data_5056 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5056 _Entry.Title ; ATT an Arabidopsis thaliana Inhibitor of Trypsin and Chymotrypsin: Sequence-Specific Multinuclear Magnetic Resonance Assignments and Secondary Structure ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-06-13 _Entry.Accession_date 2001-06-14 _Entry.Last_release_date 2001-06-13 _Entry.Original_release_date 2001-06-13 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 Qin Zhao . . . . 5056 2 Young-Kee Chae . . . . 5056 3 John Markley . L. . . 5056 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5056 coupling_constants 1 5056 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 237 5056 '15N chemical shifts' 68 5056 '1H chemical shifts' 371 5056 'coupling constants' 50 5056 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-01-06 . original BMRB . 5056 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5056 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22257244 _Citation.DOI . _Citation.PubMed_ID 12369816 _Citation.Full_citation . _Citation.Title ; NMR Solution Structure of ATTp, an Arabidopsis thaliana Trypsin Inhibitor ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 41 _Citation.Journal_issue 41 _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 12284 _Citation.Page_last 12296 _Citation.Year 2002 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Qin Zhao . . . . 5056 1 2 Young-Kee Chae . . . . 5056 1 3 John Markley . L. . . 5056 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID NMR 5056 1 'chemical shift assignments' 5056 1 'chemical shift index' 5056 1 chymotrypsin 5056 1 'protease inhibitor' 5056 1 'serine protease' 5056 1 trypsin 5056 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ATT _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ATT _Assembly.Entry_ID 5056 _Assembly.ID 1 _Assembly.Name 'Arabidopsis thaliana trypsin/chymotrypsin inhibitor' _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 'disulfide bound and free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5056 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 ATT 1 $ATT . . . native . . . . . 5056 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_asym_ID_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_asym_ID_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 11 11 SG . 1 . 1 CYS 63 63 SG . . . . . . . . . . . . 5056 1 2 disulfide single . 1 . 1 CYS 24 24 SG . 1 . 1 CYS 48 48 SG . . . . . . . . . . . . 5056 1 3 disulfide single . 1 . 1 CYS 33 33 SG . 1 . 1 CYS 58 58 SG . . . . . . . . . . . . 5056 1 4 disulfide single . 1 . 1 CYS 37 37 SG . 1 . 1 CYS 60 60 SG . . . . . . . . . . . . 5056 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID ATT abbreviation 5056 1 'Arabidopsis thaliana trypsin/chymotrypsin inhibitor' system 5056 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'serine protease inhibitor' 5056 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ATT _Entity.Sf_category entity _Entity.Sf_framecode ATT _Entity.Entry_ID 5056 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name ATT _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 ; CPEIEAQGNECLKEYGGDVG FGFCAPRIFPTICYTRCREN KGAKGGRCRWGQGSNVKCLC DFCGDTPQ ; _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 68 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'disulfide bound and free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . no BMRB 5133 . attm . . . . . 91.18 62 100.00 100.00 3.72e-28 . . . . 5056 1 . no PDB 1JXC . 'Minimized Nmr Structure Of Att, An Arabidopsis TrypsinCHYMOTRYPSIN INHIBITOR' . . . . . 100.00 68 100.00 100.00 1.03e-31 . . . . 5056 1 . no EMBL CAB62548 . 'trypsin inhibitor [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no EMBL CAG15155 . 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no EMBL CAG15160 . 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no EMBL CAG15165 . 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no EMBL CAG15170 . 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no GenBank AAB64325 . 'putative trypsin inhibitor [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no GenBank AAK92724 . 'putative trypsin inhibitor protein [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no GenBank AAM20096 . 'putative trypsin inhibitor protein [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no REF NP_181879 . 'ATTI1 (ARABIDOPSIS THALIANA TRYPSIN INHIBITOR PROTEIN 1) [Arabidopsis thaliana]' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 . no SWISS-PROT Q42328 . 'Trypsin inhibitor ATTI-2 precursor (diDi 4T-1) (ATTp)' . . . . . 98.53 89 98.51 98.51 1.69e-31 . . . . 5056 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'serine protease inhibitor' 5056 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID ATT abbreviation 5056 1 ATT common 5056 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 . CYS . 5056 1 2 . PRO . 5056 1 3 . GLU . 5056 1 4 . ILE . 5056 1 5 . GLU . 5056 1 6 . ALA . 5056 1 7 . GLN . 5056 1 8 . GLY . 5056 1 9 . ASN . 5056 1 10 . GLU . 5056 1 11 . CYS . 5056 1 12 . LEU . 5056 1 13 . LYS . 5056 1 14 . GLU . 5056 1 15 . TYR . 5056 1 16 . GLY . 5056 1 17 . GLY . 5056 1 18 . ASP . 5056 1 19 . VAL . 5056 1 20 . GLY . 5056 1 21 . PHE . 5056 1 22 . GLY . 5056 1 23 . PHE . 5056 1 24 . CYS . 5056 1 25 . ALA . 5056 1 26 . PRO . 5056 1 27 . ARG . 5056 1 28 . ILE . 5056 1 29 . PHE . 5056 1 30 . PRO . 5056 1 31 . THR . 5056 1 32 . ILE . 5056 1 33 . CYS . 5056 1 34 . TYR . 5056 1 35 . THR . 5056 1 36 . ARG . 5056 1 37 . CYS . 5056 1 38 . ARG . 5056 1 39 . GLU . 5056 1 40 . ASN . 5056 1 41 . LYS . 5056 1 42 . GLY . 5056 1 43 . ALA . 5056 1 44 . LYS . 5056 1 45 . GLY . 5056 1 46 . GLY . 5056 1 47 . ARG . 5056 1 48 . CYS . 5056 1 49 . ARG . 5056 1 50 . TRP . 5056 1 51 . GLY . 5056 1 52 . GLN . 5056 1 53 . GLY . 5056 1 54 . SER . 5056 1 55 . ASN . 5056 1 56 . VAL . 5056 1 57 . LYS . 5056 1 58 . CYS . 5056 1 59 . LEU . 5056 1 60 . CYS . 5056 1 61 . ASP . 5056 1 62 . PHE . 5056 1 63 . CYS . 5056 1 64 . GLY . 5056 1 65 . ASP . 5056 1 66 . THR . 5056 1 67 . PRO . 5056 1 68 . GLN . 5056 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 . CYS 1 1 5056 1 . PRO 2 2 5056 1 . GLU 3 3 5056 1 . ILE 4 4 5056 1 . GLU 5 5 5056 1 . ALA 6 6 5056 1 . GLN 7 7 5056 1 . GLY 8 8 5056 1 . ASN 9 9 5056 1 . GLU 10 10 5056 1 . CYS 11 11 5056 1 . LEU 12 12 5056 1 . LYS 13 13 5056 1 . GLU 14 14 5056 1 . TYR 15 15 5056 1 . GLY 16 16 5056 1 . GLY 17 17 5056 1 . ASP 18 18 5056 1 . VAL 19 19 5056 1 . GLY 20 20 5056 1 . PHE 21 21 5056 1 . GLY 22 22 5056 1 . PHE 23 23 5056 1 . CYS 24 24 5056 1 . ALA 25 25 5056 1 . PRO 26 26 5056 1 . ARG 27 27 5056 1 . ILE 28 28 5056 1 . PHE 29 29 5056 1 . PRO 30 30 5056 1 . THR 31 31 5056 1 . ILE 32 32 5056 1 . CYS 33 33 5056 1 . TYR 34 34 5056 1 . THR 35 35 5056 1 . ARG 36 36 5056 1 . CYS 37 37 5056 1 . ARG 38 38 5056 1 . GLU 39 39 5056 1 . ASN 40 40 5056 1 . LYS 41 41 5056 1 . GLY 42 42 5056 1 . ALA 43 43 5056 1 . LYS 44 44 5056 1 . GLY 45 45 5056 1 . GLY 46 46 5056 1 . ARG 47 47 5056 1 . CYS 48 48 5056 1 . ARG 49 49 5056 1 . TRP 50 50 5056 1 . GLY 51 51 5056 1 . GLN 52 52 5056 1 . GLY 53 53 5056 1 . SER 54 54 5056 1 . ASN 55 55 5056 1 . VAL 56 56 5056 1 . LYS 57 57 5056 1 . CYS 58 58 5056 1 . LEU 59 59 5056 1 . CYS 60 60 5056 1 . ASP 61 61 5056 1 . PHE 62 62 5056 1 . CYS 63 63 5056 1 . GLY 64 64 5056 1 . ASP 65 65 5056 1 . THR 66 66 5056 1 . PRO 67 67 5056 1 . GLN 68 68 5056 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 5056 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $ATT . 3702 . . 'Arabidopsis thaliana' 'thale cress' . . Eukaryota Virdiplanta Arabidopsis thaliana . . . . . . . . . . . . . 5056 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 5056 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $ATT . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 (DE3)/pLysS . . . . . . . . 