data_4374 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4374 _Entry.Title ; Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-08-05 _Entry.Accession_date 1999-08-05 _Entry.Last_release_date 2002-04-08 _Entry.Original_release_date 2002-04-08 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details 'NMR spectroscopy using uniformly U-[15N] and U-[15N,13C] labeled samples' _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 X. Zao . . . 4374 2 B. Goergieva . . . 4374 3 Andrej Chabes . A. . 4374 4 Vladimir Domkin . V. . 4374 5 Hans Ippel . J.H. . 4374 6 Juergen Schleucher . J. . 4374 7 Sybren Wijmenga . S.S. . 4374 8 Lars Thelander . L. . 4374 9 R. Rothstein . . . 4374 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4374 coupling_constants 1 4374 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 389 4374 '15N chemical shifts' 96 4374 '1H chemical shifts' 641 4374 'coupling constants' 97 4374 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-04-08 1999-08-05 original author . 4374 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4374 _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 'Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Cell. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 20 _Citation.Journal_issue 23 _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 9076 _Citation.Page_last 9083 _Citation.Year 2000 _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 X. Zao . . . 4374 1 2 B. Goergieva . . . 4374 1 3 Andrej Chabes . A. . 4374 1 4 Vladimir Domkin . V. . 4374 1 5 Hans Ippel . J.H. . 4374 1 6 Juergen Schleucher . J. . 4374 1 7 Sybren Wijmenga . S.S. . 4374 1 8 Lars Thelander . L. . 4374 1 9 R. Rothstein . . . 4374 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'carbon chemical shift' 4374 1 'inhibitory complex' 4374 1 'large subunit, RNR1' 4374 1 'nitrogen chemical shift' 4374 1 'NMR assignment' 4374 1 'NMR spectroscopy' 4374 1 'proton chemical shift' 4374 1 'ribonucleotide reductase' 4374 1 'Sml1 protein' 4374 1 structure 4374 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_Sml1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_Sml1 _Assembly.Entry_ID 4374 _Assembly.ID 1 _Assembly.Name 'Sml1 protein' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 11834 _Assembly.Enzyme_commission_number . _Assembly.Details ; Sml1 consists of 104 amino acids and binds specifically to the large R1 subunit of yeast and mouse ribonucleotide reductase, and thereby inhibit complex formation between the large R1 and small R2 subunit of ribonucleotide-diphosphate reductase ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4374 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'Sml1 protein' 1 $Sml1 . . . native . . . . . 4374 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Sml1 abbreviation 4374 1 'Sml1 protein' system 4374 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Sml1 _Entity.Sf_category entity _Entity.Sf_framecode Sml1 _Entity.Entry_ID 4374 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Sml1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MQNSQDYFYAQNRCQQQQAP STLRTVTMAEFRRVPLPPMA EVPMLSTQNSMGSSASASAS SLEMWEKDLEERLNSIDHDM NNNKFGSGELKSMFNQGKVE EMDF ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 11834.19 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 DBJ GAA25391 . "K7_Sml1p [Saccharomyces cerevisiae Kyokai no. 7]" . . . . . 100.00 104 98.08 98.08 2.84e-67 . . . . 