data_25086 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25086 _Entry.Title ; truncated EcMazE ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-07-12 _Entry.Accession_date 2014-07-12 _Entry.Last_release_date 2015-02-02 _Entry.Original_release_date 2015-02-02 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _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 Valentina Zorzini . . . 25086 2 Lieven Buts . . . 25086 3 Remy Loris . . . 25086 4 Nico 'van Nuland' . A.J. . 25086 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 25086 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID MazE . 25086 antitoxin . 25086 'DNA-binding domain' . 25086 homodimer . 25086 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25086 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 442 25086 '13C chemical shifts' 269 25086 '15N chemical shifts' 65 25086 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 . . 2015-02-02 2014-07-12 original author . 25086 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1mvf 'MazE addiction antidote' 25086 PDB 2MRN 'BMRB Entry Tracking System' 25086 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25086 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 25564525 _Citation.Full_citation . _Citation.Title 'Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nucleic Acids Res.' _Citation.Journal_name_full . _Citation.Journal_volume 43 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1241 _Citation.Page_last 1256 _Citation.Year 2015 _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 Valentina Zorzini . . . 25086 1 2 Lieven Buts . . . 25086 1 3 Evelyne Schrank . . . 25086 1 4 Yann Sterckx . G.J. . 25086 1 5 Michal Respondek . . . 25086 1 6 Hanna Engelberg-Kulka . . . 25086 1 7 Remy Loris . . . 25086 1 8 Klaus Zangger . . . 25086 1 9 Nico 'van Nuland' . A.J. . 25086 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25086 _Assembly.ID 1 _Assembly.Name 'truncated EcMazE' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'truncated EcMazE_1' 1 $truncEcMazE A . yes native no no . . . 25086 1 2 'truncated EcMazE_2' 1 $truncEcMazE B . yes native no no . . . 25086 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_truncEcMazE _Entity.Sf_category entity _Entity.Sf_framecode truncEcMazE _Entity.Entry_ID 25086 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name truncEcMazE _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A,B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; NHKVHHHHHHMSDDDDKGIH SSVKRWGNSPAVRIPATLMQ ALNLNIDDEVKIDLVDGKLI IEPVRKE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 67 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7675.774 _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 25092 . entity_1 . . . . . 100.00 67 100.00 100.00 1.56e-38 . . . . 25086 1 2 no BMRB 25093 . full_EcMazE_free . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 3 no BMRB 25094 . full_EcMazE-DNA . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 4 no PDB 1MVF . "Maze Addiction Antidote" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 5 no PDB 1UB4 . "Crystal Structure Of Mazef Complex" . . . . . 73.13 85 100.00 100.00 1.54e-24 . . . . 25086 1 6 no PDB 2MRN . "Structure Of Truncated Ecmaze" . . . . . 100.00 67 100.00 100.00 1.56e-38 . . . . 25086 1 7 no PDB 2MRU . "Structure Of Truncated Ecmaze-dna Complex" . . . . . 100.00 67 100.00 100.00 1.56e-38 . . . . 25086 1 8 no DBJ BAA41177 . "ChpAI [Escherichia coli]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 9 no DBJ BAB37066 . "suppressor of ChpA inhibitory function [Escherichia coli O157:H7 str. Sakai]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 10 no DBJ BAE76857 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia coli str. K12 substr. W3110]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 11 no DBJ BAG78565 . "suppressor of inhibitor protein [Escherichia coli SE11]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 12 no DBJ BAI27044 . "antitoxin ChpR of the ChpA-ChpR toxin-antitoxin system [Escherichia coli O26:H11 str. 11368]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 13 no EMBL CAP77216 . "PemI-like protein 1 [Escherichia coli LF82]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 14 no EMBL CAQ33107 . "MazE antitoxin of the MazF-MazE toxin-antitoxin system, subunit of MazE-MazF complex [Escherichia coli BL21(DE3)]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 15 no EMBL CAQ87849 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia fergusonii ATCC 35469]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 16 no EMBL CAQ99711 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia coli IAI1]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 17 no EMBL CAR04293 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia coli S88]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 18 no GB AAA03238 . "homologous to plasmid R100 pemI gene [Escherichia coli]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 19 no GB AAA69293 . "pemI-like protein 1 [Escherichia coli str. K-12 substr. MG1655]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 20 no GB AAC75825 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia coli str. K-12 substr. MG1655]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 21 no GB AAG57896 . "suppressor of inhibitory function of ChpA, PemI-like, autoregulated [Escherichia coli O157:H7 str. EDL933]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 22 no GB AAZ89539 . "suppressor of inhibitory function of ChpA, PemI-like, autoregulated [Shigella sonnei Ss046]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 23 no REF NP_311670 . "antitoxin MazE [Escherichia coli O157:H7 str. Sakai]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 24 no REF NP_417263 . "antitoxin of the ChpA-ChpR toxin-antitoxin system [Escherichia coli str. K-12 substr. MG1655]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 25 no REF WP_000581935 . "antitoxin MazE [Escherichia coli]" . . . . . 73.13 82 97.96 97.96 1.13e-23 . . . . 25086 1 26 no REF WP_000581936 . "antitoxin MazE [Escherichia coli]" . . . . . 73.13 82 100.00 100.00 1.07e-24 . . . . 25086 1 27 no REF WP_000581937 . "MULTISPECIES: antitoxin MazE [Proteobacteria]" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 28 no SP P0AE72 . "RecName: Full=Antitoxin MazE" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 1 29 no SP P0AE73 . "RecName: Full=Antitoxin MazE" . . . . . 73.13 82 100.00 100.00 8.88e-25 . . . . 25086 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 -16 ASN . 25086 1 2 -15 HIS . 25086 1 3 -14 LYS . 25086 1 4 -13 VAL . 25086 1 5 -12 HIS . 25086 1 6 -11 HIS . 25086 1 7 -10 HIS . 25086 1 8 -9 HIS . 25086 1 9 -8 HIS . 25086 1 10 -7 HIS . 25086 1 11 -6 MET . 25086 1 12 -5 SER . 25086 1 13 -4 ASP . 25086 1 14 -3 ASP . 25086 1 15 -2 ASP . 25086 1 16 -1 ASP . 25086 1 17 0 LYS . 25086 1 18 1 GLY . 25086 1 19 2 ILE . 25086 1 20 3 HIS . 25086 1 21 4 SER . 25086 1 22 5 SER . 25086 1 23 6 VAL . 25086 1 24 7 LYS . 25086 1 25 8 ARG . 25086 1 26 9 TRP . 25086 1 27 10 GLY . 25086 1 28 11 ASN . 25086 1 29 12 SER . 25086 1 30 13 PRO . 25086 1 31 14 ALA . 25086 1 32 15 VAL . 25086 1 33 16 ARG . 25086 1 34 17 ILE . 25086 1 35 18 PRO . 25086 1 36 19 ALA . 25086 1 37 20 THR . 25086 1 38 21 LEU . 25086 1 39 22 MET . 25086 1 40 23 GLN . 25086 1 41 24 ALA . 25086 1 42 25 LEU . 25086 1 43 26 ASN . 25086 1 44 27 LEU . 25086 1 45 28 ASN . 25086 1 46 29 ILE . 25086 1 47 30 ASP . 25086 1 48 31 ASP . 25086 1 49 32 GLU . 25086 1 50 33 VAL . 25086 1 51 34 LYS . 25086 1 52 35 ILE . 25086 1 53 36 ASP . 25086 1 54 37 LEU . 25086 1 55 38 VAL . 25086 1 56 39 ASP . 25086 1 57 40 GLY . 25086 1 58 41 LYS . 25086 1 59 42 LEU . 25086 1 60 43 ILE . 25086 1 61 44 ILE . 25086 1 62 45 GLU . 25086 1 63 46 PRO . 25086 1 64 47 VAL . 25086 1 65 48 ARG . 25086 1 66 49 LYS . 25086 1 67 50 GLU . 25086 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ASN 1 1 25086 1 . HIS 2 2 25086 1 . LYS 3 3 25086 1 . VAL 4 4 25086 1 . HIS 5 5 25086 1 . HIS 6 6 25086 1 . HIS 7 7 25086 1 . HIS 8 8 25086 1 . HIS 9 9 25086 1 . HIS 10 10 25086 1 . MET 11 11 25086 1 . SER 12 12 25086 1 . ASP 13 13 25086 1 . ASP 14 14 25086 1 . ASP 15 15 25086 1 . ASP 16 16 25086 1 . LYS 17 17 25086 1 . GLY 18 18 25086 1 . ILE 19 19 25086 1 . HIS 20 20 25086 1 . SER 21 21 25086 1 . SER 22 22 25086 1 . VAL 23 23 25086 1 . LYS 24 24 25086 1 . ARG 25 25 25086 1 . TRP 26 26 25086 1 . GLY 27 27 25086 1 . ASN 28 28 25086 1 . SER 29 29 25086 1 . PRO 30 30 25086 1 . ALA 31 31 25086 1 . VAL 32 32 25086 1 . ARG 33 33 25086 1 . ILE 34 34 25086 1 . PRO 35 35 25086 1 . ALA 36 36 25086 1 . THR 37 37 25086 1 . LEU 38 38 25086 1 . MET 39 39 25086 1 . GLN 40 40 25086 1 . ALA 41 41 25086 1 . LEU 42 42 25086 1 . ASN 43 43 25086 1 . LEU 44 44 25086 1 . ASN 45 45 25086 1 . ILE 46 46 25086 1 . ASP 47 47 25086 1 . ASP 48 48 25086 1 . GLU 49 49 25086 1 . VAL 50 50 25086 1 . LYS 51 51 25086 1 . ILE 52 52 25086 1 . ASP 53 53 25086 1 . LEU 54 54 25086 1 . VAL 55 55 25086 1 . ASP 56 56 25086 1 . GLY 57 57 25086 1 . LYS 58 58 25086 1 . LEU 59 59 25086 1 . ILE 60 60 25086 1 . ILE 61 61 25086 1 . GLU 62 62 25086 1 . PRO 63 63 25086 1 . VAL 64 64 25086 1 . ARG 65 65 25086 1 . LYS 66 66 25086 1 . GLU 67 67 25086 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 25086 _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 $truncEcMazE . