data_10269 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 10269 _Entry.Title ; Solution structures of the Chromo domain of human chromodomain helicase-DNA-binding protein 4 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-12-15 _Entry.Accession_date 2008-12-15 _Entry.Last_release_date 2009-12-14 _Entry.Original_release_date 2009-12-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.120 _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 M. Sato . . . 10269 2 N. Tochio . . . 10269 3 S. Koshiba . . . 10269 4 S. Watanabe . . . 10269 5 T. Harada . . . 10269 6 T. Kigawa . . . 10269 7 S. Yokoyama . . . 10269 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 'Protein 3000 Project' 'Protein Research Group, RIKEN Genomic Sciences Center' 'RIKEN GSC' 10269 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 10269 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 285 10269 '15N chemical shifts' 65 10269 '1H chemical shifts' 430 10269 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 . . 2009-12-14 2008-12-15 original author . 10269 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2EE1 'BMRB Entry Tracking System' 10269 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 10269 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Solution structures of the Chromo domain of human chromodomain helicase-DNA-binding protein 4 ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _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 M. Sato . . . 10269 1 2 N. Tochio . . . 10269 1 3 S. Koshiba . . . 10269 1 4 S. Watanabe . . . 10269 1 5 T. Harada . . . 10269 1 6 T. Kigawa . . . 10269 1 7 S. Yokoyama . . . 10269 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 10269 _Assembly.ID 1 _Assembly.Name 'Chromodomain helicase-DNA-binding protein 4' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 E.C.3.6.1.- _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 'Chromo domain' 1 $entity_1 . . yes native no no . . . 10269 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 2EE1 . . . . . . 10269 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 10269 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Chromo domain' _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 ; GSSGSSGKPEWMMIHRILNH SVDKKGHVHYLIKWRDLPYD QASWESEDVEIQDYDLFKQS YWNH ; _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 64 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 . _Entity.DB_query_revised_last_date 2015-11-26 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 PDB 2EE1 . "Solution Structures Of The Chromo Domain Of Human Chromodomain Helicase-Dna-Binding Protein 4" . . . . . 100.00 64 100.00 100.00 2.48e-38 . . . . 10269 1 2 no DBJ BAC28749 . "unnamed protein product [Mus musculus]" . . . . . 89.06 1045 100.00 100.00 2.13e-31 . . . . 10269 1 3 no DBJ BAD90499 . "mKIAA4075 protein [Mus musculus]" . . . . . 89.06 1945 100.00 100.00 8.50e-32 . . . . 10269 1 4 no DBJ BAE32198 . "unnamed protein product [Mus musculus]" . . . . . 89.06 895 100.00 100.00 3.10e-31 . . . . 10269 1 5 no DBJ BAG54725 . "unnamed protein product [Homo sapiens]" . . . . . 89.06 1886 100.00 100.00 1.15e-31 . . . . 10269 1 6 no EMBL CAA60384 . "Mi-2 protein [Homo sapiens]" . . . . . 89.06 1912 100.00 100.00 1.00e-31 . . . . 10269 1 7 no GB AAH38596 . "CHD4 protein [Homo sapiens]" . . . . . 89.06 1937 100.00 100.00 9.44e-32 . . . . 10269 1 8 no GB AAH58578 . "Chromodomain helicase DNA binding protein 4 [Mus musculus]" . . . . . 89.06 1915 100.00 100.00 9.30e-32 . . . . 10269 1 9 no GB ABZ92034 . "chromodomain helicase DNA binding protein 4 [synthetic construct]" . . . . . 89.06 1937 100.00 100.00 9.44e-32 . . . . 10269 1 10 no GB EAW88777 . "chromodomain helicase DNA binding protein 4, isoform CRA_a [Homo sapiens]" . . . . . 89.06 1911 100.00 100.00 1.06e-31 . . . . 10269 1 11 no GB EAW88778 . "chromodomain helicase DNA binding protein 4, isoform CRA_b [Homo sapiens]" . . . . . 89.06 1912 100.00 100.00 1.00e-31 . . . . 10269 1 12 no REF NP_001193430 . "chromodomain-helicase-DNA-binding protein 4 [Bos taurus]" . . . . . 89.06 1912 100.00 100.00 1.02e-31 . . . . 10269 1 13 no REF NP_001264 . "chromodomain-helicase-DNA-binding protein 4 isoform 1 [Homo sapiens]" . . . . . 89.06 1912 100.00 100.00 1.00e-31 . . . . 10269 1 14 no REF NP_001284482 . "chromodomain-helicase-DNA-binding protein 4 isoform 2 [Homo sapiens]" . . . . . 89.06 1905 100.00 100.00 9.93e-32 . . . . 10269 1 15 no REF NP_666091 . "chromodomain-helicase-DNA-binding protein 4 [Mus musculus]" . . . . . 89.06 1915 100.00 100.00 9.30e-32 . . . . 10269 1 16 no REF XP_001063352 . "PREDICTED: chromodomain-helicase-DNA-binding protein 4 isoform X1 [Rattus norvegicus]" . . . . . 89.06 1921 100.00 100.00 9.31e-32 . . . . 10269 1 17 no SP Q14839 . "RecName: Full=Chromodomain-helicase-DNA-binding protein 4; Short=CHD-4; AltName: Full=ATP-dependent helicase CHD4; AltName: Ful" . . . . . 89.06 1912 100.00 100.00 1.00e-31 . . . . 10269 1 18 no SP Q6PDQ2 . "RecName: Full=Chromodomain-helicase-DNA-binding protein 4; Short=CHD-4" . . . . . 89.06 1915 100.00 100.00 9.30e-32 . . . . 10269 1 19 no TPG DAA29256 . "TPA: chromodomain helicase DNA binding protein 4 [Bos taurus]" . . . . . 89.06 1912 100.00 100.00 1.02e-31 . . . . 10269 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Chromo domain' . 10269 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 . GLY . 10269 1 2 . SER . 10269 1 3 . SER . 10269 1 4 . GLY . 10269 1 5 . SER . 10269 1 6 . SER . 10269 1 7 . GLY . 10269 1 8 . LYS . 10269 1 9 . PRO . 10269 1 10 . GLU . 10269 1 11 . TRP . 10269 1 12 . MET . 10269 1 13 . MET . 10269 1 14 . ILE . 10269 1 15 . HIS . 10269 1 16 . ARG . 10269 1 17 . ILE . 10269 1 18 . LEU . 10269 1 19 . ASN . 10269 1 20 . HIS . 10269 1 21 . SER . 10269 1 22 . VAL . 10269 1 23 . ASP . 10269 1 24 . LYS . 10269 1 25 . LYS . 10269 1 26 . GLY . 10269 1 27 . HIS . 10269 1 28 . VAL . 10269 1 29 . HIS . 10269 1 30 . TYR . 10269 1 31 . LEU . 10269 1 32 . ILE . 10269 1 33 . LYS . 10269 1 34 . TRP . 10269 1 35 . ARG . 10269 1 36 . ASP . 10269 1 37 . LEU . 10269 1 38 . PRO . 10269 1 39 . TYR . 10269 1 40 . ASP . 10269 1 41 . GLN . 10269 1 42 . ALA . 10269 1 43 . SER . 10269 1 44 . TRP . 10269 1 45 . GLU . 10269 1 46 . SER . 10269 1 47 . GLU . 10269 1 48 . ASP . 10269 1 49 . VAL . 10269 1 50 . GLU . 10269 1 51 . ILE . 10269 1 52 . GLN . 10269 1 53 . ASP . 10269 1 54 . TYR . 10269 1 55 . ASP . 10269 1 56 . LEU . 10269 1 57 . PHE . 10269 1 58 . LYS . 10269 1 59 . GLN . 10269 1 60 . SER . 10269 1 61 . TYR . 10269 1 62 . TRP . 10269 1 63 . ASN . 10269 1 64 . HIS . 10269 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 . GLY 1 1 10269 1 . SER 2 2 10269 1 . SER 3 3 10269 1 . GLY 4 4 10269 1 . SER 5 5 10269 1 . SER 6 6 10269 1 . GLY 7 7 10269 1 . LYS 8 8 10269 1 . PRO 9 9 10269 1 . GLU 10 10 10269 1 . TRP 11 11 10269 1 . MET 12 12 10269 1 . MET 13 13 10269 1 . ILE 14 14 10269 1 . HIS 15 15 10269 1 . ARG 16 16 10269 1 . ILE 17 17 10269 1 . LEU 18 18 10269 1 . ASN 19 19 10269 1 . HIS 20 20 10269 1 . SER 21 21 10269 1 . VAL 22 22 10269 1 . ASP 23 23 10269 1 . LYS 24 24 10269 1 . LYS 25 25 10269 1 . GLY 26 26 10269 1 . HIS 27 27 10269 1 . VAL 28 28 10269 1 . HIS 29 29 10269 1 . TYR 30 30 10269 1 . LEU 31 31 10269 1 . ILE 32 32 10269 1 . LYS 33 33 10269 1 . TRP 34 34 10269 1 . ARG 35 35 10269 1 . ASP 36 36 10269 1 . LEU 37 37 10269 1 . PRO 38 38 10269 1 . TYR 39 39 10269 1 . ASP 40 40 10269 1 . GLN 41 41 10269 1 . ALA 42 42 10269 1 . SER 43 43 10269 1 . TRP 44 44 10269 1 . GLU 45 45 10269 1 . SER 46 46 10269 1 . GLU 47 47 10269 1 . ASP 48 48 10269 1 . VAL 49 49 10269 1 . GLU 50 50 10269 1 . ILE 51 51 10269 1 . GLN 52 52 10269 1 . ASP 53 53 10269 1 . TYR 54 54 10269 1 . ASP 55 55 10269 1 . LEU 56 56 10269 1 . PHE 57 57 10269 1 . LYS 58 58 10269 1 . GLN 59 59 10269 1 . SER 60 60 10269 1 . TYR 61 61 10269 1 . TRP 62 62 10269 1 . ASN 63 63 10269 1 . HIS 64 64 10269 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 10269 _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 $entity_1 . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 10269 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 10269 _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 $entity_1 . 'cell free synthesis' . . . . . . . . . . . . . . . . . . . plasmid . . P060904-16 . . . . . . 10269 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 10269 _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 'Chromo domain' '[U-13C; U-15N]' . . 1 $entity_1 . protein 1 . . mM . . . . 10269 1 2 'd-Tris HCl' . . . . . . buffer 20 . . mM . . . . 