data_19487 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19487 _Entry.Title ; Solution structure of the PP2WW mutant (KPP2WW) of HYPB ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2013-09-10 _Entry.Accession_date 2013-09-10 _Entry.Last_release_date 2014-02-12 _Entry.Original_release_date 2014-02-12 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Yong-Guang Gao . . . 19487 2 Hong-Yu Hu . . . 19487 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' . 19487 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID HYPB . 19487 'WW domain' . 19487 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19487 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 174 19487 '15N chemical shifts' 49 19487 '1H chemical shifts' 261 19487 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 . . 2014-02-12 2013-09-10 original author . 19487 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 19483 'WW domain of HYPB' 19487 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19487 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24412394 _Citation.Full_citation . _Citation.Title 'Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _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 2014 _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 Yong-Guang Gao . . . 19487 1 2 Hui Yang . . . 19487 1 3 Jian Zhao . . . 19487 1 4 Ya-Jun Jiang . . . 19487 1 5 Hong-Yu Hu . . . 19487 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19487 _Assembly.ID 1 _Assembly.Name 'PP2WW mutant (KPP2WW) of HYPB' _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 'PP2WW mutant (KPP2WW) of HYPB' 1 $KPP2WW A . yes native no no . . . 19487 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_KPP2WW _Entity.Sf_category entity _Entity.Sf_framecode KPP2WW _Entity.Entry_ID 19487 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name KPP2WW _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 ; GSDLPPPSPPAAATIVLPPN WKTARDPEGKIYYYHVITRQ TQWDPPTWESPGDDAS ; _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 56 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6193.844 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 19483 . WW_HYPB . . . . . 76.79 48 100.00 100.00 5.31e-22 . . . . 19487 1 2 no PDB 2MDC . "Solution Structure Of The Ww Domain Of Hypb" . . . . . 76.79 48 100.00 100.00 5.31e-22 . . . . 19487 1 3 no PDB 2MDI . "Solution Structure Of The Pp2ww Mutant (kpp2ww) Of Hypb" . . . . . 100.00 56 100.00 100.00 1.39e-30 . . . . 19487 1 4 no GB AAC26194 . "Huntingtin interacting protein [Homo sapiens]" . . . . . 76.79 178 100.00 100.00 7.31e-23 . . . . 19487 1 5 no GB AAC26846 . "huntingtin interacting protein HYPB [Homo sapiens]" . . . . . 76.79 127 100.00 100.00 1.07e-22 . . . . 19487 1 6 no REF XP_007534044 . "PREDICTED: histone-lysine N-methyltransferase SETD2 [Erinaceus europaeus]" . . . . . 76.79 2457 97.67 100.00 2.84e-21 . . . . 19487 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 1 GLY . 19487 1 2 2 SER . 19487 1 3 3 ASP . 19487 1 4 4 LEU . 19487 1 5 5 PRO . 19487 1 6 6 PRO . 19487 1 7 7 PRO . 19487 1 8 8 SER . 19487 1 9 9 PRO . 19487 1 10 10 PRO . 19487 1 11 11 ALA . 19487 1 12 12 ALA . 19487 1 13 13 ALA . 19487 1 14 14 THR . 19487 1 15 15 ILE . 19487 1 16 16 VAL . 19487 1 17 17 LEU . 19487 1 18 18 PRO . 19487 1 19 19 PRO . 19487 1 20 20 ASN . 19487 1 21 21 TRP . 19487 1 22 22 LYS . 19487 1 23 23 THR . 19487 1 24 24 ALA . 19487 1 25 25 ARG . 19487 1 26 26 ASP . 19487 1 27 27 PRO . 19487 1 28 28 GLU . 19487 1 29 29 GLY . 19487 1 30 30 LYS . 19487 1 31 31 ILE . 19487 1 32 32 TYR . 19487 1 33 33 TYR . 19487 1 34 34 TYR . 19487 1 35 35 HIS . 19487 1 36 36 VAL . 19487 1 37 37 ILE . 19487 1 38 38 THR . 19487 1 39 39 ARG . 19487 1 40 40 GLN . 19487 1 41 41 THR . 19487 1 42 42 GLN . 19487 1 43 43 TRP . 19487 1 44 44 ASP . 19487 1 45 45 PRO . 19487 1 46 46 PRO . 19487 1 47 47 THR . 19487 1 48 48 TRP . 19487 1 49 49 GLU . 19487 1 50 50 SER . 19487 1 51 51 PRO . 19487 1 52 52 GLY . 19487 1 53 53 ASP . 19487 1 54 54 ASP . 19487 1 55 55 ALA . 19487 1 56 56 SER . 19487 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 19487 1 . SER 2 2 19487 1 . ASP 3 3 19487 1 . LEU 4 4 19487 1 . PRO 5 5 19487 1 . PRO 6 6 19487 1 . PRO 7 7 19487 1 . SER 8 8 19487 1 . PRO 9 9 19487 1 . PRO 10 10 19487 1 . ALA 11 11 19487 1 . ALA 12 12 19487 1 . ALA 13 13 19487 1 . THR 14 14 19487 1 . ILE 15 15 19487 1 . VAL 16 16 19487 1 . LEU 17 17 19487 1 . PRO 18 18 19487 1 . PRO 19 19 19487 1 . ASN 20 20 19487 1 . TRP 21 21 19487 1 . LYS 22 22 19487 1 . THR 23 23 19487 1 . ALA 24 24 19487 1 . ARG 25 25 19487 1 . ASP 26 26 19487 1 . PRO 27 27 19487 1 . GLU 28 28 19487 1 . GLY 29 29 19487 1 . LYS 30 30 19487 1 . ILE 31 31 19487 1 . TYR 32 32 19487 1 . TYR 33 33 19487 1 . TYR 34 34 19487 1 . HIS 35 35 19487 1 . VAL 36 36 19487 1 . ILE 37 37 19487 1 . THR 38 38 19487 1 . ARG 39 39 19487 1 . GLN 40 40 19487 1 . THR 41 41 19487 1 . GLN 42 42 19487 1 . TRP 43 43 19487 1 . ASP 44 44 19487 1 . PRO 45 45 19487 1 . PRO 46 46 19487 1 . THR 47 47 19487 1 . TRP 48 48 19487 1 . GLU 49 49 19487 1 . SER 50 50 19487 1 . PRO 51 51 19487 1 . GLY 52 52 19487 1 . ASP 53 53 19487 1 . ASP 54 54 19487 1 . ALA 55 55 19487 1 . SER 56 56 19487 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 19487 _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 $KPP2WW . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19487 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 19487 _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 $KPP2WW . