data_10150 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 10150 _Entry.Title ; Solution structure of the SANT domain of fission yeast SPCC24B10.08c protein ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-12-11 _Entry.Accession_date 2007-12-11 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.100 _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 N. Tochio . . . 10150 2 S. Koshiba . . . 10150 3 S. Watanabe . . . 10150 4 T. Harada . . . 10150 5 T. Umehara . . . 10150 6 A. Tanaka . . . 10150 7 T. Kigawa . . . 10150 8 S. Yokoyama . . . 10150 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' 10150 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 10150 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 240 10150 '15N chemical shifts' 61 10150 '1H chemical shifts' 364 10150 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 2 . . 2010-05-25 2007-12-11 update BMRB 'update entity name' 10150 1 . . 2008-12-11 2007-12-11 original author 'original release' 10150 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2ELK 'BMRB Entry Tracking System' 10150 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 10150 _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 the SANT domain of fission yeast SPCC24B10.08c protein' _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 N. Tochio . . . 10150 1 2 S. Koshiba . . . 10150 1 3 S. Watanabe . . . 10150 1 4 T. Harada . . . 10150 1 5 T. Umehara . . . 10150 1 6 A. Tanaka . . . 10150 1 7 T. Kigawa . . . 10150 1 8 S. Yokoyama . . . 10150 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 10150 _Assembly.ID 1 _Assembly.Name 'SPCC24B10.08c protein' _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 'SPCC24B10.08c protein' 1 $entity_1 . . yes native no no . . . 10150 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 2ELK . . . . . . 10150 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 10150 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'SPCC24B10.08c protein' _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 ; GSSGSSGFDENWGADEELLL IDACETLGLGNWADIADYVG NARTKEECRDHYLKTYIE ; _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 58 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _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 2ELK . "Solution Structure Of The Sant Domain Of Fission Yeast Spcc24b10.08c Protein" . . . . . 100.00 58 100.00 100.00 8.71e-33 . . . . 10150 1 2 no EMBL CAB76217 . "SAGA complex subunit Ada2 [Schizosaccharomyces pombe]" . . . . . 87.93 437 100.00 100.00 1.35e-29 . . . . 10150 1 3 no REF NP_588011 . "SAGA complex subunit Ada2 [Schizosaccharomyces pombe 972h-]" . . . . . 87.93 437 100.00 100.00 1.35e-29 . . . . 10150 1 4 no SP Q9P7J7 . "RecName: Full=Transcriptional adapter 2" . . . . . 87.93 437 100.00 100.00 1.35e-29 . . . . 10150 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'SANT domain' . 10150 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 . 10150 1 2 . SER . 10150 1 3 . SER . 10150 1 4 . GLY . 10150 1 5 . SER . 10150 1 6 . SER . 10150 1 7 . GLY . 10150 1 8 . PHE . 10150 1 9 . ASP . 10150 1 10 . GLU . 10150 1 11 . ASN . 10150 1 12 . TRP . 10150 1 13 . GLY . 10150 1 14 . ALA . 10150 1 15 . ASP . 10150 1 16 . GLU . 10150 1 17 . GLU . 10150 1 18 . LEU . 10150 1 19 . LEU . 10150 1 20 . LEU . 10150 1 21 . ILE . 10150 1 22 . ASP . 10150 1 23 . ALA . 10150 1 24 . CYS . 10150 1 25 . GLU . 10150 1 26 . THR . 10150 1 27 . LEU . 10150 1 28 . GLY . 10150 1 29 . LEU . 10150 1 30 . GLY . 10150 1 31 . ASN . 10150 1 32 . TRP . 10150 1 33 . ALA . 10150 1 34 . ASP . 10150 1 35 . ILE . 10150 1 36 . ALA . 10150 1 37 . ASP . 10150 1 38 . TYR . 10150 1 39 . VAL . 10150 1 40 . GLY . 10150 1 41 . ASN . 10150 1 42 . ALA . 10150 1 43 . ARG . 10150 1 44 . THR . 10150 1 45 . LYS . 10150 1 46 . GLU . 10150 1 47 . GLU . 10150 1 48 . CYS . 10150 1 49 . ARG . 10150 1 50 . ASP . 10150 1 51 . HIS . 10150 1 52 . TYR . 10150 1 53 . LEU . 10150 1 54 . LYS . 10150 1 55 . THR . 10150 1 56 . TYR . 10150 1 57 . ILE . 10150 1 58 . GLU . 10150 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 10150 1 . SER 2 2 10150 1 . SER 3 3 10150 1 . GLY 4 4 10150 1 . SER 5 5 10150 1 . SER 6 6 10150 1 . GLY 7 7 10150 1 . PHE 8 8 10150 1 . ASP 9 9 10150 1 . GLU 10 10 10150 1 . ASN 11 11 10150 1 . TRP 12 12 10150 1 . GLY 13 13 10150 1 . ALA 14 14 10150 1 . ASP 15 15 10150 1 . GLU 16 16 10150 1 . GLU 17 17 10150 1 . LEU 18 18 10150 1 . LEU 19 19 10150 1 . LEU 20 20 10150 1 . ILE 21 21 10150 1 . ASP 22 22 10150 1 . ALA 23 23 10150 1 . CYS 24 24 10150 1 . GLU 25 25 10150 1 . THR 26 26 10150 1 . LEU 27 27 10150 1 . GLY 28 28 10150 1 . LEU 29 29 10150 1 . GLY 30 30 10150 1 . ASN 31 31 10150 1 . TRP 32 32 10150 1 . ALA 33 33 10150 1 . ASP 34 34 10150 1 . ILE 35 35 10150 1 . ALA 36 36 10150 1 . ASP 37 37 10150 1 . TYR 38 38 10150 1 . VAL 39 39 10150 1 . GLY 40 40 10150 1 . ASN 41 41 10150 1 . ALA 42 42 10150 1 . ARG 43 43 10150 1 . THR 44 44 10150 1 . LYS 45 45 10150 1 . GLU 46 46 10150 1 . GLU 47 47 10150 1 . CYS 48 48 10150 1 . ARG 49 49 10150 1 . ASP 50 50 10150 1 . HIS 51 51 10150 1 . TYR 52 52 10150 1 . LEU 53 53 10150 1 . LYS 54 54 10150 1 . THR 55 55 10150 1 . TYR 56 56 10150 1 . ILE 57 57 10150 1 . GLU 58 58 10150 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 10150 _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 . 4896 organism . 'Schizosaccharomyces pombe' 'Fission yeast' . . Eukaryota Fungi Schizosaccharomyces pombe . . . . . . . . . . . . . . . . . . . . . 10150 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 10150 _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 . . P060618-06 . . . . . . 10150 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 10150 _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 'SANT domain' '[U-13C; U-15N]' . . 1 $entity_1 . protein 1.2 . . mM . . . . 10150 1 2 d-Tris-HCl . . . . . . buffer 20 . . mM . . . . 10150 1 3 NaCl . . . . . . salt 100 . . mM . . . . 10150 1 4 d-DTT . . . . . . salt 1 . . mM . . . . 10150 1 5 NaN3 . . . . . . salt 0.02 . . % . . . . 10150 1 6 H2O . . . . . . solvent 90 . . % . . . . 10150 1 7 D2O . . . . . . solvent 10 . . % . . . . 10150 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 10150 _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 10150 1 pH 7.0 0.05 pH 10150 1 pressure 1 0.001 atm 10150 1 temperature 296 0.1 K 10150 1 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 10150 _Software.ID 1 _Software.Name TOPSPIN _Software.Version 1.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Bruker . . 10150 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 10150 1 stop_ save_ save_software_2 _Software.Sf_category software _Software.Sf_framecode software_2 _Software.Entry_ID 10150 _Software.ID 2 _Software.Name NMRPipe _Software.Version 20030801 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, F.' . . 10150 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 10150 2 stop_ save_ save_software_3 _Software.Sf_category software _Software.Sf_framecode software_3 _Software.Entry_ID 10150 _Software.ID 3 _Software.Name NMRView _Software.Version 5.0.