data_18449 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18449 _Entry.Title ; Structure, sulfatide-binding properties, and inhibition of platelet aggregation by a Disabled-2-derived peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-05-08 _Entry.Accession_date 2012-05-08 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 'SOLUTION NMR' _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 Shuyan Xiao . . . 18449 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' . 18449 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID peptide . 18449 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18449 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 101 18449 '15N chemical shifts' 34 18449 '1H chemical shifts' 233 18449 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 . . 2013-02-08 2012-05-08 update BMRB 'update entry citation' 18449 1 . . 2012-09-17 2012-05-08 original author 'original release' 18449 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LSW 'BMRB Entry Tracking System' 18449 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 18449 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22977233 _Citation.Full_citation . _Citation.Title 'Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 287 _Citation.Journal_issue 45 _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 37691 _Citation.Page_last 37702 _Citation.Year 2012 _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 Shuyan Xiao . . . 18449 1 2 John Charonko . J. . 18449 1 3 Xiangping Fu . . . 18449 1 4 Alireza Salmanzadeh . . . 18449 1 5 Rafael Davalos . V. . 18449 1 6 Pavlos Vlachos . P. . 18449 1 7 Carla Finkielstein . V. . 18449 1 8 Daniel Capelluto . G.S. . 18449 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18449 _Assembly.ID 1 _Assembly.Name SBM _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 SBM 1 $SBM A . yes native no no . . . 18449 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SBM _Entity.Sf_category entity _Entity.Sf_framecode SBM _Entity.Entry_ID 18449 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name SBM _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 ; SKKEKKKGPEKTDEYLLARF KGDGVKYKAKLIGID ; _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 35 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3993.754 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1M7E . "Crystal Structure Of The Phosphotyrosine Binding Domain(Ptb) Of Mouse Disabled 2(Dab2):implications For Reeling Signaling" . . . . . 74.29 160 100.00 100.00 1.50e-07 . . . . 18449 1 2 no PDB 1P3R . "Crystal Structure Of The Phosphotyrosin Binding Domain(Ptb) Of Mouse Disabled 1(Dab1)" . . . . . 74.29 160 100.00 100.00 1.50e-07 . . . . 18449 1 3 no PDB 2LSW . "Structure, Sulfatide-Binding Properties, And Inhibition Of Platelet Aggregation By A Disabled-2-Derived Peptide" . . . . . 100.00 40 100.00 100.00 3.28e-13 . . . . 18449 1 4 no DBJ BAB22405 . "unnamed protein product [Mus musculus]" . . . . . 100.00 235 97.14 97.14 7.34e-12 . . . . 18449 1 5 no DBJ BAE32784 . "unnamed protein product [Mus musculus]" . . . . . 100.00 766 97.14 97.14 9.19e-12 . . . . 18449 1 6 no DBJ BAE37047 . "unnamed protein product [Mus musculus]" . . . . . 100.00 527 97.14 97.14 1.66e-11 . . . . 18449 1 7 no DBJ BAE37084 . "unnamed protein product [Mus musculus]" . . . . . 100.00 548 97.14 97.14 1.21e-11 . . . . 18449 1 8 no DBJ BAE38234 . "unnamed protein product [Mus musculus]" . . . . . 100.00 548 97.14 97.14 1.07e-11 . . . . 18449 1 9 no EMBL CAH89644 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 552 100.00 100.00 1.10e-12 . . . . 18449 1 10 no GB AAA98975 . "DOC-2 [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 8.44e-13 . . . . 18449 1 11 no GB AAB02645 . "p93 [Mus musculus]" . . . . . 100.00 745 97.14 97.14 1.13e-11 . . . . 18449 1 12 no GB AAB02646 . "p96 [Mus musculus]" . . . . . 100.00 766 97.14 97.14 9.10e-12 . . . . 18449 1 13 no GB AAB02647 . "p67 [Mus musculus]" . . . . . 100.00 548 97.14 97.14 1.17e-11 . . . . 18449 1 14 no GB AAB19032 . "mitogen-responsive phosphoprotein [Homo sapiens]" . . . . . 100.00 229 100.00 100.00 4.42e-13 . . . . 18449 1 15 no PIR A57542 . "p96 protein - mouse" . . . . . 100.00 837 97.14 97.14 4.73e-12 . . . . 18449 1 16 no REF NP_001008702 . "disabled homolog 2 isoform b [Mus musculus]" . . . . . 100.00 548 97.14 97.14 1.21e-11 . . . . 18449 1 17 no REF NP_001032994 . "disabled homolog 2 isoform b [Mus musculus]" . . . . . 100.00 548 97.14 97.14 1.21e-11 . . . . 18449 1 18 no REF NP_001095870 . "disabled homolog 2 isoform c [Mus musculus]" . . . . . 100.00 527 97.14 97.14 1.39e-11 . . . . 