data_16104 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16104 _Entry.Title ; THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2009-01-02 _Entry.Accession_date 2009-01-02 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.125 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Sharadrao Patil . M. . 16104 2 Shihao Xu . . . 16104 3 Sarah Sheftic . R. . 16104 4 Andrei Alexandrescu . T. . 16104 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 . 'not applicable' 'not applicable' . 16104 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID amyloid . 16104 hormone . 16104 IAPP . 16104 Micelle-bound . 16104 'type II diabetes' . 16104 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16104 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 44 16104 '1H chemical shifts' 192 16104 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 3 . . 2010-05-27 2009-01-02 update BMRB 'edit entity/assembly name' 16104 2 . . 2009-04-30 2009-01-02 update BMRB 'complete entry citation' 16104 1 . . 2009-03-17 2009-01-02 original author 'original release' 16104 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 16104 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 19244249 _Citation.Full_citation . _Citation.Title 'THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 284 _Citation.Journal_issue 18 _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 11982 _Citation.Page_last 11991 _Citation.Year 2009 _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 Sharadrao Patil . M. . 16104 1 2 Shihao Xu . . . 16104 1 3 Sarah Sheftic . R. . 16104 1 4 Andrei Alexandrescu . T. . 16104 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16104 _Assembly.ID 1 _Assembly.Name AMYLIN _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 alpha-helix 1 $entity A . yes native no no . . . 16104 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 16104 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name alpha-helix _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 ; KCNTATCATQRLANFLVHSS NNFGAILSSTNVGSNTY ; _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 37 _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 3909.330 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 16105 . alpha-helix . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 16104 1 2 no BMRB 17394 . entity . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 16104 1 3 no BMRB 18795 . Amylin . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 16104 1 4 no BMRB 20045 . IAPP . . . . . 51.35 19 100.00 100.00 2.51e-03 . . . . 16104 1 5 no PDB 2G48 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amylin" . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 16104 1 6 no PDB 2KB8 . "The Dynamic Alpha-Helix Structure Of Micelle-Bound Human Amylin" . . . . . 97.30 37 100.00 100.00 8.00e-15 . . . . 16104 1 7 no PDB 2L86 . "Solution Nmr Structure Of Human Amylin In Sds Micelles At Ph 7.3" . . . . . 100.00 38 100.00 100.00 6.46e-16 . . . . 16104 1 8 no PDB 3G7V . "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" . . . . . 100.00 408 100.00 100.00 5.83e-16 . . . . 16104 1 9 no PDB 3G7W . "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" . . . . . 59.46 393 100.00 100.00 6.07e-06 . . . . 16104 1 10 no PDB 3HGZ . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amylin" . