data_19800 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19800 _Entry.Title ; Structure of the PrgK first periplasmic domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-02-14 _Entry.Accession_date 2014-02-14 _Entry.Last_release_date 2014-10-27 _Entry.Original_release_date 2014-10-27 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 'SOLUTION NMR' _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 Julien Bergeron . . . 19800 2 Lawrence McIntosh . . . 19800 3 Natalie Strynadka . . . 19800 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 19800 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'macromolecular assemblies' . 19800 Salmonella . 19800 'Secretion systems' . 19800 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19800 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 250 19800 '15N chemical shifts' 57 19800 '1H chemical shifts' 400 19800 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2014-10-27 2014-02-14 original author . 19800 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2mky 'BMRB Entry Tracking System' 19800 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19800 _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 'The structure of PrgK reveals structural rearrangements upon assembly of the type III secretion system basal body.' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev Structure _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 Julien Bergeron . . . 19800 1 2 Liam Worrall . . . 19800 1 3 Soumya De . . . 19800 1 4 Nikolaos Sgourakis . . . 19800 1 5 Adrienne Cheung . . . 19800 1 6 Emilie Lameignere . . . 19800 1 7 Mark Okon . . . 19800 1 8 David Baker . . . 19800 1 9 Lawrence McIntosh . . . 19800 1 10 Natalie Strynadka . . . 19800 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19800 _Assembly.ID 1 _Assembly.Name 'PrgK first periplasmic domain' _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 'PrgK first periplasmic domain' 1 $entity A . yes native no no . . . 19800 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 19800 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; KDKDLLKGLDQEQANEVIAV LQMHNIEANKIDSGKLGYSI TVAEPDFTAAVYWIKTYQ ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 58 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6532.430 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2MKY . "Structure Of The Prgk First Periplasmic Domain" . . . . . 100.00 58 100.00 100.00 3.98e-33 . . . . 19800 1 2 no PDB 2Y9J . "Three-Dimensional Model Of Salmonella's Needle Complex At Subnanometer Resolution" . . . . . 96.55 170 100.00 100.00 2.14e-31 . . . . 19800 1 3 no PDB 3J6D . "Model Of The Prgh-prgk Periplasmic Rings" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 4 no PDB 4W4M . "Crystal Structure Of Prgk 19-92" . . . . . 100.00 78 100.00 100.00 3.33e-33 . . . . 19800 1 5 no DBJ BAJ37863 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 6 no DBJ BAP08776 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 7 no EMBL CAD05978 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 252 100.00 100.00 7.21e-32 . . . . 19800 1 8 no EMBL CAR34291 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 9 no EMBL CAR38583 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 10 no EMBL CAR60779 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 11 no EMBL CBG25840 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 12 no GB AAB60191 . "PrgK protein [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 13 no GB AAL21751 . "cell invasion protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 14 no GB AAO70334 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. Ty2]" . . . . . 100.00 252 100.00 100.00 7.21e-32 . . . . 19800 1 15 no GB AAV78586 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. ATCC 9150]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 16 no GB AAX66709 . "cell invasion protein; lipoprotein, may link inner and outer membranes [Salmonella enterica subsp. enterica serovar Choleraesui" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 17 no PIR AC0849 . "pathogenicity 1 island effector protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 252 100.00 100.00 7.21e-32 . . . . 19800 1 18 no REF NP_457265 . "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 252 100.00 100.00 7.21e-32 . . . . 19800 1 19 no REF NP_461792 . "secretion system lipoprotein PrgK [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 1 20 no REF WP_000001630 . "hypothetical protein, partial [Salmonella enterica]" . . . . . 98.28 233 100.00 100.00 2.40e-31 . . . . 19800 1 21 no REF WP_000621236 . "hypothetical protein [Salmonella enterica]" . . . . . 100.00 252 100.00 100.00 8.92e-32 . . . . 19800 1 22 no REF WP_000621237 . "hypothetical protein [Salmonella enterica]" . . . . . 100.00 252 100.00 100.00 7.77e-32 . . . . 19800 1 23 no SP P41786 . "RecName: Full=Lipoprotein PrgK; Flags: Precursor" . . . . . 100.00 252 100.00 100.00 7.29e-32 . . . . 19800 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 19 LYS . 19800 1 2 20 ASP . 19800 1 3 21 LYS . 19800 1 4 22 ASP . 19800 1 5 23 LEU . 19800 1 6 24 LEU . 19800 1 7 25 LYS . 19800 1 8 26 GLY . 19800 1 9 27 LEU . 19800 1 10 28 ASP . 19800 1 11 29 GLN . 19800 1 12 30 GLU . 19800 1 13 31 GLN . 19800 1 14 32 ALA . 19800 1 15 33 ASN . 19800 1 16 34 GLU . 19800 1 17 35 VAL . 19800 1 18 36 ILE . 19800 1 19 37 ALA . 19800 1 20 38 VAL . 19800 1 21 39 LEU . 19800 1 22 40 GLN . 19800 1 23 41 MET . 19800 1 24 42 HIS . 19800 1 25 43 ASN . 19800 1 26 44 ILE . 19800 1 27 45 GLU . 19800 1 28 46 ALA . 19800 1 29 47 ASN . 19800 1 30 48 LYS . 19800 1 31 49 ILE . 19800 1 32 50 ASP . 19800 1 33 51 SER . 19800 1 34 52 GLY . 19800 1 35 53 LYS . 19800 1 36 54 LEU . 19800 1 37 55 GLY . 19800 1 38 56 TYR . 19800 1 39 57 SER . 19800 1 40 58 ILE . 19800 1 41 59 THR . 19800 1 42 60 VAL . 19800 1 43 61 ALA . 19800 1 44 62 GLU . 19800 1 45 63 PRO . 19800 1 46 64 ASP . 19800 1 47 65 PHE . 19800 1 48 66 THR . 19800 1 49 67 ALA . 19800 1 50 68 ALA . 19800 1 51 69 VAL . 19800 1 52 70 TYR . 19800 1 53 71 TRP . 19800 1 54 72 ILE . 19800 1 55 73 LYS . 19800 1 56 74 THR . 19800 1 57 75 TYR . 19800 1 58 76 GLN . 19800 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 . LYS 1 1 19800 1 . ASP 2 2 19800 1 . LYS 3 3 19800 1 . ASP 4 4 19800 1 . LEU 5 5 19800 1 . LEU 6 6 19800 1 . LYS 7 7 19800 1 . GLY 8 8 19800 1 . LEU 9 9 19800 1 . ASP 10 10 19800 1 . GLN 11 11 19800 1 . GLU 12 12 19800 1 . GLN 13 13 19800 1 . ALA 14 14 19800 1 . ASN 15 15 19800 1 . GLU 16 16 19800 1 . VAL 17 17 19800 1 . ILE 18 18 19800 1 . ALA 19 19 19800 1 . VAL 20 20 19800 1 . LEU 21 21 19800 1 . GLN 22 22 19800 1 . MET 23 23 19800 1 . HIS 24 24 19800 1 . ASN 25 25 19800 1 . ILE 26 26 19800 1 . GLU 27 27 19800 1 . ALA 28 28 19800 1 . ASN 29 29 19800 1 . LYS 30 30 19800 1 . ILE 31 31 19800 1 . ASP 32 32 19800 1 . SER 33 33 19800 1 . GLY 34 34 19800 1 . LYS 35 35 19800 1 . LEU 36 36 19800 1 . GLY 37 37 19800 1 . TYR 38 38 19800 1 . SER 39 39 19800 1 . ILE 40 40 19800 1 . THR 41 41 19800 1 . VAL 42 42 19800 1 . ALA 43 43 19800 1 . GLU 44 44 19800 1 . PRO 45 45 19800 1 . ASP 46 46 19800 1 . PHE 47 47 19800 1 . THR 48 48 19800 1 . ALA 49 49 19800 1 . ALA 50 50 19800 1 . VAL 51 51 19800 1 . TYR 52 52 19800 1 . TRP 53 53 19800 1 . ILE 54 54 19800 1 . LYS 55 55 19800 1 . THR 56 56 19800 1 . TYR 57 57 19800 1 . GLN 58 58 19800 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 19800 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $entity . 90371 organism . 'Salmonella typhimurium' 'Salmonella typhimurium' . . Bacteria . Salmonella typhimurium . . . . . . . . . . . . . . . . . . . . . 