data_19987 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19987 _Entry.Title ; Characterization and structure of the MIT1 domain of a chitin synthase from the Oomycete Saprolegnia monoica ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2014-05-27 _Entry.Accession_date 2014-05-27 _Entry.Last_release_date 2015-05-26 _Entry.Original_release_date 2015-05-26 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.77 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Vincent Bulone . . . 19987 2 Scarlett Szpryngiel . . . 19987 3 Christian Brown . . . 19987 4 Weihua Ye . . . 19987 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' . 19987 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'MIT domain' . 19987 NMR . 19987 Oomycete . 19987 Saprolegnia . 19987 'carbohydrate synthase' . 19987 'microtubule interacting and trafficking domain' . 19987 protein . 19987 'solution structure' . 19987 'three-helix bundle' . 19987 transferase . 19987 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19987 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 278 19987 '15N chemical shifts' 73 19987 '1H chemical shifts' 494 19987 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 . . 2015-05-26 . original BMRB . 19987 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2MPK 'BMRB Entry Tracking System' 19987 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 19987 _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 ; Characterization and structure of the MIT domains of two chitin synthases from the Oomycete Saprolegnia monoica ; _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'Biochem. J.' _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 Vincent Bulone . . . 19987 1 2 Lena Maler . . . 19987 1 3 Christian Brown . . . 19987 1 4 Scarlett Szpryngiel . . . 19987 1 5 Guanglin KUANG . . . 19987 1 6 Vaibhav SRIVASTAVA . . . 19987 1 7 Weihua Ye . . . 19987 1 8 Yaoquan Tu . . . 19987 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19987 _Assembly.ID 1 _Assembly.Name 'MIT1 domain of a chitin synthase' _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 'SmChs MIT1' 1 $SmChs_MIT1 A . yes native no no . . . 19987 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SmChs_MIT1 _Entity.Sf_category entity _Entity.Sf_framecode SmChs_MIT1 _Entity.Entry_ID 19987 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name SmChs_MIT1 _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 ; MGTIDDAFRAIERAIQAENE GRYREALKHFLDGGEMIVTA AEKEASQKVRNLLLHKGKEV LEWAEHLAEWILEH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq TIDDAFRAIERAIQAENEGRYREALKHFLDGGEMIVTAAEKEASQKVRNLLLHKGKEVLEWAEHLAEWI _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 74 _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 8527.742 _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 2MPK . "Characterization And Structure Of The Mit1 Domain Of A Chitin Synthase From The Oomycete Saprolegnia Monoica" . . . . . 100.00 74 100.00 100.00 8.91e-44 . . . . 19987 1 2 no GB ADE62520 . "chitin synthase 1 [Saprolegnia monoica]" . . . . . 93.24 910 100.00 100.00 5.86e-39 . . . . 19987 1 3 no GB EQC35650 . "hypothetical protein SDRG_06934 [Saprolegnia diclina VS20]" . . . . . 93.24 964 98.55 100.00 2.33e-38 . . . . 19987 1 4 no GB KDO24422 . "hypothetical protein SPRG_09812 [Saprolegnia parasitica CBS 223.65]" . . . . . 93.24 891 98.55 100.00 2.63e-38 . . . . 19987 1 5 no REF XP_008610967 . "hypothetical protein SDRG_06934 [Saprolegnia diclina VS20]" . . . . . 93.24 964 98.55 100.00 2.33e-38 . . . . 19987 1 6 no REF XP_012204852 . "hypothetical protein SPRG_09812 [Saprolegnia parasitica CBS 223.65]" . . . . . 93.24 891 98.55 100.00 2.63e-38 . . . . 19987 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 MET . 19987 1 2 2 GLY . 19987 1 3 3 THR . 19987 1 4 4 ILE . 19987 1 5 5 ASP . 19987 1 6 6 ASP . 19987 1 7 7 ALA . 19987 1 8 8 PHE . 19987 1 9 9 ARG . 19987 1 10 10 ALA . 19987 1 11 11 ILE . 19987 1 12 12 GLU . 19987 1 13 13 ARG . 19987 1 14 14 ALA . 19987 1 15 15 ILE . 19987 1 16 16 GLN . 19987 1 17 17 ALA . 19987 1 18 18 GLU . 19987 1 19 19 ASN . 19987 1 20 20 GLU . 19987 1 21 21 GLY . 19987 1 22 22 ARG . 19987 1 23 23 TYR . 19987 1 24 24 ARG . 19987 1 25 25 GLU . 19987 1 26 26 ALA . 19987 1 27 27 LEU . 19987 1 28 28 LYS . 19987 1 29 29 HIS . 19987 1 30 30 PHE . 19987 1 31 31 LEU . 19987 1 32 32 ASP . 19987 1 33 33 GLY . 19987 1 34 34 GLY . 19987 1 35 35 GLU . 19987 1 36 36 MET . 19987 1 37 37 ILE . 19987 1 38 38 VAL . 19987 1 39 39 THR . 19987 1 40 40 ALA . 19987 1 41 41 ALA . 19987 1 42 42 GLU . 19987 1 43 43 LYS . 19987 1 44 44 GLU . 19987 1 45 45 ALA . 19987 1 46 46 SER . 19987 1 47 47 GLN . 19987 1 48 48 LYS . 19987 1 49 49 VAL . 19987 1 50 50 ARG . 19987 1 51 51 ASN . 19987 1 52 52 LEU . 19987 1 53 53 LEU . 19987 1 54 54 LEU . 19987 1 55 55 HIS . 19987 1 56 56 LYS . 19987 1 57 57 GLY . 19987 1 58 58 LYS . 19987 1 59 59 GLU . 19987 1 60 60 VAL . 19987 1 61 61 LEU . 19987 1 62 62 GLU . 19987 1 63 63 TRP . 19987 1 64 64 ALA . 19987 1 65 65 GLU . 19987 1 66 66 HIS . 19987 1 67 67 LEU . 19987 1 68 68 ALA . 19987 1 69 69 GLU . 19987 1 70 70 TRP . 19987 1 71 71 ILE . 19987 1 72 72 LEU . 19987 1 73 73 GLU . 19987 1 74 74 HIS . 19987 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 19987 1 . GLY 2 2 19987 1 . THR 3 3 19987 1 . ILE 4 4 19987 1 . ASP 5 5 19987 1 . ASP 6 6 19987 1 . ALA 7 7 19987 1 . PHE 8 8 19987 1 . ARG 9 9 19987 1 . ALA 10 10 19987 1 . ILE 11 11 19987 1 . GLU 12 12 19987 1 . ARG 13 13 19987 1 . ALA 14 14 19987 1 . ILE 15 15 19987 1 . GLN 16 16 19987 1 . ALA 17 17 19987 1 . GLU 18 18 19987 1 . ASN 19 19 19987 1 . GLU 20 20 19987 1 . GLY 21 21 19987 1 . ARG 22 22 19987 1 . TYR 23 23 19987 1 . ARG 24 24 19987 1 . GLU 25 25 19987 1 . ALA 26 26 19987 1 . LEU 27 27 19987 1 . LYS 28 28 19987 1 . HIS 29 29 19987 1 . PHE 30 30 19987 1 . LEU 31 31 19987 1 . ASP 32 32 19987 1 . GLY 33 33 19987 1 . GLY 34 34 19987 1 . GLU 35 35 19987 1 . MET 36 36 19987 1 . ILE 37 37 19987 1 . VAL 38 38 19987 1 . THR 39 39 19987 1 . ALA 40 40 19987 1 . ALA 41 41 19987 1 . GLU 42 42 19987 1 . LYS 43 43 19987 1 . GLU 44 44 19987 1 . ALA 45 45 19987 1 . SER 46 46 19987 1 . GLN 47 47 19987 1 . LYS 48 48 19987 1 . VAL 49 49 19987 1 . ARG 50 50 19987 1 . ASN 51 51 19987 1 . LEU 52 52 19987 1 . LEU 53 53 19987 1 . LEU 54 54 19987 1 . HIS 55 55 19987 1 . LYS 56 56 19987 1 . GLY 57 57 19987 1 . LYS 58 58 19987 1 . GLU 59 59 19987 1 . VAL 60 60 19987 1 . LEU 61 61 19987 1 . GLU 62 62 19987 1 . TRP 63 63 19987 1 . ALA 64 64 19987 1 . GLU 65 65 19987 1 . HIS 66 66 19987 1 . LEU 67 67 19987 1 . ALA 68 68 19987 1 . GLU 69 69 19987 1 . TRP 70 70 19987 1 . ILE 71 71 19987 1 . LEU 72 72 19987 1 . GLU 73 73 19987 1 . HIS 74 74 19987 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 19987 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $SmChs_MIT1 . 37553 organism . 'Saprolegnia monoica' oomycetes . . Eukaryota . Saprolegnia monoica . . . . . . . . . . . . . 19987 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 19987 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $SmChs_MIT1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 (DE3)' . . . . . pET-28a(+) . . . 19987 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19987 _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 SmChs_MIT1 '[U-100% 13C; U-100% 15N]' . . 1 $SmChs_MIT1 . . . 0.3 1.0 mM . . . . 19987 1 2 D2O 'natural abundance' . . . . . . 10 . . % . . . . 19987 1 3 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 19987 1 4 'sodium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 19987 1 5 H2O 'natural abundance' . . . . . . 90 . . % . . . . 19987 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 19987 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 200 . mM 19987 1 pH 5 . pH 19987 1 pressure 1 . atm 19987 1 temperature 298 . K 19987 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 19987 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 19987 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19987 1 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 19987 _Software.ID 2 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 19987 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 19987 2 processing 19987 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 19987 _Software.ID 3 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 19987 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19987 3 'data analysis' 19987 3 'peak picking' 19987 3 stop_ save_ save_ProcheckNMR _Software.Sf_category software _Software.Sf_framecode ProcheckNMR _Software.Entry_ID 19987 _Software.ID 4 _Software.Name ProcheckNMR _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Laskowski and MacArthur' . . 