data_7349 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7349 _Entry.Title ; NMR SOLUTION STRUCTURE OF A PROTEIN ASPARTIC ACID PHOSPHATE PHOSPHATASE FROM BACILLUS ANTHRACIS ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-12-01 _Entry.Accession_date 2006-12-05 _Entry.Last_release_date 2008-08-14 _Entry.Original_release_date 2008-08-14 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 R. Grenha R. . . 7349 2 N. Rzechorzek N. . . 7349 3 J. Brannigan J. A. . 7349 4 E. Ab E. . . 7349 5 G. Folkers G. E. . 7349 6 R. 'De Jong' R. N. . 7349 7 T. Diercks T. . . 7349 8 A. Wilkinson A. J. . 7349 9 R. Kaptein R. . . 7349 10 K. Wilson K. S. . 7349 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID ANTHRACIS ANTHRACIS 7349 ANTITHETICAL ANTITHETICAL 7349 BACILLUS BACILLUS 7349 NEGATIVE NEGATIVE 7349 PHOSPHATASE PHOSPHATASE 7349 PHOSPHORYLATION PHOSPHORYLATION 7349 REGULATOR REGULATOR 7349 SPINE SPINE 7349 SPORULATION SPORULATION 7349 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 7349 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 279 7349 '15N chemical shifts' 59 7349 '1H chemical shifts' 443 7349 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 . . 2008-08-14 2006-12-01 original author . 7349 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2C0S 'BMRB Entry Tracking System' 7349 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 7349 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17001075 _Citation.Full_citation . _Citation.Title 'Structural characterization of Spo0E-like protein-aspartic acid phosphatases that regulate sporulation in bacilli.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full 'The Journal of Biological Chemistry' _Citation.Journal_volume 281 _Citation.Journal_issue 49 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD 9999 _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 37993 _Citation.Page_last 38003 _Citation.Year 2006 _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 Rosa Grenha . . . 7349 1 2 Neil Rzechorzek . J. . 7349 1 3 James Brannigan . A. . 7349 1 4 Rob 'de Jong' . N. . 7349 1 5 Eiso AB . . . 7349 1 6 Tammo Diercks . . . 7349 1 7 Vincent Truffault . . . 7349 1 8 Joanne Ladds . C. . 7349 1 9 Mark Fogg . J. . 7349 1 10 Christina Bongiorni . . . 7349 1 11 Marta Perego . . . 7349 1 12 Robert Kaptein . . . 7349 1 13 Keith Wilson . S. . 7349 1 14 Gert Folkers . E. . 7349 1 15 Anthony Wilkinson . J. . 7349 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7349 _Assembly.ID 1 _Assembly.Name CONSERVED_DOMAIN_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 CONSERVED_DOMAIN_PROTEIN 1 $CONSERVED_DOMAIN_PROTEIN A . yes native no no . . . 7349 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CONSERVED_DOMAIN_PROTEIN _Entity.Sf_category entity _Entity.Sf_framecode CONSERVED_DOMAIN_PROTEIN _Entity.Entry_ID 7349 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CONSERVED_DOMAIN_PROTEIN _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 ; MNVTKLNDRIEAKKKELIYL VEKYGFTHHKVISFSQELDR LLNLLIELKTKKKRYSL ; _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 yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 57 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID 1 _Entity.Fragment 'SMALL ASPARTIC ACID PHOSPHATE PHOSPHATASE' _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 2015-01-28 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 2C0S . "Nmr Solution Structure Of A Protein Aspartic Acid Phosphate Phosphatase From Bacillus Anthracis" . . . . . 100.00 64 100.00 100.00 3.34e-30 . . . . 7349 1 2 no DBJ GAF00519 . "stage 0 sporulation regulatory protein [Bacillus anthracis CZC5]" . . . . . 100.00 57 100.00 100.00 2.92e-30 . . . . 7349 1 3 no GB AAP28843 . "stage 0 sporulation regulatory protein [Bacillus anthracis str. Ames]" . . . . . 100.00 57 100.00 100.00 2.92e-30 . . . . 7349 1 4 no GB AAT34304 . "conserved domain protein [Bacillus anthracis str. 'Ames Ancestor']" . . . . . 100.00 108 100.00 100.00 4.68e-30 . . . . 7349 1 5 no GB AAT57102 . "conserved domain protein [Bacillus anthracis str. Sterne]" . . . . . 100.00 108 100.00 100.00 4.68e-30 . . . . 7349 1 6 no GB AAT62951 . "conserved hypothetical protein, possible sporulation regulatory protein [Bacillus thuringiensis serovar konkukian str. 97-27]" . . . . . 100.00 108 100.00 100.00 4.68e-30 . . . . 7349 1 7 no GB AAU15604 . "conserved hypothetical protein; possible sporulation regulatory protein [Bacillus cereus E33L]" . . . . . 100.00 108 98.25 98.25 6.91e-29 . . . . 7349 1 8 no REF NP_847357 . "stage 0 sporulation regulatory protein [Bacillus anthracis str. Ames]" . . . . . 100.00 57 100.00 100.00 2.92e-30 . . . . 7349 1 9 no REF WP_001103330 . "hypothetical protein [Bacillus cereus]" . . . . . 100.00 57 98.25 98.25 3.61e-29 . . . . 7349 1 10 no REF WP_001103331 . "MULTISPECIES: stage II sporulation protein E [Bacillus cereus group]" . . . . . 100.00 57 100.00 100.00 2.92e-30 . . . . 7349 1 11 no REF WP_009879807 . "MULTISPECIES: stage 0 sporulation protein [Bacillus cereus group]" . . . . . 100.00 108 100.00 100.00 4.68e-30 . . . . 7349 1 12 no REF WP_011199052 . "stage 0 sporulation protein [Bacillus cereus]" . . . . . 100.00 108 98.25 98.25 6.91e-29 . . . . 7349 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 . MET . 7349 1 2 . ASN . 7349 1 3 . VAL . 7349 1 4 . THR . 7349 1 5 . LYS . 7349 1 6 . LEU . 7349 1 7 . ASN . 7349 1 8 . ASP . 7349 1 9 . ARG . 7349 1 10 . ILE . 7349 1 11 . GLU . 7349 1 12 . ALA . 7349 1 13 . LYS . 7349 1 14 . LYS . 7349 1 15 . LYS . 7349 1 16 . GLU . 7349 1 17 . LEU . 7349 1 18 . ILE . 7349 1 19 . TYR . 7349 1 20 . LEU . 7349 1 21 . VAL . 7349 1 22 . GLU . 7349 1 23 . LYS . 7349 1 24 . TYR . 7349 1 25 . GLY . 7349 1 26 . PHE . 7349 1 27 . THR . 7349 1 28 . HIS . 7349 1 29 . HIS . 7349 1 30 . LYS . 7349 1 31 . VAL . 7349 1 32 . ILE . 7349 1 33 . SER . 7349 1 34 . PHE . 7349 1 35 . SER . 7349 1 36 . GLN . 7349 1 37 . GLU . 7349 1 38 . LEU . 7349 1 39 . ASP . 7349 1 40 . ARG . 7349 1 41 . LEU . 7349 1 42 . LEU . 7349 1 43 . ASN . 7349 1 44 . LEU . 7349 1 45 . LEU . 7349 1 46 . ILE . 7349 1 47 . GLU . 7349 1 48 . LEU . 7349 1 49 . LYS . 7349 1 50 . THR . 7349 1 51 . LYS . 7349 1 52 . LYS . 7349 1 53 . LYS . 7349 1 54 . ARG . 7349 1 55 . TYR . 7349 1 56 . SER . 7349 1 57 . LEU . 7349 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 . MET 1 1 7349 1 . ASN 2 2 7349 1 . VAL 3 3 7349 1 . THR 4 4 7349 1 . LYS 5 5 7349 1 . LEU 6 6 7349 1 . ASN 7 7 7349 1 . ASP 8 8 7349 1 . ARG 9 9 7349 1 . ILE 10 10 7349 1 . GLU 11 11 7349 1 . ALA 12 12 7349 1 . LYS 13 13 7349 1 . LYS 14 14 7349 1 . LYS 15 15 7349 1 . GLU 16 16 7349 1 . LEU 17 17 7349 1 . ILE 18 18 7349 1 . TYR 19 19 7349 1 . LEU 20 20 7349 1 . VAL 21 21 7349 1 . GLU 22 22 7349 1 . LYS 23 23 7349 1 . TYR 24 24 7349 1 . GLY 25 25 7349 1 . PHE 26 26 7349 1 . THR 27 27 7349 1 . HIS 28 28 7349 1 . HIS 29 29 7349 1 . LYS 30 30 7349 1 . VAL 31 31 7349 1 . ILE 32 32 7349 1 . SER 33 33 7349 1 . PHE 34 34 7349 1 . SER 35 35 7349 1 . GLN 36 36 7349 1 . GLU 37 37 7349 1 . LEU 38 38 7349 1 . ASP 39 39 7349 1 . ARG 40 40 7349 1 . LEU 41 41 7349 1 . LEU 42 42 7349 1 . ASN 43 43 7349 1 . LEU 44 44 7349 1 . LEU 45 45 7349 1 . ILE 46 46 7349 1 . GLU 47 47 7349 1 . LEU 48 48 7349 1 . LYS 49 49 7349 1 . THR 50 50 7349 1 . LYS 51 51 7349 1 . LYS 52 52 7349 1 . LYS 53 53 7349 1 . ARG 54 54 7349 1 . TYR 55 55 7349 1 . SER 56 56 7349 1 . LEU 57 57 7349 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 7349 _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 $CONSERVED_DOMAIN_PROTEIN . 1392 organism . 'BACILLUS ANTHRACIS' 'BACILLUS ANTHRACIS' . . Bacteria . Bacillus anthracis AMES . . . . . . . . . . . . . . . . . . . . 7349 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 7349 _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 $CONSERVED_DOMAIN_PROTEIN . 'recombinant technology' 'ESCHERICHIA COLI' . . . ESCHERICHIA COLI BL21 . . . . . . . . . . . . . . . PET28A . . . . . . 7349 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Sample.Sf_category sample _Sample.Sf_framecode sample _Sample.Entry_ID 7349 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '90% WATER/10% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 CONSERVED_DOMAIN_PROTEIN 'natural abundance' . . 1 $CONSERVED_DOMAIN_PROTEIN . . . . . mM . . . . 7349 1 2 D2O . . . . . . . 10 . . % . . . . 