19800 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 19800 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $entity . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET28a . . . . . . 19800 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19800 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 PrgK '[U-100% 13C; U-100% 15N]' . . 1 $entity . . 1 . . mM . . . . 19800 1 2 D2O 'natural abundance' . . . . . . 10 . . % . . . . 19800 1 3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19800 1 4 HEPES 'natural abundance' . . . . . . 25 . . mM . . . . 19800 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 19800 _Sample_condition_list.ID 1 _Sample_condition_list.Details '25 mM HEPES pH 6.8, 10 % D2O' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0 . M 19800 1 pH 6.8 . pH 19800 1 pressure 1 . atm 19800 1 temperature 273 . K 19800 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 19800 _Software.ID 1 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'G??ntert P.' . . 19800 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 19800 1 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 19800 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 850 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 19800 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 19800 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 850 . . . 19800 1 2 spectrometer_2 Bruker Avance . 600 . . . 19800 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 19800 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 5 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 6 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 7 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 8 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 9 '2D 1H-13C HSQC aromatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 10 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 11 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 1 12 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19800 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 19800 _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 TSP 'methyl protons' . . . . ppm . internal direct 1 . . . . . . . . . 19800 1 H 1 TSP 'methyl protons' . . . . ppm . internal direct 1 . . . . . . . . . 19800 1 N 15 TSP 'methyl protons' . . . . ppm . internal direct 1 . . . . . . . . . 19800 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 19800 _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 10 '3D 1H-13C NOESY aliphatic' 1 $sample_1 . 19800 1 11 '3D 1H-15N NOESY' 1 $sample_1 . 19800 1 12 '3D 1H-13C NOESY' 1 $sample_1 . 19800 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 LYS H H 1 8.508 0.003 . . . . . A 19 LYS H . 19800 1 2 . 1 1 1 1 LYS HA H 1 4.318 0.003 . . . . . A 19 LYS HA . 19800 1 3 . 1 1 1 1 LYS HB2 H 1 1.773 0.032 . . . . . A 19 LYS HB2 . 19800 1 4 . 1 1 1 1 LYS HB3 H 1 1.773 0.032 . . . . . A 19 LYS QB . 19800 1 5 . 1 1 1 1 LYS HG2 H 1 1.477 0 . . . . . A 19 LYS HG2 . 19800 1 6 . 1 1 1 1 LYS HG3 H 1 1.409 0.008 . . . . . A 19 LYS HG3 . 19800 1 7 . 1 1 1 1 LYS HD2 H 1 1.668 0.011 . . . . . A 19 LYS HD2 . 19800 1 8 . 1 1 1 1 LYS HD3 H 1 1.668 0.011 . . . . . A 19 LYS QD . 19800 1 9 . 1 1 1 1 LYS HE2 H 1 2.98 0.01 . . . . . A 19 LYS HE2 . 19800 1 10 . 1 1 1 1 LYS HE3 H 1 2.98 0.01 . . . . . A 19 LYS QE . 19800 1 11 . 1 1 1 1 LYS C C 13 176.021 0 . . . . . A 19 LYS C . 19800 1 12 . 1 1 1 1 LYS CA C 13 55.918 0.052 . . . . . A 19 LYS CA . 19800 1 13 . 1 1 1 1 LYS CB C 13 32.527 0.064 . . . . . A 19 LYS CB . 19800 1 14 . 1 1 1 1 LYS CG C 13 24.735 0.031 . . . . . A 19 LYS CG . 19800 1 15 . 1 1 1 1 LYS CD C 13 29.039 0.051 . . . . . A 19 LYS CD . 19800 1 16 . 1 1 1 1 LYS CE C 13 42.052 0.037 . . . . . A 19 LYS CE . 19800 1 17 . 1 1 1 1 LYS N N 15 122.797 0.028 . . . . . A 19 LYS N . 19800 1 18 . 1 1 2 2 ASP H H 1 8.066 0.005 . . . . . A 20 ASP H . 19800 1 19 . 1 1 2 2 ASP HA H 1 4.824 0.005 . . . . . A 20 ASP HA . 19800 1 20 . 1 1 2 2 ASP HB2 H 1 2.428 0.003 . . . . . A 20 ASP HB2 . 19800 1 21 . 1 1 2 2 ASP HB3 H 1 2.576 0.002 . . . . . A 20 ASP HB3 . 19800 1 22 . 1 1 2 2 ASP C C 13 176.378 0 . . . . . A 20 ASP C . 19800 1 23 . 1 1 2 2 ASP CA C 13 54.063 0.009 . . . . . A 20 ASP CA . 19800 1 24 . 1 1 2 2 ASP CB C 13 41.753 0.005 . . . . . A 20 ASP CB . 19800 1 25 . 1 1 2 2 ASP N N 15 121.855 0.045 . . . . . A 20 ASP N . 19800 1 26 . 1 1 3 3 LYS H H 1 9.136 0.003 . . . . . A 21 LYS H . 19800 1 27 . 1 1 3 3 LYS HA H 1 4.493 0.004 . . . . . A 21 LYS HA . 19800 1 28 . 1 1 3 3 LYS HB2 H 1 1.51 0.004 . . . . . A 21 LYS HB2 . 19800 1 29 . 1 1 3 3 LYS HB3 H 1 1.51 0.004 . . . . . A 21 LYS QB . 19800 1 30 . 1 1 3 3 LYS HG2 H 1 1.154 0.003 . . . . . A 21 LYS HG2 . 19800 1 31 . 1 1 3 3 LYS HG3 H 1 1.184 0.006 . . . . . A 21 LYS HG3 . 19800 1 32 . 1 1 3 3 LYS HD2 H 1 1.139 0 . . . . . A 21 LYS HD2 . 19800 1 33 . 1 1 3 3 LYS HD3 H 1 1.355 0.001 . . . . . A 21 LYS HD3 . 19800 1 34 . 1 1 3 3 LYS HE2 H 1 2.15 0 . . . . . A 21 LYS HE2 . 19800 1 35 . 1 1 3 3 LYS HE3 H 1 2.284 0 . . . . . A 21 LYS HE3 . 19800 1 36 . 1 1 3 3 LYS C C 13 175.887 0 . . . . . A 21 LYS C . 19800 1 37 . 1 1 3 3 LYS CA C 13 54.395 0.027 . . . . . A 21 LYS CA . 19800 1 38 . 1 1 3 3 LYS CB C 13 35.006 0.029 . . . . . A 21 LYS CB . 19800 1 39 . 1 1 3 3 LYS CG C 13 24.414 0.068 . . . . . A 21 LYS CG . 19800 1 40 . 1 1 3 3 LYS CD C 13 28.662 0.037 . . . . . A 21 LYS CD . 19800 1 41 . 1 1 3 3 LYS N N 15 121.556 0.011 . . . . . A 21 LYS N . 19800 1 42 . 1 1 4 4 ASP H H 1 8.429 0.003 . . . . . A 22 ASP H . 19800 1 43 . 1 1 4 4 ASP HA H 1 4.558 0.003 . . . . . A 22 ASP HA . 19800 1 44 . 1 1 4 4 ASP HB2 H 1 2.354 0.001 . . . . . A 22 ASP HB2 . 19800 1 45 . 1 1 4 4 ASP HB3 H 1 2.543 0.027 . . . . . A 22 ASP HB3 . 19800 1 46 . 1 1 4 4 ASP C C 13 175.402 0 . . . . . A 22 ASP C . 19800 1 47 . 1 1 4 4 ASP CA C 13 55.514 0.152 . . . . . A 22 ASP CA . 19800 1 48 . 1 1 4 4 ASP CB C 13 40.854 0.094 . . . . . A 22 ASP CB . 19800 1 49 . 1 1 4 4 ASP N N 15 123.097 0.023 . . . . . A 22 ASP N . 19800 1 50 . 1 1 5 5 LEU H H 1 9.313 0.003 . . . . . A 23 LEU H . 19800 1 51 . 1 1 5 5 LEU HA H 1 4.68 0.003 . . . . . A 23 LEU HA . 19800 1 52 . 1 1 5 5 LEU HB2 H 1 1.716 0.001 . . . . . A 23 LEU HB2 . 19800 1 53 . 1 1 5 5 LEU HB3 H 1 1.31 0.002 . . . . . A 23 LEU HB3 . 19800 1 54 . 1 1 5 5 LEU HG H 1 1.475 0 . . . . . A 23 LEU HG . 19800 1 55 . 1 1 5 5 LEU HD11 H 1 0.659 0.002 . . . . . A 23 LEU HD11 . 19800 1 56 . 1 1 5 5 LEU HD12 H 1 0.659 0.002 . . . . . A 23 LEU HD12 . 19800 1 57 . 1 1 5 5 LEU HD13 H 1 0.659 0.002 . . . . . A 23 LEU HD13 . 19800 1 58 . 1 1 5 5 LEU HD21 H 1 0.712 0.002 . . . . . A 23 LEU HD21 . 19800 1 59 . 1 1 5 5 LEU HD22 H 1 0.712 0.002 . . . . . A 23 LEU HD22 . 19800 1 60 . 1 1 5 5 LEU HD23 H 1 0.712 0.002 . . . . . A 23 LEU HD23 . 19800 1 61 . 1 1 5 5 LEU C C 13 176.338 0 . . . . . A 23 LEU C . 19800 1 62 . 1 1 5 5 LEU CA C 13 56.204 0.059 . . . . . A 23 LEU CA . 19800 1 63 . 1 1 5 5 LEU CB C 13 45.211 0.023 . . . . . A 23 LEU CB . 19800 1 64 . 1 1 5 5 LEU CD1 C 13 24.805 0.057 . . . . . A 23 LEU CD1 . 19800 1 65 . 1 1 5 5 LEU CD2 C 13 27.408 0.077 . . . . . A 23 LEU CD2 . 19800 1 66 . 1 1 5 5 LEU N N 15 126.265 0.013 . . . . . A 23 LEU N . 19800 1 67 . 1 1 6 6 LEU H H 1 7.346 0.002 . . . . . A 24 LEU H . 19800 1 68 . 1 1 6 6 LEU HA H 1 4.789 0 . . . . . A 24 LEU HA . 19800 1 69 . 1 1 6 6 LEU HB2 H 1 1.406 0.002 . . . . . A 24 LEU HB2 . 19800 1 70 . 1 1 6 6 LEU HB3 H 1 1.551 0.007 . . . . . A 24 LEU HB3 . 19800 1 71 . 1 1 6 6 LEU HD11 H 1 0.902 0.008 . . . . . A 24 LEU HD11 . 19800 1 72 . 