data_5250 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5250 _Entry.Title ; 1H, 13C and 15N resonance assignment of the RNA-binding domain dimer form Bacillus subtilis transcriptional antiterminator GlcT ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-01-08 _Entry.Accession_date 2002-01-08 _Entry.Last_release_date 2002-09-26 _Entry.Original_release_date 2002-09-26 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _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 Matthias Stoldt . . . 5250 2 Ines Langbein . . . 5250 3 Joerg Stuelke . . . 5250 4 Matthias Gorlach . . . 5250 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5250 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 298 5250 '15N chemical shifts' 71 5250 '1H chemical shifts' 485 5250 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 . . 2002-09-26 2002-01-08 original author . 5250 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5250 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; 1H, 13C and 15N resonance assignment of the RNA-binding domain dimer form Bacillus subtilis transcriptional antiterminator GlcT ; _Citation.Status published _Citation.Type 'BMRB only' _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Matthias Stoldt . . . 5250 1 2 Ines Langbein . . . 5250 1 3 Joerg Stuelke . . . 5250 1 4 Matthias Gorlach . . . 5250 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_GlcT-RBD _Assembly.Sf_category assembly _Assembly.Sf_framecode system_GlcT-RBD _Assembly.Entry_ID 5250 _Assembly.ID 1 _Assembly.Name 'GlcT-RBD dimer' _Assembly.BMRB_code . _Assembly.Number_of_components . _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID dimer 5250 1 stop_ 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 'GlcT-RBD subunit 1' 1 $GlcT-RBD . . . native . . 1 . . 5250 1 2 'GlcT-RBD subunit 2' 1 $GlcT-RBD . . . native . . 1 . . 5250 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID GlcT-RBD abbreviation 5250 1 'GlcT-RBD dimer' system 5250 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'transcriptional antiterminator' 5250 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_GlcT-RBD _Entity.Sf_category entity _Entity.Sf_framecode GlcT-RBD _Entity.Entry_ID 5250 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'RNA-binding domain of transcriptional antiterminator GlcT' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MRGSHHHHHHGSVDVNGSFT VKKVLNNNVLIASHHKYSEV VLIGKGIGFGKKQDDVIEDK GYDKMFILKDEKEQ ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 74 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 3RIO . "Crystal Structure Of Glct Cat-Prdi" . . . . . 81.08 180 100.00 100.00 1.13e-31 . . . . 5250 1 2 no DBJ BAI84997 . "BglG family transcriptional antiterminator [Bacillus subtilis subsp. natto BEST195]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 3 no DBJ BAM52031 . "transcriptional antiterminator BglG family [Synechocystis sp. PCC 6803]" . . . . . 81.08 288 100.00 100.00 1.56e-31 . . . . 5250 1 4 no DBJ BAM57608 . "transcriptional antiterminator BglG family [Bacillus subtilis BEST7003]" . . . . . 81.08 281 98.33 100.00 4.46e-31 . . . . 5250 1 5 no DBJ GAK78204 . "transcriptional antiterminator [Bacillus subtilis Miyagi-4]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 6 no EMBL CAA72077 . "transcription antiterminator [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 81.08 281 98.33 100.00 4.46e-31 . . . . 5250 1 7 no EMBL CAB13261 . "transcriptional antiterminator (BglG family) [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 81.08 288 100.00 100.00 1.56e-31 . . . . 5250 1 8 no EMBL CCU57949 . "transcriptional antiterminator (BglG family) [Bacillus subtilis E1]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 9 no EMBL CEI56549 . "BglG family transcription antiterminator [Bacillus subtilis]" . . . . . 81.08 281 98.33 100.00 4.46e-31 . . . . 5250 1 10 no EMBL CEJ76972 . "BglG family transcription antiterminator [Bacillus sp.]" . . . . . 81.08 281 98.33 100.00 4.46e-31 . . . . 5250 1 11 no GB ADM37475 . "transcriptional antiterminator (BglG family) protein [Bacillus subtilis subsp. spizizenii str. W23]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 12 no GB ADV96407 . "transcriptional antiterminator (BglG family) protein [Bacillus subtilis BSn5]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 13 no GB AEP86362 . "transcription antiterminator, GlcT [Bacillus subtilis subsp. spizizenii TU-B-10]" . . . . . 81.08 281 98.33 100.00 4.75e-31 . . . . 5250 1 14 no GB AEP90533 . "transcription antiterminator, GlcT [Bacillus subtilis subsp. subtilis str. RO-NN-1]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 15 no GB AFI28059 . "transcriptional antiterminator (BglG family) protein [Bacillus sp. JS]" . . . . . 81.08 288 100.00 100.00 1.54e-31 . . . . 5250 1 16 no REF NP_389271 . "BglG family transcription antiterminator [Bacillus subtilis subsp. subtilis str. 168]" . . . . . 81.08 288 100.00 100.00 1.56e-31 . . . . 5250 1 17 no REF WP_003218635 . "MULTISPECIES: transcriptional antiterminator (BglG family) protein [Bacillales]" . . . . . 81.08 288 100.00 100.00 1.50e-31 . . . . 5250 1 18 no REF WP_003232429 . "transcriptional antiterminator (BglG family) protein [Bacillus subtilis]" . . . . . 81.08 288 100.00 100.00 1.59e-31 . . . . 5250 1 19 no REF WP_003238961 . "transcriptional antiterminator (BglG family) protein [Bacillus subtilis]" . . . . . 81.08 281 98.33 100.00 5.06e-31 . . . . 5250 1 20 no REF WP_009967114 . "BglG family transcriptional antiterminator [Bacillus subtilis]" . . . . . 81.08 288 100.00 100.00 1.56e-31 . . . . 5250 1 21 no SP O31691 . "RecName: Full=PtsGHI operon antiterminator; AltName: Full=RNA-binding antitermination protein GlcT [Bacillus subtilis subsp. su" . . . . . 81.08 281 98.33 100.00 4.46e-31 . . . . 5250 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID GlcT-RBD abbreviation 5250 1 'RNA-binding domain of transcriptional antiterminator GlcT' common 5250 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 . 5250 1 2 . ARG . 5250 1 3 . GLY . 5250 1 4 . SER . 5250 1 5 . HIS . 5250 1 6 . HIS . 5250 1 7 . HIS . 5250 1 8 . HIS . 5250 1 9 . HIS . 5250 1 10 . HIS . 5250 1 11 . GLY . 5250 1 12 . SER . 5250 1 13 . VAL . 5250 1 14 . ASP . 5250 1 15 . VAL . 5250 1 16 . ASN . 5250 1 17 . GLY . 5250 1 18 . SER . 5250 1 19 . PHE . 5250 1 20 . THR . 5250 1 21 . VAL . 5250 1 22 . LYS . 5250 1 23 . LYS . 5250 1 24 . VAL . 5250 1 25 . LEU . 5250 1 26 . ASN . 5250 1 27 . ASN . 5250 1 28 . ASN . 5250 1 29 . VAL . 5250 1 30 . LEU . 5250 1 31 . ILE . 5250 1 32 . ALA . 5250 1 33 . SER . 5250 1 34 . HIS . 5250 1 35 . HIS . 5250 1 36 . LYS . 5250 1 37 . TYR . 5250 1 38 . SER . 5250 1 39 . GLU . 5250 1 40 . VAL . 5250 1 41 . VAL . 5250 1 42 . LEU . 5250 1 43 . ILE . 5250 1 44 . GLY . 5250 1 45 . LYS . 5250 1 46 . GLY . 5250 1 47 . ILE . 5250 1 48 . GLY . 5250 1 49 . PHE . 5250 1 50 . GLY . 5250 1 51 . LYS . 5250 1 52 . LYS . 5250 1 53 . GLN . 5250 1 54 . ASP . 5250 1 55 . ASP . 5250 1 56 . VAL . 5250 1 57 . ILE . 5250 1 58 . GLU . 5250 1 59 . ASP . 5250 1 60 . LYS . 5250 1 61 . GLY . 5250 1 62 . TYR . 5250 1 63 . ASP . 5250 1 64 . LYS . 5250 1 65 . MET . 5250 1 66 . PHE . 5250 1 67 . ILE . 5250 1 68 . LEU . 5250 1 69 . LYS . 5250 1 70 . ASP . 5250 1 71 . GLU . 5250 1 72 . LYS . 5250 1 73 . GLU . 5250 1 74 . GLN . 5250 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 5250 1 . ARG 2 2 5250 1 . GLY 3 3 5250 1 . SER 4 4 5250 1 . HIS 5 5 5250 1 . HIS 6 6 5250 1 . HIS 7 7 5250 1 . HIS 8 8 5250 1 . HIS 9 9 5250 1 . HIS 10 10 5250 1 . GLY 11 11 5250 1 . SER 12 12 5250 1 . VAL 13 13 5250 1 . ASP 14 14 5250 1 . VAL 15 15 5250 1 . ASN 16 16 5250 1 . GLY 17 17 5250 1 . SER 18 18 5250 1 . PHE 19 19 5250 1 . THR 20 20 5250 1 . VAL 21 21 5250 1 . LYS 22 22 5250 1 . LYS 23 23 5250 1 . VAL 24 24 5250 1 . LEU 25 25 5250 1 . ASN 26 26 5250 1 . ASN 27 27 5250 1 . ASN 28 28 5250 1 . VAL 29 29 5250 1 . LEU 30 30 5250 1 . ILE 31 31 5250 1 . ALA 32 32 5250 1 . SER 33 33 5250 1 . HIS 34 34 5250 1 . HIS 35 35 5250 1 . LYS 36 36 5250 1 . TYR 37 37 5250 1 . SER 38 38 5250 1 . GLU 39 39 5250 1 . VAL 40 40 5250 1 . VAL 41 41 5250 1 . LEU 42 42 5250 1 . ILE 43 43 5250 1 . GLY 44 44 5250 1 . LYS 45 45 5250 1 . GLY 46 46 5250 1 . ILE 47 47 5250 1 . GLY 48 48 5250 1 . PHE 49 49 5250 1 . GLY 50 50 5250 1 . LYS 51 51 5250 1 . LYS 52 52 5250 1 . GLN 53 53 5250 1 . ASP 54 54 5250 1 . ASP 55 55 5250 1 . VAL 56 56 5250 1 . ILE 57 57 5250 1 . GLU 58 58 5250 1 . ASP 59 59 5250 1 . LYS 60 60 5250 1 . GLY 61 61 5250 1 . TYR 62 62 5250 1 . ASP 63 63 5250 1 . LYS 64 64 5250 1 . MET 65 65 5250 1 . PHE 66 66 5250 1 . ILE 67 67 5250 1 . LEU 68 68 5250 1 . LYS 69 69 5250 1 . ASP 70 70 5250 1 . GLU 71 71 5250 1 . LYS 72 72 5250 1 . GLU 73 73 5250 1 . GLN 74 74 5250 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 5250 _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 $GlcT-RBD . 