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 16104 1 11 no DBJ BAG73319 . "islet amyloid polypeptide [synthetic construct]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 12 no EMBL CAA33032 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 13 no EMBL CAA37002 . "islet amyloid polypeptide [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 14 no EMBL CAA39504 . "IAPP [Homo sapiens]" . . . . . 100.00 89 97.30 97.30 2.31e-15 . . . . 16104 1 15 no EMBL CAA48724 . "islet amyloid polypeptide (IAAP) [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 16 no EMBL CAB57803 . "prepro-IAPP [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 16104 1 17 no GB AAA35524 . "amylin, partial [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 16104 1 18 no GB AAA35983 . "islet amyloid polypeptide (hIAPP), partial [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 19 no GB AAA51728 . "amyloid protein, partial [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 16104 1 20 no GB AAA52281 . "islet amyloid polypeptide [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 21 no GB AAI11850 . "IAPP protein, partial [synthetic construct]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 22 no REF NP_000406 . "islet amyloid polypeptide precursor [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 1 23 no REF XP_001144800 . "PREDICTED: islet amyloid polypeptide [Pan troglodytes]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 16104 1 24 no REF XP_003265632 . "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 16104 1 25 no REF XP_003265633 . "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 16104 1 26 no REF XP_003828947 . "PREDICTED: islet amyloid polypeptide [Pan paniscus]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 16104 1 27 no SP P10997 . "RecName: Full=Islet amyloid polypeptide; AltName: Full=Amylin; AltName: Full=Diabetes-associated peptide; Short=DAP; AltName: F" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 16104 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 . LYS . 16104 1 2 . CYS . 16104 1 3 . ASN . 16104 1 4 . THR . 16104 1 5 . ALA . 16104 1 6 . THR . 16104 1 7 . CYS . 16104 1 8 . ALA . 16104 1 9 . THR . 16104 1 10 . GLN . 16104 1 11 . ARG . 16104 1 12 . LEU . 16104 1 13 . ALA . 16104 1 14 . ASN . 16104 1 15 . PHE . 16104 1 16 . LEU . 16104 1 17 . VAL . 16104 1 18 . HIS . 16104 1 19 . SER . 16104 1 20 . SER . 16104 1 21 . ASN . 16104 1 22 . ASN . 16104 1 23 . PHE . 16104 1 24 . GLY . 16104 1 25 . ALA . 16104 1 26 . ILE . 16104 1 27 . LEU . 16104 1 28 . SER . 16104 1 29 . SER . 16104 1 30 . THR . 16104 1 31 . ASN . 16104 1 32 . VAL . 16104 1 33 . GLY . 16104 1 34 . SER . 16104 1 35 . ASN . 16104 1 36 . THR . 16104 1 37 . TYR . 16104 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 16104 1 . CYS 2 2 16104 1 . ASN 3 3 16104 1 . THR 4 4 16104 1 . ALA 5 5 16104 1 . THR 6 6 16104 1 . CYS 7 7 16104 1 . ALA 8 8 16104 1 . THR 9 9 16104 1 . GLN 10 10 16104 1 . ARG 11 11 16104 1 . LEU 12 12 16104 1 . ALA 13 13 16104 1 . ASN 14 14 16104 1 . PHE 15 15 16104 1 . LEU 16 16 16104 1 . VAL 17 17 16104 1 . HIS 18 18 16104 1 . SER 19 19 16104 1 . SER 20 20 16104 1 . ASN 21 21 16104 1 . ASN 22 22 16104 1 . PHE 23 23 16104 1 . GLY 24 24 16104 1 . ALA 25 25 16104 1 . ILE 26 26 16104 1 . LEU 27 27 16104 1 . SER 28 28 16104 1 . SER 29 29 16104 1 . THR 30 30 16104 1 . ASN 31 31 16104 1 . VAL 32 32 16104 1 . GLY 33 33 16104 1 . SER 34 34 16104 1 . ASN 35 35 16104 1 . THR 36 36 16104 1 . TYR 37 37 16104 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 16104 _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 $entity . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . 'Our recombinant peptide differs from human amylin by not having an amidated C-terminus' . . 16104 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 16104 _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 $entity . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . 'purchased from rPeptide' . . . ; Recombinant 15N-labeled amylin was purchased from rPeptide: http://www.rpeptide.com We don't have the details of the expression system. ; . . 16104 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 16104 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; 0.5 mg unlabled amylin (from rPeptide lot 70507 AM) was dissolved in 0.25 ml of 100 mM SDS-d25, containing 60 mM d4-acetic acid in 99.96% D2O. Final protein concentration was 0.5 mM, sample pD 4.2, all experiments done at 37 oC. This sample was used for NOESY experiments in D2O. ; _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% 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-100% 15N]' . . 1 $entity . . 0.5 . . mM . . . . 16104 1 2 'sodium dodecyl sulfate' '[U-99% 2H]' . . . . . . 100 . . mM . . . . 16104 1 3 'acetic acid' '[U-99% 2H]' . . . . . . 60 . . mM . . . . 16104 1 stop_ save_ save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 16104 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; 0.5 mg 15N-amylin (from rPeptide, lot 718071NAM)was dissolved in 100 mM d25-SDS, 60 mM acetic acid, 90% H2O/ 10% D2O. The final peptide concentration was 0.5 mM, pH 4.6. All experiments were done at 37 C. This sample was used for all NMR assignment data and for collecting structure data. ; _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 entity '[U-99% 15N]' . . 1 $entity . . 0.5 . . mM . . . . 16104 2 2 SDS [U-2H] . . . . . . 100 . . mM . . . . 16104 2 3 'acetic acid' 'natural abundance' . . . . . . 60 . . mM . . . . 16104 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 16104 _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 'ionic strength' 60 . mM 16104 1 pH 4.6 . pH 16104 1 pressure 1.0 . atm 16104 1 temperature 310 . K 16104 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 16104 _Sample_condition_list.ID 2 _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 'ionic strength' 60 . mM 16104 2 pH* 4.2 . pH 16104 2 temperature 310 . K 16104 2 stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 16104 _Software.ID 1 _Software.Name X-PLOR _Software.Version 3.851 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Brunger . . 16104 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 16104 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 16104 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _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 16104 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian INOVA . 600 . . . 16104 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 16104 _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 1H-15N NOESY' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 1 2 '3D HNCA' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 1 3 '3D HNHB' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 1 4 '2D 1H-1H NOESY' no . . . . . . . . . . 2 $sample_1 isotropic . . . $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 1 5 '3D TROSY' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 1 6 '3D TOCSY' no . . . . . . . . . . 