data_4990 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4990 _Entry.Title ; Solution structure of betacellulin, a new member of EGF-family ligands. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-04-16 _Entry.Accession_date 2001-04-17 _Entry.Last_release_date 2001-04-17 _Entry.Original_release_date 2001-04-17 _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 Kazunori Miura . . . . 4990 2 H. Doura . . . . 4990 3 T. Aizawa . . . . 4990 4 H. Tada . . . . 4990 5 M. Seno . . . . 4990 6 H. Yamada . . . . 4990 7 K. Kawano . . . . 4990 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4990 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 291 4990 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-09-23 . original BMRB . 4990 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4990 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22069898 _Citation.DOI . _Citation.PubMed_ID 12074582 _Citation.Full_citation . _Citation.Title ; Solution structure of betacellulin, a new member of EGF-family ligands. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. Biophys. Res. Commun.' _Citation.Journal_name_full . _Citation.Journal_volume 294 _Citation.Journal_issue 5 _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 1040 _Citation.Page_last 1046 _Citation.Year 2002 _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 Kazunori Miura . . . . 4990 1 2 H. Doura . . . . 4990 1 3 T. Aizawa . . . . 4990 1 4 H. Tada . . . . 4990 1 5 M. Seno . . . . 4990 1 6 H. Yamada . . . . 4990 1 7 K. Kawano . . . . 4990 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID Betacellulin 4990 1 EGF-family 4990 1 NMR 4990 1 'solution structure' 4990 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_BTC-2 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_BTC-2 _Assembly.Entry_ID 4990 _Assembly.ID 1 _Assembly.Name Betacellulin-2 _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 4990 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 BTC-2 1 $BTC-2_monomer . . yes native . . . . . 4990 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 8 8 SG . 1 . 1 CYS 21 21 SG . . . . . . . . . . . . 4990 1 2 disulfide single . 1 . 1 CYS 16 16 SG . 1 . 1 CYS 32 32 SG . . . . . . . . . . . . 4990 1 3 disulfide single . 1 . 1 CYS 34 34 SG . 1 . 1 CYS 43 43 SG . . . . . . . . . . . . 4990 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID BTC-2 abbreviation 4990 1 Betacellulin-2 system 4990 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_BTC-2_monomer _Entity.Sf_category entity _Entity.Sf_framecode BTC-2_monomer _Entity.Entry_ID 4990 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Betacellulin _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 ; RKGHFSRCPKQYKHYCIKGR CRFVVAEQTPSCVCDEGYIG ARCERVDLFY ; _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 50 _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 . _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 PDB 1IOX . 'Nmr Structure Of Human Betacellulin-2' . . . . . 98.00 50 100.00 100.00 1.57e-20 . . . . 4990 1 2 no PDB 1IP0 . 'Nmr Structure Of Human Betacellulin-2' . . . . . 98.00 50 100.00 100.00 1.57e-20 . . . . 4990 1 3 no EMBL CAL37603 . 'hypothetical protein [synthetic construct]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 4 no EMBL CAL37873 . 'hypothetical protein [synthetic construct]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 5 no EMBL CAL38181 . 'hypothetical protein [synthetic construct]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 6 no EMBL CAL38427 . 