data_5860 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5860 _Entry.Title ; Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Post-translational Modifications Linking Cysteine Sulfurs to alpha-Carbons of Phenylalanine and Threonine ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-07-04 _Entry.Accession_date 2003-07-04 _Entry.Last_release_date 2003-12-19 _Entry.Original_release_date 2003-12-19 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 Karen Kawulka . . . 5860 2 Tara Sprules . . . 5860 3 Ryan McKay . T. . 5860 4 Pascal Mercier . . . 5860 5 Christopher Diaper . M. . 5860 6 Peter Zuber . . . 5860 7 John Vederas . C. . 5860 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5860 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 207 5860 '13C chemical shifts' 93 5860 '15N chemical shifts' 35 5860 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 . . 2003-12-19 2003-07-04 original author . 5860 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5860 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22583854 _Citation.DOI . _Citation.PubMed_ID 12696888 _Citation.Full_citation . _Citation.Title ; Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to alpha-Carbons of Phenylalanine and Threonine ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full . _Citation.Journal_volume 125 _Citation.Journal_issue 16 _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 4726 _Citation.Page_last 4727 _Citation.Year 2003 _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 Karen Kawulka . . . 5860 1 2 Tara Sprules . . . 5860 1 3 Ryan McKay . T. . 5860 1 4 Pascal Mercier . . . 5860 1 5 Christopher Diaper . M. . 5860 1 6 Peter Zuber . . . 5860 1 7 John Vederas . C. . 5860 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID bacteriocin 5860 1 thioether 5860 1 subtilosin 5860 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5860 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12696888 _Citation.Full_citation ; Kawulka K, Sprules T, McKay RT, Mercier P, Diaper CM, Zuber P, Vederas JC. J Am Chem Soc. 2003 Apr 23;125(16):4726-7. ; _Citation.Title 'Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full 'Journal of the American Chemical Society' _Citation.Journal_volume 125 _Citation.Journal_issue 16 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0002-7863 _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 4726 _Citation.Page_last 4727 _Citation.Year 2003 _Citation.Details ; The complete primary and three-dimensional solution structures of subtilosin A (1), a bacteriocin from Bacillus subtilis, were determined by multidimensional NMR studies on peptide produced using isotopically labeled [(13)C,(15)N]medium derived from Anabaena sp. grown on sodium [(13)C]bicarbonate and [(15)N]nitrate. Additional samples of 1 were also generated by separate incorporations of [U-(13)C,(15)N]phenylalanine and [U-(13)C,(15)N]threonine using otherwise unlabeled media. The results demonstrate that in addition to having a cyclized peptide backbone (N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the alpha-positions of Phe22, Thr28, and Phe31, respectively. Such posttranslational linkage of a thiol to the alpha-carbon of an amino acid residue is very unusual in natural peptides or proteins. Subtilosin A (1) belongs to a new class of bacteriocins. ; 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 Karen Kawulka K. . . 5860 2 2 Tara Sprules T. . . 5860 2 3 'Ryan T' McKay R. T. . 5860 2 4 Pascal Mercier P. . . 5860 2 5 'Christopher M' Diaper C. M. . 5860 2 6 Peter Zuber P. . . 5860 2 7 'John C' Vederas J. C. . 5860 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_SubA _Assembly.Sf_category assembly _Assembly.Sf_framecode system_SubA _Assembly.Entry_ID 5860 _Assembly.ID 1 _Assembly.Name 'Subtilosin A' _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 'other bound, and free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5860 1 stop_ 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 'Subtilosin A' 1 $SubA . . . native . . . . . 5860 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 thioether single . 1 . 1 CYS 4 4 SG . 1 . 1 PHE 31 31 CA . . . . . . . . . . 5860 1 2 thioether single . 1 . 1 CYS 7 7 SG . 1 . 1 THR 28 28 CA . . . . . . . . . . 