18449 1 19 no REF NP_001124738 . "disabled homolog 2 [Pongo abelii]" . . . . . 100.00 552 100.00 100.00 1.10e-12 . . . . 18449 1 20 no REF NP_001180175 . "disabled homolog 2 [Bos taurus]" . . . . . 100.00 768 97.14 97.14 9.47e-12 . . . . 18449 1 21 no SP O88797 . "RecName: Full=Disabled homolog 2; AltName: Full=Adaptor molecule disabled-2; AltName: Full=C9; AltName: Full=Differentially exp" . . . . . 100.00 768 97.14 97.14 9.11e-12 . . . . 18449 1 22 no SP P98078 . "RecName: Full=Disabled homolog 2; AltName: Full=Adaptor molecule disabled-2; AltName: Full=Differentially expressed in ovarian " . . . . . 100.00 766 97.14 97.14 9.19e-12 . . . . 18449 1 23 no SP P98082 . "RecName: Full=Disabled homolog 2; AltName: Full=Adaptor molecule disabled-2; AltName: Full=Differentially expressed in ovarian " . . . . . 100.00 770 100.00 100.00 6.75e-13 . . . . 18449 1 24 no TPG DAA17841 . "TPA: disabled homolog 2, mitogen-responsive phosphoprotein [Bos taurus]" . . . . . 100.00 768 97.14 97.14 9.47e-12 . . . . 18449 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 24 SER . 18449 1 2 25 LYS . 18449 1 3 26 LYS . 18449 1 4 27 GLU . 18449 1 5 28 LYS . 18449 1 6 29 LYS . 18449 1 7 30 LYS . 18449 1 8 31 GLY . 18449 1 9 32 PRO . 18449 1 10 33 GLU . 18449 1 11 34 LYS . 18449 1 12 35 THR . 18449 1 13 36 ASP . 18449 1 14 37 GLU . 18449 1 15 38 TYR . 18449 1 16 39 LEU . 18449 1 17 40 LEU . 18449 1 18 41 ALA . 18449 1 19 42 ARG . 18449 1 20 43 PHE . 18449 1 21 44 LYS . 18449 1 22 45 GLY . 18449 1 23 46 ASP . 18449 1 24 47 GLY . 18449 1 25 48 VAL . 18449 1 26 49 LYS . 18449 1 27 50 TYR . 18449 1 28 51 LYS . 18449 1 29 52 ALA . 18449 1 30 53 LYS . 18449 1 31 54 LEU . 18449 1 32 55 ILE . 18449 1 33 56 GLY . 18449 1 34 57 ILE . 18449 1 35 58 ASP . 18449 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 18449 1 . LYS 2 2 18449 1 . LYS 3 3 18449 1 . GLU 4 4 18449 1 . LYS 5 5 18449 1 . LYS 6 6 18449 1 . LYS 7 7 18449 1 . GLY 8 8 18449 1 . PRO 9 9 18449 1 . GLU 10 10 18449 1 . LYS 11 11 18449 1 . THR 12 12 18449 1 . ASP 13 13 18449 1 . GLU 14 14 18449 1 . TYR 15 15 18449 1 . LEU 16 16 18449 1 . LEU 17 17 18449 1 . ALA 18 18 18449 1 . ARG 19 19 18449 1 . PHE 20 20 18449 1 . LYS 21 21 18449 1 . GLY 22 22 18449 1 . ASP 23 23 18449 1 . GLY 24 24 18449 1 . VAL 25 25 18449 1 . LYS 26 26 18449 1 . TYR 27 27 18449 1 . LYS 28 28 18449 1 . ALA 29 29 18449 1 . LYS 30 30 18449 1 . LEU 31 31 18449 1 . ILE 32 32 18449 1 . GLY 33 33 18449 1 . ILE 34 34 18449 1 . ASP 35 35 18449 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 18449 _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 $SBM . 9606 organism . 'Homo sapiens' Humans . . Eukaryota Metazoa Homo Sapiens . . . . . . . . . . . . . . . . . . . . . 18449 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 18449 _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 $SBM . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pgex-6p-1 . . . . . . 18449 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 18449 _Sample.ID 1 _Sample.Type micelle _Sample.Sub_type . _Sample.Details 15N-SBM _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 DSS [U-2H] . . . . . . 50 . . uM . . . . 18449 1 2 'potassium chloride' 'natural abundance' . . . . . . 40 . . mM . . . . 18449 1 3 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 18449 1 4 citric '[U-99% 2H]' . . . . . . 10 . . mM . . . . 18449 1 5 SBM 'natural abundance' . . 1 $SBM . . 1 . . mM . . . . 18449 1 stop_ save_ save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18449 _Sample.ID 2 _Sample.Type micelle _Sample.Sub_type . _Sample.Details unlabelled-SBM _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 DSS [U-2H] . . . . . . 50 . . uM . . . . 18449 2 2 'potassium chloride' 'natural abundance' . . . . . . 40 . . mM . . . . 18449 2 3 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 18449 2 4 citric '[U-99% 2H]' . . . . . . 10 . . mM . . . . 18449 2 5 SBM 'natural abundance' . . 1 $SBM . . 1 . . mM . . . . 18449 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 18449 _Sample.ID 3 _Sample.Type micelle _Sample.Sub_type . _Sample.Details 13C,15N-SBM _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 DSS [U-2H] . . . . . . 50 . . uM . . . . 18449 3 2 'potassium chloride' 'natural abundance' . . . . . . 40 . . mM . . . . 18449 3 3 'sodium azide' 'natural abundance' . . . . . . 1 . . mM . . . . 18449 3 4 citric '[U-99% 2H]' . . . . . . 10 . . mM . . . . 18449 3 5 SBM 'natural abundance' . . 1 $SBM . . 1 . . mM . . . . 