'hypothetical protein [synthetic construct]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 7 no GenBank AAB25452 . 'betacellulin; BTC [Homo sapiens]' . . . . . 100.00 178 100.00 100.00 1.26e-22 . . . . 4990 1 8 no GenBank AAH11618 . 'Betacellulin [Homo sapiens]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 9 no GenBank AAX29812 . 'betacellulin [synthetic construct]' . . . . . 100.00 179 100.00 100.00 1.15e-22 . . . . 4990 1 10 no GenBank AAX42376 . 'betacellulin [synthetic construct]' . . . . . 100.00 178 100.00 100.00 1.25e-22 . . . . 4990 1 11 no GenBank EAX05712 . 'betacellulin [Homo sapiens]' . . . . . 100.00 178 100.00 100.00 1.26e-22 . . . . 4990 1 12 no REF NP_001720 . 'betacellulin [Homo sapiens]' . . . . . 100.00 178 100.00 100.00 1.26e-22 . . . . 4990 1 13 no REF XP_001101880 . 'PREDICTED: similar to betacellulin [Macaca mulatta]' . . . . . 100.00 178 98.00 98.00 2.77e-22 . . . . 4990 1 14 no REF XP_517223 . 'PREDICTED: similar to betacellulin; BTC [Pan troglodytes]' . . . . . 100.00 178 100.00 100.00 1.10e-22 . . . . 4990 1 15 no SWISS-PROT P35070 . 'Probetacellulin precursor [Contains: Betacellulin (BTC)]' . . . . . 100.00 178 100.00 100.00 1.26e-22 . . . . 4990 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID BTC-2 abbreviation 4990 1 BTC-2 variant 4990 1 Betacellulin common 4990 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 31 ARG . 4990 1 2 32 LYS . 4990 1 3 33 GLY . 4990 1 4 34 HIS . 4990 1 5 35 PHE . 4990 1 6 36 SER . 4990 1 7 37 ARG . 4990 1 8 38 CYS . 4990 1 9 39 PRO . 4990 1 10 40 LYS . 4990 1 11 41 GLN . 4990 1 12 42 TYR . 4990 1 13 43 LYS . 4990 1 14 44 HIS . 4990 1 15 45 TYR . 4990 1 16 46 CYS . 4990 1 17 47 ILE . 4990 1 18 48 LYS . 4990 1 19 49 GLY . 4990 1 20 50 ARG . 4990 1 21 51 CYS . 4990 1 22 52 ARG . 4990 1 23 53 PHE . 4990 1 24 54 VAL . 4990 1 25 55 VAL . 4990 1 26 56 ALA . 4990 1 27 57 GLU . 4990 1 28 58 GLN . 4990 1 29 59 THR . 4990 1 30 60 PRO . 4990 1 31 61 SER . 4990 1 32 62 CYS . 4990 1 33 63 VAL . 4990 1 34 64 CYS . 4990 1 35 65 ASP . 4990 1 36 66 GLU . 4990 1 37 67 GLY . 4990 1 38 68 TYR . 4990 1 39 69 ILE . 4990 1 40 70 GLY . 4990 1 41 71 ALA . 4990 1 42 72 ARG . 4990 1 43 73 CYS . 4990 1 44 74 GLU . 4990 1 45 75 ARG . 4990 1 46 76 VAL . 4990 1 47 77 ASP . 4990 1 48 78 LEU . 4990 1 49 79 PHE . 4990 1 50 80 TYR . 4990 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 . ARG 1 1 4990 1 . LYS 2 2 4990 1 . GLY 3 3 4990 1 . HIS 4 4 4990 1 . PHE 5 5 4990 1 . SER 6 6 4990 1 . ARG 7 7 4990 1 . CYS 8 8 4990 1 . PRO 9 9 4990 1 . LYS 10 10 4990 1 . GLN 11 11 4990 1 . TYR 12 12 4990 1 . LYS 13 13 4990 1 . HIS 14 14 4990 1 . TYR 15 15 4990 1 . CYS 16 16 4990 1 . ILE 17 17 4990 1 . LYS 18 18 4990 1 . GLY 19 19 4990 1 . ARG 20 20 4990 1 . CYS 21 21 4990 1 . ARG 22 22 4990 1 . PHE 23 23 4990 1 . VAL 24 24 4990 1 . VAL 25 25 4990 1 . ALA 26 26 4990 1 . GLU 27 27 4990 1 . GLN 28 28 4990 1 . THR 29 29 4990 1 . PRO 30 30 4990 1 . SER 31 31 4990 1 . CYS 32 32 4990 1 . VAL 33 33 4990 1 . CYS 34 34 4990 1 . ASP 35 35 4990 1 . GLU 36 36 4990 1 . GLY 37 37 4990 1 . TYR 38 38 4990 1 . ILE 39 39 4990 1 . GLY 40 40 4990 1 . ALA 41 41 4990 1 . ARG 42 42 4990 1 . CYS 43 43 4990 1 . GLU 44 44 4990 1 . ARG 45 45 4990 1 . VAL 46 46 4990 1 . ASP 47 47 4990 1 . LEU 48 48 4990 1 . PHE 49 49 4990 1 . TYR 50 50 4990 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 4990 _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 $BTC-2_monomer . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 4990 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 4990 _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 $BTC-2_monomer . