data_5670 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5670 _Entry.Title ; Structural Characterization of Hellethionins from helleborus purpurascens ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-01-23 _Entry.Accession_date 2003-01-23 _Entry.Last_release_date 2003-04-30 _Entry.Original_release_date 2003-04-30 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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.Entry_ID 1 Alexander Milbradt . G. . 5670 2 Franz Kerek . . . 5670 3 Luis Moroder . . . 5670 4 Christian Renner . . . 5670 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5670 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 291 5670 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 . . 2003-04-30 2003-01-23 original author . 5670 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5670 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12600207 _Citation.Full_citation . _Citation.Title 'Structural Characterization of Hellethionins from helleborus purpurascens' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 42 _Citation.Journal_issue 8 _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 2404 _Citation.Page_last 2411 _Citation.Year 2003 _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.Entry_ID _Citation_author.Citation_ID 1 Alexander Milbradt . G. . 5670 1 2 Franz Kerek . . . 5670 1 3 Luis Moroder . . . 5670 1 4 Christian Renner . . . 5670 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Helleborus Hellethionin Thionins' 5670 1 stop_ save_ save_ref-1 _Citation.Sf_category citations _Citation.Sf_framecode ref-1 _Citation.Entry_ID 5670 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Goddard T.D. and Kneller D.G.; Sparky 3; University of California, San Francisco ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref-2 _Citation.Sf_category citations _Citation.Sf_framecode ref-2 _Citation.Entry_ID 5670 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8744573 _Citation.Full_citation ; Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51-5, 29-32. ; _Citation.Title 'MOLMOL: a program for display and analysis of macromolecular structures.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full 'Journal of molecular graphics' _Citation.Journal_volume 14 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0263-7855 _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 51 _Citation.Page_last 32 _Citation.Year 1996 _Citation.Details ; MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms. ; 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.Entry_ID _Citation_author.Citation_ID 1 R. Koradi R. . . 5670 3 2 M. Billeter M. . . 5670 3 3 K. Wuthrich K. . . 5670 3 stop_ save_ save_ref-3 _Citation.Sf_category citations _Citation.Sf_framecode ref-3 _Citation.Entry_ID 5670 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9008363 _Citation.Full_citation ; Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR. 1996 Dec;8(4):477-86. ; _Citation.Title 'AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 8 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 477 _Citation.Page_last 486 _Citation.Year 1996 _Citation.Details ; The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR. The outputs include a detailed breakdown of the restraint violations, a number of plots in PostScript format and summary statistics. These various analyses indicate both the degree of agreement of the model structures with the experimental dat, and the quality of their geometrical properties. They are intended to be of use both to support ongoing NMR structure determination and in the validation of the final results. ; 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.Entry_ID _Citation_author.Citation_ID 1 'R. A.' Laskowski R. A. . 5670 4 2 'J. A.' Rullmannn J. A. . 5670 4 3 'M. W.' MacArthur M. W. . 5670 4 4 R. Kaptein R. . . 5670 4 5 'J. M.' Thornton J. M. . 