data_5028 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5028 _Entry.Title ; Solution Structure of MCOTI-II, a Macrocyclic Trypsin Inhibitor ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-05-22 _Entry.Accession_date 2001-05-22 _Entry.Last_release_date 2001-05-22 _Entry.Original_release_date 2001-05-22 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 M. Felizmenio-Quimio . F. . . 5028 2 N. Daly . L. . . 5028 3 D. Craik . J. . . 5028 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5028 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 210 5028 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 . . 2001-05-23 . original BMRB . 5028 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1IB9 'BMRB Entry Tracking System' 5028 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5028 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Circular Proteins in Plants: Solution Structure of a Novel Macrocyclic Trypsin Inhibitor from Momordica cochinchinensis ; _Citation.Status 'in press' _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _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 2001 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Felizmenio-Quimio . F. . . 5028 1 2 N. Daly . L. . . 5028 1 3 D. Craik . J. . . 5028 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Cyclic cystine knot' 5028 1 beta-hairpin 5028 1 'circular protein' 5028 1 cyclotide 5028 1 stop_ save_ save_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode reference_1 _Citation.Entry_ID 5028 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10801322 _Citation.Full_citation ; Hernandez JF, Gagnon J, Chiche L, Nguyen TM, Andrieu JP, Heitz A, Trinh Hong T, Pham TT, Le Nguyen D. Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. Biochemistry. 2000 May 16;39(19):5722-30. ; _Citation.Title ; Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 39 _Citation.Journal_issue 19 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 5722 _Citation.Page_last 5730 _Citation.Year 2000 _Citation.Details ; Three trypsin inhibitors (TIs), from the seeds of the squash Momordica cochinchinensis (MCo), have been isolated and purified using gel filtration, ion exchange chromatography, and reverse-phase HPLC. Their sequences could be determined only after proteolytic cleavages. In the case of MCoTI-I and -II, it was shown that their polypeptide backbones are cyclic, a structure that has never been described in squash TIs. They contain 34 amino acid residues with 3 disulfide bridges and measured molecular masses of 3453.0 and 3480.7, respectively. They are the largest known macrocyclic peptides containing disulfide bridges. Their sequences show strong homology to other squash TIs, suggesting a similar three-dimensional structure and an analogous mechanism of action. A model of MCoTI-II was constructed by analogy to the crystal structure of the complex between bovine trypsin and CMTI-I, indicating that the linker connecting the two termini is flexible and does not impose significant geometrical constraints. This flexibility allows an Asp-Gly peptide bond