data_4742 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4742 _Entry.Title ; Proton and nitrogen chemical shift assignments for the chitin-binding domain of Bacillus circulans WL-12 Chitinase A1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-05-22 _Entry.Accession_date 2000-05-23 _Entry.Last_release_date 2000-06-15 _Entry.Original_release_date 2000-06-15 _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 Takahisa Ikegami . . . 4742 2 Terumasa Okada . . . 4742 3 Masayuki Hashimoto . . . 4742 4 Shizuka Seino . . . 4742 5 Takeshi Watanabe . . . 4742 6 Masahiro Shirakawa . . . 4742 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4742 coupling_constants 1 4742 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 297 4742 '15N chemical shifts' 51 4742 'coupling constants' 36 4742 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 . . 2000-06-15 2000-05-22 original author . 4742 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4742 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20250925 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solution Structure of the Chitin-Binding Domain of Bacillus circulans WL-12 Chitinase A1 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 275 _Citation.Journal_issue 18 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 13654 _Citation.Page_last 13661 _Citation.Year 2000 _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 Takahisa Ikegami . . . 4742 1 2 Terumasa Okada . . . 4742 1 3 Masayuki Hashimoto . . . 4742 1 4 Shizuka Seino . . . 4742 1 5 Takeshi Watanabe . . . 4742 1 6 Masahiro Shirakawa . . . 4742 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'twisted beta-sandwich' 4742 1 CBD 4742 1 cellulose 4742 1 ChBD 4742 1 chitin 4742 1 'binding domain' 4742 1 ChiA1 4742 1 'chitinase A1' 4742 1 NMR 4742 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4742 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10788483 _Citation.Full_citation . _Citation.Title 'Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of biological chemistry' _Citation.Journal_volume 275 _Citation.Journal_issue 18 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0021-9258 _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 13654 _Citation.Page_last 13661 _Citation.Year 2000 _Citation.Details ; The three-dimensional structure of the chitin-binding domain (ChBD) of chitinase A1 (ChiA1) from a Gram-positive bacterium, Bacillus circulans WL-12, was determined by means of multidimensional heteronuclear NMR methods. ChiA1 is a glycosidase that hydrolyzes chitin and is composed of an N-terminal catalytic domain, two fibronectin type III-like domains, and C-terminal ChBD(ChiA1) (45 residues, Ala(655)-Gln(699)), which binds specifically to insoluble chitin. ChBD(ChiA1) has a compact and globular structure with the topology of a twisted beta-sandwich. This domain contains two antiparallel beta-sheets, one composed of three strands and the other of two strands. The core region formed by the hydrophobic and aromatic residues makes the overall structure rigid and compact. The overall topology of ChBD(ChiA1) is similar to that of the cellulose-binding domain (CBD) of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). However, ChBD(ChiA1) lacks the three aromatic residues aligned linearly and exposed to the solvent, which probably interact with cellulose in CBDs. Therefore, the binding mechanism of a group of ChBDs including ChBD(ChiA1) may be different from that proposed for CBDs. ; 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 T Ikegami T. . . 4742 2 2 T Okada T. . . 4742 2 3 M Hashimoto M. . . 4742 2 4 S Seino S. . . 4742 2 5 T Watanabe T. . . 4742 2 6 M Shirakawa M. . . 4742 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_ChBD _Assembly.Sf_category assembly _Assembly.Sf_framecode ChBD _Assembly.Entry_ID 4742 _Assembly.ID 1 _Assembly.Name ChBD-ChiA1 _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 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.2.1.14 _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 4742 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 'CHITINASE A1, Chitin-binding domain' 1 $ChiA1 . . . native . . . . . 4742 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1ED7 . 'A Chain A, Solution Structure Of The Chitin-Binding Domain Of Bacillus Circulans Wl-12 Chitinase A1' . . . . 4742 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID ChBD-ChiA1 system 4742 1 ChBD abbreviation 4742 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'chitin binding domain of a chitinase' 4742 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ChiA1 _Entity.Sf_category entity _Entity.Sf_framecode ChiA1 _Entity.Entry_ID 4742 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'CHITINASE A1' _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 ; MASMTGGGGMGRGSAWQVNT AYTAGQLVTYNGKTYKCLQP HTSLAGWEPSNVPALWQLQ ; _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 59 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 5018 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The protein has a T7 tag consisting of 14 residues (H2N-Met-Ala-Ser-Met-Thr-Gly-Gly-Gly-Gly-Met-Gly-Arg-Gly-Ser-) derived from the expression vector at its N-terminus. The calculated weight of the molecule, without the T7 tag region, is 5,018 ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 4588 . "CHITINASE A1" . . . . . 