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, B.A.' . . 10150 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 10150 3 stop_ save_ save_software_4 _Software.Sf_category software _Software.Sf_framecode software_4 _Software.Entry_ID 10150 _Software.ID 4 _Software.Name Kujira _Software.Version 0.9820 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Kobayashi, N.' . . 10150 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 10150 4 stop_ save_ save_software_5 _Software.Sf_category software _Software.Sf_framecode software_5 _Software.Entry_ID 10150 _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.' . . 10150 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution & refinement' 10150 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 10150 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE2 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 10150 _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 AVANCE2 . 900 . . . 10150 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 10150 _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 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 10150 1 2 '3D 15N-separated NOESY' no . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 10150 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 10150 _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 . . . . . . . . . 10150 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 . indirect 1.0 . . . . . . . . . 10150 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 10150 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 10150 _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 10150 1 2 '3D 15N-separated NOESY' 1 $sample_1 isotropic 10150 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 3 3 SER CA C 13 58.574 0.300 . 1 . . . . 3 SER CA . 10150 1 2 . 1 1 3 3 SER HA H 1 4.477 0.030 . 1 . . . . 3 SER HA . 10150 1 3 . 1 1 3 3 SER CB C 13 63.686 0.300 . 1 . . . . 3 SER CB . 10150 1 4 . 1 1 3 3 SER HB2 H 1 3.883 0.030 . 2 . . . . 3 SER HB2 . 10150 1 5 . 1 1 3 3 SER C C 13 175.067 0.300 . 1 . . . . 3 SER C . 10150 1 6 . 1 1 4 4 GLY N N 15 111.014 0.300 . 1 . . . . 4 GLY N . 10150 1 7 . 1 1 4 4 GLY H H 1 8.466 0.030 . 1 . . . . 4 GLY H . 10150 1 8 . 1 1 4 4 GLY CA C 13 45.338 0.300 . 1 . . . . 4 GLY CA . 10150 1 9 . 1 1 4 4 GLY HA2 H 1 4.006 0.030 . 2 . . . . 4 GLY HA2 . 10150 1 10 . 1 1 4 4 GLY C C 13 174.344 0.300 . 1 . . . . 4 GLY C . 10150 1 11 . 1 1 5 5 SER N N 15 115.891 0.300 . 1 . . . . 5 SER N . 10150 1 12 . 1 1 5 5 SER H H 1 8.294 0.030 . 1 . . . . 5 SER H . 10150 1 13 . 1 1 5 5 SER CA C 13 58.277 0.300 . 1 . . . . 5 SER CA . 10150 1 14 . 1 1 5 5 SER HA H 1 4.499 0.030 . 1 . . . . 5 SER HA . 10150 1 15 . 1 1 5 5 SER CB C 13 63.850 0.300 . 1 . . . . 5 SER CB . 10150 1 16 . 1 1 5 5 SER HB2 H 1 3.862 0.030 . 2 . . . . 5 SER HB2 . 10150 1 17 . 1 1 5 5 SER C C 13 174.840 0.300 . 1 . . . . 5 SER C . 10150 1 18 . 1 1 6 6 SER N N 15 117.946 0.300 . 1 . . . . 6 SER N . 10150 1 19 . 1 1 6 6 SER H H 1 8.479 0.030 . 1 . . . . 6 SER H . 10150 1 20 . 1 1 6 6 SER CA C 13 58.632 0.300 . 1 . . . . 6 SER CA . 10150 1 21 . 1 1 6 6 SER HA H 1 4.427 0.030 . 1 . . . . 6 SER HA . 10150 1 22 . 1 1 6 6 SER CB C 13 63.855 0.300 . 1 . . . . 6 SER CB . 10150 1 23 . 1 1 6 6 SER HB2 H 1 3.852 0.030 . 2 . . . . 6 SER HB2 . 10150 1 24 . 1 1 6 6 SER C C 13 174.852 0.300 . 1 . . . . 6 SER C . 10150 1 25 . 1 1 7 7 GLY N N 15 110.490 0.300 . 1 . . . . 7 GLY N . 10150 1 26 . 1 1 7 7 GLY H H 1 8.354 0.030 . 1 . . . . 7 GLY H . 10150 1 27 . 1 1 7 7 GLY CA C 13 45.231 0.300 . 1 . . . . 7 GLY CA . 10150 1 28 . 1 1 7 7 GLY HA2 H 1 3.836 0.030 . 2 . . . . 7 GLY HA2 . 10150 1 29 . 1 1 7 7 GLY HA3 H 1 3.898 0.030 . 2 . . . . 7 GLY HA3 . 10150 1 30 . 1 1 7 7 GLY C C 13 173.829 0.300 . 1 . . . . 7 GLY C . 10150 1 31 . 1 1 8 8 PHE N N 15 119.865 0.300 . 1 . . . . 8 PHE N . 10150 1 32 . 1 1 8 8 PHE H H 1 8.094 0.030 . 1 . . . . 8 PHE H . 10150 1 33 . 1 1 8 8 PHE CA C 13 57.501 0.300 . 1 . . . . 8 PHE CA . 10150 1 34 . 1 1 8 8 PHE HA H 1 4.666 0.030 . 1 . . . . 8 PHE HA . 10150 1 35 . 1 1 8 8 PHE CB C 13 39.743 0.300 . 1 . . . . 8 PHE CB . 10150 1 36 . 1 1 8 8 PHE HB2 H 1 3.209 0.030 . 2 . . . . 8 PHE HB2 . 10150 1 37 . 1 1 8 8 PHE HB3 H 1 2.964 0.030 . 2 . . . . 8 PHE HB3 . 10150 1 38 . 1 1 8 8 PHE CD1 C 13 131.820 0.300 . 1 . . . . 8 PHE CD1 . 10150 1 39 . 1 1 8 8 PHE HD1 H 1 7.239 0.030 . 1 . . . . 8 PHE HD1 . 10150 1 40 . 1 1 8 8 PHE CD2 C 13 131.820 0.300 . 1 . . . . 8 PHE CD2 . 10150 1 41 . 1 1 8 8 PHE HD2 H 1 7.239 0.030 . 1 . . . . 8 PHE HD2 . 10150 1 42 . 1 1 8 8 PHE CE1 C 13 131.362 0.300 . 1 . . . . 8 PHE CE1 . 10150 1 43 . 1 1 8 8 PHE HE1 H 1 7.326 0.030 . 1 . . . . 8 PHE HE1 . 10150 1 44 . 1 1 8 8 PHE CE2 C 13 131.362 0.300 . 1 . . . . 8 PHE CE2 . 10150 1 45 . 1 1 8 8 PHE HE2 H 1 7.326 0.030 . 1 . . . . 8 PHE HE2 . 10150 1 46 . 1 1 8 8 PHE CZ C 13 129.672 0.300 . 1 . . . . 8 PHE CZ . 10150 1 47 . 1 1 8 8 PHE HZ H 1 7.271 0.030 . 1 . . . . 8 PHE HZ . 10150 1 48 . 1 1 8 8 PHE C C 13 175.564 0.300 . 1 . . . . 8 PHE C . 10150 1 49 . 1 1 9 9 ASP N N 15 122.084 0.300 . 1 . . . . 9 ASP N . 10150 1 50 . 1 1 9 9 ASP H H 1 8.516 0.030 . 1 . . . . 9 ASP H . 10150 1 51 . 1 1 9 9 ASP CA C 13 54.372 0.300 . 1 . . . . 9 ASP CA . 10150 1 52 . 1 1 9 9 ASP HA H 1 4.599 0.030 . 1 . . . . 9 ASP HA . 10150 1 53 . 1 1 9 9 ASP CB C 13 41.429 0.300 . 1 . . . . 9 ASP CB . 10150 1 54 . 1 1 9 9 ASP HB2 H 1 2.736 0.030 . 2 . . . . 9 ASP HB2 . 10150 1 55 . 1 1 9 9 ASP HB3 H 1 2.594 0.030 . 2 . . . . 9 ASP HB3 . 10150 1 56 . 1 1 9 9 ASP C C 13 176.168 0.300 . 1 . . . . 9 ASP C . 10150 1 57 . 1 1 10 10 GLU N N 15 121.747 0.300 . 1 . . . . 10 GLU N . 10150 1 58 . 1 1 10 10 GLU H H 1 8.489 0.030 . 1 . . . . 10 GLU H . 10150 1 59 . 1 1 10 10 GLU CA C 13 56.705 0.300 . 1 . . . . 10 GLU CA . 10150 1 60 . 1 1 10 10 GLU HA H 1 4.359 0.030 . 1 . . . . 10 GLU HA . 10150 1 61 . 1 1 10 10 GLU CB C 13 30.039 0.300 . 1 . . . . 10 GLU CB . 10150 1 62 . 1 1 10 10 GLU HB2 H 1 2.165 0.030 . 2 . . . . 10 GLU HB2 . 10150 1 63 . 1 1 10 10 GLU HB3 H 1 1.995 0.030 . 2 . . . . 10 GLU HB3 . 10150 1 64 . 1 1 10 10 GLU CG C 13 36.304 0.300 . 1 . . . . 10 GLU CG . 10150 1 65 . 1 1 10 10 GLU HG2 H 1 2.331 0.030 . 2 . . . . 10 GLU HG2 . 10150 1 66 . 1 1 10 10 GLU HG3 H 1 2.302 0.030 . 2 . . . . 10 GLU HG3 . 10150 1 67 . 1 1 10 10 GLU C C 13 176.584 0.300 . 1 . . . . 10 GLU C . 10150 1 68 . 1 1 11 11 ASN N N 15 119.867 0.300 . 1 . . . . 11 ASN N . 10150 1 69 . 1 1 11 11 ASN H H 1 8.479 0.030 . 1 . . . . 11 ASN H . 10150 1 70 . 1 1 11 11 ASN CA C 13 53.332 0.300 . 1 . . . . 11 ASN CA . 10150 1 71 . 1 1 11 11 ASN HA H 1 4.791 0.030 . 1 . . . . 11 ASN HA . 10150 1 72 . 1 1 11 11 ASN CB C 13 38.906 0.300 . 1 . . . . 11 ASN CB . 10150 1 73 . 1 1 11 11 ASN HB2 H 1 2.818 0.030 . 1 . . . . 11 ASN HB2 . 10150 1 74 . 1 1 11 11 ASN HB3 H 1 2.818 0.030 . 1 . . . . 11 ASN HB3 . 10150 1 75 . 1 1 11 11 ASN ND2 N 15 113.548 0.300 . 1 . . . . 11 ASN ND2 . 10150 1 76 . 1 1 11 11 ASN HD21 H 1 6.991 0.030 . 2 . . . . 11 ASN HD21 . 10150 1 77 . 1 1 11 11 ASN HD22 H 1 7.698 0.030 . 2 . . . . 11 ASN HD22 . 10150 1 78 . 1 1 11 11 ASN C C 13 175.284 0.300 . 1 . . . . 11 ASN C . 