18449 3 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 18449 _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 5 . pH 18449 1 temperature 298 . K 18449 1 stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Software.Sf_category software _Software.Sf_framecode X-PLOR_NIH _Software.Entry_ID 18449 _Software.ID 1 _Software.Name 'X-PLOR NIH' _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Schwieters, Kuszewski, Tjandra and Clore' . . 18449 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18449 1 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 18449 _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_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18449 _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 . . . 18449 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 18449 _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 '3D HN(CA)CO' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 2 '3D HNCO' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 3 '3D HNCACB' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 4 '3D CBCA(CO)NH' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 5 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 6 '2D 1H-1H TOCSY' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 1 7 '2D 1H-1H NOESY' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18449 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 18449 _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 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 18449 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18449 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18449 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 18449 _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 5 '3D 1H-15N NOESY' . . . 18449 1 7 '2D 1H-1H NOESY' . . . 18449 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 SER H H 1 8.407 0.02 . 1 . . . A 24 SER HN . 18449 1 2 . 1 1 1 1 SER HA H 1 4.477 0.02 . 1 . . . A 24 SER HA . 18449 1 3 . 1 1 1 1 SER HB2 H 1 3.871 0.02 . 1 . . . A 24 SER HB2 . 18449 1 4 . 1 1 1 1 SER HB3 H 1 3.871 0.02 . 1 . . . A 24 SER QB . 18449 1 5 . 1 1 1 1 SER C C 13 171.886 0.2 . 1 . . . A 24 SER C . 18449 1 6 . 1 1 1 1 SER CA C 13 54.814 0.2 . 1 . . . A 24 SER CA . 18449 1 7 . 1 1 1 1 SER CB C 13 59.958 0.2 . 1 . . . A 24 SER CB . 18449 1 8 . 1 1 1 1 SER N N 15 118.052 0.2 . 1 . . . A 24 SER N . 18449 1 9 . 1 1 2 2 LYS H H 1 8.318 0.02 . 1 . . . A 25 LYS HN . 18449 1 10 . 1 1 2 2 LYS HA H 1 4.432 0.02 . 1 . . . A 25 LYS HA . 18449 1 11 . 1 1 2 2 LYS HB2 H 1 1.728 0.02 . 2 . . . A 25 LYS HB2 . 18449 1 12 . 1 1 2 2 LYS HB3 H 1 1.728 0.02 . 2 . . . A 25 LYS QB . 18449 1 13 . 1 1 2 2 LYS HG2 H 1 1.448 0.02 . 2 . . . A 25 LYS HG2 . 18449 1 14 . 1 1 2 2 LYS HG3 H 1 1.448 0.02 . 2 . . . A 25 LYS QG . 18449 1 15 . 1 1 2 2 LYS C C 13 173.780 0.2 . 1 . . . A 25 LYS C . 18449 1 16 . 1 1 2 2 LYS CA C 13 52.743 0.2 . 1 . . . A 25 LYS CA . 18449 1 17 . 1 1 2 2 LYS CB C 13 29.179 0.2 . 1 . . . A 25 LYS CB . 18449 1 18 . 1 1 2 2 LYS N N 15 123.163 0.2 . 1 . . . A 25 LYS N . 18449 1 19 . 1 1 3 3 LYS H H 1 8.271 0.02 . 1 . . . A 26 LYS HN . 18449 1 20 . 1 1 3 3 LYS HA H 1 4.283 0.02 . 1 . . . A 26 LYS HA . 18449 1 21 . 1 1 3 3 LYS HB2 H 1 1.737 0.02 . 2 . . . A 26 LYS HB2 . 18449 1 22 . 1 1 3 3 LYS HB3 H 1 1.737 0.02 . 2 . . . A 26 LYS QB . 18449 1 23 . 1 1 3 3 LYS HG2 H 1 1.401 0.02 . 2 . . . A 26 LYS HG2 . 18449 1 24 . 1 1 3 3 LYS HG3 H 1 1.401 0.02 . 2 . . . A 26 LYS QG . 18449 1 25 . 1 1 3 3 LYS C C 13 173.736 0.2 . 1 . . . A 26 LYS C . 18449 1 26 . 1 1 3 3 LYS CA C 13 52.621 0.2 . 1 . . . A 26 LYS CA . 18449 1 27 . 1 1 3 3 LYS CB C 13 29.325 0.2 . 1 . . . A 26 LYS CB . 18449 1 28 . 1 1 3 3 LYS N N 15 122.612 0.2 . 1 . . . A 26 LYS N . 18449 1 29 . 1 1 4 4 GLU H H 1 8.350 0.02 . 1 . . . A 27 GLU HN . 18449 1 30 . 1 1 4 4 GLU HA H 1 4.268 0.02 . 1 . . . A 27 GLU HA . 18449 1 31 . 1 1 4 4 GLU HB2 H 1 1.981 0.02 . 2 . . . A 27 GLU HB2 . 18449 1 32 . 1 1 4 4 GLU HB3 H 1 1.894 0.02 . 2 . . . A 27 GLU HB3 . 18449 1 33 . 1 1 4 4 GLU HG2 H 1 2.231 0.02 . 2 . . . A 27 GLU HG2 . 18449 1 34 . 1 1 4 4 GLU HG3 H 1 2.231 0.02 . 2 . . . A 27 GLU QG . 18449 1 35 . 1 1 4 4 GLU C C 13 173.562 0.2 . 1 . . . A 27 GLU C . 18449 1 36 . 1 1 4 4 GLU CA C 13 52.535 0.2 . 1 . . . A 27 GLU CA . 18449 1 37 . 1 1 4 4 GLU CB C 13 26.714 0.2 . 1 . . . A 27 GLU CB . 18449 1 38 . 1 1 4 4 GLU N N 15 122.511 0.2 . 1 . . . A 27 GLU N . 18449 1 39 . 1 1 5 5 LYS H H 1 8.392 0.02 . 1 . . . A 28 LYS HN . 18449 1 40 . 1 1 5 5 LYS HA H 1 4.255 0.02 . 1 . . . A 28 LYS HA . 18449 1 41 . 1 1 5 5 LYS HB2 H 1 1.742 0.02 . 2 . . . A 28 LYS HB2 . 18449 1 42 . 1 1 5 5 LYS HB3 H 1 1.742 0.02 . 2 . . . A 28 LYS QB . 18449 1 43 . 