data_18497 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18497 _Entry.Title ; Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-06-01 _Entry.Accession_date 2012-06-01 _Entry.Last_release_date 2013-06-10 _Entry.Original_release_date 2013-06-10 _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 'autoinhibitory domain(AID)of human AMP-activated protein kinase catalytic subunit' _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 Bin Xia . . . 18497 2 Jicheng Hu . . . 18497 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' . 18497 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID AID . 18497 AMPK . 18497 'NMR structure' . 18497 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18497 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 231 18497 '15N chemical shifts' 62 18497 '1H chemical shifts' 361 18497 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 . . 2013-06-10 2012-06-01 original author . 18497 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LTU 'BMRB Entry Tracking System' 18497 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18497 _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 Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'Not known' _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 Bin Xia . . . 18497 1 2 Jicheng Hu . . . 18497 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18497 _Assembly.ID 1 _Assembly.Name 'autoinhibitory domain of human AMP-activated protein kinase catalytic subunit' _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 . _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 'autoinhibitory domain of human AMP-activated protein kinase catalytic subunit' 1 $entity A . yes native no no . . . 18497 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 18497 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GPHMSYDANVIDDEAVKEVC EKFECTESEVMNSLYSGDPQ DQLAVAYHLIIDNRRIMNQA SE ; _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 62 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7026.763 _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 PDB 2LTU . "Solution Structure Of Autoinhibitory Domain Of Human Amp-activated Protein Kinase Catalytic Subunit" . . . . . 100.00 62 100.00 100.00 2.68e-37 . . . . 18497 1 2 no PDB 4CFE . "Structure Of Full Length Human Ampk In Complex With A Small Molecule Activator, A Benzimidazole Derivative (991)" . . . . . 93.55 571 100.00 100.00 2.00e-30 . . . . 18497 1 3 no PDB 4CFF . "Structure Of Full Length Human Ampk In Complex With A Small Molecule Activator, A Thienopyridone Derivative (a-769662)" . . . . . 93.55 571 100.00 100.00 2.00e-30 . . . . 18497 1 4 no DBJ BAC31746 . "unnamed protein product [Mus musculus]" . . . . . 93.55 530 98.28 98.28 2.61e-29 . . . . 18497 1 5 no DBJ BAE22188 . "unnamed protein product [Mus musculus]" . . . . . 93.55 538 100.00 100.00 1.63e-30 . . . . 18497 1 6 no DBJ BAG36722 . "unnamed protein product [Homo sapiens]" . . . . . 93.55 552 100.00 100.00 1.72e-30 . . . . 18497 1 7 no EMBL CAA82620 . "AMP-activated protein kinase [Rattus norvegicus]" . . . . . 93.55 552 100.00 100.00 1.84e-30 . . . . 18497 1 8 no EMBL CAH90357 . "hypothetical protein [Pongo abelii]" . . . . . 93.55 552 100.00 100.00 1.63e-30 . . . . 18497 1 9 no GB AAA64745 . "AMP-activated protein kinase [Homo sapiens]" . . . . . 93.55 552 100.00 100.00 1.50e-30 . . . . 18497 1 10 no GB AAA85033 . "5'-AMP-activated protein kinase catalytic alpha-2 subunit [Rattus norvegicus]" . . . . . 93.55 552 100.00 100.00 1.66e-30 . . . . 18497 1 11 no GB AAB32732 . "AMP-activated protein kinase, AMPK [human, skeletal muscle, Peptide, 552 aa]" . . . . . 93.55 552 100.00 100.00 1.60e-30 . . . . 18497 1 12 no GB AAH69680 . "Protein kinase, AMP-activated, alpha 2 catalytic subunit [Homo sapiens]" . . . . . 93.55 552 100.00 100.00 1.60e-30 . . . . 18497 1 13 no GB AAH69740 . "AMP-activated protein kinase alpha 2 catalytic subunit [Homo sapiens]" . . . . . 93.55 552 100.00 100.00 1.60e-30 . . . . 18497 1 14 no REF NP_001075410 . "5'-AMP-activated protein kinase catalytic subunit alpha-2 [Equus caballus]" . . . . . 93.55 552 100.00 100.00 5.30e-31 . . . . 18497 1 15 no REF NP_001106287 . "5'-AMP-activated protein kinase catalytic subunit alpha-2 [Ovis aries]" . . . . . 93.55 552 100.00 100.00 1.77e-30 . . . . 18497 1 16 no REF NP_001125173 . "5'-AMP-activated protein kinase catalytic subunit alpha-2 [Pongo abelii]" . . . . . 93.55 552 100.00 100.00 1.63e-30 . . . . 18497 1 17 no REF NP_001135554 . "5'-AMP-activated protein kinase catalytic subunit alpha-2 [Xenopus (Silurana) tropicalis]" . . . . . 93.55 551 100.00 100.00 1.86e-30 . . . . 18497 1 18 no REF NP_001192534 . "5'-AMP-activated protein kinase catalytic subunit alpha-2 [Bos taurus]" . . . . . 93.55 552 100.00 100.00 1.77e-30 . . . . 18497 1 19 no SP P54646 . "RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; Short=AMPK subunit alpha-2; AltName: Full=Acetyl-CoA c" . . . . . 93.55 552 100.00 100.00 1.60e-30 . . . . 18497 1 20 no SP Q09137 . "RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; Short=AMPK subunit alpha-2; AltName: Full=Acetyl-CoA c" . . . . . 93.55 552 100.00 100.00 1.84e-30 . . . . 18497 1 21 no SP Q28948 . "RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; Short=AMPK subunit alpha-2; AltName: Full=Acetyl-CoA c" . . . . . 93.55 552 98.28 100.00 2.95e-30 . . . . 18497 1 22 no SP Q5RD00 . "RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; Short=AMPK subunit alpha-2; AltName: Full=Acetyl-CoA c" . . . . . 93.55 552 100.00 100.00 1.63e-30 . . . . 18497 1 23 no SP Q8BRK8 . "RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; Short=AMPK subunit alpha-2; AltName: Full=Acetyl-CoA c" . . . . . 93.55 552 100.00 100.00 1.73e-30 . . . . 18497 1 24 no TPG DAA31222 . "TPA: protein kinase, AMP-activated, alpha 2 catalytic subunit-like [Bos taurus]" . . . . . 93.55 552 100.00 100.00 1.77e-30 . . . . 18497 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 . 18497 1 2 . PRO . 18497 1 3 . HIS . 18497 1 4 . MET . 18497 1 5 . SER . 18497 1 6 . TYR . 18497 1 7 . ASP . 18497 1 8 . ALA . 18497 1 9 . ASN . 18497 1 10 . VAL . 18497 1 11 . ILE . 18497 1 12 . ASP . 18497 1 13 . ASP . 18497 1 14 . GLU . 18497 1 15 . ALA . 18497 1 16 . VAL . 18497 1 17 . LYS . 18497 1 18 . GLU . 18497 1 19 . VAL . 18497 1 20 . CYS . 18497 1 21 . GLU . 18497 1 22 . LYS . 18497 1 23 . PHE . 18497 1 24 . GLU . 18497 1 25 . CYS . 18497 1 26 . THR . 18497 1 27 . GLU . 18497 1 28 . SER . 18497 1 29 . GLU . 18497 1 30 . VAL . 18497 1 31 . MET . 18497 1 32 . ASN . 18497 1 33 . SER . 18497 1 34 . LEU . 18497 1 35 . TYR . 18497 1 36 . SER . 18497 1 37 . GLY . 18497 1 38 . ASP . 18497 1 39 . PRO . 18497 1 40 . GLN . 18497 1 41 . ASP . 18497 1 42 . GLN . 18497 1 43 . LEU . 18497 1 44 . ALA . 18497 1 45 . VAL . 18497 1 46 . ALA . 18497 1 47 . TYR . 18497 1 48 . HIS . 18497 1 49 . LEU . 18497 1 50 . ILE . 18497 1 51 . ILE . 18497 1 52 . ASP . 18497 1 53 . ASN . 18497 1 54 . ARG . 18497 1 55 . ARG . 18497 1 56 . ILE . 18497 1 57 . MET . 18497 1 58 . ASN . 18497 1 59 . GLN . 18497 1 60 . ALA . 18497 1 61 . SER . 18497 1 62 . GLU . 