10269 1 3 NaCl . . . . . . salt 100 . . mM . . . . 10269 1 4 d-DTT . . . . . . salt 1 . . mM . . . . 10269 1 5 NaN3 . . . . . . salt 0.02 . . % . . . . 10269 1 6 H2O . . . . . . solvent 90 . . % . . . . 10269 1 7 D2O . . . . . . solvent 10 . . % . . . . 10269 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 10269 _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' 120 0.1 mM 10269 1 pH 7.0 0.05 pH 10269 1 pressure 1 0.001 atm 10269 1 temperature 298 0.1 K 10269 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 10269 _Software.ID 1 _Software.Name xwinnmr _Software.Version 3.5 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Bruker . . 10269 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 10269 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 10269 _Software.ID 2 _Software.Name NMRPipe _Software.Version 20031121 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, F.' . . 10269 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 10269 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 10269 _Software.ID 3 _Software.Name NMRView _Software.Version 2.0.17 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, B.A.' . . 10269 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 10269 3 stop_ save_ save_software_4 _Software.Sf_category software _Software.Sf_framecode software_4 _Software.Entry_ID 10269 _Software.ID 4 _Software.Name Kujira _Software.Version 0.932 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Kobayashi, N.' . . 10269 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 10269 4 stop_ save_ save_software_5 _Software.Sf_category software _Software.Sf_framecode software_5 _Software.Entry_ID 10269 _Software.ID 5 _Software.Name CYANA _Software.Version 2.0.17 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, P.' . . 10269 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 10269 5 'structure solution' 10269 5 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 10269 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _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 10269 _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 Bruker AVANCE . 800 . . . 10269 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 10269 _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 '3D 13C-separated NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 10269 1 2 '3D 15N-separated NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 10269 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode reference_1 _Chem_shift_reference.Entry_ID 10269 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details ; Chemical shift reference of 1H was based on the proton of water (4.784ppm at 298K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; 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 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 10269 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 . indirect 1.0 . . . . . . . . . 10269 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 10269 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_1 _Assigned_chem_shift_list.Entry_ID 10269 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $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 '3D 13C-separated NOESY' 1 $sample_1 isotropic 10269 1 2 '3D 15N-separated NOESY' 1 $sample_1 isotropic 10269 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 6 6 SER HA H 1 4.447 0.030 . 1 . . . . 6 SER HA . 10269 1 2 . 1 1 6 6 SER HB2 H 1 3.875 0.030 . 2 . . . . 6 SER HB2 . 10269 1 3 . 1 1 6 6 SER C C 13 174.919 0.300 . 1 . . . . 6 SER C . 10269 1 4 . 1 1 6 6 SER CA C 13 58.632 0.300 . 1 . . . . 6 SER CA . 10269 1 5 . 1 1 6 6 SER CB C 13 63.826 0.300 . 1 . . . . 6 SER CB . 10269 1 6 . 1 1 7 7 GLY H H 1 8.381 0.030 . 1 . . . . 7 GLY H . 10269 1 7 . 1 1 7 7 GLY HA2 H 1 3.956 0.030 . 2 . . . . 7 GLY HA2 . 10269 1 8 . 1 1 7 7 GLY HA3 H 1 3.907 0.030 . 2 . . . . 7 GLY HA3 . 10269 1 9 . 1 1 7 7 GLY C C 13 173.610 0.300 . 1 . . . . 7 GLY C . 10269 1 10 . 1 1 7 7 GLY CA C 13 45.128 0.300 . 1 . . . . 7 GLY CA . 10269 1 11 . 1 1 7 7 GLY N N 15 110.672 0.300 . 1 . . . . 7 GLY N . 10269 1 12 . 1 1 8 8 LYS H H 1 7.989 0.030 . 1 . . . . 8 LYS H . 10269 1 13 . 1 1 8 8 LYS HA H 1 4.430 0.030 . 1 . . . . 8 LYS HA . 10269 1 14 . 1 1 8 8 LYS HB2 H 1 1.503 0.030 . 2 . . . . 8 LYS HB2 . 10269 1 15 . 1 1 8 8 LYS HB3 H 1 1.443 0.030 . 2 . . . . 8 LYS HB3 . 10269 1 16 . 1 1 8 8 LYS HD2 H 1 1.438 0.030 . 2 . . . . 8 LYS HD2 . 10269 1 17 . 1 1 8 8 LYS HD3 H 1 1.366 0.030 . 2 . . . . 8 LYS HD3 . 10269 1 18 . 1 1 8 8 LYS HE2 H 1 2.744 0.030 . 2 . . . . 8 LYS HE2 . 10269 1 19 . 1 1 8 8 LYS HE3 H 1 2.713 0.030 . 2 . . . . 8 LYS HE3 . 10269 1 20 . 1 1 8 8 LYS HG2 H 1 1.178 0.030 . 1 . . . . 8 LYS HG2 . 10269 1 21 . 1 1 8 8 LYS HG3 H 1 1.178 0.030 . 1 . . . . 8 LYS HG3 . 10269 1 22 . 1 1 8 8 LYS C C 13 174.322 0.300 . 1 . . . . 8 LYS C . 10269 1 23 . 1 1 8 8 LYS CA C 13 53.436 0.300 . 1 . . . . 8 LYS CA . 10269 1 24 . 1 1 8 8 LYS CB C 13 31.892 0.300 . 1 . . . . 8 LYS CB . 10269 1 25 . 1 1 8 8 LYS CD C 13 28.360 0.300 . 1 . . . . 8 LYS CD . 10269 1 26 . 1 1 8 8 LYS CE C 13 42.065 0.300 . 1 . . . . 8 LYS CE . 10269 1 27 . 1 1 8 8 LYS CG C 13 24.449 0.300 . 1 . . . . 8 LYS CG . 10269 1 28 . 1 1 8 8 LYS N N 15 121.270 0.300 . 1 . . . . 8 LYS N . 10269 1 29 . 1 1 9 9 PRO HA H 1 4.131 0.030 . 1 . . . . 9 PRO HA . 10269 1 30 . 1 1 9 9 PRO HB2 H 1 1.910 0.030 . 2 . . . . 9 PRO HB2 . 10269 1 31 . 1 1 9 9 PRO HB3 H 1 0.960 0.030 . 2 . . . . 9 PRO HB3 . 10269 1 32 . 1 1 9 9 PRO HD2 H 1 3.604 0.030 . 2 . . . . 9 PRO HD2 . 10269 1 33 . 1 1 9 9 PRO HD3 H 1 3.283 0.030 . 2 . . . . 9 PRO HD3 . 10269 1 34 . 1 1 9 9 PRO HG2 H 1 1.778 0.030 . 2 . . . . 9 PRO HG2 . 10269 1 35 . 1 1 9 9 PRO HG3 H 1 1.537 0.030 . 2 . . . . 9 PRO HG3 . 10269 1 36 . 1 1 9 9 PRO C C 13 177.331 0.300 . 1 . . . . 9 PRO C . 10269 1 37 . 1 1 9 9 PRO CA C 13 62.970 0.300 . 1 . . . . 9 PRO CA . 10269 1 38 . 1 1 9 9 PRO CB C 13 31.894 0.300 . 1 . . . . 9 PRO CB . 10269 1 39 . 1 1 9 9 PRO CD C 13 50.294 0.300 . 1 . . . . 9 PRO CD . 10269 1 40 . 1 1 9 9 PRO CG C 13 27.461 0.300 . 1 . . . . 9 PRO CG . 10269 1 41 . 1 1 10 10 GLU H H 1 8.649 0.030 . 1 . . . . 10 GLU H . 10269 1 42 . 1 1 10 10 GLU HA H 1 3.960 0.030 . 1 . . . . 10 GLU HA . 10269 1 43 . 1 1 10 10 GLU HB2 H 1 1.915 0.030 . 2 . . . . 10 GLU HB2 . 10269 1 44 . 1 1 10 10 GLU HB3 H 1 1.867 0.030 . 2 . . . . 10 GLU HB3 . 10269 1 45 . 1 1 10 10 GLU HG2 H 1 2.205 0.030 . 2 . . . . 10 GLU HG2 . 10269 1 46 . 1 1 10 10 GLU HG3 H 1 2.163 0.030 . 2 . . . . 10 GLU HG3 . 10269 1 47 . 1 1 10 10 GLU C C 13 175.849 0.300 . 1 . . . . 10 GLU C . 10269 1 48 . 1 1 10 10 GLU CA C 13 58.051 0.300 . 1 . . . . 10 GLU CA . 10269 1 49 . 1 1 10 10 GLU CB C 13 29.627 0.300 . 1 . . . . 10 GLU CB . 10269 1 50 . 1 1 10 10 GLU CG C 13 36.120 0.300 . 1 . . . . 10 GLU CG . 10269 1 51 . 1 1 10 10 GLU N N 15 120.707 0.300 . 1 . . . . 10 GLU N . 10269 1 52 . 1 1 11 11 TRP H H 1 7.131 0.030 . 1 . . . . 11 TRP H . 10269 1 53 . 1 1 11 11 TRP HA H 1 4.548 0.030 . 1 . . . . 11 TRP HA . 10269 1 54 . 1 1 11 11 TRP HB2 H 1 3.313 0.030 . 2 . . . . 11 TRP HB2 . 10269 1 55 . 1 1 11 11 TRP HB3 H 1 3.146 0.030 . 2 . . . . 11 TRP HB3 . 10269 1 56 . 1 1 11 11 TRP HD1 H 1 7.183 0.030 . 1 . . . . 11 TRP HD1 . 10269 1 57 . 1 1 11 11 TRP HE1 H 1 10.180 0.030 . 1 . . . . 11 TRP HE1 . 10269 1 58 . 1 1 11 11 TRP HE3 H 1 7.371 0.030 . 1 . . . . 11 TRP HE3 . 10269 1 59 . 1 1 11 11 TRP HH2 H 1 7.105 0.030 . 1 . . . . 11 TRP HH2 . 10269 1 60 . 1 1 11 11 TRP HZ2 H 1 7.372 0.030 . 1 . . . . 11 TRP HZ2 . 10269 1 61 . 1 1 11 11 TRP HZ3 H 1 6.827 0.030 . 1 . . . . 11 TRP HZ3 . 10269 1 62 . 1 1 11 11 TRP C C 13 176.362 0.300 . 1 . . . . 11 TRP C . 10269 1 63 . 1 1 11 11 TRP CA C 13 55.758 0.300 . 1 . . . . 11 TRP CA . 10269 1 64 . 1 1 11 11 TRP CB C 13 29.285 0.300 . 1 . . . . 11 TRP CB . 10269 1 65 . 1 1 11 11 TRP CD1 C 13 127.151 0.300 . 1 . . . . 11 TRP CD1 . 10269 1 66 . 1 1 11 11 TRP CE3 C 13 121.087 0.300 . 1 . . . . 11 TRP CE3 . 10269 1 67 . 1 1 11 11 TRP CH2 C 13 124.876 0.300 . 1 . . . . 11 TRP CH2 . 10269 1 68 . 1 1 11 11 TRP CZ2 C 13 114.475 0.300 . 1 . . . . 11 TRP CZ2 . 10269 1 69 . 1 1 11 11 TRP CZ3 C 13 122.092 0.300 . 1 . . . . 11 TRP CZ3 . 10269 1 70 . 1 1 11 11 TRP N N 15 115.904 0.300 . 1 . . . . 11 TRP N . 10269 1 71 . 1 1 11 11 TRP NE1 N 15 130.020 0.300 . 1 . . . . 11 TRP NE1 . 10269 1 72 . 1 1 12 12 MET H H 1 7.289 0.030 . 1 . . . . 12 MET H . 10269 1 73 . 1 1 12 12 MET HA H 1 4.054 0.030 . 1 . . . . 12 MET HA . 10269 1 74 . 1 1 12 12 MET HB2 H 1 1.454 0.030 . 2 . . . . 12 MET HB2 . 10269 1 75 . 