4374 1 2 no EMBL CAA86717 . "unknown [Saccharomyces cerevisiae]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 3 no EMBL CAY81764 . "Sml1p [Saccharomyces cerevisiae EC1118]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 4 no GB AAS56287 . "YML058W [Saccharomyces cerevisiae]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 5 no GB AHY76409 . "Sml1p [Saccharomyces cerevisiae YJM993]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 6 no GB AJP40654 . "Sml1p [Saccharomyces cerevisiae YJM1078]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 7 no GB AJS61834 . "Sml1p [Saccharomyces cerevisiae YJM189]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 8 no GB AJS62260 . "Sml1p [Saccharomyces cerevisiae YJM193]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 9 no REF NP_013653 . "ribonucleotide reductase inhibiting protein SML1 [Saccharomyces cerevisiae S288c]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 10 no SP Q04964 . "RecName: Full=Ribonucleotide reductase inhibitor protein SML1" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 11 no TPG DAA09840 . "TPA: ribonucleotide reductase inhibiting protein SML1 [Saccharomyces cerevisiae S288c]" . . . . . 100.00 104 100.00 100.00 5.13e-70 . . . . 4374 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Sml1 common 4374 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 4374 1 2 . GLN . 4374 1 3 . ASN . 4374 1 4 . SER . 4374 1 5 . GLN . 4374 1 6 . ASP . 4374 1 7 . TYR . 4374 1 8 . PHE . 4374 1 9 . TYR . 4374 1 10 . ALA . 4374 1 11 . GLN . 4374 1 12 . ASN . 4374 1 13 . ARG . 4374 1 14 . CYS . 4374 1 15 . GLN . 4374 1 16 . GLN . 4374 1 17 . GLN . 4374 1 18 . GLN . 4374 1 19 . ALA . 4374 1 20 . PRO . 4374 1 21 . SER . 4374 1 22 . THR . 4374 1 23 . LEU . 4374 1 24 . ARG . 4374 1 25 . THR . 4374 1 26 . VAL . 4374 1 27 . THR . 4374 1 28 . MET . 4374 1 29 . ALA . 4374 1 30 . GLU . 4374 1 31 . PHE . 4374 1 32 . ARG . 4374 1 33 . ARG . 4374 1 34 . VAL . 4374 1 35 . PRO . 4374 1 36 . LEU . 4374 1 37 . PRO . 4374 1 38 . PRO . 4374 1 39 . MET . 4374 1 40 . ALA . 4374 1 41 . GLU . 4374 1 42 . VAL . 4374 1 43 . PRO . 4374 1 44 . MET . 4374 1 45 . LEU . 4374 1 46 . SER . 4374 1 47 . THR . 4374 1 48 . GLN . 4374 1 49 . ASN . 4374 1 50 . SER . 4374 1 51 . MET . 4374 1 52 . GLY . 4374 1 53 . SER . 4374 1 54 . SER . 4374 1 55 . ALA . 4374 1 56 . SER . 4374 1 57 . ALA . 4374 1 58 . SER . 4374 1 59 . ALA . 4374 1 60 . SER . 4374 1 61 . SER . 4374 1 62 . LEU . 4374 1 63 . GLU . 4374 1 64 . MET . 4374 1 65 . TRP . 4374 1 66 . GLU . 4374 1 67 . LYS . 4374 1 68 . ASP . 4374 1 69 . LEU . 4374 1 70 . GLU . 4374 1 71 . GLU . 4374 1 72 . ARG . 4374 1 73 . LEU . 4374 1 74 . ASN . 4374 1 75 . SER . 4374 1 76 . ILE . 4374 1 77 . ASP . 4374 1 78 . HIS . 4374 1 79 . ASP . 4374 1 80 . MET . 4374 1 81 . ASN . 4374 1 82 . ASN . 4374 1 83 . ASN . 4374 1 84 . LYS . 4374 1 85 . PHE . 4374 1 86 . GLY . 4374 1 87 . SER . 4374 1 88 . GLY . 4374 1 89 . GLU . 4374 1 90 . LEU . 4374 1 91 . LYS . 4374 1 92 . SER . 4374 1 93 . MET . 4374 1 94 . PHE . 4374 1 95 . ASN . 4374 1 96 . GLN . 4374 1 97 . GLY . 4374 1 98 . LYS . 4374 1 99 . VAL . 4374 1 100 . GLU . 4374 1 101 . GLU . 4374 1 102 . MET . 4374 1 103 . ASP . 4374 1 104 . PHE . 4374 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 4374 1 . GLN 2 2 4374 1 . ASN 3 3 4374 1 . SER 4 4 4374 1 . GLN 5 5 4374 1 . ASP 6 6 4374 1 . TYR 7 7 4374 1 . PHE 8 8 4374 1 . TYR 9 9 4374 1 . ALA 10 10 4374 1 . GLN 11 11 4374 1 . ASN 12 12 4374 1 . ARG 13 13 4374 1 . CYS 14 14 4374 1 . GLN 15 15 4374 1 . GLN 16 16 4374 1 . GLN 17 17 4374 1 . GLN 18 18 4374 1 . ALA 19 19 4374 1 . PRO 20 20 4374 1 . SER 21 21 4374 1 . THR 22 22 4374 1 . LEU 23 23 4374 1 . ARG 24 24 4374 1 . THR 25 25 4374 1 . VAL 26 26 4374 1 . THR 27 27 4374 1 . MET 28 28 4374 1 . ALA 29 29 4374 1 . GLU 30 30 4374 1 . PHE 31 31 4374 1 . ARG 32 32 4374 1 . ARG 33 33 4374 1 . VAL 34 34 4374 1 . PRO 35 35 4374 1 . LEU 36 36 4374 1 . PRO 37 37 4374 1 . PRO 38 38 4374 1 . MET 39 39 4374 1 . ALA 40 40 4374 1 . GLU 41 41 4374 1 . VAL 42 42 4374 1 . PRO 43 43 4374 1 . MET 44 44 4374 1 . LEU 45 45 4374 1 . SER 46 46 4374 1 . THR 47 47 4374 1 . GLN 48 48 4374 1 . ASN 49 49 4374 1 . SER 50 50 4374 1 . MET 51 51 4374 1 . GLY 52 52 4374 1 . SER 53 53 4374 1 . SER 54 54 4374 1 . ALA 55 55 4374 1 . SER 56 56 4374 1 . ALA 57 57 4374 1 . SER 58 58 4374 1 . ALA 59 59 4374 1 . SER 60 60 4374 1 . SER 61 61 4374 1 . LEU 62 62 4374 1 . GLU 63 63 4374 1 . MET 64 64 4374 1 . TRP 65 65 4374 1 . GLU 66 66 4374 1 . LYS 67 67 4374 1 . ASP 68 68 4374 1 . LEU 69 69 4374 1 . GLU 70 70 4374 1 . GLU 71 71 4374 1 . ARG 72 72 4374 1 . LEU 73 73 4374 1 . ASN 74 74 4374 1 . SER 75 75 4374 1 . ILE 76 76 4374 1 . ASP 77 77 4374 1 . HIS 78 78 4374 1 . ASP 79 79 4374 1 . MET 80 80 4374 1 . ASN 81 81 4374 1 . ASN 82 82 4374 1 . ASN 83 83 4374 1 . LYS 84 84 4374 1 . PHE 85 85 4374 1 . GLY 86 86 4374 1 . SER 87 87 4374 1 . GLY 88 88 4374 1 . GLU 89 89 4374 1 . LEU 90 90 4374 1 . LYS 91 91 4374 1 . SER 92 92 4374 1 . MET 93 93 4374 1 . PHE 94 94 4374 1 . ASN 95 95 4374 1 . GLN 96 96 4374 1 . GLY 97 97 4374 1 . LYS 98 98 4374 1 . VAL 99 99 4374 1 . GLU 100 100 4374 1 . GLU 101 101 4374 1 . MET 102 102 4374 1 . ASP 103 103 4374 1 . PHE 104 104 4374 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 4374 _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 $Sml1 . 4932 organism . Saccharomyces yeast . . Eukaryota . . Saccharomyces cerevisiae . . . . . . . . . . . . . . . pET3a . . . . 4374 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 4374 _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 $Sml1 . 'recombinant technology' . yeast . . . . . . . . . . . . . . . . . . . . . . . . . . . 4374 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4374 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Sml1 protein in 90% H2O / 10% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Sml1 . . . 1 $Sml1 . . 0.6 . . mM . . . . 4374 1 2 H2O . . . . . . . 90 . . % . . . . 4374 1 3 D2O . . . . . . . 10 . . % . . . . 4374 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4374 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Sml1 protein in 90% H2O / 10% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Sml1 [U-15N] . . 1 $Sml1 . . 0.4 . . mM . . . . 4374 2 2 H2O . . . . . . . 90 . . % . . . . 4374 2 3 D2O . . . . . . . 10 . . % . . . . 4374 2 4 'sodium-phosphate buffer' . . . . . . . 25 . . mM . . . . 4374 2 5 NaCl . . . . . . . 25 . . mM . . . . 4374 2 6 Dithio-threitol . . . . . . . 10 . . mM . . . . 4374 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 4374 _Sample.ID 3 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Sml1 protein in 90% H2O / 10% D2O' _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Sml1 '[U-13C; U-15N]' . . 1 $Sml1 . . 0.6 . . mM . . . . 4374 3 2 H2O . . . . . . . 90 . . % . . . . 4374 3 3 D2O . . . . . . . 10 . . % . . . . 4374 3 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 4374 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; Typical sample conditions, as used for the [U-15N] sample of Sml1: 25 mM sodium-phosphate buffer (pH 6.9) 25 mM NaCl 10 mM Dithio-threitol (DTT) in 90% H2O / 10% D2O mixture Temperature range used for NMR studies is 2 to 23 degrees Celsius. Triple-resonance and 15N-edited NOESY 3D spectra, dedicated to assignment of resonances, were recorded at a temperature of 2 degrees Celsius. ; 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' 50 . mM 4374 1 pH 6.9 0.2 pH 4374 1 pressure 1 . bar 4374 1 temperature 275 2 K 4374 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 4374 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 4374 _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 unknown unknown . 0 'spectrometer information not available' . . 4374 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 4374 _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 . . . . . . . . . . . . . . . . . 1 $conditions_1 . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 4374 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 4374 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details ; Proton chemical shifts referenced directly to external DSS (concentration 10 mM) in D2O. Carbon and nitrogen chemical shifts are indirectly referenced to 0 ppm proton, based on the method by Wishart et al. Reference: Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR 6, 135-140 (1995). Note that the given indirectly referenced 13C and 15N chemical shifts are not corrected for temperature and pH, as recommended by the IUPAC-IUBMB-IUPAB Task Group. ; loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.000 external indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 4374 1 H 1 DSS 'methyl protons' . . . . ppm 0.000 external direct . 