data_25468 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25468 _Entry.Title ; Solution NMR Structure of PDFL2.1 from Arabidopsis thaliana ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2015-02-05 _Entry.Accession_date 2015-02-05 _Entry.Last_release_date 2016-02-15 _Entry.Original_release_date 2016-02-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1 _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.ORCID _Entry_author.Entry_ID 1 Reza Omidvar . . . . 25468 2 Holger Bohlmann . . . . 25468 3 Youlin Xia . . . . 25468 4 Gianluigi Veglia . . . . 25468 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' . 25468 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'CSAlphaBeta motif' . 25468 defensin . 25468 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25468 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 161 25468 '15N chemical shifts' 55 25468 '1H chemical shifts' 386 25468 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 2 . . 2017-03-29 2015-02-05 update BMRB 'update entry citation' 25468 1 . . 2016-02-15 2015-02-05 original author 'original release' 25468 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2MZ0 'BMRB Entry Tracking System' 25468 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 25468 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 27592418 _Citation.Full_citation . _Citation.Title ; NMR structure and conformational dynamics of AtPDFL2.1, a defensin-like peptide from Arabidopsis thaliana. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta' _Citation.Journal_name_full 'Biochimica et biophysica acta' _Citation.Journal_volume 1864 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-3002 _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 1739 _Citation.Page_last 1747 _Citation.Year 2016 _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 Reza Omidvar R. . . . 25468 1 2 Youlin Xia Y. . . . 25468 1 3 Fernando Porcelli F. . . . 25468 1 4 Holger Bohlmann H. . . . 25468 1 5 Gianluigi Veglia G. . . . 25468 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25468 _Assembly.ID 1 _Assembly.Name PDFL2.1 _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 entity 1 $entity A . yes native no no . . . 25468 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 36 36 SG . . . . . . . . . . 25468 1 2 disulfide single . 1 . 1 CYS 22 22 SG . 1 . 1 CYS 47 47 SG . . . . . . . . . . 25468 1 3 disulfide single . 1 . 1 CYS 26 26 SG . 1 . 1 CYS 49 49 SG . . . . . . . . . . 25468 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 25468 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity _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 ; KDIDGRKPLLIGTCIEFPTE KCNKTCIESNFAGGKCVHIG QSLDFVCVCFPKYYI ; _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 55 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6152.270 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 1 LYS . 25468 1 2 2 ASP . 25468 1 3 3 ILE . 25468 1 4 4 ASP . 25468 1 5 5 GLY . 25468 1 6 6 ARG . 25468 1 7 7 LYS . 25468 1 8 8 PRO . 25468 1 9 9 LEU . 25468 1 10 10 LEU . 25468 1 11 11 ILE . 25468 1 12 12 GLY . 25468 1 13 13 THR . 25468 1 14 14 CYS . 25468 1 15 15 ILE . 25468 1 16 16 GLU . 25468 1 17 17 PHE . 25468 1 18 18 PRO . 25468 1 19 19 THR . 25468 1 20 20 GLU . 25468 1 21 21 LYS . 25468 1 22 22 CYS . 25468 1 23 23 ASN . 25468 1 24 24 LYS . 25468 1 25 25 THR . 25468 1 26 26 CYS . 25468 1 27 27 ILE . 25468 1 28 28 GLU . 25468 1 29 29 SER . 25468 1 30 30 ASN . 25468 1 31 31 PHE . 25468 1 32 32 ALA . 25468 1 33 33 GLY . 25468 1 34 34 GLY . 25468 1 35 35 LYS . 25468 1 36 36 CYS . 25468 1 37 37 VAL . 25468 1 38 38 HIS . 25468 1 39 39 ILE . 25468 1 40 40 GLY . 25468 1 41 41 GLN . 25468 1 42 42 SER . 25468 1 43 43 LEU . 25468 1 44 44 ASP . 25468 1 45 45 PHE . 25468 1 46 46 VAL . 25468 1 47 47 CYS . 25468 1 48 48 VAL . 25468 1 49 49 CYS . 25468 1 50 50 PHE . 25468 1 51 51 PRO . 25468 1 52 52 LYS . 25468 1 53 53 TYR . 25468 1 54 54 TYR . 25468 1 55 55 ILE . 25468 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LYS 1 1 25468 1 . ASP 2 2 25468 1 . ILE 3 3 25468 1 . ASP 4 4 25468 1 . GLY 5 5 25468 1 . ARG 6 6 25468 1 . LYS 7 7 25468 1 . PRO 8 8 25468 1 . LEU 9 9 25468 1 . LEU 10 10 25468 1 . ILE 11 11 25468 1 . GLY 12 12 25468 1 . THR 13 13 25468 1 . CYS 14 14 25468 1 . ILE 15 15 25468 1 . GLU 16 16 25468 1 . PHE 17 17 25468 1 . PRO 18 18 25468 1 . THR 19 19 25468 1 . GLU 20 20 25468 1 . LYS 21 21 25468 1 . CYS 22 22 25468 1 . ASN 23 23 25468 1 . LYS 24 24 25468 1 . THR 25 25 25468 1 . CYS 26 26 25468 1 . ILE 27 27 25468 1 . GLU 28 28 25468 1 . SER 29 29 25468 1 . ASN 30 30 25468 1 . PHE 31 31 25468 1 . ALA 32 32 25468 1 . GLY 33 33 25468 1 . GLY 34 34 25468 1 . LYS 35 35 25468 1 . CYS 36 36 25468 1 . VAL 37 37 25468 1 . HIS 38 38 25468 1 . ILE 39 39 25468 1 . GLY 40 40 25468 1 . GLN 41 41 25468 1 . SER 42 42 25468 1 . LEU 43 43 25468 1 . ASP 44 44 25468 1 . PHE 45 45 25468 1 . VAL 46 46 25468 1 . CYS 47 47 25468 1 . VAL 48 48 25468 1 . CYS 49 49 25468 1 . PHE 50 50 25468 1 . PRO 51 51 25468 1 . LYS 52 52 25468 1 . TYR 53 53 25468 1 . TYR 54 54 25468 1 . ILE 55 55 25468 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 25468 _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 $entity . 3702 organism . 'Arabidopsis thaliana' 'thale cress' . . Eukaryota Viridiplantae Arabidopsis thaliana Columbia . . . . . . . . . . At1g35537 . 25468 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 25468 _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 $entity . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'SHuffle strain C3030' . . . . . pETtrx_1a . . . 25468 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25468 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '1 mM peptide in a buffer of 40 mM KCl, 20 mM KH2PO4, 1 mM NaN3 at pH 6.5.' _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 entity '[U-13C; U-15N]' . . 1 $entity . . 1 . . mM . . . . 25468 1 2 'potassium chloride' 'natural abundance' . . . . . . 40 . . mM . . . . 25468 1 3 'potassium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 25468 1 4 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 25468 1 5 H2O 'natural abundance' . . . . . . 95 . . % . . . . 25468 1 6 D2O 'natural abundance' . . . . . . 5 . . % . . . . 25468 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 25468 _Sample_condition_list.ID 1 _Sample_condition_list.Details '1 mM peptide in a buffer of 40 mM KCl, 20 mM KH2PO4, 1 mM NaN3 at pH 6.5.' 