1 1 12 12 MET HB3 H 1 1.359 0.030 . 2 . . . . 12 MET HB3 . 10269 1 76 . 1 1 12 12 MET HE1 H 1 1.141 0.030 . 1 . . . . 12 MET HE . 10269 1 77 . 1 1 12 12 MET HE2 H 1 1.141 0.030 . 1 . . . . 12 MET HE . 10269 1 78 . 1 1 12 12 MET HE3 H 1 1.141 0.030 . 1 . . . . 12 MET HE . 10269 1 79 . 1 1 12 12 MET HG2 H 1 1.455 0.030 . 2 . . . . 12 MET HG2 . 10269 1 80 . 1 1 12 12 MET HG3 H 1 1.153 0.030 . 2 . . . . 12 MET HG3 . 10269 1 81 . 1 1 12 12 MET C C 13 174.357 0.300 . 1 . . . . 12 MET C . 10269 1 82 . 1 1 12 12 MET CA C 13 55.900 0.300 . 1 . . . . 12 MET CA . 10269 1 83 . 1 1 12 12 MET CB C 13 31.808 0.300 . 1 . . . . 12 MET CB . 10269 1 84 . 1 1 12 12 MET CE C 13 15.898 0.300 . 1 . . . . 12 MET CE . 10269 1 85 . 1 1 12 12 MET CG C 13 32.253 0.300 . 1 . . . . 12 MET CG . 10269 1 86 . 1 1 12 12 MET N N 15 122.155 0.300 . 1 . . . . 12 MET N . 10269 1 87 . 1 1 13 13 MET H H 1 8.569 0.030 . 1 . . . . 13 MET H . 10269 1 88 . 1 1 13 13 MET HA H 1 4.890 0.030 . 1 . . . . 13 MET HA . 10269 1 89 . 1 1 13 13 MET HB2 H 1 1.960 0.030 . 2 . . . . 13 MET HB2 . 10269 1 90 . 1 1 13 13 MET HB3 H 1 1.824 0.030 . 2 . . . . 13 MET HB3 . 10269 1 91 . 1 1 13 13 MET HE1 H 1 2.099 0.030 . 1 . . . . 13 MET HE . 10269 1 92 . 1 1 13 13 MET HE2 H 1 2.099 0.030 . 1 . . . . 13 MET HE . 10269 1 93 . 1 1 13 13 MET HE3 H 1 2.099 0.030 . 1 . . . . 13 MET HE . 10269 1 94 . 1 1 13 13 MET HG2 H 1 2.571 0.030 . 2 . . . . 13 MET HG2 . 10269 1 95 . 1 1 13 13 MET HG3 H 1 2.478 0.030 . 2 . . . . 13 MET HG3 . 10269 1 96 . 1 1 13 13 MET C C 13 175.898 0.300 . 1 . . . . 13 MET C . 10269 1 97 . 1 1 13 13 MET CA C 13 53.784 0.300 . 1 . . . . 13 MET CA . 10269 1 98 . 1 1 13 13 MET CB C 13 35.100 0.300 . 1 . . . . 13 MET CB . 10269 1 99 . 1 1 13 13 MET CE C 13 17.567 0.300 . 1 . . . . 13 MET CE . 10269 1 100 . 1 1 13 13 MET CG C 13 32.306 0.300 . 1 . . . . 13 MET CG . 10269 1 101 . 1 1 13 13 MET N N 15 121.084 0.300 . 1 . . . . 13 MET N . 10269 1 102 . 1 1 14 14 ILE H H 1 9.144 0.030 . 1 . . . . 14 ILE H . 10269 1 103 . 1 1 14 14 ILE HA H 1 2.912 0.030 . 1 . . . . 14 ILE HA . 10269 1 104 . 1 1 14 14 ILE HB H 1 0.650 0.030 . 1 . . . . 14 ILE HB . 10269 1 105 . 1 1 14 14 ILE HD11 H 1 0.401 0.030 . 1 . . . . 14 ILE HD1 . 10269 1 106 . 1 1 14 14 ILE HD12 H 1 0.401 0.030 . 1 . . . . 14 ILE HD1 . 10269 1 107 . 1 1 14 14 ILE HD13 H 1 0.401 0.030 . 1 . . . . 14 ILE HD1 . 10269 1 108 . 1 1 14 14 ILE HG12 H 1 1.395 0.030 . 2 . . . . 14 ILE HG12 . 10269 1 109 . 1 1 14 14 ILE HG13 H 1 0.135 0.030 . 2 . . . . 14 ILE HG13 . 10269 1 110 . 1 1 14 14 ILE HG21 H 1 -0.436 0.030 . 1 . . . . 14 ILE HG2 . 10269 1 111 . 1 1 14 14 ILE HG22 H 1 -0.436 0.030 . 1 . . . . 14 ILE HG2 . 10269 1 112 . 1 1 14 14 ILE HG23 H 1 -0.436 0.030 . 1 . . . . 14 ILE HG2 . 10269 1 113 . 1 1 14 14 ILE C C 13 174.810 0.300 . 1 . . . . 14 ILE C . 10269 1 114 . 1 1 14 14 ILE CA C 13 63.803 0.300 . 1 . . . . 14 ILE CA . 10269 1 115 . 1 1 14 14 ILE CB C 13 38.974 0.300 . 1 . . . . 14 ILE CB . 10269 1 116 . 1 1 14 14 ILE CD1 C 13 14.086 0.300 . 1 . . . . 14 ILE CD1 . 10269 1 117 . 1 1 14 14 ILE CG1 C 13 27.608 0.300 . 1 . . . . 14 ILE CG1 . 10269 1 118 . 1 1 14 14 ILE CG2 C 13 16.446 0.300 . 1 . . . . 14 ILE CG2 . 10269 1 119 . 1 1 14 14 ILE N N 15 125.919 0.300 . 1 . . . . 14 ILE N . 10269 1 120 . 1 1 15 15 HIS H H 1 8.926 0.030 . 1 . . . . 15 HIS H . 10269 1 121 . 1 1 15 15 HIS HA H 1 4.690 0.030 . 1 . . . . 15 HIS HA . 10269 1 122 . 1 1 15 15 HIS HB2 H 1 2.816 0.030 . 2 . . . . 15 HIS HB2 . 10269 1 123 . 1 1 15 15 HIS HB3 H 1 2.418 0.030 . 2 . . . . 15 HIS HB3 . 10269 1 124 . 1 1 15 15 HIS HD2 H 1 6.942 0.030 . 1 . . . . 15 HIS HD2 . 10269 1 125 . 1 1 15 15 HIS C C 13 174.715 0.300 . 1 . . . . 15 HIS C . 10269 1 126 . 1 1 15 15 HIS CA C 13 55.829 0.300 . 1 . . . . 15 HIS CA . 10269 1 127 . 1 1 15 15 HIS CB C 13 33.853 0.300 . 1 . . . . 15 HIS CB . 10269 1 128 . 1 1 15 15 HIS CD2 C 13 116.175 0.300 . 1 . . . . 15 HIS CD2 . 10269 1 129 . 1 1 15 15 HIS N N 15 125.470 0.300 . 1 . . . . 15 HIS N . 10269 1 130 . 1 1 16 16 ARG H H 1 7.529 0.030 . 1 . . . . 16 ARG H . 10269 1 131 . 1 1 16 16 ARG HA H 1 4.193 0.030 . 1 . . . . 16 ARG HA . 10269 1 132 . 1 1 16 16 ARG HB2 H 1 1.729 0.030 . 2 . . . . 16 ARG HB2 . 10269 1 133 . 1 1 16 16 ARG HB3 H 1 1.459 0.030 . 2 . . . . 16 ARG HB3 . 10269 1 134 . 1 1 16 16 ARG HD2 H 1 2.986 0.030 . 2 . . . . 16 ARG HD2 . 10269 1 135 . 1 1 16 16 ARG HD3 H 1 2.944 0.030 . 2 . . . . 16 ARG HD3 . 10269 1 136 . 1 1 16 16 ARG HG2 H 1 1.150 0.030 . 2 . . . . 16 ARG HG2 . 10269 1 137 . 1 1 16 16 ARG HG3 H 1 1.034 0.030 . 2 . . . . 16 ARG HG3 . 10269 1 138 . 1 1 16 16 ARG C C 13 173.315 0.300 . 1 . . . . 16 ARG C . 10269 1 139 . 1 1 16 16 ARG CA C 13 55.329 0.300 . 1 . . . . 16 ARG CA . 10269 1 140 . 1 1 16 16 ARG CB C 13 33.252 0.300 . 1 . . . . 16 ARG CB . 10269 1 141 . 1 1 16 16 ARG CD C 13 43.238 0.300 . 1 . . . . 16 ARG CD . 10269 1 142 . 1 1 16 16 ARG CG C 13 25.960 0.300 . 1 . . . . 16 ARG CG . 10269 1 143 . 1 1 16 16 ARG N N 15 111.315 0.300 . 1 . . . . 16 ARG N . 10269 1 144 . 1 1 17 17 ILE H H 1 8.396 0.030 . 1 . . . . 17 ILE H . 10269 1 145 . 1 1 17 17 ILE HA H 1 4.052 0.030 . 1 . . . . 17 ILE HA . 10269 1 146 . 1 1 17 17 ILE HB H 1 1.455 0.030 . 1 . . . . 17 ILE HB . 10269 1 147 . 1 1 17 17 ILE HD11 H 1 0.248 0.030 . 1 . . . . 17 ILE HD1 . 10269 1 148 . 1 1 17 17 ILE HD12 H 1 0.248 0.030 . 1 . . . . 17 ILE HD1 . 10269 1 149 . 1 1 17 17 ILE HD13 H 1 0.248 0.030 . 1 . . . . 17 ILE HD1 . 10269 1 150 . 1 1 17 17 ILE HG12 H 1 1.319 0.030 . 2 . . . . 17 ILE HG12 . 10269 1 151 . 1 1 17 17 ILE HG13 H 1 0.578 0.030 . 2 . . . . 17 ILE HG13 . 10269 1 152 . 1 1 17 17 ILE HG21 H 1 0.244 0.030 . 1 . . . . 17 ILE HG2 . 10269 1 153 . 1 1 17 17 ILE HG22 H 1 0.244 0.030 . 1 . . . . 17 ILE HG2 . 10269 1 154 . 1 1 17 17 ILE HG23 H 1 0.244 0.030 . 1 . . . . 17 ILE HG2 . 10269 1 155 . 1 1 17 17 ILE C C 13 175.341 0.300 . 1 . . . . 17 ILE C . 10269 1 156 . 1 1 17 17 ILE CA C 13 61.859 0.300 . 1 . . . . 17 ILE CA . 10269 1 157 . 1 1 17 17 ILE CB C 13 37.952 0.300 . 1 . . . . 17 ILE CB . 10269 1 158 . 1 1 17 17 ILE CD1 C 13 12.652 0.300 . 1 . . . . 17 ILE CD1 . 10269 1 159 . 1 1 17 17 ILE CG1 C 13 28.597 0.300 . 1 . . . . 17 ILE CG1 . 10269 1 160 . 1 1 17 17 ILE CG2 C 13 17.933 0.300 . 1 . . . . 17 ILE CG2 . 10269 1 161 . 1 1 17 17 ILE N N 15 121.157 0.300 . 1 . . . . 17 ILE N . 10269 1 162 . 1 1 18 18 LEU H H 1 9.102 0.030 . 1 . . . . 18 LEU H . 10269 1 163 . 1 1 18 18 LEU HA H 1 4.253 0.030 . 1 . . . . 18 LEU HA . 10269 1 164 . 1 1 18 18 LEU HB2 H 1 1.421 0.030 . 2 . . . . 18 LEU HB2 . 10269 1 165 . 1 1 18 18 LEU HB3 H 1 1.211 0.030 . 2 . . . . 18 LEU HB3 . 10269 1 166 . 1 1 18 18 LEU HD11 H 1 0.530 0.030 . 1 . . . . 18 LEU HD1 . 10269 1 167 . 1 1 18 18 LEU HD12 H 1 0.530 0.030 . 1 . . . . 18 LEU HD1 . 10269 1 168 . 1 1 18 18 LEU HD13 H 1 0.530 0.030 . 1 . . . . 18 LEU HD1 . 10269 1 169 . 1 1 18 18 LEU HD21 H 1 0.676 0.030 . 1 . . . . 18 LEU HD2 . 10269 1 170 . 1 1 18 18 LEU HD22 H 1 0.676 0.030 . 1 . . . . 18 LEU HD2 . 10269 1 171 . 1 1 18 18 LEU HD23 H 1 0.676 0.030 . 1 . . . . 18 LEU HD2 . 10269 1 172 . 1 1 18 18 LEU HG H 1 1.332 0.030 . 1 . . . . 18 LEU HG . 10269 1 173 . 1 1 18 18 LEU C C 13 176.622 0.300 . 1 . . . . 18 LEU C . 10269 1 174 . 1 1 18 18 LEU CA C 13 55.422 0.300 . 1 . . . . 18 LEU CA . 10269 1 175 . 1 1 18 18 LEU CB C 13 43.410 0.300 . 1 . . . . 18 LEU CB . 10269 1 176 . 1 1 18 18 LEU CD1 C 13 25.047 0.300 . 2 . . . . 18 LEU CD1 . 10269 1 177 . 1 1 18 18 LEU CD2 C 13 22.130 0.300 . 2 . . . . 18 LEU CD2 . 10269 1 178 . 1 1 18 18 LEU CG C 13 26.372 0.300 . 1 . . . . 18 LEU CG . 10269 1 179 . 1 1 18 18 LEU N N 15 124.326 0.300 . 1 . . . . 18 LEU N . 10269 1 180 . 1 1 19 19 ASN H H 1 7.343 0.030 . 1 . . . . 19 ASN H . 10269 1 181 . 1 1 19 19 ASN HA H 1 5.227 0.030 . 1 . . . . 19 ASN HA . 10269 1 182 . 1 1 19 19 ASN HB2 H 1 2.733 0.030 . 2 . . . . 19 ASN HB2 . 10269 1 183 . 1 1 19 19 ASN HB3 H 1 2.302 0.030 . 2 . . . . 19 ASN HB3 . 10269 1 184 . 1 1 19 19 ASN HD21 H 1 7.451 0.030 . 2 . . . . 19 ASN HD21 . 10269 1 185 . 1 1 19 19 ASN HD22 H 1 6.992 0.030 . 2 . . . . 19 ASN HD22 . 10269 1 186 . 1 1 19 19 ASN C C 13 172.527 0.300 . 1 . . . . 19 ASN C . 10269 1 187 . 1 1 19 19 ASN CA C 13 51.140 0.300 . 1 . . . . 19 ASN CA . 10269 1 188 . 1 1 19 19 ASN CB C 13 40.795 0.300 . 1 . . . . 19 ASN CB . 10269 1 189 . 1 1 19 19 ASN N N 15 113.895 0.300 . 1 . . . . 19 ASN N . 10269 1 190 . 1 1 19 19 ASN ND2 N 15 109.984 0.300 . 1 . . . . 19 ASN ND2 . 10269 1 191 . 1 1 20 20 HIS H H 1 8.816 0.030 . 1 . . . . 20 HIS H . 10269 1 192 . 1 1 20 20 HIS HA H 1 5.875 0.030 . 1 . . . . 20 HIS HA . 10269 1 193 . 