1 1 6 6 LEU HD12 H 1 0.902 0.008 . . . . . A 24 LEU HD12 . 19800 1 73 . 1 1 6 6 LEU HD13 H 1 0.902 0.008 . . . . . A 24 LEU HD13 . 19800 1 74 . 1 1 6 6 LEU HD21 H 1 1.034 0.007 . . . . . A 24 LEU HD21 . 19800 1 75 . 1 1 6 6 LEU HD22 H 1 1.034 0.007 . . . . . A 24 LEU HD22 . 19800 1 76 . 1 1 6 6 LEU HD23 H 1 1.034 0.007 . . . . . A 24 LEU HD23 . 19800 1 77 . 1 1 6 6 LEU C C 13 174.976 0 . . . . . A 24 LEU C . 19800 1 78 . 1 1 6 6 LEU CA C 13 53.674 0.035 . . . . . A 24 LEU CA . 19800 1 79 . 1 1 6 6 LEU CB C 13 49.345 0.018 . . . . . A 24 LEU CB . 19800 1 80 . 1 1 6 6 LEU CG C 13 23.722 0 . . . . . A 24 LEU CG . 19800 1 81 . 1 1 6 6 LEU CD1 C 13 27.484 0.068 . . . . . A 24 LEU CD1 . 19800 1 82 . 1 1 6 6 LEU CD2 C 13 23.674 0.094 . . . . . A 24 LEU CD2 . 19800 1 83 . 1 1 6 6 LEU N N 15 114.484 0.013 . . . . . A 24 LEU N . 19800 1 84 . 1 1 7 7 LYS H H 1 8.516 0.003 . . . . . A 25 LYS H . 19800 1 85 . 1 1 7 7 LYS HA H 1 4.994 0.002 . . . . . A 25 LYS HA . 19800 1 86 . 1 1 7 7 LYS HB2 H 1 1.883 0.002 . . . . . A 25 LYS HB2 . 19800 1 87 . 1 1 7 7 LYS HB3 H 1 1.664 0.013 . . . . . A 25 LYS HB3 . 19800 1 88 . 1 1 7 7 LYS HG2 H 1 1.32 0.004 . . . . . A 25 LYS HG2 . 19800 1 89 . 1 1 7 7 LYS HG3 H 1 1.416 0.004 . . . . . A 25 LYS HG3 . 19800 1 90 . 1 1 7 7 LYS HE2 H 1 2.913 0.001 . . . . . A 25 LYS HE2 . 19800 1 91 . 1 1 7 7 LYS HE3 H 1 2.913 0.001 . . . . . A 25 LYS QE . 19800 1 92 . 1 1 7 7 LYS C C 13 176.242 0 . . . . . A 25 LYS C . 19800 1 93 . 1 1 7 7 LYS CA C 13 55.21 0.048 . . . . . A 25 LYS CA . 19800 1 94 . 1 1 7 7 LYS CB C 13 35.992 0.021 . . . . . A 25 LYS CB . 19800 1 95 . 1 1 7 7 LYS CG C 13 23.95 0.029 . . . . . A 25 LYS CG . 19800 1 96 . 1 1 7 7 LYS CD C 13 29.048 0 . . . . . A 25 LYS CD . 19800 1 97 . 1 1 7 7 LYS CE C 13 41.943 0.026 . . . . . A 25 LYS CE . 19800 1 98 . 1 1 7 7 LYS N N 15 118.529 0.008 . . . . . A 25 LYS N . 19800 1 99 . 1 1 8 8 GLY H H 1 8.265 0.002 . . . . . A 26 GLY H . 19800 1 100 . 1 1 8 8 GLY HA2 H 1 3.957 0.002 . . . . . A 26 GLY HA2 . 19800 1 101 . 1 1 8 8 GLY HA3 H 1 4.188 0.002 . . . . . A 26 GLY HA3 . 19800 1 102 . 1 1 8 8 GLY C C 13 176.034 0 . . . . . A 26 GLY C . 19800 1 103 . 1 1 8 8 GLY CA C 13 46.394 0.02 . . . . . A 26 GLY CA . 19800 1 104 . 1 1 8 8 GLY N N 15 107.756 0.014 . . . . . A 26 GLY N . 19800 1 105 . 1 1 9 9 LEU H H 1 8.884 0.004 . . . . . A 27 LEU H . 19800 1 106 . 1 1 9 9 LEU HA H 1 4.601 0.003 . . . . . A 27 LEU HA . 19800 1 107 . 1 1 9 9 LEU HB2 H 1 1.754 0 . . . . . A 27 LEU HB2 . 19800 1 108 . 1 1 9 9 LEU HB3 H 1 1.738 0.004 . . . . . A 27 LEU HB3 . 19800 1 109 . 1 1 9 9 LEU HG H 1 1.535 0.005 . . . . . A 27 LEU HG . 19800 1 110 . 1 1 9 9 LEU HD11 H 1 0.737 0.003 . . . . . A 27 LEU HD11 . 19800 1 111 . 1 1 9 9 LEU HD12 H 1 0.737 0.003 . . . . . A 27 LEU HD12 . 19800 1 112 . 1 1 9 9 LEU HD13 H 1 0.737 0.003 . . . . . A 27 LEU HD13 . 19800 1 113 . 1 1 9 9 LEU HD21 H 1 0.657 0.003 . . . . . A 27 LEU HD21 . 19800 1 114 . 1 1 9 9 LEU HD22 H 1 0.657 0.003 . . . . . A 27 LEU HD22 . 19800 1 115 . 1 1 9 9 LEU HD23 H 1 0.657 0.003 . . . . . A 27 LEU HD23 . 19800 1 116 . 1 1 9 9 LEU C C 13 179.874 0 . . . . . A 27 LEU C . 19800 1 117 . 1 1 9 9 LEU CA C 13 54.325 0.006 . . . . . A 27 LEU CA . 19800 1 118 . 1 1 9 9 LEU CB C 13 43.622 0.014 . . . . . A 27 LEU CB . 19800 1 119 . 1 1 9 9 LEU CG C 13 26.485 0 . . . . . A 27 LEU CG . 19800 1 120 . 1 1 9 9 LEU CD1 C 13 21.913 0.137 . . . . . A 27 LEU CD1 . 19800 1 121 . 1 1 9 9 LEU CD2 C 13 26.366 0.082 . . . . . A 27 LEU CD2 . 19800 1 122 . 1 1 9 9 LEU N N 15 120.147 0.018 . . . . . A 27 LEU N . 19800 1 123 . 1 1 10 10 ASP H H 1 8.555 0.004 . . . . . A 28 ASP H . 19800 1 124 . 1 1 10 10 ASP HA H 1 5.096 0.003 . . . . . A 28 ASP HA . 19800 1 125 . 1 1 10 10 ASP HB2 H 1 2.75 0.006 . . . . . A 28 ASP HB2 . 19800 1 126 . 1 1 10 10 ASP HB3 H 1 3.185 0.002 . . . . . A 28 ASP HB3 . 19800 1 127 . 1 1 10 10 ASP C C 13 177.406 0 . . . . . A 28 ASP C . 19800 1 128 . 1 1 10 10 ASP CA C 13 52.835 0.17 . . . . . A 28 ASP CA . 19800 1 129 . 1 1 10 10 ASP CB C 13 41.18 0.01 . . . . . A 28 ASP CB . 19800 1 130 . 1 1 10 10 ASP N N 15 119.966 0.01 . . . . . A 28 ASP N . 19800 1 131 . 1 1 11 11 GLN H H 1 8.705 0.002 . . . . . A 29 GLN H . 19800 1 132 . 1 1 11 11 GLN HA H 1 2.969 0.002 . . . . . A 29 GLN HA . 19800 1 133 . 1 1 11 11 GLN HB2 H 1 1.962 0.005 . . . . . A 29 GLN HB2 . 19800 1 134 . 1 1 11 11 GLN HB3 H 1 1.962 0.005 . . . . . A 29 GLN QB . 19800 1 135 . 1 1 11 11 GLN HG2 H 1 2.137 0.002 . . . . . A 29 GLN HG2 . 19800 1 136 . 1 1 11 11 GLN HG3 H 1 1.81 0.003 . . . . . A 29 GLN HG3 . 19800 1 137 . 1 1 11 11 GLN C C 13 178.379 0 . . . . . A 29 GLN C . 19800 1 138 . 1 1 11 11 GLN CA C 13 59.978 0.008 . . . . . A 29 GLN CA . 19800 1 139 . 1 1 11 11 GLN CB C 13 28.897 0.084 . . . . . A 29 GLN CB . 19800 1 140 . 1 1 11 11 GLN CG C 13 34.174 0.136 . . . . . A 29 GLN CG . 19800 1 141 . 1 1 11 11 GLN N N 15 118.219 0.021 . . . . . A 29 GLN N . 19800 1 142 . 1 1 12 12 GLU H H 1 8.135 0.005 . . . . . A 30 GLU H . 19800 1 143 . 1 1 12 12 GLU HA H 1 3.986 0.002 . . . . . A 30 GLU HA . 19800 1 144 . 1 1 12 12 GLU HB2 H 1 2.054 0.013 . . . . . A 30 GLU HB2 . 19800 1 145 . 1 1 12 12 GLU HB3 H 1 2.054 0.013 . . . . . A 30 GLU QB . 19800 1 146 . 1 1 12 12 GLU HG2 H 1 2.303 0.003 . . . . . A 30 GLU HG2 . 19800 1 147 . 1 1 12 12 GLU HG3 H 1 2.303 0.003 . . . . . A 30 GLU QG . 19800 1 148 . 1 1 12 12 GLU C C 13 182.812 0 . . . . . A 30 GLU C . 19800 1 149 . 1 1 12 12 GLU CA C 13 59.73 0.05 . . . . . A 30 GLU CA . 19800 1 150 . 1 1 12 12 GLU CB C 13 28.936 0.047 . . . . . A 30 GLU CB . 19800 1 151 . 1 1 12 12 GLU CG C 13 36.681 0.041 . . . . . A 30 GLU CG . 19800 1 152 . 1 1 12 12 GLU N N 15 118.429 0.008 . . . . . A 30 GLU N . 19800 1 153 . 1 1 13 13 GLN H H 1 8.742 0.003 . . . . . A 31 GLN H . 19800 1 154 . 1 1 13 13 GLN HA H 1 4.068 0.003 . . . . . A 31 GLN HA . 19800 1 155 . 1 1 13 13 GLN HB2 H 1 1.894 0.003 . . . . . A 31 GLN HB2 . 19800 1 156 . 1 1 13 13 GLN HB3 H 1 2.321 0.002 . . . . . A 31 GLN HB3 . 19800 1 157 . 1 1 13 13 GLN HG2 H 1 2.403 0.001 . . . . . A 31 GLN HG2 . 19800 1 158 . 1 1 13 13 GLN HG3 H 1 2.799 0 . . . . . A 31 GLN HG3 . 19800 1 159 . 1 1 13 13 GLN C C 13 180.864 0 . . . . . A 31 GLN C . 19800 1 160 . 1 1 13 13 GLN CA C 13 58.612 0.023 . . . . . A 31 GLN CA . 19800 1 161 . 1 1 13 13 GLN CB C 13 29.844 0.083 . . . . . A 31 GLN CB . 19800 1 162 . 1 1 13 13 GLN CG C 13 34.424 0.01 . . . . . A 31 GLN CG . 19800 1 163 . 1 1 13 13 GLN N N 15 120.672 0.005 . . . . . A 31 GLN N . 19800 1 164 . 1 1 14 14 ALA H H 1 8.408 0.003 . . . . . A 32 ALA H . 19800 1 165 . 1 1 14 14 ALA HA H 1 3.771 0.002 . . . . . A 32 ALA HA . 19800 1 166 . 1 1 14 14 ALA HB1 H 1 1.033 0.004 . . . . . A 32 ALA HB1 . 19800 1 167 . 1 1 14 14 ALA HB2 H 1 1.033 0.004 . . . . . A 32 ALA HB2 . 19800 1 168 . 1 1 14 14 ALA HB3 H 1 1.033 0.004 . . . . . A 32 ALA HB3 . 19800 1 169 . 1 1 14 14 ALA C C 13 180.339 0 . . . . . A 32 ALA C . 19800 1 170 . 1 1 14 14 ALA CA C 13 55.122 0.04 . . . . . A 32 ALA CA . 19800 1 171 . 1 1 14 14 ALA CB C 13 17.289 0.077 . . . . . A 32 ALA CB . 19800 1 172 . 1 1 14 14 ALA N N 15 120.2 0.011 . . . . . A 32 ALA N . 19800 1 173 . 1 1 15 15 ASN H H 1 8.077 0.003 . . . . . A 33 ASN H . 19800 1 174 . 1 1 15 15 ASN HA H 1 4.292 0.002 . . . . . A 33 ASN HA . 19800 1 175 . 1 1 15 15 ASN HB2 H 1 2.705 0.002 . . . . . A 33 ASN HB2 . 19800 1 176 . 1 1 15 15 ASN HB3 H 1 2.854 0.016 . . . . . A 33 ASN HB3 . 19800 1 177 . 1 1 15 15 ASN C C 13 180.713 0 . . . . . A 33 ASN C . 19800 1 178 . 1 1 15 15 ASN CA C 13 55.479 0.015 . . . . . A 33 ASN CA . 19800 1 179 . 1 1 15 15 ASN CB C 13 37.104 0.038 . . . . . A 33 ASN CB . 19800 1 180 . 