100.00 59 100.00 100.00 1.00e-33 . . . . 4742 1 2 no PDB 1ED7 . "Solution Structure Of The Chitin-Binding Domain Of Bacillus Circulans Wl-12 Chitinase A1" . . . . . 76.27 45 100.00 100.00 1.25e-23 . . . . 4742 1 3 no EMBL CAG28938 . "intein-CBD, partial [synthetic construct]" . . . . . 77.97 517 100.00 100.00 9.37e-25 . . . . 4742 1 4 no EMBL CAG28939 . "intein-CBD, partial [synthetic construct]" . . . . . 77.97 518 100.00 100.00 5.79e-25 . . . . 4742 1 5 no EMBL CDK12648 . "DnaB-Ano fusion protein [synthetic construct]" . . . . . 77.97 287 100.00 100.00 7.83e-25 . . . . 4742 1 6 no EMBL CDK12649 . "GyrA-Ano fusion protein [synthetic construct]" . . . . . 77.97 331 100.00 100.00 1.84e-24 . . . . 4742 1 7 no EMBL CDK12650 . "RIR1-Ano fusion protein [synthetic construct]" . . . . . 77.97 267 100.00 100.00 4.49e-24 . . . . 4742 1 8 no GB AAA81528 . "chitinase A1 [Bacillus circulans]" . . . . . 77.97 699 100.00 100.00 1.59e-22 . . . . 4742 1 9 no GB AAD49604 . "chitin binding domain [Expression vector pNam]" . . . . . 77.97 52 100.00 100.00 3.46e-24 . . . . 4742 1 10 no GB AAN07183 . "RNA polymerase beta prime subunit/intein-CBD fusion protein [Cloning vector pIA423]" . . . . . 77.97 1929 100.00 100.00 6.81e-25 . . . . 4742 1 11 no GB AAY41169 . "SspDnaE-C/CBD fusion protein [Expression vector pSFBAD09]" . . . . . 77.97 93 100.00 100.00 1.55e-24 . . . . 4742 1 12 no GB ABQ96889 . "glutaryl 7-aminocephalosporanic acid acylase/modified chitin binding domain fusion protein [synthetic construct]" . . . . . 77.97 746 97.83 100.00 1.47e-21 . . . . 4742 1 13 no REF WP_053782577 . "chitinase [Paenibacillus sp. A59]" . . . . . 77.97 699 97.83 97.83 5.92e-22 . . . . 4742 1 14 no SP P20533 . "RecName: Full=Chitinase A1; Flags: Precursor" . . . . . 77.97 699 100.00 100.00 1.59e-22 . . . . 4742 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'CHITINASE A1' common 4742 1 ChiA1 abbreviation 4742 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 . MET . 4742 1 2 . ALA . 4742 1 3 . SER . 4742 1 4 . MET . 4742 1 5 . THR . 4742 1 6 . GLY . 4742 1 7 . GLY . 4742 1 8 . GLY . 4742 1 9 . GLY . 4742 1 10 . MET . 4742 1 11 . GLY . 4742 1 12 . ARG . 4742 1 13 . GLY . 4742 1 14 . SER . 4742 1 15 655 ALA . 4742 1 16 656 TRP . 4742 1 17 657 GLN . 4742 1 18 658 VAL . 4742 1 19 659 ASN . 4742 1 20 660 THR . 4742 1 21 661 ALA . 4742 1 22 662 TYR . 4742 1 23 663 THR . 4742 1 24 664 ALA . 4742 1 25 665 GLY . 4742 1 26 666 GLN . 4742 1 27 667 LEU . 4742 1 28 668 VAL . 4742 1 29 669 THR . 4742 1 30 670 TYR . 4742 1 31 671 ASN . 4742 1 32 672 GLY . 4742 1 33 673 LYS . 4742 1 34 674 THR . 4742 1 35 675 TYR . 4742 1 36 676 LYS . 4742 1 37 677 CYS . 4742 1 38 678 LEU . 4742 1 39 679 GLN . 4742 1 40 680 PRO . 4742 1 41 681 HIS . 4742 1 42 682 THR . 4742 1 43 683 SER . 4742 1 44 684 LEU . 4742 1 45 685 ALA . 4742 1 46 686 GLY . 4742 1 47 687 TRP . 4742 1 48 688 GLU . 4742 1 49 689 PRO . 4742 1 50 690 SER . 4742 1 51 691 ASN . 4742 1 52 692 VAL . 4742 1 53 693 PRO . 4742 1 54 694 ALA . 4742 1 55 695 LEU . 4742 1 56 696 TRP . 4742 1 57 697 GLN . 4742 1 58 698 LEU . 4742 1 59 699 GLN . 4742 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 . MET 1 1 4742 1 . ALA 2 2 4742 1 . SER 3 3 4742 1 . MET 4 4 4742 1 . THR 5 5 4742 1 . GLY 6 6 4742 1 . GLY 7 7 4742 1 . GLY 8 8 4742 1 . GLY 9 9 4742 1 . MET 10 10 4742 1 . GLY 11 11 4742 1 . ARG 12 12 4742 1 . GLY 13 13 4742 1 . SER 14 14 4742 1 . ALA 15 15 4742 1 . TRP 16 16 4742 1 . GLN 17 17 4742 1 . VAL 18 18 4742 1 . ASN 19 19 4742 1 . THR 20 20 4742 1 . ALA 21 21 4742 1 . TYR 22 22 4742 1 . THR 23 23 4742 1 . ALA 24 24 4742 1 . GLY 25 25 4742 1 . GLN 26 26 4742 1 . LEU 27 27 4742 1 . VAL 28 28 4742 1 . THR 29 29 4742 1 . TYR 30 30 4742 1 . ASN 31 31 4742 1 . GLY 32 32 4742 1 . LYS 33 33 4742 1 . THR 34 34 4742 1 . TYR 35 35 4742 1 . LYS 36 36 4742 1 . CYS 37 37 4742 1 . LEU 38 38 4742 1 . GLN 39 39 4742 1 . PRO 40 40 4742 1 . HIS 41 41 4742 1 . THR 42 42 4742 1 . SER 43 43 4742 1 . LEU 44 44 4742 1 . ALA 45 45 4742 1 . GLY 46 46 4742 1 . TRP 47 47 4742 1 . GLU 48 48 4742 1 . PRO 49 49 4742 1 . SER 50 50 4742 1 . ASN 51 51 4742 1 . VAL 52 52 4742 1 . PRO 53 53 4742 1 . ALA 54 54 4742 1 . LEU 55 55 4742 1 . TRP 56 56 4742 1 . GLN 57 57 4742 1 . LEU 58 58 4742 1 . GLN 59 59 4742 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 4742 _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 $ChiA1 . 1397 organism . 'Bacillus circulans' 'soil bacteria' . . Eubacteria . Bacillus circulans WL12 . . . . . . . . . . . . . . . chiA1 . . . . 4742 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 4742 _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 $ChiA1 . 'recombinant technology' 'Escherichia coli' Bacteria . . Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . PET3A . . . . . . 4742 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4742 _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 'CHITINASE A1' [U-15N] . . 1 $ChiA1 . . 2.0 . . mM . . . . 4742 1 2 KH2PO4-K2HPO4 . . . . . . . 10 . . mM . . . . 4742 1 3 DTT [U-2H] . . . . . . 