36 98.36 2.77e-27 . . . . 5052 1 4 no SWISS-PROT P01427 . 'Short neurotoxin 1 (Neurotoxin alpha) (Neurotoxin II) (NTX II)' . . . . . 100.00 61 98.36 98.36 2.77e-27 . . . . 5052 1 5 no SWISS-PROT P59276 . 'Cobrotoxin-c (CBT-c) (Short neurotoxin 2) (NT2)' . . . . . 100.00 61 100.00 100.00 6.02e-28 . . . . 5052 1 6 no SWISS-PROT P60773 . 'Short neurotoxin 1 (NTX I)' . . . . . 100.00 61 98.36 98.36 2.37e-27 . . . . 5052 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID CBT abbreviation 5052 1 'cobrotoxin, neurotoxin' common 5052 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . LEU . 5052 1 2 . GLU . 5052 1 3 . CYS . 5052 1 4 . HIS . 5052 1 5 . ASN . 5052 1 6 . GLN . 5052 1 7 . GLN . 5052 1 8 . SER . 5052 1 9 . SER . 5052 1 10 . GLN . 5052 1 11 . ALA . 5052 1 12 . PRO . 5052 1 13 . THR . 5052 1 14 . THR . 5052 1 15 . LYS . 5052 1 16 . THR . 5052 1 17 . CYS . 5052 1 18 . SER . 5052 1 19 . GLY . 5052 1 20 . GLU . 5052 1 21 . THR . 5052 1 22 . ASN . 5052 1 23 . CYS . 5052 1 24 . TYR . 5052 1 25 . LYS . 5052 1 26 . LYS . 5052 1 27 . TRP . 5052 1 28 . TRP . 5052 1 29 . SER . 5052 1 30 . ASP . 5052 1 31 . HIS . 5052 1 32 . ARG . 5052 1 33 . GLY . 5052 1 34 . THR . 5052 1 35 . ILE . 5052 1 36 . ILE . 5052 1 37 . GLU . 5052 1 38 . ARG . 5052 1 39 . GLY . 5052 1 40 . CYS . 5052 1 41 . GLY . 5052 1 42 . CYS . 5052 1 43 . PRO . 5052 1 44 . LYS . 5052 1 45 . VAL . 5052 1 46 . LYS . 5052 1 47 . PRO . 5052 1 48 . GLY . 5052 1 49 . VAL . 5052 1 50 . ASN . 5052 1 51 . LEU . 5052 1 52 . ASN . 5052 1 53 . CYS . 5052 1 54 . CYS . 5052 1 55 . ARG . 5052 1 56 . THR . 5052 1 57 . ASP . 5052 1 58 . ARG . 5052 1 59 . CYS . 5052 1 60 . ASN . 5052 1 61 . ASN . 5052 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 . LEU 1 1 5052 1 . GLU 2 2 5052 1 . CYS 3 3 5052 1 . HIS 4 4 5052 1 . ASN 5 5 5052 1 . GLN 6 6 5052 1 . GLN 7 7 5052 1 . SER 8 8 5052 1 . SER 9 9 5052 1 . GLN 10 10 5052 1 . ALA 11 11 5052 1 . PRO 12 12 5052 1 . THR 13 13 5052 1 . THR 14 14 5052 1 . LYS 15 15 5052 1 . THR 16 16 5052 1 . CYS 17 17 5052 1 . SER 18 18 5052 1 . GLY 19 19 5052 1 . GLU 20 20 5052 1 . THR 21 21 5052 1 . ASN 22 22 5052 1 . CYS 23 23 5052 1 . TYR 24 24 5052 1 . LYS 25 25 5052 1 . LYS 26 26 5052 1 . TRP 27 27 5052 1 . TRP 28 28 5052 1 . SER 29 29 5052 1 . ASP 30 30 5052 1 . HIS 31 31 5052 1 . ARG 32 32 5052 1 . GLY 33 33 5052 1 . THR 34 34 5052 1 . ILE 35 35 5052 1 . ILE 36 36 5052 1 . GLU 37 37 5052 1 . ARG 38 38 5052 1 . GLY 39 39 5052 1 . CYS 40 40 5052 1 . GLY 41 41 5052 1 . CYS 42 42 5052 1 . PRO 43 43 5052 1 . LYS 44 44 5052 1 . VAL 45 45 5052 1 . LYS 46 46 5052 1 . PRO 47 47 5052 1 . GLY 48 48 5052 1 . VAL 49 49 5052 1 . ASN 50 50 5052 1 . LEU 51 51 5052 1 . ASN 52 52 5052 1 . CYS 53 53 5052 1 . CYS 54 54 5052 1 . ARG 55 55 5052 1 . THR 56 56 5052 1 . ASP 57 57 5052 1 . ARG 58 58 5052 1 . CYS 59 59 5052 1 . ASN 60 60 5052 1 . ASN 61 61 5052 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 5052 _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 $nt2 . 8649 . . 'Naja kaouthia' 'monocled cobra' . . Eukaryota Metazoa Naja kaouthia . . . . . . . . . . . . . 5052 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 5052 _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 $nt2 . 'purified from the natural source' . . . . . . . . . . . . . . . . 5052 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5052 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'cobrotoxin, neurotoxin' . . . 1 $nt2 . . 4 . . mM . . . . 5052 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5052 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 4.0 0.2 n/a 5052 1 temperature 300 1 K 5052 1 stop_ save_ save_condition_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_2 _Sample_condition_list.Entry_ID 5052 _Sample_condition_list.ID 2 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH* 4.5 0.2 n/a 5052 2 temperature 300 1 K 5052 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5052 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5052 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DMX . 