19987 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 19987 4 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 19987 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'triple-resonance probe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 19987 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details 'cryogenically cooled probe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 19987 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details 'cryogenically cooled probe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 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 19987 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 600 'triple-resonance probe' . . 19987 1 2 spectrometer_2 Bruker Avance . 700 'cryogenically cooled probe' . . 19987 1 3 spectrometer_3 Bruker Avance . 500 'cryogenically cooled probe' . . 19987 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 19987 _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 . . . . . . . . . . . . . . . . . . . . . 19987 1 2 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 4 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 5 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 6 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 1 8 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19987 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 19987 _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 water protons . . . . ppm 0.251449530 internal indirect 1 . . . . . . . . . 19987 1 H 1 water protons . . . . ppm 4.7 internal direct 1 . . . . . . . . . 19987 1 N 15 water protons . . . . ppm 0.101329118 internal indirect 1 . . . . . . . . . 19987 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 19987 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 19987 1 2 '3D HNCO' . . . 19987 1 3 '3D HNCA' . . . 19987 1 4 '3D HNCACB' . . . 19987 1 5 '3D HN(CO)CA' . . . 19987 1 6 '3D HCCH-TOCSY' . . . 19987 1 7 '3D 1H-15N NOESY' . . . 19987 1 8 '3D 1H-13C NOESY' . . . 19987 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 GLY H H 1 8.43 0.04 . 1 . . . A 2 GLY H . 19987 1 2 . 1 1 2 2 GLY HA2 H 1 3.903 0.02 . 2 . . . A 2 GLY HA2 . 19987 1 3 . 1 1 2 2 GLY HA3 H 1 3.94 0.02 . 2 . . . A 2 GLY HA3 . 19987 1 4 . 1 1 2 2 GLY C C 13 173.309 0.08 . 1 . . . A 2 GLY C . 19987 1 5 . 1 1 2 2 GLY CA C 13 43.45 0.08 . 1 . . . A 2 GLY CA . 19987 1 6 . 1 1 2 2 GLY N N 15 115.116 0.1 . 1 . . . A 2 GLY N . 19987 1 7 . 1 1 3 3 THR H H 1 8.872 0.04 . 1 . . . A 3 THR H . 19987 1 8 . 1 1 3 3 THR HA H 1 4.439 0.04 . 1 . . . A 3 THR HA . 19987 1 9 . 1 1 3 3 THR HG21 H 1 1.199 0.02 . 1 . . . A 3 THR HG21 . 19987 1 10 . 1 1 3 3 THR HG22 H 1 1.199 0.02 . 1 . . . A 3 THR HG22 . 19987 1 11 . 1 1 3 3 THR HG23 H 1 1.199 0.02 . 1 . . . A 3 THR HG23 . 19987 1 12 . 1 1 3 3 THR C C 13 178.4 0.08 . 1 . . . A 3 THR C . 19987 1 13 . 1 1 3 3 THR CA C 13 61.723 0.08 . 1 . . . A 3 THR CA . 19987 1 14 . 1 1 3 3 THR CB C 13 71.3 0.08 . 1 . . . A 3 THR CB . 19987 1 15 . 1 1 3 3 THR CG2 C 13 21.78 0.08 . 1 . . . A 3 THR CG2 . 19987 1 16 . 1 1 3 3 THR N N 15 115.748 0.1 . 1 . . . A 3 THR N . 19987 1 17 . 1 1 4 4 ILE H H 1 8.712 0.04 . 1 . . . A 4 ILE H . 19987 1 18 . 1 1 4 4 ILE HA H 1 3.543 0.04 . 1 . . . A 4 ILE HA . 19987 1 19 . 1 1 4 4 ILE HB H 1 1.7 0.04 . 1 . . . A 4 ILE HB . 19987 1 20 . 1 1 4 4 ILE HG12 H 1 0.84 0.02 . 2 . . . A 4 ILE HG12 . 19987 1 21 . 1 1 4 4 ILE HG13 H 1 1.51 0.02 . 2 . . . A 4 ILE HG13 . 19987 1 22 . 1 1 4 4 ILE HG21 H 1 0.66 0.02 . 1 . . . A 4 ILE HG21 . 19987 1 23 . 1 1 4 4 ILE HG22 H 1 0.66 0.02 . 1 . . . A 4 ILE HG22 . 19987 1 24 . 1 1 4 4 ILE HG23 H 1 0.66 0.02 . 1 . . . A 4 ILE HG23 . 19987 1 25 . 1 1 4 4 ILE HD11 H 1 0.84 0.02 . 1 . . . A 4 ILE HD11 . 19987 1 26 . 1 1 4 4 ILE HD12 H 1 0.84 0.02 . 1 . . . A 4 ILE HD12 . 19987 1 27 . 1 1 4 4 ILE HD13 H 1 0.84 0.02 . 1 . . . A 4 ILE HD13 . 19987 1 28 . 1 1 4 4 ILE C C 13 178.9 0.08 . 1 . . . A 4 ILE C . 19987 1 29 . 1 1 4 4 ILE CA C 13 65.45 0.08 . 1 . . . A 4 ILE CA . 19987 1 30 . 1 1 4 4 ILE CB C 13 37.697 0.08 . 1 . . . A 4 ILE CB . 19987 1 31 . 1 1 4 4 ILE CG1 C 13 29.804 0.08 . 1 . . . A 4 ILE CG1 . 19987 1 32 . 1 1 4 4 ILE CG2 C 13 17.6 0.08 . 1 . . . A 4 ILE CG2 . 19987 1 33 . 1 1 4 4 ILE CD1 C 13 13.4 0.08 . 1 . . . A 4 ILE CD1 . 19987 1 34 . 1 1 4 4 ILE N N 15 125.134 0.1 . 1 . . . A 4 ILE N . 19987 1 35 . 1 1 5 5 ASP H H 1 7.846 0.04 . 1 . . . A 5 ASP H . 19987 1 36 . 1 1 5 5 ASP HA H 1 4.38 0.04 . 1 . . . A 5 ASP HA . 19987 1 37 . 1 1 5 5 ASP HB2 H 1 2.5 0.04 . 2 . . . A 5 ASP HB2 . 19987 1 38 . 1 1 5 5 ASP C C 13 181.2 0.08 . 1 . . . A 5 ASP C . 19987 1 39 . 1 1 5 5 ASP CA C 13 57.05 0.08 . 1 . . . A 5 ASP CA . 19987 1 40 . 1 1 5 5 ASP CB C 13 40.744 0.08 . 1 . . . A 5 ASP CB . 19987 1 41 . 1 1 5 5 ASP N N 15 121.439 0.1 . 1 . . . A 5 ASP N . 19987 1 42 . 1 1 6 6 ASP H H 1 7.823 0.04 . 1 . . . A 6 ASP H . 19987 1 43 . 1 1 6 6 ASP HA H 1 4.24 0.04 . 1 . . . A 6 ASP HA . 19987 1 44 . 1 1 6 6 ASP HB2 H 1 2.611 0.02 . 2 . . . A 6 ASP HB2 . 19987 1 45 . 1 1 6 6 ASP HB3 H 1 2.746 0.02 . 2 . . . A 6 ASP HB3 . 19987 1 46 . 1 1 6 6 ASP C C 13 181.744 0.08 . 1 . . . A 6 ASP C . 19987 1 47 . 1 1 6 6 ASP CA C 13 57.32 0.08 . 1 . . . A 6 ASP CA . 19987 1 48 . 1 1 6 6 ASP CB C 13 40.536 0.08 . 1 . . . A 6 ASP CB . 19987 1 49 . 1 1 6 6 ASP N N 15 121.7 0.1 . 1 . . . A 6 ASP N . 19987 1 50 . 1 1 7 7 ALA H H 1 7.575 0.04 . 1 . . . A 7 ALA H . 19987 1 51 . 1 1 7 7 ALA HA H 1 3.996 0.04 . 1 . . . A 7 ALA HA . 19987 1 52 . 1 1 7 7 ALA HB1 H 1 1.273 0.04 . 1 . . . A 7 ALA HB1 . 19987 1 53 . 1 1 7 7 ALA HB2 H 1 1.273 0.04 . 1 . . . A 7 ALA HB2 . 19987 1 54 . 1 1 7 7 ALA HB3 H 1 1.273 0.04 . 1 . . . A 7 ALA HB3 . 19987 1 55 . 1 1 7 7 ALA C C 13 181.688 0.08 . 1 . . . A 7 ALA C . 19987 1 56 . 1 1 7 7 ALA CA C 13 55.257 0.08 . 1 . . . A 7 ALA CA . 19987 1 57 . 1 1 7 7 ALA CB C 13 18.2 0.08 . 1 . . . A 7 ALA CB . 19987 1 58 . 1 1 7 7 ALA N N 15 126.407 0.1 . 1 . . . A 7 ALA N . 19987 1 59 . 1 1 8 8 PHE H H 1 8.276 0.04 . 1 . . . A 8 PHE H . 19987 1 60 . 1 1 8 8 PHE HA H 1 4.11 0.04 . 1 . . . A 8 PHE HA . 19987 1 61 . 1 1 8 8 PHE HB2 H 1 3.14 0.02 . 2 . . . A 8 PHE HB2 . 19987 1 62 . 1 1 8 8 PHE HB3 H 1 3.21 0.02 . 2 . . . A 8 PHE HB3 . 19987 1 63 . 1 1 8 8 PHE HE1 H 1 7.115 0.02 . 3 . . . A 8 PHE HE1 . 19987 1 64 . 1 1 8 8 PHE HE2 H 1 7.115 0.02 . 3 . . . A 8 PHE HE2 . 19987 1 65 . 1 1 8 8 PHE C C 13 180.421 0.08 . 1 . . . A 8 PHE C . 19987 1 66 . 1 1 8 8 PHE CA C 13 60.451 0.08 . 1 . . . A 8 PHE CA . 19987 1 67 . 1 1 8 8 PHE CB C 13 38.8 0.08 . 1 . . . A 8 PHE CB . 19987 1 68 . 1 1 8 8 PHE N N 15 119.897 0.1 . 1 . . . A 8 PHE N . 19987 1 69 . 1 1 9 9 ARG H H 1 8.09 0.04 . 1 . . . A 9 ARG H . 19987 1 70 . 1 1 9 9 ARG HA H 1 3.932 0.04 . 1 . . . A 9 ARG HA . 19987 1 71 . 1 1 9 9 ARG HB2 H 1 1.881 0.02 . 2 . . . A 9 ARG HB2 . 19987 1 72 . 1 1 9 9 ARG HB3 H 1 1.783 0.02 . 2 . . . A 9 ARG HB3 . 19987 1 73 . 1 1 9 9 ARG HG2 H 1 1.63 0.02 . 2 . . . A 9 ARG HG2 . 19987 1 74 . 1 1 9 9 ARG HG3 H 1 1.77 0.02 . 2 . . . A 9 ARG HG3 . 19987 1 75 . 1 1 9 9 ARG HD2 H 1 3.116 0.02 . 2 . . . A 9 ARG HD2 . 19987 1 76 . 1 1 9 9 ARG HD3 H 1 3.194 0.02 . 2 . . . A 9 ARG HD3 . 19987 1 77 . 1 1 9 9 ARG C C 13 181.674 0.08 . 1 . . . A 9 ARG C . 19987 1 78 . 1 1 9 9 ARG CA C 13 59.344 0.08 . 1 . . . A 9 ARG CA . 19987 1 79 . 1 1 9 9 ARG CB C 13 30.278 0.08 . 1 . . . A 9 ARG CB . 19987 1 80 . 1 1 9 9 ARG CD C 13 43.5 0.08 . 1 . . . A 9 ARG CD . 19987 1 81 . 1 1 9 9 ARG N N 15 119.481 0.1 . 1 . . . A 9 ARG N . 19987 1 82 . 1 1 10 10 ALA H H 1 7.88 0.04 . 1 . . . A 10 ALA H . 19987 1 83 . 1 1 10 10 ALA HA H 1 4 0.04 . 1 . . . A 10 ALA HA . 19987 1 84 . 1 1 10 10 ALA HB1 H 1 1.444 0.04 . 1 . . . A 10 ALA HB1 . 19987 1 85 . 1 1 10 10 ALA HB2 H 1 1.444 0.04 . 1 . . . A 10 ALA HB2 . 19987 1 86 . 1 1 10 10 ALA HB3 H 1 1.444 0.04 . 1 . . . A 10 ALA HB3 . 19987 1 87 . 1 1 10 10 ALA CA C 13 55.191 0.08 . 1 . . . A 10 ALA CA . 19987 1 88 . 1 1 10 10 ALA CB C 13 18.9 0.08 . 1 . . . A 10 ALA CB . 19987 1 89 . 1 1 10 10 ALA N N 15 124.458 0.1 . 1 . . . A 10 ALA N . 19987 1 90 . 1 1 11 11 ILE H H 1 8.295 0.04 . 1 . . . A 11 ILE H . 19987 1 91 . 1 1 11 11 ILE HA H 1 3.52 0.04 . 1 . . . A 11 ILE HA . 19987 1 92 . 1 1 11 11 ILE HB H 1 1.814 0.04 . 1 . . . A 11 ILE HB . 19987 1 93 . 1 1 11 11 ILE HG12 H 1 0.6 0.02 . 2 . . . A 11 ILE HG12 . 19987 1 94 . 1 1 11 11 ILE HG13 H 1 1.83 0.02 . 2 . . . A 11 ILE HG13 . 19987 1 95 . 1 1 11 11 ILE HG21 H 1 0.9 0.02 . 1 . . . A 11 ILE HG21 . 19987 1 96 . 1 1 11 11 ILE HG22 H 1 0.9 0.02 . 1 . . . A 11 ILE HG22 . 19987 1 97 . 1 1 11 11 ILE HG23 H 1 0.9 0.02 . 1 . . . A 11 ILE HG23 . 19987 1 98 . 1 1 11 11 ILE HD11 H 1 0.94 0.02 . 1 . . . A 11 ILE HD11 . 19987 1 99 . 1 1 11 11 ILE HD12 H 1 0.94 0.02 . 1 . . . A 11 ILE HD12 . 19987 1 100 . 1 1 11 11 ILE HD13 H 1 0.94 0.02 . 1 . . . A 11 ILE HD13 . 19987 1 101 . 