data_4058 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4058 _Entry.Title ; Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1997-09-05 _Entry.Accession_date 1997-09-24 _Entry.Last_release_date . _Entry.Original_release_date . _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 Maija-Liisa Mattinen . M.-L.M. PhLic 4058 2 Maarit Kontteli . . . 4058 3 Janne Kerovuo . . . 4058 4 Markus Linder . . . 4058 5 Arto Annila . . . 4058 6 Gunnar Lindeberg . . . 4058 7 Tapani Reinikainen . . . 4058 8 Torbjorn Drakenberg . . . 4058 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4058 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 210 4058 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 . . 1998-02-25 . reformat BMRB 'converted to NMR-STAR version 2.1' 4058 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4058 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 97194052 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Mattinen, M-L. M., Kontteli, M., Kerovuo, J., Linder, M., Lindeberg, G., Reinikainen, T., and Drakenberg T., "Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei," Protein Sci. 6, 294-303 (1997). ; _Citation.Title ; Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein Science' _Citation.Journal_volume 6 _Citation.Journal_issue . _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 294 _Citation.Page_last 303 _Citation.Year 1997 _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 Maija-Liisa Mattinen . M.-L.M. PhLic 4058 1 2 Maarit Kontteli . . . 4058 1 3 Janne Kerovuo . . . 4058 1 4 Markus Linder . . . 4058 1 5 Arto Annila . . . 4058 1 6 Gunnar Lindeberg . . . 4058 1 7 Tapani Reinikainen . . . 4058 1 8 Torbjorn Drakenberg . . . 4058 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID cellulase 4058 1 'cellulose binding domain (CBD)' 4058 1 'nuclear magnetic resonance spectroscopy' 4058 1 'structure determination' 4058 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_Y31A_CBD _Assembly.Sf_category assembly _Assembly.Sf_framecode Y31A_CBD _Assembly.Entry_ID 4058 _Assembly.ID 1 _Assembly.Name Y31A_CBD_Cellobiohydrolase_I _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4058 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 Y31A 1 $Y31A_CBD_Cellobiohydrolase_I . . . native . . . . . 4058 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 8 8 SG . 1 . 1 CYS 25 25 SG . . . . . . . . . . 4058 1 2 disulfide single . 1 . 1 CYS 19 19 SG . 1 . 1 CYS 35 35 SG . . . . . . . . . . 4058 1 stop_ loop_ _Entity_deleted_atom.ID _Entity_deleted_atom.Entity_atom_list_ID _Entity_deleted_atom.Entity_assembly_ID _Entity_deleted_atom.Entity_ID _Entity_deleted_atom.Comp_ID _Entity_deleted_atom.Comp_index_ID _Entity_deleted_atom.Seq_ID _Entity_deleted_atom.Atom_ID _Entity_deleted_atom.Auth_entity_assembly_ID _Entity_deleted_atom.Auth_seq_ID _Entity_deleted_atom.Auth_comp_ID _Entity_deleted_atom.Auth_atom_ID _Entity_deleted_atom.Entry_ID _Entity_deleted_atom.Assembly_ID . 3 1 1 CYS 25 25 HG . . . . 4058 1 . 4 1 1 CYS 35 35 HG . . . . 4058 1 . 1 1 1 CYS 8 8 HG . . . . 