5860 1 3 thioether single . 1 . 1 CYS 13 13 SG . 1 . 1 PHE 22 22 CA . . . . . . . . . . 5860 1 4 amide single . 1 . 1 ASN 1 1 N . 1 . 1 GLY 35 35 C . . . . . . . . . . 5860 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Subtilosin A' system 5860 1 SubA abbreviation 5860 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID bacteriocin 5860 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SubA _Entity.Sf_category entity _Entity.Sf_framecode SubA _Entity.Entry_ID 5860 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Subtilosin A' _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 ; NKGCATCSIGAACLVDGPIP DFEIAGATGLFGLWG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 35 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'other bound, and free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3401 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 DBJ BAI87397 . "subtilosin A [Bacillus subtilis subsp. natto BEST195]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 2 no DBJ BAM55818 . "subtilosin A [Bacillus subtilis BEST7613]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 3 no DBJ BAM59830 . "subtilosin A [Bacillus subtilis BEST7003]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 4 no DBJ GAK81054 . "subtilosin A [Bacillus subtilis Miyagi-4]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 5 no EMBL CAB09701 . "subtilosin A [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 6 no EMBL CAB15763 . "subtilosin A [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 7 no EMBL CAD23198 . "subtilosin A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 8 no EMBL CCU60834 . "subtilosin A [Bacillus subtilis E1]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 9 no EMBL CEI59543 . "subtilosin-A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 10 no GB ABD92636 . "subtilosin A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 11 no GB ABD92637 . "subtilosin A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 12 no GB ABD92638 . "subtilosin A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 13 no GB ABW83032 . "SboA [Bacillus amyloliquefaciens]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 14 no GB ACO72595 . "subtilosin A [Bacillus subtilis]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 15 no REF NP_391616 . "subtilosin-A [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 16 no REF WP_003222002 . "MULTISPECIES: serine protease [Bacillales]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 17 no REF YP_003868035 . "subtilosin A [Bacillus subtilis subsp. spizizenii str. W23]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 18 no REF YP_003975177 . "subtilosin A [Bacillus atrophaeus 1942]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 19 no REF YP_004205572 . "subtilosin A [Bacillus subtilis BSn5]" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 20 no SP O07623 . "RecName: Full=Subtilosin-A; AltName: Full=Antilisterial bacteriocin subtilosin; Flags: Precursor [Bacillus subtilis subsp. subt" . . . . . 100.00 43 100.00 100.00 2.20e-15 . . . . 5860 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Subtilosin A' common 5860 1 SubA abbreviation 5860 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 . ASN . 5860 1 2 . LYS . 5860 1 3 . GLY . 5860 1 4 . CYS . 5860 1 5 . ALA . 5860 1 6 . THR . 5860 1 7 . CYS . 5860 1 8 . SER . 5860 1 9 . ILE . 5860 1 10 . GLY . 5860 1 11 . ALA . 5860 1 12 . ALA . 5860 1 13 . CYS . 5860 1 14 . LEU . 5860 1 15 . VAL . 5860 1 16 . ASP . 5860 1 17 . GLY . 5860 1 18 . PRO . 5860 1 19 . ILE . 5860 1 20 . PRO . 5860 1 21 . ASP . 5860 1 22 . PHE . 5860 1 23 . GLU . 5860 1 24 . ILE . 5860 1 25 . ALA . 5860 1 26 . GLY . 5860 1 27 . ALA . 5860 1 28 . THR . 5860 1 29 . GLY . 5860 1 30 . LEU . 5860 1 31 . PHE . 5860 1 32 . GLY . 5860 1 33 . LEU . 5860 1 34 . TRP . 5860 1 35 . GLY . 