1 1 5 5 LYS HG2 H 1 1.415 0.02 . 2 . . . A 28 LYS HG2 . 18449 1 44 . 1 1 5 5 LYS HG3 H 1 1.415 0.02 . 2 . . . A 28 LYS QG . 18449 1 45 . 1 1 5 5 LYS C C 13 173.649 0.2 . 1 . . . A 28 LYS C . 18449 1 46 . 1 1 5 5 LYS CA C 13 52.503 0.2 . 1 . . . A 28 LYS CA . 18449 1 47 . 1 1 5 5 LYS CB C 13 29.336 0.2 . 1 . . . A 28 LYS CB . 18449 1 48 . 1 1 5 5 LYS N N 15 123.542 0.2 . 1 . . . A 28 LYS N . 18449 1 49 . 1 1 6 6 LYS H H 1 8.367 0.02 . 1 . . . A 29 LYS HN . 18449 1 50 . 1 1 6 6 LYS HA H 1 4.261 0.02 . 1 . . . A 29 LYS HA . 18449 1 51 . 1 1 6 6 LYS HB2 H 1 1.735 0.02 . 2 . . . A 29 LYS HB2 . 18449 1 52 . 1 1 6 6 LYS HB3 H 1 1.735 0.02 . 2 . . . A 29 LYS QB . 18449 1 53 . 1 1 6 6 LYS HG2 H 1 1.419 0.02 . 2 . . . A 29 LYS HG2 . 18449 1 54 . 1 1 6 6 LYS HG3 H 1 1.419 0.02 . 2 . . . A 29 LYS QG . 18449 1 55 . 1 1 6 6 LYS C C 13 173.668 0.2 . 1 . . . A 29 LYS C . 18449 1 56 . 1 1 6 6 LYS CA C 13 52.457 0.2 . 1 . . . A 29 LYS CA . 18449 1 57 . 1 1 6 6 LYS CB C 13 29.346 0.2 . 1 . . . A 29 LYS CB . 18449 1 58 . 1 1 6 6 LYS N N 15 123.541 0.2 . 1 . . . A 29 LYS N . 18449 1 59 . 1 1 7 7 LYS H H 1 8.440 0.02 . 1 . . . A 30 LYS HN . 18449 1 60 . 1 1 7 7 LYS HA H 1 4.303 0.02 . 1 . . . A 30 LYS HA . 18449 1 61 . 1 1 7 7 LYS HB2 H 1 1.772 0.02 . 2 . . . A 30 LYS HB2 . 18449 1 62 . 1 1 7 7 LYS HB3 H 1 1.772 0.02 . 2 . . . A 30 LYS QB . 18449 1 63 . 1 1 7 7 LYS HG2 H 1 1.439 0.02 . 2 . . . A 30 LYS HG2 . 18449 1 64 . 1 1 7 7 LYS HG3 H 1 1.439 0.02 . 2 . . . A 30 LYS QG . 18449 1 65 . 1 1 7 7 LYS C C 13 174.004 0.2 . 1 . . . A 30 LYS C . 18449 1 66 . 1 1 7 7 LYS CA C 13 52.522 0.2 . 1 . . . A 30 LYS CA . 18449 1 67 . 1 1 7 7 LYS CB C 13 29.553 0.2 . 1 . . . A 30 LYS CB . 18449 1 68 . 1 1 7 7 LYS N N 15 123.696 0.2 . 1 . . . A 30 LYS N . 18449 1 69 . 1 1 8 8 GLY H H 1 8.318 0.02 . 1 . . . A 31 GLY HN . 18449 1 70 . 1 1 8 8 GLY HA2 H 1 4.178 0.02 . 2 . . . A 31 GLY HA2 . 18449 1 71 . 1 1 8 8 GLY HA3 H 1 3.993 0.02 . 2 . . . A 31 GLY HA3 . 18449 1 72 . 1 1 8 8 GLY C C 13 168.877 0.2 . 1 . . . A 31 GLY C . 18449 1 73 . 1 1 8 8 GLY CA C 13 40.520 0.2 . 1 . . . A 31 GLY CA . 18449 1 74 . 1 1 8 8 GLY N N 15 110.736 0.2 . 1 . . . A 31 GLY N . 18449 1 75 . 1 1 9 9 PRO HA H 1 4.402 0.02 . 1 . . . A 32 PRO HA . 18449 1 76 . 1 1 9 9 PRO HB2 H 1 2.238 0.02 . 2 . . . A 32 PRO HB2 . 18449 1 77 . 1 1 9 9 PRO HB3 H 1 1.880 0.02 . 2 . . . A 32 PRO HB3 . 18449 1 78 . 1 1 9 9 PRO HG2 H 1 1.977 0.02 . 2 . . . A 32 PRO HG2 . 18449 1 79 . 1 1 9 9 PRO HG3 H 1 1.977 0.02 . 2 . . . A 32 PRO QG . 18449 1 80 . 1 1 9 9 PRO HD2 H 1 3.591 0.02 . 2 . . . A 32 PRO HD2 . 18449 1 81 . 1 1 9 9 PRO HD3 H 1 3.591 0.02 . 2 . . . A 32 PRO QD . 18449 1 82 . 1 1 9 9 PRO C C 13 174.308 0.2 . 1 . . . A 32 PRO C . 18449 1 83 . 1 1 9 9 PRO CA C 13 59.186 0.2 . 1 . . . A 32 PRO CA . 18449 1 84 . 1 1 9 9 PRO CB C 13 28.434 0.2 . 1 . . . A 32 PRO CB . 18449 1 85 . 1 1 10 10 GLU H H 1 8.589 0.02 . 1 . . . A 33 GLU HN . 18449 1 86 . 1 1 10 10 GLU HA H 1 4.262 0.02 . 1 . . . A 33 GLU HA . 18449 1 87 . 1 1 10 10 GLU HB2 H 1 2.032 0.02 . 2 . . . A 33 GLU HB2 . 18449 1 88 . 1 1 10 10 GLU HB3 H 1 1.925 0.02 . 2 . . . A 33 GLU HB3 . 18449 1 89 . 1 1 10 10 GLU HG2 H 1 2.304 0.02 . 2 . . . A 33 GLU HG2 . 18449 1 90 . 1 1 10 10 GLU HG3 H 1 2.304 0.02 . 2 . . . A 33 GLU QG . 18449 1 91 . 1 1 10 10 GLU C C 13 173.883 0.2 . 1 . . . A 33 GLU C . 18449 1 92 . 1 1 10 10 GLU CA C 13 52.751 0.2 . 1 . . . A 33 GLU CA . 18449 1 93 . 1 1 10 10 GLU CB C 13 26.538 0.2 . 1 . . . A 33 GLU CB . 18449 1 94 . 1 1 10 10 GLU N N 15 121.419 0.2 . 1 . . . A 33 GLU N . 18449 1 95 . 1 1 11 11 LYS H H 1 8.471 0.02 . 1 . . . A 34 LYS HN . 18449 1 96 . 1 1 11 11 LYS HA H 1 4.394 0.02 . 1 . . . A 34 LYS HA . 18449 1 97 . 1 1 11 11 LYS HB2 H 1 1.943 0.02 . 2 . . . A 34 LYS HB2 . 18449 1 98 . 1 1 11 11 LYS HB3 H 1 1.756 0.02 . 2 . . . A 34 LYS HB3 . 18449 1 99 . 1 1 11 11 LYS HG2 H 1 1.454 0.02 . 2 . . . A 34 LYS HG2 . 18449 1 100 . 1 1 11 11 LYS HG3 H 1 1.454 0.02 . 2 . . . A 34 LYS QG . 18449 1 101 . 1 1 11 11 LYS HD2 H 1 1.689 0.02 . 2 . . . A 34 LYS HD2 . 18449 1 102 . 1 1 11 11 LYS HD3 H 1 1.689 0.02 . 2 . . . A 34 LYS QD . 18449 1 103 . 1 1 11 11 LYS C C 13 174.352 0.2 . 1 . . . A 34 LYS C . 18449 1 104 . 1 1 11 11 LYS CA C 13 52.548 0.2 . 1 . . . A 34 LYS CA . 18449 1 105 . 1 1 11 11 LYS CB C 13 29.297 0.2 . 1 . . . A 34 LYS CB . 18449 1 106 . 1 1 11 11 LYS N N 15 122.500 0.2 . 1 . . . A 34 LYS N . 18449 1 107 . 1 1 12 12 THR H H 1 8.356 0.02 . 1 . . . A 35 THR HN . 18449 1 108 . 1 1 12 12 THR HA H 1 4.151 0.02 . 1 . . . A 35 THR HA . 18449 1 109 . 1 1 12 12 THR HB H 1 4.112 0.02 . 1 . . . A 35 THR HB . 18449 1 110 . 