'external to the sample' . . 1 $entry_citation . . 1 $entry_citation 4374 1 N 15 DSS 'methyl protons' . . . . ppm 0.000 external indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 4374 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_chemical_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts _Assigned_chem_shift_list.Entry_ID 4374 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $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 ; # about the data. 1H, 13C, and 15N chemical shift assignments for the Sml1 protein. NMR experiments used for assignments (all recorded at 600 MHz, except stated otherwise): - triple resonance 3D spectra: HNCO, CTSL-HCANH (500 MHz), HNHA, CBCANH and CBCACONH - heteronuclear 2D spectra: 15N-1H HSQC and 13C-1H HSQC (500 MHz) - homonuclear spectra: 2D 1H-1H TOCSY (400 MHz) and 3D 15N-edited NOESY Backbone assigments (C,CA,CB,N,NH,HA) are virtually complete, except for residues Met1, Gln2, Tyr7, Tyr9, and Arg13 and residues followed by a proline. Sidechain assignments follow from a 3D 15N-edited NOESY spectrum and are mostly complete, except for proline resonances and amino protons of Asn and Gln residues. In the case of Met1 and Gln2, the increased solvent exchange prevent detection of their respective amide protons, and in doing so also preclude assignment of other resonances belonging to these residues. The one remaining cross peak in the 2D 15N-1H HSQC is ambiguously assigned to Arg13. Particularly resonances of Arg13, but also most resonances positioned between residue Asp6 and Arg13 are broad and have weak or missing cross peaks in the triple resonance spectra. The severe loss in peak intensity is probably caused by strong relaxation effects of resonances positioned in this part of the sequence. Amino signals of Asn and Gln residues could not be uniquely assigned, due to inefficient intraresidual NOE transfer between the amide proton and the amino protons. However the following amino peak positions (ppm) per residue have been resolved from a high resolution 15N-1H HSQC recorded for the [U-15N] labeled sample. Chemical shifts (ppm) are valid for a temperature of 2 degrees Celsius: Set Nr. 1H amino protons 15N amino Set 1. 7.801, 7.023 113.85 Set 2. 7.736, 7.035 113.41 Set 3. 7.700, 7.027 113.38 remark: weak intensity of crosspeaks Set 4. 7.604, 6.931 113.15 Set 5. 7.679, 6.973 113.11 Set 6. 7.707, (7.003 or 6.958) 113.05 Set 7. 7.763, (7.003 or 6.958) 113.04 Set 8. 7.677, 6.958 112.99 Set 9. 7.630, 6.947 112.98 Set 10. 7.692, 6.980 112.92 Set 11. 7.614, 6.958 112.88 Set 12. 7.628, 6.948 112.81 Set 13. 7.654, 6.92 112.73 Set 14. 7.578, 6.92 112.73 Set 15. 7.605, 6.937 112.69 Set 16. 7.485, 6.905 112.66 This accounts for 16 out of 17 expected resonance sets ( 8 Asn + 9 Gln) Absolute error limits of amino peak positions are estimated < 0.02 ppm in the 1H dimension and < 0.1 ppm in the 15N dimension. Aromatic proton resonances for the single Trp, four Phe, and two Tyr spin systems have been identified via a 2D 1H-1H TOCSY spectrum of an non-labeled Sml1 sample. Note that the Sml1 protein is highly unstructured, even at low temperature. As a result chemical shifts for the aromatic residues display a limited dispersion, in good agreement with published random coil chemical shift values. Reference random coil shifts: Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., & Sykes, B.D., "1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbour effects," J. Biomol. NMR 5, 67-81 (1995). Assignments of the aromatic protons are therefore based on analogy with known random coil chemical shifts determined for small peptides. Note that the TOCSY spectrum was recorded at higher temperature in comparison to the other spectra, so reported chemical shifts of aromatic base signals are only valid at a temperature of 23 degrees Celsius. 