5860 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 . ASN 1 1 5860 1 . LYS 2 2 5860 1 . GLY 3 3 5860 1 . CYS 4 4 5860 1 . ALA 5 5 5860 1 . THR 6 6 5860 1 . CYS 7 7 5860 1 . SER 8 8 5860 1 . ILE 9 9 5860 1 . GLY 10 10 5860 1 . ALA 11 11 5860 1 . ALA 12 12 5860 1 . CYS 13 13 5860 1 . LEU 14 14 5860 1 . VAL 15 15 5860 1 . ASP 16 16 5860 1 . GLY 17 17 5860 1 . PRO 18 18 5860 1 . ILE 19 19 5860 1 . PRO 20 20 5860 1 . ASP 21 21 5860 1 . PHE 22 22 5860 1 . GLU 23 23 5860 1 . ILE 24 24 5860 1 . ALA 25 25 5860 1 . GLY 26 26 5860 1 . ALA 27 27 5860 1 . THR 28 28 5860 1 . GLY 29 29 5860 1 . LEU 30 30 5860 1 . PHE 31 31 5860 1 . GLY 32 32 5860 1 . LEU 33 33 5860 1 . TRP 34 34 5860 1 . GLY 35 35 5860 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 5860 _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 $SubA . 1423 organism . 'Bacillus subtilis' 'Bacillus subtilis' . . Eubacteria . Bacillus subtilis JH642 . . . . . . . . . . . secreted . . . sboA . . . . 5860 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 5860 _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 $SubA . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5860 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5860 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'Subtilosin A' '[U-100% 13C; U-80% 15N]' . . 1 $SubA . . 1.0 . . mM . . . . 5860 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 5860 _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 4.5 . n/a 5860 1 temperature 288 0.5 K 5860 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5860 _Software.ID 1 _Software.Name NMRPipe _Software.Version 2.2 _Software.Details ; Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. J. Biomolecular NMR \t1995, 6, 277-293 ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5860 1 stop_ save_ save_NMRVIEW _Software.Sf_category software _Software.Sf_framecode NMRVIEW _Software.Entry_ID 5860 _Software.ID 2 _Software.Name NMRVIEW _Software.Version 5.0 _Software.Details ; Johnson, B. A.; Blevins, R. A. J. Biomolecular NMR 1994, 4, 603-614." with in-house (NANUC) modifications ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5860 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5860 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5860 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5860 _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 NMR_spectrometer_1 Varian INOVA . 500 . . . 5860 1 2 NMR_spectrometer_2 Varian INOVA . 800 . . . 5860 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 5860 _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 '1H-13C HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 2 1H-15N-HSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 3 HNHA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 4 CBCA(CO)NNH . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 5 HCCH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 6 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 7 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 8 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 9 13C-NOESYHSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 10 15N-NOESYHSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 11 15N-TOCSYHSQC . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 12 13C,15N-NOESY . . . . . . . . . . . 1 $sample_1 . . . 1 $cond_1 . . . . . . . . . . . . . . . . . . . . . 5860 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5860 _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 0.0 internal direct 1.0 . . . . . . . . . 5860 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5860 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5860 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_SubA_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode SubA_shifts _Assigned_chem_shift_list.Entry_ID 5860 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 $sample_1 . 5860 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 ASN N N 15 116.219 0.2 . 1 . . . . . . . . 5860 1 2 . 1 1 1 1 ASN H H 1 7.450 0.01 . 1 . . . . . . . . 5860 1 3 . 1 1 1 1 ASN CA C 13 52.377 0.2 . 1 . . . . . . . . 5860 1 4 . 1 1 1 1 ASN HA H 1 4.708 0.01 . 1 . . . . . . . . 5860 1 5 . 1 1 1 1 ASN CB C 13 39.328 0.2 . 1 . . . . . . . . 5860 1 6 . 1 1 1 1 ASN HB3 H 1 2.491 0.01 . 2 . . . . . . . . 5860 1 7 . 1 1 1 1 ASN HB2 H 1 3.880 0.01 . 2 . . . . . . . . 5860 1 8 . 1 1 1 1 ASN ND2 N 15 107.758 0.2 . 1 . . . . . . . . 5860 1 9 . 1 1 1 1 ASN HD21 H 1 7.968 0.01 . 2 . . . . . . . . 5860 1 10 . 1 1 1 1 ASN HD22 H 1 7.092 0.01 . 2 . . . . . . . . 5860 1 11 . 1 1 2 2 LYS N N 15 127.218 0.2 . 1 . . . . . . . . 5860 1 12 . 