7349 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 7349 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 7349 _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' 150 . mM 7349 1 pH 6.0 . pH 7349 1 pressure 1.0 . ATM 7349 1 temperature 278.0 . K 7349 1 stop_ save_ ############################ # Computer software used # ############################ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 7349 _Software.ID 1 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN' . . 7349 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 7349 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 7349 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 7349 2 stop_ save_ save_CYANA2.1 _Software.Sf_category software _Software.Sf_framecode CYANA2.1 _Software.Entry_ID 7349 _Software.ID 3 _Software.Name CYANA2.1 _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 7349 3 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 7349 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model OTHER _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_700 _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode 700 _NMR_spectrometer_list.Entry_ID 7349 _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 OTHER . 700 . . . 7349 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 7349 _Experiment_list.ID 1 _Experiment_list.Details 'THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR ON 15N- AND 13C- LABELED HIS-TAGGED SAMPLE' 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 HNCO no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 2 HNCACO no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 3 HNCACB no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 4 CBCACONH no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 5 HNCA no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 6 HBHACONH no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 7 HNCAHA no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 8 CCH-COSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 9 HCCH-TOCSY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 10 CCCONH no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 11 HNH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 12 HCH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 13 CNH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 1 14 HH-NOESY no . . . . . . . . . . 1 $sample isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7349 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 7349 _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 . . . . . . . . . . . . 1 . . . 1 $citations . . 1 $citations 7349 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 7349 _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 HNCO . . . 7349 1 2 HNCACO . . . 7349 1 3 HNCACB . . . 7349 1 4 CBCACONH . . . 7349 1 5 HNCA . . . 7349 1 6 HBHACONH . . . 7349 1 7 HNCAHA . . . 7349 1 8 CCH-COSY . . . 7349 1 9 HCCH-TOCSY . . . 7349 1 10 CCCONH . . . 7349 1 11 HNH-NOESY . . . 7349 1 12 HCH-NOESY . . . 7349 1 13 CNH-NOESY . . . 7349 1 14 HH-NOESY . . . 7349 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET HA H 1 3.782 0.025 . . . . . . 1 MET HA . 7349 1 2 . 1 1 1 1 MET HB2 H 1 1.801 0.025 . . . . . . 1 MET HB1 . 7349 1 3 . 1 1 1 1 MET HB3 H 1 1.870 0.025 . . . . . . 1 MET HB2 . 7349 1 4 . 1 1 1 1 MET HG2 H 1 2.206 0.025 . . . . . . 1 MET HG1 . 7349 1 5 . 1 1 1 1 MET HG3 H 1 2.302 0.015 . . . . . . 1 MET HG2 . 7349 1 6 . 1 1 1 1 MET C C 13 169.175 0.150 . . . . . . 1 MET C . 7349 1 7 . 1 1 1 1 MET CA C 13 52.123 0.200 . . . . . . 1 MET CA . 7349 1 8 . 1 1 1 1 MET CB C 13 30.516 0.047 . . . . . . 1 MET CB . 7349 1 9 . 1 1 1 1 MET CG C 13 27.995 0.200 . . . . . . 1 MET CG . 7349 1 10 . 1 1 2 2 ASN H H 1 8.424 0.025 . . . . . . 2 ASN HN . 7349 1 11 . 1 1 2 2 ASN HA H 1 4.505 0.025 . . . . . . 2 ASN HA . 7349 1 12 . 1 1 2 2 ASN HB2 H 1 2.514 0.025 . . . . . . 2 ASN HB1 . 7349 1 13 . 1 1 2 2 ASN HB3 H 1 2.451 0.025 . . . . . . 2 ASN HB2 . 7349 1 14 . 1 1 2 2 ASN C C 13 173.485 0.150 . . . . . . 2 ASN C . 7349 1 15 . 1 1 2 2 ASN CA C 13 50.654 0.235 . . . . . . 2 ASN CA . 7349 1 16 . 1 1 2 2 ASN CB C 13 39.326 0.259 . . . . . . 2 ASN CB . 7349 1 17 . 1 1 2 2 ASN N N 15 124.371 0.150 . . . . . . 2 ASN N . 7349 1 18 . 1 1 3 3 VAL H H 1 8.554 0.025 . . . . . . 3 VAL HN . 7349 1 19 . 1 1 3 3 VAL HA H 1 3.505 0.025 . . . . . . 3 VAL HA . 7349 1 20 . 1 1 3 3 VAL HB H 1 1.907 0.025 . . . . . . 3 VAL HB . 7349 1 21 . 1 1 3 3 VAL HG11 H 1 0.752 0.025 . . . . . . 3 VAL QG1 . 7349 1 22 . 1 1 3 3 VAL HG12 H 1 0.752 0.025 . . . . . . 3 VAL QG1 . 7349 1 23 . 1 1 3 3 VAL HG13 H 1 0.752 0.025 . . . . . . 3 VAL QG1 . 7349 1 24 . 1 1 3 3 VAL HG21 H 1 0.700 0.025 . . . . . . 3 VAL QG2 . 7349 1 25 . 1 1 3 3 VAL HG22 H 1 0.700 0.025 . . . . . . 3 VAL QG2 . 7349 1 26 . 1 1 3 3 VAL HG23 H 1 0.700 0.025 . . . . . . 3 VAL QG2 . 7349 1 27 . 1 1 3 3 VAL C C 13 173.737 0.150 . . . . . . 3 VAL C . 7349 1 28 . 1 1 3 3 VAL CA C 13 62.544 0.195 . . . . . . 3 VAL CA . 7349 1 29 . 1 1 3 3 VAL CB C 13 28.950 0.174 . . . . . . 3 VAL CB . 7349 1 30 . 1 1 3 3 VAL CG1 C 13 19.032 0.026 . . . . . . 3 VAL CG1 . 7349 1 31 . 1 1 3 3 VAL CG2 C 13 18.413 0.017 . . . . . . 3 VAL CG2 . 7349 1 32 . 1 1 3 3 VAL N N 15 123.313 0.150 . . . . . . 3 VAL N . 7349 1 33 . 1 1 4 4 THR H H 1 7.894 0.025 . . . . . . 4 THR HN . 7349 1 34 . 1 1 4 4 THR HA H 1 3.750 0.025 . . . . . . 4 THR HA . 7349 1 35 . 1 1 4 4 THR HB H 1 3.995 0.025 . . . . . . 4 THR HB . 7349 1 36 . 1 1 4 4 THR HG21 H 1 1.000 0.025 . . . . . . 4 THR QG2 . 7349 1 37 . 1 1 4 4 THR HG22 H 1 1.000 0.025 . . . . . . 4 THR QG2 . 7349 1 38 . 1 1 4 4 THR HG23 H 1 1.000 0.025 . . . . . . 4 THR QG2 . 7349 1 39 . 1 1 4 4 THR C C 13 173.434 0.150 . . . . . . 4 THR C . 7349 1 40 . 1 1 4 4 THR CA C 13 63.139 0.113 . . . . . . 4 THR CA . 7349 1 41 . 1 1 4 4 THR CB C 13 65.438 0.063 . . . . . . 4 THR CB . 7349 1 42 . 1 1 4 4 THR CG2 C 13 19.016 0.133 . . . . . . 4 THR CG2 . 7349 1 43 . 1 1 4 4 THR N N 15 117.182 0.150 . . . . . . 4 THR N . 7349 1 44 . 1 1 5 5 LYS H H 1 7.754 0.025 . . . . . . 5 LYS HN . 7349 1 45 . 1 1 5 5 LYS HA H 1 3.928 0.025 . . . . . . 5 LYS HA . 7349 1 46 . 1 1 5 5 LYS HB2 H 1 1.635 0.025 . . . . . . 5 LYS HB1 . 7349 1 47 . 1 1 5 5 LYS HB3 H 1 1.635 0.025 . . . . . . 5 LYS HB2 . 7349 1 48 . 1 1 5 5 LYS HG2 H 1 1.192 0.025 . . . . . . 5 LYS HG1 . 7349 1 49 . 1 1 5 5 LYS HG3 H 1 1.305 0.025 . . . . . . 5 LYS HG2 . 7349 1 50 . 1 1 5 5 LYS C C 13 176.501 0.150 . . . . . . 5 LYS C . 7349 1 51 . 1 1 5 5 LYS CA C 13 55.817 0.296 . . . . . . 5 LYS CA . 7349 1 52 . 1 1 5 5 LYS CB C 13 29.117 0.200 . . . . . . 5 LYS CB . 7349 1 53 . 1 1 5 5 LYS CG C 13 22.479 0.130 . . . . . . 5 LYS CG . 7349 1 54 . 1 1 5 5 LYS N N 15 121.411 0.154 . . . . . . 5 LYS N . 7349 1 55 . 1 1 6 6 LEU H H 1 7.813 0.025 . . . . . . 6 LEU HN . 7349 1 56 . 1 1 6 6 LEU HA H 1 3.927 0.025 . . . . . . 6 LEU HA . 7349 1 57 . 1 1 6 6 LEU HB2 H 1 1.317 0.025 . . . . . . 6 LEU HB1 . 7349 1 58 . 1 1 6 6 LEU HB3 H 1 1.578 0.025 . . . . . . 6 LEU HB2 . 7349 1 59 . 1 1 6 6 LEU HD11 H 1 0.652 0.025 . . . . . . 6 LEU QD1 . 7349 1 60 . 1 1 6 6 LEU HD12 H 1 0.652 0.025 . . . . . . 6 LEU QD1 . 7349 1 61 . 1 1 6 6 LEU HD13 H 1 0.652 0.025 . . . . . . 6 LEU QD1 . 7349 1 62 . 1 1 6 6 LEU HD21 H 1 0.702 0.124 . . . . . . 6 LEU QD2 . 7349 1 63 . 1 1 6 6 LEU HD22 H 1 0.702 0.124 . . . . . . 6 LEU QD2 . 7349 1 64 . 1 1 6 6 LEU HD23 H 1 0.702 0.124 . . . . . . 6 LEU QD2 . 7349 1 65 . 1 1 6 6 LEU HG H 1 1.400 0.079 . . . . . . 6 LEU HG . 7349 1 66 . 1 1 6 6 LEU C C 13 175.330 0.150 . . . . . . 6 LEU C . 7349 1 67 . 1 1 6 6 LEU CA C 13 55.191 0.200 . . . . . . 6 LEU CA . 7349 1 68 . 1 1 6 6 LEU CB C 13 38.430 0.231 . . . . . . 6 LEU CB . 7349 1 69 . 1 1 6 6 LEU CD1 C 13 23.584 0.067 . . . . . . 6 LEU CD1 . 7349 1 70 . 1 1 6 6 LEU CD2 C 13 23.564 0.150 . . . . . . 6 LEU CD2 . 7349 1 71 . 1 1 6 6 LEU CG C 13 24.600 0.285 . . . . . . 6 LEU CG . 7349 1 72 . 1 1 6 6 LEU N N 15 121.368 0.150 . . . . . . 6 LEU N . 7349 1 73 . 1 1 7 7 ASN H H 1 8.397 0.025 . . . . . . 7 ASN HN . 7349 1 74 . 1 1 7 7 ASN HA H 1 4.101 0.025 . . . . . . 7 ASN HA . 7349 1 75 . 1 1 7 7 ASN HB2 H 1 2.670 0.025 . . . . . . 7 ASN HB1 . 7349 1 76 . 1 1 7 7 ASN HB3 H 1 2.545 0.025 . . . . . . 7 ASN HB2 . 7349 1 77 . 1 1 7 7 ASN HD21 H 1 6.697 0.025 . . . . . . 7 ASN HD21 . 7349 1 78 . 1 1 7 7 ASN HD22 H 1 7.495 0.025 . . . . . . 7 ASN HD22 . 7349 1 79 . 1 1 7 7 ASN C C 13 174.649 0.150 . . . . . . 