1 1 12 12 THR HG21 H 1 1.198 0.02 . 1 . . . A 35 THR HG21 . 18449 1 111 . 1 1 12 12 THR HG22 H 1 1.198 0.02 . 1 . . . A 35 THR HG22 . 18449 1 112 . 1 1 12 12 THR HG23 H 1 1.198 0.02 . 1 . . . A 35 THR HG23 . 18449 1 113 . 1 1 12 12 THR C C 13 172.139 0.2 . 1 . . . A 35 THR C . 18449 1 114 . 1 1 12 12 THR CA C 13 60.091 0.2 . 1 . . . A 35 THR CA . 18449 1 115 . 1 1 12 12 THR CB C 13 65.388 0.2 . 1 . . . A 35 THR CB . 18449 1 116 . 1 1 12 12 THR N N 15 116.471 0.2 . 1 . . . A 35 THR N . 18449 1 117 . 1 1 13 13 ASP H H 1 8.655 0.02 . 1 . . . A 36 ASP HN . 18449 1 118 . 1 1 13 13 ASP HA H 1 4.412 0.02 . 1 . . . A 36 ASP HA . 18449 1 119 . 1 1 13 13 ASP HB2 H 1 2.670 0.02 . 2 . . . A 36 ASP HB2 . 18449 1 120 . 1 1 13 13 ASP HB3 H 1 2.670 0.02 . 2 . . . A 36 ASP QB . 18449 1 121 . 1 1 13 13 ASP C C 13 173.604 0.2 . 1 . . . A 36 ASP C . 18449 1 122 . 1 1 13 13 ASP CA C 13 51.553 0.2 . 1 . . . A 36 ASP CA . 18449 1 123 . 1 1 13 13 ASP CB C 13 35.813 0.2 . 1 . . . A 36 ASP CB . 18449 1 124 . 1 1 13 13 ASP N N 15 120.494 0.2 . 1 . . . A 36 ASP N . 18449 1 125 . 1 1 14 14 GLU H H 1 8.034 0.02 . 1 . . . A 37 GLU HN . 18449 1 126 . 1 1 14 14 GLU HA H 1 4.094 0.02 . 1 . . . A 37 GLU HA . 18449 1 127 . 1 1 14 14 GLU HB2 H 1 1.997 0.02 . 2 . . . A 37 GLU HB2 . 18449 1 128 . 1 1 14 14 GLU HB3 H 1 1.997 0.02 . 2 . . . A 37 GLU QB . 18449 1 129 . 1 1 14 14 GLU HG2 H 1 2.309 0.02 . 2 . . . A 37 GLU HG2 . 18449 1 130 . 1 1 14 14 GLU HG3 H 1 2.245 0.02 . 2 . . . A 37 GLU HG3 . 18449 1 131 . 1 1 14 14 GLU C C 13 174.696 0.2 . 1 . . . A 37 GLU C . 18449 1 132 . 1 1 14 14 GLU CA C 13 54.159 0.2 . 1 . . . A 37 GLU CA . 18449 1 133 . 1 1 14 14 GLU CB C 13 25.855 0.2 . 1 . . . A 37 GLU CB . 18449 1 134 . 1 1 14 14 GLU N N 15 120.459 0.2 . 1 . . . A 37 GLU N . 18449 1 135 . 1 1 15 15 TYR H H 1 8.245 0.02 . 1 . . . A 38 TYR HN . 18449 1 136 . 1 1 15 15 TYR HA H 1 4.400 0.02 . 1 . . . A 38 TYR HA . 18449 1 137 . 1 1 15 15 TYR HB2 H 1 3.154 0.02 . 2 . . . A 38 TYR HB2 . 18449 1 138 . 1 1 15 15 TYR HB3 H 1 3.085 0.02 . 2 . . . A 38 TYR HB3 . 18449 1 139 . 1 1 15 15 TYR HD1 H 1 7.113 0.02 . 3 . . . A 38 TYR HD1 . 18449 1 140 . 1 1 15 15 TYR HD2 H 1 7.113 0.02 . 3 . . . A 38 TYR HD2 . 18449 1 141 . 1 1 15 15 TYR HE1 H 1 6.793 0.02 . 3 . . . A 38 TYR HE1 . 18449 1 142 . 1 1 15 15 TYR HE2 H 1 6.793 0.02 . 3 . . . A 38 TYR HE2 . 18449 1 143 . 1 1 15 15 TYR C C 13 174.195 0.2 . 1 . . . A 38 TYR C . 18449 1 144 . 1 1 15 15 TYR CA C 13 55.793 0.2 . 1 . . . A 38 TYR CA . 18449 1 145 . 1 1 15 15 TYR CB C 13 34.569 0.2 . 1 . . . A 38 TYR CB . 18449 1 146 . 1 1 15 15 TYR N N 15 120.652 0.2 . 1 . . . A 38 TYR N . 18449 1 147 . 1 1 16 16 LEU H H 1 8.348 0.02 . 1 . . . A 39 LEU HN . 18449 1 148 . 1 1 16 16 LEU HA H 1 3.952 0.02 . 1 . . . A 39 LEU HA . 18449 1 149 . 1 1 16 16 LEU HB2 H 1 1.853 0.02 . 2 . . . A 39 LEU HB2 . 18449 1 150 . 1 1 16 16 LEU HB3 H 1 1.760 0.02 . 2 . . . A 39 LEU HB3 . 18449 1 151 . 1 1 16 16 LEU HG H 1 1.469 0.02 . 1 . . . A 39 LEU HG . 18449 1 152 . 1 1 16 16 LEU HD11 H 1 0.931 0.02 . 2 . . . A 39 LEU HD11 . 18449 1 153 . 1 1 16 16 LEU HD12 H 1 0.931 0.02 . 2 . . . A 39 LEU HD12 . 18449 1 154 . 1 1 16 16 LEU HD13 H 1 0.931 0.02 . 2 . . . A 39 LEU HD13 . 18449 1 155 . 1 1 16 16 LEU HD21 H 1 0.931 0.02 . 2 . . . A 39 LEU HD21 . 18449 1 156 . 1 1 16 16 LEU HD22 H 1 0.931 0.02 . 2 . . . A 39 LEU HD22 . 18449 1 157 . 1 1 16 16 LEU HD23 H 1 0.931 0.02 . 2 . . . A 39 LEU HD23 . 18449 1 158 . 1 1 16 16 LEU C C 13 175.464 0.2 . 1 . . . A 39 LEU C . 18449 1 159 . 1 1 16 16 LEU CA C 13 53.934 0.2 . 1 . . . A 39 LEU CA . 18449 1 160 . 1 1 16 16 LEU CB C 13 38.514 0.2 . 1 . . . A 39 LEU CB . 18449 1 161 . 1 1 16 16 LEU N N 15 120.954 0.2 . 1 . . . A 39 LEU N . 18449 1 162 . 1 1 17 17 LEU H H 1 8.097 0.02 . 1 . . . A 40 LEU HN . 18449 1 163 . 1 1 17 17 LEU HA H 1 4.084 0.02 . 1 . . . A 40 LEU HA . 18449 1 164 . 1 1 17 17 LEU HB2 H 1 1.730 0.02 . 2 . . . A 40 LEU HB2 . 18449 1 165 . 1 1 17 17 LEU HB3 H 1 1.730 0.02 . 2 . . . A 40 LEU QB . 18449 1 166 . 1 1 17 17 LEU HG H 1 1.470 0.02 . 1 . . . A 40 LEU HG . 18449 1 167 . 1 1 17 17 LEU HD11 H 1 0.931 0.02 . 2 . . . A 40 LEU HD11 . 18449 1 168 . 1 1 17 17 LEU HD12 H 1 0.931 0.02 . 2 . . . A 40 LEU HD12 . 18449 1 169 . 1 1 17 17 LEU HD13 H 1 0.931 0.02 . 2 . . . A 40 LEU HD13 . 18449 1 170 . 1 1 17 17 LEU HD21 H 1 0.931 0.02 . 2 . . . A 40 LEU HD21 . 18449 1 171 . 1 1 17 17 LEU HD22 H 1 0.931 0.02 . 2 . . . A 40 LEU HD22 . 18449 1 172 . 1 1 17 17 LEU HD23 H 1 0.931 0.02 . 2 . . . A 40 LEU HD23 . 18449 1 173 . 1 1 17 17 LEU C C 13 175.709 0.2 . 1 . . . A 40 LEU C . 18449 1 174 . 1 1 17 17 LEU CA C 13 53.513 0.2 . 1 . . . A 40 LEU CA . 