10 . . mM . . . . 4742 1 4 H2O . . . . . . . 90 . . % . . . . 4742 1 5 D2O . . . . . . . 10 . . % . . . . 4742 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4742 _Sample.ID 2 _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 'CHITINASE A1' [U-15N] . . 1 $ChiA1 . . 1.2 . . mM . . . . 4742 2 2 KH2PO4-K2HPO4 . . . . . . . 100 . . mM . . . . 4742 2 3 DTT [U-2H] . . . . . . 10 . . mM . . . . 4742 2 4 D2O . . . . . . . 99.8 . . % . . . . 4742 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 4742 _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 6.0 0.1 n/a 4742 1 temperature 310 0.5 K 4742 1 'ionic strength' 10 . mM 4742 1 stop_ save_ save_sample_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_2 _Sample_condition_list.Entry_ID 4742 _Sample_condition_list.ID 2 _Sample_condition_list.Details 'Samples adjusted to pH 6.0 in H2O was lyophilized and then dissolved in the same amount of D2O.' 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 6.0 0.1 n/a 4742 2 temperature 310 0.5 K 4742 2 'ionic strength' 100 . mM 4742 2 stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 4742 _Software.ID 1 _Software.Name X-PLOR _Software.Version 3.851 _Software.Details Brunger loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 4742 1 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 4742 _Software.ID 2 _Software.Name DYANA _Software.Version 1.5 _Software.Details Guentert loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 4742 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4742 _Software.ID 3 _Software.Name NMRPipe _Software.Version 1.7 _Software.Details Delaglio loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 4742 3 stop_ save_ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 4742 _Software.ID 4 _Software.Name XWINNMR _Software.Version 2.0 _Software.Details Bruker loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 4742 4 stop_ save_ save_nmrPipp _Software.Sf_category software _Software.Sf_framecode nmrPipp _Software.Entry_ID 4742 _Software.ID 5 _Software.Name nmrPipp _Software.Version 4.2.4 _Software.Details Garrett loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 4742 5 stop_ save_ save_Molmol _Software.Sf_category software _Software.Sf_framecode Molmol _Software.Entry_ID 4742 _Software.ID 6 _Software.Name Molmol _Software.Version 2.3 _Software.Details Koradi loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure analysis' 4742 6 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 4742 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4742 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4742 _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 Bruker DRX . 800 . . . 4742 1 2 NMR_spectrometer_2 Bruker DRX . 500 . . . 4742 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 4742 _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 NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4742 1 2 '3D 15N-separated_NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4742 1 3 HMQC-J . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4742 1 4 '3D (H)NNH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4742 1 5 '2D H(NN)H-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4742 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4742 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D NOESY' _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4742 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D 15N-separated_NOESY' _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4742 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HMQC-J _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4742 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D (H)NNH-TOCSY' _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4742 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '2D H(NN)H-TOCSY' _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 . _NMR_spec_expt.Software_label . _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 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4742 _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 external direct . external_to_the_sample cylindrical parallel_to_Bo . . . . . . 4742 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4742 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_chemical_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4742 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_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 . 4742 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 15 15 ALA H H 1 8.36 0.03 . 1 . . . . . . . . 4742 1 2 . 1 1 15 15 ALA HA H 1 4.69 0.03 . 1 . . . . . . . . 4742 1 3 . 1 1 15 15 ALA HB1 H 1 1.52 0.03 . 1 . . . . . . . . 4742 1 4 . 1 1 15 15 ALA HB2 H 1 1.52 0.03 . 1 . . . . . . . . 4742 1 5 . 1 1 15 15 ALA HB3 H 1 1.52 0.03 . 1 . . . . . . . . 4742 1 6 . 1 1 15 15 ALA N N 15 125.17 0.25 . 1 . . . . . . . . 4742 1 7 . 1 1 16 16 TRP H H 1 8.93 0.03 . 1 . . . . . . . . 4742 1 8 . 1 1 16 16 TRP HA H 1 4.29 0.03 . 1 . . . . . . . . 4742 1 9 . 1 1 16 16 TRP HB2 H 1 3.27 0.03 . 2 . . . . . . . . 4742 1 10 . 1 1 16 16 TRP HB3 H 1 2.64 0.03 . 2 . . . . . . . . 4742 1 11 . 1 1 16 16 TRP HE1 H 1 11.12 0.03 . 1 . . . . . . . . 