data_5029 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5029 _Entry.Title ; Solution Structure of an Insect-specific Neurotoxin from the New World Scorpion Centruroides sculpturatus Ewing ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-05-22 _Entry.Accession_date 2001-05-22 _Entry.Last_release_date 2001-05-22 _Entry.Original_release_date 2001-05-22 _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 Michael Jablonsky . J. . . 5029 2 Patricia Jackson . L. . . 5029 3 N. Krishna . Rama . . 5029 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5029 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 384 5029 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 . . 2001-06-01 . original author 'original release' 5029 1 . . 2001-06-25 . update author 'update journal name in entry citation' 5029 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4279 'Solution Structure of a beta-Neurotoxin' 5029 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5029 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21338260 _Citation.DOI . _Citation.PubMed_ID 11444973 _Citation.Full_citation . _Citation.Title ; Solution Structure of an Insect-specific Neurotoxin from the New World Scorpion Centruroides sculpturatus Ewing(,) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 40 _Citation.Journal_issue 28 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 8273 _Citation.Page_last 8282 _Citation.Year 2001 _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 Michael Jablonsky . J. . . 5029 1 2 Patricia Jackson . L. . . 5029 1 3 N. Krishna . Rama . . 5029 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Neurotoxin 5029 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CsE-v5 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CsE-v5 _Assembly.Entry_ID 5029 _Assembly.ID 1 _Assembly.Name 'Centruroides sculpturatus Ewing, toxin variant 5' _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 5029 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 CsE-v5 1 $CsE-v5 . . . native . . . . . 5029 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 11 11 SG . 1 . 1 CYS 59 59 SG . . . . . . . . . . . . 5029 1 2 disulfide single . 1 . 1 CYS 15 15 SG . 1 . 1 CYS 35 35 SG . . . . . . . . . . . . 5029 1 3 disulfide single . 1 . 1 CYS 21 21 SG . 1 . 1 CYS 40 40 SG . . . . . . . . . . . . 5029 1 4 disulfide single . 1 . 1 CYS 25 25 SG . 1 . 1 CYS 42 42 SG . . . . . . . . . . . . 5029 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1I6F . . . . . 'average structure' 5029 1 yes PDB 1I6G . . . . . 'ensemble of 20 structures' 5029 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Centruroides sculpturatus Ewing, toxin variant 5' system 5029 1 CsE-v5 abbreviation 5029 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID neurotoxin 5029 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CsE-v5 _Entity.Sf_category entity _Entity.Sf_framecode CsE-v5 _Entity.Entry_ID 5029 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Centruroides sculpturatus Ewing variant 5' _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 ; KDGYPVDSKGCKLSCVANNY CDNQCKMKKASGGHCYAMSC YCEGLPENAKVSDSATNICG ; _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 60 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6354 _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 . no BMRB 5672 . 'Neurotoxin 5' . . . . . 100.00 60 98.33 98.33 1.96e-25 . . . . 5029 1 . no PDB 1I6F . 'Nmr Solution Structure Of The Insect-Specific Neurotoxin Variant 5 (Cse-V5) From The Scorpion Centruroides Sculpturatus Ewing' . . . . . 100.00 60 100.00 100.00 2.33e-26 . . . . 5029 1 . no PDB 1I6G . 'Nmr Solution Structure Of The Insect-Specific Neurotoxin Variant 5 (Cse-V5) From The Scorpion Centruroides Sculpturatus Ewing' . . . . . 100.00 60 100.00 100.00 2.33e-26 . . . . 5029 1 . no PDB 1NH5 . 'Automatic Assignment Of Nmr Data And Determination Of The Protein Structure Of A New World Scorpion Neurotoxin Using NoahDIAMOD' . . . . . 98.33 60 100.00 100.00 7.14e-26 . . . . 5029 1 . no PIR C23727 . 'neurotoxin V-5 - bark scorpion' . . . . . 98.33 59 100.00 100.00 8.23e-26 . . . . 5029 1 . no SWISS-PROT P58779 . 'Alpha-like toxin CsEv5 (CsE-v5) (CsE v5)' . . . . . 98.33 59 100.00 100.00 8.23e-26 . . . . 