2 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16104 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 16104 _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 . indirect 0.251449530 . . . . . . . . . 16104 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 16104 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 16104 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 16104 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '3D 1H-15N NOESY' . . . 16104 1 2 '3D HNCA' . . . 16104 1 3 '3D HNHB' . . . 16104 1 4 '2D 1H-1H NOESY' . . . 16104 1 5 '3D TROSY' . . . 16104 1 6 '3D TOCSY' . . . 16104 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 4.105 0.05 . 1 . . . . 1 LYS HA . 16104 1 2 . 1 1 2 2 CYS H H 1 8.735 0.05 . 1 . . . . 2 CYS H . 16104 1 3 . 1 1 2 2 CYS HA H 1 4.815 0.05 . 1 . . . . 2 CYS HA . 16104 1 4 . 1 1 2 2 CYS HB2 H 1 3.215 0.05 . 2 . . . . 2 CYS HB2 . 16104 1 5 . 1 1 2 2 CYS HB3 H 1 3.155 0.05 . 2 . . . . 2 CYS HB3 . 16104 1 6 . 1 1 2 2 CYS N N 15 122.02 0.3 . 1 . . . . 2 CYS N . 16104 1 7 . 1 1 3 3 ASN H H 1 8.635 0.05 . 1 . . . . 3 ASN H . 16104 1 8 . 1 1 3 3 ASN HA H 1 4.795 0.05 . 1 . . . . 3 ASN HA . 16104 1 9 . 1 1 3 3 ASN HB2 H 1 2.835 0.05 . 2 . . . . 3 ASN HB2 . 16104 1 10 . 1 1 3 3 ASN HB3 H 1 2.985 0.05 . 2 . . . . 3 ASN HB3 . 16104 1 11 . 1 1 3 3 ASN HD21 H 1 7.635 0.05 . 2 . . . . 3 ASN HD21 . 16104 1 12 . 1 1 3 3 ASN HD22 H 1 6.925 0.05 . 2 . . . . 3 ASN HD22 . 16104 1 13 . 1 1 3 3 ASN N N 15 119.65 0.3 . 1 . . . . 3 ASN N . 16104 1 14 . 1 1 3 3 ASN ND2 N 15 113.04 0.3 . 1 . . . . 3 ASN ND2 . 16104 1 15 . 1 1 4 4 THR H H 1 7.432 0.05 . 1 . . . . 4 THR H . 16104 1 16 . 1 1 4 4 THR HA H 1 4.695 0.05 . 1 . . . . 4 THR HA . 16104 1 17 . 1 1 4 4 THR HG21 H 1 1.295 0.05 . 1 . . . . 4 THR MG . 16104 1 18 . 1 1 4 4 THR HG22 H 1 1.295 0.05 . 1 . . . . 4 THR MG . 16104 1 19 . 1 1 4 4 THR HG23 H 1 1.295 0.05 . 1 . . . . 4 THR MG . 16104 1 20 . 1 1 4 4 THR N N 15 107.81 0.3 . 1 . . . . 4 THR N . 16104 1 21 . 1 1 5 5 ALA H H 1 8.745 0.05 . 1 . . . . 5 ALA H . 16104 1 22 . 1 1 5 5 ALA HA H 1 4.145 0.05 . 1 . . . . 5 ALA HA . 16104 1 23 . 1 1 5 5 ALA HB1 H 1 1.535 0.05 . 1 . . . . 5 ALA MB . 16104 1 24 . 1 1 5 5 ALA HB2 H 1 1.535 0.05 . 1 . . . . 5 ALA MB . 16104 1 25 . 1 1 5 5 ALA HB3 H 1 1.535 0.05 . 1 . . . . 5 ALA MB . 16104 1 26 . 1 1 5 5 ALA N N 15 123.22 0.3 . 1 . . . . 5 ALA N . 16104 1 27 . 1 1 6 6 THR H H 1 7.991 0.05 . 1 . . . . 6 THR H . 16104 1 28 . 1 1 6 6 THR HA H 1 4.225 0.05 . 1 . . . . 6 THR HA . 16104 1 29 . 1 1 6 6 THR HG21 H 1 1.255 0.05 . . . . . . 6 THR MG . 16104 1 30 . 1 1 6 6 THR HG22 H 1 1.255 0.05 . . . . . . 6 THR MG . 16104 1 31 . 1 1 6 6 THR HG23 H 1 1.255 0.05 . . . . . . 6 THR MG . 16104 1 32 . 1 1 6 6 THR N N 15 110.78 0.3 . 1 . . . . 6 THR N . 16104 1 33 . 1 1 7 7 CYS H H 1 7.805 0.05 . 1 . . . . 7 CYS H . 16104 1 34 . 1 1 7 7 CYS HA H 1 4.465 0.05 . 1 . . . . 7 CYS HA . 16104 1 35 . 1 1 7 7 CYS HB2 H 1 3.175 0.05 . 1 . . . . 7 CYS HB2 . 16104 1 36 . 1 1 7 7 CYS HB3 H 1 3.445 0.05 . 1 . . . . 7 CYS HB3 . 16104 1 37 . 1 1 7 7 CYS N N 15 120.81 0.3 . 1 . . . . 7 CYS N . 16104 1 38 . 1 1 8 8 ALA H H 1 8.085 0.05 . 1 . . . . 8 ALA H . 16104 1 39 . 1 1 8 8 ALA HA H 1 4.045 0.05 . 1 . . . . 8 ALA HA . 16104 1 40 . 1 1 8 8 ALA HB1 H 1 1.485 0.05 . 1 . . . . 8 ALA MB . 16104 1 41 . 1 1 8 8 ALA HB2 H 1 1.485 0.05 . 1 . . . . 8 ALA MB . 16104 1 42 . 