rearrangement to occur in this region, giving rise to two isoforms of MCoTI-II. Although the importance of cyclization is not clear, it might confer increased stability and resistance to proteolysis. A minor species, MCoTI-III, was also characterized as containing 30 amino acid residues with a molecular mass of 3379.6. This component possesses a linear backbone with a blocked N-terminus. MCoTIs represent interesting candidates for drug design, either by changing their specificity of inhibition or by using their structure as natural scaffolds bearing new binding activities. ; 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 'J. F.' Hernandez J. F. . . 5028 2 2 J. Gagnon J. . . . 5028 2 3 L. Chiche L. . . . 5028 2 4 'T. M.' Nguyen T. M. . . 5028 2 5 'J. P.' Andrieu J. P. . . 5028 2 6 A. Heitz A. . . . 5028 2 7 T. 'Trinh Hong' T. . . . 5028 2 8 'T. T.' Pham T. T. . . 5028 2 9 D. 'Le Nguyen' D. . . . 5028 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_MCoTI_II _Assembly.Sf_category assembly _Assembly.Sf_framecode system_MCoTI_II _Assembly.Entry_ID 5028 _Assembly.ID 1 _Assembly.Name 'TRYPSIN INHIBITOR II' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5028 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 'MCoTI II' 1 $MCoTI_II . . . native . . . . . 5028 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 25 25 SG . . . . . . . . . . . . 5028 1 2 disulfide single . 1 . 1 CYS 15 15 SG . 1 . 1 CYS 27 27 SG . . . . . . . . . . . . 5028 1 3 disulfide single . 1 . 1 CYS 21 21 SG . 1 . 1 CYS 33 33 SG . . . . . . . . . . . . 5028 1 4 peptide single . 1 . 1 SER 1 1 N . 1 . 1 GLY 34 34 C . . . . . . . . . . . . 5028 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1IB9 . . . . . . 5028 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'MCoTI II' abbreviation 5028 1 'TRYPSIN INHIBITOR II' system 5028 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'trypsin inhibitor' 5028 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_MCoTI_II _Entity.Sf_category entity _Entity.Sf_framecode MCoTI_II _Entity.Entry_ID 5028 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'MCoTI II' _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 ; SGSDGGVCPKILKKCRRDSD CPGACICRGNGYCG ; _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 34 _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 3453 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 5176 . MCoTI-II . . . . . 100.00 34 100.00 100.00 4.33e-10 . . . . 5028 1 2 no BMRB 7361 . lin_MCoTI . . . . . 82.35 29 100.00 100.00 3.98e-07 . . . . 5028 1 3 no PDB 1HA9 . 'Solution Structure Of The Squash Trypsin Inhibitor Mcoti-Ii, Nmr, 30 Structures.' . . . . . 97.06 34 100.00 100.00 1.23e-09 . . . . 5028 1 4 no PDB 1IB9 . 'Solution Structure Of Mcoti-Ii, A Macrocyclic Trypsin Inhibitor' . . . . . 97.06 34 100.00 100.00 1.23e-09 . . . . 5028 1 5 no PDB 2IT8 . 'Solution Structure Of A Linear Analog Of The Cyclic Squash Trypsin Inhibitor Mcoti-Ii' . . . . . 85.29 30 100.00 100.00 1.29e-07 . . . . 5028 1 6 no PDB 2PO8 . 'The Structure Of A Two-Disulfide Intermediate Of Mcoti-Ii' . . . . . 