600 . . . 5052 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 5052 _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 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5052 1 2 TQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5052 1 3 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5052 1 4 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5052 1 5 E-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5052 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5052 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 internal cylindrical parallel . . 5052 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5052 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; In our COSY type spectra, cross peaks are distinguished definitely between alpha proton and belta protons of ILE35 (HA-HB) and ASN50 (HA-HB2, HA-HB3). We also ovserved this in another sample (BMRB4891). In our final calculation structure results, these protons (ILE35:HB, ASN50:HB#) are near to the indole ring of TRP29 and TRP28. We think the extraordinary high field shifts are due to the ring current. ; _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 DQF-COSY 1 $sample_1 . 5052 1 2 TQF-COSY 1 $sample_1 . 5052 1 3 TOCSY 1 $sample_1 . 5052 1 4 NOESY 1 $sample_1 . 5052 1 5 E-COSY 1 $sample_1 . 5052 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 LEU HA H 1 4.004 0.01 . 1 . . . . . . . . . 5052 1 2 . 1 1 1 1 LEU HB2 H 1 1.386 0.01 . 1 . . . . . . . . . 5052 1 3 . 1 1 1 1 LEU HB3 H 1 1.386 0.01 . 1 . . . . . . . . . 5052 1 4 . 1 1 1 1 LEU HG H 1 1.279 0.01 . 1 . . . . . . . . . 5052 1 5 . 1 1 1 1 LEU HD11 H 1 0.561 0.01 . 2 . . . . . . . . . 5052 1 6 . 1 1 1 1 LEU HD12 H 1 0.561 0.01 . 2 . . . . . . . . . 5052 1 7 . 1 1 1 1 LEU HD13 H 1 0.561 0.01 . 2 . . . . . . . . . 5052 1 8 . 1 1 1 1 LEU HD21 H 1 0.447 0.01 . 2 . . . . . . . . . 5052 1 9 . 1 1 1 1 LEU HD22 H 1 0.447 0.01 . 2 . . . . . . . . . 5052 1 10 . 1 1 1 1 LEU HD23 H 1 0.447 0.01 . 2 . . . . . . . . . 5052 1 11 . 1 1 2 2 GLU H H 1 8.551 0.01 . 1 . . . . . . . . . 5052 1 12 . 1 1 2 2 GLU HA H 1 4.996 0.01 . 1 . . . . . . . . . 5052 1 13 . 1 1 2 2 GLU HB2 H 1 1.604 0.01 . 1 . . . . . . . . . 5052 1 14 . 1 1 2 2 GLU HB3 H 1 1.604 0.01 . 1 . . . . . . . . . 5052 1 15 . 1 1 2 2 GLU HG2 H 1 2.030 0.01 . 2 . . . . . . . . . 5052 1 16 . 1 1 2 2 GLU HG3 H 1 2.139 0.01 . 2 . . . . . . . . . 5052 1 17 . 1 1 3 3 CYS H H 1 8.633 0.01 . 1 . . . . . . . . . 5052 1 18 . 1 1 3 3 CYS HA H 1 4.929 0.01 . 1 . . . . . . . . . 5052 1 19 . 1 1 3 3 CYS HB2 H 1 2.789 0.01 . 1 . . . . . . . . . 5052 1 20 . 1 1 3 3 CYS HB3 H 1 2.203 0.01 . 1 . . . . . . . . . 5052 1 21 . 1 1 4 4 HIS H H 1 9.686 0.01 . 1 . . . . . . . . . 5052 1 22 . 1 1 4 4 HIS HA H 1 5.304 0.01 . 1 . . . . . . . . . 5052 1 23 . 1 1 4 4 HIS HB2 H 1 3.655 0.01 . 1 . . . . . . . . . 5052 1 24 . 1 1 4 4 HIS HB3 H 1 2.672 0.01 . 1 . . . . . . . . . 5052 1 25 . 1 1 4 4 HIS HD2 H 1 6.623 0.01 . 1 . . . . . . . . . 5052 1 26 . 1 1 4 4 HIS HE1 H 1 8.690 0.01 . 1 . . . . . . . . . 5052 1 27 . 1 1 5 5 ASN H H 1 8.100 0.01 . 1 . . . . . . . . . 5052 1 28 . 1 1 5 5 ASN HA H 1 4.709 0.01 . 1 . . . . . . . . . 5052 1 29 . 1 1 5 5 ASN HB2 H 1 1.934 0.01 . 1 . . . . . . . . . 5052 1 30 . 1 1 5 5 ASN HB3 H 1 2.943 0.01 . 1 . . . . . . . . . 5052 1 31 . 1 1 5 5 ASN HD21 H 1 7.565 0.01 . 1 . . . . . . . . . 5052 1 32 . 1 1 5 5 ASN HD22 H 1 7.044 0.01 . 1 . . . . . . . . . 5052 1 33 . 1 1 6 6 GLN H H 1 8.988 0.01 . 1 . . . . . . . . . 5052 1 34 . 1 1 6 6 GLN HA H 1 4.412 0.01 . 1 . . . . . . . . . 5052 1 35 . 