13C (and 1H) chemical shifts of given CD,CG, and CE sidechain carbons have been determined from a 2D 13C-1H HSQC, as many sidechain carbon shifts are invariant per residue type, and often overlap exactly into a well-defined crosspeak. The reported carbon (and proton) shifts correspond to the central position in the carbon dimension of the overlapping summed crosspeak. The coresponding error values in the table corresponds to the deviation or uncertainty of the position for an individual signal inside the broader distribution envelop of the overlapping crosspeak. The ambiguity code is set to 5 for these type of assignments. Assignment of the CA and HA proton of Pro37 follows from the presence of the remaining crosspeak in the 2D 13C-1H HSQC spectrum after assignment of all other HA-CA crosspeaks by means of CBCACONH and CBCANH triple-resonance spectra. The 2D 13C-1H HSQC is also used for accurate determination of 1H and 13C chemical shifts of CH2 and methyl resonances of the single Ile76 in the sequence. Proton and carbon shifts of methyl groups of Leu and Val residues are stereospecifically linked via the 2D 13C-1H HSQC spectrum and assigned via the carbon resonances, as the average carbon shift is very close to known random coil shifts determined for small peptides. However, the ambiguity code is here set to 2, because an absolute stereospecific assignment for Leu and Val methyl groups in unstructured peptides has not been determined as yet. Accurate chemical shifts for alpha, delta en gamma protons and carbons of the five prolines have also been extracted in this way, but delta resonances can not be assigned uniquely. Although the degenerate chemical shifts prevent listing of the chemical shifts in the final table, we give these chemical shifts below to make the list complete. Two different group of prolines can be distinguished based on the chemical shift dispersion of their respective delta resonances, and are denoted group I and II: Group I: HD2/HD3 3.80 and 3.61 (0.02) ppm CD 50.33 (0.2) ppm Group II: HD2/HD3 3.86 and 3.66 (0.02) ppm CD 50.84 (0.1) ppm Values given between brackets indicate the estimated error peak position in ppm. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4374 1 . . 2 $sample_2 . 4374 1 . . 3 $sample_3 . 4374 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 GLN C C 13 175.35 0.10 . 1 . . . . . . . . 4374 1 2 . 1 1 2 2 GLN CA C 13 55.72 0.10 . 1 . . . . . . . . 4374 1 3 . 1 1 2 2 GLN CB C 13 29.55 0.10 . 1 . . . . . . . . 4374 1 4 . 1 1 2 2 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 5 . 1 1 2 2 GLN HA H 1 4.36 0.03 . 1 . . . . . . . . 4374 1 6 . 1 1 3 3 ASN C C 13 175.50 0.10 . 1 . . . . . . . . 4374 1 7 . 1 1 3 3 ASN CA C 13 53.05 0.10 . 1 . . . . . . . . 4374 1 8 . 1 1 3 3 ASN CB C 13 38.79 0.10 . 1 . . . . . . . . 4374 1 9 . 1 1 3 3 ASN HA H 1 4.70 0.03 . 1 . . . . . . . . 4374 1 10 . 1 1 3 3 ASN HB2 H 1 2.80 0.03 . 1 . . . . . . . . 4374 1 11 . 1 1 3 3 ASN HB3 H 1 2.80 0.03 . 1 . . . . . . . . 4374 1 12 . 1 1 3 3 ASN H H 1 8.83 0.01 . 1 . . . . . . . . 4374 1 13 . 1 1 3 3 ASN N N 15 121.21 0.10 . 1 . . . . . . . . 4374 1 14 . 1 1 4 4 SER C C 13 175.05 0.10 . 1 . . . . . . . . 4374 1 15 . 1 1 4 4 SER CA C 13 59.08 0.10 . 1 . . . . . . . . 4374 1 16 . 1 1 4 4 SER CB C 13 63.49 0.10 . 1 . . . . . . . . 4374 1 17 . 1 1 4 4 SER HA H 1 4.33 0.03 . 1 . . . . . . . . 4374 1 18 . 1 1 4 4 SER HB2 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 19 . 1 1 4 4 SER HB3 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 20 . 1 1 4 4 SER H H 1 8.56 0.01 . 1 . . . . . . . . 4374 1 21 . 1 1 4 4 SER N N 15 116.82 0.10 . 1 . . . . . . . . 4374 1 22 . 1 1 5 5 GLN C C 13 176.00 0.10 . 1 . . . . . . . . 4374 1 23 . 1 1 5 5 GLN CA C 13 56.58 0.10 . 1 . . . . . . . . 4374 1 24 . 1 1 5 5 GLN CB C 13 28.89 0.10 . 1 . . . . . . . . 4374 1 25 . 1 1 5 5 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 26 . 1 1 5 5 GLN HA H 1 4.27 0.03 . 