5670 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Hellethionin_D _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Hellethionin_D _Assembly.Entry_ID 5670 _Assembly.ID 1 _Assembly.Name 'Hellethionin D' _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 5670 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 'Hellethionin D' 1 $Hellethionin_D . . . native . . . . . 5670 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_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_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 3 3 SG . 1 . 1 CYS 40 40 SG . . . . . . . . . . 5670 1 2 disulfide single . 1 . . CYS 12 12 SG . 1 . 1 CYS 30 30 SG . . . . . . . . . . 5670 1 3 disulfide single . 1 . . CYS 16 16 SG . 1 . 1 CYS 26 26 SG . . . . . . . . . . 5670 1 4 disulfide single . 1 . . CYS 4 4 SG . 1 . 1 CYS 32 32 SG . . . . . . . . . . 5670 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 . PDB 1NBL . . . . . . 5670 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Hellethionin D' system 5670 1 'Hellethionin D' abbreviation 5670 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Hellethionin_D _Entity.Sf_category entity _Entity.Sf_framecode Hellethionin_D _Entity.Entry_ID 5670 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Hellethionin D' _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 ; KSCCRNTLARNCYNACRFTG GSQPTCGILCDCIHVTTTTC PSSHPS ; _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 46 _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 TTTT _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 1NBL . "Nmr Structure Of Hellethionin D" . . . . . 100.00 46 100.00 100.00 2.10e-23 . . . . 5670 1 2 no PDB 3SZS . "Crystal Structure Analysis Of Hellethionin D" . . . . . 100.00 46 100.00 100.00 2.10e-23 . . . . 5670 1 3 no SP P60057 . "RecName: Full=Hellethionin-D [Helleborus purpurascens]" . . . . . 100.00 46 100.00 100.00 2.10e-23 . . . . 5670 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Hellethionin D' common 5670 1 'Hel D' abbreviation 5670 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 . 5670 1 2 . SER . 5670 1 3 . CYS . 5670 1 4 . CYS . 5670 1 5 . ARG . 5670 1 6 . ASN . 5670 1 7 . THR . 5670 1 8 . LEU . 5670 1 9 . ALA . 5670 1 10 . ARG . 5670 1 11 . ASN . 5670 1 12 . CYS . 5670 1 13 . TYR . 5670 1 14 . ASN . 5670 1 15 . ALA . 5670 1 16 . CYS . 5670 1 17 . ARG . 5670 1 18 . PHE . 5670 1 19 . THR . 5670 1 20 . GLY . 5670 1 21 . GLY . 5670 1 22 . SER . 5670 1 23 . GLN . 5670 1 24 . PRO . 5670 1 25 . THR . 5670 1 26 . CYS . 5670 1 27 . GLY . 5670 1 28 . ILE . 5670 1 29 . LEU . 5670 1 30 . CYS . 5670 1 31 . ASP . 5670 1 32 . CYS . 5670 1 33 . ILE . 5670 1 34 . HIS . 5670 1 35 . VAL . 5670 1 36 . THR . 5670 1 37 . THR . 5670 1 38 . THR . 5670 1 39 . THR . 5670 1 40 . CYS . 5670 1 41 . PRO . 5670 1 42 . SER . 5670 1 43 . SER . 5670 1 44 . HIS . 5670 1 45 . PRO . 5670 1 46 . SER . 5670 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 5670 1 . SER 2 2 5670 1 . CYS 3 3 5670 1 . CYS 4 4 5670 1 . ARG 5 5 5670 1 . ASN 6 6 5670 1 . THR 7 7 5670 1 . LEU 8 8 5670 1 . ALA 9 9 5670 1 . ARG 10 10 5670 1 . ASN 11 11 5670 1 . CYS 12 12 5670 1 . TYR 13 13 5670 1 . ASN 14 14 5670 1 . ALA 15 15 5670 1 . CYS 16 16 5670 1 . ARG 17 17 5670 1 . PHE 18 18 5670 1 . THR 19 19 5670 1 . GLY 20 20 5670 1 . GLY 21 21 5670 1 . SER 22 22 5670 1 . GLN 23 23 5670 1 . PRO 24 24 5670 1 . THR 25 25 5670 1 . CYS 26 26 5670 1 . GLY 27 27 5670 1 . ILE 28 28 5670 1 . LEU 29 29 5670 1 . CYS 30 30 5670 1 . ASP 31 31 5670 1 . CYS 32 32 5670 1 . ILE 33 33 5670 1 . HIS 34 34 5670 1 . VAL 35 35 5670 1 . THR 36 36 5670 1 . THR 37 37 5670 1 . THR 38 38 5670 1 . THR 39 39 5670 1 . CYS 40 40 5670 1 . PRO 41 41 5670 1 . SER 42 42 5670 1 . SER 43 43 5670 1 . HIS 44 44 5670 1 . PRO 45 45 5670 1 . SER 46 46 5670 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 5670 _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.Subvariant _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.