1 1 6 6 GLN HB2 H 1 1.800 0.01 . 1 . . . . . . . . . 5052 1 36 . 1 1 6 6 GLN HB3 H 1 1.800 0.01 . 1 . . . . . . . . . 5052 1 37 . 1 1 6 6 GLN HG2 H 1 2.507 0.01 . 1 . . . . . . . . . 5052 1 38 . 1 1 6 6 GLN HG3 H 1 2.507 0.01 . 1 . . . . . . . . . 5052 1 39 . 1 1 6 6 GLN HE21 H 1 7.654 0.01 . 1 . . . . . . . . . 5052 1 40 . 1 1 6 6 GLN HE22 H 1 6.558 0.01 . 1 . . . . . . . . . 5052 1 41 . 1 1 7 7 GLN H H 1 8.263 0.01 . 1 . . . . . . . . . 5052 1 42 . 1 1 7 7 GLN HA H 1 4.642 0.01 . 1 . . . . . . . . . 5052 1 43 . 1 1 7 7 GLN HB2 H 1 1.896 0.01 . 1 . . . . . . . . . 5052 1 44 . 1 1 7 7 GLN HB3 H 1 2.043 0.01 . 1 . . . . . . . . . 5052 1 45 . 1 1 7 7 GLN HG2 H 1 2.439 0.01 . 1 . . . . . . . . . 5052 1 46 . 1 1 7 7 GLN HG3 H 1 2.439 0.01 . 1 . . . . . . . . . 5052 1 47 . 1 1 7 7 GLN HE21 H 1 7.354 0.01 . 1 . . . . . . . . . 5052 1 48 . 1 1 7 7 GLN HE22 H 1 6.823 0.01 . 1 . . . . . . . . . 5052 1 49 . 1 1 8 8 SER H H 1 9.523 0.01 . 1 . . . . . . . . . 5052 1 50 . 1 1 8 8 SER HA H 1 3.750 0.01 . 1 . . . . . . . . . 5052 1 51 . 1 1 8 8 SER HB2 H 1 3.845 0.01 . 1 . . . . . . . . . 5052 1 52 . 1 1 8 8 SER HB3 H 1 3.982 0.01 . 1 . . . . . . . . . 5052 1 53 . 1 1 9 9 SER H H 1 8.220 0.01 . 1 . . . . . . . . . 5052 1 54 . 1 1 9 9 SER HA H 1 4.508 0.01 . 1 . . . . . . . . . 5052 1 55 . 1 1 9 9 SER HB2 H 1 3.841 0.01 . 1 . . . . . . . . . 5052 1 56 . 1 1 9 9 SER HB3 H 1 3.841 0.01 . 1 . . . . . . . . . 5052 1 57 . 1 1 10 10 GLN H H 1 7.870 0.01 . 1 . . . . . . . . . 5052 1 58 . 1 1 10 10 GLN HA H 1 3.995 0.01 . 1 . . . . . . . . . 5052 1 59 . 1 1 10 10 GLN HB2 H 1 2.127 0.01 . 1 . . . . . . . . . 5052 1 60 . 1 1 10 10 GLN HB3 H 1 1.913 0.01 . 1 . . . . . . . . . 5052 1 61 . 1 1 10 10 GLN HG2 H 1 2.335 0.01 . 2 . . . . . . . . . 5052 1 62 . 1 1 10 10 GLN HG3 H 1 2.450 0.01 . 2 . . . . . . . . . 5052 1 63 . 1 1 10 10 GLN HE21 H 1 7.508 0.01 . 2 . . . . . . . . . 5052 1 64 . 1 1 10 10 GLN HE22 H 1 6.830 0.01 . 2 . . . . . . . . . 5052 1 65 . 1 1 11 11 ALA H H 1 8.341 0.01 . 1 . . . . . . . . . 5052 1 66 . 1 1 11 11 ALA HA H 1 4.244 0.01 . 1 . . . . . . . . . 5052 1 67 . 1 1 11 11 ALA HB1 H 1 1.201 0.01 . 1 . . . . . . . . . 5052 1 68 . 1 1 11 11 ALA HB2 H 1 1.201 0.01 . 1 . . . . . . . . . 5052 1 69 . 1 1 11 11 ALA HB3 H 1 1.201 0.01 . 1 . . . . . . . . . 5052 1 70 . 1 1 12 12 PRO HA H 1 3.617 0.01 . 1 . . . . . . . . . 5052 1 71 . 1 1 12 12 PRO HB2 H 1 2.376 0.01 . 1 . . . . . . . . . 5052 1 72 . 1 1 12 12 PRO HB3 H 1 2.499 0.01 . 1 . . . . . . . . . 5052 1 73 . 1 1 12 12 PRO HG2 H 1 1.673 0.01 . 2 . . . . . . . . . 5052 1 74 . 1 1 12 12 PRO HG3 H 1 1.898 0.01 . 2 . . . . . . . . . 5052 1 75 . 1 1 12 12 PRO HD2 H 1 3.414 0.01 . 2 . . . . . . . . . 5052 1 76 . 1 1 12 12 PRO HD3 H 1 3.703 0.01 . 2 . . . . . . . . . 5052 1 77 . 1 1 13 13 THR H H 1 7.790 0.01 . 1 . . . . . . . . . 5052 1 78 . 1 1 13 13 THR HA H 1 4.649 0.01 . 1 . . . . . . . . . 5052 1 79 . 1 1 13 13 THR HB H 1 4.414 0.01 . 1 . . . . . . . . . 5052 1 80 . 1 1 13 13 THR HG21 H 1 1.085 0.01 . 1 . . . . . . . . . 5052 1 81 . 1 1 13 13 THR HG22 H 1 1.085 0.01 . 1 . . . . . . . . . 5052 1 82 . 1 1 13 13 THR HG23 H 1 1.085 0.01 . 1 . . . . . . . . . 5052 1 83 . 1 1 14 14 THR H H 1 8.814 0.01 . 1 . . . . . . . . . 5052 1 84 . 1 1 14 14 THR HA H 1 4.780 0.01 . 1 . . . . . . . . . 5052 1 85 . 1 1 14 14 THR HB H 1 3.598 0.01 . 1 . . . . . . . . . 5052 1 86 . 1 1 14 14 THR HG21 H 1 0.595 0.01 . 1 . . . . . . . . . 5052 1 87 . 1 1 14 14 THR HG22 H 1 0.595 0.01 . 1 . . . . . . . . . 5052 1 88 . 1 1 14 14 THR HG23 H 1 0.595 0.01 . 1 . . . . . . . . . 5052 1 89 . 1 1 15 15 LYS H H 1 8.651 0.01 . 1 . . . . . . . . . 5052 1 90 . 1 1 15 15 LYS HA H 1 4.548 0.01 . 1 . . . . . . . . . 5052 1 91 . 1 1 15 15 LYS HB2 H 1 1.608 0.01 . 1 . . . . . . . . . 5052 1 92 . 1 1 15 15 LYS HB3 H 1 1.428 0.01 . 1 . . . . . . . . . 