1 1 2 2 LYS H H 1 9.257 0.01 . 1 . . . . . . . . 5860 1 13 . 1 1 2 2 LYS CA C 13 59.068 0.2 . 1 . . . . . . . . 5860 1 14 . 1 1 2 2 LYS HA H 1 3.933 0.01 . 1 . . . . . . . . 5860 1 15 . 1 1 2 2 LYS CB C 13 32.258 0.2 . 1 . . . . . . . . 5860 1 16 . 1 1 2 2 LYS HB3 H 1 1.836 0.01 . 2 . . . . . . . . 5860 1 17 . 1 1 2 2 LYS HB2 H 1 1.730 0.01 . 2 . . . . . . . . 5860 1 18 . 1 1 2 2 LYS CG C 13 25.692 0.2 . 1 . . . . . . . . 5860 1 19 . 1 1 2 2 LYS HG3 H 1 1.473 0.01 . 2 . . . . . . . . 5860 1 20 . 1 1 2 2 LYS HG2 H 1 1.581 0.01 . 2 . . . . . . . . 5860 1 21 . 1 1 2 2 LYS CD C 13 29.435 0.2 . 1 . . . . . . . . 5860 1 22 . 1 1 2 2 LYS HD2 H 1 1.618 0.01 . 2 . . . . . . . . 5860 1 23 . 1 1 2 2 LYS CE C 13 41.909 0.2 . 1 . . . . . . . . 5860 1 24 . 1 1 2 2 LYS HE2 H 1 2.887 0.01 . 2 . . . . . . . . 5860 1 25 . 1 1 3 3 GLY N N 15 105.736 0.2 . 1 . . . . . . . . 5860 1 26 . 1 1 3 3 GLY H H 1 9.133 0.01 . 1 . . . . . . . . 5860 1 27 . 1 1 3 3 GLY CA C 13 46.573 0.2 . 1 . . . . . . . . 5860 1 28 . 1 1 3 3 GLY HA3 H 1 3.749 0.01 . 2 . . . . . . . . 5860 1 29 . 1 1 3 3 GLY HA2 H 1 3.827 0.01 . 2 . . . . . . . . 5860 1 30 . 1 1 4 4 CYS N N 15 118.627 0.2 . 1 . . . . . . . . 5860 1 31 . 1 1 4 4 CYS H H 1 7.769 0.01 . 1 . . . . . . . . 5860 1 32 . 1 1 4 4 CYS CA C 13 57.701 0.2 . 1 . . . . . . . . 5860 1 33 . 1 1 4 4 CYS HA H 1 3.974 0.01 . 1 . . . . . . . . 5860 1 34 . 1 1 4 4 CYS CB C 13 33.339 0.2 . 1 . . . . . . . . 5860 1 35 . 1 1 4 4 CYS HB3 H 1 3.145 0.01 . 2 . . . . . . . . 5860 1 36 . 1 1 4 4 CYS HB2 H 1 3.453 0.01 . 2 . . . . . . . . 5860 1 37 . 1 1 5 5 ALA N N 15 120.179 0.2 . 1 . . . . . . . . 5860 1 38 . 1 1 5 5 ALA H H 1 7.827 0.01 . 1 . . . . . . . . 5860 1 39 . 1 1 5 5 ALA CA C 13 54.716 0.2 . 1 . . . . . . . . 5860 1 40 . 1 1 5 5 ALA HA H 1 4.104 0.01 . 1 . . . . . . . . 5860 1 41 . 1 1 5 5 ALA CB C 13 17.879 0.2 . 1 . . . . . . . . 5860 1 42 . 1 1 5 5 ALA HB1 H 1 1.474 0.01 . 1 . . . . . . . . 5860 1 43 . 1 1 5 5 ALA HB2 H 1 1.474 0.01 . 1 . . . . . . . . 5860 1 44 . 1 1 5 5 ALA HB3 H 1 1.474 0.01 . 1 . . . . . . . . 5860 1 45 . 1 1 6 6 THR N N 15 111.274 0.2 . 1 . . . . . . . . 5860 1 46 . 1 1 6 6 THR H H 1 7.783 0.01 . 1 . . . . . . . . 5860 1 47 . 1 1 6 6 THR CA C 13 65.206 0.2 . 1 . . . . . . . . 5860 1 48 . 1 1 6 6 THR HA H 1 3.895 0.01 . 1 . . . . . . . . 5860 1 49 . 1 1 6 6 THR CB C 13 68.745 0.2 . 1 . . . . . . . . 5860 1 50 . 1 1 6 6 THR HB H 1 4.128 0.01 . 1 . . . . . . . . 5860 1 51 . 1 1 6 6 THR CG2 C 13 21.609 0.2 . 1 . . . . . . . . 5860 1 52 . 1 1 6 6 THR HG21 H 1 1.237 0.01 . 1 . . . . . . . . 5860 1 53 . 1 1 6 6 THR HG22 H 1 1.237 0.01 . 1 . . . . . . . . 5860 1 54 . 1 1 6 6 THR HG23 H 1 1.237 0.01 . 1 . . . . . . . . 5860 1 55 . 1 1 7 7 CYS N N 15 117.128 0.2 . 1 . . . . . . . . 5860 1 56 . 1 1 7 7 CYS H H 1 7.147 0.01 . 1 . . . . . . . . 5860 1 57 . 1 1 7 7 CYS CA C 13 56.913 0.2 . 1 . . . . . . . . 5860 1 58 . 1 1 7 7 CYS HA H 1 4.025 0.01 . 1 . . . . . . . . 5860 1 59 . 1 1 7 7 CYS CB C 13 31.841 0.2 . 1 . . . . . . . . 5860 1 60 . 1 1 7 7 CYS HB3 H 1 3.610 0.01 . 2 . . . . . . . . 5860 1 61 . 1 1 7 7 CYS HB2 H 1 2.840 0.01 . 2 . . . . . . . . 5860 1 62 . 1 1 8 8 SER N N 15 116.232 0.2 . 1 . . . . . . . . 5860 1 63 . 1 1 8 8 SER H H 1 8.000 0.01 . 1 . . . . . . . . 5860 1 64 . 1 1 8 8 SER CA C 13 61.886 0.2 . 1 . . . . . . . . 5860 1 65 . 1 1 8 8 SER HA H 1 4.045 0.01 . 1 . . . . . . . . 5860 1 66 . 1 1 8 8 SER CB C 13 62.614 0.2 . 1 . . . . . . . . 5860 1 67 . 1 1 8 8 SER HB3 H 1 3.936 0.01 . 2 . . . . . . . . 5860 1 68 . 1 1 9 9 ILE N N 15 119.568 0.2 . 1 . . . . . . . . 5860 1 69 . 1 1 9 9 ILE H H 1 7.468 0.01 . 1 . . . . . . . . 5860 1 70 . 1 1 9 9 ILE CA C 13 62.826 0.2 . 1 . . . . . . . . 5860 1 71 . 1 1 9 9 ILE HA H 1 4.053 0.01 . 1 . . . . . . . . 5860 1 72 . 1 1 9 9 ILE CB C 13 38.438 0.2 . 1 . . . . . . . . 5860 1 73 . 1 1 9 9 ILE HB H 1 1.912 0.01 . 1 . . . . . . . . 5860 1 74 . 1 1 9 9 ILE CG1 C 13 27.658 0.2 . 1 . . . . . . . . 5860 1 75 . 1 1 9 9 ILE HG13 H 1 1.446 0.01 . 2 . . . . . . . . 5860 1 76 . 1 1 9 9 ILE HG12 H 1 1.450 0.01 . 2 . . . . . . . . 5860 1 77 . 1 1 9 9 ILE CD1 C 13 13.412 0.2 . 1 . . . . . . . . 5860 1 78 . 1 1 9 9 ILE HD11 H 1 0.875 0.01 . 1 . . . . . . . . 5860 1 79 . 1 1 9 9 ILE HD12 H 1 0.875 0.01 . 1 . . . . . . . . 5860 1 80 . 