1 1 15 15 ASN N N 15 115.507 0.017 . . . . . A 33 ASN N . 19800 1 181 . 1 1 16 16 GLU H H 1 7.973 0.003 . . . . . A 34 GLU H . 19800 1 182 . 1 1 16 16 GLU HA H 1 4.083 0.002 . . . . . A 34 GLU HA . 19800 1 183 . 1 1 16 16 GLU HB2 H 1 2.188 0.015 . . . . . A 34 GLU HB2 . 19800 1 184 . 1 1 16 16 GLU HB3 H 1 2.188 0.015 . . . . . A 34 GLU QB . 19800 1 185 . 1 1 16 16 GLU HG2 H 1 2.386 0.001 . . . . . A 34 GLU HG2 . 19800 1 186 . 1 1 16 16 GLU HG3 H 1 2.386 0.001 . . . . . A 34 GLU QG . 19800 1 187 . 1 1 16 16 GLU C C 13 180.367 0 . . . . . A 34 GLU C . 19800 1 188 . 1 1 16 16 GLU CA C 13 59.486 0.035 . . . . . A 34 GLU CA . 19800 1 189 . 1 1 16 16 GLU CB C 13 29.37 0.031 . . . . . A 34 GLU CB . 19800 1 190 . 1 1 16 16 GLU CG C 13 36.07 0.014 . . . . . A 34 GLU CG . 19800 1 191 . 1 1 16 16 GLU N N 15 122.826 0.01 . . . . . A 34 GLU N . 19800 1 192 . 1 1 17 17 VAL H H 1 8.025 0.002 . . . . . A 35 VAL H . 19800 1 193 . 1 1 17 17 VAL HA H 1 3.373 0.002 . . . . . A 35 VAL HA . 19800 1 194 . 1 1 17 17 VAL HB H 1 1.969 0.002 . . . . . A 35 VAL HB . 19800 1 195 . 1 1 17 17 VAL HG11 H 1 0.742 0.01 . . . . . A 35 VAL HG11 . 19800 1 196 . 1 1 17 17 VAL HG12 H 1 0.742 0.01 . . . . . A 35 VAL HG12 . 19800 1 197 . 1 1 17 17 VAL HG13 H 1 0.742 0.01 . . . . . A 35 VAL HG13 . 19800 1 198 . 1 1 17 17 VAL HG21 H 1 0.745 0.006 . . . . . A 35 VAL HG21 . 19800 1 199 . 1 1 17 17 VAL HG22 H 1 0.745 0.006 . . . . . A 35 VAL HG22 . 19800 1 200 . 1 1 17 17 VAL HG23 H 1 0.745 0.006 . . . . . A 35 VAL HG23 . 19800 1 201 . 1 1 17 17 VAL C C 13 179.502 0 . . . . . A 35 VAL C . 19800 1 202 . 1 1 17 17 VAL CA C 13 66.809 0.041 . . . . . A 35 VAL CA . 19800 1 203 . 1 1 17 17 VAL CB C 13 31 0 . . . . . A 35 VAL CB . 19800 1 204 . 1 1 17 17 VAL CG1 C 13 22.474 0.029 . . . . . A 35 VAL CG1 . 19800 1 205 . 1 1 17 17 VAL CG2 C 13 22.183 0.013 . . . . . A 35 VAL CG2 . 19800 1 206 . 1 1 17 17 VAL N N 15 119.909 0.007 . . . . . A 35 VAL N . 19800 1 207 . 1 1 18 18 ILE H H 1 8.031 0.004 . . . . . A 36 ILE H . 19800 1 208 . 1 1 18 18 ILE HA H 1 3.514 0.002 . . . . . A 36 ILE HA . 19800 1 209 . 1 1 18 18 ILE HB H 1 2.011 0.001 . . . . . A 36 ILE HB . 19800 1 210 . 1 1 18 18 ILE HG12 H 1 1.524 0.001 . . . . . A 36 ILE HG12 . 19800 1 211 . 1 1 18 18 ILE HG13 H 1 1.352 0.002 . . . . . A 36 ILE HG13 . 19800 1 212 . 1 1 18 18 ILE HG21 H 1 0.902 0.002 . . . . . A 36 ILE HG21 . 19800 1 213 . 1 1 18 18 ILE HG22 H 1 0.902 0.002 . . . . . A 36 ILE HG22 . 19800 1 214 . 1 1 18 18 ILE HG23 H 1 0.902 0.002 . . . . . A 36 ILE HG23 . 19800 1 215 . 1 1 18 18 ILE HD11 H 1 0.695 0.003 . . . . . A 36 ILE HD11 . 19800 1 216 . 1 1 18 18 ILE HD12 H 1 0.695 0.003 . . . . . A 36 ILE HD12 . 19800 1 217 . 1 1 18 18 ILE HD13 H 1 0.695 0.003 . . . . . A 36 ILE HD13 . 19800 1 218 . 1 1 18 18 ILE C C 13 180.436 0 . . . . . A 36 ILE C . 19800 1 219 . 1 1 18 18 ILE CA C 13 64.355 0.039 . . . . . A 36 ILE CA . 19800 1 220 . 1 1 18 18 ILE CB C 13 36.534 0.023 . . . . . A 36 ILE CB . 19800 1 221 . 1 1 18 18 ILE CG1 C 13 28.463 0.063 . . . . . A 36 ILE CG1 . 19800 1 222 . 1 1 18 18 ILE CG2 C 13 16.82 0.094 . . . . . A 36 ILE CG2 . 19800 1 223 . 1 1 18 18 ILE CD1 C 13 11.96 0.104 . . . . . A 36 ILE CD1 . 19800 1 224 . 1 1 18 18 ILE N N 15 118.626 0.017 . . . . . A 36 ILE N . 19800 1 225 . 1 1 19 19 ALA H H 1 7.69 0.003 . . . . . A 37 ALA H . 19800 1 226 . 1 1 19 19 ALA HA H 1 4.145 0.001 . . . . . A 37 ALA HA . 19800 1 227 . 1 1 19 19 ALA HB1 H 1 1.482 0.002 . . . . . A 37 ALA HB1 . 19800 1 228 . 1 1 19 19 ALA HB2 H 1 1.482 0.002 . . . . . A 37 ALA HB2 . 19800 1 229 . 1 1 19 19 ALA HB3 H 1 1.482 0.002 . . . . . A 37 ALA HB3 . 19800 1 230 . 1 1 19 19 ALA C C 13 183.902 0 . . . . . A 37 ALA C . 19800 1 231 . 1 1 19 19 ALA CA C 13 55.433 0 . . . . . A 37 ALA CA . 19800 1 232 . 1 1 19 19 ALA CB C 13 17.807 0.09 . . . . . A 37 ALA CB . 19800 1 233 . 1 1 19 19 ALA N N 15 122.361 0.007 . . . . . A 37 ALA N . 19800 1 234 . 1 1 20 20 VAL H H 1 8.177 0.001 . . . . . A 38 VAL H . 19800 1 235 . 1 1 20 20 VAL HA H 1 3.63 0.002 . . . . . A 38 VAL HA . 19800 1 236 . 1 1 20 20 VAL HB H 1 2.113 0.001 . . . . . A 38 VAL HB . 19800 1 237 . 1 1 20 20 VAL HG11 H 1 0.988 0.016 . . . . . A 38 VAL HG11 . 19800 1 238 . 1 1 20 20 VAL HG12 H 1 0.988 0.016 . . . . . A 38 VAL HG12 . 19800 1 239 . 1 1 20 20 VAL HG13 H 1 0.988 0.016 . . . . . A 38 VAL HG13 . 19800 1 240 . 1 1 20 20 VAL HG21 H 1 0.911 0.01 . . . . . A 38 VAL HG21 . 19800 1 241 . 1 1 20 20 VAL HG22 H 1 0.911 0.01 . . . . . A 38 VAL HG22 . 19800 1 242 . 1 1 20 20 VAL HG23 H 1 0.911 0.01 . . . . . A 38 VAL HG23 . 19800 1 243 . 1 1 20 20 VAL C C 13 180.529 0 . . . . . A 38 VAL C . 19800 1 244 . 1 1 20 20 VAL CA C 13 66.453 0.045 . . . . . A 38 VAL CA . 19800 1 245 . 1 1 20 20 VAL CB C 13 31.763 0.039 . . . . . A 38 VAL CB . 19800 1 246 . 1 1 20 20 VAL CG1 C 13 22.658 0.079 . . . . . A 38 VAL CG1 . 19800 1 247 . 1 1 20 20 VAL CG2 C 13 20.969 0.075 . . . . . A 38 VAL CG2 . 19800 1 248 . 1 1 20 20 VAL N N 15 120.987 0.006 . . . . . A 38 VAL N . 19800 1 249 . 1 1 21 21 LEU H H 1 8.197 0.002 . . . . . A 39 LEU H . 19800 1 250 . 1 1 21 21 LEU HA H 1 3.929 0.007 . . . . . A 39 LEU HA . 19800 1 251 . 1 1 21 21 LEU HB2 H 1 1.488 0.001 . . . . . A 39 LEU HB2 . 19800 1 252 . 1 1 21 21 LEU HB3 H 1 1.833 0.01 . . . . . A 39 LEU HB3 . 19800 1 253 . 1 1 21 21 LEU HG H 1 0.576 0.003 . . . . . A 39 LEU HG . 19800 1 254 . 1 1 21 21 LEU HD11 H 1 0.907 0.002 . . . . . A 39 LEU HD11 . 19800 1 255 . 1 1 21 21 LEU HD12 H 1 0.907 0.002 . . . . . A 39 LEU HD12 . 19800 1 256 . 1 1 21 21 LEU HD13 H 1 0.907 0.002 . . . . . A 39 LEU HD13 . 19800 1 257 . 1 1 21 21 LEU C C 13 183.063 0 . . . . . A 39 LEU C . 19800 1 258 . 1 1 21 21 LEU CA C 13 58.544 0.038 . . . . . A 39 LEU CA . 19800 1 259 . 1 1 21 21 LEU CB C 13 39.409 0.019 . . . . . A 39 LEU CB . 19800 1 260 . 1 1 21 21 LEU CG C 13 26.616 0.077 . . . . . A 39 LEU CG . 19800 1 261 . 1 1 21 21 LEU CD1 C 13 22.814 0.063 . . . . . A 39 LEU CD1 . 19800 1 262 . 1 1 21 21 LEU N N 15 119.408 0.012 . . . . . A 39 LEU N . 19800 1 263 . 1 1 22 22 GLN H H 1 8.615 0.003 . . . . . A 40 GLN H . 19800 1 264 . 1 1 22 22 GLN HA H 1 3.928 0.006 . . . . . A 40 GLN HA . 19800 1 265 . 1 1 22 22 GLN HB2 H 1 2.088 0.003 . . . . . A 40 GLN HB2 . 19800 1 266 . 1 1 22 22 GLN HB3 H 1 2.274 0.003 . . . . . A 40 GLN HB3 . 19800 1 267 . 1 1 22 22 GLN HG2 H 1 2.509 0 . . . . . A 40 GLN HG2 . 19800 1 268 . 1 1 22 22 GLN HG3 H 1 2.358 0 . . . . . A 40 GLN HG3 . 19800 1 269 . 1 1 22 22 GLN C C 13 183.366 0 . . . . . A 40 GLN C . 19800 1 270 . 1 1 22 22 GLN CA C 13 59.324 0.041 . . . . . A 40 GLN CA . 19800 1 271 . 1 1 22 22 GLN CB C 13 28.254 0.03 . . . . . A 40 GLN CB . 19800 1 272 . 1 1 22 22 GLN CG C 13 34.149 0 . . . . . A 40 GLN CG . 19800 1 273 . 1 1 22 22 GLN N N 15 121.514 0.043 . . . . . A 40 GLN N . 19800 1 274 . 1 1 23 23 MET H H 1 7.706 0.003 . . . . . A 41 MET H . 19800 1 275 . 1 1 23 23 MET HA H 1 4.032 0.004 . . . . . A 41 MET HA . 19800 1 276 . 1 1 23 23 MET HB2 H 1 1.764 0.002 . . . . . A 41 MET HB2 . 19800 1 277 . 1 1 23 23 MET HB3 H 1 2.35 0.019 . . . . . A 41 MET HB3 . 19800 1 278 . 1 1 23 23 MET HG2 H 1 2.026 0.001 . . . . . A 41 MET HG2 . 19800 1 279 . 1 1 23 23 MET HG3 H 1 2.353 0 . . . . . A 41 MET HG3 . 19800 1 280 . 1 1 23 23 MET C C 13 177.125 0 . . . . . A 41 MET C . 19800 1 281 . 1 1 23 23 MET CA C 13 57.763 0.035 . . . . . A 41 MET CA . 19800 1 282 . 1 1 23 23 MET CB C 13 31.579 0.166 . . . . . A 41 MET CB . 19800 1 283 . 1 1 23 23 MET CG C 13 31.48 0.013 . . . . . A 41 MET CG . 19800 1 284 . 1 1 23 23 MET N N 15 119.672 0.011 . . . . . A 41 MET N . 19800 1 285 . 1 1 24 24 HIS H H 1 7.218 0.003 . . . . . A 42 HIS H . 