data_17227 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17227 _Entry.Title ; SOLUTION STRUCTURE OF GS-alfa-Ktx5.4 SYNTHETIC SCORPION LIKE ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-09-30 _Entry.Accession_date 2010-09-30 _Entry.Last_release_date 2015-06-19 _Entry.Original_release_date 2015-06-19 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.77 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 'NMR, 18 STRUCTURES' _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 FEDERICO 'Del Rio-Portilla' F. . . 17227 2 BELEN Ramirez-Cordero B. E. . 17227 3 LUIS 'Brieba-De Castro' L. . . 17227 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 17227 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'ALFA HELIX' . 17227 'ALFA/BETA SCAFFOLD' . 17227 'BETA SHEET' . 17227 GS-alfa-Ktx5.4 . 17227 'Mesobuthus tamulus' . 17227 'POTASSIUM BLOCKER' . 17227 'SCORPION K+ TOXIN' . 17227 aKtx5.4 . 17227 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17227 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 201 17227 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 . . 2015-06-19 . original BMRB . 17227 stop_ save_ ############### # Citations # ############### save_citations_1 _Citation.Sf_category citations _Citation.Sf_framecode citations_1 _Citation.Entry_ID 17227 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24821061 _Citation.Full_citation . _Citation.Title ; Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Chem. Res. Toxicol.' _Citation.Journal_name_full . _Citation.Journal_volume 27 _Citation.Journal_issue 6 _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 960 _Citation.Page_last 967 _Citation.Year 2014 _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 B. Ramirez-Cordero B. E. . 17227 1 2 Y. Toledano . . . 17227 1 3 P. Cano-Sanchez P. . . 17227 1 4 R. Hernandez-Lopez R. . . 17227 1 5 D. Flores-Solis D. . . 17227 1 6 A. Saucedo-Yanez A. L. . 17227 1 7 I. Chavez-Uribe I. . . 17227 1 8 L. Brieba L. G. . 17227 1 9 F. 'Del Rio-Portilla' F. . . 17227 1 stop_ save_ save_citations_2 _Citation.Sf_category citations _Citation.Sf_framecode citations_2 _Citation.Entry_ID 17227 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Tamapin, a Venom Peptide from the Indian Red Scorpi (Mesobuthus Tamulus) Thet Targets Small Conductance Activated K+ Channels and Afterhyperpolarization Cu Central Neurons ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'Journal of Biological Chemis' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9258 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 F. 'Del Rio-Portilla' F. . . 17227 2 2 B. Ramirez-Cordero B. E. . 17227 2 3 L. 'Saucedo Yanez' L. Brieba . 17227 2 4 P. Cano-Sanchez P. . . 17227 2 5 R. Flores-Solis R. Hernandez-Lo . 17227 2 6 P. Pedarzani P. . . 17227 2 7 D. Dhoedet D. . . 17227 2 8 K. Doorty K. B. . 17227 2 9 J. Wadsworth J. D.F. . 17227 2 10 J Jeyaseelan J. K. . 17227 2 11 R. Kini R. M. . 17227 2 12 S. Gadre S. V. . 