1 1 9 9 ILE HD13 H 1 0.875 0.01 . 1 . . . . . . . . 5860 1 81 . 1 1 9 9 ILE CG2 C 13 17.439 0.2 . 1 . . . . . . . . 5860 1 82 . 1 1 9 9 ILE HG21 H 1 0.935 0.01 . 1 . . . . . . . . 5860 1 83 . 1 1 9 9 ILE HG22 H 1 0.935 0.01 . 1 . . . . . . . . 5860 1 84 . 1 1 9 9 ILE HG23 H 1 0.935 0.01 . 1 . . . . . . . . 5860 1 85 . 1 1 10 10 GLY N N 15 106.889 0.2 . 1 . . . . . . . . 5860 1 86 . 1 1 10 10 GLY H H 1 7.948 0.01 . 1 . . . . . . . . 5860 1 87 . 1 1 10 10 GLY CA C 13 47.134 0.2 . 1 . . . . . . . . 5860 1 88 . 1 1 10 10 GLY HA3 H 1 3.455 0.01 . 2 . . . . . . . . 5860 1 89 . 1 1 10 10 GLY HA2 H 1 4.008 0.01 . 2 . . . . . . . . 5860 1 90 . 1 1 11 11 ALA N N 15 121.647 0.2 . 1 . . . . . . . . 5860 1 91 . 1 1 11 11 ALA H H 1 7.988 0.01 . 1 . . . . . . . . 5860 1 92 . 1 1 11 11 ALA CA C 13 54.686 0.2 . 1 . . . . . . . . 5860 1 93 . 1 1 11 11 ALA HA H 1 3.981 0.01 . 1 . . . . . . . . 5860 1 94 . 1 1 11 11 ALA CB C 13 17.697 0.2 . 1 . . . . . . . . 5860 1 95 . 1 1 11 11 ALA HB1 H 1 1.427 0.01 . 1 . . . . . . . . 5860 1 96 . 1 1 11 11 ALA HB2 H 1 1.427 0.01 . 1 . . . . . . . . 5860 1 97 . 1 1 11 11 ALA HB3 H 1 1.427 0.01 . 1 . . . . . . . . 5860 1 98 . 1 1 12 12 ALA N N 15 118.722 0.2 . 1 . . . . . . . . 5860 1 99 . 1 1 12 12 ALA H H 1 8.023 0.01 . 1 . . . . . . . . 5860 1 100 . 1 1 12 12 ALA CA C 13 54.664 0.2 . 1 . . . . . . . . 5860 1 101 . 1 1 12 12 ALA HA H 1 3.998 0.01 . 1 . . . . . . . . 5860 1 102 . 1 1 12 12 ALA CB C 13 17.434 0.2 . 1 . . . . . . . . 5860 1 103 . 1 1 12 12 ALA HB1 H 1 1.471 0.01 . 1 . . . . . . . . 5860 1 104 . 1 1 12 12 ALA HB2 H 1 1.471 0.01 . 1 . . . . . . . . 5860 1 105 . 1 1 12 12 ALA HB3 H 1 1.471 0.01 . 1 . . . . . . . . 5860 1 106 . 1 1 13 13 CYS N N 15 110.215 0.2 . 1 . . . . . . . . 5860 1 107 . 1 1 13 13 CYS H H 1 7.515 0.01 . 1 . . . . . . . . 5860 1 108 . 1 1 13 13 CYS CA C 13 56.141 0.2 . 1 . . . . . . . . 5860 1 109 . 1 1 13 13 CYS HA H 1 4.175 0.01 . 1 . . . . . . . . 5860 1 110 . 1 1 13 13 CYS CB C 13 32.111 0.2 . 1 . . . . . . . . 5860 1 111 . 1 1 13 13 CYS HB3 H 1 3.281 0.01 . 2 . . . . . . . . 5860 1 112 . 1 1 13 13 CYS HB2 H 1 3.492 0.01 . 2 . . . . . . . . 5860 1 113 . 1 1 14 14 LEU N N 15 125.160 0.2 . 1 . . . . . . . . 5860 1 114 . 1 1 14 14 LEU H H 1 8.073 0.01 . 1 . . . . . . . . 5860 1 115 . 1 1 14 14 LEU CA C 13 56.668 0.2 . 1 . . . . . . . . 5860 1 116 . 1 1 14 14 LEU HA H 1 4.222 0.01 . 1 . . . . . . . . 5860 1 117 . 1 1 14 14 LEU CB C 13 40.939 0.2 . 1 . . . . . . . . 5860 1 118 . 1 1 14 14 LEU HB3 H 1 1.904 0.01 . 2 . . . . . . . . 5860 1 119 . 1 1 14 14 LEU HB2 H 1 1.506 0.01 . 2 . . . . . . . . 5860 1 120 . 1 1 14 14 LEU CG C 13 27.597 0.2 . 1 . . . . . . . . 5860 1 121 . 1 1 14 14 LEU HG H 1 1.691 0.01 . 1 . . . . . . . . 5860 1 122 . 1 1 14 14 LEU CD1 C 13 24.815 0.2 . 4 . . . . . . . . 5860 1 123 . 1 1 14 14 LEU HD11 H 1 0.900 0.01 . 2 . . . . . . . . 5860 1 124 . 1 1 14 14 LEU HD12 H 1 0.900 0.01 . 2 . . . . . . . . 5860 1 125 . 1 1 14 14 LEU HD13 H 1 0.900 0.01 . 2 . . . . . . . . 5860 1 126 . 1 1 14 14 LEU CD2 C 13 22.353 0.2 . 4 . . . . . . . . 5860 1 127 . 1 1 14 14 LEU HD21 H 1 0.857 0.01 . 2 . . . . . . . . 5860 1 128 . 1 1 14 14 LEU HD22 H 1 0.857 0.01 . 2 . . . . . . . . 5860 1 129 . 1 1 14 14 LEU HD23 H 1 0.857 0.01 . 2 . . . . . . . . 5860 1 130 . 1 1 15 15 VAL N N 15 118.019 0.2 . 1 . . . . . . . . 5860 1 131 . 1 1 15 15 VAL H H 1 7.516 0.01 . 1 . . . . . . . . 5860 1 132 . 1 1 15 15 VAL CA C 13 65.064 0.2 . 1 . . . . . . . . 5860 1 133 . 1 1 15 15 VAL HA H 1 3.817 0.01 . 1 . . . . . . . . 5860 1 134 . 1 1 15 15 VAL CB C 13 31.525 0.2 . 1 . . . . . . . . 5860 1 135 . 1 1 15 15 VAL HB H 1 2.225 0.01 . 1 . . . . . . . . 5860 1 136 . 1 1 15 15 VAL CG2 C 13 20.872 0.2 . 4 . . . . . . . . 5860 1 137 . 1 1 15 15 VAL HG21 H 1 1.020 0.01 . 2 . . . . . . . . 5860 1 138 . 1 1 15 15 VAL HG22 H 1 1.020 0.01 . 2 . . . . . . . . 5860 1 139 . 1 1 15 15 VAL HG23 H 1 1.020 0.01 . 2 . . . . . . . . 5860 1 140 . 1 1 15 15 VAL CG1 C 13 20.123 0.2 . 4 . . . . . . . . 5860 1 141 . 1 1 15 15 VAL HG11 H 1 0.951 0.01 . 2 . . . . . . . . 5860 1 142 . 1 1 15 15 VAL HG12 H 1 0.951 0.01 . 2 . . . . . . . . 5860 1 143 . 1 1 15 15 VAL HG13 H 1 0.951 0.01 . 2 . . . . . . . . 5860 1 144 . 1 1 16 16 ASP N N 15 114.415 0.2 . 1 . . . . . . . . 5860 1 145 . 