1 . . . . . . . . 4374 1 27 . 1 1 5 5 GLN HB2 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 28 . 1 1 5 5 GLN HB3 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 29 . 1 1 5 5 GLN HG2 H 1 2.29 0.03 . 1 . . . . . . . . 4374 1 30 . 1 1 5 5 GLN HG3 H 1 2.29 0.03 . 1 . . . . . . . . 4374 1 31 . 1 1 5 5 GLN H H 1 8.59 0.01 . 1 . . . . . . . . 4374 1 32 . 1 1 5 5 GLN N N 15 121.62 0.10 . 1 . . . . . . . . 4374 1 33 . 1 1 6 6 ASP C C 13 176.84 0.10 . 1 . . . . . . . . 4374 1 34 . 1 1 6 6 ASP CA C 13 54.96 0.10 . 1 . . . . . . . . 4374 1 35 . 1 1 6 6 ASP CB C 13 40.78 0.10 . 1 . . . . . . . . 4374 1 36 . 1 1 6 6 ASP HA H 1 4.53 0.03 . 1 . . . . . . . . 4374 1 37 . 1 1 6 6 ASP HB2 H 1 2.60 0.03 . 1 . . . . . . . . 4374 1 38 . 1 1 6 6 ASP HB3 H 1 2.60 0.03 . 1 . . . . . . . . 4374 1 39 . 1 1 6 6 ASP H H 1 8.25 0.01 . 1 . . . . . . . . 4374 1 40 . 1 1 6 6 ASP N N 15 120.52 0.10 . 1 . . . . . . . . 4374 1 41 . 1 1 7 7 TYR C C 13 177.72 0.10 . 1 . . . . . . . . 4374 1 42 . 1 1 7 7 TYR CA C 13 57.23 0.10 . 1 . . . . . . . . 4374 1 43 . 1 1 7 7 TYR HA H 1 4.34 0.03 . 1 . . . . . . . . 4374 1 44 . 1 1 7 7 TYR HB2 H 1 2.89 0.03 . 1 . . . . . . . . 4374 1 45 . 1 1 7 7 TYR HB3 H 1 2.89 0.03 . 1 . . . . . . . . 4374 1 46 . 1 1 7 7 TYR HD1 H 1 6.94 0.03 . 1 . . . . . . . . 4374 1 47 . 1 1 7 7 TYR HD2 H 1 6.94 0.02 . 1 . . . . . . . . 4374 1 48 . 1 1 7 7 TYR HE1 H 1 6.77 0.02 . 1 . . . . . . . . 4374 1 49 . 1 1 7 7 TYR HE2 H 1 6.77 0.02 . 1 . . . . . . . . 4374 1 50 . 1 1 7 7 TYR H H 1 8.10 0.01 . 1 . . . . . . . . 4374 1 51 . 1 1 7 7 TYR N N 15 120.92 0.10 . 1 . . . . . . . . 4374 1 52 . 1 1 8 8 PHE C C 13 176.90 0.10 . 1 . . . . . . . . 4374 1 53 . 1 1 8 8 PHE CA C 13 57.81 0.10 . 1 . . . . . . . . 4374 1 54 . 1 1 8 8 PHE CB C 13 39.43 0.10 . 1 . . . . . . . . 4374 1 55 . 1 1 8 8 PHE HA H 1 4.29 0.03 . 1 . . . . . . . . 4374 1 56 . 1 1 8 8 PHE HB2 H 1 2.99 0.03 . 1 . . . . . . . . 4374 1 57 . 1 1 8 8 PHE HB3 H 1 2.99 0.03 . 1 . . . . . . . . 4374 1 58 . 1 1 8 8 PHE HD1 H 1 7.27 0.03 . 1 . . . . . . . . 4374 1 59 . 1 1 8 8 PHE HD2 H 1 7.27 0.02 . 1 . . . . . . . . 4374 1 60 . 1 1 8 8 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 61 . 1 1 8 8 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 62 . 1 1 8 8 PHE H H 1 8.33 0.01 . 1 . . . . . . . . 4374 1 63 . 1 1 8 8 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 64 . 1 1 8 8 PHE N N 15 120.01 0.10 . 1 . . . . . . . . 4374 1 65 . 1 1 9 9 TYR C C 13 174.08 0.10 . 1 . . . . . . . . 4374 1 66 . 1 1 9 9 TYR CA C 13 59.02 0.10 . 1 . . . . . . . . 4374 1 67 . 1 1 9 9 TYR HA H 1 4.35 0.03 . 1 . . . . . . . . 4374 1 68 . 1 1 9 9 TYR HB2 H 1 2.97 0.03 . 1 . . . . . . . . 4374 1 69 . 1 1 9 9 TYR HB3 H 1 2.97 0.03 . 1 . . . . . . . . 4374 1 70 . 1 1 9 9 TYR HD1 H 1 7.15 0.03 . 1 . . . . . . . . 4374 1 71 . 1 1 9 9 TYR HD2 H 1 7.15 0.02 . 1 . . . . . . . . 4374 1 72 . 1 1 9 9 TYR HE1 H 1 6.86 0.02 . 1 . . . . . . . . 4374 1 73 . 1 1 9 9 TYR HE2 H 1 6.86 0.02 . 1 . . . . . . . . 4374 1 74 . 1 1 9 9 TYR H H 1 8.04 0.01 . 1 . . . . . . . . 4374 1 75 . 1 1 9 9 TYR N N 15 120.69 0.10 . 1 . . . . . . . . 4374 1 76 . 1 1 10 10 ALA C C 13 178.25 0.10 . 1 . . . . . . . . 4374 1 77 . 1 1 10 10 ALA CA C 13 52.97 0.10 . 1 . . . . . . . . 4374 1 78 . 1 1 10 10 ALA CB C 13 18.90 0.10 . 1 . . . . . . . . 4374 1 79 . 1 1 10 10 ALA HA H 1 4.12 0.03 . 1 . . . . . . . . 4374 1 80 . 1 1 10 10 ALA HB1 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 81 . 1 1 10 10 ALA HB2 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 82 . 1 1 10 10 ALA HB3 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 83 . 1 1 10 10 ALA H H 1 8.10 0.01 . 1 . . . . . . . . 4374 1 84 . 1 1 10 10 ALA N N 15 124.00 0.10 . 1 . . . . . . . . 4374 1 85 . 1 1 11 11 GLN C C 13 176.30 0.10 . 1 . . . . . . . . 4374 1 86 . 1 1 11 11 GLN CA C 13 56.30 0.10 . 1 . . . . . . . . 4374 1 87 . 1 1 11 11 GLN CB C 13 28.99 0.10 . 1 . . . . . . . . 4374 1 88 . 1 1 11 11 GLN CG C 13 33.60 0.50 . 5 . . . . . . . . 4374 1 89 . 