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . 'BTC-2 was obtained as a lysylendo-peptidase product of the recombinant human BTC-1a.' 4990 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4990 _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 Betacellulin . . . 1 $BTC-2_monomer . . 2.0 . . mM . . . . 4990 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4990 _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 3.5 0.2 n/a 4990 1 temperature 298 1 K 4990 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4990 _Software.ID 1 _Software.Type . _Software.Name NMRPipe _Software.Version 1.8 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'raw spectral data processing' 4990 1 stop_ save_ save_PIPP _Software.Sf_category software _Software.Sf_framecode PIPP _Software.Entry_ID 4990 _Software.ID 2 _Software.Type . _Software.Name PIPP _Software.Version 4.3.2 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 4990 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 4990 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4990 _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 . 500 . . . 4990 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 4990 _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 . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4990 1 2 NOESY . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4990 1 3 TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4990 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 4990 _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 . . . . . 4990 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 4990 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_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 . _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 . 4990 1 2 NOESY 1 $sample_1 . 4990 1 3 TOCSY 1 $sample_1 . 4990 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 3 3 GLY H H 1 8.42 0.03 . 1 . . . . . . . . . 4990 1 2 . 1 1 3 3 GLY HA2 H 1 3.84 0.03 . 1 . . . . . . . . . 4990 1 3 . 1 1 3 3 GLY HA3 H 1 3.84 0.03 . 1 . . . . . . . . . 4990 1 4 . 1 1 4 4 HIS H H 1 8.25 0.03 . 1 . . . . . . . . . 4990 1 5 . 1 1 4 4 HIS HA H 1 4.46 0.03 . 1 . . . . . . . . . 4990 1 6 . 1 1 4 4 HIS HB2 H 1 2.86 0.03 . 1 . . . . . . . . . 4990 1 7 . 1 1 4 4 HIS HB3 H 1 2.86 0.03 . 1 . . . . . . . . . 4990 1 8 . 1 1 4 4 HIS HD2 H 1 7.35 0.03 . 1 . . . . . . . . . 4990 1 9 . 1 1 4 4 HIS HE1 H 1 8.69 0.03 . 1 . . . . . . . . . 4990 1 10 . 1 1 5 5 PHE H H 1 8.40 0.03 . 1 . . . . . . . . . 4990 1 11 . 1 1 5 5 PHE HA H 1 5.43 0.03 . 1 . . . . . . . . . 4990 1 12 . 1 1 5 5 PHE HB2 H 1 2.85 0.03 . 1 . . . . . . . . . 4990 1 13 . 1 1 5 5 PHE HB3 H 1 3.02 0.03 . 1 . . . . . . . . . 4990 1 14 . 1 1 5 5 PHE HD1 H 1 7.03 0.03 . 1 . . . . . . . . . 4990 1 15 . 1 1 5 5 PHE HD2 H 1 7.03 0.03 . 1 . . . . . . . . . 4990 1 16 . 1 1 5 5 PHE HE1 H 1 7.16 0.03 . 1 . . . . . . . . . 4990 1 17 . 1 1 5 5 PHE HE2 H 1 7.16 0.03 . 1 . . . . . . . . . 4990 1 18 . 1 1 6 6 SER H H 1 9.24 0.03 . 1 . . . . . . . . . 4990 1 19 . 1 1 6 6 SER HA H 1 4.83 0.03 . 1 . . . . . . . . . 4990 1 20 . 1 1 6 6 SER HB2 H 1 3.76 0.03 . 1 . . . . . . . . . 4990 1 21 . 1 1 6 6 SER HB3 H 1 4.02 0.03 . 1 . . . . . . . . . 4990 1 22 . 1 1 7 7 ARG H H 1 8.43 0.03 . 1 . . . . . . . . . 4990 1 23 . 1 1 7 7 ARG HA H 1 4.34 0.03 . 1 . . . . . . . . . 4990 1 24 . 1 1 7 7 ARG HB2 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 25 . 1 1 7 7 ARG HB3 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 26 . 1 1 7 7 ARG HG2 H 1 1.59 0.03 . 1 . . . . . . . . . 