79.41 34 100.00 100.00 1.07e-06 . . . . 5028 1 7 no SWISS-PROT P82409 . 'Trypsin inhibitor 2 (Trypsin inhibitor II) (MCoTI-II)' . . . . . 100.00 34 100.00 100.00 4.33e-10 . . . . 5028 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'MCoTI II' abbreviation 5028 1 'MCoTI II' common 5028 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 . SER . 5028 1 2 . GLY . 5028 1 3 . SER . 5028 1 4 . ASP . 5028 1 5 . GLY . 5028 1 6 . GLY . 5028 1 7 . VAL . 5028 1 8 . CYS . 5028 1 9 . PRO . 5028 1 10 . LYS . 5028 1 11 . ILE . 5028 1 12 . LEU . 5028 1 13 . LYS . 5028 1 14 . LYS . 5028 1 15 . CYS . 5028 1 16 . ARG . 5028 1 17 . ARG . 5028 1 18 . ASP . 5028 1 19 . SER . 5028 1 20 . ASP . 5028 1 21 . CYS . 5028 1 22 . PRO . 5028 1 23 . GLY . 5028 1 24 . ALA . 5028 1 25 . CYS . 5028 1 26 . ILE . 5028 1 27 . CYS . 5028 1 28 . ARG . 5028 1 29 . GLY . 5028 1 30 . ASN . 5028 1 31 . GLY . 5028 1 32 . TYR . 5028 1 33 . CYS . 5028 1 34 . GLY . 5028 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 . SER 1 1 5028 1 . GLY 2 2 5028 1 . SER 3 3 5028 1 . ASP 4 4 5028 1 . GLY 5 5 5028 1 . GLY 6 6 5028 1 . VAL 7 7 5028 1 . CYS 8 8 5028 1 . PRO 9 9 5028 1 . LYS 10 10 5028 1 . ILE 11 11 5028 1 . LEU 12 12 5028 1 . LYS 13 13 5028 1 . LYS 14 14 5028 1 . CYS 15 15 5028 1 . ARG 16 16 5028 1 . ARG 17 17 5028 1 . ASP 18 18 5028 1 . SER 19 19 5028 1 . ASP 20 20 5028 1 . CYS 21 21 5028 1 . PRO 22 22 5028 1 . GLY 23 23 5028 1 . ALA 24 24 5028 1 . CYS 25 25 5028 1 . ILE 26 26 5028 1 . CYS 27 27 5028 1 . ARG 28 28 5028 1 . GLY 29 29 5028 1 . ASN 30 30 5028 1 . GLY 31 31 5028 1 . TYR 32 32 5028 1 . CYS 33 33 5028 1 . GLY 34 34 5028 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 5028 _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 $MCoTI_II . 3674 organism . 'Momordica cochinchinensis' 'spiny bitter cucumber' . . Eukaryota Viridiplantae Momordica cochinchinensis . . . seed . . . . . . . . . 5028 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 5028 _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 $MCoTI_II . 'purified from the natural source' . . . . . . . . . . . . . . . . 5028 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5028 _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 'MCoTI II' . . . 1 $MCoTI_II . . 1 . . mM . . . . 5028 1 2 H2O . . . . . . . 90 . . % . . . . 5028 1 3 D2O . . . . . . . 10 . . % . . . . 5028 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 5028 _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 5028 1 pressure 1 . atm 5028 1 temperature 293 1 K 5028 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5028 _Software.ID 1 _Software.Type . _Software.Name xwinnmr _Software.Version 2.6 _Software.DOI . _Software.Details Bruker loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 5028 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 5028 _Software.ID 2 _Software.Type . _Software.Name XEASY _Software.Version 1.3.7 _Software.DOI . _Software.Details 'Eccles, Guntert, Billeter, and Wuthrich.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5028 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 5028 _Software.ID 3 _Software.Type . _Software.Name DYANA _Software.Version 1.5 _Software.DOI . _Software.Details 'Guntert, Mumenthaler, and Wuthrich.