5029 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Centruroides sculpturatus Ewing variant 5' common 5029 1 CsE-v5 abbreviation 5029 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 . LYS . 5029 1 2 . ASP . 5029 1 3 . GLY . 5029 1 4 . TYR . 5029 1 5 . PRO . 5029 1 6 . VAL . 5029 1 7 . ASP . 5029 1 8 . SER . 5029 1 9 . LYS . 5029 1 10 . GLY . 5029 1 11 . CYS . 5029 1 12 . LYS . 5029 1 13 . LEU . 5029 1 14 . SER . 5029 1 15 . CYS . 5029 1 16 . VAL . 5029 1 17 . ALA . 5029 1 18 . ASN . 5029 1 19 . ASN . 5029 1 20 . TYR . 5029 1 21 . CYS . 5029 1 22 . ASP . 5029 1 23 . ASN . 5029 1 24 . GLN . 5029 1 25 . CYS . 5029 1 26 . LYS . 5029 1 27 . MET . 5029 1 28 . LYS . 5029 1 29 . LYS . 5029 1 30 . ALA . 5029 1 31 . SER . 5029 1 32 . GLY . 5029 1 33 . GLY . 5029 1 34 . HIS . 5029 1 35 . CYS . 5029 1 36 . TYR . 5029 1 37 . ALA . 5029 1 38 . MET . 5029 1 39 . SER . 5029 1 40 . CYS . 5029 1 41 . TYR . 5029 1 42 . CYS . 5029 1 43 . GLU . 5029 1 44 . GLY . 5029 1 45 . LEU . 5029 1 46 . PRO . 5029 1 47 . GLU . 5029 1 48 . ASN . 5029 1 49 . ALA . 5029 1 50 . LYS . 5029 1 51 . VAL . 5029 1 52 . SER . 5029 1 53 . ASP . 5029 1 54 . SER . 5029 1 55 . ALA . 5029 1 56 . THR . 5029 1 57 . ASN . 5029 1 58 . ILE . 5029 1 59 . CYS . 5029 1 60 . GLY . 5029 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 . LYS 1 1 5029 1 . ASP 2 2 5029 1 . GLY 3 3 5029 1 . TYR 4 4 5029 1 . PRO 5 5 5029 1 . VAL 6 6 5029 1 . ASP 7 7 5029 1 . SER 8 8 5029 1 . LYS 9 9 5029 1 . GLY 10 10 5029 1 . CYS 11 11 5029 1 . LYS 12 12 5029 1 . LEU 13 13 5029 1 . SER 14 14 5029 1 . CYS 15 15 5029 1 . VAL 16 16 5029 1 . ALA 17 17 5029 1 . ASN 18 18 5029 1 . ASN 19 19 5029 1 . TYR 20 20 5029 1 . CYS 21 21 5029 1 . ASP 22 22 5029 1 . ASN 23 23 5029 1 . GLN 24 24 5029 1 . CYS 25 25 5029 1 . LYS 26 26 5029 1 . MET 27 27 5029 1 . LYS 28 28 5029 1 . LYS 29 29 5029 1 . ALA 30 30 5029 1 . SER 31 31 5029 1 . GLY 32 32 5029 1 . GLY 33 33 5029 1 . HIS 34 34 5029 1 . CYS 35 35 5029 1 . TYR 36 36 5029 1 . ALA 37 37 5029 1 . MET 38 38 5029 1 . SER 39 39 5029 1 . CYS 40 40 5029 1 . TYR 41 41 5029 1 . CYS 42 42 5029 1 . GLU 43 43 5029 1 . GLY 44 44 5029 1 . LEU 45 45 5029 1 . PRO 46 46 5029 1 . GLU 47 47 5029 1 . ASN 48 48 5029 1 . ALA 49 49 5029 1 . LYS 50 50 5029 1 . VAL 51 51 5029 1 . SER 52 52 5029 1 . ASP 53 53 5029 1 . SER 54 54 5029 1 . ALA 55 55 5029 1 . THR 56 56 5029 1 . ASN 57 57 5029 1 . ILE 58 58 5029 1 . CYS 59 59 5029 1 . GLY 60 60 5029 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 5029 _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 $CsE-v5 . 6879 organism . 'Centruroides exilicauda' 'bark scorpion' . . Eukaryota Metazoa Centruroides exilicauda . Ewing . . . . . . . . . . . 5029 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 5029 _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 $CsE-v5 . 'purified from the natural source' . . . . . . . . . . . . . . . . 5029 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5029 _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 'Centruroides sculpturatus Ewing variant 5' . . . 1 $CsE-v5 . . 1.0 . . mM . . . . 5029 1 stop_ save_ ####################### # Sample conditions # ####################### save_Expt_Con _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Expt_Con _Sample_condition_list.Entry_ID 5029 _Sample_condition_list.ID 1 _Sample_condition_list.Details '1 hr. equilibration.' 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 0.1 n/a 5029 1 temperature 303 1 K 5029 1 stop_ save_ ############################ # Computer software used # ############################ save_felix _Software.Sf_category software _Software.Sf_framecode felix _Software.Entry_ID 5029 _Software.ID 1 _Software.Type . _Software.Name felix _Software.Version 9.80 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignments 5029 1 processing 5029 1 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 5029 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Am _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 5029 _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 Am . 600 . . . 5029 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 5029 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-1H NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $Expt_Con . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5029 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 5029 _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 TSP 'methyl protons' . . . . ppm 0 external direct 1.0 external cylindrical parallel . . 5029 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 5029 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Expt_Con _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-1H NOESY' 1 $sample_1 . 5029 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 LYS HA H 1 4.08 0.02 . 1 . . . . . . . . . 5029 1 2 . 1 1 1 1 LYS HB2 H 1 1.78 0.02 . 1 . . . . . . . . . 5029 1 3 . 1 1 1 1 LYS HB3 H 1 1.90 0.02 . 1 . . . . . . . . . 5029 1 4 . 1 1 1 1 LYS HG2 H 1 1.07 0.02 . 1 . . . . . . . . . 5029 1 5 . 1 1 1 1 LYS HG3 H 1 1.09 0.02 . 1 . . . . . . . . . 5029 1 6 . 1 1 1 1 LYS HD2 H 1 1.69 0.02 . 1 . . . . . . . . . 5029 1 7 . 1 1 1 1 LYS HD3 H 1 1.79 0.02 . 1 . . . . . . . . . 5029 1 8 . 1 1 1 1 LYS HE2 H 1 2.77 0.02 . 1 . . . . . . . . . 5029 1 9 . 1 1 1 1 LYS HE3 H 1 3.04 0.02 . 1 . . . . . . . . . 5029 1 10 . 1 1 1 1 LYS HZ1 H 1 7.58 0.02 . 1 . . . . . . . . . 5029 1 11 . 1 1 1 1 LYS HZ2 H 1 7.58 0.02 . 1 . . . . . . . . . 5029 1 12 . 1 1 1 1 LYS HZ3 H 1 7.58 0.02 . 1 . . . . . . . . . 5029 1 13 . 1 1 2 2 ASP H H 1 9.02 0.02 . 1 . . . . . . . . . 5029 1 14 . 1 1 2 2 ASP HA H 1 5.43 0.02 . 1 . . . . . . . . . 5029 1 15 . 1 1 2 2 ASP HB2 H 1 2.67 0.02 . 1 . . . . . . . . . 5029 1 16 . 1 1 2 2 ASP HB3 H 1 2.85 0.02 . 1 . . . . . . . . . 5029 1 17 . 1 1 3 3 GLY H H 1 7.91 0.02 . 1 . . . . . . . . . 5029 1 18 . 1 1 3 3 GLY HA2 H 1 3.49 0.02 . 1 . . . . . . . . . 5029 1 19 . 1 1 3 3 GLY HA3 H 1 3.99 0.02 . 1 . . . . . . . . . 5029 1 20 . 1 1 4 4 TYR H H 1 8.94 0.02 . 1 . . . . . . . . . 5029 1 21 . 1 1 4 4 TYR HA H 1 5.44 0.02 . 1 . . . . . . . . . 5029 1 22 . 1 1 4 4 TYR HB2 H 1 3.21 0.02 . 1 . . . . . . . . . 5029 1 23 . 1 1 4 4 TYR HB3 H 1 3.07 0.02 . 1 . . . . . . . . . 5029 1 24 . 1 1 4 4 TYR HD1 H 1 7.43 0.02 . 1 . . . . . . . . . 5029 1 25 . 1 1 4 4 TYR HD2 H 1 7.43 0.02 . 1 . . . . . . . . . 5029 1 26 . 1 1 4 4 TYR HE1 H 1 7.09 0.02 . 1 . . . . . . . . . 5029 1 27 . 1 1 4 4 TYR HE2 H 1 7.09 0.02 . 1 . . . . . . . . . 5029 1 28 . 1 1 5 5 PRO HA H 1 4.86 0.02 . 1 . . . . . . . . . 5029 1 29 . 1 1 5 5 PRO HB2 H 1 1.98 0.02 . 1 . . . . . . . . . 5029 1 30 . 1 1 5 5 PRO HB3 H 1 2.09 0.02 . 1 . . . . . . . . . 5029 1 31 . 1 1 5 5 PRO HG2 H 1 1.84 0.02 . 1 . . . . . . . . . 5029 1 32 . 1 1 5 5 PRO HG3 H 1 1.84 0.02 . 1 . . . . . . . . . 5029 1 33 . 1 1 5 5 PRO HD2 H 1 3.75 0.02 . 1 . . . . . . . . . 5029 1 34 . 1 1 5 5 PRO HD3 H 1 4.53 0.02 . 1 . . . . . . . . . 5029 1 35 . 1 1 6 6 VAL H H 1 7.25 0.02 . 1 . . . . . . . . . 5029 1 36 . 1 1 6 6 VAL HA H 1 5.20 0.02 . 1 . . . . . . . . . 5029 1 37 . 1 1 6 6 VAL HB H 1 1.71 0.02 . 1 . . . . . . . . . 5029 1 38 . 1 1 6 6 VAL HG11 H 1 0.65 0.02 . 1 . . . . . . . . . 5029 1 39 . 1 1 6 6 VAL HG12 H 1 0.65 0.02 . 1 . . . . . . . . . 5029 1 40 . 1 1 6 6 VAL HG13 H 1 0.65 0.02 . 1 . . . . . . . . . 5029 1 41 . 1 1 6 6 VAL HG21 H 1 0.69 0.02 . 1 . . . . . . . . . 5029 1 42 . 1 1 6 6 VAL HG22 H 1 0.69 0.02 . 1 . . . . . . . . . 5029 1 43 . 1 1 6 6 VAL HG23 H 1 0.69 0.02 . 1 . . . . . . . . . 5029 1 44 . 1 1 7 7 ASP H H 1 8.54 0.02 . 1 . . . . . . . . . 5029 1 45 . 1 1 7 7 ASP HA H 1 4.67 0.02 . 1 . . . . . . . . . 5029 1 46 . 1 1 7 7 ASP HB2 H 1 3.35 0.02 . 1 . . . . . . . . . 5029 1 47 . 1 1 7 7 ASP HB3 H 1 2.68 0.02 . 1 . . . . . . . . . 5029 1 48 . 1 1 8 8 SER H H 1 8.40 0.02 . 1 . . . . . . . . . 5029 1 49 . 1 1 8 8 SER HA H 1 4.19 0.02 . 1 . . . . . . . . . 5029 1 50 . 1 1 8 8 SER HB2 H 1 3.98 0.02 . 1 . . . . . . . . . 5029 1 51 . 1 1 8 8 SER HB3 H 1 4.04 0.02 . 1 . . . . . . . . . 5029 1 52 . 1 1 9 9 LYS H H 1 8.15 0.02 . 1 . . . . . . . . . 5029 1 53 . 1 1 9 9 LYS HA H 1 4.49 0.02 . 1 . . . . . . . . . 5029 1 54 . 1 1 9 9 LYS HB2 H 1 1.95 0.02 . 1 . . . . . . . . . 5029 1 55 . 1 1 9 9 LYS HB3 H 1 2.01 0.02 . 1 . . . . . . . . . 5029 1 56 . 1 1 9 9 LYS HG2 H 1 1.38 0.02 . 1 . . . . . . . . . 5029 1 57 . 1 1 9 9 LYS HG3 H 1 1.45 0.02 . 1 . . . . . . . . . 5029 1 58 . 1 1 9 9 LYS HD2 H 1 1.67 0.02 . 1 . . . . . . . . . 5029 1 59 . 1 1 9 9 LYS HD3 H 1 1.67 0.02 . 1 . . . . . . . . . 5029 1 60 . 1 1 9 9 LYS HE2 H 1 2.97 0.02 . 1 . . . . . . . . . 5029 1 61 . 1 1 9 9 LYS HE3 H 1 2.97 0.02 . 1 . . . . . . . . . 5029 1 62 . 1 1 9 9 LYS HZ1 H 1 7.53 0.02 . 