4990 1 27 . 1 1 7 7 ARG HG3 H 1 1.59 0.03 . 1 . . . . . . . . . 4990 1 28 . 1 1 8 8 CYS H H 1 9.35 0.03 . 1 . . . . . . . . . 4990 1 29 . 1 1 8 8 CYS HA H 1 3.95 0.03 . 1 . . . . . . . . . 4990 1 30 . 1 1 8 8 CYS HB2 H 1 2.90 0.03 . 1 . . . . . . . . . 4990 1 31 . 1 1 8 8 CYS HB3 H 1 3.12 0.03 . 1 . . . . . . . . . 4990 1 32 . 1 1 9 9 PRO HA H 1 3.92 0.03 . 1 . . . . . . . . . 4990 1 33 . 1 1 9 9 PRO HB2 H 1 1.50 0.03 . 1 . . . . . . . . . 4990 1 34 . 1 1 9 9 PRO HB3 H 1 1.82 0.03 . 1 . . . . . . . . . 4990 1 35 . 1 1 9 9 PRO HG2 H 1 1.00 0.03 . 1 . . . . . . . . . 4990 1 36 . 1 1 9 9 PRO HG3 H 1 1.00 0.03 . 1 . . . . . . . . . 4990 1 37 . 1 1 9 9 PRO HD2 H 1 2.83 0.03 . 1 . . . . . . . . . 4990 1 38 . 1 1 9 9 PRO HD3 H 1 2.83 0.03 . 1 . . . . . . . . . 4990 1 39 . 1 1 10 10 LYS H H 1 8.52 0.03 . 1 . . . . . . . . . 4990 1 40 . 1 1 10 10 LYS HA H 1 3.98 0.03 . 1 . . . . . . . . . 4990 1 41 . 1 1 10 10 LYS HB2 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 42 . 1 1 10 10 LYS HB3 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 43 . 1 1 11 11 GLN H H 1 9.11 0.03 . 1 . . . . . . . . . 4990 1 44 . 1 1 11 11 GLN HA H 1 4.00 0.03 . 1 . . . . . . . . . 4990 1 45 . 1 1 11 11 GLN HB2 H 1 1.45 0.03 . 1 . . . . . . . . . 4990 1 46 . 1 1 11 11 GLN HB3 H 1 1.45 0.03 . 1 . . . . . . . . . 4990 1 47 . 1 1 11 11 GLN HG2 H 1 1.67 0.03 . 1 . . . . . . . . . 4990 1 48 . 1 1 11 11 GLN HG3 H 1 1.67 0.03 . 1 . . . . . . . . . 4990 1 49 . 1 1 12 12 TYR H H 1 7.90 0.03 . 1 . . . . . . . . . 4990 1 50 . 1 1 12 12 TYR HA H 1 4.79 0.03 . 1 . . . . . . . . . 4990 1 51 . 1 1 12 12 TYR HB2 H 1 2.31 0.03 . 1 . . . . . . . . . 4990 1 52 . 1 1 12 12 TYR HB3 H 1 3.49 0.03 . 1 . . . . . . . . . 4990 1 53 . 1 1 12 12 TYR HD1 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 54 . 1 1 12 12 TYR HD2 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 55 . 1 1 12 12 TYR HE1 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 56 . 1 1 12 12 TYR HE2 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 57 . 1 1 13 13 LYS H H 1 7.37 0.03 . 1 . . . . . . . . . 4990 1 58 . 1 1 13 13 LYS HA H 1 3.89 0.03 . 1 . . . . . . . . . 4990 1 59 . 1 1 13 13 LYS HB2 H 1 1.81 0.03 . 1 . . . . . . . . . 4990 1 60 . 1 1 13 13 LYS HB3 H 1 1.81 0.03 . 1 . . . . . . . . . 4990 1 61 . 1 1 13 13 LYS HG2 H 1 0.94 0.03 . 1 . . . . . . . . . 4990 1 62 . 1 1 13 13 LYS HG3 H 1 0.94 0.03 . 1 . . . . . . . . . 4990 1 63 . 1 1 13 13 LYS HD2 H 1 1.43 0.03 . 1 . . . . . . . . . 4990 1 64 . 1 1 13 13 LYS HD3 H 1 1.43 0.03 . 1 . . . . . . . . . 4990 1 65 . 1 1 14 14 HIS H H 1 8.75 0.03 . 1 . . . . . . . . . 4990 1 66 . 1 1 14 14 HIS HA H 1 4.97 0.03 . 1 . . . . . . . . . 4990 1 67 . 1 1 14 14 HIS HB2 H 1 2.87 0.03 . 1 . . . . . . . . . 4990 1 68 . 1 1 14 14 HIS HB3 H 1 3.46 0.03 . 1 . . . . . . . . . 4990 1 69 . 1 1 14 14 HIS HD2 H 1 6.78 0.03 . 1 . . . . . . . . . 4990 1 70 . 1 1 14 14 HIS HE1 H 1 8.58 0.03 . 1 . . . . . . . . . 4990 1 71 . 1 1 15 15 TYR H H 1 7.68 0.03 . 1 . . . . . . . . . 4990 1 72 . 1 1 15 15 TYR HA H 1 4.10 0.03 . 1 . . . . . . . . . 4990 1 73 . 1 1 15 15 TYR HB2 H 1 2.90 0.03 . 1 . . . . . . . . . 4990 1 74 . 1 1 15 15 TYR HB3 H 1 3.27 0.03 . 1 . . . . . . . . . 4990 1 75 . 1 1 15 15 TYR HD1 H 1 7.07 0.03 . 1 . . . . . . . . . 4990 1 76 . 1 1 15 15 TYR HD2 H 1 7.07 0.03 . 1 . . . . . . . . . 4990 1 77 . 1 1 15 15 TYR HE1 H 1 7.43 0.03 . 1 . . . . . . . . . 4990 1 78 . 1 1 15 15 TYR HE2 H 1 7.43 0.03 . 1 . . . . . . . . . 4990 1 79 . 1 1 16 16 CYS H H 1 8.81 0.03 . 1 . . . . . . . . . 4990 1 80 . 1 1 16 16 CYS HA H 1 4.26 0.03 . 1 . . . . . . . . . 