data_15389 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15389 _Entry.Title ; solution structure of hiv-1 gp41 fusion domain bound to DPC micelle ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-07-18 _Entry.Accession_date 2007-07-18 _Entry.Last_release_date 2008-06-18 _Entry.Original_release_date 2008-06-18 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.100 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Y Li Y. . . 15389 2 L. Tamm L. K. . 15389 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID DOMAIN . 15389 DPC . 15389 FUSION . 15389 GP41 . 15389 HIV . 15389 MEMBRANE . 15389 PEPTIDE . 15389 PROTEIN . 15389 VIRUS . 15389 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15389 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 21 15389 '1H chemical shifts' 120 15389 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 . . 2008-06-18 2007-07-18 original author . 15389 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 15389 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17963720 _Citation.Full_citation . _Citation.Title 'Combined NMR and EPR spectroscopy to determine structures of viral fusion domains in membranes' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full . _Citation.Journal_volume 1768 _Citation.Journal_issue 12 _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 3052 _Citation.Page_last 3060 _Citation.Year 2007 _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 Lukas Tamm L. K. . 15389 1 2 Alex Lai A. L. . 15389 1 3 Yinling Li Y. . . 15389 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15389 _Assembly.ID 1 _Assembly.Name 'HIV fusion peptide' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 2902 _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 'HIV fusion peptide' 1 $Envelope_glycoprotein A . yes native no no . . . 15389 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Envelope_glycoprotein _Entity.Sf_category entity _Entity.Sf_framecode Envelope_glycoprotein _Entity.Entry_ID 15389 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Envelope_glycoprotein _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 ; AVGIGALFLGFLGAAGSTVG AASGGGKKKKK ; _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 31 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment '23 N-terminal residues' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 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 2PJV . "Solution Structure Of Hiv-1 Gp41 Fusion Domain Bound To Dpc Micelle" . . . . . 100.00 31 100.00 100.00 4.32e-08 . . . . 15389 1 2 no GB AAB68317 . "envelope glycoprotein, partial [Human immunodeficiency virus 1]" . . . . . 58.06 433 100.00 100.00 1.27e-01 . . . . 15389 1 3 no GB AAB68318 . "envelope glycoprotein, partial [Human immunodeficiency virus 1]" . . . . . 58.06 434 100.00 100.00 1.27e-01 . . . . 15389 1 4 no GB AAB68319 . "envelope glycoprotein, partial [Human immunodeficiency virus 1]" . . . . . 58.06 416 100.00 100.00 4.51e-01 . . . . 15389 1 5 no GB AAB68320 . "envelope glycoprotein, partial [Human immunodeficiency virus 1]" . . . . . 58.06 416 100.00 100.00 3.03e-01 . . . . 15389 1 6 no GB AAB68321 . "envelope glycoprotein, partial [Human immunodeficiency virus 1]" . . . . . 