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET-32M . . . . . . 19487 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19487 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% 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 KPP2WW '[U-99% 13C; U-99% 15N]' . . 1 $KPP2WW . . 500 . . uM . . . . 19487 1 2 'sodium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 19487 1 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 19487 1 4 'sodium azide' 'natural abundance' . . . . . . 0.05 . . w/v . . . . 19487 1 5 H2O 'natural abundance' . . . . . . 95 . . % . . . . 19487 1 6 D2O 'natural abundance' . . . . . . 5 . . % . . . . 19487 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 19487 _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' 0.08 . M 19487 1 pH 6.5 . pH 19487 1 pressure 1 . atm 19487 1 temperature 273 . K 19487 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 19487 _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' . . 19487 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 19487 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 19487 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 19487 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 19487 2 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 19487 _Software.ID 3 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 19487 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19487 3 stop_ save_ save_ARIA _Software.Sf_category software _Software.Sf_framecode ARIA _Software.Entry_ID 19487 _Software.ID 4 _Software.Name ARIA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Linge, O'Donoghue and Nilges' . . 19487 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19487 4 stop_ save_ save_Molmol _Software.Sf_category software _Software.Sf_framecode Molmol _Software.Entry_ID 19487 _Software.ID 5 _Software.Name Molmol _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Koradi, Billeter and Wuthrich' . . 19487 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19487 5 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 19487 _Software.ID 6 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 19487 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 19487 6 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 19487 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _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 19487 _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 . . . 19487 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 19487 _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 . . . . . . . . . . . . . . . . 19487 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 3 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 5 '3D HNHA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 6 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 7 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 8 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 1 9 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 19487 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 19487 _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 na indirect 0.251449530 . . . . . . . . . 19487 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 19487 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 19487 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 19487 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 19487 1 2 '3D CBCA(CO)NH' . . . 19487 1 3 '3D HNCACB' . . . 19487 1 4 '3D HNCO' . . . 19487 1 5 '3D HNHA' . . . 19487 1 6 '3D C(CO)NH' . . . 19487 1 7 '3D HCCH-TOCSY' . . . 19487 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 SER H H 1 8.038 0.000 . 1 . . . A 2 SER H . 19487 1 2 . 1 1 2 2 SER HA H 1 4.489 0.007 . 1 . . . A 2 SER HA . 19487 1 3 . 1 1 2 2 SER HB2 H 1 4.211 0.008 . 2 . . . A 2 SER HB2 . 19487 1 4 . 1 1 2 2 SER HB3 H 1 3.832 0.009 . 2 . . . A 2 SER HB3 . 19487 1 5 . 1 1 2 2 SER C C 13 176.003 0.000 . 1 . . . A 2 SER C . 19487 1 6 . 1 1 2 2 SER CA C 13 58.265 0.030 . 1 . . . A 2 SER CA . 19487 1 7 . 1 1 2 2 SER CB C 13 63.93 0.062 . 1 . . . A 2 SER CB . 19487 1 8 . 1 1 2 2 SER N N 15 117.407 0.000 . 1 . . . A 2 SER N . 19487 1 9 . 1 1 3 3 ASP H H 1 8.506 0.003 . 1 . . . A 3 ASP H . 19487 1 10 . 1 1 3 3 ASP HA H 1 4.589 0.012 . 1 . . . A 3 ASP HA . 19487 1 11 . 1 1 3 3 ASP HB2 H 1 2.674 0.000 . 2 . . . A 3 ASP HB2 . 19487 1 12 . 1 1 3 3 ASP HB3 H 1 2.624 0.001 . 2 . . . A 3 ASP HB3 . 19487 1 13 . 1 1 3 3 ASP C C 13 175.831 0.000 . 1 . . . A 3 ASP C . 19487 1 14 . 1 1 3 3 ASP CA C 13 54.207 0.106 . 1 . . . A 3 ASP CA . 19487 1 15 . 1 1 3 3 ASP CB C 13 41.183 0.014 . 1 . . . A 3 ASP CB . 19487 1 16 . 1 1 3 3 ASP N N 15 122.561 0.021 . 1 . . . A 3 ASP N . 19487 1 17 . 1 1 4 4 LEU H H 1 8.187 0.002 . 1 . . . A 4 LEU H . 19487 1 18 . 1 1 4 4 LEU HA H 1 4.548 0.004 . 1 . . . A 4 LEU HA . 19487 1 19 . 1 1 4 4 LEU HB2 H 1 1.655 0.003 . 2 . . . A 4 LEU HB2 . 19487 1 20 . 1 1 4 4 LEU HB3 H 1 1.511 0.010 . 2 . . . A 4 LEU HB3 . 19487 1 21 . 1 1 4 4 LEU HG H 1 0.882 0.003 . 1 . . . A 4 LEU HG . 19487 1 22 . 1 1 4 4 LEU CA C 13 53.089 0.056 . 1 . . . A 4 LEU CA . 19487 1 23 . 1 1 4 4 LEU N N 15 123.656 0.020 . 1 . . . A 4 LEU N . 19487 1 24 . 1 1 7 7 PRO HA H 1 4.361 0.009 . 1 . . . A 7 PRO HA . 19487 1 25 . 1 1 7 7 PRO HB2 H 1 2.157 0.005 . 2 . . . A 7 PRO HB2 . 19487 1 26 . 1 1 7 7 PRO HB3 H 1 1.841 0.007 . 2 . . . A 7 PRO HB3 . 19487 1 27 . 1 1 7 7 PRO HG2 H 1 1.517 0.010 . 1 . . . A 7 PRO HG2 . 19487 1 28 . 1 1 7 7 PRO HG3 H 1 1.517 0.010 . 