1 1 11 11 GLN HA H 1 4.13 0.03 . 1 . . . . . . . . 4374 1 90 . 1 1 11 11 GLN HB2 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 91 . 1 1 11 11 GLN HB3 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 92 . 1 1 11 11 GLN HG2 H 1 2.26 0.03 . 1 . . . . . . . . 4374 1 93 . 1 1 11 11 GLN HG3 H 1 2.26 0.03 . 1 . . . . . . . . 4374 1 94 . 1 1 11 11 GLN H H 1 8.18 0.01 . 1 . . . . . . . . 4374 1 95 . 1 1 11 11 GLN N N 15 118.19 0.10 . 1 . . . . . . . . 4374 1 96 . 1 1 12 12 ASN CA C 13 53.58 0.10 . 1 . . . . . . . . 4374 1 97 . 1 1 12 12 ASN CB C 13 38.65 0.10 . 1 . . . . . . . . 4374 1 98 . 1 1 12 12 ASN HA H 1 4.60 0.03 . 1 . . . . . . . . 4374 1 99 . 1 1 12 12 ASN HB2 H 1 2.75 0.03 . 1 . . . . . . . . 4374 1 100 . 1 1 12 12 ASN HB3 H 1 2.75 0.03 . 1 . . . . . . . . 4374 1 101 . 1 1 12 12 ASN H H 1 8.30 0.01 . 1 . . . . . . . . 4374 1 102 . 1 1 12 12 ASN N N 15 118.36 0.10 . 1 . . . . . . . . 4374 1 103 . 1 1 13 13 ARG C C 13 176.54 0.10 . 1 . . . . . . . . 4374 1 104 . 1 1 13 13 ARG HA H 1 4.32 0.03 . 1 . . . . . . . . 4374 1 105 . 1 1 13 13 ARG CA C 13 56.60 0.30 . 1 . . . . . . . . 4374 1 106 . 1 1 14 14 CYS C C 13 174.96 0.10 . 1 . . . . . . . . 4374 1 107 . 1 1 14 14 CYS CA C 13 59.00 0.10 . 1 . . . . . . . . 4374 1 108 . 1 1 14 14 CYS CB C 13 27.71 0.10 . 1 . . . . . . . . 4374 1 109 . 1 1 14 14 CYS HA H 1 4.40 0.03 . 1 . . . . . . . . 4374 1 110 . 1 1 14 14 CYS HB2 H 1 2.92 0.03 . 1 . . . . . . . . 4374 1 111 . 1 1 14 14 CYS HB3 H 1 2.92 0.03 . 1 . . . . . . . . 4374 1 112 . 1 1 14 14 CYS H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 113 . 1 1 14 14 CYS N N 15 119.42 0.10 . 1 . . . . . . . . 4374 1 114 . 1 1 15 15 GLN C C 13 176.13 0.10 . 1 . . . . . . . . 4374 1 115 . 1 1 15 15 GLN CA C 13 56.04 0.10 . 1 . . . . . . . . 4374 1 116 . 1 1 15 15 GLN CB C 13 29.15 0.10 . 1 . . . . . . . . 4374 1 117 . 1 1 15 15 GLN CG C 13 33.66 0.50 . 1 . . . . . . . . 4374 1 118 . 1 1 15 15 GLN HA H 1 4.27 0.03 . 1 . . . . . . . . 4374 1 119 . 1 1 15 15 GLN HB2 H 1 1.96 0.03 . 1 . . . . . . . . 4374 1 120 . 1 1 15 15 GLN HB3 H 1 1.96 0.03 . 1 . . . . . . . . 4374 1 121 . 1 1 15 15 GLN HG2 H 1 2.35 0.03 . 1 . . . . . . . . 4374 1 122 . 1 1 15 15 GLN HG3 H 1 2.35 0.03 . 1 . . . . . . . . 4374 1 123 . 1 1 15 15 GLN H H 1 8.49 0.01 . 1 . . . . . . . . 4374 1 124 . 1 1 15 15 GLN N N 15 122.24 0.10 . 1 . . . . . . . . 4374 1 125 . 1 1 16 16 GLN C C 13 175.86 0.10 . 1 . . . . . . . . 4374 1 126 . 1 1 16 16 GLN CA C 13 55.88 0.10 . 1 . . . . . . . . 4374 1 127 . 1 1 16 16 GLN CB C 13 29.38 0.10 . 1 . . . . . . . . 4374 1 128 . 1 1 16 16 GLN CG C 13 33.66 0.50 . 1 . . . . . . . . 4374 1 129 . 1 1 16 16 GLN HA H 1 4.26 0.03 . 1 . . . . . . . . 4374 1 130 . 1 1 16 16 GLN HB2 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 131 . 1 1 16 16 GLN HB3 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 132 . 1 1 16 16 GLN HG2 H 1 2.35 0.03 . 1 . . . . . . . . 4374 1 133 . 1 1 16 16 GLN HG3 H 1 2.35 0.03 . 1 . . . . . . . . 4374 1 134 . 1 1 16 16 GLN H H 1 8.46 0.01 . 1 . . . . . . . . 4374 1 135 . 1 1 16 16 GLN N N 15 121.28 0.10 . 1 . . . . . . . . 4374 1 136 . 1 1 17 17 GLN C C 13 175.86 0.10 . 5 . . . . . . . . 4374 1 137 . 1 1 17 17 GLN CA C 13 55.38 0.10 . 5 . . . . . . . . 4374 1 138 . 1 1 17 17 GLN CB C 13 29.60 0.10 . 5 . . . . . . . . 4374 1 139 . 1 1 17 17 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 140 . 1 1 17 17 GLN HA H 1 4.29 0.03 . 5 . . . . . . . . 4374 1 141 . 1 1 17 17 GLN HB2 H 1 2.05 0.03 . 5 . . . . . . . . 4374 1 142 . 1 1 17 17 GLN HB3 H 1 2.05 0.03 . 5 . . . . . . . . 4374 1 143 . 1 1 17 17 GLN HG2 H 1 2.35 0.03 . 5 . . . . . . . . 4374 1 144 . 1 1 17 17 GLN HG3 H 1 2.35 0.03 . 5 . . . . . . . . 4374 1 145 . 1 1 17 17 GLN H H 1 8.51 0.01 . 5 . . . . . . . . 4374 1 146 . 1 1 17 17 GLN N N 15 121.84 0.10 . 5 . . . . . . . . 4374 1 147 . 1 1 18 18 GLN C C 13 175.36 0.10 . 5 . . . . . . . . 4374 1 148 . 1 1 18 18 GLN CA C 13 55.38 0.10 . 5 . . . . . . . . 4374 1 149 . 1 1 18 18 GLN CB C 13 29.60 0.10 . 5 . . . . . . . . 