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 25086 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 25086 _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 $truncEcMazE . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pQE30-mazE . . . . . . 25086 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25086 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _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 truncEcMazE '[U-99% 13C; U-99% 15N]' . . 1 $truncEcMazE . . 1 . . mM . . . . 25086 1 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 25086 1 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 25086 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25086 1 5 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25086 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 25086 _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 temperature 298 . K 25086 1 pH 6.5 . pH 25086 1 pressure 1 . atm 25086 1 'ionic strength' 50 . mM 25086 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 25086 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 25086 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 25086 1 stop_ save_ save_CcpNMR _Software.Sf_category software _Software.Sf_framecode CcpNMR _Software.Entry_ID 25086 _Software.ID 2 _Software.Name CcpNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 25086 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25086 2 'data analysis' 25086 2 'peak picking' 25086 2 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 25086 _Software.ID 3 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 25086 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25086 3 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 25086 _Software.ID 4 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 25086 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 25086 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 25086 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 25086 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model VNMRS _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 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 25086 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian VNMRS . 600 . . . 25086 1 2 spectrometer_2 Varian VNMRS . 800 . . . 25086 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 25086 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 3 '2D 1H-13C HSQC aromatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 4 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 5 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 6 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 7 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 8 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 9 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25086 1 10 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25086 1 11 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25086 1 12 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 25086 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 25086 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 25086 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 25086 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 25086 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 25086 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 25086 1 2 '2D 1H-13C HSQC' . . . 25086 1 3 '2D 1H-13C HSQC aromatic' . . . 25086 1 4 '3D HNCACB' . . . 25086 1 5 '3D CBCA(CO)NH' . . . 25086 1 6 '3D HNCO' . . . 25086 1 7 '3D C(CO)NH' . . . 25086 1 8 '3D HBHA(CO)NH' . . . 25086 1 9 '3D HCCH-TOCSY' . . . 25086 1 10 '2D 1H-1H NOESY' . . . 25086 1 11 '3D 1H-15N NOESY' . . . 25086 1 12 '3D 1H-13C NOESY' . . . 25086 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ASN HB2 H 1 2.772 0.002 . 1 . . . A -16 ASN HB2 . 25086 1 2 . 1 1 1 1 ASN HB3 H 1 2.772 0.002 . 1 . . . A -16 ASN HB3 . 25086 1 3 . 1 1 1 1 ASN HD21 H 1 7.644 0.002 . 1 . . . A -16 ASN HD21 . 25086 1 4 . 1 1 1 1 ASN HD22 H 1 6.940 0.001 . 1 . . . A -16 ASN HD22 . 25086 1 5 . 1 1 1 1 ASN CA C 13 53.114 0.041 . 1 . . . A -16 ASN CA . 25086 1 6 . 1 1 1 1 ASN CB C 13 38.857 0.021 . 1 . . . A -16 ASN CB . 25086 1 7 . 1 1 1 1 ASN ND2 N 15 112.962 0.013 . 1 . . . A -16 ASN ND2 . 25086 1 8 . 1 1 2 2 HIS HA H 1 4.607 0.000 . 1 . . . A -15 HIS HA . 25086 1 9 . 1 1 2 2 HIS HB2 H 1 3.049 0.000 . 2 . . . A -15 HIS HB2 . 25086 1 10 . 1 1 2 2 HIS HB3 H 1 3.165 0.000 . 2 . . . A -15 HIS HB3 . 25086 1 11 . 1 1 2 2 HIS C C 13 174.805 0.000 . 1 . . . A -15 HIS C . 25086 1 12 . 1 1 2 2 HIS CA C 13 56.098 0.000 . 1 . . . A -15 HIS CA . 25086 1 13 . 1 1 2 2 HIS CB C 13 30.380 0.031 . 1 . . . A -15 HIS CB . 25086 1 14 . 1 1 3 3 LYS H H 1 8.354 0.001 . 1 . . . A -14 LYS H . 25086 1 15 . 1 1 3 3 LYS HA H 1 4.243 0.003 . 1 . . . A -14 LYS HA . 25086 1 16 . 1 1 3 3 LYS HB2 H 1 1.677 0.002 . 1 . . . A -14 LYS HB2 . 25086 1 17 . 1 1 3 3 LYS HB3 H 1 1.677 0.002 . 1 . . . A -14 LYS HB3 . 25086 1 18 . 1 1 3 3 LYS HG2 H 1 1.282 0.000 . 1 . . . A -14 LYS HG2 . 25086 1 19 . 1 1 3 3 LYS HG3 H 1 1.282 0.000 . 1 . . . A -14 LYS HG3 . 25086 1 20 . 1 1 3 3 LYS C C 13 176.150 0.000 . 1 . . . A -14 LYS C . 25086 1 21 . 1 1 3 3 LYS CA C 13 56.348 0.043 . 1 . . . A -14 LYS CA . 25086 1 22 . 1 1 3 3 LYS CB C 13 32.985 0.026 . 1 . . . A -14 LYS CB . 25086 1 23 . 1 1 3 3 LYS CG C 13 24.670 0.000 . 1 . . . A -14 LYS CG . 25086 1 24 . 1 1 3 3 LYS CD C 13 28.987 0.000 . 1 . . . A -14 LYS CD . 25086 1 25 . 1 1 3 3 LYS CE C 13 42.071 0.000 . 1 . . . A -14 LYS CE . 25086 1 26 . 1 1 3 3 LYS N N 15 122.750 0.027 . 1 . . . A -14 LYS N . 25086 1 27 . 1 1 4 4 VAL H H 1 8.098 0.002 . 1 . . . A -13 VAL H . 25086 1 28 . 1 1 4 4 VAL HA H 1 3.978 0.001 . 1 . . . A -13 VAL HA . 25086 1 29 . 1 1 4 4 VAL HB H 1 1.895 0.003 . 1 . . . A -13 VAL HB . 25086 1 30 . 1 1 4 4 VAL HG11 H 1 0.727 0.000 . 2 . . . A -13 VAL HG11 . 25086 1 31 . 1 1 4 4 VAL HG12 H 1 0.727 0.000 . 2 . . . A -13 VAL HG12 . 25086 1 32 . 1 1 4 4 VAL HG13 H 1 0.727 0.000 . 2 . . . A -13 VAL HG13 . 25086 1 33 . 1 1 4 4 VAL HG21 H 1 0.821 0.002 . 2 . . . A -13 VAL HG21 . 25086 1 34 . 1 1 4 4 VAL HG22 H 1 0.821 0.002 . 2 . . . A -13 VAL HG22 . 25086 1 35 . 1 1 4 4 VAL HG23 H 1 0.821 0.002 . 2 . . . A -13 VAL HG23 . 25086 1 36 . 1 1 4 4 VAL C C 13 175.611 0.000 . 1 . . . A -13 VAL C . 25086 1 37 . 1 1 4 4 VAL CA C 13 62.148 0.043 . 1 . . . A -13 VAL CA . 25086 1 38 . 1 1 4 4 VAL CB C 13 32.815 0.031 . 1 . . . A -13 VAL CB . 25086 1 39 . 1 1 4 4 VAL CG1 C 13 20.759 0.000 . 1 . . . A -13 VAL CG1 . 25086 1 40 . 1 1 4 4 VAL CG2 C 13 20.759 0.000 . 1 . . . A -13 VAL CG2 . 25086 1 41 . 1 1 4 4 VAL N N 15 121.546 0.047 . 1 . . . A -13 VAL N . 25086 1 42 . 1 1 5 5 HIS H H 1 8.438 0.002 . 1 . . . A -12 HIS H . 25086 1 43 . 1 1 5 5 HIS CA C 13 55.526 0.000 . 1 . . . A -12 HIS CA . 25086 1 44 . 1 1 5 5 HIS CB C 13 30.440 0.000 . 1 . . . A -12 HIS CB . 25086 1 45 . 1 1 5 5 HIS N N 15 123.329 0.008 . 1 . . . A -12 HIS N . 25086 1 46 . 1 1 10 10 HIS HA H 1 4.606 0.003 . 1 . . . A -7 HIS HA . 25086 1 47 . 1 1 10 10 HIS HB2 H 1 3.162 0.000 . 2 . . . A -7 HIS HB2 . 25086 1 48 . 1 1 10 10 HIS HB3 H 1 3.082 0.000 . 2 . . . A -7 HIS HB3 . 25086 1 49 . 1 1 10 10 HIS C C 13 174.714 0.000 . 1 . . . A -7 HIS C . 25086 1 50 . 1 1 10 10 HIS CA C 13 55.981 0.000 . 1 . . . A -7 HIS CA . 25086 1 51 . 1 1 10 10 HIS CB C 13 29.905 0.031 . 1 . . . A -7 HIS CB . 25086 1 52 . 1 1 11 11 MET H H 1 8.520 0.003 . 1 . . . A -6 MET H . 25086 1 53 . 1 1 11 11 MET HA H 1 4.453 0.002 . 1 . . . A -6 MET HA . 25086 1 54 . 1 1 11 11 MET HB2 H 1 1.959 0.009 . 2 . . . A -6 MET HB2 . 25086 1 55 . 1 1 11 11 MET HB3 H 1 2.066 0.003 . 2 . . . A -6 MET HB3 . 25086 1 56 . 1 1 11 11 MET HG2 H 1 2.453 0.001 . 2 . . . A -6 MET HG2 . 25086 1 57 . 1 1 11 11 MET HG3 H 1 2.518 0.000 . 2 . . . A -6 MET HG3 . 25086 1 58 . 1 1 11 11 MET HE1 H 1 2.043 0.000 . 1 . . . A -6 MET HE1 . 25086 1 59 . 1 1 11 11 MET HE2 H 1 2.043 0.000 . 1 . . . A -6 MET HE2 . 25086 1 60 . 