1 1 8 8 ALA HB3 H 1 1.485 0.05 . 1 . . . . 8 ALA MB . 16104 1 43 . 1 1 8 8 ALA N N 15 123.57 0.3 . 1 . . . . 8 ALA N . 16104 1 44 . 1 1 9 9 THR H H 1 8.39 0.05 . 1 . . . . 9 THR H . 16104 1 45 . 1 1 9 9 THR HA H 1 3.893 0.05 . 1 . . . . 9 THR HA . 16104 1 46 . 1 1 9 9 THR HB H 1 4.206 0.05 . 1 . . . . 9 THR HB . 16104 1 47 . 1 1 9 9 THR HG21 H 1 1.335 0.05 . 1 . . . . 9 THR MG . 16104 1 48 . 1 1 9 9 THR HG22 H 1 1.335 0.05 . 1 . . . . 9 THR MG . 16104 1 49 . 1 1 9 9 THR HG23 H 1 1.335 0.05 . 1 . . . . 9 THR MG . 16104 1 50 . 1 1 9 9 THR N N 15 109.64 0.3 . 1 . . . . 9 THR N . 16104 1 51 . 1 1 10 10 GLN H H 1 7.715 0.05 . 1 . . . . 10 GLN H . 16104 1 52 . 1 1 10 10 GLN HA H 1 4.125 0.05 . 1 . . . . 10 GLN HA . 16104 1 53 . 1 1 10 10 GLN HB2 H 1 2.055 0.05 . 2 . . . . 10 GLN HB2 . 16104 1 54 . 1 1 10 10 GLN HB3 H 1 2.195 0.05 . 2 . . . . 10 GLN HB3 . 16104 1 55 . 1 1 10 10 GLN HE21 H 1 7.405 0.05 . 2 . . . . 10 GLN HE21 . 16104 1 56 . 1 1 10 10 GLN HE22 H 1 6.755 0.05 . 2 . . . . 10 GLN HE22 . 16104 1 57 . 1 1 10 10 GLN HG2 H 1 2.405 0.05 . 2 . . . . 10 GLN HG2 . 16104 1 58 . 1 1 10 10 GLN HG3 H 1 2.515 0.05 . 2 . . . . 10 GLN HG3 . 16104 1 59 . 1 1 10 10 GLN N N 15 120.96 0.3 . 1 . . . . 10 GLN N . 16104 1 60 . 1 1 10 10 GLN NE2 N 15 111.96 0.3 . 1 . . . . 10 GLN NE2 . 16104 1 61 . 1 1 11 11 ARG H H 1 7.918 0.05 . 1 . . . . 11 ARG H . 16104 1 62 . 1 1 11 11 ARG HA H 1 4.205 0.05 . 1 . . . . 11 ARG HA . 16104 1 63 . 1 1 11 11 ARG HB2 H 1 2.017 0.05 . 2 . . . . 11 ARG HB2 . 16104 1 64 . 1 1 11 11 ARG HB3 H 1 2.105 0.05 . 2 . . . . 11 ARG HB3 . 16104 1 65 . 1 1 11 11 ARG HD2 H 1 3.245 0.05 . 2 . . . . 11 ARG HD2 . 16104 1 66 . 1 1 11 11 ARG HE H 1 7.125 0.05 . 1 . . . . 11 ARG HE . 16104 1 67 . 1 1 11 11 ARG N N 15 119.55 0.3 . 1 . . . . 11 ARG N . 16104 1 68 . 1 1 11 11 ARG NE N 15 120.54 0.3 . 1 . . . . 11 ARG NE . 16104 1 69 . 1 1 12 12 LEU H H 1 8.145 0.05 . 1 . . . . 12 LEU H . 16104 1 70 . 1 1 12 12 LEU HA H 1 4.115 0.05 . 1 . . . . 12 LEU HA . 16104 1 71 . 1 1 12 12 LEU HB2 H 1 1.755 0.05 . 1 . . . . 12 LEU HB2 . 16104 1 72 . 1 1 12 12 LEU HB3 H 1 1.875 0.05 . 1 . . . . 12 LEU HB3 . 16104 1 73 . 1 1 12 12 LEU HD11 H 1 0.945 0.05 . 2 . . . . 12 LEU MD1 . 16104 1 74 . 1 1 12 12 LEU HD12 H 1 0.945 0.05 . 2 . . . . 12 LEU MD1 . 16104 1 75 . 1 1 12 12 LEU HD13 H 1 0.945 0.05 . 2 . . . . 12 LEU MD1 . 16104 1 76 . 1 1 12 12 LEU N N 15 119.97 0.3 . 1 . . . . 12 LEU N . 16104 1 77 . 1 1 13 13 ALA H H 1 8.435 0.05 . 1 . . . . 13 ALA H . 16104 1 78 . 1 1 13 13 ALA HA H 1 3.955 0.05 . 1 . . . . 13 ALA HA . 16104 1 79 . 1 1 13 13 ALA HB1 H 1 1.548 0.05 . 1 . . . . 13 ALA MB . 16104 1 80 . 1 1 13 13 ALA HB2 H 1 1.548 0.05 . 1 . . . . 13 ALA MB . 16104 1 81 . 1 1 13 13 ALA HB3 H 1 1.548 0.05 . 1 . . . . 13 ALA MB . 16104 1 82 . 1 1 13 13 ALA N N 15 120.96 0.3 . 1 . . . . 13 ALA N . 16104 1 83 . 1 1 14 14 ASN H H 1 8.095 0.05 . 1 . . . . 14 ASN H . 16104 1 84 . 1 1 14 14 ASN HA H 1 4.425 0.05 . 1 . . . . 14 ASN HA . 16104 1 85 . 1 1 14 14 ASN HB2 H 1 2.895 0.05 . 1 . . . . 14 ASN HB2 . 16104 1 86 . 1 1 14 14 ASN HB3 H 1 2.975 0.05 . 1 . . . . 14 ASN HB3 . 16104 1 87 . 1 1 14 14 ASN HD21 H 1 7.385 0.05 . 2 . . . . 14 ASN HD21 . 16104 1 88 . 1 1 14 14 ASN HD22 H 1 6.755 0.05 . 2 . . . . 14 ASN HD22 . 16104 1 89 . 1 1 14 14 ASN N N 15 114.80 0.3 . 1 . . . . 14 ASN N . 16104 1 90 . 1 1 14 14 ASN ND2 N 15 111.63 0.3 . 1 . . . . 14 ASN ND2 . 16104 1 91 . 1 1 15 15 PHE H H 1 8.095 0.05 . 