10150 1 79 . 1 1 12 12 TRP N N 15 124.246 0.300 . 1 . . . . 12 TRP N . 10150 1 80 . 1 1 12 12 TRP H H 1 8.819 0.030 . 1 . . . . 12 TRP H . 10150 1 81 . 1 1 12 12 TRP CA C 13 57.447 0.300 . 1 . . . . 12 TRP CA . 10150 1 82 . 1 1 12 12 TRP HA H 1 4.338 0.030 . 1 . . . . 12 TRP HA . 10150 1 83 . 1 1 12 12 TRP CB C 13 29.096 0.300 . 1 . . . . 12 TRP CB . 10150 1 84 . 1 1 12 12 TRP HB2 H 1 3.022 0.030 . 2 . . . . 12 TRP HB2 . 10150 1 85 . 1 1 12 12 TRP HB3 H 1 2.907 0.030 . 2 . . . . 12 TRP HB3 . 10150 1 86 . 1 1 12 12 TRP CD1 C 13 124.765 0.300 . 1 . . . . 12 TRP CD1 . 10150 1 87 . 1 1 12 12 TRP HD1 H 1 6.897 0.030 . 1 . . . . 12 TRP HD1 . 10150 1 88 . 1 1 12 12 TRP NE1 N 15 129.592 0.300 . 1 . . . . 12 TRP NE1 . 10150 1 89 . 1 1 12 12 TRP HE1 H 1 10.193 0.030 . 1 . . . . 12 TRP HE1 . 10150 1 90 . 1 1 12 12 TRP CE3 C 13 119.822 0.300 . 1 . . . . 12 TRP CE3 . 10150 1 91 . 1 1 12 12 TRP HE3 H 1 7.033 0.030 . 1 . . . . 12 TRP HE3 . 10150 1 92 . 1 1 12 12 TRP CZ2 C 13 112.480 0.300 . 1 . . . . 12 TRP CZ2 . 10150 1 93 . 1 1 12 12 TRP HZ2 H 1 6.987 0.030 . 1 . . . . 12 TRP HZ2 . 10150 1 94 . 1 1 12 12 TRP CZ3 C 13 121.446 0.300 . 1 . . . . 12 TRP CZ3 . 10150 1 95 . 1 1 12 12 TRP HZ3 H 1 6.943 0.030 . 1 . . . . 12 TRP HZ3 . 10150 1 96 . 1 1 12 12 TRP CH2 C 13 123.475 0.300 . 1 . . . . 12 TRP CH2 . 10150 1 97 . 1 1 12 12 TRP HH2 H 1 7.325 0.030 . 1 . . . . 12 TRP HH2 . 10150 1 98 . 1 1 12 12 TRP C C 13 177.403 0.300 . 1 . . . . 12 TRP C . 10150 1 99 . 1 1 13 13 GLY N N 15 112.578 0.300 . 1 . . . . 13 GLY N . 10150 1 100 . 1 1 13 13 GLY H H 1 9.662 0.030 . 1 . . . . 13 GLY H . 10150 1 101 . 1 1 13 13 GLY CA C 13 44.383 0.300 . 1 . . . . 13 GLY CA . 10150 1 102 . 1 1 13 13 GLY HA2 H 1 4.315 0.030 . 2 . . . . 13 GLY HA2 . 10150 1 103 . 1 1 13 13 GLY HA3 H 1 3.989 0.030 . 2 . . . . 13 GLY HA3 . 10150 1 104 . 1 1 13 13 GLY C C 13 174.443 0.300 . 1 . . . . 13 GLY C . 10150 1 105 . 1 1 14 14 ALA N N 15 124.409 0.300 . 1 . . . . 14 ALA N . 10150 1 106 . 1 1 14 14 ALA H H 1 8.805 0.030 . 1 . . . . 14 ALA H . 10150 1 107 . 1 1 14 14 ALA CA C 13 55.635 0.300 . 1 . . . . 14 ALA CA . 10150 1 108 . 1 1 14 14 ALA HA H 1 4.225 0.030 . 1 . . . . 14 ALA HA . 10150 1 109 . 1 1 14 14 ALA CB C 13 18.565 0.300 . 1 . . . . 14 ALA CB . 10150 1 110 . 1 1 14 14 ALA HB1 H 1 1.532 0.030 . 1 . . . . 14 ALA HB . 10150 1 111 . 1 1 14 14 ALA HB2 H 1 1.532 0.030 . 1 . . . . 14 ALA HB . 10150 1 112 . 1 1 14 14 ALA HB3 H 1 1.532 0.030 . 1 . . . . 14 ALA HB . 10150 1 113 . 1 1 14 14 ALA C C 13 180.546 0.300 . 1 . . . . 14 ALA C . 10150 1 114 . 1 1 15 15 ASP N N 15 115.685 0.300 . 1 . . . . 15 ASP N . 10150 1 115 . 1 1 15 15 ASP H H 1 8.825 0.030 . 1 . . . . 15 ASP H . 10150 1 116 . 1 1 15 15 ASP CA C 13 56.775 0.300 . 1 . . . . 15 ASP CA . 10150 1 117 . 1 1 15 15 ASP HA H 1 4.416 0.030 . 1 . . . . 15 ASP HA . 10150 1 118 . 1 1 15 15 ASP CB C 13 39.188 0.300 . 1 . . . . 15 ASP CB . 10150 1 119 . 1 1 15 15 ASP HB2 H 1 2.787 0.030 . 2 . . . . 15 ASP HB2 . 10150 1 120 . 1 1 15 15 ASP HB3 H 1 2.666 0.030 . 2 . . . . 15 ASP HB3 . 10150 1 121 . 1 1 15 15 ASP C C 13 178.981 0.300 . 1 . . . . 15 ASP C . 10150 1 122 . 1 1 16 16 GLU N N 15 121.445 0.300 . 1 . . . . 16 GLU N . 10150 1 123 . 1 1 16 16 GLU H H 1 7.772 0.030 . 1 . . . . 16 GLU H . 10150 1 124 . 1 1 16 16 GLU CA C 13 59.380 0.300 . 1 . . . . 16 GLU CA . 10150 1 125 . 1 1 16 16 GLU HA H 1 4.203 0.030 . 1 . . . . 16 GLU HA . 10150 1 126 . 1 1 16 16 GLU CB C 13 30.556 0.300 . 1 . . . . 16 GLU CB . 10150 1 127 . 1 1 16 16 GLU HB2 H 1 2.316 0.030 . 2 . . . . 16 GLU HB2 . 10150 1 128 . 1 1 16 16 GLU HB3 H 1 2.127 0.030 . 2 . . . . 16 GLU HB3 . 10150 1 129 . 1 1 16 16 GLU CG C 13 37.329 0.300 . 1 . . . . 16 GLU CG . 10150 1 130 . 1 1 16 16 GLU HG2 H 1 2.354 0.030 . 2 . . . . 16 GLU HG2 . 10150 1 131 . 1 1 16 16 GLU HG3 H 1 2.173 0.030 . 2 . . . . 16 GLU HG3 . 10150 1 132 . 1 1 16 16 GLU C C 13 178.517 0.300 . 1 . . . . 16 GLU C . 10150 1 133 . 1 1 17 17 GLU N N 15 118.709 0.300 . 1 . . . . 17 GLU N . 10150 1 134 . 1 1 17 17 GLU H H 1 8.363 0.030 . 1 . . . . 17 GLU H . 10150 1 135 . 1 1 17 17 GLU CA C 13 59.820 0.300 . 1 . . . . 17 GLU CA . 10150 1 136 . 1 1 17 17 GLU HA H 1 4.429 0.030 . 1 . . . . 17 GLU HA . 10150 1 137 . 1 1 17 17 GLU CB C 13 29.774 0.300 . 1 . . . . 17 GLU CB . 10150 1 138 . 1 1 17 17 GLU HB2 H 1 2.364 0.030 . 2 . . . . 17 GLU HB2 . 10150 1 139 . 1 1 17 17 GLU HB3 H 1 2.283 0.030 . 2 . . . . 17 GLU HB3 . 10150 1 140 . 1 1 17 17 GLU CG C 13 36.369 0.300 . 1 . . . . 17 GLU CG . 10150 1 141 . 1 1 17 17 GLU HG2 H 1 2.570 0.030 . 2 . . . . 17 GLU HG2 . 10150 1 142 . 1 1 17 17 GLU HG3 H 1 2.486 0.030 . 2 . . . . 17 GLU HG3 . 10150 1 143 . 1 1 17 17 GLU C C 13 179.029 0.300 . 1 . . . . 17 GLU C . 10150 1 144 . 1 1 18 18 LEU N N 15 118.004 0.300 . 1 . . . . 18 LEU N . 10150 1 145 . 1 1 18 18 LEU H H 1 7.650 0.030 . 1 . . . . 18 LEU H . 10150 1 146 . 1 1 18 18 LEU CA C 13 58.128 0.300 . 1 . . . . 18 LEU CA . 10150 1 147 . 1 1 18 18 LEU HA H 1 4.212 0.030 . 1 . . . . 18 LEU HA . 10150 1 148 . 1 1 18 18 LEU CB C 13 41.700 0.300 . 1 . . . . 18 LEU CB . 10150 1 149 . 1 1 18 18 LEU HB2 H 1 1.966 0.030 . 2 . . . . 18 LEU HB2 . 10150 1 150 . 1 1 18 18 LEU HB3 H 1 1.738 0.030 . 2 . . . . 18 LEU HB3 . 10150 1 151 . 1 1 18 18 LEU CG C 13 26.966 0.300 . 1 . . . . 18 LEU CG . 10150 1 152 . 1 1 18 18 LEU HG H 1 1.932 0.030 . 1 . . . . 18 LEU HG . 10150 1 153 . 1 1 18 18 LEU CD1 C 13 25.152 0.300 . 2 . . . . 18 LEU CD1 . 10150 1 154 . 1 1 18 18 LEU HD11 H 1 1.006 0.030 . 1 . . . . 18 LEU HD1 . 10150 1 155 . 1 1 18 18 LEU HD12 H 1 1.006 0.030 . 1 . . . . 18 LEU HD1 . 10150 1 156 . 1 1 18 18 LEU HD13 H 1 1.006 0.030 . 1 . . . . 18 LEU HD1 . 10150 1 157 . 1 1 18 18 LEU CD2 C 13 23.543 0.300 . 2 . . . . 18 LEU CD2 . 10150 1 158 . 1 1 18 18 LEU HD21 H 1 0.962 0.030 . 1 . . . . 18 LEU HD2 . 10150 1 159 . 1 1 18 18 LEU HD22 H 1 0.962 0.030 . 1 . . . . 18 LEU HD2 . 10150 1 160 . 1 1 18 18 LEU HD23 H 1 0.962 0.030 . 1 . . . . 18 LEU HD2 . 10150 1 161 . 1 1 18 18 LEU C C 13 179.871 0.300 . 1 . . . . 18 LEU C . 10150 1 162 . 1 1 19 19 LEU N N 15 119.600 0.300 . 1 . . . . 19 LEU N . 10150 1 163 . 1 1 19 19 LEU H H 1 7.783 0.030 . 1 . . . . 19 LEU H . 10150 1 164 . 1 1 19 19 LEU CA C 13 58.106 0.300 . 1 . . . . 19 LEU CA . 10150 1 165 . 1 1 19 19 LEU HA H 1 4.390 0.030 . 1 . . . . 19 LEU HA . 10150 1 166 . 1 1 19 19 LEU CB C 13 43.169 0.300 . 1 . . . . 19 LEU CB . 10150 1 167 . 1 1 19 19 LEU HB2 H 1 2.247 0.030 . 2 . . . . 19 LEU HB2 . 10150 1 168 . 1 1 19 19 LEU HB3 H 1 1.679 0.030 . 2 . . . . 19 LEU HB3 . 10150 1 169 . 1 1 19 19 LEU CG C 13 27.301 0.300 . 1 . . . . 19 LEU CG . 10150 1 170 . 1 1 19 19 LEU HG H 1 1.951 0.030 . 1 . . . . 19 LEU HG . 10150 1 171 . 1 1 19 19 LEU CD1 C 13 25.828 0.300 . 2 . . . . 19 LEU CD1 . 10150 1 172 . 1 1 19 19 LEU HD11 H 1 1.090 0.030 . 1 . . . . 19 LEU HD1 . 10150 1 173 . 1 1 19 19 LEU HD12 H 1 1.090 0.030 . 1 . . . . 19 LEU HD1 . 10150 1 174 . 1 1 19 19 LEU HD13 H 1 1.090 0.030 . 1 . . . . 19 LEU HD1 . 10150 1 175 . 1 1 19 19 LEU CD2 C 13 23.791 0.300 . 2 . . . . 19 LEU CD2 . 10150 1 176 . 1 1 19 19 LEU HD21 H 1 1.020 0.030 . 1 . . . . 19 LEU HD2 . 10150 1 177 . 