1 1 11 11 MET HE3 H 1 2.043 0.000 . 1 . . . A -6 MET HE3 . 25086 1 61 . 1 1 11 11 MET C C 13 176.091 0.000 . 1 . . . A -6 MET C . 25086 1 62 . 1 1 11 11 MET CA C 13 55.658 0.031 . 1 . . . A -6 MET CA . 25086 1 63 . 1 1 11 11 MET CB C 13 32.952 0.021 . 1 . . . A -6 MET CB . 25086 1 64 . 1 1 11 11 MET CG C 13 32.027 0.063 . 1 . . . A -6 MET CG . 25086 1 65 . 1 1 11 11 MET CE C 13 16.910 0.000 . 1 . . . A -6 MET CE . 25086 1 66 . 1 1 11 11 MET N N 15 122.431 0.015 . 1 . . . A -6 MET N . 25086 1 67 . 1 1 12 12 SER H H 1 8.410 0.001 . 1 . . . A -5 SER H . 25086 1 68 . 1 1 12 12 SER HA H 1 4.444 0.004 . 1 . . . A -5 SER HA . 25086 1 69 . 1 1 12 12 SER HB2 H 1 3.891 0.001 . 2 . . . A -5 SER HB2 . 25086 1 70 . 1 1 12 12 SER HB3 H 1 3.832 0.002 . 2 . . . A -5 SER HB3 . 25086 1 71 . 1 1 12 12 SER C C 13 174.462 0.000 . 1 . . . A -5 SER C . 25086 1 72 . 1 1 12 12 SER CA C 13 58.379 0.068 . 1 . . . A -5 SER CA . 25086 1 73 . 1 1 12 12 SER CB C 13 63.989 0.035 . 1 . . . A -5 SER CB . 25086 1 74 . 1 1 12 12 SER N N 15 116.616 0.012 . 1 . . . A -5 SER N . 25086 1 75 . 1 1 13 13 ASP H H 1 8.429 0.001 . 1 . . . A -4 ASP H . 25086 1 76 . 1 1 13 13 ASP HA H 1 4.602 0.002 . 1 . . . A -4 ASP HA . 25086 1 77 . 1 1 13 13 ASP HB2 H 1 2.623 0.000 . 2 . . . A -4 ASP HB2 . 25086 1 78 . 1 1 13 13 ASP HB3 H 1 2.712 0.002 . 2 . . . A -4 ASP HB3 . 25086 1 79 . 1 1 13 13 ASP C C 13 176.198 0.000 . 1 . . . A -4 ASP C . 25086 1 80 . 1 1 13 13 ASP CA C 13 54.780 0.050 . 1 . . . A -4 ASP CA . 25086 1 81 . 1 1 13 13 ASP CB C 13 41.117 0.014 . 1 . . . A -4 ASP CB . 25086 1 82 . 1 1 13 13 ASP N N 15 122.320 0.023 . 1 . . . A -4 ASP N . 25086 1 83 . 1 1 14 14 ASP H H 1 8.206 0.002 . 1 . . . A -3 ASP H . 25086 1 84 . 1 1 14 14 ASP HA H 1 4.564 0.003 . 1 . . . A -3 ASP HA . 25086 1 85 . 1 1 14 14 ASP HB2 H 1 2.582 0.001 . 2 . . . A -3 ASP HB2 . 25086 1 86 . 1 1 14 14 ASP HB3 H 1 2.696 0.000 . 2 . . . A -3 ASP HB3 . 25086 1 87 . 1 1 14 14 ASP C C 13 176.246 0.000 . 1 . . . A -3 ASP C . 25086 1 88 . 1 1 14 14 ASP CA C 13 54.729 0.037 . 1 . . . A -3 ASP CA . 25086 1 89 . 1 1 14 14 ASP CB C 13 41.194 0.034 . 1 . . . A -3 ASP CB . 25086 1 90 . 1 1 14 14 ASP N N 15 119.793 0.027 . 1 . . . A -3 ASP N . 25086 1 91 . 1 1 15 15 ASP H H 1 8.170 0.001 . 1 . . . A -2 ASP H . 25086 1 92 . 1 1 15 15 ASP HA H 1 4.567 0.007 . 1 . . . A -2 ASP HA . 25086 1 93 . 1 1 15 15 ASP HB2 H 1 2.637 0.000 . 2 . . . A -2 ASP HB2 . 25086 1 94 . 1 1 15 15 ASP HB3 H 1 2.710 0.000 . 2 . . . A -2 ASP HB3 . 25086 1 95 . 1 1 15 15 ASP C C 13 176.053 0.000 . 1 . . . A -2 ASP C . 25086 1 96 . 1 1 15 15 ASP CA C 13 54.738 0.044 . 1 . . . A -2 ASP CA . 25086 1 97 . 1 1 15 15 ASP CB C 13 41.244 0.056 . 1 . . . A -2 ASP CB . 25086 1 98 . 1 1 15 15 ASP N N 15 120.270 0.008 . 1 . . . A -2 ASP N . 25086 1 99 . 1 1 16 16 ASP H H 1 8.225 0.001 . 1 . . . A -1 ASP H . 25086 1 100 . 1 1 16 16 ASP HA H 1 4.590 0.008 . 1 . . . A -1 ASP HA . 25086 1 101 . 1 1 16 16 ASP HB2 H 1 2.757 0.000 . 2 . . . A -1 ASP HB2 . 25086 1 102 . 1 1 16 16 ASP HB3 H 1 2.670 0.000 . 2 . . . A -1 ASP HB3 . 25086 1 103 . 1 1 16 16 ASP C C 13 176.306 0.000 . 1 . . . A -1 ASP C . 25086 1 104 . 1 1 16 16 ASP CA C 13 54.415 0.056 . 1 . . . A -1 ASP CA . 25086 1 105 . 1 1 16 16 ASP CB C 13 41.104 0.035 . 1 . . . A -1 ASP CB . 25086 1 106 . 1 1 16 16 ASP N N 15 120.279 0.017 . 1 . . . A -1 ASP N . 25086 1 107 . 1 1 17 17 LYS H H 1 8.251 0.001 . 1 . . . A 0 LYS H . 25086 1 108 . 1 1 17 17 LYS HA H 1 4.385 0.001 . 1 . . . A 0 LYS HA . 25086 1 109 . 1 1 17 17 LYS HB2 H 1 1.801 0.002 . 2 . . . A 0 LYS HB2 . 25086 1 110 . 1 1 17 17 LYS HB3 H 1 1.931 0.002 . 2 . . . A 0 LYS HB3 . 25086 1 111 . 1 1 17 17 LYS HG2 H 1 1.454 0.000 . 1 . . . A 0 LYS HG2 . 25086 1 112 . 1 1 17 17 LYS HG3 H 1 1.454 0.000 . 1 . . . A 0 LYS HG3 . 25086 1 113 . 1 1 17 17 LYS HD2 H 1 1.662 0.000 . 1 . . . A 0 LYS HD2 . 25086 1 114 . 1 1 17 17 LYS HD3 H 1 1.662 0.000 . 1 . . . A 0 LYS HD3 . 25086 1 115 . 1 1 17 17 LYS C C 13 177.017 0.000 . 1 . . . A 0 LYS C . 25086 1 116 . 1 1 17 17 LYS CA C 13 56.097 0.023 . 1 . . . A 0 LYS CA . 25086 1 117 . 1 1 17 17 LYS CB C 13 32.969 0.018 . 1 . . . A 0 LYS CB . 25086 1 118 . 1 1 17 17 LYS CG C 13 24.735 0.000 . 1 . . . A 0 LYS CG . 25086 1 119 . 1 1 17 17 LYS CD C 13 28.868 0.000 . 1 . . . A 0 LYS CD . 25086 1 120 . 1 1 17 17 LYS CE C 13 42.233 0.000 . 1 . . . A 0 LYS CE . 25086 1 121 . 1 1 17 17 LYS N N 15 121.408 0.018 . 1 . . . A 0 LYS N . 25086 1 122 . 1 1 18 18 GLY H H 1 8.370 0.002 . 1 . . . A 1 GLY H . 25086 1 123 . 1 1 18 18 GLY HA2 H 1 3.844 0.003 . 2 . . . A 1 GLY HA2 . 25086 1 124 . 1 1 18 18 GLY HA3 H 1 3.988 0.001 . 2 . . . A 1 GLY HA3 . 25086 1 125 . 1 1 18 18 GLY C C 13 173.630 0.000 . 1 . . . A 1 GLY C . 25086 1 126 . 1 1 18 18 GLY CA C 13 45.285 0.031 . 1 . . . A 1 GLY CA . 25086 1 127 . 1 1 18 18 GLY N N 15 109.054 0.014 . 1 . . . A 1 GLY N . 25086 1 128 . 1 1 19 19 ILE H H 1 8.579 0.003 . 1 . . . A 2 ILE H . 25086 1 129 . 1 1 19 19 ILE HA H 1 4.297 0.002 . 1 . . . A 2 ILE HA . 25086 1 130 . 1 1 19 19 ILE HB H 1 1.876 0.004 . 1 . . . A 2 ILE HB . 25086 1 131 . 1 1 19 19 ILE HG12 H 1 1.515 0.005 . 2 . . . A 2 ILE HG12 . 25086 1 132 . 1 1 19 19 ILE HG13 H 1 1.181 0.004 . 2 . . . A 2 ILE HG13 . 25086 1 133 . 1 1 19 19 ILE HG21 H 1 0.867 0.005 . 1 . . . A 2 ILE HG21 . 25086 1 134 . 1 1 19 19 ILE HG22 H 1 0.867 0.005 . 1 . . . A 2 ILE HG22 . 25086 1 135 . 1 1 19 19 ILE HG23 H 1 0.867 0.005 . 1 . . . A 2 ILE HG23 . 25086 1 136 . 1 1 19 19 ILE HD11 H 1 0.844 0.006 . 1 . . . A 2 ILE HD11 . 25086 1 137 . 1 1 19 19 ILE HD12 H 1 0.844 0.006 . 1 . . . A 2 ILE HD12 . 25086 1 138 . 1 1 19 19 ILE HD13 H 1 0.844 0.006 . 1 . . . A 2 ILE HD13 . 25086 1 139 . 1 1 19 19 ILE C C 13 175.993 0.000 . 1 . . . A 2 ILE C . 25086 1 140 . 1 1 19 19 ILE CA C 13 60.832 0.044 . 1 . . . A 2 ILE CA . 25086 1 141 . 1 1 19 19 ILE CB C 13 39.733 0.039 . 1 . . . A 2 ILE CB . 25086 1 142 . 1 1 19 19 ILE CG1 C 13 27.591 0.000 . 1 . . . A 2 ILE CG1 . 25086 1 143 . 1 1 19 19 ILE CG2 C 13 17.738 0.035 . 1 . . . A 2 ILE CG2 . 25086 1 144 . 1 1 19 19 ILE CD1 C 13 13.462 0.021 . 1 . . . A 2 ILE CD1 . 25086 1 145 . 1 1 19 19 ILE N N 15 120.862 0.027 . 1 . . . A 2 ILE N . 25086 1 146 . 1 1 20 20 HIS H H 1 8.920 0.003 . 1 . . . A 3 HIS H . 25086 1 147 . 1 1 20 20 HIS HA H 1 5.234 0.004 . 1 . . . A 3 HIS HA . 25086 1 148 . 1 1 20 20 HIS HB2 H 1 3.153 0.004 . 2 . . . A 3 HIS HB2 . 25086 1 149 . 1 1 20 20 HIS HB3 H 1 3.274 0.008 . 2 . . . A 3 HIS HB3 . 25086 1 150 . 1 1 20 20 HIS HD2 H 1 7.111 0.000 . 1 . . . A 3 HIS HD2 . 25086 1 151 . 1 1 20 20 HIS C C 13 174.751 0.000 . 1 . . . A 3 HIS C . 25086 1 152 . 1 1 20 20 HIS CA C 13 55.285 0.062 . 1 . . . A 3 HIS CA . 25086 1 153 . 1 1 20 20 HIS CB C 13 30.076 0.009 . 1 . . . A 3 HIS CB . 25086 1 154 . 1 1 20 20 HIS N N 15 124.483 0.014 . 1 . . . A 3 HIS N . 25086 1 155 . 1 1 21 21 SER H H 1 8.925 0.002 . 1 . . . A 4 SER H . 25086 1 156 . 1 1 21 21 SER HA H 1 4.712 0.007 . 1 . . . A 4 SER HA . 25086 1 157 . 1 1 21 21 SER HB2 H 1 3.432 0.003 . 2 . . . A 4 SER HB2 . 25086 1 158 . 1 1 21 21 SER HB3 H 1 3.768 0.004 . 2 . . . A 4 SER HB3 . 25086 1 159 . 1 1 21 21 SER C C 13 174.112 0.000 . 1 . . . A 4 SER C . 25086 1 160 . 1 1 21 21 SER CA C 13 56.102 0.043 . 1 . . . A 4 SER CA . 25086 1 161 . 1 1 21 21 SER CB C 13 64.679 0.034 . 1 . . . A 4 SER CB . 25086 1 162 . 1 1 21 21 SER N N 15 117.417 0.010 . 1 . . . A 4 SER N . 25086 1 163 . 1 1 22 22 SER H H 1 8.623 0.002 . 1 . . . A 5 SER H . 25086 1 164 . 1 1 22 22 SER HA H 1 5.390 0.003 . 1 . . . A 5 SER HA . 25086 1 165 . 1 1 22 22 SER HB2 H 1 3.536 0.004 . 2 . . . A 5 SER HB2 . 25086 1 166 . 1 1 22 22 SER HB3 H 1 3.820 0.003 . 2 . . . A 5 SER HB3 . 25086 1 167 . 1 1 22 22 SER C C 13 173.075 0.000 . 1 . . . A 5 SER C . 25086 1 168 . 1 1 22 22 SER CA C 13 57.153 0.036 . 1 . . . A 5 SER CA . 25086 1 169 . 1 1 22 22 SER CB C 13 65.752 0.023 . 1 . . . A 5 SER CB . 25086 1 170 . 1 1 22 22 SER N N 15 114.372 0.013 . 1 . . . A 5 SER N . 25086 1 171 . 1 1 23 23 VAL H H 1 8.384 0.002 . 1 . . . A 6 VAL H . 25086 1 172 . 1 1 23 23 VAL HA H 1 4.169 0.004 . 1 . . . A 6 VAL HA . 25086 1 173 . 1 1 23 23 VAL HB H 1 2.137 0.003 . 1 . . . A 6 VAL HB . 25086 1 174 . 1 1 23 23 VAL HG11 H 1 0.903 0.004 . 2 . . . A 6 VAL HG11 . 25086 1 175 . 1 1 23 23 VAL HG12 H 1 0.903 0.004 . 2 . . . A 6 VAL HG12 . 25086 1 176 . 1 1 23 23 VAL HG13 H 1 0.903 0.004 . 2 . . . A 6 VAL HG13 . 25086 1 177 . 1 1 23 23 VAL HG21 H 1 0.793 0.003 . 2 . . . A 6 VAL HG21 . 25086 1 178 . 1 1 23 23 VAL HG22 H 1 0.793 0.003 . 2 . . . A 6 VAL HG22 . 25086 1 179 . 1 1 23 23 VAL HG23 H 1 0.793 0.003 . 2 . . . A 6 VAL HG23 . 25086 1 180 . 1 1 23 23 VAL C C 13 175.872 0.000 . 1 . . . A 6 VAL C . 25086 1 181 . 