5056 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5056 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; The protein was released from its n-terminal fusion partner (Snase) by CNBr cleaveage ; _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 ATT [U-15N] . . 1 $ATT . . 1.0 . . mM . . . . 5056 1 2 'sodium acetate' '[U-99% 2H]' . . . . . . 50 . . mM . . . . 5056 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5056 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details ; The protein was released from its n-terminal fusion partner (Snase) by CNBr cleaveage ; _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 ATT '[U-15N; U-13C]' . . 1 $ATT . . 1.0 . . mM . . . . 5056 2 2 'sodium acetate' '[U-99% 2H]' . . . . . . 50 . . mM . . . . 5056 2 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 5056 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 50 . mM 5056 1 pH 5.0 0.02 n/a 5056 1 pressure 1 . atm 5056 1 temperature 298 0.1 K 5056 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5056 _Software.ID 1 _Software.Type . _Software.Name XWINNMR _Software.Version 2.6 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data acquisition' 5056 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 5056 _Software.ID 2 _Software.Type . _Software.Name SPARKY _Software.Version 3.72 _Software.DOI . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignments 5056 2 'peak picking' 5056 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectromer1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectromer1 _NMR_spectrometer.Entry_ID 5056 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectromer2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectromer2 _NMR_spectrometer.Entry_ID 5056 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5056 _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 spectromer1 Bruker DMX . 500 . . . 5056 1 2 spectromer2 Bruker DMX . 600 . . . 5056 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 5056 _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 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 2 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 3 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 4 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 5 C(CO)NH-SE . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 6 H(CCO)NH-SE . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 7 HCCH-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 8 HCCH-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5056 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_csref _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode csref _Chem_shift_reference.Entry_ID 5056 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . 5056 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 5056 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . 5056 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_cstbl_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode cstbl_1 _Assigned_chem_shift_list.Entry_ID 5056 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $csref _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 HNCA . . . 5056 1 2 HN(CO)CA . . . 5056 1 3 HNCACB . . . 5056 1 4 HNCO . . . 5056 1 5 C(CO)NH-SE . . . 5056 1 6 H(CCO)NH-SE . . . 5056 1 7 HCCH-COSY . . . 5056 1 8 HCCH-TOCSY . . . 5056 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.Ambiguity_set_ID _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 2 2 PRO HA H 1 4.437 0.02 . 1 . . . . . . . . . 5056 1 2 . 1 1 2 2 PRO HB2 H 1 2.267 0.02 . 2 . . . . . . . . . 5056 1 3 . 1 1 2 2 PRO HB3 H 1 1.846 0.02 . 2 . . . . . . . . . 5056 1 4 . 1 1 2 2 PRO HG2 H 1 1.976 0.02 . 1 . . . . . . . . . 5056 1 5 . 1 1 2 2 PRO HG3 H 1 1.976 0.02 . 1 . . . . . . . . . 5056 1 6 . 1 1 2 2 PRO HD2 H 1 3.736 0.02 . 2 . . . . . . . . . 5056 1 7 . 1 1 2 2 PRO HD3 H 1 3.637 0.02 . 2 . . . . . . . . . 5056 1 8 . 1 1 2 2 PRO C C 13 176.19 0.05 . 1 . . . . . . . . . 5056 1 9 . 1 1 2 2 PRO CA C 13 63.289 0.05 . 1 . . . . . . . . . 5056 1 10 . 1 1 2 2 PRO CB C 13 31.992 0.05 . 1 . . . . . . . . . 5056 1 11 . 1 1 2 2 PRO CG C 13 27.179 0.05 . 1 . . . . . . . . . 5056 1 12 . 1 1 2 2 PRO CD C 13 50.626 0.05 . 1 . . . . . . . . . 5056 1 13 . 1 1 3 3 GLU H H 1 8.523 0.02 . 1 . . . . . . . . . 5056 1 14 . 1 1 3 3 GLU HA H 1 4.230 0.02 . 1 . . . . . . . . . 5056 1 15 . 1 1 3 3 GLU HB2 H 1 1.972 0.02 . 2 . . . . . . . . . 5056 1 16 . 1 1 3 3 GLU HB3 H 1 1.872 0.02 . 2 . . . . . . . . . 5056 1 17 . 1 1 3 3 GLU HG2 H 1 2.261 0.02 . 1 . . . . . . . . . 5056 1 18 . 1 1 3 3 GLU HG3 H 1 2.261 0.02 . 1 . . . . . . . . . 5056 1 19 . 1 1 3 3 GLU C C 13 176.32 0.05 . 1 . . . . . . . . . 5056 1 20 . 1 1 3 3 GLU CA C 13 56.562 0.05 . 1 . . . . . . . . . 5056 1 21 . 1 1 3 3 GLU CB C 13 29.810 0.05 . 1 . . . . . . . . . 5056 1 22 . 1 1 3 3 GLU CG C 13 35.439 0.05 . 1 . . . . . . . . . 5056 1 23 . 1 1 3 3 GLU N N 15 123.03 0.05 . 1 . . . . . . . . . 5056 1 24 . 1 1 4 4 ILE H H 1 8.126 0.02 . 1 . . . . . . . . . 5056 1 25 . 1 1 4 4 ILE HA H 1 4.082 0.02 . 1 . . . . . . . . . 5056 1 26 . 1 1 4 4 ILE HB H 1 1.777 0.02 . 1 . . . . . . . . . 5056 1 27 . 1 1 4 4 ILE HG12 H 1 1.394 0.02 . 2 . . . . . . . . . 5056 1 28 . 1 1 4 4 ILE HG13 H 1 1.123 0.02 . 2 . . . . . . . . . 5056 1 29 . 1 1 4 4 ILE HG21 H 1 0.812 0.02 . 1 . . . . . . . . . 5056 1 30 . 1 1 4 4 ILE HG22 H 1 0.812 0.02 . 1 . . . . . . . . . 5056 1 31 . 1 1 4 4 ILE HG23 H 1 0.812 0.02 . 1 . . . . . . . . . 5056 1 32 . 1 1 4 4 ILE HD11 H 1 0.795 0.02 . 1 . . . . . . . . . 5056 1 33 . 1 1 4 4 ILE HD12 H 1 0.795 0.02 . 1 . . . . . . . . . 5056 1 34 . 1 1 4 4 ILE HD13 H 1 0.795 0.02 . 1 . . . . . . . . . 5056 1 35 . 1 1 4 4 ILE C C 13 176.14 0.05 . 1 . . . . . . . . . 5056 1 36 . 1 1 4 4 ILE CA C 13 61.069 0.05 . 1 . . . . . . . . . 5056 1 37 . 1 1 4 4 ILE CB C 13 38.684 0.05 . 1 . . . . . . . . . 5056 1 38 . 1 1 4 4 ILE CG1 C 13 27.145 0.05 . 1 . . . . . . . . . 5056 1 39 . 1 1 4 4 ILE CG2 C 13 17.331 0.05 . 1 . . . . . . . . . 5056 1 40 . 1 1 4 4 ILE CD1 C 13 12.667 0.05 . 1 . . . . . . . . . 5056 1 41 . 1 1 4 4 ILE N N 15 122.90 0.05 . 1 . . . . . . . . . 5056 1 42 . 1 1 5 5 GLU H H 1 8.366 0.02 . 1 . . . . . . . . . 5056 1 43 . 1 1 5 5 GLU HA H 1 4.216 0.02 . 1 . . . . . . . . . 5056 1 44 . 1 1 5 5 GLU HB2 H 1 1.979 0.02 . 2 . . . . . . . . . 5056 1 45 . 1 1 5 5 GLU HB3 H 1 1.869 0.02 . 2 . . . . . . . . . 5056 1 46 . 1 1 5 5 GLU HG2 H 1 2.247 0.02 . 1 . . . . . . . . . 5056 1 47 . 1 1 5 5 GLU HG3 H 1 2.247 0.02 . 1 . . . . . . . . . 5056 1 48 . 1 1 5 5 GLU C C 13 176.00 0.05 . 1 . . . . . . . . . 5056 1 49 . 1 1 5 5 GLU CA C 13 56.280 0.05 . 1 . . . . . . . . . 5056 1 50 . 1 1 5 5 GLU CB C 13 29.810 0.05 . 1 . . . . . . . . . 5056 1 51 . 1 1 5 5 GLU CG C 13 35.330 0.05 . 1 . . . . . . . . . 5056 1 52 . 1 1 5 5 GLU N N 15 125.85 0.05 . 1 . . . . . . . . . 5056 1 53 . 1 1 6 6 ALA H H 1 8.255 0.02 . 1 . . . . . . . . . 5056 1 54 . 1 1 6 6 ALA HA H 1 4.231 0.02 . 1 . . . . . . . . . 5056 1 55 . 1 1 6 6 ALA HB1 H 1 1.316 0.02 . 1 . . . . . . . . . 5056 1 56 . 1 1 6 6 ALA HB2 H 1 1.316 0.02 . 1 . . . . . . . . . 5056 1 57 . 1 1 6 6 ALA HB3 H 1 1.316 0.02 . 1 . . . . . . . . . 5056 1 58 . 1 1 6 6 ALA C C 13 177.52 0.05 . 1 . . . . . . . . . 5056 1 59 . 1 1 6 6 ALA CA C 13 52.557 0.05 . 1 . . . . . . . . . 5056 1 60 . 1 1 6 6 ALA CB C 13 19.202 0.05 . 1 . . . . . . . . . 5056 1 61 . 1 1 6 6 ALA N N 15 126.41 0.05 . 1 . . . . . . . . . 5056 1 62 . 1 1 7 7 GLN H H 1 8.278 0.02 . 1 . . . . . . . . . 5056 1 63 . 1 1 7 7 GLN HA H 1 4.267 0.02 . 1 . . . . . . . . . 5056 1 64 . 1 1 7 7 GLN HB2 H 1 2.079 0.02 . 2 . . . . . . . . . 5056 1 65 . 1 1 7 7 GLN HB3 H 1 1.920 0.02 . 2 . . . . . . . . . 5056 1 66 . 1 1 7 7 GLN HG2 H 1 2.308 0.02 . 1 . . . . . . . . . 5056 1 67 . 1 1 7 7 GLN HG3 H 1 2.308 0.02 . 1 . . . . . . . . . 5056 1 68 . 1 1 7 7 GLN HE21 H 1 7.462 0.02 . 2 . . . . . . . . . 