1 1 11 11 ILE CA C 13 65.682 0.08 . 1 . . . A 11 ILE CA . 19987 1 102 . 1 1 11 11 ILE CB C 13 37.9 0.08 . 1 . . . A 11 ILE CB . 19987 1 103 . 1 1 11 11 ILE CG1 C 13 29.31 0.08 . 1 . . . A 11 ILE CG1 . 19987 1 104 . 1 1 11 11 ILE CG2 C 13 19.4 0.08 . 1 . . . A 11 ILE CG2 . 19987 1 105 . 1 1 11 11 ILE CD1 C 13 15.24 0.08 . 1 . . . A 11 ILE CD1 . 19987 1 106 . 1 1 11 11 ILE N N 15 122.084 0.1 . 1 . . . A 11 ILE N . 19987 1 107 . 1 1 12 12 GLU H H 1 8.3 0.04 . 1 . . . A 12 GLU H . 19987 1 108 . 1 1 12 12 GLU HA H 1 3.81 0.04 . 1 . . . A 12 GLU HA . 19987 1 109 . 1 1 12 12 GLU HB2 H 1 2.06 0.02 . 2 . . . A 12 GLU HB2 . 19987 1 110 . 1 1 12 12 GLU HB3 H 1 1.89 0.02 . 2 . . . A 12 GLU HB3 . 19987 1 111 . 1 1 12 12 GLU HG2 H 1 2.08 0.02 . 2 . . . A 12 GLU HG2 . 19987 1 112 . 1 1 12 12 GLU HG3 H 1 2.354 0.02 . 2 . . . A 12 GLU HG3 . 19987 1 113 . 1 1 12 12 GLU C C 13 181.568 0.08 . 1 . . . A 12 GLU C . 19987 1 114 . 1 1 12 12 GLU CA C 13 59.845 0.08 . 1 . . . A 12 GLU CA . 19987 1 115 . 1 1 12 12 GLU CB C 13 28.51 0.08 . 1 . . . A 12 GLU CB . 19987 1 116 . 1 1 12 12 GLU CG C 13 35 0.08 . 1 . . . A 12 GLU CG . 19987 1 117 . 1 1 12 12 GLU N N 15 121.897 0.1 . 1 . . . A 12 GLU N . 19987 1 118 . 1 1 13 13 ARG H H 1 7.91 0.04 . 1 . . . A 13 ARG H . 19987 1 119 . 1 1 13 13 ARG HA H 1 3.963 0.04 . 1 . . . A 13 ARG HA . 19987 1 120 . 1 1 13 13 ARG HB2 H 1 1.88 0.02 . 2 . . . A 13 ARG HB2 . 19987 1 121 . 1 1 13 13 ARG HB3 H 1 1.78 0.02 . 2 . . . A 13 ARG HB3 . 19987 1 122 . 1 1 13 13 ARG HG2 H 1 1.67 0.02 . 2 . . . A 13 ARG HG2 . 19987 1 123 . 1 1 13 13 ARG HG3 H 1 1.47 0.02 . 2 . . . A 13 ARG HG3 . 19987 1 124 . 1 1 13 13 ARG HD2 H 1 3.13 0.02 . 2 . . . A 13 ARG HD2 . 19987 1 125 . 1 1 13 13 ARG HD3 H 1 3.13 0.02 . 2 . . . A 13 ARG HD3 . 19987 1 126 . 1 1 13 13 ARG CA C 13 59.397 0.08 . 1 . . . A 13 ARG CA . 19987 1 127 . 1 1 13 13 ARG CB C 13 30.272 0.08 . 1 . . . A 13 ARG CB . 19987 1 128 . 1 1 13 13 ARG CG C 13 27.81 0.08 . 1 . . . A 13 ARG CG . 19987 1 129 . 1 1 13 13 ARG CD C 13 43.49 0.08 . 1 . . . A 13 ARG CD . 19987 1 130 . 1 1 13 13 ARG N N 15 121.3 0.1 . 1 . . . A 13 ARG N . 19987 1 131 . 1 1 14 14 ALA H H 1 7.66 0.04 . 1 . . . A 14 ALA H . 19987 1 132 . 1 1 14 14 ALA HA H 1 4.01 0.04 . 1 . . . A 14 ALA HA . 19987 1 133 . 1 1 14 14 ALA HB1 H 1 1.442 0.04 . 1 . . . A 14 ALA HB1 . 19987 1 134 . 1 1 14 14 ALA HB2 H 1 1.442 0.04 . 1 . . . A 14 ALA HB2 . 19987 1 135 . 1 1 14 14 ALA HB3 H 1 1.442 0.04 . 1 . . . A 14 ALA HB3 . 19987 1 136 . 1 1 14 14 ALA CA C 13 55.2 0.08 . 1 . . . A 14 ALA CA . 19987 1 137 . 1 1 14 14 ALA CB C 13 18.9 0.08 . 1 . . . A 14 ALA CB . 19987 1 138 . 1 1 14 14 ALA N N 15 125.443 0.1 . 1 . . . A 14 ALA N . 19987 1 139 . 1 1 15 15 ILE H H 1 8.317 0.04 . 1 . . . A 15 ILE H . 19987 1 140 . 1 1 15 15 ILE HA H 1 3.38 0.04 . 1 . . . A 15 ILE HA . 19987 1 141 . 1 1 15 15 ILE HB H 1 1.86 0.04 . 1 . . . A 15 ILE HB . 19987 1 142 . 1 1 15 15 ILE HG12 H 1 1.76 0.02 . 2 . . . A 15 ILE HG12 . 19987 1 143 . 1 1 15 15 ILE HG13 H 1 0.91 0.02 . 2 . . . A 15 ILE HG13 . 19987 1 144 . 1 1 15 15 ILE HG21 H 1 0.77 0.02 . 1 . . . A 15 ILE HG21 . 19987 1 145 . 1 1 15 15 ILE HG22 H 1 0.77 0.02 . 1 . . . A 15 ILE HG22 . 19987 1 146 . 1 1 15 15 ILE HG23 H 1 0.77 0.02 . 1 . . . A 15 ILE HG23 . 19987 1 147 . 1 1 15 15 ILE HD11 H 1 0.66 0.02 . 1 . . . A 15 ILE HD11 . 19987 1 148 . 1 1 15 15 ILE HD12 H 1 0.66 0.02 . 1 . . . A 15 ILE HD12 . 19987 1 149 . 1 1 15 15 ILE HD13 H 1 0.66 0.02 . 1 . . . A 15 ILE HD13 . 19987 1 150 . 1 1 15 15 ILE CA C 13 66.151 0.08 . 1 . . . A 15 ILE CA . 19987 1 151 . 1 1 15 15 ILE CB C 13 38.34 0.08 . 1 . . . A 15 ILE CB . 19987 1 152 . 1 1 15 15 ILE CG1 C 13 31.18 0.08 . 1 . . . A 15 ILE CG1 . 19987 1 153 . 1 1 15 15 ILE CG2 C 13 17.05 0.08 . 1 . . . A 15 ILE CG2 . 19987 1 154 . 1 1 15 15 ILE CD1 C 13 15.13 0.08 . 1 . . . A 15 ILE CD1 . 19987 1 155 . 1 1 15 15 ILE N N 15 120.9 0.1 . 1 . . . A 15 ILE N . 19987 1 156 . 1 1 16 16 GLN H H 1 7.61 0.04 . 1 . . . A 16 GLN H . 19987 1 157 . 1 1 16 16 GLN HA H 1 3.94 0.04 . 1 . . . A 16 GLN HA . 19987 1 158 . 1 1 16 16 GLN HB2 H 1 2.03 0.02 . 2 . . . A 16 GLN HB2 . 19987 1 159 . 1 1 16 16 GLN HB3 H 1 2.03 0.02 . 2 . . . A 16 GLN HB3 . 19987 1 160 . 1 1 16 16 GLN HG2 H 1 2.34 0.02 . 2 . . . A 16 GLN HG2 . 19987 1 161 . 1 1 16 16 GLN HG3 H 1 2.42 0.02 . 2 . . . A 16 GLN HG3 . 19987 1 162 . 1 1 16 16 GLN C C 13 178.789 0.08 . 1 . . . A 16 GLN C . 19987 1 163 . 1 1 16 16 GLN CA C 13 57.8 0.08 . 1 . . . A 16 GLN CA . 19987 1 164 . 1 1 16 16 GLN CB C 13 28.2 0.08 . 1 . . . A 16 GLN CB . 19987 1 165 . 1 1 16 16 GLN CG C 13 33.85 0.08 . 1 . . . A 16 GLN CG . 19987 1 166 . 1 1 16 16 GLN N N 15 118.3 0.1 . 1 . . . A 16 GLN N . 19987 1 167 . 1 1 17 17 ALA H H 1 7.43 0.04 . 1 . . . A 17 ALA H . 19987 1 168 . 1 1 17 17 ALA HA H 1 4.12 0.04 . 1 . . . A 17 ALA HA . 19987 1 169 . 1 1 17 17 ALA HB1 H 1 1.299 0.04 . 1 . . . A 17 ALA HB1 . 19987 1 170 . 1 1 17 17 ALA HB2 H 1 1.299 0.04 . 1 . . . A 17 ALA HB2 . 19987 1 171 . 1 1 17 17 ALA HB3 H 1 1.299 0.04 . 1 . . . A 17 ALA HB3 . 19987 1 172 . 1 1 17 17 ALA C C 13 180.552 0.08 . 1 . . . A 17 ALA C . 19987 1 173 . 1 1 17 17 ALA CA C 13 53 0.08 . 1 . . . A 17 ALA CA . 19987 1 174 . 1 1 17 17 ALA CB C 13 19.1 0.08 . 1 . . . A 17 ALA CB . 19987 1 175 . 1 1 17 17 ALA N N 15 122.8 0.1 . 1 . . . A 17 ALA N . 19987 1 176 . 1 1 18 18 GLU H H 1 7.61 0.04 . 1 . . . A 18 GLU H . 19987 1 177 . 1 1 18 18 GLU HA H 1 4.2 0.04 . 1 . . . A 18 GLU HA . 19987 1 178 . 1 1 18 18 GLU HB2 H 1 2.08 0.02 . 2 . . . A 18 GLU HB2 . 19987 1 179 . 1 1 18 18 GLU HB3 H 1 1.98 0.02 . 2 . . . A 18 GLU HB3 . 19987 1 180 . 1 1 18 18 GLU HG2 H 1 2.23 0.02 . 2 . . . A 18 GLU HG2 . 19987 1 181 . 1 1 18 18 GLU HG3 H 1 2.23 0.02 . 2 . . . A 18 GLU HG3 . 19987 1 182 . 1 1 18 18 GLU C C 13 178.396 0.08 . 1 . . . A 18 GLU C . 19987 1 183 . 1 1 18 18 GLU CA C 13 55.91 0.08 . 1 . . . A 18 GLU CA . 19987 1 184 . 1 1 18 18 GLU CB C 13 30 0.08 . 1 . . . A 18 GLU CB . 19987 1 185 . 1 1 18 18 GLU CG C 13 35.9 0.08 . 1 . . . A 18 GLU CG . 19987 1 186 . 1 1 18 18 GLU N N 15 122.5 0.1 . 1 . . . A 18 GLU N . 19987 1 187 . 1 1 19 19 ASN H H 1 8.171 0.04 . 1 . . . A 19 ASN H . 19987 1 188 . 1 1 19 19 ASN HA H 1 4.523 0.04 . 1 . . . A 19 ASN HA . 19987 1 189 . 1 1 19 19 ASN HB2 H 1 2.686 0.02 . 2 . . . A 19 ASN HB2 . 19987 1 190 . 1 1 19 19 ASN HB3 H 1 2.809 0.02 . 2 . . . A 19 ASN HB3 . 19987 1 191 . 1 1 19 19 ASN HD21 H 1 7.526 0.02 . 2 . . . A 19 ASN HD21 . 19987 1 192 . 1 1 19 19 ASN HD22 H 1 6.88 0.02 . 2 . . . A 19 ASN HD22 . 19987 1 193 . 1 1 19 19 ASN CA C 13 54.021 0.08 . 1 . . . A 19 ASN CA . 19987 1 194 . 1 1 19 19 ASN CB C 13 39.14 0.08 . 1 . . . A 19 ASN CB . 19987 1 195 . 1 1 19 19 ASN N N 15 122.706 0.1 . 1 . . . A 19 ASN N . 19987 1 196 . 1 1 20 20 GLU H H 1 8.66 0.04 . 1 . . . A 20 GLU H . 19987 1 197 . 1 1 20 20 GLU HA H 1 4.245 0.04 . 1 . . . A 20 GLU HA . 19987 1 198 . 1 1 20 20 GLU HB2 H 1 1.94 0.02 . 2 . . . A 20 GLU HB2 . 19987 1 199 . 1 1 20 20 GLU HB3 H 1 2.07 0.02 . 2 . . . A 20 GLU HB3 . 19987 1 200 . 1 1 20 20 GLU HG2 H 1 2.24 0.02 . 2 . . . A 20 GLU HG2 . 19987 1 201 . 1 1 20 20 GLU HG3 H 1 2.24 0.02 . 2 . . . A 20 GLU HG3 . 19987 1 202 . 1 1 20 20 GLU CA C 13 56.88 0.08 . 1 . . . A 20 GLU CA . 19987 1 203 . 1 1 20 20 GLU CB C 13 29.6 0.08 . 1 . . . A 20 GLU CB . 19987 1 204 . 1 1 20 20 GLU CG C 13 35.35 0.08 . 1 . . . A 20 GLU CG . 19987 1 205 . 1 1 20 20 GLU N N 15 122.771 0.1 . 1 . . . A 20 GLU N . 19987 1 206 . 1 1 21 21 GLY H H 1 8.44 0.04 . 1 . . . A 21 GLY H . 19987 1 207 . 1 1 21 21 GLY HA2 H 1 3.77 0.02 . 2 . . . A 21 GLY HA2 . 19987 1 208 . 1 1 21 21 GLY HA3 H 1 4.3 0.02 . 2 . . . A 21 GLY HA3 . 19987 1 209 . 1 1 21 21 GLY CA C 13 45.9 0.08 . 1 . . . A 21 GLY CA . 19987 1 210 . 1 1 21 21 GLY N N 15 114.594 0.1 . 1 . . . A 21 GLY N . 19987 1 211 . 1 1 22 22 ARG H H 1 8.63 0.04 . 1 . . . A 22 ARG H . 19987 1 212 . 1 1 22 22 ARG HA H 1 4 0.04 . 1 . . . A 22 ARG HA . 19987 1 213 . 1 1 22 22 ARG HB2 H 1 1.5 0.02 . 2 . . . A 22 ARG HB2 . 19987 1 214 . 1 1 22 22 ARG HB3 H 1 1.5 0.02 . 2 . . . A 22 ARG HB3 . 19987 1 215 . 1 1 22 22 ARG HG2 H 1 1.48 0.02 . 2 . . . A 22 ARG HG2 . 19987 1 216 . 1 1 22 22 ARG HG3 H 1 1.48 0.02 . 2 . . . A 22 ARG HG3 . 19987 1 217 . 1 1 22 22 ARG HD2 H 1 3.1 0.02 . 2 . . . A 22 ARG HD2 . 19987 1 218 . 1 1 22 22 ARG HD3 H 1 3.1 0.02 . 2 . . . A 22 ARG HD3 . 19987 1 219 . 1 1 22 22 ARG CA C 13 59.26 0.08 . 1 . . . A 22 ARG CA . 19987 1 220 . 1 1 22 22 ARG CB C 13 30.4 0.08 . 1 . . . A 22 ARG CB . 19987 1 221 . 1 1 22 22 ARG CG C 13 28.05 0.08 . 1 . . . A 22 ARG CG . 19987 1 222 . 1 1 22 22 ARG CD C 13 43.12 0.08 . 1 . . . A 22 ARG CD . 19987 1 223 . 1 1 22 22 ARG N N 15 121.2 0.04 . 1 . . . A 22 ARG N . 19987 1 224 . 1 1 23 23 TYR H H 1 7.63 0.04 . 1 . . . A 23 TYR H . 19987 1 225 . 1 1 23 23 TYR HA H 1 4.2 0.04 . 