19800 1 286 . 1 1 24 24 HIS HA H 1 4.371 0.001 . . . . . A 42 HIS HA . 19800 1 287 . 1 1 24 24 HIS HB2 H 1 2.178 0.001 . . . . . A 42 HIS HB2 . 19800 1 288 . 1 1 24 24 HIS HB3 H 1 3 0.002 . . . . . A 42 HIS HB3 . 19800 1 289 . 1 1 24 24 HIS HD2 H 1 6.729 0.003 . . . . . A 42 HIS HD2 . 19800 1 290 . 1 1 24 24 HIS HE1 H 1 6.724 0 . . . . . A 42 HIS HE1 . 19800 1 291 . 1 1 24 24 HIS C C 13 171.216 0 . . . . . A 42 HIS C . 19800 1 292 . 1 1 24 24 HIS CA C 13 54.601 0.007 . . . . . A 42 HIS CA . 19800 1 293 . 1 1 24 24 HIS CB C 13 27.399 0.052 . . . . . A 42 HIS CB . 19800 1 294 . 1 1 24 24 HIS CD2 C 13 119.787 0.156 . . . . . A 42 HIS CD2 . 19800 1 295 . 1 1 24 24 HIS N N 15 115.329 0.011 . . . . . A 42 HIS N . 19800 1 296 . 1 1 25 25 ASN H H 1 7.855 0.003 . . . . . A 43 ASN H . 19800 1 297 . 1 1 25 25 ASN HA H 1 4.293 0.002 . . . . . A 43 ASN HA . 19800 1 298 . 1 1 25 25 ASN HB2 H 1 2.821 0.001 . . . . . A 43 ASN HB2 . 19800 1 299 . 1 1 25 25 ASN HB3 H 1 3.106 0.002 . . . . . A 43 ASN HB3 . 19800 1 300 . 1 1 25 25 ASN C C 13 173.011 0 . . . . . A 43 ASN C . 19800 1 301 . 1 1 25 25 ASN CA C 13 54.571 0.023 . . . . . A 43 ASN CA . 19800 1 302 . 1 1 25 25 ASN CB C 13 36.981 0.02 . . . . . A 43 ASN CB . 19800 1 303 . 1 1 25 25 ASN N N 15 112.995 0.008 . . . . . A 43 ASN N . 19800 1 304 . 1 1 26 26 ILE H H 1 7.978 0.002 . . . . . A 44 ILE H . 19800 1 305 . 1 1 26 26 ILE HA H 1 4.225 0.003 . . . . . A 44 ILE HA . 19800 1 306 . 1 1 26 26 ILE HB H 1 1.592 0.002 . . . . . A 44 ILE HB . 19800 1 307 . 1 1 26 26 ILE HG12 H 1 1.654 0.002 . . . . . A 44 ILE HG12 . 19800 1 308 . 1 1 26 26 ILE HG13 H 1 1.654 0.002 . . . . . A 44 ILE QG1 . 19800 1 309 . 1 1 26 26 ILE HG21 H 1 0.855 0.004 . . . . . A 44 ILE HG21 . 19800 1 310 . 1 1 26 26 ILE HG22 H 1 0.855 0.004 . . . . . A 44 ILE HG22 . 19800 1 311 . 1 1 26 26 ILE HG23 H 1 0.855 0.004 . . . . . A 44 ILE HG23 . 19800 1 312 . 1 1 26 26 ILE HD11 H 1 0.996 0.002 . . . . . A 44 ILE HD11 . 19800 1 313 . 1 1 26 26 ILE HD12 H 1 0.996 0.002 . . . . . A 44 ILE HD12 . 19800 1 314 . 1 1 26 26 ILE HD13 H 1 0.996 0.002 . . . . . A 44 ILE HD13 . 19800 1 315 . 1 1 26 26 ILE C C 13 174.63 0 . . . . . A 44 ILE C . 19800 1 316 . 1 1 26 26 ILE CA C 13 60.469 0.038 . . . . . A 44 ILE CA . 19800 1 317 . 1 1 26 26 ILE CB C 13 39.933 0.019 . . . . . A 44 ILE CB . 19800 1 318 . 1 1 26 26 ILE CG1 C 13 27.408 0 . . . . . A 44 ILE CG1 . 19800 1 319 . 1 1 26 26 ILE CG2 C 13 17.382 0.079 . . . . . A 44 ILE CG2 . 19800 1 320 . 1 1 26 26 ILE CD1 C 13 14.477 0.086 . . . . . A 44 ILE CD1 . 19800 1 321 . 1 1 26 26 ILE N N 15 120.077 0.011 . . . . . A 44 ILE N . 19800 1 322 . 1 1 27 27 GLU H H 1 8.866 0.003 . . . . . A 45 GLU H . 19800 1 323 . 1 1 27 27 GLU HA H 1 4.144 0.002 . . . . . A 45 GLU HA . 19800 1 324 . 1 1 27 27 GLU HB2 H 1 2.007 0.004 . . . . . A 45 GLU HB2 . 19800 1 325 . 1 1 27 27 GLU HB3 H 1 1.921 0.009 . . . . . A 45 GLU HB3 . 19800 1 326 . 1 1 27 27 GLU HG2 H 1 2.146 0.002 . . . . . A 45 GLU HG2 . 19800 1 327 . 1 1 27 27 GLU HG3 H 1 2.286 0.009 . . . . . A 45 GLU HG3 . 19800 1 328 . 1 1 27 27 GLU C C 13 174.368 0 . . . . . A 45 GLU C . 19800 1 329 . 1 1 27 27 GLU CA C 13 56.121 0.01 . . . . . A 45 GLU CA . 19800 1 330 . 1 1 27 27 GLU CB C 13 29.979 0 . . . . . A 45 GLU CB . 19800 1 331 . 1 1 27 27 GLU CG C 13 36.22 0.028 . . . . . A 45 GLU CG . 19800 1 332 . 1 1 27 27 GLU N N 15 129.083 0.017 . . . . . A 45 GLU N . 19800 1 333 . 1 1 28 28 ALA H H 1 7.897 0.003 . . . . . A 46 ALA H . 19800 1 334 . 1 1 28 28 ALA HA H 1 5.087 0.003 . . . . . A 46 ALA HA . 19800 1 335 . 1 1 28 28 ALA HB1 H 1 1.247 0.003 . . . . . A 46 ALA HB1 . 19800 1 336 . 1 1 28 28 ALA HB2 H 1 1.247 0.003 . . . . . A 46 ALA HB2 . 19800 1 337 . 1 1 28 28 ALA HB3 H 1 1.247 0.003 . . . . . A 46 ALA HB3 . 19800 1 338 . 1 1 28 28 ALA C C 13 175.515 0 . . . . . A 46 ALA C . 19800 1 339 . 1 1 28 28 ALA CA C 13 50.426 0.009 . . . . . A 46 ALA CA . 19800 1 340 . 1 1 28 28 ALA CB C 13 23.581 0.044 . . . . . A 46 ALA CB . 19800 1 341 . 1 1 28 28 ALA N N 15 127.014 0.009 . . . . . A 46 ALA N . 19800 1 342 . 1 1 29 29 ASN H H 1 8.712 0.002 . . . . . A 47 ASN H . 19800 1 343 . 1 1 29 29 ASN HA H 1 5.059 0.001 . . . . . A 47 ASN HA . 19800 1 344 . 1 1 29 29 ASN HB2 H 1 2.54 0.003 . . . . . A 47 ASN HB2 . 19800 1 345 . 1 1 29 29 ASN HB3 H 1 2.784 0.002 . . . . . A 47 ASN HB3 . 19800 1 346 . 1 1 29 29 ASN C C 13 172.618 0 . . . . . A 47 ASN C . 19800 1 347 . 1 1 29 29 ASN CA C 13 51.733 0.034 . . . . . A 47 ASN CA . 19800 1 348 . 1 1 29 29 ASN CB C 13 41.163 0 . . . . . A 47 ASN CB . 19800 1 349 . 1 1 29 29 ASN N N 15 117.293 0.008 . . . . . A 47 ASN N . 19800 1 350 . 1 1 30 30 LYS H H 1 8.607 0.003 . . . . . A 48 LYS H . 19800 1 351 . 1 1 30 30 LYS HA H 1 5.302 0.003 . . . . . A 48 LYS HA . 19800 1 352 . 1 1 30 30 LYS HB2 H 1 1.572 0.003 . . . . . A 48 LYS HB2 . 19800 1 353 . 1 1 30 30 LYS HB3 H 1 1.784 0.003 . . . . . A 48 LYS HB3 . 19800 1 354 . 1 1 30 30 LYS HG2 H 1 1.332 0 . . . . . A 48 LYS HG2 . 19800 1 355 . 1 1 30 30 LYS HG3 H 1 1.332 0 . . . . . A 48 LYS QG . 19800 1 356 . 1 1 30 30 LYS HD2 H 1 1.349 0.025 . . . . . A 48 LYS HD2 . 19800 1 357 . 1 1 30 30 LYS HD3 H 1 1.301 0.007 . . . . . A 48 LYS HD3 . 19800 1 358 . 1 1 30 30 LYS HE2 H 1 2.722 0.004 . . . . . A 48 LYS HE2 . 19800 1 359 . 1 1 30 30 LYS HE3 H 1 2.796 0.006 . . . . . A 48 LYS HE3 . 19800 1 360 . 1 1 30 30 LYS C C 13 175.186 0 . . . . . A 48 LYS C . 19800 1 361 . 1 1 30 30 LYS CA C 13 54.377 0.006 . . . . . A 48 LYS CA . 19800 1 362 . 1 1 30 30 LYS CB C 13 34.817 0.039 . . . . . A 48 LYS CB . 19800 1 363 . 1 1 30 30 LYS CG C 13 24.702 0.082 . . . . . A 48 LYS CG . 19800 1 364 . 1 1 30 30 LYS CD C 13 29.546 0.07 . . . . . A 48 LYS CD . 19800 1 365 . 1 1 30 30 LYS CE C 13 41.376 0 . . . . . A 48 LYS CE . 19800 1 366 . 1 1 30 30 LYS N N 15 121.209 0.023 . . . . . A 48 LYS N . 19800 1 367 . 1 1 31 31 ILE H H 1 9.231 0.003 . . . . . A 49 ILE H . 19800 1 368 . 1 1 31 31 ILE HA H 1 4.335 0.001 . . . . . A 49 ILE HA . 19800 1 369 . 1 1 31 31 ILE HB H 1 1.871 0.002 . . . . . A 49 ILE HB . 19800 1 370 . 1 1 31 31 ILE HG12 H 1 1.311 0.001 . . . . . A 49 ILE HG12 . 19800 1 371 . 1 1 31 31 ILE HG13 H 1 1.11 0.005 . . . . . A 49 ILE HG13 . 19800 1 372 . 1 1 31 31 ILE HG21 H 1 0.747 0.003 . . . . . A 49 ILE HG21 . 19800 1 373 . 1 1 31 31 ILE HG22 H 1 0.747 0.003 . . . . . A 49 ILE HG22 . 19800 1 374 . 1 1 31 31 ILE HG23 H 1 0.747 0.003 . . . . . A 49 ILE HG23 . 19800 1 375 . 1 1 31 31 ILE HD11 H 1 0.737 0.001 . . . . . A 49 ILE HD11 . 19800 1 376 . 1 1 31 31 ILE HD12 H 1 0.737 0.001 . . . . . A 49 ILE HD12 . 19800 1 377 . 1 1 31 31 ILE HD13 H 1 0.737 0.001 . . . . . A 49 ILE HD13 . 19800 1 378 . 1 1 31 31 ILE C C 13 175.247 0 . . . . . A 49 ILE C . 19800 1 379 . 1 1 31 31 ILE CA C 13 59.683 0.023 . . . . . A 49 ILE CA . 19800 1 380 . 1 1 31 31 ILE CB C 13 39.941 0.014 . . . . . A 49 ILE CB . 19800 1 381 . 1 1 31 31 ILE CG1 C 13 27.175 0.023 . . . . . A 49 ILE CG1 . 19800 1 382 . 1 1 31 31 ILE CG2 C 13 17.077 0.088 . . . . . A 49 ILE CG2 . 19800 1 383 . 1 1 31 31 ILE CD1 C 13 12.604 0.085 . . . . . A 49 ILE CD1 . 19800 1 384 . 1 1 31 31 ILE N N 15 127.508 0.015 . . . . . A 49 ILE N . 19800 1 385 . 1 1 32 32 ASP H H 1 8.821 0.004 . . . . . A 50 ASP H . 19800 1 386 . 1 1 32 32 ASP HA H 1 3.854 0.002 . . . . . A 50 ASP HA . 19800 1 387 . 1 1 32 32 ASP HB2 H 1 2.44 0.002 . . . . . A 50 ASP HB2 . 19800 1 388 . 1 1 32 32 ASP HB3 H 1 2.791 0.002 . . . . . A 50 ASP HB3 . 19800 1 389 . 1 1 32 32 ASP C C 13 177.327 0 . . . . . A 50 ASP C . 19800 1 390 . 1 1 32 32 ASP CA C 13 53.639 0.046 . . . . . A 50 ASP CA . 19800 1 391 . 1 1 32 32 ASP CB C 13 40.857 0.026 . . . . . A 50 ASP CB . 