7 ASN C . 7349 1 80 . 1 1 7 7 ASN CA C 13 54.544 0.127 . . . . . . 7 ASN CA . 7349 1 81 . 1 1 7 7 ASN CB C 13 36.130 0.118 . . . . . . 7 ASN CB . 7349 1 82 . 1 1 7 7 ASN N N 15 117.789 0.150 . . . . . . 7 ASN N . 7349 1 83 . 1 1 7 7 ASN ND2 N 15 113.727 0.150 . . . . . . 7 ASN ND2 . 7349 1 84 . 1 1 8 8 ASP H H 1 7.977 0.025 . . . . . . 8 ASP HN . 7349 1 85 . 1 1 8 8 ASP HA H 1 4.129 0.025 . . . . . . 8 ASP HA . 7349 1 86 . 1 1 8 8 ASP HB2 H 1 2.617 0.025 . . . . . . 8 ASP HB1 . 7349 1 87 . 1 1 8 8 ASP HB3 H 1 2.433 0.025 . . . . . . 8 ASP HB2 . 7349 1 88 . 1 1 8 8 ASP C C 13 176.423 0.150 . . . . . . 8 ASP C . 7349 1 89 . 1 1 8 8 ASP CA C 13 54.640 0.200 . . . . . . 8 ASP CA . 7349 1 90 . 1 1 8 8 ASP CB C 13 37.181 0.134 . . . . . . 8 ASP CB . 7349 1 91 . 1 1 8 8 ASP N N 15 119.190 0.150 . . . . . . 8 ASP N . 7349 1 92 . 1 1 9 9 ARG H H 1 7.916 0.025 . . . . . . 9 ARG HN . 7349 1 93 . 1 1 9 9 ARG HA H 1 3.902 0.025 . . . . . . 9 ARG HA . 7349 1 94 . 1 1 9 9 ARG HB2 H 1 1.827 0.025 . . . . . . 9 ARG HB1 . 7349 1 95 . 1 1 9 9 ARG HB3 H 1 1.729 0.025 . . . . . . 9 ARG HB2 . 7349 1 96 . 1 1 9 9 ARG HD2 H 1 2.928 0.025 . . . . . . 9 ARG HD1 . 7349 1 97 . 1 1 9 9 ARG HD3 H 1 2.928 0.025 . . . . . . 9 ARG HD2 . 7349 1 98 . 1 1 9 9 ARG HG2 H 1 1.353 0.025 . . . . . . 9 ARG HG1 . 7349 1 99 . 1 1 9 9 ARG HG3 H 1 1.628 0.025 . . . . . . 9 ARG HG2 . 7349 1 100 . 1 1 9 9 ARG C C 13 176.448 0.150 . . . . . . 9 ARG C . 7349 1 101 . 1 1 9 9 ARG CA C 13 56.349 0.151 . . . . . . 9 ARG CA . 7349 1 102 . 1 1 9 9 ARG CB C 13 27.554 0.147 . . . . . . 9 ARG CB . 7349 1 103 . 1 1 9 9 ARG CD C 13 40.947 0.200 . . . . . . 9 ARG CD . 7349 1 104 . 1 1 9 9 ARG CG C 13 24.333 0.143 . . . . . . 9 ARG CG . 7349 1 105 . 1 1 9 9 ARG N N 15 121.959 0.150 . . . . . . 9 ARG N . 7349 1 106 . 1 1 10 10 ILE H H 1 8.396 0.025 . . . . . . 10 ILE HN . 7349 1 107 . 1 1 10 10 ILE HA H 1 3.173 0.025 . . . . . . 10 ILE HA . 7349 1 108 . 1 1 10 10 ILE HB H 1 1.845 0.025 . . . . . . 10 ILE HB . 7349 1 109 . 1 1 10 10 ILE HD11 H 1 0.607 0.025 . . . . . . 10 ILE QD1 . 7349 1 110 . 1 1 10 10 ILE HD12 H 1 0.607 0.025 . . . . . . 10 ILE QD1 . 7349 1 111 . 1 1 10 10 ILE HD13 H 1 0.607 0.025 . . . . . . 10 ILE QD1 . 7349 1 112 . 1 1 10 10 ILE HG12 H 1 1.541 0.025 . . . . . . 10 ILE HG11 . 7349 1 113 . 1 1 10 10 ILE HG13 H 1 0.538 0.025 . . . . . . 10 ILE HG12 . 7349 1 114 . 1 1 10 10 ILE HG21 H 1 0.651 0.025 . . . . . . 10 ILE QG2 . 7349 1 115 . 1 1 10 10 ILE HG22 H 1 0.651 0.025 . . . . . . 10 ILE QG2 . 7349 1 116 . 1 1 10 10 ILE HG23 H 1 0.651 0.025 . . . . . . 10 ILE QG2 . 7349 1 117 . 1 1 10 10 ILE C C 13 174.653 0.150 . . . . . . 10 ILE C . 7349 1 118 . 1 1 10 10 ILE CA C 13 63.357 0.042 . . . . . . 10 ILE CA . 7349 1 119 . 1 1 10 10 ILE CB C 13 35.276 0.274 . . . . . . 10 ILE CB . 7349 1 120 . 1 1 10 10 ILE CD1 C 13 12.779 0.113 . . . . . . 10 ILE CD1 . 7349 1 121 . 1 1 10 10 ILE CG1 C 13 29.161 0.080 . . . . . . 10 ILE CG1 . 7349 1 122 . 1 1 10 10 ILE CG2 C 13 14.918 0.061 . . . . . . 10 ILE CG2 . 7349 1 123 . 1 1 10 10 ILE N N 15 121.454 0.150 . . . . . . 10 ILE N . 7349 1 124 . 1 1 11 11 GLU H H 1 8.242 0.025 . . . . . . 11 GLU HN . 7349 1 125 . 1 1 11 11 GLU HA H 1 3.720 0.025 . . . . . . 11 GLU HA . 7349 1 126 . 1 1 11 11 GLU HB2 H 1 1.877 0.025 . . . . . . 11 GLU HB1 . 7349 1 127 . 1 1 11 11 GLU HB3 H 1 1.877 0.025 . . . . . . 11 GLU HB2 . 7349 1 128 . 1 1 11 11 GLU HG2 H 1 2.160 0.025 . . . . . . 11 GLU HG1 . 7349 1 129 . 1 1 11 11 GLU HG3 H 1 2.160 0.025 . . . . . . 11 GLU HG2 . 7349 1 130 . 1 1 11 11 GLU C C 13 176.884 0.150 . . . . . . 11 GLU C . 7349 1 131 . 1 1 11 11 GLU CA C 13 56.588 0.056 . . . . . . 11 GLU CA . 7349 1 132 . 1 1 11 11 GLU CB C 13 26.163 0.051 . . . . . . 11 GLU CB . 7349 1 133 . 1 1 11 11 GLU CG C 13 33.234 0.200 . . . . . . 11 GLU CG . 7349 1 134 . 1 1 11 11 GLU N N 15 118.744 0.150 . . . . . . 11 GLU N . 7349 1 135 . 1 1 12 12 ALA H H 1 7.666 0.025 . . . . . . 12 ALA HN . 7349 1 136 . 1 1 12 12 ALA HA H 1 3.995 0.025 . . . . . . 12 ALA HA . 7349 1 137 . 1 1 12 12 ALA HB1 H 1 1.323 0.025 . . . . . . 12 ALA QB . 7349 1 138 . 1 1 12 12 ALA HB2 H 1 1.323 0.025 . . . . . . 12 ALA QB . 7349 1 139 . 1 1 12 12 ALA HB3 H 1 1.323 0.025 . . . . . . 12 ALA QB . 7349 1 140 . 1 1 12 12 ALA C C 13 178.257 0.150 . . . . . . 12 ALA C . 7349 1 141 . 1 1 12 12 ALA CA C 13 52.367 0.127 . . . . . . 12 ALA CA . 7349 1 142 . 1 1 12 12 ALA CB C 13 15.113 0.044 . . . . . . 12 ALA CB . 7349 1 143 . 1 1 12 12 ALA N N 15 121.263 0.150 . . . . . . 12 ALA N . 7349 1 144 . 1 1 13 13 LYS H H 1 8.212 0.025 . . . . . . 13 LYS HN . 7349 1 145 . 1 1 13 13 LYS HA H 1 4.196 0.025 . . . . . . 13 LYS HA . 7349 1 146 . 1 1 13 13 LYS HB2 H 1 1.740 0.025 . . . . . . 13 LYS HB1 . 7349 1 147 . 1 1 13 13 LYS HB3 H 1 1.843 0.025 . . . . . . 13 LYS HB2 . 7349 1 148 . 1 1 13 13 LYS HG2 H 1 1.230 0.016 . . . . . . 13 LYS HG1 . 7349 1 149 . 1 1 13 13 LYS HG3 H 1 1.362 0.015 . . . . . . 13 LYS HG2 . 7349 1 150 . 1 1 13 13 LYS C C 13 176.178 0.150 . . . . . . 13 LYS C . 7349 1 151 . 1 1 13 13 LYS CA C 13 56.173 0.075 . . . . . . 13 LYS CA . 7349 1 152 . 1 1 13 13 LYS CB C 13 30.289 0.101 . . . . . . 13 LYS CB . 7349 1 153 . 1 1 13 13 LYS CG C 13 22.927 0.150 . . . . . . 13 LYS CG . 7349 1 154 . 1 1 13 13 LYS N N 15 121.108 0.153 . . . . . . 13 LYS N . 7349 1 155 . 1 1 14 14 LYS H H 1 8.686 0.025 . . . . . . 14 LYS HN . 7349 1 156 . 1 1 14 14 LYS HA H 1 3.697 0.025 . . . . . . 14 LYS HA . 7349 1 157 . 1 1 14 14 LYS HB2 H 1 1.749 0.025 . . . . . . 14 LYS HB1 . 7349 1 158 . 1 1 14 14 LYS HB3 H 1 1.649 0.025 . . . . . . 14 LYS HB2 . 7349 1 159 . 1 1 14 14 LYS HD2 H 1 1.413 0.032 . . . . . . 14 LYS HD1 . 7349 1 160 . 1 1 14 14 LYS HD3 H 1 1.413 0.032 . . . . . . 14 LYS HD2 . 7349 1 161 . 1 1 14 14 LYS HE2 H 1 2.725 0.025 . . . . . . 14 LYS HE1 . 7349 1 162 . 1 1 14 14 LYS HE3 H 1 2.528 0.025 . . . . . . 14 LYS HE2 . 7349 1 163 . 1 1 14 14 LYS HG2 H 1 1.582 0.015 . . . . . . 14 LYS HG1 . 7349 1 164 . 1 1 14 14 LYS HG3 H 1 1.261 0.015 . . . . . . 14 LYS HG2 . 7349 1 165 . 1 1 14 14 LYS C C 13 176.707 0.150 . . . . . . 14 LYS C . 7349 1 166 . 1 1 14 14 LYS CA C 13 57.897 0.053 . . . . . . 14 LYS CA . 7349 1 167 . 1 1 14 14 LYS CB C 13 30.268 0.038 . . . . . . 14 LYS CB . 7349 1 168 . 1 1 14 14 LYS CD C 13 27.452 0.150 . . . . . . 14 LYS CD . 7349 1 169 . 1 1 14 14 LYS CE C 13 38.890 0.256 . . . . . . 14 LYS CE . 7349 1 170 . 1 1 14 14 LYS CG C 13 24.134 0.201 . . . . . . 14 LYS CG . 7349 1 171 . 1 1 14 14 LYS N N 15 119.567 0.150 . . . . . . 14 LYS N . 7349 1 172 . 1 1 15 15 LYS H H 1 7.128 0.025 . . . . . . 15 LYS HN . 7349 1 173 . 1 1 15 15 LYS HA H 1 3.812 0.025 . . . . . . 15 LYS HA . 7349 1 174 . 1 1 15 15 LYS HB2 H 1 1.705 0.025 . . . . . . 15 LYS HB1 . 7349 1 175 . 1 1 15 15 LYS HB3 H 1 1.705 0.025 . . . . . . 15 LYS HB2 . 7349 1 176 . 1 1 15 15 LYS HD2 H 1 1.437 0.015 . . . . . . 15 LYS HD1 . 7349 1 177 . 1 1 15 15 LYS HD3 H 1 1.465 0.015 . . . . . . 15 LYS HD2 . 7349 1 178 . 1 1 15 15 LYS HE2 H 1 2.735 0.015 . . . . . . 15 LYS HE1 . 7349 1 179 . 1 1 15 15 LYS HE3 H 1 2.755 0.025 . . . . . . 15 LYS HE2 . 7349 1 180 . 1 1 15 15 LYS HG2 H 1 1.417 0.025 . . . . . . 15 LYS HG1 . 7349 1 181 . 1 1 15 15 LYS HG3 H 1 1.208 0.019 . . . . . . 15 LYS HG2 . 7349 1 182 . 1 1 15 15 LYS C C 13 176.212 0.150 . . . . . . 15 LYS C . 7349 1 183 . 1 1 15 15 LYS CA C 13 56.572 0.281 . . . . . . 15 LYS CA . 7349 1 184 . 1 1 15 15 LYS CB C 13 29.605 0.252 . . . . . . 15 LYS CB . 7349 1 185 . 1 1 15 15 LYS CD C 13 26.507 0.150 . . . . . . 15 LYS CD . 7349 1 186 . 1 1 15 15 LYS CE C 13 39.214 0.200 . . . . . . 15 LYS CE . 7349 1 187 . 1 1 15 15 LYS CG C 13 22.597 0.270 . . . . . . 15 LYS CG . 7349 1 188 . 1 1 15 15 LYS N N 15 117.784 0.150 . . . . . . 15 LYS N . 7349 1 189 . 1 1 16 16 GLU H H 1 7.677 0.025 . . . . . . 16 GLU HN . 7349 1 190 . 1 1 16 16 GLU HA H 1 3.862 0.025 . . . . . . 16 GLU HA . 7349 1 191 . 1 1 16 16 GLU HB2 H 1 2.006 0.025 . . . . . . 16 GLU HB1 . 7349 1 192 . 1 1 16 16 GLU HB3 H 1 1.915 0.025 . . . . . . 16 GLU HB2 . 7349 1 193 . 1 1 16 16 GLU HG2 H 1 2.064 0.025 . . . . . . 16 GLU HG1 . 7349 1 194 . 1 1 16 16 GLU HG3 H 1 1.772 0.025 . . . . . . 16 GLU HG2 . 7349 1 195 . 1 1 16 16 GLU C C 13 175.508 0.150 . . . . . . 16 GLU C . 7349 1 196 . 1 1 16 16 GLU CA C 13 56.130 0.079 . . . . . . 16 GLU CA . 7349 1 197 . 1 1 16 16 GLU CB C 13 26.902 0.135 . . . . . . 16 GLU CB . 7349 1 198 . 