4742 1 12 . 1 1 16 16 TRP HD1 H 1 6.30 0.03 . 1 . . . . . . . . 4742 1 13 . 1 1 16 16 TRP HH2 H 1 7.07 0.03 . 1 . . . . . . . . 4742 1 14 . 1 1 16 16 TRP HE3 H 1 7.46 0.03 . 1 . . . . . . . . 4742 1 15 . 1 1 16 16 TRP N N 15 125.36 0.25 . 1 . . . . . . . . 4742 1 16 . 1 1 16 16 TRP NE1 N 15 130.21 0.25 . 1 . . . . . . . . 4742 1 17 . 1 1 17 17 GLN H H 1 7.59 0.03 . 1 . . . . . . . . 4742 1 18 . 1 1 17 17 GLN HA H 1 4.38 0.03 . 1 . . . . . . . . 4742 1 19 . 1 1 17 17 GLN HB2 H 1 1.71 0.03 . 2 . . . . . . . . 4742 1 20 . 1 1 17 17 GLN HB3 H 1 1.93 0.03 . 2 . . . . . . . . 4742 1 21 . 1 1 17 17 GLN HG2 H 1 2.34 0.03 . 1 . . . . . . . . 4742 1 22 . 1 1 17 17 GLN HG3 H 1 2.34 0.03 . 1 . . . . . . . . 4742 1 23 . 1 1 17 17 GLN HE21 H 1 6.79 0.03 . 2 . . . . . . . . 4742 1 24 . 1 1 17 17 GLN HE22 H 1 7.36 0.03 . 2 . . . . . . . . 4742 1 25 . 1 1 17 17 GLN N N 15 125.35 0.25 . 1 . . . . . . . . 4742 1 26 . 1 1 17 17 GLN NE2 N 15 111.91 0.25 . 1 . . . . . . . . 4742 1 27 . 1 1 18 18 VAL H H 1 7.87 0.03 . 1 . . . . . . . . 4742 1 28 . 1 1 18 18 VAL HA H 1 3.24 0.03 . 1 . . . . . . . . 4742 1 29 . 1 1 18 18 VAL HB H 1 1.96 0.03 . 1 . . . . . . . . 4742 1 30 . 1 1 18 18 VAL HG11 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 31 . 1 1 18 18 VAL HG12 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 32 . 1 1 18 18 VAL HG13 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 33 . 1 1 18 18 VAL HG21 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 34 . 1 1 18 18 VAL HG22 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 35 . 1 1 18 18 VAL HG23 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 36 . 1 1 18 18 VAL N N 15 119.02 0.25 . 1 . . . . . . . . 4742 1 37 . 1 1 19 19 ASN H H 1 7.57 0.03 . 1 . . . . . . . . 4742 1 38 . 1 1 19 19 ASN HA H 1 4.39 0.03 . 1 . . . . . . . . 4742 1 39 . 1 1 19 19 ASN HB2 H 1 3.04 0.03 . 2 . . . . . . . . 4742 1 40 . 1 1 19 19 ASN HB3 H 1 2.70 0.03 . 2 . . . . . . . . 4742 1 41 . 1 1 19 19 ASN HD21 H 1 7.52 0.03 . 2 . . . . . . . . 4742 1 42 . 1 1 19 19 ASN HD22 H 1 6.73 0.03 . 2 . . . . . . . . 4742 1 43 . 1 1 19 19 ASN N N 15 122.94 0.25 . 1 . . . . . . . . 4742 1 44 . 1 1 19 19 ASN ND2 N 15 112.09 0.25 . 1 . . . . . . . . 4742 1 45 . 1 1 20 20 THR H H 1 8.26 0.03 . 1 . . . . . . . . 4742 1 46 . 1 1 20 20 THR HA H 1 4.18 0.03 . 1 . . . . . . . . 4742 1 47 . 1 1 20 20 THR HB H 1 3.36 0.03 . 1 . . . . . . . . 4742 1 48 . 1 1 20 20 THR HG21 H 1 0.45 0.03 . 1 . . . . . . . . 4742 1 49 . 1 1 20 20 THR HG22 H 1 0.45 0.03 . 1 . . . . . . . . 4742 1 50 . 1 1 20 20 THR HG23 H 1 0.45 0.03 . 1 . . . . . . . . 4742 1 51 . 1 1 20 20 THR N N 15 115.05 0.25 . 1 . . . . . . . . 4742 1 52 . 1 1 21 21 ALA H H 1 8.24 0.03 . 1 . . . . . . . . 4742 1 53 . 1 1 21 21 ALA HA H 1 4.54 0.03 . 1 . . . . . . . . 4742 1 54 . 1 1 21 21 ALA HB1 H 1 1.21 0.03 . 1 . . . . . . . . 4742 1 55 . 1 1 21 21 ALA HB2 H 1 1.21 0.03 . 1 . . . . . . . . 4742 1 56 . 1 1 21 21 ALA HB3 H 1 1.21 0.03 . 1 . . . . . . . . 4742 1 57 . 1 1 21 21 ALA N N 15 129.51 0.25 . 1 . . . . . . . . 4742 1 58 . 1 1 22 22 TYR H H 1 8.72 0.03 . 1 . . . . . . . . 4742 1 59 . 1 1 22 22 TYR HA H 1 5.13 0.03 . 1 . . . . . . . . 4742 1 60 . 1 1 22 22 TYR HB2 H 1 3.15 0.03 . 2 . . . . . . . . 4742 1 61 . 1 1 22 22 TYR HB3 H 1 2.23 0.03 . 2 . . . . . . . . 4742 1 62 . 1 1 22 22 TYR HD1 H 1 7.17 0.03 . 3 . . . . . . . . 4742 1 63 . 1 1 22 22 TYR HE1 H 1 6.74 0.03 . 3 . . . . . . . . 4742 1 64 . 1 1 22 22 TYR N N 15 124.37 0.25 . 1 . . . . . . . . 4742 1 65 . 1 1 23 23 THR H H 1 8.74 0.03 . 1 . . . . . . . . 4742 1 66 . 1 1 23 23 THR HA H 1 4.50 0.03 . 1 . . . . . . . . 4742 1 67 . 1 1 23 23 THR HB H 1 4.30 0.03 . 1 . . . . . . . . 4742 1 68 . 1 1 23 23 THR HG21 H 1 1.25 0.03 . 1 . . . . . . . . 4742 1 69 . 1 1 23 23 THR HG22 H 1 1.25 0.03 . 1 . . . . . . . . 4742 1 70 . 1 1 23 23 THR HG23 H 1 1.25 0.03 . 1 . . . . . . . . 4742 1 71 . 1 1 23 23 THR N N 15 114.00 0.25 . 1 . . . . . . . . 4742 1 72 . 1 1 24 24 ALA H H 1 8.30 0.03 . 1 . . . . . . . . 4742 1 73 . 1 1 24 24 ALA HA H 1 3.67 0.03 . 1 . . . . . . . . 4742 1 74 . 1 1 24 24 ALA HB1 H 1 1.27 0.03 . 1 . . . . . . . . 4742 1 75 . 1 1 24 24 ALA HB2 H 1 1.27 0.03 . 1 . . . . . . . . 4742 1 76 . 1 1 24 24 ALA HB3 H 1 1.27 0.03 . 1 . . . . . . . . 4742 1 77 . 1 1 24 24 ALA N N 15 123.30 0.25 . 1 . . . . . . . . 4742 1 78 . 1 1 25 25 GLY H H 1 9.31 0.03 . 1 . . . . . . . . 4742 1 79 . 1 1 25 25 GLY HA2 H 1 3.41 0.03 . 1 . . . . . . . . 4742 1 80 . 1 1 25 25 GLY HA3 H 1 4.55 0.03 . 2 . . . . . . . . 4742 1 81 . 1 1 25 25 GLY N N 15 111.67 0.25 . 1 . . . . . . . . 4742 1 82 . 1 1 26 26 GLN H H 1 7.78 0.03 . 1 . . . . . . . . 4742 1 83 . 1 1 26 26 GLN HA H 1 4.31 0.03 . 1 . . . . . . . . 4742 1 84 . 1 1 26 26 GLN HB2 H 1 2.27 0.03 . 2 . . . . . . . . 4742 1 85 . 1 1 26 26 GLN HB3 H 1 2.50 0.03 . 2 . . . . . . . . 4742 1 86 . 1 1 26 26 GLN HG2 H 1 2.63 0.03 . 2 . . . . . . . . 4742 1 87 . 1 1 26 26 GLN HG3 H 1 2.77 0.03 . 2 . . . . . . . . 4742 1 88 . 1 1 26 26 GLN HE21 H 1 7.15 0.03 . 2 . . . . . . . . 4742 1 89 . 1 1 26 26 GLN HE22 H 1 7.78 0.03 . 2 . . . . . . . . 4742 1 90 . 1 1 26 26 GLN N N 15 121.11 0.25 . 1 . . . . . . . . 4742 1 91 . 1 1 26 26 GLN NE2 N 15 110.55 0.25 . 1 . . . . . . . . 4742 1 92 . 