1 . . . A 7 PRO HG3 . 19487 1 29 . 1 1 7 7 PRO C C 13 175.043 0.000 . 1 . . . A 7 PRO C . 19487 1 30 . 1 1 7 7 PRO CA C 13 61.87 0.042 . 1 . . . A 7 PRO CA . 19487 1 31 . 1 1 7 7 PRO CB C 13 32.143 0.055 . 1 . . . A 7 PRO CB . 19487 1 32 . 1 1 7 7 PRO CG C 13 27.823 0.000 . 1 . . . A 7 PRO CG . 19487 1 33 . 1 1 8 8 SER H H 1 8.302 0.004 . 1 . . . A 8 SER H . 19487 1 34 . 1 1 8 8 SER HA H 1 3.925 0.005 . 1 . . . A 8 SER HA . 19487 1 35 . 1 1 8 8 SER HB2 H 1 3.693 0.008 . 2 . . . A 8 SER HB2 . 19487 1 36 . 1 1 8 8 SER HB3 H 1 3.549 0.002 . 2 . . . A 8 SER HB3 . 19487 1 37 . 1 1 8 8 SER CA C 13 57.475 0.040 . 1 . . . A 8 SER CA . 19487 1 38 . 1 1 8 8 SER CB C 13 62.096 0.084 . 1 . . . A 8 SER CB . 19487 1 39 . 1 1 8 8 SER N N 15 116.762 0.017 . 1 . . . A 8 SER N . 19487 1 40 . 1 1 11 11 ALA HA H 1 4.218 0.006 . 1 . . . A 11 ALA HA . 19487 1 41 . 1 1 11 11 ALA HB1 H 1 1.435 0.004 . 1 . . . A 11 ALA MB . 19487 1 42 . 1 1 11 11 ALA HB2 H 1 1.435 0.004 . 1 . . . A 11 ALA MB . 19487 1 43 . 1 1 11 11 ALA HB3 H 1 1.435 0.004 . 1 . . . A 11 ALA MB . 19487 1 44 . 1 1 11 11 ALA C C 13 178.565 0.000 . 1 . . . A 11 ALA C . 19487 1 45 . 1 1 11 11 ALA CA C 13 52.637 0.038 . 1 . . . A 11 ALA CA . 19487 1 46 . 1 1 11 11 ALA CB C 13 18.863 0.064 . 1 . . . A 11 ALA CB . 19487 1 47 . 1 1 12 12 ALA H H 1 8.596 0.003 . 1 . . . A 12 ALA H . 19487 1 48 . 1 1 12 12 ALA HA H 1 4.247 0.008 . 1 . . . A 12 ALA HA . 19487 1 49 . 1 1 12 12 ALA HB1 H 1 1.371 0.009 . 1 . . . A 12 ALA MB . 19487 1 50 . 1 1 12 12 ALA HB2 H 1 1.371 0.009 . 1 . . . A 12 ALA MB . 19487 1 51 . 1 1 12 12 ALA HB3 H 1 1.371 0.009 . 1 . . . A 12 ALA MB . 19487 1 52 . 1 1 12 12 ALA C C 13 177.718 0.000 . 1 . . . A 12 ALA C . 19487 1 53 . 1 1 12 12 ALA CA C 13 53.529 0.068 . 1 . . . A 12 ALA CA . 19487 1 54 . 1 1 12 12 ALA CB C 13 19.033 0.054 . 1 . . . A 12 ALA CB . 19487 1 55 . 1 1 12 12 ALA N N 15 125.155 0.022 . 1 . . . A 12 ALA N . 19487 1 56 . 1 1 13 13 ALA H H 1 8.117 0.004 . 1 . . . A 13 ALA H . 19487 1 57 . 1 1 13 13 ALA HA H 1 4.387 0.006 . 1 . . . A 13 ALA HA . 19487 1 58 . 1 1 13 13 ALA HB1 H 1 1.379 0.004 . 1 . . . A 13 ALA MB . 19487 1 59 . 1 1 13 13 ALA HB2 H 1 1.379 0.004 . 1 . . . A 13 ALA MB . 19487 1 60 . 1 1 13 13 ALA HB3 H 1 1.379 0.004 . 1 . . . A 13 ALA MB . 19487 1 61 . 1 1 13 13 ALA C C 13 177.521 0.000 . 1 . . . A 13 ALA C . 19487 1 62 . 1 1 13 13 ALA CA C 13 52.079 0.035 . 1 . . . A 13 ALA CA . 19487 1 63 . 1 1 13 13 ALA CB C 13 19.732 0.052 . 1 . . . A 13 ALA CB . 19487 1 64 . 1 1 13 13 ALA N N 15 122.474 0.031 . 1 . . . A 13 ALA N . 19487 1 65 . 1 1 14 14 THR H H 1 8.202 0.006 . 1 . . . A 14 THR H . 19487 1 66 . 1 1 14 14 THR HA H 1 4.196 0.000 . 1 . . . A 14 THR HA . 19487 1 67 . 1 1 14 14 THR HG21 H 1 1.183 0.002 . 1 . . . A 14 THR MG . 19487 1 68 . 1 1 14 14 THR HG22 H 1 1.183 0.002 . 1 . . . A 14 THR MG . 19487 1 69 . 1 1 14 14 THR HG23 H 1 1.183 0.002 . 1 . . . A 14 THR MG . 19487 1 70 . 1 1 14 14 THR C C 13 174.319 0.000 . 1 . . . A 14 THR C . 19487 1 71 . 1 1 14 14 THR CA C 13 62.631 0.073 . 1 . . . A 14 THR CA . 19487 1 72 . 1 1 14 14 THR CB C 13 69.638 0.055 . 1 . . . A 14 THR CB . 19487 1 73 . 1 1 14 14 THR CG2 C 13 21.868 0.100 . 1 . . . A 14 THR CG2 . 19487 1 74 . 1 1 14 14 THR N N 15 114.271 0.008 . 1 . . . A 14 THR N . 19487 1 75 . 1 1 15 15 ILE H H 1 8.149 0.005 . 1 . . . A 15 ILE H . 19487 1 76 . 1 1 15 15 ILE HA H 1 4.139 0.014 . 1 . . . A 15 ILE HA . 19487 1 77 . 1 1 15 15 ILE HB H 1 1.814 0.003 . 1 . . . A 15 ILE HB . 19487 1 78 . 1 1 15 15 ILE HG12 H 1 1.465 0.011 . 1 . . . A 15 ILE HG12 . 19487 1 79 . 1 1 15 15 ILE HG13 H 1 1.465 0.011 . 1 . . . A 15 ILE HG13 . 19487 1 80 . 1 1 15 15 ILE HG21 H 1 0.812 0.008 . 1 . . . A 15 ILE MG . 19487 1 81 . 1 1 15 15 ILE HG22 H 1 0.812 0.008 . 1 . . . A 15 ILE MG . 19487 1 82 . 1 1 15 15 ILE HG23 H 1 0.812 0.008 . 1 . . . A 15 ILE MG . 19487 1 83 . 1 1 15 15 ILE HD11 H 1 0.768 0.007 . 1 . . . A 15 ILE MD . 19487 1 84 . 1 1 15 15 ILE HD12 H 1 0.768 0.007 . 1 . . . A 15 ILE MD . 19487 1 85 . 1 1 15 15 ILE HD13 H 1 0.768 0.007 . 1 . . . A 15 ILE MD . 19487 1 86 . 1 1 15 15 ILE C C 13 175.396 0.000 . 1 . . . A 15 ILE C . 19487 1 87 . 1 1 15 15 ILE CA C 13 61.025 0.062 . 1 . . . A 15 ILE CA . 19487 1 88 . 1 1 15 15 ILE CB C 13 38.834 0.046 . 1 . . . A 15 ILE CB . 19487 1 89 . 1 1 15 15 ILE CG1 C 13 27.357 0.073 . 1 . . . A 15 ILE CG1 . 19487 1 90 . 1 1 15 15 ILE CG2 C 13 17.44 0.042 . 1 . . . A 15 ILE CG2 . 19487 1 91 . 1 1 15 15 ILE CD1 C 13 13.212 0.133 . 1 . . . A 15 ILE CD1 . 19487 1 92 . 1 1 15 15 ILE N N 15 125.881 0.020 . 1 . . . A 15 ILE N . 19487 1 93 . 1 1 16 16 VAL H H 1 8.453 0.003 . 1 . . . A 16 VAL H . 19487 1 94 . 1 1 16 16 VAL HA H 1 4.104 0.007 . 1 . . . A 16 VAL HA . 19487 1 95 . 1 1 16 16 VAL HB H 1 2.007 0.007 . 1 . . . A 16 VAL HB . 19487 1 96 . 1 1 16 16 VAL HG11 H 1 0.945 0.005 . 2 . . . A 16 VAL MG1 . 19487 1 97 . 1 1 16 16 VAL HG12 H 1 0.945 0.005 . 2 . . . A 16 VAL MG1 . 19487 1 98 . 1 1 16 16 VAL HG13 H 1 0.945 0.005 . 2 . . . A 16 VAL MG1 . 19487 1 99 . 1 1 16 16 VAL HG21 H 1 0.918 0.007 . 2 . . . A 16 VAL MG2 . 19487 1 100 . 1 1 16 16 VAL HG22 H 1 0.918 0.007 . 2 . . . A 16 VAL MG2 . 19487 1 101 . 1 1 16 16 VAL HG23 H 1 0.918 0.007 . 2 . . . A 16 VAL MG2 . 19487 1 102 . 1 1 16 16 VAL C C 13 175.476 0.000 . 1 . . . A 16 VAL C . 19487 1 103 . 1 1 16 16 VAL CA C 13 62.134 0.053 . 1 . . . A 16 VAL CA . 19487 1 104 . 1 1 16 16 VAL CB C 13 32.473 0.065 . 1 . . . A 16 VAL CB . 19487 1 105 . 1 1 16 16 VAL CG1 C 13 22.475 0.000 . 2 . . . A 16 VAL CG1 . 