17227 2 13 S. Sapatnekar S. M. . 17227 2 14 M. Strong M. St . 17227 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17227 _Assembly.ID 1 _Assembly.Name 'GS-alfa-Ktx5.4 SCORPION TOXIN' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'GS-alfa-Ktx5.4 SCORPION TOXIN' 1 $GS-alfa-Ktx5-4_SCORPION_TOXIN A . yes native no no . . . 17227 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_GS-alfa-Ktx5-4_SCORPION_TOXIN _Entity.Sf_category entity _Entity.Sf_framecode GS-alfa-Ktx5-4_SCORPION_TOXIN _Entity.Entry_ID 17227 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name GS-alfa-Ktx5.4_SCORPION_TOXIN _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSAFCNLRRCELSCRSLGLL GKCIGEECKCVPY ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 33 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method syn _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3614.318 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 18513 . recombinant-tamapin . . . . . 93.94 31 100.00 100.00 1.50e-11 . . . . 17227 1 2 no BMRB 19519 . entity . . . . . 100.00 33 96.97 96.97 4.04e-12 . . . . 17227 1 3 no PDB 2KY3 . "Solution Structure Of Gs-alfa-ktx5.4 Synthetic Scorpion Like" . . . . . 96.97 33 100.00 100.00 7.78e-12 . . . . 17227 1 4 no PDB 2LU9 . "Nmr Solution Structure Of Recombinant Tamapin" . . . . . 90.91 31 100.00 100.00 1.60e-10 . . . . 17227 1 5 no SP P59869 . "RecName: Full=Potassium channel toxin alpha-KTx 5.4; AltName: Full=Tamapin" . . . . . 93.94 31 100.00 100.00 1.50e-11 . . . . 17227 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 . GLY . 17227 1 2 . SER . 17227 1 3 . ALA . 17227 1 4 . PHE . 17227 1 5 . CYS . 17227 1 6 . ASN . 17227 1 7 . LEU . 17227 1 8 . ARG . 17227 1 9 . ARG . 17227 1 10 . CYS . 17227 1 11 . GLU . 17227 1 12 . LEU . 17227 1 13 . SER . 17227 1 14 . CYS . 17227 1 15 . ARG . 17227 1 16 . SER . 17227 1 17 . LEU . 17227 1 18 . GLY . 17227 1 19 . LEU . 17227 1 20 . LEU . 17227 1 21 . GLY . 17227 1 22 . LYS . 17227 1 23 . CYS . 17227 1 24 . ILE . 17227 1 25 . GLY . 17227 1 26 . GLU . 17227 1 27 . GLU . 17227 1 28 . CYS . 17227 1 29 . LYS . 17227 1 30 . CYS . 17227 1 31 . VAL . 17227 1 32 . PRO . 17227 1 33 . TYR . 17227 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 . GLY 1 1 17227 1 . SER 2 2 17227 1 . ALA 3 3 17227 1 . PHE 4 4 17227 1 . CYS 5 5 17227 1 . ASN 6 6 17227 1 . LEU 7 7 17227 1 . ARG 8 8 17227 1 . ARG 9 9 17227 1 . CYS 10 10 17227 1 . GLU 11 11 17227 1 . LEU 12 12 17227 1 . SER 13 13 17227 1 . CYS 14 14 17227 1 . ARG 15 15 17227 1 . SER 16 16 17227 1 . LEU 17 17 17227 1 . GLY 18 18 17227 1 . LEU 19 19 17227 1 . LEU 20 20 17227 1 . GLY 21 21 17227 1 . LYS 22 22 17227 1 . CYS 23 23 17227 1 . ILE 24 24 17227 1 . GLY 25 25 17227 1 . GLU 26 26 17227 1 . GLU 27 27 17227 1 . CYS 28 28 17227 1 . LYS 29 29 17227 1 . CYS 30 30 17227 1 . VAL 31 31 17227 1 . PRO 32 32 17227 1 . TYR 33 33 17227 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 17227 _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 $GS-alfa-Ktx5-4_SCORPION_TOXIN . 