4058 1 . 2 1 1 CYS 19 19 HG . . . . 4058 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 1AZJ . 'Three-Dimensional Structures Of Three Engineered Cellulose-Binding Domains Of Cellobiohydrolase I From Trichoderma Reesei, Nmr, 18 Structures' . . . . 4058 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Y31A_CBD abbreviation 4058 1 Y31A_CBD_Cellobiohydrolase_I system 4058 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Y31A_CBD_Cellobiohydrolase_I _Entity.Sf_category entity _Entity.Sf_framecode Y31A_CBD_Cellobiohydrolase_I _Entity.Entry_ID 4058 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'cellulose-binding domain of Cellobiohydrolase I' _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 ; TQSHYGQCGGIGYSGPTVCA SGTTCQVLNPAYSQCL ; _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 36 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 4000 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 192 . cellobiohydrolase . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 2 no BMRB 196 . cellobiohydrolase . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 3 no BMRB 25331 . CBM_2M . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 4 no BMRB 25332 . CBM_3M . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 5 no PDB 1AZJ . "Three-Dimensional Structures Of Three Engineered Cellulose- Binding Domains Of Cellobiohydrolase I From Trichoderma Reesei, Nmr" . . . . . 100.00 36 100.00 100.00 2.04e-15 . . . . 4058 1 6 no PDB 1CBH . "Determination Of The Three-Dimensional Structure Of The C- Terminal Domain Of Cellobiohydrolase I From Trichoderma Reesei. A St" . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 7 no PDB 2CBH . "Determination Of The Three-Dimensional Structure Of The C- Terminal Domain Of Cellobiohydrolase I From Trichoderma Reesei. A St" . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 8 no PDB 2MWJ . "Solution Structure Of Family 1 Carbohydrate-binding Module From Trichoderma Reesei Cel7a With O-mannose Residues At Thr1 And Se" . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 9 no PDB 2MWK . "Family 1 Carbohydrate-binding Module From Trichoderma Reesei Cel7a With O-mannose Residues At Thr1, Ser3, And Ser14" . . . . . 100.00 36 97.22 97.22 1.91e-14 . . . . 4058 1 10 no EMBL CAA49596 . "cellulose 1,4-beta-cellobiosidase [Trichoderma koningii]" . . . . . 100.00 513 97.22 97.22 1.78e-13 . . . . 4058 1 11 no GB AAG15502 . "CBDCBHI-cohesin hybrid, partial [synthetic construct]" . . . . . 100.00 210 97.22 97.22 5.21e-15 . . . . 4058 1 12 no GB AAP57751 . "Cip1 [Trichoderma reesei]" . . . . . 91.67 316 96.97 96.97 2.28e-12 . . . . 4058 1 13 no GB AAQ76092 . "cellobiohydrolase I [Trichoderma viride]" . . . . . 100.00 514 97.22 97.22 2.07e-13 . . . . 4058 1 14 no GB AEP40512 . "chimeric cellulase FnCel5A-TrCBM1-1 [synthetic construct]" . . . . . 100.00 385 97.22 97.22 8.84e-18 . . . . 4058 1 15 no GB AGI55989 . "mEos2-CBM(Cel7A) fusion [synthetic construct]" . . . . . 100.00 294 97.22 97.22 8.80e-16 . . . . 