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Hellethionin_D . 171899 organism . 'Helleborus purpurascens' 'Helleborus purpurascens' . . Eukaryota Viridiplantae Helleborus purpurascens . . . . . . . . . . . . . . . . . . . . . 5670 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 5670 _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_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _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.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Hellethionin_D . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5670 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5670 _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 'Hellethionin D' . . . 1 $Hellethionin_D . . 3.0 . . mM . . . . 5670 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5670 _Sample.ID 2 _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 'Hellethionin D' . . . 1 $Hellethionin_D . . 5.0 . . mM . . . . 5670 2 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 5670 _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 2.5 0.1 n/a 5670 1 temperature 293 0.5 K 5670 1 stop_ save_ save_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_2 _Sample_condition_list.Entry_ID 5670 _Sample_condition_list.ID 2 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 2.5 0.1 n/a 5670 2 temperature 283 0.5 K 5670 2 stop_ save_ save_cond_3 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_3 _Sample_condition_list.Entry_ID 5670 _Sample_condition_list.ID 3 _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 2.5 0.1 n/a 5670 3 temperature 303 0.5 K 5670 3 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5670 _Software.ID 1 _Software.Name XWINNMR _Software.Version 3.0 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data acquisition' 5670 1 'data processing' 5670 1 stop_ save_ save_INSIGHT _Software.Sf_category software _Software.Sf_framecode INSIGHT _Software.Entry_ID 5670 _Software.ID 2 _Software.Name INSIGHT _Software.Version 98 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure calculation' 5670 2 stop_ save_ save_Sparky _Software.Sf_category software _Software.Sf_framecode Sparky _Software.Entry_ID 5670 _Software.ID 3 _Software.Name Sparky _Software.Version 3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignment' 5670 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $ref-1 5670 3 stop_ save_ save_MOLMOL _Software.Sf_category software _Software.Sf_framecode MOLMOL _Software.Entry_ID 5670 _Software.ID 4 _Software.Name MOLMOL _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID visualization 5670 4 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref-2 5670 4 stop_ save_ save_PROCHECK _Software.Sf_category software _Software.Sf_framecode PROCHECK _Software.Entry_ID 5670 _Software.ID 5 _Software.Name PROCHECK _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'checking the quality of the protein structure' 5670 5 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref-3 5670 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5670 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5670 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 5670 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5670 _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_1 Bruker DRX . 500 . . . 5670 1 2 NMR_spectrometer_2 Bruker DRX . 600 . . . 5670 1 3 NMR_spectrometer_3 Bruker DMX . 750 . . . 5670 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 5670 _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 '1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5670 1 2 '1H-1H TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5670 1 3 '1H-1H COSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5670 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5670 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5670 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-1H TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5670 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-1H COSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 5670 _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.