34647 organism . 'Mesobuthus tamulus' 'Indian red scorpion' . . Eukaryota Metazoa Mesobuthus tamulus . . . . . . . . . . . . . 17227 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 17227 _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 $GS-alfa-Ktx5-4_SCORPION_TOXIN . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'Rosetta gami' DE3 . . . . 'Modified pET32a' . . . 17227 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17227 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '2.3 MM GS-alfaKtx5.4 95% H2O/5% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _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 'GS-alfa-Ktx5.4 SCORPION TOXIN' 'natural abundance' . . 1 $GS-alfa-Ktx5-4_SCORPION_TOXIN . . 1.8 . . mM . . . . 17227 1 2 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17227 1 3 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17227 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 17227 _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 6.5 . pH 17227 1 pressure 1 . atm 17227 1 temperature 297 . K 17227 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 17227 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 17227 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 17227 1 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 17227 _Software.ID 2 _Software.Name AMBER _Software.Version 9 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . 17227 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 17227 2 stop_ save_ save_XEASY_MOLMOL _Software.Sf_category software _Software.Sf_framecode XEASY_MOLMOL _Software.Entry_ID 17227 _Software.ID 3 _Software.Name XEASY_MOLMOL_2K.2 _Software.Version 2K.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bartels et al.' . . 17227 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17227 3 stop_ save_ save_PROCHECK _Software.Sf_category software _Software.Sf_framecode PROCHECK _Software.Entry_ID 17227 _Software.ID 4 _Software.Name Procheck _Software.Version 3.5.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho' . . 17227 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 17227 4 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 17227 _Software.ID 5 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 17227 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17227 5 stop_ save_ save_Molmol _Software.Sf_category software _Software.Sf_framecode Molmol _Software.Entry_ID 17227 _Software.ID 6 _Software.Name Molmol _Software.Version 2k.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Koradi, Billeter and Wuthrich' . . 17227 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 17227 6 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 17227 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer VARIAN _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 17227 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 17227 _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 spectrometer_1 VARIAN INOVA . 