4990 1 81 . 1 1 16 16 CYS HB2 H 1 1.90 0.03 . 1 . . . . . . . . . 4990 1 82 . 1 1 16 16 CYS HB3 H 1 2.46 0.03 . 1 . . . . . . . . . 4990 1 83 . 1 1 17 17 ILE H H 1 8.51 0.03 . 1 . . . . . . . . . 4990 1 84 . 1 1 17 17 ILE HA H 1 3.84 0.03 . 1 . . . . . . . . . 4990 1 85 . 1 1 17 17 ILE HB H 1 1.64 0.03 . 1 . . . . . . . . . 4990 1 86 . 1 1 17 17 ILE HG21 H 1 0.77 0.03 . 1 . . . . . . . . . 4990 1 87 . 1 1 17 17 ILE HG22 H 1 0.77 0.03 . 1 . . . . . . . . . 4990 1 88 . 1 1 17 17 ILE HG23 H 1 0.77 0.03 . 1 . . . . . . . . . 4990 1 89 . 1 1 17 17 ILE HD11 H 1 0.58 0.03 . 1 . . . . . . . . . 4990 1 90 . 1 1 17 17 ILE HD12 H 1 0.58 0.03 . 1 . . . . . . . . . 4990 1 91 . 1 1 17 17 ILE HD13 H 1 0.58 0.03 . 1 . . . . . . . . . 4990 1 92 . 1 1 18 18 LYS H H 1 6.82 0.03 . 1 . . . . . . . . . 4990 1 93 . 1 1 18 18 LYS HA H 1 4.32 0.03 . 1 . . . . . . . . . 4990 1 94 . 1 1 18 18 LYS HB2 H 1 1.62 0.03 . 1 . . . . . . . . . 4990 1 95 . 1 1 18 18 LYS HB3 H 1 1.62 0.03 . 1 . . . . . . . . . 4990 1 96 . 1 1 18 18 LYS HG2 H 1 0.82 0.03 . 1 . . . . . . . . . 4990 1 97 . 1 1 18 18 LYS HG3 H 1 0.82 0.03 . 1 . . . . . . . . . 4990 1 98 . 1 1 18 18 LYS HD2 H 1 1.23 0.03 . 1 . . . . . . . . . 4990 1 99 . 1 1 18 18 LYS HD3 H 1 1.23 0.03 . 1 . . . . . . . . . 4990 1 100 . 1 1 19 19 GLY H H 1 6.92 0.03 . 1 . . . . . . . . . 4990 1 101 . 1 1 19 19 GLY HA2 H 1 3.91 0.03 . 1 . . . . . . . . . 4990 1 102 . 1 1 19 19 GLY HA3 H 1 4.11 0.03 . 1 . . . . . . . . . 4990 1 103 . 1 1 20 20 ARG H H 1 8.28 0.03 . 1 . . . . . . . . . 4990 1 104 . 1 1 20 20 ARG HA H 1 4.54 0.03 . 1 . . . . . . . . . 4990 1 105 . 1 1 20 20 ARG HB2 H 1 1.65 0.03 . 1 . . . . . . . . . 4990 1 106 . 1 1 20 20 ARG HB3 H 1 1.65 0.03 . 1 . . . . . . . . . 4990 1 107 . 1 1 20 20 ARG HG2 H 1 1.54 0.03 . 1 . . . . . . . . . 4990 1 108 . 1 1 20 20 ARG HG3 H 1 1.54 0.03 . 1 . . . . . . . . . 4990 1 109 . 1 1 20 20 ARG HD2 H 1 3.08 0.03 . 1 . . . . . . . . . 4990 1 110 . 1 1 20 20 ARG HD3 H 1 3.08 0.03 . 1 . . . . . . . . . 4990 1 111 . 1 1 21 21 CYS H H 1 8.92 0.03 . 1 . . . . . . . . . 4990 1 112 . 1 1 21 21 CYS HA H 1 5.18 0.03 . 1 . . . . . . . . . 4990 1 113 . 1 1 21 21 CYS HB2 H 1 3.18 0.03 . 1 . . . . . . . . . 4990 1 114 . 1 1 21 21 CYS HB3 H 1 3.38 0.03 . 1 . . . . . . . . . 4990 1 115 . 1 1 22 22 ARG H H 1 9.43 0.03 . 1 . . . . . . . . . 4990 1 116 . 1 1 22 22 ARG HA H 1 4.65 0.03 . 1 . . . . . . . . . 4990 1 117 . 1 1 22 22 ARG HB2 H 1 1.40 0.03 . 1 . . . . . . . . . 4990 1 118 . 1 1 22 22 ARG HB3 H 1 1.40 0.03 . 1 . . . . . . . . . 4990 1 119 . 1 1 22 22 ARG HG2 H 1 1.21 0.03 . 1 . . . . . . . . . 4990 1 120 . 1 1 22 22 ARG HG3 H 1 1.21 0.03 . 1 . . . . . . . . . 4990 1 121 . 1 1 23 23 PHE H H 1 9.05 0.03 . 1 . . . . . . . . . 4990 1 122 . 1 1 23 23 PHE HA H 1 4.86 0.03 . 1 . . . . . . . . . 4990 1 123 . 1 1 23 23 PHE HB2 H 1 2.49 0.03 . 1 . . . . . . . . . 4990 1 124 . 1 1 23 23 PHE HB3 H 1 2.83 0.03 . 1 . . . . . . . . . 4990 1 125 . 1 1 23 23 PHE HD1 H 1 6.69 0.03 . 1 . . . . . . . . . 4990 1 126 . 1 1 23 23 PHE HD2 H 1 6.69 0.03 . 1 . . . . . . . . . 4990 1 127 . 1 1 23 23 PHE HE1 H 1 7.02 0.03 . 1 . . . . . . . . . 4990 1 128 . 1 1 23 23 PHE HE2 H 1 7.02 0.03 . 1 . . . . . . . . . 4990 1 129 . 1 1 24 24 VAL H H 1 8.04 0.03 . 1 . . . . . . . . . 4990 1 130 . 1 1 24 24 VAL HA H 1 4.00 0.03 . 1 . . . . . . . . . 4990 1 131 . 1 1 24 24 VAL HB H 1 1.91 0.03 . 1 . . . . . . . . . 4990 1 132 . 1 1 24 24 VAL HG11 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 133 . 1 1 24 24 VAL HG12 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 134 . 