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 'ionic strength' 0.16 . M 25468 1 pH 6.5 . pH 25468 1 pressure 1 . atm 25468 1 temperature 298 . K 25468 1 stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Software.Sf_category software _Software.Sf_framecode X-PLOR_NIH _Software.Entry_ID 25468 _Software.ID 1 _Software.Name X-PLOR_NIH _Software.Version 2.37 _Software.Details 'structure determination' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Charles Schwieters' . Charles.Schwieters@nih.gov 25468 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25468 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 25468 _Software.ID 2 _Software.Name NMRPipe _Software.Version 7.5 _Software.Details 'NMR data processing' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 25468 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 25468 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 25468 _Software.ID 3 _Software.Name SPARKY _Software.Version 3.113 _Software.Details 'peak picking' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 25468 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25468 3 'peak picking' 25468 3 stop_ save_ save_TALOS _Software.Sf_category software _Software.Sf_framecode TALOS _Software.Entry_ID 25468 _Software.ID 4 _Software.Name TALOS _Software.Version 3.80F1 _Software.Details 'dihedral prediction' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 25468 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'geometry optimization' 25468 4 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 25468 _Software.ID 5 _Software.Name TOPSPIN _Software.Version 3.1 _Software.Details 'data acquisition' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 25468 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 25468 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 25468 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 850 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 25468 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 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 25468 _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 . 850 . . . 25468 1 2 spectrometer_2 Bruker Avance . 700 . . . 25468 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 25468 _Experiment_list.ID 1 _Experiment_list.Details 'The 850 MHz spectrometer acquired all data for structure determination' 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 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 3 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 5 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 6 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 7 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 8 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 9 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 1 10 '3D HNHA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25468 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 25468 _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 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . 25468 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . 25468 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . 25468 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 25468 _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 2 '3D HNCACB' . . . 25468 1 3 '3D CBCA(CO)NH' . . . 25468 1 4 '3D HNCO' . . . 25468 1 5 '3D HCCH-TOCSY' . . . 25468 1 6 '3D H(CCO)NH' . . . 25468 1 7 '3D C(CO)NH' . . . 25468 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LYS HA H 1 3.988 0.002 . 1 . . . . 1 LYS HA . 25468 1 2 . 1 1 1 1 LYS HB2 H 1 1.872 0.000 . 2 . . . . 1 LYS HB . 25468 1 3 . 1 1 1 1 LYS HB3 H 1 1.872 0.000 . 2 . . . . 1 LYS HB . 25468 1 4 . 1 1 1 1 LYS HG2 H 1 1.412 0.001 . 2 . . . . 1 LYS HG . 25468 1 5 . 1 1 1 1 LYS HG3 H 1 1.412 0.001 . 2 . . . . 1 LYS HG . 25468 1 6 . 1 1 1 1 LYS HD2 H 1 1.681 0.001 . 2 . . . . 1 LYS HD . 25468 1 7 . 1 1 1 1 LYS HD3 H 1 1.681 0.001 . 2 . . . . 1 LYS HD . 25468 1 8 . 1 1 1 1 LYS CA C 13 55.665 0.003 . 1 . . . . 1 LYS CA . 25468 1 9 . 1 1 1 1 LYS CB C 13 33.137 0.000 . 1 . . . . 1 LYS CB . 25468 1 10 . 1 1 1 1 LYS CG C 13 23.942 0.000 . 1 . . . . 1 LYS CG . 25468 1 11 . 1 1 1 1 LYS CD C 13 29.196 0.049 . 1 . . . . 1 LYS CD . 25468 1 12 . 1 1 2 2 ASP H H 1 8.843 0.002 . 1 . . . . 2 ASP H . 25468 1 13 . 1 1 2 2 ASP HA H 1 4.698 0.005 . 1 . . . . 2 ASP HA . 25468 1 14 . 1 1 2 2 ASP HB2 H 1 2.770 0.006 . 2 . . . . 2 ASP HB2 . 25468 1 15 . 1 1 2 2 ASP HB3 H 1 2.637 0.005 . 2 . . . . 2 ASP HB3 . 25468 1 16 . 1 1 2 2 ASP CB C 13 39.907 0.000 . 1 . . . . 2 ASP CB . 25468 1 17 . 1 1 2 2 ASP N N 15 123.544 0.029 . 1 . . . . 2 ASP N . 25468 1 18 . 1 1 3 3 ILE H H 1 8.356 0.006 . 1 . . . . 3 ILE H . 25468 1 19 . 1 1 3 3 ILE HA H 1 4.158 0.005 . 1 . . . . 3 ILE HA . 25468 1 20 . 1 1 3 3 ILE HB H 1 1.852 0.008 . 1 . . . . 3 ILE HB . 25468 1 21 . 1 1 3 3 ILE HG12 H 1 1.427 0.004 . 2 . . . . 3 ILE HG12 . 25468 1 22 . 1 1 3 3 ILE HG13 H 1 1.147 0.005 . 2 . . . . 3 ILE HG13 . 25468 1 23 . 1 1 3 3 ILE HG21 H 1 0.872 0.005 . 1 . . . . 3 ILE HG2 . 25468 1 24 . 1 1 3 3 ILE HG22 H 1 0.872 0.005 . 1 . . . . 3 ILE HG2 . 25468 1 25 . 1 1 3 3 ILE HG23 H 1 0.872 0.005 . 1 . . . . 3 ILE HG2 . 25468 1 26 . 1 1 3 3 ILE HD11 H 1 0.842 0.007 . 1 . . . . 3 ILE HD1 . 25468 1 27 . 1 1 3 3 ILE HD12 H 1 0.842 0.007 . 1 . . . . 3 ILE HD1 . 25468 1 28 . 1 1 3 3 ILE HD13 H 1 0.842 0.007 . 1 . . . . 3 ILE HD1 . 25468 1 29 . 1 1 3 3 ILE CA C 13 61.110 0.063 . 1 . . . . 3 ILE CA . 25468 1 30 . 1 1 3 3 ILE CB C 13 39.038 0.032 . 1 . . . . 3 ILE CB . 25468 1 31 . 1 1 3 3 ILE CG1 C 13 27.250 0.040 . 1 . . . . 3 ILE CG1 . 25468 1 32 . 1 1 3 3 ILE CG2 C 13 17.594 0.046 . 1 . . . . 3 ILE CG2 . 25468 1 33 . 1 1 3 3 ILE CD1 C 13 13.237 0.000 . 1 . . . . 3 ILE CD1 . 25468 1 34 . 1 1 3 3 ILE N N 15 121.633 0.008 . 1 . . . . 3 ILE N . 25468 1 35 . 1 1 4 4 ASP H H 1 8.460 0.002 . 1 . . . . 4 ASP H . 25468 1 36 . 1 1 4 4 ASP HA H 1 4.627 0.005 . 1 . . . . 4 ASP HA . 25468 1 37 . 1 1 4 4 ASP HB2 H 1 2.863 0.006 . 2 . . . . 4 ASP HB2 . 25468 1 38 . 1 1 4 4 ASP HB3 H 1 2.685 0.009 . 2 . . . . 4 ASP HB3 . 25468 1 39 . 1 1 4 4 ASP CA C 13 53.776 0.000 . 1 . . . . 4 ASP CA . 25468 1 40 . 1 1 4 4 ASP CB C 13 40.216 0.036 . 1 . . . . 4 ASP CB . 25468 1 41 . 1 1 4 4 ASP N N 15 124.028 0.017 . 1 . . . . 4 ASP N . 25468 1 42 . 1 1 5 5 GLY H H 1 8.405 0.005 . 1 . . . . 5 GLY H . 25468 1 43 . 1 1 5 5 GLY HA2 H 1 3.922 0.003 . 2 . . . . 5 GLY HA2 . 25468 1 44 . 1 1 5 5 GLY HA3 H 1 3.740 0.003 . 2 . . . . 5 GLY HA3 . 25468 1 45 . 1 1 5 5 GLY CA C 13 45.714 0.033 . 1 . . . . 5 GLY CA . 25468 1 46 . 1 1 5 5 GLY N N 15 110.531 0.038 . 1 . . . . 5 GLY N . 25468 1 47 . 1 1 6 6 ARG H H 1 8.128 0.003 . 1 . . . . 6 ARG H . 25468 1 48 . 1 1 6 6 ARG HA H 1 4.347 0.008 . 1 . . . . 6 ARG HA . 25468 1 49 . 1 1 6 6 ARG HB2 H 1 1.899 0.004 . 2 . . . . 6 ARG HB2 . 