1423 . . 'Bacillus subtilis' 'Bacillus subtilis' . . Eubacteria . Bacillus subtilis . . . . . . . . . . . . . . . . . . . . . 5250 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 5250 _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 $GlcT-RBD . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5250 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5250 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 'RNA-binding domain of transcriptional antiterminator GlcT' '[U-13C; U-15N]' . . 1 $GlcT-RBD . . . 2.0 3.0 mM . . . . 5250 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 5250 _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 pH 6.5 0.1 n/a 5250 1 temperature 298 0.2 K 5250 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5250 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UnityINOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5250 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UnityINOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5250 _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 NMR_spectrometer_1 Varian UnityINOVA . 600 . . . 5250 1 2 NMR_spectrometer_2 Varian UnityINOVA . 750 . . . 5250 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 5250 _Experiment_list.ID 1 _Experiment_list.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5250 _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 0.0 . indirect 0.251449530 . . . . . . . . . 5250 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5250 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5250 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5250 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 $sample_1 . 5250 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 CA C 13 55.6 0.05 . 1 . . . . . . . . 5250 1 2 . 1 1 1 1 MET HA H 1 4.01 0.02 . 1 . . . . . . . . 5250 1 3 . 1 1 1 1 MET CB C 13 33.9 0.05 . 1 . . . . . . . . 5250 1 4 . 1 1 1 1 MET HB2 H 1 2.06 0.02 . 1 . . . . . . . . 5250 1 5 . 1 1 1 1 MET HB3 H 1 2.06 0.02 . 1 . . . . . . . . 5250 1 6 . 1 1 1 1 MET CG C 13 31.3 0.05 . 1 . . . . . . . . 5250 1 7 . 1 1 1 1 MET HG2 H 1 2.53 0.02 . 1 . . . . . . . . 5250 1 8 . 1 1 1 1 MET HG3 H 1 2.53 0.02 . 1 . . . . . . . . 5250 1 9 . 1 1 1 1 MET HE1 H 1 2.02 0.02 . 1 . . . . . . . . 5250 1 10 . 1 1 1 1 MET HE2 H 1 2.02 0.02 . 1 . . . . . . . . 5250 1 11 . 1 1 1 1 MET HE3 H 1 2.02 0.02 . 1 . . . . . . . . 5250 1 12 . 1 1 1 1 MET CE C 13 17.1 0.05 . 1 . . . . . . . . 5250 1 13 . 1 1 2 2 ARG CA C 13 56.8 0.05 . 1 . . . . . . . . 5250 1 14 . 1 1 2 2 ARG HA H 1 4.34 0.02 . 1 . . . . . . . . 5250 1 15 . 1 1 2 2 ARG CB C 13 31.0 0.05 . 1 . . . . . . . . 5250 1 16 . 1 1 2 2 ARG HB2 H 1 1.76 0.02 . 2 . . . . . . . . 5250 1 17 . 1 1 2 2 ARG HB3 H 1 1.82 0.02 . 2 . . . . . . . . 5250 1 18 . 1 1 2 2 ARG CG C 13 27.3 0.05 . 1 . . . . . . . . 5250 1 19 . 1 1 2 2 ARG HG2 H 1 1.61 0.02 . 2 . . . . . . . . 5250 1 20 . 1 1 2 2 ARG HG3 H 1 1.63 0.02 . 2 . . . . . . . . 5250 1 21 . 1 1 2 2 ARG CD C 13 43.6 0.05 . 1 . . . . . . . . 5250 1 22 . 1 1 2 2 ARG HD2 H 1 3.14 0.02 . 1 . . . . . . . . 5250 1 23 . 1 1 2 2 ARG HD3 H 1 3.14 0.02 . 1 . . . . . . . . 5250 1 24 . 1 1 3 3 GLY N N 15 114.4 0.05 . 1 . . . . . . . . 5250 1 25 . 1 1 3 3 GLY H H 1 8.59 0.02 . 1 . . . . . . . . 5250 1 26 . 1 1 3 3 GLY CA C 13 45.5 0.05 . 1 . . . . . . . . 5250 1 27 . 1 1 3 3 GLY HA2 H 1 3.92 0.02 . 1 . . . . . . . . 5250 1 28 . 1 1 3 3 GLY HA3 H 1 3.92 0.02 . 1 . . . . . . . . 5250 1 29 . 1 1 4 4 SER N N 15 119.3 0.05 . 1 . . . . . . . . 5250 1 30 . 1 1 4 4 SER H H 1 8.22 0.02 . 1 . . . . . . . . 5250 1 31 . 1 1 4 4 SER CA C 13 58.6 0.05 . 1 . . . . . . . . 5250 1 32 . 1 1 4 4 SER HA H 1 4.46 0.02 . 1 . . . . . . . . 5250 1 33 . 1 1 4 4 SER CB C 13 64.2 0.05 . 1 . . . . . . . . 5250 1 34 . 1 1 4 4 SER HB2 H 1 3.81 0.02 . 1 . . . . . . . . 5250 1 35 . 1 1 4 4 SER HB3 H 1 3.81 0.02 . 1 . . . . . . . . 5250 1 36 . 1 1 4 4 SER C C 13 176.8 0.05 . 1 . . . . . . . . 5250 1 37 . 1 1 5 5 HIS C C 13 174.2 0.05 . 1 . . . . . . . . 5250 1 38 . 1 1 10 10 HIS CA C 13 56.5 0.05 . 1 . . . . . . . . 5250 1 39 . 1 1 10 10 HIS HA H 1 4.58 0.02 . 1 . . . . . . . . 5250 1 40 . 1 1 10 10 HIS CB C 13 30.4 0.05 . 1 . . . . . . . . 5250 1 41 . 1 1 10 10 HIS HB2 H 1 3.04 0.02 . 2 . . . . . . . . 5250 1 42 . 1 1 10 10 HIS HB3 H 1 3.14 0.02 . 2 . . . . . . . . 5250 1 43 . 1 1 10 10 HIS C C 13 175.7 0.05 . 1 . . . . . . . . 5250 1 44 . 1 1 11 11 GLY N N 15 113.9 0.05 . 1 . . . . . . . . 5250 1 45 . 1 1 11 11 GLY H H 1 8.43 0.02 . 1 . . . . . . . . 5250 1 46 . 1 1 11 11 GLY CA C 13 45.5 0.05 . 1 . . . . . . . . 5250 1 47 . 1 1 11 11 GLY HA2 H 1 3.95 0.02 . 1 . . . . . . . . 5250 1 48 . 1 1 11 11 GLY HA3 H 1 3.95 0.02 . 1 . . . . . . . . 5250 1 49 . 1 1 11 11 GLY C C 13 174.3 0.05 . 1 . . . . . . . . 5250 1 50 . 1 1 12 12 SER N N 15 118.7 0.05 . 1 . . . . . . . . 5250 1 51 . 1 1 12 12 SER H H 1 8.18 0.02 . 1 . . . . . . . . 5250 1 52 . 1 1 12 12 SER CA C 13 58.6 0.05 . 1 . . . . . . . . 5250 1 53 . 1 1 12 12 SER HA H 1 4.36 0.02 . 1 . . . . . . . . 5250 1 54 . 1 1 12 12 SER CB C 13 64.1 0.05 . 1 . . . . . . . . 5250 1 55 . 1 1 12 12 SER HB2 H 1 3.73 0.02 . 2 . . . . . . . . 5250 1 56 . 1 1 12 12 SER HB3 H 1 3.76 0.02 . 2 . . . . . . . . 5250 1 57 . 1 1 12 12 SER C C 13 174.9 0.05 . 1 . . . . . . . . 5250 1 58 . 1 1 13 13 VAL N N 15 124.3 0.05 . 1 . . . . . . . . 5250 1 59 . 1 1 13 13 VAL H H 1 8.11 0.02 . 1 . . . . . . . . 5250 1 60 . 1 1 13 13 VAL CA C 13 62.4 0.05 . 1 . . . . . . . . 5250 1 61 . 1 1 13 13 VAL HA H 1 4.09 0.02 . 1 . . . . . . . . 5250 1 62 . 1 1 13 13 VAL CB C 13 33.1 0.05 . 1 . . . . . . . . 5250 1 63 . 1 1 13 13 VAL HB H 1 2.02 0.02 . 1 . . . . . . . . 5250 1 64 . 1 1 13 13 VAL HG11 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 65 . 1 1 13 13 VAL HG12 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 66 . 1 1 13 13 VAL HG13 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 67 . 1 1 13 13 VAL HG21 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 68 . 1 1 13 13 VAL HG22 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 69 . 1 1 13 13 VAL HG23 H 1 0.83 0.02 . 1 . . . . . . . . 5250 1 70 . 1 1 13 13 VAL CG1 C 13 21.4 0.05 . 1 . . . . . . . . 5250 1 71 . 1 1 13 13 VAL CG2 C 13 20.6 0.05 . 1 . . . . . . . . 5250 1 72 . 1 1 13 13 VAL C C 13 175.9 0.05 . 1 . . . . . . . . 5250 1 73 . 1 1 14 14 ASP N N 15 127.3 0.05 . 1 . . . . . . . . 5250 1 74 . 1 1 14 14 ASP H H 1 8.33 0.02 . 1 . . . . . . . . 5250 1 75 . 1 1 14 14 ASP CA C 13 54.4 0.05 . 1 . . . . . . . . 5250 1 76 . 1 1 14 14 ASP HA H 1 4.57 0.02 . 1 . . . . . . . . 5250 1 77 . 1 1 14 14 ASP CB C 13 41.5 0.05 . 1 . . . . . . . . 5250 1 78 . 1 1 14 14 ASP HB2 H 1 2.50 0.02 . 2 . . . . . . . . 5250 1 79 . 1 1 14 14 ASP HB3 H 1 2.64 0.02 . 2 . . . . . . . . 5250 1 80 . 1 1 14 14 ASP C C 13 176.6 0.05 . 1 . . . . . . . . 5250 1 81 . 1 1 15 15 VAL N N 15 123.8 0.05 . 1 . . . . . . . . 5250 1 82 . 1 1 15 15 VAL H H 1 8.04 0.02 . 1 . . . . . . . . 5250 1 83 . 1 1 15 15 VAL CA C 13 62.7 0.05 . 1 . . . . . . . . 5250 1 84 . 1 1 15 15 VAL HA H 1 4.00 0.02 . 1 . . . . . . . . 5250 1 85 . 1 1 15 15 VAL CB C 13 32.7 0.05 . 1 . . . . . . . . 5250 1 86 . 1 1 15 15 VAL HB H 1 2.00 0.02 . 1 . . . . . . . . 5250 1 87 . 1 1 15 15 VAL HG11 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 88 . 1 1 15 15 VAL HG12 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 89 . 1 1 15 15 VAL HG13 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 90 . 1 1 15 15 VAL HG21 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 91 . 1 1 15 15 VAL HG22 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 92 . 1 1 15 15 VAL HG23 H 1 0.79 0.02 . 1 . . . . . . . . 5250 1 93 . 1 1 15 15 VAL CG1 C 13 20.3 0.05 . 1 . . . . . . . . 5250 1 94 . 