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5670 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_shift1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift1 _Assigned_chem_shift_list.Entry_ID 5670 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $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 $sample_1 . 5670 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.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 3.72 0.01 . 1 . . . . . . . . 5670 1 2 . 1 1 1 1 LYS HB2 H 1 1.48 0.01 . 2 . . . . . . . . 5670 1 3 . 1 1 1 1 LYS HB3 H 1 1.35 0.01 . 2 . . . . . . . . 5670 1 4 . 1 1 1 1 LYS HG2 H 1 0.83 0.01 . 1 . . . . . . . . 5670 1 5 . 1 1 1 1 LYS HG3 H 1 0.83 0.01 . 1 . . . . . . . . 5670 1 6 . 1 1 1 1 LYS HD2 H 1 1.03 0.01 . 2 . . . . . . . . 5670 1 7 . 1 1 1 1 LYS HD3 H 1 1.1 0.01 . 2 . . . . . . . . 5670 1 8 . 1 1 1 1 LYS HE2 H 1 2.64 0.01 . 1 . . . . . . . . 5670 1 9 . 1 1 1 1 LYS HE3 H 1 2.64 0.01 . 1 . . . . . . . . 5670 1 10 . 1 1 1 1 LYS HZ1 H 1 7.17 0.01 . 1 . . . . . . . . 5670 1 11 . 1 1 1 1 LYS HZ2 H 1 7.17 0.01 . 1 . . . . . . . . 5670 1 12 . 1 1 1 1 LYS HZ3 H 1 7.17 0.01 . 1 . . . . . . . . 5670 1 13 . 1 1 2 2 SER H H 1 8.52 0.01 . 1 . . . . . . . . 5670 1 14 . 1 1 2 2 SER HA H 1 4.65 0.01 . 1 . . . . . . . . 5670 1 15 . 1 1 2 2 SER HB2 H 1 3.41 0.01 . 2 . . . . . . . . 5670 1 16 . 1 1 2 2 SER HB3 H 1 2.96 0.01 . 2 . . . . . . . . 5670 1 17 . 1 1 3 3 CYS H H 1 8.45 0.01 . 1 . . . . . . . . 5670 1 18 . 1 1 3 3 CYS HA H 1 4.60 0.01 . 1 . . . . . . . . 5670 1 19 . 1 1 3 3 CYS HB2 H 1 4.22 0.01 . 2 . . . . . . . . 5670 1 20 . 1 1 3 3 CYS HB3 H 1 1.93 0.01 . 2 . . . . . . . . 5670 1 21 . 1 1 4 4 CYS H H 1 9.47 0.01 . 1 . . . . . . . . 5670 1 22 . 1 1 4 4 CYS HA H 1 4.90 0.01 . 1 . . . . . . . . 5670 1 23 . 1 1 4 4 CYS HB2 H 1 2.60 0.01 . 2 . . . . . . . . 5670 1 24 . 1 1 4 4 CYS HB3 H 1 2.14 0.01 . 2 . . . . . . . . 5670 1 25 . 1 1 5 5 ARG H H 1 7.52 0.01 . 1 . . . . . . . . 5670 1 26 . 1 1 5 5 ARG HA H 1 3.51 0.01 . 1 . . . . . . . . 5670 1 27 . 1 1 5 5 ARG HB2 H 1 1.65 0.01 . 1 . . . . . . . . 5670 1 28 . 1 1 5 5 ARG HB3 H 1 1.65 0.01 . 1 . . . . . . . . 5670 1 29 . 1 1 5 5 ARG HG2 H 1 1.35 0.01 . 2 . . . . . . . . 5670 1 30 . 1 1 5 5 ARG HG3 H 1 1.30 0.01 . 2 . . . . . . . . 5670 1 31 . 1 1 5 5 ARG HD2 H 1 2.93 0.01 . 2 . . . . . . . . 5670 1 32 . 1 1 5 5 ARG HD3 H 1 2.62 0.01 . 2 . . . . . . . . 5670 1 33 . 1 1 5 5 ARG HE H 1 6.72 0.01 . 1 . . . . . . . . 5670 1 34 . 1 1 5 5 ARG HH11 H 1 6.10 0.01 . 4 . . . . . . . . 5670 1 35 . 1 1 5 5 ARG HH12 H 1 6.10 0.01 . 4 . . . . . . . . 5670 1 36 . 1 1 5 5 ARG HH21 H 1 6.10 0.01 . 4 . . . . . . . . 5670 1 37 . 1 1 5 5 ARG HH22 H 1 6.10 0.01 . 4 . . . . . . . . 5670 1 38 . 1 1 6 6 ASN H H 1 6.82 0.01 . 1 . . . . . . . . 5670 1 39 . 1 1 6 6 ASN HA H 1 4.46 0.01 . 1 . . . . . . . . 5670 1 40 . 1 1 6 6 ASN HB2 H 1 3.01 0.01 . 1 . . . . . . . . 5670 1 41 . 1 1 6 6 ASN HB3 H 1 3.01 0.01 . 1 . . . . . . . . 5670 1 42 . 1 1 6 6 ASN HD21 H 1 7.51 0.01 . 2 . . . . . . . . 5670 1 43 . 1 1 6 6 ASN HD22 H 1 6.45 0.01 . 2 . . . . . . . . 5670 1 44 . 1 1 7 7 THR H H 1 8.30 0.01 . 1 . . . . . . . . 5670 1 45 . 1 1 7 7 THR HA H 1 3.58 0.01 . 1 . . . . . . . . 5670 1 46 . 1 1 7 7 THR HB H 1 3.79 0.01 . 1 . . . . . . . . 5670 1 47 . 1 1 7 7 THR HG21 H 1 0.94 0.01 . 1 . . . . . . . . 5670 1 48 . 1 1 7 7 THR HG22 H 1 0.94 0.01 . 1 . . . . . . . . 5670 1 49 . 1 1 7 7 THR HG23 H 1 0.94 0.01 . 1 . . . . . . . . 5670 1 50 . 1 1 8 8 LEU H H 1 7.65 0.01 . 1 . . . . . . . . 5670 1 51 . 1 1 8 8 LEU HA H 1 3.77 0.01 . 1 . . . . . . . . 5670 1 52 . 1 1 8 8 LEU HB2 H 1 1.38 0.01 . 2 . . . . . . . . 5670 1 53 . 1 1 8 8 LEU HB3 H 1 1.29 0.01 . 2 . . . . . . . . 5670 1 54 . 1 1 8 8 LEU HD11 H 1 0.57 0.01 . 2 . . . . . . . . 5670 1 55 . 