58.06 433 100.00 100.00 1.27e-01 . . . . 15389 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Envelope glycoprotein' RCSB_NAME 15389 1 'Envelope protein' SWS-KEYWORD 15389 1 Transmembrane SWS-KEYWORD 15389 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 . ALA . 15389 1 2 . VAL . 15389 1 3 . GLY . 15389 1 4 . ILE . 15389 1 5 . GLY . 15389 1 6 . ALA . 15389 1 7 . LEU . 15389 1 8 . PHE . 15389 1 9 . LEU . 15389 1 10 . GLY . 15389 1 11 . PHE . 15389 1 12 . LEU . 15389 1 13 . GLY . 15389 1 14 . ALA . 15389 1 15 . ALA . 15389 1 16 . GLY . 15389 1 17 . SER . 15389 1 18 . THR . 15389 1 19 . VAL . 15389 1 20 . GLY . 15389 1 21 . ALA . 15389 1 22 . ALA . 15389 1 23 . SER . 15389 1 24 . GLY . 15389 1 25 . GLY . 15389 1 26 . GLY . 15389 1 27 . LYS . 15389 1 28 . LYS . 15389 1 29 . LYS . 15389 1 30 . LYS . 15389 1 31 . LYS . 15389 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 . ALA 1 1 15389 1 . VAL 2 2 15389 1 . GLY 3 3 15389 1 . ILE 4 4 15389 1 . GLY 5 5 15389 1 . ALA 6 6 15389 1 . LEU 7 7 15389 1 . PHE 8 8 15389 1 . LEU 9 9 15389 1 . GLY 10 10 15389 1 . PHE 11 11 15389 1 . LEU 12 12 15389 1 . GLY 13 13 15389 1 . ALA 14 14 15389 1 . ALA 15 15 15389 1 . GLY 16 16 15389 1 . SER 17 17 15389 1 . THR 18 18 15389 1 . VAL 19 19 15389 1 . GLY 20 20 15389 1 . ALA 21 21 15389 1 . ALA 22 22 15389 1 . SER 23 23 15389 1 . GLY 24 24 15389 1 . GLY 25 25 15389 1 . GLY 26 26 15389 1 . LYS 27 27 15389 1 . LYS 28 28 15389 1 . LYS 29 29 15389 1 . LYS 30 30 15389 1 . LYS 31 31 15389 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 15389 _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 $Envelope_glycoprotein . 11676 organism . 'Human immunodeficiency virus 1' HIV-1 . . Viruses . Lentivirus HIV-1 LAVmal . . . . . . . . . . . . . . . env . . . . 15389 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 15389 _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 $Envelope_glycoprotein . 'recombinant technology' 'Escherichia coli' bacteria . . Escherichia coli BLR(DE3)pLysS . . . . . . . . . . . . . . . PET31b(+) . . . . . . 15389 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15389 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '1 MM N15-PEPTIDE IN THE PRESENCE OF 200 MM D38-DPC IN 0.05% NAN3, 5 MM DTT, 20 MM D4-ACETIC ACID, 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 'Envelope glycoprotein' [U-15N] . . 1 $Envelope_glycoprotein . . 1 . . mM . . . . 15389 1 2 D38-DPC . . . . . . . 200 . . mM . . . . 15389 1 3 NAN3 . . . . . . . 0.05 . . % . . . . 15389 1 4 DTT . . . . . . . 5 . . mM . . . . 15389 1 5 'D4-ACETIC ACID' . . . . . . . 20 . . mM . . . . 15389 1 6 H2O . . . . . . . 95 . . % . . . . 15389 1 7 D2O . . . . . . . 5 . . % . . . . 15389 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 15389 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details '2 MM PEPTIDE IN THE PRESENCE OF 400 MM D38-DPC IN 0.05% NAN3, 5 MM DTT, 20 MM D4-ACETIC ACID, 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 'Envelope glycoprotein' . . . 1 $Envelope_glycoprotein . . 2 . . mM . . . . 15389 2 2 D38-DPC . . . . . . . 400 . . mM . . . . 15389 2 3 NAN3 . . . . . . . 0.05 . . % . . . . 