4058 1 16 no PIR S45380 . "cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) - fungus (Trichoderma koningii)" . . . . . 100.00 513 97.22 97.22 1.78e-13 . . . . 4058 1 17 no REF XP_006961566 . "carbohydrate-binding module family 1 [Trichoderma reesei QM6a]" . . . . . 91.67 316 96.97 96.97 2.28e-12 . . . . 4058 1 18 no REF XP_006969224 . "glycoside hydrolase family 7 [Trichoderma reesei QM6a]" . . . . . 100.00 514 97.22 97.22 1.93e-13 . . . . 4058 1 19 no SP P62694 . "RecName: Full=Exoglucanase 1; AltName: Full=1,4-beta-cellobiohydrolase; AltName: Full=Exocellobiohydrolase I; Short=CBHI; AltNa" . . . . . 100.00 513 97.22 97.22 1.78e-13 . . . . 4058 1 20 no SP P62695 . "RecName: Full=Exoglucanase 1; AltName: Full=1,4-beta-cellobiohydrolase; AltName: Full=Exocellobiohydrolase I; Short=CBHI; AltNa" . . . . . 100.00 513 97.22 97.22 1.78e-13 . . . . 4058 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID CBD abbreviation 4058 1 'cellulose-binding domain of Cellobiohydrolase I' common 4058 1 Y31A variant 4058 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 . THR . 4058 1 2 . GLN . 4058 1 3 . SER . 4058 1 4 . HIS . 4058 1 5 . TYR . 4058 1 6 . GLY . 4058 1 7 . GLN . 4058 1 8 . CYS . 4058 1 9 . GLY . 4058 1 10 . GLY . 4058 1 11 . ILE . 4058 1 12 . GLY . 4058 1 13 . TYR . 4058 1 14 . SER . 4058 1 15 . GLY . 4058 1 16 . PRO . 4058 1 17 . THR . 4058 1 18 . VAL . 4058 1 19 . CYS . 4058 1 20 . ALA . 4058 1 21 . SER . 4058 1 22 . GLY . 4058 1 23 . THR . 4058 1 24 . THR . 4058 1 25 . CYS . 4058 1 26 . GLN . 4058 1 27 . VAL . 4058 1 28 . LEU . 4058 1 29 . ASN . 4058 1 30 . PRO . 4058 1 31 . ALA . 4058 1 32 . TYR . 4058 1 33 . SER . 4058 1 34 . GLN . 4058 1 35 . CYS . 4058 1 36 . LEU . 4058 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 . THR 1 1 4058 1 . GLN 2 2 4058 1 . SER 3 3 4058 1 . HIS 4 4 4058 1 . TYR 5 5 4058 1 . GLY 6 6 4058 1 . GLN 7 7 4058 1 . CYS 8 8 4058 1 . GLY 9 9 4058 1 . GLY 10 10 4058 1 . ILE 11 11 4058 1 . GLY 12 12 4058 1 . TYR 13 13 4058 1 . SER 14 14 4058 1 . GLY 15 15 4058 1 . PRO 16 16 4058 1 . THR 17 17 4058 1 . VAL 18 18 4058 1 . CYS 19 19 4058 1 . ALA 20 20 4058 1 . SER 21 21 4058 1 . GLY 22 22 4058 1 . THR 23 23 4058 1 . THR 24 24 4058 1 . CYS 25 25 4058 1 . GLN 26 26 4058 1 . VAL 27 27 4058 1 . LEU 28 28 4058 1 . ASN 29 29 4058 1 . PRO 30 30 4058 1 . ALA 31 31 4058 1 . TYR 32 32 4058 1 . SER 33 33 4058 1 . GLN 34 34 4058 1 . CYS 35 35 4058 1 . LEU 36 36 4058 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 4058 _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 $Y31A_CBD_Cellobiohydrolase_I . 51453 organism . 'Hypocrea jecorina' 'Hypocrea jecorina' . . Eukaryota Fungi Hypocrea jecorina . . . . . . . . . . . . . . . . . . ; Three-engineered cellulose binding domain (Y5A, Y31A, and Y32A) of Cellobiohydrolase I from Trichoderma reesi ; . . 4058 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 4058 _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 $Y31A_CBD_Cellobiohydrolase_I . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . ; The peptide was synthesized by automated solid-phase synthesis using Fmoc chemistry and purified as described Lindeberg et al 1991 (Int J Pept Protein Res 38: 253-259). ; . . 