1 1 8 8 LEU HD12 H 1 0.57 0.01 . 2 . . . . . . . . 5670 1 56 . 1 1 8 8 LEU HD13 H 1 0.57 0.01 . 2 . . . . . . . . 5670 1 57 . 1 1 8 8 LEU HD21 H 1 0.61 0.01 . 2 . . . . . . . . 5670 1 58 . 1 1 8 8 LEU HD22 H 1 0.61 0.01 . 2 . . . . . . . . 5670 1 59 . 1 1 8 8 LEU HD23 H 1 0.61 0.01 . 2 . . . . . . . . 5670 1 60 . 1 1 9 9 ALA H H 1 8.02 0.01 . 1 . . . . . . . . 5670 1 61 . 1 1 9 9 ALA HA H 1 4.07 0.01 . 1 . . . . . . . . 5670 1 62 . 1 1 9 9 ALA HB1 H 1 1.52 0.01 . 1 . . . . . . . . 5670 1 63 . 1 1 9 9 ALA HB2 H 1 1.52 0.01 . 1 . . . . . . . . 5670 1 64 . 1 1 9 9 ALA HB3 H 1 1.52 0.01 . 1 . . . . . . . . 5670 1 65 . 1 1 10 10 ARG H H 1 7.68 0.01 . 1 . . . . . . . . 5670 1 66 . 1 1 10 10 ARG HA H 1 4.16 0.01 . 1 . . . . . . . . 5670 1 67 . 1 1 10 10 ARG HB2 H 1 1.92 0.01 . 2 . . . . . . . . 5670 1 68 . 1 1 10 10 ARG HB3 H 1 1.36 0.01 . 2 . . . . . . . . 5670 1 69 . 1 1 10 10 ARG HG2 H 1 1.59 0.01 . 1 . . . . . . . . 5670 1 70 . 1 1 10 10 ARG HG3 H 1 1.59 0.01 . 1 . . . . . . . . 5670 1 71 . 1 1 10 10 ARG HD2 H 1 3.06 0.01 . 2 . . . . . . . . 5670 1 72 . 1 1 10 10 ARG HD3 H 1 3.00 0.01 . 2 . . . . . . . . 5670 1 73 . 1 1 10 10 ARG HE H 1 8.07 0.01 . 1 . . . . . . . . 5670 1 74 . 1 1 10 10 ARG HH11 H 1 6.79 0.01 . 4 . . . . . . . . 5670 1 75 . 1 1 10 10 ARG HH12 H 1 6.79 0.01 . 4 . . . . . . . . 5670 1 76 . 1 1 10 10 ARG HH21 H 1 6.28 0.01 . 4 . . . . . . . . 5670 1 77 . 1 1 10 10 ARG HH22 H 1 6.28 0.01 . 4 . . . . . . . . 5670 1 78 . 1 1 11 11 ASN H H 1 8.16 0.01 . 1 . . . . . . . . 5670 1 79 . 1 1 11 11 ASN HA H 1 4.21 0.01 . 1 . . . . . . . . 5670 1 80 . 1 1 11 11 ASN HB2 H 1 2.64 0.01 . 2 . . . . . . . . 5670 1 81 . 1 1 11 11 ASN HB3 H 1 2.60 0.01 . 2 . . . . . . . . 5670 1 82 . 1 1 11 11 ASN HD21 H 1 7.29 0.01 . 2 . . . . . . . . 5670 1 83 . 1 1 11 11 ASN HD22 H 1 6.70 0.01 . 2 . . . . . . . . 5670 1 84 . 1 1 12 12 CYS H H 1 8.15 0.01 . 1 . . . . . . . . 5670 1 85 . 1 1 12 12 CYS HA H 1 3.89 0.01 . 1 . . . . . . . . 5670 1 86 . 1 1 12 12 CYS HB2 H 1 3.58 0.01 . 2 . . . . . . . . 5670 1 87 . 1 1 12 12 CYS HB3 H 1 2.72 0.01 . 2 . . . . . . . . 5670 1 88 . 1 1 13 13 TYR H H 1 8.74 0.01 . 1 . . . . . . . . 5670 1 89 . 1 1 13 13 TYR HA H 1 3.36 0.01 . 1 . . . . . . . . 5670 1 90 . 1 1 13 13 TYR HB2 H 1 3.06 0.01 . 2 . . . . . . . . 5670 1 91 . 1 1 13 13 TYR HB3 H 1 2.89 0.01 . 2 . . . . . . . . 5670 1 92 . 1 1 13 13 TYR HD1 H 1 6.4 0.01 . 4 . . . . . . . . 5670 1 93 . 1 1 13 13 TYR HD2 H 1 6.4 0.01 . 4 . . . . . . . . 5670 1 94 . 1 1 13 13 TYR HE1 H 1 6.4 0.01 . 4 . . . . . . . . 5670 1 95 . 1 1 13 13 TYR HE2 H 1 6.4 0.01 . 4 . . . . . . . . 5670 1 96 . 1 1 14 14 ASN H H 1 8.55 0.01 . 1 . . . . . . . . 5670 1 97 . 1 1 14 14 ASN HA H 1 4.00 0.01 . 1 . . . . . . . . 5670 1 98 . 1 1 14 14 ASN HB2 H 1 2.62 0.01 . 2 . . . . . . . . 5670 1 99 . 1 1 14 14 ASN HB3 H 1 2.52 0.01 . 2 . . . . . . . . 5670 1 100 . 1 1 14 14 ASN HD21 H 1 7.6 0.01 . 1 . . . . . . . . 5670 1 101 . 1 1 14 14 ASN HD22 H 1 7.6 0.01 . 1 . . . . . . . . 5670 1 102 . 1 1 15 15 ALA H H 1 7.63 0.01 . 1 . . . . . . . . 5670 1 103 . 1 1 15 15 ALA HA H 1 3.93 0.01 . 1 . . . . . . . . 5670 1 104 . 1 1 15 15 ALA HB1 H 1 1.19 0.01 . 1 . . . . . . . . 5670 1 105 . 1 1 15 15 ALA HB2 H 1 1.19 0.01 . 1 . . . . . . . . 5670 1 106 . 1 1 15 15 ALA HB3 H 1 1.19 0.01 . 1 . . . . . . . . 5670 1 107 . 1 1 16 16 CYS H H 1 7.98 0.01 . 1 . . . . . . . . 5670 1 108 . 1 1 16 16 CYS HA H 1 3.80 0.01 . 1 . . . . . . . . 5670 1 109 . 1 1 16 16 CYS HB2 H 1 2.83 0.01 . 2 . . . . . . . . 5670 1 110 . 1 1 16 16 CYS HB3 H 1 2.78 0.01 . 2 . . . . . . . . 5670 1 111 . 1 1 17 17 ARG H H 1 8.26 0.01 . 1 . . . . . . . . 5670 1 112 . 1 1 17 17 ARG HA H 1 3.79 0.01 . 1 . . . . . . . . 5670 1 113 . 1 1 17 17 ARG HB2 H 1 1.48 0.01 . 2 . . . . . . . . 5670 1 114 . 1 1 17 17 ARG HB3 H 1 1.37 0.01 . 2 . . . . . . . . 5670 1 115 . 1 1 17 17 ARG HG2 H 1 0.88 0.01 . 2 . . . . . . . . 5670 1 116 . 1 1 17 17 ARG HG3 H 1 0.62 0.01 . 2 . . . . . . . . 5670 1 117 . 