1 1 16 16 ASP H H 1 6.758 0.01 . 1 . . . . . . . . 5860 1 146 . 1 1 16 16 ASP CA C 13 50.473 0.2 . 1 . . . . . . . . 5860 1 147 . 1 1 16 16 ASP HA H 1 4.804 0.01 . 1 . . . . . . . . 5860 1 148 . 1 1 16 16 ASP CB C 13 38.405 0.2 . 1 . . . . . . . . 5860 1 149 . 1 1 16 16 ASP HB3 H 1 2.420 0.01 . 2 . . . . . . . . 5860 1 150 . 1 1 16 16 ASP HB2 H 1 3.197 0.01 . 2 . . . . . . . . 5860 1 151 . 1 1 17 17 GLY N N 15 104.272 0.2 . 1 . . . . . . . . 5860 1 152 . 1 1 17 17 GLY H H 1 7.897 0.01 . 1 . . . . . . . . 5860 1 153 . 1 1 17 17 GLY CA C 13 44.130 0.2 . 1 . . . . . . . . 5860 1 154 . 1 1 17 17 GLY HA3 H 1 3.727 0.01 . 2 . . . . . . . . 5860 1 155 . 1 1 17 17 GLY HA2 H 1 4.402 0.01 . 2 . . . . . . . . 5860 1 156 . 1 1 18 18 PRO CA C 13 63.577 0.2 . 1 . . . . . . . . 5860 1 157 . 1 1 18 18 PRO HA H 1 4.497 0.01 . 1 . . . . . . . . 5860 1 158 . 1 1 18 18 PRO CB C 13 30.965 0.2 . 1 . . . . . . . . 5860 1 159 . 1 1 18 18 PRO HB3 H 1 1.940 0.01 . 2 . . . . . . . . 5860 1 160 . 1 1 18 18 PRO HB2 H 1 2.093 0.01 . 2 . . . . . . . . 5860 1 161 . 1 1 18 18 PRO CG C 13 26.391 0.2 . 1 . . . . . . . . 5860 1 162 . 1 1 18 18 PRO HG3 H 1 1.753 0.01 . 2 . . . . . . . . 5860 1 163 . 1 1 18 18 PRO HG2 H 1 1.920 0.01 . 2 . . . . . . . . 5860 1 164 . 1 1 18 18 PRO CD C 13 49.738 0.2 . 1 . . . . . . . . 5860 1 165 . 1 1 18 18 PRO HD3 H 1 3.500 0.01 . 2 . . . . . . . . 5860 1 166 . 1 1 18 18 PRO HD2 H 1 3.765 0.01 . 2 . . . . . . . . 5860 1 167 . 1 1 19 19 ILE N N 15 121.987 0.2 . 1 . . . . . . . . 5860 1 168 . 1 1 19 19 ILE H H 1 7.067 0.01 . 1 . . . . . . . . 5860 1 169 . 1 1 19 19 ILE CA C 13 60.079 0.2 . 1 . . . . . . . . 5860 1 170 . 1 1 19 19 ILE HA H 1 4.036 0.01 . 1 . . . . . . . . 5860 1 171 . 1 1 19 19 ILE CB C 13 38.228 0.2 . 1 . . . . . . . . 5860 1 172 . 1 1 19 19 ILE HB H 1 1.563 0.01 . 1 . . . . . . . . 5860 1 173 . 1 1 19 19 ILE CG1 C 13 28.186 0.2 . 1 . . . . . . . . 5860 1 174 . 1 1 19 19 ILE HG13 H 1 1.543 0.01 . 2 . . . . . . . . 5860 1 175 . 1 1 19 19 ILE HG12 H 1 1.050 0.01 . 2 . . . . . . . . 5860 1 176 . 1 1 19 19 ILE CD1 C 13 12.892 0.2 . 1 . . . . . . . . 5860 1 177 . 1 1 19 19 ILE HD11 H 1 0.858 0.01 . 1 . . . . . . . . 5860 1 178 . 1 1 19 19 ILE HD12 H 1 0.858 0.01 . 1 . . . . . . . . 5860 1 179 . 1 1 19 19 ILE HD13 H 1 0.858 0.01 . 1 . . . . . . . . 5860 1 180 . 1 1 19 19 ILE CG2 C 13 16.157 0.2 . 1 . . . . . . . . 5860 1 181 . 1 1 19 19 ILE HG21 H 1 0.726 0.01 . 1 . . . . . . . . 5860 1 182 . 1 1 19 19 ILE HG22 H 1 0.726 0.01 . 1 . . . . . . . . 5860 1 183 . 1 1 19 19 ILE HG23 H 1 0.726 0.01 . 1 . . . . . . . . 5860 1 184 . 1 1 20 20 PRO CA C 13 63.046 0.2 . 1 . . . . . . . . 5860 1 185 . 1 1 20 20 PRO HA H 1 4.115 0.01 . 1 . . . . . . . . 5860 1 186 . 1 1 20 20 PRO CB C 13 30.602 0.2 . 1 . . . . . . . . 5860 1 187 . 1 1 20 20 PRO HB3 H 1 1.887 0.01 . 2 . . . . . . . . 5860 1 188 . 1 1 20 20 PRO HB2 H 1 1.952 0.01 . 2 . . . . . . . . 5860 1 189 . 1 1 20 20 PRO CG C 13 27.704 0.2 . 1 . . . . . . . . 5860 1 190 . 1 1 20 20 PRO HG3 H 1 2.281 0.01 . 2 . . . . . . . . 5860 1 191 . 1 1 20 20 PRO HG2 H 1 1.948 0.01 . 2 . . . . . . . . 5860 1 192 . 1 1 20 20 PRO CD C 13 51.552 0.2 . 1 . . . . . . . . 5860 1 193 . 1 1 20 20 PRO HD3 H 1 3.545 0.01 . 2 . . . . . . . . 5860 1 194 . 1 1 20 20 PRO HD2 H 1 3.873 0.01 . 2 . . . . . . . . 5860 1 195 . 1 1 21 21 ASP N N 15 122.249 0.2 . 1 . . . . . . . . 5860 1 196 . 1 1 21 21 ASP H H 1 8.917 0.01 . 1 . . . . . . . . 5860 1 197 . 1 1 21 21 ASP CA C 13 54.223 0.2 . 1 . . . . . . . . 5860 1 198 . 1 1 21 21 ASP HA H 1 4.447 0.01 . 1 . . . . . . . . 5860 1 199 . 1 1 21 21 ASP CB C 13 38.190 0.2 . 1 . . . . . . . . 5860 1 200 . 1 1 21 21 ASP HB3 H 1 2.244 0.01 . 2 . . . . . . . . 5860 1 201 . 1 1 21 21 ASP HB2 H 1 2.759 0.01 . 2 . . . . . . . . 5860 1 202 . 1 1 22 22 PHE N N 15 124.887 0.2 . 1 . . . . . . . . 5860 1 203 . 1 1 22 22 PHE H H 1 7.979 0.01 . 1 . . . . . . . . 5860 1 204 . 1 1 22 22 PHE CA C 13 69.380 0.2 . 1 . . . . . . . . 5860 1 205 . 1 1 22 22 PHE CB C 13 40.743 0.2 . 1 . . . . . . . . 5860 1 206 . 1 1 22 22 PHE HB3 H 1 3.752 0.01 . 2 . . . . . . . . 5860 1 207 . 1 1 22 22 PHE HB2 H 1 3.213 0.01 . 2 . . . . . . . . 5860 1 208 . 1 1 22 22 PHE HD1 H 1 7.120 0.01 . 3 . . . . . . . . 5860 1 209 . 1 1 23 23 GLU N N 15 120.458 0.2 . 