1 1 20 20 HIS HB2 H 1 2.817 0.030 . 2 . . . . 20 HIS HB2 . 10269 1 194 . 1 1 20 20 HIS HB3 H 1 2.643 0.030 . 2 . . . . 20 HIS HB3 . 10269 1 195 . 1 1 20 20 HIS HD2 H 1 6.698 0.030 . 1 . . . . 20 HIS HD2 . 10269 1 196 . 1 1 20 20 HIS HE1 H 1 7.953 0.030 . 1 . . . . 20 HIS HE1 . 10269 1 197 . 1 1 20 20 HIS C C 13 173.013 0.300 . 1 . . . . 20 HIS C . 10269 1 198 . 1 1 20 20 HIS CA C 13 55.932 0.300 . 1 . . . . 20 HIS CA . 10269 1 199 . 1 1 20 20 HIS CB C 13 35.190 0.300 . 1 . . . . 20 HIS CB . 10269 1 200 . 1 1 20 20 HIS CD2 C 13 116.364 0.300 . 1 . . . . 20 HIS CD2 . 10269 1 201 . 1 1 20 20 HIS CE1 C 13 138.772 0.300 . 1 . . . . 20 HIS CE1 . 10269 1 202 . 1 1 20 20 HIS N N 15 118.537 0.300 . 1 . . . . 20 HIS N . 10269 1 203 . 1 1 21 21 SER H H 1 9.203 0.030 . 1 . . . . 21 SER H . 10269 1 204 . 1 1 21 21 SER HA H 1 4.399 0.030 . 1 . . . . 21 SER HA . 10269 1 205 . 1 1 21 21 SER HB2 H 1 3.414 0.030 . 2 . . . . 21 SER HB2 . 10269 1 206 . 1 1 21 21 SER HB3 H 1 3.127 0.030 . 2 . . . . 21 SER HB3 . 10269 1 207 . 1 1 21 21 SER C C 13 172.382 0.300 . 1 . . . . 21 SER C . 10269 1 208 . 1 1 21 21 SER CA C 13 57.063 0.300 . 1 . . . . 21 SER CA . 10269 1 209 . 1 1 21 21 SER CB C 13 65.417 0.300 . 1 . . . . 21 SER CB . 10269 1 210 . 1 1 21 21 SER N N 15 115.006 0.300 . 1 . . . . 21 SER N . 10269 1 211 . 1 1 22 22 VAL H H 1 8.493 0.030 . 1 . . . . 22 VAL H . 10269 1 212 . 1 1 22 22 VAL HA H 1 4.961 0.030 . 1 . . . . 22 VAL HA . 10269 1 213 . 1 1 22 22 VAL HB H 1 1.979 0.030 . 1 . . . . 22 VAL HB . 10269 1 214 . 1 1 22 22 VAL HG11 H 1 1.087 0.030 . 1 . . . . 22 VAL HG1 . 10269 1 215 . 1 1 22 22 VAL HG12 H 1 1.087 0.030 . 1 . . . . 22 VAL HG1 . 10269 1 216 . 1 1 22 22 VAL HG13 H 1 1.087 0.030 . 1 . . . . 22 VAL HG1 . 10269 1 217 . 1 1 22 22 VAL HG21 H 1 1.002 0.030 . 1 . . . . 22 VAL HG2 . 10269 1 218 . 1 1 22 22 VAL HG22 H 1 1.002 0.030 . 1 . . . . 22 VAL HG2 . 10269 1 219 . 1 1 22 22 VAL HG23 H 1 1.002 0.030 . 1 . . . . 22 VAL HG2 . 10269 1 220 . 1 1 22 22 VAL C C 13 176.199 0.300 . 1 . . . . 22 VAL C . 10269 1 221 . 1 1 22 22 VAL CA C 13 61.066 0.300 . 1 . . . . 22 VAL CA . 10269 1 222 . 1 1 22 22 VAL CB C 13 33.732 0.300 . 1 . . . . 22 VAL CB . 10269 1 223 . 1 1 22 22 VAL CG1 C 13 21.387 0.300 . 2 . . . . 22 VAL CG1 . 10269 1 224 . 1 1 22 22 VAL CG2 C 13 20.885 0.300 . 2 . . . . 22 VAL CG2 . 10269 1 225 . 1 1 22 22 VAL N N 15 124.080 0.300 . 1 . . . . 22 VAL N . 10269 1 226 . 1 1 23 23 ASP H H 1 8.667 0.030 . 1 . . . . 23 ASP H . 10269 1 227 . 1 1 23 23 ASP HA H 1 4.688 0.030 . 1 . . . . 23 ASP HA . 10269 1 228 . 1 1 23 23 ASP HB2 H 1 3.354 0.030 . 2 . . . . 23 ASP HB2 . 10269 1 229 . 1 1 23 23 ASP HB3 H 1 2.695 0.030 . 2 . . . . 23 ASP HB3 . 10269 1 230 . 1 1 23 23 ASP C C 13 178.629 0.300 . 1 . . . . 23 ASP C . 10269 1 231 . 1 1 23 23 ASP CA C 13 52.814 0.300 . 1 . . . . 23 ASP CA . 10269 1 232 . 1 1 23 23 ASP CB C 13 41.525 0.300 . 1 . . . . 23 ASP CB . 10269 1 233 . 1 1 23 23 ASP N N 15 127.673 0.300 . 1 . . . . 23 ASP N . 10269 1 234 . 1 1 24 24 LYS H H 1 8.242 0.030 . 1 . . . . 24 LYS H . 10269 1 235 . 1 1 24 24 LYS HA H 1 4.077 0.030 . 1 . . . . 24 LYS HA . 10269 1 236 . 1 1 24 24 LYS HB2 H 1 1.858 0.030 . 1 . . . . 24 LYS HB2 . 10269 1 237 . 1 1 24 24 LYS HB3 H 1 1.858 0.030 . 1 . . . . 24 LYS HB3 . 10269 1 238 . 1 1 24 24 LYS HD2 H 1 1.652 0.030 . 1 . . . . 24 LYS HD2 . 10269 1 239 . 1 1 24 24 LYS HD3 H 1 1.652 0.030 . 1 . . . . 24 LYS HD3 . 10269 1 240 . 1 1 24 24 LYS HE2 H 1 2.944 0.030 . 1 . . . . 24 LYS HE2 . 10269 1 241 . 1 1 24 24 LYS HE3 H 1 2.944 0.030 . 1 . . . . 24 LYS HE3 . 10269 1 242 . 1 1 24 24 LYS HG2 H 1 1.464 0.030 . 1 . . . . 24 LYS HG2 . 10269 1 243 . 1 1 24 24 LYS HG3 H 1 1.464 0.030 . 1 . . . . 24 LYS HG3 . 10269 1 244 . 1 1 24 24 LYS C C 13 177.637 0.300 . 1 . . . . 24 LYS C . 10269 1 245 . 1 1 24 24 LYS CA C 13 58.419 0.300 . 1 . . . . 24 LYS CA . 10269 1 246 . 1 1 24 24 LYS CB C 13 32.057 0.300 . 1 . . . . 24 LYS CB . 10269 1 247 . 1 1 24 24 LYS CD C 13 28.931 0.300 . 1 . . . . 24 LYS CD . 10269 1 248 . 1 1 24 24 LYS CE C 13 42.113 0.300 . 1 . . . . 24 LYS CE . 10269 1 249 . 1 1 24 24 LYS CG C 13 24.956 0.300 . 1 . . . . 24 LYS CG . 10269 1 250 . 1 1 24 24 LYS N N 15 116.378 0.300 . 1 . . . . 24 LYS N . 10269 1 251 . 1 1 25 25 LYS H H 1 8.128 0.030 . 1 . . . . 25 LYS H . 10269 1 252 . 1 1 25 25 LYS HA H 1 4.379 0.030 . 1 . . . . 25 LYS HA . 10269 1 253 . 1 1 25 25 LYS HB2 H 1 1.894 0.030 . 2 . . . . 25 LYS HB2 . 10269 1 254 . 1 1 25 25 LYS HB3 H 1 1.776 0.030 . 2 . . . . 25 LYS HB3 . 10269 1 255 . 1 1 25 25 LYS HD2 H 1 1.645 0.030 . 1 . . . . 25 LYS HD2 . 10269 1 256 . 1 1 25 25 LYS HD3 H 1 1.645 0.030 . 1 . . . . 25 LYS HD3 . 10269 1 257 . 1 1 25 25 LYS HE2 H 1 2.941 0.030 . 1 . . . . 25 LYS HE2 . 10269 1 258 . 1 1 25 25 LYS HE3 H 1 2.941 0.030 . 1 . . . . 25 LYS HE3 . 10269 1 259 . 1 1 25 25 LYS HG2 H 1 1.395 0.030 . 2 . . . . 25 LYS HG2 . 10269 1 260 . 1 1 25 25 LYS HG3 H 1 1.345 0.030 . 2 . . . . 25 LYS HG3 . 10269 1 261 . 1 1 25 25 LYS C C 13 176.600 0.300 . 1 . . . . 25 LYS C . 10269 1 262 . 1 1 25 25 LYS CA C 13 55.411 0.300 . 1 . . . . 25 LYS CA . 10269 1 263 . 1 1 25 25 LYS CB C 13 32.516 0.300 . 1 . . . . 25 LYS CB . 10269 1 264 . 1 1 25 25 LYS CD C 13 28.927 0.300 . 1 . . . . 25 LYS CD . 10269 1 265 . 1 1 25 25 LYS CE C 13 42.037 0.300 . 1 . . . . 25 LYS CE . 10269 1 266 . 1 1 25 25 LYS CG C 13 25.248 0.300 . 1 . . . . 25 LYS CG . 10269 1 267 . 1 1 25 25 LYS N N 15 118.184 0.300 . 1 . . . . 25 LYS N . 10269 1 268 . 1 1 26 26 GLY H H 1 8.040 0.030 . 1 . . . . 26 GLY H . 10269 1 269 . 1 1 26 26 GLY HA2 H 1 4.125 0.030 . 2 . . . . 26 GLY HA2 . 10269 1 270 . 1 1 26 26 GLY HA3 H 1 3.428 0.030 . 2 . . . . 26 GLY HA3 . 10269 1 271 . 1 1 26 26 GLY C C 13 174.048 0.300 . 1 . . . . 26 GLY C . 10269 1 272 . 1 1 26 26 GLY CA C 13 45.235 0.300 . 1 . . . . 26 GLY CA . 10269 1 273 . 1 1 26 26 GLY N N 15 108.208 0.300 . 1 . . . . 26 GLY N . 10269 1 274 . 1 1 27 27 HIS H H 1 8.599 0.030 . 1 . . . . 27 HIS H . 10269 1 275 . 1 1 27 27 HIS HA H 1 4.491 0.030 . 1 . . . . 27 HIS HA . 10269 1 276 . 1 1 27 27 HIS HB2 H 1 3.280 0.030 . 1 . . . . 27 HIS HB2 . 10269 1 277 . 1 1 27 27 HIS HB3 H 1 3.280 0.030 . 1 . . . . 27 HIS HB3 . 10269 1 278 . 1 1 27 27 HIS HD2 H 1 6.853 0.030 . 1 . . . . 27 HIS HD2 . 10269 1 279 . 1 1 27 27 HIS C C 13 174.516 0.300 . 1 . . . . 27 HIS C . 10269 1 280 . 1 1 27 27 HIS CA C 13 55.935 0.300 . 1 . . . . 27 HIS CA . 10269 1 281 . 1 1 27 27 HIS CB C 13 29.257 0.300 . 1 . . . . 27 HIS CB . 10269 1 282 . 1 1 27 27 HIS CD2 C 13 122.434 0.300 . 1 . . . . 27 HIS CD2 . 10269 1 283 . 1 1 27 27 HIS N N 15 123.031 0.300 . 1 . . . . 27 HIS N . 10269 1 284 . 1 1 28 28 VAL H H 1 8.330 0.030 . 1 . . . . 28 VAL H . 10269 1 285 . 1 1 28 28 VAL HA H 1 4.776 0.030 . 1 . . . . 28 VAL HA . 10269 1 286 . 1 1 28 28 VAL HB H 1 1.616 0.030 . 1 . . . . 28 VAL HB . 10269 1 287 . 1 1 28 28 VAL HG11 H 1 0.974 0.030 . 1 . . . . 28 VAL HG1 . 10269 1 288 . 1 1 28 28 VAL HG12 H 1 0.974 0.030 . 1 . . . . 28 VAL HG1 . 10269 1 289 . 1 1 28 28 VAL HG13 H 1 0.974 0.030 . 1 . . . . 28 VAL HG1 . 10269 1 290 . 1 1 28 28 VAL HG21 H 1 0.562 0.030 . 1 . . . . 28 VAL HG2 . 10269 1 291 . 1 1 28 28 VAL HG22 H 1 0.562 0.030 . 1 . . . . 28 VAL HG2 . 10269 1 292 . 1 1 28 28 VAL HG23 H 1 0.562 0.030 . 1 . . . . 28 VAL HG2 . 10269 1 293 . 1 1 28 28 VAL C C 13 174.798 0.300 . 1 . . . . 28 VAL C . 10269 1 294 . 1 1 28 28 VAL CA C 13 62.070 0.300 . 1 . . . . 28 VAL CA . 10269 1 295 . 1 1 28 28 VAL CB C 13 32.965 0.300 . 1 . . . . 28 VAL CB . 10269 1 296 . 1 1 28 28 VAL CG1 C 13 22.412 0.300 . 2 . . . . 28 VAL CG1 . 10269 1 297 . 1 1 28 28 VAL CG2 C 13 21.649 0.300 . 2 . . . . 28 VAL CG2 . 10269 1 298 . 1 1 28 28 VAL N N 15 127.641 0.300 . 1 . . . . 28 VAL N . 10269 1 299 . 1 1 29 29 HIS H H 1 8.887 0.030 . 1 . . . . 29 HIS H . 10269 1 300 . 1 1 29 29 HIS HA H 1 5.071 0.030 . 1 . . . . 29 HIS HA . 10269 1 301 . 1 1 29 29 HIS HB2 H 1 2.944 0.030 . 2 . . . . 29 HIS HB2 . 10269 1 302 . 1 1 29 29 HIS HB3 H 1 2.848 0.030 . 2 . . . . 29 HIS HB3 . 10269 1 303 . 1 1 29 29 HIS HD2 H 1 6.789 0.030 . 1 . . . . 29 HIS HD2 . 10269 1 304 . 1 1 29 29 HIS HE1 H 1 7.791 0.030 . 1 . . . . 29 HIS HE1 . 10269 1 305 . 1 1 29 29 HIS C C 13 173.998 0.300 . 1 . . . . 29 HIS C . 10269 1 306 . 1 1 29 29 HIS CA C 13 54.841 0.300 . 1 . . . . 29 HIS CA . 10269 1 307 . 1 1 29 29 HIS CB C 13 33.921 0.300 . 1 . . . . 29 HIS CB . 10269 1 308 . 1 1 29 29 HIS CD2 C 13 120.245 0.300 . 1 . . . . 29 HIS CD2 . 10269 1 309 . 1 1 29 29 HIS CE1 C 13 137.943 0.300 . 1 . . . . 29 HIS CE1 . 10269 1 310 . 1 1 29 29 HIS N N 15 124.946 0.300 . 1 . . . . 29 HIS N . 10269 1 311 . 