18449 1 175 . 1 1 17 17 LEU CB C 13 37.771 0.2 . 1 . . . A 40 LEU CB . 18449 1 176 . 1 1 17 17 LEU N N 15 117.546 0.2 . 1 . . . A 40 LEU N . 18449 1 177 . 1 1 18 18 ALA H H 1 7.829 0.02 . 1 . . . A 41 ALA HN . 18449 1 178 . 1 1 18 18 ALA HA H 1 4.072 0.02 . 1 . . . A 41 ALA HA . 18449 1 179 . 1 1 18 18 ALA HB1 H 1 1.446 0.02 . 1 . . . A 41 ALA HB1 . 18449 1 180 . 1 1 18 18 ALA HB2 H 1 1.446 0.02 . 1 . . . A 41 ALA HB2 . 18449 1 181 . 1 1 18 18 ALA HB3 H 1 1.446 0.02 . 1 . . . A 41 ALA HB3 . 18449 1 182 . 1 1 18 18 ALA C C 13 177.428 0.2 . 1 . . . A 41 ALA C . 18449 1 183 . 1 1 18 18 ALA CA C 13 51.126 0.2 . 1 . . . A 41 ALA CA . 18449 1 184 . 1 1 18 18 ALA CB C 13 14.780 0.2 . 1 . . . A 41 ALA CB . 18449 1 185 . 1 1 18 18 ALA N N 15 120.206 0.2 . 1 . . . A 41 ALA N . 18449 1 186 . 1 1 19 19 ARG H H 1 7.888 0.02 . 1 . . . A 42 ARG HN . 18449 1 187 . 1 1 19 19 ARG HA H 1 4.056 0.02 . 1 . . . A 42 ARG HA . 18449 1 188 . 1 1 19 19 ARG HB2 H 1 1.593 0.02 . 2 . . . A 42 ARG HB2 . 18449 1 189 . 1 1 19 19 ARG HB3 H 1 1.593 0.02 . 2 . . . A 42 ARG QB . 18449 1 190 . 1 1 19 19 ARG HG2 H 1 1.255 0.02 . 2 . . . A 42 ARG HG2 . 18449 1 191 . 1 1 19 19 ARG HG3 H 1 1.179 0.02 . 2 . . . A 42 ARG HG3 . 18449 1 192 . 1 1 19 19 ARG HD2 H 1 2.998 0.02 . 2 . . . A 42 ARG HD2 . 18449 1 193 . 1 1 19 19 ARG HD3 H 1 2.911 0.02 . 2 . . . A 42 ARG HD3 . 18449 1 194 . 1 1 19 19 ARG HE H 1 7.428 0.02 . 1 . . . A 42 ARG HE . 18449 1 195 . 1 1 19 19 ARG C C 13 174.758 0.2 . 1 . . . A 42 ARG C . 18449 1 196 . 1 1 19 19 ARG CA C 13 53.809 0.2 . 1 . . . A 42 ARG CA . 18449 1 197 . 1 1 19 19 ARG CB C 13 25.921 0.2 . 1 . . . A 42 ARG CB . 18449 1 198 . 1 1 19 19 ARG N N 15 117.440 0.2 . 1 . . . A 42 ARG N . 18449 1 199 . 1 1 20 20 PHE H H 1 7.955 0.02 . 1 . . . A 43 PHE HN . 18449 1 200 . 1 1 20 20 PHE HA H 1 4.572 0.02 . 1 . . . A 43 PHE HA . 18449 1 201 . 1 1 20 20 PHE HB2 H 1 3.307 0.02 . 2 . . . A 43 PHE HB2 . 18449 1 202 . 1 1 20 20 PHE HB3 H 1 2.960 0.02 . 2 . . . A 43 PHE HB3 . 18449 1 203 . 1 1 20 20 PHE HD1 H 1 7.232 0.02 . 3 . . . A 43 PHE HD1 . 18449 1 204 . 1 1 20 20 PHE HD2 H 1 7.232 0.02 . 3 . . . A 43 PHE HD2 . 18449 1 205 . 1 1 20 20 PHE HE1 H 1 7.171 0.02 . 3 . . . A 43 PHE HE1 . 18449 1 206 . 1 1 20 20 PHE HE2 H 1 7.171 0.02 . 3 . . . A 43 PHE HE2 . 18449 1 207 . 1 1 20 20 PHE C C 13 173.259 0.2 . 1 . . . A 43 PHE C . 18449 1 208 . 1 1 20 20 PHE CA C 13 54.930 0.2 . 1 . . . A 43 PHE CA . 18449 1 209 . 1 1 20 20 PHE CB C 13 35.522 0.2 . 1 . . . A 43 PHE CB . 18449 1 210 . 1 1 20 20 PHE N N 15 117.423 0.2 . 1 . . . A 43 PHE N . 18449 1 211 . 1 1 21 21 LYS H H 1 7.929 0.02 . 1 . . . A 44 LYS HN . 18449 1 212 . 1 1 21 21 LYS HA H 1 4.074 0.02 . 1 . . . A 44 LYS HA . 18449 1 213 . 1 1 21 21 LYS HB2 H 1 1.883 0.02 . 2 . . . A 44 LYS HB2 . 18449 1 214 . 1 1 21 21 LYS HB3 H 1 1.883 0.02 . 2 . . . A 44 LYS QB . 18449 1 215 . 1 1 21 21 LYS HG2 H 1 1.533 0.02 . 2 . . . A 44 LYS HG2 . 18449 1 216 . 1 1 21 21 LYS HG3 H 1 1.533 0.02 . 2 . . . A 44 LYS QG . 18449 1 217 . 1 1 21 21 LYS HD2 H 1 1.685 0.02 . 2 . . . A 44 LYS HD2 . 18449 1 218 . 1 1 21 21 LYS HD3 H 1 1.685 0.02 . 2 . . . A 44 LYS QD . 18449 1 219 . 1 1 21 21 LYS C C 13 174.903 0.2 . 1 . . . A 44 LYS C . 18449 1 220 . 1 1 21 21 LYS CA C 13 54.765 0.2 . 1 . . . A 44 LYS CA . 18449 1 221 . 1 1 21 21 LYS CB C 13 28.883 0.2 . 1 . . . A 44 LYS CB . 18449 1 222 . 1 1 21 21 LYS N N 15 119.081 0.2 . 1 . . . A 44 LYS N . 18449 1 223 . 1 1 22 22 GLY H H 1 8.416 0.02 . 1 . . . A 45 GLY HN . 18449 1 224 . 1 1 22 22 GLY HA2 H 1 3.985 0.02 . 2 . . . A 45 GLY HA2 . 18449 1 225 . 1 1 22 22 GLY HA3 H 1 3.898 0.02 . 2 . . . A 45 GLY HA3 . 18449 1 226 . 1 1 22 22 GLY C C 13 172.596 0.2 . 1 . . . A 45 GLY C . 18449 1 227 . 1 1 22 22 GLY CA C 13 42.389 0.2 . 1 . . . A 45 GLY CA . 18449 1 228 . 1 1 22 22 GLY N N 15 108.400 0.2 . 1 . . . A 45 GLY N . 18449 1 229 . 1 1 23 23 ASP H H 1 8.345 0.02 . 1 . . . A 46 ASP HN . 18449 1 230 . 1 1 23 23 ASP HA H 1 4.610 0.02 . 1 . . . A 46 ASP HA . 18449 1 231 . 1 1 23 23 ASP HB2 H 1 2.866 0.02 . 2 . . . A 46 ASP HB2 . 18449 1 232 . 1 1 23 23 ASP HB3 H 1 2.696 0.02 . 2 . . . A 46 ASP HB3 . 18449 1 233 . 1 1 23 23 ASP C C 13 174.568 0.2 . 1 . . . A 46 ASP C . 18449 1 234 . 1 1 23 23 ASP CA C 13 51.540 0.2 . 1 . . . A 46 ASP CA . 18449 1 235 . 1 1 23 23 ASP CB C 13 36.249 0.2 . 1 . . . A 46 ASP CB . 18449 1 236 . 1 1 23 23 ASP N N 15 120.595 0.2 . 1 . . . A 46 ASP N . 18449 1 237 . 1 1 24 24 GLY H H 1 8.587 0.02 . 1 . . . A 47 GLY HN . 18449 1 238 . 1 1 24 24 GLY HA2 H 1 3.825 0.02 . 2 . . . A 47 GLY HA2 . 18449 1 239 . 1 1 24 24 GLY HA3 H 1 3.825 0.02 . 2 . . . A 47 GLY QA . 