1 1 24 24 VAL HG13 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 135 . 1 1 24 24 VAL HG21 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 136 . 1 1 24 24 VAL HG22 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 137 . 1 1 24 24 VAL HG23 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 138 . 1 1 25 25 VAL H H 1 8.00 0.03 . 1 . . . . . . . . . 4990 1 139 . 1 1 25 25 VAL HA H 1 3.16 0.03 . 1 . . . . . . . . . 4990 1 140 . 1 1 25 25 VAL HB H 1 1.81 0.03 . 1 . . . . . . . . . 4990 1 141 . 1 1 25 25 VAL HG11 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 142 . 1 1 25 25 VAL HG12 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 143 . 1 1 25 25 VAL HG13 H 1 0.81 0.03 . 1 . . . . . . . . . 4990 1 144 . 1 1 25 25 VAL HG21 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 145 . 1 1 25 25 VAL HG22 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 146 . 1 1 25 25 VAL HG23 H 1 0.69 0.03 . 1 . . . . . . . . . 4990 1 147 . 1 1 26 26 ALA H H 1 8.97 0.03 . 1 . . . . . . . . . 4990 1 148 . 1 1 26 26 ALA HA H 1 3.98 0.03 . 1 . . . . . . . . . 4990 1 149 . 1 1 26 26 ALA HB1 H 1 1.25 0.03 . 1 . . . . . . . . . 4990 1 150 . 1 1 26 26 ALA HB2 H 1 1.25 0.03 . 1 . . . . . . . . . 4990 1 151 . 1 1 26 26 ALA HB3 H 1 1.25 0.03 . 1 . . . . . . . . . 4990 1 152 . 1 1 27 27 GLU H H 1 6.34 0.03 . 1 . . . . . . . . . 4990 1 153 . 1 1 27 27 GLU HA H 1 4.31 0.03 . 1 . . . . . . . . . 4990 1 154 . 1 1 27 27 GLU HB2 H 1 1.44 0.03 . 1 . . . . . . . . . 4990 1 155 . 1 1 27 27 GLU HB3 H 1 1.44 0.03 . 1 . . . . . . . . . 4990 1 156 . 1 1 27 27 GLU HG2 H 1 2.15 0.03 . 1 . . . . . . . . . 4990 1 157 . 1 1 27 27 GLU HG3 H 1 2.15 0.03 . 1 . . . . . . . . . 4990 1 158 . 1 1 28 28 GLN H H 1 7.83 0.03 . 1 . . . . . . . . . 4990 1 159 . 1 1 28 28 GLN HA H 1 3.09 0.03 . 1 . . . . . . . . . 4990 1 160 . 1 1 28 28 GLN HB2 H 1 1.24 0.03 . 1 . . . . . . . . . 4990 1 161 . 1 1 28 28 GLN HB3 H 1 1.24 0.03 . 1 . . . . . . . . . 4990 1 162 . 1 1 28 28 GLN HG2 H 1 2.19 0.03 . 1 . . . . . . . . . 4990 1 163 . 1 1 28 28 GLN HG3 H 1 2.19 0.03 . 1 . . . . . . . . . 4990 1 164 . 1 1 29 29 THR H H 1 6.45 0.03 . 1 . . . . . . . . . 4990 1 165 . 1 1 29 29 THR HA H 1 4.63 0.03 . 1 . . . . . . . . . 4990 1 166 . 1 1 29 29 THR HB H 1 3.67 0.03 . 1 . . . . . . . . . 4990 1 167 . 1 1 29 29 THR HG21 H 1 0.97 0.03 . 1 . . . . . . . . . 4990 1 168 . 1 1 29 29 THR HG22 H 1 0.97 0.03 . 1 . . . . . . . . . 4990 1 169 . 1 1 29 29 THR HG23 H 1 0.97 0.03 . 1 . . . . . . . . . 4990 1 170 . 1 1 30 30 PRO HA H 1 3.87 0.03 . 1 . . . . . . . . . 4990 1 171 . 1 1 30 30 PRO HB2 H 1 1.74 0.03 . 1 . . . . . . . . . 4990 1 172 . 1 1 30 30 PRO HB3 H 1 1.78 0.03 . 1 . . . . . . . . . 4990 1 173 . 1 1 30 30 PRO HG2 H 1 1.35 0.03 . 1 . . . . . . . . . 4990 1 174 . 1 1 30 30 PRO HG3 H 1 1.60 0.03 . 1 . . . . . . . . . 4990 1 175 . 1 1 30 30 PRO HD2 H 1 2.80 0.03 . 1 . . . . . . . . . 4990 1 176 . 1 1 30 30 PRO HD3 H 1 2.80 0.03 . 1 . . . . . . . . . 4990 1 177 . 1 1 31 31 SER H H 1 8.57 0.03 . 1 . . . . . . . . . 4990 1 178 . 1 1 31 31 SER HA H 1 4.79 0.03 . 1 . . . . . . . . . 4990 1 179 . 1 1 31 31 SER HB2 H 1 3.74 0.03 . 1 . . . . . . . . . 4990 1 180 . 1 1 31 31 SER HB3 H 1 3.74 0.03 . 1 . . . . . . . . . 4990 1 181 . 1 1 32 32 CYS H H 1 8.85 0.03 . 1 . . . . . . . . . 4990 1 182 . 1 1 32 32 CYS HA H 1 5.49 0.03 . 1 . . . . . . . . . 4990 1 183 . 1 1 32 32 CYS HB2 H 1 2.47 0.03 . 1 . . . . . . . . . 4990 1 184 . 1 1 32 32 CYS HB3 H 1 2.66 0.03 . 1 . . . . . . . . . 4990 1 185 . 1 1 33 33 VAL H H 1 9.01 0.03 . 1 . . . . . . . . . 4990 1 186 . 1 1 33 33 VAL HA H 1 4.13 0.03 . 