1 . . . . . . . . . 5029 1 63 . 1 1 9 9 LYS HZ2 H 1 7.53 0.02 . 1 . . . . . . . . . 5029 1 64 . 1 1 9 9 LYS HZ3 H 1 7.53 0.02 . 1 . . . . . . . . . 5029 1 65 . 1 1 10 10 GLY H H 1 8.07 0.02 . 1 . . . . . . . . . 5029 1 66 . 1 1 10 10 GLY HA2 H 1 4.28 0.02 . 1 . . . . . . . . . 5029 1 67 . 1 1 10 10 GLY HA3 H 1 3.54 0.02 . 1 . . . . . . . . . 5029 1 68 . 1 1 11 11 CYS H H 1 8.62 0.02 . 1 . . . . . . . . . 5029 1 69 . 1 1 11 11 CYS HA H 1 4.87 0.02 . 1 . . . . . . . . . 5029 1 70 . 1 1 11 11 CYS HB2 H 1 3.38 0.02 . 1 . . . . . . . . . 5029 1 71 . 1 1 11 11 CYS HB3 H 1 3.25 0.02 . 1 . . . . . . . . . 5029 1 72 . 1 1 12 12 LYS H H 1 8.44 0.02 . 1 . . . . . . . . . 5029 1 73 . 1 1 12 12 LYS HA H 1 4.65 0.02 . 1 . . . . . . . . . 5029 1 74 . 1 1 12 12 LYS HB2 H 1 1.63 0.02 . 1 . . . . . . . . . 5029 1 75 . 1 1 12 12 LYS HB3 H 1 2.19 0.02 . 1 . . . . . . . . . 5029 1 76 . 1 1 12 12 LYS HG2 H 1 1.63 0.02 . 1 . . . . . . . . . 5029 1 77 . 1 1 12 12 LYS HG3 H 1 1.63 0.02 . 1 . . . . . . . . . 5029 1 78 . 1 1 12 12 LYS HD2 H 1 1.38 0.02 . 1 . . . . . . . . . 5029 1 79 . 1 1 12 12 LYS HD3 H 1 1.40 0.02 . 1 . . . . . . . . . 5029 1 80 . 1 1 12 12 LYS HE2 H 1 2.65 0.02 . 1 . . . . . . . . . 5029 1 81 . 1 1 12 12 LYS HE3 H 1 2.75 0.02 . 1 . . . . . . . . . 5029 1 82 . 1 1 12 12 LYS HZ1 H 1 7.04 0.02 . 1 . . . . . . . . . 5029 1 83 . 1 1 12 12 LYS HZ2 H 1 7.04 0.02 . 1 . . . . . . . . . 5029 1 84 . 1 1 12 12 LYS HZ3 H 1 7.04 0.02 . 1 . . . . . . . . . 5029 1 85 . 1 1 13 13 LEU H H 1 9.36 0.02 . 1 . . . . . . . . . 5029 1 86 . 1 1 13 13 LEU HA H 1 4.51 0.02 . 1 . . . . . . . . . 5029 1 87 . 1 1 13 13 LEU HB2 H 1 1.70 0.02 . 1 . . . . . . . . . 5029 1 88 . 1 1 13 13 LEU HB3 H 1 1.84 0.02 . 1 . . . . . . . . . 5029 1 89 . 1 1 13 13 LEU HG H 1 1.84 0.02 . 1 . . . . . . . . . 5029 1 90 . 1 1 13 13 LEU HD11 H 1 0.83 0.02 . 1 . . . . . . . . . 5029 1 91 . 1 1 13 13 LEU HD12 H 1 0.83 0.02 . 1 . . . . . . . . . 5029 1 92 . 1 1 13 13 LEU HD13 H 1 0.83 0.02 . 1 . . . . . . . . . 5029 1 93 . 1 1 13 13 LEU HD21 H 1 0.86 0.02 . 1 . . . . . . . . . 5029 1 94 . 1 1 13 13 LEU HD22 H 1 0.86 0.02 . 1 . . . . . . . . . 5029 1 95 . 1 1 13 13 LEU HD23 H 1 0.86 0.02 . 1 . . . . . . . . . 5029 1 96 . 1 1 14 14 SER H H 1 8.28 0.02 . 1 . . . . . . . . . 5029 1 97 . 1 1 14 14 SER HA H 1 5.00 0.02 . 1 . . . . . . . . . 5029 1 98 . 1 1 14 14 SER HB2 H 1 3.89 0.02 . 1 . . . . . . . . . 5029 1 99 . 1 1 14 14 SER HB3 H 1 3.93 0.02 . 1 . . . . . . . . . 5029 1 100 . 1 1 15 15 CYS H H 1 8.14 0.02 . 1 . . . . . . . . . 5029 1 101 . 1 1 15 15 CYS HA H 1 4.75 0.02 . 1 . . . . . . . . . 5029 1 102 . 1 1 15 15 CYS HB2 H 1 3.20 0.02 . 1 . . . . . . . . . 5029 1 103 . 1 1 15 15 CYS HB3 H 1 3.25 0.02 . 1 . . . . . . . . . 5029 1 104 . 1 1 16 16 VAL H H 1 8.86 0.02 . 1 . . . . . . . . . 5029 1 105 . 1 1 16 16 VAL HA H 1 4.47 0.02 . 1 . . . . . . . . . 5029 1 106 . 1 1 16 16 VAL HB H 1 2.24 0.02 . 1 . . . . . . . . . 5029 1 107 . 1 1 16 16 VAL HG11 H 1 0.79 0.02 . 1 . . . . . . . . . 5029 1 108 . 1 1 16 16 VAL HG12 H 1 0.79 0.02 . 1 . . . . . . . . . 5029 1 109 . 1 1 16 16 VAL HG13 H 1 0.79 0.02 . 1 . . . . . . . . . 5029 1 110 . 1 1 16 16 VAL HG21 H 1 0.89 0.02 . 1 . . . . . . . . . 5029 1 111 . 1 1 16 16 VAL HG22 H 1 0.89 0.02 . 1 . . . . . . . . . 5029 1 112 . 1 1 16 16 VAL HG23 H 1 0.89 0.02 . 1 . . . . . . . . . 5029 1 113 . 1 1 17 17 ALA H H 1 7.70 0.02 . 1 . . . . . . . . . 5029 1 114 . 1 1 17 17 ALA HA H 1 4.93 0.02 . 1 . . . . . . . . . 5029 1 115 . 1 1 17 17 ALA HB1 H 1 1.59 0.02 . 1 . . . . . . . . . 5029 1 116 . 1 1 17 17 ALA HB2 H 1 1.59 0.02 . 1 . . . . . . . . . 5029 1 117 . 1 1 17 17 ALA HB3 H 1 1.59 0.02 . 1 . . . . . . . . . 5029 1 118 . 1 1 18 18 ASN H H 1 9.08 0.02 . 1 . . . . . . . . . 5029 1 119 . 1 1 18 18 ASN HA H 1 4.35 0.02 . 1 . . . . . . . . . 5029 1 120 . 1 1 18 18 ASN HB2 H 1 2.95 0.02 . 1 . . . . . . . . . 5029 1 121 . 1 1 18 18 ASN HB3 H 1 3.15 0.02 . 1 . . . . . . . . . 5029 1 122 . 1 1 18 18 ASN HD21 H 1 8.04 0.02 . 1 . . . . . . . . . 5029 1 123 . 1 1 18 18 ASN HD22 H 1 7.36 0.02 . 1 . . . . . . . . . 5029 1 124 . 1 1 19 19 ASN H H 1 9.23 0.02 . 1 . . . . . . . . . 5029 1 125 . 1 1 19 19 ASN HA H 1 4.42 0.02 . 1 . . . . . . . . . 5029 1 126 . 1 1 19 19 ASN HB2 H 1 2.93 0.02 . 1 . . . . . . . . . 5029 1 127 . 1 1 19 19 ASN HB3 H 1 2.98 0.02 . 1 . . . . . . . . . 