1 1 27 27 LEU H H 1 8.66 0.03 . 1 . . . . . . . . 4742 1 93 . 1 1 27 27 LEU HA H 1 5.86 0.03 . 1 . . . . . . . . 4742 1 94 . 1 1 27 27 LEU HB2 H 1 1.89 0.03 . 2 . . . . . . . . 4742 1 95 . 1 1 27 27 LEU HB3 H 1 1.33 0.03 . 2 . . . . . . . . 4742 1 96 . 1 1 27 27 LEU HD11 H 1 0.97 0.03 . 1 . . . . . . . . 4742 1 97 . 1 1 27 27 LEU HD12 H 1 0.97 0.03 . 1 . . . . . . . . 4742 1 98 . 1 1 27 27 LEU HD13 H 1 0.97 0.03 . 1 . . . . . . . . 4742 1 99 . 1 1 27 27 LEU HD21 H 1 0.90 0.03 . 1 . . . . . . . . 4742 1 100 . 1 1 27 27 LEU HD22 H 1 0.90 0.03 . 1 . . . . . . . . 4742 1 101 . 1 1 27 27 LEU HD23 H 1 0.90 0.03 . 1 . . . . . . . . 4742 1 102 . 1 1 27 27 LEU N N 15 123.79 0.25 . 1 . . . . . . . . 4742 1 103 . 1 1 28 28 VAL H H 1 9.20 0.03 . 1 . . . . . . . . 4742 1 104 . 1 1 28 28 VAL HA H 1 5.53 0.03 . 1 . . . . . . . . 4742 1 105 . 1 1 28 28 VAL HB H 1 2.33 0.03 . 1 . . . . . . . . 4742 1 106 . 1 1 28 28 VAL HG11 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 107 . 1 1 28 28 VAL HG12 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 108 . 1 1 28 28 VAL HG13 H 1 0.94 0.03 . 1 . . . . . . . . 4742 1 109 . 1 1 28 28 VAL HG21 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 110 . 1 1 28 28 VAL HG22 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 111 . 1 1 28 28 VAL HG23 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 112 . 1 1 28 28 VAL N N 15 114.95 0.25 . 1 . . . . . . . . 4742 1 113 . 1 1 29 29 THR H H 1 8.38 0.03 . 1 . . . . . . . . 4742 1 114 . 1 1 29 29 THR HA H 1 5.60 0.03 . 1 . . . . . . . . 4742 1 115 . 1 1 29 29 THR HB H 1 4.01 0.03 . 1 . . . . . . . . 4742 1 116 . 1 1 29 29 THR HG21 H 1 1.13 0.03 . 1 . . . . . . . . 4742 1 117 . 1 1 29 29 THR HG22 H 1 1.13 0.03 . 1 . . . . . . . . 4742 1 118 . 1 1 29 29 THR HG23 H 1 1.13 0.03 . 1 . . . . . . . . 4742 1 119 . 1 1 29 29 THR N N 15 112.03 0.25 . 1 . . . . . . . . 4742 1 120 . 1 1 30 30 TYR H H 1 9.39 0.03 . 1 . . . . . . . . 4742 1 121 . 1 1 30 30 TYR HA H 1 4.77 0.03 . 1 . . . . . . . . 4742 1 122 . 1 1 30 30 TYR HB2 H 1 2.69 0.03 . 2 . . . . . . . . 4742 1 123 . 1 1 30 30 TYR HB3 H 1 2.48 0.03 . 2 . . . . . . . . 4742 1 124 . 1 1 30 30 TYR HD1 H 1 7.01 0.03 . 3 . . . . . . . . 4742 1 125 . 1 1 30 30 TYR HE1 H 1 6.79 0.03 . 3 . . . . . . . . 4742 1 126 . 1 1 30 30 TYR N N 15 122.42 0.25 . 1 . . . . . . . . 4742 1 127 . 1 1 31 31 ASN HD21 H 1 6.52 0.03 . 2 . . . . . . . . 4742 1 128 . 1 1 31 31 ASN HD22 H 1 7.04 0.03 . 2 . . . . . . . . 4742 1 129 . 1 1 31 31 ASN ND2 N 15 109.90 0.25 . 1 . . . . . . . . 4742 1 130 . 1 1 32 32 GLY HA2 H 1 3.63 0.03 . 2 . . . . . . . . 4742 1 131 . 1 1 32 32 GLY HA3 H 1 4.16 0.03 . 2 . . . . . . . . 4742 1 132 . 1 1 33 33 LYS H H 1 7.63 0.03 . 1 . . . . . . . . 4742 1 133 . 1 1 33 33 LYS HA H 1 4.68 0.03 . 1 . . . . . . . . 4742 1 134 . 1 1 33 33 LYS HB2 H 1 1.76 0.03 . 1 . . . . . . . . 4742 1 135 . 1 1 33 33 LYS HB3 H 1 1.76 0.03 . 1 . . . . . . . . 4742 1 136 . 1 1 33 33 LYS HG2 H 1 1.43 0.03 . 1 . . . . . . . . 4742 1 137 . 1 1 33 33 LYS HG3 H 1 1.43 0.03 . 1 . . . . . . . . 4742 1 138 . 1 1 33 33 LYS HD2 H 1 1.60 0.03 . 1 . . . . . . . . 4742 1 139 . 1 1 33 33 LYS HD3 H 1 1.60 0.03 . 1 . . . . . . . . 4742 1 140 . 1 1 33 33 LYS HE2 H 1 3.07 0.03 . 1 . . . . . . . . 4742 1 141 . 1 1 33 33 LYS HE3 H 1 3.07 0.03 . 1 . . . . . . . . 4742 1 142 . 1 1 33 33 LYS N N 15 120.52 0.25 . 1 . . . . . . . . 4742 1 143 . 1 1 34 34 THR H H 1 8.72 0.03 . 1 . . . . . . . . 4742 1 144 . 1 1 34 34 THR HA H 1 5.13 0.03 . 1 . . . . . . . . 4742 1 145 . 1 1 34 34 THR HB H 1 3.87 0.03 . 1 . . . . . . . . 4742 1 146 . 1 1 34 34 THR HG21 H 1 1.22 0.03 . 1 . . . . . . . . 4742 1 147 . 1 1 34 34 THR HG22 H 1 1.22 0.03 . 1 . . . . . . . . 4742 1 148 . 1 1 34 34 THR HG23 H 1 1.22 0.03 . 1 . . . . . . . . 4742 1 149 . 1 1 34 34 THR N N 15 118.17 0.25 . 1 . . . . . . . . 4742 1 150 . 1 1 35 35 TYR H H 1 9.37 0.03 . 1 . . . . . . . . 4742 1 151 . 1 1 35 35 TYR HA H 1 5.33 0.03 . 1 . . . . . . . . 4742 1 152 . 1 1 35 35 TYR HB2 H 1 2.89 0.03 . 2 . . . . . . . . 4742 1 153 . 1 1 35 35 TYR HB3 H 1 2.44 0.03 . 2 . . . . . . . . 4742 1 154 . 1 1 35 35 TYR HD1 H 1 6.69 0.03 . 3 . . . . . . . . 4742 1 155 . 1 1 35 35 TYR HE1 H 1 6.87 0.03 . 3 . . . . . . . . 4742 1 156 . 1 1 35 35 TYR N N 15 122.42 0.25 . 1 . . . . . . . . 4742 1 157 . 1 1 36 36 LYS H H 1 9.35 0.03 . 1 . . . . . . . . 4742 1 158 . 1 1 36 36 LYS HA H 1 5.39 0.03 . 1 . . . . . . . . 4742 1 159 . 1 1 36 36 LYS HB2 H 1 1.86 0.03 . 2 . . . . . . . . 4742 1 160 . 1 1 36 36 LYS HB3 H 1 1.72 0.03 . 2 . . . . . . . . 4742 1 161 . 1 1 36 36 LYS HG2 H 1 1.29 0.03 . 1 . . . . . . . . 4742 1 162 . 1 1 36 36 LYS HG3 H 1 1.29 0.03 . 1 . . . . . . . . 4742 1 163 . 1 1 36 36 LYS HD2 H 1 1.52 0.03 . 1 . . . . . . . . 4742 1 164 . 1 1 36 36 LYS HD3 H 1 1.52 0.03 . 1 . . . . . . . . 4742 1 165 . 1 1 36 36 LYS HE2 H 1 2.96 0.03 . 1 . . . . . . . . 4742 1 166 . 1 1 36 36 LYS HE3 H 1 2.96 0.03 . 1 . . . . . . . . 4742 1 167 . 1 1 36 36 LYS N N 15 121.59 0.25 . 1 . . . . . . . . 4742 1 168 . 1 1 37 37 CYS H H 1 9.48 0.03 . 1 . . . . . . . . 4742 1 169 . 1 1 37 37 CYS HA H 1 3.64 0.03 . 1 . . . . . . . . 4742 1 170 . 1 1 37 37 CYS HB2 H 1 2.86 0.03 . 2 . . . . . . . . 4742 1 171 . 1 1 37 37 CYS HB3 H 1 2.56 0.03 . 