15389 2 4 DTT . . . . . . . 5 . . mM . . . . 15389 2 5 'D4-ACETIC ACID' . . . . . . . 20 . . mM . . . . 15389 2 6 H2O . . . . . . . 95 . . % . . . . 15389 2 7 D2O . . . . . . . 5 . . % . . . . 15389 2 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 15389 _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 7.4 . pH 15389 1 pressure 1 1 atm 15389 1 temperature 303 . K 15389 1 stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Software.Sf_category software _Software.Sf_framecode VNMR _Software.Entry_ID 15389 _Software.ID 1 _Software.Name VNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 15389 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 15389 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 15389 _Software.ID 2 _Software.Name NMRPipe _Software.Version 2.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 15389 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15389 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 15389 _Software.ID 3 _Software.Name SPARKY _Software.Version 3.110 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 15389 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 15389 3 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 15389 _Software.ID 4 _Software.Name DYANA _Software.Version 1.5 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Braun and Wuthrich' . . 15389 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 15389 4 stop_ save_ save_OPAL _Software.Sf_category software _Software.Sf_framecode OPAL _Software.Entry_ID 15389 _Software.ID 5 _Software.Name OPAL _Software.Version 2.6 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Luginbuhl, Guntert, Billeter and Wuthrich' . . 15389 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 15389 5 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 15389 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 15389 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 15389 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_500 _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode 500 _NMR_spectrometer_list.Entry_ID 15389 _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 Bruker AVANCE . 600 . . . 15389 1 2 spectrometer_1 Varian INOVA . 600 . . . 15389 1 3 spectrometer_1 Varian INOVA . 500 . . . 15389 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 15389 _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' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 15389 1 2 '2D TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 15389 1 3 3D_15N-separated_NOESY no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 15389 1 4 HNHA no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 15389 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 15389 _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 . . . . . . . . . 15389 1 N 15 DSS 'methyl protons' . . . . ppm 0 external indirect 0.1 . . . . . . . . . 15389 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 15389 _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 . _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' . . . 15389 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 VAL HA H 1 4.253 0.042 . . . . . . 2 V HA . 15389 1 2 . 