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 5028 3 stop_ save_ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 5028 _Software.ID 4 _Software.Type . _Software.Name X-PLOR _Software.Version 3.851 _Software.DOI . _Software.Details Brunger loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 5028 4 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 5028 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _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 5028 _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 AVANCE . 750 . . . 5028 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 5028 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5028 1 2 DQF-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5028 1 3 E-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5028 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_ref_1 _Chem_shift_reference.Entry_ID 5028 _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 . . . . . 5028 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_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 5028 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_ref_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D NOESY' 1 $sample_1 . 5028 1 2 DQF-COSY 1 $sample_1 . 5028 1 3 E-COSY 1 $sample_1 . 5028 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 SER H H 1 8.852 0.02 . 1 . . . . . . . . . 5028 1 2 . 1 1 1 1 SER HA H 1 4.529 0.02 . 1 . . . . . . . . . 5028 1 3 . 1 1 1 1 SER HB2 H 1 3.933 0.02 . 1 . . . . . . . . . 5028 1 4 . 1 1 1 1 SER HB3 H 1 3.933 0.02 . 1 . . . . . . . . . 5028 1 5 . 1 1 2 2 GLY H H 1 9.189 0.02 . 1 . . . . . . . . . 5028 1 6 . 1 1 2 2 GLY HA2 H 1 4.443 0.02 . 2 . . . . . . . . . 5028 1 7 . 1 1 2 2 GLY HA3 H 1 3.898 0.02 . 2 . . . . . . . . . 5028 1 8 . 1 1 3 3 SER H H 1 8.738 0.02 . 1 . . . . . . . . . 5028 1 9 . 1 1 3 3 SER HA H 1 4.486 0.02 . 1 . . . . . . . . . 5028 1 10 . 1 1 3 3 SER HB2 H 1 3.915 0.02 . 1 . . . . . . . . . 5028 1 11 . 1 1 3 3 SER HB3 H 1 3.915 0.02 . 1 . . . . . . . . . 5028 1 12 . 1 1 4 4 ASP H H 1 8.621 0.02 . 1 . . . . . . . . . 5028 1 13 . 1 1 4 4 ASP HA H 1 4.824 0.02 . 1 . . . . . . . . . 5028 1 14 . 1 1 4 4 ASP HB2 H 1 2.947 0.02 . 2 . . . . . . . . . 5028 1 15 . 1 1 4 4 ASP HB3 H 1 2.862 0.02 . 2 . . . . . . . . . 5028 1 16 . 1 1 5 5 GLY H H 1 8.25 0.02 . 1 . . . . . . . . . 5028 1 17 . 1 1 5 5 GLY HA2 H 1 4.11 0.02 . 2 . . . . . . . . . 5028 1 18 . 1 1 5 5 GLY HA3 H 1 3.834 0.02 . 2 . . . . . . . . . 5028 1 19 . 1 1 6 6 GLY H H 1 8.162 0.02 . 1 . . . . . . . . . 5028 1 20 . 1 1 6 6 GLY HA2 H 1 3.93 0.02 . 1 . . . . . . . . . 5028 1 21 . 1 1 6 6 GLY HA3 H 1 3.93 0.02 . 1 . . . . . . . . . 5028 1 22 . 1 1 7 7 VAL H H 1 8.542 0.02 . 1 . . . . . . . . . 5028 1 23 . 1 1 7 7 VAL HA H 1 4.016 0.02 . 1 . . . . . . . . . 5028 1 24 . 1 1 7 7 VAL HB H 1 1.991 0.02 . 1 . . . . . . . . . 5028 1 25 . 1 1 7 7 VAL HG11 H 1 0.943 0.02 . 1 . . . . . . . . . 5028 1 26 . 1 1 7 7 VAL HG12 H 1 0.943 0.02 . 1 . . . . . . . . . 