4058 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4058 _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 'cellulose-binding domain of Cellobiohydrolase I' . . . 1 $Y31A_CBD_Cellobiohydrolase_I . . 7.9 . . mg/ml . . . . 4058 1 stop_ save_ ####################### # Sample conditions # ####################### save_experimental_conditions_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode experimental_conditions_set_one _Sample_condition_list.Entry_ID 4058 _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 3.90 0.005 n/a 4058 1 temperature 298 . K 4058 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 4058 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 4058 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 4058 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 4058 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $experimental_conditions_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 4058 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_parameter_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_parameter_set_one _Chem_shift_reference.Entry_ID 4058 _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 H2O proton . . . . ppm 4.88 internal direct . . . . . . . . . . 4058 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_assignment_Y31A_CBD_Cellobiohydrolase_I _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignment_Y31A_CBD_Cellobiohydrolase_I _Assigned_chem_shift_list.Entry_ID 4058 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $experimental_conditions_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_parameter_set_one _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_one . 4058 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 THR HA H 1 3.92 0.01 . 1 . . . . . . . . 4058 1 2 . 1 1 1 1 THR HB H 1 4.12 0.01 . 1 . . . . . . . . 4058 1 3 . 1 1 1 1 THR HG21 H 1 1.23 0.01 . 1 . . . . . . . . 4058 1 4 . 1 1 1 1 THR HG22 H 1 1.23 0.01 . 1 . . . . . . . . 4058 1 5 . 1 1 1 1 THR HG23 H 1 1.23 0.01 . 1 . . . . . . . . 4058 1 6 . 1 1 2 2 GLN H H 1 9.22 0.01 . 1 . . . . . . . . 4058 1 7 . 1 1 2 2 GLN HA H 1 4.72 0.01 . 1 . . . . . . . . 4058 1 8 . 1 1 2 2 GLN HB2 H 1 1.88 0.01 . 1 . . . . . . . . 4058 1 9 . 1 1 2 2 GLN HB3 H 1 1.84 0.01 . 1 . . . . . . . . 4058 1 10 . 1 1 2 2 GLN HG2 H 1 2.60 0.01 . 1 . . . . . . . . 4058 1 11 . 1 1 2 2 GLN HG3 H 1 2.23 0.01 . 1 . . . . . . . . 4058 1 12 . 1 1 2 2 GLN HE21 H 1 8.67 0.01 . 1 . . . . . . . . 4058 1 13 . 1 1 2 2 GLN HE22 H 1 7.08 0.01 . 1 . . . . . . . . 4058 1 14 . 1 1 3 3 SER H H 1 8.82 0.01 . 1 . . . . . . . . 4058 1 15 . 1 1 3 3 SER HA H 1 4.40 0.01 . 1 . . . . . . . . 4058 1 16 . 1 1 3 3 SER HB2 H 1 3.93 0.01 . 1 . . . . . . . . 4058 1 17 . 1 1 3 3 SER HB3 H 1 3.88 0.01 . 1 . . . . . . . . 4058 1 18 . 1 1 4 4 HIS H H 1 8.81 0.01 . 1 . . . . . . . . 4058 1 19 . 1 1 4 4 HIS HA H 1 4.14 0.01 . 1 . . . . . . . . 4058 1 20 . 1 1 4 4 HIS HB2 H 1 3.12 0.01 . 1 . . . . . . . . 4058 1 21 . 