2 . . . . . . . . 4742 1 172 . 1 1 37 37 CYS N N 15 129.28 0.25 . 1 . . . . . . . . 4742 1 173 . 1 1 38 38 LEU H H 1 8.97 0.03 . 1 . . . . . . . . 4742 1 174 . 1 1 38 38 LEU HA H 1 4.42 0.03 . 1 . . . . . . . . 4742 1 175 . 1 1 38 38 LEU HB2 H 1 1.59 0.03 . 2 . . . . . . . . 4742 1 176 . 1 1 38 38 LEU HB3 H 1 1.47 0.03 . 2 . . . . . . . . 4742 1 177 . 1 1 38 38 LEU HD11 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 178 . 1 1 38 38 LEU HD12 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 179 . 1 1 38 38 LEU HD13 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 180 . 1 1 38 38 LEU HD21 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 181 . 1 1 38 38 LEU HD22 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 182 . 1 1 38 38 LEU HD23 H 1 0.81 0.03 . 1 . . . . . . . . 4742 1 183 . 1 1 38 38 LEU N N 15 130.58 0.25 . 1 . . . . . . . . 4742 1 184 . 1 1 39 39 GLN H H 1 7.02 0.03 . 1 . . . . . . . . 4742 1 185 . 1 1 39 39 GLN HA H 1 4.93 0.03 . 1 . . . . . . . . 4742 1 186 . 1 1 39 39 GLN HB2 H 1 1.98 0.03 . 2 . . . . . . . . 4742 1 187 . 1 1 39 39 GLN HB3 H 1 1.75 0.03 . 2 . . . . . . . . 4742 1 188 . 1 1 39 39 GLN HG2 H 1 2.27 0.03 . 1 . . . . . . . . 4742 1 189 . 1 1 39 39 GLN HG3 H 1 2.27 0.03 . 1 . . . . . . . . 4742 1 190 . 1 1 39 39 GLN HE21 H 1 6.79 0.03 . 2 . . . . . . . . 4742 1 191 . 1 1 39 39 GLN HE22 H 1 7.19 0.03 . 2 . . . . . . . . 4742 1 192 . 1 1 39 39 GLN N N 15 116.87 0.25 . 1 . . . . . . . . 4742 1 193 . 1 1 39 39 GLN NE2 N 15 110.86 0.25 . 1 . . . . . . . . 4742 1 194 . 1 1 40 40 PRO HA H 1 4.69 0.03 . 1 . . . . . . . . 4742 1 195 . 1 1 40 40 PRO HB2 H 1 2.19 0.03 . 2 . . . . . . . . 4742 1 196 . 1 1 40 40 PRO HB3 H 1 2.32 0.03 . 2 . . . . . . . . 4742 1 197 . 1 1 40 40 PRO HG2 H 1 1.27 0.03 . 1 . . . . . . . . 4742 1 198 . 1 1 40 40 PRO HG3 H 1 1.27 0.03 . 1 . . . . . . . . 4742 1 199 . 1 1 40 40 PRO HD2 H 1 3.67 0.03 . 2 . . . . . . . . 4742 1 200 . 1 1 40 40 PRO HD3 H 1 3.96 0.03 . 2 . . . . . . . . 4742 1 201 . 1 1 41 41 HIS H H 1 8.28 0.03 . 1 . . . . . . . . 4742 1 202 . 1 1 41 41 HIS HA H 1 4.84 0.03 . 1 . . . . . . . . 4742 1 203 . 1 1 41 41 HIS HB2 H 1 3.43 0.03 . 2 . . . . . . . . 4742 1 204 . 1 1 41 41 HIS HB3 H 1 3.28 0.03 . 2 . . . . . . . . 4742 1 205 . 1 1 41 41 HIS HD2 H 1 7.03 0.03 . 1 . . . . . . . . 4742 1 206 . 1 1 41 41 HIS HE1 H 1 7.23 0.03 . 1 . . . . . . . . 4742 1 207 . 1 1 41 41 HIS N N 15 117.71 0.25 . 1 . . . . . . . . 4742 1 208 . 1 1 42 42 THR H H 1 8.52 0.03 . 1 . . . . . . . . 4742 1 209 . 1 1 42 42 THR HA H 1 5.05 0.03 . 1 . . . . . . . . 4742 1 210 . 1 1 42 42 THR HB H 1 3.97 0.03 . 1 . . . . . . . . 4742 1 211 . 1 1 42 42 THR HG21 H 1 1.05 0.03 . 1 . . . . . . . . 4742 1 212 . 1 1 42 42 THR HG22 H 1 1.05 0.03 . 1 . . . . . . . . 4742 1 213 . 1 1 42 42 THR HG23 H 1 1.05 0.03 . 1 . . . . . . . . 4742 1 214 . 1 1 42 42 THR N N 15 116.85 0.25 . 1 . . . . . . . . 4742 1 215 . 1 1 43 43 SER H H 1 9.45 0.03 . 1 . . . . . . . . 4742 1 216 . 1 1 43 43 SER HA H 1 4.78 0.03 . 1 . . . . . . . . 4742 1 217 . 1 1 43 43 SER HB2 H 1 4.54 0.03 . 2 . . . . . . . . 4742 1 218 . 1 1 43 43 SER HB3 H 1 4.65 0.03 . 2 . . . . . . . . 4742 1 219 . 1 1 43 43 SER N N 15 124.09 0.25 . 1 . . . . . . . . 4742 1 220 . 1 1 44 44 LEU H H 1 6.79 0.03 . 1 . . . . . . . . 4742 1 221 . 1 1 44 44 LEU HA H 1 4.70 0.03 . 1 . . . . . . . . 4742 1 222 . 1 1 44 44 LEU HB2 H 1 1.40 0.03 . 1 . . . . . . . . 4742 1 223 . 1 1 44 44 LEU HB3 H 1 1.40 0.03 . 1 . . . . . . . . 4742 1 224 . 1 1 44 44 LEU HG H 1 0.89 0.03 . 1 . . . . . . . . 4742 1 225 . 1 1 44 44 LEU HD21 H 1 0.65 0.03 . 1 . . . . . . . . 4742 1 226 . 1 1 44 44 LEU HD22 H 1 0.65 0.03 . 1 . . . . . . . . 4742 1 227 . 1 1 44 44 LEU HD23 H 1 0.65 0.03 . 1 . . . . . . . . 4742 1 228 . 1 1 44 44 LEU HD11 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 229 . 1 1 44 44 LEU HD12 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 230 . 1 1 44 44 LEU HD13 H 1 0.29 0.03 . 1 . . . . . . . . 4742 1 231 . 1 1 44 44 LEU N N 15 118.25 0.25 . 1 . . . . . . . . 4742 1 232 . 1 1 45 45 ALA H H 1 8.61 0.03 . 1 . . . . . . . . 4742 1 233 . 1 1 45 45 ALA HA H 1 4.44 0.03 . 1 . . . . . . . . 4742 1 234 . 1 1 45 45 ALA HB1 H 1 1.51 0.03 . 1 . . . . . . . . 4742 1 235 . 1 1 45 45 ALA HB2 H 1 1.51 0.03 . 1 . . . . . . . . 4742 1 236 . 1 1 45 45 ALA HB3 H 1 1.51 0.03 . 1 . . . . . . . . 4742 1 237 . 1 1 45 45 ALA N N 15 124.72 0.25 . 1 . . . . . . . . 4742 1 238 . 1 1 46 46 GLY H H 1 9.54 0.03 . 1 . . . . . . . . 4742 1 239 . 1 1 46 46 GLY HA2 H 1 4.52 0.03 . 2 . . . . . . . . 4742 1 240 . 1 1 46 46 GLY HA3 H 1 3.97 0.03 . 2 . . . . . . . . 4742 1 241 . 1 1 46 46 GLY N N 15 114.78 0.25 . 1 . . . . . . . . 4742 1 242 . 1 1 47 47 TRP H H 1 8.46 0.03 . 1 . . . . . . . . 4742 1 243 . 1 1 47 47 TRP HA H 1 5.11 0.03 . 1 . . . . . . . . 4742 1 244 . 1 1 47 47 TRP HB2 H 1 3.81 0.03 . 2 . . . . . . . . 4742 1 245 . 1 1 47 47 TRP HB3 H 1 3.54 0.03 . 2 . . . . . . . . 4742 1 246 . 1 1 47 47 TRP HE1 H 1 10.04 0.03 . 1 . . . . . . . . 4742 1 247 . 1 1 47 47 TRP HD1 H 1 7.05 0.03 . 1 . . . . . . . . 4742 1 248 . 1 1 47 47 TRP HZ2 H 1 7.51 0.03 . 1 . . . . . . . . 4742 1 249 . 1 1 47 47 TRP HH2 H 1 7.32 0.03 . 1 . . . . . . . . 4742 1 250 . 