25468 1 50 . 1 1 6 6 ARG HB3 H 1 1.781 0.006 . 2 . . . . 6 ARG HB3 . 25468 1 51 . 1 1 6 6 ARG HG2 H 1 1.658 0.009 . 2 . . . . 6 ARG HG2 . 25468 1 52 . 1 1 6 6 ARG HG3 H 1 1.614 0.011 . 2 . . . . 6 ARG HG3 . 25468 1 53 . 1 1 6 6 ARG HD2 H 1 3.026 0.004 . 2 . . . . 6 ARG HD . 25468 1 54 . 1 1 6 6 ARG HD3 H 1 3.026 0.004 . 2 . . . . 6 ARG HD . 25468 1 55 . 1 1 6 6 ARG HE H 1 7.387 0.005 . 1 . . . . 6 ARG HE . 25468 1 56 . 1 1 6 6 ARG CA C 13 56.247 0.044 . 1 . . . . 6 ARG CA . 25468 1 57 . 1 1 6 6 ARG CB C 13 31.089 0.032 . 1 . . . . 6 ARG CB . 25468 1 58 . 1 1 6 6 ARG CG C 13 27.013 0.031 . 1 . . . . 6 ARG CG . 25468 1 59 . 1 1 6 6 ARG CD C 13 43.307 0.025 . 1 . . . . 6 ARG CD . 25468 1 60 . 1 1 6 6 ARG N N 15 119.193 0.030 . 1 . . . . 6 ARG N . 25468 1 61 . 1 1 6 6 ARG NE N 15 84.633 0.026 . 1 . . . . 6 ARG NE . 25468 1 62 . 1 1 7 7 LYS H H 1 7.984 0.006 . 1 . . . . 7 LYS H . 25468 1 63 . 1 1 7 7 LYS HA H 1 4.769 0.003 . 1 . . . . 7 LYS HA . 25468 1 64 . 1 1 7 7 LYS HB2 H 1 1.891 0.003 . 2 . . . . 7 LYS HB2 . 25468 1 65 . 1 1 7 7 LYS HB3 H 1 1.693 0.005 . 2 . . . . 7 LYS HB3 . 25468 1 66 . 1 1 7 7 LYS HG2 H 1 1.528 0.000 . 2 . . . . 7 LYS HG2 . 25468 1 67 . 1 1 7 7 LYS HG3 H 1 1.503 0.003 . 2 . . . . 7 LYS HG3 . 25468 1 68 . 1 1 7 7 LYS HD2 H 1 1.758 0.000 . 2 . . . . 7 LYS HD . 25468 1 69 . 1 1 7 7 LYS HD3 H 1 1.758 0.000 . 2 . . . . 7 LYS HD . 25468 1 70 . 1 1 7 7 LYS HE2 H 1 3.031 0.000 . 2 . . . . 7 LYS HE . 25468 1 71 . 1 1 7 7 LYS HE3 H 1 3.031 0.000 . 2 . . . . 7 LYS HE . 25468 1 72 . 1 1 7 7 LYS CB C 13 33.230 0.035 . 1 . . . . 7 LYS CB . 25468 1 73 . 1 1 7 7 LYS N N 15 120.971 0.018 . 1 . . . . 7 LYS N . 25468 1 74 . 1 1 8 8 PRO HA H 1 4.538 0.005 . 1 . . . . 8 PRO HA . 25468 1 75 . 1 1 8 8 PRO HB2 H 1 1.757 0.005 . 2 . . . . 8 PRO HB2 . 25468 1 76 . 1 1 8 8 PRO HB3 H 1 1.453 0.006 . 2 . . . . 8 PRO HB3 . 25468 1 77 . 1 1 8 8 PRO HG2 H 1 2.040 0.005 . 2 . . . . 8 PRO HG2 . 25468 1 78 . 1 1 8 8 PRO HG3 H 1 1.658 0.008 . 2 . . . . 8 PRO HG3 . 25468 1 79 . 1 1 8 8 PRO HD2 H 1 3.723 0.006 . 2 . . . . 8 PRO HD2 . 25468 1 80 . 1 1 8 8 PRO HD3 H 1 3.548 0.014 . 2 . . . . 8 PRO HD3 . 25468 1 81 . 1 1 8 8 PRO CA C 13 63.203 0.000 . 1 . . . . 8 PRO CA . 25468 1 82 . 1 1 8 8 PRO CB C 13 31.855 0.049 . 1 . . . . 8 PRO CB . 25468 1 83 . 1 1 8 8 PRO CG C 13 28.208 0.043 . 1 . . . . 8 PRO CG . 25468 1 84 . 1 1 8 8 PRO CD C 13 50.573 0.019 . 1 . . . . 8 PRO CD . 25468 1 85 . 1 1 9 9 LEU H H 1 7.801 0.005 . 1 . . . . 9 LEU H . 25468 1 86 . 1 1 9 9 LEU HA H 1 4.487 0.007 . 1 . . . . 9 LEU HA . 25468 1 87 . 1 1 9 9 LEU HB2 H 1 0.997 0.013 . 2 . . . . 9 LEU HB2 . 25468 1 88 . 1 1 9 9 LEU HB3 H 1 1.283 0.007 . 2 . . . . 9 LEU HB3 . 25468 1 89 . 1 1 9 9 LEU HG H 1 1.079 0.009 . 1 . . . . 9 LEU HG . 25468 1 90 . 1 1 9 9 LEU HD11 H 1 0.769 0.008 . 2 . . . . 9 LEU HD1 . 25468 1 91 . 1 1 9 9 LEU HD12 H 1 0.769 0.008 . 2 . . . . 9 LEU HD1 . 25468 1 92 . 1 1 9 9 LEU HD13 H 1 0.769 0.008 . 2 . . . . 9 LEU HD1 . 25468 1 93 . 1 1 9 9 LEU HD21 H 1 0.901 0.005 . 2 . . . . 9 LEU HD2 . 25468 1 94 . 1 1 9 9 LEU HD22 H 1 0.901 0.005 . 2 . . . . 9 LEU HD2 . 25468 1 95 . 1 1 9 9 LEU HD23 H 1 0.901 0.005 . 2 . . . . 9 LEU HD2 . 25468 1 96 . 1 1 9 9 LEU CA C 13 53.511 0.026 . 1 . . . . 9 LEU CA . 25468 1 97 . 1 1 9 9 LEU CB C 13 46.759 0.057 . 1 . . . . 9 LEU CB . 25468 1 98 . 1 1 9 9 LEU CG C 13 26.931 0.022 . 1 . . . . 9 LEU CG . 25468 1 99 . 1 1 9 9 LEU CD1 C 13 26.225 0.087 . 2 . . . . 9 LEU CD1 . 25468 1 100 . 1 1 9 9 LEU CD2 C 13 23.032 0.021 . 2 . . . . 9 LEU CD2 . 25468 1 101 . 1 1 9 9 LEU N N 15 123.948 0.014 . 1 . . . . 9 LEU N . 25468 1 102 . 1 1 10 10 LEU H H 1 8.422 0.006 . 1 . . . . 10 LEU H . 25468 1 103 . 1 1 10 10 LEU HA H 1 4.554 0.006 . 1 . . . . 10 LEU HA . 25468 1 104 . 1 1 10 10 LEU HB2 H 1 1.668 0.004 . 2 . . . . 10 LEU HB2 . 25468 1 105 . 1 1 10 10 LEU HB3 H 1 1.444 0.010 . 2 . . . . 10 LEU HB3 . 25468 1 106 . 1 1 10 10 LEU HG H 1 1.409 0.006 . 1 . . . . 10 LEU HG . 25468 1 107 . 1 1 10 10 LEU HD11 H 1 0.737 0.007 . 2 . . . . 10 LEU HD1 . 25468 1 108 . 1 1 10 10 LEU HD12 H 1 0.737 0.007 . 2 . . . . 10 LEU HD1 . 25468 1 109 . 1 1 10 10 LEU HD13 H 1 0.737 0.007 . 2 . . . . 10 LEU HD1 . 25468 1 110 . 1 1 10 10 LEU HD21 H 1 0.826 0.008 . 2 . . . . 10 LEU HD2 . 25468 1 111 . 1 1 10 10 LEU HD22 H 1 0.826 0.008 . 2 . . . . 10 LEU HD2 . 25468 1 112 . 1 1 10 10 LEU HD23 H 1 0.826 0.008 . 2 . . . . 10 LEU HD2 . 25468 1 113 . 1 1 10 10 LEU CA C 13 55.471 0.000 . 1 . . . . 10 LEU CA . 25468 1 114 . 1 1 10 10 LEU CB C 13 42.103 0.033 . 1 . . . . 10 LEU CB . 25468 1 115 . 1 1 10 10 LEU CG C 13 28.158 0.023 . 1 . . . . 10 LEU CG . 25468 1 116 . 1 1 10 10 LEU CD1 C 13 24.923 0.050 . 2 . . . . 10 LEU CD1 . 25468 1 117 . 1 1 10 10 LEU CD2 C 13 25.529 0.051 . 2 . . . . 10 LEU CD2 . 25468 1 118 . 1 1 10 10 LEU N N 15 130.176 0.016 . 1 . . . . 10 LEU N . 25468 1 119 . 1 1 11 11 ILE H H 1 8.289 0.005 . 1 . . . . 11 ILE H . 25468 1 120 . 1 1 11 11 ILE HA H 1 4.386 0.005 . 1 . . . . 11 ILE HA . 25468 1 121 . 1 1 11 11 ILE HB H 1 1.492 0.005 . 1 . . . . 11 ILE HB . 25468 1 122 . 1 1 11 11 ILE HG12 H 1 0.746 0.007 . 2 . . . . 11 ILE HG12 . 25468 1 123 . 1 1 11 11 ILE HG13 H 1 0.457 0.009 . 2 . . . . 11 ILE HG13 . 25468 1 124 . 1 1 11 11 ILE HG21 H 1 0.359 0.009 . 1 . . . . 11 ILE HG2 . 25468 1 125 . 1 1 11 11 ILE HG22 H 1 0.359 0.009 . 1 . . . . 11 ILE HG2 . 25468 1 126 . 1 1 11 11 ILE HG23 H 1 0.359 0.009 . 1 . . . . 11 ILE HG2 . 25468 1 127 . 1 1 11 11 ILE HD11 H 1 0.067 0.003 . 1 . . . . 11 ILE HD1 . 25468 1 128 . 1 1 11 11 ILE HD12 H 1 0.067 0.003 . 1 . . . . 11 ILE HD1 . 25468 1 129 . 1 1 11 11 ILE HD13 H 1 0.067 0.003 . 1 . . . . 11 ILE HD1 . 25468 1 130 . 1 1 11 11 ILE CA C 13 61.531 0.019 . 1 . . . . 11 ILE CA . 25468 1 131 . 1 1 11 11 ILE CB C 13 39.357 0.043 . 1 . . . . 11 ILE CB . 25468 1 132 . 1 1 11 11 ILE CG1 C 13 26.366 0.053 . 1 . . . . 11 ILE CG1 . 25468 1 133 . 1 1 11 11 ILE CG2 C 13 17.466 0.025 . 1 . . . . 11 ILE CG2 . 25468 1 134 . 1 1 11 11 ILE CD1 C 13 13.067 0.021 . 1 . . . . 11 ILE CD1 . 25468 1 135 . 1 1 11 11 ILE N N 15 120.839 0.036 . 1 . . . . 11 ILE N . 25468 1 136 . 1 1 12 12 GLY H H 1 7.125 0.004 . 1 . . . . 12 GLY H . 25468 1 137 . 1 1 12 12 GLY HA2 H 1 4.163 0.004 . 2 . . . . 12 GLY HA2 . 25468 1 138 . 1 1 12 12 GLY HA3 H 1 4.573 0.005 . 2 . . . . 12 GLY HA3 . 25468 1 139 . 1 1 12 12 GLY CA C 13 44.743 0.045 . 1 . . . . 12 GLY CA . 25468 1 140 . 1 1 12 12 GLY N N 15 106.385 0.020 . 1 . . . . 12 GLY N . 25468 1 141 . 1 1 13 13 THR H H 1 9.046 0.004 . 1 . . . . 13 THR H . 25468 1 142 . 1 1 13 13 THR HA H 1 4.676 0.009 . 1 . . . . 13 THR HA . 25468 1 143 . 1 1 13 13 THR HB H 1 4.861 0.007 . 1 . . . . 13 THR HB . 25468 1 144 . 