1 1 4 4 HIS HB3 H 1 2.98 0.01 . 1 . . . . . . . . 4058 1 22 . 1 1 4 4 HIS HD2 H 1 6.83 0.01 . 1 . . . . . . . . 4058 1 23 . 1 1 5 5 TYR H H 1 9.37 0.01 . 1 . . . . . . . . 4058 1 24 . 1 1 5 5 TYR HA H 1 4.14 0.01 . 1 . . . . . . . . 4058 1 25 . 1 1 5 5 TYR HB2 H 1 3.15 0.01 . 1 . . . . . . . . 4058 1 26 . 1 1 5 5 TYR HB3 H 1 3.34 0.01 . 1 . . . . . . . . 4058 1 27 . 1 1 5 5 TYR HE1 H 1 6.90 0.01 . 1 . . . . . . . . 4058 1 28 . 1 1 5 5 TYR HE2 H 1 6.90 0.01 . 1 . . . . . . . . 4058 1 29 . 1 1 5 5 TYR HD1 H 1 6.55 0.01 . 1 . . . . . . . . 4058 1 30 . 1 1 5 5 TYR HD2 H 1 6.55 0.01 . 1 . . . . . . . . 4058 1 31 . 1 1 6 6 GLY H H 1 8.88 0.01 . 1 . . . . . . . . 4058 1 32 . 1 1 6 6 GLY HA2 H 1 4.18 0.01 . 1 . . . . . . . . 4058 1 33 . 1 1 6 6 GLY HA3 H 1 3.55 0.01 . 1 . . . . . . . . 4058 1 34 . 1 1 7 7 GLN H H 1 8.71 0.01 . 1 . . . . . . . . 4058 1 35 . 1 1 7 7 GLN HA H 1 4.27 0.01 . 1 . . . . . . . . 4058 1 36 . 1 1 7 7 GLN HB2 H 1 1.67 0.01 . 1 . . . . . . . . 4058 1 37 . 1 1 7 7 GLN HB3 H 1 2.07 0.01 . 1 . . . . . . . . 4058 1 38 . 1 1 7 7 GLN HG2 H 1 2.31 0.01 . 1 . . . . . . . . 4058 1 39 . 1 1 7 7 GLN HG3 H 1 1.06 0.01 . 1 . . . . . . . . 4058 1 40 . 1 1 7 7 GLN HE21 H 1 7.19 0.01 . 1 . . . . . . . . 4058 1 41 . 1 1 7 7 GLN HE22 H 1 7.11 0.01 . 1 . . . . . . . . 4058 1 42 . 1 1 8 8 CYS H H 1 7.96 0.01 . 1 . . . . . . . . 4058 1 43 . 1 1 8 8 CYS HA H 1 5.17 0.01 . 1 . . . . . . . . 4058 1 44 . 1 1 8 8 CYS HB2 H 1 2.85 0.01 . 1 . . . . . . . . 4058 1 45 . 1 1 8 8 CYS HB3 H 1 3.48 0.01 . 1 . . . . . . . . 4058 1 46 . 1 1 9 9 GLY H H 1 6.71 0.01 . 1 . . . . . . . . 4058 1 47 . 1 1 9 9 GLY HA2 H 1 4.48 0.01 . 1 . . . . . . . . 4058 1 48 . 1 1 9 9 GLY HA3 H 1 4.26 0.01 . 1 . . . . . . . . 4058 1 49 . 1 1 10 10 GLY H H 1 8.75 0.01 . 1 . . . . . . . . 4058 1 50 . 1 1 10 10 GLY HA2 H 1 3.94 0.01 . 1 . . . . . . . . 4058 1 51 . 1 1 10 10 GLY HA3 H 1 4.43 0.01 . 1 . . . . . . . . 4058 1 52 . 1 1 11 11 ILE H H 1 8.40 0.01 . 1 . . . . . . . . 4058 1 53 . 1 1 11 11 ILE HA H 1 3.96 0.01 . 1 . . . . . . . . 4058 1 54 . 1 1 11 11 ILE HB H 1 1.20 0.01 . 1 . . . . . . . . 4058 1 55 . 1 1 11 11 ILE HG12 H 1 1.71 0.01 . 1 . . . . . . . . 4058 1 56 . 1 1 11 11 ILE HG13 H 1 0.94 0.01 . 1 . . . . . . . . 4058 1 57 . 1 1 11 11 ILE HG21 H 1 0.92 0.01 . 1 . . . . . . . . 4058 1 58 . 1 1 11 11 ILE HG22 H 1 0.92 0.01 . 1 . . . . . . . . 4058 1 59 . 1 1 11 11 ILE HG23 H 1 0.92 0.01 . 1 . . . . . . . . 4058 1 60 . 1 1 12 12 GLY H H 1 9.19 0.01 . 1 . . . . . . . . 4058 1 61 . 1 1 12 12 GLY HA2 H 1 3.76 0.01 . 1 . . . . . . . . 4058 1 62 . 1 1 12 12 GLY HA3 H 1 4.22 0.01 . 1 . . . . . . . . 4058 1 63 . 1 1 13 13 TYR H H 1 7.89 0.01 . 1 . . . . . . . . 4058 1 64 . 1 1 13 13 TYR HA H 1 4.59 0.01 . 1 . . . . . . . . 4058 1 65 . 1 1 13 13 TYR HB2 H 1 2.87 0.01 . 1 . . . . . . . . 4058 1 66 . 1 1 13 13 TYR HB3 H 1 2.77 0.01 . 1 . . . . . . . . 4058 1 67 . 1 1 13 13 TYR HD1 H 1 6.90 0.01 . 1 . . . . . . . . 4058 1 68 . 1 1 13 13 TYR HD2 H 1 6.90 0.01 . 1 . . . . . . . . 4058 1 69 . 1 1 13 13 TYR HE1 H 1 6.46 0.01 . 1 . . . . . . . . 4058 1 70 . 