1 1 47 47 TRP HZ3 H 1 7.25 0.03 . 1 . . . . . . . . 4742 1 251 . 1 1 47 47 TRP HE3 H 1 7.66 0.03 . 1 . . . . . . . . 4742 1 252 . 1 1 47 47 TRP N N 15 121.76 0.25 . 1 . . . . . . . . 4742 1 253 . 1 1 47 47 TRP NE1 N 15 127.55 0.25 . 1 . . . . . . . . 4742 1 254 . 1 1 48 48 GLU H H 1 8.68 0.03 . 1 . . . . . . . . 4742 1 255 . 1 1 48 48 GLU HA H 1 4.47 0.03 . 1 . . . . . . . . 4742 1 256 . 1 1 48 48 GLU HB2 H 1 0.12 0.03 . 2 . . . . . . . . 4742 1 257 . 1 1 48 48 GLU HB3 H 1 1.23 0.03 . 2 . . . . . . . . 4742 1 258 . 1 1 48 48 GLU HG2 H 1 1.47 0.03 . 2 . . . . . . . . 4742 1 259 . 1 1 48 48 GLU HG3 H 1 2.19 0.03 . 2 . . . . . . . . 4742 1 260 . 1 1 48 48 GLU N N 15 120.02 0.25 . 1 . . . . . . . . 4742 1 261 . 1 1 49 49 PRO HD2 H 1 3.79 0.03 . 2 . . . . . . . . 4742 1 262 . 1 1 49 49 PRO HD3 H 1 4.05 0.03 . 2 . . . . . . . . 4742 1 263 . 1 1 50 50 SER H H 1 5.62 0.03 . 1 . . . . . . . . 4742 1 264 . 1 1 50 50 SER HA H 1 3.97 0.03 . 1 . . . . . . . . 4742 1 265 . 1 1 50 50 SER HB2 H 1 3.81 0.03 . 2 . . . . . . . . 4742 1 266 . 1 1 50 50 SER HB3 H 1 4.06 0.03 . 2 . . . . . . . . 4742 1 267 . 1 1 50 50 SER N N 15 102.76 0.25 . 1 . . . . . . . . 4742 1 268 . 1 1 51 51 ASN H H 1 7.94 0.03 . 1 . . . . . . . . 4742 1 269 . 1 1 51 51 ASN HA H 1 4.98 0.03 . 1 . . . . . . . . 4742 1 270 . 1 1 51 51 ASN HB2 H 1 2.98 0.03 . 2 . . . . . . . . 4742 1 271 . 1 1 51 51 ASN HB3 H 1 2.75 0.03 . 2 . . . . . . . . 4742 1 272 . 1 1 51 51 ASN HD21 H 1 6.88 0.03 . 2 . . . . . . . . 4742 1 273 . 1 1 51 51 ASN HD22 H 1 7.51 0.03 . 2 . . . . . . . . 4742 1 274 . 1 1 51 51 ASN N N 15 117.95 0.25 . 1 . . . . . . . . 4742 1 275 . 1 1 51 51 ASN ND2 N 15 114.45 0.25 . 1 . . . . . . . . 4742 1 276 . 1 1 52 52 VAL H H 1 6.72 0.03 . 1 . . . . . . . . 4742 1 277 . 1 1 52 52 VAL HA H 1 4.88 0.03 . 1 . . . . . . . . 4742 1 278 . 1 1 52 52 VAL HB H 1 2.01 0.03 . 1 . . . . . . . . 4742 1 279 . 1 1 52 52 VAL HG21 H 1 0.95 0.03 . 1 . . . . . . . . 4742 1 280 . 1 1 52 52 VAL HG22 H 1 0.95 0.03 . 1 . . . . . . . . 4742 1 281 . 1 1 52 52 VAL HG23 H 1 0.95 0.03 . 1 . . . . . . . . 4742 1 282 . 1 1 52 52 VAL HG11 H 1 0.73 0.03 . 1 . . . . . . . . 4742 1 283 . 1 1 52 52 VAL HG12 H 1 0.73 0.03 . 1 . . . . . . . . 4742 1 284 . 1 1 52 52 VAL HG13 H 1 0.73 0.03 . 1 . . . . . . . . 4742 1 285 . 1 1 52 52 VAL N N 15 112.80 0.25 . 1 . . . . . . . . 4742 1 286 . 1 1 53 53 PRO HD2 H 1 3.40 0.03 . 2 . . . . . . . . 4742 1 287 . 1 1 53 53 PRO HD3 H 1 3.81 0.03 . 2 . . . . . . . . 4742 1 288 . 1 1 54 54 ALA H H 1 8.10 0.03 . 1 . . . . . . . . 4742 1 289 . 1 1 54 54 ALA HA H 1 4.16 0.03 . 1 . . . . . . . . 4742 1 290 . 1 1 54 54 ALA HB1 H 1 1.23 0.03 . 1 . . . . . . . . 4742 1 291 . 1 1 54 54 ALA HB2 H 1 1.23 0.03 . 1 . . . . . . . . 4742 1 292 . 1 1 54 54 ALA HB3 H 1 1.23 0.03 . 1 . . . . . . . . 4742 1 293 . 1 1 54 54 ALA N N 15 116.81 0.25 . 1 . . . . . . . . 4742 1 294 . 1 1 55 55 LEU H H 1 7.59 0.03 . 1 . . . . . . . . 4742 1 295 . 1 1 55 55 LEU HA H 1 4.15 0.03 . 1 . . . . . . . . 4742 1 296 . 1 1 55 55 LEU HB2 H 1 1.45 0.03 . 2 . . . . . . . . 4742 1 297 . 1 1 55 55 LEU HB3 H 1 0.72 0.03 . 2 . . . . . . . . 4742 1 298 . 1 1 55 55 LEU HG H 1 1.03 0.03 . 1 . . . . . . . . 4742 1 299 . 1 1 55 55 LEU HD21 H 1 0.15 0.03 . 1 . . . . . . . . 4742 1 300 . 1 1 55 55 LEU HD22 H 1 0.15 0.03 . 1 . . . . . . . . 4742 1 301 . 1 1 55 55 LEU HD23 H 1 0.15 0.03 . 1 . . . . . . . . 4742 1 302 . 1 1 55 55 LEU HD11 H 1 -0.11 0.03 . 1 . . . . . . . . 4742 1 303 . 1 1 55 55 LEU HD12 H 1 -0.11 0.03 . 1 . . . . . . . . 4742 1 304 . 1 1 55 55 LEU HD13 H 1 -0.11 0.03 . 1 . . . . . . . . 4742 1 305 . 1 1 55 55 LEU N N 15 113.72 0.25 . 1 . . . . . . . . 4742 1 306 . 1 1 56 56 TRP H H 1 7.61 0.03 . 1 . . . . . . . . 4742 1 307 . 1 1 56 56 TRP HA H 1 5.31 0.03 . 1 . . . . . . . . 4742 1 308 . 1 1 56 56 TRP HB2 H 1 2.85 0.03 . 1 . . . . . . . . 4742 1 309 . 1 1 56 56 TRP HB3 H 1 2.85 0.03 . 1 . . . . . . . . 4742 1 310 . 1 1 56 56 TRP HE1 H 1 10.54 0.03 . 1 . . . . . . . . 4742 1 311 . 1 1 56 56 TRP HD1 H 1 6.86 0.03 . 1 . . . . . . . . 4742 1 312 . 1 1 56 56 TRP HZ2 H 1 7.33 0.03 . 1 . . . . . . . . 4742 1 313 . 1 1 56 56 TRP HH2 H 1 6.14 0.03 . 1 . . . . . . . . 4742 1 314 . 1 1 56 56 TRP HZ3 H 1 7.11 0.03 . 1 . . . . . . . . 4742 1 315 . 1 1 56 56 TRP HE3 H 1 7.14 0.03 . 1 . . . . . . . . 4742 1 316 . 1 1 56 56 TRP N N 15 118.40 0.25 . 1 . . . . . . . . 4742 1 317 . 1 1 56 56 TRP NE1 N 15 127.47 0.25 . 1 . . . . . . . . 4742 1 318 . 1 1 57 57 GLN H H 1 9.53 0.03 . 1 . . . . . . . . 4742 1 319 . 1 1 57 57 GLN HA H 1 5.11 0.03 . 1 . . . . . . . . 4742 1 320 . 1 1 57 57 GLN HB2 H 1 2.23 0.03 . 2 . . . . . . . . 4742 1 321 . 1 1 57 57 GLN HB3 H 1 2.16 0.03 . 2 . . . . . . . . 4742 1 322 . 1 1 57 57 GLN HG2 H 1 2.50 0.03 . 1 . . . . . . . . 4742 1 323 . 1 1 57 57 GLN HG3 H 1 2.50 0.03 . 1 . . . . . . . . 4742 1 324 . 1 1 57 57 GLN HE21 H 1 6.85 0.03 . 2 . . . . . . . . 4742 1 325 . 1 1 57 57 GLN HE22 H 1 7.71 0.03 . 2 . . . . . . . . 4742 1 326 . 1 1 57 57 GLN N N 15 122.74 0.25 . 1 . . . . . . . . 4742 1 327 . 1 1 57 57 GLN NE2 N 15 112.24 0.25 . 1 . . . . . . . . 4742 1 328 . 1 1 58 58 LEU H H 1 9.29 0.03 . 1 . . . . . . . . 4742 1 329 . 1 1 58 58 LEU HA H 1 3.91 0.03 . 1 . . . . . . . . 4742 1 330 . 