1 1 16 16 GLU CG C 13 33.126 0.001 . . . . . . 16 GLU CG . 7349 1 199 . 1 1 16 16 GLU N N 15 121.227 0.150 . . . . . . 16 GLU N . 7349 1 200 . 1 1 17 17 LEU H H 1 8.325 0.025 . . . . . . 17 LEU HN . 7349 1 201 . 1 1 17 17 LEU HA H 1 3.600 0.025 . . . . . . 17 LEU HA . 7349 1 202 . 1 1 17 17 LEU HB2 H 1 1.940 0.025 . . . . . . 17 LEU HB1 . 7349 1 203 . 1 1 17 17 LEU HB3 H 1 1.477 0.025 . . . . . . 17 LEU HB2 . 7349 1 204 . 1 1 17 17 LEU HD11 H 1 0.846 0.025 . . . . . . 17 LEU QD1 . 7349 1 205 . 1 1 17 17 LEU HD12 H 1 0.846 0.025 . . . . . . 17 LEU QD1 . 7349 1 206 . 1 1 17 17 LEU HD13 H 1 0.846 0.025 . . . . . . 17 LEU QD1 . 7349 1 207 . 1 1 17 17 LEU HD21 H 1 0.803 0.025 . . . . . . 17 LEU QD2 . 7349 1 208 . 1 1 17 17 LEU HD22 H 1 0.803 0.025 . . . . . . 17 LEU QD2 . 7349 1 209 . 1 1 17 17 LEU HD23 H 1 0.803 0.025 . . . . . . 17 LEU QD2 . 7349 1 210 . 1 1 17 17 LEU HG H 1 1.477 0.031 . . . . . . 17 LEU HG . 7349 1 211 . 1 1 17 17 LEU C C 13 174.465 0.150 . . . . . . 17 LEU C . 7349 1 212 . 1 1 17 17 LEU CA C 13 55.131 0.021 . . . . . . 17 LEU CA . 7349 1 213 . 1 1 17 17 LEU CB C 13 38.439 0.118 . . . . . . 17 LEU CB . 7349 1 214 . 1 1 17 17 LEU CD1 C 13 21.383 0.060 . . . . . . 17 LEU CD1 . 7349 1 215 . 1 1 17 17 LEU CD2 C 13 24.008 0.102 . . . . . . 17 LEU CD2 . 7349 1 216 . 1 1 17 17 LEU CG C 13 24.357 0.140 . . . . . . 17 LEU CG . 7349 1 217 . 1 1 17 17 LEU N N 15 120.053 0.150 . . . . . . 17 LEU N . 7349 1 218 . 1 1 18 18 ILE H H 1 7.070 0.025 . . . . . . 18 ILE HN . 7349 1 219 . 1 1 18 18 ILE HA H 1 3.310 0.025 . . . . . . 18 ILE HA . 7349 1 220 . 1 1 18 18 ILE HB H 1 1.661 0.025 . . . . . . 18 ILE HB . 7349 1 221 . 1 1 18 18 ILE HD11 H 1 0.644 0.025 . . . . . . 18 ILE QD1 . 7349 1 222 . 1 1 18 18 ILE HD12 H 1 0.644 0.025 . . . . . . 18 ILE QD1 . 7349 1 223 . 1 1 18 18 ILE HD13 H 1 0.644 0.025 . . . . . . 18 ILE QD1 . 7349 1 224 . 1 1 18 18 ILE HG12 H 1 1.533 0.025 . . . . . . 18 ILE HG11 . 7349 1 225 . 1 1 18 18 ILE HG13 H 1 0.933 0.025 . . . . . . 18 ILE HG12 . 7349 1 226 . 1 1 18 18 ILE HG21 H 1 0.607 0.025 . . . . . . 18 ILE QG2 . 7349 1 227 . 1 1 18 18 ILE HG22 H 1 0.607 0.025 . . . . . . 18 ILE QG2 . 7349 1 228 . 1 1 18 18 ILE HG23 H 1 0.607 0.025 . . . . . . 18 ILE QG2 . 7349 1 229 . 1 1 18 18 ILE C C 13 175.680 0.150 . . . . . . 18 ILE C . 7349 1 230 . 1 1 18 18 ILE CA C 13 62.223 0.100 . . . . . . 18 ILE CA . 7349 1 231 . 1 1 18 18 ILE CB C 13 35.068 0.117 . . . . . . 18 ILE CB . 7349 1 232 . 1 1 18 18 ILE CD1 C 13 10.223 0.033 . . . . . . 18 ILE CD1 . 7349 1 233 . 1 1 18 18 ILE CG1 C 13 26.143 0.146 . . . . . . 18 ILE CG1 . 7349 1 234 . 1 1 18 18 ILE CG2 C 13 14.080 0.029 . . . . . . 18 ILE CG2 . 7349 1 235 . 1 1 18 18 ILE N N 15 117.477 0.150 . . . . . . 18 ILE N . 7349 1 236 . 1 1 19 19 TYR H H 1 6.857 0.025 . . . . . . 19 TYR HN . 7349 1 237 . 1 1 19 19 TYR HA H 1 4.008 0.025 . . . . . . 19 TYR HA . 7349 1 238 . 1 1 19 19 TYR HB2 H 1 2.822 0.033 . . . . . . 19 TYR HB1 . 7349 1 239 . 1 1 19 19 TYR HB3 H 1 2.950 0.025 . . . . . . 19 TYR HB2 . 7349 1 240 . 1 1 19 19 TYR HD1 H 1 6.828 0.024 . . . . . . 19 TYR QD . 7349 1 241 . 1 1 19 19 TYR HD2 H 1 6.828 0.024 . . . . . . 19 TYR QD . 7349 1 242 . 1 1 19 19 TYR HE1 H 1 6.481 0.015 . . . . . . 19 TYR QE . 7349 1 243 . 1 1 19 19 TYR HE2 H 1 6.481 0.015 . . . . . . 19 TYR QE . 7349 1 244 . 1 1 19 19 TYR C C 13 174.933 0.150 . . . . . . 19 TYR C . 7349 1 245 . 1 1 19 19 TYR CA C 13 57.710 0.138 . . . . . . 19 TYR CA . 7349 1 246 . 1 1 19 19 TYR CB C 13 34.657 0.079 . . . . . . 19 TYR CB . 7349 1 247 . 1 1 19 19 TYR CD1 C 13 130.482 0.150 . . . . . . 19 TYR CD1 . 7349 1 248 . 1 1 19 19 TYR CD2 C 13 130.482 0.150 . . . . . . 19 TYR CD2 . 7349 1 249 . 1 1 19 19 TYR CE1 C 13 115.113 0.150 . . . . . . 19 TYR CE1 . 7349 1 250 . 1 1 19 19 TYR CE2 C 13 115.113 0.150 . . . . . . 19 TYR CE2 . 7349 1 251 . 1 1 19 19 TYR N N 15 119.162 0.150 . . . . . . 19 TYR N . 7349 1 252 . 1 1 20 20 LEU H H 1 8.080 0.025 . . . . . . 20 LEU HN . 7349 1 253 . 1 1 20 20 LEU HA H 1 3.576 0.025 . . . . . . 20 LEU HA . 7349 1 254 . 1 1 20 20 LEU HB2 H 1 0.988 0.016 . . . . . . 20 LEU HB1 . 7349 1 255 . 1 1 20 20 LEU HB3 H 1 1.659 0.025 . . . . . . 20 LEU HB2 . 7349 1 256 . 1 1 20 20 LEU HD11 H 1 -0.084 0.025 . . . . . . 20 LEU QD1 . 7349 1 257 . 1 1 20 20 LEU HD12 H 1 -0.084 0.025 . . . . . . 20 LEU QD1 . 7349 1 258 . 1 1 20 20 LEU HD13 H 1 -0.084 0.025 . . . . . . 20 LEU QD1 . 7349 1 259 . 1 1 20 20 LEU HD21 H 1 0.552 0.025 . . . . . . 20 LEU QD2 . 7349 1 260 . 1 1 20 20 LEU HD22 H 1 0.552 0.025 . . . . . . 20 LEU QD2 . 7349 1 261 . 1 1 20 20 LEU HD23 H 1 0.552 0.025 . . . . . . 20 LEU QD2 . 7349 1 262 . 1 1 20 20 LEU HG H 1 1.486 0.025 . . . . . . 20 LEU HG . 7349 1 263 . 1 1 20 20 LEU C C 13 176.036 0.150 . . . . . . 20 LEU C . 7349 1 264 . 1 1 20 20 LEU CA C 13 54.904 0.028 . . . . . . 20 LEU CA . 7349 1 265 . 1 1 20 20 LEU CB C 13 39.960 0.321 . . . . . . 20 LEU CB . 7349 1 266 . 1 1 20 20 LEU CD1 C 13 22.600 0.080 . . . . . . 20 LEU CD1 . 7349 1 267 . 1 1 20 20 LEU CD2 C 13 20.466 0.162 . . . . . . 20 LEU CD2 . 7349 1 268 . 1 1 20 20 LEU CG C 13 23.550 0.226 . . . . . . 20 LEU CG . 7349 1 269 . 1 1 20 20 LEU N N 15 120.426 0.150 . . . . . . 20 LEU N . 7349 1 270 . 1 1 21 21 VAL H H 1 8.561 0.025 . . . . . . 21 VAL HN . 7349 1 271 . 1 1 21 21 VAL HA H 1 3.013 0.025 . . . . . . 21 VAL HA . 7349 1 272 . 1 1 21 21 VAL HB H 1 1.728 0.025 . . . . . . 21 VAL HB . 7349 1 273 . 1 1 21 21 VAL HG11 H 1 0.312 0.025 . . . . . . 21 VAL QG1 . 7349 1 274 . 1 1 21 21 VAL HG12 H 1 0.312 0.025 . . . . . . 21 VAL QG1 . 7349 1 275 . 1 1 21 21 VAL HG13 H 1 0.312 0.025 . . . . . . 21 VAL QG1 . 7349 1 276 . 1 1 21 21 VAL HG21 H 1 0.677 0.025 . . . . . . 21 VAL QG2 . 7349 1 277 . 1 1 21 21 VAL HG22 H 1 0.677 0.025 . . . . . . 21 VAL QG2 . 7349 1 278 . 1 1 21 21 VAL HG23 H 1 0.677 0.025 . . . . . . 21 VAL QG2 . 7349 1 279 . 1 1 21 21 VAL C C 13 148.258 0.150 . . . . . . 21 VAL C . 7349 1 280 . 1 1 21 21 VAL CA C 13 63.819 0.185 . . . . . . 21 VAL CA . 7349 1 281 . 1 1 21 21 VAL CB C 13 28.645 0.095 . . . . . . 21 VAL CB . 7349 1 282 . 1 1 21 21 VAL CG1 C 13 18.560 0.080 . . . . . . 21 VAL CG1 . 7349 1 283 . 1 1 21 21 VAL CG2 C 13 20.980 0.125 . . . . . . 21 VAL CG2 . 7349 1 284 . 1 1 21 21 VAL N N 15 120.008 0.150 . . . . . . 21 VAL N . 7349 1 285 . 1 1 22 22 GLU H H 1 7.499 0.025 . . . . . . 22 GLU HN . 7349 1 286 . 1 1 22 22 GLU HA H 1 3.542 0.025 . . . . . . 22 GLU HA . 7349 1 287 . 1 1 22 22 GLU HB2 H 1 1.785 0.025 . . . . . . 22 GLU HB1 . 7349 1 288 . 1 1 22 22 GLU HB3 H 1 1.688 0.025 . . . . . . 22 GLU HB2 . 7349 1 289 . 1 1 22 22 GLU HG2 H 1 2.101 0.025 . . . . . . 22 GLU HG1 . 7349 1 290 . 1 1 22 22 GLU HG3 H 1 1.863 0.025 . . . . . . 22 GLU HG2 . 7349 1 291 . 1 1 22 22 GLU C C 13 174.643 0.150 . . . . . . 22 GLU C . 7349 1 292 . 1 1 22 22 GLU CA C 13 56.297 0.057 . . . . . . 22 GLU CA . 7349 1 293 . 1 1 22 22 GLU CB C 13 26.262 0.110 . . . . . . 22 GLU CB . 7349 1 294 . 1 1 22 22 GLU CG C 13 33.391 0.067 . . . . . . 22 GLU CG . 7349 1 295 . 1 1 22 22 GLU N N 15 120.082 0.150 . . . . . . 22 GLU N . 7349 1 296 . 1 1 23 23 LYS H H 1 7.354 0.025 . . . . . . 23 LYS HN . 7349 1 297 . 1 1 23 23 LYS HA H 1 3.490 0.025 . . . . . . 23 LYS HA . 7349 1 298 . 1 1 23 23 LYS HB2 H 1 0.729 0.025 . . . . . . 23 LYS HB1 . 7349 1 299 . 1 1 23 23 LYS HB3 H 1 0.856 0.025 . . . . . . 23 LYS HB2 . 7349 1 300 . 1 1 23 23 LYS HD2 H 1 0.837 0.025 . . . . . . 23 LYS HD1 . 7349 1 301 . 1 1 23 23 LYS HD3 H 1 0.968 0.025 . . . . . . 23 LYS HD2 . 7349 1 302 . 1 1 23 23 LYS HE2 H 1 2.357 0.025 . . . . . . 23 LYS HE1 . 7349 1 303 . 1 1 23 23 LYS HE3 H 1 2.423 0.025 . . . . . . 23 LYS HE2 . 7349 1 304 . 1 1 23 23 LYS HG2 H 1 0.353 0.025 . . . . . . 23 LYS HG1 . 7349 1 305 . 1 1 23 23 LYS HG3 H 1 -0.252 0.025 . . . . . . 23 LYS HG2 . 7349 1 306 . 1 1 23 23 LYS C C 13 175.150 0.150 . . . . . . 23 LYS C . 7349 1 307 . 1 1 23 23 LYS CA C 13 55.514 0.044 . . . . . . 23 LYS CA . 7349 1 308 . 1 1 23 23 LYS CB C 13 30.489 0.154 . . . . . . 23 LYS CB . 7349 1 309 . 1 1 23 23 LYS CD C 13 26.370 0.273 . . . . . . 23 LYS CD . 7349 1 310 . 1 1 23 23 LYS CE C 13 39.027 0.074 . . . . . . 23 LYS CE . 7349 1 311 . 1 1 23 23 LYS CG C 13 21.221 0.091 . . . . . . 23 LYS CG . 7349 1 312 . 1 1 23 23 LYS N N 15 117.373 0.150 . . . . . . 23 LYS N . 7349 1 313 . 1 1 24 24 TYR H H 1 8.259 0.025 . . . . . . 24 TYR HN . 7349 1 314 . 1 1 24 24 TYR HA H 1 4.192 0.025 . . . . . . 