data_18795 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18795 _Entry.Title ; NMR assignments of Amylin in DMSO ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-10-20 _Entry.Accession_date 2012-10-20 _Entry.Last_release_date 2013-04-02 _Entry.Original_release_date 2013-04-02 _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 _Entry.Details 'NMR assignments of Amylin in 95% DMSO / 5% Dichloroacetic acid for quenched hydrogen exchange studies of amylin fibrils.' _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 Andrei Alexandrescu . . . 18795 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18795 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 35 18795 '1H chemical shifts' 136 18795 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2013-04-02 2012-10-20 original author . 18795 stop_ save_ ############### # Citations # ############### save_NMR_assignments_of_amylin_in_DMSO _Citation.Sf_category citations _Citation.Sf_framecode NMR_assignments_of_amylin_in_DMSO _Citation.Entry_ID 18795 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23457571 _Citation.Full_citation . _Citation.Title 'Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'PLOS One' _Citation.Journal_name_full . _Citation.Journal_volume 8 _Citation.Journal_issue 2 _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 e56467 _Citation.Page_last e56467 _Citation.Year 2013 _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 Andrei Alexandrescu . T. . 18795 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'amyloidogenic proteins' 18795 1 IAPP 18795 1 'islet amyloid polypeptide' 18795 1 'protein dynamics' 18795 1 'type 2 diabetes' 18795 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18795 _Assembly.ID 1 _Assembly.Name 'Amylin monomer' _Assembly.BMRB_code . _Assembly.Number_of_components . _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 Amylin 1 $Amylin A . yes denatured no no . . . 18795 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 2 2 SG . 1 . 1 CYS 7 7 SG . . . . . . . . . . 18795 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Amylin _Entity.Sf_category entity _Entity.Sf_framecode Amylin _Entity.Entry_ID 18795 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Amylin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _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 ; The naturally occurring human amylin hormone has an amidated C-terminus. This is an enzymatic post-translational modification. The sample used for NMR was recombinantely expressed in E. coli and has a free alpha-caroxylic acid at the C-terminus. ; _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 . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 16104 . alpha-helix . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 18795 1 2 no BMRB 16105 . alpha-helix . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 18795 1 3 no BMRB 17394 . entity . . . . . 100.00 37 100.00 100.00 6.37e-16 . . . . 18795 1 4 no BMRB 20045 . IAPP . . . . . 51.35 19 100.00 100.00 2.51e-03 . . . . 