1 . . . A 23 TYR HA . 19987 1 226 . 1 1 23 23 TYR HB2 H 1 2.9 0.02 . 2 . . . A 23 TYR HB2 . 19987 1 227 . 1 1 23 23 TYR HB3 H 1 3 0.02 . 2 . . . A 23 TYR HB3 . 19987 1 228 . 1 1 23 23 TYR HD1 H 1 7 0.02 . 3 . . . A 23 TYR HD1 . 19987 1 229 . 1 1 23 23 TYR HD2 H 1 7 0.02 . 3 . . . A 23 TYR HD2 . 19987 1 230 . 1 1 23 23 TYR HE1 H 1 6.77 0.02 . 3 . . . A 23 TYR HE1 . 19987 1 231 . 1 1 23 23 TYR HE2 H 1 6.77 0.02 . 3 . . . A 23 TYR HE2 . 19987 1 232 . 1 1 23 23 TYR C C 13 180 0.08 . 1 . . . A 23 TYR C . 19987 1 233 . 1 1 23 23 TYR CA C 13 61.5 0.08 . 1 . . . A 23 TYR CA . 19987 1 234 . 1 1 23 23 TYR CB C 13 37.725 0.08 . 1 . . . A 23 TYR CB . 19987 1 235 . 1 1 23 23 TYR N N 15 118.4 0.1 . 1 . . . A 23 TYR N . 19987 1 236 . 1 1 24 24 ARG H H 1 8.115 0.04 . 1 . . . A 24 ARG H . 19987 1 237 . 1 1 24 24 ARG HA H 1 3.7 0.04 . 1 . . . A 24 ARG HA . 19987 1 238 . 1 1 24 24 ARG HB2 H 1 1.96 0.02 . 2 . . . A 24 ARG HB2 . 19987 1 239 . 1 1 24 24 ARG HB3 H 1 1.88 0.02 . 2 . . . A 24 ARG HB3 . 19987 1 240 . 1 1 24 24 ARG HG2 H 1 1.55 0.02 . 2 . . . A 24 ARG HG2 . 19987 1 241 . 1 1 24 24 ARG HG3 H 1 1.55 0.02 . 2 . . . A 24 ARG HG3 . 19987 1 242 . 1 1 24 24 ARG HD2 H 1 3.12 0.02 . 2 . . . A 24 ARG HD2 . 19987 1 243 . 1 1 24 24 ARG HD3 H 1 3.12 0.02 . 2 . . . A 24 ARG HD3 . 19987 1 244 . 1 1 24 24 ARG C C 13 180.296 0.08 . 1 . . . A 24 ARG C . 19987 1 245 . 1 1 24 24 ARG CA C 13 60.719 0.08 . 1 . . . A 24 ARG CA . 19987 1 246 . 1 1 24 24 ARG CB C 13 30.74 0.08 . 1 . . . A 24 ARG CB . 19987 1 247 . 1 1 24 24 ARG CG C 13 27.9 0.08 . 1 . . . A 24 ARG CG . 19987 1 248 . 1 1 24 24 ARG CD C 13 43.7 0.08 . 1 . . . A 24 ARG CD . 19987 1 249 . 1 1 24 24 ARG N N 15 122.775 0.1 . 1 . . . A 24 ARG N . 19987 1 250 . 1 1 25 25 GLU H H 1 8.129 0.04 . 1 . . . A 25 GLU H . 19987 1 251 . 1 1 25 25 GLU HA H 1 3.838 0.04 . 1 . . . A 25 GLU HA . 19987 1 252 . 1 1 25 25 GLU HB2 H 1 2.091 0.02 . 2 . . . A 25 GLU HB2 . 19987 1 253 . 1 1 25 25 GLU HB3 H 1 1.938 0.02 . 2 . . . A 25 GLU HB3 . 19987 1 254 . 1 1 25 25 GLU HG2 H 1 2.28 0.02 . 2 . . . A 25 GLU HG2 . 19987 1 255 . 1 1 25 25 GLU HG3 H 1 2.34 0.02 . 2 . . . A 25 GLU HG3 . 19987 1 256 . 1 1 25 25 GLU C C 13 181.79 0.08 . 1 . . . A 25 GLU C . 19987 1 257 . 1 1 25 25 GLU CA C 13 58.901 0.08 . 1 . . . A 25 GLU CA . 19987 1 258 . 1 1 25 25 GLU CB C 13 29.415 0.08 . 1 . . . A 25 GLU CB . 19987 1 259 . 1 1 25 25 GLU CG C 13 35.9 0.08 . 1 . . . A 25 GLU CG . 19987 1 260 . 1 1 25 25 GLU N N 15 118.953 0.1 . 1 . . . A 25 GLU N . 19987 1 261 . 1 1 26 26 ALA H H 1 8.322 0.04 . 1 . . . A 26 ALA H . 19987 1 262 . 1 1 26 26 ALA HA H 1 3.897 0.04 . 1 . . . A 26 ALA HA . 19987 1 263 . 1 1 26 26 ALA HB1 H 1 1.56 0.04 . 1 . . . A 26 ALA HB1 . 19987 1 264 . 1 1 26 26 ALA HB2 H 1 1.56 0.04 . 1 . . . A 26 ALA HB2 . 19987 1 265 . 1 1 26 26 ALA HB3 H 1 1.56 0.04 . 1 . . . A 26 ALA HB3 . 19987 1 266 . 1 1 26 26 ALA C C 13 180.8 0.08 . 1 . . . A 26 ALA C . 19987 1 267 . 1 1 26 26 ALA CA C 13 56.069 0.08 . 1 . . . A 26 ALA CA . 19987 1 268 . 1 1 26 26 ALA CB C 13 18.315 0.08 . 1 . . . A 26 ALA CB . 19987 1 269 . 1 1 26 26 ALA N N 15 125.639 0.1 . 1 . . . A 26 ALA N . 19987 1 270 . 1 1 27 27 LEU H H 1 8 0.04 . 1 . . . A 27 LEU H . 19987 1 271 . 1 1 27 27 LEU HA H 1 4.08 0.04 . 1 . . . A 27 LEU HA . 19987 1 272 . 1 1 27 27 LEU HB2 H 1 2.053 0.02 . 2 . . . A 27 LEU HB2 . 19987 1 273 . 1 1 27 27 LEU HB3 H 1 1.234 0.02 . 2 . . . A 27 LEU HB3 . 19987 1 274 . 1 1 27 27 LEU HG H 1 2 0.04 . 1 . . . A 27 LEU HG . 19987 1 275 . 1 1 27 27 LEU HD11 H 1 0.91 0.02 . 2 . . . A 27 LEU HD11 . 19987 1 276 . 1 1 27 27 LEU HD12 H 1 0.91 0.02 . 2 . . . A 27 LEU HD12 . 19987 1 277 . 1 1 27 27 LEU HD13 H 1 0.91 0.02 . 2 . . . A 27 LEU HD13 . 19987 1 278 . 1 1 27 27 LEU HD21 H 1 0.8 0.02 . 2 . . . A 27 LEU HD21 . 19987 1 279 . 1 1 27 27 LEU HD22 H 1 0.8 0.02 . 2 . . . A 27 LEU HD22 . 19987 1 280 . 1 1 27 27 LEU HD23 H 1 0.8 0.02 . 2 . . . A 27 LEU HD23 . 19987 1 281 . 1 1 27 27 LEU CA C 13 58.3 0.08 . 1 . . . A 27 LEU CA . 19987 1 282 . 1 1 27 27 LEU CB C 13 42.3 0.08 . 1 . . . A 27 LEU CB . 19987 1 283 . 1 1 27 27 LEU CG C 13 26.78 0.08 . 1 . . . A 27 LEU CG . 19987 1 284 . 1 1 27 27 LEU CD1 C 13 22.85 0.08 . 2 . . . A 27 LEU CD1 . 19987 1 285 . 1 1 27 27 LEU CD2 C 13 25.6 0.08 . 2 . . . A 27 LEU CD2 . 19987 1 286 . 1 1 27 27 LEU N N 15 117.6 0.1 . 1 . . . A 27 LEU N . 19987 1 287 . 1 1 28 28 LYS H H 1 7.971 0.04 . 1 . . . A 28 LYS H . 19987 1 288 . 1 1 28 28 LYS HA H 1 3.779 0.04 . 1 . . . A 28 LYS HA . 19987 1 289 . 1 1 28 28 LYS HB2 H 1 1.82 0.02 . 2 . . . A 28 LYS HB2 . 19987 1 290 . 1 1 28 28 LYS HB3 H 1 1.578 0.02 . 2 . . . A 28 LYS HB3 . 19987 1 291 . 1 1 28 28 LYS HG2 H 1 1.32 0.02 . 2 . . . A 28 LYS HG2 . 19987 1 292 . 1 1 28 28 LYS HG3 H 1 1.32 0.02 . 2 . . . A 28 LYS HG3 . 19987 1 293 . 1 1 28 28 LYS HD2 H 1 1.4 0.02 . 2 . . . A 28 LYS HD2 . 19987 1 294 . 1 1 28 28 LYS HD3 H 1 1.4 0.02 . 2 . . . A 28 LYS HD3 . 19987 1 295 . 1 1 28 28 LYS HE2 H 1 2.79 0.02 . 2 . . . A 28 LYS HE2 . 19987 1 296 . 1 1 28 28 LYS HE3 H 1 2.86 0.02 . 2 . . . A 28 LYS HE3 . 19987 1 297 . 1 1 28 28 LYS C C 13 179.4 0.08 . 1 . . . A 28 LYS C . 19987 1 298 . 1 1 28 28 LYS CA C 13 58.297 0.08 . 1 . . . A 28 LYS CA . 19987 1 299 . 1 1 28 28 LYS CB C 13 32.2 0.08 . 1 . . . A 28 LYS CB . 19987 1 300 . 1 1 28 28 LYS CG C 13 25.05 0.08 . 1 . . . A 28 LYS CG . 19987 1 301 . 1 1 28 28 LYS CD C 13 28.9 0.08 . 1 . . . A 28 LYS CD . 19987 1 302 . 1 1 28 28 LYS CE C 13 42.1 0.08 . 1 . . . A 28 LYS CE . 19987 1 303 . 1 1 28 28 LYS N N 15 121.2 0.1 . 1 . . . A 28 LYS N . 19987 1 304 . 1 1 29 29 HIS H H 1 7.67 0.04 . 1 . . . A 29 HIS H . 19987 1 305 . 1 1 29 29 HIS HA H 1 4.55 0.04 . 1 . . . A 29 HIS HA . 19987 1 306 . 1 1 29 29 HIS HB2 H 1 3.163 0.02 . 2 . . . A 29 HIS HB2 . 19987 1 307 . 1 1 29 29 HIS HB3 H 1 2.928 0.02 . 2 . . . A 29 HIS HB3 . 19987 1 308 . 1 1 29 29 HIS HD2 H 1 7.16 0.04 . 1 . . . A 29 HIS HD2 . 19987 1 309 . 1 1 29 29 HIS C C 13 178.209 0.08 . 1 . . . A 29 HIS C . 19987 1 310 . 1 1 29 29 HIS CA C 13 55.4 0.08 . 1 . . . A 29 HIS CA . 19987 1 311 . 1 1 29 29 HIS N N 15 119.923 0.1 . 1 . . . A 29 HIS N . 19987 1 312 . 1 1 30 30 PHE H H 1 7.906 0.04 . 1 . . . A 30 PHE H . 19987 1 313 . 1 1 30 30 PHE HA H 1 4.532 0.04 . 1 . . . A 30 PHE HA . 19987 1 314 . 1 1 30 30 PHE HB2 H 1 3.16 0.02 . 2 . . . A 30 PHE HB2 . 19987 1 315 . 1 1 30 30 PHE HB3 H 1 3.24 0.02 . 2 . . . A 30 PHE HB3 . 19987 1 316 . 1 1 30 30 PHE HD1 H 1 7.28 0.02 . 3 . . . A 30 PHE HD1 . 19987 1 317 . 1 1 30 30 PHE HD2 H 1 7.28 0.02 . 3 . . . A 30 PHE HD2 . 19987 1 318 . 1 1 30 30 PHE HE1 H 1 7.19 0.02 . 3 . . . A 30 PHE HE1 . 19987 1 319 . 1 1 30 30 PHE HE2 H 1 7.19 0.02 . 3 . . . A 30 PHE HE2 . 19987 1 320 . 1 1 30 30 PHE C C 13 180.101 0.08 . 1 . . . A 30 PHE C . 19987 1 321 . 1 1 30 30 PHE CA C 13 60.962 0.08 . 1 . . . A 30 PHE CA . 19987 1 322 . 1 1 30 30 PHE CB C 13 38.315 0.08 . 1 . . . A 30 PHE CB . 19987 1 323 . 1 1 30 30 PHE N N 15 120.6 0.1 . 1 . . . A 30 PHE N . 19987 1 324 . 1 1 31 31 LEU H H 1 8.428 0.04 . 1 . . . A 31 LEU H . 19987 1 325 . 1 1 31 31 LEU HA H 1 3.964 0.04 . 1 . . . A 31 LEU HA . 19987 1 326 . 1 1 31 31 LEU HB2 H 1 1.49 0.02 . 2 . . . A 31 LEU HB2 . 19987 1 327 . 1 1 31 31 LEU HB3 H 1 1.882 0.02 . 2 . . . A 31 LEU HB3 . 19987 1 328 . 1 1 31 31 LEU HD11 H 1 0.78 0.02 . 2 . . . A 31 LEU HD11 . 19987 1 329 . 1 1 31 31 LEU HD12 H 1 0.78 0.02 . 2 . . . A 31 LEU HD12 . 19987 1 330 . 1 1 31 31 LEU HD13 H 1 0.78 0.02 . 2 . . . A 31 LEU HD13 . 19987 1 331 . 1 1 31 31 LEU HD21 H 1 0.7 0.02 . 2 . . . A 31 LEU HD21 . 19987 1 332 . 1 1 31 31 LEU HD22 H 1 0.7 0.02 . 2 . . . A 31 LEU HD22 . 19987 1 333 . 1 1 31 31 LEU HD23 H 1 0.7 0.02 . 2 . . . A 31 LEU HD23 . 19987 1 334 . 1 1 31 31 LEU C C 13 180.185 0.08 . 1 . . . A 31 LEU C . 19987 1 335 . 1 1 31 31 LEU CA C 13 58.458 0.08 . 1 . . . A 31 LEU CA . 19987 1 336 . 1 1 31 31 LEU CB C 13 42.216 0.08 . 1 . . . A 31 LEU CB . 19987 1 337 . 1 1 31 31 LEU CG C 13 26.7 0.08 . 1 . . . A 31 LEU CG . 19987 1 338 . 1 1 31 31 LEU CD1 C 13 24.7 0.08 . 2 . . . A 31 LEU CD1 . 19987 1 339 . 1 1 31 31 LEU CD2 C 13 26.1 0.08 . 2 . . . A 31 LEU CD2 . 19987 1 340 . 1 1 31 31 LEU N N 15 123.705 0.1 . 1 . . . A 31 LEU N . 19987 1 341 . 1 1 32 32 ASP H H 1 8.6 0.04 . 1 . . . A 32 ASP H . 19987 1 342 . 1 1 32 32 ASP HA H 1 4.123 0.04 . 1 . . . A 32 ASP HA . 19987 1 343 . 1 1 32 32 ASP HB2 H 1 1.71 0.02 . 2 . . . A 32 ASP HB2 . 19987 1 344 . 1 1 32 32 ASP HB3 H 1 1.71 0.02 . 2 . . . A 32 ASP HB3 . 19987 1 345 . 1 1 32 32 ASP C C 13 182.699 0.08 . 1 . . . A 32 ASP C . 19987 1 346 . 1 1 32 32 ASP CA C 13 56.8 0.08 . 1 . . . A 32 ASP CA . 19987 1 347 . 1 1 32 32 ASP CB C 13 38.5 0.08 . 1 . . . A 32 ASP CB . 19987 1 348 . 1 1 32 32 ASP N N 15 121.2 0.1 . 1 . . . A 32 ASP N . 19987 1 349 . 1 1 33 33 GLY H H 1 8.59 0.04 . 1 . . . A 33 GLY H . 19987 1 350 . 