1 1 2 2 VAL HB H 1 2.168 0.009 . . . . . . 2 V HB . 15389 1 3 . 1 1 2 2 VAL HG11 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 4 . 1 1 2 2 VAL HG12 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 5 . 1 1 2 2 VAL HG13 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 6 . 1 1 2 2 VAL HG21 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 7 . 1 1 2 2 VAL HG22 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 8 . 1 1 2 2 VAL HG23 H 1 1.028 0.009 . . . . . . 2 V QQG . 15389 1 9 . 1 1 3 3 GLY H H 1 8.521 0.010 . . . . . . 3 G HN . 15389 1 10 . 1 1 3 3 GLY HA2 H 1 4.207 0.003 . . . . . . 3 G HA1 . 15389 1 11 . 1 1 3 3 GLY HA3 H 1 4.102 0.002 . . . . . . 3 G HA2 . 15389 1 12 . 1 1 3 3 GLY N N 15 111.710 0.036 . . . . . . 3 G N . 15389 1 13 . 1 1 4 4 ILE H H 1 8.772 0.007 . . . . . . 4 I HN . 15389 1 14 . 1 1 4 4 ILE HA H 1 3.934 0.009 . . . . . . 4 I HA . 15389 1 15 . 1 1 4 4 ILE HB H 1 1.965 0.009 . . . . . . 4 I HB . 15389 1 16 . 1 1 4 4 ILE HD11 H 1 0.958 0.005 . . . . . . 4 I QD1 . 15389 1 17 . 1 1 4 4 ILE HD12 H 1 0.958 0.005 . . . . . . 4 I QD1 . 15389 1 18 . 1 1 4 4 ILE HD13 H 1 0.958 0.005 . . . . . . 4 I QD1 . 15389 1 19 . 1 1 4 4 ILE HG12 H 1 1.641 0.005 . . . . . . 4 I HG12 . 15389 1 20 . 1 1 4 4 ILE HG13 H 1 1.352 0.005 . . . . . . 4 I HG13 . 15389 1 21 . 1 1 4 4 ILE HG21 H 1 0.990 0.005 . . . . . . 4 I QG2 . 15389 1 22 . 1 1 4 4 ILE HG22 H 1 0.990 0.005 . . . . . . 4 I QG2 . 15389 1 23 . 1 1 4 4 ILE HG23 H 1 0.990 0.005 . . . . . . 4 I QG2 . 15389 1 24 . 1 1 4 4 ILE N N 15 121.300 0.068 . . . . . . 4 I N . 15389 1 25 . 1 1 5 5 GLY H H 1 9.112 0.005 . . . . . . 5 G HN . 15389 1 26 . 1 1 5 5 GLY HA2 H 1 3.940 0.003 . . . . . . 5 G HA1 . 15389 1 27 . 1 1 5 5 GLY HA3 H 1 3.773 0.009 . . . . . . 5 G HA2 . 15389 1 28 . 1 1 5 5 GLY N N 15 109.870 0.033 . . . . . . 5 G N . 15389 1 29 . 1 1 6 6 ALA H H 1 8.132 0.007 . . . . . . 6 A HN . 15389 1 30 . 1 1 6 6 ALA HA H 1 4.144 0.008 . . . . . . 6 A HA . 15389 1 31 . 1 1 6 6 ALA HB1 H 1 1.502 0.006 . . . . . . 6 A QB . 15389 1 32 . 1 1 6 6 ALA HB2 H 1 1.502 0.006 . . . . . . 6 A QB . 15389 1 33 . 1 1 6 6 ALA HB3 H 1 1.502 0.006 . . . . . . 6 A QB . 15389 1 34 . 1 1 6 6 ALA N N 15 122.981 0.056 . . . . . . 6 A N . 15389 1 35 . 1 1 7 7 LEU H H 1 8.031 0.005 . . . . . . 7 L HN . 15389 1 36 . 1 1 7 7 LEU HA H 1 4.136 0.007 . . . . . . 7 L HA . 15389 1 37 . 1 1 7 7 LEU HB2 H 1 1.908 0.009 . . . . . . 7 L HB2 . 15389 1 38 . 1 1 7 7 LEU HB3 H 1 1.706 0.022 . . . . . . 7 L HB3 . 15389 1 39 . 1 1 7 7 LEU HD11 H 1 0.951 0.005 . . . . . . 7 L QD1 . 15389 1 40 . 1 1 7 7 LEU HD12 H 1 0.951 0.005 . . . . . . 7 L QD1 . 15389 1 41 . 1 1 7 7 LEU HD13 H 1 0.951 0.005 . . . . . . 7 L QD1 . 15389 1 42 . 1 1 7 7 LEU HD21 H 1 0.914 0.005 . . . . . . 7 L QD2 . 15389 1 43 . 1 1 7 7 LEU HD22 H 1 0.914 0.005 . . . . . . 7 L QD2 . 15389 1 44 . 1 1 7 7 LEU HD23 H 1 0.914 0.005 . . . . . . 7 L QD2 . 15389 1 45 . 1 1 7 7 LEU HG H 1 1.655 0.052 . . . . . . 7 L HG . 15389 1 46 . 1 1 7 7 LEU N N 15 120.130 0.055 . . . . . . 7 L N . 15389 1 47 . 1 1 8 8 PHE H H 1 8.392 0.008 . . . . . . 8 F HN . 15389 1 48 . 1 1 8 8 PHE HA H 1 4.377 0.010 . . . . . . 8 F HA . 15389 1 49 . 1 1 8 8 PHE N N 15 118.680 0.069 . . . . . . 