1 . . . . . . . . 5860 1 210 . 1 1 23 23 GLU H H 1 10.482 0.01 . 1 . . . . . . . . 5860 1 211 . 1 1 23 23 GLU CA C 13 61.498 0.2 . 1 . . . . . . . . 5860 1 212 . 1 1 23 23 GLU HA H 1 3.853 0.01 . 1 . . . . . . . . 5860 1 213 . 1 1 23 23 GLU CB C 13 28.737 0.2 . 1 . . . . . . . . 5860 1 214 . 1 1 23 23 GLU HB3 H 1 1.729 0.01 . 2 . . . . . . . . 5860 1 215 . 1 1 23 23 GLU HB2 H 1 1.883 0.01 . 2 . . . . . . . . 5860 1 216 . 1 1 23 23 GLU CG C 13 36.879 0.2 . 1 . . . . . . . . 5860 1 217 . 1 1 23 23 GLU HG3 H 1 2.119 0.01 . 2 . . . . . . . . 5860 1 218 . 1 1 23 23 GLU HG2 H 1 2.514 0.01 . 2 . . . . . . . . 5860 1 219 . 1 1 24 24 ILE N N 15 117.787 0.2 . 1 . . . . . . . . 5860 1 220 . 1 1 24 24 ILE H H 1 7.771 0.01 . 1 . . . . . . . . 5860 1 221 . 1 1 24 24 ILE CA C 13 63.861 0.2 . 1 . . . . . . . . 5860 1 222 . 1 1 24 24 ILE HA H 1 3.791 0.01 . 1 . . . . . . . . 5860 1 223 . 1 1 24 24 ILE CB C 13 38.086 0.2 . 1 . . . . . . . . 5860 1 224 . 1 1 24 24 ILE HB H 1 1.908 0.01 . 1 . . . . . . . . 5860 1 225 . 1 1 24 24 ILE CG1 C 13 28.629 0.2 . 1 . . . . . . . . 5860 1 226 . 1 1 24 24 ILE HG13 H 1 1.323 0.01 . 2 . . . . . . . . 5860 1 227 . 1 1 24 24 ILE HG12 H 1 1.495 0.01 . 2 . . . . . . . . 5860 1 228 . 1 1 24 24 ILE CD1 C 13 17.093 0.2 . 1 . . . . . . . . 5860 1 229 . 1 1 24 24 ILE HD11 H 1 0.947 0.01 . 1 . . . . . . . . 5860 1 230 . 1 1 24 24 ILE HD12 H 1 0.947 0.01 . 1 . . . . . . . . 5860 1 231 . 1 1 24 24 ILE HD13 H 1 0.947 0.01 . 1 . . . . . . . . 5860 1 232 . 1 1 24 24 ILE CG2 C 13 20.030 0.2 . 1 . . . . . . . . 5860 1 233 . 1 1 24 24 ILE HG21 H 1 0.905 0.01 . 1 . . . . . . . . 5860 1 234 . 1 1 24 24 ILE HG22 H 1 0.905 0.01 . 1 . . . . . . . . 5860 1 235 . 1 1 24 24 ILE HG23 H 1 0.905 0.01 . 1 . . . . . . . . 5860 1 236 . 1 1 25 25 ALA N N 15 120.818 0.2 . 1 . . . . . . . . 5860 1 237 . 1 1 25 25 ALA H H 1 8.017 0.01 . 1 . . . . . . . . 5860 1 238 . 1 1 25 25 ALA CA C 13 53.946 0.2 . 1 . . . . . . . . 5860 1 239 . 1 1 25 25 ALA HA H 1 4.116 0.01 . 1 . . . . . . . . 5860 1 240 . 1 1 25 25 ALA CB C 13 17.953 0.2 . 1 . . . . . . . . 5860 1 241 . 1 1 25 25 ALA HB1 H 1 1.440 0.01 . 1 . . . . . . . . 5860 1 242 . 1 1 25 25 ALA HB2 H 1 1.440 0.01 . 1 . . . . . . . . 5860 1 243 . 1 1 25 25 ALA HB3 H 1 1.440 0.01 . 1 . . . . . . . . 5860 1 244 . 1 1 26 26 GLY N N 15 102.808 0.2 . 1 . . . . . . . . 5860 1 245 . 1 1 26 26 GLY H H 1 8.137 0.01 . 1 . . . . . . . . 5860 1 246 . 1 1 26 26 GLY CA C 13 45.993 0.2 . 1 . . . . . . . . 5860 1 247 . 1 1 26 26 GLY HA3 H 1 3.783 0.01 . 2 . . . . . . . . 5860 1 248 . 1 1 26 26 GLY HA2 H 1 4.228 0.01 . 2 . . . . . . . . 5860 1 249 . 1 1 27 27 ALA N N 15 123.622 0.2 . 1 . . . . . . . . 5860 1 250 . 1 1 27 27 ALA H H 1 7.748 0.01 . 1 . . . . . . . . 5860 1 251 . 1 1 27 27 ALA CA C 13 54.881 0.2 . 1 . . . . . . . . 5860 1 252 . 1 1 27 27 ALA HA H 1 3.946 0.01 . 1 . . . . . . . . 5860 1 253 . 1 1 27 27 ALA CB C 13 17.850 0.2 . 1 . . . . . . . . 5860 1 254 . 1 1 27 27 ALA HB1 H 1 1.429 0.01 . 1 . . . . . . . . 5860 1 255 . 1 1 27 27 ALA HB2 H 1 1.429 0.01 . 1 . . . . . . . . 5860 1 256 . 1 1 27 27 ALA HB3 H 1 1.429 0.01 . 1 . . . . . . . . 5860 1 257 . 1 1 28 28 THR N N 15 120.253 0.2 . 1 . . . . . . . . 5860 1 258 . 1 1 28 28 THR H H 1 8.105 0.01 . 1 . . . . . . . . 5860 1 259 . 1 1 28 28 THR CA C 13 72.797 0.2 . 1 . . . . . . . . 5860 1 260 . 1 1 28 28 THR CB C 13 70.885 0.2 . 1 . . . . . . . . 5860 1 261 . 1 1 28 28 THR HB H 1 4.228 0.01 . 1 . . . . . . . . 5860 1 262 . 1 1 28 28 THR CG2 C 13 18.425 0.2 . 1 . . . . . . . . 5860 1 263 . 1 1 28 28 THR HG21 H 1 0.995 0.01 . 1 . . . . . . . . 5860 1 264 . 1 1 28 28 THR HG22 H 1 0.995 0.01 . 1 . . . . . . . . 5860 1 265 . 1 1 28 28 THR HG23 H 1 0.995 0.01 . 1 . . . . . . . . 5860 1 266 . 1 1 29 29 GLY N N 15 108.686 0.2 . 1 . . . . . . . . 5860 1 267 . 1 1 29 29 GLY H H 1 8.115 0.01 . 1 . . . . . . . . 5860 1 268 . 1 1 29 29 GLY CA C 13 46.828 0.2 . 1 . . . . . . . . 5860 1 269 . 1 1 29 29 GLY HA3 H 1 3.889 0.01 . 2 . . . . . . . . 5860 1 270 . 1 1 29 29 GLY HA2 H 1 3.808 0.01 . 2 . . . . . . . . 5860 1 271 . 1 1 30 30 LEU N N 15 120.842 0.2 . 1 . . . . . . . . 5860 1 272 . 1 1 30 30 LEU H H 1 7.616 0.01 . 1 . . . . . . . . 5860 1 273 . 1 1 30 30 LEU CA C 13 57.845 0.2 . 1 . . . . . . . . 5860 1 274 . 1 1 30 30 LEU HA H 1 3.943 0.01 . 