18497 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 18497 1 . PRO 2 2 18497 1 . HIS 3 3 18497 1 . MET 4 4 18497 1 . SER 5 5 18497 1 . TYR 6 6 18497 1 . ASP 7 7 18497 1 . ALA 8 8 18497 1 . ASN 9 9 18497 1 . VAL 10 10 18497 1 . ILE 11 11 18497 1 . ASP 12 12 18497 1 . ASP 13 13 18497 1 . GLU 14 14 18497 1 . ALA 15 15 18497 1 . VAL 16 16 18497 1 . LYS 17 17 18497 1 . GLU 18 18 18497 1 . VAL 19 19 18497 1 . CYS 20 20 18497 1 . GLU 21 21 18497 1 . LYS 22 22 18497 1 . PHE 23 23 18497 1 . GLU 24 24 18497 1 . CYS 25 25 18497 1 . THR 26 26 18497 1 . GLU 27 27 18497 1 . SER 28 28 18497 1 . GLU 29 29 18497 1 . VAL 30 30 18497 1 . MET 31 31 18497 1 . ASN 32 32 18497 1 . SER 33 33 18497 1 . LEU 34 34 18497 1 . TYR 35 35 18497 1 . SER 36 36 18497 1 . GLY 37 37 18497 1 . ASP 38 38 18497 1 . PRO 39 39 18497 1 . GLN 40 40 18497 1 . ASP 41 41 18497 1 . GLN 42 42 18497 1 . LEU 43 43 18497 1 . ALA 44 44 18497 1 . VAL 45 45 18497 1 . ALA 46 46 18497 1 . TYR 47 47 18497 1 . HIS 48 48 18497 1 . LEU 49 49 18497 1 . ILE 50 50 18497 1 . ILE 51 51 18497 1 . ASP 52 52 18497 1 . ASN 53 53 18497 1 . ARG 54 54 18497 1 . ARG 55 55 18497 1 . ILE 56 56 18497 1 . MET 57 57 18497 1 . ASN 58 58 18497 1 . GLN 59 59 18497 1 . ALA 60 60 18497 1 . SER 61 61 18497 1 . GLU 62 62 18497 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 18497 _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 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18497 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 18497 _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 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'E. coli' BL21(DE3) . . . . . . . . . . . . . . pGEX . . . 'GST fusion protein' . . 18497 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18497 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '15N/13C labeled AID protein' _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 'AID protein' '[U-100% 13C; U-100% 15N]' . . 1 $entity . . 0.2 . . mM . . . . 18497 1 2 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 18497 1 3 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 18497 1 4 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18497 1 5 EDTA 'natural abundance' . . . . . . 1 . . mM . . . . 18497 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 18497 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 50 . mM 18497 1 pH 7.0 . pH 18497 1 pressure 1 . atm 18497 1 temperature 298 . K 18497 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18497 _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' . . 18497 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18497 1 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 18497 _Software.ID 2 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 18497 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 18497 2 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 18497 _Software.ID 3 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 18497 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18497 3 stop_ save_ save_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRDraw _Software.Entry_ID 18497 _Software.ID 4 _Software.Name NMRDraw _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' . . 18497 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18497 4 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 18497 _Software.ID 5 _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' . . 18497 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18497 5 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 18497 _Software.ID 6 _Software.Name DYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Braun and Wuthrich' . . 18497 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18497 6 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 18497 _Software.ID 7 _Software.Name AMBER _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . 18497 7 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18497 7 stop_ save_ save_ProcheckNMR _Software.Sf_category software _Software.Sf_framecode ProcheckNMR _Software.Entry_ID 18497 _Software.ID 8 _Software.Name ProcheckNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Laskowski and MacArthur' . . 18497 8 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'geometry optimization' 18497 8 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 18497 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details cryo-probe _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 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 18497 _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 . 600 cryo-probe . . 18497 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 18497 _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 . . . . . . . . . . . . . . . . 18497 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 3 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 4 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 5 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 6 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 7 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 8 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 9 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 10 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 11 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 12 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 13 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 1 14 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18497 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 18497 _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 C 13 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . . . . . . . 18497 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18497 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 18497 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 18497 _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 0.03 _Assigned_chem_shift_list.Chem_shift_13C_err 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _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' . . . 18497 1 2 '2D 1H-13C HSQC' . . . 18497 1 13 '3D 1H-15N NOESY' . . . 18497 1 14 '3D 1H-13C NOESY' . . . 18497 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 2 2 PRO HA H 1 4.430 0.03 . 1 . . . A 2 PRO HA . 18497 1 2 . 1 1 2 2 PRO HB2 H 1 2.234 0.03 . 2 . . . A 2 PRO HB2 . 18497 1 3 . 1 1 2 2 PRO HB3 H 1 1.840 0.03 . 2 . . . A 2 PRO HB3 . 18497 1 4 . 1 1 2 2 PRO CA C 13 62.947 0.3 . 1 . . . A 2 PRO CA . 18497 1 5 . 1 1 2 2 PRO CB C 13 32.130 0.3 . 1 . . . A 2 PRO CB . 18497 1 6 . 1 1 3 3 HIS H H 1 8.526 0.03 . 1 . . . A 3 HIS H . 18497 1 7 . 1 1 3 3 HIS HA H 1 4.606 0.03 . 1 . . . A 3 HIS HA . 18497 1 8 . 1 1 3 3 HIS HB2 H 1 3.113 0.03 . 2 . . . A 3 HIS HB2 . 18497 1 9 . 1 1 3 3 HIS C C 13 176.587 0.3 . 1 . . . A 3 HIS C . 18497 1 10 . 1 1 3 3 HIS CA C 13 56.185 0.3 . 1 . . . A 3 HIS CA . 18497 1 11 . 1 1 3 3 HIS CB C 13 30.471 0.3 . 1 . . . A 3 HIS CB . 18497 1 12 . 1 1 3 3 HIS N N 15 119.985 0.3 . 1 . . . A 3 HIS N . 18497 1 13 . 1 1 4 4 MET H H 1 8.337 0.03 . 1 . . . A 4 MET H . 18497 1 14 . 1 1 4 4 MET HA H 1 4.448 0.03 . 1 . . . A 4 MET HA . 18497 1 15 . 1 1 4 4 MET HB3 H 1 1.913 0.03 . 2 . . . A 4 MET HB3 . 18497 1 16 . 1 1 4 4 MET HG3 H 1 2.454 0.03 . 2 . . . A 4 MET HG3 . 18497 1 17 . 1 1 4 4 MET C C 13 175.108 0.3 . 1 . . . A 4 MET C . 18497 1 18 . 1 1 4 4 MET CA C 13 55.562 0.3 . 1 . . . A 4 MET CA . 18497 1 19 . 1 1 4 4 MET CB C 13 33.141 0.3 . 1 . . . A 4 MET CB . 18497 1 20 . 1 1 4 4 MET N N 15 122.338 0.3 . 1 . . . A 4 MET N . 18497 1 21 . 1 1 5 5 SER H H 1 8.330 0.03 . 1 . . . A 5 SER H . 18497 1 22 . 1 1 5 5 SER HA H 1 4.400 0.03 . 1 . . . A 5 SER HA . 18497 1 23 . 1 1 5 5 SER HB3 H 1 3.800 0.03 . 2 . . . A 5 SER HB3 . 18497 1 24 . 