1 1 33 33 GLY HA2 H 1 3.493 0.02 . 2 . . . A 33 GLY HA2 . 19987 1 351 . 1 1 33 33 GLY HA3 H 1 3.165 0.02 . 2 . . . A 33 GLY HA3 . 19987 1 352 . 1 1 33 33 GLY C C 13 178.2 0.08 . 1 . . . A 33 GLY C . 19987 1 353 . 1 1 33 33 GLY CA C 13 48.092 0.08 . 1 . . . A 33 GLY CA . 19987 1 354 . 1 1 33 33 GLY N N 15 109.8 0.1 . 1 . . . A 33 GLY N . 19987 1 355 . 1 1 34 34 GLY H H 1 8.891 0.04 . 1 . . . A 34 GLY H . 19987 1 356 . 1 1 34 34 GLY HA2 H 1 3.902 0.02 . 2 . . . A 34 GLY HA2 . 19987 1 357 . 1 1 34 34 GLY HA3 H 1 3.801 0.02 . 2 . . . A 34 GLY HA3 . 19987 1 358 . 1 1 34 34 GLY C C 13 177.497 0.08 . 1 . . . A 34 GLY C . 19987 1 359 . 1 1 34 34 GLY CA C 13 47.9 0.08 . 1 . . . A 34 GLY CA . 19987 1 360 . 1 1 34 34 GLY N N 15 113.215 0.1 . 1 . . . A 34 GLY N . 19987 1 361 . 1 1 35 35 GLU H H 1 8.92 0.04 . 1 . . . A 35 GLU H . 19987 1 362 . 1 1 35 35 GLU HA H 1 4.129 0.04 . 1 . . . A 35 GLU HA . 19987 1 363 . 1 1 35 35 GLU HB2 H 1 2.16 0.02 . 2 . . . A 35 GLU HB2 . 19987 1 364 . 1 1 35 35 GLU HB3 H 1 2.08 0.02 . 2 . . . A 35 GLU HB3 . 19987 1 365 . 1 1 35 35 GLU HG2 H 1 2.35 0.02 . 2 . . . A 35 GLU HG2 . 19987 1 366 . 1 1 35 35 GLU HG3 H 1 2.2 0.02 . 2 . . . A 35 GLU HG3 . 19987 1 367 . 1 1 35 35 GLU C C 13 181.687 0.08 . 1 . . . A 35 GLU C . 19987 1 368 . 1 1 35 35 GLU CA C 13 59.458 0.08 . 1 . . . A 35 GLU CA . 19987 1 369 . 1 1 35 35 GLU CB C 13 28.4 0.08 . 1 . . . A 35 GLU CB . 19987 1 370 . 1 1 35 35 GLU CG C 13 34 0.08 . 1 . . . A 35 GLU CG . 19987 1 371 . 1 1 35 35 GLU N N 15 123.4 0.1 . 1 . . . A 35 GLU N . 19987 1 372 . 1 1 36 36 MET H H 1 8.098 0.04 . 1 . . . A 36 MET H . 19987 1 373 . 1 1 36 36 MET HA H 1 4.127 0.04 . 1 . . . A 36 MET HA . 19987 1 374 . 1 1 36 36 MET HB2 H 1 2.35 0.02 . 2 . . . A 36 MET HB2 . 19987 1 375 . 1 1 36 36 MET HB3 H 1 2.03 0.02 . 2 . . . A 36 MET HB3 . 19987 1 376 . 1 1 36 36 MET HG2 H 1 2.83 0.02 . 2 . . . A 36 MET HG2 . 19987 1 377 . 1 1 36 36 MET HG3 H 1 2.55 0.02 . 2 . . . A 36 MET HG3 . 19987 1 378 . 1 1 36 36 MET C C 13 181.05 0.08 . 1 . . . A 36 MET C . 19987 1 379 . 1 1 36 36 MET CA C 13 59.399 0.08 . 1 . . . A 36 MET CA . 19987 1 380 . 1 1 36 36 MET CB C 13 33.2 0.08 . 1 . . . A 36 MET CB . 19987 1 381 . 1 1 36 36 MET CG C 13 33.943 0.08 . 1 . . . A 36 MET CG . 19987 1 382 . 1 1 36 36 MET N N 15 121.995 0.1 . 1 . . . A 36 MET N . 19987 1 383 . 1 1 37 37 ILE H H 1 7.984 0.04 . 1 . . . A 37 ILE H . 19987 1 384 . 1 1 37 37 ILE HA H 1 3.889 0.04 . 1 . . . A 37 ILE HA . 19987 1 385 . 1 1 37 37 ILE HB H 1 2.38 0.04 . 1 . . . A 37 ILE HB . 19987 1 386 . 1 1 37 37 ILE HG12 H 1 1.95 0.02 . 2 . . . A 37 ILE HG12 . 19987 1 387 . 1 1 37 37 ILE HG13 H 1 1.75 0.02 . 2 . . . A 37 ILE HG13 . 19987 1 388 . 1 1 37 37 ILE HG21 H 1 1.02 0.04 . 1 . . . A 37 ILE HG21 . 19987 1 389 . 1 1 37 37 ILE HG22 H 1 1.02 0.04 . 1 . . . A 37 ILE HG22 . 19987 1 390 . 1 1 37 37 ILE HG23 H 1 1.02 0.04 . 1 . . . A 37 ILE HG23 . 19987 1 391 . 1 1 37 37 ILE HD11 H 1 1 0.02 . 1 . . . A 37 ILE HD11 . 19987 1 392 . 1 1 37 37 ILE HD12 H 1 1 0.02 . 1 . . . A 37 ILE HD12 . 19987 1 393 . 1 1 37 37 ILE HD13 H 1 1 0.02 . 1 . . . A 37 ILE HD13 . 19987 1 394 . 1 1 37 37 ILE C C 13 179.434 0.08 . 1 . . . A 37 ILE C . 19987 1 395 . 1 1 37 37 ILE CA C 13 63.177 0.08 . 1 . . . A 37 ILE CA . 19987 1 396 . 1 1 37 37 ILE CB C 13 36.411 0.08 . 1 . . . A 37 ILE CB . 19987 1 397 . 1 1 37 37 ILE CG1 C 13 27.9 0.08 . 1 . . . A 37 ILE CG1 . 19987 1 398 . 1 1 37 37 ILE CG2 C 13 18.5 0.08 . 1 . . . A 37 ILE CG2 . 19987 1 399 . 1 1 37 37 ILE CD1 C 13 11.2 0.08 . 1 . . . A 37 ILE CD1 . 19987 1 400 . 1 1 37 37 ILE N N 15 121.6 0.1 . 1 . . . A 37 ILE N . 19987 1 401 . 1 1 38 38 VAL H H 1 7.98 0.04 . 1 . . . A 38 VAL H . 19987 1 402 . 1 1 38 38 VAL HA H 1 3.569 0.04 . 1 . . . A 38 VAL HA . 19987 1 403 . 1 1 38 38 VAL HB H 1 2.282 0.04 . 1 . . . A 38 VAL HB . 19987 1 404 . 1 1 38 38 VAL HG11 H 1 1.082 0.02 . 2 . . . A 38 VAL HG11 . 19987 1 405 . 1 1 38 38 VAL HG12 H 1 1.082 0.02 . 2 . . . A 38 VAL HG12 . 19987 1 406 . 1 1 38 38 VAL HG13 H 1 1.082 0.02 . 2 . . . A 38 VAL HG13 . 19987 1 407 . 1 1 38 38 VAL HG21 H 1 0.94 0.02 . 2 . . . A 38 VAL HG21 . 19987 1 408 . 1 1 38 38 VAL HG22 H 1 0.94 0.02 . 2 . . . A 38 VAL HG22 . 19987 1 409 . 1 1 38 38 VAL HG23 H 1 0.94 0.02 . 2 . . . A 38 VAL HG23 . 19987 1 410 . 1 1 38 38 VAL C C 13 180.416 0.08 . 1 . . . A 38 VAL C . 19987 1 411 . 1 1 38 38 VAL CA C 13 67.302 0.08 . 1 . . . A 38 VAL CA . 19987 1 412 . 1 1 38 38 VAL CB C 13 31.6 0.08 . 1 . . . A 38 VAL CB . 19987 1 413 . 1 1 38 38 VAL CG1 C 13 22.6 0.08 . 2 . . . A 38 VAL CG1 . 19987 1 414 . 1 1 38 38 VAL CG2 C 13 21.23 0.08 . 2 . . . A 38 VAL CG2 . 19987 1 415 . 1 1 38 38 VAL N N 15 121.9 0.1 . 1 . . . A 38 VAL N . 19987 1 416 . 1 1 39 39 THR H H 1 8.34 0.04 . 1 . . . A 39 THR H . 19987 1 417 . 1 1 39 39 THR HA H 1 3.894 0.04 . 1 . . . A 39 THR HA . 19987 1 418 . 1 1 39 39 THR HB H 1 4.103 0.04 . 1 . . . A 39 THR HB . 19987 1 419 . 1 1 39 39 THR HG21 H 1 1.14 0.04 . 1 . . . A 39 THR HG21 . 19987 1 420 . 1 1 39 39 THR HG22 H 1 1.14 0.04 . 1 . . . A 39 THR HG22 . 19987 1 421 . 1 1 39 39 THR HG23 H 1 1.14 0.04 . 1 . . . A 39 THR HG23 . 19987 1 422 . 1 1 39 39 THR C C 13 179.461 0.08 . 1 . . . A 39 THR C . 19987 1 423 . 1 1 39 39 THR CA C 13 66.393 0.08 . 1 . . . A 39 THR CA . 19987 1 424 . 1 1 39 39 THR CB C 13 69.3 0.08 . 1 . . . A 39 THR CB . 19987 1 425 . 1 1 39 39 THR CG2 C 13 21.795 0.08 . 1 . . . A 39 THR CG2 . 19987 1 426 . 1 1 39 39 THR N N 15 117.704 0.1 . 1 . . . A 39 THR N . 19987 1 427 . 1 1 40 40 ALA H H 1 8.14 0.04 . 1 . . . A 40 ALA H . 19987 1 428 . 1 1 40 40 ALA HA H 1 3.863 0.04 . 1 . . . A 40 ALA HA . 19987 1 429 . 1 1 40 40 ALA HB1 H 1 1.16 0.04 . 1 . . . A 40 ALA HB1 . 19987 1 430 . 1 1 40 40 ALA HB2 H 1 1.16 0.04 . 1 . . . A 40 ALA HB2 . 19987 1 431 . 1 1 40 40 ALA HB3 H 1 1.16 0.04 . 1 . . . A 40 ALA HB3 . 19987 1 432 . 1 1 40 40 ALA C C 13 183.3 0.08 . 1 . . . A 40 ALA C . 19987 1 433 . 1 1 40 40 ALA CA C 13 55.162 0.08 . 1 . . . A 40 ALA CA . 19987 1 434 . 1 1 40 40 ALA CB C 13 18.001 0.08 . 1 . . . A 40 ALA CB . 19987 1 435 . 1 1 40 40 ALA N N 15 126.4 0.1 . 1 . . . A 40 ALA N . 19987 1 436 . 1 1 41 41 ALA H H 1 8.49 0.04 . 1 . . . A 41 ALA H . 19987 1 437 . 1 1 41 41 ALA HA H 1 3.96 0.04 . 1 . . . A 41 ALA HA . 19987 1 438 . 1 1 41 41 ALA HB1 H 1 1.61 0.04 . 1 . . . A 41 ALA HB1 . 19987 1 439 . 1 1 41 41 ALA HB2 H 1 1.61 0.04 . 1 . . . A 41 ALA HB2 . 19987 1 440 . 1 1 41 41 ALA HB3 H 1 1.61 0.04 . 1 . . . A 41 ALA HB3 . 19987 1 441 . 1 1 41 41 ALA C C 13 181.903 0.08 . 1 . . . A 41 ALA C . 19987 1 442 . 1 1 41 41 ALA CA C 13 55.304 0.08 . 1 . . . A 41 ALA CA . 19987 1 443 . 1 1 41 41 ALA CB C 13 19.022 0.08 . 1 . . . A 41 ALA CB . 19987 1 444 . 1 1 41 41 ALA N N 15 123.8 0.1 . 1 . . . A 41 ALA N . 19987 1 445 . 1 1 42 42 GLU H H 1 7.507 0.04 . 1 . . . A 42 GLU H . 19987 1 446 . 1 1 42 42 GLU HA H 1 3.963 0.04 . 1 . . . A 42 GLU HA . 19987 1 447 . 1 1 42 42 GLU HB2 H 1 2.13 0.02 . 2 . . . A 42 GLU HB2 . 19987 1 448 . 1 1 42 42 GLU HB3 H 1 2.05 0.02 . 2 . . . A 42 GLU HB3 . 19987 1 449 . 1 1 42 42 GLU HG2 H 1 2.6 0.02 . 2 . . . A 42 GLU HG2 . 19987 1 450 . 1 1 42 42 GLU HG3 H 1 2.42 0.02 . 2 . . . A 42 GLU HG3 . 19987 1 451 . 1 1 42 42 GLU C C 13 180.24 0.08 . 1 . . . A 42 GLU C . 19987 1 452 . 1 1 42 42 GLU CA C 13 58.1 0.08 . 1 . . . A 42 GLU CA . 19987 1 453 . 1 1 42 42 GLU CB C 13 29 0.08 . 1 . . . A 42 GLU CB . 19987 1 454 . 1 1 42 42 GLU CG C 13 34.9 0.08 . 1 . . . A 42 GLU CG . 19987 1 455 . 1 1 42 42 GLU N N 15 115.497 0.1 . 1 . . . A 42 GLU N . 19987 1 456 . 1 1 43 43 LYS H H 1 7.4 0.04 . 1 . . . A 43 LYS H . 19987 1 457 . 1 1 43 43 LYS HA H 1 4.298 0.04 . 1 . . . A 43 LYS HA . 19987 1 458 . 1 1 43 43 LYS HB2 H 1 1.748 0.02 . 2 . . . A 43 LYS HB2 . 19987 1 459 . 1 1 43 43 LYS HB3 H 1 2.04 0.02 . 2 . . . A 43 LYS HB3 . 19987 1 460 . 1 1 43 43 LYS HG2 H 1 1.46 0.02 . 2 . . . A 43 LYS HG2 . 19987 1 461 . 1 1 43 43 LYS HG3 H 1 1.46 0.02 . 2 . . . A 43 LYS HG3 . 19987 1 462 . 1 1 43 43 LYS HD2 H 1 1.59 0.02 . 2 . . . A 43 LYS HD2 . 19987 1 463 . 1 1 43 43 LYS HD3 H 1 1.59 0.02 . 2 . . . A 43 LYS HD3 . 19987 1 464 . 1 1 43 43 LYS C C 13 179.5 0.08 . 1 . . . A 43 LYS C . 19987 1 465 . 1 1 43 43 LYS CA C 13 55.203 0.08 . 1 . . . A 43 LYS CA . 19987 1 466 . 1 1 43 43 LYS CB C 13 32.63 0.08 . 1 . . . A 43 LYS CB . 19987 1 467 . 1 1 43 43 LYS CG C 13 24.7 0.08 . 1 . . . A 43 LYS CG . 19987 1 468 . 1 1 43 43 LYS CD C 13 28.5 0.08 . 1 . . . A 43 LYS CD . 19987 1 469 . 1 1 43 43 LYS CE C 13 42.184 0.08 . 1 . . . A 43 LYS CE . 19987 1 470 . 1 1 43 43 LYS N N 15 118.3 0.1 . 1 . . . A 43 LYS N . 19987 1 471 . 1 1 44 44 GLU H H 1 7.46 0.04 . 1 . . . A 44 GLU H . 19987 1 472 . 1 1 44 44 GLU HA H 1 4.19 0.04 . 1 . . . A 44 GLU HA . 19987 1 473 . 1 1 44 44 GLU HB2 H 1 2.14 0.02 . 2 . . . A 44 GLU HB2 . 19987 1 474 . 