8 F N . 15389 1 50 . 1 1 9 9 LEU H H 1 8.510 0.007 . . . . . . 9 L HN . 15389 1 51 . 1 1 9 9 LEU HA H 1 4.208 0.006 . . . . . . 9 L HA . 15389 1 52 . 1 1 9 9 LEU HB2 H 1 1.949 0.005 . . . . . . 9 L HB2 . 15389 1 53 . 1 1 9 9 LEU HB3 H 1 1.918 0.005 . . . . . . 9 L HB3 . 15389 1 54 . 1 1 9 9 LEU HD11 H 1 0.988 0.006 . . . . . . 9 L QD1 . 15389 1 55 . 1 1 9 9 LEU HD12 H 1 0.988 0.006 . . . . . . 9 L QD1 . 15389 1 56 . 1 1 9 9 LEU HD13 H 1 0.988 0.006 . . . . . . 9 L QD1 . 15389 1 57 . 1 1 9 9 LEU HD21 H 1 0.964 0.008 . . . . . . 9 L QD2 . 15389 1 58 . 1 1 9 9 LEU HD22 H 1 0.964 0.008 . . . . . . 9 L QD2 . 15389 1 59 . 1 1 9 9 LEU HD23 H 1 0.964 0.008 . . . . . . 9 L QD2 . 15389 1 60 . 1 1 9 9 LEU HG H 1 1.600 0.006 . . . . . . 9 L HG . 15389 1 61 . 1 1 9 9 LEU N N 15 118.147 0.165 . . . . . . 9 L N . 15389 1 62 . 1 1 10 10 GLY H H 1 8.239 0.008 . . . . . . 10 G HN . 15389 1 63 . 1 1 10 10 GLY HA2 H 1 3.947 0.002 . . . . . . 10 G QA . 15389 1 64 . 1 1 10 10 GLY HA3 H 1 3.947 0.002 . . . . . . 10 G QA . 15389 1 65 . 1 1 10 10 GLY N N 15 107.291 0.049 . . . . . . 10 G N . 15389 1 66 . 1 1 11 11 PHE H H 1 8.065 0.005 . . . . . . 11 F HN . 15389 1 67 . 1 1 11 11 PHE HA H 1 4.493 0.023 . . . . . . 11 F HA . 15389 1 68 . 1 1 11 11 PHE HB2 H 1 3.271 0.016 . . . . . . 11 F QB . 15389 1 69 . 1 1 11 11 PHE HB3 H 1 3.271 0.016 . . . . . . 11 F QB . 15389 1 70 . 1 1 11 11 PHE N N 15 122.459 0.127 . . . . . . 11 F N . 15389 1 71 . 1 1 12 12 LEU H H 1 8.027 0.006 . . . . . . 12 L HN . 15389 1 72 . 1 1 12 12 LEU HA H 1 3.958 0.009 . . . . . . 12 L HA . 15389 1 73 . 1 1 12 12 LEU HB2 H 1 1.762 0.007 . . . . . . 12 L HB2 . 15389 1 74 . 1 1 12 12 LEU HB3 H 1 1.724 0.006 . . . . . . 12 L HB3 . 15389 1 75 . 1 1 12 12 LEU HD11 H 1 0.851 0.007 . . . . . . 12 L QD1 . 15389 1 76 . 1 1 12 12 LEU HD12 H 1 0.851 0.007 . . . . . . 12 L QD1 . 15389 1 77 . 1 1 12 12 LEU HD13 H 1 0.851 0.007 . . . . . . 12 L QD1 . 15389 1 78 . 1 1 12 12 LEU HD21 H 1 0.834 0.016 . . . . . . 12 L QD2 . 15389 1 79 . 1 1 12 12 LEU HD22 H 1 0.834 0.016 . . . . . . 12 L QD2 . 15389 1 80 . 1 1 12 12 LEU HD23 H 1 0.834 0.016 . . . . . . 12 L QD2 . 15389 1 81 . 1 1 12 12 LEU HG H 1 1.553 0.013 . . . . . . 12 L HG . 15389 1 82 . 1 1 12 12 LEU N N 15 117.843 0.195 . . . . . . 12 L N . 15389 1 83 . 1 1 13 13 GLY H H 1 8.080 0.016 . . . . . . 13 G HN . 15389 1 84 . 1 1 13 13 GLY HA2 H 1 3.954 0.006 . . . . . . 13 G HA1 . 15389 1 85 . 1 1 13 13 GLY HA3 H 1 3.913 0.006 . . . . . . 13 G HA2 . 15389 1 86 . 1 1 13 13 GLY N N 15 105.014 0.140 . . . . . . 13 G N . 15389 1 87 . 1 1 14 14 ALA H H 1 7.965 0.052 . . . . . . 14 A HN . 15389 1 88 . 1 1 14 14 ALA HA H 1 4.369 0.009 . . . . . . 14 A HA . 15389 1 89 . 1 1 14 14 ALA HB1 H 1 1.472 0.002 . . . . . . 14 A QB . 15389 1 90 . 1 1 14 14 ALA HB2 H 1 1.472 0.002 . . . . . . 14 A QB . 15389 1 91 . 1 1 14 14 ALA HB3 H 1 1.472 0.002 . . . . . . 14 A QB . 15389 1 92 . 1 1 14 14 ALA N N 15 123.634 0.140 . . . . . . 14 A N . 15389 1 93 . 1 1 15 15 ALA H H 1 8.254 0.005 . . . . . . 15 A HN . 15389 1 94 . 1 1 15 15 ALA HA H 1 4.203 0.010 . . . . . . 15 A HA . 15389 1 95 . 1 1 15 15 ALA HB1 H 1 1.358 0.002 . . . . . . 15 A QB . 15389 1 96 . 