1 1 17 17 ARG HD2 H 1 2.72 0.01 . 2 . . . . . . . . 5670 1 118 . 1 1 17 17 ARG HD3 H 1 2.15 0.01 . 2 . . . . . . . . 5670 1 119 . 1 1 17 17 ARG HE H 1 6.72 0.01 . 1 . . . . . . . . 5670 1 120 . 1 1 17 17 ARG HH11 H 1 6.79 0.01 . 4 . . . . . . . . 5670 1 121 . 1 1 17 17 ARG HH12 H 1 6.79 0.01 . 4 . . . . . . . . 5670 1 122 . 1 1 17 17 ARG HH21 H 1 6.28 0.01 . 4 . . . . . . . . 5670 1 123 . 1 1 17 17 ARG HH22 H 1 6.28 0.01 . 4 . . . . . . . . 5670 1 124 . 1 1 18 18 PHE H H 1 8.00 0.01 . 1 . . . . . . . . 5670 1 125 . 1 1 18 18 PHE HA H 1 4.01 0.01 . 1 . . . . . . . . 5670 1 126 . 1 1 18 18 PHE HB2 H 1 3.07 0.01 . 2 . . . . . . . . 5670 1 127 . 1 1 18 18 PHE HB3 H 1 2.94 0.01 . 2 . . . . . . . . 5670 1 128 . 1 1 18 18 PHE HD1 H 1 7.01 0.01 . 4 . . . . . . . . 5670 1 129 . 1 1 18 18 PHE HD2 H 1 7.01 0.01 . 4 . . . . . . . . 5670 1 130 . 1 1 18 18 PHE HE1 H 1 6.91 0.01 . 4 . . . . . . . . 5670 1 131 . 1 1 18 18 PHE HE2 H 1 6.91 0.01 . 4 . . . . . . . . 5670 1 132 . 1 1 18 18 PHE HZ H 1 6.91 0.01 . 4 . . . . . . . . 5670 1 133 . 1 1 19 19 THR H H 1 7.24 0.01 . 1 . . . . . . . . 5670 1 134 . 1 1 19 19 THR HA H 1 3.94 0.01 . 1 . . . . . . . . 5670 1 135 . 1 1 19 19 THR HB H 1 4.27 0.01 . 1 . . . . . . . . 5670 1 136 . 1 1 19 19 THR HG21 H 1 1.06 0.01 . 1 . . . . . . . . 5670 1 137 . 1 1 19 19 THR HG22 H 1 1.06 0.01 . 1 . . . . . . . . 5670 1 138 . 1 1 19 19 THR HG23 H 1 1.06 0.01 . 1 . . . . . . . . 5670 1 139 . 1 1 20 20 GLY H H 1 7.24 0.01 . 1 . . . . . . . . 5670 1 140 . 1 1 20 20 GLY HA2 H 1 4.04 0.01 . 2 . . . . . . . . 5670 1 141 . 1 1 20 20 GLY HA3 H 1 3.30 0.01 . 2 . . . . . . . . 5670 1 142 . 1 1 21 21 GLY H H 1 7.88 0.01 . 1 . . . . . . . . 5670 1 143 . 1 1 21 21 GLY HA2 H 1 3.73 0.01 . 2 . . . . . . . . 5670 1 144 . 1 1 21 21 GLY HA3 H 1 3.12 0.01 . 2 . . . . . . . . 5670 1 145 . 1 1 22 22 SER H H 1 8.45 0.01 . 1 . . . . . . . . 5670 1 146 . 1 1 22 22 SER HA H 1 4.03 0.01 . 1 . . . . . . . . 5670 1 147 . 1 1 22 22 SER HB2 H 1 3.90 0.01 . 2 . . . . . . . . 5670 1 148 . 1 1 22 22 SER HB3 H 1 3.74 0.01 . 2 . . . . . . . . 5670 1 149 . 1 1 23 23 GLN H H 1 9.01 0.01 . 1 . . . . . . . . 5670 1 150 . 1 1 23 23 GLN HA H 1 3.76 0.01 . 1 . . . . . . . . 5670 1 151 . 1 1 23 23 GLN HB2 H 1 1.84 0.01 . 2 . . . . . . . . 5670 1 152 . 1 1 23 23 GLN HB3 H 1 1.77 0.01 . 2 . . . . . . . . 5670 1 153 . 1 1 23 23 GLN HG2 H 1 2.20 0.01 . 2 . . . . . . . . 5670 1 154 . 1 1 23 23 GLN HG3 H 1 1.95 0.01 . 2 . . . . . . . . 5670 1 155 . 1 1 23 23 GLN HE21 H 1 7.13 0.01 . 2 . . . . . . . . 5670 1 156 . 1 1 23 23 GLN HE22 H 1 6.56 0.01 . 2 . . . . . . . . 5670 1 157 . 1 1 24 24 PRO HA H 1 4.05 0.01 . 1 . . . . . . . . 5670 1 158 . 1 1 24 24 PRO HB2 H 1 1.99 0.01 . 2 . . . . . . . . 5670 1 159 . 1 1 24 24 PRO HB3 H 1 1.56 0.01 . 2 . . . . . . . . 5670 1 160 . 1 1 24 24 PRO HG2 H 1 1.78 0.01 . 2 . . . . . . . . 5670 1 161 . 1 1 24 24 PRO HG3 H 1 1.65 0.01 . 2 . . . . . . . . 5670 1 162 . 1 1 24 24 PRO HD2 H 1 3.54 0.01 . 2 . . . . . . . . 5670 1 163 . 1 1 24 24 PRO HD3 H 1 3.39 0.01 . 2 . . . . . . . . 5670 1 164 . 1 1 25 25 THR H H 1 7.10 0.01 . 1 . . . . . . . . 5670 1 165 . 1 1 25 25 THR HA H 1 3.55 0.01 . 1 . . . . . . . . 5670 1 166 . 1 1 25 25 THR HB H 1 3.80 0.01 . 1 . . . . . . . . 5670 1 167 . 1 1 25 25 THR HG21 H 1 0.84 0.01 . 1 . . . . . . . . 5670 1 168 . 1 1 25 25 THR HG22 H 1 0.84 0.01 . 1 . . . . . . . . 5670 1 169 . 1 1 25 25 THR HG23 H 1 0.84 0.01 . 1 . . . . . . . . 5670 1 170 . 1 1 26 26 CYS H H 1 8.40 0.01 . 1 . . . . . . . . 5670 1 171 . 1 1 26 26 CYS HA H 1 4.28 0.01 . 1 . . . . . . . . 5670 1 172 . 1 1 26 26 CYS HB2 H 1 2.29 0.01 . 2 . . . . . . . . 5670 1 173 . 1 1 26 26 CYS HB3 H 1 2.16 0.01 . 2 . . . . . . . . 5670 1 174 . 1 1 27 27 GLY H H 1 8.42 0.01 . 1 . . . . . . . . 5670 1 175 . 1 1 27 27 GLY HA2 H 1 3.83 0.01 . 2 . . . . . . . . 5670 1 176 . 1 1 27 27 GLY HA3 H 1 3.45 0.01 . 2 . . . . . . . . 5670 1 177 . 1 1 28 28 ILE H H 1 7.44 0.01 . 1 . . . . . . . . 