1 1 5 5 SER C C 13 177.979 0.3 . 1 . . . A 5 SER C . 18497 1 25 . 1 1 5 5 SER CA C 13 58.039 0.3 . 1 . . . A 5 SER CA . 18497 1 26 . 1 1 5 5 SER CB C 13 63.797 0.3 . 1 . . . A 5 SER CB . 18497 1 27 . 1 1 5 5 SER N N 15 116.990 0.3 . 1 . . . A 5 SER N . 18497 1 28 . 1 1 6 6 TYR H H 1 8.201 0.03 . 1 . . . A 6 TYR H . 18497 1 29 . 1 1 6 6 TYR HA H 1 4.510 0.03 . 1 . . . A 6 TYR HA . 18497 1 30 . 1 1 6 6 TYR HB2 H 1 2.990 0.03 . 2 . . . A 6 TYR HB2 . 18497 1 31 . 1 1 6 6 TYR HB3 H 1 2.890 0.03 . 2 . . . A 6 TYR HB3 . 18497 1 32 . 1 1 6 6 TYR C C 13 174.060 0.3 . 1 . . . A 6 TYR C . 18497 1 33 . 1 1 6 6 TYR CA C 13 57.800 0.3 . 1 . . . A 6 TYR CA . 18497 1 34 . 1 1 6 6 TYR CB C 13 38.685 0.3 . 1 . . . A 6 TYR CB . 18497 1 35 . 1 1 6 6 TYR N N 15 122.027 0.3 . 1 . . . A 6 TYR N . 18497 1 36 . 1 1 7 7 ASP H H 1 8.119 0.03 . 1 . . . A 7 ASP H . 18497 1 37 . 1 1 7 7 ASP HA H 1 4.549 0.03 . 1 . . . A 7 ASP HA . 18497 1 38 . 1 1 7 7 ASP HB2 H 1 2.717 0.03 . 2 . . . A 7 ASP HB2 . 18497 1 39 . 1 1 7 7 ASP HB3 H 1 2.568 0.03 . 2 . . . A 7 ASP HB3 . 18497 1 40 . 1 1 7 7 ASP C C 13 175.150 0.3 . 1 . . . A 7 ASP C . 18497 1 41 . 1 1 7 7 ASP CA C 13 53.640 0.3 . 1 . . . A 7 ASP CA . 18497 1 42 . 1 1 7 7 ASP CB C 13 41.300 0.3 . 1 . . . A 7 ASP CB . 18497 1 43 . 1 1 7 7 ASP N N 15 122.439 0.3 . 1 . . . A 7 ASP N . 18497 1 44 . 1 1 8 8 ALA H H 1 8.235 0.03 . 1 . . . A 8 ALA H . 18497 1 45 . 1 1 8 8 ALA HA H 1 4.230 0.03 . 1 . . . A 8 ALA HA . 18497 1 46 . 1 1 8 8 ALA HB1 H 1 1.410 0.03 . 1 . . . A 8 ALA HB1 . 18497 1 47 . 1 1 8 8 ALA HB2 H 1 1.410 0.03 . 1 . . . A 8 ALA HB2 . 18497 1 48 . 1 1 8 8 ALA HB3 H 1 1.410 0.03 . 1 . . . A 8 ALA HB3 . 18497 1 49 . 1 1 8 8 ALA C C 13 175.935 0.3 . 1 . . . A 8 ALA C . 18497 1 50 . 1 1 8 8 ALA CA C 13 52.893 0.3 . 1 . . . A 8 ALA CA . 18497 1 51 . 1 1 8 8 ALA CB C 13 18.850 0.3 . 1 . . . A 8 ALA CB . 18497 1 52 . 1 1 8 8 ALA N N 15 124.655 0.3 . 1 . . . A 8 ALA N . 18497 1 53 . 1 1 9 9 ASN H H 1 8.417 0.03 . 1 . . . A 9 ASN H . 18497 1 54 . 1 1 9 9 ASN HA H 1 4.690 0.03 . 1 . . . A 9 ASN HA . 18497 1 55 . 1 1 9 9 ASN HB3 H 1 2.810 0.03 . 2 . . . A 9 ASN HB3 . 18497 1 56 . 1 1 9 9 ASN HD21 H 1 6.915 0.03 . 2 . . . A 9 ASN HD21 . 18497 1 57 . 1 1 9 9 ASN HD22 H 1 7.690 0.03 . 2 . . . A 9 ASN HD22 . 18497 1 58 . 1 1 9 9 ASN C C 13 177.718 0.3 . 1 . . . A 9 ASN C . 18497 1 59 . 1 1 9 9 ASN CA C 13 53.800 0.3 . 1 . . . A 9 ASN CA . 18497 1 60 . 1 1 9 9 ASN CB C 13 38.770 0.3 . 1 . . . A 9 ASN CB . 18497 1 61 . 1 1 9 9 ASN N N 15 116.133 0.3 . 1 . . . A 9 ASN N . 18497 1 62 . 1 1 9 9 ASN ND2 N 15 113.740 0.3 . 1 . . . A 9 ASN ND2 . 18497 1 63 . 1 1 10 10 VAL H H 1 7.859 0.03 . 1 . . . A 10 VAL H . 18497 1 64 . 1 1 10 10 VAL HA H 1 4.177 0.03 . 1 . . . A 10 VAL HA . 18497 1 65 . 1 1 10 10 VAL HB H 1 2.110 0.03 . 1 . . . A 10 VAL HB . 18497 1 66 . 1 1 10 10 VAL HG21 H 1 0.930 0.03 . 2 . . . A 10 VAL HG21 . 18497 1 67 . 1 1 10 10 VAL HG22 H 1 0.930 0.03 . 2 . . . A 10 VAL HG22 . 18497 1 68 . 1 1 10 10 VAL HG23 H 1 0.930 0.03 . 2 . . . A 10 VAL HG23 . 18497 1 69 . 1 1 10 10 VAL C C 13 174.930 0.3 . 1 . . . A 10 VAL C . 18497 1 70 . 1 1 10 10 VAL CA C 13 61.880 0.3 . 1 . . . A 10 VAL CA . 18497 1 71 . 1 1 10 10 VAL CB C 13 32.660 0.3 . 1 . . . A 10 VAL CB . 18497 1 72 . 1 1 10 10 VAL CG2 C 13 20.710 0.3 . 1 . . . A 10 VAL CG2 . 18497 1 73 . 1 1 10 10 VAL N N 15 119.557 0.3 . 1 . . . A 10 VAL N . 18497 1 74 . 1 1 11 11 ILE H H 1 8.283 0.03 . 1 . . . A 11 ILE H . 18497 1 75 . 1 1 11 11 ILE HA H 1 4.040 0.03 . 1 . . . A 11 ILE HA . 18497 1 76 . 1 1 11 11 ILE HB H 1 1.856 0.03 . 1 . . . A 11 ILE HB . 18497 1 77 . 1 1 11 11 ILE HG12 H 1 1.390 0.03 . 1 . . . A 11 ILE HG12 . 18497 1 78 . 1 1 11 11 ILE HG13 H 1 1.270 0.03 . 1 . . . A 11 ILE HG13 . 18497 1 79 . 1 1 11 11 ILE HG21 H 1 0.700 0.03 . 2 . . . A 11 ILE HG21 . 18497 1 80 . 1 1 11 11 ILE HG22 H 1 0.700 0.03 . 2 . . . A 11 ILE HG22 . 18497 1 81 . 1 1 11 11 ILE HG23 H 1 0.700 0.03 . 2 . . . A 11 ILE HG23 . 18497 1 82 . 1 1 11 11 ILE HD11 H 1 0.640 0.03 . 1 . . . A 11 ILE HD11 . 18497 1 83 . 1 1 11 11 ILE HD12 H 1 0.640 0.03 . 1 . . . A 11 ILE HD12 . 18497 1 84 . 1 1 11 11 ILE HD13 H 1 0.640 0.03 . 1 . . . A 11 ILE HD13 . 18497 1 85 . 1 1 11 11 ILE C C 13 175.935 0.3 . 1 . . . A 11 ILE C . 18497 1 86 . 1 1 11 11 ILE CA C 13 59.500 0.3 . 1 . . . A 11 ILE CA . 18497 1 87 . 1 1 11 11 ILE CB C 13 37.700 0.3 . 1 . . . A 11 ILE CB . 18497 1 88 . 1 1 11 11 ILE CG1 C 13 27.400 0.3 . 2 . . . A 11 ILE CG1 . 18497 1 89 . 1 1 11 11 ILE CG2 C 13 17.800 0.3 . 1 . . . A 11 ILE CG2 . 18497 1 90 . 1 1 11 11 ILE CD1 C 13 11.200 0.3 . 1 . . . A 11 ILE CD1 . 18497 1 91 . 1 1 11 11 ILE N N 15 126.561 0.3 . 1 . . . A 11 ILE N . 18497 1 92 . 1 1 12 12 ASP H H 1 8.477 0.03 . 1 . . . A 12 ASP H . 18497 1 93 . 1 1 12 12 ASP HA H 1 4.730 0.03 . 1 . . . A 12 ASP HA . 18497 1 94 . 1 1 12 12 ASP HB2 H 1 3.034 0.03 . 2 . . . A 12 ASP HB2 . 18497 1 95 . 1 1 12 12 ASP HB3 H 1 2.470 0.03 . 2 . . . A 12 ASP HB3 . 18497 1 96 . 1 1 12 12 ASP C C 13 174.891 0.3 . 1 . . . A 12 ASP C . 18497 1 97 . 1 1 12 12 ASP CA C 13 53.427 0.3 . 1 . . . A 12 ASP CA . 18497 1 98 . 1 1 12 12 ASP CB C 13 42.220 0.3 . 1 . . . A 12 ASP CB . 18497 1 99 . 1 1 12 12 ASP N N 15 128.161 0.3 . 1 . . . A 12 ASP N . 18497 1 100 . 1 1 13 13 ASP H H 1 8.698 0.03 . 1 . . . A 13 ASP H . 18497 1 101 . 1 1 13 13 ASP HA H 1 4.316 0.03 . 1 . . . A 13 ASP HA . 18497 1 102 . 1 1 13 13 ASP HB2 H 1 2.680 0.03 . 2 . . . A 13 ASP HB2 . 18497 1 103 . 1 1 13 13 ASP HB3 H 1 2.680 0.03 . 2 . . . A 13 ASP HB3 . 18497 1 104 . 1 1 13 13 ASP C C 13 175.369 0.3 . 1 . . . A 13 ASP C . 18497 1 105 . 1 1 13 13 ASP CA C 13 57.600 0.3 . 1 . . . A 13 ASP CA . 18497 1 106 . 1 1 13 13 ASP CB C 13 41.160 0.3 . 1 . . . A 13 ASP CB . 18497 1 107 . 1 1 13 13 ASP N N 15 127.435 0.3 . 1 . . . A 13 ASP N . 18497 1 108 . 1 1 14 14 GLU H H 1 8.205 0.03 . 1 . . . A 14 GLU H . 18497 1 109 . 1 1 14 14 GLU HA H 1 4.035 0.03 . 1 . . . A 14 GLU HA . 18497 1 110 . 1 1 14 14 GLU HB2 H 1 2.060 0.03 . 2 . . . A 14 GLU HB2 . 18497 1 111 . 1 1 14 14 GLU HB3 H 1 2.130 0.03 . 2 . . . A 14 GLU HB3 . 18497 1 112 . 1 1 14 14 GLU HG2 H 1 2.400 0.03 . 2 . . . A 14 GLU HG2 . 18497 1 113 . 1 1 14 14 GLU HG3 H 1 2.300 0.03 . 2 . . . A 14 GLU HG3 . 18497 1 114 . 1 1 14 14 GLU C C 13 178.588 0.3 . 1 . . . A 14 GLU C . 18497 1 115 . 1 1 14 14 GLU CA C 13 59.500 0.3 . 1 . . . A 14 GLU CA . 18497 1 116 . 1 1 14 14 GLU CB C 13 28.900 0.3 . 1 . . . A 14 GLU CB . 18497 1 117 . 1 1 14 14 GLU CG C 13 36.600 0.3 . 1 . . . A 14 GLU CG . 18497 1 118 . 1 1 14 14 GLU N N 15 119.796 0.3 . 1 . . . A 14 GLU N . 18497 1 119 . 1 1 15 15 ALA H H 1 8.473 0.03 . 1 . . . A 15 ALA H . 18497 1 120 . 1 1 15 15 ALA HA H 1 4.176 0.03 . 1 . . . A 15 ALA HA . 18497 1 121 . 1 1 15 15 ALA HB1 H 1 1.260 0.03 . 1 . . . A 15 ALA HB1 . 18497 1 122 . 1 1 15 15 ALA HB2 H 1 1.260 0.03 . 1 . . . A 15 ALA HB2 . 18497 1 123 . 1 1 15 15 ALA HB3 H 1 1.260 0.03 . 1 . . . A 15 ALA HB3 . 18497 1 124 . 1 1 15 15 ALA C C 13 179.502 0.3 . 1 . . . A 15 ALA C . 18497 1 125 . 1 1 15 15 ALA CA C 13 55.000 0.3 . 1 . . . A 15 ALA CA . 18497 1 126 . 1 1 15 15 ALA CB C 13 18.900 0.3 . 1 . . . A 15 ALA CB . 18497 1 127 . 1 1 15 15 ALA N N 15 124.156 0.3 . 1 . . . A 15 ALA N . 18497 1 128 . 1 1 16 16 VAL H H 1 8.181 0.03 . 1 . . . A 16 VAL H . 18497 1 129 . 1 1 16 16 VAL HA H 1 3.534 0.03 . 1 . . . A 16 VAL HA . 18497 1 130 . 1 1 16 16 VAL HB H 1 2.420 0.03 . 1 . . . A 16 VAL HB . 18497 1 131 . 1 1 16 16 VAL HG11 H 1 0.910 0.03 . 2 . . . A 16 VAL HG11 . 