1 1 13 13 TYR HE2 H 1 6.46 0.01 . 1 . . . . . . . . 4058 1 71 . 1 1 14 14 SER H H 1 8.51 0.01 . 1 . . . . . . . . 4058 1 72 . 1 1 14 14 SER HA H 1 4.52 0.01 . 1 . . . . . . . . 4058 1 73 . 1 1 14 14 SER HB2 H 1 3.62 0.01 . 1 . . . . . . . . 4058 1 74 . 1 1 14 14 SER HB3 H 1 3.79 0.01 . 1 . . . . . . . . 4058 1 75 . 1 1 15 15 GLY H H 1 5.07 0.01 . 1 . . . . . . . . 4058 1 76 . 1 1 15 15 GLY HA2 H 1 4.05 0.01 . 1 . . . . . . . . 4058 1 77 . 1 1 15 15 GLY HA3 H 1 3.59 0.01 . 1 . . . . . . . . 4058 1 78 . 1 1 16 16 PRO HA H 1 4.49 0.01 . 1 . . . . . . . . 4058 1 79 . 1 1 16 16 PRO HB2 H 1 2.37 0.01 . 1 . . . . . . . . 4058 1 80 . 1 1 16 16 PRO HB3 H 1 1.94 0.01 . 1 . . . . . . . . 4058 1 81 . 1 1 16 16 PRO HG2 H 1 2.04 0.01 . 1 . . . . . . . . 4058 1 82 . 1 1 16 16 PRO HG3 H 1 2.01 0.01 . 1 . . . . . . . . 4058 1 83 . 1 1 16 16 PRO HD2 H 1 3.64 0.01 . 1 . . . . . . . . 4058 1 84 . 1 1 16 16 PRO HD3 H 1 3.51 0.01 . 1 . . . . . . . . 4058 1 85 . 1 1 17 17 THR H H 1 8.48 0.01 . 1 . . . . . . . . 4058 1 86 . 1 1 17 17 THR HA H 1 4.75 0.01 . 1 . . . . . . . . 4058 1 87 . 1 1 17 17 THR HB H 1 4.62 0.01 . 1 . . . . . . . . 4058 1 88 . 1 1 17 17 THR HG21 H 1 1.34 0.01 . 1 . . . . . . . . 4058 1 89 . 1 1 17 17 THR HG22 H 1 1.34 0.01 . 1 . . . . . . . . 4058 1 90 . 1 1 17 17 THR HG23 H 1 1.34 0.01 . 1 . . . . . . . . 4058 1 91 . 1 1 18 18 VAL H H 1 7.23 0.01 . 1 . . . . . . . . 4058 1 92 . 1 1 18 18 VAL HA H 1 4.11 0.01 . 1 . . . . . . . . 4058 1 93 . 1 1 18 18 VAL HB H 1 2.01 0.01 . 1 . . . . . . . . 4058 1 94 . 1 1 18 18 VAL HG11 H 1 0.97 0.01 . 2 . . . . . . . . 4058 1 95 . 1 1 18 18 VAL HG12 H 1 0.97 0.01 . 2 . . . . . . . . 4058 1 96 . 1 1 18 18 VAL HG13 H 1 0.97 0.01 . 2 . . . . . . . . 4058 1 97 . 1 1 18 18 VAL HG21 H 1 0.96 0.01 . 2 . . . . . . . . 4058 1 98 . 1 1 18 18 VAL HG22 H 1 0.96 0.01 . 2 . . . . . . . . 4058 1 99 . 1 1 18 18 VAL HG23 H 1 0.96 0.01 . 2 . . . . . . . . 4058 1 100 . 1 1 19 19 CYS H H 1 8.74 0.01 . 1 . . . . . . . . 4058 1 101 . 1 1 19 19 CYS HA H 1 4.65 0.01 . 1 . . . . . . . . 4058 1 102 . 1 1 19 19 CYS HB2 H 1 3.67 0.01 . 1 . . . . . . . . 4058 1 103 . 1 1 19 19 CYS HB3 H 1 2.25 0.01 . 1 . . . . . . . . 4058 1 104 . 1 1 20 20 ALA H H 1 8.17 0.01 . 1 . . . . . . . . 4058 1 105 . 1 1 20 20 ALA HA H 1 4.06 0.01 . 1 . . . . . . . . 4058 1 106 . 1 1 20 20 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 4058 1 107 . 1 1 20 20 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 4058 1 108 . 1 1 20 20 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 4058 1 109 . 1 1 21 21 SER H H 1 8.50 0.01 . 1 . . . . . . . . 4058 1 110 . 1 1 21 21 SER HA H 1 4.20 0.01 . 1 . . . . . . . . 4058 1 111 . 1 1 21 21 SER HB2 H 1 3.85 0.01 . 2 . . . . . . . . 4058 1 112 . 1 1 21 21 SER HB3 H 1 3.85 0.01 . 2 . . . . . . . . 4058 1 113 . 1 1 22 22 GLY H H 1 8.94 0.01 . 1 . . . . . . . . 4058 1 114 . 1 1 22 22 GLY HA2 H 1 4.62 0.01 . 1 . . . . . . . . 4058 1 115 . 1 1 22 22 GLY HA3 H 1 4.33 0.01 . 1 . . . . . . . . 4058 1 116 . 1 1 23 23 THR H H 1 8.16 0.01 . 1 . . . . . . . . 4058 1 117 . 1 1 23 23 THR HA H 1 4.73 0.01 . 