24 TYR HA . 7349 1 315 . 1 1 24 24 TYR HB2 H 1 2.227 0.015 . . . . . . 24 TYR HB1 . 7349 1 316 . 1 1 24 24 TYR HB3 H 1 2.530 0.025 . . . . . . 24 TYR HB2 . 7349 1 317 . 1 1 24 24 TYR HD1 H 1 6.472 0.015 . . . . . . 24 TYR QD . 7349 1 318 . 1 1 24 24 TYR HD2 H 1 6.472 0.015 . . . . . . 24 TYR QD . 7349 1 319 . 1 1 24 24 TYR HE1 H 1 6.328 0.015 . . . . . . 24 TYR QE . 7349 1 320 . 1 1 24 24 TYR HE2 H 1 6.328 0.015 . . . . . . 24 TYR QE . 7349 1 321 . 1 1 24 24 TYR C C 13 174.049 0.150 . . . . . . 24 TYR C . 7349 1 322 . 1 1 24 24 TYR CA C 13 56.082 0.023 . . . . . . 24 TYR CA . 7349 1 323 . 1 1 24 24 TYR CB C 13 37.070 0.200 . . . . . . 24 TYR CB . 7349 1 324 . 1 1 24 24 TYR CD1 C 13 129.559 0.150 . . . . . . 24 TYR CD1 . 7349 1 325 . 1 1 24 24 TYR CD2 C 13 129.559 0.150 . . . . . . 24 TYR CD2 . 7349 1 326 . 1 1 24 24 TYR CE1 C 13 114.499 0.150 . . . . . . 24 TYR CE1 . 7349 1 327 . 1 1 24 24 TYR CE2 C 13 114.499 0.150 . . . . . . 24 TYR CE2 . 7349 1 328 . 1 1 24 24 TYR N N 15 114.131 0.150 . . . . . . 24 TYR N . 7349 1 329 . 1 1 25 25 GLY H H 1 7.829 0.025 . . . . . . 25 GLY HN . 7349 1 330 . 1 1 25 25 GLY HA2 H 1 3.592 0.025 . . . . . . 25 GLY HA1 . 7349 1 331 . 1 1 25 25 GLY HA3 H 1 4.282 0.025 . . . . . . 25 GLY HA2 . 7349 1 332 . 1 1 25 25 GLY C C 13 170.783 0.150 . . . . . . 25 GLY C . 7349 1 333 . 1 1 25 25 GLY CA C 13 41.361 0.054 . . . . . . 25 GLY CA . 7349 1 334 . 1 1 25 25 GLY N N 15 109.673 0.150 . . . . . . 25 GLY N . 7349 1 335 . 1 1 26 26 PHE H H 1 8.142 0.025 . . . . . . 26 PHE HN . 7349 1 336 . 1 1 26 26 PHE HA H 1 4.081 0.025 . . . . . . 26 PHE HA . 7349 1 337 . 1 1 26 26 PHE HB2 H 1 2.941 0.025 . . . . . . 26 PHE HB1 . 7349 1 338 . 1 1 26 26 PHE HB3 H 1 2.835 0.025 . . . . . . 26 PHE HB2 . 7349 1 339 . 1 1 26 26 PHE HD1 H 1 7.076 0.024 . . . . . . 26 PHE QD . 7349 1 340 . 1 1 26 26 PHE HD2 H 1 7.076 0.024 . . . . . . 26 PHE QD . 7349 1 341 . 1 1 26 26 PHE HE1 H 1 7.064 0.015 . . . . . . 26 PHE QE . 7349 1 342 . 1 1 26 26 PHE HE2 H 1 7.064 0.015 . . . . . . 26 PHE QE . 7349 1 343 . 1 1 26 26 PHE HZ H 1 7.055 0.015 . . . . . . 26 PHE HZ . 7349 1 344 . 1 1 26 26 PHE C C 13 173.524 0.150 . . . . . . 26 PHE C . 7349 1 345 . 1 1 26 26 PHE CA C 13 58.261 0.215 . . . . . . 26 PHE CA . 7349 1 346 . 1 1 26 26 PHE CB C 13 37.159 0.049 . . . . . . 26 PHE CB . 7349 1 347 . 1 1 26 26 PHE CD1 C 13 128.911 0.150 . . . . . . 26 PHE CD1 . 7349 1 348 . 1 1 26 26 PHE CD2 C 13 128.911 0.150 . . . . . . 26 PHE CD2 . 7349 1 349 . 1 1 26 26 PHE CE1 C 13 128.942 0.150 . . . . . . 26 PHE CE1 . 7349 1 350 . 1 1 26 26 PHE CE2 C 13 128.942 0.150 . . . . . . 26 PHE CE2 . 7349 1 351 . 1 1 26 26 PHE CZ C 13 127.250 0.150 . . . . . . 26 PHE CZ . 7349 1 352 . 1 1 26 26 PHE N N 15 114.812 0.150 . . . . . . 26 PHE N . 7349 1 353 . 1 1 27 27 THR H H 1 7.859 0.025 . . . . . . 27 THR HN . 7349 1 354 . 1 1 27 27 THR HA H 1 4.126 0.025 . . . . . . 27 THR HA . 7349 1 355 . 1 1 27 27 THR HB H 1 4.261 0.025 . . . . . . 27 THR HB . 7349 1 356 . 1 1 27 27 THR HG21 H 1 0.800 0.025 . . . . . . 27 THR QG2 . 7349 1 357 . 1 1 27 27 THR HG22 H 1 0.800 0.025 . . . . . . 27 THR QG2 . 7349 1 358 . 1 1 27 27 THR HG23 H 1 0.800 0.025 . . . . . . 27 THR QG2 . 7349 1 359 . 1 1 27 27 THR C C 13 171.000 0.150 . . . . . . 27 THR C . 7349 1 360 . 1 1 27 27 THR CA C 13 57.796 0.059 . . . . . . 27 THR CA . 7349 1 361 . 1 1 27 27 THR CB C 13 66.137 0.049 . . . . . . 27 THR CB . 7349 1 362 . 1 1 27 27 THR CG2 C 13 18.635 0.021 . . . . . . 27 THR CG2 . 7349 1 363 . 1 1 27 27 THR N N 15 104.629 0.150 . . . . . . 27 THR N . 7349 1 364 . 1 1 28 28 HIS H H 1 6.982 0.025 . . . . . . 28 HIS HN . 7349 1 365 . 1 1 28 28 HIS HA H 1 3.994 0.025 . . . . . . 28 HIS HA . 7349 1 366 . 1 1 28 28 HIS HB2 H 1 2.340 0.025 . . . . . . 28 HIS HB1 . 7349 1 367 . 1 1 28 28 HIS HB3 H 1 2.888 0.025 . . . . . . 28 HIS HB2 . 7349 1 368 . 1 1 28 28 HIS HD2 H 1 6.713 0.015 . . . . . . 28 HIS HD2 . 7349 1 369 . 1 1 28 28 HIS C C 13 174.576 0.150 . . . . . . 28 HIS C . 7349 1 370 . 1 1 28 28 HIS CA C 13 55.184 0.001 . . . . . . 28 HIS CA . 7349 1 371 . 1 1 28 28 HIS CB C 13 30.465 0.106 . . . . . . 28 HIS CB . 7349 1 372 . 1 1 28 28 HIS CD2 C 13 134.670 0.150 . . . . . . 28 HIS CD2 . 7349 1 373 . 1 1 28 28 HIS N N 15 123.387 0.150 . . . . . . 28 HIS N . 7349 1 374 . 1 1 29 29 HIS H H 1 8.426 0.025 . . . . . . 29 HIS HN . 7349 1 375 . 1 1 29 29 HIS HA H 1 3.955 0.025 . . . . . . 29 HIS HA . 7349 1 376 . 1 1 29 29 HIS HB2 H 1 2.792 0.025 . . . . . . 29 HIS HB1 . 7349 1 377 . 1 1 29 29 HIS HB3 H 1 2.917 0.025 . . . . . . 29 HIS HB2 . 7349 1 378 . 1 1 29 29 HIS C C 13 174.715 0.150 . . . . . . 29 HIS C . 7349 1 379 . 1 1 29 29 HIS CA C 13 57.102 0.128 . . . . . . 29 HIS CA . 7349 1 380 . 1 1 29 29 HIS CB C 13 26.300 0.249 . . . . . . 29 HIS CB . 7349 1 381 . 1 1 29 29 HIS N N 15 127.331 0.150 . . . . . . 29 HIS N . 7349 1 382 . 1 1 30 30 LYS H H 1 10.737 0.025 . . . . . . 30 LYS HN . 7349 1 383 . 1 1 30 30 LYS HA H 1 3.751 0.025 . . . . . . 30 LYS HA . 7349 1 384 . 1 1 30 30 LYS HB2 H 1 1.141 0.024 . . . . . . 30 LYS HB1 . 7349 1 385 . 1 1 30 30 LYS HB3 H 1 1.152 0.028 . . . . . . 30 LYS HB2 . 7349 1 386 . 1 1 30 30 LYS HD2 H 1 0.795 0.025 . . . . . . 30 LYS HD1 . 7349 1 387 . 1 1 30 30 LYS HD3 H 1 0.924 0.025 . . . . . . 30 LYS HD2 . 7349 1 388 . 1 1 30 30 LYS HE2 H 1 2.577 0.025 . . . . . . 30 LYS HE1 . 7349 1 389 . 1 1 30 30 LYS HE3 H 1 2.577 0.025 . . . . . . 30 LYS HE2 . 7349 1 390 . 1 1 30 30 LYS HG2 H 1 0.856 0.015 . . . . . . 30 LYS HG1 . 7349 1 391 . 1 1 30 30 LYS HG3 H 1 0.937 0.025 . . . . . . 30 LYS HG2 . 7349 1 392 . 1 1 30 30 LYS C C 13 176.775 0.150 . . . . . . 30 LYS C . 7349 1 393 . 1 1 30 30 LYS CA C 13 56.690 0.200 . . . . . . 30 LYS CA . 7349 1 394 . 1 1 30 30 LYS CB C 13 29.643 0.150 . . . . . . 30 LYS CB . 7349 1 395 . 1 1 30 30 LYS CD C 13 26.090 0.134 . . . . . . 30 LYS CD . 7349 1 396 . 1 1 30 30 LYS CE C 13 38.943 0.150 . . . . . . 30 LYS CE . 7349 1 397 . 1 1 30 30 LYS CG C 13 22.988 0.200 . . . . . . 30 LYS CG . 7349 1 398 . 1 1 30 30 LYS N N 15 124.235 0.150 . . . . . . 30 LYS N . 7349 1 399 . 1 1 31 31 VAL H H 1 6.899 0.025 . . . . . . 31 VAL HN . 7349 1 400 . 1 1 31 31 VAL HA H 1 3.210 0.025 . . . . . . 31 VAL HA . 7349 1 401 . 1 1 31 31 VAL HB H 1 2.102 0.025 . . . . . . 31 VAL HB . 7349 1 402 . 1 1 31 31 VAL HG11 H 1 0.687 0.025 . . . . . . 31 VAL QG1 . 7349 1 403 . 1 1 31 31 VAL HG12 H 1 0.687 0.025 . . . . . . 31 VAL QG1 . 7349 1 404 . 1 1 31 31 VAL HG13 H 1 0.687 0.025 . . . . . . 31 VAL QG1 . 7349 1 405 . 1 1 31 31 VAL HG21 H 1 0.733 0.025 . . . . . . 31 VAL QG2 . 7349 1 406 . 1 1 31 31 VAL HG22 H 1 0.733 0.025 . . . . . . 31 VAL QG2 . 7349 1 407 . 1 1 31 31 VAL HG23 H 1 0.733 0.025 . . . . . . 31 VAL QG2 . 7349 1 408 . 1 1 31 31 VAL C C 13 175.023 0.150 . . . . . . 31 VAL C . 7349 1 409 . 1 1 31 31 VAL CA C 13 63.153 0.114 . . . . . . 31 VAL CA . 7349 1 410 . 1 1 31 31 VAL CB C 13 29.197 0.057 . . . . . . 31 VAL CB . 7349 1 411 . 1 1 31 31 VAL CG1 C 13 19.242 0.134 . . . . . . 31 VAL CG1 . 7349 1 412 . 1 1 31 31 VAL CG2 C 13 21.173 0.093 . . . . . . 31 VAL CG2 . 7349 1 413 . 1 1 31 31 VAL N N 15 119.853 0.150 . . . . . . 31 VAL N . 7349 1 414 . 1 1 32 32 ILE H H 1 7.960 0.025 . . . . . . 32 ILE HN . 7349 1 415 . 1 1 32 32 ILE HA H 1 3.457 0.025 . . . . . . 32 ILE HA . 7349 1 416 . 1 1 32 32 ILE HB H 1 1.527 0.025 . . . . . . 32 ILE HB . 7349 1 417 . 1 1 32 32 ILE HD11 H 1 0.513 0.025 . . . . . . 32 ILE QD1 . 7349 1 418 . 1 1 32 32 ILE HD12 H 1 0.513 0.025 . . . . . . 32 ILE QD1 . 7349 1 419 . 1 1 32 32 ILE HD13 H 1 0.513 0.025 . . . . . . 32 ILE QD1 . 7349 1 420 . 1 1 32 32 ILE HG12 H 1 0.928 0.025 . . . . . . 32 ILE HG11 . 7349 1 421 . 1 1 32 32 ILE HG13 H 1 1.297 0.025 . . . . . . 32 ILE HG12 . 7349 1 422 . 1 1 32 32 ILE HG21 H 1 0.630 0.025 . . . . . . 32 ILE QG2 . 7349 1 423 . 1 1 32 32 ILE HG22 H 1 0.630 0.025 . . . . . . 32 ILE QG2 . 7349 1 424 . 1 1 32 32 ILE HG23 H 1 0.630 0.025 . . . . . . 32 ILE QG2 . 7349 1 425 . 1 1 32 32 ILE C C 13 176.538 0.150 . . . . . . 32 ILE C . 7349 1 426 . 1 1 32 32 ILE CA C 13 61.931 0.084 . . . . . . 32 ILE CA . 7349 1 427 . 1 1 32 32 ILE CB C 13 34.999 0.219 . . . . . . 32 ILE CB . 7349 1 428 . 1 1 32 32 ILE CD1 C 13 9.667 0.084 . . . . . . 32 ILE CD1 . 7349 1 429 . 1 1 32 32 ILE CG1 C 13 25.449 0.110 . . . . . . 32 ILE CG1 . 7349 1 430 . 1 1 32 32 ILE CG2 C 13 13.964 0.168 . . . . . . 32 ILE CG2 . 7349 1 431 . 1 1 32 32 ILE N N 15 121.529 0.150 . . . . . . 