5056 1 69 . 1 1 7 7 GLN HE22 H 1 6.780 0.02 . 2 . . . . . . . . . 5056 1 70 . 1 1 7 7 GLN C C 13 176.50 0.05 . 1 . . . . . . . . . 5056 1 71 . 1 1 7 7 GLN CA C 13 55.909 0.05 . 1 . . . . . . . . . 5056 1 72 . 1 1 7 7 GLN CB C 13 29.461 0.05 . 1 . . . . . . . . . 5056 1 73 . 1 1 7 7 GLN CG C 13 33.890 0.05 . 1 . . . . . . . . . 5056 1 74 . 1 1 7 7 GLN CD C 13 180.45 0.05 . 1 . . . . . . . . . 5056 1 75 . 1 1 7 7 GLN N N 15 120.25 0.05 . 1 . . . . . . . . . 5056 1 76 . 1 1 8 8 GLY H H 1 8.376 0.02 . 1 . . . . . . . . . 5056 1 77 . 1 1 8 8 GLY HA2 H 1 3.924 0.02 . 2 . . . . . . . . . 5056 1 78 . 1 1 8 8 GLY HA3 H 1 3.832 0.02 . 2 . . . . . . . . . 5056 1 79 . 1 1 8 8 GLY C C 13 174.09 0.05 . 1 . . . . . . . . . 5056 1 80 . 1 1 8 8 GLY CA C 13 45.477 0.05 . 1 . . . . . . . . . 5056 1 81 . 1 1 8 8 GLY N N 15 110.91 0.05 . 1 . . . . . . . . . 5056 1 82 . 1 1 9 9 ASN H H 1 8.304 0.02 . 1 . . . . . . . . . 5056 1 83 . 1 1 9 9 ASN HA H 1 4.618 0.02 . 1 . . . . . . . . . 5056 1 84 . 1 1 9 9 ASN HB2 H 1 2.760 0.02 . 1 . . . . . . . . . 5056 1 85 . 1 1 9 9 ASN HB3 H 1 2.760 0.02 . 1 . . . . . . . . . 5056 1 86 . 1 1 9 9 ASN HD21 H 1 7.566 0.02 . 2 . . . . . . . . . 5056 1 87 . 1 1 9 9 ASN HD22 H 1 6.874 0.02 . 2 . . . . . . . . . 5056 1 88 . 1 1 9 9 ASN C C 13 175.49 0.05 . 1 . . . . . . . . . 5056 1 89 . 1 1 9 9 ASN CA C 13 53.478 0.05 . 1 . . . . . . . . . 5056 1 90 . 1 1 9 9 ASN CB C 13 38.864 0.05 . 1 . . . . . . . . . 5056 1 91 . 1 1 9 9 ASN CG C 13 177.05 0.05 . 1 . . . . . . . . . 5056 1 92 . 1 1 9 9 ASN N N 15 120.08 0.05 . 1 . . . . . . . . . 5056 1 93 . 1 1 9 9 ASN ND2 N 15 114.05 0.05 . 1 . . . . . . . . . 5056 1 94 . 1 1 10 10 GLU H H 1 8.598 0.02 . 1 . . . . . . . . . 5056 1 95 . 1 1 10 10 GLU HA H 1 4.263 0.02 . 1 . . . . . . . . . 5056 1 96 . 1 1 10 10 GLU HB2 H 1 2.067 0.02 . 2 . . . . . . . . . 5056 1 97 . 1 1 10 10 GLU HB3 H 1 1.905 0.02 . 2 . . . . . . . . . 5056 1 98 . 1 1 10 10 GLU HG2 H 1 2.227 0.02 . 1 . . . . . . . . . 5056 1 99 . 1 1 10 10 GLU HG3 H 1 2.227 0.02 . 1 . . . . . . . . . 5056 1 100 . 1 1 10 10 GLU C C 13 176.63 0.05 . 1 . . . . . . . . . 5056 1 101 . 1 1 10 10 GLU CA C 13 56.915 0.05 . 1 . . . . . . . . . 5056 1 102 . 1 1 10 10 GLU CB C 13 29.204 0.05 . 1 . . . . . . . . . 5056 1 103 . 1 1 10 10 GLU CG C 13 35.492 0.05 . 1 . . . . . . . . . 5056 1 104 . 1 1 10 10 GLU N N 15 121.61 0.05 . 1 . . . . . . . . . 5056 1 105 . 1 1 11 11 CYS H H 1 8.185 0.02 . 1 . . . . . . . . . 5056 1 106 . 1 1 11 11 CYS HA H 1 4.551 0.02 . 1 . . . . . . . . . 5056 1 107 . 1 1 11 11 CYS HB2 H 1 3.086 0.02 . 1 . . . . . . . . . 5056 1 108 . 1 1 11 11 CYS HB3 H 1 2.949 0.02 . 1 . . . . . . . . . 5056 1 109 . 1 1 11 11 CYS C C 13 173.92 0.05 . 1 . . . . . . . . . 5056 1 110 . 1 1 11 11 CYS CA C 13 57.120 0.05 . 1 . . . . . . . . . 5056 1 111 . 1 1 11 11 CYS CB C 13 41.472 0.05 . 1 . . . . . . . . . 5056 1 112 . 1 1 11 11 CYS N N 15 118.19 0.05 . 1 . . . . . . . . . 5056 1 113 . 1 1 12 12 LEU H H 1 7.779 0.02 . 1 . . . . . . . . . 5056 1 114 . 1 1 12 12 LEU HA H 1 5.633 0.02 . 1 . . . . . . . . . 5056 1 115 . 1 1 12 12 LEU HB2 H 1 1.742 0.02 . 1 . . . . . . . . . 5056 1 116 . 1 1 12 12 LEU HB3 H 1 1.152 0.02 . 1 . . . . . . . . . 5056 1 117 . 1 1 12 12 LEU HG H 1 0.769 0.02 . 1 . . . . . . . . . 5056 1 118 . 1 1 12 12 LEU HD11 H 1 1.488 0.02 . 1 . . . . . . . . . 5056 1 119 . 1 1 12 12 LEU HD12 H 1 1.488 0.02 . 1 . . . . . . . . . 5056 1 120 . 1 1 12 12 LEU HD13 H 1 1.488 0.02 . 1 . . . . . . . . . 5056 1 121 . 1 1 12 12 LEU HD21 H 1 0.718 0.02 . 1 . . . . . . . . . 5056 1 122 . 1 1 12 12 LEU HD22 H 1 0.718 0.02 . 1 . . . . . . . . . 5056 1 123 . 1 1 12 12 LEU HD23 H 1 0.718 0.02 . 1 . . . . . . . . . 5056 1 124 . 1 1 12 12 LEU C C 13 176.65 0.05 . 1 . . . . . . . . . 5056 1 125 . 1 1 12 12 LEU CA C 13 53.190 0.05 . 1 . . . . . . . . . 5056 1 126 . 1 1 12 12 LEU CB C 13 43.766 0.05 . 1 . . . . . . . . . 5056 1 127 . 1 1 12 12 LEU CG C 13 25.617 0.05 . 1 . . . . . . . . . 5056 1 128 . 1 1 12 12 LEU CD1 C 13 23.054 0.05 . 1 . . . . . . . . . 5056 1 129 . 1 1 12 12 LEU CD2 C 13 23.054 0.05 . 1 . . . . . . . . . 5056 1 130 . 1 1 12 12 LEU N N 15 119.94 0.05 . 1 . . . . . . . . . 5056 1 131 . 1 1 13 13 LYS H H 1 8.885 0.02 . 1 . . . . . . . . . 5056 1 132 . 1 1 13 13 LYS HA H 1 4.661 0.02 . 1 . . . . . . . . . 5056 1 133 . 1 1 13 13 LYS HB2 H 1 1.812 0.02 . 1 . . . . . . . . . 5056 1 134 . 1 1 13 13 LYS HB3 H 1 1.727 0.02 . 1 . . . . . . . . . 5056 1 135 . 1 1 13 13 LYS HG2 H 1 1.338 0.02 . 1 . . . . . . . . . 5056 1 136 . 1 1 13 13 LYS HG3 H 1 1.338 0.02 . 1 . . . . . . . . . 5056 1 137 . 1 1 13 13 LYS HD2 H 1 1.532 0.02 . 2 . . . . . . . . . 5056 1 138 . 1 1 13 13 LYS HD3 H 1 1.392 0.02 . 2 . . . . . . . . . 5056 1 139 . 1 1 13 13 LYS HE2 H 1 2.725 0.02 . 1 . . . . . . . . . 5056 1 140 . 1 1 13 13 LYS HE3 H 1 2.725 0.02 . 1 . . . . . . . . . 5056 1 141 . 1 1 13 13 LYS C C 13 175.90 0.05 . 1 . . . . . . . . . 5056 1 142 . 1 1 13 13 LYS CA C 13 54.441 0.05 . 1 . . . . . . . . . 5056 1 143 . 1 1 13 13 LYS CB C 13 36.511 0.05 . 1 . . . . . . . . . 5056 1 144 . 1 1 13 13 LYS CG C 13 24.391 0.05 . 1 . . . . . . . . . 5056 1 145 . 1 1 13 13 LYS CD C 13 29.019 0.05 . 1 . . . . . . . . . 5056 1 146 . 1 1 13 13 LYS CE C 13 42.021 0.05 . 1 . . . . . . . . . 5056 1 147 . 1 1 13 13 LYS N N 15 122.74 0.05 . 1 . . . . . . . . . 5056 1 148 . 1 1 14 14 GLU H H 1 9.169 0.02 . 1 . . . . . . . . . 5056 1 149 . 1 1 14 14 GLU HA H 1 4.481 0.02 . 1 . . . . . . . . . 5056 1 150 . 1 1 14 14 GLU HB2 H 1 2.033 0.02 . 1 . . . . . . . . . 5056 1 151 . 1 1 14 14 GLU HB3 H 1 2.033 0.02 . 1 . . . . . . . . . 5056 1 152 . 1 1 14 14 GLU HG2 H 1 2.196 0.02 . 1 . . . . . . . . . 5056 1 153 . 1 1 14 14 GLU HG3 H 1 2.196 0.02 . 1 . . . . . . . . . 5056 1 154 . 1 1 14 14 GLU C C 13 176.60 0.05 . 1 . . . . . . . . . 5056 1 155 . 1 1 14 14 GLU CA C 13 57.695 0.05 . 1 . . . . . . . . . 5056 1 156 . 1 1 14 14 GLU CB C 13 29.982 0.05 . 1 . . . . . . . . . 5056 1 157 . 1 1 14 14 GLU CG C 13 36.958 0.05 . 1 . . . . . . . . . 5056 1 158 . 1 1 14 14 GLU N N 15 125.82 0.05 . 1 . . . . . . . . . 5056 1 159 . 1 1 15 15 TYR H H 1 8.631 0.02 . 1 . . . . . . . . . 5056 1 160 . 1 1 15 15 TYR HA H 1 3.898 0.02 . 1 . . . . . . . . . 5056 1 161 . 1 1 15 15 TYR HB2 H 1 2.865 0.02 . 1 . . . . . . . . . 5056 1 162 . 1 1 15 15 TYR HB3 H 1 2.649 0.02 . 1 . . . . . . . . . 5056 1 163 . 1 1 15 15 TYR C C 13 175.75 0.05 . 1 . . . . . . . . . 5056 1 164 . 1 1 15 15 TYR CA C 13 62.521 0.05 . 1 . . . . . . . . . 5056 1 165 . 1 1 15 15 TYR CB C 13 39.014 0.05 . 1 . . . . . . . . . 5056 1 166 . 1 1 15 15 TYR N N 15 125.52 0.05 . 1 . . . . . . . . . 5056 1 167 . 1 1 16 16 GLY H H 1 8.457 0.02 . 1 . . . . . . . . . 5056 1 168 . 1 1 16 16 GLY HA2 H 1 4.445 0.02 . 2 . . . . . . . . . 5056 1 169 . 1 1 16 16 GLY HA3 H 1 3.473 0.02 . 2 . . . . . . . . . 5056 1 170 . 1 1 16 16 GLY C C 13 174.38 0.05 . 1 . . . . . . . . . 5056 1 171 . 1 1 16 16 GLY CA C 13 44.722 0.05 . 1 . . . . . . . . . 5056 1 172 . 1 1 16 16 GLY N N 15 107.93 0.05 . 1 . . . . . . . . . 5056 1 173 . 1 1 17 17 GLY H H 1 8.478 0.02 . 1 . . . . . . . . . 5056 1 174 . 1 1 17 17 GLY HA2 H 1 4.181 0.02 . 2 . . . . . . . . . 5056 1 175 . 1 1 17 17 GLY HA3 H 1 3.783 0.02 . 2 . . . . . . . . . 5056 1 176 . 1 1 17 17 GLY C C 13 175.08 0.05 . 1 . . . . . . . . . 5056 1 177 . 1 1 17 17 GLY CA C 13 44.034 0.05 . 1 . . . . . . . . . 5056 1 178 . 1 1 17 17 GLY N N 15 113.21 0.05 . 1 . . . . . . . . . 5056 1 179 . 1 1 18 18 ASP H H 1 8.727 0.02 . 1 . . . . . . . . . 5056 1 180 . 1 1 18 18 ASP HA H 1 4.901 0.02 . 1 . . . . . . . . . 5056 1 181 . 1 1 18 18 ASP HB2 H 1 2.768 0.02 . 1 . . . . . . . . . 5056 1 182 . 1 1 18 18 ASP HB3 H 1 2.456 0.02 . 1 . . . . . . . . . 5056 1 183 . 1 1 18 18 ASP C C 13 177.07 0.05 . 1 . . . . . . . . . 5056 1 184 . 1 1 18 18 ASP CA C 13 53.512 0.05 . 1 . . . . . . . . . 5056 1 185 . 1 1 18 18 ASP CB C 13 38.793 0.05 . 