5028 1 27 . 1 1 7 7 VAL HG13 H 1 0.943 0.02 . 1 . . . . . . . . . 5028 1 28 . 1 1 7 7 VAL HG21 H 1 0.839 0.02 . 1 . . . . . . . . . 5028 1 29 . 1 1 7 7 VAL HG22 H 1 0.839 0.02 . 1 . . . . . . . . . 5028 1 30 . 1 1 7 7 VAL HG23 H 1 0.839 0.02 . 1 . . . . . . . . . 5028 1 31 . 1 1 8 8 CYS H H 1 8.75 0.02 . 1 . . . . . . . . . 5028 1 32 . 1 1 8 8 CYS HA H 1 5.198 0.02 . 1 . . . . . . . . . 5028 1 33 . 1 1 8 8 CYS HB2 H 1 2.875 0.02 . 1 . . . . . . . . . 5028 1 34 . 1 1 8 8 CYS HB3 H 1 2.875 0.02 . 1 . . . . . . . . . 5028 1 35 . 1 1 9 9 PRO HA H 1 4.371 0.02 . 1 . . . . . . . . . 5028 1 36 . 1 1 9 9 PRO HB2 H 1 2.31 0.02 . 2 . . . . . . . . . 5028 1 37 . 1 1 9 9 PRO HB3 H 1 1.862 0.02 . 2 . . . . . . . . . 5028 1 38 . 1 1 9 9 PRO HG2 H 1 2.007 0.02 . 2 . . . . . . . . . 5028 1 39 . 1 1 9 9 PRO HG3 H 1 1.947 0.02 . 2 . . . . . . . . . 5028 1 40 . 1 1 9 9 PRO HD2 H 1 3.853 0.02 . 1 . . . . . . . . . 5028 1 41 . 1 1 9 9 PRO HD3 H 1 3.853 0.02 . 1 . . . . . . . . . 5028 1 42 . 1 1 10 10 LYS H H 1 8.29 0.02 . 1 . . . . . . . . . 5028 1 43 . 1 1 10 10 LYS HA H 1 4.263 0.02 . 1 . . . . . . . . . 5028 1 44 . 1 1 10 10 LYS HB2 H 1 1.829 0.02 . 2 . . . . . . . . . 5028 1 45 . 1 1 10 10 LYS HB3 H 1 1.704 0.02 . 2 . . . . . . . . . 5028 1 46 . 1 1 10 10 LYS HG2 H 1 1.367 0.02 . 1 . . . . . . . . . 5028 1 47 . 1 1 10 10 LYS HG3 H 1 1.367 0.02 . 1 . . . . . . . . . 5028 1 48 . 1 1 10 10 LYS HD2 H 1 1.481 0.02 . 1 . . . . . . . . . 5028 1 49 . 1 1 10 10 LYS HD3 H 1 1.481 0.02 . 1 . . . . . . . . . 5028 1 50 . 1 1 10 10 LYS HE2 H 1 2.993 0.02 . 1 . . . . . . . . . 5028 1 51 . 1 1 10 10 LYS HE3 H 1 2.993 0.02 . 1 . . . . . . . . . 5028 1 52 . 1 1 10 10 LYS HZ1 H 1 7.542 0.02 . 1 . . . . . . . . . 5028 1 53 . 1 1 10 10 LYS HZ2 H 1 7.542 0.02 . 1 . . . . . . . . . 5028 1 54 . 1 1 10 10 LYS HZ3 H 1 7.542 0.02 . 1 . . . . . . . . . 5028 1 55 . 1 1 11 11 ILE H H 1 7.752 0.02 . 1 . . . . . . . . . 5028 1 56 . 1 1 11 11 ILE HA H 1 4.387 0.02 . 1 . . . . . . . . . 5028 1 57 . 1 1 11 11 ILE HB H 1 1.795 0.02 . 1 . . . . . . . . . 5028 1 58 . 1 1 11 11 ILE HG12 H 1 1.356 0.02 . 1 . . . . . . . . . 5028 1 59 . 1 1 11 11 ILE HG13 H 1 1.356 0.02 . 1 . . . . . . . . . 5028 1 60 . 1 1 11 11 ILE HG21 H 1 0.831 0.02 . 1 . . . . . . . . . 5028 1 61 . 1 1 11 11 ILE HG22 H 1 0.831 0.02 . 1 . . . . . . . . . 5028 1 62 . 1 1 11 11 ILE HG23 H 1 0.831 0.02 . 1 . . . . . . . . . 5028 1 63 . 1 1 11 11 ILE HD11 H 1 1.07 0.02 . 1 . . . . . . . . . 5028 1 64 . 1 1 11 11 ILE HD12 H 1 1.07 0.02 . 1 . . . . . . . . . 5028 1 65 . 1 1 11 11 ILE HD13 H 1 1.07 0.02 . 1 . . . . . . . . . 5028 1 66 . 1 1 12 12 LEU H H 1 8.736 0.02 . 1 . . . . . . . . . 5028 1 67 . 1 1 12 12 LEU HA H 1 4.548 0.02 . 1 . . . . . . . . . 5028 1 68 . 1 1 12 12 LEU HB2 H 1 1.747 0.02 . 1 . . . . . . . . . 5028 1 69 . 1 1 12 12 LEU HB3 H 1 1.747 0.02 . 1 . . . . . . . . . 5028 1 70 . 1 1 12 12 LEU HG H 1 1.478 0.02 . 1 . . . . . . . . . 5028 1 71 . 1 1 12 12 LEU HD11 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 72 . 1 1 12 12 LEU HD12 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 73 . 