1 1 15 15 VAL CG2 C 13 21.4 0.05 . 1 . . . . . . . . 5250 1 95 . 1 1 15 15 VAL C C 13 176.3 0.05 . 1 . . . . . . . . 5250 1 96 . 1 1 16 16 ASN N N 15 124.6 0.05 . 1 . . . . . . . . 5250 1 97 . 1 1 16 16 ASN H H 1 8.41 0.02 . 1 . . . . . . . . 5250 1 98 . 1 1 16 16 ASN CA C 13 53.9 0.05 . 1 . . . . . . . . 5250 1 99 . 1 1 16 16 ASN HA H 1 4.64 0.02 . 1 . . . . . . . . 5250 1 100 . 1 1 16 16 ASN CB C 13 39.4 0.05 . 1 . . . . . . . . 5250 1 101 . 1 1 16 16 ASN HB2 H 1 2.71 0.02 . 1 . . . . . . . . 5250 1 102 . 1 1 16 16 ASN HB3 H 1 2.71 0.02 . 1 . . . . . . . . 5250 1 103 . 1 1 16 16 ASN ND2 N 15 116.8 0.05 . 1 . . . . . . . . 5250 1 104 . 1 1 16 16 ASN HD21 H 1 6.84 0.02 . 2 . . . . . . . . 5250 1 105 . 1 1 16 16 ASN HD22 H 1 7.62 0.02 . 2 . . . . . . . . 5250 1 106 . 1 1 16 16 ASN C C 13 176.0 0.05 . 1 . . . . . . . . 5250 1 107 . 1 1 17 17 GLY N N 15 112.8 0.05 . 1 . . . . . . . . 5250 1 108 . 1 1 17 17 GLY H H 1 8.21 0.02 . 1 . . . . . . . . 5250 1 109 . 1 1 17 17 GLY CA C 13 45.8 0.05 . 1 . . . . . . . . 5250 1 110 . 1 1 17 17 GLY HA2 H 1 3.86 0.02 . 2 . . . . . . . . 5250 1 111 . 1 1 17 17 GLY HA3 H 1 3.90 0.02 . 2 . . . . . . . . 5250 1 112 . 1 1 17 17 GLY C C 13 173.4 0.05 . 1 . . . . . . . . 5250 1 113 . 1 1 18 18 SER N N 15 117.4 0.05 . 1 . . . . . . . . 5250 1 114 . 1 1 18 18 SER H H 1 7.69 0.02 . 1 . . . . . . . . 5250 1 115 . 1 1 18 18 SER CA C 13 58.3 0.05 . 1 . . . . . . . . 5250 1 116 . 1 1 18 18 SER HA H 1 4.61 0.02 . 1 . . . . . . . . 5250 1 117 . 1 1 18 18 SER CB C 13 65.2 0.05 . 1 . . . . . . . . 5250 1 118 . 1 1 18 18 SER HB2 H 1 3.66 0.02 . 2 . . . . . . . . 5250 1 119 . 1 1 18 18 SER HB3 H 1 3.77 0.02 . 2 . . . . . . . . 5250 1 120 . 1 1 18 18 SER C C 13 173.3 0.05 . 1 . . . . . . . . 5250 1 121 . 1 1 19 19 PHE N N 15 122.6 0.05 . 1 . . . . . . . . 5250 1 122 . 1 1 19 19 PHE H H 1 8.76 0.02 . 1 . . . . . . . . 5250 1 123 . 1 1 19 19 PHE CA C 13 56.7 0.05 . 1 . . . . . . . . 5250 1 124 . 1 1 19 19 PHE HA H 1 5.32 0.02 . 1 . . . . . . . . 5250 1 125 . 1 1 19 19 PHE CB C 13 42.0 0.05 . 1 . . . . . . . . 5250 1 126 . 1 1 19 19 PHE HB2 H 1 2.78 0.02 . 2 . . . . . . . . 5250 1 127 . 1 1 19 19 PHE HB3 H 1 2.91 0.02 . 2 . . . . . . . . 5250 1 128 . 1 1 19 19 PHE CD1 C 13 131.8 0.05 . 1 . . . . . . . . 5250 1 129 . 1 1 19 19 PHE HD1 H 1 7.11 0.02 . 1 . . . . . . . . 5250 1 130 . 1 1 19 19 PHE CE1 C 13 132.0 0.05 . 1 . . . . . . . . 5250 1 131 . 1 1 19 19 PHE HE1 H 1 7.24 0.02 . 1 . . . . . . . . 5250 1 132 . 1 1 19 19 PHE CZ C 13 130.5 0.05 . 1 . . . . . . . . 5250 1 133 . 1 1 19 19 PHE HZ H 1 7.16 0.02 . 1 . . . . . . . . 5250 1 134 . 1 1 19 19 PHE C C 13 175.7 0.05 . 1 . . . . . . . . 5250 1 135 . 1 1 20 20 THR N N 15 120.1 0.05 . 1 . . . . . . . . 5250 1 136 . 1 1 20 20 THR H H 1 8.40 0.02 . 1 . . . . . . . . 5250 1 137 . 1 1 20 20 THR CA C 13 61.8 0.05 . 1 . . . . . . . . 5250 1 138 . 1 1 20 20 THR HA H 1 5.08 0.02 . 1 . . . . . . . . 5250 1 139 . 1 1 20 20 THR CB C 13 69.9 0.05 . 1 . . . . . . . . 5250 1 140 . 1 1 20 20 THR HB H 1 4.01 0.02 . 1 . . . . . . . . 5250 1 141 . 1 1 20 20 THR HG21 H 1 1.09 0.02 . 1 . . . . . . . . 5250 1 142 . 1 1 20 20 THR HG22 H 1 1.09 0.02 . 1 . . . . . . . . 5250 1 143 . 1 1 20 20 THR HG23 H 1 1.09 0.02 . 1 . . . . . . . . 5250 1 144 . 1 1 20 20 THR CG2 C 13 21.9 0.05 . 1 . . . . . . . . 5250 1 145 . 1 1 20 20 THR C C 13 175.2 0.05 . 1 . . . . . . . . 5250 1 146 . 1 1 21 21 VAL N N 15 130.3 0.05 . 1 . . . . . . . . 5250 1 147 . 1 1 21 21 VAL H H 1 9.57 0.02 . 1 . . . . . . . . 5250 1 148 . 1 1 21 21 VAL CA C 13 66.2 0.05 . 1 . . . . . . . . 5250 1 149 . 1 1 21 21 VAL HA H 1 3.41 0.02 . 1 . . . . . . . . 5250 1 150 . 1 1 21 21 VAL CB C 13 32.4 0.05 . 1 . . . . . . . . 5250 1 151 . 1 1 21 21 VAL HB H 1 2.31 0.02 . 1 . . . . . . . . 5250 1 152 . 1 1 21 21 VAL HG11 H 1 0.61 0.02 . 2 . . . . . . . . 5250 1 153 . 1 1 21 21 VAL HG12 H 1 0.61 0.02 . 2 . . . . . . . . 5250 1 154 . 1 1 21 21 VAL HG13 H 1 0.61 0.02 . 2 . . . . . . . . 5250 1 155 . 1 1 21 21 VAL HG21 H 1 0.94 0.02 . 2 . . . . . . . . 5250 1 156 . 1 1 21 21 VAL HG22 H 1 0.94 0.02 . 2 . . . . . . . . 5250 1 157 . 1 1 21 21 VAL HG23 H 1 0.94 0.02 . 2 . . . . . . . . 5250 1 158 . 1 1 21 21 VAL CG1 C 13 22.6 0.05 . 1 . . . . . . . . 5250 1 159 . 1 1 21 21 VAL CG2 C 13 24.0 0.05 . 1 . . . . . . . . 5250 1 160 . 1 1 21 21 VAL C C 13 176.3 0.05 . 1 . . . . . . . . 5250 1 161 . 1 1 22 22 LYS N N 15 133.1 0.05 . 1 . . . . . . . . 5250 1 162 . 1 1 22 22 LYS H H 1 9.72 0.02 . 1 . . . . . . . . 5250 1 163 . 1 1 22 22 LYS CA C 13 57.7 0.05 . 1 . . . . . . . . 5250 1 164 . 1 1 22 22 LYS HA H 1 4.56 0.02 . 1 . . . . . . . . 5250 1 165 . 1 1 22 22 LYS CB C 13 33.9 0.05 . 1 . . . . . . . . 5250 1 166 . 1 1 22 22 LYS HB2 H 1 1.46 0.02 . 2 . . . . . . . . 5250 1 167 . 1 1 22 22 LYS HB3 H 1 1.77 0.02 . 2 . . . . . . . . 5250 1 168 . 1 1 22 22 LYS CG C 13 25.0 0.05 . 1 . . . . . . . . 5250 1 169 . 1 1 22 22 LYS HG2 H 1 1.38 0.02 . 2 . . . . . . . . 5250 1 170 . 1 1 22 22 LYS HG3 H 1 1.56 0.02 . 2 . . . . . . . . 5250 1 171 . 1 1 22 22 LYS CD C 13 29.1 0.05 . 1 . . . . . . . . 5250 1 172 . 1 1 22 22 LYS HD2 H 1 1.59 0.02 . 2 . . . . . . . . 5250 1 173 . 1 1 22 22 LYS HD3 H 1 1.70 0.02 . 2 . . . . . . . . 5250 1 174 . 1 1 22 22 LYS CE C 13 41.9 0.05 . 1 . . . . . . . . 5250 1 175 . 1 1 22 22 LYS HE2 H 1 2.94 0.02 . 1 . . . . . . . . 5250 1 176 . 1 1 22 22 LYS HE3 H 1 2.94 0.02 . 1 . . . . . . . . 5250 1 177 . 1 1 22 22 LYS C C 13 175.8 0.05 . 1 . . . . . . . . 5250 1 178 . 1 1 23 23 LYS N N 15 120.0 0.05 . 1 . . . . . . . . 5250 1 179 . 1 1 23 23 LYS H H 1 7.77 0.02 . 1 . . . . . . . . 5250 1 180 . 1 1 23 23 LYS CA C 13 56.1 0.05 . 1 . . . . . . . . 5250 1 181 . 1 1 23 23 LYS HA H 1 4.36 0.02 . 1 . . . . . . . . 5250 1 182 . 1 1 23 23 LYS CB C 13 36.7 0.05 . 1 . . . . . . . . 5250 1 183 . 1 1 23 23 LYS HB2 H 1 1.52 0.02 . 2 . . . . . . . . 5250 1 184 . 1 1 23 23 LYS HB3 H 1 1.66 0.02 . 2 . . . . . . . . 5250 1 185 . 1 1 23 23 LYS CG C 13 25.0 0.05 . 1 . . . . . . . . 5250 1 186 . 1 1 23 23 LYS HG2 H 1 1.14 0.02 . 2 . . . . . . . . 5250 1 187 . 1 1 23 23 LYS HG3 H 1 1.22 0.02 . 2 . . . . . . . . 5250 1 188 . 1 1 23 23 LYS CD C 13 29.3 0.05 . 1 . . . . . . . . 5250 1 189 . 1 1 23 23 LYS HD2 H 1 1.59 0.02 . 1 . . . . . . . . 5250 1 190 . 1 1 23 23 LYS HD3 H 1 1.59 0.02 . 1 . . . . . . . . 5250 1 191 . 1 1 23 23 LYS CE C 13 42.2 0.05 . 1 . . . . . . . . 5250 1 192 . 1 1 23 23 LYS HE2 H 1 2.88 0.02 . 2 . . . . . . . . 5250 1 193 . 1 1 23 23 LYS HE3 H 1 2.90 0.02 . 2 . . . . . . . . 5250 1 194 . 1 1 23 23 LYS C C 13 174.2 0.05 . 1 . . . . . . . . 5250 1 195 . 1 1 24 24 VAL N N 15 131.2 0.05 . 1 . . . . . . . . 5250 1 196 . 1 1 24 24 VAL H H 1 9.11 0.02 . 1 . . . . . . . . 5250 1 197 . 1 1 24 24 VAL CA C 13 63.1 0.05 . 1 . . . . . . . . 5250 1 198 . 1 1 24 24 VAL HA H 1 3.98 0.02 . 1 . . . . . . . . 5250 1 199 . 1 1 24 24 VAL CB C 13 32.3 0.05 . 1 . . . . . . . . 5250 1 200 . 1 1 24 24 VAL HB H 1 1.97 0.02 . 1 . . . . . . . . 5250 1 201 . 1 1 24 24 VAL HG11 H 1 0.70 0.02 . 2 . . . . . . . . 5250 1 202 . 1 1 24 24 VAL HG12 H 1 0.70 0.02 . 2 . . . . . . . . 5250 1 203 . 1 1 24 24 VAL HG13 H 1 0.70 0.02 . 2 . . . . . . . . 5250 1 204 . 1 1 24 24 VAL HG21 H 1 0.83 0.02 . 2 . . . . . . . . 5250 1 205 . 1 1 24 24 VAL HG22 H 1 0.83 0.02 . 2 . . . . . . . . 5250 1 206 . 1 1 24 24 VAL HG23 H 1 0.83 0.02 . 2 . . . . . . . . 5250 1 207 . 1 1 24 24 VAL CG1 C 13 21.7 0.05 . 1 . . . . . . . . 5250 1 208 . 1 1 24 24 VAL CG2 C 13 22.3 0.05 . 1 . . . . . . . . 5250 1 209 . 1 1 24 24 VAL C C 13 176.2 0.05 . 1 . . . . . . . . 5250 1 210 . 1 1 25 25 LEU N N 15 131.6 0.05 . 1 . . . . . . . . 5250 1 211 . 1 1 25 25 LEU H H 1 8.37 0.02 . 1 . . . . . . . . 5250 1 212 . 1 1 25 25 LEU CA C 13 57.2 0.05 . 1 . . . . . . . . 5250 1 213 . 1 1 25 25 LEU HA H 1 4.30 0.02 . 1 . . . . . . . . 5250 1 214 . 1 1 25 25 LEU CB C 13 42.2 0.05 . 1 . . . . . . . . 5250 1 215 . 1 1 25 25 LEU HB2 H 1 1.18 0.02 . 2 . . . . . . . . 5250 1 216 . 1 1 25 25 LEU HB3 H 1 1.43 0.02 . 2 . . . . . . . . 5250 1 217 . 1 1 25 25 LEU CG C 13 28.2 0.05 . 1 . . . . . . . . 5250 1 218 . 1 1 25 25 LEU HG H 1 1.39 0.02 . 1 . . . . . . . . 5250 1 219 . 1 1 25 25 LEU HD11 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 220 . 1 1 25 25 LEU HD12 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 221 . 