18497 1 132 . 1 1 16 16 VAL HG12 H 1 0.910 0.03 . 2 . . . A 16 VAL HG12 . 18497 1 133 . 1 1 16 16 VAL HG13 H 1 0.910 0.03 . 2 . . . A 16 VAL HG13 . 18497 1 134 . 1 1 16 16 VAL HG21 H 1 1.050 0.03 . 2 . . . A 16 VAL HG21 . 18497 1 135 . 1 1 16 16 VAL HG22 H 1 1.050 0.03 . 2 . . . A 16 VAL HG22 . 18497 1 136 . 1 1 16 16 VAL HG23 H 1 1.050 0.03 . 2 . . . A 16 VAL HG23 . 18497 1 137 . 1 1 16 16 VAL C C 13 179.545 0.3 . 1 . . . A 16 VAL C . 18497 1 138 . 1 1 16 16 VAL CA C 13 68.000 0.3 . 1 . . . A 16 VAL CA . 18497 1 139 . 1 1 16 16 VAL CB C 13 31.600 0.3 . 1 . . . A 16 VAL CB . 18497 1 140 . 1 1 16 16 VAL CG1 C 13 21.500 0.3 . 1 . . . A 16 VAL CG1 . 18497 1 141 . 1 1 16 16 VAL CG2 C 13 24.300 0.3 . 1 . . . A 16 VAL CG2 . 18497 1 142 . 1 1 16 16 VAL N N 15 117.585 0.3 . 1 . . . A 16 VAL N . 18497 1 143 . 1 1 17 17 LYS H H 1 8.001 0.03 . 1 . . . A 17 LYS H . 18497 1 144 . 1 1 17 17 LYS HA H 1 3.956 0.03 . 1 . . . A 17 LYS HA . 18497 1 145 . 1 1 17 17 LYS HB2 H 1 1.980 0.03 . 2 . . . A 17 LYS HB2 . 18497 1 146 . 1 1 17 17 LYS HB3 H 1 1.980 0.03 . 2 . . . A 17 LYS HB3 . 18497 1 147 . 1 1 17 17 LYS HG2 H 1 1.630 0.03 . 2 . . . A 17 LYS HG2 . 18497 1 148 . 1 1 17 17 LYS HG3 H 1 1.474 0.03 . 2 . . . A 17 LYS HG3 . 18497 1 149 . 1 1 17 17 LYS HD2 H 1 1.930 0.03 . 2 . . . A 17 LYS HD2 . 18497 1 150 . 1 1 17 17 LYS HE2 H 1 2.984 0.03 . 2 . . . A 17 LYS HE2 . 18497 1 151 . 1 1 17 17 LYS C C 13 178.197 0.3 . 1 . . . A 17 LYS C . 18497 1 152 . 1 1 17 17 LYS CA C 13 60.020 0.3 . 1 . . . A 17 LYS CA . 18497 1 153 . 1 1 17 17 LYS CB C 13 32.130 0.3 . 1 . . . A 17 LYS CB . 18497 1 154 . 1 1 17 17 LYS CG C 13 25.200 0.3 . 1 . . . A 17 LYS CG . 18497 1 155 . 1 1 17 17 LYS CD C 13 29.200 0.3 . 1 . . . A 17 LYS CD . 18497 1 156 . 1 1 17 17 LYS CE C 13 41.950 0.3 . 1 . . . A 17 LYS CE . 18497 1 157 . 1 1 17 17 LYS N N 15 119.377 0.3 . 1 . . . A 17 LYS N . 18497 1 158 . 1 1 18 18 GLU H H 1 7.943 0.03 . 1 . . . A 18 GLU H . 18497 1 159 . 1 1 18 18 GLU HA H 1 4.140 0.03 . 1 . . . A 18 GLU HA . 18497 1 160 . 1 1 18 18 GLU HB2 H 1 2.229 0.03 . 2 . . . A 18 GLU HB2 . 18497 1 161 . 1 1 18 18 GLU HB3 H 1 2.171 0.03 . 2 . . . A 18 GLU HB3 . 18497 1 162 . 1 1 18 18 GLU HG2 H 1 2.170 0.03 . 2 . . . A 18 GLU HG2 . 18497 1 163 . 1 1 18 18 GLU HG3 H 1 2.460 0.03 . 2 . . . A 18 GLU HG3 . 18497 1 164 . 1 1 18 18 GLU C C 13 178.849 0.3 . 1 . . . A 18 GLU C . 18497 1 165 . 1 1 18 18 GLU CA C 13 59.800 0.3 . 1 . . . A 18 GLU CA . 18497 1 166 . 1 1 18 18 GLU CB C 13 29.493 0.3 . 1 . . . A 18 GLU CB . 18497 1 167 . 1 1 18 18 GLU CG C 13 36.380 0.3 . 1 . . . A 18 GLU CG . 18497 1 168 . 1 1 18 18 GLU N N 15 120.395 0.3 . 1 . . . A 18 GLU N . 18497 1 169 . 1 1 19 19 VAL H H 1 8.335 0.03 . 1 . . . A 19 VAL H . 18497 1 170 . 1 1 19 19 VAL HA H 1 3.650 0.03 . 1 . . . A 19 VAL HA . 18497 1 171 . 1 1 19 19 VAL HB H 1 2.420 0.03 . 1 . . . A 19 VAL HB . 18497 1 172 . 1 1 19 19 VAL HG11 H 1 1.060 0.03 . 2 . . . A 19 VAL HG11 . 18497 1 173 . 1 1 19 19 VAL HG12 H 1 1.060 0.03 . 2 . . . A 19 VAL HG12 . 18497 1 174 . 1 1 19 19 VAL HG13 H 1 1.060 0.03 . 2 . . . A 19 VAL HG13 . 18497 1 175 . 1 1 19 19 VAL HG21 H 1 1.185 0.03 . 2 . . . A 19 VAL HG21 . 18497 1 176 . 1 1 19 19 VAL HG22 H 1 1.185 0.03 . 2 . . . A 19 VAL HG22 . 18497 1 177 . 1 1 19 19 VAL HG23 H 1 1.185 0.03 . 2 . . . A 19 VAL HG23 . 18497 1 178 . 1 1 19 19 VAL C C 13 179.415 0.3 . 1 . . . A 19 VAL C . 18497 1 179 . 1 1 19 19 VAL CA C 13 67.980 0.3 . 1 . . . A 19 VAL CA . 18497 1 180 . 1 1 19 19 VAL CB C 13 31.600 0.3 . 1 . . . A 19 VAL CB . 18497 1 181 . 1 1 19 19 VAL CG1 C 13 23.900 0.3 . 1 . . . A 19 VAL CG1 . 18497 1 182 . 1 1 19 19 VAL CG2 C 13 23.890 0.3 . 1 . . . A 19 VAL CG2 . 18497 1 183 . 1 1 19 19 VAL N N 15 121.088 0.3 . 1 . . . A 19 VAL N . 18497 1 184 . 1 1 20 20 CYS H H 1 8.434 0.03 . 1 . . . A 20 CYS H . 18497 1 185 . 1 1 20 20 CYS HA H 1 4.680 0.03 . 1 . . . A 20 CYS HA . 18497 1 186 . 1 1 20 20 CYS HB2 H 1 3.240 0.03 . 2 . . . A 20 CYS HB2 . 18497 1 187 . 1 1 20 20 CYS HB3 H 1 3.011 0.03 . 2 . . . A 20 CYS HB3 . 18497 1 188 . 1 1 20 20 CYS C C 13 178.110 0.3 . 1 . . . A 20 CYS C . 18497 1 189 . 1 1 20 20 CYS CA C 13 63.200 0.3 . 1 . . . A 20 CYS CA . 18497 1 190 . 1 1 20 20 CYS CB C 13 26.800 0.3 . 1 . . . A 20 CYS CB . 18497 1 191 . 1 1 20 20 CYS N N 15 117.290 0.3 . 1 . . . A 20 CYS N . 18497 1 192 . 1 1 21 21 GLU H H 1 7.972 0.03 . 1 . . . A 21 GLU H . 18497 1 193 . 1 1 21 21 GLU HA H 1 4.139 0.03 . 1 . . . A 21 GLU HA . 18497 1 194 . 1 1 21 21 GLU HB2 H 1 2.180 0.03 . 2 . . . A 21 GLU HB2 . 18497 1 195 . 1 1 21 21 GLU HB3 H 1 2.130 0.03 . 2 . . . A 21 GLU HB3 . 18497 1 196 . 1 1 21 21 GLU HG2 H 1 2.170 0.03 . 2 . . . A 21 GLU HG2 . 18497 1 197 . 1 1 21 21 GLU HG3 H 1 2.470 0.03 . 2 . . . A 21 GLU HG3 . 18497 1 198 . 1 1 21 21 GLU C C 13 178.153 0.3 . 1 . . . A 21 GLU C . 18497 1 199 . 1 1 21 21 GLU CA C 13 59.750 0.3 . 1 . . . A 21 GLU CA . 18497 1 200 . 1 1 21 21 GLU CB C 13 29.500 0.3 . 1 . . . A 21 GLU CB . 18497 1 201 . 1 1 21 21 GLU CG C 13 36.380 0.3 . 1 . . . A 21 GLU CG . 18497 1 202 . 1 1 21 21 GLU N N 15 118.195 0.3 . 1 . . . A 21 GLU N . 18497 1 203 . 1 1 22 22 LYS H H 1 8.071 0.03 . 1 . . . A 22 LYS H . 18497 1 204 . 1 1 22 22 LYS HA H 1 4.005 0.03 . 1 . . . A 22 LYS HA . 18497 1 205 . 1 1 22 22 LYS HB2 H 1 1.892 0.03 . 2 . . . A 22 LYS HB2 . 18497 1 206 . 1 1 22 22 LYS HB3 H 1 1.652 0.03 . 2 . . . A 22 LYS HB3 . 18497 1 207 . 1 1 22 22 LYS HG2 H 1 1.330 0.03 . 2 . . . A 22 LYS HG2 . 18497 1 208 . 1 1 22 22 LYS HG3 H 1 1.005 0.03 . 2 . . . A 22 LYS HG3 . 18497 1 209 . 1 1 22 22 LYS HD2 H 1 1.560 0.03 . 2 . . . A 22 LYS HD2 . 18497 1 210 . 1 1 22 22 LYS C C 13 179.371 0.3 . 1 . . . A 22 LYS C . 18497 1 211 . 1 1 22 22 LYS CA C 13 58.700 0.3 . 1 . . . A 22 LYS CA . 18497 1 212 . 1 1 22 22 LYS CB C 13 32.920 0.3 . 1 . . . A 22 LYS CB . 18497 1 213 . 1 1 22 22 LYS CG C 13 24.960 0.3 . 1 . . . A 22 LYS CG . 18497 1 214 . 1 1 22 22 LYS CD C 13 28.700 0.3 . 1 . . . A 22 LYS CD . 18497 1 215 . 1 1 22 22 LYS N N 15 119.095 0.3 . 1 . . . A 22 LYS N . 18497 1 216 . 1 1 23 23 PHE H H 1 8.491 0.03 . 1 . . . A 23 PHE H . 18497 1 217 . 1 1 23 23 PHE HA H 1 4.430 0.03 . 1 . . . A 23 PHE HA . 18497 1 218 . 1 1 23 23 PHE HB2 H 1 3.195 0.03 . 2 . . . A 23 PHE HB2 . 18497 1 219 . 1 1 23 23 PHE HB3 H 1 2.830 0.03 . 2 . . . A 23 PHE HB3 . 18497 1 220 . 1 1 23 23 PHE HD2 H 1 7.475 0.03 . 3 . . . A 23 PHE HD2 . 18497 1 221 . 1 1 23 23 PHE HE1 H 1 7.350 0.03 . 3 . . . A 23 PHE HE1 . 18497 1 222 . 1 1 23 23 PHE HE2 H 1 7.240 0.03 . 3 . . . A 23 PHE HE2 . 18497 1 223 . 1 1 23 23 PHE C C 13 178.197 0.3 . 1 . . . A 23 PHE C . 18497 1 224 . 1 1 23 23 PHE CA C 13 58.430 0.3 . 1 . . . A 23 PHE CA . 18497 1 225 . 1 1 23 23 PHE CB C 13 38.770 0.3 . 1 . . . A 23 PHE CB . 18497 1 226 . 1 1 23 23 PHE N N 15 114.252 0.3 . 1 . . . A 23 PHE N . 18497 1 227 . 1 1 24 24 GLU H H 1 7.867 0.03 . 1 . . . A 24 GLU H . 18497 1 228 . 1 1 24 24 GLU HA H 1 4.070 0.03 . 1 . . . A 24 GLU HA . 18497 1 229 . 1 1 24 24 GLU HB2 H 1 2.180 0.03 . 2 . . . A 24 GLU HB2 . 18497 1 230 . 1 1 24 24 GLU HB3 H 1 2.180 0.03 . 2 . . . A 24 GLU HB3 . 18497 1 231 . 1 1 24 24 GLU HG2 H 1 2.210 0.03 . 2 . . . A 24 GLU HG2 . 18497 1 232 . 1 1 24 24 GLU HG3 H 1 2.125 0.03 . 2 . . . A 24 GLU HG3 . 18497 1 233 . 1 1 24 24 GLU C C 13 177.457 0.3 . 1 . . . A 24 GLU C . 18497 1 234 . 1 1 24 24 GLU CA C 13 56.830 0.3 . 1 . . . A 24 GLU CA . 18497 1 235 . 1 1 24 24 GLU CB C 13 26.800 0.3 . 1 . . . A 24 GLU CB . 18497 1 236 . 1 1 24 24 GLU CG C 13 36.900 0.3 . 