5029 1 128 . 1 1 19 19 ASN HD21 H 1 7.75 0.02 . 1 . . . . . . . . . 5029 1 129 . 1 1 19 19 ASN HD22 H 1 6.98 0.02 . 1 . . . . . . . . . 5029 1 130 . 1 1 20 20 TYR H H 1 7.31 0.02 . 1 . . . . . . . . . 5029 1 131 . 1 1 20 20 TYR HA H 1 4.40 0.02 . 1 . . . . . . . . . 5029 1 132 . 1 1 20 20 TYR HB2 H 1 3.38 0.02 . 1 . . . . . . . . . 5029 1 133 . 1 1 20 20 TYR HB3 H 1 3.16 0.02 . 1 . . . . . . . . . 5029 1 134 . 1 1 20 20 TYR HD1 H 1 7.15 0.02 . 1 . . . . . . . . . 5029 1 135 . 1 1 20 20 TYR HD2 H 1 7.15 0.02 . 1 . . . . . . . . . 5029 1 136 . 1 1 20 20 TYR HE1 H 1 6.86 0.02 . 1 . . . . . . . . . 5029 1 137 . 1 1 20 20 TYR HE2 H 1 6.86 0.02 . 1 . . . . . . . . . 5029 1 138 . 1 1 21 21 CYS H H 1 7.04 0.02 . 1 . . . . . . . . . 5029 1 139 . 1 1 21 21 CYS HA H 1 4.20 0.02 . 1 . . . . . . . . . 5029 1 140 . 1 1 21 21 CYS HB2 H 1 2.43 0.02 . 1 . . . . . . . . . 5029 1 141 . 1 1 21 21 CYS HB3 H 1 2.62 0.02 . 1 . . . . . . . . . 5029 1 142 . 1 1 22 22 ASP H H 1 8.82 0.02 . 1 . . . . . . . . . 5029 1 143 . 1 1 22 22 ASP HA H 1 4.05 0.02 . 1 . . . . . . . . . 5029 1 144 . 1 1 22 22 ASP HB2 H 1 2.78 0.02 . 1 . . . . . . . . . 5029 1 145 . 1 1 22 22 ASP HB3 H 1 2.68 0.02 . 1 . . . . . . . . . 5029 1 146 . 1 1 23 23 ASN H H 1 7.65 0.02 . 1 . . . . . . . . . 5029 1 147 . 1 1 23 23 ASN HA H 1 4.35 0.02 . 1 . . . . . . . . . 5029 1 148 . 1 1 23 23 ASN HB2 H 1 2.72 0.02 . 1 . . . . . . . . . 5029 1 149 . 1 1 23 23 ASN HB3 H 1 2.90 0.02 . 1 . . . . . . . . . 5029 1 150 . 1 1 23 23 ASN HD21 H 1 7.71 0.02 . 1 . . . . . . . . . 5029 1 151 . 1 1 23 23 ASN HD22 H 1 6.97 0.02 . 1 . . . . . . . . . 5029 1 152 . 1 1 24 24 GLN H H 1 8.24 0.02 . 1 . . . . . . . . . 5029 1 153 . 1 1 24 24 GLN HA H 1 3.76 0.02 . 1 . . . . . . . . . 5029 1 154 . 1 1 24 24 GLN HB2 H 1 1.62 0.02 . 1 . . . . . . . . . 5029 1 155 . 1 1 24 24 GLN HB3 H 1 1.56 0.02 . 1 . . . . . . . . . 5029 1 156 . 1 1 24 24 GLN HG2 H 1 1.77 0.02 . 1 . . . . . . . . . 5029 1 157 . 1 1 24 24 GLN HG3 H 1 1.89 0.02 . 1 . . . . . . . . . 5029 1 158 . 1 1 25 25 CYS H H 1 8.87 0.02 . 1 . . . . . . . . . 5029 1 159 . 1 1 25 25 CYS HA H 1 4.98 0.02 . 1 . . . . . . . . . 5029 1 160 . 1 1 25 25 CYS HB2 H 1 2.68 0.02 . 1 . . . . . . . . . 5029 1 161 . 1 1 25 25 CYS HB3 H 1 2.56 0.02 . 1 . . . . . . . . . 5029 1 162 . 1 1 26 26 LYS H H 1 8.12 0.02 . 1 . . . . . . . . . 5029 1 163 . 1 1 26 26 LYS HA H 1 4.27 0.02 . 1 . . . . . . . . . 5029 1 164 . 1 1 26 26 LYS HB2 H 1 1.86 0.02 . 1 . . . . . . . . . 5029 1 165 . 1 1 26 26 LYS HB3 H 1 1.83 0.02 . 1 . . . . . . . . . 5029 1 166 . 1 1 26 26 LYS HG2 H 1 1.29 0.02 . 1 . . . . . . . . . 5029 1 167 . 1 1 26 26 LYS HG3 H 1 1.40 0.02 . 1 . . . . . . . . . 5029 1 168 . 1 1 26 26 LYS HD2 H 1 1.54 0.02 . 1 . . . . . . . . . 5029 1 169 . 1 1 26 26 LYS HD3 H 1 1.62 0.02 . 1 . . . . . . . . . 5029 1 170 . 1 1 26 26 LYS HE2 H 1 2.99 0.02 . 1 . . . . . . . . . 5029 1 171 . 1 1 26 26 LYS HE3 H 1 2.99 0.02 . 1 . . . . . . . . . 5029 1 172 . 1 1 27 27 MET H H 1 7.97 0.02 . 1 . . . . . . . . . 5029 1 173 . 1 1 27 27 MET HA H 1 4.24 0.02 . 1 . . . . . . . . . 5029 1 174 . 1 1 27 27 MET HB2 H 1 2.25 0.02 . 1 . . . . . . . . . 5029 1 175 . 1 1 27 27 MET HB3 H 1 2.18 0.02 . 1 . . . . . . . . . 5029 1 176 . 1 1 27 27 MET HG2 H 1 2.56 0.02 . 1 . . . . . . . . . 5029 1 177 . 1 1 27 27 MET HG3 H 1 2.71 0.02 . 1 . . . . . . . . . 5029 1 178 . 1 1 27 27 MET HE1 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 179 . 1 1 27 27 MET HE2 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 180 . 1 1 27 27 MET HE3 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 181 . 1 1 28 28 LYS H H 1 7.22 0.02 . 1 . . . . . . . . . 5029 1 182 . 1 1 28 28 LYS HA H 1 4.29 0.02 . 1 . . . . . . . . . 5029 1 183 . 1 1 28 28 LYS HB2 H 1 1.77 0.02 . 1 . . . . . . . . . 5029 1 184 . 1 1 28 28 LYS HB3 H 1 2.08 0.02 . 1 . . . . . . . . . 5029 1 185 . 1 1 28 28 LYS HG2 H 1 1.41 0.02 . 1 . . . . . . . . . 5029 1 186 . 1 1 28 28 LYS HG3 H 1 1.53 0.02 . 1 . . . . . . . . . 5029 1 187 . 1 1 28 28 LYS HD2 H 1 1.72 0.02 . 1 . . . . . . . . . 5029 1 188 . 1 1 28 28 LYS HD3 H 1 1.78 0.02 . 1 . . . . . . . . . 5029 1 189 . 1 1 28 28 LYS HE2 H 1 2.93 0.02 . 1 . . . . . . . . . 5029 1 190 . 1 1 28 28 LYS HE3 H 1 2.93 0.02 . 1 . . . . . . . . . 5029 1 191 . 1 1 28 28 LYS HZ1 H 1 7.78 0.02 . 1 . . . . . . . . . 5029 1 192 . 