1 1 19 19 LEU HD22 H 1 1.020 0.030 . 1 . . . . 19 LEU HD2 . 10150 1 178 . 1 1 19 19 LEU HD23 H 1 1.020 0.030 . 1 . . . . 19 LEU HD2 . 10150 1 179 . 1 1 19 19 LEU C C 13 178.634 0.300 . 1 . . . . 19 LEU C . 10150 1 180 . 1 1 20 20 LEU N N 15 120.243 0.300 . 1 . . . . 20 LEU N . 10150 1 181 . 1 1 20 20 LEU H H 1 8.364 0.030 . 1 . . . . 20 LEU H . 10150 1 182 . 1 1 20 20 LEU CA C 13 58.390 0.300 . 1 . . . . 20 LEU CA . 10150 1 183 . 1 1 20 20 LEU HA H 1 4.083 0.030 . 1 . . . . 20 LEU HA . 10150 1 184 . 1 1 20 20 LEU CB C 13 42.005 0.300 . 1 . . . . 20 LEU CB . 10150 1 185 . 1 1 20 20 LEU HB2 H 1 2.558 0.030 . 2 . . . . 20 LEU HB2 . 10150 1 186 . 1 1 20 20 LEU HB3 H 1 1.929 0.030 . 2 . . . . 20 LEU HB3 . 10150 1 187 . 1 1 20 20 LEU CG C 13 27.570 0.300 . 1 . . . . 20 LEU CG . 10150 1 188 . 1 1 20 20 LEU HG H 1 1.798 0.030 . 1 . . . . 20 LEU HG . 10150 1 189 . 1 1 20 20 LEU CD1 C 13 26.887 0.300 . 2 . . . . 20 LEU CD1 . 10150 1 190 . 1 1 20 20 LEU HD11 H 1 1.072 0.030 . 1 . . . . 20 LEU HD1 . 10150 1 191 . 1 1 20 20 LEU HD12 H 1 1.072 0.030 . 1 . . . . 20 LEU HD1 . 10150 1 192 . 1 1 20 20 LEU HD13 H 1 1.072 0.030 . 1 . . . . 20 LEU HD1 . 10150 1 193 . 1 1 20 20 LEU CD2 C 13 24.435 0.300 . 2 . . . . 20 LEU CD2 . 10150 1 194 . 1 1 20 20 LEU HD21 H 1 1.166 0.030 . 1 . . . . 20 LEU HD2 . 10150 1 195 . 1 1 20 20 LEU HD22 H 1 1.166 0.030 . 1 . . . . 20 LEU HD2 . 10150 1 196 . 1 1 20 20 LEU HD23 H 1 1.166 0.030 . 1 . . . . 20 LEU HD2 . 10150 1 197 . 1 1 20 20 LEU C C 13 178.135 0.300 . 1 . . . . 20 LEU C . 10150 1 198 . 1 1 21 21 ILE N N 15 119.379 0.300 . 1 . . . . 21 ILE N . 10150 1 199 . 1 1 21 21 ILE H H 1 8.133 0.030 . 1 . . . . 21 ILE H . 10150 1 200 . 1 1 21 21 ILE CA C 13 64.962 0.300 . 1 . . . . 21 ILE CA . 10150 1 201 . 1 1 21 21 ILE HA H 1 3.685 0.030 . 1 . . . . 21 ILE HA . 10150 1 202 . 1 1 21 21 ILE CB C 13 37.895 0.300 . 1 . . . . 21 ILE CB . 10150 1 203 . 1 1 21 21 ILE HB H 1 1.998 0.030 . 1 . . . . 21 ILE HB . 10150 1 204 . 1 1 21 21 ILE CG1 C 13 28.914 0.300 . 1 . . . . 21 ILE CG1 . 10150 1 205 . 1 1 21 21 ILE HG12 H 1 1.713 0.030 . 2 . . . . 21 ILE HG12 . 10150 1 206 . 1 1 21 21 ILE HG13 H 1 1.234 0.030 . 2 . . . . 21 ILE HG13 . 10150 1 207 . 1 1 21 21 ILE CG2 C 13 17.463 0.300 . 1 . . . . 21 ILE CG2 . 10150 1 208 . 1 1 21 21 ILE HG21 H 1 0.975 0.030 . 1 . . . . 21 ILE HG2 . 10150 1 209 . 1 1 21 21 ILE HG22 H 1 0.975 0.030 . 1 . . . . 21 ILE HG2 . 10150 1 210 . 1 1 21 21 ILE HG23 H 1 0.975 0.030 . 1 . . . . 21 ILE HG2 . 10150 1 211 . 1 1 21 21 ILE CD1 C 13 12.671 0.300 . 1 . . . . 21 ILE CD1 . 10150 1 212 . 1 1 21 21 ILE HD11 H 1 0.821 0.030 . 1 . . . . 21 ILE HD1 . 10150 1 213 . 1 1 21 21 ILE HD12 H 1 0.821 0.030 . 1 . . . . 21 ILE HD1 . 10150 1 214 . 1 1 21 21 ILE HD13 H 1 0.821 0.030 . 1 . . . . 21 ILE HD1 . 10150 1 215 . 1 1 21 21 ILE C C 13 178.423 0.300 . 1 . . . . 21 ILE C . 10150 1 216 . 1 1 22 22 ASP N N 15 120.464 0.300 . 1 . . . . 22 ASP N . 10150 1 217 . 1 1 22 22 ASP H H 1 8.203 0.030 . 1 . . . . 22 ASP H . 10150 1 218 . 1 1 22 22 ASP CA C 13 57.332 0.300 . 1 . . . . 22 ASP CA . 10150 1 219 . 1 1 22 22 ASP HA H 1 4.400 0.030 . 1 . . . . 22 ASP HA . 10150 1 220 . 1 1 22 22 ASP CB C 13 41.023 0.300 . 1 . . . . 22 ASP CB . 10150 1 221 . 1 1 22 22 ASP HB2 H 1 2.983 0.030 . 2 . . . . 22 ASP HB2 . 10150 1 222 . 1 1 22 22 ASP HB3 H 1 2.828 0.030 . 2 . . . . 22 ASP HB3 . 10150 1 223 . 1 1 22 22 ASP C C 13 179.117 0.300 . 1 . . . . 22 ASP C . 10150 1 224 . 1 1 23 23 ALA N N 15 123.634 0.300 . 1 . . . . 23 ALA N . 10150 1 225 . 1 1 23 23 ALA H H 1 8.819 0.030 . 1 . . . . 23 ALA H . 10150 1 226 . 1 1 23 23 ALA CA C 13 55.058 0.300 . 1 . . . . 23 ALA CA . 10150 1 227 . 1 1 23 23 ALA HA H 1 3.050 0.030 . 1 . . . . 23 ALA HA . 10150 1 228 . 1 1 23 23 ALA CB C 13 20.405 0.300 . 1 . . . . 23 ALA CB . 10150 1 229 . 1 1 23 23 ALA HB1 H 1 1.461 0.030 . 1 . . . . 23 ALA HB . 10150 1 230 . 1 1 23 23 ALA HB2 H 1 1.461 0.030 . 1 . . . . 23 ALA HB . 10150 1 231 . 1 1 23 23 ALA HB3 H 1 1.461 0.030 . 1 . . . . 23 ALA HB . 10150 1 232 . 1 1 23 23 ALA C C 13 179.042 0.300 . 1 . . . . 23 ALA C . 10150 1 233 . 1 1 24 24 CYS N N 15 115.941 0.300 . 1 . . . . 24 CYS N . 10150 1 234 . 1 1 24 24 CYS H H 1 8.227 0.030 . 1 . . . . 24 CYS H . 10150 1 235 . 1 1 24 24 CYS CA C 13 63.657 0.300 . 1 . . . . 24 CYS CA . 10150 1 236 . 1 1 24 24 CYS HA H 1 3.524 0.030 . 1 . . . . 24 CYS HA . 10150 1 237 . 1 1 24 24 CYS CB C 13 27.165 0.300 . 1 . . . . 24 CYS CB . 10150 1 238 . 1 1 24 24 CYS HB2 H 1 2.733 0.030 . 2 . . . . 24 CYS HB2 . 10150 1 239 . 1 1 24 24 CYS HB3 H 1 2.262 0.030 . 2 . . . . 24 CYS HB3 . 10150 1 240 . 1 1 24 24 CYS C C 13 177.855 0.300 . 1 . . . . 24 CYS C . 10150 1 241 . 1 1 25 25 GLU N N 15 118.624 0.300 . 1 . . . . 25 GLU N . 10150 1 242 . 1 1 25 25 GLU H H 1 8.262 0.030 . 1 . . . . 25 GLU H . 10150 1 243 . 1 1 25 25 GLU CA C 13 58.829 0.300 . 1 . . . . 25 GLU CA . 10150 1 244 . 1 1 25 25 GLU HA H 1 3.974 0.030 . 1 . . . . 25 GLU HA . 10150 1 245 . 1 1 25 25 GLU CB C 13 29.896 0.300 . 1 . . . . 25 GLU CB . 10150 1 246 . 1 1 25 25 GLU HB2 H 1 2.122 0.030 . 2 . . . . 25 GLU HB2 . 10150 1 247 . 1 1 25 25 GLU HB3 H 1 2.031 0.030 . 2 . . . . 25 GLU HB3 . 10150 1 248 . 1 1 25 25 GLU CG C 13 36.390 0.300 . 1 . . . . 25 GLU CG . 10150 1 249 . 1 1 25 25 GLU HG2 H 1 2.405 0.030 . 2 . . . . 25 GLU HG2 . 10150 1 250 . 1 1 25 25 GLU HG3 H 1 2.239 0.030 . 2 . . . . 25 GLU HG3 . 10150 1 251 . 1 1 25 25 GLU C C 13 178.082 0.300 . 1 . . . . 25 GLU C . 10150 1 252 . 1 1 26 26 THR N N 15 113.708 0.300 . 1 . . . . 26 THR N . 10150 1 253 . 1 1 26 26 THR H H 1 8.046 0.030 . 1 . . . . 26 THR H . 10150 1 254 . 1 1 26 26 THR CA C 13 65.448 0.300 . 1 . . . . 26 THR CA . 10150 1 255 . 1 1 26 26 THR HA H 1 4.003 0.030 . 1 . . . . 26 THR HA . 10150 1 256 . 1 1 26 26 THR CB C 13 69.475 0.300 . 1 . . . . 26 THR CB . 10150 1 257 . 1 1 26 26 THR HB H 1 3.953 0.030 . 1 . . . . 26 THR HB . 10150 1 258 . 1 1 26 26 THR CG2 C 13 21.321 0.300 . 1 . . . . 26 THR CG2 . 10150 1 259 . 1 1 26 26 THR HG21 H 1 1.192 0.030 . 1 . . . . 26 THR HG2 . 10150 1 260 . 1 1 26 26 THR HG22 H 1 1.192 0.030 . 1 . . . . 26 THR HG2 . 10150 1 261 . 1 1 26 26 THR HG23 H 1 1.192 0.030 . 1 . . . . 26 THR HG2 . 10150 1 262 . 1 1 26 26 THR C C 13 175.986 0.300 . 1 . . . . 26 THR C . 10150 1 263 . 1 1 27 27 LEU N N 15 119.789 0.300 . 1 . . . . 27 LEU N . 10150 1 264 . 1 1 27 27 LEU H H 1 8.609 0.030 . 1 . . . . 27 LEU H . 10150 1 265 . 1 1 27 27 LEU CA C 13 55.566 0.300 . 1 . . . . 27 LEU CA . 10150 1 266 . 1 1 27 27 LEU HA H 1 4.238 0.030 . 1 . . . . 27 LEU HA . 10150 1 267 . 1 1 27 27 LEU CB C 13 42.130 0.300 . 1 . . . . 27 LEU CB . 10150 1 268 . 1 1 27 27 LEU HB2 H 1 1.764 0.030 . 2 . . . . 27 LEU HB2 . 10150 1 269 . 1 1 27 27 LEU HB3 H 1 1.351 0.030 . 2 . . . . 27 LEU HB3 . 10150 1 270 . 1 1 27 27 LEU CG C 13 26.964 0.300 . 1 . . . . 27 LEU CG . 10150 1 271 . 1 1 27 27 LEU HG H 1 1.449 0.030 . 1 . . . . 27 LEU HG . 10150 1 272 . 1 1 27 27 LEU CD1 C 13 25.906 0.300 . 2 . . . . 27 LEU CD1 . 10150 1 273 . 1 1 27 27 LEU HD11 H 1 0.597 0.030 . 1 . . . . 27 LEU HD1 . 10150 1 274 . 1 1 27 27 LEU HD12 H 1 0.597 0.030 . 1 . . . . 27 LEU HD1 . 