1 . . . A 24 GLU CG . 18497 1 237 . 1 1 24 24 GLU N N 15 119.819 0.3 . 1 . . . A 24 GLU N . 18497 1 238 . 1 1 25 25 CYS H H 1 8.156 0.03 . 1 . . . A 25 CYS H . 18497 1 239 . 1 1 25 25 CYS HA H 1 5.387 0.03 . 1 . . . A 25 CYS HA . 18497 1 240 . 1 1 25 25 CYS HB2 H 1 3.450 0.03 . 2 . . . A 25 CYS HB2 . 18497 1 241 . 1 1 25 25 CYS HB3 H 1 2.560 0.03 . 2 . . . A 25 CYS HB3 . 18497 1 242 . 1 1 25 25 CYS C C 13 174.760 0.3 . 1 . . . A 25 CYS C . 18497 1 243 . 1 1 25 25 CYS CA C 13 54.761 0.3 . 1 . . . A 25 CYS CA . 18497 1 244 . 1 1 25 25 CYS CB C 13 31.600 0.3 . 1 . . . A 25 CYS CB . 18497 1 245 . 1 1 25 25 CYS N N 15 114.633 0.3 . 1 . . . A 25 CYS N . 18497 1 246 . 1 1 26 26 THR H H 1 8.460 0.03 . 1 . . . A 26 THR H . 18497 1 247 . 1 1 26 26 THR HA H 1 4.770 0.03 . 1 . . . A 26 THR HA . 18497 1 248 . 1 1 26 26 THR HB H 1 4.667 0.03 . 1 . . . A 26 THR HB . 18497 1 249 . 1 1 26 26 THR HG21 H 1 1.308 0.03 . 1 . . . A 26 THR HG21 . 18497 1 250 . 1 1 26 26 THR HG22 H 1 1.308 0.03 . 1 . . . A 26 THR HG22 . 18497 1 251 . 1 1 26 26 THR HG23 H 1 1.308 0.03 . 1 . . . A 26 THR HG23 . 18497 1 252 . 1 1 26 26 THR C C 13 173.499 0.3 . 1 . . . A 26 THR C . 18497 1 253 . 1 1 26 26 THR CA C 13 60.723 0.3 . 1 . . . A 26 THR CA . 18497 1 254 . 1 1 26 26 THR CB C 13 72.000 0.3 . 1 . . . A 26 THR CB . 18497 1 255 . 1 1 26 26 THR CG2 C 13 21.500 0.3 . 1 . . . A 26 THR CG2 . 18497 1 256 . 1 1 26 26 THR N N 15 109.312 0.3 . 1 . . . A 26 THR N . 18497 1 257 . 1 1 27 27 GLU H H 1 9.327 0.03 . 1 . . . A 27 GLU H . 18497 1 258 . 1 1 27 27 GLU HA H 1 3.510 0.03 . 1 . . . A 27 GLU HA . 18497 1 259 . 1 1 27 27 GLU HB2 H 1 2.040 0.03 . 2 . . . A 27 GLU HB2 . 18497 1 260 . 1 1 27 27 GLU HB3 H 1 1.980 0.03 . 2 . . . A 27 GLU HB3 . 18497 1 261 . 1 1 27 27 GLU HG2 H 1 2.325 0.03 . 2 . . . A 27 GLU HG2 . 18497 1 262 . 1 1 27 27 GLU HG3 H 1 2.253 0.03 . 2 . . . A 27 GLU HG3 . 18497 1 263 . 1 1 27 27 GLU C C 13 176.544 0.3 . 1 . . . A 27 GLU C . 18497 1 264 . 1 1 27 27 GLU CA C 13 60.550 0.3 . 1 . . . A 27 GLU CA . 18497 1 265 . 1 1 27 27 GLU CB C 13 28.950 0.3 . 1 . . . A 27 GLU CB . 18497 1 266 . 1 1 27 27 GLU CG C 13 36.640 0.3 . 1 . . . A 27 GLU CG . 18497 1 267 . 1 1 27 27 GLU N N 15 122.233 0.3 . 1 . . . A 27 GLU N . 18497 1 268 . 1 1 28 28 SER H H 1 8.320 0.03 . 1 . . . A 28 SER H . 18497 1 269 . 1 1 28 28 SER HA H 1 4.062 0.03 . 1 . . . A 28 SER HA . 18497 1 270 . 1 1 28 28 SER HB2 H 1 3.840 0.03 . 2 . . . A 28 SER HB2 . 18497 1 271 . 1 1 28 28 SER HB3 H 1 3.840 0.03 . 2 . . . A 28 SER HB3 . 18497 1 272 . 1 1 28 28 SER C C 13 178.545 0.3 . 1 . . . A 28 SER C . 18497 1 273 . 1 1 28 28 SER CA C 13 61.350 0.3 . 1 . . . A 28 SER CA . 18497 1 274 . 1 1 28 28 SER CB C 13 62.400 0.3 . 1 . . . A 28 SER CB . 18497 1 275 . 1 1 28 28 SER N N 15 112.925 0.3 . 1 . . . A 28 SER N . 18497 1 276 . 1 1 29 29 GLU H H 1 7.512 0.03 . 1 . . . A 29 GLU H . 18497 1 277 . 1 1 29 29 GLU HA H 1 3.990 0.03 . 1 . . . A 29 GLU HA . 18497 1 278 . 1 1 29 29 GLU HB2 H 1 2.318 0.03 . 2 . . . A 29 GLU HB2 . 18497 1 279 . 1 1 29 29 GLU HB3 H 1 1.937 0.03 . 2 . . . A 29 GLU HB3 . 18497 1 280 . 1 1 29 29 GLU HG2 H 1 2.280 0.03 . 2 . . . A 29 GLU HG2 . 18497 1 281 . 1 1 29 29 GLU HG3 H 1 2.280 0.03 . 2 . . . A 29 GLU HG3 . 18497 1 282 . 1 1 29 29 GLU C C 13 176.674 0.3 . 1 . . . A 29 GLU C . 18497 1 283 . 1 1 29 29 GLU CA C 13 59.750 0.3 . 1 . . . A 29 GLU CA . 18497 1 284 . 1 1 29 29 GLU CB C 13 29.470 0.3 . 1 . . . A 29 GLU CB . 18497 1 285 . 1 1 29 29 GLU CG C 13 37.924 0.3 . 1 . . . A 29 GLU CG . 18497 1 286 . 1 1 29 29 GLU N N 15 121.736 0.3 . 1 . . . A 29 GLU N . 18497 1 287 . 1 1 30 30 VAL H H 1 7.492 0.03 . 1 . . . A 30 VAL H . 18497 1 288 . 1 1 30 30 VAL HA H 1 3.377 0.03 . 1 . . . A 30 VAL HA . 18497 1 289 . 1 1 30 30 VAL HB H 1 2.086 0.03 . 1 . . . A 30 VAL HB . 18497 1 290 . 1 1 30 30 VAL HG11 H 1 0.740 0.03 . 2 . . . A 30 VAL HG11 . 18497 1 291 . 1 1 30 30 VAL HG12 H 1 0.740 0.03 . 2 . . . A 30 VAL HG12 . 18497 1 292 . 1 1 30 30 VAL HG13 H 1 0.740 0.03 . 2 . . . A 30 VAL HG13 . 18497 1 293 . 1 1 30 30 VAL HG21 H 1 1.060 0.03 . 2 . . . A 30 VAL HG21 . 18497 1 294 . 1 1 30 30 VAL HG22 H 1 1.060 0.03 . 2 . . . A 30 VAL HG22 . 18497 1 295 . 1 1 30 30 VAL HG23 H 1 1.060 0.03 . 2 . . . A 30 VAL HG23 . 18497 1 296 . 1 1 30 30 VAL C C 13 179.241 0.3 . 1 . . . A 30 VAL C . 18497 1 297 . 1 1 30 30 VAL CA C 13 66.660 0.3 . 1 . . . A 30 VAL CA . 18497 1 298 . 1 1 30 30 VAL CB C 13 31.070 0.3 . 1 . . . A 30 VAL CB . 18497 1 299 . 1 1 30 30 VAL CG1 C 13 21.240 0.3 . 1 . . . A 30 VAL CG1 . 18497 1 300 . 1 1 30 30 VAL CG2 C 13 24.420 0.3 . 1 . . . A 30 VAL CG2 . 18497 1 301 . 1 1 30 30 VAL N N 15 119.480 0.3 . 1 . . . A 30 VAL N . 18497 1 302 . 1 1 31 31 MET H H 1 8.302 0.03 . 1 . . . A 31 MET H . 18497 1 303 . 1 1 31 31 MET HA H 1 3.870 0.03 . 1 . . . A 31 MET HA . 18497 1 304 . 1 1 31 31 MET HB2 H 1 2.067 0.03 . 2 . . . A 31 MET HB2 . 18497 1 305 . 1 1 31 31 MET HB3 H 1 1.900 0.03 . 2 . . . A 31 MET HB3 . 18497 1 306 . 1 1 31 31 MET HG2 H 1 2.650 0.03 . 2 . . . A 31 MET HG2 . 18497 1 307 . 1 1 31 31 MET HG3 H 1 2.510 0.03 . 2 . . . A 31 MET HG3 . 18497 1 308 . 1 1 31 31 MET C C 13 177.936 0.3 . 1 . . . A 31 MET C . 18497 1 309 . 1 1 31 31 MET CA C 13 57.630 0.3 . 1 . . . A 31 MET CA . 18497 1 310 . 1 1 31 31 MET CB C 13 30.270 0.3 . 1 . . . A 31 MET CB . 18497 1 311 . 1 1 31 31 MET CG C 13 32.130 0.3 . 1 . . . A 31 MET CG . 18497 1 312 . 1 1 31 31 MET N N 15 117.220 0.3 . 1 . . . A 31 MET N . 18497 1 313 . 1 1 32 32 ASN H H 1 8.313 0.03 . 1 . . . A 32 ASN H . 18497 1 314 . 1 1 32 32 ASN HA H 1 4.390 0.03 . 1 . . . A 32 ASN HA . 18497 1 315 . 1 1 32 32 ASN HB2 H 1 2.800 0.03 . 2 . . . A 32 ASN HB2 . 18497 1 316 . 1 1 32 32 ASN HB3 H 1 2.860 0.03 . 2 . . . A 32 ASN HB3 . 18497 1 317 . 1 1 32 32 ASN C C 13 176.065 0.3 . 1 . . . A 32 ASN C . 18497 1 318 . 1 1 32 32 ASN CA C 13 56.030 0.3 . 1 . . . A 32 ASN CA . 18497 1 319 . 1 1 32 32 ASN CB C 13 37.710 0.3 . 1 . . . A 32 ASN CB . 18497 1 320 . 1 1 32 32 ASN N N 15 116.672 0.3 . 1 . . . A 32 ASN N . 18497 1 321 . 1 1 33 33 SER H H 1 7.851 0.03 . 1 . . . A 33 SER H . 18497 1 322 . 1 1 33 33 SER HA H 1 4.150 0.03 . 1 . . . A 33 SER HA . 18497 1 323 . 1 1 33 33 SER HB2 H 1 3.790 0.03 . 2 . . . A 33 SER HB2 . 18497 1 324 . 1 1 33 33 SER HB3 H 1 3.947 0.03 . 2 . . . A 33 SER HB3 . 18497 1 325 . 1 1 33 33 SER C C 13 178.806 0.3 . 1 . . . A 33 SER C . 18497 1 326 . 1 1 33 33 SER CA C 13 62.950 0.3 . 1 . . . A 33 SER CA . 18497 1 327 . 1 1 33 33 SER CB C 13 62.600 0.3 . 1 . . . A 33 SER CB . 18497 1 328 . 1 1 33 33 SER N N 15 117.471 0.3 . 1 . . . A 33 SER N . 18497 1 329 . 1 1 34 34 LEU H H 1 8.128 0.03 . 1 . . . A 34 LEU H . 18497 1 330 . 1 1 34 34 LEU HA H 1 3.879 0.03 . 1 . . . A 34 LEU HA . 18497 1 331 . 1 1 34 34 LEU HB2 H 1 1.530 0.03 . 2 . . . A 34 LEU HB2 . 18497 1 332 . 1 1 34 34 LEU HB3 H 1 0.930 0.03 . 2 . . . A 34 LEU HB3 . 18497 1 333 . 1 1 34 34 LEU HG H 1 1.379 0.03 . 1 . . . A 34 LEU HG . 18497 1 334 . 1 1 34 34 LEU HD11 H 1 -0.051 0.03 . 2 . . . A 34 LEU HD11 . 18497 1 335 . 1 1 34 34 LEU HD12 H 1 -0.051 0.03 . 2 . . . A 34 LEU HD12 . 18497 1 336 . 1 1 34 34 LEU HD13 H 1 -0.051 0.03 . 2 . . . A 34 LEU HD13 . 18497 1 337 . 1 1 34 34 LEU HD21 H 1 0.310 0.03 . 2 . . . A 34 LEU HD21 . 18497 1 338 . 1 1 34 34 LEU HD22 H 1 0.310 0.03 . 2 . . . A 34 LEU HD22 . 18497 1 339 . 1 1 34 34 LEU HD23 H 1 0.310 0.03 . 2 . . . A 34 LEU HD23 . 18497 1 340 . 1 1 34 34 LEU C C 13 177.892 0.3 . 1 . . . A 34 LEU C . 18497 1 341 . 1 1 34 34 LEU CA C 13 57.630 0.3 . 