5052 1 93 . 1 1 15 15 LYS HG2 H 1 1.105 0.01 . 1 . . . . . . . . . 5052 1 94 . 1 1 15 15 LYS HG3 H 1 1.105 0.01 . 1 . . . . . . . . . 5052 1 95 . 1 1 16 16 THR H H 1 8.608 0.01 . 1 . . . . . . . . . 5052 1 96 . 1 1 16 16 THR HA H 1 4.286 0.01 . 1 . . . . . . . . . 5052 1 97 . 1 1 16 16 THR HB H 1 3.916 0.01 . 1 . . . . . . . . . 5052 1 98 . 1 1 16 16 THR HG21 H 1 1.101 0.01 . 1 . . . . . . . . . 5052 1 99 . 1 1 16 16 THR HG22 H 1 1.101 0.01 . 1 . . . . . . . . . 5052 1 100 . 1 1 16 16 THR HG23 H 1 1.101 0.01 . 1 . . . . . . . . . 5052 1 101 . 1 1 17 17 CYS H H 1 8.637 0.01 . 1 . . . . . . . . . 5052 1 102 . 1 1 17 17 CYS HA H 1 4.743 0.01 . 1 . . . . . . . . . 5052 1 103 . 1 1 17 17 CYS HB2 H 1 3.350 0.01 . 1 . . . . . . . . . 5052 1 104 . 1 1 17 17 CYS HB3 H 1 2.751 0.01 . 1 . . . . . . . . . 5052 1 105 . 1 1 18 18 SER H H 1 8.734 0.01 . 1 . . . . . . . . . 5052 1 106 . 1 1 18 18 SER HA H 1 4.380 0.01 . 1 . . . . . . . . . 5052 1 107 . 1 1 18 18 SER HB2 H 1 3.703 0.01 . 2 . . . . . . . . . 5052 1 108 . 1 1 18 18 SER HB3 H 1 3.769 0.01 . 2 . . . . . . . . . 5052 1 109 . 1 1 19 19 GLY H H 1 8.556 0.01 . 1 . . . . . . . . . 5052 1 110 . 1 1 19 19 GLY HA2 H 1 3.651 0.01 . 2 . . . . . . . . . 5052 1 111 . 1 1 19 19 GLY HA3 H 1 3.979 0.01 . 2 . . . . . . . . . 5052 1 112 . 1 1 20 20 GLU H H 1 7.531 0.01 . 1 . . . . . . . . . 5052 1 113 . 1 1 20 20 GLU HA H 1 4.568 0.01 . 1 . . . . . . . . . 5052 1 114 . 1 1 20 20 GLU HB2 H 1 2.125 0.01 . 1 . . . . . . . . . 5052 1 115 . 1 1 20 20 GLU HB3 H 1 1.813 0.01 . 1 . . . . . . . . . 5052 1 116 . 1 1 20 20 GLU HG2 H 1 2.272 0.01 . 1 . . . . . . . . . 5052 1 117 . 1 1 20 20 GLU HG3 H 1 2.272 0.01 . 1 . . . . . . . . . 5052 1 118 . 1 1 21 21 THR H H 1 8.569 0.01 . 1 . . . . . . . . . 5052 1 119 . 1 1 21 21 THR HA H 1 4.279 0.01 . 1 . . . . . . . . . 5052 1 120 . 1 1 21 21 THR HB H 1 4.279 0.01 . 1 . . . . . . . . . 5052 1 121 . 1 1 21 21 THR HG21 H 1 1.039 0.01 . 1 . . . . . . . . . 5052 1 122 . 1 1 21 21 THR HG22 H 1 1.039 0.01 . 1 . . . . . . . . . 5052 1 123 . 1 1 21 21 THR HG23 H 1 1.039 0.01 . 1 . . . . . . . . . 5052 1 124 . 1 1 22 22 ASN H H 1 7.557 0.01 . 1 . . . . . . . . . 5052 1 125 . 1 1 22 22 ASN HA H 1 5.328 0.01 . 1 . . . . . . . . . 5052 1 126 . 1 1 22 22 ASN HB2 H 1 2.592 0.01 . 1 . . . . . . . . . 5052 1 127 . 1 1 22 22 ASN HB3 H 1 2.236 0.01 . 1 . . . . . . . . . 5052 1 128 . 1 1 22 22 ASN HD21 H 1 7.071 0.01 . 1 . . . . . . . . . 5052 1 129 . 1 1 22 22 ASN HD22 H 1 6.681 0.01 . 1 . . . . . . . . . 5052 1 130 . 1 1 23 23 CYS H H 1 9.182 0.01 . 1 . . . . . . . . . 5052 1 131 . 1 1 23 23 CYS HA H 1 5.512 0.01 . 1 . . . . . . . . . 5052 1 132 . 1 1 23 23 CYS HB2 H 1 3.168 0.01 . 1 . . . . . . . . . 5052 1 133 . 1 1 23 23 CYS HB3 H 1 2.644 0.01 . 1 . . . . . . . . . 5052 1 134 . 1 1 24 24 TYR H H 1 8.632 0.01 . 1 . . . . . . . . . 5052 1 135 . 1 1 24 24 TYR HA H 1 6.116 0.01 . 1 . . . . . . . . . 5052 1 136 . 1 1 24 24 TYR HB2 H 1 3.720 0.01 . 1 . . . . . . . . . 5052 1 137 . 1 1 24 24 TYR HB3 H 1 2.865 0.01 . 1 . . . . . . . . . 5052 1 138 . 1 1 24 24 TYR HD1 H 1 6.600 0.01 . 3 . . . . . . . . . 5052 1 139 . 1 1 25 25 LYS H H 1 9.032 0.01 . 1 . . . . . . . . . 5052 1 140 . 1 1 25 25 LYS HA H 1 5.020 0.01 . 1 . . . . . . . . . 5052 1 141 . 1 1 25 25 LYS HB2 H 1 1.897 0.01 . 1 . . . . . . . . . 5052 1 142 . 1 1 25 25 LYS HB3 H 1 1.473 0.01 . 1 . . . . . . . . . 5052 1 143 . 1 1 25 25 LYS HG2 H 1 1.178 0.01 . 1 . . . . . . . . . 5052 1 144 . 1 1 25 25 LYS HG3 H 1 1.178 0.01 . 1 . . . . . . . . . 5052 1 145 . 1 1 25 25 LYS HD2 H 1 1.308 0.01 . 1 . . . . . . . . . 5052 1 146 . 1 1 25 25 LYS HD3 H 1 1.308 0.01 . 1 . . . . . . . . . 5052 1 147 . 1 1 26 26 LYS H H 1 9.908 0.01 . 1 . . . . . . . . . 5052 1 148 . 1 1 26 26 LYS HA H 1 5.866 0.01 . 1 . . . . . . . . . 5052 1 149 . 1 1 26 26 LYS HB2 H 1 1.896 0.01 . 