800 . . . 17227 1 2 spectrometer_2 Varian INOVA . 500 . . . 17227 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 17227 _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 NOESY no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17227 1 2 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17227 1 3 '2D DQF -COSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17227 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 17227 _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 external direct 1.0 . . . . . . . . . 17227 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17227 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.005 _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 NOESY . . . 17227 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 3 $XEASY_MOLMOL . . 17227 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 2 2 SER H H 1 8.629 0.005 . 1 . . . . 2 S H . 17227 1 2 . 1 1 2 2 SER HA H 1 4.512 0.001 . 1 . . . . 2 S HA . 17227 1 3 . 1 1 2 2 SER HB2 H 1 3.844 0.005 . 2 . . . . 2 S QB . 17227 1 4 . 1 1 2 2 SER HB3 H 1 3.844 0.005 . 2 . . . . 2 S QB . 17227 1 5 . 1 1 3 3 ALA H H 1 8.370 0.005 . 1 . . . . 3 A H . 17227 1 6 . 1 1 3 3 ALA HA H 1 4.385 0.005 . 1 . . . . 3 A HA . 17227 1 7 . 1 1 3 3 ALA HB1 H 1 1.327 0.005 . . . . . . 3 A QB . 17227 1 8 . 1 1 3 3 ALA HB2 H 1 1.327 0.005 . . . . . . 3 A QB . 17227 1 9 . 1 1 3 3 ALA HB3 H 1 1.327 0.005 . . . . . . 3 A QB . 17227 1 10 . 1 1 4 4 PHE H H 1 8.052 0.005 . 1 . . . . 4 F H . 17227 1 11 . 1 1 4 4 PHE HA H 1 4.650 0.005 . 1 . . . . 4 F HA . 17227 1 12 . 1 1 4 4 PHE HB2 H 1 3.112 0.005 . 2 . . . . 4 F HB2 . 17227 1 13 . 1 1 4 4 PHE HB3 H 1 2.988 0.005 . 2 . . . . 4 F HB3 . 17227 1 14 . 1 1 5 5 CYS H H 1 8.162 0.001 . 1 . . . . 5 C H . 17227 1 15 . 1 1 5 5 CYS HA H 1 4.406 0.001 . 1 . . . . 5 C HA . 17227 1 16 . 1 1 5 5 CYS HB2 H 1 2.796 0.004 . 2 . . . . 5 C HB2 . 17227 1 17 . 1 1 5 5 CYS HB3 H 1 2.708 0.005 . 2 . . . . 5 C HB3 . 17227 1 18 . 1 1 6 6 ASN H H 1 8.705 0.005 . 1 . . . . 6 N H . 17227 1 19 . 1 1 6 6 ASN HA H 1 4.820 0.005 . 1 . . . . 6 N HA . 17227 1 20 . 1 1 6 6 ASN HB2 H 1 2.900 0.005 . 2 . . . . 6 N HB2 . 17227 1 21 . 1 1 6 6 ASN HB3 H 1 2.777 0.005 . 2 . . . . 6 N HB3 . 17227 1 22 . 1 1 7 7 LEU H H 1 8.799 0.005 . 1 . . . . 7 L H . 17227 1 23 . 1 1 7 7 LEU HA H 1 3.989 0.003 . 1 . . . . 7 L HA . 17227 1 24 . 1 1 7 7 LEU HB2 H 1 1.787 0.005 . 2 . . . . 7 L HB2 . 17227 1 25 . 1 1 7 7 LEU HB3 H 1 1.577 0.005 . 2 . . . . 7 L HB3 . 17227 1 26 . 1 1 7 7 LEU HD11 H 1 0.960 0.006 . . . . . . 7 L QD1 . 17227 1 27 . 1 1 7 7 LEU HD12 H 1 0.960 0.006 . . . . . . 7 L QD1 . 17227 1 28 . 1 1 7 7 LEU HD13 H 1 0.960 0.006 . . . . . . 7 L QD1 . 17227 1 29 . 1 1 7 7 LEU HG H 1 1.502 0.005 . 1 . . . . 7 L HG . 17227 1 30 . 1 1 8 8 ARG H H 1 8.304 0.005 . 1 . . . . 8 R H . 17227 1 31 . 1 1 8 8 ARG HA H 1 4.069 0.005 . 