19487 1 106 . 1 1 16 16 VAL CG2 C 13 21.229 0.015 . 2 . . . A 16 VAL CG2 . 19487 1 107 . 1 1 16 16 VAL N N 15 128.849 0.019 . 1 . . . A 16 VAL N . 19487 1 108 . 1 1 17 17 LEU H H 1 8.538 0.005 . 1 . . . A 17 LEU H . 19487 1 109 . 1 1 17 17 LEU HA H 1 4.587 0.009 . 1 . . . A 17 LEU HA . 19487 1 110 . 1 1 17 17 LEU HB2 H 1 1.673 0.006 . 2 . . . A 17 LEU HB2 . 19487 1 111 . 1 1 17 17 LEU HB3 H 1 1.300 0.003 . 2 . . . A 17 LEU HB3 . 19487 1 112 . 1 1 17 17 LEU HD11 H 1 0.932 0.012 . 2 . . . A 17 LEU MD1 . 19487 1 113 . 1 1 17 17 LEU HD12 H 1 0.932 0.012 . 2 . . . A 17 LEU MD1 . 19487 1 114 . 1 1 17 17 LEU HD13 H 1 0.932 0.012 . 2 . . . A 17 LEU MD1 . 19487 1 115 . 1 1 17 17 LEU HD21 H 1 0.711 0.004 . 2 . . . A 17 LEU MD2 . 19487 1 116 . 1 1 17 17 LEU HD22 H 1 0.711 0.004 . 2 . . . A 17 LEU MD2 . 19487 1 117 . 1 1 17 17 LEU HD23 H 1 0.711 0.004 . 2 . . . A 17 LEU MD2 . 19487 1 118 . 1 1 17 17 LEU CA C 13 52.193 0.035 . 1 . . . A 17 LEU CA . 19487 1 119 . 1 1 17 17 LEU CB C 13 42.309 0.052 . 1 . . . A 17 LEU CB . 19487 1 120 . 1 1 17 17 LEU N N 15 128.264 0.018 . 1 . . . A 17 LEU N . 19487 1 121 . 1 1 19 19 PRO HA H 1 4.200 0.002 . 1 . . . A 19 PRO HA . 19487 1 122 . 1 1 19 19 PRO HB2 H 1 2.264 0.009 . 2 . . . A 19 PRO HB2 . 19487 1 123 . 1 1 19 19 PRO HB3 H 1 1.719 0.006 . 2 . . . A 19 PRO HB3 . 19487 1 124 . 1 1 19 19 PRO HG2 H 1 2.041 0.009 . 2 . . . A 19 PRO HG2 . 19487 1 125 . 1 1 19 19 PRO HG3 H 1 1.982 0.003 . 2 . . . A 19 PRO HG3 . 19487 1 126 . 1 1 19 19 PRO HD2 H 1 3.437 0.006 . 2 . . . A 19 PRO HD2 . 19487 1 127 . 1 1 19 19 PRO HD3 H 1 3.272 0.014 . 2 . . . A 19 PRO HD3 . 19487 1 128 . 1 1 19 19 PRO C C 13 176.905 0.000 . 1 . . . A 19 PRO C . 19487 1 129 . 1 1 19 19 PRO CA C 13 63.913 0.035 . 1 . . . A 19 PRO CA . 19487 1 130 . 1 1 19 19 PRO CB C 13 32.066 0.047 . 1 . . . A 19 PRO CB . 19487 1 131 . 1 1 19 19 PRO CG C 13 27.708 0.103 . 1 . . . A 19 PRO CG . 19487 1 132 . 1 1 19 19 PRO CD C 13 50.223 0.070 . 1 . . . A 19 PRO CD . 19487 1 133 . 1 1 20 20 ASN H H 1 8.543 0.003 . 1 . . . A 20 ASN H . 19487 1 134 . 1 1 20 20 ASN HA H 1 3.984 0.006 . 1 . . . A 20 ASN HA . 19487 1 135 . 1 1 20 20 ASN HB2 H 1 2.777 0.006 . 2 . . . A 20 ASN HB2 . 19487 1 136 . 1 1 20 20 ASN HD21 H 1 7.441 0.003 . 2 . . . A 20 ASN HD21 . 19487 1 137 . 1 1 20 20 ASN HD22 H 1 7.026 0.003 . 2 . . . A 20 ASN HD22 . 19487 1 138 . 1 1 20 20 ASN C C 13 172.258 0.000 . 1 . . . A 20 ASN C . 19487 1 139 . 1 1 20 20 ASN CA C 13 55.148 0.049 . 1 . . . A 20 ASN CA . 19487 1 140 . 1 1 20 20 ASN CB C 13 36.841 0.064 . 1 . . . A 20 ASN CB . 19487 1 141 . 1 1 20 20 ASN N N 15 111.422 0.129 . 1 . . . A 20 ASN N . 19487 1 142 . 1 1 20 20 ASN ND2 N 15 114.058 0.030 . 1 . . . A 20 ASN ND2 . 19487 1 143 . 1 1 21 21 TRP H H 1 7.400 0.009 . 1 . . . A 21 TRP H . 19487 1 144 . 1 1 21 21 TRP HA H 1 5.082 0.021 . 1 . . . A 21 TRP HA . 19487 1 145 . 1 1 21 21 TRP HB2 H 1 2.936 0.009 . 2 . . . A 21 TRP HB2 . 19487 1 146 . 1 1 21 21 TRP HB3 H 1 2.831 0.005 . 2 . . . A 21 TRP HB3 . 19487 1 147 . 1 1 21 21 TRP HE1 H 1 10.430 0.000 . 1 . . . A 21 TRP HE1 . 19487 1 148 . 1 1 21 21 TRP C C 13 175.610 0.000 . 1 . . . A 21 TRP C . 19487 1 149 . 1 1 21 21 TRP CA C 13 57.096 0.052 . 1 . . . A 21 TRP CA . 19487 1 150 . 1 1 21 21 TRP CB C 13 31.695 0.034 . 1 . . . A 21 TRP CB . 19487 1 151 . 1 1 21 21 TRP N N 15 117.593 0.014 . 1 . . . A 21 TRP N . 19487 1 152 . 1 1 21 21 TRP NE1 N 15 129.244 0.000 . 1 . . . A 21 TRP NE1 . 19487 1 153 . 1 1 22 22 LYS H H 1 9.007 0.003 . 1 . . . A 22 LYS H . 19487 1 154 . 1 1 22 22 LYS HA H 1 4.532 0.005 . 1 . . . A 22 LYS HA . 19487 1 155 . 1 1 22 22 LYS HB2 H 1 1.538 0.006 . 2 . . . A 22 LYS HB2 . 19487 1 156 . 1 1 22 22 LYS HG2 H 1 1.098 0.016 . 2 . . . A 22 LYS HG2 . 19487 1 157 . 1 1 22 22 LYS HG3 H 1 1.053 0.014 . 2 . . . A 22 LYS HG3 . 19487 1 158 . 1 1 22 22 LYS HD2 H 1 1.592 0.004 . 2 . . . A 22 LYS HD2 . 19487 1 159 . 1 1 22 22 LYS HD3 H 1 1.541 0.015 . 2 . . . A 22 LYS HD3 . 19487 1 160 . 1 1 22 22 LYS HE2 H 1 2.917 0.020 . 2 . . . A 22 LYS HE2 . 19487 1 161 . 1 1 22 22 LYS HE3 H 1 2.859 0.002 . 2 . . . A 22 LYS HE3 . 19487 1 162 . 1 1 22 22 LYS C C 13 174.616 0.000 . 1 . . . A 22 LYS C . 19487 1 163 . 1 1 22 22 LYS CA C 13 54.332 0.033 . 1 . . . A 22 LYS CA . 19487 1 164 . 1 1 22 22 LYS CG C 13 25.618 0.063 . 1 . . . A 22 LYS CG . 19487 1 165 . 1 1 22 22 LYS CD C 13 29.073 0.038 . 1 . . . A 22 LYS CD . 19487 1 166 . 1 1 22 22 LYS CE C 13 42.191 0.035 . 1 . . . A 22 LYS CE . 19487 1 167 . 1 1 22 22 LYS N N 15 121.362 0.045 . 1 . . . A 22 LYS N . 19487 1 168 . 1 1 23 23 THR H H 1 7.757 0.009 . 1 . . . A 23 THR H . 19487 1 169 . 1 1 23 23 THR HA H 1 4.986 0.005 . 1 . . . A 23 THR HA . 19487 1 170 . 1 1 23 23 THR HB H 1 3.883 0.007 . 1 . . . A 23 THR HB . 19487 1 171 . 1 1 23 23 THR HG21 H 1 1.082 0.003 . 1 . . . A 23 THR MG . 19487 1 172 . 1 1 23 23 THR HG22 H 1 1.082 0.003 . 1 . . . A 23 THR MG . 19487 1 173 . 1 1 23 23 THR HG23 H 1 1.082 0.003 . 1 . . . A 23 THR MG . 19487 1 174 . 1 1 23 23 THR C C 13 173.623 0.000 . 1 . . . A 23 THR C . 19487 1 175 . 1 1 23 23 THR CA C 13 59.791 0.030 . 1 . . . A 23 THR CA . 19487 1 176 . 1 1 23 23 THR CB C 13 71.679 0.063 . 1 . . . A 23 THR CB . 19487 1 177 . 1 1 23 23 THR CG2 C 13 22.959 0.080 . 1 . . . A 23 THR CG2 . 19487 1 178 . 1 1 23 23 THR N N 15 108.761 0.017 . 1 . . . A 23 THR N . 19487 1 179 . 1 1 24 24 ALA H H 1 8.352 0.005 . 1 . . . A 24 ALA H . 19487 1 180 . 1 1 24 24 ALA HA H 1 4.332 0.008 . 1 . . . A 24 ALA HA . 19487 1 181 . 1 1 24 24 ALA C C 13 173.702 0.000 . 