1 . . . . . . . . . 5056 1 186 . 1 1 18 18 ASP N N 15 123.10 0.05 . 1 . . . . . . . . . 5056 1 187 . 1 1 19 19 VAL H H 1 7.137 0.02 . 1 . . . . . . . . . 5056 1 188 . 1 1 19 19 VAL HA H 1 3.855 0.02 . 1 . . . . . . . . . 5056 1 189 . 1 1 19 19 VAL HB H 1 0.280 0.02 . 1 . . . . . . . . . 5056 1 190 . 1 1 19 19 VAL HG11 H 1 0.469 0.02 . 1 . . . . . . . . . 5056 1 191 . 1 1 19 19 VAL HG12 H 1 0.469 0.02 . 1 . . . . . . . . . 5056 1 192 . 1 1 19 19 VAL HG13 H 1 0.469 0.02 . 1 . . . . . . . . . 5056 1 193 . 1 1 19 19 VAL HG21 H 1 0.127 0.02 . 1 . . . . . . . . . 5056 1 194 . 1 1 19 19 VAL HG22 H 1 0.127 0.02 . 1 . . . . . . . . . 5056 1 195 . 1 1 19 19 VAL HG23 H 1 0.127 0.02 . 1 . . . . . . . . . 5056 1 196 . 1 1 19 19 VAL C C 13 176.85 0.05 . 1 . . . . . . . . . 5056 1 197 . 1 1 19 19 VAL CA C 13 60.635 0.05 . 1 . . . . . . . . . 5056 1 198 . 1 1 19 19 VAL CB C 13 31.844 0.05 . 1 . . . . . . . . . 5056 1 199 . 1 1 19 19 VAL CG1 C 13 20.543 0.05 . 1 . . . . . . . . . 5056 1 200 . 1 1 19 19 VAL CG2 C 13 18.054 0.05 . 1 . . . . . . . . . 5056 1 201 . 1 1 19 19 VAL N N 15 112.03 0.05 . 1 . . . . . . . . . 5056 1 202 . 1 1 20 20 GLY H H 1 8.305 0.02 . 1 . . . . . . . . . 5056 1 203 . 1 1 20 20 GLY HA2 H 1 3.689 0.02 . 2 . . . . . . . . . 5056 1 204 . 1 1 20 20 GLY HA3 H 1 2.977 0.02 . 2 . . . . . . . . . 5056 1 205 . 1 1 20 20 GLY C C 13 174.26 0.05 . 1 . . . . . . . . . 5056 1 206 . 1 1 20 20 GLY CA C 13 48.137 0.05 . 1 . . . . . . . . . 5056 1 207 . 1 1 20 20 GLY N N 15 110.14 0.05 . 1 . . . . . . . . . 5056 1 208 . 1 1 21 21 PHE H H 1 8.770 0.02 . 1 . . . . . . . . . 5056 1 209 . 1 1 21 21 PHE HA H 1 3.649 0.02 . 1 . . . . . . . . . 5056 1 210 . 1 1 21 21 PHE HB2 H 1 3.013 0.02 . 1 . . . . . . . . . 5056 1 211 . 1 1 21 21 PHE HB3 H 1 2.882 0.02 . 1 . . . . . . . . . 5056 1 212 . 1 1 21 21 PHE C C 13 178.17 0.05 . 1 . . . . . . . . . 5056 1 213 . 1 1 21 21 PHE CA C 13 63.156 0.05 . 1 . . . . . . . . . 5056 1 214 . 1 1 21 21 PHE CB C 13 38.697 0.05 . 1 . . . . . . . . . 5056 1 215 . 1 1 21 21 PHE N N 15 123.76 0.05 . 1 . . . . . . . . . 5056 1 216 . 1 1 22 22 GLY H H 1 8.480 0.02 . 1 . . . . . . . . . 5056 1 217 . 1 1 22 22 GLY HA2 H 1 3.812 0.02 . 1 . . . . . . . . . 5056 1 218 . 1 1 22 22 GLY HA3 H 1 3.812 0.02 . 1 . . . . . . . . . 5056 1 219 . 1 1 22 22 GLY C C 13 175.69 0.05 . 1 . . . . . . . . . 5056 1 220 . 1 1 22 22 GLY CA C 13 46.485 0.05 . 1 . . . . . . . . . 5056 1 221 . 1 1 22 22 GLY N N 15 107.01 0.05 . 1 . . . . . . . . . 5056 1 222 . 1 1 23 23 PHE H H 1 7.898 0.02 . 1 . . . . . . . . . 5056 1 223 . 1 1 23 23 PHE HA H 1 4.746 0.02 . 1 . . . . . . . . . 5056 1 224 . 1 1 23 23 PHE HB2 H 1 2.933 0.02 . 2 . . . . . . . . . 5056 1 225 . 1 1 23 23 PHE HB3 H 1 2.680 0.02 . 2 . . . . . . . . . 5056 1 226 . 1 1 23 23 PHE C C 13 178.23 0.05 . 1 . . . . . . . . . 5056 1 227 . 1 1 23 23 PHE CA C 13 54.720 0.05 . 1 . . . . . . . . . 5056 1 228 . 1 1 23 23 PHE CB C 13 36.779 0.05 . 1 . . . . . . . . . 5056 1 229 . 1 1 23 23 PHE N N 15 115.85 0.05 . 1 . . . . . . . . . 5056 1 230 . 1 1 24 24 CYS H H 1 8.175 0.02 . 1 . . . . . . . . . 5056 1 231 . 1 1 24 24 CYS HA H 1 4.908 0.02 . 1 . . . . . . . . . 5056 1 232 . 1 1 24 24 CYS HB2 H 1 2.83 0.02 . 1 . . . . . . . . . 5056 1 233 . 1 1 24 24 CYS HB3 H 1 2.55 0.02 . 1 . . . . . . . . . 5056 1 234 . 1 1 24 24 CYS C C 13 173.28 0.05 . 1 . . . . . . . . . 5056 1 235 . 1 1 24 24 CYS CA C 13 56.840 0.05 . 1 . . . . . . . . . 5056 1 236 . 1 1 24 24 CYS CB C 13 45.666 0.05 . 1 . . . . . . . . . 5056 1 237 . 1 1 24 24 CYS N N 15 119.11 0.05 . 1 . . . . . . . . . 5056 1 238 . 1 1 25 25 ALA H H 1 8.604 0.02 . 1 . . . . . . . . . 5056 1 239 . 1 1 25 25 ALA CA C 13 55.236 0.05 . 1 . . . . . . . . . 5056 1 240 . 1 1 25 25 ALA N N 15 125.68 0.05 . 1 . . . . . . . . . 5056 1 241 . 1 1 27 27 ARG HA H 1 4.272 0.02 . 1 . . . . . . . . . 5056 1 242 . 1 1 27 27 ARG HB2 H 1 1.801 0.02 . 1 . . . . . . . . . 5056 1 243 . 1 1 27 27 ARG HB3 H 1 1.739 0.02 . 1 . . . . . . . . . 5056 1 244 . 1 1 27 27 ARG HG2 H 1 1.635 0.02 . 2 . . . . . . . . . 5056 1 245 . 1 1 27 27 ARG HG3 H 1 1.523 0.02 . 2 . . . . . . . . . 5056 1 246 . 1 1 27 27 ARG HD2 H 1 3.153 0.02 . 1 . . . . . . . . . 5056 1 247 . 1 1 27 27 ARG HD3 H 1 3.153 0.02 . 1 . . . . . . . . . 5056 1 248 . 1 1 27 27 ARG HE H 1 7.040 0.02 . 1 . . . . . . . . . 5056 1 249 . 1 1 27 27 ARG CA C 13 55.338 0.05 . 1 . . . . . . . . . 5056 1 250 . 1 1 27 27 ARG CB C 13 27.93 0.05 . 1 . . . . . . . . . 5056 1 251 . 1 1 27 27 ARG CG C 13 26.469 0.05 . 1 . . . . . . . . . 5056 1 252 . 1 1 27 27 ARG CD C 13 43.259 0.05 . 1 . . . . . . . . . 5056 1 253 . 1 1 28 28 ILE H H 1 7.345 0.02 . 1 . . . . . . . . . 5056 1 254 . 1 1 28 28 ILE HA H 1 4.156 0.02 . 1 . . . . . . . . . 5056 1 255 . 1 1 28 28 ILE HB H 1 1.554 0.02 . 1 . . . . . . . . . 5056 1 256 . 1 1 28 28 ILE HG12 H 1 1.312 0.02 . 2 . . . . . . . . . 5056 1 257 . 1 1 28 28 ILE HG13 H 1 0.929 0.02 . 2 . . . . . . . . . 5056 1 258 . 1 1 28 28 ILE HG21 H 1 0.792 0.02 . 1 . . . . . . . . . 5056 1 259 . 1 1 28 28 ILE HG22 H 1 0.792 0.02 . 1 . . . . . . . . . 5056 1 260 . 1 1 28 28 ILE HG23 H 1 0.792 0.02 . 1 . . . . . . . . . 5056 1 261 . 1 1 28 28 ILE HD11 H 1 0.765 0.02 . 1 . . . . . . . . . 5056 1 262 . 1 1 28 28 ILE HD12 H 1 0.765 0.02 . 1 . . . . . . . . . 5056 1 263 . 1 1 28 28 ILE HD13 H 1 0.765 0.02 . 1 . . . . . . . . . 5056 1 264 . 1 1 28 28 ILE CA C 13 59.530 0.05 . 1 . . . . . . . . . 5056 1 265 . 1 1 28 28 ILE CB C 13 41.016 0.05 . 1 . . . . . . . . . 5056 1 266 . 1 1 28 28 ILE CG1 C 13 27.028 0.05 . 1 . . . . . . . . . 5056 1 267 . 1 1 28 28 ILE CG2 C 13 16.061 0.05 . 1 . . . . . . . . . 5056 1 268 . 1 1 28 28 ILE CD1 C 13 13.065 0.05 . 1 . . . . . . . . . 5056 1 269 . 1 1 28 28 ILE N N 15 125.06 0.05 . 1 . . . . . . . . . 5056 1 270 . 1 1 29 29 PHE H H 1 8.102 0.02 . 1 . . . . . . . . . 5056 1 271 . 1 1 29 29 PHE CA C 13 54.462 0.05 . 1 . . . . . . . . . 5056 1 272 . 1 1 29 29 PHE CB C 13 42.168 0.05 . 1 . . . . . . . . . 5056 1 273 . 1 1 29 29 PHE N N 15 125.52 0.05 . 1 . . . . . . . . . 5056 1 274 . 1 1 30 30 PRO HA H 1 3.712 0.02 . 1 . . . . . . . . . 5056 1 275 . 1 1 30 30 PRO HB2 H 1 1.449 0.02 . 1 . . . . . . . . . 5056 1 276 . 1 1 30 30 PRO HB3 H 1 1.237 0.02 . 1 . . . . . . . . . 5056 1 277 . 1 1 30 30 PRO HG2 H 1 1.449 0.02 . 2 . . . . . . . . . 5056 1 278 . 1 1 30 30 PRO HG3 H 1 1.168 0.02 . 2 . . . . . . . . . 5056 1 279 . 1 1 30 30 PRO HD2 H 1 3.229 0.02 . 2 . . . . . . . . . 5056 1 280 . 1 1 30 30 PRO HD3 H 1 3.053 0.02 . 2 . . . . . . . . . 5056 1 281 . 1 1 30 30 PRO C C 13 175.36 0.05 . 1 . . . . . . . . . 5056 1 282 . 1 1 30 30 PRO CA C 13 62.685 0.05 . 1 . . . . . . . . . 5056 1 283 . 1 1 30 30 PRO CB C 13 34.247 0.05 . 1 . . . . . . . . . 5056 1 284 . 1 1 30 30 PRO CG C 13 24.93 0.05 . 1 . . . . . . . . . 5056 1 285 . 1 1 30 30 PRO CD C 13 49.244 0.05 . 1 . . . . . . . . . 5056 1 286 . 1 1 31 31 THR H H 1 8.309 0.02 . 1 . . . . . . . . . 5056 1 287 . 1 1 31 31 THR HA H 1 4.159 0.02 . 1 . . . . . . . . . 5056 1 288 . 1 1 31 31 THR HB H 1 4.570 0.02 . 1 . . . . . . . . . 5056 1 289 . 1 1 31 31 THR HG21 H 1 1.682 0.02 . 1 . . . . . . . . . 5056 1 290 . 1 1 31 31 THR HG22 H 1 1.682 0.02 . 1 . . . . . . . . . 5056 1 291 . 1 1 31 31 THR HG23 H 1 1.682 0.02 . 1 . . . . . . . . . 5056 1 292 . 1 1 31 31 THR C C 13 175.42 0.05 . 1 . . . . . . . . . 5056 1 293 . 1 1 31 31 THR CA C 13 62.098 0.05 . 1 . . . . . . . . . 5056 1 294 . 1 1 31 31 THR CB C 13 71.837 0.05 . 1 . . . . . . . . . 5056 1 295 . 1 1 31 31 THR CG2 C 13 22.108 0.05 . 1 . . . . . . . . . 5056 1 296 . 1 1 31 31 THR N N 15 110.76 0.05 . 1 . . . . . . . . . 5056 1 297 . 1 1 32 32 ILE H H 1 8.259 0.02 . 1 . . . . . . . . . 5056 1 298 . 1 1 32 32 ILE HA H 1 3.474 0.02 . 1 . . . . . . . . . 5056 1 299 . 1 1 32 32 ILE HB H 1 2.048 0.02 . 1 . . . . . . . . . 5056 1 300 . 1 1 32 32 ILE HG12 H 1 1.580 0.02 . 2 . . . . . . . . . 5056 1 301 . 