1 . . . . 8 R HA . 17227 1 32 . 1 1 8 8 ARG HB2 H 1 1.945 0.002 . 2 . . . . 8 R HB2 . 17227 1 33 . 1 1 8 8 ARG HB3 H 1 1.768 0.005 . 2 . . . . 8 R HB3 . 17227 1 34 . 1 1 8 8 ARG HD2 H 1 3.296 0.005 . 2 . . . . 8 R QD . 17227 1 35 . 1 1 8 8 ARG HD3 H 1 3.296 0.005 . 2 . . . . 8 R QD . 17227 1 36 . 1 1 8 8 ARG HE H 1 7.296 0.005 . 1 . . . . 8 R HE . 17227 1 37 . 1 1 8 8 ARG HG2 H 1 1.655 0.005 . 2 . . . . 8 R QG . 17227 1 38 . 1 1 8 8 ARG HG3 H 1 1.655 0.005 . 2 . . . . 8 R QG . 17227 1 39 . 1 1 9 9 ARG H H 1 8.004 0.003 . 1 . . . . 9 R H . 17227 1 40 . 1 1 9 9 ARG HA H 1 4.023 0.005 . 1 . . . . 9 R HA . 17227 1 41 . 1 1 9 9 ARG HB2 H 1 1.943 0.001 . 2 . . . . 9 R HB2 . 17227 1 42 . 1 1 9 9 ARG HB3 H 1 1.863 0.002 . 2 . . . . 9 R HB3 . 17227 1 43 . 1 1 9 9 ARG HD2 H 1 3.249 0.002 . 2 . . . . 9 R QD . 17227 1 44 . 1 1 9 9 ARG HD3 H 1 3.249 0.002 . 2 . . . . 9 R QD . 17227 1 45 . 1 1 9 9 ARG HE H 1 7.279 0.005 . 1 . . . . 9 R HE . 17227 1 46 . 1 1 9 9 ARG HG2 H 1 1.676 0.001 . 2 . . . . 9 R QG . 17227 1 47 . 1 1 9 9 ARG HG3 H 1 1.676 0.001 . 2 . . . . 9 R QG . 17227 1 48 . 1 1 10 10 CYS H H 1 8.709 0.006 . 1 . . . . 10 C H . 17227 1 49 . 1 1 10 10 CYS HA H 1 4.655 0.003 . 1 . . . . 10 C HA . 17227 1 50 . 1 1 10 10 CYS HB2 H 1 3.206 0.003 . 2 . . . . 10 C HB2 . 17227 1 51 . 1 1 10 10 CYS HB3 H 1 2.784 0.014 . 2 . . . . 10 C HB3 . 17227 1 52 . 1 1 11 11 GLU H H 1 9.058 0.005 . 1 . . . . 11 E H . 17227 1 53 . 1 1 11 11 GLU HA H 1 3.811 0.015 . 1 . . . . 11 E HA . 17227 1 54 . 1 1 11 11 GLU HB2 H 1 2.416 0.004 . 2 . . . . 11 E HB2 . 17227 1 55 . 1 1 11 11 GLU HB3 H 1 2.104 0.002 . 2 . . . . 11 E HB3 . 17227 1 56 . 1 1 11 11 GLU HG2 H 1 2.673 0.008 . 2 . . . . 11 E HG2 . 17227 1 57 . 1 1 11 11 GLU HG3 H 1 2.590 0.008 . 2 . . . . 11 E HG3 . 17227 1 58 . 1 1 12 12 LEU H H 1 8.123 0.005 . 1 . . . . 12 L H . 17227 1 59 . 1 1 12 12 LEU HA H 1 4.099 0.007 . 1 . . . . 12 L HA . 17227 1 60 . 1 1 12 12 LEU HB2 H 1 1.901 0.004 . 2 . . . . 12 L HB2 . 17227 1 61 . 1 1 12 12 LEU HB3 H 1 1.833 0.001 . 2 . . . . 12 L HB3 . 17227 1 62 . 1 1 12 12 LEU HD11 H 1 0.935 0.001 . . . . . . 12 L QD1 . 17227 1 63 . 1 1 12 12 LEU HD12 H 1 0.935 0.001 . . . . . . 12 L QD1 . 17227 1 64 . 1 1 12 12 LEU HD13 H 1 0.935 0.001 . . . . . . 12 L QD1 . 17227 1 65 . 1 1 12 12 LEU HG H 1 1.704 0.001 . 1 . . . . 12 L HG . 17227 1 66 . 1 1 13 13 SER H H 1 8.459 0.005 . 1 . . . . 13 S H . 17227 1 67 . 1 1 13 13 SER HA H 1 4.310 0.004 . 1 . . . . 13 S HA . 17227 1 68 . 1 1 13 13 SER HB2 H 1 4.049 0.001 . 2 . . . . 13 S QB . 17227 1 69 . 1 1 13 13 SER HB3 H 1 4.049 0.001 . 2 . . . . 13 S QB . 17227 1 70 . 1 1 14 14 CYS H H 1 8.285 0.005 . 1 . . . . 14 C H . 17227 1 71 . 1 1 14 14 CYS HA H 1 4.491 0.005 . 1 . . . . 14 C HA . 17227 1 72 . 1 1 14 14 CYS HB2 H 1 2.410 0.005 . 2 . . . . 14 C QB . 17227 1 73 . 1 1 14 14 CYS HB3 H 1 2.410 0.005 . 2 . . . . 14 C QB . 17227 1 74 . 1 1 15 15 ARG H H 1 8.334 0.005 . 1 . . . . 15 R H . 17227 1 75 . 1 1 15 15 ARG HA H 1 4.471 0.005 . 