1 1 13 13 THR HG21 H 1 1.438 0.006 . 1 . . . . 13 THR HG2 . 25468 1 145 . 1 1 13 13 THR HG22 H 1 1.438 0.006 . 1 . . . . 13 THR HG2 . 25468 1 146 . 1 1 13 13 THR HG23 H 1 1.438 0.006 . 1 . . . . 13 THR HG2 . 25468 1 147 . 1 1 13 13 THR CA C 13 62.119 0.000 . 1 . . . . 13 THR CA . 25468 1 148 . 1 1 13 13 THR CB C 13 71.115 0.000 . 1 . . . . 13 THR CB . 25468 1 149 . 1 1 13 13 THR CG2 C 13 21.399 0.061 . 1 . . . . 13 THR CG2 . 25468 1 150 . 1 1 13 13 THR N N 15 110.566 0.016 . 1 . . . . 13 THR N . 25468 1 151 . 1 1 14 14 CYS H H 1 8.436 0.005 . 1 . . . . 14 CYS H . 25468 1 152 . 1 1 14 14 CYS HA H 1 4.900 0.011 . 1 . . . . 14 CYS HA . 25468 1 153 . 1 1 14 14 CYS HB2 H 1 3.174 0.002 . 2 . . . . 14 CYS HB . 25468 1 154 . 1 1 14 14 CYS HB3 H 1 3.174 0.002 . 2 . . . . 14 CYS HB . 25468 1 155 . 1 1 14 14 CYS CA C 13 58.201 0.000 . 1 . . . . 14 CYS CA . 25468 1 156 . 1 1 14 14 CYS CB C 13 44.631 0.013 . 1 . . . . 14 CYS CB . 25468 1 157 . 1 1 14 14 CYS N N 15 117.216 0.022 . 1 . . . . 14 CYS N . 25468 1 158 . 1 1 15 15 ILE H H 1 7.244 0.004 . 1 . . . . 15 ILE H . 25468 1 159 . 1 1 15 15 ILE HA H 1 3.886 0.004 . 1 . . . . 15 ILE HA . 25468 1 160 . 1 1 15 15 ILE HB H 1 1.783 0.009 . 1 . . . . 15 ILE HB . 25468 1 161 . 1 1 15 15 ILE HG12 H 1 1.584 0.005 . 2 . . . . 15 ILE HG12 . 25468 1 162 . 1 1 15 15 ILE HG13 H 1 1.302 0.002 . 2 . . . . 15 ILE HG13 . 25468 1 163 . 1 1 15 15 ILE HG21 H 1 0.850 0.006 . 1 . . . . 15 ILE HG2 . 25468 1 164 . 1 1 15 15 ILE HG22 H 1 0.850 0.006 . 1 . . . . 15 ILE HG2 . 25468 1 165 . 1 1 15 15 ILE HG23 H 1 0.850 0.006 . 1 . . . . 15 ILE HG2 . 25468 1 166 . 1 1 15 15 ILE HD11 H 1 0.863 0.006 . 1 . . . . 15 ILE HD1 . 25468 1 167 . 1 1 15 15 ILE HD12 H 1 0.863 0.006 . 1 . . . . 15 ILE HD1 . 25468 1 168 . 1 1 15 15 ILE HD13 H 1 0.863 0.006 . 1 . . . . 15 ILE HD1 . 25468 1 169 . 1 1 15 15 ILE CA C 13 63.301 0.021 . 1 . . . . 15 ILE CA . 25468 1 170 . 1 1 15 15 ILE CB C 13 37.496 0.022 . 1 . . . . 15 ILE CB . 25468 1 171 . 1 1 15 15 ILE CG1 C 13 28.062 0.070 . 1 . . . . 15 ILE CG1 . 25468 1 172 . 1 1 15 15 ILE CG2 C 13 17.237 0.042 . 1 . . . . 15 ILE CG2 . 25468 1 173 . 1 1 15 15 ILE CD1 C 13 11.664 0.025 . 1 . . . . 15 ILE CD1 . 25468 1 174 . 1 1 15 15 ILE N N 15 118.247 0.016 . 1 . . . . 15 ILE N . 25468 1 175 . 1 1 16 16 GLU H H 1 7.066 0.006 . 1 . . . . 16 GLU H . 25468 1 176 . 1 1 16 16 GLU HA H 1 3.833 0.007 . 1 . . . . 16 GLU HA . 25468 1 177 . 1 1 16 16 GLU HB2 H 1 1.929 0.005 . 2 . . . . 16 GLU HB2 . 25468 1 178 . 1 1 16 16 GLU HB3 H 1 1.686 0.004 . 2 . . . . 16 GLU HB3 . 25468 1 179 . 1 1 16 16 GLU HG2 H 1 2.043 0.009 . 2 . . . . 16 GLU HG2 . 25468 1 180 . 1 1 16 16 GLU HG3 H 1 1.571 0.004 . 2 . . . . 16 GLU HG3 . 25468 1 181 . 1 1 16 16 GLU CA C 13 57.902 0.018 . 1 . . . . 16 GLU CA . 25468 1 182 . 1 1 16 16 GLU CB C 13 28.781 0.042 . 1 . . . . 16 GLU CB . 25468 1 183 . 1 1 16 16 GLU CG C 13 33.636 0.055 . 1 . . . . 16 GLU CG . 25468 1 184 . 1 1 16 16 GLU N N 15 119.649 0.030 . 1 . . . . 16 GLU N . 25468 1 185 . 1 1 17 17 PHE H H 1 8.148 0.004 . 1 . . . . 17 PHE H . 25468 1 186 . 1 1 17 17 PHE HA H 1 4.564 0.007 . 1 . . . . 17 PHE HA . 25468 1 187 . 1 1 17 17 PHE HB2 H 1 2.424 0.005 . 2 . . . . 17 PHE HB2 . 25468 1 188 . 1 1 17 17 PHE HB3 H 1 2.943 0.006 . 2 . . . . 17 PHE HB3 . 25468 1 189 . 1 1 17 17 PHE HD1 H 1 7.245 0.007 . 3 . . . . 17 PHE HD . 25468 1 190 . 1 1 17 17 PHE HD2 H 1 7.245 0.007 . 3 . . . . 17 PHE HD . 25468 1 191 . 1 1 17 17 PHE HE1 H 1 6.936 0.005 . 3 . . . . 17 PHE HE . 25468 1 192 . 1 1 17 17 PHE HE2 H 1 6.936 0.005 . 3 . . . . 17 PHE HE . 25468 1 193 . 1 1 17 17 PHE CA C 13 54.528 0.000 . 1 . . . . 17 PHE CA . 25468 1 194 . 1 1 17 17 PHE CB C 13 39.890 0.051 . 1 . . . . 17 PHE CB . 25468 1 195 . 1 1 17 17 PHE N N 15 114.996 0.030 . 1 . . . . 17 PHE N . 25468 1 196 . 1 1 18 18 PRO HA H 1 4.853 0.014 . 1 . . . . 18 PRO HA . 25468 1 197 . 1 1 18 18 PRO HB2 H 1 2.408 0.005 . 2 . . . . 18 PRO HB2 . 25468 1 198 . 1 1 18 18 PRO HB3 H 1 2.044 0.005 . 2 . . . . 18 PRO HB3 . 25468 1 199 . 1 1 18 18 PRO HG2 H 1 1.949 0.015 . 2 . . . . 18 PRO HG2 . 25468 1 200 . 1 1 18 18 PRO HG3 H 1 1.920 0.004 . 2 . . . . 18 PRO HG3 . 25468 1 201 . 1 1 18 18 PRO HD2 H 1 3.181 0.005 . 2 . . . . 18 PRO HD2 . 25468 1 202 . 1 1 18 18 PRO HD3 H 1 3.292 0.007 . 2 . . . . 18 PRO HD3 . 25468 1 203 . 1 1 18 18 PRO CA C 13 62.917 0.000 . 1 . . . . 18 PRO CA . 25468 1 204 . 1 1 18 18 PRO CB C 13 31.868 0.055 . 1 . . . . 18 PRO CB . 25468 1 205 . 1 1 18 18 PRO CG C 13 27.737 0.025 . 1 . . . . 18 PRO CG . 25468 1 206 . 1 1 18 18 PRO CD C 13 49.628 0.060 . 1 . . . . 18 PRO CD . 25468 1 207 . 1 1 19 19 THR H H 1 8.370 0.002 . 1 . . . . 19 THR H . 25468 1 208 . 1 1 19 19 THR HA H 1 3.650 0.003 . 1 . . . . 19 THR HA . 25468 1 209 . 1 1 19 19 THR HB H 1 4.050 0.005 . 1 . . . . 19 THR HB . 25468 1 210 . 1 1 19 19 THR HG21 H 1 1.244 0.003 . 1 . . . . 19 THR HG2 . 25468 1 211 . 1 1 19 19 THR HG22 H 1 1.244 0.003 . 1 . . . . 19 THR HG2 . 25468 1 212 . 1 1 19 19 THR HG23 H 1 1.244 0.003 . 1 . . . . 19 THR HG2 . 25468 1 213 . 1 1 19 19 THR CA C 13 68.731 0.057 . 1 . . . . 19 THR CA . 25468 1 214 . 1 1 19 19 THR CB C 13 69.792 0.055 . 1 . . . . 19 THR CB . 25468 1 215 . 1 1 19 19 THR CG2 C 13 21.544 0.056 . 1 . . . . 19 THR CG2 . 25468 1 216 . 1 1 19 19 THR N N 15 114.536 0.030 . 1 . . . . 19 THR N . 25468 1 217 . 1 1 20 20 GLU H H 1 9.038 0.003 . 1 . . . . 20 GLU H . 25468 1 218 . 1 1 20 20 GLU HA H 1 4.193 0.005 . 1 . . . . 20 GLU HA . 25468 1 219 . 1 1 20 20 GLU HB2 H 1 2.078 0.014 . 2 . . . . 20 GLU HB . 25468 1 220 . 1 1 20 20 GLU HB3 H 1 2.078 0.014 . 2 . . . . 20 GLU HB . 25468 1 221 . 1 1 20 20 GLU HG2 H 1 2.480 0.005 . 2 . . . . 20 GLU HG2 . 25468 1 222 . 1 1 20 20 GLU HG3 H 1 2.425 0.010 . 2 . . . . 20 GLU HG3 . 25468 1 223 . 1 1 20 20 GLU CA C 13 60.045 0.022 . 1 . . . . 20 GLU CA . 25468 1 224 . 1 1 20 20 GLU CB C 13 28.256 0.043 . 1 . . . . 20 GLU CB . 25468 1 225 . 1 1 20 20 GLU CG C 13 34.633 0.034 . 1 . . . . 20 GLU CG . 25468 1 226 . 1 1 20 20 GLU N N 15 120.374 0.018 . 1 . . . . 20 GLU N . 25468 1 227 . 1 1 21 21 LYS H H 1 7.622 0.006 . 1 . . . . 21 LYS H . 25468 1 228 . 1 1 21 21 LYS HA H 1 4.165 0.005 . 1 . . . . 21 LYS HA . 25468 1 229 . 1 1 21 21 LYS HB2 H 1 1.998 0.010 . 2 . . . . 21 LYS HB2 . 25468 1 230 . 1 1 21 21 LYS HB3 H 1 1.891 0.010 . 2 . . . . 21 LYS HB3 . 25468 1 231 . 1 1 21 21 LYS HG2 H 1 1.631 0.007 . 2 . . . . 21 LYS HG2 . 25468 1 232 . 1 1 21 21 LYS HG3 H 1 1.480 0.004 . 2 . . . . 21 LYS HG3 . 25468 1 233 . 1 1 21 21 LYS HD2 H 1 1.776 0.008 . 2 . . . . 21 LYS HD . 25468 1 234 . 1 1 21 21 LYS HD3 H 1 1.776 0.008 . 2 . . . . 21 LYS HD . 25468 1 235 . 1 1 21 21 LYS HE2 H 1 2.962 0.009 . 2 . . . . 21 LYS HE2 . 25468 1 236 . 