1 . . . A 24 ALA C . 19487 1 182 . 1 1 24 24 ALA CA C 13 50.62 0.029 . 1 . . . A 24 ALA CA . 19487 1 183 . 1 1 24 24 ALA CB C 13 21.927 0.050 . 1 . . . A 24 ALA CB . 19487 1 184 . 1 1 24 24 ALA N N 15 124.455 0.034 . 1 . . . A 24 ALA N . 19487 1 185 . 1 1 25 25 ARG H H 1 7.882 0.020 . 1 . . . A 25 ARG H . 19487 1 186 . 1 1 25 25 ARG HB2 H 1 1.660 0.010 . 2 . . . A 25 ARG HB2 . 19487 1 187 . 1 1 25 25 ARG HB3 H 1 1.612 0.017 . 2 . . . A 25 ARG HB3 . 19487 1 188 . 1 1 25 25 ARG HG2 H 1 1.557 0.012 . 2 . . . A 25 ARG HG2 . 19487 1 189 . 1 1 25 25 ARG HG3 H 1 1.460 0.008 . 2 . . . A 25 ARG HG3 . 19487 1 190 . 1 1 25 25 ARG HD2 H 1 3.022 0.006 . 2 . . . A 25 ARG HD2 . 19487 1 191 . 1 1 25 25 ARG HD3 H 1 2.885 0.000 . 2 . . . A 25 ARG HD3 . 19487 1 192 . 1 1 25 25 ARG C C 13 176.810 0.000 . 1 . . . A 25 ARG C . 19487 1 193 . 1 1 25 25 ARG CA C 13 53.6 0.052 . 1 . . . A 25 ARG CA . 19487 1 194 . 1 1 25 25 ARG CB C 13 33.731 0.055 . 1 . . . A 25 ARG CB . 19487 1 195 . 1 1 25 25 ARG CG C 13 27.214 0.041 . 1 . . . A 25 ARG CG . 19487 1 196 . 1 1 25 25 ARG CD C 13 43.567 0.000 . 1 . . . A 25 ARG CD . 19487 1 197 . 1 1 25 25 ARG N N 15 115.144 0.012 . 1 . . . A 25 ARG N . 19487 1 198 . 1 1 26 26 ASP H H 1 9.402 0.004 . 1 . . . A 26 ASP H . 19487 1 199 . 1 1 26 26 ASP HA H 1 4.951 0.006 . 1 . . . A 26 ASP HA . 19487 1 200 . 1 1 26 26 ASP HB2 H 1 3.511 0.002 . 2 . . . A 26 ASP HB2 . 19487 1 201 . 1 1 26 26 ASP HB3 H 1 2.887 0.006 . 2 . . . A 26 ASP HB3 . 19487 1 202 . 1 1 26 26 ASP CA C 13 52.811 0.039 . 1 . . . A 26 ASP CA . 19487 1 203 . 1 1 26 26 ASP CB C 13 40.672 0.013 . 1 . . . A 26 ASP CB . 19487 1 204 . 1 1 26 26 ASP N N 15 126.595 0.021 . 1 . . . A 26 ASP N . 19487 1 205 . 1 1 27 27 PRO HA H 1 4.398 0.004 . 1 . . . A 27 PRO HA . 19487 1 206 . 1 1 27 27 PRO HB2 H 1 2.497 0.001 . 2 . . . A 27 PRO HB2 . 19487 1 207 . 1 1 27 27 PRO HB3 H 1 1.984 0.023 . 2 . . . A 27 PRO HB3 . 19487 1 208 . 1 1 27 27 PRO HG2 H 1 2.256 0.000 . 2 . . . A 27 PRO HG2 . 19487 1 209 . 1 1 27 27 PRO HG3 H 1 2.166 0.009 . 2 . . . A 27 PRO HG3 . 19487 1 210 . 1 1 27 27 PRO HD2 H 1 3.971 0.004 . 2 . . . A 27 PRO HD2 . 19487 1 211 . 1 1 27 27 PRO HD3 H 1 3.741 0.012 . 2 . . . A 27 PRO HD3 . 19487 1 212 . 1 1 27 27 PRO C C 13 177.645 0.000 . 1 . . . A 27 PRO C . 19487 1 213 . 1 1 27 27 PRO CA C 13 65.772 0.067 . 1 . . . A 27 PRO CA . 19487 1 214 . 1 1 27 27 PRO CB C 13 32.111 0.026 . 1 . . . A 27 PRO CB . 19487 1 215 . 1 1 27 27 PRO CG C 13 28.181 0.024 . 1 . . . A 27 PRO CG . 19487 1 216 . 1 1 27 27 PRO CD C 13 51.355 0.037 . 1 . . . A 27 PRO CD . 19487 1 217 . 1 1 28 28 GLU H H 1 7.970 0.003 . 1 . . . A 28 GLU H . 19487 1 218 . 1 1 28 28 GLU HA H 1 4.434 0.003 . 1 . . . A 28 GLU HA . 19487 1 219 . 1 1 28 28 GLU HB2 H 1 2.294 0.010 . 1 . . . A 28 GLU HB2 . 19487 1 220 . 1 1 28 28 GLU HB3 H 1 2.294 0.010 . 1 . . . A 28 GLU HB3 . 19487 1 221 . 1 1 28 28 GLU HG2 H 1 2.298 0.002 . 1 . . . A 28 GLU HG2 . 19487 1 222 . 1 1 28 28 GLU HG3 H 1 2.298 0.002 . 1 . . . A 28 GLU HG3 . 19487 1 223 . 1 1 28 28 GLU C C 13 176.259 0.000 . 1 . . . A 28 GLU C . 19487 1 224 . 1 1 28 28 GLU CA C 13 55.837 0.044 . 1 . . . A 28 GLU CA . 19487 1 225 . 1 1 28 28 GLU CB C 13 30.536 0.090 . 1 . . . A 28 GLU CB . 19487 1 226 . 1 1 28 28 GLU CG C 13 36.922 0.019 . 1 . . . A 28 GLU CG . 19487 1 227 . 1 1 28 28 GLU N N 15 115.064 0.085 . 1 . . . A 28 GLU N . 19487 1 228 . 1 1 29 29 GLY H H 1 8.445 0.003 . 1 . . . A 29 GLY H . 19487 1 229 . 1 1 29 29 GLY HA2 H 1 4.617 0.006 . 2 . . . A 29 GLY HA2 . 19487 1 230 . 1 1 29 29 GLY HA3 H 1 3.674 0.006 . 2 . . . A 29 GLY HA3 . 19487 1 231 . 1 1 29 29 GLY C C 13 175.283 0.000 . 1 . . . A 29 GLY C . 19487 1 232 . 1 1 29 29 GLY CA C 13 45.501 0.060 . 1 . . . A 29 GLY CA . 19487 1 233 . 1 1 29 29 GLY N N 15 107.797 0.021 . 1 . . . A 29 GLY N . 19487 1 234 . 1 1 30 30 LYS H H 1 9.011 0.005 . 1 . . . A 30 LYS H . 19487 1 235 . 1 1 30 30 LYS C C 13 176.712 0.000 . 1 . . . A 30 LYS C . 19487 1 236 . 1 1 30 30 LYS CA C 13 57.736 0.011 . 1 . . . A 30 LYS CA . 19487 1 237 . 1 1 30 30 LYS CB C 13 32.661 0.073 . 1 . . . A 30 LYS CB . 19487 1 238 . 1 1 30 30 LYS CG C 13 25.291 0.000 . 1 . . . A 30 LYS CG . 19487 1 239 . 1 1 30 30 LYS CD C 13 29.132 0.000 . 1 . . . A 30 LYS CD . 19487 1 240 . 1 1 30 30 LYS N N 15 124.471 0.020 . 1 . . . A 30 LYS N . 19487 1 241 . 1 1 31 31 ILE H H 1 8.425 0.004 . 1 . . . A 31 ILE H . 19487 1 242 . 1 1 31 31 ILE HA H 1 4.790 0.015 . 1 . . . A 31 ILE HA . 19487 1 243 . 1 1 31 31 ILE HB H 1 1.695 0.030 . 1 . . . A 31 ILE HB . 19487 1 244 . 1 1 31 31 ILE HG12 H 1 1.484 0.006 . 2 . . . A 31 ILE HG12 . 19487 1 245 . 1 1 31 31 ILE HG13 H 1 1.069 0.004 . 2 . . . A 31 ILE HG13 . 19487 1 246 . 1 1 31 31 ILE HG21 H 1 0.826 0.015 . 1 . . . A 31 ILE MG . 19487 1 247 . 1 1 31 31 ILE HG22 H 1 0.826 0.015 . 1 . . . A 31 ILE MG . 19487 1 248 . 1 1 31 31 ILE HG23 H 1 0.826 0.015 . 1 . . . A 31 ILE MG . 19487 1 249 . 1 1 31 31 ILE HD11 H 1 0.717 0.007 . 1 . . . A 31 ILE MD . 19487 1 250 . 1 1 31 31 ILE HD12 H 1 0.717 0.007 . 1 . . . A 31 ILE MD . 19487 1 251 . 1 1 31 31 ILE HD13 H 1 0.717 0.007 . 1 . . . A 31 ILE MD . 19487 1 252 . 1 1 31 31 ILE C C 13 174.765 0.000 . 1 . . . A 31 ILE C . 19487 1 253 . 1 1 31 31 ILE CA C 13 61.312 0.014 . 1 . . . A 31 ILE CA . 19487 1 254 . 1 1 31 31 ILE CB C 13 39.514 0.063 . 1 . . . A 31 ILE CB . 19487 1 255 . 1 1 31 31 ILE CG1 C 13 29.298 0.054 . 1 . . . A 31 ILE CG1 . 19487 1 256 . 1 1 31 31 ILE CG2 C 13 17.193 0.035 . 1 . . . A 31 ILE CG2 . 19487 1 257 . 