32 ILE N . 7349 1 432 . 1 1 33 33 SER H H 1 8.036 0.025 . . . . . . 33 SER HN . 7349 1 433 . 1 1 33 33 SER HA H 1 3.977 0.025 . . . . . . 33 SER HA . 7349 1 434 . 1 1 33 33 SER HB2 H 1 3.656 0.025 . . . . . . 33 SER HB1 . 7349 1 435 . 1 1 33 33 SER C C 13 174.173 0.150 . . . . . . 33 SER C . 7349 1 436 . 1 1 33 33 SER CA C 13 58.917 0.128 . . . . . . 33 SER CA . 7349 1 437 . 1 1 33 33 SER CB C 13 59.676 0.200 . . . . . . 33 SER CB . 7349 1 438 . 1 1 33 33 SER N N 15 113.938 0.150 . . . . . . 33 SER N . 7349 1 439 . 1 1 34 34 PHE H H 1 7.598 0.025 . . . . . . 34 PHE HN . 7349 1 440 . 1 1 34 34 PHE HA H 1 3.890 0.025 . . . . . . 34 PHE HA . 7349 1 441 . 1 1 34 34 PHE HB2 H 1 2.806 0.025 . . . . . . 34 PHE HB1 . 7349 1 442 . 1 1 34 34 PHE HB3 H 1 3.106 0.025 . . . . . . 34 PHE HB2 . 7349 1 443 . 1 1 34 34 PHE HD1 H 1 6.906 0.020 . . . . . . 34 PHE QD . 7349 1 444 . 1 1 34 34 PHE HD2 H 1 6.906 0.020 . . . . . . 34 PHE QD . 7349 1 445 . 1 1 34 34 PHE HE1 H 1 7.273 0.015 . . . . . . 34 PHE QE . 7349 1 446 . 1 1 34 34 PHE HE2 H 1 7.273 0.015 . . . . . . 34 PHE QE . 7349 1 447 . 1 1 34 34 PHE C C 13 175.579 0.150 . . . . . . 34 PHE C . 7349 1 448 . 1 1 34 34 PHE CA C 13 58.867 0.064 . . . . . . 34 PHE CA . 7349 1 449 . 1 1 34 34 PHE CB C 13 36.917 0.145 . . . . . . 34 PHE CB . 7349 1 450 . 1 1 34 34 PHE CD1 C 13 129.345 0.150 . . . . . . 34 PHE CD1 . 7349 1 451 . 1 1 34 34 PHE CD2 C 13 129.345 0.150 . . . . . . 34 PHE CD2 . 7349 1 452 . 1 1 34 34 PHE CE1 C 13 128.236 0.150 . . . . . . 34 PHE CE1 . 7349 1 453 . 1 1 34 34 PHE CE2 C 13 128.236 0.150 . . . . . . 34 PHE CE2 . 7349 1 454 . 1 1 34 34 PHE N N 15 124.363 0.150 . . . . . . 34 PHE N . 7349 1 455 . 1 1 35 35 SER H H 1 8.753 0.025 . . . . . . 35 SER HN . 7349 1 456 . 1 1 35 35 SER HA H 1 3.902 0.025 . . . . . . 35 SER HA . 7349 1 457 . 1 1 35 35 SER HB2 H 1 3.883 0.025 . . . . . . 35 SER HB1 . 7349 1 458 . 1 1 35 35 SER HB3 H 1 3.894 0.025 . . . . . . 35 SER HB2 . 7349 1 459 . 1 1 35 35 SER C C 13 173.562 0.150 . . . . . . 35 SER C . 7349 1 460 . 1 1 35 35 SER CA C 13 59.031 0.200 . . . . . . 35 SER CA . 7349 1 461 . 1 1 35 35 SER CB C 13 59.940 0.099 . . . . . . 35 SER CB . 7349 1 462 . 1 1 35 35 SER N N 15 114.383 0.150 . . . . . . 35 SER N . 7349 1 463 . 1 1 36 36 GLN H H 1 7.811 0.025 . . . . . . 36 GLN HN . 7349 1 464 . 1 1 36 36 GLN HA H 1 3.928 0.018 . . . . . . 36 GLN HA . 7349 1 465 . 1 1 36 36 GLN HB2 H 1 1.824 0.025 . . . . . . 36 GLN HB1 . 7349 1 466 . 1 1 36 36 GLN HB3 H 1 2.076 0.025 . . . . . . 36 GLN HB2 . 7349 1 467 . 1 1 36 36 GLN HE21 H 1 6.642 0.025 . . . . . . 36 GLN HE21 . 7349 1 468 . 1 1 36 36 GLN HE22 H 1 7.289 0.025 . . . . . . 36 GLN HE22 . 7349 1 469 . 1 1 36 36 GLN HG2 H 1 2.445 0.025 . . . . . . 36 GLN HG1 . 7349 1 470 . 1 1 36 36 GLN HG3 H 1 2.183 0.025 . . . . . . 36 GLN HG2 . 7349 1 471 . 1 1 36 36 GLN C C 13 176.298 0.150 . . . . . . 36 GLN C . 7349 1 472 . 1 1 36 36 GLN CA C 13 56.194 0.150 . . . . . . 36 GLN CA . 7349 1 473 . 1 1 36 36 GLN CB C 13 25.132 0.220 . . . . . . 36 GLN CB . 7349 1 474 . 1 1 36 36 GLN CG C 13 31.301 0.072 . . . . . . 36 GLN CG . 7349 1 475 . 1 1 36 36 GLN N N 15 120.391 0.150 . . . . . . 36 GLN N . 7349 1 476 . 1 1 36 36 GLN NE2 N 15 111.391 0.150 . . . . . . 36 GLN NE2 . 7349 1 477 . 1 1 37 37 GLU H H 1 7.337 0.025 . . . . . . 37 GLU HN . 7349 1 478 . 1 1 37 37 GLU HA H 1 3.934 0.025 . . . . . . 37 GLU HA . 7349 1 479 . 1 1 37 37 GLU HB2 H 1 1.544 0.025 . . . . . . 37 GLU HB1 . 7349 1 480 . 1 1 37 37 GLU HB3 H 1 1.750 0.025 . . . . . . 37 GLU HB2 . 7349 1 481 . 1 1 37 37 GLU HG2 H 1 1.944 0.025 . . . . . . 37 GLU HG1 . 7349 1 482 . 1 1 37 37 GLU HG3 H 1 1.955 0.025 . . . . . . 37 GLU HG2 . 7349 1 483 . 1 1 37 37 GLU C C 13 175.941 0.150 . . . . . . 37 GLU C . 7349 1 484 . 1 1 37 37 GLU CA C 13 55.753 0.085 . . . . . . 37 GLU CA . 7349 1 485 . 1 1 37 37 GLU CB C 13 25.720 0.103 . . . . . . 37 GLU CB . 7349 1 486 . 1 1 37 37 GLU CG C 13 32.268 0.162 . . . . . . 37 GLU CG . 7349 1 487 . 1 1 37 37 GLU N N 15 120.553 0.150 . . . . . . 37 GLU N . 7349 1 488 . 1 1 38 38 LEU H H 1 7.803 0.025 . . . . . . 38 LEU HN . 7349 1 489 . 1 1 38 38 LEU HA H 1 3.691 0.015 . . . . . . 38 LEU HA . 7349 1 490 . 1 1 38 38 LEU HB2 H 1 1.943 0.025 . . . . . . 38 LEU HB1 . 7349 1 491 . 1 1 38 38 LEU HB3 H 1 1.028 0.025 . . . . . . 38 LEU HB2 . 7349 1 492 . 1 1 38 38 LEU HD11 H 1 0.759 0.025 . . . . . . 38 LEU QD1 . 7349 1 493 . 1 1 38 38 LEU HD12 H 1 0.759 0.025 . . . . . . 38 LEU QD1 . 7349 1 494 . 1 1 38 38 LEU HD13 H 1 0.759 0.025 . . . . . . 38 LEU QD1 . 7349 1 495 . 1 1 38 38 LEU HG H 1 1.436 0.015 . . . . . . 38 LEU HG . 7349 1 496 . 1 1 38 38 LEU C C 13 174.945 0.150 . . . . . . 38 LEU C . 7349 1 497 . 1 1 38 38 LEU CA C 13 55.499 0.150 . . . . . . 38 LEU CA . 7349 1 498 . 1 1 38 38 LEU CB C 13 38.341 0.243 . . . . . . 38 LEU CB . 7349 1 499 . 1 1 38 38 LEU CD1 C 13 24.260 0.200 . . . . . . 38 LEU CD1 . 7349 1 500 . 1 1 38 38 LEU CG C 13 24.561 0.150 . . . . . . 38 LEU CG . 7349 1 501 . 1 1 38 38 LEU N N 15 121.675 0.150 . . . . . . 38 LEU N . 7349 1 502 . 1 1 39 39 ASP H H 1 8.201 0.025 . . . . . . 39 ASP HN . 7349 1 503 . 1 1 39 39 ASP HA H 1 4.146 0.025 . . . . . . 39 ASP HA . 7349 1 504 . 1 1 39 39 ASP HB2 H 1 2.579 0.025 . . . . . . 39 ASP HB1 . 7349 1 505 . 1 1 39 39 ASP HB3 H 1 2.366 0.025 . . . . . . 39 ASP HB2 . 7349 1 506 . 1 1 39 39 ASP C C 13 175.756 0.150 . . . . . . 39 ASP C . 7349 1 507 . 1 1 39 39 ASP CA C 13 54.805 0.089 . . . . . . 39 ASP CA . 7349 1 508 . 1 1 39 39 ASP CB C 13 37.392 0.147 . . . . . . 39 ASP CB . 7349 1 509 . 1 1 39 39 ASP N N 15 119.049 0.150 . . . . . . 39 ASP N . 7349 1 510 . 1 1 40 40 ARG H H 1 7.400 0.025 . . . . . . 40 ARG HN . 7349 1 511 . 1 1 40 40 ARG HA H 1 3.818 0.025 . . . . . . 40 ARG HA . 7349 1 512 . 1 1 40 40 ARG HB2 H 1 1.764 0.025 . . . . . . 40 ARG HB1 . 7349 1 513 . 1 1 40 40 ARG HB3 H 1 1.693 0.025 . . . . . . 40 ARG HB2 . 7349 1 514 . 1 1 40 40 ARG HD2 H 1 2.899 0.025 . . . . . . 40 ARG HD1 . 7349 1 515 . 1 1 40 40 ARG HD3 H 1 3.021 0.025 . . . . . . 40 ARG HD2 . 7349 1 516 . 1 1 40 40 ARG HG2 H 1 1.254 0.025 . . . . . . 40 ARG HG1 . 7349 1 517 . 1 1 40 40 ARG HG3 H 1 1.557 0.025 . . . . . . 40 ARG HG2 . 7349 1 518 . 1 1 40 40 ARG C C 13 177.070 0.150 . . . . . . 40 ARG C . 7349 1 519 . 1 1 40 40 ARG CA C 13 56.998 0.026 . . . . . . 40 ARG CA . 7349 1 520 . 1 1 40 40 ARG CB C 13 27.305 0.154 . . . . . . 40 ARG CB . 7349 1 521 . 1 1 40 40 ARG CD C 13 40.380 0.209 . . . . . . 40 ARG CD . 7349 1 522 . 1 1 40 40 ARG CG C 13 25.207 0.101 . . . . . . 40 ARG CG . 7349 1 523 . 1 1 40 40 ARG N N 15 119.194 0.150 . . . . . . 40 ARG N . 7349 1 524 . 1 1 41 41 LEU H H 1 7.623 0.025 . . . . . . 41 LEU HN . 7349 1 525 . 1 1 41 41 LEU HA H 1 3.837 0.025 . . . . . . 41 LEU HA . 7349 1 526 . 1 1 41 41 LEU HB2 H 1 1.131 0.015 . . . . . . 41 LEU HB1 . 7349 1 527 . 1 1 41 41 LEU HB3 H 1 1.842 0.025 . . . . . . 41 LEU HB2 . 7349 1 528 . 1 1 41 41 LEU HD11 H 1 0.523 0.025 . . . . . . 41 LEU QD1 . 7349 1 529 . 1 1 41 41 LEU HD12 H 1 0.523 0.025 . . . . . . 41 LEU QD1 . 7349 1 530 . 1 1 41 41 LEU HD13 H 1 0.523 0.025 . . . . . . 41 LEU QD1 . 7349 1 531 . 1 1 41 41 LEU HD21 H 1 0.519 0.025 . . . . . . 41 LEU QD2 . 7349 1 532 . 1 1 41 41 LEU HD22 H 1 0.519 0.025 . . . . . . 41 LEU QD2 . 7349 1 533 . 1 1 41 41 LEU HD23 H 1 0.519 0.025 . . . . . . 41 LEU QD2 . 7349 1 534 . 1 1 41 41 LEU HG H 1 1.658 0.025 . . . . . . 41 LEU HG . 7349 1 535 . 1 1 41 41 LEU C C 13 175.891 0.150 . . . . . . 41 LEU C . 7349 1 536 . 1 1 41 41 LEU CA C 13 55.153 0.096 . . . . . . 41 LEU CA . 7349 1 537 . 1 1 41 41 LEU CB C 13 39.015 0.117 . . . . . . 41 LEU CB . 7349 1 538 . 1 1 41 41 LEU CD1 C 13 19.258 0.042 . . . . . . 41 LEU CD1 . 7349 1 539 . 1 1 41 41 LEU CD2 C 13 22.862 0.200 . . . . . . 41 LEU CD2 . 7349 1 540 . 1 1 41 41 LEU CG C 13 23.642 0.169 . . . . . . 41 LEU CG . 7349 1 541 . 1 1 41 41 LEU N N 15 120.340 0.150 . . . . . . 41 LEU N . 7349 1 542 . 1 1 42 42 LEU H H 1 8.466 0.025 . . . . . . 42 LEU HN . 7349 1 543 . 1 1 42 42 LEU HA H 1 3.737 0.025 . . . . . . 42 LEU HA . 7349 1 544 . 1 1 42 42 LEU HB2 H 1 1.248 0.025 . . . . . . 42 LEU HB1 . 7349 1 545 . 1 1 42 42 LEU HB3 H 1 1.744 0.025 . . . . . . 42 LEU HB2 . 7349 1 546 . 1 1 42 42 LEU HD11 H 1 0.685 0.015 . . . . . . 42 LEU QD1 . 7349 1 547 . 1 1 42 42 LEU HD12 H 1 0.685 0.015 . . . . . . 42 LEU QD1 . 7349 1 548 . 1 1 42 42 LEU HD13 H 1 0.685 0.015 . . . . . . 