1 1 21 21 LYS HE3 H 1 2.890 0.006 . 2 . . . . 21 LYS HE3 . 25468 1 237 . 1 1 21 21 LYS CA C 13 59.210 0.025 . 1 . . . . 21 LYS CA . 25468 1 238 . 1 1 21 21 LYS CB C 13 33.127 0.045 . 1 . . . . 21 LYS CB . 25468 1 239 . 1 1 21 21 LYS CG C 13 25.878 0.040 . 1 . . . . 21 LYS CG . 25468 1 240 . 1 1 21 21 LYS CD C 13 29.663 0.082 . 1 . . . . 21 LYS CD . 25468 1 241 . 1 1 21 21 LYS CE C 13 42.159 0.061 . 1 . . . . 21 LYS CE . 25468 1 242 . 1 1 21 21 LYS N N 15 122.432 0.030 . 1 . . . . 21 LYS N . 25468 1 243 . 1 1 22 22 CYS H H 1 9.356 0.004 . 1 . . . . 22 CYS H . 25468 1 244 . 1 1 22 22 CYS HA H 1 4.085 0.005 . 1 . . . . 22 CYS HA . 25468 1 245 . 1 1 22 22 CYS HB2 H 1 3.643 0.005 . 2 . . . . 22 CYS HB2 . 25468 1 246 . 1 1 22 22 CYS HB3 H 1 2.736 0.005 . 2 . . . . 22 CYS HB3 . 25468 1 247 . 1 1 22 22 CYS CA C 13 58.769 0.025 . 1 . . . . 22 CYS CA . 25468 1 248 . 1 1 22 22 CYS CB C 13 36.594 0.017 . 1 . . . . 22 CYS CB . 25468 1 249 . 1 1 22 22 CYS N N 15 121.466 0.023 . 1 . . . . 22 CYS N . 25468 1 250 . 1 1 23 23 ASN H H 1 7.925 0.006 . 1 . . . . 23 ASN H . 25468 1 251 . 1 1 23 23 ASN HA H 1 4.045 0.006 . 1 . . . . 23 ASN HA . 25468 1 252 . 1 1 23 23 ASN HB2 H 1 2.861 0.007 . 2 . . . . 23 ASN HB . 25468 1 253 . 1 1 23 23 ASN HB3 H 1 2.861 0.007 . 2 . . . . 23 ASN HB . 25468 1 254 . 1 1 23 23 ASN HD21 H 1 7.753 0.002 . 2 . . . . 23 ASN HD21 . 25468 1 255 . 1 1 23 23 ASN HD22 H 1 6.930 0.004 . 2 . . . . 23 ASN HD22 . 25468 1 256 . 1 1 23 23 ASN CA C 13 57.867 0.019 . 1 . . . . 23 ASN CA . 25468 1 257 . 1 1 23 23 ASN CB C 13 39.304 0.015 . 1 . . . . 23 ASN CB . 25468 1 258 . 1 1 23 23 ASN N N 15 115.604 0.030 . 1 . . . . 23 ASN N . 25468 1 259 . 1 1 23 23 ASN ND2 N 15 114.746 0.029 . 1 . . . . 23 ASN ND2 . 25468 1 260 . 1 1 24 24 LYS H H 1 7.955 0.006 . 1 . . . . 24 LYS H . 25468 1 261 . 1 1 24 24 LYS HA H 1 3.912 0.008 . 1 . . . . 24 LYS HA . 25468 1 262 . 1 1 24 24 LYS HB2 H 1 1.957 0.012 . 2 . . . . 24 LYS HB2 . 25468 1 263 . 1 1 24 24 LYS HB3 H 1 1.876 0.008 . 2 . . . . 24 LYS HB3 . 25468 1 264 . 1 1 24 24 LYS HG2 H 1 1.548 0.009 . 2 . . . . 24 LYS HG2 . 25468 1 265 . 1 1 24 24 LYS HG3 H 1 1.427 0.005 . 2 . . . . 24 LYS HG3 . 25468 1 266 . 1 1 24 24 LYS HD2 H 1 1.690 0.010 . 2 . . . . 24 LYS HD2 . 25468 1 267 . 1 1 24 24 LYS HD3 H 1 1.657 0.006 . 2 . . . . 24 LYS HD3 . 25468 1 268 . 1 1 24 24 LYS HE2 H 1 2.984 0.010 . 2 . . . . 24 LYS HE . 25468 1 269 . 1 1 24 24 LYS HE3 H 1 2.984 0.010 . 2 . . . . 24 LYS HE . 25468 1 270 . 1 1 24 24 LYS CA C 13 59.909 0.014 . 1 . . . . 24 LYS CA . 25468 1 271 . 1 1 24 24 LYS CB C 13 33.035 0.051 . 1 . . . . 24 LYS CB . 25468 1 272 . 1 1 24 24 LYS CG C 13 24.994 0.046 . 1 . . . . 24 LYS CG . 25468 1 273 . 1 1 24 24 LYS CD C 13 29.244 0.017 . 1 . . . . 24 LYS CD . 25468 1 274 . 1 1 24 24 LYS CE C 13 42.083 0.000 . 1 . . . . 24 LYS CE . 25468 1 275 . 1 1 24 24 LYS N N 15 116.665 0.041 . 1 . . . . 24 LYS N . 25468 1 276 . 1 1 25 25 THR H H 1 8.518 0.009 . 1 . . . . 25 THR H . 25468 1 277 . 1 1 25 25 THR HA H 1 3.859 0.005 . 1 . . . . 25 THR HA . 25468 1 278 . 1 1 25 25 THR HB H 1 3.967 0.005 . 1 . . . . 25 THR HB . 25468 1 279 . 1 1 25 25 THR HG21 H 1 0.989 0.007 . 1 . . . . 25 THR HG2 . 25468 1 280 . 1 1 25 25 THR HG22 H 1 0.989 0.007 . 1 . . . . 25 THR HG2 . 25468 1 281 . 1 1 25 25 THR HG23 H 1 0.989 0.007 . 1 . . . . 25 THR HG2 . 25468 1 282 . 1 1 25 25 THR CA C 13 67.243 0.029 . 1 . . . . 25 THR CA . 25468 1 283 . 1 1 25 25 THR CB C 13 68.752 0.034 . 1 . . . . 25 THR CB . 25468 1 284 . 1 1 25 25 THR CG2 C 13 20.948 0.035 . 1 . . . . 25 THR CG2 . 25468 1 285 . 1 1 25 25 THR N N 15 116.759 0.022 . 1 . . . . 25 THR N . 25468 1 286 . 1 1 26 26 CYS H H 1 8.062 0.004 . 1 . . . . 26 CYS H . 25468 1 287 . 1 1 26 26 CYS HA H 1 4.259 0.007 . 1 . . . . 26 CYS HA . 25468 1 288 . 1 1 26 26 CYS HB2 H 1 2.564 0.004 . 2 . . . . 26 CYS HB2 . 25468 1 289 . 1 1 26 26 CYS HB3 H 1 2.405 0.029 . 2 . . . . 26 CYS HB3 . 25468 1 290 . 1 1 26 26 CYS CA C 13 57.603 0.034 . 1 . . . . 26 CYS CA . 25468 1 291 . 1 1 26 26 CYS CB C 13 34.189 0.050 . 1 . . . . 26 CYS CB . 25468 1 292 . 1 1 26 26 CYS N N 15 121.616 0.048 . 1 . . . . 26 CYS N . 25468 1 293 . 1 1 27 27 ILE H H 1 8.313 0.003 . 1 . . . . 27 ILE H . 25468 1 294 . 1 1 27 27 ILE HA H 1 4.154 0.009 . 1 . . . . 27 ILE HA . 25468 1 295 . 1 1 27 27 ILE HB H 1 1.872 0.006 . 1 . . . . 27 ILE HB . 25468 1 296 . 1 1 27 27 ILE HG12 H 1 1.521 0.005 . 2 . . . . 27 ILE HG12 . 25468 1 297 . 1 1 27 27 ILE HG13 H 1 0.975 0.011 . 2 . . . . 27 ILE HG13 . 25468 1 298 . 1 1 27 27 ILE HG21 H 1 0.943 0.010 . 1 . . . . 27 ILE HG2 . 25468 1 299 . 1 1 27 27 ILE HG22 H 1 0.943 0.010 . 1 . . . . 27 ILE HG2 . 25468 1 300 . 1 1 27 27 ILE HG23 H 1 0.943 0.010 . 1 . . . . 27 ILE HG2 . 25468 1 301 . 1 1 27 27 ILE HD11 H 1 0.839 0.008 . 1 . . . . 27 ILE HD1 . 25468 1 302 . 1 1 27 27 ILE HD12 H 1 0.839 0.008 . 1 . . . . 27 ILE HD1 . 25468 1 303 . 1 1 27 27 ILE HD13 H 1 0.839 0.008 . 1 . . . . 27 ILE HD1 . 25468 1 304 . 1 1 27 27 ILE CA C 13 65.260 0.036 . 1 . . . . 27 ILE CA . 25468 1 305 . 1 1 27 27 ILE CB C 13 38.035 0.038 . 1 . . . . 27 ILE CB . 25468 1 306 . 1 1 27 27 ILE CG1 C 13 29.802 0.033 . 1 . . . . 27 ILE CG1 . 25468 1 307 . 1 1 27 27 ILE CG2 C 13 16.889 0.059 . 1 . . . . 27 ILE CG2 . 25468 1 308 . 1 1 27 27 ILE CD1 C 13 13.599 0.041 . 1 . . . . 27 ILE CD1 . 25468 1 309 . 1 1 27 27 ILE N N 15 124.036 0.033 . 1 . . . . 27 ILE N . 25468 1 310 . 1 1 28 28 GLU H H 1 8.312 0.004 . 1 . . . . 28 GLU H . 25468 1 311 . 1 1 28 28 GLU HA H 1 4.194 0.005 . 1 . . . . 28 GLU HA . 25468 1 312 . 1 1 28 28 GLU HB2 H 1 2.248 0.016 . 2 . . . . 28 GLU HB2 . 25468 1 313 . 1 1 28 28 GLU HB3 H 1 2.314 0.005 . 2 . . . . 28 GLU HB3 . 25468 1 314 . 1 1 28 28 GLU HG2 H 1 2.688 0.011 . 2 . . . . 28 GLU HG2 . 25468 1 315 . 1 1 28 28 GLU HG3 H 1 2.566 0.005 . 2 . . . . 28 GLU HG3 . 25468 1 316 . 1 1 28 28 GLU CA C 13 58.497 0.032 . 1 . . . . 28 GLU CA . 25468 1 317 . 1 1 28 28 GLU CB C 13 27.957 0.082 . 1 . . . . 28 GLU CB . 25468 1 318 . 1 1 28 28 GLU CG C 13 34.188 0.044 . 1 . . . . 28 GLU CG . 25468 1 319 . 1 1 28 28 GLU N N 15 121.780 0.035 . 1 . . . . 28 GLU N . 25468 1 320 . 1 1 29 29 SER H H 1 7.459 0.005 . 1 . . . . 29 SER H . 25468 1 321 . 1 1 29 29 SER HA H 1 4.661 0.007 . 1 . . . . 29 SER HA . 25468 1 322 . 1 1 29 29 SER HB2 H 1 4.334 0.011 . 2 . . . . 29 SER HB2 . 25468 1 323 . 1 1 29 29 SER HB3 H 1 4.157 0.006 . 2 . . . . 29 SER HB3 . 25468 1 324 . 1 1 29 29 SER CA C 13 58.377 0.000 . 1 . . . . 29 SER CA . 25468 1 325 . 1 1 29 29 SER CB C 13 63.484 0.064 . 1 . . . . 29 SER CB . 25468 1 326 . 1 1 29 29 SER N N 15 114.001 0.023 . 1 . . . . 29 SER N . 25468 1 327 . 1 1 30 30 ASN H H 1 8.067 0.003 . 1 . . . . 