10150 1 275 . 1 1 27 27 LEU HD13 H 1 0.597 0.030 . 1 . . . . 27 LEU HD1 . 10150 1 276 . 1 1 27 27 LEU CD2 C 13 22.311 0.300 . 2 . . . . 27 LEU CD2 . 10150 1 277 . 1 1 27 27 LEU HD21 H 1 0.784 0.030 . 1 . . . . 27 LEU HD2 . 10150 1 278 . 1 1 27 27 LEU HD22 H 1 0.784 0.030 . 1 . . . . 27 LEU HD2 . 10150 1 279 . 1 1 27 27 LEU HD23 H 1 0.784 0.030 . 1 . . . . 27 LEU HD2 . 10150 1 280 . 1 1 27 27 LEU C C 13 179.075 0.300 . 1 . . . . 27 LEU C . 10150 1 281 . 1 1 28 28 GLY N N 15 107.009 0.300 . 1 . . . . 28 GLY N . 10150 1 282 . 1 1 28 28 GLY H H 1 6.965 0.030 . 1 . . . . 28 GLY H . 10150 1 283 . 1 1 28 28 GLY CA C 13 44.545 0.300 . 1 . . . . 28 GLY CA . 10150 1 284 . 1 1 28 28 GLY HA2 H 1 4.057 0.030 . 2 . . . . 28 GLY HA2 . 10150 1 285 . 1 1 28 28 GLY HA3 H 1 3.664 0.030 . 2 . . . . 28 GLY HA3 . 10150 1 286 . 1 1 28 28 GLY C C 13 173.046 0.300 . 1 . . . . 28 GLY C . 10150 1 287 . 1 1 29 29 LEU N N 15 117.364 0.300 . 1 . . . . 29 LEU N . 10150 1 288 . 1 1 29 29 LEU H H 1 7.960 0.030 . 1 . . . . 29 LEU H . 10150 1 289 . 1 1 29 29 LEU CA C 13 54.626 0.300 . 1 . . . . 29 LEU CA . 10150 1 290 . 1 1 29 29 LEU HA H 1 3.487 0.030 . 1 . . . . 29 LEU HA . 10150 1 291 . 1 1 29 29 LEU CB C 13 40.949 0.300 . 1 . . . . 29 LEU CB . 10150 1 292 . 1 1 29 29 LEU HB2 H 1 1.476 0.030 . 2 . . . . 29 LEU HB2 . 10150 1 293 . 1 1 29 29 LEU HB3 H 1 1.397 0.030 . 2 . . . . 29 LEU HB3 . 10150 1 294 . 1 1 29 29 LEU CG C 13 27.115 0.300 . 1 . . . . 29 LEU CG . 10150 1 295 . 1 1 29 29 LEU HG H 1 1.413 0.030 . 1 . . . . 29 LEU HG . 10150 1 296 . 1 1 29 29 LEU CD1 C 13 23.081 0.300 . 2 . . . . 29 LEU CD1 . 10150 1 297 . 1 1 29 29 LEU HD11 H 1 0.410 0.030 . 1 . . . . 29 LEU HD1 . 10150 1 298 . 1 1 29 29 LEU HD12 H 1 0.410 0.030 . 1 . . . . 29 LEU HD1 . 10150 1 299 . 1 1 29 29 LEU HD13 H 1 0.410 0.030 . 1 . . . . 29 LEU HD1 . 10150 1 300 . 1 1 29 29 LEU CD2 C 13 25.395 0.300 . 2 . . . . 29 LEU CD2 . 10150 1 301 . 1 1 29 29 LEU HD21 H 1 0.820 0.030 . 1 . . . . 29 LEU HD2 . 10150 1 302 . 1 1 29 29 LEU HD22 H 1 0.820 0.030 . 1 . . . . 29 LEU HD2 . 10150 1 303 . 1 1 29 29 LEU HD23 H 1 0.820 0.030 . 1 . . . . 29 LEU HD2 . 10150 1 304 . 1 1 29 29 LEU C C 13 177.460 0.300 . 1 . . . . 29 LEU C . 10150 1 305 . 1 1 30 30 GLY N N 15 106.469 0.300 . 1 . . . . 30 GLY N . 10150 1 306 . 1 1 30 30 GLY H H 1 7.503 0.030 . 1 . . . . 30 GLY H . 10150 1 307 . 1 1 30 30 GLY CA C 13 46.003 0.300 . 1 . . . . 30 GLY CA . 10150 1 308 . 1 1 30 30 GLY HA2 H 1 3.781 0.030 . 2 . . . . 30 GLY HA2 . 10150 1 309 . 1 1 30 30 GLY HA3 H 1 3.638 0.030 . 2 . . . . 30 GLY HA3 . 10150 1 310 . 1 1 30 30 GLY C C 13 174.269 0.300 . 1 . . . . 30 GLY C . 10150 1 311 . 1 1 31 31 ASN N N 15 117.981 0.300 . 1 . . . . 31 ASN N . 10150 1 312 . 1 1 31 31 ASN H H 1 7.643 0.030 . 1 . . . . 31 ASN H . 10150 1 313 . 1 1 31 31 ASN CA C 13 52.135 0.300 . 1 . . . . 31 ASN CA . 10150 1 314 . 1 1 31 31 ASN HA H 1 4.899 0.030 . 1 . . . . 31 ASN HA . 10150 1 315 . 1 1 31 31 ASN CB C 13 38.492 0.300 . 1 . . . . 31 ASN CB . 10150 1 316 . 1 1 31 31 ASN HB2 H 1 2.921 0.030 . 2 . . . . 31 ASN HB2 . 10150 1 317 . 1 1 31 31 ASN HB3 H 1 2.529 0.030 . 2 . . . . 31 ASN HB3 . 10150 1 318 . 1 1 31 31 ASN ND2 N 15 113.868 0.300 . 1 . . . . 31 ASN ND2 . 10150 1 319 . 1 1 31 31 ASN HD21 H 1 7.545 0.030 . 2 . . . . 31 ASN HD21 . 10150 1 320 . 1 1 31 31 ASN HD22 H 1 6.994 0.030 . 2 . . . . 31 ASN HD22 . 10150 1 321 . 1 1 31 31 ASN C C 13 176.436 0.300 . 1 . . . . 31 ASN C . 10150 1 322 . 1 1 32 32 TRP N N 15 124.932 0.300 . 1 . . . . 32 TRP N . 10150 1 323 . 1 1 32 32 TRP H H 1 8.638 0.030 . 1 . . . . 32 TRP H . 10150 1 324 . 1 1 32 32 TRP CA C 13 60.578 0.300 . 1 . . . . 32 TRP CA . 10150 1 325 . 1 1 32 32 TRP HA H 1 4.257 0.030 . 1 . . . . 32 TRP HA . 10150 1 326 . 1 1 32 32 TRP CB C 13 29.185 0.300 . 1 . . . . 32 TRP CB . 10150 1 327 . 1 1 32 32 TRP HB2 H 1 3.602 0.030 . 2 . . . . 32 TRP HB2 . 10150 1 328 . 1 1 32 32 TRP HB3 H 1 2.986 0.030 . 2 . . . . 32 TRP HB3 . 10150 1 329 . 1 1 32 32 TRP CD1 C 13 127.368 0.300 . 1 . . . . 32 TRP CD1 . 10150 1 330 . 1 1 32 32 TRP HD1 H 1 7.389 0.030 . 1 . . . . 32 TRP HD1 . 10150 1 331 . 1 1 32 32 TRP NE1 N 15 129.039 0.300 . 1 . . . . 32 TRP NE1 . 10150 1 332 . 1 1 32 32 TRP HE1 H 1 10.217 0.030 . 1 . . . . 32 TRP HE1 . 10150 1 333 . 1 1 32 32 TRP CE3 C 13 119.942 0.300 . 1 . . . . 32 TRP CE3 . 10150 1 334 . 1 1 32 32 TRP HE3 H 1 7.274 0.030 . 1 . . . . 32 TRP HE3 . 10150 1 335 . 1 1 32 32 TRP CZ2 C 13 114.109 0.300 . 1 . . . . 32 TRP CZ2 . 10150 1 336 . 1 1 32 32 TRP HZ2 H 1 7.350 0.030 . 1 . . . . 32 TRP HZ2 . 10150 1 337 . 1 1 32 32 TRP CZ3 C 13 121.756 0.300 . 1 . . . . 32 TRP CZ3 . 10150 1 338 . 1 1 32 32 TRP HZ3 H 1 6.615 0.030 . 1 . . . . 32 TRP HZ3 . 10150 1 339 . 1 1 32 32 TRP CH2 C 13 125.499 0.300 . 1 . . . . 32 TRP CH2 . 10150 1 340 . 1 1 32 32 TRP HH2 H 1 6.808 0.030 . 1 . . . . 32 TRP HH2 . 10150 1 341 . 1 1 32 32 TRP C C 13 177.477 0.300 . 1 . . . . 32 TRP C . 10150 1 342 . 1 1 33 33 ALA N N 15 123.791 0.300 . 1 . . . . 33 ALA N . 10150 1 343 . 1 1 33 33 ALA H H 1 8.522 0.030 . 1 . . . . 33 ALA H . 10150 1 344 . 1 1 33 33 ALA CA C 13 55.609 0.300 . 1 . . . . 33 ALA CA . 10150 1 345 . 1 1 33 33 ALA HA H 1 4.245 0.030 . 1 . . . . 33 ALA HA . 10150 1 346 . 1 1 33 33 ALA CB C 13 17.931 0.300 . 1 . . . . 33 ALA CB . 10150 1 347 . 1 1 33 33 ALA HB1 H 1 1.570 0.030 . 1 . . . . 33 ALA HB . 10150 1 348 . 1 1 33 33 ALA HB2 H 1 1.570 0.030 . 1 . . . . 33 ALA HB . 10150 1 349 . 1 1 33 33 ALA HB3 H 1 1.570 0.030 . 1 . . . . 33 ALA HB . 10150 1 350 . 1 1 33 33 ALA C C 13 179.868 0.300 . 1 . . . . 33 ALA C . 10150 1 351 . 1 1 34 34 ASP N N 15 118.553 0.300 . 1 . . . . 34 ASP N . 10150 1 352 . 1 1 34 34 ASP H H 1 7.463 0.030 . 1 . . . . 34 ASP H . 10150 1 353 . 1 1 34 34 ASP CA C 13 56.937 0.300 . 1 . . . . 34 ASP CA . 10150 1 354 . 1 1 34 34 ASP HA H 1 4.378 0.030 . 1 . . . . 34 ASP HA . 10150 1 355 . 1 1 34 34 ASP CB C 13 40.089 0.300 . 1 . . . . 34 ASP CB . 10150 1 356 . 1 1 34 34 ASP HB2 H 1 2.662 0.030 . 2 . . . . 34 ASP HB2 . 10150 1 357 . 1 1 34 34 ASP HB3 H 1 2.544 0.030 . 2 . . . . 34 ASP HB3 . 10150 1 358 . 1 1 34 34 ASP C C 13 179.385 0.300 . 1 . . . . 34 ASP C . 10150 1 359 . 1 1 35 35 ILE N N 15 121.343 0.300 . 1 . . . . 35 ILE N . 10150 1 360 . 1 1 35 35 ILE H H 1 7.308 0.030 . 1 . . . . 35 ILE H . 10150 1 361 . 1 1 35 35 ILE CA C 13 64.900 0.300 . 1 . . . . 35 ILE CA . 10150 1 362 . 1 1 35 35 ILE HA H 1 3.528 0.030 . 1 . . . . 35 ILE HA . 10150 1 363 . 1 1 35 35 ILE CB C 13 37.842 0.300 . 1 . . . . 35 ILE CB . 10150 1 364 . 1 1 35 35 ILE HB H 1 2.023 0.030 . 1 . . . . 35 ILE HB . 10150 1 365 . 1 1 35 35 ILE CG1 C 13 29.311 0.300 . 1 . . . . 35 ILE CG1 . 10150 1 366 . 1 1 35 35 ILE HG12 H 1 1.232 0.030 . 2 . . . . 35 ILE HG12 . 10150 1 367 . 1 1 35 35 ILE HG13 H 1 0.739 0.030 . 2 . . . . 35 ILE HG13 . 10150 1 368 . 1 1 35 35 ILE CG2 C 13 17.574 0.300 . 1 . . . . 35 ILE CG2 . 10150 1 369 . 1 1 35 35 ILE HG21 H 1 1.036 0.030 . 1 . . . . 35 ILE HG2 . 10150 1 370 . 1 1 35 35 ILE HG22 H 1 1.036 0.030 . 1 . . . . 35 ILE HG2 . 10150 1 371 . 1 1 35 35 ILE HG23 H 1 1.036 0.030 . 1 . . . . 35 ILE HG2 . 10150 1 372 . 1 1 35 35 ILE CD1 C 13 12.433 0.300 . 