1 . . . . 15 R HA . 17227 1 76 . 1 1 15 15 ARG HB2 H 1 2.247 0.003 . 2 . . . . 15 R HB2 . 17227 1 77 . 1 1 15 15 ARG HB3 H 1 2.094 0.003 . 2 . . . . 15 R HB3 . 17227 1 78 . 1 1 15 15 ARG HD2 H 1 3.289 0.004 . 2 . . . . 15 R QD . 17227 1 79 . 1 1 15 15 ARG HD3 H 1 3.289 0.004 . 2 . . . . 15 R QD . 17227 1 80 . 1 1 15 15 ARG HE H 1 7.260 0.005 . 1 . . . . 15 R HE . 17227 1 81 . 1 1 15 15 ARG HG2 H 1 1.879 0.007 . 2 . . . . 15 R QG . 17227 1 82 . 1 1 15 15 ARG HG3 H 1 1.879 0.007 . 2 . . . . 15 R QG . 17227 1 83 . 1 1 16 16 SER H H 1 7.728 0.004 . 1 . . . . 16 S H . 17227 1 84 . 1 1 16 16 SER HA H 1 4.406 0.019 . 1 . . . . 16 S HA . 17227 1 85 . 1 1 16 16 SER HB2 H 1 4.093 0.005 . 2 . . . . 16 S QB . 17227 1 86 . 1 1 16 16 SER HB3 H 1 4.093 0.005 . 2 . . . . 16 S QB . 17227 1 87 . 1 1 17 17 LEU H H 1 7.401 0.001 . 1 . . . . 17 L H . 17227 1 88 . 1 1 17 17 LEU HA H 1 4.556 0.005 . 1 . . . . 17 L HA . 17227 1 89 . 1 1 17 17 LEU HB2 H 1 1.867 0.001 . 2 . . . . 17 L QB . 17227 1 90 . 1 1 17 17 LEU HB3 H 1 1.867 0.001 . 2 . . . . 17 L QB . 17227 1 91 . 1 1 17 17 LEU HD11 H 1 1.005 0.003 . . . . . . 17 L QD1 . 17227 1 92 . 1 1 17 17 LEU HD12 H 1 1.005 0.003 . . . . . . 17 L QD1 . 17227 1 93 . 1 1 17 17 LEU HD13 H 1 1.005 0.003 . . . . . . 17 L QD1 . 17227 1 94 . 1 1 17 17 LEU HD21 H 1 0.895 0.003 . . . . . . 17 L QD2 . 17227 1 95 . 1 1 17 17 LEU HD22 H 1 0.895 0.003 . . . . . . 17 L QD2 . 17227 1 96 . 1 1 17 17 LEU HD23 H 1 0.895 0.003 . . . . . . 17 L QD2 . 17227 1 97 . 1 1 17 17 LEU HG H 1 1.761 0.002 . 1 . . . . 17 L HG . 17227 1 98 . 1 1 18 18 GLY H H 1 8.170 0.001 . 1 . . . . 18 G H . 17227 1 99 . 1 1 18 18 GLY HA2 H 1 3.988 0.005 . 2 . . . . 18 G HA2 . 17227 1 100 . 1 1 18 18 GLY HA3 H 1 4.176 0.005 . 2 . . . . 18 G HA3 . 17227 1 101 . 1 1 19 19 LEU H H 1 7.449 0.005 . 1 . . . . 19 L H . 17227 1 102 . 1 1 19 19 LEU HA H 1 4.665 0.005 . 1 . . . . 19 L HA . 17227 1 103 . 1 1 19 19 LEU HB2 H 1 1.273 0.007 . 2 . . . . 19 L QB . 17227 1 104 . 1 1 19 19 LEU HB3 H 1 1.273 0.007 . 2 . . . . 19 L QB . 17227 1 105 . 1 1 19 19 LEU HD11 H 1 0.730 0.005 . . . . . . 19 L QD1 . 17227 1 106 . 1 1 19 19 LEU HD12 H 1 0.730 0.005 . . . . . . 19 L QD1 . 17227 1 107 . 1 1 19 19 LEU HD13 H 1 0.730 0.005 . . . . . . 19 L QD1 . 17227 1 108 . 1 1 19 19 LEU HG H 1 1.441 0.005 . 1 . . . . 19 L HG . 17227 1 109 . 1 1 20 20 LEU H H 1 8.641 0.005 . 1 . . . . 20 L H . 17227 1 110 . 1 1 20 20 LEU HA H 1 4.316 0.002 . 1 . . . . 20 L HA . 17227 1 111 . 1 1 20 20 LEU HB2 H 1 1.454 0.003 . 2 . . . . 20 L QB . 17227 1 112 . 1 1 20 20 LEU HB3 H 1 1.454 0.003 . 2 . . . . 20 L QB . 17227 1 113 . 1 1 20 20 LEU HD11 H 1 0.851 0.001 . . . . . . 20 L QD1 . 17227 1 114 . 1 1 20 20 LEU HD12 H 1 0.851 0.001 . . . . . . 20 L QD1 . 17227 1 115 . 1 1 20 20 LEU HD13 H 1 0.851 0.001 . . . . . . 20 L QD1 . 17227 1 116 . 1 1 20 20 LEU HD21 H 1 0.736 0.001 . . . . . . 20 L QD2 . 17227 1 117 . 1 1 20 20 LEU HD22 H 1 0.736 0.001 . . . . . . 20 L QD2 . 