42 LEU QD1 . 7349 1 549 . 1 1 42 42 LEU C C 13 177.200 0.150 . . . . . . 42 LEU C . 7349 1 550 . 1 1 42 42 LEU CA C 13 55.463 0.072 . . . . . . 42 LEU CA . 7349 1 551 . 1 1 42 42 LEU CB C 13 38.475 0.040 . . . . . . 42 LEU CB . 7349 1 552 . 1 1 42 42 LEU CG C 13 24.483 0.150 . . . . . . 42 LEU CG . 7349 1 553 . 1 1 42 42 LEU N N 15 119.790 0.150 . . . . . . 42 LEU N . 7349 1 554 . 1 1 43 43 ASN H H 1 7.880 0.025 . . . . . . 43 ASN HN . 7349 1 555 . 1 1 43 43 ASN HA H 1 4.267 0.026 . . . . . . 43 ASN HA . 7349 1 556 . 1 1 43 43 ASN HB2 H 1 2.591 0.025 . . . . . . 43 ASN HB1 . 7349 1 557 . 1 1 43 43 ASN HB3 H 1 2.507 0.025 . . . . . . 43 ASN HB2 . 7349 1 558 . 1 1 43 43 ASN HD21 H 1 6.755 0.025 . . . . . . 43 ASN HD21 . 7349 1 559 . 1 1 43 43 ASN HD22 H 1 7.327 0.025 . . . . . . 43 ASN HD22 . 7349 1 560 . 1 1 43 43 ASN C C 13 174.988 0.150 . . . . . . 43 ASN C . 7349 1 561 . 1 1 43 43 ASN CA C 13 53.143 0.289 . . . . . . 43 ASN CA . 7349 1 562 . 1 1 43 43 ASN CB C 13 35.319 0.102 . . . . . . 43 ASN CB . 7349 1 563 . 1 1 43 43 ASN N N 15 116.995 0.150 . . . . . . 43 ASN N . 7349 1 564 . 1 1 43 43 ASN ND2 N 15 113.349 0.150 . . . . . . 43 ASN ND2 . 7349 1 565 . 1 1 44 44 LEU H H 1 7.704 0.025 . . . . . . 44 LEU HN . 7349 1 566 . 1 1 44 44 LEU HA H 1 3.946 0.025 . . . . . . 44 LEU HA . 7349 1 567 . 1 1 44 44 LEU HB2 H 1 1.630 0.025 . . . . . . 44 LEU HB1 . 7349 1 568 . 1 1 44 44 LEU HB3 H 1 1.592 0.025 . . . . . . 44 LEU HB2 . 7349 1 569 . 1 1 44 44 LEU HD11 H 1 0.672 0.025 . . . . . . 44 LEU QD1 . 7349 1 570 . 1 1 44 44 LEU HD12 H 1 0.672 0.025 . . . . . . 44 LEU QD1 . 7349 1 571 . 1 1 44 44 LEU HD13 H 1 0.672 0.025 . . . . . . 44 LEU QD1 . 7349 1 572 . 1 1 44 44 LEU HD21 H 1 0.515 0.025 . . . . . . 44 LEU QD2 . 7349 1 573 . 1 1 44 44 LEU HD22 H 1 0.515 0.025 . . . . . . 44 LEU QD2 . 7349 1 574 . 1 1 44 44 LEU HD23 H 1 0.515 0.025 . . . . . . 44 LEU QD2 . 7349 1 575 . 1 1 44 44 LEU HG H 1 1.330 0.025 . . . . . . 44 LEU HG . 7349 1 576 . 1 1 44 44 LEU C C 13 175.563 0.150 . . . . . . 44 LEU C . 7349 1 577 . 1 1 44 44 LEU CA C 13 54.868 0.112 . . . . . . 44 LEU CA . 7349 1 578 . 1 1 44 44 LEU CB C 13 38.757 0.116 . . . . . . 44 LEU CB . 7349 1 579 . 1 1 44 44 LEU CD1 C 13 20.966 0.200 . . . . . . 44 LEU CD1 . 7349 1 580 . 1 1 44 44 LEU CD2 C 13 20.932 0.200 . . . . . . 44 LEU CD2 . 7349 1 581 . 1 1 44 44 LEU CG C 13 23.801 0.200 . . . . . . 44 LEU CG . 7349 1 582 . 1 1 44 44 LEU N N 15 123.227 0.150 . . . . . . 44 LEU N . 7349 1 583 . 1 1 45 45 LEU H H 1 7.909 0.025 . . . . . . 45 LEU HN . 7349 1 584 . 1 1 45 45 LEU HA H 1 3.736 0.016 . . . . . . 45 LEU HA . 7349 1 585 . 1 1 45 45 LEU HB2 H 1 1.747 0.025 . . . . . . 45 LEU HB1 . 7349 1 586 . 1 1 45 45 LEU HD11 H 1 0.685 0.035 . . . . . . 45 LEU QD1 . 7349 1 587 . 1 1 45 45 LEU HD12 H 1 0.685 0.035 . . . . . . 45 LEU QD1 . 7349 1 588 . 1 1 45 45 LEU HD13 H 1 0.685 0.035 . . . . . . 45 LEU QD1 . 7349 1 589 . 1 1 45 45 LEU HD21 H 1 0.677 0.025 . . . . . . 45 LEU QD2 . 7349 1 590 . 1 1 45 45 LEU HD22 H 1 0.677 0.025 . . . . . . 45 LEU QD2 . 7349 1 591 . 1 1 45 45 LEU HD23 H 1 0.677 0.025 . . . . . . 45 LEU QD2 . 7349 1 592 . 1 1 45 45 LEU HG H 1 1.494 0.025 . . . . . . 45 LEU HG . 7349 1 593 . 1 1 45 45 LEU C C 13 175.453 0.150 . . . . . . 45 LEU C . 7349 1 594 . 1 1 45 45 LEU CA C 13 55.403 0.150 . . . . . . 45 LEU CA . 7349 1 595 . 1 1 45 45 LEU CB C 13 38.415 0.200 . . . . . . 45 LEU CB . 7349 1 596 . 1 1 45 45 LEU CD1 C 13 22.757 0.180 . . . . . . 45 LEU CD1 . 7349 1 597 . 1 1 45 45 LEU CD2 C 13 21.445 0.054 . . . . . . 45 LEU CD2 . 7349 1 598 . 1 1 45 45 LEU CG C 13 24.355 0.194 . . . . . . 45 LEU CG . 7349 1 599 . 1 1 45 45 LEU N N 15 120.090 0.177 . . . . . . 45 LEU N . 7349 1 600 . 1 1 46 46 ILE H H 1 7.476 0.025 . . . . . . 46 ILE HN . 7349 1 601 . 1 1 46 46 ILE HA H 1 3.389 0.025 . . . . . . 46 ILE HA . 7349 1 602 . 1 1 46 46 ILE HB H 1 1.727 0.025 . . . . . . 46 ILE HB . 7349 1 603 . 1 1 46 46 ILE HD11 H 1 0.636 0.025 . . . . . . 46 ILE QD1 . 7349 1 604 . 1 1 46 46 ILE HD12 H 1 0.636 0.025 . . . . . . 46 ILE QD1 . 7349 1 605 . 1 1 46 46 ILE HD13 H 1 0.636 0.025 . . . . . . 46 ILE QD1 . 7349 1 606 . 1 1 46 46 ILE HG12 H 1 1.534 0.025 . . . . . . 46 ILE HG11 . 7349 1 607 . 1 1 46 46 ILE HG13 H 1 0.919 0.025 . . . . . . 46 ILE HG12 . 7349 1 608 . 1 1 46 46 ILE HG21 H 1 0.657 0.025 . . . . . . 46 ILE QG2 . 7349 1 609 . 1 1 46 46 ILE HG22 H 1 0.657 0.025 . . . . . . 46 ILE QG2 . 7349 1 610 . 1 1 46 46 ILE HG23 H 1 0.657 0.025 . . . . . . 46 ILE QG2 . 7349 1 611 . 1 1 46 46 ILE C C 13 176.546 0.150 . . . . . . 46 ILE C . 7349 1 612 . 1 1 46 46 ILE CA C 13 62.106 0.200 . . . . . . 46 ILE CA . 7349 1 613 . 1 1 46 46 ILE CB C 13 35.212 0.081 . . . . . . 46 ILE CB . 7349 1 614 . 1 1 46 46 ILE CD1 C 13 10.146 0.106 . . . . . . 46 ILE CD1 . 7349 1 615 . 1 1 46 46 ILE CG1 C 13 26.346 0.097 . . . . . . 46 ILE CG1 . 7349 1 616 . 1 1 46 46 ILE CG2 C 13 14.323 0.122 . . . . . . 46 ILE CG2 . 7349 1 617 . 1 1 46 46 ILE N N 15 118.045 0.150 . . . . . . 46 ILE N . 7349 1 618 . 1 1 47 47 GLU H H 1 7.751 0.025 . . . . . . 47 GLU HN . 7349 1 619 . 1 1 47 47 GLU HA H 1 3.771 0.025 . . . . . . 47 GLU HA . 7349 1 620 . 1 1 47 47 GLU HB2 H 1 1.937 0.025 . . . . . . 47 GLU HB1 . 7349 1 621 . 1 1 47 47 GLU HB3 H 1 1.937 0.025 . . . . . . 47 GLU HB2 . 7349 1 622 . 1 1 47 47 GLU HG2 H 1 2.119 0.025 . . . . . . 47 GLU HG1 . 7349 1 623 . 1 1 47 47 GLU HG3 H 1 2.119 0.025 . . . . . . 47 GLU HG2 . 7349 1 624 . 1 1 47 47 GLU C C 13 176.322 0.150 . . . . . . 47 GLU C . 7349 1 625 . 1 1 47 47 GLU CA C 13 56.605 0.127 . . . . . . 47 GLU CA . 7349 1 626 . 1 1 47 47 GLU CB C 13 26.573 0.091 . . . . . . 47 GLU CB . 7349 1 627 . 1 1 47 47 GLU CG C 13 33.276 0.016 . . . . . . 47 GLU CG . 7349 1 628 . 1 1 47 47 GLU N N 15 121.604 0.150 . . . . . . 47 GLU N . 7349 1 629 . 1 1 48 48 LEU H H 1 8.260 0.025 . . . . . . 48 LEU HN . 7349 1 630 . 1 1 48 48 LEU HA H 1 3.852 0.025 . . . . . . 48 LEU HA . 7349 1 631 . 1 1 48 48 LEU HB2 H 1 1.304 0.025 . . . . . . 48 LEU HB1 . 7349 1 632 . 1 1 48 48 LEU HB3 H 1 1.613 0.025 . . . . . . 48 LEU HB2 . 7349 1 633 . 1 1 48 48 LEU HD11 H 1 0.598 0.025 . . . . . . 48 LEU QD1 . 7349 1 634 . 1 1 48 48 LEU HD12 H 1 0.598 0.025 . . . . . . 48 LEU QD1 . 7349 1 635 . 1 1 48 48 LEU HD13 H 1 0.598 0.025 . . . . . . 48 LEU QD1 . 7349 1 636 . 1 1 48 48 LEU HD21 H 1 0.598 0.025 . . . . . . 48 LEU QD2 . 7349 1 637 . 1 1 48 48 LEU HD22 H 1 0.598 0.025 . . . . . . 48 LEU QD2 . 7349 1 638 . 1 1 48 48 LEU HD23 H 1 0.598 0.025 . . . . . . 48 LEU QD2 . 7349 1 639 . 1 1 48 48 LEU HG H 1 1.595 0.025 . . . . . . 48 LEU HG . 7349 1 640 . 1 1 48 48 LEU C C 13 176.999 0.150 . . . . . . 48 LEU C . 7349 1 641 . 1 1 48 48 LEU CA C 13 54.733 0.257 . . . . . . 48 LEU CA . 7349 1 642 . 1 1 48 48 LEU CB C 13 39.188 0.157 . . . . . . 48 LEU CB . 7349 1 643 . 1 1 48 48 LEU CD1 C 13 22.779 0.073 . . . . . . 48 LEU CD1 . 7349 1 644 . 1 1 48 48 LEU CD2 C 13 20.334 0.056 . . . . . . 48 LEU CD2 . 7349 1 645 . 1 1 48 48 LEU CG C 13 23.638 0.200 . . . . . . 48 LEU CG . 7349 1 646 . 1 1 48 48 LEU N N 15 119.757 0.150 . . . . . . 48 LEU N . 7349 1 647 . 1 1 49 49 LYS H H 1 8.118 0.025 . . . . . . 49 LYS HN . 7349 1 648 . 1 1 49 49 LYS HA H 1 3.817 0.025 . . . . . . 49 LYS HA . 7349 1 649 . 1 1 49 49 LYS HB2 H 1 1.656 0.017 . . . . . . 49 LYS HB1 . 7349 1 650 . 1 1 49 49 LYS HB3 H 1 1.656 0.017 . . . . . . 49 LYS HB2 . 7349 1 651 . 1 1 49 49 LYS HD2 H 1 1.155 0.015 . . . . . . 49 LYS HD1 . 7349 1 652 . 1 1 49 49 LYS HD3 H 1 1.231 0.015 . . . . . . 49 LYS HD2 . 7349 1 653 . 1 1 49 49 LYS HE2 H 1 2.044 0.025 . . . . . . 49 LYS HE1 . 7349 1 654 . 1 1 49 49 LYS HE3 H 1 2.313 0.025 . . . . . . 49 LYS HE2 . 7349 1 655 . 1 1 49 49 LYS HG2 H 1 1.229 0.015 . . . . . . 49 LYS HG1 . 7349 1 656 . 1 1 49 49 LYS HG3 H 1 1.373 0.016 . . . . . . 49 LYS HG2 . 7349 1 657 . 1 1 49 49 LYS C C 13 175.843 0.150 . . . . . . 49 LYS C . 7349 1 658 . 1 1 49 49 LYS CA C 13 56.187 0.200 . . . . . . 49 LYS CA . 7349 1 659 . 1 1 49 49 LYS CB C 13 29.915 0.150 . . . . . . 49 LYS CB . 7349 1 660 . 1 1 49 49 LYS CD C 13 26.639 0.150 . . . . . . 49 LYS CD . 7349 1 661 . 1 1 49 49 LYS CE C 13 38.785 0.004 . . . . . . 49 LYS CE . 7349 1 662 . 1 1 49 49 LYS CG C 13 23.006 0.245 . . . . . . 49 LYS CG . 7349 1 663 . 1 1 49 49 LYS N N 15 118.269 0.150 . . . . . . 49 LYS N . 7349 1 664 . 1 1 50 50 THR H H 1 7.808 0.025 . . . . . . 50 THR HN . 7349 1 665 . 