1 1 12 12 LEU HD13 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 74 . 1 1 12 12 LEU HD21 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 75 . 1 1 12 12 LEU HD22 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 76 . 1 1 12 12 LEU HD23 H 1 0.767 0.02 . 1 . . . . . . . . . 5028 1 77 . 1 1 13 13 LYS H H 1 8.946 0.02 . 1 . . . . . . . . . 5028 1 78 . 1 1 13 13 LYS HA H 1 4.592 0.02 . 1 . . . . . . . . . 5028 1 79 . 1 1 13 13 LYS HB2 H 1 1.606 0.02 . 2 . . . . . . . . . 5028 1 80 . 1 1 13 13 LYS HB3 H 1 1.566 0.02 . 2 . . . . . . . . . 5028 1 81 . 1 1 13 13 LYS HG2 H 1 1.414 0.02 . 1 . . . . . . . . . 5028 1 82 . 1 1 13 13 LYS HG3 H 1 1.414 0.02 . 1 . . . . . . . . . 5028 1 83 . 1 1 13 13 LYS HD2 H 1 1.754 0.02 . 1 . . . . . . . . . 5028 1 84 . 1 1 13 13 LYS HD3 H 1 1.754 0.02 . 1 . . . . . . . . . 5028 1 85 . 1 1 13 13 LYS HE2 H 1 3.089 0.02 . 1 . . . . . . . . . 5028 1 86 . 1 1 13 13 LYS HE3 H 1 3.089 0.02 . 1 . . . . . . . . . 5028 1 87 . 1 1 13 13 LYS HZ1 H 1 7.626 0.02 . 1 . . . . . . . . . 5028 1 88 . 1 1 13 13 LYS HZ2 H 1 7.626 0.02 . 1 . . . . . . . . . 5028 1 89 . 1 1 13 13 LYS HZ3 H 1 7.626 0.02 . 1 . . . . . . . . . 5028 1 90 . 1 1 14 14 LYS H H 1 8.672 0.02 . 1 . . . . . . . . . 5028 1 91 . 1 1 14 14 LYS HA H 1 4.316 0.02 . 1 . . . . . . . . . 5028 1 92 . 1 1 14 14 LYS HB2 H 1 1.643 0.02 . 2 . . . . . . . . . 5028 1 93 . 1 1 14 14 LYS HB3 H 1 1.513 0.02 . 2 . . . . . . . . . 5028 1 94 . 1 1 14 14 LYS HG2 H 1 0.937 0.02 . 1 . . . . . . . . . 5028 1 95 . 1 1 14 14 LYS HG3 H 1 0.937 0.02 . 1 . . . . . . . . . 5028 1 96 . 1 1 14 14 LYS HD2 H 1 1.309 0.02 . 1 . . . . . . . . . 5028 1 97 . 1 1 14 14 LYS HD3 H 1 1.309 0.02 . 1 . . . . . . . . . 5028 1 98 . 1 1 14 14 LYS HE2 H 1 2.93 0.02 . 1 . . . . . . . . . 5028 1 99 . 1 1 14 14 LYS HE3 H 1 2.93 0.02 . 1 . . . . . . . . . 5028 1 100 . 1 1 14 14 LYS HZ1 H 1 7.474 0.02 . 1 . . . . . . . . . 5028 1 101 . 1 1 14 14 LYS HZ2 H 1 7.474 0.02 . 1 . . . . . . . . . 5028 1 102 . 1 1 14 14 LYS HZ3 H 1 7.474 0.02 . 1 . . . . . . . . . 5028 1 103 . 1 1 15 15 CYS H H 1 8.437 0.02 . 1 . . . . . . . . . 5028 1 104 . 1 1 15 15 CYS HA H 1 4.888 0.02 . 1 . . . . . . . . . 5028 1 105 . 1 1 15 15 CYS HB2 H 1 3.198 0.02 . 2 . . . . . . . . . 5028 1 106 . 1 1 15 15 CYS HB3 H 1 2.932 0.02 . 2 . . . . . . . . . 5028 1 107 . 1 1 16 16 ARG H H 1 9.399 0.02 . 1 . . . . . . . . . 5028 1 108 . 1 1 16 16 ARG HA H 1 4.443 0.02 . 1 . . . . . . . . . 5028 1 109 . 1 1 16 16 ARG HB2 H 1 1.881 0.02 . 2 . . . . . . . . . 5028 1 110 . 1 1 16 16 ARG HB3 H 1 1.729 0.02 . 2 . . . . . . . . . 5028 1 111 . 1 1 16 16 ARG HG2 H 1 1.63 0.02 . 1 . . . . . . . . . 5028 1 112 . 1 1 16 16 ARG HG3 H 1 1.63 0.02 . 1 . . . . . . . . . 5028 1 113 . 1 1 16 16 ARG HD2 H 1 3.186 0.02 . 1 . . . . . . . . . 5028 1 114 . 1 1 16 16 ARG HD3 H 1 3.186 0.02 . 1 . . . . . . . . . 5028 1 115 . 1 1 16 16 ARG HE H 1 7.308 0.02 . 1 . . . . . . . . . 5028 1 116 . 1 1 17 17 ARG H H 1 8.081 0.02 . 1 . . . . . . . . . 5028 1 117 . 1 1 17 17 ARG HA H 1 4.742 0.02 . 1 . . . . . . . . . 5028 1 118 . 1 1 17 17 ARG HB2 H 1 2.034 0.02 . 2 . . . . . . . . . 5028 1 119 . 