18795 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 . . . . 18795 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 . . . . 18795 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 . . . . 18795 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 . . . . 18795 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 . . . . 18795 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 . . . . 18795 1 11 no DBJ BAG73319 . "islet amyloid polypeptide [synthetic construct]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 12 no EMBL CAA33032 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 13 no EMBL CAA37002 . "islet amyloid polypeptide [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 14 no EMBL CAA39504 . "IAPP [Homo sapiens]" . . . . . 100.00 89 97.30 97.30 2.31e-15 . . . . 18795 1 15 no EMBL CAA48724 . "islet amyloid polypeptide (IAAP) [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 16 no EMBL CAB57803 . "prepro-IAPP [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 18795 1 17 no GB AAA35524 . "amylin, partial [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 18795 1 18 no GB AAA35983 . "islet amyloid polypeptide (hIAPP), partial [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 19 no GB AAA51728 . "amyloid protein, partial [Homo sapiens]" . . . . . 100.00 62 100.00 100.00 3.01e-16 . . . . 18795 1 20 no GB AAA52281 . "islet amyloid polypeptide [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 21 no GB AAI11850 . "IAPP protein, partial [synthetic construct]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 22 no REF NP_000406 . "islet amyloid polypeptide precursor [Homo sapiens]" . . . . . 100.00 89 100.00 100.00 2.29e-16 . . . . 18795 1 23 no REF XP_001144800 . "PREDICTED: islet amyloid polypeptide [Pan troglodytes]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 18795 1 24 no REF XP_003265632 . "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 18795 1 25 no REF XP_003265633 . "PREDICTED: islet amyloid polypeptide [Nomascus leucogenys]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 18795 1 26 no REF XP_003828947 . "PREDICTED: islet amyloid polypeptide [Pan paniscus]" . . . . . 100.00 89 97.30 97.30 4.16e-15 . . . . 18795 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 . . . . 18795 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 . 18795 1 2 . CYS . 18795 1 3 . ASN . 18795 1 4 . THR . 18795 1 5 . ALA . 18795 1 6 . THR . 18795 1 7 . CYS . 18795 1 8 . ALA . 18795 1 9 . THR . 18795 1 10 . GLN . 18795 1 11 . ARG . 18795 1 12 . LEU . 18795 1 13 . ALA . 18795 1 14 . ASN . 18795 1 15 . PHE . 18795 1 16 . LEU . 18795 1 17 . VAL . 18795 1 18 . HIS . 18795 1 19 . SER . 18795 1 20 . SER . 18795 1 21 . ASN . 18795 1 22 . ASN . 18795 1 23 . PHE . 18795 1 24 . GLY . 18795 1 25 . ALA . 18795 1 26 . ILE . 18795 1 27 . LEU . 18795 1 28 . SER . 18795 1 29 . SER . 18795 1 30 . THR . 18795 1 31 . ASN . 18795 1 32 . VAL . 18795 1 33 . GLY . 18795 1 34 . SER . 18795 1 35 . ASN . 18795 1 36 . THR . 