1 . . . . . . . . . 5052 1 150 . 1 1 26 26 LYS HB3 H 1 1.841 0.01 . 1 . . . . . . . . . 5052 1 151 . 1 1 26 26 LYS HG2 H 1 1.463 0.01 . 1 . . . . . . . . . 5052 1 152 . 1 1 26 26 LYS HG3 H 1 1.463 0.01 . 1 . . . . . . . . . 5052 1 153 . 1 1 26 26 LYS HE2 H 1 2.629 0.01 . 1 . . . . . . . . . 5052 1 154 . 1 1 26 26 LYS HE3 H 1 2.629 0.01 . 1 . . . . . . . . . 5052 1 155 . 1 1 27 27 TRP H H 1 9.014 0.01 . 1 . . . . . . . . . 5052 1 156 . 1 1 27 27 TRP HA H 1 6.087 0.01 . 1 . . . . . . . . . 5052 1 157 . 1 1 27 27 TRP HB2 H 1 3.179 0.01 . 1 . . . . . . . . . 5052 1 158 . 1 1 27 27 TRP HB3 H 1 3.019 0.01 . 1 . . . . . . . . . 5052 1 159 . 1 1 27 27 TRP HD1 H 1 6.932 0.01 . 1 . . . . . . . . . 5052 1 160 . 1 1 27 27 TRP HE1 H 1 10.264 0.01 . 1 . . . . . . . . . 5052 1 161 . 1 1 27 27 TRP HE3 H 1 7.039 0.01 . 1 . . . . . . . . . 5052 1 162 . 1 1 27 27 TRP HZ3 H 1 6.744 0.01 . 1 . . . . . . . . . 5052 1 163 . 1 1 27 27 TRP HH2 H 1 7.027 0.01 . 1 . . . . . . . . . 5052 1 164 . 1 1 27 27 TRP HZ2 H 1 7.307 0.01 . 1 . . . . . . . . . 5052 1 165 . 1 1 28 28 TRP H H 1 8.569 0.01 . 1 . . . . . . . . . 5052 1 166 . 1 1 28 28 TRP HA H 1 4.917 0.01 . 1 . . . . . . . . . 5052 1 167 . 1 1 28 28 TRP HB2 H 1 3.505 0.01 . 1 . . . . . . . . . 5052 1 168 . 1 1 28 28 TRP HB3 H 1 3.222 0.01 . 1 . . . . . . . . . 5052 1 169 . 1 1 28 28 TRP HD1 H 1 6.900 0.01 . 1 . . . . . . . . . 5052 1 170 . 1 1 28 28 TRP HE1 H 1 10.158 0.01 . 1 . . . . . . . . . 5052 1 171 . 1 1 28 28 TRP HE3 H 1 7.081 0.01 . 1 . . . . . . . . . 5052 1 172 . 1 1 28 28 TRP HZ3 H 1 6.588 0.01 . 1 . . . . . . . . . 5052 1 173 . 1 1 28 28 TRP HH2 H 1 6.972 0.01 . 1 . . . . . . . . . 5052 1 174 . 1 1 28 28 TRP HZ2 H 1 7.294 0.01 . 1 . . . . . . . . . 5052 1 175 . 1 1 29 29 SER H H 1 8.553 0.01 . 1 . . . . . . . . . 5052 1 176 . 1 1 29 29 SER HA H 1 5.106 0.01 . 1 . . . . . . . . . 5052 1 177 . 1 1 29 29 SER HB2 H 1 3.635 0.01 . 1 . . . . . . . . . 5052 1 178 . 1 1 29 29 SER HB3 H 1 3.750 0.01 . 1 . . . . . . . . . 5052 1 179 . 1 1 30 30 ASP H H 1 8.576 0.01 . 1 . . . . . . . . . 5052 1 180 . 1 1 30 30 ASP HA H 1 4.742 0.01 . 1 . . . . . . . . . 5052 1 181 . 1 1 30 30 ASP HB2 H 1 2.726 0.01 . 1 . . . . . . . . . 5052 1 182 . 1 1 30 30 ASP HB3 H 1 3.009 0.01 . 1 . . . . . . . . . 5052 1 183 . 1 1 31 31 HIS H H 1 8.783 0.01 . 1 . . . . . . . . . 5052 1 184 . 1 1 31 31 HIS HA H 1 4.257 0.01 . 1 . . . . . . . . . 5052 1 185 . 1 1 31 31 HIS HB2 H 1 3.218 0.01 . 1 . . . . . . . . . 5052 1 186 . 1 1 31 31 HIS HB3 H 1 3.270 0.01 . 1 . . . . . . . . . 5052 1 187 . 1 1 31 31 HIS HD2 H 1 7.209 0.01 . 1 . . . . . . . . . 5052 1 188 . 1 1 31 31 HIS HE1 H 1 8.513 0.01 . 1 . . . . . . . . . 5052 1 189 . 1 1 32 32 ARG H H 1 8.410 0.01 . 1 . . . . . . . . . 5052 1 190 . 1 1 32 32 ARG HA H 1 4.133 0.01 . 1 . . . . . . . . . 5052 1 191 . 1 1 32 32 ARG HB2 H 1 1.724 0.01 . 1 . . . . . . . . . 5052 1 192 . 1 1 32 32 ARG HB3 H 1 1.807 0.01 . 1 . . . . . . . . . 5052 1 193 . 1 1 32 32 ARG HG2 H 1 1.342 0.01 . 2 . . . . . . . . . 5052 1 194 . 1 1 32 32 ARG HG3 H 1 1.442 0.01 . 2 . . . . . . . . . 5052 1 195 . 1 1 32 32 ARG HD2 H 1 3.058 0.01 . 1 . . . . . . . . . 5052 1 196 . 1 1 32 32 ARG HD3 H 1 3.058 0.01 . 1 . . . . . . . . . 5052 1 197 . 1 1 32 32 ARG HE H 1 7.191 0.01 . 1 . . . . . . . . . 5052 1 198 . 1 1 33 33 GLY H H 1 7.770 0.01 . 1 . . . . . . . . . 5052 1 199 . 1 1 33 33 GLY HA2 H 1 3.844 0.01 . 2 . . . . . . . . . 5052 1 200 . 1 1 33 33 GLY HA3 H 1 4.092 0.01 . 2 . . . . . . . . . 5052 1 201 . 1 1 34 34 THR H H 1 8.315 0.01 . 1 . . . . . . . . . 5052 1 202 . 1 1 34 34 THR HA H 1 4.556 0.01 . 1 . . . . . . . . . 5052 1 203 . 1 1 34 34 THR HB H 1 3.689 0.01 . 1 . . . . . . . . . 5052 1 204 . 1 1 34 34 THR HG21 H 1 0.944 0.01 . 1 . . . . . . . . . 5052 1 205 . 1 1 34 34 THR HG22 H 1 0.944 0.01 . 