1 . . . . . . . . . 4990 1 187 . 1 1 33 33 VAL HB H 1 1.80 0.03 . 1 . . . . . . . . . 4990 1 188 . 1 1 33 33 VAL HG11 H 1 0.79 0.03 . 1 . . . . . . . . . 4990 1 189 . 1 1 33 33 VAL HG12 H 1 0.79 0.03 . 1 . . . . . . . . . 4990 1 190 . 1 1 33 33 VAL HG13 H 1 0.79 0.03 . 1 . . . . . . . . . 4990 1 191 . 1 1 33 33 VAL HG21 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 192 . 1 1 33 33 VAL HG22 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 193 . 1 1 33 33 VAL HG23 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 194 . 1 1 34 34 CYS H H 1 9.02 0.03 . 1 . . . . . . . . . 4990 1 195 . 1 1 34 34 CYS HA H 1 4.95 0.03 . 1 . . . . . . . . . 4990 1 196 . 1 1 34 34 CYS HB2 H 1 2.60 0.03 . 1 . . . . . . . . . 4990 1 197 . 1 1 34 34 CYS HB3 H 1 3.25 0.03 . 1 . . . . . . . . . 4990 1 198 . 1 1 35 35 ASP H H 1 8.76 0.03 . 1 . . . . . . . . . 4990 1 199 . 1 1 35 35 ASP HA H 1 4.44 0.03 . 1 . . . . . . . . . 4990 1 200 . 1 1 35 35 ASP HB2 H 1 2.33 0.03 . 1 . . . . . . . . . 4990 1 201 . 1 1 35 35 ASP HB3 H 1 2.86 0.03 . 1 . . . . . . . . . 4990 1 202 . 1 1 36 36 GLU H H 1 8.47 0.03 . 1 . . . . . . . . . 4990 1 203 . 1 1 36 36 GLU HA H 1 4.80 0.03 . 1 . . . . . . . . . 4990 1 204 . 1 1 36 36 GLU HB2 H 1 1.51 0.03 . 1 . . . . . . . . . 4990 1 205 . 1 1 36 36 GLU HB3 H 1 1.51 0.03 . 1 . . . . . . . . . 4990 1 206 . 1 1 36 36 GLU HG2 H 1 1.63 0.03 . 1 . . . . . . . . . 4990 1 207 . 1 1 36 36 GLU HG3 H 1 1.63 0.03 . 1 . . . . . . . . . 4990 1 208 . 1 1 37 37 GLY H H 1 8.51 0.03 . 1 . . . . . . . . . 4990 1 209 . 1 1 37 37 GLY HA2 H 1 3.28 0.03 . 1 . . . . . . . . . 4990 1 210 . 1 1 37 37 GLY HA3 H 1 3.28 0.03 . 1 . . . . . . . . . 4990 1 211 . 1 1 38 38 TYR H H 1 7.89 0.03 . 1 . . . . . . . . . 4990 1 212 . 1 1 38 38 TYR HA H 1 5.12 0.03 . 1 . . . . . . . . . 4990 1 213 . 1 1 38 38 TYR HB2 H 1 2.59 0.03 . 1 . . . . . . . . . 4990 1 214 . 1 1 38 38 TYR HB3 H 1 2.74 0.03 . 1 . . . . . . . . . 4990 1 215 . 1 1 38 38 TYR HD1 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 216 . 1 1 38 38 TYR HD2 H 1 6.64 0.03 . 1 . . . . . . . . . 4990 1 217 . 1 1 38 38 TYR HE1 H 1 6.59 0.03 . 1 . . . . . . . . . 4990 1 218 . 1 1 38 38 TYR HE2 H 1 6.59 0.03 . 1 . . . . . . . . . 4990 1 219 . 1 1 39 39 ILE H H 1 9.11 0.03 . 1 . . . . . . . . . 4990 1 220 . 1 1 39 39 ILE HA H 1 4.67 0.03 . 1 . . . . . . . . . 4990 1 221 . 1 1 39 39 ILE HB H 1 1.76 0.03 . 1 . . . . . . . . . 4990 1 222 . 1 1 39 39 ILE HG12 H 1 1.18 0.03 . 1 . . . . . . . . . 4990 1 223 . 1 1 39 39 ILE HG13 H 1 1.18 0.03 . 1 . . . . . . . . . 4990 1 224 . 1 1 39 39 ILE HD11 H 1 0.70 0.03 . 1 . . . . . . . . . 4990 1 225 . 1 1 39 39 ILE HD12 H 1 0.70 0.03 . 1 . . . . . . . . . 4990 1 226 . 1 1 39 39 ILE HD13 H 1 0.70 0.03 . 1 . . . . . . . . . 4990 1 227 . 1 1 39 39 ILE HG21 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 228 . 1 1 39 39 ILE HG22 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 229 . 1 1 39 39 ILE HG23 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 230 . 1 1 40 40 GLY H H 1 7.73 0.03 . 1 . . . . . . . . . 4990 1 231 . 1 1 40 40 GLY HA2 H 1 3.69 0.03 . 1 . . . . . . . . . 4990 1 232 . 1 1 40 40 GLY HA3 H 1 4.89 0.03 . 1 . . . . . . . . . 4990 1 233 . 1 1 41 41 ALA H H 1 9.05 0.03 . 1 . . . . . . . . . 4990 1 234 . 1 1 41 41 ALA HA H 1 4.02 0.03 . 1 . . . . . . . . . 4990 1 235 . 1 1 41 41 ALA HB1 H 1 1.43 0.03 . 1 . . . . . . . . . 4990 1 236 . 1 1 41 41 ALA HB2 H 1 1.43 0.03 . 1 . . . . . . . . . 4990 1 237 . 1 1 41 41 ALA HB3 H 1 1.43 0.03 . 1 . . . . . . . . . 4990 1 238 . 1 1 42 42 ARG H H 1 8.17 0.03 . 1 . . . . . . . . . 4990 1 239 . 