18795 1 37 . TYR . 18795 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 18795 1 . CYS 2 2 18795 1 . ASN 3 3 18795 1 . THR 4 4 18795 1 . ALA 5 5 18795 1 . THR 6 6 18795 1 . CYS 7 7 18795 1 . ALA 8 8 18795 1 . THR 9 9 18795 1 . GLN 10 10 18795 1 . ARG 11 11 18795 1 . LEU 12 12 18795 1 . ALA 13 13 18795 1 . ASN 14 14 18795 1 . PHE 15 15 18795 1 . LEU 16 16 18795 1 . VAL 17 17 18795 1 . HIS 18 18 18795 1 . SER 19 19 18795 1 . SER 20 20 18795 1 . ASN 21 21 18795 1 . ASN 22 22 18795 1 . PHE 23 23 18795 1 . GLY 24 24 18795 1 . ALA 25 25 18795 1 . ILE 26 26 18795 1 . LEU 27 27 18795 1 . SER 28 28 18795 1 . SER 29 29 18795 1 . THR 30 30 18795 1 . ASN 31 31 18795 1 . VAL 32 32 18795 1 . GLY 33 33 18795 1 . SER 34 34 18795 1 . ASN 35 35 18795 1 . THR 36 36 18795 1 . TYR 37 37 18795 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 18795 _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 $Amylin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18795 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 18795 _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 $Amylin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . 'Purchased from rPeptide - proprietary vector' . . . . . . 18795 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18795 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '95% DMSO, 5% DCA, apparent pH 3.5' _Sample.Aggregate_sample_number . _Sample.Solvent_system DMSO _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 Amylin '[U-99% 15N]' . . 1 $Amylin . . 0.5 . . mM . . . . 18795 1 2 DMSO-d6 [U-2H] . . . . . . 95 . . % . . . . 18795 1 3 DCA-d2 [U-2H] . . . . . . 5 . . % . . . . 18795 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18795 _Sample_condition_list.ID 1 _Sample_condition_list.Details 'no added salts' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0 . mM 18795 1 pH* 3.5 . pH 18795 1 pressure 1 . atm 18795 1 temperature 273 . K 18795 1 stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18795 _Software.ID 1 _Software.Name VNMRJ _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Varian-Agilent Technologies' . . 18795 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18795 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 18795 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'With Cryogenic Probe' _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 18795 _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 'With Cryogenic Probe' . . 18795 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 18795 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18795 1 2 '3D 1H-15N NOESY' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18795 1 3 '3D 1H-15N TOCSY' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18795 1 stop_ save_ save_NMR_spectrometer_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spectrometer_expt _NMR_spec_expt.Entry_ID 18795 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $VNMRJ _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . 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 18795 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18795 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18795 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 18795 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18795 1 2 '3D 1H-15N NOESY' . . . 18795 1 3 '3D 1H-15N TOCSY' . . . 18795 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LYS HA H 1 3.86 0.08 . 1 . . . . 1 LYS HA . 18795 1 2 . 1 1 1 1 LYS HB2 H 1 1.83 0.08 . 2 . . . . 1 LYS HB2 . 18795 1 3 . 1 1 2 2 CYS H H 1 9.034 0.001 . 1 . . . . 2 CYS H . 18795 1 4 . 1 1 2 2 CYS HA H 1 4.80 0.08 . 1 . . . . 2 CYS HA . 18795 1 5 . 1 1 2 2 CYS HB2 H 1 3.08 0.08 . 2 . . . . 2 CYS HB2 . 18795 1 6 . 1 1 2 2 CYS HB3 H 1 3.24 0.08 . 2 . . . . 2 CYS HB3 . 18795 1 7 . 1 1 2 2 CYS N N 15 119.38 0.14 . 1 . . . . 2 CYS N . 18795 1 8 . 1 1 3 3 ASN H H 1 8.801 0.001 . 1 . . . . 3 ASN H . 18795 1 9 . 1 1 3 3 ASN HA H 1 4.64 0.08 . 1 . . . . 3 ASN HA . 18795 1 10 . 1 1 3 3 ASN HB2 H 1 2.92 0.08 . 2 . . . . 3 ASN HB2 . 18795 1 11 . 1 1 3 3 ASN N N 15 118.81 0.14 . 1 . . . . 3 ASN N . 18795 1 12 . 1 1 4 4 THR H H 1 7.698 0.001 . 1 . . . . 4 THR H . 18795 1 13 . 1 1 4 4 THR HA H 1 4.49 0.08 . 1 . . . . 4 THR HA . 18795 1 14 . 1 1 4 4 THR N N 15 111.18 0.14 . 1 . . . . 4 THR N . 18795 1 15 . 1 1 5 5 ALA H H 1 8.752 0.001 . 1 . . . . 5 ALA H . 18795 1 16 . 1 1 5 5 ALA HA H 1 4.17 0.08 . 1 . . . . 5 ALA HA . 18795 1 17 . 1 1 5 5 ALA HB1 H 1 1.36 0.08 . 1 . . . . 5 ALA MB . 18795 1 18 . 1 1 5 5 ALA HB2 H 1 1.36 0.08 . 1 . . . . 5 ALA MB . 18795 1 19 . 1 1 5 5 ALA HB3 H 1 1.36 0.08 . 1 . . . . 5 ALA MB . 18795 1 20 . 1 1 5 5 ALA N N 15 120.96 0.14 . 1 . . . . 5 ALA N . 18795 1 21 . 1 1 7 7 CYS H H 1 7.910 0.001 . 1 . . . . 7 CYS H . 18795 1 22 . 1 1 7 7 CYS HB2 H 1 2.92 0.08 . 2 . . . . 7 CYS HB2 . 18795 1 23 . 1 1 7 7 CYS N N 15 119.69 0.14 . 1 . . . . 7 CYS N . 18795 1 24 . 1 1 8 8 ALA H H 1 7.586 0.001 . 1 . . . . 8 ALA H . 18795 1 25 . 1 1 8 8 ALA HA H 1 4.32 0.08 . 1 . . . . 8 ALA HA . 18795 1 26 . 1 1 8 8 ALA HB1 H 1 1.29 0.08 . 1 . . . . 8 ALA MB . 18795 1 27 . 1 1 8 8 ALA HB2 H 1 1.29 0.08 . 1 . . . . 8 ALA MB . 18795 1 28 . 1 1 8 8 ALA HB3 H 1 1.29 0.08 . 1 . . . . 8 ALA MB . 18795 1 29 . 1 1 8 8 ALA N N 15 120.76 0.14 . 1 . . . . 8 ALA N . 18795 1 30 . 1 1 9 9 THR H H 1 8.194 0.001 . 1 . . . . 9 THR H . 18795 1 31 . 1 1 9 9 THR HA H 1 4.33 0.08 . 1 . . . . 9 THR HA . 18795 1 32 . 1 1 9 9 THR HG21 H 1 1.32 0.08 . 1 . . . . 9 THR MG . 18795 1 33 . 1 1 9 9 THR HG22 H 1 1.32 0.08 . 1 . . . . 9 THR MG . 18795 1 34 . 1 1 9 9 THR HG23 H 1 1.32 0.08 . 1 . . . . 9 THR MG . 18795 1 35 . 1 1 9 9 THR N N 15 111.60 0.14 . 1 . . . . 9 THR N . 18795 1 36 . 1 1 10 10 GLN H H 1 8.009 0.001 . 1 . . . . 10 GLN H . 18795 1 37 . 1 1 10 10 GLN HA H 1 4.33 0.08 . 1 . . . . 10 GLN HA . 18795 1 38 . 1 1 10 10 GLN HB2 H 1 1.99 0.08 . 2 . . . . 10 GLN HB2 . 18795 1 39 . 1 1 10 10 GLN HG3 H 1 2.30 0.08 . 2 . . . . 10 GLN HG3 . 18795 1 40 . 1 1 10 10 GLN N N 15 118.79 0.14 . 1 . . . . 10 GLN N . 18795 1 41 . 1 1 11 11 ARG H H 1 8.226 0.001 . 