1 . . . . 15 PHE H . 16104 1 92 . 1 1 15 15 PHE HA H 1 4.455 0.05 . 1 . . . . 15 PHE HA . 16104 1 93 . 1 1 15 15 PHE HB2 H 1 3.335 0.05 . 1 . . . . 15 PHE HB2 . 16104 1 94 . 1 1 15 15 PHE HB3 H 1 2.595 0.05 . 1 . . . . 15 PHE HB3 . 16104 1 95 . 1 1 15 15 PHE N N 15 120.67 0.3 . 1 . . . . 15 PHE N . 16104 1 96 . 1 1 16 16 LEU H H 1 8.385 0.05 . 1 . . . . 16 LEU H . 16104 1 97 . 1 1 16 16 LEU HA H 1 3.955 0.05 . 1 . . . . 16 LEU HA . 16104 1 98 . 1 1 16 16 LEU HB2 H 1 1.995 0.05 . 2 . . . . 16 LEU HB2 . 16104 1 99 . 1 1 16 16 LEU HD11 H 1 0.945 0.05 . 2 . . . . 16 LEU MD1 . 16104 1 100 . 1 1 16 16 LEU HD12 H 1 0.945 0.05 . 2 . . . . 16 LEU MD1 . 16104 1 101 . 1 1 16 16 LEU HD13 H 1 0.945 0.05 . 2 . . . . 16 LEU MD1 . 16104 1 102 . 1 1 16 16 LEU N N 15 119.62 0.3 . 1 . . . . 16 LEU N . 16104 1 103 . 1 1 17 17 VAL H H 1 8.058 0.05 . 1 . . . . 17 VAL H . 16104 1 104 . 1 1 17 17 VAL HA H 1 3.875 0.05 . 1 . . . . 17 VAL HA . 16104 1 105 . 1 1 17 17 VAL HB H 1 2.115 0.05 . 1 . . . . 17 VAL HB . 16104 1 106 . 1 1 17 17 VAL HG11 H 1 0.985 0.05 . 2 . . . . 17 VAL MG1 . 16104 1 107 . 1 1 17 17 VAL HG12 H 1 0.985 0.05 . 2 . . . . 17 VAL MG1 . 16104 1 108 . 1 1 17 17 VAL HG13 H 1 0.985 0.05 . 2 . . . . 17 VAL MG1 . 16104 1 109 . 1 1 17 17 VAL HG21 H 1 0.825 0.05 . 2 . . . . 17 VAL MG2 . 16104 1 110 . 1 1 17 17 VAL HG22 H 1 0.825 0.05 . 2 . . . . 17 VAL MG2 . 16104 1 111 . 1 1 17 17 VAL HG23 H 1 0.825 0.05 . 2 . . . . 17 VAL MG2 . 16104 1 112 . 1 1 17 17 VAL N N 15 116.51 0.3 . 1 . . . . 17 VAL N . 16104 1 113 . 1 1 18 18 HIS H H 1 7.777 0.05 . 1 . . . . 18 HIS H . 16104 1 114 . 1 1 18 18 HIS HA H 1 4.615 0.05 . 1 . . . . 18 HIS HA . 16104 1 115 . 1 1 18 18 HIS HB2 H 1 3.285 0.05 . 1 . . . . 18 HIS HB2 . 16104 1 116 . 1 1 18 18 HIS HB3 H 1 3.405 0.05 . 1 . . . . 18 HIS HB3 . 16104 1 117 . 1 1 18 18 HIS N N 15 116.79 0.3 . 1 . . . . 18 HIS N . 16104 1 118 . 1 1 19 19 SER H H 1 7.87 0.05 . 1 . . . . 19 SER H . 16104 1 119 . 1 1 19 19 SER HA H 1 4.345 0.05 . 1 . . . . 19 SER HA . 16104 1 120 . 1 1 19 19 SER HB2 H 1 3.685 0.05 . 2 . . . . 19 SER HB2 . 16104 1 121 . 1 1 19 19 SER N N 15 115.59 0.3 . 1 . . . . 19 SER N . 16104 1 122 . 1 1 20 20 SER H H 1 8.092 0.05 . 1 . . . . 20 SER H . 16104 1 123 . 1 1 20 20 SER HA H 1 4.225 0.05 . 1 . . . . 20 SER HA . 16104 1 124 . 1 1 20 20 SER HB2 H 1 3.893 0.05 . . . . . . 20 SER HB2 . 16104 1 125 . 1 1 20 20 SER N N 15 117.00 0.3 . 1 . . . . 20 SER N . 16104 1 126 . 1 1 21 21 ASN H H 1 8.123 0.05 . 1 . . . . 21 ASN H . 16104 1 127 . 1 1 21 21 ASN HA H 1 4.615 0.05 . 1 . . . . 21 ASN HA . 16104 1 128 . 1 1 21 21 ASN HB2 H 1 2.665 0.05 . 2 . . . . 21 ASN HB2 . 16104 1 129 . 1 1 21 21 ASN HD21 H 1 7.385 0.05 . 2 . . . . 21 ASN HD21 . 16104 1 130 . 1 1 21 21 ASN HD22 H 1 6.785 0.05 . 2 . . . . 21 ASN HD22 . 16104 1 131 . 1 1 21 21 ASN N N 15 119.55 0.3 . 1 . . . . 21 ASN N . 16104 1 132 . 1 1 21 21 ASN ND2 N 15 112.61 0.3 . 1 . . . . 21 ASN ND2 . 16104 1 133 . 1 1 22 22 ASN H H 1 8.177 0.05 . 1 . . . . 22 ASN H . 16104 1 134 . 1 1 22 22 ASN HA H 1 4.775 0.05 . 1 . . . . 22 ASN HA . 16104 1 135 . 1 1 22 22 ASN HB2 H 1 2.785 0.05 . 2 . . . . 22 ASN HB2 . 16104 1 136 . 1 1 22 22 ASN HB3 H 1 2.625 0.05 . 2 . . . . 22 ASN HB3 . 16104 1 137 . 1 1 22 22 ASN HD21 H 1 7.385 0.05 . 2 . . . . 22 ASN HD21 . 16104 1 138 . 1 1 22 22 ASN HD22 H 1 6.785 0.05 . 2 . . . . 22 ASN HD22 . 16104 1 139 . 1 1 22 22 ASN N N 15 117.85 0.3 . 1 . . . . 22 ASN N . 16104 1 140 . 