1 1 30 30 TYR H H 1 9.630 0.030 . 1 . . . . 30 TYR H . 10269 1 312 . 1 1 30 30 TYR HA H 1 5.092 0.030 . 1 . . . . 30 TYR HA . 10269 1 313 . 1 1 30 30 TYR HB2 H 1 2.863 0.030 . 2 . . . . 30 TYR HB2 . 10269 1 314 . 1 1 30 30 TYR HB3 H 1 2.671 0.030 . 2 . . . . 30 TYR HB3 . 10269 1 315 . 1 1 30 30 TYR HD1 H 1 6.968 0.030 . 1 . . . . 30 TYR HD1 . 10269 1 316 . 1 1 30 30 TYR HD2 H 1 6.968 0.030 . 1 . . . . 30 TYR HD2 . 10269 1 317 . 1 1 30 30 TYR HE1 H 1 6.503 0.030 . 1 . . . . 30 TYR HE1 . 10269 1 318 . 1 1 30 30 TYR HE2 H 1 6.503 0.030 . 1 . . . . 30 TYR HE2 . 10269 1 319 . 1 1 30 30 TYR C C 13 173.451 0.300 . 1 . . . . 30 TYR C . 10269 1 320 . 1 1 30 30 TYR CA C 13 57.627 0.300 . 1 . . . . 30 TYR CA . 10269 1 321 . 1 1 30 30 TYR CB C 13 41.124 0.300 . 1 . . . . 30 TYR CB . 10269 1 322 . 1 1 30 30 TYR CD1 C 13 133.274 0.300 . 1 . . . . 30 TYR CD1 . 10269 1 323 . 1 1 30 30 TYR CD2 C 13 133.274 0.300 . 1 . . . . 30 TYR CD2 . 10269 1 324 . 1 1 30 30 TYR CE1 C 13 116.851 0.300 . 1 . . . . 30 TYR CE1 . 10269 1 325 . 1 1 30 30 TYR CE2 C 13 116.851 0.300 . 1 . . . . 30 TYR CE2 . 10269 1 326 . 1 1 30 30 TYR N N 15 119.246 0.300 . 1 . . . . 30 TYR N . 10269 1 327 . 1 1 31 31 LEU H H 1 7.804 0.030 . 1 . . . . 31 LEU H . 10269 1 328 . 1 1 31 31 LEU HA H 1 3.561 0.030 . 1 . . . . 31 LEU HA . 10269 1 329 . 1 1 31 31 LEU HB2 H 1 0.657 0.030 . 2 . . . . 31 LEU HB2 . 10269 1 330 . 1 1 31 31 LEU HB3 H 1 -1.658 0.030 . 2 . . . . 31 LEU HB3 . 10269 1 331 . 1 1 31 31 LEU HD11 H 1 0.341 0.030 . 1 . . . . 31 LEU HD1 . 10269 1 332 . 1 1 31 31 LEU HD12 H 1 0.341 0.030 . 1 . . . . 31 LEU HD1 . 10269 1 333 . 1 1 31 31 LEU HD13 H 1 0.341 0.030 . 1 . . . . 31 LEU HD1 . 10269 1 334 . 1 1 31 31 LEU HD21 H 1 -0.623 0.030 . 1 . . . . 31 LEU HD2 . 10269 1 335 . 1 1 31 31 LEU HD22 H 1 -0.623 0.030 . 1 . . . . 31 LEU HD2 . 10269 1 336 . 1 1 31 31 LEU HD23 H 1 -0.623 0.030 . 1 . . . . 31 LEU HD2 . 10269 1 337 . 1 1 31 31 LEU HG H 1 0.519 0.030 . 1 . . . . 31 LEU HG . 10269 1 338 . 1 1 31 31 LEU C C 13 173.742 0.300 . 1 . . . . 31 LEU C . 10269 1 339 . 1 1 31 31 LEU CA C 13 53.120 0.300 . 1 . . . . 31 LEU CA . 10269 1 340 . 1 1 31 31 LEU CB C 13 39.479 0.300 . 1 . . . . 31 LEU CB . 10269 1 341 . 1 1 31 31 LEU CD1 C 13 25.433 0.300 . 2 . . . . 31 LEU CD1 . 10269 1 342 . 1 1 31 31 LEU CD2 C 13 19.751 0.300 . 2 . . . . 31 LEU CD2 . 10269 1 343 . 1 1 31 31 LEU CG C 13 26.143 0.300 . 1 . . . . 31 LEU CG . 10269 1 344 . 1 1 31 31 LEU N N 15 125.982 0.300 . 1 . . . . 31 LEU N . 10269 1 345 . 1 1 32 32 ILE H H 1 8.861 0.030 . 1 . . . . 32 ILE H . 10269 1 346 . 1 1 32 32 ILE HA H 1 3.402 0.030 . 1 . . . . 32 ILE HA . 10269 1 347 . 1 1 32 32 ILE HB H 1 1.066 0.030 . 1 . . . . 32 ILE HB . 10269 1 348 . 1 1 32 32 ILE HD11 H 1 0.244 0.030 . 1 . . . . 32 ILE HD1 . 10269 1 349 . 1 1 32 32 ILE HD12 H 1 0.244 0.030 . 1 . . . . 32 ILE HD1 . 10269 1 350 . 1 1 32 32 ILE HD13 H 1 0.244 0.030 . 1 . . . . 32 ILE HD1 . 10269 1 351 . 1 1 32 32 ILE HG12 H 1 1.133 0.030 . 2 . . . . 32 ILE HG12 . 10269 1 352 . 1 1 32 32 ILE HG13 H 1 0.497 0.030 . 2 . . . . 32 ILE HG13 . 10269 1 353 . 1 1 32 32 ILE HG21 H 1 -1.137 0.030 . 1 . . . . 32 ILE HG2 . 10269 1 354 . 1 1 32 32 ILE HG22 H 1 -1.137 0.030 . 1 . . . . 32 ILE HG2 . 10269 1 355 . 1 1 32 32 ILE HG23 H 1 -1.137 0.030 . 1 . . . . 32 ILE HG2 . 10269 1 356 . 1 1 32 32 ILE C C 13 173.769 0.300 . 1 . . . . 32 ILE C . 10269 1 357 . 1 1 32 32 ILE CA C 13 61.356 0.300 . 1 . . . . 32 ILE CA . 10269 1 358 . 1 1 32 32 ILE CB C 13 39.405 0.300 . 1 . . . . 32 ILE CB . 10269 1 359 . 1 1 32 32 ILE CD1 C 13 12.668 0.300 . 1 . . . . 32 ILE CD1 . 10269 1 360 . 1 1 32 32 ILE CG1 C 13 27.649 0.300 . 1 . . . . 32 ILE CG1 . 10269 1 361 . 1 1 32 32 ILE CG2 C 13 16.400 0.300 . 1 . . . . 32 ILE CG2 . 10269 1 362 . 1 1 32 32 ILE N N 15 129.827 0.300 . 1 . . . . 32 ILE N . 10269 1 363 . 1 1 33 33 LYS H H 1 7.951 0.030 . 1 . . . . 33 LYS H . 10269 1 364 . 1 1 33 33 LYS HA H 1 4.111 0.030 . 1 . . . . 33 LYS HA . 10269 1 365 . 1 1 33 33 LYS HB2 H 1 1.732 0.030 . 2 . . . . 33 LYS HB2 . 10269 1 366 . 1 1 33 33 LYS HB3 H 1 1.302 0.030 . 2 . . . . 33 LYS HB3 . 10269 1 367 . 1 1 33 33 LYS HD2 H 1 1.322 0.030 . 2 . . . . 33 LYS HD2 . 10269 1 368 . 1 1 33 33 LYS HD3 H 1 1.273 0.030 . 2 . . . . 33 LYS HD3 . 10269 1 369 . 1 1 33 33 LYS HE2 H 1 2.737 0.030 . 2 . . . . 33 LYS HE2 . 10269 1 370 . 1 1 33 33 LYS HE3 H 1 2.668 0.030 . 2 . . . . 33 LYS HE3 . 10269 1 371 . 1 1 33 33 LYS HG2 H 1 1.194 0.030 . 1 . . . . 33 LYS HG2 . 10269 1 372 . 1 1 33 33 LYS HG3 H 1 1.194 0.030 . 1 . . . . 33 LYS HG3 . 10269 1 373 . 1 1 33 33 LYS C C 13 174.920 0.300 . 1 . . . . 33 LYS C . 10269 1 374 . 1 1 33 33 LYS CA C 13 54.849 0.300 . 1 . . . . 33 LYS CA . 10269 1 375 . 1 1 33 33 LYS CB C 13 33.162 0.300 . 1 . . . . 33 LYS CB . 10269 1 376 . 1 1 33 33 LYS CD C 13 29.140 0.300 . 1 . . . . 33 LYS CD . 10269 1 377 . 1 1 33 33 LYS CE C 13 42.656 0.300 . 1 . . . . 33 LYS CE . 10269 1 378 . 1 1 33 33 LYS CG C 13 26.125 0.300 . 1 . . . . 33 LYS CG . 10269 1 379 . 1 1 33 33 LYS N N 15 124.612 0.300 . 1 . . . . 33 LYS N . 10269 1 380 . 1 1 34 34 TRP H H 1 8.145 0.030 . 1 . . . . 34 TRP H . 10269 1 381 . 1 1 34 34 TRP HA H 1 4.690 0.030 . 1 . . . . 34 TRP HA . 10269 1 382 . 1 1 34 34 TRP HB2 H 1 3.446 0.030 . 2 . . . . 34 TRP HB2 . 10269 1 383 . 1 1 34 34 TRP HB3 H 1 2.851 0.030 . 2 . . . . 34 TRP HB3 . 10269 1 384 . 1 1 34 34 TRP HD1 H 1 7.208 0.030 . 1 . . . . 34 TRP HD1 . 10269 1 385 . 1 1 34 34 TRP HE1 H 1 10.514 0.030 . 1 . . . . 34 TRP HE1 . 10269 1 386 . 1 1 34 34 TRP HE3 H 1 7.171 0.030 . 1 . . . . 34 TRP HE3 . 10269 1 387 . 1 1 34 34 TRP HH2 H 1 6.666 0.030 . 1 . . . . 34 TRP HH2 . 10269 1 388 . 1 1 34 34 TRP HZ2 H 1 7.246 0.030 . 1 . . . . 34 TRP HZ2 . 10269 1 389 . 1 1 34 34 TRP HZ3 H 1 6.482 0.030 . 1 . . . . 34 TRP HZ3 . 10269 1 390 . 1 1 34 34 TRP C C 13 177.144 0.300 . 1 . . . . 34 TRP C . 10269 1 391 . 1 1 34 34 TRP CA C 13 55.582 0.300 . 1 . . . . 34 TRP CA . 10269 1 392 . 1 1 34 34 TRP CB C 13 30.832 0.300 . 1 . . . . 34 TRP CB . 10269 1 393 . 1 1 34 34 TRP CD1 C 13 128.077 0.300 . 1 . . . . 34 TRP CD1 . 10269 1 394 . 1 1 34 34 TRP CE3 C 13 120.604 0.300 . 1 . . . . 34 TRP CE3 . 10269 1 395 . 1 1 34 34 TRP CH2 C 13 123.495 0.300 . 1 . . . . 34 TRP CH2 . 10269 1 396 . 1 1 34 34 TRP CZ2 C 13 113.821 0.300 . 1 . . . . 34 TRP CZ2 . 10269 1 397 . 1 1 34 34 TRP CZ3 C 13 120.880 0.300 . 1 . . . . 34 TRP CZ3 . 10269 1 398 . 1 1 34 34 TRP N N 15 132.766 0.300 . 1 . . . . 34 TRP N . 10269 1 399 . 1 1 34 34 TRP NE1 N 15 130.136 0.300 . 1 . . . . 34 TRP NE1 . 10269 1 400 . 1 1 35 35 ARG H H 1 9.199 0.030 . 1 . . . . 35 ARG H . 10269 1 401 . 1 1 35 35 ARG HA H 1 3.742 0.030 . 1 . . . . 35 ARG HA . 10269 1 402 . 1 1 35 35 ARG HB2 H 1 1.706 0.030 . 2 . . . . 35 ARG HB2 . 10269 1 403 . 1 1 35 35 ARG HB3 H 1 1.569 0.030 . 2 . . . . 35 ARG HB3 . 10269 1 404 . 1 1 35 35 ARG HD2 H 1 3.043 0.030 . 1 . . . . 35 ARG HD2 . 10269 1 405 . 1 1 35 35 ARG HD3 H 1 3.043 0.030 . 1 . . . . 35 ARG HD3 . 10269 1 406 . 1 1 35 35 ARG HG2 H 1 1.375 0.030 . 2 . . . . 35 ARG HG2 . 10269 1 407 . 1 1 35 35 ARG HG3 H 1 1.306 0.030 . 2 . . . . 35 ARG HG3 . 10269 1 408 . 1 1 35 35 ARG C C 13 176.307 0.300 . 1 . . . . 35 ARG C . 10269 1 409 . 1 1 35 35 ARG CA C 13 58.738 0.300 . 1 . . . . 35 ARG CA . 10269 1 410 . 1 1 35 35 ARG CB C 13 30.254 0.300 . 1 . . . . 35 ARG CB . 10269 1 411 . 1 1 35 35 ARG CD C 13 43.349 0.300 . 1 . . . . 35 ARG CD . 10269 1 412 . 1 1 35 35 ARG CG C 13 26.951 0.300 . 1 . . . . 35 ARG CG . 10269 1 413 . 1 1 35 35 ARG N N 15 124.433 0.300 . 1 . . . . 35 ARG N . 10269 1 414 . 1 1 36 36 ASP H H 1 8.812 0.030 . 1 . . . . 36 ASP H . 10269 1 415 . 1 1 36 36 ASP HA H 1 4.294 0.030 . 1 . . . . 36 ASP HA . 10269 1 416 . 1 1 36 36 ASP HB2 H 1 2.903 0.030 . 2 . . . . 36 ASP HB2 . 10269 1 417 . 1 1 36 36 ASP HB3 H 1 2.806 0.030 . 2 . . . . 36 ASP HB3 . 10269 1 418 . 1 1 36 36 ASP C C 13 174.269 0.300 . 1 . . . . 36 ASP C . 10269 1 419 . 1 1 36 36 ASP CA C 13 55.948 0.300 . 1 . . . . 36 ASP CA . 10269 1 420 . 1 1 36 36 ASP CB C 13 39.960 0.300 . 1 . . . . 36 ASP CB . 10269 1 421 . 1 1 36 36 ASP N N 15 115.622 0.300 . 1 . . . . 36 ASP N . 10269 1 422 . 1 1 37 37 LEU H H 1 7.372 0.030 . 1 . . . . 37 LEU H . 10269 1 423 . 1 1 37 37 LEU HA H 1 4.966 0.030 . 1 . . . . 37 LEU HA . 10269 1 424 . 1 1 37 37 LEU HB2 H 1 1.711 0.030 . 2 . . . . 37 LEU HB2 . 10269 1 425 . 1 1 37 37 LEU HB3 H 1 1.346 0.030 . 2 . . . . 37 LEU HB3 . 10269 1 426 . 1 1 37 37 LEU HD11 H 1 0.812 0.030 . 1 . . . . 37 LEU HD1 . 10269 1 427 . 1 1 37 37 LEU HD12 H 1 0.812 0.030 . 1 . . . . 37 LEU HD1 . 10269 1 428 . 1 1 37 37 LEU HD13 H 1 0.812 0.030 . 