1 1 23 23 VAL CA C 13 62.746 0.036 . 1 . . . A 6 VAL CA . 25086 1 182 . 1 1 23 23 VAL CB C 13 31.497 0.063 . 1 . . . A 6 VAL CB . 25086 1 183 . 1 1 23 23 VAL CG1 C 13 22.689 0.025 . 2 . . . A 6 VAL CG1 . 25086 1 184 . 1 1 23 23 VAL CG2 C 13 21.625 0.050 . 2 . . . A 6 VAL CG2 . 25086 1 185 . 1 1 23 23 VAL N N 15 121.311 0.014 . 1 . . . A 6 VAL N . 25086 1 186 . 1 1 24 24 LYS H H 1 9.042 0.002 . 1 . . . A 7 LYS H . 25086 1 187 . 1 1 24 24 LYS HA H 1 4.965 0.005 . 1 . . . A 7 LYS HA . 25086 1 188 . 1 1 24 24 LYS HB2 H 1 1.874 0.004 . 2 . . . A 7 LYS HB2 . 25086 1 189 . 1 1 24 24 LYS HB3 H 1 2.248 0.004 . 2 . . . A 7 LYS HB3 . 25086 1 190 . 1 1 24 24 LYS HG2 H 1 1.559 0.006 . 1 . . . A 7 LYS HG2 . 25086 1 191 . 1 1 24 24 LYS HG3 H 1 1.559 0.006 . 1 . . . A 7 LYS HG3 . 25086 1 192 . 1 1 24 24 LYS HD2 H 1 1.749 0.006 . 2 . . . A 7 LYS HD2 . 25086 1 193 . 1 1 24 24 LYS HD3 H 1 1.676 0.002 . 2 . . . A 7 LYS HD3 . 25086 1 194 . 1 1 24 24 LYS HE2 H 1 2.915 0.001 . 2 . . . A 7 LYS HE2 . 25086 1 195 . 1 1 24 24 LYS HE3 H 1 3.038 0.001 . 2 . . . A 7 LYS HE3 . 25086 1 196 . 1 1 24 24 LYS C C 13 174.655 0.000 . 1 . . . A 7 LYS C . 25086 1 197 . 1 1 24 24 LYS CA C 13 53.609 0.038 . 1 . . . A 7 LYS CA . 25086 1 198 . 1 1 24 24 LYS CB C 13 36.574 0.029 . 1 . . . A 7 LYS CB . 25086 1 199 . 1 1 24 24 LYS CG C 13 24.549 0.000 . 1 . . . A 7 LYS CG . 25086 1 200 . 1 1 24 24 LYS CD C 13 28.355 0.018 . 1 . . . A 7 LYS CD . 25086 1 201 . 1 1 24 24 LYS CE C 13 42.162 0.000 . 1 . . . A 7 LYS CE . 25086 1 202 . 1 1 24 24 LYS N N 15 128.341 0.014 . 1 . . . A 7 LYS N . 25086 1 203 . 1 1 25 25 ARG H H 1 8.791 0.003 . 1 . . . A 8 ARG H . 25086 1 204 . 1 1 25 25 ARG HA H 1 4.364 0.004 . 1 . . . A 8 ARG HA . 25086 1 205 . 1 1 25 25 ARG HB2 H 1 1.589 0.005 . 2 . . . A 8 ARG HB2 . 25086 1 206 . 1 1 25 25 ARG HB3 H 1 1.939 0.003 . 2 . . . A 8 ARG HB3 . 25086 1 207 . 1 1 25 25 ARG HG2 H 1 1.205 0.008 . 2 . . . A 8 ARG HG2 . 25086 1 208 . 1 1 25 25 ARG HG3 H 1 1.395 0.005 . 2 . . . A 8 ARG HG3 . 25086 1 209 . 1 1 25 25 ARG HD2 H 1 3.198 0.011 . 2 . . . A 8 ARG HD2 . 25086 1 210 . 1 1 25 25 ARG HD3 H 1 3.249 0.011 . 2 . . . A 8 ARG HD3 . 25086 1 211 . 1 1 25 25 ARG HE H 1 7.330 0.005 . 1 . . . A 8 ARG HE . 25086 1 212 . 1 1 25 25 ARG C C 13 174.148 0.000 . 1 . . . A 8 ARG C . 25086 1 213 . 1 1 25 25 ARG CA C 13 56.176 0.037 . 1 . . . A 8 ARG CA . 25086 1 214 . 1 1 25 25 ARG CB C 13 31.506 0.045 . 1 . . . A 8 ARG CB . 25086 1 215 . 1 1 25 25 ARG CG C 13 27.913 0.027 . 1 . . . A 8 ARG CG . 25086 1 216 . 1 1 25 25 ARG CD C 13 43.535 0.037 . 1 . . . A 8 ARG CD . 25086 1 217 . 1 1 25 25 ARG N N 15 120.527 0.008 . 1 . . . A 8 ARG N . 25086 1 218 . 1 1 25 25 ARG NE N 15 83.770 0.016 . 1 . . . A 8 ARG NE . 25086 1 219 . 1 1 26 26 TRP H H 1 8.994 0.004 . 1 . . . A 9 TRP H . 25086 1 220 . 1 1 26 26 TRP HA H 1 4.652 0.002 . 1 . . . A 9 TRP HA . 25086 1 221 . 1 1 26 26 TRP HB2 H 1 0.678 0.004 . 2 . . . A 9 TRP HB2 . 25086 1 222 . 1 1 26 26 TRP HB3 H 1 2.344 0.004 . 2 . . . A 9 TRP HB3 . 25086 1 223 . 1 1 26 26 TRP HD1 H 1 6.415 0.002 . 1 . . . A 9 TRP HD1 . 25086 1 224 . 1 1 26 26 TRP HE1 H 1 9.709 0.002 . 1 . . . A 9 TRP HE1 . 25086 1 225 . 1 1 26 26 TRP HE3 H 1 6.502 0.009 . 1 . . . A 9 TRP HE3 . 25086 1 226 . 1 1 26 26 TRP HZ2 H 1 7.403 0.001 . 1 . . . A 9 TRP HZ2 . 25086 1 227 . 1 1 26 26 TRP HZ3 H 1 6.775 0.004 . 1 . . . A 9 TRP HZ3 . 25086 1 228 . 1 1 26 26 TRP HH2 H 1 6.771 0.002 . 1 . . . A 9 TRP HH2 . 25086 1 229 . 1 1 26 26 TRP C C 13 176.351 0.000 . 1 . . . A 9 TRP C . 25086 1 230 . 1 1 26 26 TRP CA C 13 53.037 0.018 . 1 . . . A 9 TRP CA . 25086 1 231 . 1 1 26 26 TRP CB C 13 28.066 0.044 . 1 . . . A 9 TRP CB . 25086 1 232 . 1 1 26 26 TRP CD1 C 13 122.831 0.000 . 1 . . . A 9 TRP CD1 . 25086 1 233 . 1 1 26 26 TRP CE3 C 13 119.646 0.000 . 1 . . . A 9 TRP CE3 . 25086 1 234 . 1 1 26 26 TRP CZ2 C 13 114.426 0.000 . 1 . . . A 9 TRP CZ2 . 25086 1 235 . 1 1 26 26 TRP CZ3 C 13 124.053 0.000 . 1 . . . A 9 TRP CZ3 . 25086 1 236 . 1 1 26 26 TRP CH2 C 13 124.292 0.000 . 1 . . . A 9 TRP CH2 . 25086 1 237 . 1 1 26 26 TRP N N 15 131.164 0.014 . 1 . . . A 9 TRP N . 25086 1 238 . 1 1 26 26 TRP NE1 N 15 127.859 0.021 . 1 . . . A 9 TRP NE1 . 25086 1 239 . 1 1 27 27 GLY H H 1 9.134 0.004 . 1 . . . A 10 GLY H . 25086 1 240 . 1 1 27 27 GLY HA2 H 1 3.545 0.006 . 2 . . . A 10 GLY HA2 . 25086 1 241 . 1 1 27 27 GLY HA3 H 1 3.815 0.003 . 2 . . . A 10 GLY HA3 . 25086 1 242 . 1 1 27 27 GLY C C 13 173.798 0.000 . 1 . . . A 10 GLY C . 25086 1 243 . 1 1 27 27 GLY CA C 13 47.324 0.044 . 1 . . . A 10 GLY CA . 25086 1 244 . 1 1 27 27 GLY N N 15 117.757 0.026 . 1 . . . A 10 GLY N . 25086 1 245 . 1 1 28 28 ASN H H 1 8.667 0.004 . 1 . . . A 11 ASN H . 25086 1 246 . 1 1 28 28 ASN HA H 1 4.769 0.003 . 1 . . . A 11 ASN HA . 25086 1 247 . 1 1 28 28 ASN HB2 H 1 2.716 0.003 . 2 . . . A 11 ASN HB2 . 25086 1 248 . 1 1 28 28 ASN HB3 H 1 2.837 0.003 . 2 . . . A 11 ASN HB3 . 25086 1 249 . 1 1 28 28 ASN HD21 H 1 6.849 0.003 . 1 . . . A 11 ASN HD21 . 25086 1 250 . 1 1 28 28 ASN HD22 H 1 7.545 0.002 . 1 . . . A 11 ASN HD22 . 25086 1 251 . 1 1 28 28 ASN C C 13 175.190 0.000 . 1 . . . A 11 ASN C . 25086 1 252 . 1 1 28 28 ASN CA C 13 52.742 0.027 . 1 . . . A 11 ASN CA . 25086 1 253 . 1 1 28 28 ASN CB C 13 39.310 0.030 . 1 . . . A 11 ASN CB . 25086 1 254 . 1 1 28 28 ASN N N 15 125.396 0.000 . 1 . . . A 11 ASN N . 25086 1 255 . 1 1 28 28 ASN ND2 N 15 112.741 0.018 . 1 . . . A 11 ASN ND2 . 25086 1 256 . 1 1 29 29 SER H H 1 7.798 0.002 . 1 . . . A 12 SER H . 25086 1 257 . 1 1 29 29 SER HA H 1 5.038 0.002 . 1 . . . A 12 SER HA . 25086 1 258 . 1 1 29 29 SER HB2 H 1 3.627 0.007 . 2 . . . A 12 SER HB2 . 25086 1 259 . 1 1 29 29 SER HB3 H 1 3.707 0.001 . 2 . . . A 12 SER HB3 . 25086 1 260 . 1 1 29 29 SER CA C 13 56.293 0.000 . 1 . . . A 12 SER CA . 25086 1 261 . 1 1 29 29 SER CB C 13 65.254 0.033 . 1 . . . A 12 SER CB . 25086 1 262 . 1 1 29 29 SER N N 15 115.939 0.014 . 1 . . . A 12 SER N . 25086 1 263 . 1 1 30 30 PRO HA H 1 4.863 0.006 . 1 . . . A 13 PRO HA . 25086 1 264 . 1 1 30 30 PRO HB2 H 1 1.993 0.001 . 2 . . . A 13 PRO HB2 . 25086 1 265 . 1 1 30 30 PRO HB3 H 1 1.933 0.003 . 2 . . . A 13 PRO HB3 . 25086 1 266 . 1 1 30 30 PRO HG2 H 1 1.931 0.002 . 2 . . . A 13 PRO HG2 . 25086 1 267 . 1 1 30 30 PRO HG3 H 1 2.334 0.003 . 2 . . . A 13 PRO HG3 . 25086 1 268 . 1 1 30 30 PRO HD2 H 1 3.865 0.004 . 2 . . . A 13 PRO HD2 . 25086 1 269 . 1 1 30 30 PRO HD3 H 1 3.995 0.004 . 2 . . . A 13 PRO HD3 . 25086 1 270 . 1 1 30 30 PRO C C 13 177.322 0.000 . 1 . . . A 13 PRO C . 25086 1 271 . 1 1 30 30 PRO CA C 13 62.129 0.038 . 1 . . . A 13 PRO CA . 25086 1 272 . 1 1 30 30 PRO CB C 13 32.618 0.009 . 1 . . . A 13 PRO CB . 25086 1 273 . 1 1 30 30 PRO CG C 13 27.837 0.016 . 1 . . . A 13 PRO CG . 25086 1 274 . 1 1 30 30 PRO CD C 13 50.834 0.064 . 1 . . . A 13 PRO CD . 25086 1 275 . 1 1 31 31 ALA H H 1 9.419 0.003 . 1 . . . A 14 ALA H . 25086 1 276 . 1 1 31 31 ALA HA H 1 5.289 0.004 . 1 . . . A 14 ALA HA . 25086 1 277 . 1 1 31 31 ALA HB1 H 1 1.334 0.003 . 1 . . . A 14 ALA HB1 . 25086 1 278 . 1 1 31 31 ALA HB2 H 1 1.334 0.003 . 1 . . . A 14 ALA HB2 . 25086 1 279 . 1 1 31 31 ALA HB3 H 1 1.334 0.003 . 1 . . . A 14 ALA HB3 . 25086 1 280 . 1 1 31 31 ALA C C 13 174.888 0.000 . 1 . . . A 14 ALA C . 25086 1 281 . 1 1 31 31 ALA CA C 13 51.770 0.018 . 1 . . . A 14 ALA CA . 25086 1 282 . 1 1 31 31 ALA CB C 13 24.271 0.031 . 1 . . . A 14 ALA CB . 25086 1 283 . 1 1 31 31 ALA N N 15 125.096 0.023 . 1 . . . A 14 ALA N . 25086 1 284 . 1 1 32 32 VAL H H 1 8.491 0.002 . 1 . . . A 15 VAL H . 25086 1 285 . 1 1 32 32 VAL HA H 1 4.741 0.005 . 1 . . . A 15 VAL HA . 25086 1 286 . 1 1 32 32 VAL HB H 1 1.785 0.008 . 1 . . . A 15 VAL HB . 25086 1 287 . 1 1 32 32 VAL HG11 H 1 0.835 0.003 . 1 . . . A 15 VAL HG11 . 25086 1 288 . 1 1 32 32 VAL HG12 H 1 0.835 0.003 . 1 . . . A 15 VAL HG12 . 25086 1 289 . 1 1 32 32 VAL HG13 H 1 0.835 0.003 . 1 . . . A 15 VAL HG13 . 25086 1 290 . 1 1 32 32 VAL HG21 H 1 0.835 0.003 . 1 . . . A 15 VAL HG21 . 25086 1 291 . 1 1 32 32 VAL HG22 H 1 0.835 0.003 . 1 . . . A 15 VAL HG22 . 25086 1 292 . 1 1 32 32 VAL HG23 H 1 0.835 0.003 . 1 . . . A 15 VAL HG23 . 25086 1 293 . 1 1 32 32 VAL C C 13 175.375 0.000 . 1 . . . A 15 VAL C . 25086 1 294 . 1 1 32 32 VAL CA C 13 59.832 0.036 . 1 . . . A 15 VAL CA . 25086 1 295 . 1 1 32 32 VAL CB C 13 35.541 0.053 . 1 . . . A 15 VAL CB . 25086 1 296 . 1 1 32 32 VAL CG1 C 13 21.064 0.011 . 1 . . . A 15 VAL CG1 . 25086 1 297 . 1 1 32 32 VAL CG2 C 13 21.064 0.011 . 1 . . . A 15 VAL CG2 . 25086 1 298 . 1 1 32 32 VAL N N 15 116.316 0.024 . 1 . . . A 15 VAL N . 25086 1 299 . 1 1 33 33 ARG H H 1 8.812 0.003 . 1 . . . A 16 ARG H . 25086 1 300 . 1 1 33 33 ARG HA H 1 4.733 0.005 . 1 . . . A 16 ARG HA . 25086 1 301 . 1 1 33 33 ARG HB2 H 1 1.660 0.006 . 