1 1 44 44 GLU HB3 H 1 2.01 0.02 . 2 . . . A 44 GLU HB3 . 19987 1 475 . 1 1 44 44 GLU HG2 H 1 2.3 0.02 . 2 . . . A 44 GLU HG2 . 19987 1 476 . 1 1 44 44 GLU HG3 H 1 2.61 0.02 . 2 . . . A 44 GLU HG3 . 19987 1 477 . 1 1 44 44 GLU C C 13 178.824 0.08 . 1 . . . A 44 GLU C . 19987 1 478 . 1 1 44 44 GLU CA C 13 56.47 0.08 . 1 . . . A 44 GLU CA . 19987 1 479 . 1 1 44 44 GLU CG C 13 36.03 0.08 . 1 . . . A 44 GLU CG . 19987 1 480 . 1 1 44 44 GLU N N 15 124.1 0.1 . 1 . . . A 44 GLU N . 19987 1 481 . 1 1 45 45 ALA H H 1 8.501 0.04 . 1 . . . A 45 ALA H . 19987 1 482 . 1 1 45 45 ALA HA H 1 4.107 0.04 . 1 . . . A 45 ALA HA . 19987 1 483 . 1 1 45 45 ALA HB1 H 1 1.42 0.04 . 1 . . . A 45 ALA HB1 . 19987 1 484 . 1 1 45 45 ALA HB2 H 1 1.42 0.04 . 1 . . . A 45 ALA HB2 . 19987 1 485 . 1 1 45 45 ALA HB3 H 1 1.42 0.04 . 1 . . . A 45 ALA HB3 . 19987 1 486 . 1 1 45 45 ALA CA C 13 54.171 0.08 . 1 . . . A 45 ALA CA . 19987 1 487 . 1 1 45 45 ALA CB C 13 19.5 0.08 . 1 . . . A 45 ALA CB . 19987 1 488 . 1 1 45 45 ALA N N 15 129.098 0.1 . 1 . . . A 45 ALA N . 19987 1 489 . 1 1 46 46 SER H H 1 8.56 0.04 . 1 . . . A 46 SER H . 19987 1 490 . 1 1 46 46 SER HA H 1 4.61 0.04 . 1 . . . A 46 SER HA . 19987 1 491 . 1 1 46 46 SER HB2 H 1 4 0.04 . 2 . . . A 46 SER HB2 . 19987 1 492 . 1 1 46 46 SER HB3 H 1 4 0.04 . 2 . . . A 46 SER HB3 . 19987 1 493 . 1 1 46 46 SER CA C 13 56.3 0.08 . 1 . . . A 46 SER CA . 19987 1 494 . 1 1 46 46 SER CB C 13 63.29 0.08 . 1 . . . A 46 SER CB . 19987 1 495 . 1 1 46 46 SER N N 15 115.5 0.1 . 1 . . . A 46 SER N . 19987 1 496 . 1 1 47 47 GLN H H 1 9.158 0.04 . 1 . . . A 47 GLN H . 19987 1 497 . 1 1 47 47 GLN HA H 1 3.8 0.04 . 1 . . . A 47 GLN HA . 19987 1 498 . 1 1 47 47 GLN HB2 H 1 2.14 0.02 . 2 . . . A 47 GLN HB2 . 19987 1 499 . 1 1 47 47 GLN HB3 H 1 2.05 0.02 . 2 . . . A 47 GLN HB3 . 19987 1 500 . 1 1 47 47 GLN HG2 H 1 2.365 0.02 . 2 . . . A 47 GLN HG2 . 19987 1 501 . 1 1 47 47 GLN HG3 H 1 2.365 0.02 . 2 . . . A 47 GLN HG3 . 19987 1 502 . 1 1 47 47 GLN CA C 13 59.36 0.08 . 1 . . . A 47 GLN CA . 19987 1 503 . 1 1 47 47 GLN CB C 13 28.203 0.08 . 1 . . . A 47 GLN CB . 19987 1 504 . 1 1 47 47 GLN CG C 13 33.7 0.08 . 1 . . . A 47 GLN CG . 19987 1 505 . 1 1 47 47 GLN N N 15 133.5 0.1 . 1 . . . A 47 GLN N . 19987 1 506 . 1 1 48 48 LYS H H 1 8.15 0.04 . 1 . . . A 48 LYS H . 19987 1 507 . 1 1 48 48 LYS HA H 1 4.022 0.04 . 1 . . . A 48 LYS HA . 19987 1 508 . 1 1 48 48 LYS HB2 H 1 1.809 0.02 . 2 . . . A 48 LYS HB2 . 19987 1 509 . 1 1 48 48 LYS HB3 H 1 1.71 0.02 . 2 . . . A 48 LYS HB3 . 19987 1 510 . 1 1 48 48 LYS HG2 H 1 1.5 0.02 . 2 . . . A 48 LYS HG2 . 19987 1 511 . 1 1 48 48 LYS HG3 H 1 1.35 0.02 . 2 . . . A 48 LYS HG3 . 19987 1 512 . 1 1 48 48 LYS HD2 H 1 1.6 0.02 . 2 . . . A 48 LYS HD2 . 19987 1 513 . 1 1 48 48 LYS HD3 H 1 1.6 0.02 . 2 . . . A 48 LYS HD3 . 19987 1 514 . 1 1 48 48 LYS HE2 H 1 2.96 0.02 . 2 . . . A 48 LYS HE2 . 19987 1 515 . 1 1 48 48 LYS HE3 H 1 2.96 0.02 . 2 . . . A 48 LYS HE3 . 19987 1 516 . 1 1 48 48 LYS C C 13 181.969 0.08 . 1 . . . A 48 LYS C . 19987 1 517 . 1 1 48 48 LYS CA C 13 59.53 0.08 . 1 . . . A 48 LYS CA . 19987 1 518 . 1 1 48 48 LYS CB C 13 32.604 0.08 . 1 . . . A 48 LYS CB . 19987 1 519 . 1 1 48 48 LYS CG C 13 25.26 0.08 . 1 . . . A 48 LYS CG . 19987 1 520 . 1 1 48 48 LYS CD C 13 29 0.08 . 1 . . . A 48 LYS CD . 19987 1 521 . 1 1 48 48 LYS CE C 13 42.1 0.08 . 1 . . . A 48 LYS CE . 19987 1 522 . 1 1 48 48 LYS N N 15 121.01 0.1 . 1 . . . A 48 LYS N . 19987 1 523 . 1 1 49 49 VAL H H 1 7.258 0.04 . 1 . . . A 49 VAL H . 19987 1 524 . 1 1 49 49 VAL HA H 1 3.59 0.04 . 1 . . . A 49 VAL HA . 19987 1 525 . 1 1 49 49 VAL HB H 1 2.159 0.04 . 1 . . . A 49 VAL HB . 19987 1 526 . 1 1 49 49 VAL HG11 H 1 1.12 0.02 . 2 . . . A 49 VAL HG11 . 19987 1 527 . 1 1 49 49 VAL HG12 H 1 1.12 0.02 . 2 . . . A 49 VAL HG12 . 19987 1 528 . 1 1 49 49 VAL HG13 H 1 1.12 0.02 . 2 . . . A 49 VAL HG13 . 19987 1 529 . 1 1 49 49 VAL HG21 H 1 1 0.02 . 2 . . . A 49 VAL HG21 . 19987 1 530 . 1 1 49 49 VAL HG22 H 1 1 0.02 . 2 . . . A 49 VAL HG22 . 19987 1 531 . 1 1 49 49 VAL HG23 H 1 1 0.02 . 2 . . . A 49 VAL HG23 . 19987 1 532 . 1 1 49 49 VAL C C 13 179.395 0.08 . 1 . . . A 49 VAL C . 19987 1 533 . 1 1 49 49 VAL CA C 13 66.263 0.08 . 1 . . . A 49 VAL CA . 19987 1 534 . 1 1 49 49 VAL CB C 13 32.09 0.08 . 1 . . . A 49 VAL CB . 19987 1 535 . 1 1 49 49 VAL CG1 C 13 22.7 0.08 . 2 . . . A 49 VAL CG1 . 19987 1 536 . 1 1 49 49 VAL CG2 C 13 22 0.08 . 2 . . . A 49 VAL CG2 . 19987 1 537 . 1 1 49 49 VAL N N 15 123.8 0.1 . 1 . . . A 49 VAL N . 19987 1 538 . 1 1 50 50 ARG H H 1 8.489 0.04 . 1 . . . A 50 ARG H . 19987 1 539 . 1 1 50 50 ARG HA H 1 3.8 0.04 . 1 . . . A 50 ARG HA . 19987 1 540 . 1 1 50 50 ARG HB2 H 1 1.779 0.02 . 2 . . . A 50 ARG HB2 . 19987 1 541 . 1 1 50 50 ARG HB3 H 1 1.94 0.02 . 2 . . . A 50 ARG HB3 . 19987 1 542 . 1 1 50 50 ARG HG2 H 1 1.45 0.02 . 2 . . . A 50 ARG HG2 . 19987 1 543 . 1 1 50 50 ARG HG3 H 1 1.67 0.02 . 2 . . . A 50 ARG HG3 . 19987 1 544 . 1 1 50 50 ARG HD2 H 1 3.21 0.02 . 2 . . . A 50 ARG HD2 . 19987 1 545 . 1 1 50 50 ARG HD3 H 1 3.21 0.02 . 2 . . . A 50 ARG HD3 . 19987 1 546 . 1 1 50 50 ARG C C 13 180.319 0.08 . 1 . . . A 50 ARG C . 19987 1 547 . 1 1 50 50 ARG CA C 13 60.425 0.08 . 1 . . . A 50 ARG CA . 19987 1 548 . 1 1 50 50 ARG CB C 13 30.751 0.08 . 1 . . . A 50 ARG CB . 19987 1 549 . 1 1 50 50 ARG CG C 13 26.62 0.08 . 1 . . . A 50 ARG CG . 19987 1 550 . 1 1 50 50 ARG CD C 13 44.12 0.08 . 1 . . . A 50 ARG CD . 19987 1 551 . 1 1 50 50 ARG N N 15 123.299 0.1 . 1 . . . A 50 ARG N . 19987 1 552 . 1 1 51 51 ASN H H 1 8.283 0.04 . 1 . . . A 51 ASN H . 19987 1 553 . 1 1 51 51 ASN HA H 1 4.33 0.04 . 1 . . . A 51 ASN HA . 19987 1 554 . 1 1 51 51 ASN HB2 H 1 2.64 0.02 . 2 . . . A 51 ASN HB2 . 19987 1 555 . 1 1 51 51 ASN HB3 H 1 2.814 0.02 . 2 . . . A 51 ASN HB3 . 19987 1 556 . 1 1 51 51 ASN C C 13 180.704 0.08 . 1 . . . A 51 ASN C . 19987 1 557 . 1 1 51 51 ASN CA C 13 56.151 0.08 . 1 . . . A 51 ASN CA . 19987 1 558 . 1 1 51 51 ASN CB C 13 37.903 0.08 . 1 . . . A 51 ASN CB . 19987 1 559 . 1 1 51 51 ASN N N 15 117.4 0.1 . 1 . . . A 51 ASN N . 19987 1 560 . 1 1 52 52 LEU H H 1 7.55 0.04 . 1 . . . A 52 LEU H . 19987 1 561 . 1 1 52 52 LEU HA H 1 4.04 0.04 . 1 . . . A 52 LEU HA . 19987 1 562 . 1 1 52 52 LEU HB2 H 1 1.52 0.02 . 2 . . . A 52 LEU HB2 . 19987 1 563 . 1 1 52 52 LEU HB3 H 1 1.64 0.02 . 2 . . . A 52 LEU HB3 . 19987 1 564 . 1 1 52 52 LEU HG H 1 1.21 0.04 . 1 . . . A 52 LEU HG . 19987 1 565 . 1 1 52 52 LEU HD11 H 1 0.16 0.02 . 2 . . . A 52 LEU HD11 . 19987 1 566 . 1 1 52 52 LEU HD12 H 1 0.16 0.02 . 2 . . . A 52 LEU HD12 . 19987 1 567 . 1 1 52 52 LEU HD13 H 1 0.16 0.02 . 2 . . . A 52 LEU HD13 . 19987 1 568 . 1 1 52 52 LEU HD21 H 1 0.44 0.02 . 2 . . . A 52 LEU HD21 . 19987 1 569 . 1 1 52 52 LEU HD22 H 1 0.44 0.02 . 2 . . . A 52 LEU HD22 . 19987 1 570 . 1 1 52 52 LEU HD23 H 1 0.44 0.02 . 2 . . . A 52 LEU HD23 . 19987 1 571 . 1 1 52 52 LEU C C 13 181.214 0.08 . 1 . . . A 52 LEU C . 19987 1 572 . 1 1 52 52 LEU CA C 13 58.258 0.08 . 1 . . . A 52 LEU CA . 19987 1 573 . 1 1 52 52 LEU CB C 13 41.7 0.08 . 1 . . . A 52 LEU CB . 19987 1 574 . 1 1 52 52 LEU CG C 13 26.99 0.08 . 1 . . . A 52 LEU CG . 19987 1 575 . 1 1 52 52 LEU CD1 C 13 23.62 0.08 . 2 . . . A 52 LEU CD1 . 19987 1 576 . 1 1 52 52 LEU CD2 C 13 24.28 0.08 . 2 . . . A 52 LEU CD2 . 19987 1 577 . 1 1 52 52 LEU N N 15 125.806 0.1 . 1 . . . A 52 LEU N . 19987 1 578 . 1 1 53 53 LEU H H 1 8.36 0.04 . 1 . . . A 53 LEU H . 19987 1 579 . 1 1 53 53 LEU HA H 1 3.674 0.04 . 1 . . . A 53 LEU HA . 19987 1 580 . 1 1 53 53 LEU HB2 H 1 1.26 0.02 . 2 . . . A 53 LEU HB2 . 19987 1 581 . 1 1 53 53 LEU HB3 H 1 1.84 0.02 . 2 . . . A 53 LEU HB3 . 19987 1 582 . 1 1 53 53 LEU HG H 1 0.86 0.04 . 1 . . . A 53 LEU HG . 19987 1 583 . 1 1 53 53 LEU HD11 H 1 1 0.02 . 2 . . . A 53 LEU HD11 . 19987 1 584 . 1 1 53 53 LEU HD12 H 1 1 0.02 . 2 . . . A 53 LEU HD12 . 19987 1 585 . 1 1 53 53 LEU HD13 H 1 1 0.02 . 2 . . . A 53 LEU HD13 . 19987 1 586 . 1 1 53 53 LEU HD21 H 1 0.4 0.02 . 2 . . . A 53 LEU HD21 . 19987 1 587 . 1 1 53 53 LEU HD22 H 1 0.4 0.02 . 2 . . . A 53 LEU HD22 . 19987 1 588 . 1 1 53 53 LEU HD23 H 1 0.4 0.02 . 2 . . . A 53 LEU HD23 . 19987 1 589 . 1 1 53 53 LEU C C 13 181.637 0.08 . 1 . . . A 53 LEU C . 19987 1 590 . 1 1 53 53 LEU CA C 13 57.989 0.08 . 1 . . . A 53 LEU CA . 19987 1 591 . 1 1 53 53 LEU CB C 13 42.63 0.08 . 1 . . . A 53 LEU CB . 19987 1 592 . 1 1 53 53 LEU CG C 13 26.7 0.08 . 1 . . . A 53 LEU CG . 19987 1 593 . 1 1 53 53 LEU CD1 C 13 21.89 0.08 . 2 . . . A 53 LEU CD1 . 19987 1 594 . 1 1 53 53 LEU CD2 C 13 21.89 0.08 . 2 . . . A 53 LEU CD2 . 19987 1 595 . 1 1 53 53 LEU N N 15 122.7 0.1 . 1 . . . A 53 LEU N . 19987 1 596 . 1 1 54 54 LEU H H 1 8.605 0.04 . 1 . . . A 54 LEU H . 19987 1 597 . 1 1 54 54 LEU HA H 1 3.94 0.04 . 1 . . . A 54 LEU HA . 19987 1 598 . 1 1 54 54 LEU HB2 H 1 1.85 0.02 . 