1 . . . . 37 LEU HD1 . 10269 1 429 . 1 1 37 37 LEU HD21 H 1 0.909 0.030 . 1 . . . . 37 LEU HD2 . 10269 1 430 . 1 1 37 37 LEU HD22 H 1 0.909 0.030 . 1 . . . . 37 LEU HD2 . 10269 1 431 . 1 1 37 37 LEU HD23 H 1 0.909 0.030 . 1 . . . . 37 LEU HD2 . 10269 1 432 . 1 1 37 37 LEU HG H 1 1.586 0.030 . 1 . . . . 37 LEU HG . 10269 1 433 . 1 1 37 37 LEU C C 13 174.638 0.300 . 1 . . . . 37 LEU C . 10269 1 434 . 1 1 37 37 LEU CA C 13 51.968 0.300 . 1 . . . . 37 LEU CA . 10269 1 435 . 1 1 37 37 LEU CB C 13 44.421 0.300 . 1 . . . . 37 LEU CB . 10269 1 436 . 1 1 37 37 LEU CD1 C 13 25.483 0.300 . 2 . . . . 37 LEU CD1 . 10269 1 437 . 1 1 37 37 LEU CD2 C 13 23.199 0.300 . 2 . . . . 37 LEU CD2 . 10269 1 438 . 1 1 37 37 LEU CG C 13 27.043 0.300 . 1 . . . . 37 LEU CG . 10269 1 439 . 1 1 37 37 LEU N N 15 119.137 0.300 . 1 . . . . 37 LEU N . 10269 1 440 . 1 1 38 38 PRO HA H 1 4.559 0.030 . 1 . . . . 38 PRO HA . 10269 1 441 . 1 1 38 38 PRO HB2 H 1 2.442 0.030 . 2 . . . . 38 PRO HB2 . 10269 1 442 . 1 1 38 38 PRO HB3 H 1 2.171 0.030 . 2 . . . . 38 PRO HB3 . 10269 1 443 . 1 1 38 38 PRO HD2 H 1 3.812 0.030 . 2 . . . . 38 PRO HD2 . 10269 1 444 . 1 1 38 38 PRO HD3 H 1 3.444 0.030 . 2 . . . . 38 PRO HD3 . 10269 1 445 . 1 1 38 38 PRO HG2 H 1 2.048 0.030 . 2 . . . . 38 PRO HG2 . 10269 1 446 . 1 1 38 38 PRO HG3 H 1 1.990 0.030 . 2 . . . . 38 PRO HG3 . 10269 1 447 . 1 1 38 38 PRO C C 13 178.256 0.300 . 1 . . . . 38 PRO C . 10269 1 448 . 1 1 38 38 PRO CA C 13 62.332 0.300 . 1 . . . . 38 PRO CA . 10269 1 449 . 1 1 38 38 PRO CB C 13 33.232 0.300 . 1 . . . . 38 PRO CB . 10269 1 450 . 1 1 38 38 PRO CD C 13 50.632 0.300 . 1 . . . . 38 PRO CD . 10269 1 451 . 1 1 38 38 PRO CG C 13 27.804 0.300 . 1 . . . . 38 PRO CG . 10269 1 452 . 1 1 39 39 TYR H H 1 8.933 0.030 . 1 . . . . 39 TYR H . 10269 1 453 . 1 1 39 39 TYR HA H 1 3.758 0.030 . 1 . . . . 39 TYR HA . 10269 1 454 . 1 1 39 39 TYR HB2 H 1 3.030 0.030 . 2 . . . . 39 TYR HB2 . 10269 1 455 . 1 1 39 39 TYR HB3 H 1 2.949 0.030 . 2 . . . . 39 TYR HB3 . 10269 1 456 . 1 1 39 39 TYR HD1 H 1 7.062 0.030 . 1 . . . . 39 TYR HD1 . 10269 1 457 . 1 1 39 39 TYR HD2 H 1 7.062 0.030 . 1 . . . . 39 TYR HD2 . 10269 1 458 . 1 1 39 39 TYR HE1 H 1 6.722 0.030 . 1 . . . . 39 TYR HE1 . 10269 1 459 . 1 1 39 39 TYR HE2 H 1 6.722 0.030 . 1 . . . . 39 TYR HE2 . 10269 1 460 . 1 1 39 39 TYR C C 13 177.241 0.300 . 1 . . . . 39 TYR C . 10269 1 461 . 1 1 39 39 TYR CA C 13 62.934 0.300 . 1 . . . . 39 TYR CA . 10269 1 462 . 1 1 39 39 TYR CB C 13 38.451 0.300 . 1 . . . . 39 TYR CB . 10269 1 463 . 1 1 39 39 TYR CD1 C 13 132.901 0.300 . 1 . . . . 39 TYR CD1 . 10269 1 464 . 1 1 39 39 TYR CD2 C 13 132.901 0.300 . 1 . . . . 39 TYR CD2 . 10269 1 465 . 1 1 39 39 TYR CE1 C 13 118.389 0.300 . 1 . . . . 39 TYR CE1 . 10269 1 466 . 1 1 39 39 TYR CE2 C 13 118.389 0.300 . 1 . . . . 39 TYR CE2 . 10269 1 467 . 1 1 39 39 TYR N N 15 122.113 0.300 . 1 . . . . 39 TYR N . 10269 1 468 . 1 1 40 40 ASP H H 1 8.439 0.030 . 1 . . . . 40 ASP H . 10269 1 469 . 1 1 40 40 ASP HA H 1 4.407 0.030 . 1 . . . . 40 ASP HA . 10269 1 470 . 1 1 40 40 ASP HB2 H 1 2.844 0.030 . 2 . . . . 40 ASP HB2 . 10269 1 471 . 1 1 40 40 ASP HB3 H 1 2.632 0.030 . 2 . . . . 40 ASP HB3 . 10269 1 472 . 1 1 40 40 ASP C C 13 176.645 0.300 . 1 . . . . 40 ASP C . 10269 1 473 . 1 1 40 40 ASP CA C 13 55.335 0.300 . 1 . . . . 40 ASP CA . 10269 1 474 . 1 1 40 40 ASP CB C 13 39.476 0.300 . 1 . . . . 40 ASP CB . 10269 1 475 . 1 1 40 40 ASP N N 15 115.019 0.300 . 1 . . . . 40 ASP N . 10269 1 476 . 1 1 41 41 GLN H H 1 7.761 0.030 . 1 . . . . 41 GLN H . 10269 1 477 . 1 1 41 41 GLN HA H 1 4.457 0.030 . 1 . . . . 41 GLN HA . 10269 1 478 . 1 1 41 41 GLN HB2 H 1 2.558 0.030 . 2 . . . . 41 GLN HB2 . 10269 1 479 . 1 1 41 41 GLN HB3 H 1 1.701 0.030 . 2 . . . . 41 GLN HB3 . 10269 1 480 . 1 1 41 41 GLN HE21 H 1 7.760 0.030 . 2 . . . . 41 GLN HE21 . 10269 1 481 . 1 1 41 41 GLN HE22 H 1 6.753 0.030 . 2 . . . . 41 GLN HE22 . 10269 1 482 . 1 1 41 41 GLN HG2 H 1 2.314 0.030 . 1 . . . . 41 GLN HG2 . 10269 1 483 . 1 1 41 41 GLN HG3 H 1 2.314 0.030 . 1 . . . . 41 GLN HG3 . 10269 1 484 . 1 1 41 41 GLN C C 13 175.665 0.300 . 1 . . . . 41 GLN C . 10269 1 485 . 1 1 41 41 GLN CA C 13 55.031 0.300 . 1 . . . . 41 GLN CA . 10269 1 486 . 1 1 41 41 GLN CB C 13 29.606 0.300 . 1 . . . . 41 GLN CB . 10269 1 487 . 1 1 41 41 GLN CG C 13 34.449 0.300 . 1 . . . . 41 GLN CG . 10269 1 488 . 1 1 41 41 GLN N N 15 117.630 0.300 . 1 . . . . 41 GLN N . 10269 1 489 . 1 1 41 41 GLN NE2 N 15 112.841 0.300 . 1 . . . . 41 GLN NE2 . 10269 1 490 . 1 1 42 42 ALA H H 1 7.379 0.030 . 1 . . . . 42 ALA H . 10269 1 491 . 1 1 42 42 ALA HA H 1 4.776 0.030 . 1 . . . . 42 ALA HA . 10269 1 492 . 1 1 42 42 ALA HB1 H 1 0.908 0.030 . 1 . . . . 42 ALA HB . 10269 1 493 . 1 1 42 42 ALA HB2 H 1 0.908 0.030 . 1 . . . . 42 ALA HB . 10269 1 494 . 1 1 42 42 ALA HB3 H 1 0.908 0.030 . 1 . . . . 42 ALA HB . 10269 1 495 . 1 1 42 42 ALA C C 13 177.103 0.300 . 1 . . . . 42 ALA C . 10269 1 496 . 1 1 42 42 ALA CA C 13 53.572 0.300 . 1 . . . . 42 ALA CA . 10269 1 497 . 1 1 42 42 ALA CB C 13 18.951 0.300 . 1 . . . . 42 ALA CB . 10269 1 498 . 1 1 42 42 ALA N N 15 123.425 0.300 . 1 . . . . 42 ALA N . 10269 1 499 . 1 1 43 43 SER H H 1 8.521 0.030 . 1 . . . . 43 SER H . 10269 1 500 . 1 1 43 43 SER HA H 1 4.861 0.030 . 1 . . . . 43 SER HA . 10269 1 501 . 1 1 43 43 SER HB2 H 1 4.202 0.030 . 2 . . . . 43 SER HB2 . 10269 1 502 . 1 1 43 43 SER HB3 H 1 3.846 0.030 . 2 . . . . 43 SER HB3 . 10269 1 503 . 1 1 43 43 SER C C 13 172.947 0.300 . 1 . . . . 43 SER C . 10269 1 504 . 1 1 43 43 SER CA C 13 56.852 0.300 . 1 . . . . 43 SER CA . 10269 1 505 . 1 1 43 43 SER CB C 13 66.734 0.300 . 1 . . . . 43 SER CB . 10269 1 506 . 1 1 43 43 SER N N 15 115.967 0.300 . 1 . . . . 43 SER N . 10269 1 507 . 1 1 44 44 TRP H H 1 8.699 0.030 . 1 . . . . 44 TRP H . 10269 1 508 . 1 1 44 44 TRP HA H 1 5.081 0.030 . 1 . . . . 44 TRP HA . 10269 1 509 . 1 1 44 44 TRP HB2 H 1 3.033 0.030 . 2 . . . . 44 TRP HB2 . 10269 1 510 . 1 1 44 44 TRP HB3 H 1 2.866 0.030 . 2 . . . . 44 TRP HB3 . 10269 1 511 . 1 1 44 44 TRP HD1 H 1 7.258 0.030 . 1 . . . . 44 TRP HD1 . 10269 1 512 . 1 1 44 44 TRP HE1 H 1 10.186 0.030 . 1 . . . . 44 TRP HE1 . 10269 1 513 . 1 1 44 44 TRP HE3 H 1 6.628 0.030 . 1 . . . . 44 TRP HE3 . 10269 1 514 . 1 1 44 44 TRP HH2 H 1 6.630 0.030 . 1 . . . . 44 TRP HH2 . 10269 1 515 . 1 1 44 44 TRP HZ2 H 1 7.366 0.030 . 1 . . . . 44 TRP HZ2 . 10269 1 516 . 1 1 44 44 TRP HZ3 H 1 7.020 0.030 . 1 . . . . 44 TRP HZ3 . 10269 1 517 . 1 1 44 44 TRP C C 13 177.207 0.300 . 1 . . . . 44 TRP C . 10269 1 518 . 1 1 44 44 TRP CA C 13 56.648 0.300 . 1 . . . . 44 TRP CA . 10269 1 519 . 1 1 44 44 TRP CB C 13 29.592 0.300 . 1 . . . . 44 TRP CB . 10269 1 520 . 1 1 44 44 TRP CD1 C 13 127.735 0.300 . 1 . . . . 44 TRP CD1 . 10269 1 521 . 1 1 44 44 TRP CE3 C 13 122.256 0.300 . 1 . . . . 44 TRP CE3 . 10269 1 522 . 1 1 44 44 TRP CH2 C 13 122.666 0.300 . 1 . . . . 44 TRP CH2 . 10269 1 523 . 1 1 44 44 TRP CZ2 C 13 115.195 0.300 . 1 . . . . 44 TRP CZ2 . 10269 1 524 . 1 1 44 44 TRP CZ3 C 13 119.695 0.300 . 1 . . . . 44 TRP CZ3 . 10269 1 525 . 1 1 44 44 TRP N N 15 123.015 0.300 . 1 . . . . 44 TRP N . 10269 1 526 . 1 1 44 44 TRP NE1 N 15 130.168 0.300 . 1 . . . . 44 TRP NE1 . 10269 1 527 . 1 1 45 45 GLU H H 1 9.773 0.030 . 1 . . . . 45 GLU H . 10269 1 528 . 1 1 45 45 GLU HA H 1 5.156 0.030 . 1 . . . . 45 GLU HA . 10269 1 529 . 1 1 45 45 GLU HB2 H 1 2.291 0.030 . 2 . . . . 45 GLU HB2 . 10269 1 530 . 1 1 45 45 GLU HB3 H 1 1.736 0.030 . 2 . . . . 45 GLU HB3 . 10269 1 531 . 1 1 45 45 GLU HG2 H 1 2.435 0.030 . 2 . . . . 45 GLU HG2 . 10269 1 532 . 1 1 45 45 GLU HG3 H 1 2.263 0.030 . 2 . . . . 45 GLU HG3 . 10269 1 533 . 1 1 45 45 GLU C C 13 176.249 0.300 . 1 . . . . 45 GLU C . 10269 1 534 . 1 1 45 45 GLU CA C 13 53.378 0.300 . 1 . . . . 45 GLU CA . 10269 1 535 . 1 1 45 45 GLU CB C 13 31.950 0.300 . 1 . . . . 45 GLU CB . 10269 1 536 . 1 1 45 45 GLU CG C 13 34.985 0.300 . 1 . . . . 45 GLU CG . 10269 1 537 . 1 1 45 45 GLU N N 15 122.799 0.300 . 1 . . . . 45 GLU N . 10269 1 538 . 1 1 46 46 SER H H 1 9.121 0.030 . 1 . . . . 46 SER H . 10269 1 539 . 1 1 46 46 SER HA H 1 4.106 0.030 . 1 . . . . 46 SER HA . 10269 1 540 . 1 1 46 46 SER HB2 H 1 4.119 0.030 . 2 . . . . 46 SER HB2 . 10269 1 541 . 1 1 46 46 SER HB3 H 1 3.884 0.030 . 2 . . . . 46 SER HB3 . 10269 1 542 . 1 1 46 46 SER C C 13 178.218 0.300 . 1 . . . . 46 SER C . 10269 1 543 . 1 1 46 46 SER CA C 13 58.791 0.300 . 1 . . . . 46 SER CA . 10269 1 544 . 1 1 46 46 SER CB C 13 63.100 0.300 . 1 . . . . 46 SER CB . 10269 1 545 . 1 1 46 46 SER N N 15 116.892 0.300 . 1 . . . . 46 SER N . 10269 1 546 . 