1 1 50 50 THR HA H 1 3.895 0.025 . . . . . . 50 THR HA . 7349 1 666 . 1 1 50 50 THR HB H 1 4.077 0.025 . . . . . . 50 THR HB . 7349 1 667 . 1 1 50 50 THR HG21 H 1 1.007 0.025 . . . . . . 50 THR QG2 . 7349 1 668 . 1 1 50 50 THR HG22 H 1 1.007 0.025 . . . . . . 50 THR QG2 . 7349 1 669 . 1 1 50 50 THR HG23 H 1 1.007 0.025 . . . . . . 50 THR QG2 . 7349 1 670 . 1 1 50 50 THR C C 13 172.581 0.150 . . . . . . 50 THR C . 7349 1 671 . 1 1 50 50 THR CA C 13 61.493 0.038 . . . . . . 50 THR CA . 7349 1 672 . 1 1 50 50 THR CB C 13 66.688 0.033 . . . . . . 50 THR CB . 7349 1 673 . 1 1 50 50 THR CG2 C 13 18.569 0.055 . . . . . . 50 THR CG2 . 7349 1 674 . 1 1 50 50 THR N N 15 113.760 0.150 . . . . . . 50 THR N . 7349 1 675 . 1 1 51 51 LYS H H 1 7.832 0.025 . . . . . . 51 LYS HN . 7349 1 676 . 1 1 51 51 LYS HA H 1 3.899 0.025 . . . . . . 51 LYS HA . 7349 1 677 . 1 1 51 51 LYS HB2 H 1 1.638 0.025 . . . . . . 51 LYS HB1 . 7349 1 678 . 1 1 51 51 LYS HB3 H 1 1.637 0.025 . . . . . . 51 LYS HB2 . 7349 1 679 . 1 1 51 51 LYS HD2 H 1 1.419 0.025 . . . . . . 51 LYS HD1 . 7349 1 680 . 1 1 51 51 LYS HD3 H 1 1.430 0.023 . . . . . . 51 LYS HD2 . 7349 1 681 . 1 1 51 51 LYS HE2 H 1 2.713 0.015 . . . . . . 51 LYS HE1 . 7349 1 682 . 1 1 51 51 LYS HE3 H 1 2.713 0.015 . . . . . . 51 LYS HE2 . 7349 1 683 . 1 1 51 51 LYS HG2 H 1 1.302 0.015 . . . . . . 51 LYS HG1 . 7349 1 684 . 1 1 51 51 LYS HG3 H 1 1.299 0.015 . . . . . . 51 LYS HG2 . 7349 1 685 . 1 1 51 51 LYS C C 13 174.435 0.150 . . . . . . 51 LYS C . 7349 1 686 . 1 1 51 51 LYS CA C 13 55.006 0.200 . . . . . . 51 LYS CA . 7349 1 687 . 1 1 51 51 LYS CB C 13 29.560 0.215 . . . . . . 51 LYS CB . 7349 1 688 . 1 1 51 51 LYS CD C 13 26.261 0.200 . . . . . . 51 LYS CD . 7349 1 689 . 1 1 51 51 LYS CE C 13 39.193 0.150 . . . . . . 51 LYS CE . 7349 1 690 . 1 1 51 51 LYS CG C 13 22.443 0.150 . . . . . . 51 LYS CG . 7349 1 691 . 1 1 51 51 LYS N N 15 122.638 0.150 . . . . . . 51 LYS N . 7349 1 692 . 1 1 52 52 LYS H H 1 7.870 0.025 . . . . . . 52 LYS HN . 7349 1 693 . 1 1 52 52 LYS HA H 1 3.963 0.025 . . . . . . 52 LYS HA . 7349 1 694 . 1 1 52 52 LYS HB2 H 1 1.602 0.025 . . . . . . 52 LYS HB1 . 7349 1 695 . 1 1 52 52 LYS HB3 H 1 1.602 0.025 . . . . . . 52 LYS HB2 . 7349 1 696 . 1 1 52 52 LYS HD2 H 1 1.395 0.015 . . . . . . 52 LYS HD1 . 7349 1 697 . 1 1 52 52 LYS HD3 H 1 1.395 0.015 . . . . . . 52 LYS HD2 . 7349 1 698 . 1 1 52 52 LYS HE2 H 1 2.721 0.015 . . . . . . 52 LYS HE1 . 7349 1 699 . 1 1 52 52 LYS HE3 H 1 2.721 0.015 . . . . . . 52 LYS HE2 . 7349 1 700 . 1 1 52 52 LYS HG2 H 1 1.124 0.025 . . . . . . 52 LYS HG1 . 7349 1 701 . 1 1 52 52 LYS HG3 H 1 1.124 0.025 . . . . . . 52 LYS HG2 . 7349 1 702 . 1 1 52 52 LYS C C 13 174.467 0.150 . . . . . . 52 LYS C . 7349 1 703 . 1 1 52 52 LYS CA C 13 54.256 0.200 . . . . . . 52 LYS CA . 7349 1 704 . 1 1 52 52 LYS CB C 13 29.858 0.200 . . . . . . 52 LYS CB . 7349 1 705 . 1 1 52 52 LYS CD C 13 26.199 0.150 . . . . . . 52 LYS CD . 7349 1 706 . 1 1 52 52 LYS CE C 13 39.185 0.150 . . . . . . 52 LYS CE . 7349 1 707 . 1 1 52 52 LYS CG C 13 21.988 0.200 . . . . . . 52 LYS CG . 7349 1 708 . 1 1 52 52 LYS N N 15 120.443 0.150 . . . . . . 52 LYS N . 7349 1 709 . 1 1 53 53 LYS H H 1 7.912 0.025 . . . . . . 53 LYS HN . 7349 1 710 . 1 1 53 53 LYS HA H 1 3.932 0.015 . . . . . . 53 LYS HA . 7349 1 711 . 1 1 53 53 LYS HB2 H 1 1.537 0.015 . . . . . . 53 LYS HB1 . 7349 1 712 . 1 1 53 53 LYS HB3 H 1 1.537 0.015 . . . . . . 53 LYS HB2 . 7349 1 713 . 1 1 53 53 LYS HD2 H 1 1.433 0.015 . . . . . . 53 LYS HD1 . 7349 1 714 . 1 1 53 53 LYS HD3 H 1 1.433 0.015 . . . . . . 53 LYS HD2 . 7349 1 715 . 1 1 53 53 LYS HE2 H 1 2.701 0.015 . . . . . . 53 LYS HE1 . 7349 1 716 . 1 1 53 53 LYS HE3 H 1 2.701 0.015 . . . . . . 53 LYS HE2 . 7349 1 717 . 1 1 53 53 LYS HG2 H 1 1.190 0.025 . . . . . . 53 LYS HG1 . 7349 1 718 . 1 1 53 53 LYS HG3 H 1 1.253 0.015 . . . . . . 53 LYS HG2 . 7349 1 719 . 1 1 53 53 LYS C C 13 174.258 0.150 . . . . . . 53 LYS C . 7349 1 720 . 1 1 53 53 LYS CA C 13 54.258 0.150 . . . . . . 53 LYS CA . 7349 1 721 . 1 1 53 53 LYS CB C 13 29.837 0.150 . . . . . . 53 LYS CB . 7349 1 722 . 1 1 53 53 LYS CD C 13 26.262 0.150 . . . . . . 53 LYS CD . 7349 1 723 . 1 1 53 53 LYS CE C 13 39.239 0.150 . . . . . . 53 LYS CE . 7349 1 724 . 1 1 53 53 LYS CG C 13 22.137 0.039 . . . . . . 53 LYS CG . 7349 1 725 . 1 1 53 53 LYS N N 15 121.411 0.150 . . . . . . 53 LYS N . 7349 1 726 . 1 1 54 54 ARG H H 1 8.002 0.025 . . . . . . 54 ARG HN . 7349 1 727 . 1 1 54 54 ARG HA H 1 3.935 0.025 . . . . . . 54 ARG HA . 7349 1 728 . 1 1 54 54 ARG HB2 H 1 1.484 0.025 . . . . . . 54 ARG HB1 . 7349 1 729 . 1 1 54 54 ARG HB3 H 1 1.484 0.025 . . . . . . 54 ARG HB2 . 7349 1 730 . 1 1 54 54 ARG HD2 H 1 2.867 0.025 . . . . . . 54 ARG HD1 . 7349 1 731 . 1 1 54 54 ARG HD3 H 1 2.867 0.025 . . . . . . 54 ARG HD2 . 7349 1 732 . 1 1 54 54 ARG HG2 H 1 1.212 0.025 . . . . . . 54 ARG HG1 . 7349 1 733 . 1 1 54 54 ARG HG3 H 1 1.320 0.025 . . . . . . 54 ARG HG2 . 7349 1 734 . 1 1 54 54 ARG C C 13 173.815 0.150 . . . . . . 54 ARG C . 7349 1 735 . 1 1 54 54 ARG CA C 13 54.150 0.200 . . . . . . 54 ARG CA . 7349 1 736 . 1 1 54 54 ARG CB C 13 27.744 0.074 . . . . . . 54 ARG CB . 7349 1 737 . 1 1 54 54 ARG CD C 13 40.418 0.200 . . . . . . 54 ARG CD . 7349 1 738 . 1 1 54 54 ARG CG C 13 24.236 0.062 . . . . . . 54 ARG CG . 7349 1 739 . 1 1 54 54 ARG N N 15 121.127 0.150 . . . . . . 54 ARG N . 7349 1 740 . 1 1 55 55 TYR H H 1 8.027 0.025 . . . . . . 55 TYR HN . 7349 1 741 . 1 1 55 55 TYR HA H 1 4.257 0.025 . . . . . . 55 TYR HA . 7349 1 742 . 1 1 55 55 TYR HB2 H 1 2.704 0.025 . . . . . . 55 TYR HB1 . 7349 1 743 . 1 1 55 55 TYR HB3 H 1 2.823 0.025 . . . . . . 55 TYR HB2 . 7349 1 744 . 1 1 55 55 TYR HD1 H 1 6.846 0.017 . . . . . . 55 TYR QD . 7349 1 745 . 1 1 55 55 TYR HD2 H 1 6.846 0.017 . . . . . . 55 TYR QD . 7349 1 746 . 1 1 55 55 TYR HE1 H 1 6.500 0.017 . . . . . . 55 TYR QE . 7349 1 747 . 1 1 55 55 TYR HE2 H 1 6.500 0.017 . . . . . . 55 TYR QE . 7349 1 748 . 1 1 55 55 TYR C C 13 173.526 0.150 . . . . . . 55 TYR C . 7349 1 749 . 1 1 55 55 TYR CA C 13 55.631 0.106 . . . . . . 55 TYR CA . 7349 1 750 . 1 1 55 55 TYR CB C 13 35.681 0.084 . . . . . . 55 TYR CB . 7349 1 751 . 1 1 55 55 TYR CD1 C 13 130.315 0.150 . . . . . . 55 TYR CD1 . 7349 1 752 . 1 1 55 55 TYR CD2 C 13 130.315 0.150 . . . . . . 55 TYR CD2 . 7349 1 753 . 1 1 55 55 TYR CE1 C 13 115.197 0.150 . . . . . . 55 TYR CE1 . 7349 1 754 . 1 1 55 55 TYR CE2 C 13 115.197 0.150 . . . . . . 55 TYR CE2 . 7349 1 755 . 1 1 55 55 TYR N N 15 120.446 0.150 . . . . . . 55 TYR N . 7349 1 756 . 1 1 56 56 SER H H 1 8.046 0.025 . . . . . . 56 SER HN . 7349 1 757 . 1 1 56 56 SER HA H 1 4.131 0.025 . . . . . . 56 SER HA . 7349 1 758 . 1 1 56 56 SER HB2 H 1 3.607 0.025 . . . . . . 56 SER HB1 . 7349 1 759 . 1 1 56 56 SER HB3 H 1 3.644 0.025 . . . . . . 56 SER HB2 . 7349 1 760 . 1 1 56 56 SER C C 13 171.968 0.150 . . . . . . 56 SER C . 7349 1 761 . 1 1 56 56 SER CA C 13 55.890 0.200 . . . . . . 56 SER CA . 7349 1 762 . 1 1 56 56 SER CB C 13 60.812 0.094 . . . . . . 56 SER CB . 7349 1 763 . 1 1 56 56 SER N N 15 116.809 0.150 . . . . . . 56 SER N . 7349 1 764 . 1 1 57 57 LEU H H 1 7.975 0.025 . . . . . . 57 LEU HN . 7349 1 765 . 1 1 57 57 LEU HA H 1 4.008 0.025 . . . . . . 57 LEU HA . 7349 1 766 . 1 1 57 57 LEU HB2 H 1 1.353 0.015 . . . . . . 57 LEU HB1 . 7349 1 767 . 1 1 57 57 LEU HB3 H 1 1.407 0.025 . . . . . . 57 LEU HB2 . 7349 1 768 . 1 1 57 57 LEU HD11 H 1 0.604 0.025 . . . . . . 57 LEU QD1 . 7349 1 769 . 1 1 57 57 LEU HD12 H 1 0.604 0.025 . . . . . . 57 LEU QD1 . 7349 1 770 . 1 1 57 57 LEU HD13 H 1 0.604 0.025 . . . . . . 57 LEU QD1 . 7349 1 771 . 1 1 57 57 LEU HD21 H 1 0.655 0.025 . . . . . . 57 LEU QD2 . 7349 1 772 . 1 1 57 57 LEU HD22 H 1 0.655 0.025 . . . . . . 57 LEU QD2 . 7349 1 773 . 1 1 57 57 LEU HD23 H 1 0.655 0.025 . . . . . . 57 LEU QD2 . 7349 1 774 . 1 1 57 57 LEU HG H 1 1.390 0.025 . . . . . . 57 LEU HG . 7349 1 775 . 1 1 57 57 LEU C C 13 174.808 0.150 . . . . . . 57 LEU C . 7349 1 776 . 1 1 57 57 LEU CA C 13 52.970 0.170 . . . . . . 57 LEU CA . 7349 1 777 . 1 1 57 57 LEU CB C 13 39.142 0.096 . . . . . . 57 LEU CB . 7349 1 778 . 1 1 57 57 LEU CD1 C 13 20.547 0.082 . . . . . . 57 LEU CD1 . 7349 1 779 . 1 1 57 57 LEU CD2 C 13 21.977 0.040 . . . . . . 57 LEU CD2 . 7349 1 780 . 1 1 57 57 LEU CG C 13 24.051 0.200 . . . . . . 57 LEU CG . 7349 1 781 . 1 1 57 57 LEU N N 15 123.508 0.150 . . . . . . 57 LEU N . 7349 1 stop_ save_