1 1 25 25 LEU HD13 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 222 . 1 1 25 25 LEU HD21 H 1 0.64 0.02 . 2 . . . . . . . . 5250 1 223 . 1 1 25 25 LEU HD22 H 1 0.64 0.02 . 2 . . . . . . . . 5250 1 224 . 1 1 25 25 LEU HD23 H 1 0.64 0.02 . 2 . . . . . . . . 5250 1 225 . 1 1 25 25 LEU CD1 C 13 25.7 0.05 . 1 . . . . . . . . 5250 1 226 . 1 1 25 25 LEU CD2 C 13 23.7 0.05 . 1 . . . . . . . . 5250 1 227 . 1 1 25 25 LEU C C 13 177.5 0.05 . 1 . . . . . . . . 5250 1 228 . 1 1 26 26 ASN N N 15 117.5 0.05 . 1 . . . . . . . . 5250 1 229 . 1 1 26 26 ASN H H 1 8.44 0.02 . 1 . . . . . . . . 5250 1 230 . 1 1 26 26 ASN CA C 13 53.1 0.05 . 1 . . . . . . . . 5250 1 231 . 1 1 26 26 ASN HA H 1 4.44 0.02 . 1 . . . . . . . . 5250 1 232 . 1 1 26 26 ASN CB C 13 37.5 0.05 . 1 . . . . . . . . 5250 1 233 . 1 1 26 26 ASN HB2 H 1 3.24 0.02 . 2 . . . . . . . . 5250 1 234 . 1 1 26 26 ASN HB3 H 1 3.31 0.02 . 2 . . . . . . . . 5250 1 235 . 1 1 26 26 ASN ND2 N 15 114.4 0.05 . 1 . . . . . . . . 5250 1 236 . 1 1 26 26 ASN HD21 H 1 6.49 0.02 . 2 . . . . . . . . 5250 1 237 . 1 1 26 26 ASN HD22 H 1 7.72 0.02 . 2 . . . . . . . . 5250 1 238 . 1 1 26 26 ASN C C 13 174.1 0.05 . 1 . . . . . . . . 5250 1 239 . 1 1 27 27 ASN N N 15 115.1 0.05 . 1 . . . . . . . . 5250 1 240 . 1 1 27 27 ASN H H 1 8.33 0.02 . 1 . . . . . . . . 5250 1 241 . 1 1 27 27 ASN CA C 13 56.3 0.05 . 1 . . . . . . . . 5250 1 242 . 1 1 27 27 ASN HA H 1 4.18 0.02 . 1 . . . . . . . . 5250 1 243 . 1 1 27 27 ASN CB C 13 38.8 0.05 . 1 . . . . . . . . 5250 1 244 . 1 1 27 27 ASN HB2 H 1 2.69 0.02 . 1 . . . . . . . . 5250 1 245 . 1 1 27 27 ASN HB3 H 1 2.69 0.02 . 1 . . . . . . . . 5250 1 246 . 1 1 27 27 ASN ND2 N 15 115.6 0.05 . 1 . . . . . . . . 5250 1 247 . 1 1 27 27 ASN HD21 H 1 7.05 0.02 . 2 . . . . . . . . 5250 1 248 . 1 1 27 27 ASN HD22 H 1 7.58 0.02 . 2 . . . . . . . . 5250 1 249 . 1 1 27 27 ASN C C 13 176.2 0.05 . 1 . . . . . . . . 5250 1 250 . 1 1 28 28 ASN N N 15 118.5 0.05 . 1 . . . . . . . . 5250 1 251 . 1 1 28 28 ASN H H 1 8.98 0.02 . 1 . . . . . . . . 5250 1 252 . 1 1 28 28 ASN CA C 13 52.4 0.05 . 1 . . . . . . . . 5250 1 253 . 1 1 28 28 ASN HA H 1 5.63 0.02 . 1 . . . . . . . . 5250 1 254 . 1 1 28 28 ASN CB C 13 41.8 0.05 . 1 . . . . . . . . 5250 1 255 . 1 1 28 28 ASN HB2 H 1 2.69 0.02 . 2 . . . . . . . . 5250 1 256 . 1 1 28 28 ASN HB3 H 1 3.20 0.02 . 2 . . . . . . . . 5250 1 257 . 1 1 28 28 ASN ND2 N 15 118.2 0.05 . 1 . . . . . . . . 5250 1 258 . 1 1 28 28 ASN HD21 H 1 6.86 0.02 . 2 . . . . . . . . 5250 1 259 . 1 1 28 28 ASN HD22 H 1 7.56 0.02 . 2 . . . . . . . . 5250 1 260 . 1 1 28 28 ASN C C 13 173.9 0.05 . 1 . . . . . . . . 5250 1 261 . 1 1 29 29 VAL N N 15 121.2 0.05 . 1 . . . . . . . . 5250 1 262 . 1 1 29 29 VAL H H 1 7.10 0.02 . 1 . . . . . . . . 5250 1 263 . 1 1 29 29 VAL CA C 13 61.6 0.05 . 1 . . . . . . . . 5250 1 264 . 1 1 29 29 VAL HA H 1 5.14 0.02 . 1 . . . . . . . . 5250 1 265 . 1 1 29 29 VAL CB C 13 35.4 0.05 . 1 . . . . . . . . 5250 1 266 . 1 1 29 29 VAL HB H 1 1.60 0.02 . 1 . . . . . . . . 5250 1 267 . 1 1 29 29 VAL HG11 H 1 0.52 0.02 . 2 . . . . . . . . 5250 1 268 . 1 1 29 29 VAL HG12 H 1 0.52 0.02 . 2 . . . . . . . . 5250 1 269 . 1 1 29 29 VAL HG13 H 1 0.52 0.02 . 2 . . . . . . . . 5250 1 270 . 1 1 29 29 VAL HG21 H 1 0.91 0.02 . 2 . . . . . . . . 5250 1 271 . 1 1 29 29 VAL HG22 H 1 0.91 0.02 . 2 . . . . . . . . 5250 1 272 . 1 1 29 29 VAL HG23 H 1 0.91 0.02 . 2 . . . . . . . . 5250 1 273 . 1 1 29 29 VAL CG1 C 13 22.0 0.05 . 1 . . . . . . . . 5250 1 274 . 1 1 29 29 VAL CG2 C 13 21.5 0.05 . 1 . . . . . . . . 5250 1 275 . 1 1 29 29 VAL C C 13 174.5 0.05 . 1 . . . . . . . . 5250 1 276 . 1 1 30 30 LEU N N 15 126.2 0.05 . 1 . . . . . . . . 5250 1 277 . 1 1 30 30 LEU H H 1 8.81 0.02 . 1 . . . . . . . . 5250 1 278 . 1 1 30 30 LEU CA C 13 53.6 0.05 . 1 . . . . . . . . 5250 1 279 . 1 1 30 30 LEU HA H 1 4.90 0.02 . 1 . . . . . . . . 5250 1 280 . 1 1 30 30 LEU CB C 13 47.0 0.05 . 1 . . . . . . . . 5250 1 281 . 1 1 30 30 LEU HB2 H 1 1.65 0.02 . 1 . . . . . . . . 5250 1 282 . 1 1 30 30 LEU HB3 H 1 1.65 0.02 . 1 . . . . . . . . 5250 1 283 . 1 1 30 30 LEU CG C 13 26.0 0.05 . 1 . . . . . . . . 5250 1 284 . 1 1 30 30 LEU HG H 1 1.57 0.02 . 1 . . . . . . . . 5250 1 285 . 1 1 30 30 LEU HD11 H 1 0.68 0.02 . 2 . . . . . . . . 5250 1 286 . 1 1 30 30 LEU HD12 H 1 0.68 0.02 . 2 . . . . . . . . 5250 1 287 . 1 1 30 30 LEU HD13 H 1 0.68 0.02 . 2 . . . . . . . . 5250 1 288 . 1 1 30 30 LEU HD21 H 1 0.74 0.02 . 2 . . . . . . . . 5250 1 289 . 1 1 30 30 LEU HD22 H 1 0.74 0.02 . 2 . . . . . . . . 5250 1 290 . 1 1 30 30 LEU HD23 H 1 0.74 0.02 . 2 . . . . . . . . 5250 1 291 . 1 1 30 30 LEU CD1 C 13 26.1 0.05 . 1 . . . . . . . . 5250 1 292 . 1 1 30 30 LEU CD2 C 13 28.6 0.05 . 1 . . . . . . . . 5250 1 293 . 1 1 30 30 LEU C C 13 173.9 0.05 . 1 . . . . . . . . 5250 1 294 . 1 1 31 31 ILE N N 15 123.6 0.05 . 1 . . . . . . . . 5250 1 295 . 1 1 31 31 ILE H H 1 9.01 0.02 . 1 . . . . . . . . 5250 1 296 . 1 1 31 31 ILE CA C 13 60.4 0.05 . 1 . . . . . . . . 5250 1 297 . 1 1 31 31 ILE HA H 1 4.93 0.02 . 1 . . . . . . . . 5250 1 298 . 1 1 31 31 ILE CB C 13 39.5 0.05 . 1 . . . . . . . . 5250 1 299 . 1 1 31 31 ILE HB H 1 1.56 0.02 . 1 . . . . . . . . 5250 1 300 . 1 1 31 31 ILE HG21 H 1 0.88 0.02 . 1 . . . . . . . . 5250 1 301 . 1 1 31 31 ILE HG22 H 1 0.88 0.02 . 1 . . . . . . . . 5250 1 302 . 1 1 31 31 ILE HG23 H 1 0.88 0.02 . 1 . . . . . . . . 5250 1 303 . 1 1 31 31 ILE CG2 C 13 17.6 0.05 . 1 . . . . . . . . 5250 1 304 . 1 1 31 31 ILE CG1 C 13 28.1 0.05 . 1 . . . . . . . . 5250 1 305 . 1 1 31 31 ILE HG12 H 1 0.64 0.02 . 2 . . . . . . . . 5250 1 306 . 1 1 31 31 ILE HG13 H 1 1.36 0.02 . 2 . . . . . . . . 5250 1 307 . 1 1 31 31 ILE HD11 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 308 . 1 1 31 31 ILE HD12 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 309 . 1 1 31 31 ILE HD13 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 310 . 1 1 31 31 ILE CD1 C 13 13.7 0.05 . 1 . . . . . . . . 5250 1 311 . 1 1 31 31 ILE C C 13 175.9 0.05 . 1 . . . . . . . . 5250 1 312 . 1 1 32 32 ALA N N 15 134.8 0.05 . 1 . . . . . . . . 5250 1 313 . 1 1 32 32 ALA H H 1 9.45 0.02 . 1 . . . . . . . . 5250 1 314 . 1 1 32 32 ALA CA C 13 50.6 0.05 . 1 . . . . . . . . 5250 1 315 . 1 1 32 32 ALA HA H 1 5.33 0.02 . 1 . . . . . . . . 5250 1 316 . 1 1 32 32 ALA HB1 H 1 1.14 0.02 . 1 . . . . . . . . 5250 1 317 . 1 1 32 32 ALA HB2 H 1 1.14 0.02 . 1 . . . . . . . . 5250 1 318 . 1 1 32 32 ALA HB3 H 1 1.14 0.02 . 1 . . . . . . . . 5250 1 319 . 1 1 32 32 ALA CB C 13 24.4 0.05 . 1 . . . . . . . . 5250 1 320 . 1 1 32 32 ALA C C 13 175.1 0.05 . 1 . . . . . . . . 5250 1 321 . 1 1 33 33 SER N N 15 118.1 0.05 . 1 . . . . . . . . 5250 1 322 . 1 1 33 33 SER H H 1 9.44 0.02 . 1 . . . . . . . . 5250 1 323 . 1 1 33 33 SER CA C 13 57.6 0.05 . 1 . . . . . . . . 5250 1 324 . 1 1 33 33 SER HA H 1 5.17 0.02 . 1 . . . . . . . . 5250 1 325 . 1 1 33 33 SER CB C 13 66.1 0.05 . 1 . . . . . . . . 5250 1 326 . 1 1 33 33 SER HB2 H 1 3.87 0.02 . 2 . . . . . . . . 5250 1 327 . 1 1 33 33 SER HB3 H 1 4.03 0.02 . 2 . . . . . . . . 5250 1 328 . 1 1 33 33 SER C C 13 173.3 0.05 . 1 . . . . . . . . 5250 1 329 . 1 1 34 34 HIS N N 15 124.3 0.05 . 1 . . . . . . . . 5250 1 330 . 1 1 34 34 HIS H H 1 7.80 0.02 . 1 . . . . . . . . 5250 1 331 . 1 1 34 34 HIS CA C 13 57.3 0.05 . 1 . . . . . . . . 5250 1 332 . 1 1 34 34 HIS HA H 1 4.70 0.02 . 1 . . . . . . . . 5250 1 333 . 1 1 34 34 HIS CB C 13 36.8 0.05 . 1 . . . . . . . . 5250 1 334 . 1 1 34 34 HIS HB2 H 1 2.82 0.02 . 2 . . . . . . . . 5250 1 335 . 1 1 34 34 HIS HB3 H 1 3.15 0.02 . 2 . . . . . . . . 5250 1 336 . 1 1 34 34 HIS CD2 C 13 120.1 0.05 . 1 . . . . . . . . 5250 1 337 . 1 1 34 34 HIS CE1 C 13 138.8 0.05 . 1 . . . . . . . . 5250 1 338 . 1 1 34 34 HIS HD2 H 1 5.90 0.02 . 1 . . . . . . . . 5250 1 339 . 1 1 34 34 HIS HE1 H 1 7.21 0.02 . 1 . . . . . . . . 5250 1 340 . 1 1 35 35 HIS CA C 13 59.7 0.05 . 1 . . . . . . . . 5250 1 341 . 1 1 35 35 HIS HA H 1 4.22 0.02 . 1 . . . . . . . . 5250 1 342 . 1 1 35 35 HIS CB C 13 29.9 0.05 . 1 . . . . . . . . 5250 1 343 . 1 1 35 35 HIS HB2 H 1 2.86 0.02 . 2 . . . . . . . . 5250 1 344 . 1 1 35 35 HIS HB3 H 1 2.99 0.02 . 2 . . . . . . . . 5250 1 345 . 1 1 35 35 HIS CD2 C 13 120.3 0.05 . 1 . . . . . . . . 5250 1 346 . 1 1 35 35 HIS CE1 C 13 138.2 0.05 . 1 . . . . . . . . 5250 1 347 . 1 1 35 35 HIS HD2 H 1 6.76 0.02 . 1 . . . . . . . . 5250 1 348 . 