1 . . . . . . . . . 5052 1 206 . 1 1 34 34 THR HG23 H 1 0.944 0.01 . 1 . . . . . . . . . 5052 1 207 . 1 1 35 35 ILE H H 1 8.558 0.01 . 1 . . . . . . . . . 5052 1 208 . 1 1 35 35 ILE HA H 1 3.800 0.01 . 1 . . . . . . . . . 5052 1 209 . 1 1 35 35 ILE HB H 1 0.010 0.01 . 1 . . . . . . . . . 5052 1 210 . 1 1 35 35 ILE HG12 H 1 0.928 0.01 . 2 . . . . . . . . . 5052 1 211 . 1 1 35 35 ILE HG13 H 1 0.653 0.01 . 2 . . . . . . . . . 5052 1 212 . 1 1 35 35 ILE HG21 H 1 0.190 0.01 . 1 . . . . . . . . . 5052 1 213 . 1 1 35 35 ILE HG22 H 1 0.190 0.01 . 1 . . . . . . . . . 5052 1 214 . 1 1 35 35 ILE HG23 H 1 0.190 0.01 . 1 . . . . . . . . . 5052 1 215 . 1 1 35 35 ILE HD11 H 1 0.446 0.01 . 1 . . . . . . . . . 5052 1 216 . 1 1 35 35 ILE HD12 H 1 0.446 0.01 . 1 . . . . . . . . . 5052 1 217 . 1 1 35 35 ILE HD13 H 1 0.446 0.01 . 1 . . . . . . . . . 5052 1 218 . 1 1 36 36 ILE H H 1 7.441 0.01 . 1 . . . . . . . . . 5052 1 219 . 1 1 36 36 ILE HA H 1 5.027 0.01 . 1 . . . . . . . . . 5052 1 220 . 1 1 36 36 ILE HB H 1 1.345 0.01 . 1 . . . . . . . . . 5052 1 221 . 1 1 36 36 ILE HG12 H 1 1.264 0.01 . 1 . . . . . . . . . 5052 1 222 . 1 1 36 36 ILE HG13 H 1 1.264 0.01 . 1 . . . . . . . . . 5052 1 223 . 1 1 36 36 ILE HG21 H 1 0.708 0.01 . 1 . . . . . . . . . 5052 1 224 . 1 1 36 36 ILE HG22 H 1 0.708 0.01 . 1 . . . . . . . . . 5052 1 225 . 1 1 36 36 ILE HG23 H 1 0.708 0.01 . 1 . . . . . . . . . 5052 1 226 . 1 1 36 36 ILE HD11 H 1 0.498 0.01 . 1 . . . . . . . . . 5052 1 227 . 1 1 36 36 ILE HD12 H 1 0.498 0.01 . 1 . . . . . . . . . 5052 1 228 . 1 1 36 36 ILE HD13 H 1 0.498 0.01 . 1 . . . . . . . . . 5052 1 229 . 1 1 37 37 GLU H H 1 9.768 0.01 . 1 . . . . . . . . . 5052 1 230 . 1 1 37 37 GLU HA H 1 4.828 0.01 . 1 . . . . . . . . . 5052 1 231 . 1 1 37 37 GLU HB2 H 1 2.033 0.01 . 1 . . . . . . . . . 5052 1 232 . 1 1 37 37 GLU HB3 H 1 2.290 0.01 . 1 . . . . . . . . . 5052 1 233 . 1 1 37 37 GLU HG2 H 1 2.381 0.01 . 2 . . . . . . . . . 5052 1 234 . 1 1 37 37 GLU HG3 H 1 2.448 0.01 . 2 . . . . . . . . . 5052 1 235 . 1 1 38 38 ARG H H 1 8.601 0.01 . 1 . . . . . . . . . 5052 1 236 . 1 1 38 38 ARG HA H 1 4.721 0.01 . 1 . . . . . . . . . 5052 1 237 . 1 1 38 38 ARG HB2 H 1 1.301 0.01 . 1 . . . . . . . . . 5052 1 238 . 1 1 38 38 ARG HB3 H 1 1.443 0.01 . 1 . . . . . . . . . 5052 1 239 . 1 1 38 38 ARG HG2 H 1 1.015 0.01 . 1 . . . . . . . . . 5052 1 240 . 1 1 38 38 ARG HG3 H 1 1.015 0.01 . 1 . . . . . . . . . 5052 1 241 . 1 1 38 38 ARG HD2 H 1 2.935 0.01 . 1 . . . . . . . . . 5052 1 242 . 1 1 38 38 ARG HD3 H 1 2.935 0.01 . 1 . . . . . . . . . 5052 1 243 . 1 1 38 38 ARG HE H 1 6.890 0.01 . 1 . . . . . . . . . 5052 1 244 . 1 1 39 39 GLY H H 1 6.138 0.01 . 1 . . . . . . . . . 5052 1 245 . 1 1 39 39 GLY HA2 H 1 3.665 0.01 . 2 . . . . . . . . . 5052 1 246 . 1 1 39 39 GLY HA3 H 1 3.730 0.01 . 2 . . . . . . . . . 5052 1 247 . 1 1 40 40 CYS H H 1 8.639 0.01 . 1 . . . . . . . . . 5052 1 248 . 1 1 40 40 CYS HA H 1 5.073 0.01 . 1 . . . . . . . . . 5052 1 249 . 1 1 40 40 CYS HB2 H 1 2.814 0.01 . 1 . . . . . . . . . 5052 1 250 . 1 1 40 40 CYS HB3 H 1 3.020 0.01 . 1 . . . . . . . . . 5052 1 251 . 1 1 41 41 GLY H H 1 9.145 0.01 . 1 . . . . . . . . . 5052 1 252 . 1 1 41 41 GLY HA2 H 1 3.601 0.01 . 2 . . . . . . . . . 5052 1 253 . 1 1 41 41 GLY HA3 H 1 4.144 0.01 . 2 . . . . . . . . . 5052 1 254 . 1 1 42 42 CYS H H 1 7.959 0.01 . 1 . . . . . . . . . 5052 1 255 . 1 1 42 42 CYS HA H 1 4.988 0.01 . 1 . . . . . . . . . 5052 1 256 . 1 1 42 42 CYS HB2 H 1 2.485 0.01 . 1 . . . . . . . . . 5052 1 257 . 1 1 42 42 CYS HB3 H 1 2.736 0.01 . 1 . . . . . . . . . 5052 1 258 . 1 1 43 43 PRO HA H 1 4.161 0.01 . 1 . . . . . . . . . 5052 1 259 . 1 1 43 43 PRO HB2 H 1 1.510 0.01 . 1 . . . . . . . . . 5052 1 260 . 1 1 43 43 PRO HB3 H 1 1.750 0.01 . 1 . . . . . . . . . 5052 1 261 . 1 1 43 43 PRO HG2 H 1 0.653 0.01 . 