18449 1 240 . 1 1 24 24 GLY C C 13 172.152 0.2 . 1 . . . A 47 GLY C . 18449 1 241 . 1 1 24 24 GLY CA C 13 43.502 0.2 . 1 . . . A 47 GLY CA . 18449 1 242 . 1 1 24 24 GLY N N 15 108.925 0.2 . 1 . . . A 47 GLY N . 18449 1 243 . 1 1 25 25 VAL H H 1 7.979 0.02 . 1 . . . A 48 VAL HN . 18449 1 244 . 1 1 25 25 VAL HA H 1 3.764 0.02 . 1 . . . A 48 VAL HA . 18449 1 245 . 1 1 25 25 VAL HB H 1 2.115 0.02 . 1 . . . A 48 VAL HB . 18449 1 246 . 1 1 25 25 VAL HG11 H 1 1.047 0.02 . 1 . . . A 48 VAL HG11 . 18449 1 247 . 1 1 25 25 VAL HG12 H 1 1.047 0.02 . 1 . . . A 48 VAL HG12 . 18449 1 248 . 1 1 25 25 VAL HG13 H 1 1.047 0.02 . 1 . . . A 48 VAL HG13 . 18449 1 249 . 1 1 25 25 VAL HG21 H 1 0.947 0.02 . 1 . . . A 48 VAL HG21 . 18449 1 250 . 1 1 25 25 VAL HG22 H 1 0.947 0.02 . 1 . . . A 48 VAL HG22 . 18449 1 251 . 1 1 25 25 VAL HG23 H 1 0.947 0.02 . 1 . . . A 48 VAL HG23 . 18449 1 252 . 1 1 25 25 VAL C C 13 174.894 0.2 . 1 . . . A 48 VAL C . 18449 1 253 . 1 1 25 25 VAL CA C 13 61.430 0.2 . 1 . . . A 48 VAL CA . 18449 1 254 . 1 1 25 25 VAL CB C 13 28.106 0.2 . 1 . . . A 48 VAL CB . 18449 1 255 . 1 1 25 25 VAL N N 15 119.548 0.2 . 1 . . . A 48 VAL N . 18449 1 256 . 1 1 26 26 LYS H H 1 7.862 0.02 . 1 . . . A 49 LYS HN . 18449 1 257 . 1 1 26 26 LYS HA H 1 4.059 0.02 . 1 . . . A 49 LYS HA . 18449 1 258 . 1 1 26 26 LYS HB2 H 1 1.718 0.02 . 2 . . . A 49 LYS HB2 . 18449 1 259 . 1 1 26 26 LYS HB3 H 1 1.718 0.02 . 2 . . . A 49 LYS QB . 18449 1 260 . 1 1 26 26 LYS HG2 H 1 1.424 0.02 . 2 . . . A 49 LYS HG2 . 18449 1 261 . 1 1 26 26 LYS HG3 H 1 1.424 0.02 . 2 . . . A 49 LYS QG . 18449 1 262 . 1 1 26 26 LYS HD2 H 1 1.672 0.02 . 2 . . . A 49 LYS HD2 . 18449 1 263 . 1 1 26 26 LYS HD3 H 1 1.672 0.02 . 2 . . . A 49 LYS QD . 18449 1 264 . 1 1 26 26 LYS C C 13 175.545 0.2 . 1 . . . A 49 LYS C . 18449 1 265 . 1 1 26 26 LYS CA C 13 54.765 0.2 . 1 . . . A 49 LYS CA . 18449 1 266 . 1 1 26 26 LYS CB C 13 28.675 0.2 . 1 . . . A 49 LYS CB . 18449 1 267 . 1 1 26 26 LYS N N 15 120.856 0.2 . 1 . . . A 49 LYS N . 18449 1 268 . 1 1 27 27 TYR H H 1 8.006 0.02 . 1 . . . A 50 TYR HN . 18449 1 269 . 1 1 27 27 TYR HA H 1 4.376 0.02 . 1 . . . A 50 TYR HA . 18449 1 270 . 1 1 27 27 TYR HB2 H 1 3.053 0.02 . 2 . . . A 50 TYR HB2 . 18449 1 271 . 1 1 27 27 TYR HB3 H 1 2.926 0.02 . 2 . . . A 50 TYR HB3 . 18449 1 272 . 1 1 27 27 TYR HD1 H 1 7.056 0.02 . 3 . . . A 50 TYR HD1 . 18449 1 273 . 1 1 27 27 TYR HD2 H 1 7.056 0.02 . 3 . . . A 50 TYR HD2 . 18449 1 274 . 1 1 27 27 TYR HE1 H 1 6.791 0.02 . 3 . . . A 50 TYR HE1 . 18449 1 275 . 1 1 27 27 TYR HE2 H 1 6.791 0.02 . 3 . . . A 50 TYR HE2 . 18449 1 276 . 1 1 27 27 TYR C C 13 174.292 0.2 . 1 . . . A 50 TYR C . 18449 1 277 . 1 1 27 27 TYR CA C 13 56.534 0.2 . 1 . . . A 50 TYR CA . 18449 1 278 . 1 1 27 27 TYR CB C 13 34.319 0.2 . 1 . . . A 50 TYR CB . 18449 1 279 . 1 1 27 27 TYR N N 15 117.994 0.2 . 1 . . . A 50 TYR N . 18449 1 280 . 1 1 28 28 LYS H H 1 8.119 0.02 . 1 . . . A 51 LYS HN . 18449 1 281 . 1 1 28 28 LYS HA H 1 3.932 0.02 . 1 . . . A 51 LYS HA . 18449 1 282 . 1 1 28 28 LYS HB2 H 1 1.950 0.02 . 2 . . . A 51 LYS HB2 . 18449 1 283 . 1 1 28 28 LYS HB3 H 1 1.894 0.02 . 2 . . . A 51 LYS HB3 . 18449 1 284 . 1 1 28 28 LYS HG2 H 1 1.438 0.02 . 2 . . . A 51 LYS HG2 . 18449 1 285 . 1 1 28 28 LYS HG3 H 1 1.438 0.02 . 2 . . . A 51 LYS QG . 18449 1 286 . 1 1 28 28 LYS HD2 H 1 1.674 0.02 . 2 . . . A 51 LYS HD2 . 18449 1 287 . 1 1 28 28 LYS HD3 H 1 1.674 0.02 . 2 . . . A 51 LYS QD . 18449 1 288 . 1 1 28 28 LYS C C 13 174.680 0.2 . 1 . . . A 51 LYS C . 18449 1 289 . 1 1 28 28 LYS CA C 13 55.577 0.2 . 1 . . . A 51 LYS CA . 18449 1 290 . 1 1 28 28 LYS CB C 13 28.509 0.2 . 1 . . . A 51 LYS CB . 18449 1 291 . 1 1 28 28 LYS N N 15 120.354 0.2 . 1 . . . A 51 LYS N . 18449 1 292 . 1 1 29 29 ALA H H 1 7.968 0.02 . 1 . . . A 52 ALA HN . 18449 1 293 . 1 1 29 29 ALA HA H 1 4.072 0.02 . 1 . . . A 52 ALA HA . 18449 1 294 . 1 1 29 29 ALA HB1 H 1 1.435 0.02 . 1 . . . A 52 ALA HB1 . 18449 1 295 . 1 1 29 29 ALA HB2 H 1 1.435 0.02 . 1 . . . A 52 ALA HB2 . 18449 1 296 . 1 1 29 29 ALA HB3 H 1 1.435 0.02 . 1 . . . A 52 ALA HB3 . 18449 1 297 . 1 1 29 29 ALA C C 13 176.530 0.2 . 1 . . . A 52 ALA C . 18449 1 298 . 1 1 29 29 ALA CA C 13 50.718 0.2 . 1 . . . A 52 ALA CA . 18449 1 299 . 1 1 29 29 ALA CB C 13 14.812 0.2 . 1 . . . A 52 ALA CB . 18449 1 300 . 1 1 29 29 ALA N N 15 120.186 0.2 . 1 . . . A 52 ALA N . 18449 1 301 . 1 1 30 30 LYS H H 1 7.712 0.02 . 1 . . . A 53 LYS HN . 18449 1 302 . 1 1 30 30 LYS HA H 1 4.126 0.02 . 1 . . . A 53 LYS HA . 18449 1 303 . 1 1 30 30 LYS HB2 H 1 1.960 0.02 . 2 . . . A 53 LYS HB2 . 18449 1 304 . 1 1 30 30 LYS HB3 H 1 1.892 0.02 . 2 . . . A 53 LYS HB3 . 