1 1 32 32 ILE HG13 H 1 1.033 0.02 . 2 . . . . . . . . . 5056 1 302 . 1 1 32 32 ILE HG21 H 1 0.303 0.02 . 1 . . . . . . . . . 5056 1 303 . 1 1 32 32 ILE HG22 H 1 0.303 0.02 . 1 . . . . . . . . . 5056 1 304 . 1 1 32 32 ILE HG23 H 1 0.303 0.02 . 1 . . . . . . . . . 5056 1 305 . 1 1 32 32 ILE HD11 H 1 0.833 0.02 . 1 . . . . . . . . . 5056 1 306 . 1 1 32 32 ILE HD12 H 1 0.833 0.02 . 1 . . . . . . . . . 5056 1 307 . 1 1 32 32 ILE HD13 H 1 0.833 0.02 . 1 . . . . . . . . . 5056 1 308 . 1 1 32 32 ILE C C 13 177.61 0.05 . 1 . . . . . . . . . 5056 1 309 . 1 1 32 32 ILE CA C 13 64.933 0.05 . 1 . . . . . . . . . 5056 1 310 . 1 1 32 32 ILE CB C 13 36.536 0.05 . 1 . . . . . . . . . 5056 1 311 . 1 1 32 32 ILE CG1 C 13 28.788 0.05 . 1 . . . . . . . . . 5056 1 312 . 1 1 32 32 ILE CG2 C 13 18.187 0.05 . 1 . . . . . . . . . 5056 1 313 . 1 1 32 32 ILE CD1 C 13 18.187 0.05 . 1 . . . . . . . . . 5056 1 314 . 1 1 32 32 ILE N N 15 121.66 0.05 . 1 . . . . . . . . . 5056 1 315 . 1 1 33 33 CYS H H 1 7.154 0.02 . 1 . . . . . . . . . 5056 1 316 . 1 1 33 33 CYS HA H 1 3.891 0.02 . 1 . . . . . . . . . 5056 1 317 . 1 1 33 33 CYS HB2 H 1 2.865 0.02 . 1 . . . . . . . . . 5056 1 318 . 1 1 33 33 CYS HB3 H 1 2.700 0.02 . 1 . . . . . . . . . 5056 1 319 . 1 1 33 33 CYS C C 13 173.40 0.05 . 1 . . . . . . . . . 5056 1 320 . 1 1 33 33 CYS CA C 13 58.473 0.05 . 1 . . . . . . . . . 5056 1 321 . 1 1 33 33 CYS CB C 13 37.937 0.05 . 1 . . . . . . . . . 5056 1 322 . 1 1 33 33 CYS N N 15 115.09 0.05 . 1 . . . . . . . . . 5056 1 323 . 1 1 34 34 TYR H H 1 7.813 0.02 . 1 . . . . . . . . . 5056 1 324 . 1 1 34 34 TYR HA H 1 3.373 0.02 . 1 . . . . . . . . . 5056 1 325 . 1 1 34 34 TYR HB2 H 1 3.401 0.02 . 1 . . . . . . . . . 5056 1 326 . 1 1 34 34 TYR HB3 H 1 2.825 0.02 . 1 . . . . . . . . . 5056 1 327 . 1 1 34 34 TYR C C 13 176.25 0.05 . 1 . . . . . . . . . 5056 1 328 . 1 1 34 34 TYR CA C 13 62.219 0.05 . 1 . . . . . . . . . 5056 1 329 . 1 1 34 34 TYR CB C 13 37.994 0.05 . 1 . . . . . . . . . 5056 1 330 . 1 1 34 34 TYR N N 15 121.82 0.05 . 1 . . . . . . . . . 5056 1 331 . 1 1 35 35 THR H H 1 7.987 0.02 . 1 . . . . . . . . . 5056 1 332 . 1 1 35 35 THR HA H 1 3.584 0.02 . 1 . . . . . . . . . 5056 1 333 . 1 1 35 35 THR HB H 1 3.942 0.02 . 1 . . . . . . . . . 5056 1 334 . 1 1 35 35 THR HG21 H 1 1.058 0.02 . 1 . . . . . . . . . 5056 1 335 . 1 1 35 35 THR HG22 H 1 1.058 0.02 . 1 . . . . . . . . . 5056 1 336 . 1 1 35 35 THR HG23 H 1 1.058 0.02 . 1 . . . . . . . . . 5056 1 337 . 1 1 35 35 THR C C 13 176.52 0.05 . 1 . . . . . . . . . 5056 1 338 . 1 1 35 35 THR CA C 13 66.731 0.05 . 1 . . . . . . . . . 5056 1 339 . 1 1 35 35 THR CB C 13 68.614 0.05 . 1 . . . . . . . . . 5056 1 340 . 1 1 35 35 THR CG2 C 13 21.906 0.05 . 1 . . . . . . . . . 5056 1 341 . 1 1 35 35 THR N N 15 117.55 0.05 . 1 . . . . . . . . . 5056 1 342 . 1 1 36 36 ARG H H 1 9.190 0.02 . 1 . . . . . . . . . 5056 1 343 . 1 1 36 36 ARG HA H 1 3.962 0.02 . 1 . . . . . . . . . 5056 1 344 . 1 1 36 36 ARG HB2 H 1 1.474 0.02 . 1 . . . . . . . . . 5056 1 345 . 1 1 36 36 ARG HB3 H 1 1.236 0.02 . 1 . . . . . . . . . 5056 1 346 . 1 1 36 36 ARG HD2 H 1 2.879 0.02 . 2 . . . . . . . . . 5056 1 347 . 1 1 36 36 ARG HD3 H 1 2.501 0.02 . 2 . . . . . . . . . 5056 1 348 . 1 1 36 36 ARG HE H 1 6.874 0.02 . 1 . . . . . . . . . 5056 1 349 . 1 1 36 36 ARG C C 13 180.40 0.05 . 1 . . . . . . . . . 5056 1 350 . 1 1 36 36 ARG CA C 13 58.123 0.05 . 1 . . . . . . . . . 5056 1 351 . 1 1 36 36 ARG CB C 13 28.906 0.05 . 1 . . . . . . . . . 5056 1 352 . 1 1 36 36 ARG CG C 13 26.842 0.05 . 1 . . . . . . . . . 5056 1 353 . 1 1 36 36 ARG N N 15 121.56 0.05 . 1 . . . . . . . . . 5056 1 354 . 1 1 37 37 CYS H H 1 8.588 0.02 . 1 . . . . . . . . . 5056 1 355 . 1 1 37 37 CYS HA H 1 4.136 0.02 . 1 . . . . . . . . . 5056 1 356 . 1 1 37 37 CYS HB2 H 1 2.695 0.02 . 1 . . . . . . . . . 5056 1 357 . 1 1 37 37 CYS HB3 H 1 2.310 0.02 . 1 . . . . . . . . . 5056 1 358 . 1 1 37 37 CYS C C 13 177.51 0.05 . 1 . . . . . . . . . 5056 1 359 . 1 1 37 37 CYS CA C 13 60.232 0.05 . 1 . . . . . . . . . 5056 1 360 . 1 1 37 37 CYS CB C 13 37.353 0.05 . 1 . . . . . . . . . 5056 1 361 . 1 1 37 37 CYS N N 15 120.37 0.05 . 1 . . . . . . . . . 5056 1 362 . 1 1 38 38 ARG H H 1 7.341 0.02 . 1 . . . . . . . . . 5056 1 363 . 1 1 38 38 ARG HA H 1 3.934 0.02 . 1 . . . . . . . . . 5056 1 364 . 1 1 38 38 ARG HB2 H 1 1.664 0.02 . 1 . . . . . . . . . 5056 1 365 . 1 1 38 38 ARG HB3 H 1 1.534 0.02 . 1 . . . . . . . . . 5056 1 366 . 1 1 38 38 ARG HG2 H 1 1.007 0.02 . 2 . . . . . . . . . 5056 1 367 . 1 1 38 38 ARG HG3 H 1 0.864 0.02 . 2 . . . . . . . . . 5056 1 368 . 1 1 38 38 ARG HD2 H 1 2.647 0.02 . 2 . . . . . . . . . 5056 1 369 . 1 1 38 38 ARG HD3 H 1 2.395 0.02 . 2 . . . . . . . . . 5056 1 370 . 1 1 38 38 ARG C C 13 178.69 0.05 . 1 . . . . . . . . . 5056 1 371 . 1 1 38 38 ARG CA C 13 59.439 0.05 . 1 . . . . . . . . . 5056 1 372 . 1 1 38 38 ARG CB C 13 30.219 0.05 . 1 . . . . . . . . . 5056 1 373 . 1 1 38 38 ARG CG C 13 26.523 0.05 . 1 . . . . . . . . . 5056 1 374 . 1 1 38 38 ARG CD C 13 43.763 0.05 . 1 . . . . . . . . . 5056 1 375 . 1 1 38 38 ARG N N 15 120.85 0.05 . 1 . . . . . . . . . 5056 1 376 . 1 1 39 39 GLU H H 1 8.533 0.02 . 1 . . . . . . . . . 5056 1 377 . 1 1 39 39 GLU HA H 1 3.955 0.02 . 1 . . . . . . . . . 5056 1 378 . 1 1 39 39 GLU HB2 H 1 1.932 0.02 . 1 . . . . . . . . . 5056 1 379 . 1 1 39 39 GLU HB3 H 1 1.885 0.02 . 1 . . . . . . . . . 5056 1 380 . 1 1 39 39 GLU HG2 H 1 2.428 0.02 . 2 . . . . . . . . . 5056 1 381 . 1 1 39 39 GLU HG3 H 1 2.200 0.02 . 2 . . . . . . . . . 5056 1 382 . 1 1 39 39 GLU C C 13 178.45 0.05 . 1 . . . . . . . . . 5056 1 383 . 1 1 39 39 GLU CA C 13 58.817 0.05 . 1 . . . . . . . . . 5056 1 384 . 1 1 39 39 GLU CB C 13 30.238 0.05 . 1 . . . . . . . . . 5056 1 385 . 1 1 39 39 GLU CG C 13 35.735 0.05 . 1 . . . . . . . . . 5056 1 386 . 1 1 39 39 GLU N N 15 117.83 0.05 . 1 . . . . . . . . . 5056 1 387 . 1 1 40 40 ASN H H 1 8.673 0.02 . 1 . . . . . . . . . 5056 1 388 . 1 1 40 40 ASN HA H 1 4.970 0.02 . 1 . . . . . . . . . 5056 1 389 . 1 1 40 40 ASN HB2 H 1 3.095 0.02 . 1 . . . . . . . . . 5056 1 390 . 1 1 40 40 ASN HB3 H 1 2.901 0.02 . 1 . . . . . . . . . 5056 1 391 . 1 1 40 40 ASN C C 13 176.71 0.05 . 1 . . . . . . . . . 5056 1 392 . 1 1 40 40 ASN CA C 13 54.018 0.05 . 1 . . . . . . . . . 5056 1 393 . 1 1 40 40 ASN CB C 13 39.767 0.05 . 1 . . . . . . . . . 5056 1 394 . 1 1 40 40 ASN N N 15 113.80 0.05 . 1 . . . . . . . . . 5056 1 395 . 1 1 41 41 LYS H H 1 6.987 0.02 . 1 . . . . . . . . . 5056 1 396 . 1 1 41 41 LYS HA H 1 4.758 0.02 . 1 . . . . . . . . . 5056 1 397 . 1 1 41 41 LYS HB2 H 1 2.400 0.02 . 1 . . . . . . . . . 5056 1 398 . 1 1 41 41 LYS HB3 H 1 2.109 0.02 . 1 . . . . . . . . . 5056 1 399 . 1 1 41 41 LYS HG2 H 1 1.443 0.02 . 1 . . . . . . . . . 5056 1 400 . 1 1 41 41 LYS HD2 H 1 1.396 0.02 . 2 . . . . . . . . . 5056 1 401 . 1 1 41 41 LYS HD3 H 1 1.330 0.02 . 2 . . . . . . . . . 5056 1 402 . 1 1 41 41 LYS HE2 H 1 2.184 0.02 . 2 . . . . . . . . . 5056 1 403 . 1 1 41 41 LYS HE3 H 1 2.125 0.02 . 2 . . . . . . . . . 5056 1 404 . 1 1 41 41 LYS C C 13 177.09 0.05 . 1 . . . . . . . . . 5056 1 405 . 1 1 41 41 LYS CA C 13 53.532 0.05 . 1 . . . . . . . . . 5056 1 406 . 1 1 41 41 LYS CB C 13 32.529 0.05 . 1 . . . . . . . . . 5056 1 407 . 1 1 41 41 LYS CG C 13 24.834 0.05 . 1 . . . . . . . . . 5056 1 408 . 1 1 41 41 LYS CD C 13 27.640 0.05 . 1 . . . . . . . . . 5056 1 409 . 1 1 41 41 LYS CE C 13 41.235 0.05 . 1 . . . . . . . . . 5056 1 410 . 1 1 41 41 LYS N N 15 115.11 0.05 . 1 . . . . . . . . . 5056 1 411 . 1 1 42 42 GLY H H 1 7.508 0.02 . 1 . . . . . . . . . 5056 1 412 . 1 1 42 42 GLY HA2 H 1 3.918 0.02 . 1 . . . . . . . . . 5056 1 413 . 1 1 42 42 GLY HA3 H 1 3.918 0.02 . 1 . . . . . . . . . 5056 1 414 . 1 1 42 42 GLY C C 13 174.33 0.05 . 1 . . . . . . . . . 5056 1 415 . 1 1 42 42 GLY CA C 13 46.364 0.05 . 1 . . . . . . . . . 5056 1 416 . 1 1 42 42 GLY N N 15 108.62 0.05 . 