30 ASN H . 25468 1 328 . 1 1 30 30 ASN HA H 1 4.427 0.004 . 1 . . . . 30 ASN HA . 25468 1 329 . 1 1 30 30 ASN HB2 H 1 2.989 0.002 . 2 . . . . 30 ASN HB2 . 25468 1 330 . 1 1 30 30 ASN HB3 H 1 2.806 0.004 . 2 . . . . 30 ASN HB3 . 25468 1 331 . 1 1 30 30 ASN HD21 H 1 7.425 0.003 . 2 . . . . 30 ASN HD21 . 25468 1 332 . 1 1 30 30 ASN HD22 H 1 6.839 0.003 . 2 . . . . 30 ASN HD22 . 25468 1 333 . 1 1 30 30 ASN CA C 13 55.041 0.105 . 1 . . . . 30 ASN CA . 25468 1 334 . 1 1 30 30 ASN CB C 13 36.344 0.041 . 1 . . . . 30 ASN CB . 25468 1 335 . 1 1 30 30 ASN N N 15 112.213 0.040 . 1 . . . . 30 ASN N . 25468 1 336 . 1 1 30 30 ASN ND2 N 15 112.519 0.026 . 1 . . . . 30 ASN ND2 . 25468 1 337 . 1 1 31 31 PHE H H 1 7.861 0.004 . 1 . . . . 31 PHE H . 25468 1 338 . 1 1 31 31 PHE HA H 1 4.574 0.007 . 1 . . . . 31 PHE HA . 25468 1 339 . 1 1 31 31 PHE HB2 H 1 3.246 0.005 . 2 . . . . 31 PHE HB2 . 25468 1 340 . 1 1 31 31 PHE HB3 H 1 2.427 0.007 . 2 . . . . 31 PHE HB3 . 25468 1 341 . 1 1 31 31 PHE HD1 H 1 6.905 0.007 . 3 . . . . 31 PHE HD . 25468 1 342 . 1 1 31 31 PHE HD2 H 1 6.905 0.007 . 3 . . . . 31 PHE HD . 25468 1 343 . 1 1 31 31 PHE HE1 H 1 7.233 0.011 . 3 . . . . 31 PHE HE . 25468 1 344 . 1 1 31 31 PHE HE2 H 1 7.233 0.011 . 3 . . . . 31 PHE HE . 25468 1 345 . 1 1 31 31 PHE CA C 13 57.969 0.000 . 1 . . . . 31 PHE CA . 25468 1 346 . 1 1 31 31 PHE CB C 13 38.699 0.053 . 1 . . . . 31 PHE CB . 25468 1 347 . 1 1 31 31 PHE N N 15 116.306 0.035 . 1 . . . . 31 PHE N . 25468 1 348 . 1 1 32 32 ALA H H 1 8.403 0.009 . 1 . . . . 32 ALA H . 25468 1 349 . 1 1 32 32 ALA HA H 1 4.191 0.006 . 1 . . . . 32 ALA HA . 25468 1 350 . 1 1 32 32 ALA HB1 H 1 1.303 0.004 . 1 . . . . 32 ALA HB . 25468 1 351 . 1 1 32 32 ALA HB2 H 1 1.303 0.004 . 1 . . . . 32 ALA HB . 25468 1 352 . 1 1 32 32 ALA HB3 H 1 1.303 0.004 . 1 . . . . 32 ALA HB . 25468 1 353 . 1 1 32 32 ALA CA C 13 53.586 0.027 . 1 . . . . 32 ALA CA . 25468 1 354 . 1 1 32 32 ALA CB C 13 19.211 0.049 . 1 . . . . 32 ALA CB . 25468 1 355 . 1 1 32 32 ALA N N 15 121.103 0.037 . 1 . . . . 32 ALA N . 25468 1 356 . 1 1 33 33 GLY H H 1 7.258 0.007 . 1 . . . . 33 GLY H . 25468 1 357 . 1 1 33 33 GLY HA2 H 1 4.078 0.011 . 2 . . . . 33 GLY HA2 . 25468 1 358 . 1 1 33 33 GLY HA3 H 1 3.846 0.009 . 2 . . . . 33 GLY HA3 . 25468 1 359 . 1 1 33 33 GLY CA C 13 44.870 0.071 . 1 . . . . 33 GLY CA . 25468 1 360 . 1 1 33 33 GLY N N 15 100.820 0.032 . 1 . . . . 33 GLY N . 25468 1 361 . 1 1 34 34 GLY H H 1 8.978 0.004 . 1 . . . . 34 GLY H . 25468 1 362 . 1 1 34 34 GLY HA2 H 1 3.838 0.004 . 2 . . . . 34 GLY HA2 . 25468 1 363 . 1 1 34 34 GLY HA3 H 1 5.379 0.006 . 2 . . . . 34 GLY HA3 . 25468 1 364 . 1 1 34 34 GLY CA C 13 46.437 0.031 . 1 . . . . 34 GLY CA . 25468 1 365 . 1 1 34 34 GLY N N 15 108.312 0.031 . 1 . . . . 34 GLY N . 25468 1 366 . 1 1 35 35 LYS H H 1 8.756 0.005 . 1 . . . . 35 LYS H . 25468 1 367 . 1 1 35 35 LYS HA H 1 4.594 0.006 . 1 . . . . 35 LYS HA . 25468 1 368 . 1 1 35 35 LYS HB2 H 1 1.866 0.009 . 2 . . . . 35 LYS HB2 . 25468 1 369 . 1 1 35 35 LYS HB3 H 1 1.700 0.006 . 2 . . . . 35 LYS HB3 . 25468 1 370 . 1 1 35 35 LYS HG2 H 1 1.424 0.012 . 2 . . . . 35 LYS HG2 . 25468 1 371 . 1 1 35 35 LYS HG3 H 1 1.318 0.006 . 2 . . . . 35 LYS HG3 . 25468 1 372 . 1 1 35 35 LYS HD2 H 1 1.525 0.006 . 2 . . . . 35 LYS HD2 . 25468 1 373 . 1 1 35 35 LYS HD3 H 1 1.458 0.010 . 2 . . . . 35 LYS HD3 . 25468 1 374 . 1 1 35 35 LYS HE2 H 1 2.693 0.009 . 2 . . . . 35 LYS HE . 25468 1 375 . 1 1 35 35 LYS HE3 H 1 2.693 0.009 . 2 . . . . 35 LYS HE . 25468 1 376 . 1 1 35 35 LYS CA C 13 54.655 0.000 . 1 . . . . 35 LYS CA . 25468 1 377 . 1 1 35 35 LYS CB C 13 37.284 0.026 . 1 . . . . 35 LYS CB . 25468 1 378 . 1 1 35 35 LYS CG C 13 24.461 0.030 . 1 . . . . 35 LYS CG . 25468 1 379 . 1 1 35 35 LYS CD C 13 29.452 0.029 . 1 . . . . 35 LYS CD . 25468 1 380 . 1 1 35 35 LYS CE C 13 42.013 0.029 . 1 . . . . 35 LYS CE . 25468 1 381 . 1 1 35 35 LYS N N 15 119.929 0.032 . 1 . . . . 35 LYS N . 25468 1 382 . 1 1 36 36 CYS H H 1 8.553 0.010 . 1 . . . . 36 CYS H . 25468 1 383 . 1 1 36 36 CYS HA H 1 5.364 0.004 . 1 . . . . 36 CYS HA . 25468 1 384 . 1 1 36 36 CYS HB2 H 1 2.488 0.002 . 2 . . . . 36 CYS HB2 . 25468 1 385 . 1 1 36 36 CYS HB3 H 1 2.985 0.003 . 2 . . . . 36 CYS HB3 . 25468 1 386 . 1 1 36 36 CYS CA C 13 57.218 0.026 . 1 . . . . 36 CYS CA . 25468 1 387 . 1 1 36 36 CYS CB C 13 44.150 0.019 . 1 . . . . 36 CYS CB . 25468 1 388 . 1 1 36 36 CYS N N 15 119.831 0.017 . 1 . . . . 36 CYS N . 25468 1 389 . 1 1 37 37 VAL H H 1 9.587 0.002 . 1 . . . . 37 VAL H . 25468 1 390 . 1 1 37 37 VAL HA H 1 4.764 0.011 . 1 . . . . 37 VAL HA . 25468 1 391 . 1 1 37 37 VAL HB H 1 2.310 0.003 . 1 . . . . 37 VAL HB . 25468 1 392 . 1 1 37 37 VAL HG11 H 1 0.961 0.007 . 2 . . . . 37 VAL HG1 . 25468 1 393 . 1 1 37 37 VAL HG12 H 1 0.961 0.007 . 2 . . . . 37 VAL HG1 . 25468 1 394 . 1 1 37 37 VAL HG13 H 1 0.961 0.007 . 2 . . . . 37 VAL HG1 . 25468 1 395 . 1 1 37 37 VAL HG21 H 1 0.860 0.002 . 2 . . . . 37 VAL HG2 . 25468 1 396 . 1 1 37 37 VAL HG22 H 1 0.860 0.002 . 2 . . . . 37 VAL HG2 . 25468 1 397 . 1 1 37 37 VAL HG23 H 1 0.860 0.002 . 2 . . . . 37 VAL HG2 . 25468 1 398 . 1 1 37 37 VAL CB C 13 36.247 0.022 . 1 . . . . 37 VAL CB . 25468 1 399 . 1 1 37 37 VAL CG1 C 13 22.033 0.036 . 2 . . . . 37 VAL CG1 . 25468 1 400 . 1 1 37 37 VAL CG2 C 13 18.921 0.097 . 2 . . . . 37 VAL CG2 . 25468 1 401 . 1 1 37 37 VAL N N 15 120.392 0.033 . 1 . . . . 37 VAL N . 25468 1 402 . 1 1 38 38 HIS H H 1 8.698 0.003 . 1 . . . . 38 HIS H . 25468 1 403 . 1 1 38 38 HIS HA H 1 5.040 0.005 . 1 . . . . 38 HIS HA . 25468 1 404 . 1 1 38 38 HIS HB2 H 1 2.998 0.004 . 2 . . . . 38 HIS HB2 . 25468 1 405 . 1 1 38 38 HIS HB3 H 1 2.932 0.009 . 2 . . . . 38 HIS HB3 . 25468 1 406 . 1 1 38 38 HIS HD2 H 1 6.976 0.012 . 1 . . . . 38 HIS HD2 . 25468 1 407 . 1 1 38 38 HIS CA C 13 53.975 0.027 . 1 . . . . 38 HIS CA . 25468 1 408 . 1 1 38 38 HIS CB C 13 29.480 0.017 . 1 . . . . 38 HIS CB . 25468 1 409 . 1 1 38 38 HIS N N 15 118.311 0.018 . 1 . . . . 38 HIS N . 25468 1 410 . 1 1 39 39 ILE H H 1 8.969 0.004 . 1 . . . . 39 ILE H . 25468 1 411 . 1 1 39 39 ILE HA H 1 4.302 0.003 . 1 . . . . 39 ILE HA . 25468 1 412 . 1 1 39 39 ILE HB H 1 1.795 0.005 . 1 . . . . 39 ILE HB . 25468 1 413 . 1 1 39 39 ILE HG12 H 1 1.360 0.006 . 2 . . . . 39 ILE HG12 . 25468 1 414 . 1 1 39 39 ILE HG13 H 1 1.128 0.008 . 2 . . . . 39 ILE HG13 . 25468 1 415 . 1 1 39 39 ILE HG21 H 1 0.835 0.007 . 1 . . . . 39 ILE HG2 . 25468 1 416 . 1 1 39 39 ILE HG22 H 1 0.835 0.007 . 1 . . . . 39 ILE HG2 . 25468 1 417 . 1 1 39 39 ILE HG23 H 1 0.835 0.007 . 1 . . . . 39 ILE HG2 . 25468 1 418 . 1 1 39 39 ILE HD11 H 1 0.738 0.011 . 1 . . . . 39 ILE HD1 . 25468 1 419 . 1 1 39 39 ILE HD12 H 1 0.738 0.011 . 