1 1 58 58 LEU HB2 H 1 0.88 0.03 . 2 . . . . . . . . 4742 1 331 . 1 1 58 58 LEU HB3 H 1 1.39 0.03 . 2 . . . . . . . . 4742 1 332 . 1 1 58 58 LEU HD21 H 1 0.84 0.03 . 1 . . . . . . . . 4742 1 333 . 1 1 58 58 LEU HD22 H 1 0.84 0.03 . 1 . . . . . . . . 4742 1 334 . 1 1 58 58 LEU HD23 H 1 0.84 0.03 . 1 . . . . . . . . 4742 1 335 . 1 1 58 58 LEU HD11 H 1 0.59 0.03 . 1 . . . . . . . . 4742 1 336 . 1 1 58 58 LEU HD12 H 1 0.59 0.03 . 1 . . . . . . . . 4742 1 337 . 1 1 58 58 LEU HD13 H 1 0.59 0.03 . 1 . . . . . . . . 4742 1 338 . 1 1 58 58 LEU N N 15 135.42 0.25 . 1 . . . . . . . . 4742 1 339 . 1 1 59 59 GLN H H 1 8.52 0.03 . 1 . . . . . . . . 4742 1 340 . 1 1 59 59 GLN HA H 1 4.26 0.03 . 1 . . . . . . . . 4742 1 341 . 1 1 59 59 GLN HB2 H 1 2.13 0.03 . 2 . . . . . . . . 4742 1 342 . 1 1 59 59 GLN HB3 H 1 1.71 0.03 . 2 . . . . . . . . 4742 1 343 . 1 1 59 59 GLN HG2 H 1 2.30 0.03 . 1 . . . . . . . . 4742 1 344 . 1 1 59 59 GLN HG3 H 1 2.30 0.03 . 1 . . . . . . . . 4742 1 345 . 1 1 59 59 GLN HE21 H 1 7.22 0.03 . 2 . . . . . . . . 4742 1 346 . 1 1 59 59 GLN HE22 H 1 6.92 0.03 . 2 . . . . . . . . 4742 1 347 . 1 1 59 59 GLN N N 15 131.69 0.25 . 1 . . . . . . . . 4742 1 348 . 1 1 59 59 GLN NE2 N 15 115.55 0.25 . 1 . . . . . . . . 4742 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode J_values_set_1 _Coupling_constant_list.Entry_ID 4742 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $sample_cond_1 _Coupling_constant_list.Spectrometer_frequency_1H 800 _Coupling_constant_list.Details . _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_1 . 4742 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 16 16 TRP H . . . . 1 1 16 16 TRP HA . . . 0.0 . . 0.5 . . . . . . . . . . . 4742 1 2 3JHNHA . 1 1 17 17 GLN H . . . . 1 1 17 17 GLN HA . . . 9.6 . . 0.5 . . . . . . . . . . . 4742 1 3 3JHNHA . 1 1 18 18 VAL H . . . . 1 1 18 18 VAL HA . . . 4.4 . . 0.5 . . . . . . . . . . . 4742 1 4 3JHNHA . 1 1 19 19 ASN H . . . . 1 1 19 19 ASN HA . . . 8.1 . . 0.5 . . . . . . . . . . . 4742 1 5 3JHNHA . 1 1 20 20 THR H . . . . 1 1 20 20 THR HA . . . 10.9 . . 0.5 . . . . . . . . . . . 4742 1 6 3JHNHA . 1 1 21 21 ALA H . . . . 1 1 21 21 ALA HA . . . 7.5 . . 0.5 . . . . . . . . . . . 4742 1 7 3JHNHA . 1 1 22 22 TYR H . . . . 1 1 22 22 TYR HA . . . 10.5 . . 0.5 . . . . . . . . . . . 4742 1 8 3JHNHA . 1 1 23 23 THR H . . . . 1 1 23 23 THR HA . . . 10.7 . . 0.5 . . . . . . . . . . . 4742 1 9 3JHNHA . 1 1 24 24 ALA H . . . . 1 1 24 24 ALA HA . . . 0.0 . . 0.5 . . . . . . . . . . . 4742 1 10 3JHNHA . 1 1 26 26 GLN H . . . . 1 1 26 26 GLN HA . . . 4.1 . . 0.5 . . . . . . . . . . . 4742 1 11 3JHNHA . 1 1 27 27 LEU H . . . . 1 1 27 27 LEU HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4742 1 12 3JHNHA . 1 1 28 28 VAL H . . . . 1 1 28 28 VAL HA . . . 10.4 . . 0.5 . . . . . . . . . . . 4742 1 13 3JHNHA . 1 1 29 29 THR H . . . . 1 1 29 29 THR HA . . . 11.4 . . 0.5 . . . . . . . . . . . 4742 1 14 3JHNHA . 1 1 30 30 TYR H . . . . 1 1 30 30 TYR HA . . . 9.2 . . 0.5 . . . . . . . . . . . 4742 1 15 3JHNHA . 1 1 33 33 LYS H . . . . 1 1 33 33 LYS HA . . . 10.9 . . 0.5 . . . . . . . . . . . 4742 1 16 3JHNHA . 1 1 34 34 THR H . . . . 1 1 34 34 THR HA . . . 10.4 . . 0.5 . . . . . . . . . . . 4742 1 17 3JHNHA . 1 1 35 35 TYR H . . . . 1 1 35 35 TYR HA . . . 9.2 . . 0.5 . . . . . . . . . . . 4742 1 18 3JHNHA . 1 1 36 36 LYS H . . . . 1 1 36 36 LYS HA . . . 10.6 . . 0.5 . . . . . . . . . . . 4742 1 19 3JHNHA . 1 1 37 37 CYS H . . . . 1 1 37 37 CYS HA . . . 2.4 . . 0.5 . . . . . . . . . . . 4742 1 20 3JHNHA . 1 1 38 38 LEU H . . . . 1 1 38 38 LEU HA . . . 9.1 . . 0.5 . . . . . . . . . . . 4742 1 21 3JHNHA . 1 1 39 39 GLN H . . . . 1 1 39 39 GLN HA . . . 8.9 . . 0.5 . . . . . . . . . . . 4742 1 22 3JHNHA . 1 1 41 41 HIS H . . . . 1 1 41 41 HIS HA . . . 5.1 . . 0.5 . . . . . . . . . . . 4742 1 23 3JHNHA . 1 1 42 42 THR H . . . . 1 1 42 42 THR HA . . . 10.8 . . 0.5 . . . . . . . . . . . 4742 1 24 3JHNHA . 1 1 43 43 SER H . . . . 1 1 43 43 SER HA . . . 0.0 . . 0.5 . . . . . . . . . . . 4742 1 25 3JHNHA . 1 1 44 44 LEU H . . . . 1 1 44 44 LEU HA . . . 9.7 . . 0.5 . . . . . . . . . . . 4742 1 26 3JHNHA . 1 1 45 45 ALA H . . . . 1 1 45 45 ALA HA . . . 0.0 . . 0.5 . . . . . . . . . . . 4742 1 27 3JHNHA . 1 1 47 47 TRP H . . . . 1 1 47 47 TRP HA . . . 10.5 . . 0.5 . . . . . . . . . . . 4742 1 28 3JHNHA . 1 1 48 48 GLU H . . . . 1 1 48 48 GLU HA . . . 0.0 . . 0.5 . . . . . . . . . . . 4742 1 29 3JHNHA . 1 1 50 50 SER H . . . . 1 1 50 50 SER HA . . . 5.9 . . 0.5 . . . . . . . . . . . 4742 1 30 3JHNHA . 1 1 51 51 ASN H . . . . 1 1 51 51 ASN HA . . . 9.7 . . 0.5 . . . . . . . . . . . 4742 1 31 3JHNHA . 1 1 52 52 VAL H . . . . 1 1 52 52 VAL HA . . . 11.3 . . 0.5 . . . . . . . . . . . 4742 1 32 3JHNHA . 1 1 54 54 ALA H . . . . 1 1 54 54 ALA HA . . . 4.6 . . 0.5 . . . . . . . . . . . 4742 1 33 3JHNHA . 1 1 55 55 LEU H . . . . 1 1 55 55 LEU HA . . . 11.0 . . 0.5 . . . . . . . . . . . 4742 1 34 3JHNHA . 1 1 56 56 TRP H . . . . 1 1 56 56 TRP HA . . . 10.5 . . 0.5 . . . . . . . . . . . 4742 1 35 3JHNHA . 1 1 57 57 GLN H . . . . 1 1 57 57 GLN HA . . . 10.1 . . 0.5 . . . . . . . . . . . 4742 1 36 3JHNHA . 1 1 59 59 GLN H . . . . 1 1 59 59 GLN HA . . . 9.9 . . 0.5 . . . . . . . . . . . 4742 1 stop_ save_