1 1 47 47 GLU H H 1 8.588 0.030 . 1 . . . . 47 GLU H . 10269 1 547 . 1 1 47 47 GLU HA H 1 4.327 0.030 . 1 . . . . 47 GLU HA . 10269 1 548 . 1 1 47 47 GLU HB2 H 1 2.189 0.030 . 2 . . . . 47 GLU HB2 . 10269 1 549 . 1 1 47 47 GLU HB3 H 1 2.104 0.030 . 2 . . . . 47 GLU HB3 . 10269 1 550 . 1 1 47 47 GLU HG2 H 1 2.290 0.030 . 2 . . . . 47 GLU HG2 . 10269 1 551 . 1 1 47 47 GLU HG3 H 1 2.112 0.030 . 2 . . . . 47 GLU HG3 . 10269 1 552 . 1 1 47 47 GLU C C 13 174.707 0.300 . 1 . . . . 47 GLU C . 10269 1 553 . 1 1 47 47 GLU CA C 13 58.693 0.300 . 1 . . . . 47 GLU CA . 10269 1 554 . 1 1 47 47 GLU CB C 13 29.990 0.300 . 1 . . . . 47 GLU CB . 10269 1 555 . 1 1 47 47 GLU CG C 13 34.620 0.300 . 1 . . . . 47 GLU CG . 10269 1 556 . 1 1 47 47 GLU N N 15 125.534 0.300 . 1 . . . . 47 GLU N . 10269 1 557 . 1 1 48 48 ASP H H 1 8.415 0.030 . 1 . . . . 48 ASP H . 10269 1 558 . 1 1 48 48 ASP HA H 1 4.847 0.030 . 1 . . . . 48 ASP HA . 10269 1 559 . 1 1 48 48 ASP HB2 H 1 2.829 0.030 . 2 . . . . 48 ASP HB2 . 10269 1 560 . 1 1 48 48 ASP HB3 H 1 2.616 0.030 . 2 . . . . 48 ASP HB3 . 10269 1 561 . 1 1 48 48 ASP C C 13 176.853 0.300 . 1 . . . . 48 ASP C . 10269 1 562 . 1 1 48 48 ASP CA C 13 54.472 0.300 . 1 . . . . 48 ASP CA . 10269 1 563 . 1 1 48 48 ASP CB C 13 41.795 0.300 . 1 . . . . 48 ASP CB . 10269 1 564 . 1 1 48 48 ASP N N 15 117.812 0.300 . 1 . . . . 48 ASP N . 10269 1 565 . 1 1 49 49 VAL H H 1 7.192 0.030 . 1 . . . . 49 VAL H . 10269 1 566 . 1 1 49 49 VAL HA H 1 4.137 0.030 . 1 . . . . 49 VAL HA . 10269 1 567 . 1 1 49 49 VAL HB H 1 2.146 0.030 . 1 . . . . 49 VAL HB . 10269 1 568 . 1 1 49 49 VAL HG11 H 1 1.089 0.030 . 1 . . . . 49 VAL HG1 . 10269 1 569 . 1 1 49 49 VAL HG12 H 1 1.089 0.030 . 1 . . . . 49 VAL HG1 . 10269 1 570 . 1 1 49 49 VAL HG13 H 1 1.089 0.030 . 1 . . . . 49 VAL HG1 . 10269 1 571 . 1 1 49 49 VAL HG21 H 1 1.206 0.030 . 1 . . . . 49 VAL HG2 . 10269 1 572 . 1 1 49 49 VAL HG22 H 1 1.206 0.030 . 1 . . . . 49 VAL HG2 . 10269 1 573 . 1 1 49 49 VAL HG23 H 1 1.206 0.030 . 1 . . . . 49 VAL HG2 . 10269 1 574 . 1 1 49 49 VAL C C 13 175.326 0.300 . 1 . . . . 49 VAL C . 10269 1 575 . 1 1 49 49 VAL CA C 13 62.987 0.300 . 1 . . . . 49 VAL CA . 10269 1 576 . 1 1 49 49 VAL CB C 13 32.759 0.300 . 1 . . . . 49 VAL CB . 10269 1 577 . 1 1 49 49 VAL CG1 C 13 21.942 0.300 . 2 . . . . 49 VAL CG1 . 10269 1 578 . 1 1 49 49 VAL CG2 C 13 21.485 0.300 . 2 . . . . 49 VAL CG2 . 10269 1 579 . 1 1 49 49 VAL N N 15 118.329 0.300 . 1 . . . . 49 VAL N . 10269 1 580 . 1 1 50 50 GLU H H 1 8.417 0.030 . 1 . . . . 50 GLU H . 10269 1 581 . 1 1 50 50 GLU HA H 1 4.526 0.030 . 1 . . . . 50 GLU HA . 10269 1 582 . 1 1 50 50 GLU HB2 H 1 2.006 0.030 . 2 . . . . 50 GLU HB2 . 10269 1 583 . 1 1 50 50 GLU HB3 H 1 1.949 0.030 . 2 . . . . 50 GLU HB3 . 10269 1 584 . 1 1 50 50 GLU HG2 H 1 2.285 0.030 . 2 . . . . 50 GLU HG2 . 10269 1 585 . 1 1 50 50 GLU HG3 H 1 2.189 0.030 . 2 . . . . 50 GLU HG3 . 10269 1 586 . 1 1 50 50 GLU C C 13 175.395 0.300 . 1 . . . . 50 GLU C . 10269 1 587 . 1 1 50 50 GLU CA C 13 56.376 0.300 . 1 . . . . 50 GLU CA . 10269 1 588 . 1 1 50 50 GLU CB C 13 29.216 0.300 . 1 . . . . 50 GLU CB . 10269 1 589 . 1 1 50 50 GLU CG C 13 36.229 0.300 . 1 . . . . 50 GLU CG . 10269 1 590 . 1 1 50 50 GLU N N 15 124.475 0.300 . 1 . . . . 50 GLU N . 10269 1 591 . 1 1 51 51 ILE H H 1 7.483 0.030 . 1 . . . . 51 ILE H . 10269 1 592 . 1 1 51 51 ILE HA H 1 4.068 0.030 . 1 . . . . 51 ILE HA . 10269 1 593 . 1 1 51 51 ILE HB H 1 0.819 0.030 . 1 . . . . 51 ILE HB . 10269 1 594 . 1 1 51 51 ILE HD11 H 1 -0.032 0.030 . 1 . . . . 51 ILE HD1 . 10269 1 595 . 1 1 51 51 ILE HD12 H 1 -0.032 0.030 . 1 . . . . 51 ILE HD1 . 10269 1 596 . 1 1 51 51 ILE HD13 H 1 -0.032 0.030 . 1 . . . . 51 ILE HD1 . 10269 1 597 . 1 1 51 51 ILE HG12 H 1 1.063 0.030 . 2 . . . . 51 ILE HG12 . 10269 1 598 . 1 1 51 51 ILE HG13 H 1 0.550 0.030 . 2 . . . . 51 ILE HG13 . 10269 1 599 . 1 1 51 51 ILE HG21 H 1 0.892 0.030 . 1 . . . . 51 ILE HG2 . 10269 1 600 . 1 1 51 51 ILE HG22 H 1 0.892 0.030 . 1 . . . . 51 ILE HG2 . 10269 1 601 . 1 1 51 51 ILE HG23 H 1 0.892 0.030 . 1 . . . . 51 ILE HG2 . 10269 1 602 . 1 1 51 51 ILE C C 13 175.838 0.300 . 1 . . . . 51 ILE C . 10269 1 603 . 1 1 51 51 ILE CA C 13 60.572 0.300 . 1 . . . . 51 ILE CA . 10269 1 604 . 1 1 51 51 ILE CB C 13 41.701 0.300 . 1 . . . . 51 ILE CB . 10269 1 605 . 1 1 51 51 ILE CD1 C 13 13.256 0.300 . 1 . . . . 51 ILE CD1 . 10269 1 606 . 1 1 51 51 ILE CG1 C 13 27.554 0.300 . 1 . . . . 51 ILE CG1 . 10269 1 607 . 1 1 51 51 ILE CG2 C 13 18.103 0.300 . 1 . . . . 51 ILE CG2 . 10269 1 608 . 1 1 51 51 ILE N N 15 125.565 0.300 . 1 . . . . 51 ILE N . 10269 1 609 . 1 1 52 52 GLN H H 1 9.055 0.030 . 1 . . . . 52 GLN H . 10269 1 610 . 1 1 52 52 GLN HA H 1 4.042 0.030 . 1 . . . . 52 GLN HA . 10269 1 611 . 1 1 52 52 GLN HB2 H 1 2.154 0.030 . 2 . . . . 52 GLN HB2 . 10269 1 612 . 1 1 52 52 GLN HB3 H 1 2.015 0.030 . 2 . . . . 52 GLN HB3 . 10269 1 613 . 1 1 52 52 GLN HE21 H 1 7.615 0.030 . 2 . . . . 52 GLN HE21 . 10269 1 614 . 1 1 52 52 GLN HE22 H 1 6.876 0.030 . 2 . . . . 52 GLN HE22 . 10269 1 615 . 1 1 52 52 GLN HG2 H 1 2.355 0.030 . 1 . . . . 52 GLN HG2 . 10269 1 616 . 1 1 52 52 GLN HG3 H 1 2.355 0.030 . 1 . . . . 52 GLN HG3 . 10269 1 617 . 1 1 52 52 GLN C C 13 176.011 0.300 . 1 . . . . 52 GLN C . 10269 1 618 . 1 1 52 52 GLN CA C 13 58.264 0.300 . 1 . . . . 52 GLN CA . 10269 1 619 . 1 1 52 52 GLN CB C 13 28.458 0.300 . 1 . . . . 52 GLN CB . 10269 1 620 . 1 1 52 52 GLN CG C 13 33.551 0.300 . 1 . . . . 52 GLN CG . 10269 1 621 . 1 1 52 52 GLN N N 15 130.354 0.300 . 1 . . . . 52 GLN N . 10269 1 622 . 1 1 52 52 GLN NE2 N 15 113.203 0.300 . 1 . . . . 52 GLN NE2 . 10269 1 623 . 1 1 53 53 ASP H H 1 9.244 0.030 . 1 . . . . 53 ASP H . 10269 1 624 . 1 1 53 53 ASP HA H 1 4.529 0.030 . 1 . . . . 53 ASP HA . 10269 1 625 . 1 1 53 53 ASP HB2 H 1 3.254 0.030 . 2 . . . . 53 ASP HB2 . 10269 1 626 . 1 1 53 53 ASP HB3 H 1 3.210 0.030 . 2 . . . . 53 ASP HB3 . 10269 1 627 . 1 1 53 53 ASP C C 13 176.419 0.300 . 1 . . . . 53 ASP C . 10269 1 628 . 1 1 53 53 ASP CA C 13 56.605 0.300 . 1 . . . . 53 ASP CA . 10269 1 629 . 1 1 53 53 ASP CB C 13 39.788 0.300 . 1 . . . . 53 ASP CB . 10269 1 630 . 1 1 53 53 ASP N N 15 119.289 0.300 . 1 . . . . 53 ASP N . 10269 1 631 . 1 1 54 54 TYR H H 1 7.920 0.030 . 1 . . . . 54 TYR H . 10269 1 632 . 1 1 54 54 TYR HA H 1 4.388 0.030 . 1 . . . . 54 TYR HA . 10269 1 633 . 1 1 54 54 TYR HB2 H 1 3.666 0.030 . 2 . . . . 54 TYR HB2 . 10269 1 634 . 1 1 54 54 TYR HB3 H 1 3.508 0.030 . 2 . . . . 54 TYR HB3 . 10269 1 635 . 1 1 54 54 TYR HD1 H 1 7.251 0.030 . 1 . . . . 54 TYR HD1 . 10269 1 636 . 1 1 54 54 TYR HD2 H 1 7.251 0.030 . 1 . . . . 54 TYR HD2 . 10269 1 637 . 1 1 54 54 TYR HE1 H 1 6.594 0.030 . 1 . . . . 54 TYR HE1 . 10269 1 638 . 1 1 54 54 TYR HE2 H 1 6.594 0.030 . 1 . . . . 54 TYR HE2 . 10269 1 639 . 1 1 54 54 TYR C C 13 178.807 0.300 . 1 . . . . 54 TYR C . 10269 1 640 . 1 1 54 54 TYR CA C 13 57.557 0.300 . 1 . . . . 54 TYR CA . 10269 1 641 . 1 1 54 54 TYR CB C 13 37.745 0.300 . 1 . . . . 54 TYR CB . 10269 1 642 . 1 1 54 54 TYR CD1 C 13 131.193 0.300 . 1 . . . . 54 TYR CD1 . 10269 1 643 . 1 1 54 54 TYR CD2 C 13 131.193 0.300 . 1 . . . . 54 TYR CD2 . 10269 1 644 . 1 1 54 54 TYR CE1 C 13 118.061 0.300 . 1 . . . . 54 TYR CE1 . 10269 1 645 . 1 1 54 54 TYR CE2 C 13 118.061 0.300 . 1 . . . . 54 TYR CE2 . 10269 1 646 . 1 1 54 54 TYR N N 15 120.852 0.300 . 1 . . . . 54 TYR N . 10269 1 647 . 1 1 55 55 ASP H H 1 8.942 0.030 . 1 . . . . 55 ASP H . 10269 1 648 . 1 1 55 55 ASP HA H 1 4.155 0.030 . 1 . . . . 55 ASP HA . 10269 1 649 . 1 1 55 55 ASP HB2 H 1 2.633 0.030 . 1 . . . . 55 ASP HB2 . 10269 1 650 . 1 1 55 55 ASP HB3 H 1 2.633 0.030 . 1 . . . . 55 ASP HB3 . 10269 1 651 . 1 1 55 55 ASP C C 13 178.492 0.300 . 1 . . . . 55 ASP C . 10269 1 652 . 1 1 55 55 ASP CA C 13 57.839 0.300 . 1 . . . . 55 ASP CA . 10269 1 653 . 1 1 55 55 ASP CB C 13 39.955 0.300 . 1 . . . . 55 ASP CB . 10269 1 654 . 1 1 55 55 ASP N N 15 114.884 0.300 . 1 . . . . 55 ASP N . 10269 1 655 . 1 1 56 56 LEU H H 1 7.585 0.030 . 1 . . . . 56 LEU H . 10269 1 656 . 1 1 56 56 LEU HA H 1 3.968 0.030 . 1 . . . . 56 LEU HA . 10269 1 657 . 1 1 56 56 LEU HB2 H 1 1.620 0.030 . 2 . . . . 56 LEU HB2 . 10269 1 658 . 1 1 56 56 LEU HB3 H 1 1.389 0.030 . 2 . . . . 56 LEU HB3 . 10269 1 659 . 1 1 56 56 LEU HD11 H 1 0.736 0.030 . 1 . . . . 56 LEU HD1 . 10269 1 660 . 1 1 56 56 LEU HD12 H 1 0.736 0.030 . 1 . . . . 56 LEU HD1 . 10269 1 661 . 1 1 56 56 LEU HD13 H 1 0.736 0.030 . 1 . . . . 56 LEU HD1 . 10269 1 662 . 1 1 56 56 LEU HD21 H 1 0.609 0.030 . 1 . . . . 56 LEU HD2 . 10269 1 663 . 1 1 56 56 LEU HD22 H 1 0.609 0.030 . 1 . . . . 