1 . . . . . . . . . 5056 1 417 . 1 1 43 43 ALA H H 1 7.175 0.02 . 1 . . . . . . . . . 5056 1 418 . 1 1 43 43 ALA HA H 1 3.822 0.02 . 1 . . . . . . . . . 5056 1 419 . 1 1 43 43 ALA HB1 H 1 0.457 0.02 . 1 . . . . . . . . . 5056 1 420 . 1 1 43 43 ALA HB2 H 1 0.457 0.02 . 1 . . . . . . . . . 5056 1 421 . 1 1 43 43 ALA HB3 H 1 0.457 0.02 . 1 . . . . . . . . . 5056 1 422 . 1 1 43 43 ALA C C 13 175.31 0.05 . 1 . . . . . . . . . 5056 1 423 . 1 1 43 43 ALA CA C 13 50.595 0.05 . 1 . . . . . . . . . 5056 1 424 . 1 1 43 43 ALA CB C 13 19.485 0.05 . 1 . . . . . . . . . 5056 1 425 . 1 1 43 43 ALA N N 15 121.18 0.05 . 1 . . . . . . . . . 5056 1 426 . 1 1 44 44 LYS H H 1 7.910 0.02 . 1 . . . . . . . . . 5056 1 427 . 1 1 44 44 LYS HA H 1 4.029 0.02 . 1 . . . . . . . . . 5056 1 428 . 1 1 44 44 LYS HB2 H 1 1.484 0.02 . 1 . . . . . . . . . 5056 1 429 . 1 1 44 44 LYS HB3 H 1 1.275 0.02 . 1 . . . . . . . . . 5056 1 430 . 1 1 44 44 LYS HG2 H 1 1.194 0.02 . 1 . . . . . . . . . 5056 1 431 . 1 1 44 44 LYS HG3 H 1 1.194 0.02 . 1 . . . . . . . . . 5056 1 432 . 1 1 44 44 LYS HD2 H 1 1.376 0.02 . 2 . . . . . . . . . 5056 1 433 . 1 1 44 44 LYS HD3 H 1 1.194 0.02 . 2 . . . . . . . . . 5056 1 434 . 1 1 44 44 LYS HE2 H 1 2.825 0.02 . 1 . . . . . . . . . 5056 1 435 . 1 1 44 44 LYS HE3 H 1 2.825 0.02 . 1 . . . . . . . . . 5056 1 436 . 1 1 44 44 LYS C C 13 176.63 0.05 . 1 . . . . . . . . . 5056 1 437 . 1 1 44 44 LYS CA C 13 56.840 0.05 . 1 . . . . . . . . . 5056 1 438 . 1 1 44 44 LYS CB C 13 32.838 0.05 . 1 . . . . . . . . . 5056 1 439 . 1 1 44 44 LYS CG C 13 25.233 0.05 . 1 . . . . . . . . . 5056 1 440 . 1 1 44 44 LYS CD C 13 28.726 0.05 . 1 . . . . . . . . . 5056 1 441 . 1 1 44 44 LYS CE C 13 42.081 0.05 . 1 . . . . . . . . . 5056 1 442 . 1 1 44 44 LYS N N 15 117.65 0.05 . 1 . . . . . . . . . 5056 1 443 . 1 1 45 45 GLY H H 1 7.314 0.02 . 1 . . . . . . . . . 5056 1 444 . 1 1 45 45 GLY HA2 H 1 3.912 0.02 . 2 . . . . . . . . . 5056 1 445 . 1 1 45 45 GLY HA3 H 1 2.950 0.02 . 2 . . . . . . . . . 5056 1 446 . 1 1 45 45 GLY C C 13 172.23 0.05 . 1 . . . . . . . . . 5056 1 447 . 1 1 45 45 GLY CA C 13 45.150 0.05 . 1 . . . . . . . . . 5056 1 448 . 1 1 45 45 GLY N N 15 105.25 0.05 . 1 . . . . . . . . . 5056 1 449 . 1 1 46 46 GLY H H 1 7.462 0.02 . 1 . . . . . . . . . 5056 1 450 . 1 1 46 46 GLY HA2 H 1 4.815 0.02 . 2 . . . . . . . . . 5056 1 451 . 1 1 46 46 GLY HA3 H 1 3.834 0.02 . 2 . . . . . . . . . 5056 1 452 . 1 1 46 46 GLY C C 13 170.89 0.05 . 1 . . . . . . . . . 5056 1 453 . 1 1 46 46 GLY CA C 13 46.355 0.05 . 1 . . . . . . . . . 5056 1 454 . 1 1 46 46 GLY N N 15 110.79 0.05 . 1 . . . . . . . . . 5056 1 455 . 1 1 47 47 ARG H H 1 9.670 0.02 . 1 . . . . . . . . . 5056 1 456 . 1 1 47 47 ARG HA H 1 4.696 0.02 . 1 . . . . . . . . . 5056 1 457 . 1 1 47 47 ARG HB2 H 1 1.899 0.02 . 1 . . . . . . . . . 5056 1 458 . 1 1 47 47 ARG HB3 H 1 1.693 0.02 . 1 . . . . . . . . . 5056 1 459 . 1 1 47 47 ARG HG2 H 1 1.527 0.02 . 2 . . . . . . . . . 5056 1 460 . 1 1 47 47 ARG HG3 H 1 1.53 0.02 . 2 . . . . . . . . . 5056 1 461 . 1 1 47 47 ARG HD2 H 1 3.186 0.02 . 2 . . . . . . . . . 5056 1 462 . 1 1 47 47 ARG HD3 H 1 3.063 0.02 . 2 . . . . . . . . . 5056 1 463 . 1 1 47 47 ARG HE H 1 7.335 0.02 . 1 . . . . . . . . . 5056 1 464 . 1 1 47 47 ARG C C 13 173.31 0.05 . 1 . . . . . . . . . 5056 1 465 . 1 1 47 47 ARG CA C 13 54.236 0.05 . 1 . . . . . . . . . 5056 1 466 . 1 1 47 47 ARG CB C 13 33.447 0.05 . 1 . . . . . . . . . 5056 1 467 . 1 1 47 47 ARG CG C 13 26.422 0.05 . 1 . . . . . . . . . 5056 1 468 . 1 1 47 47 ARG CD C 13 43.332 0.05 . 1 . . . . . . . . . 5056 1 469 . 1 1 47 47 ARG N N 15 121.86 0.05 . 1 . . . . . . . . . 5056 1 470 . 1 1 47 47 ARG NE N 15 124.06 0.05 . 1 . . . . . . . . . 5056 1 471 . 1 1 48 48 CYS H H 1 8.857 0.02 . 1 . . . . . . . . . 5056 1 472 . 1 1 48 48 CYS HA H 1 5.143 0.02 . 1 . . . . . . . . . 5056 1 473 . 1 1 48 48 CYS HB2 H 1 3.332 0.02 . 1 . . . . . . . . . 5056 1 474 . 1 1 48 48 CYS HB3 H 1 2.214 0.02 . 1 . . . . . . . . . 5056 1 475 . 1 1 48 48 CYS C C 13 174.08 0.05 . 1 . . . . . . . . . 5056 1 476 . 1 1 48 48 CYS CA C 13 56.823 0.05 . 1 . . . . . . . . . 5056 1 477 . 1 1 48 48 CYS CB C 13 45.750 0.05 . 1 . . . . . . . . . 5056 1 478 . 1 1 48 48 CYS N N 15 123.23 0.05 . 1 . . . . . . . . . 5056 1 479 . 1 1 49 49 ARG H H 1 8.966 0.02 . 1 . . . . . . . . . 5056 1 480 . 1 1 49 49 ARG HA H 1 4.734 0.02 . 1 . . . . . . . . . 5056 1 481 . 1 1 49 49 ARG HB2 H 1 1.689 0.02 . 2 . . . . . . . . . 5056 1 482 . 1 1 49 49 ARG HB3 H 1 1.471 0.02 . 2 . . . . . . . . . 5056 1 483 . 1 1 49 49 ARG HG2 H 1 1.905 0.02 . 2 . . . . . . . . . 5056 1 484 . 1 1 49 49 ARG HG3 H 1 1.520 0.02 . 2 . . . . . . . . . 5056 1 485 . 1 1 49 49 ARG HD2 H 1 3.171 0.02 . 2 . . . . . . . . . 5056 1 486 . 1 1 49 49 ARG HD3 H 1 3.077 0.02 . 2 . . . . . . . . . 5056 1 487 . 1 1 49 49 ARG HE H 1 7.568 0.02 . 1 . . . . . . . . . 5056 1 488 . 1 1 49 49 ARG C C 13 175.04 0.05 . 1 . . . . . . . . . 5056 1 489 . 1 1 49 49 ARG CA C 13 54.448 0.05 . 1 . . . . . . . . . 5056 1 490 . 1 1 49 49 ARG CB C 13 31.978 0.05 . 1 . . . . . . . . . 5056 1 491 . 1 1 49 49 ARG CG C 13 26.219 0.05 . 1 . . . . . . . . . 5056 1 492 . 1 1 49 49 ARG CD C 13 43.322 0.05 . 1 . . . . . . . . . 5056 1 493 . 1 1 49 49 ARG N N 15 127.08 0.05 . 1 . . . . . . . . . 5056 1 494 . 1 1 50 50 TRP H H 1 9.310 0.02 . 1 . . . . . . . . . 5056 1 495 . 1 1 50 50 TRP HA H 1 4.372 0.02 . 1 . . . . . . . . . 5056 1 496 . 1 1 50 50 TRP HB2 H 1 3.417 0.02 . 1 . . . . . . . . . 5056 1 497 . 1 1 50 50 TRP HB3 H 1 3.088 0.02 . 1 . . . . . . . . . 5056 1 498 . 1 1 50 50 TRP C C 13 176.78 0.05 . 1 . . . . . . . . . 5056 1 499 . 1 1 50 50 TRP CA C 13 58.468 0.05 . 1 . . . . . . . . . 5056 1 500 . 1 1 50 50 TRP CB C 13 29.479 0.05 . 1 . . . . . . . . . 5056 1 501 . 1 1 50 50 TRP N N 15 133.19 0.05 . 1 . . . . . . . . . 5056 1 502 . 1 1 50 50 TRP NE1 N 15 130.6 0.05 . 1 . . . . . . . . . 5056 1 503 . 1 1 51 51 GLY H H 1 8.715 0.02 . 1 . . . . . . . . . 5056 1 504 . 1 1 51 51 GLY HA2 H 1 4.443 0.02 . 2 . . . . . . . . . 5056 1 505 . 1 1 51 51 GLY HA3 H 1 3.614 0.02 . 2 . . . . . . . . . 5056 1 506 . 1 1 51 51 GLY C C 13 173.52 0.05 . 1 . . . . . . . . . 5056 1 507 . 1 1 51 51 GLY CA C 13 44.401 0.05 . 1 . . . . . . . . . 5056 1 508 . 1 1 51 51 GLY N N 15 114.21 0.05 . 1 . . . . . . . . . 5056 1 509 . 1 1 52 52 GLN H H 1 8.675 0.02 . 1 . . . . . . . . . 5056 1 510 . 1 1 52 52 GLN HA H 1 4.366 0.02 . 1 . . . . . . . . . 5056 1 511 . 1 1 52 52 GLN HB2 H 1 2.072 0.02 . 1 . . . . . . . . . 5056 1 512 . 1 1 52 52 GLN HB3 H 1 1.963 0.02 . 1 . . . . . . . . . 5056 1 513 . 1 1 52 52 GLN HG2 H 1 2.379 0.02 . 1 . . . . . . . . . 5056 1 514 . 1 1 52 52 GLN HG3 H 1 2.379 0.02 . 1 . . . . . . . . . 5056 1 515 . 1 1 52 52 GLN HE21 H 1 7.525 0.02 . 1 . . . . . . . . . 5056 1 516 . 1 1 52 52 GLN HE22 H 1 6.836 0.02 . 1 . . . . . . . . . 5056 1 517 . 1 1 52 52 GLN C C 13 177.42 0.05 . 1 . . . . . . . . . 5056 1 518 . 1 1 52 52 GLN CA C 13 55.647 0.05 . 1 . . . . . . . . . 5056 1 519 . 1 1 52 52 GLN CB C 13 29.298 0.05 . 1 . . . . . . . . . 5056 1 520 . 1 1 52 52 GLN CG C 13 33.899 0.05 . 1 . . . . . . . . . 5056 1 521 . 1 1 52 52 GLN CD C 13 180.48 0.05 . 1 . . . . . . . . . 5056 1 522 . 1 1 52 52 GLN N N 15 123.96 0.05 . 1 . . . . . . . . . 5056 1 523 . 1 1 52 52 GLN NE2 N 15 113.55 0.05 . 1 . . . . . . . . . 5056 1 524 . 1 1 53 53 GLY H H 1 8.848 0.02 . 1 . . . . . . . . . 5056 1 525 . 1 1 53 53 GLY HA2 H 1 3.915 0.02 . 1 . . . . . . . . . 5056 1 526 . 1 1 53 53 GLY HA3 H 1 3.765 0.02 . 1 . . . . . . . . . 5056 1 527 . 1 1 53 53 GLY C C 13 174.98 0.05 . 1 . . . . . . . . . 5056 1 528 . 1 1 53 53 GLY CA C 13 46.925 0.05 . 1 . . . . . . . . . 5056 1 529 . 1 1 53 53 GLY N N 15 113.77 0.05 . 1 . . . . . . . . . 5056 1 530 . 1 1 54 54 SER H H 1 8.661 0.02 . 1 . . . . . . . . . 5056 1 531 . 1 1 54 54 SER HA H 1 4.629 0.02 . 1 . . . . . . . . . 5056 1 532 . 