1 1 35 35 HIS HE1 H 1 7.78 0.02 . 1 . . . . . . . . 5250 1 349 . 1 1 35 35 HIS C C 13 175.7 0.05 . 1 . . . . . . . . 5250 1 350 . 1 1 36 36 LYS N N 15 125.5 0.05 . 1 . . . . . . . . 5250 1 351 . 1 1 36 36 LYS H H 1 9.25 0.02 . 1 . . . . . . . . 5250 1 352 . 1 1 36 36 LYS CA C 13 57.4 0.05 . 1 . . . . . . . . 5250 1 353 . 1 1 36 36 LYS HA H 1 4.16 0.02 . 1 . . . . . . . . 5250 1 354 . 1 1 36 36 LYS CB C 13 34.4 0.05 . 1 . . . . . . . . 5250 1 355 . 1 1 36 36 LYS HB2 H 1 1.10 0.02 . 2 . . . . . . . . 5250 1 356 . 1 1 36 36 LYS HB3 H 1 1.18 0.02 . 2 . . . . . . . . 5250 1 357 . 1 1 36 36 LYS CG C 13 25.1 0.05 . 1 . . . . . . . . 5250 1 358 . 1 1 36 36 LYS HG2 H 1 0.65 0.02 . 2 . . . . . . . . 5250 1 359 . 1 1 36 36 LYS HG3 H 1 1.01 0.02 . 2 . . . . . . . . 5250 1 360 . 1 1 36 36 LYS CD C 13 29.5 0.05 . 1 . . . . . . . . 5250 1 361 . 1 1 36 36 LYS HD2 H 1 1.31 0.02 . 2 . . . . . . . . 5250 1 362 . 1 1 36 36 LYS HD3 H 1 1.43 0.02 . 2 . . . . . . . . 5250 1 363 . 1 1 36 36 LYS CE C 13 42.3 0.05 . 1 . . . . . . . . 5250 1 364 . 1 1 36 36 LYS HE2 H 1 2.81 0.02 . 1 . . . . . . . . 5250 1 365 . 1 1 36 36 LYS HE3 H 1 2.81 0.02 . 1 . . . . . . . . 5250 1 366 . 1 1 36 36 LYS C C 13 177.6 0.05 . 1 . . . . . . . . 5250 1 367 . 1 1 37 37 TYR N N 15 121.0 0.05 . 1 . . . . . . . . 5250 1 368 . 1 1 37 37 TYR H H 1 7.97 0.02 . 1 . . . . . . . . 5250 1 369 . 1 1 37 37 TYR CA C 13 57.4 0.05 . 1 . . . . . . . . 5250 1 370 . 1 1 37 37 TYR HA H 1 4.72 0.02 . 1 . . . . . . . . 5250 1 371 . 1 1 37 37 TYR CB C 13 40.4 0.05 . 1 . . . . . . . . 5250 1 372 . 1 1 37 37 TYR HB2 H 1 2.24 0.02 . 2 . . . . . . . . 5250 1 373 . 1 1 37 37 TYR HB3 H 1 3.31 0.02 . 2 . . . . . . . . 5250 1 374 . 1 1 37 37 TYR CD1 C 13 133.1 0.05 . 1 . . . . . . . . 5250 1 375 . 1 1 37 37 TYR HD1 H 1 6.59 0.02 . 1 . . . . . . . . 5250 1 376 . 1 1 37 37 TYR CE1 C 13 117.9 0.05 . 1 . . . . . . . . 5250 1 377 . 1 1 37 37 TYR HE1 H 1 6.58 0.02 . 1 . . . . . . . . 5250 1 378 . 1 1 37 37 TYR C C 13 176.3 0.05 . 1 . . . . . . . . 5250 1 379 . 1 1 38 38 SER N N 15 118.7 0.05 . 1 . . . . . . . . 5250 1 380 . 1 1 38 38 SER H H 1 8.41 0.02 . 1 . . . . . . . . 5250 1 381 . 1 1 38 38 SER CA C 13 63.2 0.05 . 1 . . . . . . . . 5250 1 382 . 1 1 38 38 SER HA H 1 4.20 0.02 . 1 . . . . . . . . 5250 1 383 . 1 1 38 38 SER CB C 13 62.5 0.05 . 1 . . . . . . . . 5250 1 384 . 1 1 38 38 SER HB2 H 1 4.13 0.02 . 2 . . . . . . . . 5250 1 385 . 1 1 38 38 SER HB3 H 1 4.23 0.02 . 2 . . . . . . . . 5250 1 386 . 1 1 38 38 SER C C 13 175.8 0.05 . 1 . . . . . . . . 5250 1 387 . 1 1 39 39 GLU N N 15 125.8 0.05 . 1 . . . . . . . . 5250 1 388 . 1 1 39 39 GLU H H 1 8.15 0.02 . 1 . . . . . . . . 5250 1 389 . 1 1 39 39 GLU CA C 13 56.7 0.05 . 1 . . . . . . . . 5250 1 390 . 1 1 39 39 GLU HA H 1 5.17 0.02 . 1 . . . . . . . . 5250 1 391 . 1 1 39 39 GLU CB C 13 34.9 0.05 . 1 . . . . . . . . 5250 1 392 . 1 1 39 39 GLU HB2 H 1 1.99 0.02 . 2 . . . . . . . . 5250 1 393 . 1 1 39 39 GLU HB3 H 1 2.13 0.02 . 2 . . . . . . . . 5250 1 394 . 1 1 39 39 GLU CG C 13 38.2 0.05 . 1 . . . . . . . . 5250 1 395 . 1 1 39 39 GLU HG2 H 1 2.20 0.02 . 2 . . . . . . . . 5250 1 396 . 1 1 39 39 GLU HG3 H 1 2.23 0.02 . 2 . . . . . . . . 5250 1 397 . 1 1 39 39 GLU C C 13 174.4 0.05 . 1 . . . . . . . . 5250 1 398 . 1 1 40 40 VAL N N 15 119.6 0.05 . 1 . . . . . . . . 5250 1 399 . 1 1 40 40 VAL H H 1 9.16 0.02 . 1 . . . . . . . . 5250 1 400 . 1 1 40 40 VAL CA C 13 58.7 0.05 . 1 . . . . . . . . 5250 1 401 . 1 1 40 40 VAL HA H 1 5.41 0.02 . 1 . . . . . . . . 5250 1 402 . 1 1 40 40 VAL CB C 13 36.2 0.05 . 1 . . . . . . . . 5250 1 403 . 1 1 40 40 VAL HB H 1 2.00 0.02 . 1 . . . . . . . . 5250 1 404 . 1 1 40 40 VAL HG11 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 405 . 1 1 40 40 VAL HG12 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 406 . 1 1 40 40 VAL HG13 H 1 0.59 0.02 . 2 . . . . . . . . 5250 1 407 . 1 1 40 40 VAL HG21 H 1 0.88 0.02 . 2 . . . . . . . . 5250 1 408 . 1 1 40 40 VAL HG22 H 1 0.88 0.02 . 2 . . . . . . . . 5250 1 409 . 1 1 40 40 VAL HG23 H 1 0.88 0.02 . 2 . . . . . . . . 5250 1 410 . 1 1 40 40 VAL CG1 C 13 20.1 0.05 . 1 . . . . . . . . 5250 1 411 . 1 1 40 40 VAL CG2 C 13 23.6 0.05 . 1 . . . . . . . . 5250 1 412 . 1 1 40 40 VAL C C 13 174.4 0.05 . 1 . . . . . . . . 5250 1 413 . 1 1 41 41 VAL N N 15 124.1 0.05 . 1 . . . . . . . . 5250 1 414 . 1 1 41 41 VAL H H 1 8.57 0.02 . 1 . . . . . . . . 5250 1 415 . 1 1 41 41 VAL CA C 13 61.0 0.05 . 1 . . . . . . . . 5250 1 416 . 1 1 41 41 VAL HA H 1 4.52 0.02 . 1 . . . . . . . . 5250 1 417 . 1 1 41 41 VAL CB C 13 33.9 0.05 . 1 . . . . . . . . 5250 1 418 . 1 1 41 41 VAL HB H 1 1.20 0.02 . 1 . . . . . . . . 5250 1 419 . 1 1 41 41 VAL HG11 H 1 -0.50 0.02 . 2 . . . . . . . . 5250 1 420 . 1 1 41 41 VAL HG12 H 1 -0.50 0.02 . 2 . . . . . . . . 5250 1 421 . 1 1 41 41 VAL HG13 H 1 -0.50 0.02 . 2 . . . . . . . . 5250 1 422 . 1 1 41 41 VAL HG21 H 1 0.32 0.02 . 2 . . . . . . . . 5250 1 423 . 1 1 41 41 VAL HG22 H 1 0.32 0.02 . 2 . . . . . . . . 5250 1 424 . 1 1 41 41 VAL HG23 H 1 0.32 0.02 . 2 . . . . . . . . 5250 1 425 . 1 1 41 41 VAL CG1 C 13 19.4 0.05 . 1 . . . . . . . . 5250 1 426 . 1 1 41 41 VAL CG2 C 13 21.3 0.05 . 1 . . . . . . . . 5250 1 427 . 1 1 41 41 VAL C C 13 175.1 0.05 . 1 . . . . . . . . 5250 1 428 . 1 1 42 42 LEU N N 15 128.9 0.05 . 1 . . . . . . . . 5250 1 429 . 1 1 42 42 LEU H H 1 8.75 0.02 . 1 . . . . . . . . 5250 1 430 . 1 1 42 42 LEU CA C 13 52.9 0.05 . 1 . . . . . . . . 5250 1 431 . 1 1 42 42 LEU HA H 1 4.95 0.02 . 1 . . . . . . . . 5250 1 432 . 1 1 42 42 LEU CB C 13 45.2 0.05 . 1 . . . . . . . . 5250 1 433 . 1 1 42 42 LEU HB2 H 1 0.74 0.02 . 2 . . . . . . . . 5250 1 434 . 1 1 42 42 LEU HB3 H 1 1.33 0.02 . 2 . . . . . . . . 5250 1 435 . 1 1 42 42 LEU CG C 13 26.3 0.05 . 1 . . . . . . . . 5250 1 436 . 1 1 42 42 LEU HG H 1 0.88 0.02 . 1 . . . . . . . . 5250 1 437 . 1 1 42 42 LEU HD11 H 1 -0.30 0.02 . 2 . . . . . . . . 5250 1 438 . 1 1 42 42 LEU HD12 H 1 -0.30 0.02 . 2 . . . . . . . . 5250 1 439 . 1 1 42 42 LEU HD13 H 1 -0.30 0.02 . 2 . . . . . . . . 5250 1 440 . 1 1 42 42 LEU HD21 H 1 -0.17 0.02 . 2 . . . . . . . . 5250 1 441 . 1 1 42 42 LEU HD22 H 1 -0.17 0.02 . 2 . . . . . . . . 5250 1 442 . 1 1 42 42 LEU HD23 H 1 -0.17 0.02 . 2 . . . . . . . . 5250 1 443 . 1 1 42 42 LEU CD1 C 13 22.3 0.05 . 1 . . . . . . . . 5250 1 444 . 1 1 42 42 LEU CD2 C 13 24.6 0.05 . 1 . . . . . . . . 5250 1 445 . 1 1 42 42 LEU C C 13 175.5 0.05 . 1 . . . . . . . . 5250 1 446 . 1 1 43 43 ILE N N 15 122.2 0.05 . 1 . . . . . . . . 5250 1 447 . 1 1 43 43 ILE H H 1 8.41 0.02 . 1 . . . . . . . . 5250 1 448 . 1 1 43 43 ILE CA C 13 59.9 0.05 . 1 . . . . . . . . 5250 1 449 . 1 1 43 43 ILE HA H 1 5.39 0.02 . 1 . . . . . . . . 5250 1 450 . 1 1 43 43 ILE CB C 13 41.0 0.05 . 1 . . . . . . . . 5250 1 451 . 1 1 43 43 ILE HB H 1 1.72 0.02 . 1 . . . . . . . . 5250 1 452 . 1 1 43 43 ILE HG21 H 1 0.91 0.02 . 1 . . . . . . . . 5250 1 453 . 1 1 43 43 ILE HG22 H 1 0.91 0.02 . 1 . . . . . . . . 5250 1 454 . 1 1 43 43 ILE HG23 H 1 0.91 0.02 . 1 . . . . . . . . 5250 1 455 . 1 1 43 43 ILE CG2 C 13 16.4 0.05 . 1 . . . . . . . . 5250 1 456 . 1 1 43 43 ILE CG1 C 13 27.6 0.05 . 1 . . . . . . . . 5250 1 457 . 1 1 43 43 ILE HG12 H 1 1.15 0.02 . 2 . . . . . . . . 5250 1 458 . 1 1 43 43 ILE HG13 H 1 1.55 0.02 . 2 . . . . . . . . 5250 1 459 . 1 1 43 43 ILE HD11 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 460 . 1 1 43 43 ILE HD12 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 461 . 1 1 43 43 ILE HD13 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 462 . 1 1 43 43 ILE CD1 C 13 14.0 0.05 . 1 . . . . . . . . 5250 1 463 . 1 1 43 43 ILE C C 13 176.9 0.05 . 1 . . . . . . . . 5250 1 464 . 1 1 44 44 GLY N N 15 119.4 0.05 . 1 . . . . . . . . 5250 1 465 . 1 1 44 44 GLY H H 1 9.11 0.02 . 1 . . . . . . . . 5250 1 466 . 1 1 44 44 GLY CA C 13 46.1 0.05 . 1 . . . . . . . . 5250 1 467 . 1 1 44 44 GLY HA2 H 1 4.01 0.02 . 2 . . . . . . . . 5250 1 468 . 1 1 44 44 GLY HA3 H 1 4.32 0.02 . 2 . . . . . . . . 5250 1 469 . 1 1 44 44 GLY C C 13 172.6 0.05 . 1 . . . . . . . . 5250 1 470 . 1 1 45 45 LYS N N 15 127.4 0.05 . 1 . . . . . . . . 5250 1 471 . 1 1 45 45 LYS H H 1 8.61 0.02 . 1 . . . . . . . . 5250 1 472 . 1 1 45 45 LYS CA C 13 58.2 0.05 . 1 . . . . . . . . 5250 1 473 . 1 1 45 45 LYS HA H 1 4.14 0.02 . 1 . . . . . . . . 5250 1 474 . 1 1 45 45 LYS CB C 13 31.6 0.05 . 