1 . . . . . . . . 4058 1 118 . 1 1 23 23 THR HB H 1 3.78 0.01 . 1 . . . . . . . . 4058 1 119 . 1 1 23 23 THR HG21 H 1 0.51 0.01 . 1 . . . . . . . . 4058 1 120 . 1 1 23 23 THR HG22 H 1 0.51 0.01 . 1 . . . . . . . . 4058 1 121 . 1 1 23 23 THR HG23 H 1 0.51 0.01 . 1 . . . . . . . . 4058 1 122 . 1 1 24 24 THR H H 1 9.37 0.01 . 1 . . . . . . . . 4058 1 123 . 1 1 24 24 THR HA H 1 4.51 0.01 . 1 . . . . . . . . 4058 1 124 . 1 1 24 24 THR HB H 1 4.04 0.01 . 1 . . . . . . . . 4058 1 125 . 1 1 24 24 THR HG21 H 1 1.13 0.01 . 1 . . . . . . . . 4058 1 126 . 1 1 24 24 THR HG22 H 1 1.13 0.01 . 1 . . . . . . . . 4058 1 127 . 1 1 24 24 THR HG23 H 1 1.13 0.01 . 1 . . . . . . . . 4058 1 128 . 1 1 25 25 CYS H H 1 8.92 0.01 . 1 . . . . . . . . 4058 1 129 . 1 1 25 25 CYS HA H 1 4.59 0.01 . 1 . . . . . . . . 4058 1 130 . 1 1 25 25 CYS HB2 H 1 2.94 0.01 . 1 . . . . . . . . 4058 1 131 . 1 1 25 25 CYS HB3 H 1 3.17 0.01 . 1 . . . . . . . . 4058 1 132 . 1 1 26 26 GLN H H 1 9.07 0.01 . 1 . . . . . . . . 4058 1 133 . 1 1 26 26 GLN HA H 1 4.61 0.01 . 1 . . . . . . . . 4058 1 134 . 1 1 26 26 GLN HB2 H 1 2.07 0.01 . 1 . . . . . . . . 4058 1 135 . 1 1 26 26 GLN HB3 H 1 1.94 0.01 . 1 . . . . . . . . 4058 1 136 . 1 1 26 26 GLN HG2 H 1 2.44 0.01 . 1 . . . . . . . . 4058 1 137 . 1 1 26 26 GLN HG3 H 1 2.26 0.01 . 1 . . . . . . . . 4058 1 138 . 1 1 26 26 GLN HE21 H 1 7.03 0.01 . 1 . . . . . . . . 4058 1 139 . 1 1 26 26 GLN HE22 H 1 6.78 0.01 . 1 . . . . . . . . 4058 1 140 . 1 1 27 27 VAL H H 1 8.72 0.01 . 1 . . . . . . . . 4058 1 141 . 1 1 27 27 VAL HA H 1 4.07 0.01 . 1 . . . . . . . . 4058 1 142 . 1 1 27 27 VAL HB H 1 1.94 0.01 . 1 . . . . . . . . 4058 1 143 . 1 1 27 27 VAL HG11 H 1 0.69 0.01 . 2 . . . . . . . . 4058 1 144 . 1 1 27 27 VAL HG12 H 1 0.69 0.01 . 2 . . . . . . . . 4058 1 145 . 1 1 27 27 VAL HG13 H 1 0.69 0.01 . 2 . . . . . . . . 4058 1 146 . 1 1 27 27 VAL HG21 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 147 . 1 1 27 27 VAL HG22 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 148 . 1 1 27 27 VAL HG23 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 149 . 1 1 28 28 LEU H H 1 8.68 0.01 . 1 . . . . . . . . 4058 1 150 . 1 1 28 28 LEU HA H 1 4.69 0.01 . 1 . . . . . . . . 4058 1 151 . 1 1 28 28 LEU HB2 H 1 1.93 0.01 . 1 . . . . . . . . 4058 1 152 . 1 1 28 28 LEU HB3 H 1 1.80 0.01 . 1 . . . . . . . . 4058 1 153 . 1 1 28 28 LEU HG H 1 1.80 0.01 . 1 . . . . . . . . 4058 1 154 . 1 1 28 28 LEU HD11 H 1 1.05 0.01 . 2 . . . . . . . . 4058 1 155 . 1 1 28 28 LEU HD12 H 1 1.05 0.01 . 2 . . . . . . . . 4058 1 156 . 1 1 28 28 LEU HD13 H 1 1.05 0.01 . 2 . . . . . . . . 4058 1 157 . 1 1 28 28 LEU HD21 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 158 . 1 1 28 28 LEU HD22 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 159 . 1 1 28 28 LEU HD23 H 1 0.93 0.01 . 2 . . . . . . . . 4058 1 160 . 1 1 29 29 ASN H H 1 8.62 0.01 . 1 . . . . . . . . 4058 1 161 . 1 1 29 29 ASN HB2 H 1 3.16 0.01 . 1 . . . . . . . . 4058 1 162 . 1 1 29 29 ASN HB3 H 1 3.05 0.01 . 1 . . . . . . . . 4058 1 163 . 1 1 29 29 ASN HD21 H 1 7.75 0.01 . 1 . . . . . . . . 