5670 1 178 . 1 1 28 28 ILE HA H 1 3.66 0.01 . 1 . . . . . . . . 5670 1 179 . 1 1 28 28 ILE HB H 1 1.67 0.01 . 1 . . . . . . . . 5670 1 180 . 1 1 28 28 ILE HG12 H 1 1.41 0.01 . 2 . . . . . . . . 5670 1 181 . 1 1 28 28 ILE HG13 H 1 1.00 0.01 . 2 . . . . . . . . 5670 1 182 . 1 1 28 28 ILE HG21 H 1 0.66 0.01 . 1 . . . . . . . . 5670 1 183 . 1 1 28 28 ILE HG22 H 1 0.66 0.01 . 1 . . . . . . . . 5670 1 184 . 1 1 28 28 ILE HG23 H 1 0.66 0.01 . 1 . . . . . . . . 5670 1 185 . 1 1 28 28 ILE HD11 H 1 0.56 0.01 . 1 . . . . . . . . 5670 1 186 . 1 1 28 28 ILE HD12 H 1 0.56 0.01 . 1 . . . . . . . . 5670 1 187 . 1 1 28 28 ILE HD13 H 1 0.56 0.01 . 1 . . . . . . . . 5670 1 188 . 1 1 29 29 LEU H H 1 7.81 0.01 . 1 . . . . . . . . 5670 1 189 . 1 1 29 29 LEU HA H 1 3.81 0.01 . 1 . . . . . . . . 5670 1 190 . 1 1 29 29 LEU HB2 H 1 1.40 0.01 . 1 . . . . . . . . 5670 1 191 . 1 1 29 29 LEU HB3 H 1 1.40 0.01 . 1 . . . . . . . . 5670 1 192 . 1 1 29 29 LEU HG H 1 1.28 0.01 . 1 . . . . . . . . 5670 1 193 . 1 1 29 29 LEU HD11 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 194 . 1 1 29 29 LEU HD12 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 195 . 1 1 29 29 LEU HD13 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 196 . 1 1 29 29 LEU HD21 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 197 . 1 1 29 29 LEU HD22 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 198 . 1 1 29 29 LEU HD23 H 1 0.57 0.01 . 1 . . . . . . . . 5670 1 199 . 1 1 30 30 CYS H H 1 7.40 0.01 . 1 . . . . . . . . 5670 1 200 . 1 1 30 30 CYS HA H 1 4.51 0.01 . 1 . . . . . . . . 5670 1 201 . 1 1 30 30 CYS HB2 H 1 3.54 0.01 . 2 . . . . . . . . 5670 1 202 . 1 1 30 30 CYS HB3 H 1 2.65 0.01 . 2 . . . . . . . . 5670 1 203 . 1 1 31 31 ASP H H 1 7.70 0.01 . 1 . . . . . . . . 5670 1 204 . 1 1 31 31 ASP HA H 1 4.27 0.01 . 1 . . . . . . . . 5670 1 205 . 1 1 31 31 ASP HB2 H 1 3.36 0.01 . 2 . . . . . . . . 5670 1 206 . 1 1 31 31 ASP HB3 H 1 2.62 0.01 . 2 . . . . . . . . 5670 1 207 . 1 1 32 32 CYS H H 1 8.84 0.01 . 1 . . . . . . . . 5670 1 208 . 1 1 32 32 CYS HA H 1 5.24 0.01 . 1 . . . . . . . . 5670 1 209 . 1 1 32 32 CYS HB2 H 1 2.64 0.01 . 2 . . . . . . . . 5670 1 210 . 1 1 32 32 CYS HB3 H 1 1.79 0.01 . 2 . . . . . . . . 5670 1 211 . 1 1 33 33 ILE H H 1 8.64 0.01 . 1 . . . . . . . . 5670 1 212 . 1 1 33 33 ILE HA H 1 4.25 0.01 . 1 . . . . . . . . 5670 1 213 . 1 1 33 33 ILE HB H 1 1.40 0.01 . 1 . . . . . . . . 5670 1 214 . 1 1 33 33 ILE HG12 H 1 0.573 0.01 . 2 . . . . . . . . 5670 1 215 . 1 1 33 33 ILE HG13 H 1 -0.07 0.01 . 2 . . . . . . . . 5670 1 216 . 1 1 33 33 ILE HG21 H 1 0.03 0.01 . 1 . . . . . . . . 5670 1 217 . 1 1 33 33 ILE HG22 H 1 0.03 0.01 . 1 . . . . . . . . 5670 1 218 . 1 1 33 33 ILE HG23 H 1 0.03 0.01 . 1 . . . . . . . . 5670 1 219 . 1 1 33 33 ILE HD11 H 1 -0.01 0.01 . 1 . . . . . . . . 5670 1 220 . 1 1 33 33 ILE HD12 H 1 -0.01 0.01 . 1 . . . . . . . . 5670 1 221 . 1 1 33 33 ILE HD13 H 1 -0.01 0.01 . 1 . . . . . . . . 5670 1 222 . 1 1 34 34 HIS H H 1 8.52 0.01 . 1 . . . . . . . . 5670 1 223 . 1 1 34 34 HIS HA H 1 4.82 0.01 . 1 . . . . . . . . 5670 1 224 . 1 1 34 34 HIS HB2 H 1 2.73 0.01 . 2 . . . . . . . . 5670 1 225 . 1 1 34 34 HIS HB3 H 1 2.69 0.01 . 2 . . . . . . . . 5670 1 226 . 1 1 34 34 HIS HD1 H 1 8.52 0.01 . 4 . . . . . . . . 5670 1 227 . 1 1 35 35 VAL H H 1 7.96 0.01 . 1 . . . . . . . . 5670 1 228 . 1 1 35 35 VAL HA H 1 4.44 0.01 . 1 . . . . . . . . 5670 1 229 . 1 1 35 35 VAL HB H 1 1.99 0.01 . 1 . . . . . . . . 5670 1 230 . 1 1 35 35 VAL HG11 H 1 0.44 0.01 . 2 . . . . . . . . 5670 1 231 . 1 1 35 35 VAL HG12 H 1 0.44 0.01 . 2 . . . . . . . . 5670 1 232 . 1 1 35 35 VAL HG13 H 1 0.44 0.01 . 2 . . . . . . . . 5670 1 233 . 1 1 35 35 VAL HG21 H 1 0.39 0.01 . 2 . . . . . . . . 5670 1 234 . 1 1 35 35 VAL HG22 H 1 0.39 0.01 . 2 . . . . . . . . 5670 1 235 . 1 1 35 35 VAL HG23 H 1 0.39 0.01 . 2 . . . . . . . . 5670 1 236 . 1 1 36 36 THR H H 1 8.54 0.01 . 1 . . . . . . . . 5670 1 237 . 1 1 36 36 THR HA H 1 4.15 0.01 . 