1 . . . . 11 ARG H . 18795 1 42 . 1 1 11 11 ARG HA H 1 4.33 0.08 . 1 . . . . 11 ARG HA . 18795 1 43 . 1 1 11 11 ARG HB2 H 1 1.67 0.08 . 4 . . . . 11 ARG HB2 . 18795 1 44 . 1 1 11 11 ARG N N 15 118.59 0.14 . 1 . . . . 11 ARG N . 18795 1 45 . 1 1 12 12 LEU H H 1 8.040 0.001 . 1 . . . . 12 LEU H . 18795 1 46 . 1 1 12 12 LEU HA H 1 4.33 0.08 . 1 . . . . 12 LEU HA . 18795 1 47 . 1 1 12 12 LEU HB2 H 1 1.67 0.08 . 2 . . . . 12 LEU HB2 . 18795 1 48 . 1 1 12 12 LEU N N 15 119.12 0.14 . 1 . . . . 12 LEU N . 18795 1 49 . 1 1 13 13 ALA H H 1 8.091 0.001 . 1 . . . . 13 ALA H . 18795 1 50 . 1 1 13 13 ALA HA H 1 4.33 0.08 . 1 . . . . 13 ALA HA . 18795 1 51 . 1 1 13 13 ALA HB1 H 1 1.20 0.08 . 1 . . . . 13 ALA MB . 18795 1 52 . 1 1 13 13 ALA HB2 H 1 1.20 0.08 . 1 . . . . 13 ALA MB . 18795 1 53 . 1 1 13 13 ALA HB3 H 1 1.20 0.08 . 1 . . . . 13 ALA MB . 18795 1 54 . 1 1 13 13 ALA N N 15 120.10 0.14 . 1 . . . . 13 ALA N . 18795 1 55 . 1 1 14 14 ASN H H 1 8.149 0.001 . 1 . . . . 14 ASN H . 18795 1 56 . 1 1 14 14 ASN HA H 1 4.64 0.08 . 1 . . . . 14 ASN HA . 18795 1 57 . 1 1 14 14 ASN HB2 H 1 2.61 0.08 . 2 . . . . 14 ASN HB2 . 18795 1 58 . 1 1 14 14 ASN N N 15 115.62 0.14 . 1 . . . . 14 ASN N . 18795 1 59 . 1 1 15 15 PHE H H 1 8.094 0.001 . 1 . . . . 15 PHE H . 18795 1 60 . 1 1 15 15 PHE HA H 1 4.49 0.08 . 1 . . . . 15 PHE HA . 18795 1 61 . 1 1 15 15 PHE HB2 H 1 3.24 0.08 . 2 . . . . 15 PHE HB2 . 18795 1 62 . 1 1 15 15 PHE HB3 H 1 2.92 0.08 . 2 . . . . 15 PHE HB3 . 18795 1 63 . 1 1 15 15 PHE N N 15 116.34 0.14 . 1 . . . . 15 PHE N . 18795 1 64 . 1 1 16 16 LEU H H 1 8.215 0.001 . 1 . . . . 16 LEU H . 18795 1 65 . 1 1 16 16 LEU HA H 1 4.33 0.08 . 1 . . . . 16 LEU HA . 18795 1 66 . 1 1 16 16 LEU HB2 H 1 1.67 0.08 . 2 . . . . 16 LEU HB2 . 18795 1 67 . 1 1 16 16 LEU HD11 H 1 0.88 0.08 . 2 . . . . 16 LEU MD1 . 18795 1 68 . 1 1 16 16 LEU HD12 H 1 0.88 0.08 . 2 . . . . 16 LEU MD1 . 18795 1 69 . 1 1 16 16 LEU HD13 H 1 0.88 0.08 . 2 . . . . 16 LEU MD1 . 18795 1 70 . 1 1 16 16 LEU N N 15 117.86 0.14 . 1 . . . . 16 LEU N . 18795 1 71 . 1 1 17 17 VAL H H 1 7.78 0.001 . 1 . . . . 17 VAL H . 18795 1 72 . 1 1 17 17 VAL HA H 1 4.17 0.08 . 1 . . . . 17 VAL HA . 18795 1 73 . 1 1 17 17 VAL HB H 1 2.14 0.08 . 1 . . . . 17 VAL HB . 18795 1 74 . 1 1 17 17 VAL HG11 H 1 0.89 0.08 . 2 . . . . 17 VAL MG1 . 18795 1 75 . 1 1 17 17 VAL HG12 H 1 0.89 0.08 . 2 . . . . 17 VAL MG1 . 18795 1 76 . 1 1 17 17 VAL HG13 H 1 0.89 0.08 . 2 . . . . 17 VAL MG1 . 18795 1 77 . 1 1 17 17 VAL N N 15 114.77 0.14 . 1 . . . . 17 VAL N . 18795 1 78 . 1 1 18 18 HIS H H 1 8.326 0.001 . 1 . . . . 18 HIS H . 18795 1 79 . 1 1 18 18 HIS HA H 1 4.80 0.08 . 1 . . . . 18 HIS HA . 18795 1 80 . 1 1 18 18 HIS HB2 H 1 3.08 0.08 . 2 . . . . 18 HIS HB2 . 18795 1 81 . 1 1 18 18 HIS HB3 H 1 3.24 0.08 . 2 . . . . 18 HIS HB3 . 18795 1 82 . 1 1 18 18 HIS N N 15 118.74 0.14 . 1 . . . . 18 HIS N . 18795 1 83 . 1 1 19 19 SER H H 1 8.191 0.001 . 1 . . . . 19 SER H . 18795 1 84 . 1 1 19 19 SER HA H 1 4.49 0.08 . 1 . . . . 19 SER HA . 18795 1 85 . 1 1 19 19 SER HB2 H 1 3.70 0.08 . 