17227 1 118 . 1 1 20 20 LEU HD23 H 1 0.736 0.001 . . . . . . 20 L QD2 . 17227 1 119 . 1 1 20 20 LEU HG H 1 1.230 0.002 . 1 . . . . 20 L HG . 17227 1 120 . 1 1 21 21 GLY H H 1 8.042 0.007 . 1 . . . . 21 G H . 17227 1 121 . 1 1 21 21 GLY HA2 H 1 5.213 0.004 . 2 . . . . 21 G HA2 . 17227 1 122 . 1 1 21 21 GLY HA3 H 1 3.000 0.002 . 2 . . . . 21 G HA3 . 17227 1 123 . 1 1 22 22 LYS H H 1 8.864 0.002 . 1 . . . . 22 K H . 17227 1 124 . 1 1 22 22 LYS HA H 1 4.400 0.001 . 1 . . . . 22 K HA . 17227 1 125 . 1 1 22 22 LYS HB2 H 1 1.691 0.005 . 2 . . . . 22 K HB2 . 17227 1 126 . 1 1 22 22 LYS HB3 H 1 1.559 0.001 . 2 . . . . 22 K HB3 . 17227 1 127 . 1 1 22 22 LYS HD2 H 1 2.852 0.005 . 2 . . . . 22 K QD . 17227 1 128 . 1 1 22 22 LYS HD3 H 1 2.852 0.005 . 2 . . . . 22 K QD . 17227 1 129 . 1 1 22 22 LYS HG2 H 1 1.293 0.001 . 2 . . . . 22 K QG . 17227 1 130 . 1 1 22 22 LYS HG3 H 1 1.293 0.001 . 2 . . . . 22 K QG . 17227 1 131 . 1 1 23 23 CYS H H 1 8.254 0.006 . 1 . . . . 23 C H . 17227 1 132 . 1 1 23 23 CYS HA H 1 5.300 0.008 . 1 . . . . 23 C HA . 17227 1 133 . 1 1 23 23 CYS HB2 H 1 2.964 0.004 . 2 . . . . 23 C HB2 . 17227 1 134 . 1 1 23 23 CYS HB3 H 1 2.845 0.005 . 2 . . . . 23 C HB3 . 17227 1 135 . 1 1 24 24 ILE H H 1 9.049 0.005 . 1 . . . . 24 I H . 17227 1 136 . 1 1 24 24 ILE HA H 1 4.266 0.006 . 1 . . . . 24 I HA . 17227 1 137 . 1 1 24 24 ILE HB H 1 1.811 0.004 . 1 . . . . 24 I HB . 17227 1 138 . 1 1 24 24 ILE HD11 H 1 0.811 0.005 . . . . . . 24 I QD1 . 17227 1 139 . 1 1 24 24 ILE HD12 H 1 0.811 0.005 . . . . . . 24 I QD1 . 17227 1 140 . 1 1 24 24 ILE HD13 H 1 0.811 0.005 . . . . . . 24 I QD1 . 17227 1 141 . 1 1 24 24 ILE HG12 H 1 1.412 0.005 . 2 . . . . 24 I HG12 . 17227 1 142 . 1 1 24 24 ILE HG13 H 1 1.116 0.005 . 2 . . . . 24 I HG13 . 17227 1 143 . 1 1 24 24 ILE HG21 H 1 0.888 0.001 . . . . . . 24 I QG2 . 17227 1 144 . 1 1 24 24 ILE HG22 H 1 0.888 0.001 . . . . . . 24 I QG2 . 17227 1 145 . 1 1 24 24 ILE HG23 H 1 0.888 0.001 . . . . . . 24 I QG2 . 17227 1 146 . 1 1 25 25 GLY H H 1 9.013 0.002 . 1 . . . . 25 G H . 17227 1 147 . 1 1 25 25 GLY HA2 H 1 3.956 0.005 . 2 . . . . 25 G HA2 . 17227 1 148 . 1 1 25 25 GLY HA3 H 1 3.728 0.003 . 2 . . . . 25 G HA3 . 17227 1 149 . 1 1 26 26 GLU H H 1 8.851 0.005 . 1 . . . . 26 E H . 17227 1 150 . 1 1 26 26 GLU HA H 1 4.166 0.005 . 1 . . . . 26 E HA . 17227 1 151 . 1 1 26 26 GLU HB2 H 1 1.972 0.006 . 2 . . . . 26 E QB . 17227 1 152 . 1 1 26 26 GLU HB3 H 1 1.972 0.006 . 2 . . . . 26 E QB . 17227 1 153 . 1 1 26 26 GLU HG2 H 1 2.263 0.010 . 2 . . . . 26 E HG2 . 17227 1 154 . 1 1 26 26 GLU HG3 H 1 2.429 0.005 . 2 . . . . 26 E HG3 . 17227 1 155 . 1 1 27 27 GLU H H 1 7.734 0.006 . 1 . . . . 27 E H . 17227 1 156 . 1 1 27 27 GLU HA H 1 4.534 0.005 . 1 . . . . 27 E HA . 17227 1 157 . 1 1 27 27 GLU HB2 H 1 2.074 0.002 . 2 . . . . 27 E HB2 . 17227 1 158 . 1 1 27 27 GLU HB3 H 1 2.013 0.005 . 2 . . . . 27 E HB3 . 17227 1 159 . 1 1 27 27 GLU HG2 H 1 2.428 0.014 . 2 . . . . 27 E HG2 . 17227 1 160 . 