1 1 15 15 ALA HB2 H 1 1.358 0.002 . . . . . . 15 A QB . 15389 1 97 . 1 1 15 15 ALA HB3 H 1 1.358 0.002 . . . . . . 15 A QB . 15389 1 98 . 1 1 15 15 ALA N N 15 121.566 0.032 . . . . . . 15 A N . 15389 1 99 . 1 1 16 16 GLY H H 1 8.359 0.005 . . . . . . 16 G HN . 15389 1 100 . 1 1 16 16 GLY HA2 H 1 3.939 0.004 . . . . . . 16 G QA . 15389 1 101 . 1 1 16 16 GLY HA3 H 1 3.939 0.004 . . . . . . 16 G QA . 15389 1 102 . 1 1 16 16 GLY N N 15 105.920 0.037 . . . . . . 16 G N . 15389 1 103 . 1 1 17 17 SER H H 1 8.024 0.023 . . . . . . 17 S HN . 15389 1 104 . 1 1 17 17 SER HA H 1 4.253 0.005 . . . . . . 17 S HA . 15389 1 105 . 1 1 17 17 SER N N 15 115.091 0.016 . . . . . . 17 S N . 15389 1 106 . 1 1 18 18 THR H H 1 8.164 0.006 . . . . . . 18 T HN . 15389 1 107 . 1 1 18 18 THR HA H 1 4.344 0.017 . . . . . . 18 T HA . 15389 1 108 . 1 1 18 18 THR HB H 1 4.312 0.009 . . . . . . 18 T HB . 15389 1 109 . 1 1 18 18 THR HG21 H 1 1.265 0.009 . . . . . . 18 T QG2 . 15389 1 110 . 1 1 18 18 THR HG22 H 1 1.265 0.009 . . . . . . 18 T QG2 . 15389 1 111 . 1 1 18 18 THR HG23 H 1 1.265 0.009 . . . . . . 18 T QG2 . 15389 1 112 . 1 1 18 18 THR N N 15 116.174 0.088 . . . . . . 18 T N . 15389 1 113 . 1 1 19 19 VAL H H 1 8.031 0.003 . . . . . . 19 V HN . 15389 1 114 . 1 1 19 19 VAL HA H 1 4.106 0.008 . . . . . . 19 V HA . 15389 1 115 . 1 1 19 19 VAL HB H 1 2.185 0.008 . . . . . . 19 V HB . 15389 1 116 . 1 1 19 19 VAL HG11 H 1 1.022 0.007 . . . . . . 19 V QG1 . 15389 1 117 . 1 1 19 19 VAL HG12 H 1 1.022 0.007 . . . . . . 19 V QG1 . 15389 1 118 . 1 1 19 19 VAL HG13 H 1 1.022 0.007 . . . . . . 19 V QG1 . 15389 1 119 . 1 1 19 19 VAL HG21 H 1 0.992 0.005 . . . . . . 19 V QG2 . 15389 1 120 . 1 1 19 19 VAL HG22 H 1 0.992 0.005 . . . . . . 19 V QG2 . 15389 1 121 . 1 1 19 19 VAL HG23 H 1 0.992 0.005 . . . . . . 19 V QG2 . 15389 1 122 . 1 1 19 19 VAL N N 15 120.323 0.018 . . . . . . 19 V N . 15389 1 123 . 1 1 20 20 GLY H H 1 8.412 0.005 . . . . . . 20 G HN . 15389 1 124 . 1 1 20 20 GLY HA2 H 1 3.975 0.006 . . . . . . 20 G QA . 15389 1 125 . 1 1 20 20 GLY HA3 H 1 3.975 0.006 . . . . . . 20 G QA . 15389 1 126 . 1 1 20 20 GLY N N 15 110.759 0.091 . . . . . . 20 G N . 15389 1 127 . 1 1 21 21 ALA H H 1 8.084 0.004 . . . . . . 21 A HN . 15389 1 128 . 1 1 21 21 ALA HA H 1 4.344 0.016 . . . . . . 21 A HA . 15389 1 129 . 1 1 21 21 ALA HB1 H 1 1.488 0.008 . . . . . . 21 A QB . 15389 1 130 . 1 1 21 21 ALA HB2 H 1 1.488 0.008 . . . . . . 21 A QB . 15389 1 131 . 1 1 21 21 ALA HB3 H 1 1.488 0.008 . . . . . . 21 A QB . 15389 1 132 . 1 1 21 21 ALA N N 15 123.556 0.011 . . . . . . 21 A N . 15389 1 133 . 1 1 22 22 ALA H H 1 8.303 0.004 . . . . . . 22 A HN . 15389 1 134 . 1 1 22 22 ALA HA H 1 4.392 0.008 . . . . . . 22 A HA . 15389 1 135 . 1 1 22 22 ALA HB1 H 1 1.460 0.003 . . . . . . 22 A QB . 15389 1 136 . 1 1 22 22 ALA HB2 H 1 1.460 0.003 . . . . . . 22 A QB . 15389 1 137 . 1 1 22 22 ALA HB3 H 1 1.460 0.003 . . . . . . 22 A QB . 15389 1 138 . 1 1 22 22 ALA N N 15 122.426 0.129 . . . . . . 22 A N . 15389 1 139 . 1 1 23 23 SER H H 1 8.210 0.003 . . . . . . 23 S HN . 15389 1 140 . 1 1 23 23 SER HA H 1 4.475 0.003 . . . . . . 23 S HA . 15389 1 141 . 1 1 23 23 SER N N 15 114.254 0.087 . . . . . . 23 S N . 15389 1 stop_ save_