1 1 22 22 ASN ND2 N 15 112.61 0.3 . 1 . . . . 22 ASN ND2 . 16104 1 141 . 1 1 23 23 PHE H H 1 8.16 0.05 . 1 . . . . 23 PHE H . 16104 1 142 . 1 1 23 23 PHE HA H 1 4.465 0.05 . 1 . . . . 23 PHE HA . 16104 1 143 . 1 1 23 23 PHE HB2 H 1 3.135 0.05 . 2 . . . . 23 PHE HB2 . 16104 1 144 . 1 1 23 23 PHE HD1 H 1 7.245 0.05 . 4 . . . . 23 PHE HD1 . 16104 1 145 . 1 1 23 23 PHE HD2 H 1 7.555 0.05 . 4 . . . . 23 PHE HD2 . 16104 1 146 . 1 1 23 23 PHE N N 15 119.97 0.3 . 1 . . . . 23 PHE N . 16104 1 147 . 1 1 24 24 GLY H H 1 8.459 0.05 . 1 . . . . 24 GLY H . 16104 1 148 . 1 1 24 24 GLY HA2 H 1 3.725 0.05 . 1 . . . . 24 GLY HA2 . 16104 1 149 . 1 1 24 24 GLY HA3 H 1 4.035 0.05 . 1 . . . . 24 GLY HA3 . 16104 1 150 . 1 1 24 24 GLY N N 15 107.81 0.3 . 1 . . . . 24 GLY N . 16104 1 151 . 1 1 25 25 ALA H H 1 7.894 0.05 . 1 . . . . 25 ALA H . 16104 1 152 . 1 1 25 25 ALA HA H 1 4.225 0.05 . 1 . . . . 25 ALA HA . 16104 1 153 . 1 1 25 25 ALA HB1 H 1 1.455 0.05 . 1 . . . . 25 ALA MB . 16104 1 154 . 1 1 25 25 ALA HB2 H 1 1.455 0.05 . 1 . . . . 25 ALA MB . 16104 1 155 . 1 1 25 25 ALA HB3 H 1 1.455 0.05 . 1 . . . . 25 ALA MB . 16104 1 156 . 1 1 25 25 ALA N N 15 123.71 0.3 . 1 . . . . 25 ALA N . 16104 1 157 . 1 1 26 26 ILE H H 1 7.845 0.05 . 1 . . . . 26 ILE H . 16104 1 158 . 1 1 26 26 ILE HA H 1 3.915 0.05 . 1 . . . . 26 ILE HA . 16104 1 159 . 1 1 26 26 ILE HB H 1 1.995 0.05 . 1 . . . . 26 ILE HB . 16104 1 160 . 1 1 26 26 ILE HG12 H 1 1.455 0.05 . 2 . . . . 26 ILE HG12 . 16104 1 161 . 1 1 26 26 ILE HG13 H 1 1.255 0.05 . 2 . . . . 26 ILE HG13 . 16104 1 162 . 1 1 26 26 ILE HG21 H 1 0.905 0.05 . 1 . . . . 26 ILE MG . 16104 1 163 . 1 1 26 26 ILE HG22 H 1 0.905 0.05 . 1 . . . . 26 ILE MG . 16104 1 164 . 1 1 26 26 ILE HG23 H 1 0.905 0.05 . 1 . . . . 26 ILE MG . 16104 1 165 . 1 1 26 26 ILE N N 15 118.76 0.3 . 1 . . . . 26 ILE N . 16104 1 166 . 1 1 27 27 LEU H H 1 7.975 0.05 . 1 . . . . 27 LEU H . 16104 1 167 . 1 1 27 27 LEU HA H 1 4.145 0.05 . 1 . . . . 27 LEU HA . 16104 1 168 . 1 1 27 27 LEU HB2 H 1 1.725 0.05 . 1 . . . . 27 LEU HB2 . 16104 1 169 . 1 1 27 27 LEU HB3 H 1 1.625 0.05 . 1 . . . . 27 LEU HB3 . 16104 1 170 . 1 1 27 27 LEU HD11 H 1 0.885 0.05 . 2 . . . . 27 LEU MD1 . 16104 1 171 . 1 1 27 27 LEU HD12 H 1 0.885 0.05 . 2 . . . . 27 LEU MD1 . 16104 1 172 . 1 1 27 27 LEU HD13 H 1 0.885 0.05 . 2 . . . . 27 LEU MD1 . 16104 1 173 . 1 1 27 27 LEU N N 15 119.61 0.3 . 1 . . . . 27 LEU N . 16104 1 174 . 1 1 28 28 SER H H 1 8.004 0.05 . 1 . . . . 28 SER H . 16104 1 175 . 1 1 28 28 SER HA H 1 4.386 0.05 . 1 . . . . 28 SER HA . 16104 1 176 . 1 1 28 28 SER HB2 H 1 3.995 0.05 . 2 . . . . 28 SER HB2 . 16104 1 177 . 1 1 28 28 SER HB3 H 1 3.935 0.05 . 2 . . . . 28 SER HB3 . 16104 1 178 . 1 1 28 28 SER N N 15 113.32 0.3 . 1 . . . . 28 SER N . 16104 1 179 . 1 1 29 29 SER H H 1 7.85 0.05 . 1 . . . . 29 SER H . 16104 1 180 . 1 1 29 29 SER HA H 1 4.58 0.05 . 1 . . . . 29 SER HA . 16104 1 181 . 1 1 29 29 SER HB2 H 1 4.035 0.05 . 2 . . . . 29 SER HB2 . 16104 1 182 . 1 1 29 29 SER HB3 H 1 4.305 0.05 . 2 . . . . 29 SER HB3 . 16104 1 183 . 1 1 29 29 SER N N 15 116.36 0.3 . 1 . . . . 29 SER N . 16104 1 184 . 1 1 30 30 THR H H 1 7.704 0.05 . 1 . . . . 30 THR H . 16104 1 185 . 1 1 30 30 THR HA H 1 4.505 0.05 . 1 . . . . 30 THR HA . 16104 1 186 . 1 1 30 30 THR HB H 1 4.345 0.05 . 1 . . . . 30 THR HB . 16104 1 187 . 1 1 30 30 THR HG21 H 1 1.255 0.05 . 1 . . . . 30 THR MG . 16104 1 188 . 1 1 30 30 THR HG22 H 1 1.255 0.05 . 1 . . . . 