19800 1 392 . 1 1 32 32 ASP N N 15 127.775 0.004 . . . . . A 50 ASP N . 19800 1 393 . 1 1 33 33 SER H H 1 8.035 0.003 . . . . . A 51 SER H . 19800 1 394 . 1 1 33 33 SER HA H 1 4.66 0.004 . . . . . A 51 SER HA . 19800 1 395 . 1 1 33 33 SER HB2 H 1 3.728 0.002 . . . . . A 51 SER HB2 . 19800 1 396 . 1 1 33 33 SER HB3 H 1 4.032 0.002 . . . . . A 51 SER HB3 . 19800 1 397 . 1 1 33 33 SER C C 13 177.258 0 . . . . . A 51 SER C . 19800 1 398 . 1 1 33 33 SER CA C 13 57.111 0.07 . . . . . A 51 SER CA . 19800 1 399 . 1 1 33 33 SER CB C 13 63.271 0.023 . . . . . A 51 SER CB . 19800 1 400 . 1 1 33 33 SER N N 15 123.948 0.005 . . . . . A 51 SER N . 19800 1 401 . 1 1 34 34 GLY H H 1 8.643 0.002 . . . . . A 52 GLY H . 19800 1 402 . 1 1 34 34 GLY HA2 H 1 3.945 0.003 . . . . . A 52 GLY HA2 . 19800 1 403 . 1 1 34 34 GLY HA3 H 1 3.632 0.002 . . . . . A 52 GLY HA3 . 19800 1 404 . 1 1 34 34 GLY C C 13 178.261 0 . . . . . A 52 GLY C . 19800 1 405 . 1 1 34 34 GLY CA C 13 46.45 0.02 . . . . . A 52 GLY CA . 19800 1 406 . 1 1 34 34 GLY N N 15 112.626 0.015 . . . . . A 52 GLY N . 19800 1 407 . 1 1 35 35 LYS HA H 1 4.119 0.002 . . . . . A 53 LYS HA . 19800 1 408 . 1 1 35 35 LYS HB2 H 1 1.851 0.003 . . . . . A 53 LYS HB2 . 19800 1 409 . 1 1 35 35 LYS HB3 H 1 1.851 0.003 . . . . . A 53 LYS QB . 19800 1 410 . 1 1 35 35 LYS HG2 H 1 1.477 0.005 . . . . . A 53 LYS HG2 . 19800 1 411 . 1 1 35 35 LYS HG3 H 1 1.477 0.005 . . . . . A 53 LYS QG . 19800 1 412 . 1 1 35 35 LYS HD2 H 1 1.687 0.003 . . . . . A 53 LYS HD2 . 19800 1 413 . 1 1 35 35 LYS HD3 H 1 1.687 0.003 . . . . . A 53 LYS QD . 19800 1 414 . 1 1 35 35 LYS HE2 H 1 2.986 0.001 . . . . . A 53 LYS HE2 . 19800 1 415 . 1 1 35 35 LYS HE3 H 1 2.986 0.001 . . . . . A 53 LYS QE . 19800 1 416 . 1 1 35 35 LYS C C 13 178.526 0 . . . . . A 53 LYS C . 19800 1 417 . 1 1 35 35 LYS CA C 13 58.349 0.018 . . . . . A 53 LYS CA . 19800 1 418 . 1 1 35 35 LYS CB C 13 32.038 0.052 . . . . . A 53 LYS CB . 19800 1 419 . 1 1 35 35 LYS CG C 13 24.747 0.037 . . . . . A 53 LYS CG . 19800 1 420 . 1 1 35 35 LYS CD C 13 28.946 0.076 . . . . . A 53 LYS CD . 19800 1 421 . 1 1 35 35 LYS CE C 13 42.001 0.019 . . . . . A 53 LYS CE . 19800 1 422 . 1 1 36 36 LEU H H 1 7.453 0.003 . . . . . A 54 LEU H . 19800 1 423 . 1 1 36 36 LEU HA H 1 4.309 0.014 . . . . . A 54 LEU HA . 19800 1 424 . 1 1 36 36 LEU HB2 H 1 1.67 0.012 . . . . . A 54 LEU HB2 . 19800 1 425 . 1 1 36 36 LEU HB3 H 1 1.67 0.012 . . . . . A 54 LEU QB . 19800 1 426 . 1 1 36 36 LEU HG H 1 1.612 0.006 . . . . . A 54 LEU HG . 19800 1 427 . 1 1 36 36 LEU HD11 H 1 0.919 0.003 . . . . . A 54 LEU HD11 . 19800 1 428 . 1 1 36 36 LEU HD12 H 1 0.919 0.003 . . . . . A 54 LEU HD12 . 19800 1 429 . 1 1 36 36 LEU HD13 H 1 0.919 0.003 . . . . . A 54 LEU HD13 . 19800 1 430 . 1 1 36 36 LEU HD21 H 1 0.836 0.006 . . . . . A 54 LEU HD21 . 19800 1 431 . 1 1 36 36 LEU HD22 H 1 0.836 0.006 . . . . . A 54 LEU HD22 . 19800 1 432 . 1 1 36 36 LEU HD23 H 1 0.836 0.006 . . . . . A 54 LEU HD23 . 19800 1 433 . 1 1 36 36 LEU C C 13 178.832 0 . . . . . A 54 LEU C . 19800 1 434 . 1 1 36 36 LEU CA C 13 54.958 0.085 . . . . . A 54 LEU CA . 19800 1 435 . 1 1 36 36 LEU CB C 13 41.155 0.019 . . . . . A 54 LEU CB . 19800 1 436 . 1 1 36 36 LEU CG C 13 27.183 0.04 . . . . . A 54 LEU CG . 19800 1 437 . 1 1 36 36 LEU CD1 C 13 24.926 0.043 . . . . . A 54 LEU CD1 . 19800 1 438 . 1 1 36 36 LEU CD2 C 13 22.477 0.132 . . . . . A 54 LEU CD2 . 19800 1 439 . 1 1 36 36 LEU N N 15 117.133 0.01 . . . . . A 54 LEU N . 19800 1 440 . 1 1 37 37 GLY H H 1 7.727 0.002 . . . . . A 55 GLY H . 19800 1 441 . 1 1 37 37 GLY HA2 H 1 3.759 0.002 . . . . . A 55 GLY HA2 . 19800 1 442 . 1 1 37 37 GLY HA3 H 1 4.016 0.003 . . . . . A 55 GLY HA3 . 19800 1 443 . 1 1 37 37 GLY C C 13 172.511 0 . . . . . A 55 GLY C . 19800 1 444 . 1 1 37 37 GLY CA C 13 44.519 0.027 . . . . . A 55 GLY CA . 19800 1 445 . 1 1 37 37 GLY N N 15 106.946 0.019 . . . . . A 55 GLY N . 19800 1 446 . 1 1 38 38 TYR H H 1 9.77 0.004 . . . . . A 56 TYR H . 19800 1 447 . 1 1 38 38 TYR HA H 1 5.267 0.003 . . . . . A 56 TYR HA . 19800 1 448 . 1 1 38 38 TYR HB2 H 1 2.452 0.002 . . . . . A 56 TYR HB2 . 19800 1 449 . 1 1 38 38 TYR HB3 H 1 2.611 0.002 . . . . . A 56 TYR HB3 . 19800 1 450 . 1 1 38 38 TYR HD1 H 1 6.922 0.004 . . . . . A 56 TYR HD1 . 19800 1 451 . 1 1 38 38 TYR HD2 H 1 6.922 0.004 . . . . . A 56 TYR HD2 . 19800 1 452 . 1 1 38 38 TYR HE1 H 1 6.764 0.009 . . . . . A 56 TYR HE1 . 19800 1 453 . 1 1 38 38 TYR HE2 H 1 6.764 0.009 . . . . . A 56 TYR HE2 . 19800 1 454 . 1 1 38 38 TYR C C 13 177.412 0 . . . . . A 56 TYR C . 19800 1 455 . 1 1 38 38 TYR CA C 13 57.986 0.073 . . . . . A 56 TYR CA . 19800 1 456 . 1 1 38 38 TYR CB C 13 40.838 0.011 . . . . . A 56 TYR CB . 19800 1 457 . 1 1 38 38 TYR CD1 C 13 132.549 0.039 . . . . . A 56 TYR CD1 . 19800 1 458 . 1 1 38 38 TYR CE1 C 13 117.815 0.105 . . . . . A 56 TYR CE1 . 19800 1 459 . 1 1 38 38 TYR N N 15 119.5 0.006 . . . . . A 56 TYR N . 19800 1 460 . 1 1 39 39 SER H H 1 9.13 0.003 . . . . . A 57 SER H . 19800 1 461 . 1 1 39 39 SER HA H 1 5.386 0.002 . . . . . A 57 SER HA . 19800 1 462 . 1 1 39 39 SER HB2 H 1 3.833 0.004 . . . . . A 57 SER HB2 . 19800 1 463 . 1 1 39 39 SER HB3 H 1 3.905 0.006 . . . . . A 57 SER HB3 . 19800 1 464 . 1 1 39 39 SER C C 13 171.818 0 . . . . . A 57 SER C . 19800 1 465 . 1 1 39 39 SER CA C 13 55.817 0.037 . . . . . A 57 SER CA . 19800 1 466 . 1 1 39 39 SER CB C 13 65.566 0.02 . . . . . A 57 SER CB . 19800 1 467 . 1 1 39 39 SER N N 15 114.46 0.005 . . . . . A 57 SER N . 19800 1 468 . 1 1 40 40 ILE H H 1 8.604 0.004 . . . . . A 58 ILE H . 19800 1 469 . 1 1 40 40 ILE HA H 1 5.538 0.002 . . . . . A 58 ILE HA . 19800 1 470 . 1 1 40 40 ILE HB H 1 1.837 0.003 . . . . . A 58 ILE HB . 19800 1 471 . 1 1 40 40 ILE HG12 H 1 1.242 0.011 . . . . . A 58 ILE HG12 . 19800 1 472 . 1 1 40 40 ILE HG13 H 1 1.453 0.006 . . . . . A 58 ILE HG13 . 19800 1 473 . 1 1 40 40 ILE HG21 H 1 0.808 0.002 . . . . . A 58 ILE HG21 . 19800 1 474 . 1 1 40 40 ILE HG22 H 1 0.808 0.002 . . . . . A 58 ILE HG22 . 19800 1 475 . 1 1 40 40 ILE HG23 H 1 0.808 0.002 . . . . . A 58 ILE HG23 . 19800 1 476 . 1 1 40 40 ILE HD11 H 1 0.808 0.001 . . . . . A 58 ILE HD11 . 19800 1 477 . 1 1 40 40 ILE HD12 H 1 0.808 0.001 . . . . . A 58 ILE HD12 . 19800 1 478 . 1 1 40 40 ILE HD13 H 1 0.808 0.001 . . . . . A 58 ILE HD13 . 19800 1 479 . 1 1 40 40 ILE C C 13 176.822 0 . . . . . A 58 ILE C . 19800 1 480 . 1 1 40 40 ILE CA C 13 57.04 0.043 . . . . . A 58 ILE CA . 19800 1 481 . 1 1 40 40 ILE CB C 13 39.157 0.134 . . . . . A 58 ILE CB . 19800 1 482 . 1 1 40 40 ILE CG1 C 13 27.019 0.142 . . . . . A 58 ILE CG1 . 19800 1 483 . 1 1 40 40 ILE CG2 C 13 17.784 0.068 . . . . . A 58 ILE CG2 . 19800 1 484 . 1 1 40 40 ILE CD1 C 13 10.554 0.096 . . . . . A 58 ILE CD1 . 19800 1 485 . 1 1 40 40 ILE N N 15 121.24 0.032 . . . . . A 58 ILE N . 19800 1 486 . 1 1 41 41 THR H H 1 8.969 0.003 . . . . . A 59 THR H . 19800 1 487 . 1 1 41 41 THR HA H 1 5.435 0.002 . . . . . A 59 THR HA . 19800 1 488 . 1 1 41 41 THR HB H 1 4.039 0.001 . . . . . A 59 THR HB . 19800 1 489 . 1 1 41 41 THR HG21 H 1 1.109 0.003 . . . . . A 59 THR HG21 . 19800 1 490 . 1 1 41 41 THR HG22 H 1 1.109 0.003 . . . . . A 59 THR HG22 . 19800 1 491 . 1 1 41 41 THR HG23 H 1 1.109 0.003 . . . . . A 59 THR HG23 . 19800 1 492 . 1 1 41 41 THR C C 13 172.703 0 . . . . . A 59 THR C . 19800 1 493 . 1 1 41 41 THR CA C 13 58.889 0.136 . . . . . A 59 THR CA . 19800 1 494 . 1 1 41 41 THR CB C 13 71.574 0.018 . . . . . A 59 THR CB . 19800 1 495 . 1 1 41 41 THR CG2 C 13 21.524 0.064 . . . . . A 59 THR CG2 . 19800 1 496 . 1 1 41 41 THR N N 15 118.505 0.009 . . . . . A 59 THR N . 