1 . . . . 39 ILE HD1 . 25468 1 420 . 1 1 39 39 ILE HD13 H 1 0.738 0.011 . 1 . . . . 39 ILE HD1 . 25468 1 421 . 1 1 39 39 ILE CA C 13 59.840 0.048 . 1 . . . . 39 ILE CA . 25468 1 422 . 1 1 39 39 ILE CB C 13 38.709 0.026 . 1 . . . . 39 ILE CB . 25468 1 423 . 1 1 39 39 ILE CG1 C 13 26.782 0.045 . 1 . . . . 39 ILE CG1 . 25468 1 424 . 1 1 39 39 ILE CG2 C 13 17.126 0.039 . 1 . . . . 39 ILE CG2 . 25468 1 425 . 1 1 39 39 ILE CD1 C 13 12.186 0.032 . 1 . . . . 39 ILE CD1 . 25468 1 426 . 1 1 39 39 ILE N N 15 124.114 0.021 . 1 . . . . 39 ILE N . 25468 1 427 . 1 1 40 40 GLY H H 1 8.715 0.006 . 1 . . . . 40 GLY H . 25468 1 428 . 1 1 40 40 GLY HA2 H 1 3.883 0.004 . 2 . . . . 40 GLY HA2 . 25468 1 429 . 1 1 40 40 GLY HA3 H 1 3.756 0.004 . 2 . . . . 40 GLY HA3 . 25468 1 430 . 1 1 40 40 GLY CA C 13 46.226 0.036 . 1 . . . . 40 GLY CA . 25468 1 431 . 1 1 40 40 GLY N N 15 115.080 0.022 . 1 . . . . 40 GLY N . 25468 1 432 . 1 1 41 41 GLN H H 1 8.672 0.004 . 1 . . . . 41 GLN H . 25468 1 433 . 1 1 41 41 GLN HA H 1 4.304 0.002 . 1 . . . . 41 GLN HA . 25468 1 434 . 1 1 41 41 GLN HB2 H 1 2.258 0.010 . 2 . . . . 41 GLN HB2 . 25468 1 435 . 1 1 41 41 GLN HB3 H 1 1.907 0.003 . 2 . . . . 41 GLN HB3 . 25468 1 436 . 1 1 41 41 GLN HG2 H 1 2.323 0.006 . 2 . . . . 41 GLN HG . 25468 1 437 . 1 1 41 41 GLN HG3 H 1 2.323 0.006 . 2 . . . . 41 GLN HG . 25468 1 438 . 1 1 41 41 GLN HE21 H 1 7.525 0.002 . 2 . . . . 41 GLN HE21 . 25468 1 439 . 1 1 41 41 GLN HE22 H 1 6.833 0.002 . 2 . . . . 41 GLN HE22 . 25468 1 440 . 1 1 41 41 GLN CA C 13 55.650 0.014 . 1 . . . . 41 GLN CA . 25468 1 441 . 1 1 41 41 GLN CB C 13 28.480 0.032 . 1 . . . . 41 GLN CB . 25468 1 442 . 1 1 41 41 GLN CG C 13 34.234 0.039 . 1 . . . . 41 GLN CG . 25468 1 443 . 1 1 41 41 GLN N N 15 121.798 0.014 . 1 . . . . 41 GLN N . 25468 1 444 . 1 1 41 41 GLN NE2 N 15 112.363 0.015 . 1 . . . . 41 GLN NE2 . 25468 1 445 . 1 1 42 42 SER H H 1 7.725 0.004 . 1 . . . . 42 SER H . 25468 1 446 . 1 1 42 42 SER HA H 1 4.347 0.005 . 1 . . . . 42 SER HA . 25468 1 447 . 1 1 42 42 SER HB2 H 1 4.013 0.011 . 2 . . . . 42 SER HB2 . 25468 1 448 . 1 1 42 42 SER HB3 H 1 3.969 0.009 . 2 . . . . 42 SER HB3 . 25468 1 449 . 1 1 42 42 SER CA C 13 58.072 0.114 . 1 . . . . 42 SER CA . 25468 1 450 . 1 1 42 42 SER CB C 13 64.037 0.036 . 1 . . . . 42 SER CB . 25468 1 451 . 1 1 42 42 SER N N 15 114.462 0.014 . 1 . . . . 42 SER N . 25468 1 452 . 1 1 43 43 LEU H H 1 8.576 0.002 . 1 . . . . 43 LEU H . 25468 1 453 . 1 1 43 43 LEU HA H 1 3.950 0.003 . 1 . . . . 43 LEU HA . 25468 1 454 . 1 1 43 43 LEU HB2 H 1 1.631 0.010 . 2 . . . . 43 LEU HB2 . 25468 1 455 . 1 1 43 43 LEU HB3 H 1 1.566 0.006 . 2 . . . . 43 LEU HB3 . 25468 1 456 . 1 1 43 43 LEU HG H 1 1.610 0.001 . 1 . . . . 43 LEU HG . 25468 1 457 . 1 1 43 43 LEU HD11 H 1 0.866 0.004 . 2 . . . . 43 LEU HD1 . 25468 1 458 . 1 1 43 43 LEU HD12 H 1 0.866 0.004 . 2 . . . . 43 LEU HD1 . 25468 1 459 . 1 1 43 43 LEU HD13 H 1 0.866 0.004 . 2 . . . . 43 LEU HD1 . 25468 1 460 . 1 1 43 43 LEU HD21 H 1 0.724 0.004 . 2 . . . . 43 LEU HD2 . 25468 1 461 . 1 1 43 43 LEU HD22 H 1 0.724 0.004 . 2 . . . . 43 LEU HD2 . 25468 1 462 . 1 1 43 43 LEU HD23 H 1 0.724 0.004 . 2 . . . . 43 LEU HD2 . 25468 1 463 . 1 1 43 43 LEU CA C 13 55.295 0.020 . 1 . . . . 43 LEU CA . 25468 1 464 . 1 1 43 43 LEU CB C 13 41.400 0.011 . 1 . . . . 43 LEU CB . 25468 1 465 . 1 1 43 43 LEU CG C 13 26.945 0.052 . 1 . . . . 43 LEU CG . 25468 1 466 . 1 1 43 43 LEU CD1 C 13 24.845 0.000 . 2 . . . . 43 LEU CD1 . 25468 1 467 . 1 1 43 43 LEU CD2 C 13 22.713 0.036 . 2 . . . . 43 LEU CD2 . 25468 1 468 . 1 1 43 43 LEU N N 15 124.166 0.011 . 1 . . . . 43 LEU N . 25468 1 469 . 1 1 44 44 ASP H H 1 8.163 0.004 . 1 . . . . 44 ASP H . 25468 1 470 . 1 1 44 44 ASP HA H 1 4.731 0.000 . 1 . . . . 44 ASP HA . 25468 1 471 . 1 1 44 44 ASP HB2 H 1 2.796 0.005 . 2 . . . . 44 ASP HB2 . 25468 1 472 . 1 1 44 44 ASP HB3 H 1 2.644 0.004 . 2 . . . . 44 ASP HB3 . 25468 1 473 . 1 1 44 44 ASP CB C 13 39.979 0.035 . 1 . . . . 44 ASP CB . 25468 1 474 . 1 1 44 44 ASP N N 15 118.797 0.033 . 1 . . . . 44 ASP N . 25468 1 475 . 1 1 45 45 PHE H H 1 9.042 0.003 . 1 . . . . 45 PHE H . 25468 1 476 . 1 1 45 45 PHE HA H 1 4.920 0.014 . 1 . . . . 45 PHE HA . 25468 1 477 . 1 1 45 45 PHE HB2 H 1 3.021 0.009 . 2 . . . . 45 PHE HB2 . 25468 1 478 . 1 1 45 45 PHE HB3 H 1 2.992 0.008 . 2 . . . . 45 PHE HB3 . 25468 1 479 . 1 1 45 45 PHE HD1 H 1 6.959 0.017 . 3 . . . . 45 PHE HD . 25468 1 480 . 1 1 45 45 PHE HD2 H 1 6.959 0.017 . 3 . . . . 45 PHE HD . 25468 1 481 . 1 1 45 45 PHE HE1 H 1 7.210 0.012 . 3 . . . . 45 PHE HE . 25468 1 482 . 1 1 45 45 PHE HE2 H 1 7.210 0.012 . 3 . . . . 45 PHE HE . 25468 1 483 . 1 1 45 45 PHE CA C 13 57.607 0.098 . 1 . . . . 45 PHE CA . 25468 1 484 . 1 1 45 45 PHE CB C 13 40.083 0.020 . 1 . . . . 45 PHE CB . 25468 1 485 . 1 1 45 45 PHE N N 15 123.595 0.040 . 1 . . . . 45 PHE N . 25468 1 486 . 1 1 46 46 VAL H H 1 9.555 0.009 . 1 . . . . 46 VAL H . 25468 1 487 . 1 1 46 46 VAL HA H 1 4.693 0.008 . 1 . . . . 46 VAL HA . 25468 1 488 . 1 1 46 46 VAL HB H 1 2.067 0.006 . 1 . . . . 46 VAL HB . 25468 1 489 . 1 1 46 46 VAL HG11 H 1 0.848 0.005 . 2 . . . . 46 VAL HG1 . 25468 1 490 . 1 1 46 46 VAL HG12 H 1 0.848 0.005 . 2 . . . . 46 VAL HG1 . 25468 1 491 . 1 1 46 46 VAL HG13 H 1 0.848 0.005 . 2 . . . . 46 VAL HG1 . 25468 1 492 . 1 1 46 46 VAL HG21 H 1 0.848 0.005 . 2 . . . . 46 VAL HG2 . 25468 1 493 . 1 1 46 46 VAL HG22 H 1 0.848 0.005 . 2 . . . . 46 VAL HG2 . 25468 1 494 . 1 1 46 46 VAL HG23 H 1 0.848 0.005 . 2 . . . . 46 VAL HG2 . 25468 1 495 . 1 1 46 46 VAL CA C 13 59.915 0.000 . 1 . . . . 46 VAL CA . 25468 1 496 . 1 1 46 46 VAL CB C 13 34.666 0.061 . 1 . . . . 46 VAL CB . 25468 1 497 . 1 1 46 46 VAL CG1 C 13 21.908 0.024 . 2 . . . . 46 VAL CG1 . 25468 1 498 . 1 1 46 46 VAL CG2 C 13 18.687 0.046 . 2 . . . . 46 VAL CG2 . 25468 1 499 . 1 1 46 46 VAL N N 15 119.357 0.021 . 1 . . . . 46 VAL N . 25468 1 500 . 1 1 47 47 CYS H H 1 9.044 0.005 . 1 . . . . 47 CYS H . 25468 1 501 . 1 1 47 47 CYS HA H 1 4.830 0.012 . 1 . . . . 47 CYS HA . 25468 1 502 . 1 1 47 47 CYS HB2 H 1 3.196 0.003 . 2 . . . . 47 CYS HB2 . 25468 1 503 . 1 1 47 47 CYS HB3 H 1 2.313 0.005 . 2 . . . . 47 CYS HB3 . 25468 1 504 . 1 1 47 47 CYS CB C 13 38.730 0.056 . 1 . . . . 47 CYS CB . 25468 1 505 . 1 1 47 47 CYS N N 15 122.793 0.040 . 1 . . . . 47 CYS N . 25468 1 506 . 1 1 48 48 VAL H H 1 8.616 0.006 . 1 . . . . 48 VAL H . 25468 1 507 . 1 1 48 48 VAL HA H 1 4.533 0.005 . 1 . . . . 48 VAL HA . 25468 1 508 . 1 1 48 48 VAL HB H 1 1.681 0.002 . 1 . . . . 48 VAL HB . 25468 1 509 . 1 1 48 48 VAL HG11 H 1 0.703 0.006 . 2 . . . . 48 VAL HG1 . 25468 1 510 . 1 1 48 48 VAL HG12 H 1 0.703 0.006 . 2 . . . . 48 VAL HG1 . 25468 1 511 . 1 1 48 48 VAL HG13 H 1 0.703 0.006 . 