5 . . . . . . . . 5670 1 238 . 1 1 37 37 THR H H 1 6.65 0.01 . 1 . . . . . . . . 5670 1 239 . 1 1 37 37 THR HA H 1 4.17 0.01 . 1 . . . . . . . . 5670 1 240 . 1 1 37 37 THR HB H 1 4.31 0.01 . 1 . . . . . . . . 5670 1 241 . 1 1 37 37 THR HG21 H 1 0.91 0.01 . 1 . . . . . . . . 5670 1 242 . 1 1 37 37 THR HG22 H 1 0.91 0.01 . 1 . . . . . . . . 5670 1 243 . 1 1 37 37 THR HG23 H 1 0.91 0.01 . 1 . . . . . . . . 5670 1 244 . 1 1 38 38 THR H H 1 8.22 0.01 . 1 . . . . . . . . 5670 1 245 . 1 1 38 38 THR HA H 1 3.79 0.01 . 1 . . . . . . . . 5670 1 246 . 1 1 38 38 THR HB H 1 4.02 0.01 . 1 . . . . . . . . 5670 1 247 . 1 1 38 38 THR HG21 H 1 0.93 0.01 . 1 . . . . . . . . 5670 1 248 . 1 1 38 38 THR HG22 H 1 0.93 0.01 . 1 . . . . . . . . 5670 1 249 . 1 1 38 38 THR HG23 H 1 0.93 0.01 . 1 . . . . . . . . 5670 1 250 . 1 1 39 39 THR H H 1 6.78 0.01 . 1 . . . . . . . . 5670 1 251 . 1 1 39 39 THR HA H 1 4.16 0.01 . 1 . . . . . . . . 5670 1 252 . 1 1 39 39 THR HB H 1 3.79 0.01 . 1 . . . . . . . . 5670 1 253 . 1 1 39 39 THR HG21 H 1 0.82 0.01 . 1 . . . . . . . . 5670 1 254 . 1 1 39 39 THR HG22 H 1 0.82 0.01 . 1 . . . . . . . . 5670 1 255 . 1 1 39 39 THR HG23 H 1 0.82 0.01 . 1 . . . . . . . . 5670 1 256 . 1 1 40 40 CYS H H 1 8.57 0.01 . 1 . . . . . . . . 5670 1 257 . 1 1 40 40 CYS HA H 1 4.59 0.01 . 1 . . . . . . . . 5670 1 258 . 1 1 40 40 CYS HB2 H 1 3.55 0.01 . 2 . . . . . . . . 5670 1 259 . 1 1 40 40 CYS HB3 H 1 2.14 0.01 . 2 . . . . . . . . 5670 1 260 . 1 1 41 41 PRO HA H 1 4.29 0.01 . 1 . . . . . . . . 5670 1 261 . 1 1 41 41 PRO HB2 H 1 1.98 0.01 . 2 . . . . . . . . 5670 1 262 . 1 1 41 41 PRO HB3 H 1 1.84 0.01 . 2 . . . . . . . . 5670 1 263 . 1 1 41 41 PRO HG2 H 1 1.50 0.01 . 1 . . . . . . . . 5670 1 264 . 1 1 41 41 PRO HG3 H 1 1.50 0.01 . 1 . . . . . . . . 5670 1 265 . 1 1 41 41 PRO HD2 H 1 3.51 0.01 . 2 . . . . . . . . 5670 1 266 . 1 1 41 41 PRO HD3 H 1 3.30 0.01 . 2 . . . . . . . . 5670 1 267 . 1 1 42 42 SER H H 1 8.55 0.01 . 1 . . . . . . . . 5670 1 268 . 1 1 42 42 SER HA H 1 3.71 0.01 . 4 . . . . . . . . 5670 1 269 . 1 1 42 42 SER HB2 H 1 3.59 0.01 . 4 . . . . . . . . 5670 1 270 . 1 1 42 42 SER HB3 H 1 3.59 0.01 . 4 . . . . . . . . 5670 1 271 . 1 1 43 43 SER H H 1 7.62 0.01 . 1 . . . . . . . . 5670 1 272 . 1 1 43 43 SER HA H 1 3.87 0.01 . 1 . . . . . . . . 5670 1 273 . 1 1 43 43 SER HB2 H 1 3.76 0.01 . 2 . . . . . . . . 5670 1 274 . 1 1 43 43 SER HB3 H 1 3.65 0.01 . 2 . . . . . . . . 5670 1 275 . 1 1 44 44 HIS H H 1 7.41 0.01 . 1 . . . . . . . . 5670 1 276 . 1 1 44 44 HIS HA H 1 4.37 0.01 . 1 . . . . . . . . 5670 1 277 . 1 1 44 44 HIS HB2 H 1 2.21 0.01 . 2 . . . . . . . . 5670 1 278 . 1 1 44 44 HIS HB3 H 1 2.01 0.01 . 2 . . . . . . . . 5670 1 279 . 1 1 44 44 HIS HD2 H 1 6.72 0.01 . 1 . . . . . . . . 5670 1 280 . 1 1 44 44 HIS HE1 H 1 8.44 0.01 . 1 . . . . . . . . 5670 1 281 . 1 1 45 45 PRO HA H 1 4.00 0.01 . 1 . . . . . . . . 5670 1 282 . 1 1 45 45 PRO HB2 H 1 1.66 0.01 . 4 . . . . . . . . 5670 1 283 . 1 1 45 45 PRO HB3 H 1 1.66 0.01 . 4 . . . . . . . . 5670 1 284 . 1 1 45 45 PRO HG2 H 1 1.66 0.01 . 4 . . . . . . . . 5670 1 285 . 1 1 45 45 PRO HG3 H 1 1.66 0.01 . 4 . . . . . . . . 5670 1 286 . 1 1 45 45 PRO HD2 H 1 3.42 0.01 . 2 . . . . . . . . 5670 1 287 . 1 1 45 45 PRO HD3 H 1 3.07 0.01 . 2 . . . . . . . . 5670 1 288 . 1 1 46 46 SER H H 1 7.78 0.01 . 1 . . . . . . . . 5670 1 289 . 1 1 46 46 SER HA H 1 4.04 0.01 . 1 . . . . . . . . 5670 1 290 . 1 1 46 46 SER HB2 H 1 3.42 0.01 . 2 . . . . . . . . 5670 1 291 . 1 1 46 46 SER HB3 H 1 2.56 0.01 . 2 . . . . . . . . 5670 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 37 5670 1 1 36 5670 1 1 35 5670 1 1 34 5670 1 2 77 5670 1 2 76 5670 1 2 75 5670 1 2 74 5670 1 3 95 5670 1 3 94 5670 1 3 93 5670 1 3 92 5670 1 4 123 5670 1 4 122 5670 1 4 121 5670 1 4 120 5670 1 5 132 5670 1 5 131 5670 1 5 130 5670 1 5 129 5670 1 5 128 5670 1 6 270 5670 1 6 269 5670 1 6 268 5670 1 7 285 5670 1 7 284 5670 1 7 283 5670 1 7 282 5670 1 stop_ save_