56 LEU HD2 . 10269 1 664 . 1 1 56 56 LEU HD23 H 1 0.609 0.030 . 1 . . . . 56 LEU HD2 . 10269 1 665 . 1 1 56 56 LEU HG H 1 1.433 0.030 . 1 . . . . 56 LEU HG . 10269 1 666 . 1 1 56 56 LEU C C 13 180.237 0.300 . 1 . . . . 56 LEU C . 10269 1 667 . 1 1 56 56 LEU CA C 13 57.892 0.300 . 1 . . . . 56 LEU CA . 10269 1 668 . 1 1 56 56 LEU CB C 13 41.204 0.300 . 1 . . . . 56 LEU CB . 10269 1 669 . 1 1 56 56 LEU CD1 C 13 24.784 0.300 . 2 . . . . 56 LEU CD1 . 10269 1 670 . 1 1 56 56 LEU CD2 C 13 23.126 0.300 . 2 . . . . 56 LEU CD2 . 10269 1 671 . 1 1 56 56 LEU CG C 13 26.713 0.300 . 1 . . . . 56 LEU CG . 10269 1 672 . 1 1 56 56 LEU N N 15 121.328 0.300 . 1 . . . . 56 LEU N . 10269 1 673 . 1 1 57 57 PHE H H 1 7.735 0.030 . 1 . . . . 57 PHE H . 10269 1 674 . 1 1 57 57 PHE HA H 1 4.182 0.030 . 1 . . . . 57 PHE HA . 10269 1 675 . 1 1 57 57 PHE HB2 H 1 2.959 0.030 . 2 . . . . 57 PHE HB2 . 10269 1 676 . 1 1 57 57 PHE HB3 H 1 2.874 0.030 . 2 . . . . 57 PHE HB3 . 10269 1 677 . 1 1 57 57 PHE HD1 H 1 7.387 0.030 . 1 . . . . 57 PHE HD1 . 10269 1 678 . 1 1 57 57 PHE HD2 H 1 7.387 0.030 . 1 . . . . 57 PHE HD2 . 10269 1 679 . 1 1 57 57 PHE HE1 H 1 7.361 0.030 . 1 . . . . 57 PHE HE1 . 10269 1 680 . 1 1 57 57 PHE HE2 H 1 7.361 0.030 . 1 . . . . 57 PHE HE2 . 10269 1 681 . 1 1 57 57 PHE HZ H 1 7.316 0.030 . 1 . . . . 57 PHE HZ . 10269 1 682 . 1 1 57 57 PHE C C 13 179.437 0.300 . 1 . . . . 57 PHE C . 10269 1 683 . 1 1 57 57 PHE CA C 13 62.756 0.300 . 1 . . . . 57 PHE CA . 10269 1 684 . 1 1 57 57 PHE CB C 13 38.803 0.300 . 1 . . . . 57 PHE CB . 10269 1 685 . 1 1 57 57 PHE CD1 C 13 131.761 0.300 . 1 . . . . 57 PHE CD1 . 10269 1 686 . 1 1 57 57 PHE CD2 C 13 131.761 0.300 . 1 . . . . 57 PHE CD2 . 10269 1 687 . 1 1 57 57 PHE CE1 C 13 131.833 0.300 . 1 . . . . 57 PHE CE1 . 10269 1 688 . 1 1 57 57 PHE CE2 C 13 131.833 0.300 . 1 . . . . 57 PHE CE2 . 10269 1 689 . 1 1 57 57 PHE CZ C 13 131.336 0.300 . 1 . . . . 57 PHE CZ . 10269 1 690 . 1 1 57 57 PHE N N 15 118.200 0.300 . 1 . . . . 57 PHE N . 10269 1 691 . 1 1 58 58 LYS H H 1 8.834 0.030 . 1 . . . . 58 LYS H . 10269 1 692 . 1 1 58 58 LYS HA H 1 3.515 0.030 . 1 . . . . 58 LYS HA . 10269 1 693 . 1 1 58 58 LYS HB2 H 1 1.860 0.030 . 2 . . . . 58 LYS HB2 . 10269 1 694 . 1 1 58 58 LYS HB3 H 1 1.801 0.030 . 2 . . . . 58 LYS HB3 . 10269 1 695 . 1 1 58 58 LYS HD2 H 1 1.357 0.030 . 2 . . . . 58 LYS HD2 . 10269 1 696 . 1 1 58 58 LYS HD3 H 1 1.220 0.030 . 2 . . . . 58 LYS HD3 . 10269 1 697 . 1 1 58 58 LYS HE2 H 1 2.010 0.030 . 2 . . . . 58 LYS HE2 . 10269 1 698 . 1 1 58 58 LYS HE3 H 1 1.184 0.030 . 2 . . . . 58 LYS HE3 . 10269 1 699 . 1 1 58 58 LYS HG2 H 1 1.023 0.030 . 2 . . . . 58 LYS HG2 . 10269 1 700 . 1 1 58 58 LYS HG3 H 1 0.244 0.030 . 2 . . . . 58 LYS HG3 . 10269 1 701 . 1 1 58 58 LYS C C 13 177.565 0.300 . 1 . . . . 58 LYS C . 10269 1 702 . 1 1 58 58 LYS CA C 13 60.851 0.300 . 1 . . . . 58 LYS CA . 10269 1 703 . 1 1 58 58 LYS CB C 13 33.102 0.300 . 1 . . . . 58 LYS CB . 10269 1 704 . 1 1 58 58 LYS CD C 13 30.793 0.300 . 1 . . . . 58 LYS CD . 10269 1 705 . 1 1 58 58 LYS CE C 13 40.403 0.300 . 1 . . . . 58 LYS CE . 10269 1 706 . 1 1 58 58 LYS CG C 13 25.272 0.300 . 1 . . . . 58 LYS CG . 10269 1 707 . 1 1 58 58 LYS N N 15 123.283 0.300 . 1 . . . . 58 LYS N . 10269 1 708 . 1 1 59 59 GLN H H 1 7.955 0.030 . 1 . . . . 59 GLN H . 10269 1 709 . 1 1 59 59 GLN HA H 1 4.104 0.030 . 1 . . . . 59 GLN HA . 10269 1 710 . 1 1 59 59 GLN HB2 H 1 2.136 0.030 . 1 . . . . 59 GLN HB2 . 10269 1 711 . 1 1 59 59 GLN HB3 H 1 2.136 0.030 . 1 . . . . 59 GLN HB3 . 10269 1 712 . 1 1 59 59 GLN HE21 H 1 7.476 0.030 . 2 . . . . 59 GLN HE21 . 10269 1 713 . 1 1 59 59 GLN HE22 H 1 6.795 0.030 . 2 . . . . 59 GLN HE22 . 10269 1 714 . 1 1 59 59 GLN HG2 H 1 2.496 0.030 . 2 . . . . 59 GLN HG2 . 10269 1 715 . 1 1 59 59 GLN HG3 H 1 2.385 0.030 . 2 . . . . 59 GLN HG3 . 10269 1 716 . 1 1 59 59 GLN C C 13 178.948 0.300 . 1 . . . . 59 GLN C . 10269 1 717 . 1 1 59 59 GLN CA C 13 59.249 0.300 . 1 . . . . 59 GLN CA . 10269 1 718 . 1 1 59 59 GLN CB C 13 28.185 0.300 . 1 . . . . 59 GLN CB . 10269 1 719 . 1 1 59 59 GLN CG C 13 33.979 0.300 . 1 . . . . 59 GLN CG . 10269 1 720 . 1 1 59 59 GLN N N 15 117.353 0.300 . 1 . . . . 59 GLN N . 10269 1 721 . 1 1 59 59 GLN NE2 N 15 111.771 0.300 . 1 . . . . 59 GLN NE2 . 10269 1 722 . 1 1 60 60 SER H H 1 7.821 0.030 . 1 . . . . 60 SER H . 10269 1 723 . 1 1 60 60 SER HA H 1 4.233 0.030 . 1 . . . . 60 SER HA . 10269 1 724 . 1 1 60 60 SER HB2 H 1 3.926 0.030 . 2 . . . . 60 SER HB2 . 10269 1 725 . 1 1 60 60 SER HB3 H 1 3.883 0.030 . 2 . . . . 60 SER HB3 . 10269 1 726 . 1 1 60 60 SER C C 13 176.403 0.300 . 1 . . . . 60 SER C . 10269 1 727 . 1 1 60 60 SER CA C 13 60.954 0.300 . 1 . . . . 60 SER CA . 10269 1 728 . 1 1 60 60 SER CB C 13 63.007 0.300 . 1 . . . . 60 SER CB . 10269 1 729 . 1 1 60 60 SER N N 15 112.660 0.300 . 1 . . . . 60 SER N . 10269 1 730 . 1 1 61 61 TYR H H 1 7.858 0.030 . 1 . . . . 61 TYR H . 10269 1 731 . 1 1 61 61 TYR HA H 1 4.084 0.030 . 1 . . . . 61 TYR HA . 10269 1 732 . 1 1 61 61 TYR HB2 H 1 2.909 0.030 . 2 . . . . 61 TYR HB2 . 10269 1 733 . 1 1 61 61 TYR HB3 H 1 2.802 0.030 . 2 . . . . 61 TYR HB3 . 10269 1 734 . 1 1 61 61 TYR C C 13 177.358 0.300 . 1 . . . . 61 TYR C . 10269 1 735 . 1 1 61 61 TYR CA C 13 61.217 0.300 . 1 . . . . 61 TYR CA . 10269 1 736 . 1 1 61 61 TYR CB C 13 38.470 0.300 . 1 . . . . 61 TYR CB . 10269 1 737 . 1 1 61 61 TYR CD1 C 13 135.210 0.300 . 1 . . . . 61 TYR CD1 . 10269 1 738 . 1 1 61 61 TYR CD2 C 13 135.210 0.300 . 1 . . . . 61 TYR CD2 . 10269 1 739 . 1 1 61 61 TYR N N 15 122.550 0.300 . 1 . . . . 61 TYR N . 10269 1 740 . 1 1 62 62 TRP H H 1 7.754 0.030 . 1 . . . . 62 TRP H . 10269 1 741 . 1 1 62 62 TRP HA H 1 4.273 0.030 . 1 . . . . 62 TRP HA . 10269 1 742 . 1 1 62 62 TRP HB2 H 1 3.258 0.030 . 2 . . . . 62 TRP HB2 . 10269 1 743 . 1 1 62 62 TRP HB3 H 1 2.898 0.030 . 2 . . . . 62 TRP HB3 . 10269 1 744 . 1 1 62 62 TRP HD1 H 1 7.345 0.030 . 1 . . . . 62 TRP HD1 . 10269 1 745 . 1 1 62 62 TRP HE1 H 1 10.659 0.030 . 1 . . . . 62 TRP HE1 . 10269 1 746 . 1 1 62 62 TRP HE3 H 1 7.576 0.030 . 1 . . . . 62 TRP HE3 . 10269 1 747 . 1 1 62 62 TRP HH2 H 1 6.020 0.030 . 1 . . . . 62 TRP HH2 . 10269 1 748 . 1 1 62 62 TRP HZ2 H 1 7.106 0.030 . 1 . . . . 62 TRP HZ2 . 10269 1 749 . 1 1 62 62 TRP HZ3 H 1 6.917 0.030 . 1 . . . . 62 TRP HZ3 . 10269 1 750 . 1 1 62 62 TRP C C 13 176.694 0.300 . 1 . . . . 62 TRP C . 10269 1 751 . 1 1 62 62 TRP CA C 13 58.061 0.300 . 1 . . . . 62 TRP CA . 10269 1 752 . 1 1 62 62 TRP CB C 13 30.047 0.300 . 1 . . . . 62 TRP CB . 10269 1 753 . 1 1 62 62 TRP CD1 C 13 129.026 0.300 . 1 . . . . 62 TRP CD1 . 10269 1 754 . 1 1 62 62 TRP CE3 C 13 120.872 0.300 . 1 . . . . 62 TRP CE3 . 10269 1 755 . 1 1 62 62 TRP CH2 C 13 123.916 0.300 . 1 . . . . 62 TRP CH2 . 10269 1 756 . 1 1 62 62 TRP CZ2 C 13 113.434 0.300 . 1 . . . . 62 TRP CZ2 . 10269 1 757 . 1 1 62 62 TRP CZ3 C 13 121.599 0.300 . 1 . . . . 62 TRP CZ3 . 10269 1 758 . 1 1 62 62 TRP N N 15 116.320 0.300 . 1 . . . . 62 TRP N . 10269 1 759 . 1 1 62 62 TRP NE1 N 15 127.952 0.300 . 1 . . . . 62 TRP NE1 . 10269 1 760 . 1 1 63 63 ASN H H 1 7.800 0.030 . 1 . . . . 63 ASN H . 10269 1 761 . 1 1 63 63 ASN HA H 1 4.688 0.030 . 1 . . . . 63 ASN HA . 10269 1 762 . 1 1 63 63 ASN HB2 H 1 2.842 0.030 . 2 . . . . 63 ASN HB2 . 10269 1 763 . 1 1 63 63 ASN HB3 H 1 2.752 0.030 . 2 . . . . 63 ASN HB3 . 10269 1 764 . 1 1 63 63 ASN HD21 H 1 7.601 0.030 . 2 . . . . 63 ASN HD21 . 10269 1 765 . 1 1 63 63 ASN HD22 H 1 6.873 0.030 . 2 . . . . 63 ASN HD22 . 10269 1 766 . 1 1 63 63 ASN C C 13 174.055 0.300 . 1 . . . . 63 ASN C . 10269 1 767 . 1 1 63 63 ASN CA C 13 53.484 0.300 . 1 . . . . 63 ASN CA . 10269 1 768 . 1 1 63 63 ASN CB C 13 38.645 0.300 . 1 . . . . 63 ASN CB . 10269 1 769 . 1 1 63 63 ASN N N 15 117.543 0.300 . 1 . . . . 63 ASN N . 10269 1 770 . 1 1 63 63 ASN ND2 N 15 112.718 0.300 . 1 . . . . 63 ASN ND2 . 10269 1 771 . 1 1 64 64 HIS H H 1 7.732 0.030 . 1 . . . . 64 HIS H . 10269 1 772 . 1 1 64 64 HIS HA H 1 4.396 0.030 . 1 . . . . 64 HIS HA . 10269 1 773 . 1 1 64 64 HIS HB2 H 1 3.183 0.030 . 2 . . . . 64 HIS HB2 . 10269 1 774 . 1 1 64 64 HIS HB3 H 1 3.078 0.030 . 2 . . . . 64 HIS HB3 . 10269 1 775 . 1 1 64 64 HIS HD2 H 1 7.055 0.030 . 1 . . . . 64 HIS HD2 . 10269 1 776 . 1 1 64 64 HIS C C 13 179.203 0.300 . 1 . . . . 64 HIS C . 10269 1 777 . 1 1 64 64 HIS CA C 13 57.398 0.300 . 1 . . . . 64 HIS CA . 10269 1 778 . 1 1 64 64 HIS CB C 13 30.081 0.300 . 1 . . . . 64 HIS CB . 10269 1 779 . 1 1 64 64 HIS CD2 C 13 120.088 0.300 . 1 . . . . 64 HIS CD2 . 10269 1 780 . 1 1 64 64 HIS N N 15 123.554 0.300 . 1 . . . . 64 HIS N . 10269 1 stop_ save_