1 . . . A 16 ARG HB2 . 25086 1 302 . 1 1 33 33 ARG HB3 H 1 1.660 0.006 . 1 . . . A 16 ARG HB3 . 25086 1 303 . 1 1 33 33 ARG HG2 H 1 1.665 0.005 . 2 . . . A 16 ARG HG2 . 25086 1 304 . 1 1 33 33 ARG HG3 H 1 1.283 0.005 . 2 . . . A 16 ARG HG3 . 25086 1 305 . 1 1 33 33 ARG HD2 H 1 2.833 0.003 . 2 . . . A 16 ARG HD2 . 25086 1 306 . 1 1 33 33 ARG HD3 H 1 2.770 0.002 . 2 . . . A 16 ARG HD3 . 25086 1 307 . 1 1 33 33 ARG C C 13 176.071 0.000 . 1 . . . A 16 ARG C . 25086 1 308 . 1 1 33 33 ARG CA C 13 56.204 0.044 . 1 . . . A 16 ARG CA . 25086 1 309 . 1 1 33 33 ARG CB C 13 30.493 0.043 . 1 . . . A 16 ARG CB . 25086 1 310 . 1 1 33 33 ARG CG C 13 29.430 0.045 . 1 . . . A 16 ARG CG . 25086 1 311 . 1 1 33 33 ARG CD C 13 43.113 0.072 . 1 . . . A 16 ARG CD . 25086 1 312 . 1 1 33 33 ARG N N 15 125.595 0.016 . 1 . . . A 16 ARG N . 25086 1 313 . 1 1 34 34 ILE H H 1 8.020 0.003 . 1 . . . A 17 ILE H . 25086 1 314 . 1 1 34 34 ILE HA H 1 4.395 0.002 . 1 . . . A 17 ILE HA . 25086 1 315 . 1 1 34 34 ILE HB H 1 1.749 0.002 . 1 . . . A 17 ILE HB . 25086 1 316 . 1 1 34 34 ILE HG12 H 1 1.327 0.003 . 2 . . . A 17 ILE HG12 . 25086 1 317 . 1 1 34 34 ILE HG13 H 1 1.071 0.003 . 2 . . . A 17 ILE HG13 . 25086 1 318 . 1 1 34 34 ILE HG21 H 1 0.771 0.004 . 1 . . . A 17 ILE HG21 . 25086 1 319 . 1 1 34 34 ILE HG22 H 1 0.771 0.004 . 1 . . . A 17 ILE HG22 . 25086 1 320 . 1 1 34 34 ILE HG23 H 1 0.771 0.004 . 1 . . . A 17 ILE HG23 . 25086 1 321 . 1 1 34 34 ILE HD11 H 1 0.583 0.006 . 1 . . . A 17 ILE HD11 . 25086 1 322 . 1 1 34 34 ILE HD12 H 1 0.583 0.006 . 1 . . . A 17 ILE HD12 . 25086 1 323 . 1 1 34 34 ILE HD13 H 1 0.583 0.006 . 1 . . . A 17 ILE HD13 . 25086 1 324 . 1 1 34 34 ILE CA C 13 56.591 0.000 . 1 . . . A 17 ILE CA . 25086 1 325 . 1 1 34 34 ILE CB C 13 38.781 0.000 . 1 . . . A 17 ILE CB . 25086 1 326 . 1 1 34 34 ILE CG1 C 13 26.843 0.022 . 1 . . . A 17 ILE CG1 . 25086 1 327 . 1 1 34 34 ILE CG2 C 13 17.202 0.012 . 1 . . . A 17 ILE CG2 . 25086 1 328 . 1 1 34 34 ILE CD1 C 13 10.790 0.004 . 1 . . . A 17 ILE CD1 . 25086 1 329 . 1 1 34 34 ILE N N 15 123.572 0.015 . 1 . . . A 17 ILE N . 25086 1 330 . 1 1 35 35 PRO HA H 1 4.391 0.002 . 1 . . . A 18 PRO HA . 25086 1 331 . 1 1 35 35 PRO HB2 H 1 1.787 0.007 . 2 . . . A 18 PRO HB2 . 25086 1 332 . 1 1 35 35 PRO HB3 H 1 2.561 0.005 . 2 . . . A 18 PRO HB3 . 25086 1 333 . 1 1 35 35 PRO HG2 H 1 1.932 0.005 . 2 . . . A 18 PRO HG2 . 25086 1 334 . 1 1 35 35 PRO HG3 H 1 2.075 0.005 . 2 . . . A 18 PRO HG3 . 25086 1 335 . 1 1 35 35 PRO HD2 H 1 3.373 0.003 . 2 . . . A 18 PRO HD2 . 25086 1 336 . 1 1 35 35 PRO HD3 H 1 4.102 0.004 . 2 . . . A 18 PRO HD3 . 25086 1 337 . 1 1 35 35 PRO C C 13 177.860 0.000 . 1 . . . A 18 PRO C . 25086 1 338 . 1 1 35 35 PRO CA C 13 62.868 0.063 . 1 . . . A 18 PRO CA . 25086 1 339 . 1 1 35 35 PRO CB C 13 32.836 0.030 . 1 . . . A 18 PRO CB . 25086 1 340 . 1 1 35 35 PRO CG C 13 27.894 0.025 . 1 . . . A 18 PRO CG . 25086 1 341 . 1 1 35 35 PRO CD C 13 50.918 0.034 . 1 . . . A 18 PRO CD . 25086 1 342 . 1 1 36 36 ALA H H 1 8.975 0.002 . 1 . . . A 19 ALA H . 25086 1 343 . 1 1 36 36 ALA HA H 1 3.938 0.002 . 1 . . . A 19 ALA HA . 25086 1 344 . 1 1 36 36 ALA HB1 H 1 1.500 0.004 . 1 . . . A 19 ALA HB1 . 25086 1 345 . 1 1 36 36 ALA HB2 H 1 1.500 0.004 . 1 . . . A 19 ALA HB2 . 25086 1 346 . 1 1 36 36 ALA HB3 H 1 1.500 0.004 . 1 . . . A 19 ALA HB3 . 25086 1 347 . 1 1 36 36 ALA C C 13 180.059 0.000 . 1 . . . A 19 ALA C . 25086 1 348 . 1 1 36 36 ALA CA C 13 55.875 0.056 . 1 . . . A 19 ALA CA . 25086 1 349 . 1 1 36 36 ALA CB C 13 18.300 0.042 . 1 . . . A 19 ALA CB . 25086 1 350 . 1 1 36 36 ALA N N 15 128.602 0.021 . 1 . . . A 19 ALA N . 25086 1 351 . 1 1 37 37 THR H H 1 8.263 0.003 . 1 . . . A 20 THR H . 25086 1 352 . 1 1 37 37 THR HA H 1 4.041 0.003 . 1 . . . A 20 THR HA . 25086 1 353 . 1 1 37 37 THR HB H 1 4.123 0.000 . 1 . . . A 20 THR HB . 25086 1 354 . 1 1 37 37 THR HG21 H 1 1.285 0.002 . 1 . . . A 20 THR HG21 . 25086 1 355 . 1 1 37 37 THR HG22 H 1 1.285 0.002 . 1 . . . A 20 THR HG22 . 25086 1 356 . 1 1 37 37 THR HG23 H 1 1.285 0.002 . 1 . . . A 20 THR HG23 . 25086 1 357 . 1 1 37 37 THR C C 13 177.381 0.000 . 1 . . . A 20 THR C . 25086 1 358 . 1 1 37 37 THR CA C 13 64.688 0.066 . 1 . . . A 20 THR CA . 25086 1 359 . 1 1 37 37 THR CB C 13 68.155 0.040 . 1 . . . A 20 THR CB . 25086 1 360 . 1 1 37 37 THR CG2 C 13 22.531 0.028 . 1 . . . A 20 THR CG2 . 25086 1 361 . 1 1 37 37 THR N N 15 108.352 0.015 . 1 . . . A 20 THR N . 25086 1 362 . 1 1 38 38 LEU H H 1 7.040 0.003 . 1 . . . A 21 LEU H . 25086 1 363 . 1 1 38 38 LEU HA H 1 4.226 0.004 . 1 . . . A 21 LEU HA . 25086 1 364 . 1 1 38 38 LEU HB2 H 1 1.296 0.003 . 2 . . . A 21 LEU HB2 . 25086 1 365 . 1 1 38 38 LEU HB3 H 1 1.720 0.002 . 2 . . . A 21 LEU HB3 . 25086 1 366 . 1 1 38 38 LEU HG H 1 1.595 0.002 . 1 . . . A 21 LEU HG . 25086 1 367 . 1 1 38 38 LEU HD11 H 1 0.790 0.008 . 1 . . . A 21 LEU HD11 . 25086 1 368 . 1 1 38 38 LEU HD12 H 1 0.790 0.008 . 1 . . . A 21 LEU HD12 . 25086 1 369 . 1 1 38 38 LEU HD13 H 1 0.790 0.008 . 1 . . . A 21 LEU HD13 . 25086 1 370 . 1 1 38 38 LEU HD21 H 1 0.790 0.008 . 1 . . . A 21 LEU HD21 . 25086 1 371 . 1 1 38 38 LEU HD22 H 1 0.790 0.008 . 1 . . . A 21 LEU HD22 . 25086 1 372 . 1 1 38 38 LEU HD23 H 1 0.790 0.008 . 1 . . . A 21 LEU HD23 . 25086 1 373 . 1 1 38 38 LEU C C 13 178.002 0.000 . 1 . . . A 21 LEU C . 25086 1 374 . 1 1 38 38 LEU CA C 13 56.943 0.038 . 1 . . . A 21 LEU CA . 25086 1 375 . 1 1 38 38 LEU CB C 13 41.032 0.028 . 1 . . . A 21 LEU CB . 25086 1 376 . 1 1 38 38 LEU CG C 13 27.532 0.000 . 1 . . . A 21 LEU CG . 25086 1 377 . 1 1 38 38 LEU CD1 C 13 22.708 0.034 . 2 . . . A 21 LEU CD1 . 25086 1 378 . 1 1 38 38 LEU CD2 C 13 25.834 0.015 . 2 . . . A 21 LEU CD2 . 25086 1 379 . 1 1 38 38 LEU N N 15 121.199 0.021 . 1 . . . A 21 LEU N . 25086 1 380 . 1 1 39 39 MET H H 1 7.415 0.002 . 1 . . . A 22 MET H . 25086 1 381 . 1 1 39 39 MET HA H 1 4.019 0.004 . 1 . . . A 22 MET HA . 25086 1 382 . 1 1 39 39 MET HB2 H 1 2.205 0.003 . 1 . . . A 22 MET HB2 . 25086 1 383 . 1 1 39 39 MET HB3 H 1 2.205 0.003 . 1 . . . A 22 MET HB3 . 25086 1 384 . 1 1 39 39 MET HG2 H 1 2.463 0.004 . 2 . . . A 22 MET HG2 . 25086 1 385 . 1 1 39 39 MET HG3 H 1 2.326 0.005 . 2 . . . A 22 MET HG3 . 25086 1 386 . 1 1 39 39 MET HE1 H 1 1.729 0.002 . 1 . . . A 22 MET HE1 . 25086 1 387 . 1 1 39 39 MET HE2 H 1 1.729 0.002 . 1 . . . A 22 MET HE2 . 25086 1 388 . 1 1 39 39 MET HE3 H 1 1.729 0.002 . 1 . . . A 22 MET HE3 . 25086 1 389 . 1 1 39 39 MET C C 13 178.951 0.000 . 1 . . . A 22 MET C . 25086 1 390 . 1 1 39 39 MET CA C 13 57.881 0.040 . 1 . . . A 22 MET CA . 25086 1 391 . 1 1 39 39 MET CB C 13 30.803 0.032 . 1 . . . A 22 MET CB . 25086 1 392 . 1 1 39 39 MET CG C 13 31.993 0.047 . 1 . . . A 22 MET CG . 25086 1 393 . 1 1 39 39 MET CE C 13 16.505 0.014 . 1 . . . A 22 MET CE . 25086 1 394 . 1 1 39 39 MET N N 15 117.150 0.017 . 1 . . . A 22 MET N . 25086 1 395 . 1 1 40 40 GLN H H 1 7.953 0.002 . 1 . . . A 23 GLN H . 25086 1 396 . 1 1 40 40 GLN HA H 1 4.160 0.002 . 1 . . . A 23 GLN HA . 25086 1 397 . 1 1 40 40 GLN HB2 H 1 2.095 0.005 . 1 . . . A 23 GLN HB2 . 25086 1 398 . 1 1 40 40 GLN HB3 H 1 2.095 0.005 . 1 . . . A 23 GLN HB3 . 25086 1 399 . 1 1 40 40 GLN HG2 H 1 2.389 0.004 . 2 . . . A 23 GLN HG2 . 25086 1 400 . 1 1 40 40 GLN HG3 H 1 2.475 0.005 . 2 . . . A 23 GLN HG3 . 25086 1 401 . 1 1 40 40 GLN HE21 H 1 6.791 0.003 . 1 . . . A 23 GLN HE21 . 25086 1 402 . 1 1 40 40 GLN HE22 H 1 7.435 0.002 . 1 . . . A 23 GLN HE22 . 25086 1 403 . 1 1 40 40 GLN C C 13 179.589 0.000 . 1 . . . A 23 GLN C . 25086 1 404 . 1 1 40 40 GLN CA C 13 58.515 0.018 . 1 . . . A 23 GLN CA . 25086 1 405 . 1 1 40 40 GLN CB C 13 28.288 0.064 . 1 . . . A 23 GLN CB . 25086 1 406 . 1 1 40 40 GLN CG C 13 33.917 0.034 . 1 . . . A 23 GLN CG . 25086 1 407 . 1 1 40 40 GLN N N 15 116.690 0.022 . 1 . . . A 23 GLN N . 25086 1 408 . 1 1 40 40 GLN NE2 N 15 111.372 0.011 . 1 . . . A 23 GLN NE2 . 25086 1 409 . 1 1 41 41 ALA H H 1 7.617 0.002 . 1 . . . A 24 ALA H . 25086 1 410 . 1 1 41 41 ALA HA H 1 4.108 0.002 . 1 . . . A 24 ALA HA . 25086 1 411 . 1 1 41 41 ALA HB1 H 1 1.471 0.002 . 1 . . . A 24 ALA HB1 . 25086 1 412 . 1 1 41 41 ALA HB2 H 1 1.471 0.002 . 1 . . . A 24 ALA HB2 . 25086 1 413 . 1 1 41 41 ALA HB3 H 1 1.471 0.002 . 1 . . . A 24 ALA HB3 . 25086 1 414 . 1 1 41 41 ALA C C 13 179.010 0.000 . 1 . . . A 24 ALA C . 25086 1 415 . 1 1 41 41 ALA CA C 13 54.745 0.041 . 1 . . . A 24 ALA CA . 25086 1 416 . 1 1 41 41 ALA CB C 13 18.719 0.031 . 1 . . . A 24 ALA CB . 25086 1 417 . 1 1 41 41 ALA N N 15 122.104 0.012 . 1 . . . A 24 ALA N . 25086 1 418 . 1 1 42 42 LEU H H 1 7.381 0.002 . 1 . . . A 25 LEU H . 25086 1 419 . 1 1 42 42 LEU HA H 1 4.306 0.006 . 1 . . . A 25 LEU HA . 25086 1 420 . 1 1 42 42 LEU HB2 H 1 1.611 0.002 . 