2 . . . . 19 SER HB2 . 18795 1 86 . 1 1 19 19 SER N N 15 114.83 0.14 . 1 . . . . 19 SER N . 18795 1 87 . 1 1 20 20 SER H H 1 8.111 0.001 . 1 . . . . 20 SER H . 18795 1 88 . 1 1 20 20 SER HA H 1 4.49 0.08 . 1 . . . . 20 SER HA . 18795 1 89 . 1 1 20 20 SER HB2 H 1 3.71 0.08 . 2 . . . . 20 SER HB2 . 18795 1 90 . 1 1 20 20 SER N N 15 114.83 0.14 . 1 . . . . 20 SER N . 18795 1 91 . 1 1 21 21 ASN H H 1 8.264 0.001 . 1 . . . . 21 ASN H . 18795 1 92 . 1 1 21 21 ASN HA H 1 4.64 0.08 . 1 . . . . 21 ASN HA . 18795 1 93 . 1 1 21 21 ASN HB2 H 1 2.61 0.08 . 2 . . . . 21 ASN HB2 . 18795 1 94 . 1 1 21 21 ASN N N 15 117.98 0.14 . 1 . . . . 21 ASN N . 18795 1 95 . 1 1 22 22 ASN H H 1 8.205 0.001 . 1 . . . . 22 ASN H . 18795 1 96 . 1 1 22 22 ASN HA H 1 4.64 0.08 . 1 . . . . 22 ASN HA . 18795 1 97 . 1 1 22 22 ASN HB2 H 1 2.61 0.08 . 2 . . . . 22 ASN HB2 . 18795 1 98 . 1 1 22 22 ASN N N 15 116.73 0.14 . 1 . . . . 22 ASN N . 18795 1 99 . 1 1 23 23 PHE H H 1 8.241 0.001 . 1 . . . . 23 PHE H . 18795 1 100 . 1 1 23 23 PHE HA H 1 4.49 0.08 . 1 . . . . 23 PHE HA . 18795 1 101 . 1 1 23 23 PHE HB2 H 1 3.08 0.08 . 2 . . . . 23 PHE HB2 . 18795 1 102 . 1 1 23 23 PHE N N 15 116.68 0.14 . 1 . . . . 23 PHE N . 18795 1 103 . 1 1 24 24 GLY H H 1 8.292 0.001 . 1 . . . . 24 GLY H . 18795 1 104 . 1 1 24 24 GLY HA2 H 1 3.82 0.08 . 2 . . . . 24 GLY HA2 . 18795 1 105 . 1 1 24 24 GLY N N 15 105.43 0.14 . 1 . . . . 24 GLY N . 18795 1 106 . 1 1 25 25 ALA H H 1 7.961 0.001 . 1 . . . . 25 ALA H . 18795 1 107 . 1 1 25 25 ALA HA H 1 4.49 0.08 . 1 . . . . 25 ALA HA . 18795 1 108 . 1 1 25 25 ALA HB1 H 1 1.36 0.08 . 1 . . . . 25 ALA MB . 18795 1 109 . 1 1 25 25 ALA HB2 H 1 1.36 0.08 . 1 . . . . 25 ALA MB . 18795 1 110 . 1 1 25 25 ALA HB3 H 1 1.36 0.08 . 1 . . . . 25 ALA MB . 18795 1 111 . 1 1 25 25 ALA N N 15 119.83 0.14 . 1 . . . . 25 ALA N . 18795 1 112 . 1 1 26 26 ILE H H 1 8.043 0.001 . 1 . . . . 26 ILE H . 18795 1 113 . 1 1 26 26 ILE HA H 1 4.17 0.08 . 1 . . . . 26 ILE HA . 18795 1 114 . 1 1 26 26 ILE HB H 1 1.83 0.08 . 1 . . . . 26 ILE HB . 18795 1 115 . 1 1 26 26 ILE HG21 H 1 0.90 0.08 . 1 . . . . 26 ILE MG . 18795 1 116 . 1 1 26 26 ILE HG22 H 1 0.90 0.08 . 1 . . . . 26 ILE MG . 18795 1 117 . 1 1 26 26 ILE HG23 H 1 0.90 0.08 . 1 . . . . 26 ILE MG . 18795 1 118 . 1 1 26 26 ILE N N 15 115.87 0.14 . 1 . . . . 26 ILE N . 18795 1 119 . 1 1 27 27 LEU H H 1 8.052 0.001 . 1 . . . . 27 LEU H . 18795 1 120 . 1 1 27 27 LEU HA H 1 4.49 0.08 . 1 . . . . 27 LEU HA . 18795 1 121 . 1 1 27 27 LEU HB2 H 1 1.52 0.08 . 2 . . . . 27 LEU HB2 . 18795 1 122 . 1 1 27 27 LEU N N 15 121.48 0.14 . 1 . . . . 27 LEU N . 18795 1 123 . 1 1 28 28 SER H H 1 8.005 0.001 . 1 . . . . 28 SER H . 18795 1 124 . 1 1 28 28 SER HA H 1 4.49 0.08 . 1 . . . . 28 SER HA . 18795 1 125 . 1 1 28 28 SER HB2 H 1 3.71 0.08 . 2 . . . . 28 SER HB2 . 18795 1 126 . 1 1 28 28 SER N N 15 112.92 0.14 . 1 . . . . 28 SER N . 18795 1 127 . 1 1 29 29 SER H H 1 8.249 0.001 . 1 . . . . 29 SER H . 18795 1 128 . 1 1 29 29 SER HA H 1 4.49 0.08 . 1 . . . . 29 SER HA . 18795 1 129 . 