1 1 28 28 LYS HZ2 H 1 7.78 0.02 . 1 . . . . . . . . . 5029 1 193 . 1 1 28 28 LYS HZ3 H 1 7.78 0.02 . 1 . . . . . . . . . 5029 1 194 . 1 1 29 29 LYS H H 1 7.71 0.02 . 1 . . . . . . . . . 5029 1 195 . 1 1 29 29 LYS HA H 1 3.88 0.02 . 1 . . . . . . . . . 5029 1 196 . 1 1 29 29 LYS HB2 H 1 2.08 0.02 . 1 . . . . . . . . . 5029 1 197 . 1 1 29 29 LYS HB3 H 1 2.27 0.02 . 1 . . . . . . . . . 5029 1 198 . 1 1 29 29 LYS HG2 H 1 1.33 0.02 . 1 . . . . . . . . . 5029 1 199 . 1 1 29 29 LYS HG3 H 1 1.42 0.02 . 1 . . . . . . . . . 5029 1 200 . 1 1 29 29 LYS HD2 H 1 1.68 0.02 . 1 . . . . . . . . . 5029 1 201 . 1 1 29 29 LYS HD3 H 1 1.70 0.02 . 1 . . . . . . . . . 5029 1 202 . 1 1 29 29 LYS HE2 H 1 3.03 0.02 . 1 . . . . . . . . . 5029 1 203 . 1 1 29 29 LYS HE3 H 1 3.03 0.02 . 1 . . . . . . . . . 5029 1 204 . 1 1 29 29 LYS HZ1 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 205 . 1 1 29 29 LYS HZ2 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 206 . 1 1 29 29 LYS HZ3 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 207 . 1 1 30 30 ALA H H 1 7.83 0.02 . 1 . . . . . . . . . 5029 1 208 . 1 1 30 30 ALA HA H 1 4.76 0.02 . 1 . . . . . . . . . 5029 1 209 . 1 1 30 30 ALA HB1 H 1 1.27 0.02 . 1 . . . . . . . . . 5029 1 210 . 1 1 30 30 ALA HB2 H 1 1.27 0.02 . 1 . . . . . . . . . 5029 1 211 . 1 1 30 30 ALA HB3 H 1 1.27 0.02 . 1 . . . . . . . . . 5029 1 212 . 1 1 31 31 SER H H 1 8.50 0.02 . 1 . . . . . . . . . 5029 1 213 . 1 1 31 31 SER HA H 1 4.36 0.02 . 1 . . . . . . . . . 5029 1 214 . 1 1 31 31 SER HB2 H 1 3.86 0.02 . 1 . . . . . . . . . 5029 1 215 . 1 1 31 31 SER HB3 H 1 3.86 0.02 . 1 . . . . . . . . . 5029 1 216 . 1 1 32 32 GLY H H 1 7.56 0.02 . 1 . . . . . . . . . 5029 1 217 . 1 1 32 32 GLY HA2 H 1 3.97 0.02 . 1 . . . . . . . . . 5029 1 218 . 1 1 32 32 GLY HA3 H 1 4.28 0.02 . 1 . . . . . . . . . 5029 1 219 . 1 1 33 33 GLY H H 1 8.62 0.02 . 1 . . . . . . . . . 5029 1 220 . 1 1 33 33 GLY HA2 H 1 4.62 0.02 . 1 . . . . . . . . . 5029 1 221 . 1 1 33 33 GLY HA3 H 1 4.80 0.02 . 1 . . . . . . . . . 5029 1 222 . 1 1 34 34 HIS H H 1 8.95 0.02 . 1 . . . . . . . . . 5029 1 223 . 1 1 34 34 HIS HA H 1 4.69 0.02 . 1 . . . . . . . . . 5029 1 224 . 1 1 34 34 HIS HB2 H 1 2.44 0.02 . 1 . . . . . . . . . 5029 1 225 . 1 1 34 34 HIS HB3 H 1 2.47 0.02 . 1 . . . . . . . . . 5029 1 226 . 1 1 34 34 HIS HD2 H 1 7.03 0.02 . 1 . . . . . . . . . 5029 1 227 . 1 1 34 34 HIS HE1 H 1 8.43 0.02 . 1 . . . . . . . . . 5029 1 228 . 1 1 35 35 CYS H H 1 9.68 0.02 . 1 . . . . . . . . . 5029 1 229 . 1 1 35 35 CYS HA H 1 5.14 0.02 . 1 . . . . . . . . . 5029 1 230 . 1 1 35 35 CYS HB2 H 1 2.95 0.02 . 1 . . . . . . . . . 5029 1 231 . 1 1 35 35 CYS HB3 H 1 2.82 0.02 . 1 . . . . . . . . . 5029 1 232 . 1 1 36 36 TYR H H 1 9.18 0.02 . 1 . . . . . . . . . 5029 1 233 . 1 1 36 36 TYR HA H 1 5.17 0.02 . 1 . . . . . . . . . 5029 1 234 . 1 1 36 36 TYR HB2 H 1 3.18 0.02 . 1 . . . . . . . . . 5029 1 235 . 1 1 36 36 TYR HB3 H 1 2.90 0.02 . 1 . . . . . . . . . 5029 1 236 . 1 1 36 36 TYR HD1 H 1 7.00 0.02 . 1 . . . . . . . . . 5029 1 237 . 1 1 36 36 TYR HD2 H 1 7.00 0.02 . 1 . . . . . . . . . 5029 1 238 . 1 1 36 36 TYR HE1 H 1 6.54 0.02 . 1 . . . . . . . . . 5029 1 239 . 1 1 36 36 TYR HE2 H 1 6.54 0.02 . 1 . . . . . . . . . 5029 1 240 . 1 1 37 37 ALA H H 1 9.11 0.02 . 1 . . . . . . . . . 5029 1 241 . 1 1 37 37 ALA HA H 1 3.95 0.02 . 1 . . . . . . . . . 5029 1 242 . 1 1 37 37 ALA HB1 H 1 1.25 0.02 . 1 . . . . . . . . . 5029 1 243 . 1 1 37 37 ALA HB2 H 1 1.25 0.02 . 1 . . . . . . . . . 5029 1 244 . 1 1 37 37 ALA HB3 H 1 1.25 0.02 . 1 . . . . . . . . . 5029 1 245 . 1 1 38 38 MET H H 1 8.37 0.02 . 1 . . . . . . . . . 5029 1 246 . 1 1 38 38 MET HA H 1 4.09 0.02 . 1 . . . . . . . . . 5029 1 247 . 1 1 38 38 MET HB2 H 1 2.50 0.02 . 1 . . . . . . . . . 5029 1 248 . 1 1 38 38 MET HB3 H 1 2.59 0.02 . 1 . . . . . . . . . 5029 1 249 . 1 1 38 38 MET HE1 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 250 . 1 1 38 38 MET HE2 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 251 . 1 1 38 38 MET HE3 H 1 2.03 0.02 . 1 . . . . . . . . . 5029 1 252 . 1 1 39 39 SER H H 1 8.09 0.02 . 1 . . . . . . . . . 5029 1 253 . 1 1 39 39 SER HA H 1 5.74 0.02 . 1 . . . . . . . . . 5029 1 254 . 1 1 39 39 SER HB2 H 1 3.77 0.02 . 1 . . . . . . . . . 5029 1 255 . 1 1 39 39 SER HB3 H 1 3.89 0.02 . 1 . . . . . . . . . 5029 1 256 . 