1 . . . A 25 LEU HB2 . 25086 1 421 . 1 1 42 42 LEU HB3 H 1 1.611 0.002 . 1 . . . A 25 LEU HB3 . 25086 1 422 . 1 1 42 42 LEU HG H 1 1.701 0.003 . 1 . . . A 25 LEU HG . 25086 1 423 . 1 1 42 42 LEU HD11 H 1 0.702 0.005 . 1 . . . A 25 LEU HD11 . 25086 1 424 . 1 1 42 42 LEU HD12 H 1 0.702 0.005 . 1 . . . A 25 LEU HD12 . 25086 1 425 . 1 1 42 42 LEU HD13 H 1 0.702 0.005 . 1 . . . A 25 LEU HD13 . 25086 1 426 . 1 1 42 42 LEU HD21 H 1 0.702 0.005 . 1 . . . A 25 LEU HD21 . 25086 1 427 . 1 1 42 42 LEU HD22 H 1 0.702 0.005 . 1 . . . A 25 LEU HD22 . 25086 1 428 . 1 1 42 42 LEU HD23 H 1 0.702 0.005 . 1 . . . A 25 LEU HD23 . 25086 1 429 . 1 1 42 42 LEU C C 13 175.862 0.000 . 1 . . . A 25 LEU C . 25086 1 430 . 1 1 42 42 LEU CA C 13 54.009 0.018 . 1 . . . A 25 LEU CA . 25086 1 431 . 1 1 42 42 LEU CB C 13 43.617 0.040 . 1 . . . A 25 LEU CB . 25086 1 432 . 1 1 42 42 LEU CG C 13 27.007 0.023 . 1 . . . A 25 LEU CG . 25086 1 433 . 1 1 42 42 LEU CD1 C 13 23.961 0.014 . 2 . . . A 25 LEU CD1 . 25086 1 434 . 1 1 42 42 LEU CD2 C 13 25.190 0.022 . 2 . . . A 25 LEU CD2 . 25086 1 435 . 1 1 42 42 LEU N N 15 115.630 0.023 . 1 . . . A 25 LEU N . 25086 1 436 . 1 1 43 43 ASN H H 1 7.966 0.003 . 1 . . . A 26 ASN H . 25086 1 437 . 1 1 43 43 ASN HA H 1 4.289 0.003 . 1 . . . A 26 ASN HA . 25086 1 438 . 1 1 43 43 ASN HB2 H 1 2.655 0.004 . 2 . . . A 26 ASN HB2 . 25086 1 439 . 1 1 43 43 ASN HB3 H 1 3.118 0.003 . 2 . . . A 26 ASN HB3 . 25086 1 440 . 1 1 43 43 ASN HD21 H 1 6.769 0.003 . 1 . . . A 26 ASN HD21 . 25086 1 441 . 1 1 43 43 ASN HD22 H 1 7.517 0.003 . 1 . . . A 26 ASN HD22 . 25086 1 442 . 1 1 43 43 ASN C C 13 173.478 0.000 . 1 . . . A 26 ASN C . 25086 1 443 . 1 1 43 43 ASN CA C 13 54.193 0.065 . 1 . . . A 26 ASN CA . 25086 1 444 . 1 1 43 43 ASN CB C 13 37.358 0.026 . 1 . . . A 26 ASN CB . 25086 1 445 . 1 1 43 43 ASN N N 15 118.019 0.018 . 1 . . . A 26 ASN N . 25086 1 446 . 1 1 43 43 ASN ND2 N 15 111.906 0.298 . 1 . . . A 26 ASN ND2 . 25086 1 447 . 1 1 44 44 LEU H H 1 8.023 0.001 . 1 . . . A 27 LEU H . 25086 1 448 . 1 1 44 44 LEU HA H 1 4.583 0.002 . 1 . . . A 27 LEU HA . 25086 1 449 . 1 1 44 44 LEU HB2 H 1 1.536 0.008 . 2 . . . A 27 LEU HB2 . 25086 1 450 . 1 1 44 44 LEU HB3 H 1 1.473 0.002 . 2 . . . A 27 LEU HB3 . 25086 1 451 . 1 1 44 44 LEU HG H 1 1.543 0.004 . 1 . . . A 27 LEU HG . 25086 1 452 . 1 1 44 44 LEU HD11 H 1 0.843 0.001 . 2 . . . A 27 LEU HD11 . 25086 1 453 . 1 1 44 44 LEU HD12 H 1 0.843 0.001 . 2 . . . A 27 LEU HD12 . 25086 1 454 . 1 1 44 44 LEU HD13 H 1 0.843 0.001 . 2 . . . A 27 LEU HD13 . 25086 1 455 . 1 1 44 44 LEU HD21 H 1 0.786 0.002 . 2 . . . A 27 LEU HD21 . 25086 1 456 . 1 1 44 44 LEU HD22 H 1 0.786 0.002 . 2 . . . A 27 LEU HD22 . 25086 1 457 . 1 1 44 44 LEU HD23 H 1 0.786 0.002 . 2 . . . A 27 LEU HD23 . 25086 1 458 . 1 1 44 44 LEU C C 13 174.995 0.000 . 1 . . . A 27 LEU C . 25086 1 459 . 1 1 44 44 LEU CA C 13 53.740 0.052 . 1 . . . A 27 LEU CA . 25086 1 460 . 1 1 44 44 LEU CB C 13 46.165 0.018 . 1 . . . A 27 LEU CB . 25086 1 461 . 1 1 44 44 LEU CG C 13 26.596 0.007 . 1 . . . A 27 LEU CG . 25086 1 462 . 1 1 44 44 LEU CD1 C 13 25.156 0.061 . 2 . . . A 27 LEU CD1 . 25086 1 463 . 1 1 44 44 LEU CD2 C 13 24.774 0.037 . 2 . . . A 27 LEU CD2 . 25086 1 464 . 1 1 44 44 LEU N N 15 118.539 0.011 . 1 . . . A 27 LEU N . 25086 1 465 . 1 1 45 45 ASN H H 1 8.889 0.002 . 1 . . . A 28 ASN H . 25086 1 466 . 1 1 45 45 ASN HA H 1 4.880 0.004 . 1 . . . A 28 ASN HA . 25086 1 467 . 1 1 45 45 ASN HB2 H 1 2.579 0.004 . 1 . . . A 28 ASN HB2 . 25086 1 468 . 1 1 45 45 ASN HB3 H 1 2.579 0.004 . 1 . . . A 28 ASN HB3 . 25086 1 469 . 1 1 45 45 ASN HD21 H 1 6.862 0.003 . 1 . . . A 28 ASN HD21 . 25086 1 470 . 1 1 45 45 ASN HD22 H 1 8.021 0.004 . 1 . . . A 28 ASN HD22 . 25086 1 471 . 1 1 45 45 ASN C C 13 174.980 0.000 . 1 . . . A 28 ASN C . 25086 1 472 . 1 1 45 45 ASN CA C 13 51.344 0.047 . 1 . . . A 28 ASN CA . 25086 1 473 . 1 1 45 45 ASN CB C 13 42.553 0.036 . 1 . . . A 28 ASN CB . 25086 1 474 . 1 1 45 45 ASN N N 15 121.416 0.008 . 1 . . . A 28 ASN N . 25086 1 475 . 1 1 45 45 ASN ND2 N 15 116.340 0.020 . 1 . . . A 28 ASN ND2 . 25086 1 476 . 1 1 46 46 ILE H H 1 8.396 0.003 . 1 . . . A 29 ILE H . 25086 1 477 . 1 1 46 46 ILE HA H 1 3.327 0.005 . 1 . . . A 29 ILE HA . 25086 1 478 . 1 1 46 46 ILE HB H 1 1.731 0.006 . 1 . . . A 29 ILE HB . 25086 1 479 . 1 1 46 46 ILE HG12 H 1 1.234 0.005 . 2 . . . A 29 ILE HG12 . 25086 1 480 . 1 1 46 46 ILE HG13 H 1 1.496 0.003 . 2 . . . A 29 ILE HG13 . 25086 1 481 . 1 1 46 46 ILE HG21 H 1 0.924 0.004 . 1 . . . A 29 ILE HG21 . 25086 1 482 . 1 1 46 46 ILE HG22 H 1 0.924 0.004 . 1 . . . A 29 ILE HG22 . 25086 1 483 . 1 1 46 46 ILE HG23 H 1 0.924 0.004 . 1 . . . A 29 ILE HG23 . 25086 1 484 . 1 1 46 46 ILE HD11 H 1 0.655 0.004 . 1 . . . A 29 ILE HD11 . 25086 1 485 . 1 1 46 46 ILE HD12 H 1 0.655 0.004 . 1 . . . A 29 ILE HD12 . 25086 1 486 . 1 1 46 46 ILE HD13 H 1 0.655 0.004 . 1 . . . A 29 ILE HD13 . 25086 1 487 . 1 1 46 46 ILE C C 13 176.499 0.000 . 1 . . . A 29 ILE C . 25086 1 488 . 1 1 46 46 ILE CA C 13 63.244 0.032 . 1 . . . A 29 ILE CA . 25086 1 489 . 1 1 46 46 ILE CB C 13 36.266 0.038 . 1 . . . A 29 ILE CB . 25086 1 490 . 1 1 46 46 ILE CG1 C 13 28.639 0.041 . 1 . . . A 29 ILE CG1 . 25086 1 491 . 1 1 46 46 ILE CG2 C 13 18.529 0.062 . 1 . . . A 29 ILE CG2 . 25086 1 492 . 1 1 46 46 ILE CD1 C 13 10.963 0.019 . 1 . . . A 29 ILE CD1 . 25086 1 493 . 1 1 46 46 ILE N N 15 120.022 0.009 . 1 . . . A 29 ILE N . 25086 1 494 . 1 1 47 47 ASP H H 1 9.114 0.003 . 1 . . . A 30 ASP H . 25086 1 495 . 1 1 47 47 ASP HA H 1 4.401 0.002 . 1 . . . A 30 ASP HA . 25086 1 496 . 1 1 47 47 ASP HB2 H 1 3.343 0.009 . 2 . . . A 30 ASP HB2 . 25086 1 497 . 1 1 47 47 ASP HB3 H 1 2.916 0.004 . 2 . . . A 30 ASP HB3 . 25086 1 498 . 1 1 47 47 ASP C C 13 175.994 0.000 . 1 . . . A 30 ASP C . 25086 1 499 . 1 1 47 47 ASP CA C 13 57.943 0.070 . 1 . . . A 30 ASP CA . 25086 1 500 . 1 1 47 47 ASP CB C 13 38.815 0.042 . 1 . . . A 30 ASP CB . 25086 1 501 . 1 1 47 47 ASP N N 15 121.326 0.017 . 1 . . . A 30 ASP N . 25086 1 502 . 1 1 48 48 ASP H H 1 8.056 0.002 . 1 . . . A 31 ASP H . 25086 1 503 . 1 1 48 48 ASP HA H 1 4.693 0.004 . 1 . . . A 31 ASP HA . 25086 1 504 . 1 1 48 48 ASP HB2 H 1 2.709 0.003 . 2 . . . A 31 ASP HB2 . 25086 1 505 . 1 1 48 48 ASP HB3 H 1 3.007 0.007 . 2 . . . A 31 ASP HB3 . 25086 1 506 . 1 1 48 48 ASP C C 13 175.904 0.000 . 1 . . . A 31 ASP C . 25086 1 507 . 1 1 48 48 ASP CA C 13 55.292 0.074 . 1 . . . A 31 ASP CA . 25086 1 508 . 1 1 48 48 ASP CB C 13 41.176 0.033 . 1 . . . A 31 ASP CB . 25086 1 509 . 1 1 48 48 ASP N N 15 121.764 0.017 . 1 . . . A 31 ASP N . 25086 1 510 . 1 1 49 49 GLU H H 1 8.683 0.003 . 1 . . . A 32 GLU H . 25086 1 511 . 1 1 49 49 GLU HA H 1 4.696 0.003 . 1 . . . A 32 GLU HA . 25086 1 512 . 1 1 49 49 GLU HB2 H 1 2.047 0.004 . 1 . . . A 32 GLU HB2 . 25086 1 513 . 1 1 49 49 GLU HB3 H 1 2.047 0.004 . 1 . . . A 32 GLU HB3 . 25086 1 514 . 1 1 49 49 GLU HG2 H 1 2.607 0.002 . 2 . . . A 32 GLU HG2 . 25086 1 515 . 1 1 49 49 GLU HG3 H 1 2.239 0.004 . 2 . . . A 32 GLU HG3 . 25086 1 516 . 1 1 49 49 GLU C C 13 176.717 0.000 . 1 . . . A 32 GLU C . 25086 1 517 . 1 1 49 49 GLU CA C 13 56.409 0.057 . 1 . . . A 32 GLU CA . 25086 1 518 . 1 1 49 49 GLU CB C 13 31.304 0.033 . 1 . . . A 32 GLU CB . 25086 1 519 . 1 1 49 49 GLU CG C 13 37.069 0.040 . 1 . . . A 32 GLU CG . 25086 1 520 . 1 1 49 49 GLU N N 15 120.895 0.020 . 1 . . . A 32 GLU N . 25086 1 521 . 1 1 50 50 VAL H H 1 8.423 0.002 . 1 . . . A 33 VAL H . 25086 1 522 . 1 1 50 50 VAL HA H 1 5.006 0.006 . 1 . . . A 33 VAL HA . 25086 1 523 . 1 1 50 50 VAL HB H 1 1.859 0.002 . 1 . . . A 33 VAL HB . 25086 1 524 . 1 1 50 50 VAL HG11 H 1 0.425 0.003 . 2 . . . A 33 VAL HG11 . 25086 1 525 . 1 1 50 50 VAL HG12 H 1 0.425 0.003 . 2 . . . A 33 VAL HG12 . 25086 1 526 . 1 1 50 50 VAL HG13 H 1 0.425 0.003 . 2 . . . A 33 VAL HG13 . 25086 1 527 . 1 1 50 50 VAL HG21 H 1 0.615 0.002 . 2 . . . A 33 VAL HG21 . 25086 1 528 . 1 1 50 50 VAL HG22 H 1 0.615 0.002 . 2 . . . A 33 VAL HG22 . 25086 1 529 . 1 1 50 50 VAL HG23 H 1 0.615 0.002 . 2 . . . A 33 VAL HG23 . 25086 1 530 . 1 1 50 50 VAL C C 13 173.447 0.000 . 1 . . . A 33 VAL C . 25086 1 531 . 1 1 50 50 VAL CA C 13 58.428 0.020 . 1 . . . A 33 VAL CA . 25086 1 532 . 1 1 50 50 VAL CB C 13 35.764 0.023 . 1 . . . A 33 VAL CB . 25086 1 533 . 1 1 50 50 VAL CG1 C 13 17.688 0.023 . 2 . . . A 33 VAL CG1 . 25086 1 534 . 1 1 50 50 VAL CG2 C 13 22.154 0.029 . 2 . . . A 33 VAL CG2 . 25086 1 535 . 1 1 50 50 VAL N N 15 114.605 0.021 . 1 . . . A 33 VAL N . 25086 1 536 . 1 1 51 51 LYS H H 1 8.989 0.003 . 1 . . . A 34 LYS H . 25086 1 537 . 1 1 51 51 LYS HA H 1 4.767 0.003 . 1 . . . A 34 LYS HA . 25086 1 538 . 1 1 51 51 LYS HB2 H 1 1.331 0.004 . 2 . . . A 34 LYS HB2 . 25086 1 539 . 