1 1 31 31 ILE CD1 C 13 13.565 0.146 . 1 . . . A 31 ILE CD1 . 19487 1 258 . 1 1 31 31 ILE N N 15 125.370 0.023 . 1 . . . A 31 ILE N . 19487 1 259 . 1 1 32 32 TYR H H 1 8.673 0.004 . 1 . . . A 32 TYR H . 19487 1 260 . 1 1 32 32 TYR HA H 1 4.910 0.010 . 1 . . . A 32 TYR HA . 19487 1 261 . 1 1 32 32 TYR HB2 H 1 3.028 0.005 . 2 . . . A 32 TYR HB2 . 19487 1 262 . 1 1 32 32 TYR HB3 H 1 2.447 0.004 . 2 . . . A 32 TYR HB3 . 19487 1 263 . 1 1 32 32 TYR C C 13 170.944 0.000 . 1 . . . A 32 TYR C . 19487 1 264 . 1 1 32 32 TYR CA C 13 55.548 0.038 . 1 . . . A 32 TYR CA . 19487 1 265 . 1 1 32 32 TYR CB C 13 39.647 0.031 . 1 . . . A 32 TYR CB . 19487 1 266 . 1 1 32 32 TYR N N 15 121.507 0.019 . 1 . . . A 32 TYR N . 19487 1 267 . 1 1 33 33 TYR H H 1 8.700 0.004 . 1 . . . A 33 TYR H . 19487 1 268 . 1 1 33 33 TYR HA H 1 5.415 0.005 . 1 . . . A 33 TYR HA . 19487 1 269 . 1 1 33 33 TYR HB2 H 1 3.023 0.014 . 2 . . . A 33 TYR HB2 . 19487 1 270 . 1 1 33 33 TYR HB3 H 1 2.736 0.009 . 2 . . . A 33 TYR HB3 . 19487 1 271 . 1 1 33 33 TYR C C 13 175.515 0.000 . 1 . . . A 33 TYR C . 19487 1 272 . 1 1 33 33 TYR CA C 13 56.55 0.041 . 1 . . . A 33 TYR CA . 19487 1 273 . 1 1 33 33 TYR CB C 13 42.035 0.069 . 1 . . . A 33 TYR CB . 19487 1 274 . 1 1 33 33 TYR N N 15 116.433 0.018 . 1 . . . A 33 TYR N . 19487 1 275 . 1 1 34 34 TYR H H 1 9.324 0.006 . 1 . . . A 34 TYR H . 19487 1 276 . 1 1 34 34 TYR HB2 H 1 2.661 0.004 . 1 . . . A 34 TYR HB2 . 19487 1 277 . 1 1 34 34 TYR HB3 H 1 2.661 0.004 . 1 . . . A 34 TYR HB3 . 19487 1 278 . 1 1 34 34 TYR C C 13 171.057 0.000 . 1 . . . A 34 TYR C . 19487 1 279 . 1 1 34 34 TYR CA C 13 55.465 0.055 . 1 . . . A 34 TYR CA . 19487 1 280 . 1 1 34 34 TYR CB C 13 43.75 0.013 . 1 . . . A 34 TYR CB . 19487 1 281 . 1 1 34 34 TYR N N 15 117.980 0.016 . 1 . . . A 34 TYR N . 19487 1 282 . 1 1 35 35 HIS H H 1 7.704 0.010 . 1 . . . A 35 HIS H . 19487 1 283 . 1 1 35 35 HIS HA H 1 3.878 0.006 . 1 . . . A 35 HIS HA . 19487 1 284 . 1 1 35 35 HIS HB2 H 1 2.853 0.007 . 2 . . . A 35 HIS HB2 . 19487 1 285 . 1 1 35 35 HIS C C 13 178.739 0.000 . 1 . . . A 35 HIS C . 19487 1 286 . 1 1 35 35 HIS CA C 13 54.747 0.057 . 1 . . . A 35 HIS CA . 19487 1 287 . 1 1 35 35 HIS CB C 13 32.302 0.061 . 1 . . . A 35 HIS CB . 19487 1 288 . 1 1 35 35 HIS N N 15 124.333 0.024 . 1 . . . A 35 HIS N . 19487 1 289 . 1 1 36 36 VAL H H 1 8.559 0.004 . 1 . . . A 36 VAL H . 19487 1 290 . 1 1 36 36 VAL HA H 1 3.753 0.004 . 1 . . . A 36 VAL HA . 19487 1 291 . 1 1 36 36 VAL HB H 1 1.960 0.004 . 1 . . . A 36 VAL HB . 19487 1 292 . 1 1 36 36 VAL HG11 H 1 0.751 0.006 . 2 . . . A 36 VAL MG1 . 19487 1 293 . 1 1 36 36 VAL HG12 H 1 0.751 0.006 . 2 . . . A 36 VAL MG1 . 19487 1 294 . 1 1 36 36 VAL HG13 H 1 0.751 0.006 . 2 . . . A 36 VAL MG1 . 19487 1 295 . 1 1 36 36 VAL HG21 H 1 0.761 0.004 . 2 . . . A 36 VAL MG2 . 19487 1 296 . 1 1 36 36 VAL HG22 H 1 0.761 0.004 . 2 . . . A 36 VAL MG2 . 19487 1 297 . 1 1 36 36 VAL HG23 H 1 0.761 0.004 . 2 . . . A 36 VAL MG2 . 19487 1 298 . 1 1 36 36 VAL C C 13 176.638 0.000 . 1 . . . A 36 VAL C . 19487 1 299 . 1 1 36 36 VAL CA C 13 64.697 0.049 . 1 . . . A 36 VAL CA . 19487 1 300 . 1 1 36 36 VAL CB C 13 32.06 0.066 . 1 . . . A 36 VAL CB . 19487 1 301 . 1 1 36 36 VAL CG1 C 13 21.432 0.045 . 2 . . . A 36 VAL CG1 . 19487 1 302 . 1 1 36 36 VAL CG2 C 13 20.793 0.096 . 2 . . . A 36 VAL CG2 . 19487 1 303 . 1 1 36 36 VAL N N 15 123.002 0.021 . 1 . . . A 36 VAL N . 19487 1 304 . 1 1 37 37 ILE H H 1 8.904 0.007 . 1 . . . A 37 ILE H . 19487 1 305 . 1 1 37 37 ILE HA H 1 4.194 0.005 . 1 . . . A 37 ILE HA . 19487 1 306 . 1 1 37 37 ILE HB H 1 2.065 0.007 . 1 . . . A 37 ILE HB . 19487 1 307 . 1 1 37 37 ILE HG12 H 1 1.487 0.006 . 2 . . . A 37 ILE HG12 . 19487 1 308 . 1 1 37 37 ILE HG13 H 1 1.164 0.009 . 2 . . . A 37 ILE HG13 . 19487 1 309 . 1 1 37 37 ILE HD11 H 1 0.799 0.005 . 1 . . . A 37 ILE MD . 19487 1 310 . 1 1 37 37 ILE HD12 H 1 0.799 0.005 . 1 . . . A 37 ILE MD . 19487 1 311 . 1 1 37 37 ILE HD13 H 1 0.799 0.005 . 1 . . . A 37 ILE MD . 19487 1 312 . 1 1 37 37 ILE C C 13 178.269 0.000 . 1 . . . A 37 ILE C . 19487 1 313 . 1 1 37 37 ILE CA C 13 62.546 0.089 . 1 . . . A 37 ILE CA . 19487 1 314 . 1 1 37 37 ILE CB C 13 38.259 0.054 . 1 . . . A 37 ILE CB . 19487 1 315 . 1 1 37 37 ILE CG1 C 13 27.409 0.060 . 1 . . . A 37 ILE CG1 . 19487 1 316 . 1 1 37 37 ILE CG2 C 13 17.398 0.000 . 1 . . . A 37 ILE CG2 . 19487 1 317 . 1 1 37 37 ILE CD1 C 13 11.259 0.101 . 1 . . . A 37 ILE CD1 . 19487 1 318 . 1 1 37 37 ILE N N 15 120.608 0.013 . 1 . . . A 37 ILE N . 19487 1 319 . 1 1 38 38 THR H H 1 8.942 0.003 . 1 . . . A 38 THR H . 19487 1 320 . 1 1 38 38 THR HA H 1 4.014 0.004 . 1 . . . A 38 THR HA . 19487 1 321 . 1 1 38 38 THR HB H 1 4.243 0.004 . 1 . . . A 38 THR HB . 19487 1 322 . 1 1 38 38 THR HG21 H 1 0.777 0.009 . 1 . . . A 38 THR MG . 19487 1 323 . 1 1 38 38 THR HG22 H 1 0.777 0.009 . 1 . . . A 38 THR MG . 19487 1 324 . 1 1 38 38 THR HG23 H 1 0.777 0.009 . 1 . . . A 38 THR MG . 19487 1 325 . 1 1 38 38 THR C C 13 176.608 0.000 . 1 . . . A 38 THR C . 19487 1 326 . 1 1 38 38 THR CA C 13 63.181 0.035 . 1 . . . A 38 THR CA . 19487 1 327 . 1 1 38 38 THR CB C 13 69.34 0.041 . 1 . . . A 38 THR CB . 19487 1 328 . 1 1 38 38 THR CG2 C 13 21.1 0.081 . 1 . . . A 38 THR CG2 . 19487 1 329 . 1 1 38 38 THR N N 15 112.000 0.009 . 1 . . . A 38 THR N . 19487 1 330 . 1 1 39 39 ARG H H 1 8.111 0.005 . 1 . . . A 39 ARG H . 19487 1 331 . 1 1 39 39 ARG HA H 1 4.019 0.009 . 1 . . . A 39 ARG HA . 19487 1 332 . 1 1 39 39 ARG HB2 H 1 2.122 0.027 . 2 . . . A 39 ARG HB2 . 19487 1 333 . 