1 1 17 17 ARG HB3 H 1 1.793 0.02 . 2 . . . . . . . . . 5028 1 120 . 1 1 17 17 ARG HG2 H 1 1.559 0.02 . 2 . . . . . . . . . 5028 1 121 . 1 1 17 17 ARG HG3 H 1 1.457 0.02 . 2 . . . . . . . . . 5028 1 122 . 1 1 17 17 ARG HD2 H 1 3.153 0.02 . 1 . . . . . . . . . 5028 1 123 . 1 1 17 17 ARG HD3 H 1 3.153 0.02 . 1 . . . . . . . . . 5028 1 124 . 1 1 17 17 ARG HE H 1 7.169 0.02 . 1 . . . . . . . . . 5028 1 125 . 1 1 18 18 ASP H H 1 9.348 0.02 . 1 . . . . . . . . . 5028 1 126 . 1 1 18 18 ASP HA H 1 4.118 0.02 . 1 . . . . . . . . . 5028 1 127 . 1 1 18 18 ASP HB2 H 1 3.004 0.02 . 2 . . . . . . . . . 5028 1 128 . 1 1 18 18 ASP HB3 H 1 2.83 0.02 . 2 . . . . . . . . . 5028 1 129 . 1 1 19 19 SER H H 1 8.217 0.02 . 1 . . . . . . . . . 5028 1 130 . 1 1 19 19 SER HA H 1 4.303 0.02 . 1 . . . . . . . . . 5028 1 131 . 1 1 19 19 SER HB2 H 1 4.119 0.02 . 1 . . . . . . . . . 5028 1 132 . 1 1 19 19 SER HB3 H 1 3.834 0.02 . 1 . . . . . . . . . 5028 1 133 . 1 1 20 20 ASP H H 1 7.739 0.02 . 1 . . . . . . . . . 5028 1 134 . 1 1 20 20 ASP HA H 1 4.634 0.02 . 1 . . . . . . . . . 5028 1 135 . 1 1 20 20 ASP HB2 H 1 3.039 0.02 . 2 . . . . . . . . . 5028 1 136 . 1 1 20 20 ASP HB3 H 1 2.965 0.02 . 2 . . . . . . . . . 5028 1 137 . 1 1 21 21 CYS H H 1 8.16 0.02 . 1 . . . . . . . . . 5028 1 138 . 1 1 21 21 CYS HA H 1 5.063 0.02 . 1 . . . . . . . . . 5028 1 139 . 1 1 21 21 CYS HB2 H 1 2.845 0.02 . 1 . . . . . . . . . 5028 1 140 . 1 1 21 21 CYS HB3 H 1 2.674 0.02 . 1 . . . . . . . . . 5028 1 141 . 1 1 22 22 PRO HA H 1 4.624 0.02 . 1 . . . . . . . . . 5028 1 142 . 1 1 22 22 PRO HB2 H 1 2.26 0.02 . 2 . . . . . . . . . 5028 1 143 . 1 1 22 22 PRO HB3 H 1 1.938 0.02 . 2 . . . . . . . . . 5028 1 144 . 1 1 22 22 PRO HG2 H 1 2.099 0.02 . 2 . . . . . . . . . 5028 1 145 . 1 1 22 22 PRO HG3 H 1 2.041 0.02 . 2 . . . . . . . . . 5028 1 146 . 1 1 22 22 PRO HD2 H 1 3.742 0.02 . 2 . . . . . . . . . 5028 1 147 . 1 1 22 22 PRO HD3 H 1 3.43 0.02 . 2 . . . . . . . . . 5028 1 148 . 1 1 23 23 GLY H H 1 8.525 0.02 . 1 . . . . . . . . . 5028 1 149 . 1 1 23 23 GLY HA2 H 1 3.838 0.02 . 1 . . . . . . . . . 5028 1 150 . 1 1 23 23 GLY HA3 H 1 3.758 0.02 . 1 . . . . . . . . . 5028 1 151 . 1 1 24 24 ALA H H 1 8.451 0.02 . 1 . . . . . . . . . 5028 1 152 . 1 1 24 24 ALA HA H 1 4.537 0.02 . 1 . . . . . . . . . 5028 1 153 . 1 1 24 24 ALA HB1 H 1 1.366 0.02 . 1 . . . . . . . . . 5028 1 154 . 1 1 24 24 ALA HB2 H 1 1.366 0.02 . 1 . . . . . . . . . 5028 1 155 . 1 1 24 24 ALA HB3 H 1 1.366 0.02 . 1 . . . . . . . . . 5028 1 156 . 1 1 25 25 CYS H H 1 8.325 0.02 . 1 . . . . . . . . . 5028 1 157 . 1 1 25 25 CYS HA H 1 4.59 0.02 . 1 . . . . . . . . . 5028 1 158 . 1 1 25 25 CYS HB2 H 1 3.199 0.02 . 1 . . . . . . . . . 5028 1 159 . 1 1 25 25 CYS HB3 H 1 3.199 0.02 . 1 . . . . . . . . . 5028 1 160 . 1 1 26 26 ILE H H 1 9.083 0.02 . 1 . . . . . . . . . 5028 1 161 . 1 1 26 26 ILE HA H 1 4.427 0.02 . 1 . . . . . . . . . 5028 1 162 . 1 1 26 26 ILE HB H 1 1.928 0.02 . 1 . . . . . . . . . 5028 1 163 . 1 1 26 26 ILE HG12 H 1 1.071 0.02 . 1 . . . . . . . . . 5028 1 164 . 1 1 26 26 ILE HG13 H 1 1.071 0.02 . 1 . . . . . . . . . 5028 1 165 . 