4058 1 164 . 1 1 29 29 ASN HD22 H 1 7.04 0.01 . 1 . . . . . . . . 4058 1 165 . 1 1 30 30 PRO HA H 1 4.31 0.01 . 1 . . . . . . . . 4058 1 166 . 1 1 30 30 PRO HB2 H 1 2.49 0.01 . 1 . . . . . . . . 4058 1 167 . 1 1 30 30 PRO HG2 H 1 2.17 0.01 . 1 . . . . . . . . 4058 1 168 . 1 1 30 30 PRO HG3 H 1 1.96 0.01 . 1 . . . . . . . . 4058 1 169 . 1 1 30 30 PRO HD2 H 1 3.88 0.01 . 1 . . . . . . . . 4058 1 170 . 1 1 30 30 PRO HD3 H 1 3.76 0.01 . 1 . . . . . . . . 4058 1 171 . 1 1 31 31 ALA H H 1 8.39 0.01 . 1 . . . . . . . . 4058 1 172 . 1 1 31 31 ALA HA H 1 4.54 0.01 . 1 . . . . . . . . 4058 1 173 . 1 1 31 31 ALA HB1 H 1 1.52 0.01 . 1 . . . . . . . . 4058 1 174 . 1 1 31 31 ALA HB2 H 1 1.52 0.01 . 1 . . . . . . . . 4058 1 175 . 1 1 31 31 ALA HB3 H 1 1.52 0.01 . 1 . . . . . . . . 4058 1 176 . 1 1 32 32 TYR H H 1 8.01 0.01 . 1 . . . . . . . . 4058 1 177 . 1 1 32 32 TYR HA H 1 4.66 0.01 . 1 . . . . . . . . 4058 1 178 . 1 1 32 32 TYR HB2 H 1 2.79 0.01 . 1 . . . . . . . . 4058 1 179 . 1 1 32 32 TYR HB3 H 1 2.78 0.01 . 1 . . . . . . . . 4058 1 180 . 1 1 32 32 TYR HD1 H 1 6.95 0.01 . 1 . . . . . . . . 4058 1 181 . 1 1 32 32 TYR HD2 H 1 6.95 0.01 . 1 . . . . . . . . 4058 1 182 . 1 1 32 32 TYR HE1 H 1 6.59 0.01 . 1 . . . . . . . . 4058 1 183 . 1 1 32 32 TYR HE2 H 1 6.59 0.01 . 1 . . . . . . . . 4058 1 184 . 1 1 33 33 SER H H 1 6.78 0.01 . 1 . . . . . . . . 4058 1 185 . 1 1 33 33 SER HA H 1 5.22 0.01 . 1 . . . . . . . . 4058 1 186 . 1 1 33 33 SER HB2 H 1 3.55 0.01 . 1 . . . . . . . . 4058 1 187 . 1 1 33 33 SER HB3 H 1 2.85 0.01 . 1 . . . . . . . . 4058 1 188 . 1 1 34 34 GLN H H 1 9.10 0.01 . 1 . . . . . . . . 4058 1 189 . 1 1 34 34 GLN HA H 1 4.79 0.01 . 1 . . . . . . . . 4058 1 190 . 1 1 34 34 GLN HB2 H 1 1.89 0.01 . 1 . . . . . . . . 4058 1 191 . 1 1 34 34 GLN HB3 H 1 1.64 0.01 . 1 . . . . . . . . 4058 1 192 . 1 1 34 34 GLN HG2 H 1 2.12 0.01 . 1 . . . . . . . . 4058 1 193 . 1 1 34 34 GLN HG3 H 1 2.08 0.01 . 1 . . . . . . . . 4058 1 194 . 1 1 34 34 GLN HE21 H 1 7.79 0.01 . 1 . . . . . . . . 4058 1 195 . 1 1 34 34 GLN HE22 H 1 6.88 0.01 . 1 . . . . . . . . 4058 1 196 . 1 1 35 35 CYS H H 1 8.55 0.01 . 1 . . . . . . . . 4058 1 197 . 1 1 35 35 CYS HA H 1 5.07 0.01 . 1 . . . . . . . . 4058 1 198 . 1 1 35 35 CYS HB2 H 1 3.40 0.01 . 1 . . . . . . . . 4058 1 199 . 1 1 35 35 CYS HB3 H 1 2.90 0.01 . 1 . . . . . . . . 4058 1 200 . 1 1 36 36 LEU H H 1 9.08 0.01 . 1 . . . . . . . . 4058 1 201 . 1 1 36 36 LEU HA H 1 4.52 0.01 . 1 . . . . . . . . 4058 1 202 . 1 1 36 36 LEU HB2 H 1 1.59 0.01 . 1 . . . . . . . . 4058 1 203 . 1 1 36 36 LEU HB3 H 1 1.56 0.01 . 1 . . . . . . . . 4058 1 204 . 1 1 36 36 LEU HG H 1 1.35 0.01 . 1 . . . . . . . . 4058 1 205 . 1 1 36 36 LEU HD11 H 1 0.99 0.01 . 2 . . . . . . . . 4058 1 206 . 1 1 36 36 LEU HD12 H 1 0.99 0.01 . 2 . . . . . . . . 4058 1 207 . 1 1 36 36 LEU HD13 H 1 0.99 0.01 . 2 . . . . . . . . 4058 1 208 . 1 1 36 36 LEU HD21 H 1 0.94 0.01 . 2 . . . . . . . . 4058 1 209 . 1 1 36 36 LEU HD22 H 1 0.94 0.01 . 2 . . . . . . . . 4058 1 210 . 1 1 36 36 LEU HD23 H 1 0.94 0.01 . 2 . . . . . . . . 4058 1 stop_ save_