1 1 40 40 CYS H H 1 9.06 0.02 . 1 . . . . . . . . . 5029 1 257 . 1 1 40 40 CYS HA H 1 5.42 0.02 . 1 . . . . . . . . . 5029 1 258 . 1 1 40 40 CYS HB2 H 1 2.72 0.02 . 1 . . . . . . . . . 5029 1 259 . 1 1 40 40 CYS HB3 H 1 2.78 0.02 . 1 . . . . . . . . . 5029 1 260 . 1 1 41 41 TYR H H 1 9.41 0.02 . 1 . . . . . . . . . 5029 1 261 . 1 1 41 41 TYR HA H 1 4.24 0.02 . 1 . . . . . . . . . 5029 1 262 . 1 1 41 41 TYR HB2 H 1 2.40 0.02 . 1 . . . . . . . . . 5029 1 263 . 1 1 41 41 TYR HB3 H 1 2.36 0.02 . 1 . . . . . . . . . 5029 1 264 . 1 1 41 41 TYR HD1 H 1 6.09 0.02 . 1 . . . . . . . . . 5029 1 265 . 1 1 41 41 TYR HD2 H 1 6.09 0.02 . 1 . . . . . . . . . 5029 1 266 . 1 1 41 41 TYR HE1 H 1 5.43 0.02 . 1 . . . . . . . . . 5029 1 267 . 1 1 41 41 TYR HE2 H 1 5.43 0.02 . 1 . . . . . . . . . 5029 1 268 . 1 1 42 42 CYS H H 1 8.52 0.02 . 1 . . . . . . . . . 5029 1 269 . 1 1 42 42 CYS HA H 1 5.55 0.02 . 1 . . . . . . . . . 5029 1 270 . 1 1 42 42 CYS HB2 H 1 2.28 0.02 . 1 . . . . . . . . . 5029 1 271 . 1 1 42 42 CYS HB3 H 1 2.95 0.02 . 1 . . . . . . . . . 5029 1 272 . 1 1 43 43 GLU H H 1 8.25 0.02 . 1 . . . . . . . . . 5029 1 273 . 1 1 43 43 GLU HA H 1 4.80 0.02 . 1 . . . . . . . . . 5029 1 274 . 1 1 43 43 GLU HB2 H 1 1.92 0.02 . 1 . . . . . . . . . 5029 1 275 . 1 1 43 43 GLU HB3 H 1 1.80 0.02 . 1 . . . . . . . . . 5029 1 276 . 1 1 43 43 GLU HG2 H 1 2.15 0.02 . 1 . . . . . . . . . 5029 1 277 . 1 1 43 43 GLU HG3 H 1 2.42 0.02 . 1 . . . . . . . . . 5029 1 278 . 1 1 44 44 GLY H H 1 8.64 0.02 . 1 . . . . . . . . . 5029 1 279 . 1 1 44 44 GLY HA2 H 1 3.96 0.02 . 1 . . . . . . . . . 5029 1 280 . 1 1 44 44 GLY HA3 H 1 3.99 0.02 . 1 . . . . . . . . . 5029 1 281 . 1 1 45 45 LEU H H 1 8.51 0.02 . 1 . . . . . . . . . 5029 1 282 . 1 1 45 45 LEU HA H 1 4.02 0.02 . 1 . . . . . . . . . 5029 1 283 . 1 1 45 45 LEU HB2 H 1 1.60 0.02 . 1 . . . . . . . . . 5029 1 284 . 1 1 45 45 LEU HB3 H 1 1.28 0.02 . 1 . . . . . . . . . 5029 1 285 . 1 1 45 45 LEU HG H 1 1.28 0.02 . 1 . . . . . . . . . 5029 1 286 . 1 1 45 45 LEU HD11 H 1 0.41 0.02 . 1 . . . . . . . . . 5029 1 287 . 1 1 45 45 LEU HD12 H 1 0.41 0.02 . 1 . . . . . . . . . 5029 1 288 . 1 1 45 45 LEU HD13 H 1 0.41 0.02 . 1 . . . . . . . . . 5029 1 289 . 1 1 45 45 LEU HD21 H 1 0.78 0.02 . 1 . . . . . . . . . 5029 1 290 . 1 1 45 45 LEU HD22 H 1 0.78 0.02 . 1 . . . . . . . . . 5029 1 291 . 1 1 45 45 LEU HD23 H 1 0.78 0.02 . 1 . . . . . . . . . 5029 1 292 . 1 1 46 46 PRO HA H 1 4.49 0.02 . 1 . . . . . . . . . 5029 1 293 . 1 1 46 46 PRO HB2 H 1 1.97 0.02 . 1 . . . . . . . . . 5029 1 294 . 1 1 46 46 PRO HB3 H 1 2.43 0.02 . 1 . . . . . . . . . 5029 1 295 . 1 1 46 46 PRO HG2 H 1 2.08 0.02 . 1 . . . . . . . . . 5029 1 296 . 1 1 46 46 PRO HG3 H 1 2.10 0.02 . 1 . . . . . . . . . 5029 1 297 . 1 1 46 46 PRO HD2 H 1 3.45 0.02 . 1 . . . . . . . . . 5029 1 298 . 1 1 46 46 PRO HD3 H 1 3.67 0.02 . 1 . . . . . . . . . 5029 1 299 . 1 1 47 47 GLU H H 1 8.66 0.02 . 1 . . . . . . . . . 5029 1 300 . 1 1 47 47 GLU HA H 1 3.87 0.02 . 1 . . . . . . . . . 5029 1 301 . 1 1 47 47 GLU HB2 H 1 2.07 0.02 . 1 . . . . . . . . . 5029 1 302 . 1 1 47 47 GLU HB3 H 1 2.02 0.02 . 1 . . . . . . . . . 5029 1 303 . 1 1 47 47 GLU HG2 H 1 2.42 0.02 . 1 . . . . . . . . . 5029 1 304 . 1 1 47 47 GLU HG3 H 1 2.44 0.02 . 1 . . . . . . . . . 5029 1 305 . 1 1 48 48 ASN H H 1 8.02 0.02 . 1 . . . . . . . . . 5029 1 306 . 1 1 48 48 ASN HA H 1 4.65 0.02 . 1 . . . . . . . . . 5029 1 307 . 1 1 48 48 ASN HB2 H 1 3.04 0.02 . 1 . . . . . . . . . 5029 1 308 . 1 1 48 48 ASN HB3 H 1 2.75 0.02 . 1 . . . . . . . . . 5029 1 309 . 1 1 48 48 ASN HD21 H 1 7.59 0.02 . 1 . . . . . . . . . 5029 1 310 . 1 1 48 48 ASN HD22 H 1 6.78 0.02 . 1 . . . . . . . . . 5029 1 311 . 1 1 49 49 ALA H H 1 7.59 0.02 . 1 . . . . . . . . . 5029 1 312 . 1 1 49 49 ALA HA H 1 4.15 0.02 . 1 . . . . . . . . . 5029 1 313 . 1 1 49 49 ALA HB1 H 1 1.32 0.02 . 1 . . . . . . . . . 5029 1 314 . 1 1 49 49 ALA HB2 H 1 1.32 0.02 . 1 . . . . . . . . . 5029 1 315 . 1 1 49 49 ALA HB3 H 1 1.32 0.02 . 1 . . . . . . . . . 5029 1 316 . 1 1 50 50 LYS H H 1 8.56 0.02 . 1 . . . . . . . . . 5029 1 317 . 1 1 50 50 LYS HA H 1 4.42 0.02 . 1 . . . . . . . . . 5029 1 318 . 1 1 50 50 LYS HB2 H 1 1.76 0.02 . 1 . . . . . . . . . 5029 1 319 . 1 1 50 50 LYS HB3 H 1 1.72 0.02 . 1 . . . . . . . . . 5029 1 320 . 1 1 50 50 LYS HG2 H 1 1.47 0.02 . 1 . . . . . . . . . 