2 . . . A 54 LEU HB2 . 19987 1 599 . 1 1 54 54 LEU HB3 H 1 1.42 0.02 . 2 . . . A 54 LEU HB3 . 19987 1 600 . 1 1 54 54 LEU HG H 1 1.74 0.04 . 1 . . . A 54 LEU HG . 19987 1 601 . 1 1 54 54 LEU HD11 H 1 0.86 0.02 . 2 . . . A 54 LEU HD11 . 19987 1 602 . 1 1 54 54 LEU HD12 H 1 0.86 0.02 . 2 . . . A 54 LEU HD12 . 19987 1 603 . 1 1 54 54 LEU HD13 H 1 0.86 0.02 . 2 . . . A 54 LEU HD13 . 19987 1 604 . 1 1 54 54 LEU HD21 H 1 0.9 0.02 . 2 . . . A 54 LEU HD21 . 19987 1 605 . 1 1 54 54 LEU HD22 H 1 0.9 0.02 . 2 . . . A 54 LEU HD22 . 19987 1 606 . 1 1 54 54 LEU HD23 H 1 0.9 0.02 . 2 . . . A 54 LEU HD23 . 19987 1 607 . 1 1 54 54 LEU C C 13 182.157 0.08 . 1 . . . A 54 LEU C . 19987 1 608 . 1 1 54 54 LEU CA C 13 58.4 0.08 . 1 . . . A 54 LEU CA . 19987 1 609 . 1 1 54 54 LEU CB C 13 41.64 0.08 . 1 . . . A 54 LEU CB . 19987 1 610 . 1 1 54 54 LEU CG C 13 26.9 0.08 . 1 . . . A 54 LEU CG . 19987 1 611 . 1 1 54 54 LEU CD1 C 13 25.03 0.08 . 2 . . . A 54 LEU CD1 . 19987 1 612 . 1 1 54 54 LEU CD2 C 13 24.04 0.08 . 2 . . . A 54 LEU CD2 . 19987 1 613 . 1 1 54 54 LEU N N 15 123 0.1 . 1 . . . A 54 LEU N . 19987 1 614 . 1 1 55 55 HIS H H 1 7.785 0.04 . 1 . . . A 55 HIS H . 19987 1 615 . 1 1 55 55 HIS HA H 1 4.196 0.04 . 1 . . . A 55 HIS HA . 19987 1 616 . 1 1 55 55 HIS HB2 H 1 3.418 0.02 . 2 . . . A 55 HIS HB2 . 19987 1 617 . 1 1 55 55 HIS HB3 H 1 3.315 0.02 . 2 . . . A 55 HIS HB3 . 19987 1 618 . 1 1 55 55 HIS HD2 H 1 7.16 0.04 . 1 . . . A 55 HIS HD2 . 19987 1 619 . 1 1 55 55 HIS HE1 H 1 8 0.04 . 1 . . . A 55 HIS HE1 . 19987 1 620 . 1 1 55 55 HIS C C 13 180.151 0.08 . 1 . . . A 55 HIS C . 19987 1 621 . 1 1 55 55 HIS CA C 13 59.663 0.08 . 1 . . . A 55 HIS CA . 19987 1 622 . 1 1 55 55 HIS CB C 13 27.6 0.08 . 1 . . . A 55 HIS CB . 19987 1 623 . 1 1 55 55 HIS N N 15 120.612 0.1 . 1 . . . A 55 HIS N . 19987 1 624 . 1 1 56 56 LYS H H 1 8.33 0.04 . 1 . . . A 56 LYS H . 19987 1 625 . 1 1 56 56 LYS HA H 1 4.305 0.04 . 1 . . . A 56 LYS HA . 19987 1 626 . 1 1 56 56 LYS HB2 H 1 1.733 0.02 . 2 . . . A 56 LYS HB2 . 19987 1 627 . 1 1 56 56 LYS HB3 H 1 2.068 0.02 . 2 . . . A 56 LYS HB3 . 19987 1 628 . 1 1 56 56 LYS HG2 H 1 1.51 0.02 . 2 . . . A 56 LYS HG2 . 19987 1 629 . 1 1 56 56 LYS HG3 H 1 1.097 0.02 . 2 . . . A 56 LYS HG3 . 19987 1 630 . 1 1 56 56 LYS C C 13 181.205 0.08 . 1 . . . A 56 LYS C . 19987 1 631 . 1 1 56 56 LYS CA C 13 58.238 0.08 . 1 . . . A 56 LYS CA . 19987 1 632 . 1 1 56 56 LYS CB C 13 31.2 0.08 . 1 . . . A 56 LYS CB . 19987 1 633 . 1 1 56 56 LYS CG C 13 24.51 0.08 . 1 . . . A 56 LYS CG . 19987 1 634 . 1 1 56 56 LYS CD C 13 27.88 0.08 . 1 . . . A 56 LYS CD . 19987 1 635 . 1 1 56 56 LYS CE C 13 41.623 0.08 . 1 . . . A 56 LYS CE . 19987 1 636 . 1 1 56 56 LYS N N 15 122.107 0.1 . 1 . . . A 56 LYS N . 19987 1 637 . 1 1 57 57 GLY H H 1 8.868 0.04 . 1 . . . A 57 GLY H . 19987 1 638 . 1 1 57 57 GLY HA2 H 1 3.72 0.02 . 2 . . . A 57 GLY HA2 . 19987 1 639 . 1 1 57 57 GLY HA3 H 1 3.518 0.02 . 2 . . . A 57 GLY HA3 . 19987 1 640 . 1 1 57 57 GLY C C 13 176.4 0.08 . 1 . . . A 57 GLY C . 19987 1 641 . 1 1 57 57 GLY CA C 13 47.3 0.08 . 1 . . . A 57 GLY CA . 19987 1 642 . 1 1 57 57 GLY N N 15 109.3 0.1 . 1 . . . A 57 GLY N . 19987 1 643 . 1 1 58 58 LYS H H 1 8.021 0.04 . 1 . . . A 58 LYS H . 19987 1 644 . 1 1 58 58 LYS HA H 1 3.655 0.04 . 1 . . . A 58 LYS HA . 19987 1 645 . 1 1 58 58 LYS HB2 H 1 1.87 0.02 . 2 . . . A 58 LYS HB2 . 19987 1 646 . 1 1 58 58 LYS HB3 H 1 1.69 0.02 . 2 . . . A 58 LYS HB3 . 19987 1 647 . 1 1 58 58 LYS HG2 H 1 1.27 0.02 . 2 . . . A 58 LYS HG2 . 19987 1 648 . 1 1 58 58 LYS HG3 H 1 1.16 0.02 . 2 . . . A 58 LYS HG3 . 19987 1 649 . 1 1 58 58 LYS HD2 H 1 1.55 0.02 . 2 . . . A 58 LYS HD2 . 19987 1 650 . 1 1 58 58 LYS HD3 H 1 1.55 0.02 . 2 . . . A 58 LYS HD3 . 19987 1 651 . 1 1 58 58 LYS HE2 H 1 2.82 0.02 . 2 . . . A 58 LYS HE2 . 19987 1 652 . 1 1 58 58 LYS HE3 H 1 2.82 0.02 . 2 . . . A 58 LYS HE3 . 19987 1 653 . 1 1 58 58 LYS C C 13 180.159 0.08 . 1 . . . A 58 LYS C . 19987 1 654 . 1 1 58 58 LYS CA C 13 60.492 0.08 . 1 . . . A 58 LYS CA . 19987 1 655 . 1 1 58 58 LYS CB C 13 32.33 0.08 . 1 . . . A 58 LYS CB . 19987 1 656 . 1 1 58 58 LYS CG C 13 25.54 0.08 . 1 . . . A 58 LYS CG . 19987 1 657 . 1 1 58 58 LYS CD C 13 29.61 0.08 . 1 . . . A 58 LYS CD . 19987 1 658 . 1 1 58 58 LYS CE C 13 42.16 0.08 . 1 . . . A 58 LYS CE . 19987 1 659 . 1 1 58 58 LYS N N 15 123.3 0.1 . 1 . . . A 58 LYS N . 19987 1 660 . 1 1 59 59 GLU H H 1 8.04 0.04 . 1 . . . A 59 GLU H . 19987 1 661 . 1 1 59 59 GLU HA H 1 3.88 0.04 . 1 . . . A 59 GLU HA . 19987 1 662 . 1 1 59 59 GLU HB2 H 1 2.317 0.02 . 2 . . . A 59 GLU HB2 . 19987 1 663 . 1 1 59 59 GLU HB3 H 1 1.96 0.02 . 2 . . . A 59 GLU HB3 . 19987 1 664 . 1 1 59 59 GLU HG2 H 1 2.32 0.02 . 2 . . . A 59 GLU HG2 . 19987 1 665 . 1 1 59 59 GLU HG3 H 1 2.12 0.02 . 2 . . . A 59 GLU HG3 . 19987 1 666 . 1 1 59 59 GLU C C 13 182.277 0.08 . 1 . . . A 59 GLU C . 19987 1 667 . 1 1 59 59 GLU CA C 13 59.415 0.08 . 1 . . . A 59 GLU CA . 19987 1 668 . 1 1 59 59 GLU CB C 13 29.907 0.08 . 1 . . . A 59 GLU CB . 19987 1 669 . 1 1 59 59 GLU CG C 13 36.074 0.08 . 1 . . . A 59 GLU CG . 19987 1 670 . 1 1 59 59 GLU N N 15 120.785 0.1 . 1 . . . A 59 GLU N . 19987 1 671 . 1 1 60 60 VAL H H 1 7.43 0.04 . 1 . . . A 60 VAL H . 19987 1 672 . 1 1 60 60 VAL HA H 1 3.632 0.04 . 1 . . . A 60 VAL HA . 19987 1 673 . 1 1 60 60 VAL HB H 1 0.18 0.04 . 1 . . . A 60 VAL HB . 19987 1 674 . 1 1 60 60 VAL HG11 H 1 0.86 0.02 . 2 . . . A 60 VAL HG11 . 19987 1 675 . 1 1 60 60 VAL HG12 H 1 0.86 0.02 . 2 . . . A 60 VAL HG12 . 19987 1 676 . 1 1 60 60 VAL HG13 H 1 0.86 0.02 . 2 . . . A 60 VAL HG13 . 19987 1 677 . 1 1 60 60 VAL HG21 H 1 -0.01 0.02 . 2 . . . A 60 VAL HG21 . 19987 1 678 . 1 1 60 60 VAL HG22 H 1 -0.01 0.02 . 2 . . . A 60 VAL HG22 . 19987 1 679 . 1 1 60 60 VAL HG23 H 1 -0.01 0.02 . 2 . . . A 60 VAL HG23 . 19987 1 680 . 1 1 60 60 VAL C C 13 179.101 0.08 . 1 . . . A 60 VAL C . 19987 1 681 . 1 1 60 60 VAL CA C 13 63.873 0.08 . 1 . . . A 60 VAL CA . 19987 1 682 . 1 1 60 60 VAL CB C 13 29.99 0.08 . 1 . . . A 60 VAL CB . 19987 1 683 . 1 1 60 60 VAL CG1 C 13 22.03 0.08 . 2 . . . A 60 VAL CG1 . 19987 1 684 . 1 1 60 60 VAL CG2 C 13 19.5 0.08 . 2 . . . A 60 VAL CG2 . 19987 1 685 . 1 1 60 60 VAL N N 15 122.1 0.1 . 1 . . . A 60 VAL N . 19987 1 686 . 1 1 61 61 LEU H H 1 7.794 0.04 . 1 . . . A 61 LEU H . 19987 1 687 . 1 1 61 61 LEU HA H 1 4.01 0.04 . 1 . . . A 61 LEU HA . 19987 1 688 . 1 1 61 61 LEU HB2 H 1 1.792 0.02 . 2 . . . A 61 LEU HB2 . 19987 1 689 . 1 1 61 61 LEU HB3 H 1 1.06 0.02 . 2 . . . A 61 LEU HB3 . 19987 1 690 . 1 1 61 61 LEU HG H 1 1.75 0.04 . 1 . . . A 61 LEU HG . 19987 1 691 . 1 1 61 61 LEU HD11 H 1 0.56 0.02 . 2 . . . A 61 LEU HD11 . 19987 1 692 . 1 1 61 61 LEU HD12 H 1 0.56 0.02 . 2 . . . A 61 LEU HD12 . 19987 1 693 . 1 1 61 61 LEU HD13 H 1 0.56 0.02 . 2 . . . A 61 LEU HD13 . 19987 1 694 . 1 1 61 61 LEU HD21 H 1 0.892 0.02 . 2 . . . A 61 LEU HD21 . 19987 1 695 . 1 1 61 61 LEU HD22 H 1 0.892 0.02 . 2 . . . A 61 LEU HD22 . 19987 1 696 . 1 1 61 61 LEU HD23 H 1 0.892 0.02 . 2 . . . A 61 LEU HD23 . 19987 1 697 . 1 1 61 61 LEU C C 13 181.589 0.08 . 1 . . . A 61 LEU C . 19987 1 698 . 1 1 61 61 LEU CA C 13 58.074 0.08 . 1 . . . A 61 LEU CA . 19987 1 699 . 1 1 61 61 LEU CB C 13 41.15 0.08 . 1 . . . A 61 LEU CB . 19987 1 700 . 1 1 61 61 LEU CG C 13 27.18 0.08 . 1 . . . A 61 LEU CG . 19987 1 701 . 1 1 61 61 LEU CD1 C 13 26.24 0.08 . 2 . . . A 61 LEU CD1 . 19987 1 702 . 1 1 61 61 LEU CD2 C 13 23.39 0.08 . 2 . . . A 61 LEU CD2 . 19987 1 703 . 1 1 61 61 LEU N N 15 126.812 0.1 . 1 . . . A 61 LEU N . 19987 1 704 . 1 1 62 62 GLU H H 1 8.472 0.04 . 1 . . . A 62 GLU H . 19987 1 705 . 1 1 62 62 GLU HA H 1 3.818 0.04 . 1 . . . A 62 GLU HA . 19987 1 706 . 1 1 62 62 GLU HB2 H 1 1.973 0.02 . 2 . . . A 62 GLU HB2 . 19987 1 707 . 1 1 62 62 GLU HB3 H 1 1.761 0.02 . 2 . . . A 62 GLU HB3 . 19987 1 708 . 1 1 62 62 GLU HG2 H 1 2.34 0.02 . 2 . . . A 62 GLU HG2 . 19987 1 709 . 1 1 62 62 GLU HG3 H 1 1.98 0.02 . 2 . . . A 62 GLU HG3 . 19987 1 710 . 1 1 62 62 GLU CA C 13 59.75 0.08 . 1 . . . A 62 GLU CA . 19987 1 711 . 1 1 62 62 GLU CB C 13 28.7 0.08 . 1 . . . A 62 GLU CB . 19987 1 712 . 1 1 62 62 GLU CG C 13 37.2 0.08 . 1 . . . A 62 GLU CG . 19987 1 713 . 1 1 62 62 GLU N N 15 122.3 0.1 . 1 . . . A 62 GLU N . 19987 1 714 . 1 1 63 63 TRP H H 1 7.96 0.04 . 1 . . . A 63 TRP H . 19987 1 715 . 1 1 63 63 TRP HA H 1 3.85 0.04 . 1 . . . A 63 TRP HA . 19987 1 716 . 1 1 63 63 TRP HB2 H 1 2.97 0.02 . 2 . . . A 63 TRP HB2 . 19987 1 717 . 1 1 63 63 TRP HB3 H 1 3.21 0.02 . 2 . . . A 63 TRP HB3 . 19987 1 718 . 1 1 63 63 TRP HZ3 H 1 6.84 0.04 . 1 . . . A 63 TRP HZ3 . 19987 1 719 . 1 1 63 63 TRP HH2 H 1 7.06 0.04 . 1 . . . A 63 TRP HH2 . 19987 1 720 . 1 1 63 63 TRP CA C 13 62.401 0.08 . 1 . . . A 63 TRP CA . 19987 1 721 . 1 1 63 63 TRP CB C 13 28.312 0.08 . 1 . . . A 63 TRP CB . 19987 1 722 . 