1 . . . . . . . . 5250 1 475 . 1 1 45 45 LYS HB2 H 1 1.75 0.02 . 1 . . . . . . . . 5250 1 476 . 1 1 45 45 LYS HB3 H 1 1.75 0.02 . 1 . . . . . . . . 5250 1 477 . 1 1 45 45 LYS CG C 13 24.8 0.05 . 1 . . . . . . . . 5250 1 478 . 1 1 45 45 LYS HG2 H 1 1.27 0.02 . 2 . . . . . . . . 5250 1 479 . 1 1 45 45 LYS HG3 H 1 1.42 0.02 . 2 . . . . . . . . 5250 1 480 . 1 1 45 45 LYS CD C 13 29.3 0.05 . 1 . . . . . . . . 5250 1 481 . 1 1 45 45 LYS HD2 H 1 1.66 0.02 . 1 . . . . . . . . 5250 1 482 . 1 1 45 45 LYS HD3 H 1 1.66 0.02 . 1 . . . . . . . . 5250 1 483 . 1 1 45 45 LYS CE C 13 42.4 0.05 . 1 . . . . . . . . 5250 1 484 . 1 1 45 45 LYS HE2 H 1 2.96 0.02 . 1 . . . . . . . . 5250 1 485 . 1 1 45 45 LYS HE3 H 1 2.96 0.02 . 1 . . . . . . . . 5250 1 486 . 1 1 45 45 LYS C C 13 178.8 0.05 . 1 . . . . . . . . 5250 1 487 . 1 1 46 46 GLY N N 15 120.4 0.05 . 1 . . . . . . . . 5250 1 488 . 1 1 46 46 GLY H H 1 9.29 0.02 . 1 . . . . . . . . 5250 1 489 . 1 1 46 46 GLY CA C 13 47.2 0.05 . 1 . . . . . . . . 5250 1 490 . 1 1 46 46 GLY HA2 H 1 3.81 0.02 . 2 . . . . . . . . 5250 1 491 . 1 1 46 46 GLY HA3 H 1 4.07 0.02 . 2 . . . . . . . . 5250 1 492 . 1 1 46 46 GLY C C 13 177.2 0.05 . 1 . . . . . . . . 5250 1 493 . 1 1 47 47 ILE N N 15 121.8 0.05 . 1 . . . . . . . . 5250 1 494 . 1 1 47 47 ILE H H 1 7.54 0.02 . 1 . . . . . . . . 5250 1 495 . 1 1 47 47 ILE CA C 13 64.3 0.05 . 1 . . . . . . . . 5250 1 496 . 1 1 47 47 ILE HA H 1 4.04 0.02 . 1 . . . . . . . . 5250 1 497 . 1 1 47 47 ILE CB C 13 38.6 0.05 . 1 . . . . . . . . 5250 1 498 . 1 1 47 47 ILE HB H 1 1.73 0.02 . 1 . . . . . . . . 5250 1 499 . 1 1 47 47 ILE HG21 H 1 0.73 0.02 . 1 . . . . . . . . 5250 1 500 . 1 1 47 47 ILE HG22 H 1 0.73 0.02 . 1 . . . . . . . . 5250 1 501 . 1 1 47 47 ILE HG23 H 1 0.73 0.02 . 1 . . . . . . . . 5250 1 502 . 1 1 47 47 ILE CG2 C 13 17.6 0.05 . 1 . . . . . . . . 5250 1 503 . 1 1 47 47 ILE CG1 C 13 27.1 0.05 . 1 . . . . . . . . 5250 1 504 . 1 1 47 47 ILE HG12 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 505 . 1 1 47 47 ILE HG13 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 506 . 1 1 47 47 ILE HD11 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 507 . 1 1 47 47 ILE HD12 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 508 . 1 1 47 47 ILE HD13 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 509 . 1 1 47 47 ILE CD1 C 13 15.2 0.05 . 1 . . . . . . . . 5250 1 510 . 1 1 47 47 ILE C C 13 175.6 0.05 . 1 . . . . . . . . 5250 1 511 . 1 1 48 48 GLY N N 15 109.1 0.05 . 1 . . . . . . . . 5250 1 512 . 1 1 48 48 GLY H H 1 8.39 0.02 . 1 . . . . . . . . 5250 1 513 . 1 1 48 48 GLY CA C 13 45.0 0.05 . 1 . . . . . . . . 5250 1 514 . 1 1 48 48 GLY HA2 H 1 3.50 0.02 . 2 . . . . . . . . 5250 1 515 . 1 1 48 48 GLY HA3 H 1 3.96 0.02 . 2 . . . . . . . . 5250 1 516 . 1 1 48 48 GLY C C 13 174.7 0.05 . 1 . . . . . . . . 5250 1 517 . 1 1 49 49 PHE N N 15 125.8 0.05 . 1 . . . . . . . . 5250 1 518 . 1 1 49 49 PHE H H 1 7.42 0.02 . 1 . . . . . . . . 5250 1 519 . 1 1 49 49 PHE CA C 13 59.9 0.05 . 1 . . . . . . . . 5250 1 520 . 1 1 49 49 PHE HA H 1 4.24 0.02 . 1 . . . . . . . . 5250 1 521 . 1 1 49 49 PHE CB C 13 39.1 0.05 . 1 . . . . . . . . 5250 1 522 . 1 1 49 49 PHE HB2 H 1 3.01 0.02 . 2 . . . . . . . . 5250 1 523 . 1 1 49 49 PHE HB3 H 1 3.10 0.02 . 2 . . . . . . . . 5250 1 524 . 1 1 49 49 PHE CD1 C 13 132.1 0.05 . 1 . . . . . . . . 5250 1 525 . 1 1 49 49 PHE HD1 H 1 7.22 0.02 . 1 . . . . . . . . 5250 1 526 . 1 1 49 49 PHE CE1 C 13 132.2 0.05 . 1 . . . . . . . . 5250 1 527 . 1 1 49 49 PHE HE1 H 1 7.35 0.02 . 1 . . . . . . . . 5250 1 528 . 1 1 49 49 PHE CZ C 13 130.3 0.05 . 1 . . . . . . . . 5250 1 529 . 1 1 49 49 PHE HZ H 1 7.30 0.02 . 1 . . . . . . . . 5250 1 530 . 1 1 49 49 PHE C C 13 177.4 0.05 . 1 . . . . . . . . 5250 1 531 . 1 1 50 50 GLY N N 15 119.8 0.05 . 1 . . . . . . . . 5250 1 532 . 1 1 50 50 GLY H H 1 8.61 0.02 . 1 . . . . . . . . 5250 1 533 . 1 1 50 50 GLY CA C 13 46.0 0.05 . 1 . . . . . . . . 5250 1 534 . 1 1 50 50 GLY HA2 H 1 3.41 0.02 . 2 . . . . . . . . 5250 1 535 . 1 1 50 50 GLY HA3 H 1 3.72 0.02 . 2 . . . . . . . . 5250 1 536 . 1 1 50 50 GLY C C 13 174.2 0.05 . 1 . . . . . . . . 5250 1 537 . 1 1 51 51 LYS N N 15 120.8 0.05 . 1 . . . . . . . . 5250 1 538 . 1 1 51 51 LYS H H 1 7.26 0.02 . 1 . . . . . . . . 5250 1 539 . 1 1 51 51 LYS CA C 13 54.1 0.05 . 1 . . . . . . . . 5250 1 540 . 1 1 51 51 LYS HA H 1 4.69 0.02 . 1 . . . . . . . . 5250 1 541 . 1 1 51 51 LYS CB C 13 34.7 0.05 . 1 . . . . . . . . 5250 1 542 . 1 1 51 51 LYS HB2 H 1 1.56 0.02 . 2 . . . . . . . . 5250 1 543 . 1 1 51 51 LYS HB3 H 1 1.79 0.02 . 2 . . . . . . . . 5250 1 544 . 1 1 51 51 LYS CG C 13 25.2 0.05 . 1 . . . . . . . . 5250 1 545 . 1 1 51 51 LYS HG2 H 1 1.23 0.02 . 2 . . . . . . . . 5250 1 546 . 1 1 51 51 LYS HG3 H 1 1.53 0.02 . 2 . . . . . . . . 5250 1 547 . 1 1 51 51 LYS CD C 13 28.3 0.05 . 1 . . . . . . . . 5250 1 548 . 1 1 51 51 LYS HD2 H 1 1.52 0.02 . 2 . . . . . . . . 5250 1 549 . 1 1 51 51 LYS HD3 H 1 1.62 0.02 . 2 . . . . . . . . 5250 1 550 . 1 1 51 51 LYS CE C 13 42.9 0.05 . 1 . . . . . . . . 5250 1 551 . 1 1 51 51 LYS HE2 H 1 2.93 0.02 . 2 . . . . . . . . 5250 1 552 . 1 1 51 51 LYS HE3 H 1 3.12 0.02 . 2 . . . . . . . . 5250 1 553 . 1 1 51 51 LYS C C 13 175.6 0.05 . 1 . . . . . . . . 5250 1 554 . 1 1 52 52 LYS N N 15 122.9 0.05 . 1 . . . . . . . . 5250 1 555 . 1 1 52 52 LYS H H 1 8.79 0.02 . 1 . . . . . . . . 5250 1 556 . 1 1 52 52 LYS CA C 13 54.3 0.05 . 1 . . . . . . . . 5250 1 557 . 1 1 52 52 LYS HA H 1 4.47 0.02 . 1 . . . . . . . . 5250 1 558 . 1 1 52 52 LYS CB C 13 36.2 0.05 . 1 . . . . . . . . 5250 1 559 . 1 1 52 52 LYS HB2 H 1 1.72 0.02 . 1 . . . . . . . . 5250 1 560 . 1 1 52 52 LYS HB3 H 1 1.72 0.02 . 1 . . . . . . . . 5250 1 561 . 1 1 52 52 LYS CG C 13 23.5 0.05 . 1 . . . . . . . . 5250 1 562 . 1 1 52 52 LYS HG2 H 1 1.23 0.02 . 2 . . . . . . . . 5250 1 563 . 1 1 52 52 LYS HG3 H 1 1.42 0.02 . 2 . . . . . . . . 5250 1 564 . 1 1 52 52 LYS CD C 13 29.4 0.05 . 1 . . . . . . . . 5250 1 565 . 1 1 52 52 LYS HD2 H 1 1.61 0.02 . 1 . . . . . . . . 5250 1 566 . 1 1 52 52 LYS HD3 H 1 1.61 0.02 . 1 . . . . . . . . 5250 1 567 . 1 1 52 52 LYS CE C 13 42.5 0.05 . 1 . . . . . . . . 5250 1 568 . 1 1 52 52 LYS HE2 H 1 2.99 0.02 . 1 . . . . . . . . 5250 1 569 . 1 1 52 52 LYS HE3 H 1 2.99 0.02 . 1 . . . . . . . . 5250 1 570 . 1 1 52 52 LYS C C 13 174.9 0.05 . 1 . . . . . . . . 5250 1 571 . 1 1 53 53 GLN N N 15 122.5 0.05 . 1 . . . . . . . . 5250 1 572 . 1 1 53 53 GLN H H 1 8.30 0.02 . 1 . . . . . . . . 5250 1 573 . 1 1 53 53 GLN CA C 13 58.5 0.05 . 1 . . . . . . . . 5250 1 574 . 1 1 53 53 GLN HA H 1 3.44 0.02 . 1 . . . . . . . . 5250 1 575 . 1 1 53 53 GLN CB C 13 29.1 0.05 . 1 . . . . . . . . 5250 1 576 . 1 1 53 53 GLN HB2 H 1 1.83 0.02 . 2 . . . . . . . . 5250 1 577 . 1 1 53 53 GLN HB3 H 1 2.00 0.02 . 2 . . . . . . . . 5250 1 578 . 1 1 53 53 GLN CG C 13 33.9 0.05 . 1 . . . . . . . . 5250 1 579 . 1 1 53 53 GLN HG2 H 1 2.30 0.02 . 2 . . . . . . . . 5250 1 580 . 1 1 53 53 GLN HG3 H 1 2.46 0.02 . 2 . . . . . . . . 5250 1 581 . 1 1 53 53 GLN NE2 N 15 115.3 0.05 . 1 . . . . . . . . 5250 1 582 . 1 1 53 53 GLN HE21 H 1 6.82 0.02 . 2 . . . . . . . . 5250 1 583 . 1 1 53 53 GLN HE22 H 1 7.57 0.02 . 2 . . . . . . . . 5250 1 584 . 1 1 53 53 GLN C C 13 176.2 0.05 . 1 . . . . . . . . 5250 1 585 . 1 1 54 54 ASP N N 15 121.6 0.05 . 1 . . . . . . . . 5250 1 586 . 1 1 54 54 ASP H H 1 8.98 0.02 . 1 . . . . . . . . 5250 1 587 . 1 1 54 54 ASP CA C 13 58.2 0.05 . 1 . . . . . . . . 5250 1 588 . 1 1 54 54 ASP HA H 1 4.16 0.02 . 1 . . . . . . . . 5250 1 589 . 1 1 54 54 ASP CB C 13 39.1 0.05 . 1 . . . . . . . . 5250 1 590 . 1 1 54 54 ASP HB2 H 1 2.82 0.02 . 2 . . . . . . . . 5250 1 591 . 1 1 54 54 ASP HB3 H 1 3.30 0.02 . 2 . . . . . . . . 5250 1 592 . 1 1 54 54 ASP C C 13 176.0 0.05 . 1 . . . . . . . . 5250 1 593 . 1 1 55 55 ASP N N 15 124.6 0.05 . 1 . . . . . . . . 5250 1 594 . 1 1 55 55 ASP H H 1 7.98 0.02 . 1 . . . . . . . . 5250 1 595 . 1 1 55 55 ASP CA C 13 56.0 0.05 . 1 . . . . . . . . 5250 1 596 . 1 1 55 55 ASP HA H 1 4.64 0.02 . 1 . . . . . . . . 5250 1 597 . 1 1 55 55 ASP CB C 13 41.7 0.05 . 1 . . . . . . . . 5250 1 598 . 1 1 55 55 ASP HB2 H 1 2.60 0.02 . 2 . . . . . . . . 5250 1 599 . 1 1 55 55 ASP HB3 H 1 2.81 0.02 . 2 . . . . . . . . 5250 1 600 . 1 1 55 55 ASP C C 13 175.4 0.05 . 1 . . . . . . . . 5250 1 601 . 1 1 56 56 VAL N N 15 124.3 0.05 . 