1 1 27 27 GLU HG3 H 1 2.353 0.005 . 2 . . . . 27 E HG3 . 17227 1 161 . 1 1 28 28 CYS H H 1 8.690 0.001 . 1 . . . . 28 C H . 17227 1 162 . 1 1 28 28 CYS HA H 1 5.044 0.014 . 1 . . . . 28 C HA . 17227 1 163 . 1 1 28 28 CYS HB2 H 1 3.065 0.003 . 2 . . . . 28 C HB2 . 17227 1 164 . 1 1 28 28 CYS HB3 H 1 2.695 0.001 . 2 . . . . 28 C HB3 . 17227 1 165 . 1 1 29 29 LYS H H 1 9.499 0.005 . 1 . . . . 29 K H . 17227 1 166 . 1 1 29 29 LYS HA H 1 4.682 0.003 . 1 . . . . 29 K HA . 17227 1 167 . 1 1 29 29 LYS HB2 H 1 1.742 0.005 . 2 . . . . 29 K HB2 . 17227 1 168 . 1 1 29 29 LYS HB3 H 1 1.641 0.005 . 2 . . . . 29 K HB3 . 17227 1 169 . 1 1 29 29 LYS HD2 H 1 1.412 0.005 . 2 . . . . 29 K QD . 17227 1 170 . 1 1 29 29 LYS HD3 H 1 1.412 0.005 . 2 . . . . 29 K QD . 17227 1 171 . 1 1 29 29 LYS HE2 H 1 2.852 0.005 . 2 . . . . 29 K QE . 17227 1 172 . 1 1 29 29 LYS HE3 H 1 2.852 0.005 . 2 . . . . 29 K QE . 17227 1 173 . 1 1 29 29 LYS HG2 H 1 1.319 0.015 . 2 . . . . 29 K QG . 17227 1 174 . 1 1 29 29 LYS HG3 H 1 1.319 0.015 . 2 . . . . 29 K QG . 17227 1 175 . 1 1 30 30 CYS H H 1 8.541 0.005 . 1 . . . . 30 C H . 17227 1 176 . 1 1 30 30 CYS HA H 1 5.699 0.005 . 1 . . . . 30 C HA . 17227 1 177 . 1 1 30 30 CYS HB2 H 1 2.950 0.005 . 2 . . . . 30 C HB2 . 17227 1 178 . 1 1 30 30 CYS HB3 H 1 2.665 0.002 . 2 . . . . 30 C HB3 . 17227 1 179 . 1 1 31 31 VAL H H 1 9.515 0.002 . 1 . . . . 31 V H . 17227 1 180 . 1 1 31 31 VAL HA H 1 4.955 0.005 . 1 . . . . 31 V HA . 17227 1 181 . 1 1 31 31 VAL HB H 1 2.284 0.007 . 1 . . . . 31 V HB . 17227 1 182 . 1 1 31 31 VAL HG11 H 1 0.857 0.001 . . . . . . 31 V QG1 . 17227 1 183 . 1 1 31 31 VAL HG12 H 1 0.857 0.001 . . . . . . 31 V QG1 . 17227 1 184 . 1 1 31 31 VAL HG13 H 1 0.857 0.001 . . . . . . 31 V QG1 . 17227 1 185 . 1 1 31 31 VAL HG21 H 1 0.740 0.004 . . . . . . 31 V QG2 . 17227 1 186 . 1 1 31 31 VAL HG22 H 1 0.740 0.004 . . . . . . 31 V QG2 . 17227 1 187 . 1 1 31 31 VAL HG23 H 1 0.740 0.004 . . . . . . 31 V QG2 . 17227 1 188 . 1 1 32 32 PRO HB2 H 1 2.333 0.005 . 2 . . . . 32 P HB2 . 17227 1 189 . 1 1 32 32 PRO HB3 H 1 2.058 0.005 . 2 . . . . 32 P HB3 . 17227 1 190 . 1 1 32 32 PRO HD2 H 1 3.810 0.005 . 2 . . . . 32 P HD2 . 17227 1 191 . 1 1 32 32 PRO HD3 H 1 3.640 0.007 . 2 . . . . 32 P HD3 . 17227 1 192 . 1 1 32 32 PRO HG2 H 1 1.940 0.005 . 2 . . . . 32 P QG . 17227 1 193 . 1 1 32 32 PRO HG3 H 1 1.940 0.005 . 2 . . . . 32 P QG . 17227 1 194 . 1 1 33 33 TYR H H 1 8.262 0.005 . 1 . . . . 33 Y H . 17227 1 195 . 1 1 33 33 TYR HA H 1 4.247 0.005 . 1 . . . . 33 Y HA . 17227 1 196 . 1 1 33 33 TYR HB2 H 1 3.109 0.005 . 2 . . . . 33 Y HB2 . 17227 1 197 . 1 1 33 33 TYR HB3 H 1 2.905 0.005 . 2 . . . . 33 Y HB3 . 17227 1 198 . 1 1 33 33 TYR HD1 H 1 7.223 0.005 . 3 . . . . 33 Y QD . 17227 1 199 . 1 1 33 33 TYR HD2 H 1 7.223 0.005 . 3 . . . . 33 Y QD . 17227 1 200 . 1 1 33 33 TYR HE1 H 1 6.732 0.005 . 3 . . . . 33 Y QE . 17227 1 201 . 1 1 33 33 TYR HE2 H 1 6.732 0.005 . 3 . . . . 33 Y QE . 17227 1 stop_ save_