1 . . . . . . . . 5860 1 275 . 1 1 30 30 LEU CB C 13 42.402 0.2 . 1 . . . . . . . . 5860 1 276 . 1 1 30 30 LEU HB2 H 1 1.491 0.01 . 2 . . . . . . . . 5860 1 277 . 1 1 30 30 LEU CG C 13 27.057 0.2 . 1 . . . . . . . . 5860 1 278 . 1 1 30 30 LEU HG H 1 1.840 0.01 . 1 . . . . . . . . 5860 1 279 . 1 1 30 30 LEU CD1 C 13 25.476 0.2 . 4 . . . . . . . . 5860 1 280 . 1 1 30 30 LEU HD11 H 1 0.865 0.01 . 2 . . . . . . . . 5860 1 281 . 1 1 30 30 LEU HD12 H 1 0.865 0.01 . 2 . . . . . . . . 5860 1 282 . 1 1 30 30 LEU HD13 H 1 0.865 0.01 . 2 . . . . . . . . 5860 1 283 . 1 1 30 30 LEU CD2 C 13 24.985 0.2 . 4 . . . . . . . . 5860 1 284 . 1 1 30 30 LEU HD21 H 1 0.945 0.01 . 2 . . . . . . . . 5860 1 285 . 1 1 30 30 LEU HD22 H 1 0.945 0.01 . 2 . . . . . . . . 5860 1 286 . 1 1 30 30 LEU HD23 H 1 0.945 0.01 . 2 . . . . . . . . 5860 1 287 . 1 1 31 31 PHE N N 15 122.357 0.2 . 1 . . . . . . . . 5860 1 288 . 1 1 31 31 PHE H H 1 8.430 0.01 . 1 . . . . . . . . 5860 1 289 . 1 1 31 31 PHE CA C 13 69.821 0.2 . 1 . . . . . . . . 5860 1 290 . 1 1 31 31 PHE CB C 13 42.503 0.2 . 1 . . . . . . . . 5860 1 291 . 1 1 31 31 PHE HB3 H 1 3.896 0.01 . 2 . . . . . . . . 5860 1 292 . 1 1 31 31 PHE HB2 H 1 3.323 0.01 . 2 . . . . . . . . 5860 1 293 . 1 1 31 31 PHE HD1 H 1 6.997 0.01 . 3 . . . . . . . . 5860 1 294 . 1 1 31 31 PHE HE1 H 1 7.100 0.01 . 3 . . . . . . . . 5860 1 295 . 1 1 32 32 GLY N N 15 107.682 0.2 . 1 . . . . . . . . 5860 1 296 . 1 1 32 32 GLY H H 1 8.147 0.01 . 1 . . . . . . . . 5860 1 297 . 1 1 32 32 GLY CA C 13 47.161 0.2 . 1 . . . . . . . . 5860 1 298 . 1 1 32 32 GLY HA3 H 1 3.809 0.01 . 2 . . . . . . . . 5860 1 299 . 1 1 32 32 GLY HA2 H 1 4.014 0.01 . 2 . . . . . . . . 5860 1 300 . 1 1 33 33 LEU N N 15 120.187 0.2 . 1 . . . . . . . . 5860 1 301 . 1 1 33 33 LEU H H 1 7.893 0.01 . 1 . . . . . . . . 5860 1 302 . 1 1 33 33 LEU CA C 13 57.029 0.2 . 1 . . . . . . . . 5860 1 303 . 1 1 33 33 LEU HA H 1 3.977 0.01 . 1 . . . . . . . . 5860 1 304 . 1 1 33 33 LEU CB C 13 40.867 0.2 . 1 . . . . . . . . 5860 1 305 . 1 1 33 33 LEU HB3 H 1 1.188 0.01 . 2 . . . . . . . . 5860 1 306 . 1 1 33 33 LEU HB2 H 1 1.773 0.01 . 2 . . . . . . . . 5860 1 307 . 1 1 33 33 LEU CG C 13 27.187 0.2 . 1 . . . . . . . . 5860 1 308 . 1 1 33 33 LEU HG H 1 1.634 0.01 . 1 . . . . . . . . 5860 1 309 . 1 1 33 33 LEU CD1 C 13 22.219 0.2 . 4 . . . . . . . . 5860 1 310 . 1 1 33 33 LEU HD11 H 1 0.747 0.01 . 2 . . . . . . . . 5860 1 311 . 1 1 33 33 LEU HD12 H 1 0.747 0.01 . 2 . . . . . . . . 5860 1 312 . 1 1 33 33 LEU HD13 H 1 0.747 0.01 . 2 . . . . . . . . 5860 1 313 . 1 1 33 33 LEU CD2 C 13 25.199 0.2 . 4 . . . . . . . . 5860 1 314 . 1 1 33 33 LEU HD21 H 1 0.875 0.01 . 2 . . . . . . . . 5860 1 315 . 1 1 33 33 LEU HD22 H 1 0.875 0.01 . 2 . . . . . . . . 5860 1 316 . 1 1 33 33 LEU HD23 H 1 0.875 0.01 . 2 . . . . . . . . 5860 1 317 . 1 1 34 34 TRP N N 15 114.289 0.2 . 1 . . . . . . . . 5860 1 318 . 1 1 34 34 TRP H H 1 7.124 0.01 . 1 . . . . . . . . 5860 1 319 . 1 1 34 34 TRP CA C 13 56.045 0.2 . 1 . . . . . . . . 5860 1 320 . 1 1 34 34 TRP HA H 1 4.722 0.01 . 1 . . . . . . . . 5860 1 321 . 1 1 34 34 TRP CB C 13 29.924 0.2 . 1 . . . . . . . . 5860 1 322 . 1 1 34 34 TRP HB3 H 1 3.700 0.01 . 2 . . . . . . . . 5860 1 323 . 1 1 34 34 TRP HB2 H 1 2.985 0.01 . 2 . . . . . . . . 5860 1 324 . 1 1 34 34 TRP HD1 H 1 7.243 0.01 . 1 . . . . . . . . 5860 1 325 . 1 1 34 34 TRP NE1 N 15 127.108 0.2 . 1 . . . . . . . . 5860 1 326 . 1 1 34 34 TRP HE1 H 1 10.406 0.01 . 1 . . . . . . . . 5860 1 327 . 1 1 34 34 TRP HZ2 H 1 7.050 0.01 . 1 . . . . . . . . 5860 1 328 . 1 1 34 34 TRP HH2 H 1 7.457 0.01 . 1 . . . . . . . . 5860 1 329 . 1 1 34 34 TRP HZ3 H 1 6.895 0.01 . 1 . . . . . . . . 5860 1 330 . 1 1 34 34 TRP HE3 H 1 7.050 0.01 . 1 . . . . . . . . 5860 1 331 . 1 1 35 35 GLY N N 15 105.341 0.2 . 1 . . . . . . . . 5860 1 332 . 1 1 35 35 GLY H H 1 7.813 0.01 . 1 . . . . . . . . 5860 1 333 . 1 1 35 35 GLY CA C 13 45.836 0.2 . 1 . . . . . . . . 5860 1 334 . 1 1 35 35 GLY HA3 H 1 3.664 0.01 . 2 . . . . . . . . 5860 1 335 . 1 1 35 35 GLY HA2 H 1 4.038 0.01 . 2 . . . . . . . . 5860 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 126 5860 1 1 122 5860 1 2 140 5860 1 2 136 5860 1 3 283 5860 1 3 279 5860 1 4 294 5860 1 4 293 5860 1 5 313 5860 1 5 309 5860 1 stop_ save_