1 . . . A 34 LEU CA . 18497 1 342 . 1 1 34 34 LEU CB C 13 40.800 0.3 . 1 . . . A 34 LEU CB . 18497 1 343 . 1 1 34 34 LEU CG C 13 26.020 0.3 . 1 . . . A 34 LEU CG . 18497 1 344 . 1 1 34 34 LEU CD1 C 13 23.890 0.3 . 1 . . . A 34 LEU CD1 . 18497 1 345 . 1 1 34 34 LEU CD2 C 13 22.030 0.3 . 1 . . . A 34 LEU CD2 . 18497 1 346 . 1 1 34 34 LEU N N 15 122.839 0.3 . 1 . . . A 34 LEU N . 18497 1 347 . 1 1 35 35 TYR H H 1 7.924 0.03 . 1 . . . A 35 TYR H . 18497 1 348 . 1 1 35 35 TYR HA H 1 4.610 0.03 . 1 . . . A 35 TYR HA . 18497 1 349 . 1 1 35 35 TYR HB2 H 1 3.272 0.03 . 2 . . . A 35 TYR HB2 . 18497 1 350 . 1 1 35 35 TYR HB3 H 1 2.851 0.03 . 2 . . . A 35 TYR HB3 . 18497 1 351 . 1 1 35 35 TYR C C 13 179.067 0.3 . 1 . . . A 35 TYR C . 18497 1 352 . 1 1 35 35 TYR CA C 13 57.890 0.3 . 1 . . . A 35 TYR CA . 18497 1 353 . 1 1 35 35 TYR CB C 13 37.710 0.3 . 1 . . . A 35 TYR CB . 18497 1 354 . 1 1 35 35 TYR N N 15 116.666 0.3 . 1 . . . A 35 TYR N . 18497 1 355 . 1 1 36 36 SER H H 1 7.715 0.03 . 1 . . . A 36 SER H . 18497 1 356 . 1 1 36 36 SER HA H 1 4.080 0.03 . 1 . . . A 36 SER HA . 18497 1 357 . 1 1 36 36 SER HB2 H 1 4.210 0.03 . 2 . . . A 36 SER HB2 . 18497 1 358 . 1 1 36 36 SER HB3 H 1 4.280 0.03 . 2 . . . A 36 SER HB3 . 18497 1 359 . 1 1 36 36 SER C C 13 177.283 0.3 . 1 . . . A 36 SER C . 18497 1 360 . 1 1 36 36 SER CA C 13 60.519 0.3 . 1 . . . A 36 SER CA . 18497 1 361 . 1 1 36 36 SER CB C 13 64.240 0.3 . 1 . . . A 36 SER CB . 18497 1 362 . 1 1 36 36 SER N N 15 114.801 0.3 . 1 . . . A 36 SER N . 18497 1 363 . 1 1 37 37 GLY H H 1 8.017 0.03 . 1 . . . A 37 GLY H . 18497 1 364 . 1 1 37 37 GLY HA2 H 1 4.100 0.03 . 2 . . . A 37 GLY HA2 . 18497 1 365 . 1 1 37 37 GLY HA3 H 1 3.790 0.03 . 2 . . . A 37 GLY HA3 . 18497 1 366 . 1 1 37 37 GLY C C 13 175.978 0.3 . 1 . . . A 37 GLY C . 18497 1 367 . 1 1 37 37 GLY CA C 13 45.678 0.3 . 1 . . . A 37 GLY CA . 18497 1 368 . 1 1 37 37 GLY N N 15 109.803 0.3 . 1 . . . A 37 GLY N . 18497 1 369 . 1 1 38 38 ASP H H 1 8.006 0.03 . 1 . . . A 38 ASP H . 18497 1 370 . 1 1 38 38 ASP HA H 1 5.025 0.03 . 1 . . . A 38 ASP HA . 18497 1 371 . 1 1 38 38 ASP HB2 H 1 2.570 0.03 . 2 . . . A 38 ASP HB2 . 18497 1 372 . 1 1 38 38 ASP HB3 H 1 2.950 0.03 . 2 . . . A 38 ASP HB3 . 18497 1 373 . 1 1 38 38 ASP C C 13 173.368 0.3 . 1 . . . A 38 ASP C . 18497 1 374 . 1 1 38 38 ASP CA C 13 50.720 0.3 . 1 . . . A 38 ASP CA . 18497 1 375 . 1 1 38 38 ASP CB C 13 41.420 0.3 . 1 . . . A 38 ASP CB . 18497 1 376 . 1 1 38 38 ASP N N 15 120.613 0.3 . 1 . . . A 38 ASP N . 18497 1 377 . 1 1 39 39 PRO HA H 1 4.340 0.03 . 1 . . . A 39 PRO HA . 18497 1 378 . 1 1 39 39 PRO HB2 H 1 2.220 0.03 . 2 . . . A 39 PRO HB2 . 18497 1 379 . 1 1 39 39 PRO HB3 H 1 1.822 0.03 . 2 . . . A 39 PRO HB3 . 18497 1 380 . 1 1 39 39 PRO HG2 H 1 2.030 0.03 . 2 . . . A 39 PRO HG2 . 18497 1 381 . 1 1 39 39 PRO HG3 H 1 1.970 0.03 . 2 . . . A 39 PRO HG3 . 18497 1 382 . 1 1 39 39 PRO CA C 13 63.750 0.3 . 1 . . . A 39 PRO CA . 18497 1 383 . 1 1 39 39 PRO CB C 13 32.130 0.3 . 1 . . . A 39 PRO CB . 18497 1 384 . 1 1 39 39 PRO CG C 13 26.800 0.3 . 1 . . . A 39 PRO CG . 18497 1 385 . 1 1 39 39 PRO CD C 13 49.579 0.3 . 1 . . . A 39 PRO CD . 18497 1 386 . 1 1 40 40 GLN H H 1 8.237 0.03 . 1 . . . A 40 GLN H . 18497 1 387 . 1 1 40 40 GLN HA H 1 4.280 0.03 . 1 . . . A 40 GLN HA . 18497 1 388 . 1 1 40 40 GLN HB2 H 1 2.269 0.03 . 2 . . . A 40 GLN HB2 . 18497 1 389 . 1 1 40 40 GLN HB3 H 1 1.990 0.03 . 2 . . . A 40 GLN HB3 . 18497 1 390 . 1 1 40 40 GLN HG2 H 1 2.350 0.03 . 2 . . . A 40 GLN HG2 . 18497 1 391 . 1 1 40 40 GLN HG3 H 1 2.250 0.03 . 2 . . . A 40 GLN HG3 . 18497 1 392 . 1 1 40 40 GLN HE21 H 1 6.960 0.03 . 2 . . . A 40 GLN HE21 . 18497 1 393 . 1 1 40 40 GLN HE22 H 1 7.480 0.03 . 2 . . . A 40 GLN HE22 . 18497 1 394 . 1 1 40 40 GLN C C 13 177.066 0.3 . 1 . . . A 40 GLN C . 18497 1 395 . 1 1 40 40 GLN CA C 13 54.710 0.3 . 1 . . . A 40 GLN CA . 18497 1 396 . 1 1 40 40 GLN CB C 13 28.680 0.3 . 1 . . . A 40 GLN CB . 18497 1 397 . 1 1 40 40 GLN CG C 13 34.250 0.3 . 1 . . . A 40 GLN CG . 18497 1 398 . 1 1 40 40 GLN N N 15 115.056 0.3 . 1 . . . A 40 GLN N . 18497 1 399 . 1 1 40 40 GLN NE2 N 15 111.960 0.3 . 1 . . . A 40 GLN NE2 . 18497 1 400 . 1 1 41 41 ASP H H 1 7.211 0.03 . 1 . . . A 41 ASP H . 18497 1 401 . 1 1 41 41 ASP HA H 1 4.313 0.03 . 1 . . . A 41 ASP HA . 18497 1 402 . 1 1 41 41 ASP HB2 H 1 2.700 0.03 . 2 . . . A 41 ASP HB2 . 18497 1 403 . 1 1 41 41 ASP HB3 H 1 2.700 0.03 . 2 . . . A 41 ASP HB3 . 18497 1 404 . 1 1 41 41 ASP C C 13 175.804 0.3 . 1 . . . A 41 ASP C . 18497 1 405 . 1 1 41 41 ASP CA C 13 55.240 0.3 . 1 . . . A 41 ASP CA . 18497 1 406 . 1 1 41 41 ASP CB C 13 42.220 0.3 . 1 . . . A 41 ASP CB . 18497 1 407 . 1 1 41 41 ASP N N 15 122.839 0.3 . 1 . . . A 41 ASP N . 18497 1 408 . 1 1 42 42 GLN H H 1 8.719 0.03 . 1 . . . A 42 GLN H . 18497 1 409 . 1 1 42 42 GLN HA H 1 3.860 0.03 . 1 . . . A 42 GLN HA . 18497 1 410 . 1 1 42 42 GLN HB2 H 1 2.040 0.03 . 2 . . . A 42 GLN HB2 . 18497 1 411 . 1 1 42 42 GLN HB3 H 1 2.040 0.03 . 2 . . . A 42 GLN HB3 . 18497 1 412 . 1 1 42 42 GLN HG2 H 1 2.270 0.03 . 2 . . . A 42 GLN HG2 . 18497 1 413 . 1 1 42 42 GLN HG3 H 1 2.200 0.03 . 2 . . . A 42 GLN HG3 . 18497 1 414 . 1 1 42 42 GLN C C 13 177.196 0.3 . 1 . . . A 42 GLN C . 18497 1 415 . 1 1 42 42 GLN CA C 13 59.220 0.3 . 1 . . . A 42 GLN CA . 18497 1 416 . 1 1 42 42 GLN CB C 13 28.400 0.3 . 1 . . . A 42 GLN CB . 18497 1 417 . 1 1 42 42 GLN CG C 13 33.362 0.3 . 1 . . . A 42 GLN CG . 18497 1 418 . 1 1 42 42 GLN N N 15 124.547 0.3 . 1 . . . A 42 GLN N . 18497 1 419 . 1 1 43 43 LEU H H 1 8.206 0.03 . 1 . . . A 43 LEU H . 18497 1 420 . 1 1 43 43 LEU HA H 1 3.685 0.03 . 1 . . . A 43 LEU HA . 18497 1 421 . 1 1 43 43 LEU HB2 H 1 1.930 0.03 . 2 . . . A 43 LEU HB2 . 18497 1 422 . 1 1 43 43 LEU HB3 H 1 1.058 0.03 . 2 . . . A 43 LEU HB3 . 18497 1 423 . 1 1 43 43 LEU HG H 1 1.520 0.03 . 1 . . . A 43 LEU HG . 18497 1 424 . 1 1 43 43 LEU HD11 H 1 0.760 0.03 . 2 . . . A 43 LEU HD11 . 18497 1 425 . 1 1 43 43 LEU HD12 H 1 0.760 0.03 . 2 . . . A 43 LEU HD12 . 18497 1 426 . 1 1 43 43 LEU HD13 H 1 0.760 0.03 . 2 . . . A 43 LEU HD13 . 18497 1 427 . 1 1 43 43 LEU HD21 H 1 0.214 0.03 . 2 . . . A 43 LEU HD21 . 18497 1 428 . 1 1 43 43 LEU HD22 H 1 0.214 0.03 . 2 . . . A 43 LEU HD22 . 18497 1 429 . 1 1 43 43 LEU HD23 H 1 0.214 0.03 . 2 . . . A 43 LEU HD23 . 18497 1 430 . 1 1 43 43 LEU C C 13 178.066 0.3 . 1 . . . A 43 LEU C . 18497 1 431 . 1 1 43 43 LEU CA C 13 57.360 0.3 . 1 . . . A 43 LEU CA . 18497 1 432 . 1 1 43 43 LEU CB C 13 40.390 0.3 . 1 . . . A 43 LEU CB . 18497 1 433 . 1 1 43 43 LEU CG C 13 26.820 0.3 . 1 . . . A 43 LEU CG . 18497 1 434 . 1 1 43 43 LEU CD1 C 13 24.960 0.3 . 1 . . . A 43 LEU CD1 . 18497 1 435 . 1 1 43 43 LEU CD2 C 13 22.030 0.3 . 1 . . . A 43 LEU CD2 . 18497 1 436 . 1 1 43 43 LEU N N 15 118.960 0.3 . 1 . . . A 43 LEU N . 18497 1 437 . 1 1 44 44 ALA H H 1 7.402 0.03 . 1 . . . A 44 ALA H . 18497 1 438 . 1 1 44 44 ALA HA H 1 3.879 0.03 . 1 . . . A 44 ALA HA . 18497 1 439 . 1 1 44 44 ALA HB1 H 1 1.410 0.03 . 1 . . . A 44 ALA HB1 . 18497 1 440 . 1 1 44 44 ALA HB2 H 1 1.410 0.03 . 1 . . . A 44 ALA HB2 . 18497 1 441 . 1 1 44 44 ALA HB3 H 1 1.410 0.03 . 1 . . . A 44 ALA HB3 . 18497 1 442 . 1 1 44 44 ALA C C 13 178.327 0.3 . 1 . . . A 44 ALA C . 18497 1 443 . 1 1 44 44 ALA CA C 13 54.710 0.3 . 1 . . . A 44 ALA CA . 18497 1 444 . 1 1 44 44 ALA CB C 13 18.580 0.3 . 1 . . . A 44 ALA CB . 18497 1 445 . 1 1 44 44 ALA N N 15 121.666 0.3 . 1 . . . A 44 ALA N . 18497 1 446 . 