18449 1 305 . 1 1 30 30 LYS HG2 H 1 1.528 0.02 . 2 . . . A 53 LYS HG2 . 18449 1 306 . 1 1 30 30 LYS HG3 H 1 1.528 0.02 . 2 . . . A 53 LYS QG . 18449 1 307 . 1 1 30 30 LYS HE2 H 1 2.946 0.02 . 2 . . . A 53 LYS HE2 . 18449 1 308 . 1 1 30 30 LYS HE3 H 1 2.946 0.02 . 2 . . . A 53 LYS QE . 18449 1 309 . 1 1 30 30 LYS C C 13 174.833 0.2 . 1 . . . A 53 LYS C . 18449 1 310 . 1 1 30 30 LYS CA C 13 53.962 0.2 . 1 . . . A 53 LYS CA . 18449 1 311 . 1 1 30 30 LYS CB C 13 28.773 0.2 . 1 . . . A 53 LYS CB . 18449 1 312 . 1 1 30 30 LYS N N 15 116.894 0.2 . 1 . . . A 53 LYS N . 18449 1 313 . 1 1 31 31 LEU H H 1 7.826 0.02 . 1 . . . A 54 LEU HN . 18449 1 314 . 1 1 31 31 LEU HA H 1 4.181 0.02 . 1 . . . A 54 LEU HA . 18449 1 315 . 1 1 31 31 LEU HB2 H 1 1.790 0.02 . 2 . . . A 54 LEU HB2 . 18449 1 316 . 1 1 31 31 LEU HB3 H 1 1.790 0.02 . 2 . . . A 54 LEU QB . 18449 1 317 . 1 1 31 31 LEU HG H 1 1.550 0.02 . 1 . . . A 54 LEU HG . 18449 1 318 . 1 1 31 31 LEU HD11 H 1 0.883 0.02 . 2 . . . A 54 LEU HD11 . 18449 1 319 . 1 1 31 31 LEU HD12 H 1 0.883 0.02 . 2 . . . A 54 LEU HD12 . 18449 1 320 . 1 1 31 31 LEU HD13 H 1 0.883 0.02 . 2 . . . A 54 LEU HD13 . 18449 1 321 . 1 1 31 31 LEU HD21 H 1 0.883 0.02 . 2 . . . A 54 LEU HD21 . 18449 1 322 . 1 1 31 31 LEU HD22 H 1 0.883 0.02 . 2 . . . A 54 LEU HD22 . 18449 1 323 . 1 1 31 31 LEU HD23 H 1 0.883 0.02 . 2 . . . A 54 LEU HD23 . 18449 1 324 . 1 1 31 31 LEU C C 13 174.274 0.2 . 1 . . . A 54 LEU C . 18449 1 325 . 1 1 31 31 LEU CA C 13 52.844 0.2 . 1 . . . A 54 LEU CA . 18449 1 326 . 1 1 31 31 LEU CB C 13 38.948 0.2 . 1 . . . A 54 LEU CB . 18449 1 327 . 1 1 31 31 LEU N N 15 118.047 0.2 . 1 . . . A 54 LEU N . 18449 1 328 . 1 1 32 32 ILE H H 1 7.663 0.02 . 1 . . . A 55 ILE HN . 18449 1 329 . 1 1 32 32 ILE HA H 1 4.190 0.02 . 1 . . . A 55 ILE HA . 18449 1 330 . 1 1 32 32 ILE HB H 1 1.984 0.02 . 1 . . . A 55 ILE HB . 18449 1 331 . 1 1 32 32 ILE HG12 H 1 1.504 0.02 . 2 . . . A 55 ILE HG12 . 18449 1 332 . 1 1 32 32 ILE HG13 H 1 1.275 0.02 . 2 . . . A 55 ILE HG13 . 18449 1 333 . 1 1 32 32 ILE HG21 H 1 0.905 0.02 . 1 . . . A 55 ILE HG21 . 18449 1 334 . 1 1 32 32 ILE HG22 H 1 0.905 0.02 . 1 . . . A 55 ILE HG22 . 18449 1 335 . 1 1 32 32 ILE HG23 H 1 0.905 0.02 . 1 . . . A 55 ILE HG23 . 18449 1 336 . 1 1 32 32 ILE HD11 H 1 0.866 0.02 . 1 . . . A 55 ILE HD11 . 18449 1 337 . 1 1 32 32 ILE HD12 H 1 0.866 0.02 . 1 . . . A 55 ILE HD12 . 18449 1 338 . 1 1 32 32 ILE HD13 H 1 0.866 0.02 . 1 . . . A 55 ILE HD13 . 18449 1 339 . 1 1 32 32 ILE C C 13 173.572 0.2 . 1 . . . A 55 ILE C . 18449 1 340 . 1 1 32 32 ILE CA C 13 57.711 0.2 . 1 . . . A 55 ILE CA . 18449 1 341 . 1 1 32 32 ILE CB C 13 34.774 0.2 . 1 . . . A 55 ILE CB . 18449 1 342 . 1 1 32 32 ILE N N 15 113.992 0.2 . 1 . . . A 55 ILE N . 18449 1 343 . 1 1 33 33 GLY H H 1 8.008 0.02 . 1 . . . A 56 GLY HN . 18449 1 344 . 1 1 33 33 GLY HA2 H 1 4.122 0.02 . 2 . . . A 56 GLY HA2 . 18449 1 345 . 1 1 33 33 GLY HA3 H 1 3.913 0.02 . 2 . . . A 56 GLY HA3 . 18449 1 346 . 1 1 33 33 GLY C C 13 171.340 0.2 . 1 . . . A 56 GLY C . 18449 1 347 . 1 1 33 33 GLY CA C 13 41.754 0.2 . 1 . . . A 56 GLY CA . 18449 1 348 . 1 1 33 33 GLY N N 15 109.333 0.2 . 1 . . . A 56 GLY N . 18449 1 349 . 1 1 34 34 ILE H H 1 7.762 0.02 . 1 . . . A 57 ILE HN . 18449 1 350 . 1 1 34 34 ILE HA H 1 4.199 0.02 . 1 . . . A 57 ILE HA . 18449 1 351 . 1 1 34 34 ILE HB H 1 1.882 0.02 . 1 . . . A 57 ILE HB . 18449 1 352 . 1 1 34 34 ILE HG12 H 1 1.457 0.02 . 2 . . . A 57 ILE HG12 . 18449 1 353 . 1 1 34 34 ILE HG13 H 1 1.140 0.02 . 2 . . . A 57 ILE HG13 . 18449 1 354 . 1 1 34 34 ILE HG21 H 1 0.885 0.02 . 1 . . . A 57 ILE HG21 . 18449 1 355 . 1 1 34 34 ILE HG22 H 1 0.885 0.02 . 1 . . . A 57 ILE HG22 . 18449 1 356 . 1 1 34 34 ILE HG23 H 1 0.885 0.02 . 1 . . . A 57 ILE HG23 . 18449 1 357 . 1 1 34 34 ILE C C 13 171.858 0.2 . 1 . . . A 57 ILE C . 18449 1 358 . 1 1 34 34 ILE CA C 13 57.508 0.2 . 1 . . . A 57 ILE CA . 18449 1 359 . 1 1 34 34 ILE CB C 13 35.215 0.2 . 1 . . . A 57 ILE CB . 18449 1 360 . 1 1 34 34 ILE N N 15 117.833 0.2 . 1 . . . A 57 ILE N . 18449 1 361 . 1 1 35 35 ASP H H 1 7.882 0.02 . 1 . . . A 58 ASP HN . 18449 1 362 . 1 1 35 35 ASP HA H 1 4.423 0.02 . 1 . . . A 58 ASP HA . 18449 1 363 . 1 1 35 35 ASP HB2 H 1 2.721 0.02 . 2 . . . A 58 ASP HB2 . 18449 1 364 . 1 1 35 35 ASP HB3 H 1 2.591 0.02 . 2 . . . A 58 ASP HB3 . 18449 1 365 . 1 1 35 35 ASP C C 13 176.607 0.2 . 1 . . . A 58 ASP C . 18449 1 366 . 1 1 35 35 ASP CA C 13 50.638 0.2 . 1 . . . A 58 ASP CA . 18449 1 367 . 1 1 35 35 ASP CB C 13 36.952 0.2 . 1 . . . A 58 ASP CB . 18449 1 368 . 1 1 35 35 ASP N N 15 125.807 0.2 . 1 . . . A 58 ASP N . 18449 1 stop_ save_