1 1 29 29 SER HB2 H 1 3.71 0.08 . 2 . . . . 29 SER HB2 . 18795 1 130 . 1 1 29 29 SER N N 15 115.10 0.14 . 1 . . . . 29 SER N . 18795 1 131 . 1 1 30 30 THR H H 1 7.872 0.001 . 1 . . . . 30 THR H . 18795 1 132 . 1 1 30 30 THR HA H 1 4.33 0.08 . 1 . . . . 30 THR HA . 18795 1 133 . 1 1 30 30 THR HG21 H 1 1.20 0.08 . 1 . . . . 30 THR MG . 18795 1 134 . 1 1 30 30 THR HG22 H 1 1.20 0.08 . 1 . . . . 30 THR MG . 18795 1 135 . 1 1 30 30 THR HG23 H 1 1.20 0.08 . 1 . . . . 30 THR MG . 18795 1 136 . 1 1 30 30 THR N N 15 111.13 0.14 . 1 . . . . 30 THR N . 18795 1 137 . 1 1 31 31 ASN H H 1 8.185 0.001 . 1 . . . . 31 ASN H . 18795 1 138 . 1 1 31 31 ASN HA H 1 4.64 0.08 . 1 . . . . 31 ASN HA . 18795 1 139 . 1 1 31 31 ASN HB2 H 1 2.61 0.08 . 2 . . . . 31 ASN HB2 . 18795 1 140 . 1 1 31 31 ASN N N 15 118.81 0.14 . 1 . . . . 31 ASN N . 18795 1 141 . 1 1 32 32 VAL H H 1 7.869 0.001 . 1 . . . . 32 VAL H . 18795 1 142 . 1 1 32 32 VAL HA H 1 4.18 0.08 . 1 . . . . 32 VAL HA . 18795 1 143 . 1 1 32 32 VAL HB H 1 2.14 0.08 . 1 . . . . 32 VAL HB . 18795 1 144 . 1 1 32 32 VAL HG11 H 1 0.89 0.08 . 2 . . . . 32 VAL MG1 . 18795 1 145 . 1 1 32 32 VAL HG12 H 1 0.89 0.08 . 2 . . . . 32 VAL MG1 . 18795 1 146 . 1 1 32 32 VAL HG13 H 1 0.89 0.08 . 2 . . . . 32 VAL MG1 . 18795 1 147 . 1 1 32 32 VAL HG21 H 1 1.05 0.08 . 2 . . . . 32 VAL MG2 . 18795 1 148 . 1 1 32 32 VAL HG22 H 1 1.05 0.08 . 2 . . . . 32 VAL MG2 . 18795 1 149 . 1 1 32 32 VAL HG23 H 1 1.05 0.08 . 2 . . . . 32 VAL MG2 . 18795 1 150 . 1 1 32 32 VAL N N 15 114.34 0.14 . 1 . . . . 32 VAL N . 18795 1 151 . 1 1 33 33 GLY H H 1 8.304 0.001 . 1 . . . . 33 GLY H . 18795 1 152 . 1 1 33 33 GLY HA2 H 1 3.86 0.08 . 2 . . . . 33 GLY HA2 . 18795 1 153 . 1 1 33 33 GLY N N 15 107.85 0.14 . 1 . . . . 33 GLY N . 18795 1 154 . 1 1 34 34 SER H H 1 8.042 0.001 . 1 . . . . 34 SER H . 18795 1 155 . 1 1 34 34 SER HA H 1 4.49 0.08 . 1 . . . . 34 SER HA . 18795 1 156 . 1 1 34 34 SER HB2 H 1 3.71 0.08 . 2 . . . . 34 SER HB2 . 18795 1 157 . 1 1 34 34 SER N N 15 112.49 0.14 . 1 . . . . 34 SER N . 18795 1 158 . 1 1 35 35 ASN H H 1 8.416 0.001 . 1 . . . . 35 ASN H . 18795 1 159 . 1 1 35 35 ASN HA H 1 4.64 0.08 . 1 . . . . 35 ASN HA . 18795 1 160 . 1 1 35 35 ASN HB2 H 1 2.61 0.08 . 2 . . . . 35 ASN HB2 . 18795 1 161 . 1 1 35 35 ASN N N 15 119.41 0.14 . 1 . . . . 35 ASN N . 18795 1 162 . 1 1 36 36 THR H H 1 7.715 0.001 . 1 . . . . 36 THR H . 18795 1 163 . 1 1 36 36 THR HA H 1 4.33 0.08 . 1 . . . . 36 THR HA . 18795 1 164 . 1 1 36 36 THR HG21 H 1 1.20 0.08 . 1 . . . . 36 THR MG . 18795 1 165 . 1 1 36 36 THR HG22 H 1 1.20 0.08 . 1 . . . . 36 THR MG . 18795 1 166 . 1 1 36 36 THR HG23 H 1 1.20 0.08 . 1 . . . . 36 THR MG . 18795 1 167 . 1 1 36 36 THR N N 15 109.73 0.14 . 1 . . . . 36 THR N . 18795 1 168 . 1 1 37 37 TYR H H 1 8.089 0.001 . 1 . . . . 37 TYR H . 18795 1 169 . 1 1 37 37 TYR HA H 1 4.49 0.08 . 1 . . . . 37 TYR HA . 18795 1 170 . 1 1 37 37 TYR HB2 H 1 2.92 0.08 . 2 . . . . 37 TYR HB2 . 18795 1 171 . 1 1 37 37 TYR N N 15 118.08 0.14 . 1 . . . . 37 TYR N . 18795 1 stop_ save_