1 . . . . 35 ILE CD1 . 10150 1 373 . 1 1 35 35 ILE HD11 H 1 0.106 0.030 . 1 . . . . 35 ILE HD1 . 10150 1 374 . 1 1 35 35 ILE HD12 H 1 0.106 0.030 . 1 . . . . 35 ILE HD1 . 10150 1 375 . 1 1 35 35 ILE HD13 H 1 0.106 0.030 . 1 . . . . 35 ILE HD1 . 10150 1 376 . 1 1 35 35 ILE C C 13 176.832 0.300 . 1 . . . . 35 ILE C . 10150 1 377 . 1 1 36 36 ALA N N 15 122.328 0.300 . 1 . . . . 36 ALA N . 10150 1 378 . 1 1 36 36 ALA H H 1 8.446 0.030 . 1 . . . . 36 ALA H . 10150 1 379 . 1 1 36 36 ALA CA C 13 55.724 0.300 . 1 . . . . 36 ALA CA . 10150 1 380 . 1 1 36 36 ALA HA H 1 4.281 0.030 . 1 . . . . 36 ALA HA . 10150 1 381 . 1 1 36 36 ALA CB C 13 17.153 0.300 . 1 . . . . 36 ALA CB . 10150 1 382 . 1 1 36 36 ALA HB1 H 1 1.473 0.030 . 1 . . . . 36 ALA HB . 10150 1 383 . 1 1 36 36 ALA HB2 H 1 1.473 0.030 . 1 . . . . 36 ALA HB . 10150 1 384 . 1 1 36 36 ALA HB3 H 1 1.473 0.030 . 1 . . . . 36 ALA HB . 10150 1 385 . 1 1 36 36 ALA C C 13 181.002 0.300 . 1 . . . . 36 ALA C . 10150 1 386 . 1 1 37 37 ASP N N 15 119.092 0.300 . 1 . . . . 37 ASP N . 10150 1 387 . 1 1 37 37 ASP H H 1 7.997 0.030 . 1 . . . . 37 ASP H . 10150 1 388 . 1 1 37 37 ASP CA C 13 57.105 0.300 . 1 . . . . 37 ASP CA . 10150 1 389 . 1 1 37 37 ASP HA H 1 4.392 0.030 . 1 . . . . 37 ASP HA . 10150 1 390 . 1 1 37 37 ASP CB C 13 40.808 0.300 . 1 . . . . 37 ASP CB . 10150 1 391 . 1 1 37 37 ASP HB2 H 1 2.818 0.030 . 2 . . . . 37 ASP HB2 . 10150 1 392 . 1 1 37 37 ASP HB3 H 1 2.716 0.030 . 2 . . . . 37 ASP HB3 . 10150 1 393 . 1 1 37 37 ASP C C 13 177.292 0.300 . 1 . . . . 37 ASP C . 10150 1 394 . 1 1 38 38 TYR N N 15 121.825 0.300 . 1 . . . . 38 TYR N . 10150 1 395 . 1 1 38 38 TYR H H 1 7.648 0.030 . 1 . . . . 38 TYR H . 10150 1 396 . 1 1 38 38 TYR CA C 13 60.838 0.300 . 1 . . . . 38 TYR CA . 10150 1 397 . 1 1 38 38 TYR HA H 1 4.046 0.030 . 1 . . . . 38 TYR HA . 10150 1 398 . 1 1 38 38 TYR CB C 13 39.411 0.300 . 1 . . . . 38 TYR CB . 10150 1 399 . 1 1 38 38 TYR HB2 H 1 3.316 0.030 . 2 . . . . 38 TYR HB2 . 10150 1 400 . 1 1 38 38 TYR HB3 H 1 3.002 0.030 . 2 . . . . 38 TYR HB3 . 10150 1 401 . 1 1 38 38 TYR CD1 C 13 133.754 0.300 . 1 . . . . 38 TYR CD1 . 10150 1 402 . 1 1 38 38 TYR HD1 H 1 7.025 0.030 . 1 . . . . 38 TYR HD1 . 10150 1 403 . 1 1 38 38 TYR CD2 C 13 133.754 0.300 . 1 . . . . 38 TYR CD2 . 10150 1 404 . 1 1 38 38 TYR HD2 H 1 7.025 0.030 . 1 . . . . 38 TYR HD2 . 10150 1 405 . 1 1 38 38 TYR CE1 C 13 118.252 0.300 . 1 . . . . 38 TYR CE1 . 10150 1 406 . 1 1 38 38 TYR HE1 H 1 6.895 0.030 . 1 . . . . 38 TYR HE1 . 10150 1 407 . 1 1 38 38 TYR CE2 C 13 118.252 0.300 . 1 . . . . 38 TYR CE2 . 10150 1 408 . 1 1 38 38 TYR HE2 H 1 6.895 0.030 . 1 . . . . 38 TYR HE2 . 10150 1 409 . 1 1 38 38 TYR C C 13 177.306 0.300 . 1 . . . . 38 TYR C . 10150 1 410 . 1 1 39 39 VAL N N 15 118.437 0.300 . 1 . . . . 39 VAL N . 10150 1 411 . 1 1 39 39 VAL H H 1 8.306 0.030 . 1 . . . . 39 VAL H . 10150 1 412 . 1 1 39 39 VAL CA C 13 65.398 0.300 . 1 . . . . 39 VAL CA . 10150 1 413 . 1 1 39 39 VAL HA H 1 3.707 0.030 . 1 . . . . 39 VAL HA . 10150 1 414 . 1 1 39 39 VAL CB C 13 32.833 0.300 . 1 . . . . 39 VAL CB . 10150 1 415 . 1 1 39 39 VAL HB H 1 2.220 0.030 . 1 . . . . 39 VAL HB . 10150 1 416 . 1 1 39 39 VAL CG1 C 13 21.759 0.300 . 2 . . . . 39 VAL CG1 . 10150 1 417 . 1 1 39 39 VAL HG11 H 1 1.080 0.030 . 1 . . . . 39 VAL HG1 . 10150 1 418 . 1 1 39 39 VAL HG12 H 1 1.080 0.030 . 1 . . . . 39 VAL HG1 . 10150 1 419 . 1 1 39 39 VAL HG13 H 1 1.080 0.030 . 1 . . . . 39 VAL HG1 . 10150 1 420 . 1 1 39 39 VAL CG2 C 13 23.281 0.300 . 2 . . . . 39 VAL CG2 . 10150 1 421 . 1 1 39 39 VAL HG21 H 1 1.258 0.030 . 1 . . . . 39 VAL HG2 . 10150 1 422 . 1 1 39 39 VAL HG22 H 1 1.258 0.030 . 1 . . . . 39 VAL HG2 . 10150 1 423 . 1 1 39 39 VAL HG23 H 1 1.258 0.030 . 1 . . . . 39 VAL HG2 . 10150 1 424 . 1 1 39 39 VAL C C 13 177.244 0.300 . 1 . . . . 39 VAL C . 10150 1 425 . 1 1 40 40 GLY N N 15 105.738 0.300 . 1 . . . . 40 GLY N . 10150 1 426 . 1 1 40 40 GLY H H 1 8.117 0.030 . 1 . . . . 40 GLY H . 10150 1 427 . 1 1 40 40 GLY CA C 13 45.890 0.300 . 1 . . . . 40 GLY CA . 10150 1 428 . 1 1 40 40 GLY HA2 H 1 3.896 0.030 . 2 . . . . 40 GLY HA2 . 10150 1 429 . 1 1 40 40 GLY HA3 H 1 3.694 0.030 . 2 . . . . 40 GLY HA3 . 10150 1 430 . 1 1 40 40 GLY C C 13 173.930 0.300 . 1 . . . . 40 GLY C . 10150 1 431 . 1 1 41 41 ASN N N 15 116.713 0.300 . 1 . . . . 41 ASN N . 10150 1 432 . 1 1 41 41 ASN H H 1 8.620 0.030 . 1 . . . . 41 ASN H . 10150 1 433 . 1 1 41 41 ASN CA C 13 54.192 0.300 . 1 . . . . 41 ASN CA . 10150 1 434 . 1 1 41 41 ASN HA H 1 4.253 0.030 . 1 . . . . 41 ASN HA . 10150 1 435 . 1 1 41 41 ASN CB C 13 38.370 0.300 . 1 . . . . 41 ASN CB . 10150 1 436 . 1 1 41 41 ASN HB2 H 1 2.909 0.030 . 2 . . . . 41 ASN HB2 . 10150 1 437 . 1 1 41 41 ASN HB3 H 1 2.623 0.030 . 2 . . . . 41 ASN HB3 . 10150 1 438 . 1 1 41 41 ASN ND2 N 15 113.392 0.300 . 1 . . . . 41 ASN ND2 . 10150 1 439 . 1 1 41 41 ASN HD21 H 1 7.668 0.030 . 2 . . . . 41 ASN HD21 . 10150 1 440 . 1 1 41 41 ASN HD22 H 1 6.797 0.030 . 2 . . . . 41 ASN HD22 . 10150 1 441 . 1 1 41 41 ASN C C 13 173.935 0.300 . 1 . . . . 41 ASN C . 10150 1 442 . 1 1 42 42 ALA N N 15 115.074 0.300 . 1 . . . . 42 ALA N . 10150 1 443 . 1 1 42 42 ALA H H 1 8.425 0.030 . 1 . . . . 42 ALA H . 10150 1 444 . 1 1 42 42 ALA CA C 13 52.968 0.300 . 1 . . . . 42 ALA CA . 10150 1 445 . 1 1 42 42 ALA HA H 1 3.876 0.030 . 1 . . . . 42 ALA HA . 10150 1 446 . 1 1 42 42 ALA CB C 13 17.871 0.300 . 1 . . . . 42 ALA CB . 10150 1 447 . 1 1 42 42 ALA HB1 H 1 1.377 0.030 . 1 . . . . 42 ALA HB . 10150 1 448 . 1 1 42 42 ALA HB2 H 1 1.377 0.030 . 1 . . . . 42 ALA HB . 10150 1 449 . 1 1 42 42 ALA HB3 H 1 1.377 0.030 . 1 . . . . 42 ALA HB . 10150 1 450 . 1 1 42 42 ALA C C 13 177.531 0.300 . 1 . . . . 42 ALA C . 10150 1 451 . 1 1 43 43 ARG N N 15 119.427 0.300 . 1 . . . . 43 ARG N . 10150 1 452 . 1 1 43 43 ARG H H 1 7.773 0.030 . 1 . . . . 43 ARG H . 10150 1 453 . 1 1 43 43 ARG CA C 13 54.411 0.300 . 1 . . . . 43 ARG CA . 10150 1 454 . 1 1 43 43 ARG HA H 1 4.447 0.030 . 1 . . . . 43 ARG HA . 10150 1 455 . 1 1 43 43 ARG CB C 13 30.954 0.300 . 1 . . . . 43 ARG CB . 10150 1 456 . 1 1 43 43 ARG HB2 H 1 1.905 0.030 . 2 . . . . 43 ARG HB2 . 10150 1 457 . 1 1 43 43 ARG HB3 H 1 1.484 0.030 . 2 . . . . 43 ARG HB3 . 10150 1 458 . 1 1 43 43 ARG CG C 13 25.261 0.300 . 1 . . . . 43 ARG CG . 10150 1 459 . 1 1 43 43 ARG HG2 H 1 0.996 0.030 . 2 . . . . 43 ARG HG2 . 10150 1 460 . 1 1 43 43 ARG HG3 H 1 1.492 0.030 . 2 . . . . 43 ARG HG3 . 10150 1 461 . 1 1 43 43 ARG CD C 13 42.973 0.300 . 1 . . . . 43 ARG CD . 10150 1 462 . 1 1 43 43 ARG HD2 H 1 2.809 0.030 . 2 . . . . 43 ARG HD2 . 10150 1 463 . 1 1 43 43 ARG HD3 H 1 2.118 0.030 . 2 . . . . 43 ARG HD3 . 10150 1 464 . 1 1 43 43 ARG NE N 15 83.747 0.300 . 1 . . . . 43 ARG NE . 10150 1 465 . 1 1 43 43 ARG HE H 1 6.765 0.030 . 1 . . . . 43 ARG HE . 10150 1 466 . 1 1 43 43 ARG C C 13 177.734 0.300 . 1 . . . . 43 ARG C . 10150 1 467 . 1 1 44 44 THR N N 15 113.165 0.300 . 1 . . . . 44 THR N . 10150 1 468 . 1 1 44 44 THR H H 1 8.918 0.030 . 1 . . . . 44 THR H . 10150 1 469 . 1 1 44 44 THR CA C 13 60.337 0.300 . 1 . . . . 44 THR CA . 10150 1 470 . 1 1 44 44 THR HA H 1 4.625 0.030 . 