19800 1 497 . 1 1 42 42 VAL H H 1 8.602 0.003 . . . . . A 60 VAL H . 19800 1 498 . 1 1 42 42 VAL HA H 1 4.787 0.001 . . . . . A 60 VAL HA . 19800 1 499 . 1 1 42 42 VAL HB H 1 2.402 0.007 . . . . . A 60 VAL HB . 19800 1 500 . 1 1 42 42 VAL HG11 H 1 0.935 0.003 . . . . . A 60 VAL HG11 . 19800 1 501 . 1 1 42 42 VAL HG12 H 1 0.935 0.003 . . . . . A 60 VAL HG12 . 19800 1 502 . 1 1 42 42 VAL HG13 H 1 0.935 0.003 . . . . . A 60 VAL HG13 . 19800 1 503 . 1 1 42 42 VAL HG21 H 1 0.871 0.005 . . . . . A 60 VAL HG21 . 19800 1 504 . 1 1 42 42 VAL HG22 H 1 0.871 0.005 . . . . . A 60 VAL HG22 . 19800 1 505 . 1 1 42 42 VAL HG23 H 1 0.871 0.005 . . . . . A 60 VAL HG23 . 19800 1 506 . 1 1 42 42 VAL C C 13 173.802 0 . . . . . A 60 VAL C . 19800 1 507 . 1 1 42 42 VAL CA C 13 58.594 0.066 . . . . . A 60 VAL CA . 19800 1 508 . 1 1 42 42 VAL CB C 13 36.56 0.091 . . . . . A 60 VAL CB . 19800 1 509 . 1 1 42 42 VAL CG1 C 13 22.942 0.068 . . . . . A 60 VAL CG1 . 19800 1 510 . 1 1 42 42 VAL CG2 C 13 18.868 0.093 . . . . . A 60 VAL CG2 . 19800 1 511 . 1 1 42 42 VAL N N 15 111.299 0.007 . . . . . A 60 VAL N . 19800 1 512 . 1 1 43 43 ALA H H 1 9.41 0.004 . . . . . A 61 ALA H . 19800 1 513 . 1 1 43 43 ALA HA H 1 4.678 0.003 . . . . . A 61 ALA HA . 19800 1 514 . 1 1 43 43 ALA HB1 H 1 1.482 0.004 . . . . . A 61 ALA HB1 . 19800 1 515 . 1 1 43 43 ALA HB2 H 1 1.482 0.004 . . . . . A 61 ALA HB2 . 19800 1 516 . 1 1 43 43 ALA HB3 H 1 1.482 0.004 . . . . . A 61 ALA HB3 . 19800 1 517 . 1 1 43 43 ALA C C 13 182.244 0 . . . . . A 61 ALA C . 19800 1 518 . 1 1 43 43 ALA CA C 13 52.304 0.004 . . . . . A 61 ALA CA . 19800 1 519 . 1 1 43 43 ALA CB C 13 19.742 0.112 . . . . . A 61 ALA CB . 19800 1 520 . 1 1 43 43 ALA N N 15 125.688 0.008 . . . . . A 61 ALA N . 19800 1 521 . 1 1 44 44 GLU H H 1 9.047 0.004 . . . . . A 62 GLU H . 19800 1 522 . 1 1 44 44 GLU HA H 1 3.97 0.001 . . . . . A 62 GLU HA . 19800 1 523 . 1 1 44 44 GLU HB2 H 1 2.134 0.009 . . . . . A 62 GLU HB2 . 19800 1 524 . 1 1 44 44 GLU HB3 H 1 2.134 0.009 . . . . . A 62 GLU QB . 19800 1 525 . 1 1 44 44 GLU HG2 H 1 2.213 0.002 . . . . . A 62 GLU HG2 . 19800 1 526 . 1 1 44 44 GLU HG3 H 1 2.284 0 . . . . . A 62 GLU HG3 . 19800 1 527 . 1 1 44 44 GLU C C 13 175.922 0 . . . . . A 62 GLU C . 19800 1 528 . 1 1 44 44 GLU CA C 13 62.328 0.03 . . . . . A 62 GLU CA . 19800 1 529 . 1 1 44 44 GLU CB C 13 27.421 0.035 . . . . . A 62 GLU CB . 19800 1 530 . 1 1 44 44 GLU N N 15 122.612 0.013 . . . . . A 62 GLU N . 19800 1 531 . 1 1 45 45 PRO HA H 1 4.486 0.002 . . . . . A 63 PRO HA . 19800 1 532 . 1 1 45 45 PRO HB2 H 1 1.844 0.006 . . . . . A 63 PRO HB2 . 19800 1 533 . 1 1 45 45 PRO HB3 H 1 2.396 0.001 . . . . . A 63 PRO HB3 . 19800 1 534 . 1 1 45 45 PRO HG2 H 1 1.947 0.001 . . . . . A 63 PRO HG2 . 19800 1 535 . 1 1 45 45 PRO HG3 H 1 1.947 0.001 . . . . . A 63 PRO QG . 19800 1 536 . 1 1 45 45 PRO HD2 H 1 3.83 0.002 . . . . . A 63 PRO HD2 . 19800 1 537 . 1 1 45 45 PRO HD3 H 1 3.61 0.002 . . . . . A 63 PRO HD3 . 19800 1 538 . 1 1 45 45 PRO C C 13 178.721 0 . . . . . A 63 PRO C . 19800 1 539 . 1 1 45 45 PRO CA C 13 65.517 0.004 . . . . . A 63 PRO CA . 19800 1 540 . 1 1 45 45 PRO CB C 13 31.124 0.043 . . . . . A 63 PRO CB . 19800 1 541 . 1 1 45 45 PRO CG C 13 27.985 0.082 . . . . . A 63 PRO CG . 19800 1 542 . 1 1 45 45 PRO CD C 13 50.389 0.02 . . . . . A 63 PRO CD . 19800 1 543 . 1 1 46 46 ASP H H 1 7.812 0.002 . . . . . A 64 ASP H . 19800 1 544 . 1 1 46 46 ASP HA H 1 4.994 0.002 . . . . . A 64 ASP HA . 19800 1 545 . 1 1 46 46 ASP HB2 H 1 3.001 0.002 . . . . . A 64 ASP HB2 . 19800 1 546 . 1 1 46 46 ASP HB3 H 1 2.807 0.002 . . . . . A 64 ASP HB3 . 19800 1 547 . 1 1 46 46 ASP C C 13 176.565 0 . . . . . A 64 ASP C . 19800 1 548 . 1 1 46 46 ASP CA C 13 54.701 0.013 . . . . . A 64 ASP CA . 19800 1 549 . 1 1 46 46 ASP CB C 13 43.082 0.008 . . . . . A 64 ASP CB . 19800 1 550 . 1 1 46 46 ASP N N 15 115.002 0.005 . . . . . A 64 ASP N . 19800 1 551 . 1 1 47 47 PHE H H 1 7.902 0.003 . . . . . A 65 PHE H . 19800 1 552 . 1 1 47 47 PHE HA H 1 3.926 0.003 . . . . . A 65 PHE HA . 19800 1 553 . 1 1 47 47 PHE HB2 H 1 3.002 0.001 . . . . . A 65 PHE HB2 . 19800 1 554 . 1 1 47 47 PHE HB3 H 1 3.285 0.002 . . . . . A 65 PHE HB3 . 19800 1 555 . 1 1 47 47 PHE HD1 H 1 6.982 0.004 . . . . . A 65 PHE HD1 . 19800 1 556 . 1 1 47 47 PHE HD2 H 1 6.982 0.004 . . . . . A 65 PHE HD2 . 19800 1 557 . 1 1 47 47 PHE HE1 H 1 7.347 0.004 . . . . . A 65 PHE HE1 . 19800 1 558 . 1 1 47 47 PHE HE2 H 1 7.347 0.004 . . . . . A 65 PHE HE2 . 19800 1 559 . 1 1 47 47 PHE C C 13 175.918 0 . . . . . A 65 PHE C . 19800 1 560 . 1 1 47 47 PHE CA C 13 63.611 0.029 . . . . . A 65 PHE CA . 19800 1 561 . 1 1 47 47 PHE CB C 13 40.354 0.044 . . . . . A 65 PHE CB . 19800 1 562 . 1 1 47 47 PHE CD1 C 13 131.561 0.027 . . . . . A 65 PHE CD1 . 19800 1 563 . 1 1 47 47 PHE CE1 C 13 132.029 0 . . . . . A 65 PHE CE1 . 19800 1 564 . 1 1 47 47 PHE N N 15 122.01 0.022 . . . . . A 65 PHE N . 19800 1 565 . 1 1 48 48 THR H H 1 8.648 0.003 . . . . . A 66 THR H . 19800 1 566 . 1 1 48 48 THR HA H 1 3.66 0.002 . . . . . A 66 THR HA . 19800 1 567 . 1 1 48 48 THR HB H 1 4.167 0.002 . . . . . A 66 THR HB . 19800 1 568 . 1 1 48 48 THR HG21 H 1 1.27 0.002 . . . . . A 66 THR HG21 . 19800 1 569 . 1 1 48 48 THR HG22 H 1 1.27 0.002 . . . . . A 66 THR HG22 . 19800 1 570 . 1 1 48 48 THR HG23 H 1 1.27 0.002 . . . . . A 66 THR HG23 . 19800 1 571 . 1 1 48 48 THR C C 13 178.106 0 . . . . . A 66 THR C . 19800 1 572 . 1 1 48 48 THR CA C 13 66.742 0.031 . . . . . A 66 THR CA . 19800 1 573 . 1 1 48 48 THR CB C 13 68.412 0.189 . . . . . A 66 THR CB . 19800 1 574 . 1 1 48 48 THR CG2 C 13 22.183 0.111 . . . . . A 66 THR CG2 . 19800 1 575 . 1 1 48 48 THR N N 15 112.195 0.023 . . . . . A 66 THR N . 19800 1 576 . 1 1 49 49 ALA H H 1 8.198 0.002 . . . . . A 67 ALA H . 19800 1 577 . 1 1 49 49 ALA HA H 1 4.044 0.002 . . . . . A 67 ALA HA . 19800 1 578 . 1 1 49 49 ALA HB1 H 1 1.528 0.001 . . . . . A 67 ALA HB1 . 19800 1 579 . 1 1 49 49 ALA HB2 H 1 1.528 0.001 . . . . . A 67 ALA HB2 . 19800 1 580 . 1 1 49 49 ALA HB3 H 1 1.528 0.001 . . . . . A 67 ALA HB3 . 19800 1 581 . 1 1 49 49 ALA C C 13 180.268 0 . . . . . A 67 ALA C . 19800 1 582 . 1 1 49 49 ALA CA C 13 54.618 0.009 . . . . . A 67 ALA CA . 19800 1 583 . 1 1 49 49 ALA CB C 13 18.408 0.076 . . . . . A 67 ALA CB . 19800 1 584 . 1 1 49 49 ALA N N 15 124.955 0.019 . . . . . A 67 ALA N . 19800 1 585 . 1 1 50 50 ALA H H 1 8.469 0.003 . . . . . A 68 ALA H . 19800 1 586 . 1 1 50 50 ALA HA H 1 3.966 0.003 . . . . . A 68 ALA HA . 19800 1 587 . 1 1 50 50 ALA HB1 H 1 1.473 0.002 . . . . . A 68 ALA HB1 . 19800 1 588 . 1 1 50 50 ALA HB2 H 1 1.473 0.002 . . . . . A 68 ALA HB2 . 19800 1 589 . 1 1 50 50 ALA HB3 H 1 1.473 0.002 . . . . . A 68 ALA HB3 . 19800 1 590 . 1 1 50 50 ALA C C 13 181.033 0 . . . . . A 68 ALA C . 19800 1 591 . 1 1 50 50 ALA CA C 13 55.623 0 . . . . . A 68 ALA CA . 19800 1 592 . 1 1 50 50 ALA CB C 13 19.802 0.063 . . . . . A 68 ALA CB . 19800 1 593 . 1 1 50 50 ALA N N 15 119.593 0.025 . . . . . A 68 ALA N . 19800 1 594 . 1 1 51 51 VAL H H 1 8.034 0.002 . . . . . A 69 VAL H . 19800 1 595 . 1 1 51 51 VAL HA H 1 3.257 0.002 . . . . . A 69 VAL HA . 19800 1 596 . 1 1 51 51 VAL HB H 1 1.744 0.004 . . . . . A 69 VAL HB . 19800 1 597 . 1 1 51 51 VAL HG11 H 1 0.698 0.002 . . . . . A 69 VAL HG11 . 19800 1 598 . 1 1 51 51 VAL HG12 H 1 0.698 0.002 . . . . . A 69 VAL HG12 . 19800 1 599 . 1 1 51 51 VAL HG13 H 1 0.698 0.002 . . . . . A 69 VAL HG13 . 19800 1 600 . 1 1 51 51 VAL HG21 H 1 0.413 0.003 . . . . . A 69 VAL HG21 . 19800 1 601 . 1 1 51 51 VAL HG22 H 1 0.413 0.003 . . . . . A 69 VAL HG22 . 19800 1 602 . 1 1 51 51 VAL HG23 H 1 0.413 0.003 . . . . . A 69 VAL HG23 . 