5029 1 321 . 1 1 50 50 LYS HG3 H 1 1.34 0.02 . 1 . . . . . . . . . 5029 1 322 . 1 1 50 50 LYS HD2 H 1 1.63 0.02 . 1 . . . . . . . . . 5029 1 323 . 1 1 50 50 LYS HD3 H 1 1.63 0.02 . 1 . . . . . . . . . 5029 1 324 . 1 1 50 50 LYS HE2 H 1 2.97 0.02 . 1 . . . . . . . . . 5029 1 325 . 1 1 50 50 LYS HE3 H 1 2.97 0.02 . 1 . . . . . . . . . 5029 1 326 . 1 1 50 50 LYS HZ1 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 327 . 1 1 50 50 LYS HZ2 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 328 . 1 1 50 50 LYS HZ3 H 1 7.57 0.02 . 1 . . . . . . . . . 5029 1 329 . 1 1 51 51 VAL H H 1 8.45 0.02 . 1 . . . . . . . . . 5029 1 330 . 1 1 51 51 VAL HA H 1 5.21 0.02 . 1 . . . . . . . . . 5029 1 331 . 1 1 51 51 VAL HB H 1 2.14 0.02 . 1 . . . . . . . . . 5029 1 332 . 1 1 51 51 VAL HG11 H 1 0.76 0.02 . 1 . . . . . . . . . 5029 1 333 . 1 1 51 51 VAL HG12 H 1 0.76 0.02 . 1 . . . . . . . . . 5029 1 334 . 1 1 51 51 VAL HG13 H 1 0.76 0.02 . 1 . . . . . . . . . 5029 1 335 . 1 1 51 51 VAL HG21 H 1 0.40 0.02 . 1 . . . . . . . . . 5029 1 336 . 1 1 51 51 VAL HG22 H 1 0.40 0.02 . 1 . . . . . . . . . 5029 1 337 . 1 1 51 51 VAL HG23 H 1 0.40 0.02 . 1 . . . . . . . . . 5029 1 338 . 1 1 52 52 SER H H 1 8.74 0.02 . 1 . . . . . . . . . 5029 1 339 . 1 1 52 52 SER HA H 1 4.51 0.02 . 1 . . . . . . . . . 5029 1 340 . 1 1 52 52 SER HB2 H 1 3.91 0.02 . 1 . . . . . . . . . 5029 1 341 . 1 1 52 52 SER HB3 H 1 3.69 0.02 . 1 . . . . . . . . . 5029 1 342 . 1 1 53 53 ASP H H 1 8.68 0.02 . 1 . . . . . . . . . 5029 1 343 . 1 1 53 53 ASP HA H 1 4.96 0.02 . 1 . . . . . . . . . 5029 1 344 . 1 1 53 53 ASP HB2 H 1 2.86 0.02 . 1 . . . . . . . . . 5029 1 345 . 1 1 53 53 ASP HB3 H 1 2.97 0.02 . 1 . . . . . . . . . 5029 1 346 . 1 1 54 54 SER H H 1 8.33 0.02 . 1 . . . . . . . . . 5029 1 347 . 1 1 54 54 SER HA H 1 4.54 0.02 . 1 . . . . . . . . . 5029 1 348 . 1 1 54 54 SER HB2 H 1 3.82 0.02 . 1 . . . . . . . . . 5029 1 349 . 1 1 54 54 SER HB3 H 1 3.95 0.02 . 1 . . . . . . . . . 5029 1 350 . 1 1 55 55 ALA H H 1 8.63 0.02 . 1 . . . . . . . . . 5029 1 351 . 1 1 55 55 ALA HA H 1 4.07 0.02 . 1 . . . . . . . . . 5029 1 352 . 1 1 55 55 ALA HB1 H 1 1.44 0.02 . 1 . . . . . . . . . 5029 1 353 . 1 1 55 55 ALA HB2 H 1 1.44 0.02 . 1 . . . . . . . . . 5029 1 354 . 1 1 55 55 ALA HB3 H 1 1.44 0.02 . 1 . . . . . . . . . 5029 1 355 . 1 1 56 56 THR H H 1 7.87 0.02 . 1 . . . . . . . . . 5029 1 356 . 1 1 56 56 THR HA H 1 4.21 0.02 . 1 . . . . . . . . . 5029 1 357 . 1 1 56 56 THR HB H 1 4.15 0.02 . 1 . . . . . . . . . 5029 1 358 . 1 1 56 56 THR HG21 H 1 1.20 0.02 . 1 . . . . . . . . . 5029 1 359 . 1 1 56 56 THR HG22 H 1 1.20 0.02 . 1 . . . . . . . . . 5029 1 360 . 1 1 56 56 THR HG23 H 1 1.20 0.02 . 1 . . . . . . . . . 5029 1 361 . 1 1 57 57 ASN H H 1 8.61 0.02 . 1 . . . . . . . . . 5029 1 362 . 1 1 57 57 ASN HA H 1 4.86 0.02 . 1 . . . . . . . . . 5029 1 363 . 1 1 57 57 ASN HB2 H 1 2.90 0.02 . 1 . . . . . . . . . 5029 1 364 . 1 1 57 57 ASN HB3 H 1 2.72 0.02 . 1 . . . . . . . . . 5029 1 365 . 1 1 57 57 ASN HD21 H 1 6.98 0.02 . 1 . . . . . . . . . 5029 1 366 . 1 1 57 57 ASN HD22 H 1 7.67 0.02 . 1 . . . . . . . . . 5029 1 367 . 1 1 58 58 ILE H H 1 8.32 0.02 . 1 . . . . . . . . . 5029 1 368 . 1 1 58 58 ILE HA H 1 4.20 0.02 . 1 . . . . . . . . . 5029 1 369 . 1 1 58 58 ILE HB H 1 1.95 0.02 . 1 . . . . . . . . . 5029 1 370 . 1 1 58 58 ILE HG12 H 1 1.48 0.02 . 1 . . . . . . . . . 5029 1 371 . 1 1 58 58 ILE HG13 H 1 1.32 0.02 . 1 . . . . . . . . . 5029 1 372 . 1 1 58 58 ILE HG21 H 1 0.93 0.02 . 1 . . . . . . . . . 5029 1 373 . 1 1 58 58 ILE HG22 H 1 0.93 0.02 . 1 . . . . . . . . . 5029 1 374 . 1 1 58 58 ILE HG23 H 1 0.93 0.02 . 1 . . . . . . . . . 5029 1 375 . 1 1 58 58 ILE HD11 H 1 0.87 0.02 . 1 . . . . . . . . . 5029 1 376 . 1 1 58 58 ILE HD12 H 1 0.87 0.02 . 1 . . . . . . . . . 5029 1 377 . 1 1 58 58 ILE HD13 H 1 0.87 0.02 . 1 . . . . . . . . . 5029 1 378 . 1 1 59 59 CYS H H 1 8.35 0.02 . 1 . . . . . . . . . 5029 1 379 . 1 1 59 59 CYS HA H 1 4.71 0.02 . 1 . . . . . . . . . 5029 1 380 . 1 1 59 59 CYS HB2 H 1 3.75 0.02 . 1 . . . . . . . . . 5029 1 381 . 1 1 59 59 CYS HB3 H 1 3.75 0.02 . 1 . . . . . . . . . 5029 1 382 . 1 1 60 60 GLY H H 1 8.41 0.02 . 1 . . . . . . . . . 5029 1 383 . 1 1 60 60 GLY HA2 H 1 3.92 0.02 . 1 . . . . . . . . . 5029 1 384 . 1 1 60 60 GLY HA3 H 1 3.97 0.02 . 1 . . . . . . . . . 5029 1 stop_ save_