1 . . . . 44 THR HA . 10150 1 471 . 1 1 44 44 THR CB C 13 72.316 0.300 . 1 . . . . 44 THR CB . 10150 1 472 . 1 1 44 44 THR HB H 1 4.841 0.030 . 1 . . . . 44 THR HB . 10150 1 473 . 1 1 44 44 THR CG2 C 13 22.007 0.300 . 1 . . . . 44 THR CG2 . 10150 1 474 . 1 1 44 44 THR HG21 H 1 1.410 0.030 . 1 . . . . 44 THR HG2 . 10150 1 475 . 1 1 44 44 THR HG22 H 1 1.410 0.030 . 1 . . . . 44 THR HG2 . 10150 1 476 . 1 1 44 44 THR HG23 H 1 1.410 0.030 . 1 . . . . 44 THR HG2 . 10150 1 477 . 1 1 44 44 THR C C 13 177.134 0.300 . 1 . . . . 44 THR C . 10150 1 478 . 1 1 45 45 LYS N N 15 121.142 0.300 . 1 . . . . 45 LYS N . 10150 1 479 . 1 1 45 45 LYS H H 1 9.432 0.030 . 1 . . . . 45 LYS H . 10150 1 480 . 1 1 45 45 LYS CA C 13 59.938 0.300 . 1 . . . . 45 LYS CA . 10150 1 481 . 1 1 45 45 LYS HA H 1 4.137 0.030 . 1 . . . . 45 LYS HA . 10150 1 482 . 1 1 45 45 LYS CB C 13 32.188 0.300 . 1 . . . . 45 LYS CB . 10150 1 483 . 1 1 45 45 LYS HB2 H 1 1.875 0.030 . 2 . . . . 45 LYS HB2 . 10150 1 484 . 1 1 45 45 LYS HB3 H 1 1.710 0.030 . 2 . . . . 45 LYS HB3 . 10150 1 485 . 1 1 45 45 LYS CG C 13 23.855 0.300 . 1 . . . . 45 LYS CG . 10150 1 486 . 1 1 45 45 LYS HG2 H 1 1.280 0.030 . 2 . . . . 45 LYS HG2 . 10150 1 487 . 1 1 45 45 LYS HG3 H 1 1.651 0.030 . 2 . . . . 45 LYS HG3 . 10150 1 488 . 1 1 45 45 LYS CD C 13 30.354 0.300 . 1 . . . . 45 LYS CD . 10150 1 489 . 1 1 45 45 LYS HD2 H 1 1.736 0.030 . 2 . . . . 45 LYS HD2 . 10150 1 490 . 1 1 45 45 LYS HD3 H 1 1.712 0.030 . 2 . . . . 45 LYS HD3 . 10150 1 491 . 1 1 45 45 LYS CE C 13 42.305 0.300 . 1 . . . . 45 LYS CE . 10150 1 492 . 1 1 45 45 LYS HE2 H 1 3.181 0.030 . 2 . . . . 45 LYS HE2 . 10150 1 493 . 1 1 45 45 LYS HE3 H 1 3.080 0.030 . 2 . . . . 45 LYS HE3 . 10150 1 494 . 1 1 45 45 LYS C C 13 177.330 0.300 . 1 . . . . 45 LYS C . 10150 1 495 . 1 1 46 46 GLU N N 15 120.446 0.300 . 1 . . . . 46 GLU N . 10150 1 496 . 1 1 46 46 GLU H H 1 8.577 0.030 . 1 . . . . 46 GLU H . 10150 1 497 . 1 1 46 46 GLU CA C 13 61.051 0.300 . 1 . . . . 46 GLU CA . 10150 1 498 . 1 1 46 46 GLU HA H 1 3.716 0.030 . 1 . . . . 46 GLU HA . 10150 1 499 . 1 1 46 46 GLU CB C 13 28.270 0.300 . 1 . . . . 46 GLU CB . 10150 1 500 . 1 1 46 46 GLU HB2 H 1 2.116 0.030 . 2 . . . . 46 GLU HB2 . 10150 1 501 . 1 1 46 46 GLU HB3 H 1 1.905 0.030 . 2 . . . . 46 GLU HB3 . 10150 1 502 . 1 1 46 46 GLU CG C 13 37.585 0.300 . 1 . . . . 46 GLU CG . 10150 1 503 . 1 1 46 46 GLU HG2 H 1 2.596 0.030 . 2 . . . . 46 GLU HG2 . 10150 1 504 . 1 1 46 46 GLU HG3 H 1 2.149 0.030 . 2 . . . . 46 GLU HG3 . 10150 1 505 . 1 1 46 46 GLU C C 13 178.200 0.300 . 1 . . . . 46 GLU C . 10150 1 506 . 1 1 47 47 GLU N N 15 119.411 0.300 . 1 . . . . 47 GLU N . 10150 1 507 . 1 1 47 47 GLU H H 1 7.874 0.030 . 1 . . . . 47 GLU H . 10150 1 508 . 1 1 47 47 GLU CA C 13 59.209 0.300 . 1 . . . . 47 GLU CA . 10150 1 509 . 1 1 47 47 GLU HA H 1 4.139 0.030 . 1 . . . . 47 GLU HA . 10150 1 510 . 1 1 47 47 GLU CB C 13 30.970 0.300 . 1 . . . . 47 GLU CB . 10150 1 511 . 1 1 47 47 GLU HB2 H 1 2.470 0.030 . 2 . . . . 47 GLU HB2 . 10150 1 512 . 1 1 47 47 GLU HB3 H 1 2.218 0.030 . 2 . . . . 47 GLU HB3 . 10150 1 513 . 1 1 47 47 GLU CG C 13 37.829 0.300 . 1 . . . . 47 GLU CG . 10150 1 514 . 1 1 47 47 GLU HG2 H 1 2.466 0.030 . 1 . . . . 47 GLU HG2 . 10150 1 515 . 1 1 47 47 GLU HG3 H 1 2.466 0.030 . 1 . . . . 47 GLU HG3 . 10150 1 516 . 1 1 47 47 GLU C C 13 180.380 0.300 . 1 . . . . 47 GLU C . 10150 1 517 . 1 1 48 48 CYS N N 15 117.778 0.300 . 1 . . . . 48 CYS N . 10150 1 518 . 1 1 48 48 CYS H H 1 8.354 0.030 . 1 . . . . 48 CYS H . 10150 1 519 . 1 1 48 48 CYS CA C 13 65.002 0.300 . 1 . . . . 48 CYS CA . 10150 1 520 . 1 1 48 48 CYS HA H 1 4.331 0.030 . 1 . . . . 48 CYS HA . 10150 1 521 . 1 1 48 48 CYS CB C 13 27.262 0.300 . 1 . . . . 48 CYS CB . 10150 1 522 . 1 1 48 48 CYS HB2 H 1 3.429 0.030 . 2 . . . . 48 CYS HB2 . 10150 1 523 . 1 1 48 48 CYS HB3 H 1 2.812 0.030 . 2 . . . . 48 CYS HB3 . 10150 1 524 . 1 1 48 48 CYS C C 13 174.443 0.300 . 1 . . . . 48 CYS C . 10150 1 525 . 1 1 49 49 ARG N N 15 121.012 0.300 . 1 . . . . 49 ARG N . 10150 1 526 . 1 1 49 49 ARG H H 1 7.364 0.030 . 1 . . . . 49 ARG H . 10150 1 527 . 1 1 49 49 ARG CA C 13 58.352 0.300 . 1 . . . . 49 ARG CA . 10150 1 528 . 1 1 49 49 ARG HA H 1 1.940 0.030 . 1 . . . . 49 ARG HA . 10150 1 529 . 1 1 49 49 ARG CB C 13 29.691 0.300 . 1 . . . . 49 ARG CB . 10150 1 530 . 1 1 49 49 ARG HB2 H 1 1.243 0.030 . 2 . . . . 49 ARG HB2 . 10150 1 531 . 1 1 49 49 ARG HB3 H 1 0.040 0.030 . 2 . . . . 49 ARG HB3 . 10150 1 532 . 1 1 49 49 ARG CG C 13 26.546 0.300 . 1 . . . . 49 ARG CG . 10150 1 533 . 1 1 49 49 ARG HG2 H 1 0.879 0.030 . 2 . . . . 49 ARG HG2 . 10150 1 534 . 1 1 49 49 ARG HG3 H 1 0.560 0.030 . 2 . . . . 49 ARG HG3 . 10150 1 535 . 1 1 49 49 ARG CD C 13 43.280 0.300 . 1 . . . . 49 ARG CD . 10150 1 536 . 1 1 49 49 ARG HD2 H 1 2.767 0.030 . 2 . . . . 49 ARG HD2 . 10150 1 537 . 1 1 49 49 ARG HD3 H 1 2.602 0.030 . 2 . . . . 49 ARG HD3 . 10150 1 538 . 1 1 49 49 ARG C C 13 177.306 0.300 . 1 . . . . 49 ARG C . 10150 1 539 . 1 1 50 50 ASP N N 15 116.931 0.300 . 1 . . . . 50 ASP N . 10150 1 540 . 1 1 50 50 ASP H H 1 8.183 0.030 . 1 . . . . 50 ASP H . 10150 1 541 . 1 1 50 50 ASP CA C 13 57.267 0.300 . 1 . . . . 50 ASP CA . 10150 1 542 . 1 1 50 50 ASP HA H 1 4.170 0.030 . 1 . . . . 50 ASP HA . 10150 1 543 . 1 1 50 50 ASP CB C 13 40.569 0.300 . 1 . . . . 50 ASP CB . 10150 1 544 . 1 1 50 50 ASP HB2 H 1 2.653 0.030 . 2 . . . . 50 ASP HB2 . 10150 1 545 . 1 1 50 50 ASP HB3 H 1 2.539 0.030 . 2 . . . . 50 ASP HB3 . 10150 1 546 . 1 1 50 50 ASP C C 13 178.695 0.300 . 1 . . . . 50 ASP C . 10150 1 547 . 1 1 51 51 HIS N N 15 116.759 0.300 . 1 . . . . 51 HIS N . 10150 1 548 . 1 1 51 51 HIS H H 1 8.276 0.030 . 1 . . . . 51 HIS H . 10150 1 549 . 1 1 51 51 HIS CA C 13 59.374 0.300 . 1 . . . . 51 HIS CA . 10150 1 550 . 1 1 51 51 HIS HA H 1 3.986 0.030 . 1 . . . . 51 HIS HA . 10150 1 551 . 1 1 51 51 HIS CB C 13 28.534 0.300 . 1 . . . . 51 HIS CB . 10150 1 552 . 1 1 51 51 HIS HB2 H 1 2.994 0.030 . 2 . . . . 51 HIS HB2 . 10150 1 553 . 1 1 51 51 HIS HB3 H 1 2.442 0.030 . 2 . . . . 51 HIS HB3 . 10150 1 554 . 1 1 51 51 HIS CD2 C 13 117.909 0.300 . 1 . . . . 51 HIS CD2 . 10150 1 555 . 1 1 51 51 HIS HD2 H 1 5.673 0.030 . 1 . . . . 51 HIS HD2 . 10150 1 556 . 1 1 51 51 HIS CE1 C 13 136.629 0.300 . 1 . . . . 51 HIS CE1 . 10150 1 557 . 1 1 51 51 HIS HE1 H 1 8.130 0.030 . 1 . . . . 51 HIS HE1 . 10150 1 558 . 1 1 51 51 HIS C C 13 177.514 0.300 . 1 . . . . 51 HIS C . 10150 1 559 . 1 1 52 52 TYR N N 15 121.013 0.300 . 1 . . . . 52 TYR N . 10150 1 560 . 1 1 52 52 TYR H H 1 8.364 0.030 . 1 . . . . 52 TYR H . 10150 1 561 . 1 1 52 52 TYR CA C 13 62.363 0.300 . 1 . . . . 52 TYR CA . 10150 1 562 . 1 1 52 52 TYR HA H 1 3.951 0.030 . 1 . . . . 52 TYR HA . 10150 1 563 . 1 1 52 52 TYR CB C 13 39.610 0.300 . 1 . . . . 52 TYR CB . 10150 1 564 . 1 1 52 52 TYR HB2 H 1 3.218 0.030 . 1 . . . . 52 TYR HB2 . 10150 1 565 . 1 1 52 52 TYR HB3 H 1 3.218 0.030 . 1 . . . . 52 TYR HB3 . 10150 1 566 . 1 1 52 52 TYR CD1 C 13 133.330 0.300 . 1 . . . . 52 TYR CD1 . 10150 1 567 . 1 1 52 52 TYR HD1 H 1 6.992 0.030 . 1 . . . . 52 TYR HD1 . 10150 1 568 . 1 1 52 52 TYR CD2 C 13 133.330 0.300 . 1 . . . . 