1 1 45 45 VAL H H 1 8.449 0.03 . 1 . . . A 45 VAL H . 18497 1 447 . 1 1 45 45 VAL HA H 1 3.660 0.03 . 1 . . . A 45 VAL HA . 18497 1 448 . 1 1 45 45 VAL HB H 1 1.949 0.03 . 1 . . . A 45 VAL HB . 18497 1 449 . 1 1 45 45 VAL HG11 H 1 0.730 0.03 . 2 . . . A 45 VAL HG11 . 18497 1 450 . 1 1 45 45 VAL HG12 H 1 0.730 0.03 . 2 . . . A 45 VAL HG12 . 18497 1 451 . 1 1 45 45 VAL HG13 H 1 0.730 0.03 . 2 . . . A 45 VAL HG13 . 18497 1 452 . 1 1 45 45 VAL HG21 H 1 0.990 0.03 . 2 . . . A 45 VAL HG21 . 18497 1 453 . 1 1 45 45 VAL HG22 H 1 0.990 0.03 . 2 . . . A 45 VAL HG22 . 18497 1 454 . 1 1 45 45 VAL HG23 H 1 0.990 0.03 . 2 . . . A 45 VAL HG23 . 18497 1 455 . 1 1 45 45 VAL C C 13 179.893 0.3 . 1 . . . A 45 VAL C . 18497 1 456 . 1 1 45 45 VAL CA C 13 66.400 0.3 . 1 . . . A 45 VAL CA . 18497 1 457 . 1 1 45 45 VAL CB C 13 32.131 0.3 . 1 . . . A 45 VAL CB . 18497 1 458 . 1 1 45 45 VAL CG1 C 13 21.230 0.3 . 1 . . . A 45 VAL CG1 . 18497 1 459 . 1 1 45 45 VAL CG2 C 13 23.360 0.3 . 1 . . . A 45 VAL CG2 . 18497 1 460 . 1 1 45 45 VAL N N 15 118.589 0.3 . 1 . . . A 45 VAL N . 18497 1 461 . 1 1 46 46 ALA H H 1 7.654 0.03 . 1 . . . A 46 ALA H . 18497 1 462 . 1 1 46 46 ALA HA H 1 4.130 0.03 . 1 . . . A 46 ALA HA . 18497 1 463 . 1 1 46 46 ALA HB1 H 1 1.610 0.03 . 1 . . . A 46 ALA HB1 . 18497 1 464 . 1 1 46 46 ALA HB2 H 1 1.610 0.03 . 1 . . . A 46 ALA HB2 . 18497 1 465 . 1 1 46 46 ALA HB3 H 1 1.610 0.03 . 1 . . . A 46 ALA HB3 . 18497 1 466 . 1 1 46 46 ALA C C 13 179.110 0.3 . 1 . . . A 46 ALA C . 18497 1 467 . 1 1 46 46 ALA CA C 13 54.970 0.3 . 1 . . . A 46 ALA CA . 18497 1 468 . 1 1 46 46 ALA CB C 13 19.110 0.3 . 1 . . . A 46 ALA CB . 18497 1 469 . 1 1 46 46 ALA N N 15 121.006 0.3 . 1 . . . A 46 ALA N . 18497 1 470 . 1 1 47 47 TYR H H 1 8.077 0.03 . 1 . . . A 47 TYR H . 18497 1 471 . 1 1 47 47 TYR HA H 1 3.750 0.03 . 1 . . . A 47 TYR HA . 18497 1 472 . 1 1 47 47 TYR HB2 H 1 3.090 0.03 . 2 . . . A 47 TYR HB2 . 18497 1 473 . 1 1 47 47 TYR HB3 H 1 2.770 0.03 . 2 . . . A 47 TYR HB3 . 18497 1 474 . 1 1 47 47 TYR HD2 H 1 6.200 0.03 . 3 . . . A 47 TYR HD2 . 18497 1 475 . 1 1 47 47 TYR C C 13 179.328 0.3 . 1 . . . A 47 TYR C . 18497 1 476 . 1 1 47 47 TYR CA C 13 61.880 0.3 . 1 . . . A 47 TYR CA . 18497 1 477 . 1 1 47 47 TYR CB C 13 38.500 0.3 . 1 . . . A 47 TYR CB . 18497 1 478 . 1 1 47 47 TYR N N 15 119.140 0.3 . 1 . . . A 47 TYR N . 18497 1 479 . 1 1 48 48 HIS H H 1 8.326 0.03 . 1 . . . A 48 HIS H . 18497 1 480 . 1 1 48 48 HIS HA H 1 4.100 0.03 . 1 . . . A 48 HIS HA . 18497 1 481 . 1 1 48 48 HIS HB2 H 1 3.210 0.03 . 2 . . . A 48 HIS HB2 . 18497 1 482 . 1 1 48 48 HIS HB3 H 1 3.210 0.03 . 2 . . . A 48 HIS HB3 . 18497 1 483 . 1 1 48 48 HIS C C 13 178.023 0.3 . 1 . . . A 48 HIS C . 18497 1 484 . 1 1 48 48 HIS CA C 13 60.020 0.3 . 1 . . . A 48 HIS CA . 18497 1 485 . 1 1 48 48 HIS CB C 13 28.940 0.3 . 1 . . . A 48 HIS CB . 18497 1 486 . 1 1 48 48 HIS N N 15 116.422 0.3 . 1 . . . A 48 HIS N . 18497 1 487 . 1 1 49 49 LEU H H 1 8.237 0.03 . 1 . . . A 49 LEU H . 18497 1 488 . 1 1 49 49 LEU HA H 1 4.155 0.03 . 1 . . . A 49 LEU HA . 18497 1 489 . 1 1 49 49 LEU HB2 H 1 1.835 0.03 . 2 . . . A 49 LEU HB2 . 18497 1 490 . 1 1 49 49 LEU HB3 H 1 1.710 0.03 . 2 . . . A 49 LEU HB3 . 18497 1 491 . 1 1 49 49 LEU HG H 1 1.760 0.03 . 1 . . . A 49 LEU HG . 18497 1 492 . 1 1 49 49 LEU HD11 H 1 0.940 0.03 . 2 . . . A 49 LEU HD11 . 18497 1 493 . 1 1 49 49 LEU HD12 H 1 0.940 0.03 . 2 . . . A 49 LEU HD12 . 18497 1 494 . 1 1 49 49 LEU HD13 H 1 0.940 0.03 . 2 . . . A 49 LEU HD13 . 18497 1 495 . 1 1 49 49 LEU HD21 H 1 0.940 0.03 . 2 . . . A 49 LEU HD21 . 18497 1 496 . 1 1 49 49 LEU HD22 H 1 0.940 0.03 . 2 . . . A 49 LEU HD22 . 18497 1 497 . 1 1 49 49 LEU HD23 H 1 0.940 0.03 . 2 . . . A 49 LEU HD23 . 18497 1 498 . 1 1 49 49 LEU C C 13 177.417 0.3 . 1 . . . A 49 LEU C . 18497 1 499 . 1 1 49 49 LEU CA C 13 57.890 0.3 . 1 . . . A 49 LEU CA . 18497 1 500 . 1 1 49 49 LEU CB C 13 41.960 0.3 . 1 . . . A 49 LEU CB . 18497 1 501 . 1 1 49 49 LEU CG C 13 26.800 0.3 . 1 . . . A 49 LEU CG . 18497 1 502 . 1 1 49 49 LEU CD1 C 13 24.700 0.3 . 1 . . . A 49 LEU CD1 . 18497 1 503 . 1 1 49 49 LEU CD2 C 13 20.700 0.3 . 1 . . . A 49 LEU CD2 . 18497 1 504 . 1 1 49 49 LEU N N 15 120.974 0.3 . 1 . . . A 49 LEU N . 18497 1 505 . 1 1 50 50 ILE H H 1 7.543 0.03 . 1 . . . A 50 ILE H . 18497 1 506 . 1 1 50 50 ILE HA H 1 3.620 0.03 . 1 . . . A 50 ILE HA . 18497 1 507 . 1 1 50 50 ILE HB H 1 1.820 0.03 . 1 . . . A 50 ILE HB . 18497 1 508 . 1 1 50 50 ILE HG12 H 1 1.720 0.03 . 1 . . . A 50 ILE HG12 . 18497 1 509 . 1 1 50 50 ILE HG13 H 1 1.070 0.03 . 1 . . . A 50 ILE HG13 . 18497 1 510 . 1 1 50 50 ILE HG21 H 1 0.760 0.03 . 2 . . . A 50 ILE HG21 . 18497 1 511 . 1 1 50 50 ILE HG22 H 1 0.760 0.03 . 2 . . . A 50 ILE HG22 . 18497 1 512 . 1 1 50 50 ILE HG23 H 1 0.760 0.03 . 2 . . . A 50 ILE HG23 . 18497 1 513 . 1 1 50 50 ILE HD11 H 1 0.880 0.03 . 1 . . . A 50 ILE HD11 . 18497 1 514 . 1 1 50 50 ILE HD12 H 1 0.880 0.03 . 1 . . . A 50 ILE HD12 . 18497 1 515 . 1 1 50 50 ILE HD13 H 1 0.880 0.03 . 1 . . . A 50 ILE HD13 . 18497 1 516 . 1 1 50 50 ILE C C 13 179.502 0.3 . 1 . . . A 50 ILE C . 18497 1 517 . 1 1 50 50 ILE CA C 13 65.060 0.3 . 1 . . . A 50 ILE CA . 18497 1 518 . 1 1 50 50 ILE CB C 13 37.970 0.3 . 1 . . . A 50 ILE CB . 18497 1 519 . 1 1 50 50 ILE CG1 C 13 29.200 0.3 . 2 . . . A 50 ILE CG1 . 18497 1 520 . 1 1 50 50 ILE CG2 C 13 17.300 0.3 . 1 . . . A 50 ILE CG2 . 18497 1 521 . 1 1 50 50 ILE CD1 C 13 14.860 0.3 . 1 . . . A 50 ILE CD1 . 18497 1 522 . 1 1 50 50 ILE N N 15 119.715 0.3 . 1 . . . A 50 ILE N . 18497 1 523 . 1 1 51 51 ILE H H 1 7.475 0.03 . 1 . . . A 51 ILE H . 18497 1 524 . 1 1 51 51 ILE HA H 1 3.540 0.03 . 1 . . . A 51 ILE HA . 18497 1 525 . 1 1 51 51 ILE HB H 1 1.870 0.03 . 1 . . . A 51 ILE HB . 18497 1 526 . 1 1 51 51 ILE HG12 H 1 1.180 0.03 . 1 . . . A 51 ILE HG12 . 18497 1 527 . 1 1 51 51 ILE HG13 H 1 0.900 0.03 . 1 . . . A 51 ILE HG13 . 18497 1 528 . 1 1 51 51 ILE HG21 H 1 0.780 0.03 . 2 . . . A 51 ILE HG21 . 18497 1 529 . 1 1 51 51 ILE HG22 H 1 0.780 0.03 . 2 . . . A 51 ILE HG22 . 18497 1 530 . 1 1 51 51 ILE HG23 H 1 0.780 0.03 . 2 . . . A 51 ILE HG23 . 18497 1 531 . 1 1 51 51 ILE HD11 H 1 0.480 0.03 . 1 . . . A 51 ILE HD11 . 18497 1 532 . 1 1 51 51 ILE HD12 H 1 0.480 0.03 . 1 . . . A 51 ILE HD12 . 18497 1 533 . 1 1 51 51 ILE HD13 H 1 0.480 0.03 . 1 . . . A 51 ILE HD13 . 18497 1 534 . 1 1 51 51 ILE C C 13 179.197 0.3 . 1 . . . A 51 ILE C . 18497 1 535 . 1 1 51 51 ILE CA C 13 63.740 0.3 . 1 . . . A 51 ILE CA . 18497 1 536 . 1 1 51 51 ILE CB C 13 36.650 0.3 . 1 . . . A 51 ILE CB . 18497 1 537 . 1 1 51 51 ILE CG1 C 13 27.100 0.3 . 2 . . . A 51 ILE CG1 . 18497 1 538 . 1 1 51 51 ILE CG2 C 13 17.520 0.3 . 1 . . . A 51 ILE CG2 . 18497 1 539 . 1 1 51 51 ILE CD1 C 13 11.940 0.3 . 1 . . . A 51 ILE CD1 . 18497 1 540 . 1 1 51 51 ILE N N 15 117.995 0.3 . 1 . . . A 51 ILE N . 18497 1 541 . 1 1 52 52 ASP H H 1 8.559 0.03 . 1 . . . A 52 ASP H . 18497 1 542 . 1 1 52 52 ASP HA H 1 4.440 0.03 . 1 . . . A 52 ASP HA . 18497 1 543 . 1 1 52 52 ASP HB2 H 1 2.790 0.03 . 2 . . . A 52 ASP HB2 . 18497 1 544 . 1 1 52 52 ASP HB3 H 1 2.650 0.03 . 2 . . . A 52 ASP HB3 . 18497 1 545 . 1 1 52 52 ASP C C 13 179.197 0.3 . 1 . . . A 52 ASP C . 18497 1 546 . 1 1 52 52 ASP CA C 13 57.100 0.3 . 1 . . . A 52 ASP CA . 18497 1 547 . 1 1 52 52 ASP CB C 13 40.300 0.3 . 1 . . . A 52 ASP CB . 18497 1 548 . 1 1 52 52 ASP N N 15 121.642 0.3 . 1 . . . A 52 ASP N . 18497 1 549 . 1 1 53 53 ASN H H 1 8.106 0.03 . 1 . . . A 53 ASN H . 18497 1 550 . 1 1 53 53 ASN HA H 1 4.610 0.03 . 