1 1 39 39 ARG HB3 H 1 2.022 0.021 . 2 . . . A 39 ARG HB3 . 19487 1 334 . 1 1 39 39 ARG HG2 H 1 1.566 0.012 . 2 . . . A 39 ARG HG2 . 19487 1 335 . 1 1 39 39 ARG HG3 H 1 1.471 0.006 . 2 . . . A 39 ARG HG3 . 19487 1 336 . 1 1 39 39 ARG HD2 H 1 3.109 0.007 . 1 . . . A 39 ARG HD2 . 19487 1 337 . 1 1 39 39 ARG HD3 H 1 3.109 0.007 . 1 . . . A 39 ARG HD3 . 19487 1 338 . 1 1 39 39 ARG C C 13 174.659 0.000 . 1 . . . A 39 ARG C . 19487 1 339 . 1 1 39 39 ARG CA C 13 56.924 0.049 . 1 . . . A 39 ARG CA . 19487 1 340 . 1 1 39 39 ARG CG C 13 26.772 0.012 . 1 . . . A 39 ARG CG . 19487 1 341 . 1 1 39 39 ARG CD C 13 42.492 0.046 . 1 . . . A 39 ARG CD . 19487 1 342 . 1 1 39 39 ARG N N 15 113.683 0.023 . 1 . . . A 39 ARG N . 19487 1 343 . 1 1 40 40 GLN H H 1 7.740 0.007 . 1 . . . A 40 GLN H . 19487 1 344 . 1 1 40 40 GLN HA H 1 4.335 0.009 . 1 . . . A 40 GLN HA . 19487 1 345 . 1 1 40 40 GLN HB2 H 1 2.048 0.005 . 2 . . . A 40 GLN HB2 . 19487 1 346 . 1 1 40 40 GLN HB3 H 1 1.998 0.019 . 2 . . . A 40 GLN HB3 . 19487 1 347 . 1 1 40 40 GLN HG2 H 1 2.409 0.004 . 2 . . . A 40 GLN HG2 . 19487 1 348 . 1 1 40 40 GLN HG3 H 1 2.215 0.004 . 2 . . . A 40 GLN HG3 . 19487 1 349 . 1 1 40 40 GLN HE21 H 1 7.913 0.002 . 2 . . . A 40 GLN HE21 . 19487 1 350 . 1 1 40 40 GLN HE22 H 1 7.043 0.099 . 2 . . . A 40 GLN HE22 . 19487 1 351 . 1 1 40 40 GLN C C 13 174.969 0.000 . 1 . . . A 40 GLN C . 19487 1 352 . 1 1 40 40 GLN CA C 13 56.216 0.047 . 1 . . . A 40 GLN CA . 19487 1 353 . 1 1 40 40 GLN CB C 13 29.661 0.033 . 1 . . . A 40 GLN CB . 19487 1 354 . 1 1 40 40 GLN CG C 13 33.952 0.048 . 1 . . . A 40 GLN CG . 19487 1 355 . 1 1 40 40 GLN N N 15 118.822 0.016 . 1 . . . A 40 GLN N . 19487 1 356 . 1 1 40 40 GLN NE2 N 15 113.412 0.016 . 1 . . . A 40 GLN NE2 . 19487 1 357 . 1 1 41 41 THR H H 1 8.192 0.004 . 1 . . . A 41 THR H . 19487 1 358 . 1 1 41 41 THR HB H 1 3.931 0.005 . 1 . . . A 41 THR HB . 19487 1 359 . 1 1 41 41 THR HG21 H 1 1.273 0.004 . 1 . . . A 41 THR MG . 19487 1 360 . 1 1 41 41 THR HG22 H 1 1.273 0.004 . 1 . . . A 41 THR MG . 19487 1 361 . 1 1 41 41 THR HG23 H 1 1.273 0.004 . 1 . . . A 41 THR MG . 19487 1 362 . 1 1 41 41 THR C C 13 174.918 0.000 . 1 . . . A 41 THR C . 19487 1 363 . 1 1 41 41 THR CA C 13 59.191 0.023 . 1 . . . A 41 THR CA . 19487 1 364 . 1 1 41 41 THR CB C 13 73.145 0.209 . 1 . . . A 41 THR CB . 19487 1 365 . 1 1 41 41 THR CG2 C 13 22.428 0.065 . 1 . . . A 41 THR CG2 . 19487 1 366 . 1 1 41 41 THR N N 15 110.403 0.016 . 1 . . . A 41 THR N . 19487 1 367 . 1 1 42 42 GLN H H 1 9.120 0.004 . 1 . . . A 42 GLN H . 19487 1 368 . 1 1 42 42 GLN HA H 1 4.785 0.015 . 1 . . . A 42 GLN HA . 19487 1 369 . 1 1 42 42 GLN HG2 H 1 2.347 0.015 . 2 . . . A 42 GLN HG2 . 19487 1 370 . 1 1 42 42 GLN HG3 H 1 2.166 0.003 . 2 . . . A 42 GLN HG3 . 19487 1 371 . 1 1 42 42 GLN HE21 H 1 7.533 0.001 . 2 . . . A 42 GLN HE21 . 19487 1 372 . 1 1 42 42 GLN HE22 H 1 6.380 0.002 . 2 . . . A 42 GLN HE22 . 19487 1 373 . 1 1 42 42 GLN C C 13 174.918 0.000 . 1 . . . A 42 GLN C . 19487 1 374 . 1 1 42 42 GLN CA C 13 55.285 0.061 . 1 . . . A 42 GLN CA . 19487 1 375 . 1 1 42 42 GLN CB C 13 32.073 0.090 . 1 . . . A 42 GLN CB . 19487 1 376 . 1 1 42 42 GLN N N 15 113.850 0.018 . 1 . . . A 42 GLN N . 19487 1 377 . 1 1 42 42 GLN NE2 N 15 112.561 0.028 . 1 . . . A 42 GLN NE2 . 19487 1 378 . 1 1 43 43 TRP H H 1 9.019 0.005 . 1 . . . A 43 TRP H . 19487 1 379 . 1 1 43 43 TRP HA H 1 5.119 0.007 . 1 . . . A 43 TRP HA . 19487 1 380 . 1 1 43 43 TRP HB2 H 1 3.613 0.004 . 2 . . . A 43 TRP HB2 . 19487 1 381 . 1 1 43 43 TRP HB3 H 1 3.226 0.003 . 2 . . . A 43 TRP HB3 . 19487 1 382 . 1 1 43 43 TRP HE1 H 1 9.891 0.000 . 1 . . . A 43 TRP HE1 . 19487 1 383 . 1 1 43 43 TRP C C 13 176.115 0.000 . 1 . . . A 43 TRP C . 19487 1 384 . 1 1 43 43 TRP CA C 13 59.184 0.045 . 1 . . . A 43 TRP CA . 19487 1 385 . 1 1 43 43 TRP CB C 13 31.495 0.051 . 1 . . . A 43 TRP CB . 19487 1 386 . 1 1 43 43 TRP N N 15 120.166 0.022 . 1 . . . A 43 TRP N . 19487 1 387 . 1 1 43 43 TRP NE1 N 15 129.099 0.000 . 1 . . . A 43 TRP NE1 . 19487 1 388 . 1 1 44 44 ASP H H 1 7.976 0.003 . 1 . . . A 44 ASP H . 19487 1 389 . 1 1 44 44 ASP HA H 1 5.113 0.006 . 1 . . . A 44 ASP HA . 19487 1 390 . 1 1 44 44 ASP HB2 H 1 2.660 0.007 . 2 . . . A 44 ASP HB2 . 19487 1 391 . 1 1 44 44 ASP HB3 H 1 2.324 0.004 . 2 . . . A 44 ASP HB3 . 19487 1 392 . 1 1 44 44 ASP CA C 13 51.787 0.021 . 1 . . . A 44 ASP CA . 19487 1 393 . 1 1 44 44 ASP CB C 13 40.54 0.100 . 1 . . . A 44 ASP CB . 19487 1 394 . 1 1 44 44 ASP N N 15 115.913 0.049 . 1 . . . A 44 ASP N . 19487 1 395 . 1 1 46 46 PRO HA H 1 3.808 0.002 . 1 . . . A 46 PRO HA . 19487 1 396 . 1 1 46 46 PRO C C 13 175.510 0.000 . 1 . . . A 46 PRO C . 19487 1 397 . 1 1 46 46 PRO CA C 13 61.219 0.053 . 1 . . . A 46 PRO CA . 19487 1 398 . 1 1 46 46 PRO CB C 13 30.572 0.044 . 1 . . . A 46 PRO CB . 19487 1 399 . 1 1 46 46 PRO CG C 13 26.413 0.042 . 1 . . . A 46 PRO CG . 19487 1 400 . 1 1 46 46 PRO CD C 13 49.607 0.022 . 1 . . . A 46 PRO CD . 19487 1 401 . 1 1 47 47 THR H H 1 7.690 0.005 . 1 . . . A 47 THR H . 19487 1 402 . 1 1 47 47 THR HA H 1 4.234 0.005 . 1 . . . A 47 THR HA . 19487 1 403 . 1 1 47 47 THR HB H 1 4.148 0.007 . 1 . . . A 47 THR HB . 19487 1 404 . 1 1 47 47 THR HG21 H 1 1.095 0.012 . 1 . . . A 47 THR MG . 19487 1 405 . 1 1 47 47 THR HG22 H 1 1.095 0.012 . 1 . . . A 47 THR MG . 19487 1 406 . 1 1 47 47 THR HG23 H 1 1.095 0.012 . 1 . . . A 47 THR MG . 19487 1 407 . 1 1 47 47 THR C C 13 174.205 0.000 . 1 . . . A 47 THR C . 19487 1 408 . 1 1 47 47 THR CA C 13 60.797 0.074 . 1 . . . A 47 THR CA . 19487 1 409 . 