1 1 54 54 SER HB2 H 1 3.858 0.02 . 1 . . . . . . . . . 5056 1 533 . 1 1 54 54 SER HB3 H 1 3.858 0.02 . 1 . . . . . . . . . 5056 1 534 . 1 1 54 54 SER C C 13 173.69 0.05 . 1 . . . . . . . . . 5056 1 535 . 1 1 54 54 SER CA C 13 57.882 0.05 . 1 . . . . . . . . . 5056 1 536 . 1 1 54 54 SER CB C 13 62.993 0.05 . 1 . . . . . . . . . 5056 1 537 . 1 1 54 54 SER N N 15 120.30 0.05 . 1 . . . . . . . . . 5056 1 538 . 1 1 55 55 ASN H H 1 7.899 0.02 . 1 . . . . . . . . . 5056 1 539 . 1 1 55 55 ASN HA H 1 4.606 0.02 . 1 . . . . . . . . . 5056 1 540 . 1 1 55 55 ASN HB2 H 1 2.884 0.02 . 1 . . . . . . . . . 5056 1 541 . 1 1 55 55 ASN HB3 H 1 2.743 0.02 . 1 . . . . . . . . . 5056 1 542 . 1 1 55 55 ASN HD21 H 1 7.617 0.02 . 1 . . . . . . . . . 5056 1 543 . 1 1 55 55 ASN HD22 H 1 6.929 0.02 . 1 . . . . . . . . . 5056 1 544 . 1 1 55 55 ASN C C 13 173.35 0.05 . 1 . . . . . . . . . 5056 1 545 . 1 1 55 55 ASN CA C 13 53.611 0.05 . 1 . . . . . . . . . 5056 1 546 . 1 1 55 55 ASN CB C 13 38.964 0.05 . 1 . . . . . . . . . 5056 1 547 . 1 1 55 55 ASN CG C 13 177.41 0.05 . 1 . . . . . . . . . 5056 1 548 . 1 1 55 55 ASN N N 15 121.55 0.05 . 1 . . . . . . . . . 5056 1 549 . 1 1 55 55 ASN ND2 N 15 114.81 0.05 . 1 . . . . . . . . . 5056 1 550 . 1 1 56 56 VAL H H 1 7.914 0.02 . 1 . . . . . . . . . 5056 1 551 . 1 1 56 56 VAL HA H 1 4.427 0.02 . 1 . . . . . . . . . 5056 1 552 . 1 1 56 56 VAL HB H 1 1.083 0.02 . 1 . . . . . . . . . 5056 1 553 . 1 1 56 56 VAL HG11 H 1 0.033 0.02 . 1 . . . . . . . . . 5056 1 554 . 1 1 56 56 VAL HG12 H 1 0.033 0.02 . 1 . . . . . . . . . 5056 1 555 . 1 1 56 56 VAL HG13 H 1 0.033 0.02 . 1 . . . . . . . . . 5056 1 556 . 1 1 56 56 VAL HG21 H 1 -0.623 0.02 . 1 . . . . . . . . . 5056 1 557 . 1 1 56 56 VAL HG22 H 1 -0.623 0.02 . 1 . . . . . . . . . 5056 1 558 . 1 1 56 56 VAL HG23 H 1 -0.623 0.02 . 1 . . . . . . . . . 5056 1 559 . 1 1 56 56 VAL C C 13 172.34 0.05 . 1 . . . . . . . . . 5056 1 560 . 1 1 56 56 VAL CA C 13 59.370 0.05 . 1 . . . . . . . . . 5056 1 561 . 1 1 56 56 VAL CB C 13 32.174 0.05 . 1 . . . . . . . . . 5056 1 562 . 1 1 56 56 VAL CG1 C 13 20.058 0.05 . 1 . . . . . . . . . 5056 1 563 . 1 1 56 56 VAL CG2 C 13 17.786 0.05 . 1 . . . . . . . . . 5056 1 564 . 1 1 56 56 VAL N N 15 123.30 0.05 . 1 . . . . . . . . . 5056 1 565 . 1 1 57 57 LYS H H 1 7.688 0.02 . 1 . . . . . . . . . 5056 1 566 . 1 1 57 57 LYS HA H 1 4.544 0.02 . 1 . . . . . . . . . 5056 1 567 . 1 1 57 57 LYS C C 13 174.26 0.05 . 1 . . . . . . . . . 5056 1 568 . 1 1 57 57 LYS CA C 13 53.338 0.05 . 1 . . . . . . . . . 5056 1 569 . 1 1 57 57 LYS CB C 13 36.785 0.05 . 1 . . . . . . . . . 5056 1 570 . 1 1 57 57 LYS CG C 13 24.661 0.05 . 1 . . . . . . . . . 5056 1 571 . 1 1 57 57 LYS CD C 13 29.189 0.05 . 1 . . . . . . . . . 5056 1 572 . 1 1 57 57 LYS CE C 13 42.151 0.05 . 1 . . . . . . . . . 5056 1 573 . 1 1 57 57 LYS N N 15 124.40 0.05 . 1 . . . . . . . . . 5056 1 574 . 1 1 58 58 CYS H H 1 9.514 0.02 . 1 . . . . . . . . . 5056 1 575 . 1 1 58 58 CYS HA H 1 4.954 0.02 . 1 . . . . . . . . . 5056 1 576 . 1 1 58 58 CYS HB2 H 1 2.757 0.02 . 1 . . . . . . . . . 5056 1 577 . 1 1 58 58 CYS HB3 H 1 2.419 0.02 . 1 . . . . . . . . . 5056 1 578 . 1 1 58 58 CYS C C 13 172.20 0.05 . 1 . . . . . . . . . 5056 1 579 . 1 1 58 58 CYS CA C 13 54.261 0.05 . 1 . . . . . . . . . 5056 1 580 . 1 1 58 58 CYS CB C 13 36.946 0.05 . 1 . . . . . . . . . 5056 1 581 . 1 1 58 58 CYS N N 15 121.56 0.05 . 1 . . . . . . . . . 5056 1 582 . 1 1 59 59 LEU H H 1 9.126 0.02 . 1 . . . . . . . . . 5056 1 583 . 1 1 59 59 LEU HA H 1 4.546 0.02 . 1 . . . . . . . . . 5056 1 584 . 1 1 59 59 LEU HB2 H 1 1.829 0.02 . 2 . . . . . . . . . 5056 1 585 . 1 1 59 59 LEU HB3 H 1 1.041 0.02 . 2 . . . . . . . . . 5056 1 586 . 1 1 59 59 LEU HG H 1 1.462 0.02 . 1 . . . . . . . . . 5056 1 587 . 1 1 59 59 LEU HD11 H 1 0.757 0.02 . 2 . . . . . . . . . 5056 1 588 . 1 1 59 59 LEU HD12 H 1 0.757 0.02 . 2 . . . . . . . . . 5056 1 589 . 1 1 59 59 LEU HD13 H 1 0.757 0.02 . 2 . . . . . . . . . 5056 1 590 . 1 1 59 59 LEU HD21 H 1 0.668 0.02 . 2 . . . . . . . . . 5056 1 591 . 1 1 59 59 LEU HD22 H 1 0.668 0.02 . 2 . . . . . . . . . 5056 1 592 . 1 1 59 59 LEU HD23 H 1 0.668 0.02 . 2 . . . . . . . . . 5056 1 593 . 1 1 59 59 LEU C C 13 175.16 0.05 . 1 . . . . . . . . . 5056 1 594 . 1 1 59 59 LEU CA C 13 52.799 0.05 . 1 . . . . . . . . . 5056 1 595 . 1 1 59 59 LEU CB C 13 42.959 0.05 . 1 . . . . . . . . . 5056 1 596 . 1 1 59 59 LEU CG C 13 26.382 0.05 . 1 . . . . . . . . . 5056 1 597 . 1 1 59 59 LEU CD1 C 13 23.846 0.05 . 1 . . . . . . . . . 5056 1 598 . 1 1 59 59 LEU N N 15 130.21 0.05 . 1 . . . . . . . . . 5056 1 599 . 1 1 60 60 CYS H H 1 8.986 0.02 . 1 . . . . . . . . . 5056 1 600 . 1 1 60 60 CYS HA H 1 5.052 0.02 . 1 . . . . . . . . . 5056 1 601 . 1 1 60 60 CYS HB2 H 1 2.947 0.02 . 1 . . . . . . . . . 5056 1 602 . 1 1 60 60 CYS HB3 H 1 2.358 0.02 . 1 . . . . . . . . . 5056 1 603 . 1 1 60 60 CYS C C 13 172.42 0.05 . 1 . . . . . . . . . 5056 1 604 . 1 1 60 60 CYS CA C 13 51.934 0.05 . 1 . . . . . . . . . 5056 1 605 . 1 1 60 60 CYS CB C 13 34.253 0.05 . 1 . . . . . . . . . 5056 1 606 . 1 1 60 60 CYS N N 15 122.20 0.05 . 1 . . . . . . . . . 5056 1 607 . 1 1 61 61 ASP H H 1 7.867 0.02 . 1 . . . . . . . . . 5056 1 608 . 1 1 61 61 ASP HA H 1 5.231 0.02 . 1 . . . . . . . . . 5056 1 609 . 1 1 61 61 ASP HB2 H 1 2.422 0.02 . 1 . . . . . . . . . 5056 1 610 . 1 1 61 61 ASP HB3 H 1 1.952 0.02 . 1 . . . . . . . . . 5056 1 611 . 1 1 61 61 ASP C C 13 175.77 0.05 . 1 . . . . . . . . . 5056 1 612 . 1 1 61 61 ASP CA C 13 51.866 0.05 . 1 . . . . . . . . . 5056 1 613 . 1 1 61 61 ASP CB C 13 42.871 0.05 . 1 . . . . . . . . . 5056 1 614 . 1 1 61 61 ASP N N 15 123.02 0.05 . 1 . . . . . . . . . 5056 1 615 . 1 1 62 62 PHE H H 1 9.698 0.02 . 1 . . . . . . . . . 5056 1 616 . 1 1 62 62 PHE HA H 1 4.288 0.02 . 1 . . . . . . . . . 5056 1 617 . 1 1 62 62 PHE HB2 H 1 3.493 0.02 . 1 . . . . . . . . . 5056 1 618 . 1 1 62 62 PHE HB3 H 1 2.869 0.02 . 1 . . . . . . . . . 5056 1 619 . 1 1 62 62 PHE C C 13 175.38 0.05 . 1 . . . . . . . . . 5056 1 620 . 1 1 62 62 PHE CA C 13 59.070 0.05 . 1 . . . . . . . . . 5056 1 621 . 1 1 62 62 PHE CB C 13 39.033 0.05 . 1 . . . . . . . . . 5056 1 622 . 1 1 62 62 PHE N N 15 125.84 0.05 . 1 . . . . . . . . . 5056 1 623 . 1 1 63 63 CYS H H 1 9.189 0.02 . 1 . . . . . . . . . 5056 1 624 . 1 1 63 63 CYS HA H 1 4.519 0.02 . 1 . . . . . . . . . 5056 1 625 . 1 1 63 63 CYS HB2 H 1 3.656 0.02 . 1 . . . . . . . . . 5056 1 626 . 1 1 63 63 CYS HB3 H 1 3.024 0.02 . 1 . . . . . . . . . 5056 1 627 . 1 1 63 63 CYS C C 13 174.15 0.05 . 1 . . . . . . . . . 5056 1 628 . 1 1 63 63 CYS CA C 13 55.569 0.05 . 1 . . . . . . . . . 5056 1 629 . 1 1 63 63 CYS CB C 13 44.204 0.05 . 1 . . . . . . . . . 5056 1 630 . 1 1 63 63 CYS N N 15 120.65 0.05 . 1 . . . . . . . . . 5056 1 631 . 1 1 64 64 GLY H H 1 8.639 0.02 . 1 . . . . . . . . . 5056 1 632 . 1 1 64 64 GLY HA2 H 1 3.932 0.02 . 2 . . . . . . . . . 5056 1 633 . 1 1 64 64 GLY HA3 H 1 3.817 0.02 . 2 . . . . . . . . . 5056 1 634 . 1 1 64 64 GLY C C 13 172.18 0.05 . 1 . . . . . . . . . 5056 1 635 . 1 1 64 64 GLY CA C 13 45.576 0.05 . 1 . . . . . . . . . 5056 1 636 . 1 1 64 64 GLY N N 15 111.40 0.05 . 1 . . . . . . . . . 5056 1 637 . 1 1 65 65 ASP H H 1 8.091 0.02 . 1 . . . . . . . . . 5056 1 638 . 1 1 65 65 ASP HA H 1 4.620 0.02 . 1 . . . . . . . . . 5056 1 639 . 1 1 65 65 ASP HB2 H 1 2.735 0.02 . 1 . . . . . . . . . 5056 1 640 . 1 1 65 65 ASP HB3 H 1 2.506 0.02 . 1 . . . . . . . . . 5056 1 641 . 1 1 65 65 ASP C C 13 176.94 0.05 . 1 . . . . . . . . . 5056 1 642 . 1 1 65 65 ASP CA C 13 53.080 0.05 . 1 . . . . . . . . . 5056 1 643 . 1 1 65 65 ASP CB C 13 41.639 0.05 . 1 . . . . . . . . . 5056 1 644 . 1 1 65 65 ASP N N 15 119.98 0.05 . 1 . . . . . . . . . 5056 1 645 . 1 1 66 66 THR H H 1 8.120 0.02 . 1 . . . . . . . . . 5056 1 646 . 1 1 66 66 THR HA H 1 4.476 0.02 . 1 . . . . . . . . . 5056 1 647 . 1 1 66 66 THR HB H 1 4.057 0.02 . 