52 TYR CD2 . 10150 1 569 . 1 1 52 52 TYR HD2 H 1 6.992 0.030 . 1 . . . . 52 TYR HD2 . 10150 1 570 . 1 1 52 52 TYR CE1 C 13 118.497 0.300 . 1 . . . . 52 TYR CE1 . 10150 1 571 . 1 1 52 52 TYR HE1 H 1 6.664 0.030 . 1 . . . . 52 TYR HE1 . 10150 1 572 . 1 1 52 52 TYR CE2 C 13 118.497 0.300 . 1 . . . . 52 TYR CE2 . 10150 1 573 . 1 1 52 52 TYR HE2 H 1 6.664 0.030 . 1 . . . . 52 TYR HE2 . 10150 1 574 . 1 1 52 52 TYR C C 13 177.492 0.300 . 1 . . . . 52 TYR C . 10150 1 575 . 1 1 53 53 LEU N N 15 117.616 0.300 . 1 . . . . 53 LEU N . 10150 1 576 . 1 1 53 53 LEU H H 1 8.354 0.030 . 1 . . . . 53 LEU H . 10150 1 577 . 1 1 53 53 LEU CA C 13 57.261 0.300 . 1 . . . . 53 LEU CA . 10150 1 578 . 1 1 53 53 LEU HA H 1 3.985 0.030 . 1 . . . . 53 LEU HA . 10150 1 579 . 1 1 53 53 LEU CB C 13 41.403 0.300 . 1 . . . . 53 LEU CB . 10150 1 580 . 1 1 53 53 LEU HB2 H 1 1.823 0.030 . 2 . . . . 53 LEU HB2 . 10150 1 581 . 1 1 53 53 LEU HB3 H 1 1.486 0.030 . 2 . . . . 53 LEU HB3 . 10150 1 582 . 1 1 53 53 LEU CG C 13 27.131 0.300 . 1 . . . . 53 LEU CG . 10150 1 583 . 1 1 53 53 LEU HG H 1 1.970 0.030 . 1 . . . . 53 LEU HG . 10150 1 584 . 1 1 53 53 LEU CD1 C 13 25.641 0.300 . 2 . . . . 53 LEU CD1 . 10150 1 585 . 1 1 53 53 LEU HD11 H 1 0.897 0.030 . 1 . . . . 53 LEU HD1 . 10150 1 586 . 1 1 53 53 LEU HD12 H 1 0.897 0.030 . 1 . . . . 53 LEU HD1 . 10150 1 587 . 1 1 53 53 LEU HD13 H 1 0.897 0.030 . 1 . . . . 53 LEU HD1 . 10150 1 588 . 1 1 53 53 LEU CD2 C 13 22.749 0.300 . 2 . . . . 53 LEU CD2 . 10150 1 589 . 1 1 53 53 LEU HD21 H 1 1.017 0.030 . 1 . . . . 53 LEU HD2 . 10150 1 590 . 1 1 53 53 LEU HD22 H 1 1.017 0.030 . 1 . . . . 53 LEU HD2 . 10150 1 591 . 1 1 53 53 LEU HD23 H 1 1.017 0.030 . 1 . . . . 53 LEU HD2 . 10150 1 592 . 1 1 53 53 LEU C C 13 178.921 0.300 . 1 . . . . 53 LEU C . 10150 1 593 . 1 1 54 54 LYS N N 15 116.037 0.300 . 1 . . . . 54 LYS N . 10150 1 594 . 1 1 54 54 LYS H H 1 7.468 0.030 . 1 . . . . 54 LYS H . 10150 1 595 . 1 1 54 54 LYS CA C 13 57.859 0.300 . 1 . . . . 54 LYS CA . 10150 1 596 . 1 1 54 54 LYS HA H 1 4.006 0.030 . 1 . . . . 54 LYS HA . 10150 1 597 . 1 1 54 54 LYS CB C 13 32.668 0.300 . 1 . . . . 54 LYS CB . 10150 1 598 . 1 1 54 54 LYS HB2 H 1 1.712 0.030 . 2 . . . . 54 LYS HB2 . 10150 1 599 . 1 1 54 54 LYS HB3 H 1 1.639 0.030 . 2 . . . . 54 LYS HB3 . 10150 1 600 . 1 1 54 54 LYS CG C 13 25.129 0.300 . 1 . . . . 54 LYS CG . 10150 1 601 . 1 1 54 54 LYS HG2 H 1 1.375 0.030 . 2 . . . . 54 LYS HG2 . 10150 1 602 . 1 1 54 54 LYS HG3 H 1 1.313 0.030 . 2 . . . . 54 LYS HG3 . 10150 1 603 . 1 1 54 54 LYS CD C 13 29.119 0.300 . 1 . . . . 54 LYS CD . 10150 1 604 . 1 1 54 54 LYS HD2 H 1 1.533 0.030 . 1 . . . . 54 LYS HD2 . 10150 1 605 . 1 1 54 54 LYS HD3 H 1 1.533 0.030 . 1 . . . . 54 LYS HD3 . 10150 1 606 . 1 1 54 54 LYS CE C 13 42.064 0.300 . 1 . . . . 54 LYS CE . 10150 1 607 . 1 1 54 54 LYS HE2 H 1 2.866 0.030 . 1 . . . . 54 LYS HE2 . 10150 1 608 . 1 1 54 54 LYS HE3 H 1 2.866 0.030 . 1 . . . . 54 LYS HE3 . 10150 1 609 . 1 1 54 54 LYS C C 13 177.318 0.300 . 1 . . . . 54 LYS C . 10150 1 610 . 1 1 55 55 THR N N 15 111.885 0.300 . 1 . . . . 55 THR N . 10150 1 611 . 1 1 55 55 THR H H 1 7.259 0.030 . 1 . . . . 55 THR H . 10150 1 612 . 1 1 55 55 THR CA C 13 63.882 0.300 . 1 . . . . 55 THR CA . 10150 1 613 . 1 1 55 55 THR HA H 1 3.864 0.030 . 1 . . . . 55 THR HA . 10150 1 614 . 1 1 55 55 THR CB C 13 69.759 0.300 . 1 . . . . 55 THR CB . 10150 1 615 . 1 1 55 55 THR HB H 1 3.442 0.030 . 1 . . . . 55 THR HB . 10150 1 616 . 1 1 55 55 THR CG2 C 13 20.811 0.300 . 1 . . . . 55 THR CG2 . 10150 1 617 . 1 1 55 55 THR HG21 H 1 0.473 0.030 . 1 . . . . 55 THR HG2 . 10150 1 618 . 1 1 55 55 THR HG22 H 1 0.473 0.030 . 1 . . . . 55 THR HG2 . 10150 1 619 . 1 1 55 55 THR HG23 H 1 0.473 0.030 . 1 . . . . 55 THR HG2 . 10150 1 620 . 1 1 55 55 THR C C 13 174.423 0.300 . 1 . . . . 55 THR C . 10150 1 621 . 1 1 56 56 TYR N N 15 120.015 0.300 . 1 . . . . 56 TYR N . 10150 1 622 . 1 1 56 56 TYR H H 1 7.767 0.030 . 1 . . . . 56 TYR H . 10150 1 623 . 1 1 56 56 TYR CA C 13 58.699 0.300 . 1 . . . . 56 TYR CA . 10150 1 624 . 1 1 56 56 TYR HA H 1 4.388 0.030 . 1 . . . . 56 TYR HA . 10150 1 625 . 1 1 56 56 TYR CB C 13 38.568 0.300 . 1 . . . . 56 TYR CB . 10150 1 626 . 1 1 56 56 TYR HB2 H 1 2.794 0.030 . 2 . . . . 56 TYR HB2 . 10150 1 627 . 1 1 56 56 TYR HB3 H 1 2.124 0.030 . 2 . . . . 56 TYR HB3 . 10150 1 628 . 1 1 56 56 TYR CD1 C 13 133.324 0.300 . 1 . . . . 56 TYR CD1 . 10150 1 629 . 1 1 56 56 TYR HD1 H 1 6.875 0.030 . 1 . . . . 56 TYR HD1 . 10150 1 630 . 1 1 56 56 TYR CD2 C 13 133.324 0.300 . 1 . . . . 56 TYR CD2 . 10150 1 631 . 1 1 56 56 TYR HD2 H 1 6.875 0.030 . 1 . . . . 56 TYR HD2 . 10150 1 632 . 1 1 56 56 TYR CE1 C 13 117.643 0.300 . 1 . . . . 56 TYR CE1 . 10150 1 633 . 1 1 56 56 TYR HE1 H 1 6.654 0.030 . 1 . . . . 56 TYR HE1 . 10150 1 634 . 1 1 56 56 TYR CE2 C 13 117.643 0.300 . 1 . . . . 56 TYR CE2 . 10150 1 635 . 1 1 56 56 TYR HE2 H 1 6.654 0.030 . 1 . . . . 56 TYR HE2 . 10150 1 636 . 1 1 56 56 TYR C C 13 175.031 0.300 . 1 . . . . 56 TYR C . 10150 1 637 . 1 1 57 57 ILE N N 15 121.611 0.300 . 1 . . . . 57 ILE N . 10150 1 638 . 1 1 57 57 ILE H H 1 7.376 0.030 . 1 . . . . 57 ILE H . 10150 1 639 . 1 1 57 57 ILE CA C 13 60.560 0.300 . 1 . . . . 57 ILE CA . 10150 1 640 . 1 1 57 57 ILE HA H 1 4.155 0.030 . 1 . . . . 57 ILE HA . 10150 1 641 . 1 1 57 57 ILE CB C 13 38.585 0.300 . 1 . . . . 57 ILE CB . 10150 1 642 . 1 1 57 57 ILE HB H 1 1.944 0.030 . 1 . . . . 57 ILE HB . 10150 1 643 . 1 1 57 57 ILE CG1 C 13 27.135 0.300 . 1 . . . . 57 ILE CG1 . 10150 1 644 . 1 1 57 57 ILE HG12 H 1 1.384 0.030 . 2 . . . . 57 ILE HG12 . 10150 1 645 . 1 1 57 57 ILE HG13 H 1 1.155 0.030 . 2 . . . . 57 ILE HG13 . 10150 1 646 . 1 1 57 57 ILE CG2 C 13 17.399 0.300 . 1 . . . . 57 ILE CG2 . 10150 1 647 . 1 1 57 57 ILE HG21 H 1 0.858 0.030 . 1 . . . . 57 ILE HG2 . 10150 1 648 . 1 1 57 57 ILE HG22 H 1 0.858 0.030 . 1 . . . . 57 ILE HG2 . 10150 1 649 . 1 1 57 57 ILE HG23 H 1 0.858 0.030 . 1 . . . . 57 ILE HG2 . 10150 1 650 . 1 1 57 57 ILE CD1 C 13 12.020 0.300 . 1 . . . . 57 ILE CD1 . 10150 1 651 . 1 1 57 57 ILE HD11 H 1 0.821 0.030 . 1 . . . . 57 ILE HD1 . 10150 1 652 . 1 1 57 57 ILE HD12 H 1 0.821 0.030 . 1 . . . . 57 ILE HD1 . 10150 1 653 . 1 1 57 57 ILE HD13 H 1 0.821 0.030 . 1 . . . . 57 ILE HD1 . 10150 1 654 . 1 1 57 57 ILE C C 13 175.122 0.300 . 1 . . . . 57 ILE C . 10150 1 655 . 1 1 58 58 GLU N N 15 129.417 0.300 . 1 . . . . 58 GLU N . 10150 1 656 . 1 1 58 58 GLU H H 1 7.969 0.030 . 1 . . . . 58 GLU H . 10150 1 657 . 1 1 58 58 GLU CA C 13 58.257 0.300 . 1 . . . . 58 GLU CA . 10150 1 658 . 1 1 58 58 GLU HA H 1 4.001 0.030 . 1 . . . . 58 GLU HA . 10150 1 659 . 1 1 58 58 GLU CB C 13 31.112 0.300 . 1 . . . . 58 GLU CB . 10150 1 660 . 1 1 58 58 GLU HB2 H 1 1.977 0.030 . 2 . . . . 58 GLU HB2 . 10150 1 661 . 1 1 58 58 GLU HB3 H 1 1.861 0.030 . 2 . . . . 58 GLU HB3 . 10150 1 662 . 1 1 58 58 GLU CG C 13 36.844 0.300 . 1 . . . . 58 GLU CG . 10150 1 663 . 1 1 58 58 GLU HG2 H 1 2.181 0.030 . 1 . . . . 58 GLU HG2 . 10150 1 664 . 1 1 58 58 GLU HG3 H 1 2.181 0.030 . 1 . . . . 58 GLU HG3 . 10150 1 665 . 1 1 58 58 GLU C C 13 181.090 0.300 . 1 . . . . 58 GLU C . 10150 1 stop_ save_