2 . . . . . . . . . 5052 1 262 . 1 1 43 43 PRO HG3 H 1 0.909 0.01 . 2 . . . . . . . . . 5052 1 263 . 1 1 43 43 PRO HD2 H 1 2.662 0.01 . 2 . . . . . . . . . 5052 1 264 . 1 1 43 43 PRO HD3 H 1 2.841 0.01 . 2 . . . . . . . . . 5052 1 265 . 1 1 44 44 LYS H H 1 7.726 0.01 . 1 . . . . . . . . . 5052 1 266 . 1 1 44 44 LYS HA H 1 4.066 0.01 . 1 . . . . . . . . . 5052 1 267 . 1 1 44 44 LYS HB2 H 1 1.472 0.01 . 1 . . . . . . . . . 5052 1 268 . 1 1 44 44 LYS HB3 H 1 1.531 0.01 . 1 . . . . . . . . . 5052 1 269 . 1 1 44 44 LYS HG2 H 1 1.215 0.01 . 2 . . . . . . . . . 5052 1 270 . 1 1 44 44 LYS HG3 H 1 1.312 0.01 . 2 . . . . . . . . . 5052 1 271 . 1 1 45 45 VAL H H 1 8.115 0.01 . 1 . . . . . . . . . 5052 1 272 . 1 1 45 45 VAL HA H 1 4.297 0.01 . 1 . . . . . . . . . 5052 1 273 . 1 1 45 45 VAL HB H 1 1.886 0.01 . 1 . . . . . . . . . 5052 1 274 . 1 1 45 45 VAL HG21 H 1 0.577 0.01 . 2 . . . . . . . . . 5052 1 275 . 1 1 45 45 VAL HG22 H 1 0.577 0.01 . 2 . . . . . . . . . 5052 1 276 . 1 1 45 45 VAL HG23 H 1 0.577 0.01 . 2 . . . . . . . . . 5052 1 277 . 1 1 46 46 LYS H H 1 7.839 0.01 . 1 . . . . . . . . . 5052 1 278 . 1 1 46 46 LYS HA H 1 4.301 0.01 . 1 . . . . . . . . . 5052 1 279 . 1 1 46 46 LYS HB2 H 1 1.571 0.01 . 1 . . . . . . . . . 5052 1 280 . 1 1 46 46 LYS HB3 H 1 1.347 0.01 . 1 . . . . . . . . . 5052 1 281 . 1 1 46 46 LYS HG2 H 1 1.386 0.01 . 2 . . . . . . . . . 5052 1 282 . 1 1 46 46 LYS HG3 H 1 1.216 0.01 . 2 . . . . . . . . . 5052 1 283 . 1 1 47 47 PRO HA H 1 4.140 0.01 . 1 . . . . . . . . . 5052 1 284 . 1 1 47 47 PRO HB2 H 1 2.144 0.01 . 1 . . . . . . . . . 5052 1 285 . 1 1 47 47 PRO HB3 H 1 1.943 0.01 . 1 . . . . . . . . . 5052 1 286 . 1 1 47 47 PRO HG2 H 1 1.823 0.01 . 2 . . . . . . . . . 5052 1 287 . 1 1 47 47 PRO HG3 H 1 1.645 0.01 . 2 . . . . . . . . . 5052 1 288 . 1 1 47 47 PRO HD2 H 1 3.368 0.01 . 2 . . . . . . . . . 5052 1 289 . 1 1 47 47 PRO HD3 H 1 3.641 0.01 . 2 . . . . . . . . . 5052 1 290 . 1 1 48 48 GLY H H 1 8.560 0.01 . 1 . . . . . . . . . 5052 1 291 . 1 1 48 48 GLY HA2 H 1 4.103 0.01 . 2 . . . . . . . . . 5052 1 292 . 1 1 48 48 GLY HA3 H 1 3.439 0.01 . 2 . . . . . . . . . 5052 1 293 . 1 1 49 49 VAL H H 1 7.483 0.01 . 1 . . . . . . . . . 5052 1 294 . 1 1 49 49 VAL HA H 1 3.939 0.01 . 1 . . . . . . . . . 5052 1 295 . 1 1 49 49 VAL HB H 1 1.885 0.01 . 1 . . . . . . . . . 5052 1 296 . 1 1 49 49 VAL HG21 H 1 0.697 0.01 . 2 . . . . . . . . . 5052 1 297 . 1 1 49 49 VAL HG22 H 1 0.697 0.01 . 2 . . . . . . . . . 5052 1 298 . 1 1 49 49 VAL HG23 H 1 0.697 0.01 . 2 . . . . . . . . . 5052 1 299 . 1 1 50 50 ASN H H 1 8.166 0.01 . 1 . . . . . . . . . 5052 1 300 . 1 1 50 50 ASN HA H 1 4.167 0.01 . 1 . . . . . . . . . 5052 1 301 . 1 1 50 50 ASN HB2 H 1 0.643 0.01 . 1 . . . . . . . . . 5052 1 302 . 1 1 50 50 ASN HB3 H 1 0.544 0.01 . 1 . . . . . . . . . 5052 1 303 . 1 1 50 50 ASN HD21 H 1 5.924 0.01 . 1 . . . . . . . . . 5052 1 304 . 1 1 50 50 ASN HD22 H 1 6.871 0.01 . 1 . . . . . . . . . 5052 1 305 . 1 1 51 51 LEU H H 1 8.064 0.01 . 1 . . . . . . . . . 5052 1 306 . 1 1 51 51 LEU HA H 1 5.130 0.01 . 1 . . . . . . . . . 5052 1 307 . 1 1 51 51 LEU HB2 H 1 1.536 0.01 . 1 . . . . . . . . . 5052 1 308 . 1 1 51 51 LEU HB3 H 1 1.536 0.01 . 1 . . . . . . . . . 5052 1 309 . 1 1 51 51 LEU HG H 1 1.315 0.01 . 1 . . . . . . . . . 5052 1 310 . 1 1 51 51 LEU HD11 H 1 0.748 0.01 . 2 . . . . . . . . . 5052 1 311 . 1 1 51 51 LEU HD12 H 1 0.748 0.01 . 2 . . . . . . . . . 5052 1 312 . 1 1 51 51 LEU HD13 H 1 0.748 0.01 . 2 . . . . . . . . . 5052 1 313 . 1 1 51 51 LEU HD21 H 1 1.109 0.01 . 2 . . . . . . . . . 5052 1 314 . 1 1 51 51 LEU HD22 H 1 1.109 0.01 . 2 . . . . . . . . . 5052 1 315 . 1 1 51 51 LEU HD23 H 1 1.109 0.01 . 2 . . . . . . . . . 5052 1 316 . 1 1 52 52 ASN H H 1 9.326 0.01 . 1 . . . . . . . . . 5052 1 317 . 1 1 52 52 ASN HA H 1 5.073 0.01 . 1 . . . . . . . . . 