19800 1 603 . 1 1 51 51 VAL C C 13 179 0 . . . . . A 69 VAL C . 19800 1 604 . 1 1 51 51 VAL CA C 13 66.077 0.034 . . . . . A 69 VAL CA . 19800 1 605 . 1 1 51 51 VAL CB C 13 31.684 0.102 . . . . . A 69 VAL CB . 19800 1 606 . 1 1 51 51 VAL CG1 C 13 21.184 0.12 . . . . . A 69 VAL CG1 . 19800 1 607 . 1 1 51 51 VAL CG2 C 13 22.941 0.127 . . . . . A 69 VAL CG2 . 19800 1 608 . 1 1 51 51 VAL N N 15 115.582 0.011 . . . . . A 69 VAL N . 19800 1 609 . 1 1 52 52 TYR H H 1 7.179 0.005 . . . . . A 70 TYR H . 19800 1 610 . 1 1 52 52 TYR HA H 1 3.805 0.002 . . . . . A 70 TYR HA . 19800 1 611 . 1 1 52 52 TYR HB2 H 1 2.708 0.006 . . . . . A 70 TYR HB2 . 19800 1 612 . 1 1 52 52 TYR HB3 H 1 2.708 0.006 . . . . . A 70 TYR QB . 19800 1 613 . 1 1 52 52 TYR HD1 H 1 5.898 0.003 . . . . . A 70 TYR HD1 . 19800 1 614 . 1 1 52 52 TYR HD2 H 1 5.898 0.003 . . . . . A 70 TYR HD2 . 19800 1 615 . 1 1 52 52 TYR HE1 H 1 6.001 0.003 . . . . . A 70 TYR HE1 . 19800 1 616 . 1 1 52 52 TYR HE2 H 1 6.001 0.003 . . . . . A 70 TYR HE2 . 19800 1 617 . 1 1 52 52 TYR C C 13 180.084 0 . . . . . A 70 TYR C . 19800 1 618 . 1 1 52 52 TYR CA C 13 61.459 0.032 . . . . . A 70 TYR CA . 19800 1 619 . 1 1 52 52 TYR CB C 13 37.712 0.059 . . . . . A 70 TYR CB . 19800 1 620 . 1 1 52 52 TYR CD1 C 13 132.675 0.025 . . . . . A 70 TYR CD1 . 19800 1 621 . 1 1 52 52 TYR CE1 C 13 117.778 0.05 . . . . . A 70 TYR CE1 . 19800 1 622 . 1 1 52 52 TYR N N 15 118.722 0.01 . . . . . A 70 TYR N . 19800 1 623 . 1 1 53 53 TRP H H 1 7.924 0.002 . . . . . A 71 TRP H . 19800 1 624 . 1 1 53 53 TRP HA H 1 4.482 0.015 . . . . . A 71 TRP HA . 19800 1 625 . 1 1 53 53 TRP HB2 H 1 2.929 0.03 . . . . . A 71 TRP HB2 . 19800 1 626 . 1 1 53 53 TRP HB3 H 1 3.079 0.043 . . . . . A 71 TRP HB3 . 19800 1 627 . 1 1 53 53 TRP HD1 H 1 6.925 0.003 . . . . . A 71 TRP HD1 . 19800 1 628 . 1 1 53 53 TRP HE1 H 1 10.291 0 . . . . . A 71 TRP HE1 . 19800 1 629 . 1 1 53 53 TRP HE3 H 1 7.397 0.006 . . . . . A 71 TRP HE3 . 19800 1 630 . 1 1 53 53 TRP HZ2 H 1 7.41 0.001 . . . . . A 71 TRP HZ2 . 19800 1 631 . 1 1 53 53 TRP HZ3 H 1 7.101 0.002 . . . . . A 71 TRP HZ3 . 19800 1 632 . 1 1 53 53 TRP HH2 H 1 7.267 0.002 . . . . . A 71 TRP HH2 . 19800 1 633 . 1 1 53 53 TRP C C 13 180.643 0 . . . . . A 71 TRP C . 19800 1 634 . 1 1 53 53 TRP CA C 13 58.833 0.028 . . . . . A 71 TRP CA . 19800 1 635 . 1 1 53 53 TRP CB C 13 30.133 0.097 . . . . . A 71 TRP CB . 19800 1 636 . 1 1 53 53 TRP CD1 C 13 127.675 0.052 . . . . . A 71 TRP CD1 . 19800 1 637 . 1 1 53 53 TRP CE3 C 13 120.961 0.042 . . . . . A 71 TRP CE3 . 19800 1 638 . 1 1 53 53 TRP CZ2 C 13 114.61 0.114 . . . . . A 71 TRP CZ2 . 19800 1 639 . 1 1 53 53 TRP CZ3 C 13 122.001 0.06 . . . . . A 71 TRP CZ3 . 19800 1 640 . 1 1 53 53 TRP CH2 C 13 124.639 0.019 . . . . . A 71 TRP CH2 . 19800 1 641 . 1 1 53 53 TRP N N 15 117.18 0.022 . . . . . A 71 TRP N . 19800 1 642 . 1 1 53 53 TRP NE1 N 15 127.809 0 . . . . . A 71 TRP NE1 . 19800 1 643 . 1 1 54 54 ILE H H 1 7.978 0.003 . . . . . A 72 ILE H . 19800 1 644 . 1 1 54 54 ILE HA H 1 4.452 0.002 . . . . . A 72 ILE HA . 19800 1 645 . 1 1 54 54 ILE HB H 1 2.224 0.003 . . . . . A 72 ILE HB . 19800 1 646 . 1 1 54 54 ILE HG12 H 1 1.462 0 . . . . . A 72 ILE HG12 . 19800 1 647 . 1 1 54 54 ILE HG13 H 1 1.512 0.001 . . . . . A 72 ILE HG13 . 19800 1 648 . 1 1 54 54 ILE HG21 H 1 0.924 0.003 . . . . . A 72 ILE HG21 . 19800 1 649 . 1 1 54 54 ILE HG22 H 1 0.924 0.003 . . . . . A 72 ILE HG22 . 19800 1 650 . 1 1 54 54 ILE HG23 H 1 0.924 0.003 . . . . . A 72 ILE HG23 . 19800 1 651 . 1 1 54 54 ILE HD11 H 1 0.79 0.002 . . . . . A 72 ILE HD11 . 19800 1 652 . 1 1 54 54 ILE HD12 H 1 0.79 0.002 . . . . . A 72 ILE HD12 . 19800 1 653 . 1 1 54 54 ILE HD13 H 1 0.79 0.002 . . . . . A 72 ILE HD13 . 19800 1 654 . 1 1 54 54 ILE C C 13 178.49 0 . . . . . A 72 ILE C . 19800 1 655 . 1 1 54 54 ILE CA C 13 61.563 0.011 . . . . . A 72 ILE CA . 19800 1 656 . 1 1 54 54 ILE CB C 13 37.491 0.014 . . . . . A 72 ILE CB . 19800 1 657 . 1 1 54 54 ILE CG1 C 13 27.431 0.042 . . . . . A 72 ILE CG1 . 19800 1 658 . 1 1 54 54 ILE CG2 C 13 18.936 0.045 . . . . . A 72 ILE CG2 . 19800 1 659 . 1 1 54 54 ILE CD1 C 13 13.745 0.028 . . . . . A 72 ILE CD1 . 19800 1 660 . 1 1 54 54 ILE N N 15 113.422 0.048 . . . . . A 72 ILE N . 19800 1 661 . 1 1 55 55 LYS H H 1 7.677 0.006 . . . . . A 73 LYS H . 19800 1 662 . 1 1 55 55 LYS HA H 1 4.177 0.003 . . . . . A 73 LYS HA . 19800 1 663 . 1 1 55 55 LYS HB2 H 1 1.768 0.003 . . . . . A 73 LYS HB2 . 19800 1 664 . 1 1 55 55 LYS HB3 H 1 1.768 0.003 . . . . . A 73 LYS QB . 19800 1 665 . 1 1 55 55 LYS HG2 H 1 1.363 0.001 . . . . . A 73 LYS HG2 . 19800 1 666 . 1 1 55 55 LYS HG3 H 1 1.401 0.005 . . . . . A 73 LYS HG3 . 19800 1 667 . 1 1 55 55 LYS HD2 H 1 1.552 0.002 . . . . . A 73 LYS HD2 . 19800 1 668 . 1 1 55 55 LYS HD3 H 1 1.552 0.002 . . . . . A 73 LYS QD . 19800 1 669 . 1 1 55 55 LYS HE2 H 1 2.834 0.001 . . . . . A 73 LYS HE2 . 19800 1 670 . 1 1 55 55 LYS HE3 H 1 2.834 0.001 . . . . . A 73 LYS QE . 19800 1 671 . 1 1 55 55 LYS C C 13 179.46 0 . . . . . A 73 LYS C . 19800 1 672 . 1 1 55 55 LYS CA C 13 58.31 0.021 . . . . . A 73 LYS CA . 19800 1 673 . 1 1 55 55 LYS CB C 13 32.247 0.036 . . . . . A 73 LYS CB . 19800 1 674 . 1 1 55 55 LYS CG C 13 24.707 0.046 . . . . . A 73 LYS CG . 19800 1 675 . 1 1 55 55 LYS CD C 13 28.962 0.054 . . . . . A 73 LYS CD . 19800 1 676 . 1 1 55 55 LYS CE C 13 42.022 0.018 . . . . . A 73 LYS CE . 19800 1 677 . 1 1 55 55 LYS N N 15 120.911 0.033 . . . . . A 73 LYS N . 19800 1 678 . 1 1 56 56 THR H H 1 7.647 0.003 . . . . . A 74 THR H . 19800 1 679 . 1 1 56 56 THR HA H 1 4.14 0.016 . . . . . A 74 THR HA . 19800 1 680 . 1 1 56 56 THR HB H 1 4.066 0.002 . . . . . A 74 THR HB . 19800 1 681 . 1 1 56 56 THR HG21 H 1 0.978 0.01 . . . . . A 74 THR HG21 . 19800 1 682 . 1 1 56 56 THR HG22 H 1 0.978 0.01 . . . . . A 74 THR HG22 . 19800 1 683 . 1 1 56 56 THR HG23 H 1 0.978 0.01 . . . . . A 74 THR HG23 . 19800 1 684 . 1 1 56 56 THR C C 13 174.574 0 . . . . . A 74 THR C . 19800 1 685 . 1 1 56 56 THR CA C 13 63.019 0.157 . . . . . A 74 THR CA . 19800 1 686 . 1 1 56 56 THR CB C 13 69.394 0.034 . . . . . A 74 THR CB . 19800 1 687 . 1 1 56 56 THR CG2 C 13 21.249 0.051 . . . . . A 74 THR CG2 . 19800 1 688 . 1 1 56 56 THR N N 15 110.017 0.05 . . . . . A 74 THR N . 19800 1 689 . 1 1 57 57 TYR H H 1 7.915 0.008 . . . . . A 75 TYR H . 19800 1 690 . 1 1 57 57 TYR HA H 1 4.468 0 . . . . . A 75 TYR HA . 19800 1 691 . 1 1 57 57 TYR HB2 H 1 3.132 0 . . . . . A 75 TYR HB2 . 19800 1 692 . 1 1 57 57 TYR HB3 H 1 2.969 0 . . . . . A 75 TYR HB3 . 19800 1 693 . 1 1 57 57 TYR HD1 H 1 7.116 0.004 . . . . . A 75 TYR HD1 . 19800 1 694 . 1 1 57 57 TYR HD2 H 1 7.116 0.004 . . . . . A 75 TYR HD2 . 19800 1 695 . 1 1 57 57 TYR HE1 H 1 6.76 0.011 . . . . . A 75 TYR HE1 . 19800 1 696 . 1 1 57 57 TYR HE2 H 1 6.76 0.011 . . . . . A 75 TYR HE2 . 19800 1 697 . 1 1 57 57 TYR C C 13 174.634 0 . . . . . A 75 TYR C . 19800 1 698 . 1 1 57 57 TYR CA C 13 58.964 0 . . . . . A 75 TYR CA . 19800 1 699 . 1 1 57 57 TYR CB C 13 38.945 0.068 . . . . . A 75 TYR CB . 19800 1 700 . 1 1 57 57 TYR CD1 C 13 133.363 0.096 . . . . . A 75 TYR CD1 . 19800 1 701 . 1 1 57 57 TYR CE1 C 13 117.608 0 . . . . . A 75 TYR CE1 . 19800 1 702 . 1 1 57 57 TYR N N 15 122.005 0.012 . . . . . A 75 TYR N . 19800 1 703 . 1 1 58 58 GLN H H 1 7.467 0.008 . . . . . A 76 GLN H . 19800 1 704 . 1 1 58 58 GLN C C 13 183.049 0 . . . . . A 76 GLN C . 19800 1 705 . 1 1 58 58 GLN CA C 13 57.5 0 . . . . . A 76 GLN CA . 19800 1 706 . 1 1 58 58 GLN CB C 13 30.632 0 . . . . . A 76 GLN CB . 19800 1 707 . 1 1 58 58 GLN N N 15 125.769 0.003 . . . . . A 76 GLN N . 19800 1 stop_ save_