1 1 63 63 TRP N N 15 124.3 0.1 . 1 . . . A 63 TRP N . 19987 1 723 . 1 1 64 64 ALA H H 1 8.988 0.04 . 1 . . . A 64 ALA H . 19987 1 724 . 1 1 64 64 ALA HA H 1 3.492 0.04 . 1 . . . A 64 ALA HA . 19987 1 725 . 1 1 64 64 ALA HB1 H 1 1.47 0.04 . 1 . . . A 64 ALA HB1 . 19987 1 726 . 1 1 64 64 ALA HB2 H 1 1.47 0.04 . 1 . . . A 64 ALA HB2 . 19987 1 727 . 1 1 64 64 ALA HB3 H 1 1.47 0.04 . 1 . . . A 64 ALA HB3 . 19987 1 728 . 1 1 64 64 ALA CA C 13 54.81 0.08 . 1 . . . A 64 ALA CA . 19987 1 729 . 1 1 64 64 ALA CB C 13 17.58 0.08 . 1 . . . A 64 ALA CB . 19987 1 730 . 1 1 64 64 ALA N N 15 126.1 0.1 . 1 . . . A 64 ALA N . 19987 1 731 . 1 1 65 65 GLU H H 1 8.57 0.04 . 1 . . . A 65 GLU H . 19987 1 732 . 1 1 65 65 GLU HA H 1 3.699 0.04 . 1 . . . A 65 GLU HA . 19987 1 733 . 1 1 65 65 GLU HB2 H 1 1.95 0.02 . 2 . . . A 65 GLU HB2 . 19987 1 734 . 1 1 65 65 GLU HB3 H 1 2.16 0.02 . 2 . . . A 65 GLU HB3 . 19987 1 735 . 1 1 65 65 GLU HG2 H 1 1.99 0.02 . 2 . . . A 65 GLU HG2 . 19987 1 736 . 1 1 65 65 GLU HG3 H 1 2.17 0.02 . 2 . . . A 65 GLU HG3 . 19987 1 737 . 1 1 65 65 GLU CA C 13 59.51 0.08 . 1 . . . A 65 GLU CA . 19987 1 738 . 1 1 65 65 GLU CB C 13 28.4 0.08 . 1 . . . A 65 GLU CB . 19987 1 739 . 1 1 65 65 GLU CG C 13 33.6 0.08 . 1 . . . A 65 GLU CG . 19987 1 740 . 1 1 65 65 GLU N N 15 124.2 0.1 . 1 . . . A 65 GLU N . 19987 1 741 . 1 1 66 66 HIS H H 1 7.75 0.04 . 1 . . . A 66 HIS H . 19987 1 742 . 1 1 66 66 HIS HA H 1 4.45 0.04 . 1 . . . A 66 HIS HA . 19987 1 743 . 1 1 66 66 HIS HB2 H 1 3.06 0.02 . 2 . . . A 66 HIS HB2 . 19987 1 744 . 1 1 66 66 HIS HB3 H 1 3.04 0.02 . 2 . . . A 66 HIS HB3 . 19987 1 745 . 1 1 66 66 HIS HD2 H 1 7.19 0.04 . 1 . . . A 66 HIS HD2 . 19987 1 746 . 1 1 66 66 HIS HE1 H 1 7.94 0.04 . 1 . . . A 66 HIS HE1 . 19987 1 747 . 1 1 66 66 HIS CA C 13 57.877 0.08 . 1 . . . A 66 HIS CA . 19987 1 748 . 1 1 66 66 HIS CB C 13 27.35 0.08 . 1 . . . A 66 HIS CB . 19987 1 749 . 1 1 66 66 HIS N N 15 120 0.1 . 1 . . . A 66 HIS N . 19987 1 750 . 1 1 67 67 LEU H H 1 7.7 0.04 . 1 . . . A 67 LEU H . 19987 1 751 . 1 1 67 67 LEU HA H 1 3.864 0.04 . 1 . . . A 67 LEU HA . 19987 1 752 . 1 1 67 67 LEU HB2 H 1 1.48 0.02 . 2 . . . A 67 LEU HB2 . 19987 1 753 . 1 1 67 67 LEU HB3 H 1 0.29 0.02 . 2 . . . A 67 LEU HB3 . 19987 1 754 . 1 1 67 67 LEU HG H 1 1.39 0.04 . 1 . . . A 67 LEU HG . 19987 1 755 . 1 1 67 67 LEU HD11 H 1 0.72 0.02 . 2 . . . A 67 LEU HD11 . 19987 1 756 . 1 1 67 67 LEU HD12 H 1 0.72 0.02 . 2 . . . A 67 LEU HD12 . 19987 1 757 . 1 1 67 67 LEU HD13 H 1 0.72 0.02 . 2 . . . A 67 LEU HD13 . 19987 1 758 . 1 1 67 67 LEU HD21 H 1 0.52 0.02 . 2 . . . A 67 LEU HD21 . 19987 1 759 . 1 1 67 67 LEU HD22 H 1 0.52 0.02 . 2 . . . A 67 LEU HD22 . 19987 1 760 . 1 1 67 67 LEU HD23 H 1 0.52 0.02 . 2 . . . A 67 LEU HD23 . 19987 1 761 . 1 1 67 67 LEU C C 13 180.2 0.08 . 1 . . . A 67 LEU C . 19987 1 762 . 1 1 67 67 LEU CA C 13 57.939 0.08 . 1 . . . A 67 LEU CA . 19987 1 763 . 1 1 67 67 LEU CB C 13 40.43 0.08 . 1 . . . A 67 LEU CB . 19987 1 764 . 1 1 67 67 LEU CG C 13 26.57 0.08 . 1 . . . A 67 LEU CG . 19987 1 765 . 1 1 67 67 LEU CD1 C 13 26.42 0.08 . 2 . . . A 67 LEU CD1 . 19987 1 766 . 1 1 67 67 LEU CD2 C 13 22.36 0.08 . 2 . . . A 67 LEU CD2 . 19987 1 767 . 1 1 67 67 LEU N N 15 126.6 0.1 . 1 . . . A 67 LEU N . 19987 1 768 . 1 1 68 68 ALA H H 1 8.734 0.04 . 1 . . . A 68 ALA H . 19987 1 769 . 1 1 68 68 ALA HA H 1 3.762 0.04 . 1 . . . A 68 ALA HA . 19987 1 770 . 1 1 68 68 ALA HB1 H 1 1.41 0.04 . 1 . . . A 68 ALA HB1 . 19987 1 771 . 1 1 68 68 ALA HB2 H 1 1.41 0.04 . 1 . . . A 68 ALA HB2 . 19987 1 772 . 1 1 68 68 ALA HB3 H 1 1.41 0.04 . 1 . . . A 68 ALA HB3 . 19987 1 773 . 1 1 68 68 ALA C C 13 181.4 0.08 . 1 . . . A 68 ALA C . 19987 1 774 . 1 1 68 68 ALA CA C 13 55.43 0.08 . 1 . . . A 68 ALA CA . 19987 1 775 . 1 1 68 68 ALA CB C 13 18.01 0.08 . 1 . . . A 68 ALA CB . 19987 1 776 . 1 1 68 68 ALA N N 15 124.6 0.1 . 1 . . . A 68 ALA N . 19987 1 777 . 1 1 69 69 GLU H H 1 7.92 0.04 . 1 . . . A 69 GLU H . 19987 1 778 . 1 1 69 69 GLU HA H 1 3.833 0.04 . 1 . . . A 69 GLU HA . 19987 1 779 . 1 1 69 69 GLU HB2 H 1 2.16 0.02 . 2 . . . A 69 GLU HB2 . 19987 1 780 . 1 1 69 69 GLU HB3 H 1 1.97 0.02 . 2 . . . A 69 GLU HB3 . 19987 1 781 . 1 1 69 69 GLU HG2 H 1 2.44 0.02 . 2 . . . A 69 GLU HG2 . 19987 1 782 . 1 1 69 69 GLU HG3 H 1 2.28 0.02 . 2 . . . A 69 GLU HG3 . 19987 1 783 . 1 1 69 69 GLU C C 13 181.181 0.08 . 1 . . . A 69 GLU C . 19987 1 784 . 1 1 69 69 GLU CA C 13 59.27 0.08 . 1 . . . A 69 GLU CA . 19987 1 785 . 1 1 69 69 GLU CB C 13 29.3 0.08 . 1 . . . A 69 GLU CB . 19987 1 786 . 1 1 69 69 GLU CG C 13 35.3 0.08 . 1 . . . A 69 GLU CG . 19987 1 787 . 1 1 69 69 GLU N N 15 119 0.1 . 1 . . . A 69 GLU N . 19987 1 788 . 1 1 70 70 TRP H H 1 7.773 0.04 . 1 . . . A 70 TRP H . 19987 1 789 . 1 1 70 70 TRP HA H 1 3.975 0.04 . 1 . . . A 70 TRP HA . 19987 1 790 . 1 1 70 70 TRP HB2 H 1 3.18 0.02 . 2 . . . A 70 TRP HB2 . 19987 1 791 . 1 1 70 70 TRP HB3 H 1 3.47 0.02 . 2 . . . A 70 TRP HB3 . 19987 1 792 . 1 1 70 70 TRP HD1 H 1 7.17 0.04 . 1 . . . A 70 TRP HD1 . 19987 1 793 . 1 1 70 70 TRP HH2 H 1 7.05 0.04 . 1 . . . A 70 TRP HH2 . 19987 1 794 . 1 1 70 70 TRP C C 13 181.639 0.08 . 1 . . . A 70 TRP C . 19987 1 795 . 1 1 70 70 TRP CA C 13 62.791 0.08 . 1 . . . A 70 TRP CA . 19987 1 796 . 1 1 70 70 TRP CB C 13 28.8 0.08 . 1 . . . A 70 TRP CB . 19987 1 797 . 1 1 70 70 TRP N N 15 124.1 0.1 . 1 . . . A 70 TRP N . 19987 1 798 . 1 1 71 71 ILE H H 1 8.801 0.04 . 1 . . . A 71 ILE H . 19987 1 799 . 1 1 71 71 ILE HA H 1 2.998 0.04 . 1 . . . A 71 ILE HA . 19987 1 800 . 1 1 71 71 ILE HB H 1 1.86 0.04 . 1 . . . A 71 ILE HB . 19987 1 801 . 1 1 71 71 ILE HG12 H 1 0.75 0.02 . 2 . . . A 71 ILE HG12 . 19987 1 802 . 1 1 71 71 ILE HG13 H 1 1.923 0.02 . 2 . . . A 71 ILE HG13 . 19987 1 803 . 1 1 71 71 ILE HG21 H 1 0.52 0.02 . 1 . . . A 71 ILE HG21 . 19987 1 804 . 1 1 71 71 ILE HG22 H 1 0.52 0.02 . 1 . . . A 71 ILE HG22 . 19987 1 805 . 1 1 71 71 ILE HG23 H 1 0.52 0.02 . 1 . . . A 71 ILE HG23 . 19987 1 806 . 1 1 71 71 ILE HD11 H 1 0.65 0.02 . 1 . . . A 71 ILE HD11 . 19987 1 807 . 1 1 71 71 ILE HD12 H 1 0.65 0.02 . 1 . . . A 71 ILE HD12 . 19987 1 808 . 1 1 71 71 ILE HD13 H 1 0.65 0.02 . 1 . . . A 71 ILE HD13 . 19987 1 809 . 1 1 71 71 ILE C C 13 180.222 0.08 . 1 . . . A 71 ILE C . 19987 1 810 . 1 1 71 71 ILE CA C 13 65.591 0.08 . 1 . . . A 71 ILE CA . 19987 1 811 . 1 1 71 71 ILE CB C 13 37.852 0.08 . 1 . . . A 71 ILE CB . 19987 1 812 . 1 1 71 71 ILE CG1 C 13 29.24 0.08 . 1 . . . A 71 ILE CG1 . 19987 1 813 . 1 1 71 71 ILE CG2 C 13 16.88 0.08 . 1 . . . A 71 ILE CG2 . 19987 1 814 . 1 1 71 71 ILE CD1 C 13 14.12 0.08 . 1 . . . A 71 ILE CD1 . 19987 1 815 . 1 1 71 71 ILE N N 15 124.4 0.1 . 1 . . . A 71 ILE N . 19987 1 816 . 1 1 72 72 LEU H H 1 8.165 0.04 . 1 . . . A 72 LEU H . 19987 1 817 . 1 1 72 72 LEU HA H 1 3.83 0.04 . 1 . . . A 72 LEU HA . 19987 1 818 . 1 1 72 72 LEU HB2 H 1 1.707 0.02 . 2 . . . A 72 LEU HB2 . 19987 1 819 . 1 1 72 72 LEU HB3 H 1 1.39 0.02 . 2 . . . A 72 LEU HB3 . 19987 1 820 . 1 1 72 72 LEU HG H 1 1.63 0.04 . 1 . . . A 72 LEU HG . 19987 1 821 . 1 1 72 72 LEU HD11 H 1 0.75 0.02 . 2 . . . A 72 LEU HD11 . 19987 1 822 . 1 1 72 72 LEU HD12 H 1 0.75 0.02 . 2 . . . A 72 LEU HD12 . 19987 1 823 . 1 1 72 72 LEU HD13 H 1 0.75 0.02 . 2 . . . A 72 LEU HD13 . 19987 1 824 . 1 1 72 72 LEU HD21 H 1 0.75 0.02 . 2 . . . A 72 LEU HD21 . 19987 1 825 . 1 1 72 72 LEU HD22 H 1 0.75 0.02 . 2 . . . A 72 LEU HD22 . 19987 1 826 . 1 1 72 72 LEU HD23 H 1 0.75 0.02 . 2 . . . A 72 LEU HD23 . 19987 1 827 . 1 1 72 72 LEU C C 13 181.794 0.08 . 1 . . . A 72 LEU C . 19987 1 828 . 1 1 72 72 LEU CA C 13 58.092 0.08 . 1 . . . A 72 LEU CA . 19987 1 829 . 1 1 72 72 LEU CB C 13 41.64 0.08 . 1 . . . A 72 LEU CB . 19987 1 830 . 1 1 72 72 LEU CG C 13 26.99 0.08 . 1 . . . A 72 LEU CG . 19987 1 831 . 1 1 72 72 LEU CD1 C 13 24.89 0.08 . 2 . . . A 72 LEU CD1 . 19987 1 832 . 1 1 72 72 LEU CD2 C 13 23.53 0.08 . 2 . . . A 72 LEU CD2 . 19987 1 833 . 1 1 72 72 LEU N N 15 122.292 0.1 . 1 . . . A 72 LEU N . 19987 1 834 . 1 1 73 73 GLU H H 1 7.544 0.04 . 1 . . . A 73 GLU H . 19987 1 835 . 1 1 73 73 GLU HB2 H 1 1.75 0.02 . 2 . . . A 73 GLU HB2 . 19987 1 836 . 1 1 73 73 GLU HB3 H 1 1.62 0.02 . 2 . . . A 73 GLU HB3 . 19987 1 837 . 1 1 73 73 GLU C C 13 180.821 0.08 . 1 . . . A 73 GLU C . 19987 1 838 . 1 1 73 73 GLU CA C 13 58.263 0.08 . 1 . . . A 73 GLU CA . 19987 1 839 . 1 1 73 73 GLU CB C 13 29.1 0.08 . 1 . . . A 73 GLU CB . 19987 1 840 . 1 1 73 73 GLU CG C 13 35.3 0.08 . 1 . . . A 73 GLU CG . 19987 1 841 . 1 1 73 73 GLU N N 15 120 0.1 . 1 . . . A 73 GLU N . 19987 1 842 . 1 1 74 74 HIS H H 1 7.8 0.04 . 1 . . . A 74 HIS H . 19987 1 843 . 1 1 74 74 HIS HA H 1 4.02 0.04 . 1 . . . A 74 HIS HA . 19987 1 844 . 1 1 74 74 HIS CA C 13 55.53 0.08 . 1 . . . A 74 HIS CA . 19987 1 845 . 1 1 74 74 HIS N N 15 119 0.1 . 1 . . . A 74 HIS N . 19987 1 stop_ save_