1 1 51 51 LYS HB3 H 1 1.565 0.006 . 2 . . . A 34 LYS HB3 . 25086 1 540 . 1 1 51 51 LYS HG2 H 1 1.086 0.002 . 1 . . . A 34 LYS HG2 . 25086 1 541 . 1 1 51 51 LYS HG3 H 1 1.086 0.002 . 1 . . . A 34 LYS HG3 . 25086 1 542 . 1 1 51 51 LYS HD2 H 1 1.497 0.000 . 1 . . . A 34 LYS HD2 . 25086 1 543 . 1 1 51 51 LYS HD3 H 1 1.497 0.000 . 1 . . . A 34 LYS HD3 . 25086 1 544 . 1 1 51 51 LYS HE2 H 1 2.822 0.003 . 1 . . . A 34 LYS HE2 . 25086 1 545 . 1 1 51 51 LYS HE3 H 1 2.822 0.003 . 1 . . . A 34 LYS HE3 . 25086 1 546 . 1 1 51 51 LYS C C 13 175.062 0.000 . 1 . . . A 34 LYS C . 25086 1 547 . 1 1 51 51 LYS CA C 13 54.652 0.031 . 1 . . . A 34 LYS CA . 25086 1 548 . 1 1 51 51 LYS CB C 13 34.857 0.038 . 1 . . . A 34 LYS CB . 25086 1 549 . 1 1 51 51 LYS CG C 13 24.662 0.017 . 1 . . . A 34 LYS CG . 25086 1 550 . 1 1 51 51 LYS CD C 13 29.435 0.000 . 1 . . . A 34 LYS CD . 25086 1 551 . 1 1 51 51 LYS CE C 13 41.658 0.042 . 1 . . . A 34 LYS CE . 25086 1 552 . 1 1 51 51 LYS N N 15 122.276 0.013 . 1 . . . A 34 LYS N . 25086 1 553 . 1 1 52 52 ILE H H 1 8.717 0.003 . 1 . . . A 35 ILE H . 25086 1 554 . 1 1 52 52 ILE HA H 1 5.054 0.005 . 1 . . . A 35 ILE HA . 25086 1 555 . 1 1 52 52 ILE HB H 1 1.577 0.006 . 1 . . . A 35 ILE HB . 25086 1 556 . 1 1 52 52 ILE HG12 H 1 1.485 0.004 . 1 . . . A 35 ILE HG12 . 25086 1 557 . 1 1 52 52 ILE HG13 H 1 1.485 0.004 . 1 . . . A 35 ILE HG13 . 25086 1 558 . 1 1 52 52 ILE HG21 H 1 0.718 0.006 . 1 . . . A 35 ILE HG21 . 25086 1 559 . 1 1 52 52 ILE HG22 H 1 0.718 0.006 . 1 . . . A 35 ILE HG22 . 25086 1 560 . 1 1 52 52 ILE HG23 H 1 0.718 0.006 . 1 . . . A 35 ILE HG23 . 25086 1 561 . 1 1 52 52 ILE HD11 H 1 0.750 0.005 . 1 . . . A 35 ILE HD11 . 25086 1 562 . 1 1 52 52 ILE HD12 H 1 0.750 0.005 . 1 . . . A 35 ILE HD12 . 25086 1 563 . 1 1 52 52 ILE HD13 H 1 0.750 0.005 . 1 . . . A 35 ILE HD13 . 25086 1 564 . 1 1 52 52 ILE C C 13 174.111 0.000 . 1 . . . A 35 ILE C . 25086 1 565 . 1 1 52 52 ILE CA C 13 60.238 0.045 . 1 . . . A 35 ILE CA . 25086 1 566 . 1 1 52 52 ILE CB C 13 39.989 0.035 . 1 . . . A 35 ILE CB . 25086 1 567 . 1 1 52 52 ILE CG1 C 13 27.267 0.000 . 1 . . . A 35 ILE CG1 . 25086 1 568 . 1 1 52 52 ILE CG2 C 13 17.902 0.016 . 1 . . . A 35 ILE CG2 . 25086 1 569 . 1 1 52 52 ILE CD1 C 13 14.207 0.028 . 1 . . . A 35 ILE CD1 . 25086 1 570 . 1 1 52 52 ILE N N 15 124.021 0.010 . 1 . . . A 35 ILE N . 25086 1 571 . 1 1 53 53 ASP H H 1 8.948 0.005 . 1 . . . A 36 ASP H . 25086 1 572 . 1 1 53 53 ASP HA H 1 5.054 0.003 . 1 . . . A 36 ASP HA . 25086 1 573 . 1 1 53 53 ASP HB2 H 1 2.419 0.003 . 1 . . . A 36 ASP HB2 . 25086 1 574 . 1 1 53 53 ASP HB3 H 1 2.419 0.003 . 1 . . . A 36 ASP HB3 . 25086 1 575 . 1 1 53 53 ASP C C 13 173.496 0.000 . 1 . . . A 36 ASP C . 25086 1 576 . 1 1 53 53 ASP CA C 13 52.243 0.037 . 1 . . . A 36 ASP CA . 25086 1 577 . 1 1 53 53 ASP CB C 13 45.280 0.024 . 1 . . . A 36 ASP CB . 25086 1 578 . 1 1 53 53 ASP N N 15 126.126 0.014 . 1 . . . A 36 ASP N . 25086 1 579 . 1 1 54 54 LEU H H 1 8.629 0.002 . 1 . . . A 37 LEU H . 25086 1 580 . 1 1 54 54 LEU HA H 1 5.201 0.006 . 1 . . . A 37 LEU HA . 25086 1 581 . 1 1 54 54 LEU HB2 H 1 1.257 0.004 . 2 . . . A 37 LEU HB2 . 25086 1 582 . 1 1 54 54 LEU HB3 H 1 1.762 0.003 . 2 . . . A 37 LEU HB3 . 25086 1 583 . 1 1 54 54 LEU HG H 1 1.449 0.003 . 1 . . . A 37 LEU HG . 25086 1 584 . 1 1 54 54 LEU HD11 H 1 0.801 0.002 . 2 . . . A 37 LEU HD11 . 25086 1 585 . 1 1 54 54 LEU HD12 H 1 0.801 0.002 . 2 . . . A 37 LEU HD12 . 25086 1 586 . 1 1 54 54 LEU HD13 H 1 0.801 0.002 . 2 . . . A 37 LEU HD13 . 25086 1 587 . 1 1 54 54 LEU HD21 H 1 0.757 0.005 . 2 . . . A 37 LEU HD21 . 25086 1 588 . 1 1 54 54 LEU HD22 H 1 0.757 0.005 . 2 . . . A 37 LEU HD22 . 25086 1 589 . 1 1 54 54 LEU HD23 H 1 0.757 0.005 . 2 . . . A 37 LEU HD23 . 25086 1 590 . 1 1 54 54 LEU C C 13 175.865 0.000 . 1 . . . A 37 LEU C . 25086 1 591 . 1 1 54 54 LEU CA C 13 54.061 0.025 . 1 . . . A 37 LEU CA . 25086 1 592 . 1 1 54 54 LEU CB C 13 44.306 0.040 . 1 . . . A 37 LEU CB . 25086 1 593 . 1 1 54 54 LEU CG C 13 27.900 0.000 . 1 . . . A 37 LEU CG . 25086 1 594 . 1 1 54 54 LEU CD1 C 13 25.624 0.097 . 1 . . . A 37 LEU CD1 . 25086 1 595 . 1 1 54 54 LEU CD2 C 13 25.624 0.097 . 1 . . . A 37 LEU CD2 . 25086 1 596 . 1 1 54 54 LEU N N 15 123.664 0.013 . 1 . . . A 37 LEU N . 25086 1 597 . 1 1 55 55 VAL H H 1 8.772 0.003 . 1 . . . A 38 VAL H . 25086 1 598 . 1 1 55 55 VAL HA H 1 4.189 0.008 . 1 . . . A 38 VAL HA . 25086 1 599 . 1 1 55 55 VAL HB H 1 1.820 0.005 . 1 . . . A 38 VAL HB . 25086 1 600 . 1 1 55 55 VAL HG11 H 1 0.803 0.004 . 1 . . . A 38 VAL HG11 . 25086 1 601 . 1 1 55 55 VAL HG12 H 1 0.803 0.004 . 1 . . . A 38 VAL HG12 . 25086 1 602 . 1 1 55 55 VAL HG13 H 1 0.803 0.004 . 1 . . . A 38 VAL HG13 . 25086 1 603 . 1 1 55 55 VAL HG21 H 1 0.803 0.004 . 1 . . . A 38 VAL HG21 . 25086 1 604 . 1 1 55 55 VAL HG22 H 1 0.803 0.004 . 1 . . . A 38 VAL HG22 . 25086 1 605 . 1 1 55 55 VAL HG23 H 1 0.803 0.004 . 1 . . . A 38 VAL HG23 . 25086 1 606 . 1 1 55 55 VAL C C 13 175.379 0.000 . 1 . . . A 38 VAL C . 25086 1 607 . 1 1 55 55 VAL CA C 13 61.480 0.021 . 1 . . . A 38 VAL CA . 25086 1 608 . 1 1 55 55 VAL CB C 13 35.102 0.036 . 1 . . . A 38 VAL CB . 25086 1 609 . 1 1 55 55 VAL CG1 C 13 20.798 0.000 . 2 . . . A 38 VAL CG1 . 25086 1 610 . 1 1 55 55 VAL CG2 C 13 21.082 0.000 . 2 . . . A 38 VAL CG2 . 25086 1 611 . 1 1 55 55 VAL N N 15 126.795 0.015 . 1 . . . A 38 VAL N . 25086 1 612 . 1 1 56 56 ASP H H 1 9.154 0.002 . 1 . . . A 39 ASP H . 25086 1 613 . 1 1 56 56 ASP HA H 1 4.221 0.011 . 1 . . . A 39 ASP HA . 25086 1 614 . 1 1 56 56 ASP HB2 H 1 2.488 0.003 . 2 . . . A 39 ASP HB2 . 25086 1 615 . 1 1 56 56 ASP HB3 H 1 2.891 0.003 . 2 . . . A 39 ASP HB3 . 25086 1 616 . 1 1 56 56 ASP C C 13 175.944 0.000 . 1 . . . A 39 ASP C . 25086 1 617 . 1 1 56 56 ASP CA C 13 55.224 0.063 . 1 . . . A 39 ASP CA . 25086 1 618 . 1 1 56 56 ASP CB C 13 40.006 0.020 . 1 . . . A 39 ASP CB . 25086 1 619 . 1 1 56 56 ASP N N 15 127.355 0.016 . 1 . . . A 39 ASP N . 25086 1 620 . 1 1 57 57 GLY H H 1 8.425 0.002 . 1 . . . A 40 GLY H . 25086 1 621 . 1 1 57 57 GLY HA2 H 1 3.480 0.002 . 2 . . . A 40 GLY HA2 . 25086 1 622 . 1 1 57 57 GLY HA3 H 1 3.992 0.003 . 2 . . . A 40 GLY HA3 . 25086 1 623 . 1 1 57 57 GLY C C 13 172.842 0.000 . 1 . . . A 40 GLY C . 25086 1 624 . 1 1 57 57 GLY CA C 13 46.062 0.042 . 1 . . . A 40 GLY CA . 25086 1 625 . 1 1 57 57 GLY N N 15 103.124 0.020 . 1 . . . A 40 GLY N . 25086 1 626 . 1 1 58 58 LYS H H 1 7.676 0.001 . 1 . . . A 41 LYS H . 25086 1 627 . 1 1 58 58 LYS HA H 1 4.745 0.001 . 1 . . . A 41 LYS HA . 25086 1 628 . 1 1 58 58 LYS HB2 H 1 1.646 0.005 . 2 . . . A 41 LYS HB2 . 25086 1 629 . 1 1 58 58 LYS HB3 H 1 1.740 0.003 . 2 . . . A 41 LYS HB3 . 25086 1 630 . 1 1 58 58 LYS HG2 H 1 1.336 0.000 . 1 . . . A 41 LYS HG2 . 25086 1 631 . 1 1 58 58 LYS HG3 H 1 1.336 0.000 . 1 . . . A 41 LYS HG3 . 25086 1 632 . 1 1 58 58 LYS HD2 H 1 1.547 0.000 . 1 . . . A 41 LYS HD2 . 25086 1 633 . 1 1 58 58 LYS HD3 H 1 1.547 0.000 . 1 . . . A 41 LYS HD3 . 25086 1 634 . 1 1 58 58 LYS HE2 H 1 2.928 0.013 . 2 . . . A 41 LYS HE2 . 25086 1 635 . 1 1 58 58 LYS HE3 H 1 2.911 0.005 . 2 . . . A 41 LYS HE3 . 25086 1 636 . 1 1 58 58 LYS C C 13 174.385 0.000 . 1 . . . A 41 LYS C . 25086 1 637 . 1 1 58 58 LYS CA C 13 54.490 0.059 . 1 . . . A 41 LYS CA . 25086 1 638 . 1 1 58 58 LYS CB C 13 35.244 0.031 . 1 . . . A 41 LYS CB . 25086 1 639 . 1 1 58 58 LYS CG C 13 24.591 0.000 . 1 . . . A 41 LYS CG . 25086 1 640 . 1 1 58 58 LYS CD C 13 29.425 0.000 . 1 . . . A 41 LYS CD . 25086 1 641 . 1 1 58 58 LYS CE C 13 42.168 0.000 . 1 . . . A 41 LYS CE . 25086 1 642 . 1 1 58 58 LYS N N 15 117.155 0.017 . 1 . . . A 41 LYS N . 25086 1 643 . 1 1 59 59 LEU H H 1 8.585 0.003 . 1 . . . A 42 LEU H . 25086 1 644 . 1 1 59 59 LEU HA H 1 5.066 0.005 . 1 . . . A 42 LEU HA . 25086 1 645 . 1 1 59 59 LEU HB2 H 1 1.309 0.003 . 2 . . . A 42 LEU HB2 . 25086 1 646 . 1 1 59 59 LEU HB3 H 1 1.662 0.006 . 2 . . . A 42 LEU HB3 . 25086 1 647 . 1 1 59 59 LEU HG H 1 1.539 0.000 . 1 . . . A 42 LEU HG . 25086 1 648 . 1 1 59 59 LEU HD11 H 1 0.692 0.008 . 2 . . . A 42 LEU HD11 . 25086 1 649 . 1 1 59 59 LEU HD12 H 1 0.692 0.008 . 2 . . . A 42 LEU HD12 . 25086 1 650 . 1 1 59 59 LEU HD13 H 1 0.692 0.008 . 2 . . . A 42 LEU HD13 . 25086 1 651 . 1 1 59 59 LEU HD21 H 1 0.670 0.013 . 2 . . . A 42 LEU HD21 . 25086 1 652 . 1 1 59 59 LEU HD22 H 1 0.670 0.013 . 2 . . . A 42 LEU HD22 . 25086 1 653 . 1 1 59 59 LEU HD23 H 1 0.670 0.013 . 2 . . . A 42 LEU HD23 . 25086 1 654 . 1 1 59 59 LEU C C 13 174.895 0.000 . 1 . . . A 42 LEU C . 25086 1 655 . 1 1 59 59 LEU CA C 13 53.560 0.026 . 1 . . . A 42 LEU CA . 25086 1 656 . 1 1 59 59 LEU CB C 13 43.448 0.027 . 1 . . . A 42 LEU CB . 25086 1 657 . 1 1 59 59 LEU CG C 13 26.640 0.020 . 1 . . . A 42 LEU CG . 25086 1 658 . 