1 . . . . . . . . . 5056 1 648 . 1 1 66 66 THR HG21 H 1 1.208 0.02 . 1 . . . . . . . . . 5056 1 649 . 1 1 66 66 THR HG22 H 1 1.208 0.02 . 1 . . . . . . . . . 5056 1 650 . 1 1 66 66 THR HG23 H 1 1.208 0.02 . 1 . . . . . . . . . 5056 1 651 . 1 1 66 66 THR CA C 13 60.626 0.05 . 1 . . . . . . . . . 5056 1 652 . 1 1 66 66 THR CB C 13 69.627 0.05 . 1 . . . . . . . . . 5056 1 653 . 1 1 66 66 THR N N 15 119.42 0.05 . 1 . . . . . . . . . 5056 1 654 . 1 1 67 67 PRO HA H 1 4.184 0.02 . 1 . . . . . . . . . 5056 1 655 . 1 1 67 67 PRO HB2 H 1 1.884 0.02 . 1 . . . . . . . . . 5056 1 656 . 1 1 67 67 PRO HB3 H 1 1.779 0.02 . 1 . . . . . . . . . 5056 1 657 . 1 1 67 67 PRO HG2 H 1 2.002 0.02 . 2 . . . . . . . . . 5056 1 658 . 1 1 67 67 PRO HG3 H 1 1.884 0.02 . 2 . . . . . . . . . 5056 1 659 . 1 1 67 67 PRO HD2 H 1 3.890 0.02 . 2 . . . . . . . . . 5056 1 660 . 1 1 67 67 PRO HD3 H 1 3.693 0.02 . 2 . . . . . . . . . 5056 1 661 . 1 1 67 67 PRO CA C 13 63.536 0.05 . 1 . . . . . . . . . 5056 1 662 . 1 1 67 67 PRO CB C 13 31.727 0.05 . 1 . . . . . . . . . 5056 1 663 . 1 1 67 67 PRO CG C 13 29.383 0.05 . 1 . . . . . . . . . 5056 1 664 . 1 1 68 68 GLN H H 1 7.523 0.02 . 1 . . . . . . . . . 5056 1 665 . 1 1 68 68 GLN HA H 1 4.140 0.02 . 1 . . . . . . . . . 5056 1 666 . 1 1 68 68 GLN HB2 H 1 2.091 0.02 . 2 . . . . . . . . . 5056 1 667 . 1 1 68 68 GLN HB3 H 1 1.924 0.02 . 2 . . . . . . . . . 5056 1 668 . 1 1 68 68 GLN HG2 H 1 2.035 0.02 . 1 . . . . . . . . . 5056 1 669 . 1 1 68 68 GLN HG3 H 1 2.035 0.02 . 1 . . . . . . . . . 5056 1 670 . 1 1 68 68 GLN HE21 H 1 7.474 0.02 . 2 . . . . . . . . . 5056 1 671 . 1 1 68 68 GLN HE22 H 1 6.770 0.02 . 2 . . . . . . . . . 5056 1 672 . 1 1 68 68 GLN CA C 13 57.344 0.05 . 1 . . . . . . . . . 5056 1 673 . 1 1 68 68 GLN CB C 13 31.307 0.05 . 1 . . . . . . . . . 5056 1 674 . 1 1 68 68 GLN CD C 13 181.24 0.05 . 1 . . . . . . . . . 5056 1 675 . 1 1 68 68 GLN N N 15 126.30 0.05 . 1 . . . . . . . . . 5056 1 676 . 1 1 68 68 GLN NE2 N 15 113.56 0.05 . 1 . . . . . . . . . 5056 1 stop_ save_ ######################## # Coupling constants # ######################## save_HNHA _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode HNHA _Coupling_constant_list.Entry_ID 5056 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $cond_1 _Coupling_constant_list.Spectrometer_frequency_1H 600 _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 HNCA . . . 5056 1 2 HN(CO)CA . . . 5056 1 3 HNCACB . . . 5056 1 4 HNCO . . . 5056 1 5 C(CO)NH-SE . . . 5056 1 6 H(CCO)NH-SE . . . 5056 1 7 HCCH-COSY . . . 5056 1 8 HCCH-TOCSY . . . 5056 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_asym_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_asym_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 4 4 ILE HA H 1 . . 1 1 4 4 ILE H H 1 . 6.70 . . . . . . . . . . . . . . . . 5056 1 2 3JHNHA . 1 1 5 5 GLU HA H 1 . . 1 1 5 5 GLU H H 1 . 5.64 . . . . . . . . . . . . . . . . 5056 1 3 3JHNHA . 1 1 6 6 ALA HA H 1 . . 1 1 6 6 ALA H H 1 . 6.34 . . . . . . . . . . . . . . . . 5056 1 4 3JHNHA . 1 1 10 10 GLU HA H 1 . . 1 1 10 10 GLU H H 1 . 5.92 . . . . . . . . . . . . . . . . 5056 1 5 3JHNHA . 1 1 12 12 LEU HA H 1 . . 1 1 12 12 LEU H H 1 . 8.45 . . . . . . . . . . . . . . . . 5056 1 6 3JHNHA . 1 1 14 14 GLU HA H 1 . . 1 1 14 14 GLU H H 1 . 8.89 . . . . . . . . . . . . . . . . 5056 1 7 3JHNHA . 1 1 17 17 GLY HA2 H 1 . . 1 1 17 17 GLY H H 1 . 6.79 . . . . . . . . . . . . . . . . 5056 1 8 3JHNHA . 1 1 17 17 GLY HA3 H 1 . . 1 1 17 17 GLY H H 1 . 4.83 . . . . . . . . . . . . . . . . 5056 1 9 3JHNHA . 1 1 18 18 ASP HA H 1 . . 1 1 18 18 ASP H H 1 . 6.48 . . . . . . . . . . . . . . . . 5056 1 10 3JHNHA . 1 1 19 19 VAL HA H 1 . . 1 1 19 19 VAL H H 1 . 8.44 . . . . . . . . . . . . . . . . 5056 1 11 3JHNHA . 1 1 20 20 GLY HA2 H 1 . . 1 1 20 20 GLY H H 1 . 5.65 . . . . . . . . . . . . . . . . 5056 1 12 3JHNHA . 1 1 20 20 GLY HA3 H 1 . . 1 1 20 20 GLY H H 1 . 5.65 . . . . . . . . . . . . . . . . 5056 1 13 3JHNHA . 1 1 21 21 PHE HA H 1 . . 1 1 21 21 PHE H H 1 . 3.50 . . . . . . . . . . . . . . . . 5056 1 14 3JHNHA . 1 1 22 22 GLY HA2 H 1 . . 1 1 22 22 GLY H H 1 . 4.03 . . . . . . . . . . . . . . . . 5056 1 15 3JHNHA . 1 1 22 22 GLY HA3 H 1 . . 1 1 22 22 GLY H H 1 . 5.00 . . . . . . . . . . . . . . . . 5056 1 16 3JHNHA . 1 1 23 23 PHE HA H 1 . . 1 1 23 23 PHE H H 1 . 5.29 . . . . . . . . . . . . . . . . 5056 1 17 3JHNHA . 1 1 24 24 CYS HA H 1 . . 1 1 24 24 CYS H H 1 . 9.49 . . . . . . . . . . . . . . . . 5056 1 18 3JHNHA . 1 1 28 28 ILE HA H 1 . . 1 1 28 28 ILE H H 1 . 7.91 . . . . . . . . . . . . . . . . 5056 1 19 3JHNHA . 1 1 29 29 PHE HA H 1 . . 1 1 29 29 PHE H H 1 . 8.14 . . . . . . . . . . . . . . . . 5056 1 20 3JHNHA . 1 1 31 31 THR HA H 1 . . 1 1 31 31 THR H H 1 . 4.07 . . . . . . . . . . . . . . . . 5056 1 21 3JHNHA . 1 1 32 32 ILE HA H 1 . . 1 1 32 32 ILE H H 1 . 3.68 . . . . . . . . . . . . . . . . 5056 1 22 3JHNHA . 1 1 34 34 TYR HA H 1 . . 1 1 34 34 TYR H H 1 . 3.18 . . . . . . . . . . . . . . . . 5056 1 23 3JHNHA . 1 1 35 35 THR HA H 1 . . 1 1 35 35 THR H H 1 . 3.57 . . . . . . . . . . . . . . . . 5056 1 24 3JHNHA . 1 1 37 37 CYS HA H 1 . . 1 1 37 37 CYS H H 1 . 4.03 . . . . . . . . . . . . . . . . 5056 1 25 3JHNHA . 1 1 39 39 GLU HA H 1 . . 1 1 39 39 GLU H H 1 . 4.71 . . . . . . . . . . . . . . . . 5056 1 26 3JHNHA . 1 1 40 40 ASN HA H 1 . . 1 1 40 40 ASN H H 1 . 7.48 . . . . . . . . . . . . . . . . 5056 1 27 3JHNHA . 1 1 41 41 LYS HA H 1 . . 1 1 41 41 LYS H H 1 . 9.58 . . . . . . . . . . . . . . . . 5056 1 28 3JHNHA . 1 1 42 42 GLY HA2 H 1 . . 1 1 42 42 GLY H H 1 . 6.57 . . . . . . . . . . . . . . . . 5056 1 29 3JHNHA . 1 1 42 42 GLY HA3 H 1 . . 1 1 42 42 GLY H H 1 . 6.57 . . . . . . . . . . . . . . . . 5056 1 30 3JHNHA . 1 1 43 43 ALA HA H 1 . . 1 1 43 43 ALA H H 1 . 6.35 . . . . . . . . . . . . . . . . 5056 1 31 3JHNHA . 1 1 44 44 LYS HA H 1 . . 1 1 44 44 LYS H H 1 . 7.64 . . . . . . . . . . . . . . . . 5056 1 32 3JHNHA . 1 1 45 45 GLY HA2 H 1 . . 1 1 45 45 GLY H H 1 . 4.40 . . . . . . . . . . . . . . . . 5056 1 33 3JHNHA . 1 1 46 46 GLY HA3 H 1 . . 1 1 46 46 GLY H H 1 . 4.94 . . . . . . . . . . . . . . . . 5056 1 34 3JHNHA . 1 1 47 47 ARG HA H 1 . . 1 1 47 47 ARG H H 1 . 8.75 . . . . . . . . . . . . . . . . 5056 1 35 3JHNHA . 1 1 48 48 CYS HA H 1 . . 1 1 48 48 CYS H H 1 . 7.71 . . . . . . . . . . . . . . . . 5056 1 36 3JHNHA . 1 1 49 49 ARG HA H 1 . . 1 1 49 49 ARG H H 1 . 8.46 . . . . . . . . . . . . . . . . 5056 1 37 3JHNHA . 1 1 50 50 TRP HA H 1 . . 1 1 50 50 TRP H H 1 . 6.55 . . . . . . . . . . . . . . . . 5056 1 38 3JHNHA . 1 1 51 51 GLY HA2 H 1 . . 1 1 51 51 GLY H H 1 . 7.69 . . . . . . . . . . . . . . . . 5056 1 39 3JHNHA . 1 1 51 51 GLY HA3 H 1 . . 1 1 51 51 GLY H H 1 . 7.69 . . . . . . . . . . . . . . . . 5056 1 40 3JHNHA . 1 1 52 52 GLN HA H 1 . . 1 1 52 52 GLN H H 1 . 6.48 . . . . . . . . . . . . . . . . 5056 1 41 3JHNHA . 1 1 53 53 GLY HA2 H 1 . . 1 1 53 53 GLY H H 1 . 2.97 . . . . . . . . . . . . . . . . 5056 1 42 3JHNHA . 1 1 53 53 GLY HA3 H 1 . . 1 1 53 53 GLY H H 1 . 5.44 . . . . . . . . . . . . . . . . 5056 1 43 3JHNHA . 1 1 55 55 ASN HA H 1 . . 1 1 55 55 ASN H H 1 . 6.70 . . . . . . . . . . . . . . . . 5056 1 44 3JHNHA . 1 1 56 56 VAL HA H 1 . . 1 1 56 56 VAL H H 1 . 6.53 . . . . . . . . . . . . . . . . 5056 1 45 3JHNHA . 1 1 57 57 LYS HA H 1 . . 1 1 57 57 LYS H H 1 . 9.44 . . . . . . . . . . . . . . . . 5056 1 46 3JHNHA . 1 1 58 58 CYS HA H 1 . . 1 1 58 58 CYS H H 1 . 8.71 . . . . . . . . . . . . . . . . 5056 1 47 3JHNHA . 1 1 59 59 LEU HA H 1 . . 1 1 59 59 LEU H H 1 . 8.74 . . . . . . . . . . . . . . . . 5056 1 48 3JHNHA . 1 1 60 60 CYS HA H 1 . . 1 1 60 60 CYS H H 1 . 7.70 . . . . . . . . . . . . . . . . 5056 1 49 3JHNHA . 1 1 61 61 ASP HA H 1 . . 1 1 61 61 ASP H H 1 . 8.46 . . . . . . . . . . . . . . . . 5056 1 50 3JHNHA . 1 1 66 66 THR HA H 1 . . 1 1 66 66 THR H H 1 . 5.78 . . . . . . . . . . . . . . . . 5056 1 stop_ save_