1 . . . . . . . . 5250 1 602 . 1 1 56 56 VAL H H 1 8.46 0.02 . 1 . . . . . . . . 5250 1 603 . 1 1 56 56 VAL CA C 13 62.0 0.05 . 1 . . . . . . . . 5250 1 604 . 1 1 56 56 VAL HA H 1 4.90 0.02 . 1 . . . . . . . . 5250 1 605 . 1 1 56 56 VAL CB C 13 33.5 0.05 . 1 . . . . . . . . 5250 1 606 . 1 1 56 56 VAL HB H 1 1.90 0.02 . 1 . . . . . . . . 5250 1 607 . 1 1 56 56 VAL HG11 H 1 0.85 0.02 . 2 . . . . . . . . 5250 1 608 . 1 1 56 56 VAL HG12 H 1 0.85 0.02 . 2 . . . . . . . . 5250 1 609 . 1 1 56 56 VAL HG13 H 1 0.85 0.02 . 2 . . . . . . . . 5250 1 610 . 1 1 56 56 VAL HG21 H 1 0.96 0.02 . 2 . . . . . . . . 5250 1 611 . 1 1 56 56 VAL HG22 H 1 0.96 0.02 . 2 . . . . . . . . 5250 1 612 . 1 1 56 56 VAL HG23 H 1 0.96 0.02 . 2 . . . . . . . . 5250 1 613 . 1 1 56 56 VAL CG1 C 13 21.8 0.05 . 1 . . . . . . . . 5250 1 614 . 1 1 56 56 VAL CG2 C 13 21.6 0.05 . 1 . . . . . . . . 5250 1 615 . 1 1 56 56 VAL C C 13 177.1 0.05 . 1 . . . . . . . . 5250 1 616 . 1 1 57 57 ILE N N 15 127.7 0.05 . 1 . . . . . . . . 5250 1 617 . 1 1 57 57 ILE H H 1 9.05 0.02 . 1 . . . . . . . . 5250 1 618 . 1 1 57 57 ILE CA C 13 59.4 0.05 . 1 . . . . . . . . 5250 1 619 . 1 1 57 57 ILE HA H 1 4.66 0.02 . 1 . . . . . . . . 5250 1 620 . 1 1 57 57 ILE CB C 13 40.7 0.05 . 1 . . . . . . . . 5250 1 621 . 1 1 57 57 ILE HB H 1 1.97 0.02 . 1 . . . . . . . . 5250 1 622 . 1 1 57 57 ILE HG21 H 1 0.93 0.02 . 1 . . . . . . . . 5250 1 623 . 1 1 57 57 ILE HG22 H 1 0.93 0.02 . 1 . . . . . . . . 5250 1 624 . 1 1 57 57 ILE HG23 H 1 0.93 0.02 . 1 . . . . . . . . 5250 1 625 . 1 1 57 57 ILE CG2 C 13 17.6 0.05 . 1 . . . . . . . . 5250 1 626 . 1 1 57 57 ILE CG1 C 13 27.0 0.05 . 1 . . . . . . . . 5250 1 627 . 1 1 57 57 ILE HG12 H 1 1.05 0.02 . 2 . . . . . . . . 5250 1 628 . 1 1 57 57 ILE HG13 H 1 1.47 0.02 . 2 . . . . . . . . 5250 1 629 . 1 1 57 57 ILE HD11 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 630 . 1 1 57 57 ILE HD12 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 631 . 1 1 57 57 ILE HD13 H 1 0.68 0.02 . 1 . . . . . . . . 5250 1 632 . 1 1 57 57 ILE CD1 C 13 13.2 0.05 . 1 . . . . . . . . 5250 1 633 . 1 1 57 57 ILE C C 13 175.3 0.05 . 1 . . . . . . . . 5250 1 634 . 1 1 58 58 GLU N N 15 126.4 0.05 . 1 . . . . . . . . 5250 1 635 . 1 1 58 58 GLU H H 1 8.68 0.02 . 1 . . . . . . . . 5250 1 636 . 1 1 58 58 GLU CA C 13 56.6 0.05 . 1 . . . . . . . . 5250 1 637 . 1 1 58 58 GLU HA H 1 4.40 0.02 . 1 . . . . . . . . 5250 1 638 . 1 1 58 58 GLU CB C 13 31.6 0.05 . 1 . . . . . . . . 5250 1 639 . 1 1 58 58 GLU HB2 H 1 1.93 0.02 . 2 . . . . . . . . 5250 1 640 . 1 1 58 58 GLU HB3 H 1 2.08 0.02 . 2 . . . . . . . . 5250 1 641 . 1 1 58 58 GLU CG C 13 37.1 0.05 . 1 . . . . . . . . 5250 1 642 . 1 1 58 58 GLU HG2 H 1 2.27 0.02 . 2 . . . . . . . . 5250 1 643 . 1 1 58 58 GLU HG3 H 1 2.33 0.02 . 2 . . . . . . . . 5250 1 644 . 1 1 58 58 GLU C C 13 176.3 0.05 . 1 . . . . . . . . 5250 1 645 . 1 1 59 59 ASP N N 15 122.5 0.05 . 1 . . . . . . . . 5250 1 646 . 1 1 59 59 ASP H H 1 8.36 0.02 . 1 . . . . . . . . 5250 1 647 . 1 1 59 59 ASP CA C 13 54.5 0.05 . 1 . . . . . . . . 5250 1 648 . 1 1 59 59 ASP HA H 1 4.82 0.02 . 1 . . . . . . . . 5250 1 649 . 1 1 59 59 ASP CB C 13 40.2 0.05 . 1 . . . . . . . . 5250 1 650 . 1 1 59 59 ASP HB2 H 1 2.57 0.02 . 2 . . . . . . . . 5250 1 651 . 1 1 59 59 ASP HB3 H 1 2.73 0.02 . 2 . . . . . . . . 5250 1 652 . 1 1 59 59 ASP C C 13 175.8 0.05 . 1 . . . . . . . . 5250 1 653 . 1 1 60 60 LYS N N 15 122.4 0.05 . 1 . . . . . . . . 5250 1 654 . 1 1 60 60 LYS H H 1 8.20 0.02 . 1 . . . . . . . . 5250 1 655 . 1 1 60 60 LYS CA C 13 56.3 0.05 . 1 . . . . . . . . 5250 1 656 . 1 1 60 60 LYS HA H 1 4.21 0.02 . 1 . . . . . . . . 5250 1 657 . 1 1 60 60 LYS CB C 13 33.1 0.05 . 1 . . . . . . . . 5250 1 658 . 1 1 60 60 LYS HB2 H 1 1.71 0.02 . 2 . . . . . . . . 5250 1 659 . 1 1 60 60 LYS HB3 H 1 1.89 0.02 . 2 . . . . . . . . 5250 1 660 . 1 1 60 60 LYS CG C 13 24.5 0.05 . 1 . . . . . . . . 5250 1 661 . 1 1 60 60 LYS HG2 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 662 . 1 1 60 60 LYS HG3 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 663 . 1 1 60 60 LYS CD C 13 29.4 0.05 . 1 . . . . . . . . 5250 1 664 . 1 1 60 60 LYS HD2 H 1 1.56 0.02 . 2 . . . . . . . . 5250 1 665 . 1 1 60 60 LYS HD3 H 1 1.61 0.02 . 2 . . . . . . . . 5250 1 666 . 1 1 60 60 LYS CE C 13 42.5 0.05 . 1 . . . . . . . . 5250 1 667 . 1 1 60 60 LYS HE2 H 1 2.92 0.02 . 1 . . . . . . . . 5250 1 668 . 1 1 60 60 LYS HE3 H 1 2.92 0.02 . 1 . . . . . . . . 5250 1 669 . 1 1 60 60 LYS C C 13 176.6 0.05 . 1 . . . . . . . . 5250 1 670 . 1 1 61 61 GLY N N 15 110.9 0.05 . 1 . . . . . . . . 5250 1 671 . 1 1 61 61 GLY H H 1 8.27 0.02 . 1 . . . . . . . . 5250 1 672 . 1 1 61 61 GLY CA C 13 46.5 0.05 . 1 . . . . . . . . 5250 1 673 . 1 1 61 61 GLY HA2 H 1 3.79 0.02 . 2 . . . . . . . . 5250 1 674 . 1 1 61 61 GLY HA3 H 1 3.85 0.02 . 2 . . . . . . . . 5250 1 675 . 1 1 61 61 GLY C C 13 173.4 0.05 . 1 . . . . . . . . 5250 1 676 . 1 1 62 62 TYR N N 15 117.6 0.05 . 1 . . . . . . . . 5250 1 677 . 1 1 62 62 TYR H H 1 6.89 0.02 . 1 . . . . . . . . 5250 1 678 . 1 1 62 62 TYR CA C 13 55.1 0.05 . 1 . . . . . . . . 5250 1 679 . 1 1 62 62 TYR HA H 1 4.69 0.02 . 1 . . . . . . . . 5250 1 680 . 1 1 62 62 TYR CB C 13 39.8 0.05 . 1 . . . . . . . . 5250 1 681 . 1 1 62 62 TYR HB2 H 1 2.52 0.02 . 2 . . . . . . . . 5250 1 682 . 1 1 62 62 TYR HB3 H 1 2.92 0.02 . 2 . . . . . . . . 5250 1 683 . 1 1 62 62 TYR CD1 C 13 134.0 0.05 . 1 . . . . . . . . 5250 1 684 . 1 1 62 62 TYR HD1 H 1 6.50 0.02 . 1 . . . . . . . . 5250 1 685 . 1 1 62 62 TYR CE1 C 13 118.3 0.05 . 1 . . . . . . . . 5250 1 686 . 1 1 62 62 TYR HE1 H 1 6.78 0.02 . 1 . . . . . . . . 5250 1 687 . 1 1 62 62 TYR C C 13 173.7 0.05 . 1 . . . . . . . . 5250 1 688 . 1 1 63 63 ASP N N 15 123.6 0.05 . 1 . . . . . . . . 5250 1 689 . 1 1 63 63 ASP H H 1 9.37 0.02 . 1 . . . . . . . . 5250 1 690 . 1 1 63 63 ASP CA C 13 56.1 0.05 . 1 . . . . . . . . 5250 1 691 . 1 1 63 63 ASP HA H 1 4.76 0.02 . 1 . . . . . . . . 5250 1 692 . 1 1 63 63 ASP CB C 13 43.1 0.05 . 1 . . . . . . . . 5250 1 693 . 1 1 63 63 ASP HB2 H 1 2.63 0.02 . 2 . . . . . . . . 5250 1 694 . 1 1 63 63 ASP HB3 H 1 2.77 0.02 . 2 . . . . . . . . 5250 1 695 . 1 1 63 63 ASP C C 13 176.7 0.05 . 1 . . . . . . . . 5250 1 696 . 1 1 64 64 LYS N N 15 120.5 0.05 . 1 . . . . . . . . 5250 1 697 . 1 1 64 64 LYS H H 1 8.15 0.02 . 1 . . . . . . . . 5250 1 698 . 1 1 64 64 LYS CA C 13 55.8 0.05 . 1 . . . . . . . . 5250 1 699 . 1 1 64 64 LYS HA H 1 4.63 0.02 . 1 . . . . . . . . 5250 1 700 . 1 1 64 64 LYS CB C 13 39.1 0.05 . 1 . . . . . . . . 5250 1 701 . 1 1 64 64 LYS HB2 H 1 1.41 0.02 . 2 . . . . . . . . 5250 1 702 . 1 1 64 64 LYS HB3 H 1 1.48 0.02 . 2 . . . . . . . . 5250 1 703 . 1 1 64 64 LYS CG C 13 26.3 0.05 . 1 . . . . . . . . 5250 1 704 . 1 1 64 64 LYS HG2 H 1 1.26 0.02 . 1 . . . . . . . . 5250 1 705 . 1 1 64 64 LYS HG3 H 1 1.26 0.02 . 1 . . . . . . . . 5250 1 706 . 1 1 64 64 LYS CD C 13 30.4 0.05 . 1 . . . . . . . . 5250 1 707 . 1 1 64 64 LYS HD2 H 1 1.53 0.02 . 2 . . . . . . . . 5250 1 708 . 1 1 64 64 LYS HD3 H 1 1.58 0.02 . 2 . . . . . . . . 5250 1 709 . 1 1 64 64 LYS CE C 13 42.3 0.05 . 1 . . . . . . . . 5250 1 710 . 1 1 64 64 LYS HE2 H 1 2.82 0.02 . 1 . . . . . . . . 5250 1 711 . 1 1 64 64 LYS HE3 H 1 2.82 0.02 . 1 . . . . . . . . 5250 1 712 . 1 1 64 64 LYS C C 13 173.3 0.05 . 1 . . . . . . . . 5250 1 713 . 1 1 65 65 MET N N 15 125.1 0.05 . 1 . . . . . . . . 5250 1 714 . 1 1 65 65 MET H H 1 8.42 0.02 . 1 . . . . . . . . 5250 1 715 . 1 1 65 65 MET CA C 13 54.4 0.05 . 1 . . . . . . . . 5250 1 716 . 1 1 65 65 MET HA H 1 4.89 0.02 . 1 . . . . . . . . 5250 1 717 . 1 1 65 65 MET CB C 13 36.5 0.05 . 1 . . . . . . . . 5250 1 718 . 1 1 65 65 MET HB2 H 1 1.23 0.02 . 2 . . . . . . . . 5250 1 719 . 1 1 65 65 MET HB3 H 1 1.63 0.02 . 2 . . . . . . . . 5250 1 720 . 1 1 65 65 MET CG C 13 31.8 0.05 . 1 . . . . . . . . 5250 1 721 . 1 1 65 65 MET HG2 H 1 1.66 0.02 . 2 . . . . . . . . 5250 1 722 . 1 1 65 65 MET HG3 H 1 1.84 0.02 . 2 . . . . . . . . 5250 1 723 . 1 1 65 65 MET HE1 H 1 1.65 0.02 . 1 . . . . . . . . 5250 1 724 . 1 1 65 65 MET HE2 H 1 1.65 0.02 . 1 . . . . . . . . 5250 1 725 . 1 1 65 65 MET HE3 H 1 1.65 0.02 . 1 . . . . . . . . 5250 1 726 . 1 1 65 65 MET CE C 13 17.6 0.05 . 1 . . . . . . . . 5250 1 727 . 1 1 65 65 MET C C 13 173.2 0.05 . 1 . . . . . . . . 5250 1 728 . 1 1 66 66 PHE N N 15 128.2 0.05 . 