5052 1 318 . 1 1 52 52 ASN HB2 H 1 2.808 0.01 . 1 . . . . . . . . . 5052 1 319 . 1 1 52 52 ASN HB3 H 1 2.808 0.01 . 1 . . . . . . . . . 5052 1 320 . 1 1 52 52 ASN HD21 H 1 7.026 0.01 . 1 . . . . . . . . . 5052 1 321 . 1 1 52 52 ASN HD22 H 1 6.742 0.01 . 1 . . . . . . . . . 5052 1 322 . 1 1 53 53 CYS H H 1 8.966 0.01 . 1 . . . . . . . . . 5052 1 323 . 1 1 53 53 CYS HA H 1 5.764 0.01 . 1 . . . . . . . . . 5052 1 324 . 1 1 53 53 CYS HB2 H 1 3.300 0.01 . 1 . . . . . . . . . 5052 1 325 . 1 1 53 53 CYS HB3 H 1 3.068 0.01 . 1 . . . . . . . . . 5052 1 326 . 1 1 54 54 CYS H H 1 9.262 0.01 . 1 . . . . . . . . . 5052 1 327 . 1 1 54 54 CYS HA H 1 5.097 0.01 . 1 . . . . . . . . . 5052 1 328 . 1 1 54 54 CYS HB2 H 1 3.182 0.01 . 1 . . . . . . . . . 5052 1 329 . 1 1 54 54 CYS HB3 H 1 3.453 0.01 . 1 . . . . . . . . . 5052 1 330 . 1 1 55 55 ARG H H 1 8.771 0.01 . 1 . . . . . . . . . 5052 1 331 . 1 1 55 55 ARG HA H 1 4.901 0.01 . 1 . . . . . . . . . 5052 1 332 . 1 1 55 55 ARG HB2 H 1 1.700 0.01 . 1 . . . . . . . . . 5052 1 333 . 1 1 55 55 ARG HB3 H 1 2.085 0.01 . 1 . . . . . . . . . 5052 1 334 . 1 1 55 55 ARG HG2 H 1 1.459 0.01 . 2 . . . . . . . . . 5052 1 335 . 1 1 55 55 ARG HG3 H 1 1.640 0.01 . 2 . . . . . . . . . 5052 1 336 . 1 1 55 55 ARG HD2 H 1 3.116 0.01 . 1 . . . . . . . . . 5052 1 337 . 1 1 55 55 ARG HD3 H 1 3.116 0.01 . 1 . . . . . . . . . 5052 1 338 . 1 1 55 55 ARG HE H 1 7.074 0.01 . 1 . . . . . . . . . 5052 1 339 . 1 1 56 56 THR H H 1 7.346 0.01 . 1 . . . . . . . . . 5052 1 340 . 1 1 56 56 THR HA H 1 4.594 0.01 . 1 . . . . . . . . . 5052 1 341 . 1 1 56 56 THR HB H 1 4.176 0.01 . 1 . . . . . . . . . 5052 1 342 . 1 1 56 56 THR HG21 H 1 1.034 0.01 . 1 . . . . . . . . . 5052 1 343 . 1 1 56 56 THR HG22 H 1 1.034 0.01 . 1 . . . . . . . . . 5052 1 344 . 1 1 56 56 THR HG23 H 1 1.034 0.01 . 1 . . . . . . . . . 5052 1 345 . 1 1 57 57 ASP H H 1 8.304 0.01 . 1 . . . . . . . . . 5052 1 346 . 1 1 57 57 ASP HA H 1 4.534 0.01 . 1 . . . . . . . . . 5052 1 347 . 1 1 57 57 ASP HB2 H 1 2.424 0.01 . 1 . . . . . . . . . 5052 1 348 . 1 1 57 57 ASP HB3 H 1 2.267 0.01 . 1 . . . . . . . . . 5052 1 349 . 1 1 58 58 ARG H H 1 9.308 0.01 . 1 . . . . . . . . . 5052 1 350 . 1 1 58 58 ARG HA H 1 2.945 0.01 . 1 . . . . . . . . . 5052 1 351 . 1 1 58 58 ARG HB2 H 1 1.628 0.01 . 2 . . . . . . . . . 5052 1 352 . 1 1 58 58 ARG HB3 H 1 1.810 0.01 . 2 . . . . . . . . . 5052 1 353 . 1 1 58 58 ARG HG2 H 1 0.414 0.01 . 2 . . . . . . . . . 5052 1 354 . 1 1 58 58 ARG HG3 H 1 1.094 0.01 . 2 . . . . . . . . . 5052 1 355 . 1 1 58 58 ARG HD2 H 1 2.816 0.01 . 2 . . . . . . . . . 5052 1 356 . 1 1 58 58 ARG HD3 H 1 3.001 0.01 . 2 . . . . . . . . . 5052 1 357 . 1 1 58 58 ARG HE H 1 7.127 0.01 . 1 . . . . . . . . . 5052 1 358 . 1 1 59 59 CYS H H 1 7.596 0.01 . 1 . . . . . . . . . 5052 1 359 . 1 1 59 59 CYS HA H 1 4.300 0.01 . 1 . . . . . . . . . 5052 1 360 . 1 1 59 59 CYS HB2 H 1 3.224 0.01 . 2 . . . . . . . . . 5052 1 361 . 1 1 59 59 CYS HB3 H 1 3.673 0.01 . 2 . . . . . . . . . 5052 1 362 . 1 1 60 60 ASN H H 1 9.034 0.01 . 1 . . . . . . . . . 5052 1 363 . 1 1 60 60 ASN HA H 1 4.670 0.01 . 1 . . . . . . . . . 5052 1 364 . 1 1 60 60 ASN HB2 H 1 2.621 0.01 . 1 . . . . . . . . . 5052 1 365 . 1 1 60 60 ASN HB3 H 1 2.093 0.01 . 1 . . . . . . . . . 5052 1 366 . 1 1 60 60 ASN HD21 H 1 8.209 0.01 . 1 . . . . . . . . . 5052 1 367 . 1 1 60 60 ASN HD22 H 1 7.904 0.01 . 1 . . . . . . . . . 5052 1 368 . 1 1 61 61 ASN H H 1 7.475 0.01 . 1 . . . . . . . . . 5052 1 369 . 1 1 61 61 ASN HA H 1 3.897 0.01 . 1 . . . . . . . . . 5052 1 370 . 1 1 61 61 ASN HB2 H 1 2.312 0.01 . 2 . . . . . . . . . 5052 1 371 . 1 1 61 61 ASN HB3 H 1 2.381 0.01 . 2 . . . . . . . . . 5052 1 372 . 1 1 61 61 ASN HD21 H 1 7.370 0.01 . 1 . . . . . . . . . 5052 1 373 . 1 1 61 61 ASN HD22 H 1 6.492 0.01 . 1 . . . . . . . . . 5052 1 stop_ save_