2 . . . . 48 VAL HG1 . 25468 1 512 . 1 1 48 48 VAL HG21 H 1 0.197 0.008 . 2 . . . . 48 VAL HG2 . 25468 1 513 . 1 1 48 48 VAL HG22 H 1 0.197 0.008 . 2 . . . . 48 VAL HG2 . 25468 1 514 . 1 1 48 48 VAL HG23 H 1 0.197 0.008 . 2 . . . . 48 VAL HG2 . 25468 1 515 . 1 1 48 48 VAL CA C 13 59.817 0.000 . 1 . . . . 48 VAL CA . 25468 1 516 . 1 1 48 48 VAL CB C 13 34.398 0.020 . 1 . . . . 48 VAL CB . 25468 1 517 . 1 1 48 48 VAL CG1 C 13 22.161 0.220 . 1 . . . . 48 VAL CG1 . 25468 1 518 . 1 1 48 48 VAL CG2 C 13 22.161 0.220 . 1 . . . . 48 VAL CG2 . 25468 1 519 . 1 1 48 48 VAL N N 15 129.864 0.029 . 1 . . . . 48 VAL N . 25468 1 520 . 1 1 49 49 CYS H H 1 8.652 0.006 . 1 . . . . 49 CYS H . 25468 1 521 . 1 1 49 49 CYS HA H 1 5.148 0.009 . 1 . . . . 49 CYS HA . 25468 1 522 . 1 1 49 49 CYS HB2 H 1 1.029 0.006 . 2 . . . . 49 CYS HB2 . 25468 1 523 . 1 1 49 49 CYS HB3 H 1 1.916 0.009 . 2 . . . . 49 CYS HB3 . 25468 1 524 . 1 1 49 49 CYS CA C 13 50.429 0.043 . 1 . . . . 49 CYS CA . 25468 1 525 . 1 1 49 49 CYS CB C 13 33.873 0.044 . 1 . . . . 49 CYS CB . 25468 1 526 . 1 1 49 49 CYS N N 15 121.329 0.051 . 1 . . . . 49 CYS N . 25468 1 527 . 1 1 50 50 PHE H H 1 8.472 0.005 . 1 . . . . 50 PHE H . 25468 1 528 . 1 1 50 50 PHE HA H 1 4.949 0.006 . 1 . . . . 50 PHE HA . 25468 1 529 . 1 1 50 50 PHE HB2 H 1 2.745 0.005 . 2 . . . . 50 PHE HB2 . 25468 1 530 . 1 1 50 50 PHE HB3 H 1 2.979 0.006 . 2 . . . . 50 PHE HB3 . 25468 1 531 . 1 1 50 50 PHE HD1 H 1 7.041 0.012 . 3 . . . . 50 PHE HD . 25468 1 532 . 1 1 50 50 PHE HD2 H 1 7.041 0.012 . 3 . . . . 50 PHE HD . 25468 1 533 . 1 1 50 50 PHE HE1 H 1 7.149 0.008 . 3 . . . . 50 PHE HE . 25468 1 534 . 1 1 50 50 PHE HE2 H 1 7.149 0.008 . 3 . . . . 50 PHE HE . 25468 1 535 . 1 1 50 50 PHE CA C 13 54.652 0.033 . 1 . . . . 50 PHE CA . 25468 1 536 . 1 1 50 50 PHE CB C 13 40.593 0.055 . 1 . . . . 50 PHE CB . 25468 1 537 . 1 1 50 50 PHE N N 15 119.026 0.028 . 1 . . . . 50 PHE N . 25468 1 538 . 1 1 51 51 PRO HA H 1 4.732 0.015 . 1 . . . . 51 PRO HA . 25468 1 539 . 1 1 51 51 PRO HB2 H 1 2.339 0.005 . 2 . . . . 51 PRO HB2 . 25468 1 540 . 1 1 51 51 PRO HB3 H 1 2.054 0.007 . 2 . . . . 51 PRO HB3 . 25468 1 541 . 1 1 51 51 PRO HG2 H 1 1.884 0.005 . 2 . . . . 51 PRO HG . 25468 1 542 . 1 1 51 51 PRO HG3 H 1 1.884 0.005 . 2 . . . . 51 PRO HG . 25468 1 543 . 1 1 51 51 PRO HD2 H 1 3.738 0.004 . 2 . . . . 51 PRO HD2 . 25468 1 544 . 1 1 51 51 PRO HD3 H 1 3.598 0.003 . 2 . . . . 51 PRO HD3 . 25468 1 545 . 1 1 51 51 PRO CB C 13 33.209 0.059 . 1 . . . . 51 PRO CB . 25468 1 546 . 1 1 51 51 PRO CG C 13 27.172 0.022 . 1 . . . . 51 PRO CG . 25468 1 547 . 1 1 51 51 PRO CD C 13 51.147 0.017 . 1 . . . . 51 PRO CD . 25468 1 548 . 1 1 52 52 LYS H H 1 8.681 0.005 . 1 . . . . 52 LYS H . 25468 1 549 . 1 1 52 52 LYS HA H 1 3.959 0.005 . 1 . . . . 52 LYS HA . 25468 1 550 . 1 1 52 52 LYS HB2 H 1 1.554 0.003 . 2 . . . . 52 LYS HB . 25468 1 551 . 1 1 52 52 LYS HB3 H 1 1.554 0.003 . 2 . . . . 52 LYS HB . 25468 1 552 . 1 1 52 52 LYS HG2 H 1 1.176 0.009 . 2 . . . . 52 LYS HG2 . 25468 1 553 . 1 1 52 52 LYS HG3 H 1 1.075 0.004 . 2 . . . . 52 LYS HG3 . 25468 1 554 . 1 1 52 52 LYS HD2 H 1 1.541 0.005 . 2 . . . . 52 LYS HD . 25468 1 555 . 1 1 52 52 LYS HD3 H 1 1.541 0.005 . 2 . . . . 52 LYS HD . 25468 1 556 . 1 1 52 52 LYS HE2 H 1 2.817 0.010 . 2 . . . . 52 LYS HE2 . 25468 1 557 . 1 1 52 52 LYS HE3 H 1 2.778 0.012 . 2 . . . . 52 LYS HE3 . 25468 1 558 . 1 1 52 52 LYS CA C 13 57.670 0.026 . 1 . . . . 52 LYS CA . 25468 1 559 . 1 1 52 52 LYS CB C 13 33.225 0.023 . 1 . . . . 52 LYS CB . 25468 1 560 . 1 1 52 52 LYS CG C 13 25.140 0.036 . 1 . . . . 52 LYS CG . 25468 1 561 . 1 1 52 52 LYS CD C 13 29.410 0.024 . 1 . . . . 52 LYS CD . 25468 1 562 . 1 1 52 52 LYS CE C 13 42.050 0.033 . 1 . . . . 52 LYS CE . 25468 1 563 . 1 1 52 52 LYS N N 15 119.951 0.057 . 1 . . . . 52 LYS N . 25468 1 564 . 1 1 53 53 TYR H H 1 8.215 0.003 . 1 . . . . 53 TYR H . 25468 1 565 . 1 1 53 53 TYR HA H 1 4.471 0.002 . 1 . . . . 53 TYR HA . 25468 1 566 . 1 1 53 53 TYR HB2 H 1 2.985 0.007 . 2 . . . . 53 TYR HB . 25468 1 567 . 1 1 53 53 TYR HB3 H 1 2.985 0.007 . 2 . . . . 53 TYR HB . 25468 1 568 . 1 1 53 53 TYR HD1 H 1 7.029 0.009 . 3 . . . . 53 TYR HD . 25468 1 569 . 1 1 53 53 TYR HD2 H 1 7.029 0.009 . 3 . . . . 53 TYR HD . 25468 1 570 . 1 1 53 53 TYR HE1 H 1 6.793 0.012 . 3 . . . . 53 TYR HE . 25468 1 571 . 1 1 53 53 TYR HE2 H 1 6.793 0.012 . 3 . . . . 53 TYR HE . 25468 1 572 . 1 1 53 53 TYR CA C 13 58.049 0.027 . 1 . . . . 53 TYR CA . 25468 1 573 . 1 1 53 53 TYR CB C 13 38.268 0.028 . 1 . . . . 53 TYR CB . 25468 1 574 . 1 1 53 53 TYR N N 15 118.889 0.024 . 1 . . . . 53 TYR N . 25468 1 575 . 1 1 54 54 TYR H H 1 7.919 0.005 . 1 . . . . 54 TYR H . 25468 1 576 . 1 1 54 54 TYR HA H 1 4.494 0.008 . 1 . . . . 54 TYR HA . 25468 1 577 . 1 1 54 54 TYR HB2 H 1 3.024 0.007 . 2 . . . . 54 TYR HB2 . 25468 1 578 . 1 1 54 54 TYR HB3 H 1 2.899 0.006 . 2 . . . . 54 TYR HB3 . 25468 1 579 . 1 1 54 54 TYR HD1 H 1 7.087 0.002 . 3 . . . . 54 TYR HD . 25468 1 580 . 1 1 54 54 TYR HD2 H 1 7.087 0.002 . 3 . . . . 54 TYR HD . 25468 1 581 . 1 1 54 54 TYR HE1 H 1 6.817 0.004 . 3 . . . . 54 TYR HE . 25468 1 582 . 1 1 54 54 TYR HE2 H 1 6.817 0.004 . 3 . . . . 54 TYR HE . 25468 1 583 . 1 1 54 54 TYR CA C 13 58.101 0.016 . 1 . . . . 54 TYR CA . 25468 1 584 . 1 1 54 54 TYR CB C 13 39.611 0.042 . 1 . . . . 54 TYR CB . 25468 1 585 . 1 1 54 54 TYR N N 15 121.087 0.035 . 1 . . . . 54 TYR N . 25468 1 586 . 1 1 55 55 ILE H H 1 7.675 0.004 . 1 . . . . 55 ILE H . 25468 1 587 . 1 1 55 55 ILE HA H 1 4.008 0.002 . 1 . . . . 55 ILE HA . 25468 1 588 . 1 1 55 55 ILE HB H 1 1.726 0.002 . 1 . . . . 55 ILE HB . 25468 1 589 . 1 1 55 55 ILE HG12 H 1 1.355 0.009 . 2 . . . . 55 ILE HG12 . 25468 1 590 . 1 1 55 55 ILE HG13 H 1 1.093 0.005 . 2 . . . . 55 ILE HG13 . 25468 1 591 . 1 1 55 55 ILE HG21 H 1 0.819 0.002 . 1 . . . . 55 ILE HG2 . 25468 1 592 . 1 1 55 55 ILE HG22 H 1 0.819 0.002 . 1 . . . . 55 ILE HG2 . 25468 1 593 . 1 1 55 55 ILE HG23 H 1 0.819 0.002 . 1 . . . . 55 ILE HG2 . 25468 1 594 . 1 1 55 55 ILE HD11 H 1 0.809 0.001 . 1 . . . . 55 ILE HD1 . 25468 1 595 . 1 1 55 55 ILE HD12 H 1 0.809 0.001 . 1 . . . . 55 ILE HD1 . 25468 1 596 . 1 1 55 55 ILE HD13 H 1 0.809 0.001 . 1 . . . . 55 ILE HD1 . 25468 1 597 . 1 1 55 55 ILE CA C 13 61.773 0.018 . 1 . . . . 55 ILE CA . 25468 1 598 . 1 1 55 55 ILE CB C 13 39.615 0.018 . 1 . . . . 55 ILE CB . 25468 1 599 . 1 1 55 55 ILE CG1 C 13 27.450 0.100 . 1 . . . . 55 ILE CG1 . 25468 1 600 . 1 1 55 55 ILE CG2 C 13 17.708 0.016 . 1 . . . . 55 ILE CG2 . 25468 1 601 . 1 1 55 55 ILE CD1 C 13 13.465 0.031 . 1 . . . . 55 ILE CD1 . 25468 1 602 . 1 1 55 55 ILE N N 15 124.915 0.012 . 1 . . . . 55 ILE N . 25468 1 stop_ save_