1 . . . A 53 ASN HA . 18497 1 551 . 1 1 53 53 ASN HB2 H 1 2.990 0.03 . 2 . . . A 53 ASN HB2 . 18497 1 552 . 1 1 53 53 ASN HB3 H 1 2.880 0.03 . 2 . . . A 53 ASN HB3 . 18497 1 553 . 1 1 53 53 ASN HD21 H 1 6.920 0.03 . 2 . . . A 53 ASN HD21 . 18497 1 554 . 1 1 53 53 ASN HD22 H 1 7.610 0.03 . 2 . . . A 53 ASN HD22 . 18497 1 555 . 1 1 53 53 ASN C C 13 178.545 0.3 . 1 . . . A 53 ASN C . 18497 1 556 . 1 1 53 53 ASN CA C 13 54.700 0.3 . 1 . . . A 53 ASN CA . 18497 1 557 . 1 1 53 53 ASN CB C 13 38.700 0.3 . 1 . . . A 53 ASN CB . 18497 1 558 . 1 1 53 53 ASN N N 15 117.131 0.3 . 1 . . . A 53 ASN N . 18497 1 559 . 1 1 53 53 ASN ND2 N 15 112.660 0.3 . 1 . . . A 53 ASN ND2 . 18497 1 560 . 1 1 54 54 ARG H H 1 7.797 0.03 . 1 . . . A 54 ARG H . 18497 1 561 . 1 1 54 54 ARG HA H 1 4.120 0.03 . 1 . . . A 54 ARG HA . 18497 1 562 . 1 1 54 54 ARG HB2 H 1 1.960 0.03 . 2 . . . A 54 ARG HB2 . 18497 1 563 . 1 1 54 54 ARG HB3 H 1 1.900 0.03 . 2 . . . A 54 ARG HB3 . 18497 1 564 . 1 1 54 54 ARG HG2 H 1 1.700 0.03 . 2 . . . A 54 ARG HG2 . 18497 1 565 . 1 1 54 54 ARG HG3 H 1 1.880 0.03 . 2 . . . A 54 ARG HG3 . 18497 1 566 . 1 1 54 54 ARG HD2 H 1 3.160 0.03 . 2 . . . A 54 ARG HD2 . 18497 1 567 . 1 1 54 54 ARG HD3 H 1 3.120 0.03 . 2 . . . A 54 ARG HD3 . 18497 1 568 . 1 1 54 54 ARG C C 13 176.892 0.3 . 1 . . . A 54 ARG C . 18497 1 569 . 1 1 54 54 ARG CA C 13 58.160 0.3 . 1 . . . A 54 ARG CA . 18497 1 570 . 1 1 54 54 ARG CB C 13 30.270 0.3 . 1 . . . A 54 ARG CB . 18497 1 571 . 1 1 54 54 ARG CG C 13 27.080 0.3 . 1 . . . A 54 ARG CG . 18497 1 572 . 1 1 54 54 ARG CD C 13 43.820 0.3 . 1 . . . A 54 ARG CD . 18497 1 573 . 1 1 54 54 ARG N N 15 119.929 0.3 . 1 . . . A 54 ARG N . 18497 1 574 . 1 1 55 55 ARG H H 1 7.857 0.03 . 1 . . . A 55 ARG H . 18497 1 575 . 1 1 55 55 ARG HA H 1 4.174 0.03 . 1 . . . A 55 ARG HA . 18497 1 576 . 1 1 55 55 ARG HB2 H 1 2.120 0.03 . 2 . . . A 55 ARG HB2 . 18497 1 577 . 1 1 55 55 ARG HB3 H 1 2.120 0.03 . 2 . . . A 55 ARG HB3 . 18497 1 578 . 1 1 55 55 ARG HG2 H 1 0.930 0.03 . 2 . . . A 55 ARG HG2 . 18497 1 579 . 1 1 55 55 ARG HG3 H 1 0.930 0.03 . 2 . . . A 55 ARG HG3 . 18497 1 580 . 1 1 55 55 ARG C C 13 175.108 0.3 . 1 . . . A 55 ARG C . 18497 1 581 . 1 1 55 55 ARG CA C 13 61.880 0.3 . 1 . . . A 55 ARG CA . 18497 1 582 . 1 1 55 55 ARG CB C 13 32.660 0.3 . 1 . . . A 55 ARG CB . 18497 1 583 . 1 1 55 55 ARG CG C 13 20.700 0.3 . 1 . . . A 55 ARG CG . 18497 1 584 . 1 1 55 55 ARG N N 15 119.227 0.3 . 1 . . . A 55 ARG N . 18497 1 585 . 1 1 56 56 ILE H H 1 8.317 0.03 . 1 . . . A 56 ILE H . 18497 1 586 . 1 1 56 56 ILE HA H 1 4.010 0.03 . 1 . . . A 56 ILE HA . 18497 1 587 . 1 1 56 56 ILE HB H 1 1.920 0.03 . 1 . . . A 56 ILE HB . 18497 1 588 . 1 1 56 56 ILE HG12 H 1 1.550 0.03 . 1 . . . A 56 ILE HG12 . 18497 1 589 . 1 1 56 56 ILE HG13 H 1 1.220 0.03 . 1 . . . A 56 ILE HG13 . 18497 1 590 . 1 1 56 56 ILE HG21 H 1 0.910 0.03 . 2 . . . A 56 ILE HG21 . 18497 1 591 . 1 1 56 56 ILE HG22 H 1 0.910 0.03 . 2 . . . A 56 ILE HG22 . 18497 1 592 . 1 1 56 56 ILE HG23 H 1 0.910 0.03 . 2 . . . A 56 ILE HG23 . 18497 1 593 . 1 1 56 56 ILE HD11 H 1 0.870 0.03 . 1 . . . A 56 ILE HD11 . 18497 1 594 . 1 1 56 56 ILE HD12 H 1 0.870 0.03 . 1 . . . A 56 ILE HD12 . 18497 1 595 . 1 1 56 56 ILE HD13 H 1 0.870 0.03 . 1 . . . A 56 ILE HD13 . 18497 1 596 . 1 1 56 56 ILE C C 13 176.065 0.3 . 1 . . . A 56 ILE C . 18497 1 597 . 1 1 56 56 ILE CA C 13 62.140 0.3 . 1 . . . A 56 ILE CA . 18497 1 598 . 1 1 56 56 ILE CB C 13 38.240 0.3 . 1 . . . A 56 ILE CB . 18497 1 599 . 1 1 56 56 ILE CG1 C 13 27.800 0.3 . 2 . . . A 56 ILE CG1 . 18497 1 600 . 1 1 56 56 ILE CG2 C 13 17.250 0.3 . 1 . . . A 56 ILE CG2 . 18497 1 601 . 1 1 56 56 ILE CD1 C 13 12.740 0.3 . 1 . . . A 56 ILE CD1 . 18497 1 602 . 1 1 56 56 ILE N N 15 116.676 0.3 . 1 . . . A 56 ILE N . 18497 1 603 . 1 1 57 57 MET H H 1 8.177 0.03 . 1 . . . A 57 MET H . 18497 1 604 . 1 1 57 57 MET HA H 1 4.420 0.03 . 1 . . . A 57 MET HA . 18497 1 605 . 1 1 57 57 MET HB2 H 1 2.100 0.03 . 2 . . . A 57 MET HB2 . 18497 1 606 . 1 1 57 57 MET HB3 H 1 2.060 0.03 . 2 . . . A 57 MET HB3 . 18497 1 607 . 1 1 57 57 MET C C 13 177.283 0.3 . 1 . . . A 57 MET C . 18497 1 608 . 1 1 57 57 MET CA C 13 56.030 0.3 . 1 . . . A 57 MET CA . 18497 1 609 . 1 1 57 57 MET CB C 13 32.515 0.3 . 1 . . . A 57 MET CB . 18497 1 610 . 1 1 57 57 MET N N 15 122.058 0.3 . 1 . . . A 57 MET N . 18497 1 611 . 1 1 58 58 ASN H H 1 8.238 0.03 . 1 . . . A 58 ASN H . 18497 1 612 . 1 1 58 58 ASN HA H 1 4.690 0.03 . 1 . . . A 58 ASN HA . 18497 1 613 . 1 1 58 58 ASN HB2 H 1 2.860 0.03 . 2 . . . A 58 ASN HB2 . 18497 1 614 . 1 1 58 58 ASN HB3 H 1 2.810 0.03 . 2 . . . A 58 ASN HB3 . 18497 1 615 . 1 1 58 58 ASN C C 13 176.500 0.3 . 1 . . . A 58 ASN C . 18497 1 616 . 1 1 58 58 ASN CA C 13 53.653 0.3 . 1 . . . A 58 ASN CA . 18497 1 617 . 1 1 58 58 ASN CB C 13 38.770 0.3 . 1 . . . A 58 ASN CB . 18497 1 618 . 1 1 58 58 ASN N N 15 118.892 0.3 . 1 . . . A 58 ASN N . 18497 1 619 . 1 1 59 59 GLN H H 1 8.196 0.03 . 1 . . . A 59 GLN H . 18497 1 620 . 1 1 59 59 GLN HA H 1 4.310 0.03 . 1 . . . A 59 GLN HA . 18497 1 621 . 1 1 59 59 GLN HB2 H 1 2.132 0.03 . 2 . . . A 59 GLN HB2 . 18497 1 622 . 1 1 59 59 GLN HB3 H 1 2.017 0.03 . 2 . . . A 59 GLN HB3 . 18497 1 623 . 1 1 59 59 GLN HG3 H 1 2.400 0.03 . 2 . . . A 59 GLN HG3 . 18497 1 624 . 1 1 59 59 GLN C C 13 175.326 0.3 . 1 . . . A 59 GLN C . 18497 1 625 . 1 1 59 59 GLN CA C 13 56.030 0.3 . 1 . . . A 59 GLN CA . 18497 1 626 . 1 1 59 59 GLN CB C 13 28.800 0.3 . 1 . . . A 59 GLN CB . 18497 1 627 . 1 1 59 59 GLN CG C 13 33.700 0.3 . 1 . . . A 59 GLN CG . 18497 1 628 . 1 1 59 59 GLN N N 15 120.456 0.3 . 1 . . . A 59 GLN N . 18497 1 629 . 1 1 60 60 ALA H H 1 8.293 0.03 . 1 . . . A 60 ALA H . 18497 1 630 . 1 1 60 60 ALA HA H 1 4.382 0.03 . 1 . . . A 60 ALA HA . 18497 1 631 . 1 1 60 60 ALA HB1 H 1 1.440 0.03 . 1 . . . A 60 ALA HB1 . 18497 1 632 . 1 1 60 60 ALA HB2 H 1 1.440 0.03 . 1 . . . A 60 ALA HB2 . 18497 1 633 . 1 1 60 60 ALA HB3 H 1 1.440 0.03 . 1 . . . A 60 ALA HB3 . 18497 1 634 . 1 1 60 60 ALA CA C 13 52.300 0.3 . 1 . . . A 60 ALA CA . 18497 1 635 . 1 1 60 60 ALA CB C 13 19.110 0.3 . 1 . . . A 60 ALA CB . 18497 1 636 . 1 1 60 60 ALA N N 15 125.116 0.3 . 1 . . . A 60 ALA N . 18497 1 637 . 1 1 61 61 SER H H 1 8.290 0.03 . 1 . . . A 61 SER H . 18497 1 638 . 1 1 61 61 SER HA H 1 4.470 0.03 . 1 . . . A 61 SER HA . 18497 1 639 . 1 1 61 61 SER HB3 H 1 3.880 0.03 . 2 . . . A 61 SER HB3 . 18497 1 640 . 1 1 61 61 SER C C 13 175.674 0.3 . 1 . . . A 61 SER C . 18497 1 641 . 1 1 61 61 SER CA C 13 58.160 0.3 . 1 . . . A 61 SER CA . 18497 1 642 . 1 1 61 61 SER CB C 13 63.740 0.3 . 1 . . . A 61 SER CB . 18497 1 643 . 1 1 61 61 SER N N 15 115.686 0.3 . 1 . . . A 61 SER N . 18497 1 644 . 1 1 62 62 GLU H H 1 7.999 0.03 . 1 . . . A 62 GLU H . 18497 1 645 . 1 1 62 62 GLU HA H 1 4.127 0.03 . 1 . . . A 62 GLU HA . 18497 1 646 . 1 1 62 62 GLU HB2 H 1 1.900 0.03 . 2 . . . A 62 GLU HB2 . 18497 1 647 . 1 1 62 62 GLU HB3 H 1 1.900 0.03 . 2 . . . A 62 GLU HB3 . 18497 1 648 . 1 1 62 62 GLU HG2 H 1 2.170 0.03 . 2 . . . A 62 GLU HG2 . 18497 1 649 . 1 1 62 62 GLU HG3 H 1 2.170 0.03 . 2 . . . A 62 GLU HG3 . 18497 1 650 . 1 1 62 62 GLU C C 13 177.675 0.3 . 1 . . . A 62 GLU C . 18497 1 651 . 1 1 62 62 GLU CA C 13 58.100 0.3 . 1 . . . A 62 GLU CA . 18497 1 652 . 1 1 62 62 GLU CB C 13 31.100 0.3 . 1 . . . A 62 GLU CB . 18497 1 653 . 1 1 62 62 GLU CG C 13 36.400 0.3 . 1 . . . A 62 GLU CG . 18497 1 654 . 1 1 62 62 GLU N N 15 127.521 0.3 . 1 . . . A 62 GLU N . 18497 1 stop_ save_