1 1 42 42 ARG HA H 1 4.49 0.03 . 1 . . . . . . . . . 4990 1 240 . 1 1 42 42 ARG HB2 H 1 1.18 0.03 . 1 . . . . . . . . . 4990 1 241 . 1 1 42 42 ARG HB3 H 1 1.12 0.03 . 1 . . . . . . . . . 4990 1 242 . 1 1 42 42 ARG HG2 H 1 0.35 0.03 . 1 . . . . . . . . . 4990 1 243 . 1 1 42 42 ARG HG3 H 1 0.35 0.03 . 1 . . . . . . . . . 4990 1 244 . 1 1 43 43 CYS H H 1 7.91 0.03 . 1 . . . . . . . . . 4990 1 245 . 1 1 43 43 CYS HA H 1 3.80 0.03 . 1 . . . . . . . . . 4990 1 246 . 1 1 43 43 CYS HB2 H 1 2.37 0.03 . 1 . . . . . . . . . 4990 1 247 . 1 1 43 43 CYS HB3 H 1 2.77 0.03 . 1 . . . . . . . . . 4990 1 248 . 1 1 44 44 GLU H H 1 9.42 0.03 . 1 . . . . . . . . . 4990 1 249 . 1 1 44 44 GLU HA H 1 4.36 0.03 . 1 . . . . . . . . . 4990 1 250 . 1 1 44 44 GLU HB2 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 251 . 1 1 44 44 GLU HB3 H 1 1.68 0.03 . 1 . . . . . . . . . 4990 1 252 . 1 1 44 44 GLU HG2 H 1 2.14 0.03 . 1 . . . . . . . . . 4990 1 253 . 1 1 44 44 GLU HG3 H 1 2.14 0.03 . 1 . . . . . . . . . 4990 1 254 . 1 1 45 45 ARG H H 1 8.47 0.03 . 1 . . . . . . . . . 4990 1 255 . 1 1 45 45 ARG HA H 1 4.77 0.03 . 1 . . . . . . . . . 4990 1 256 . 1 1 45 45 ARG HB2 H 1 1.57 0.03 . 1 . . . . . . . . . 4990 1 257 . 1 1 45 45 ARG HB3 H 1 1.57 0.03 . 1 . . . . . . . . . 4990 1 258 . 1 1 45 45 ARG HG2 H 1 1.49 0.03 . 1 . . . . . . . . . 4990 1 259 . 1 1 45 45 ARG HG3 H 1 1.49 0.03 . 1 . . . . . . . . . 4990 1 260 . 1 1 46 46 VAL H H 1 8.22 0.03 . 1 . . . . . . . . . 4990 1 261 . 1 1 46 46 VAL HA H 1 3.71 0.03 . 1 . . . . . . . . . 4990 1 262 . 1 1 46 46 VAL HB H 1 1.73 0.03 . 1 . . . . . . . . . 4990 1 263 . 1 1 46 46 VAL HG11 H 1 0.75 0.03 . 1 . . . . . . . . . 4990 1 264 . 1 1 46 46 VAL HG12 H 1 0.75 0.03 . 1 . . . . . . . . . 4990 1 265 . 1 1 46 46 VAL HG13 H 1 0.75 0.03 . 1 . . . . . . . . . 4990 1 266 . 1 1 46 46 VAL HG21 H 1 0.64 0.03 . 1 . . . . . . . . . 4990 1 267 . 1 1 46 46 VAL HG22 H 1 0.64 0.03 . 1 . . . . . . . . . 4990 1 268 . 1 1 46 46 VAL HG23 H 1 0.64 0.03 . 1 . . . . . . . . . 4990 1 269 . 1 1 47 47 ASP H H 1 8.08 0.03 . 1 . . . . . . . . . 4990 1 270 . 1 1 47 47 ASP HA H 1 4.36 0.03 . 1 . . . . . . . . . 4990 1 271 . 1 1 47 47 ASP HB2 H 1 2.12 0.03 . 1 . . . . . . . . . 4990 1 272 . 1 1 47 47 ASP HB3 H 1 2.49 0.03 . 1 . . . . . . . . . 4990 1 273 . 1 1 48 48 LEU H H 1 7.89 0.03 . 1 . . . . . . . . . 4990 1 274 . 1 1 48 48 LEU HA H 1 4.03 0.03 . 1 . . . . . . . . . 4990 1 275 . 1 1 48 48 LEU HB2 H 1 1.31 0.03 . 1 . . . . . . . . . 4990 1 276 . 1 1 48 48 LEU HB3 H 1 1.31 0.03 . 1 . . . . . . . . . 4990 1 277 . 1 1 48 48 LEU HG H 1 1.20 0.03 . 1 . . . . . . . . . 4990 1 278 . 1 1 48 48 LEU HD11 H 1 0.66 0.03 . 1 . . . . . . . . . 4990 1 279 . 1 1 48 48 LEU HD12 H 1 0.66 0.03 . 1 . . . . . . . . . 4990 1 280 . 1 1 48 48 LEU HD13 H 1 0.66 0.03 . 1 . . . . . . . . . 4990 1 281 . 1 1 48 48 LEU HD21 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 282 . 1 1 48 48 LEU HD22 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 283 . 1 1 48 48 LEU HD23 H 1 0.67 0.03 . 1 . . . . . . . . . 4990 1 284 . 1 1 49 49 PHE H H 1 7.85 0.03 . 1 . . . . . . . . . 4990 1 285 . 1 1 49 49 PHE HA H 1 4.41 0.03 . 1 . . . . . . . . . 4990 1 286 . 1 1 49 49 PHE HB2 H 1 2.81 0.03 . 1 . . . . . . . . . 4990 1 287 . 1 1 49 49 PHE HB3 H 1 3.02 0.03 . 1 . . . . . . . . . 4990 1 288 . 1 1 50 50 TYR H H 1 7.48 0.03 . 1 . . . . . . . . . 4990 1 289 . 1 1 50 50 TYR HA H 1 4.25 0.03 . 1 . . . . . . . . . 4990 1 290 . 1 1 50 50 TYR HB2 H 1 2.79 0.03 . 1 . . . . . . . . . 4990 1 291 . 1 1 50 50 TYR HB3 H 1 2.90 0.03 . 1 . . . . . . . . . 4990 1 stop_ save_