1 . . . . . . . . 5250 1 729 . 1 1 66 66 PHE H H 1 9.26 0.02 . 1 . . . . . . . . 5250 1 730 . 1 1 66 66 PHE CA C 13 55.2 0.05 . 1 . . . . . . . . 5250 1 731 . 1 1 66 66 PHE HA H 1 5.12 0.02 . 1 . . . . . . . . 5250 1 732 . 1 1 66 66 PHE CB C 13 42.1 0.05 . 1 . . . . . . . . 5250 1 733 . 1 1 66 66 PHE HB2 H 1 2.54 0.02 . 2 . . . . . . . . 5250 1 734 . 1 1 66 66 PHE HB3 H 1 2.63 0.02 . 2 . . . . . . . . 5250 1 735 . 1 1 66 66 PHE CD1 C 13 131.5 0.05 . 1 . . . . . . . . 5250 1 736 . 1 1 66 66 PHE HD1 H 1 6.86 0.02 . 1 . . . . . . . . 5250 1 737 . 1 1 66 66 PHE CE1 C 13 132.0 0.05 . 1 . . . . . . . . 5250 1 738 . 1 1 66 66 PHE HE1 H 1 6.86 0.02 . 1 . . . . . . . . 5250 1 739 . 1 1 66 66 PHE CZ C 13 130.0 0.05 . 1 . . . . . . . . 5250 1 740 . 1 1 66 66 PHE HZ H 1 7.24 0.02 . 1 . . . . . . . . 5250 1 741 . 1 1 66 66 PHE C C 13 176.0 0.05 . 1 . . . . . . . . 5250 1 742 . 1 1 67 67 ILE N N 15 120.9 0.05 . 1 . . . . . . . . 5250 1 743 . 1 1 67 67 ILE H H 1 9.29 0.02 . 1 . . . . . . . . 5250 1 744 . 1 1 67 67 ILE CA C 13 60.1 0.05 . 1 . . . . . . . . 5250 1 745 . 1 1 67 67 ILE HA H 1 4.86 0.02 . 1 . . . . . . . . 5250 1 746 . 1 1 67 67 ILE CB C 13 41.0 0.05 . 1 . . . . . . . . 5250 1 747 . 1 1 67 67 ILE HB H 1 1.82 0.02 . 1 . . . . . . . . 5250 1 748 . 1 1 67 67 ILE HG21 H 1 0.34 0.02 . 1 . . . . . . . . 5250 1 749 . 1 1 67 67 ILE HG22 H 1 0.34 0.02 . 1 . . . . . . . . 5250 1 750 . 1 1 67 67 ILE HG23 H 1 0.34 0.02 . 1 . . . . . . . . 5250 1 751 . 1 1 67 67 ILE CG2 C 13 18.4 0.05 . 1 . . . . . . . . 5250 1 752 . 1 1 67 67 ILE CG1 C 13 26.6 0.05 . 1 . . . . . . . . 5250 1 753 . 1 1 67 67 ILE HG12 H 1 0.77 0.02 . 2 . . . . . . . . 5250 1 754 . 1 1 67 67 ILE HG13 H 1 1.36 0.02 . 2 . . . . . . . . 5250 1 755 . 1 1 67 67 ILE HD11 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 756 . 1 1 67 67 ILE HD12 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 757 . 1 1 67 67 ILE HD13 H 1 0.63 0.02 . 1 . . . . . . . . 5250 1 758 . 1 1 67 67 ILE CD1 C 13 14.4 0.05 . 1 . . . . . . . . 5250 1 759 . 1 1 67 67 ILE C C 13 175.9 0.05 . 1 . . . . . . . . 5250 1 760 . 1 1 68 68 LEU N N 15 129.7 0.05 . 1 . . . . . . . . 5250 1 761 . 1 1 68 68 LEU H H 1 8.32 0.02 . 1 . . . . . . . . 5250 1 762 . 1 1 68 68 LEU CA C 13 56.8 0.05 . 1 . . . . . . . . 5250 1 763 . 1 1 68 68 LEU HA H 1 3.53 0.02 . 1 . . . . . . . . 5250 1 764 . 1 1 68 68 LEU CB C 13 42.7 0.05 . 1 . . . . . . . . 5250 1 765 . 1 1 68 68 LEU HB2 H 1 1.35 0.02 . 2 . . . . . . . . 5250 1 766 . 1 1 68 68 LEU HB3 H 1 1.69 0.02 . 2 . . . . . . . . 5250 1 767 . 1 1 68 68 LEU CG C 13 26.7 0.05 . 1 . . . . . . . . 5250 1 768 . 1 1 68 68 LEU HG H 1 1.24 0.02 . 1 . . . . . . . . 5250 1 769 . 1 1 68 68 LEU HD11 H 1 0.26 0.02 . 2 . . . . . . . . 5250 1 770 . 1 1 68 68 LEU HD12 H 1 0.26 0.02 . 2 . . . . . . . . 5250 1 771 . 1 1 68 68 LEU HD13 H 1 0.26 0.02 . 2 . . . . . . . . 5250 1 772 . 1 1 68 68 LEU HD21 H 1 0.63 0.02 . 2 . . . . . . . . 5250 1 773 . 1 1 68 68 LEU HD22 H 1 0.63 0.02 . 2 . . . . . . . . 5250 1 774 . 1 1 68 68 LEU HD23 H 1 0.63 0.02 . 2 . . . . . . . . 5250 1 775 . 1 1 68 68 LEU CD1 C 13 23.1 0.05 . 1 . . . . . . . . 5250 1 776 . 1 1 68 68 LEU CD2 C 13 26.0 0.05 . 1 . . . . . . . . 5250 1 777 . 1 1 68 68 LEU C C 13 176.7 0.05 . 1 . . . . . . . . 5250 1 778 . 1 1 69 69 LYS N N 15 130.7 0.05 . 1 . . . . . . . . 5250 1 779 . 1 1 69 69 LYS H H 1 8.58 0.02 . 1 . . . . . . . . 5250 1 780 . 1 1 69 69 LYS CA C 13 56.4 0.05 . 1 . . . . . . . . 5250 1 781 . 1 1 69 69 LYS HA H 1 4.26 0.02 . 1 . . . . . . . . 5250 1 782 . 1 1 69 69 LYS CB C 13 33.9 0.05 . 1 . . . . . . . . 5250 1 783 . 1 1 69 69 LYS HB2 H 1 1.38 0.02 . 2 . . . . . . . . 5250 1 784 . 1 1 69 69 LYS HB3 H 1 1.68 0.02 . 2 . . . . . . . . 5250 1 785 . 1 1 69 69 LYS CG C 13 24.9 0.05 . 1 . . . . . . . . 5250 1 786 . 1 1 69 69 LYS HG2 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 787 . 1 1 69 69 LYS HG3 H 1 1.23 0.02 . 1 . . . . . . . . 5250 1 788 . 1 1 69 69 LYS CD C 13 29.3 0.05 . 1 . . . . . . . . 5250 1 789 . 1 1 69 69 LYS HD2 H 1 1.47 0.02 . 2 . . . . . . . . 5250 1 790 . 1 1 69 69 LYS HD3 H 1 1.63 0.02 . 2 . . . . . . . . 5250 1 791 . 1 1 69 69 LYS CE C 13 42.5 0.05 . 1 . . . . . . . . 5250 1 792 . 1 1 69 69 LYS HE2 H 1 2.95 0.02 . 1 . . . . . . . . 5250 1 793 . 1 1 69 69 LYS HE3 H 1 2.95 0.02 . 1 . . . . . . . . 5250 1 794 . 1 1 69 69 LYS C C 13 175.5 0.05 . 1 . . . . . . . . 5250 1 795 . 1 1 70 70 ASP N N 15 126.7 0.05 . 1 . . . . . . . . 5250 1 796 . 1 1 70 70 ASP H H 1 8.36 0.02 . 1 . . . . . . . . 5250 1 797 . 1 1 70 70 ASP CA C 13 54.3 0.05 . 1 . . . . . . . . 5250 1 798 . 1 1 70 70 ASP HA H 1 4.68 0.02 . 1 . . . . . . . . 5250 1 799 . 1 1 70 70 ASP CB C 13 42.5 0.05 . 1 . . . . . . . . 5250 1 800 . 1 1 70 70 ASP HB2 H 1 2.56 0.02 . 2 . . . . . . . . 5250 1 801 . 1 1 70 70 ASP HB3 H 1 2.67 0.02 . 2 . . . . . . . . 5250 1 802 . 1 1 70 70 ASP C C 13 175.9 0.05 . 1 . . . . . . . . 5250 1 803 . 1 1 71 71 GLU N N 15 125.6 0.05 . 1 . . . . . . . . 5250 1 804 . 1 1 71 71 GLU H H 1 8.34 0.02 . 1 . . . . . . . . 5250 1 805 . 1 1 71 71 GLU CA C 13 56.5 0.05 . 1 . . . . . . . . 5250 1 806 . 1 1 71 71 GLU HA H 1 4.46 0.02 . 1 . . . . . . . . 5250 1 807 . 1 1 71 71 GLU CB C 13 31.0 0.05 . 1 . . . . . . . . 5250 1 808 . 1 1 71 71 GLU HB2 H 1 1.93 0.02 . 2 . . . . . . . . 5250 1 809 . 1 1 71 71 GLU HB3 H 1 2.13 0.02 . 2 . . . . . . . . 5250 1 810 . 1 1 71 71 GLU CG C 13 36.6 0.05 . 1 . . . . . . . . 5250 1 811 . 1 1 71 71 GLU HG2 H 1 2.24 0.02 . 1 . . . . . . . . 5250 1 812 . 1 1 71 71 GLU HG3 H 1 2.24 0.02 . 1 . . . . . . . . 5250 1 813 . 1 1 71 71 GLU C C 13 176.3 0.05 . 1 . . . . . . . . 5250 1 814 . 1 1 72 72 LYS N N 15 125.3 0.05 . 1 . . . . . . . . 5250 1 815 . 1 1 72 72 LYS H H 1 8.23 0.02 . 1 . . . . . . . . 5250 1 816 . 1 1 72 72 LYS CA C 13 56.9 0.05 . 1 . . . . . . . . 5250 1 817 . 1 1 72 72 LYS HA H 1 4.26 0.02 . 1 . . . . . . . . 5250 1 818 . 1 1 72 72 LYS CB C 13 33.3 0.05 . 1 . . . . . . . . 5250 1 819 . 1 1 72 72 LYS HB2 H 1 1.82 0.02 . 1 . . . . . . . . 5250 1 820 . 1 1 72 72 LYS HB3 H 1 1.82 0.02 . 1 . . . . . . . . 5250 1 821 . 1 1 72 72 LYS CG C 13 25.0 0.05 . 1 . . . . . . . . 5250 1 822 . 1 1 72 72 LYS HG2 H 1 1.41 0.02 . 1 . . . . . . . . 5250 1 823 . 1 1 72 72 LYS HG3 H 1 1.41 0.02 . 1 . . . . . . . . 5250 1 824 . 1 1 72 72 LYS CD C 13 29.5 0.05 . 1 . . . . . . . . 5250 1 825 . 1 1 72 72 LYS HD2 H 1 1.64 0.02 . 1 . . . . . . . . 5250 1 826 . 1 1 72 72 LYS HD3 H 1 1.64 0.02 . 1 . . . . . . . . 5250 1 827 . 1 1 72 72 LYS CE C 13 42.4 0.05 . 1 . . . . . . . . 5250 1 828 . 1 1 72 72 LYS HE2 H 1 2.98 0.02 . 1 . . . . . . . . 5250 1 829 . 1 1 72 72 LYS HE3 H 1 2.98 0.02 . 1 . . . . . . . . 5250 1 830 . 1 1 72 72 LYS C C 13 176.8 0.05 . 1 . . . . . . . . 5250 1 831 . 1 1 73 73 GLU N N 15 126.0 0.05 . 1 . . . . . . . . 5250 1 832 . 1 1 73 73 GLU H H 1 8.37 0.02 . 1 . . . . . . . . 5250 1 833 . 1 1 73 73 GLU CA C 13 56.9 0.05 . 1 . . . . . . . . 5250 1 834 . 1 1 73 73 GLU HA H 1 4.28 0.02 . 1 . . . . . . . . 5250 1 835 . 1 1 73 73 GLU CB C 13 30.6 0.05 . 1 . . . . . . . . 5250 1 836 . 1 1 73 73 GLU HB2 H 1 1.92 0.02 . 2 . . . . . . . . 5250 1 837 . 1 1 73 73 GLU HB3 H 1 2.06 0.02 . 2 . . . . . . . . 5250 1 838 . 1 1 73 73 GLU CG C 13 36.6 0.05 . 1 . . . . . . . . 5250 1 839 . 1 1 73 73 GLU HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5250 1 840 . 1 1 73 73 GLU HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5250 1 841 . 1 1 73 73 GLU C C 13 175.9 0.05 . 1 . . . . . . . . 5250 1 842 . 1 1 74 74 GLN N N 15 129.8 0.05 . 1 . . . . . . . . 5250 1 843 . 1 1 74 74 GLN H H 1 7.98 0.02 . 1 . . . . . . . . 5250 1 844 . 1 1 74 74 GLN CA C 13 57.7 0.05 . 1 . . . . . . . . 5250 1 845 . 1 1 74 74 GLN HA H 1 4.12 0.02 . 1 . . . . . . . . 5250 1 846 . 1 1 74 74 GLN CB C 13 30.7 0.05 . 1 . . . . . . . . 5250 1 847 . 1 1 74 74 GLN HB2 H 1 1.90 0.02 . 2 . . . . . . . . 5250 1 848 . 1 1 74 74 GLN HB3 H 1 2.08 0.02 . 2 . . . . . . . . 5250 1 849 . 1 1 74 74 GLN CG C 13 34.5 0.05 . 1 . . . . . . . . 5250 1 850 . 1 1 74 74 GLN HG2 H 1 2.28 0.02 . 1 . . . . . . . . 5250 1 851 . 1 1 74 74 GLN HG3 H 1 2.28 0.02 . 1 . . . . . . . . 5250 1 852 . 1 1 74 74 GLN NE2 N 15 115.8 0.05 . 1 . . . . . . . . 5250 1 853 . 1 1 74 74 GLN HE21 H 1 6.78 0.02 . 2 . . . . . . . . 5250 1 854 . 1 1 74 74 GLN HE22 H 1 7.51 0.02 . 2 . . . . . . . . 5250 1 stop_ save_