1 1 26 26 ILE HG21 H 1 0.853 0.02 . 1 . . . . . . . . . 5028 1 166 . 1 1 26 26 ILE HG22 H 1 0.853 0.02 . 1 . . . . . . . . . 5028 1 167 . 1 1 26 26 ILE HG23 H 1 0.853 0.02 . 1 . . . . . . . . . 5028 1 168 . 1 1 26 26 ILE HD11 H 1 0.973 0.02 . 1 . . . . . . . . . 5028 1 169 . 1 1 26 26 ILE HD12 H 1 0.973 0.02 . 1 . . . . . . . . . 5028 1 170 . 1 1 26 26 ILE HD13 H 1 0.973 0.02 . 1 . . . . . . . . . 5028 1 171 . 1 1 27 27 CYS H H 1 8.951 0.02 . 1 . . . . . . . . . 5028 1 172 . 1 1 27 27 CYS HA H 1 4.963 0.02 . 1 . . . . . . . . . 5028 1 173 . 1 1 27 27 CYS HB2 H 1 2.811 0.02 . 1 . . . . . . . . . 5028 1 174 . 1 1 27 27 CYS HB3 H 1 2.471 0.02 . 1 . . . . . . . . . 5028 1 175 . 1 1 28 28 ARG H H 1 8.086 0.02 . 1 . . . . . . . . . 5028 1 176 . 1 1 28 28 ARG HA H 1 4.325 0.02 . 1 . . . . . . . . . 5028 1 177 . 1 1 28 28 ARG HB2 H 1 2.507 0.02 . 2 . . . . . . . . . 5028 1 178 . 1 1 28 28 ARG HB3 H 1 2.067 0.02 . 2 . . . . . . . . . 5028 1 179 . 1 1 28 28 ARG HG2 H 1 1.751 0.02 . 2 . . . . . . . . . 5028 1 180 . 1 1 28 28 ARG HG3 H 1 1.606 0.02 . 2 . . . . . . . . . 5028 1 181 . 1 1 28 28 ARG HD2 H 1 3.254 0.02 . 1 . . . . . . . . . 5028 1 182 . 1 1 28 28 ARG HD3 H 1 3.254 0.02 . 1 . . . . . . . . . 5028 1 183 . 1 1 28 28 ARG HE H 1 6.99 0.02 . 2 . . . . . . . . . 5028 1 184 . 1 1 29 29 GLY H H 1 8.942 0.02 . 1 . . . . . . . . . 5028 1 185 . 1 1 29 29 GLY HA2 H 1 3.933 0.02 . 1 . . . . . . . . . 5028 1 186 . 1 1 29 29 GLY HA3 H 1 3.933 0.02 . 1 . . . . . . . . . 5028 1 187 . 1 1 30 30 ASN H H 1 7.822 0.02 . 1 . . . . . . . . . 5028 1 188 . 1 1 30 30 ASN HA H 1 4.706 0.02 . 1 . . . . . . . . . 5028 1 189 . 1 1 30 30 ASN HB2 H 1 3.331 0.02 . 1 . . . . . . . . . 5028 1 190 . 1 1 30 30 ASN HB3 H 1 2.867 0.02 . 1 . . . . . . . . . 5028 1 191 . 1 1 30 30 ASN HD21 H 1 7.59 0.02 . 2 . . . . . . . . . 5028 1 192 . 1 1 30 30 ASN HD22 H 1 6.634 0.02 . 2 . . . . . . . . . 5028 1 193 . 1 1 31 31 GLY H H 1 8.439 0.02 . 1 . . . . . . . . . 5028 1 194 . 1 1 31 31 GLY HA2 H 1 3.999 0.02 . 2 . . . . . . . . . 5028 1 195 . 1 1 31 31 GLY HA3 H 1 3.686 0.02 . 2 . . . . . . . . . 5028 1 196 . 1 1 32 32 TYR H H 1 7.302 0.02 . 1 . . . . . . . . . 5028 1 197 . 1 1 32 32 TYR HA H 1 5.267 0.02 . 1 . . . . . . . . . 5028 1 198 . 1 1 32 32 TYR HB2 H 1 3.073 0.02 . 1 . . . . . . . . . 5028 1 199 . 1 1 32 32 TYR HB3 H 1 2.652 0.02 . 1 . . . . . . . . . 5028 1 200 . 1 1 32 32 TYR HD1 H 1 6.882 0.02 . 1 . . . . . . . . . 5028 1 201 . 1 1 32 32 TYR HD2 H 1 6.882 0.02 . 1 . . . . . . . . . 5028 1 202 . 1 1 32 32 TYR HE1 H 1 6.707 0.02 . 1 . . . . . . . . . 5028 1 203 . 1 1 32 32 TYR HE2 H 1 6.707 0.02 . 1 . . . . . . . . . 5028 1 204 . 1 1 33 33 CYS H H 1 8.831 0.02 . 1 . . . . . . . . . 5028 1 205 . 1 1 33 33 CYS HA H 1 5.41 0.02 . 1 . . . . . . . . . 5028 1 206 . 1 1 33 33 CYS HB2 H 1 3.057 0.02 . 1 . . . . . . . . . 5028 1 207 . 1 1 33 33 CYS HB3 H 1 2.801 0.02 . 1 . . . . . . . . . 5028 1 208 . 1 1 34 34 GLY H H 1 9.838 0.02 . 1 . . . . . . . . . 5028 1 209 . 1 1 34 34 GLY HA2 H 1 4.522 0.02 . 2 . . . . . . . . . 5028 1 210 . 1 1 34 34 GLY HA3 H 1 3.967 0.02 . 2 . . . . . . . . . 5028 1 stop_ save_