1 1 47 47 THR CB C 13 70.25 0.032 . 1 . . . A 47 THR CB . 19487 1 410 . 1 1 47 47 THR CG2 C 13 21.679 0.039 . 1 . . . A 47 THR CG2 . 19487 1 411 . 1 1 47 47 THR N N 15 112.072 0.013 . 1 . . . A 47 THR N . 19487 1 412 . 1 1 48 48 TRP H H 1 8.480 0.004 . 1 . . . A 48 TRP H . 19487 1 413 . 1 1 48 48 TRP HA H 1 4.404 0.009 . 1 . . . A 48 TRP HA . 19487 1 414 . 1 1 48 48 TRP HB2 H 1 3.282 0.008 . 2 . . . A 48 TRP HB2 . 19487 1 415 . 1 1 48 48 TRP HB3 H 1 3.048 0.003 . 2 . . . A 48 TRP HB3 . 19487 1 416 . 1 1 48 48 TRP HE1 H 1 10.088 0.000 . 1 . . . A 48 TRP HE1 . 19487 1 417 . 1 1 48 48 TRP C C 13 175.934 0.000 . 1 . . . A 48 TRP C . 19487 1 418 . 1 1 48 48 TRP CA C 13 57.797 0.070 . 1 . . . A 48 TRP CA . 19487 1 419 . 1 1 48 48 TRP CB C 13 29.345 0.068 . 1 . . . A 48 TRP CB . 19487 1 420 . 1 1 48 48 TRP N N 15 123.257 0.019 . 1 . . . A 48 TRP N . 19487 1 421 . 1 1 48 48 TRP NE1 N 15 129.362 0.000 . 1 . . . A 48 TRP NE1 . 19487 1 422 . 1 1 49 49 GLU H H 1 8.296 0.006 . 1 . . . A 49 GLU H . 19487 1 423 . 1 1 49 49 GLU HA H 1 4.273 0.006 . 1 . . . A 49 GLU HA . 19487 1 424 . 1 1 49 49 GLU HB2 H 1 1.971 0.002 . 2 . . . A 49 GLU HB2 . 19487 1 425 . 1 1 49 49 GLU HB3 H 1 1.871 0.021 . 2 . . . A 49 GLU HB3 . 19487 1 426 . 1 1 49 49 GLU HG2 H 1 2.174 0.007 . 1 . . . A 49 GLU HG2 . 19487 1 427 . 1 1 49 49 GLU HG3 H 1 2.174 0.007 . 1 . . . A 49 GLU HG3 . 19487 1 428 . 1 1 49 49 GLU C C 13 175.847 0.000 . 1 . . . A 49 GLU C . 19487 1 429 . 1 1 49 49 GLU CA C 13 56.213 0.031 . 1 . . . A 49 GLU CA . 19487 1 430 . 1 1 49 49 GLU CB C 13 30.752 0.105 . 1 . . . A 49 GLU CB . 19487 1 431 . 1 1 49 49 GLU CG C 13 36.203 0.036 . 1 . . . A 49 GLU CG . 19487 1 432 . 1 1 49 49 GLU N N 15 122.782 0.169 . 1 . . . A 49 GLU N . 19487 1 433 . 1 1 50 50 SER H H 1 8.344 0.013 . 1 . . . A 50 SER H . 19487 1 434 . 1 1 50 50 SER HA H 1 4.613 0.000 . 1 . . . A 50 SER HA . 19487 1 435 . 1 1 50 50 SER CA C 13 56.220 0.000 . 1 . . . A 50 SER CA . 19487 1 436 . 1 1 50 50 SER CB C 13 63.397 0.000 . 1 . . . A 50 SER CB . 19487 1 437 . 1 1 50 50 SER N N 15 118.313 0.021 . 1 . . . A 50 SER N . 19487 1 438 . 1 1 51 51 PRO HA H 1 4.400 0.006 . 1 . . . A 51 PRO HA . 19487 1 439 . 1 1 51 51 PRO HB2 H 1 2.250 0.004 . 1 . . . A 51 PRO HB2 . 19487 1 440 . 1 1 51 51 PRO HB3 H 1 2.250 0.004 . 1 . . . A 51 PRO HB3 . 19487 1 441 . 1 1 51 51 PRO HD2 H 1 3.761 0.012 . 1 . . . A 51 PRO HD2 . 19487 1 442 . 1 1 51 51 PRO HD3 H 1 3.761 0.012 . 1 . . . A 51 PRO HD3 . 19487 1 443 . 1 1 51 51 PRO C C 13 177.481 0.000 . 1 . . . A 51 PRO C . 19487 1 444 . 1 1 51 51 PRO CA C 13 63.571 0.029 . 1 . . . A 51 PRO CA . 19487 1 445 . 1 1 51 51 PRO CB C 13 32.162 0.071 . 1 . . . A 51 PRO CB . 19487 1 446 . 1 1 51 51 PRO CG C 13 27.438 0.000 . 1 . . . A 51 PRO CG . 19487 1 447 . 1 1 51 51 PRO CD C 13 50.821 0.011 . 1 . . . A 51 PRO CD . 19487 1 448 . 1 1 52 52 GLY H H 1 8.345 0.002 . 1 . . . A 52 GLY H . 19487 1 449 . 1 1 52 52 GLY HA2 H 1 3.943 0.003 . 1 . . . A 52 GLY HA2 . 19487 1 450 . 1 1 52 52 GLY HA3 H 1 3.943 0.003 . 1 . . . A 52 GLY HA3 . 19487 1 451 . 1 1 52 52 GLY C C 13 173.969 0.000 . 1 . . . A 52 GLY C . 19487 1 452 . 1 1 52 52 GLY CA C 13 45.147 0.067 . 1 . . . A 52 GLY CA . 19487 1 453 . 1 1 52 52 GLY N N 15 109.070 0.008 . 1 . . . A 52 GLY N . 19487 1 454 . 1 1 53 53 ASP H H 1 8.216 0.013 . 1 . . . A 53 ASP H . 19487 1 455 . 1 1 53 53 ASP HA H 1 4.589 0.007 . 1 . . . A 53 ASP HA . 19487 1 456 . 1 1 53 53 ASP HB2 H 1 2.684 0.000 . 2 . . . A 53 ASP HB2 . 19487 1 457 . 1 1 53 53 ASP HB3 H 1 2.639 0.013 . 2 . . . A 53 ASP HB3 . 19487 1 458 . 1 1 53 53 ASP C C 13 176.133 0.000 . 1 . . . A 53 ASP C . 19487 1 459 . 1 1 53 53 ASP CA C 13 54.417 0.036 . 1 . . . A 53 ASP CA . 19487 1 460 . 1 1 53 53 ASP CB C 13 41.256 0.076 . 1 . . . A 53 ASP CB . 19487 1 461 . 1 1 53 53 ASP N N 15 120.558 0.012 . 1 . . . A 53 ASP N . 19487 1 462 . 1 1 54 54 ASP H H 1 8.338 0.002 . 1 . . . A 54 ASP H . 19487 1 463 . 1 1 54 54 ASP HA H 1 4.552 0.003 . 1 . . . A 54 ASP HA . 19487 1 464 . 1 1 54 54 ASP HB2 H 1 1.645 0.001 . 2 . . . A 54 ASP HB2 . 19487 1 465 . 1 1 54 54 ASP C C 13 175.904 0.000 . 1 . . . A 54 ASP C . 19487 1 466 . 1 1 54 54 ASP CA C 13 54.311 0.003 . 1 . . . A 54 ASP CA . 19487 1 467 . 1 1 54 54 ASP CB C 13 41.107 0.052 . 1 . . . A 54 ASP CB . 19487 1 468 . 1 1 54 54 ASP N N 15 120.383 0.015 . 1 . . . A 54 ASP N . 19487 1 469 . 1 1 55 55 ALA H H 1 8.153 0.008 . 1 . . . A 55 ALA H . 19487 1 470 . 1 1 55 55 ALA HA H 1 4.383 0.008 . 1 . . . A 55 ALA HA . 19487 1 471 . 1 1 55 55 ALA HB1 H 1 1.384 0.003 . 1 . . . A 55 ALA MB . 19487 1 472 . 1 1 55 55 ALA HB2 H 1 1.384 0.003 . 1 . . . A 55 ALA MB . 19487 1 473 . 1 1 55 55 ALA HB3 H 1 1.384 0.003 . 1 . . . A 55 ALA MB . 19487 1 474 . 1 1 55 55 ALA C C 13 176.939 0.000 . 1 . . . A 55 ALA C . 19487 1 475 . 1 1 55 55 ALA CA C 13 52.436 0.118 . 1 . . . A 55 ALA CA . 19487 1 476 . 1 1 55 55 ALA CB C 13 19.413 0.022 . 1 . . . A 55 ALA CB . 19487 1 477 . 1 1 55 55 ALA N N 15 124.730 0.025 . 1 . . . A 55 ALA N . 19487 1 478 . 1 1 56 56 SER H H 1 7.908 0.002 . 1 . . . A 56 SER H . 19487 1 479 . 1 1 56 56 SER HA H 1 4.221 0.006 . 1 . . . A 56 SER HA . 19487 1 480 . 1 1 56 56 SER HB2 H 1 4.143 0.001 . 2 . . . A 56 SER HB2 . 19487 1 481 . 1 1 56 56 SER HB3 H 1 3.835 0.002 . 2 . . . A 56 SER HB3 . 19487 1 482 . 1 1 56 56 SER CA C 13 60.182 0.013 . 1 . . . A 56 SER CA . 19487 1 483 . 1 1 56 56 SER CB C 13 64.911 0.008 . 1 . . . A 56 SER CB . 19487 1 484 . 1 1 56 56 SER N N 15 121.157 0.020 . 1 . . . A 56 SER N . 19487 1 stop_ save_