30 THR MG . 16104 1 189 . 1 1 30 30 THR HG23 H 1 1.255 0.05 . 1 . . . . 30 THR MG . 16104 1 190 . 1 1 30 30 THR N N 15 113.67 0.3 . 1 . . . . 30 THR N . 16104 1 191 . 1 1 31 31 ASN H H 1 8.385 0.05 . 1 . . . . 31 ASN H . 16104 1 192 . 1 1 31 31 ASN HA H 1 4.835 0.05 . 1 . . . . 31 ASN HA . 16104 1 193 . 1 1 31 31 ASN HB2 H 1 2.925 0.05 . 2 . . . . 31 ASN HB2 . 16104 1 194 . 1 1 31 31 ASN HB3 H 1 2.795 0.05 . 2 . . . . 31 ASN HB3 . 16104 1 195 . 1 1 31 31 ASN HD21 H 1 7.515 0.05 . 2 . . . . 31 ASN HD21 . 16104 1 196 . 1 1 31 31 ASN HD22 H 1 6.825 0.05 . 2 . . . . 31 ASN HD22 . 16104 1 197 . 1 1 31 31 ASN N N 15 119.68 0.3 . 1 . . . . 31 ASN N . 16104 1 198 . 1 1 31 31 ASN ND2 N 15 113.04 0.3 . 1 . . . . 31 ASN ND2 . 16104 1 199 . 1 1 32 32 VAL H H 1 7.965 0.05 . 1 . . . . 32 VAL H . 16104 1 200 . 1 1 32 32 VAL HA H 1 4.035 0.05 . 1 . . . . 32 VAL HA . 16104 1 201 . 1 1 32 32 VAL HB H 1 1.705 0.05 . 1 . . . . 32 VAL HB . 16104 1 202 . 1 1 32 32 VAL HG11 H 1 0.985 0.05 . 2 . . . . 32 VAL MG1 . 16104 1 203 . 1 1 32 32 VAL HG12 H 1 0.985 0.05 . 2 . . . . 32 VAL MG1 . 16104 1 204 . 1 1 32 32 VAL HG13 H 1 0.985 0.05 . 2 . . . . 32 VAL MG1 . 16104 1 205 . 1 1 32 32 VAL N N 15 119.62 0.3 . 1 . . . . 32 VAL N . 16104 1 206 . 1 1 33 33 GLY H H 1 8.346 0.05 . 1 . . . . 33 GLY H . 16104 1 207 . 1 1 33 33 GLY HA2 H 1 4.075 0.05 . 2 . . . . 33 GLY HA2 . 16104 1 208 . 1 1 33 33 GLY HA3 H 1 3.955 0.05 . 2 . . . . 33 GLY HA3 . 16104 1 209 . 1 1 33 33 GLY N N 15 111.06 0.3 . 1 . . . . 33 GLY N . 16104 1 210 . 1 1 34 34 SER H H 1 8.014 0.05 . 1 . . . . 34 SER H . 16104 1 211 . 1 1 34 34 SER HA H 1 4.425 0.05 . 1 . . . . 34 SER HA . 16104 1 212 . 1 1 34 34 SER HB2 H 1 3.905 0.05 . 2 . . . . 34 SER HB2 . 16104 1 213 . 1 1 34 34 SER N N 15 114.95 0.3 . 1 . . . . 34 SER N . 16104 1 214 . 1 1 35 35 ASN H H 1 8.231 0.05 . 1 . . . . 35 ASN H . 16104 1 215 . 1 1 35 35 ASN HA H 1 4.775 0.05 . 1 . . . . 35 ASN HA . 16104 1 216 . 1 1 35 35 ASN HB2 H 1 2.786 0.05 . 2 . . . . 35 ASN HB2 . 16104 1 217 . 1 1 35 35 ASN HD21 H 1 7.445 0.05 . 2 . . . . 35 ASN HD21 . 16104 1 218 . 1 1 35 35 ASN HD22 H 1 6.825 0.05 . 2 . . . . 35 ASN HD22 . 16104 1 219 . 1 1 35 35 ASN N N 15 119.90 0.3 . 1 . . . . 35 ASN N . 16104 1 220 . 1 1 35 35 ASN ND2 N 15 112.61 0.3 . 1 . . . . 35 ASN ND2 . 16104 1 221 . 1 1 36 36 THR H H 1 7.924 0.05 . 1 . . . . 36 THR H . 16104 1 222 . 1 1 36 36 THR HA H 1 4.265 0.05 . 1 . . . . 36 THR HA . 16104 1 223 . 1 1 36 36 THR HB H 1 4.075 0.05 . 1 . . . . 36 THR HB . 16104 1 224 . 1 1 36 36 THR HG21 H 1 1.095 0.05 . 1 . . . . 36 THR MG . 16104 1 225 . 1 1 36 36 THR HG22 H 1 1.095 0.05 . 1 . . . . 36 THR MG . 16104 1 226 . 1 1 36 36 THR HG23 H 1 1.095 0.05 . 1 . . . . 36 THR MG . 16104 1 227 . 1 1 36 36 THR N N 15 113.89 0.3 . 1 . . . . 36 THR N . 16104 1 228 . 1 1 37 37 TYR H H 1 7.905 0.05 . 1 . . . . 37 TYR H . 16104 1 229 . 1 1 37 37 TYR HA H 1 4.585 0.05 . 1 . . . . 37 TYR HA . 16104 1 230 . 1 1 37 37 TYR HB2 H 1 2.895 0.05 . 1 . . . . 37 TYR HB2 . 16104 1 231 . 1 1 37 37 TYR HB3 H 1 3.135 0.05 . 1 . . . . 37 TYR HB3 . 16104 1 232 . 1 1 37 37 TYR HD1 H 1 7.085 0.05 . 1 . . . . 37 TYR HD1 . 16104 1 233 . 1 1 37 37 TYR HD2 H 1 7.085 0.05 . 1 . . . . 37 TYR HD2 . 16104 1 234 . 1 1 37 37 TYR HE1 H 1 6.805 0.05 . 1 . . . . 37 TYR HE1 . 16104 1 235 . 1 1 37 37 TYR HE2 H 1 6.805 0.05 . 1 . . . . 37 TYR HE2 . 16104 1 236 . 1 1 37 37 TYR N N 15 123.15 0.3 . 1 . . . . 37 TYR N . 16104 1 stop_ save_