1 1 59 59 LEU CD1 C 13 25.161 0.016 . 2 . . . A 42 LEU CD1 . 25086 1 659 . 1 1 59 59 LEU CD2 C 13 25.568 0.027 . 2 . . . A 42 LEU CD2 . 25086 1 660 . 1 1 59 59 LEU N N 15 119.938 0.013 . 1 . . . A 42 LEU N . 25086 1 661 . 1 1 60 60 ILE H H 1 9.075 0.002 . 1 . . . A 43 ILE H . 25086 1 662 . 1 1 60 60 ILE HA H 1 4.925 0.004 . 1 . . . A 43 ILE HA . 25086 1 663 . 1 1 60 60 ILE HB H 1 1.804 0.002 . 1 . . . A 43 ILE HB . 25086 1 664 . 1 1 60 60 ILE HG12 H 1 1.388 0.002 . 2 . . . A 43 ILE HG12 . 25086 1 665 . 1 1 60 60 ILE HG13 H 1 1.230 0.001 . 2 . . . A 43 ILE HG13 . 25086 1 666 . 1 1 60 60 ILE HG21 H 1 0.812 0.002 . 1 . . . A 43 ILE HG21 . 25086 1 667 . 1 1 60 60 ILE HG22 H 1 0.812 0.002 . 1 . . . A 43 ILE HG22 . 25086 1 668 . 1 1 60 60 ILE HG23 H 1 0.812 0.002 . 1 . . . A 43 ILE HG23 . 25086 1 669 . 1 1 60 60 ILE HD11 H 1 0.748 0.003 . 1 . . . A 43 ILE HD11 . 25086 1 670 . 1 1 60 60 ILE HD12 H 1 0.748 0.003 . 1 . . . A 43 ILE HD12 . 25086 1 671 . 1 1 60 60 ILE HD13 H 1 0.748 0.003 . 1 . . . A 43 ILE HD13 . 25086 1 672 . 1 1 60 60 ILE C C 13 175.893 0.000 . 1 . . . A 43 ILE C . 25086 1 673 . 1 1 60 60 ILE CA C 13 59.287 0.039 . 1 . . . A 43 ILE CA . 25086 1 674 . 1 1 60 60 ILE CB C 13 39.178 0.044 . 1 . . . A 43 ILE CB . 25086 1 675 . 1 1 60 60 ILE CG1 C 13 27.603 0.027 . 1 . . . A 43 ILE CG1 . 25086 1 676 . 1 1 60 60 ILE CG2 C 13 18.688 0.063 . 1 . . . A 43 ILE CG2 . 25086 1 677 . 1 1 60 60 ILE CD1 C 13 12.786 0.031 . 1 . . . A 43 ILE CD1 . 25086 1 678 . 1 1 60 60 ILE N N 15 123.764 0.014 . 1 . . . A 43 ILE N . 25086 1 679 . 1 1 61 61 ILE H H 1 9.411 0.003 . 1 . . . A 44 ILE H . 25086 1 680 . 1 1 61 61 ILE HA H 1 4.956 0.002 . 1 . . . A 44 ILE HA . 25086 1 681 . 1 1 61 61 ILE HB H 1 1.869 0.005 . 1 . . . A 44 ILE HB . 25086 1 682 . 1 1 61 61 ILE HG12 H 1 1.477 0.002 . 2 . . . A 44 ILE HG12 . 25086 1 683 . 1 1 61 61 ILE HG13 H 1 0.942 0.003 . 2 . . . A 44 ILE HG13 . 25086 1 684 . 1 1 61 61 ILE HG21 H 1 0.613 0.006 . 1 . . . A 44 ILE HG21 . 25086 1 685 . 1 1 61 61 ILE HG22 H 1 0.613 0.006 . 1 . . . A 44 ILE HG22 . 25086 1 686 . 1 1 61 61 ILE HG23 H 1 0.613 0.006 . 1 . . . A 44 ILE HG23 . 25086 1 687 . 1 1 61 61 ILE HD11 H 1 0.641 0.006 . 1 . . . A 44 ILE HD11 . 25086 1 688 . 1 1 61 61 ILE HD12 H 1 0.641 0.006 . 1 . . . A 44 ILE HD12 . 25086 1 689 . 1 1 61 61 ILE HD13 H 1 0.641 0.006 . 1 . . . A 44 ILE HD13 . 25086 1 690 . 1 1 61 61 ILE C C 13 174.230 0.000 . 1 . . . A 44 ILE C . 25086 1 691 . 1 1 61 61 ILE CA C 13 60.218 0.044 . 1 . . . A 44 ILE CA . 25086 1 692 . 1 1 61 61 ILE CB C 13 39.161 0.026 . 1 . . . A 44 ILE CB . 25086 1 693 . 1 1 61 61 ILE CG1 C 13 27.809 0.059 . 1 . . . A 44 ILE CG1 . 25086 1 694 . 1 1 61 61 ILE CG2 C 13 16.692 0.034 . 1 . . . A 44 ILE CG2 . 25086 1 695 . 1 1 61 61 ILE CD1 C 13 13.691 0.037 . 1 . . . A 44 ILE CD1 . 25086 1 696 . 1 1 61 61 ILE N N 15 126.815 0.009 . 1 . . . A 44 ILE N . 25086 1 697 . 1 1 62 62 GLU H H 1 8.929 0.002 . 1 . . . A 45 GLU H . 25086 1 698 . 1 1 62 62 GLU HA H 1 5.174 0.003 . 1 . . . A 45 GLU HA . 25086 1 699 . 1 1 62 62 GLU HB2 H 1 1.860 0.001 . 2 . . . A 45 GLU HB2 . 25086 1 700 . 1 1 62 62 GLU HB3 H 1 2.023 0.003 . 2 . . . A 45 GLU HB3 . 25086 1 701 . 1 1 62 62 GLU HG2 H 1 2.187 0.004 . 2 . . . A 45 GLU HG2 . 25086 1 702 . 1 1 62 62 GLU HG3 H 1 2.327 0.004 . 2 . . . A 45 GLU HG3 . 25086 1 703 . 1 1 62 62 GLU CA C 13 51.951 0.012 . 1 . . . A 45 GLU CA . 25086 1 704 . 1 1 62 62 GLU CB C 13 33.866 0.029 . 1 . . . A 45 GLU CB . 25086 1 705 . 1 1 62 62 GLU CG C 13 35.906 0.038 . 1 . . . A 45 GLU CG . 25086 1 706 . 1 1 62 62 GLU N N 15 126.742 0.021 . 1 . . . A 45 GLU N . 25086 1 707 . 1 1 63 63 PRO HA H 1 4.552 0.004 . 1 . . . A 46 PRO HA . 25086 1 708 . 1 1 63 63 PRO HB2 H 1 1.925 0.003 . 2 . . . A 46 PRO HB2 . 25086 1 709 . 1 1 63 63 PRO HB3 H 1 2.392 0.003 . 2 . . . A 46 PRO HB3 . 25086 1 710 . 1 1 63 63 PRO HG2 H 1 2.321 0.003 . 2 . . . A 46 PRO HG2 . 25086 1 711 . 1 1 63 63 PRO HG3 H 1 1.817 0.012 . 2 . . . A 46 PRO HG3 . 25086 1 712 . 1 1 63 63 PRO HD2 H 1 3.933 0.006 . 2 . . . A 46 PRO HD2 . 25086 1 713 . 1 1 63 63 PRO HD3 H 1 3.921 0.013 . 2 . . . A 46 PRO HD3 . 25086 1 714 . 1 1 63 63 PRO C C 13 175.856 0.000 . 1 . . . A 46 PRO C . 25086 1 715 . 1 1 63 63 PRO CA C 13 63.215 0.051 . 1 . . . A 46 PRO CA . 25086 1 716 . 1 1 63 63 PRO CB C 13 32.438 0.051 . 1 . . . A 46 PRO CB . 25086 1 717 . 1 1 63 63 PRO CG C 13 28.590 0.092 . 1 . . . A 46 PRO CG . 25086 1 718 . 1 1 63 63 PRO CD C 13 51.382 0.010 . 1 . . . A 46 PRO CD . 25086 1 719 . 1 1 64 64 VAL H H 1 7.893 0.002 . 1 . . . A 47 VAL H . 25086 1 720 . 1 1 64 64 VAL HA H 1 4.017 0.002 . 1 . . . A 47 VAL HA . 25086 1 721 . 1 1 64 64 VAL HB H 1 1.770 0.003 . 1 . . . A 47 VAL HB . 25086 1 722 . 1 1 64 64 VAL HG11 H 1 0.857 0.003 . 2 . . . A 47 VAL HG11 . 25086 1 723 . 1 1 64 64 VAL HG12 H 1 0.857 0.003 . 2 . . . A 47 VAL HG12 . 25086 1 724 . 1 1 64 64 VAL HG13 H 1 0.857 0.003 . 2 . . . A 47 VAL HG13 . 25086 1 725 . 1 1 64 64 VAL HG21 H 1 0.739 0.003 . 2 . . . A 47 VAL HG21 . 25086 1 726 . 1 1 64 64 VAL HG22 H 1 0.739 0.003 . 2 . . . A 47 VAL HG22 . 25086 1 727 . 1 1 64 64 VAL HG23 H 1 0.739 0.003 . 2 . . . A 47 VAL HG23 . 25086 1 728 . 1 1 64 64 VAL C C 13 175.776 0.000 . 1 . . . A 47 VAL C . 25086 1 729 . 1 1 64 64 VAL CA C 13 62.656 0.024 . 1 . . . A 47 VAL CA . 25086 1 730 . 1 1 64 64 VAL CB C 13 32.271 0.060 . 1 . . . A 47 VAL CB . 25086 1 731 . 1 1 64 64 VAL CG1 C 13 21.032 0.018 . 2 . . . A 47 VAL CG1 . 25086 1 732 . 1 1 64 64 VAL CG2 C 13 21.494 0.030 . 2 . . . A 47 VAL CG2 . 25086 1 733 . 1 1 64 64 VAL N N 15 123.846 0.006 . 1 . . . A 47 VAL N . 25086 1 734 . 1 1 65 65 ARG H H 1 8.646 0.002 . 1 . . . A 48 ARG H . 25086 1 735 . 1 1 65 65 ARG HA H 1 4.406 0.004 . 1 . . . A 48 ARG HA . 25086 1 736 . 1 1 65 65 ARG HB2 H 1 1.786 0.006 . 2 . . . A 48 ARG HB2 . 25086 1 737 . 1 1 65 65 ARG HB3 H 1 1.853 0.004 . 2 . . . A 48 ARG HB3 . 25086 1 738 . 1 1 65 65 ARG HG2 H 1 1.653 0.003 . 2 . . . A 48 ARG HG2 . 25086 1 739 . 1 1 65 65 ARG HG3 H 1 1.592 0.002 . 2 . . . A 48 ARG HG3 . 25086 1 740 . 1 1 65 65 ARG HD2 H 1 3.166 0.003 . 1 . . . A 48 ARG HD2 . 25086 1 741 . 1 1 65 65 ARG HD3 H 1 3.166 0.003 . 1 . . . A 48 ARG HD3 . 25086 1 742 . 1 1 65 65 ARG HE H 1 7.284 0.003 . 1 . . . A 48 ARG HE . 25086 1 743 . 1 1 65 65 ARG C C 13 175.887 0.000 . 1 . . . A 48 ARG C . 25086 1 744 . 1 1 65 65 ARG CA C 13 55.520 0.031 . 1 . . . A 48 ARG CA . 25086 1 745 . 1 1 65 65 ARG CB C 13 30.801 0.021 . 1 . . . A 48 ARG CB . 25086 1 746 . 1 1 65 65 ARG CG C 13 27.067 0.017 . 1 . . . A 48 ARG CG . 25086 1 747 . 1 1 65 65 ARG CD C 13 43.253 0.020 . 1 . . . A 48 ARG CD . 25086 1 748 . 1 1 65 65 ARG N N 15 126.674 0.008 . 1 . . . A 48 ARG N . 25086 1 749 . 1 1 65 65 ARG NE N 15 85.040 0.003 . 1 . . . A 48 ARG NE . 25086 1 750 . 1 1 66 66 LYS H H 1 8.563 0.002 . 1 . . . A 49 LYS H . 25086 1 751 . 1 1 66 66 LYS HA H 1 4.359 0.002 . 1 . . . A 49 LYS HA . 25086 1 752 . 1 1 66 66 LYS HB2 H 1 1.744 0.003 . 2 . . . A 49 LYS HB2 . 25086 1 753 . 1 1 66 66 LYS HB3 H 1 1.860 0.003 . 2 . . . A 49 LYS HB3 . 25086 1 754 . 1 1 66 66 LYS HG2 H 1 1.447 0.006 . 1 . . . A 49 LYS HG2 . 25086 1 755 . 1 1 66 66 LYS HG3 H 1 1.447 0.006 . 1 . . . A 49 LYS HG3 . 25086 1 756 . 1 1 66 66 LYS HD2 H 1 1.668 0.000 . 1 . . . A 49 LYS HD2 . 25086 1 757 . 1 1 66 66 LYS HD3 H 1 1.668 0.000 . 1 . . . A 49 LYS HD3 . 25086 1 758 . 1 1 66 66 LYS HE2 H 1 3.008 0.000 . 1 . . . A 49 LYS HE2 . 25086 1 759 . 1 1 66 66 LYS HE3 H 1 3.008 0.000 . 1 . . . A 49 LYS HE3 . 25086 1 760 . 1 1 66 66 LYS C C 13 175.579 0.000 . 1 . . . A 49 LYS C . 25086 1 761 . 1 1 66 66 LYS CA C 13 56.170 0.030 . 1 . . . A 49 LYS CA . 25086 1 762 . 1 1 66 66 LYS CB C 13 33.218 0.015 . 1 . . . A 49 LYS CB . 25086 1 763 . 1 1 66 66 LYS CG C 13 24.667 0.000 . 1 . . . A 49 LYS CG . 25086 1 764 . 1 1 66 66 LYS CD C 13 29.024 0.000 . 1 . . . A 49 LYS CD . 25086 1 765 . 1 1 66 66 LYS CE C 13 42.078 0.000 . 1 . . . A 49 LYS CE . 25086 1 766 . 1 1 66 66 LYS N N 15 124.176 0.006 . 1 . . . A 49 LYS N . 25086 1 767 . 1 1 67 67 GLU H H 1 8.010 0.001 . 1 . . . A 50 GLU H . 25086 1 768 . 1 1 67 67 GLU HA H 1 4.125 0.000 . 1 . . . A 50 GLU HA . 25086 1 769 . 1 1 67 67 GLU HB2 H 1 1.862 0.000 . 2 . . . A 50 GLU HB2 . 25086 1 770 . 1 1 67 67 GLU HB3 H 1 2.025 0.000 . 2 . . . A 50 GLU HB3 . 25086 1 771 . 1 1 67 67 GLU HG2 H 1 2.175 0.001 . 1 . . . A 50 GLU HG2 . 25086 1 772 . 1 1 67 67 GLU HG3 H 1 2.175 0.001 . 1 . . . A 50 GLU HG3 . 25086 1 773 . 1 1 67 67 GLU CA C 13 57.890 0.019 . 1 . . . A 50 GLU CA . 25086 1 774 . 1 1 67 67 GLU CB C 13 31.265 0.000 . 1 . . . A 50 GLU CB . 25086 1 775 . 1 1 67 67 GLU CG C 13 36.547 0.000 . 1 . . . A 50 GLU CG . 25086 1 776 . 1 1 67 67 GLU N N 15 127.072 0.012 . 1 . . . A 50 GLU N . 25086 1 stop_ save_