4374 1 150 . 1 1 18 18 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 151 . 1 1 18 18 GLN HA H 1 4.29 0.03 . 5 . . . . . . . . 4374 1 152 . 1 1 18 18 GLN HB2 H 1 2.05 0.03 . 5 . . . . . . . . 4374 1 153 . 1 1 18 18 GLN HB3 H 1 2.05 0.03 . 5 . . . . . . . . 4374 1 154 . 1 1 18 18 GLN HG2 H 1 2.35 0.03 . 5 . . . . . . . . 4374 1 155 . 1 1 18 18 GLN HG3 H 1 2.35 0.03 . 5 . . . . . . . . 4374 1 156 . 1 1 18 18 GLN H H 1 8.51 0.01 . 5 . . . . . . . . 4374 1 157 . 1 1 18 18 GLN N N 15 121.84 0.10 . 5 . . . . . . . . 4374 1 158 . 1 1 19 19 ALA CA C 13 50.57 0.10 . 1 . . . . . . . . 4374 1 159 . 1 1 19 19 ALA CB C 13 18.03 0.10 . 1 . . . . . . . . 4374 1 160 . 1 1 19 19 ALA HA H 1 4.54 0.03 . 1 . . . . . . . . 4374 1 161 . 1 1 19 19 ALA HB1 H 1 1.35 0.03 . 1 . . . . . . . . 4374 1 162 . 1 1 19 19 ALA HB2 H 1 1.35 0.03 . 1 . . . . . . . . 4374 1 163 . 1 1 19 19 ALA HB3 H 1 1.35 0.03 . 1 . . . . . . . . 4374 1 164 . 1 1 19 19 ALA H H 1 8.55 0.01 . 1 . . . . . . . . 4374 1 165 . 1 1 19 19 ALA N N 15 127.13 0.10 . 1 . . . . . . . . 4374 1 166 . 1 1 20 20 PRO C C 13 177.10 0.10 . 1 . . . . . . . . 4374 1 167 . 1 1 20 20 PRO CA C 13 63.06 0.10 . 1 . . . . . . . . 4374 1 168 . 1 1 20 20 PRO CB C 13 31.98 0.10 . 1 . . . . . . . . 4374 1 169 . 1 1 20 20 PRO CG C 13 27.33 0.40 . 5 . . . . . . . . 4374 1 170 . 1 1 20 20 PRO HA H 1 4.42 0.03 . 5 . . . . . . . . 4374 1 171 . 1 1 20 20 PRO HG2 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 172 . 1 1 20 20 PRO HG3 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 173 . 1 1 21 21 SER C C 13 175.15 0.10 . 1 . . . . . . . . 4374 1 174 . 1 1 21 21 SER CA C 13 58.40 0.10 . 1 . . . . . . . . 4374 1 175 . 1 1 21 21 SER CB C 13 63.56 0.10 . 1 . . . . . . . . 4374 1 176 . 1 1 21 21 SER HA H 1 4.43 0.03 . 1 . . . . . . . . 4374 1 177 . 1 1 21 21 SER HB2 H 1 3.86 0.03 . 1 . . . . . . . . 4374 1 178 . 1 1 21 21 SER HB3 H 1 3.86 0.03 . 1 . . . . . . . . 4374 1 179 . 1 1 21 21 SER H H 1 8.60 0.01 . 1 . . . . . . . . 4374 1 180 . 1 1 21 21 SER N N 15 115.98 0.10 . 1 . . . . . . . . 4374 1 181 . 1 1 22 22 THR C C 13 174.51 0.10 . 1 . . . . . . . . 4374 1 182 . 1 1 22 22 THR CA C 13 61.94 0.10 . 1 . . . . . . . . 4374 1 183 . 1 1 22 22 THR CB C 13 69.48 0.10 . 1 . . . . . . . . 4374 1 184 . 1 1 22 22 THR CG2 C 13 21.61 0.30 . 5 . . . . . . . . 4374 1 185 . 1 1 22 22 THR HA H 1 4.30 0.03 . 1 . . . . . . . . 4374 1 186 . 1 1 22 22 THR HB H 1 4.28 0.03 . 1 . . . . . . . . 4374 1 187 . 1 1 22 22 THR HG21 H 1 1.21 0.03 . 1 . . . . . . . . 4374 1 188 . 1 1 22 22 THR HG22 H 1 1.21 0.03 . 1 . . . . . . . . 4374 1 189 . 1 1 22 22 THR HG23 H 1 1.21 0.03 . 1 . . . . . . . . 4374 1 190 . 1 1 22 22 THR H H 1 8.29 0.01 . 1 . . . . . . . . 4374 1 191 . 1 1 22 22 THR N N 15 116.16 0.10 . 1 . . . . . . . . 4374 1 192 . 1 1 23 23 LEU C C 13 177.26 0.10 . 1 . . . . . . . . 4374 1 193 . 1 1 23 23 LEU CA C 13 55.16 0.10 . 1 . . . . . . . . 4374 1 194 . 1 1 23 23 LEU CB C 13 42.14 0.10 . 1 . . . . . . . . 4374 1 195 . 1 1 23 23 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 196 . 1 1 23 23 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 197 . 1 1 23 23 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 198 . 1 1 23 23 LEU HA H 1 4.32 0.03 . 1 . . . . . . . . 4374 1 199 . 1 1 23 23 LEU HB2 H 1 1.60 0.03 . 1 . . . . . . . . 4374 1 200 . 1 1 23 23 LEU HB3 H 1 1.60 0.03 . 1 . . . . . . . . 4374 1 201 . 1 1 23 23 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 202 . 1 1 23 23 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 203 . 1 1 23 23 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 204 . 1 1 23 23 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 205 . 1 1 23 23 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 206 . 1 1 23 23 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 207 . 1 1 23 23 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 208 . 1 1 23 23 LEU H H 1 8.24 0.01 . 1 . . . . . . . . 4374 1 209 . 1 1 23 23 LEU N N 15 124.31 0.10 . 1 . . . . . . . . 4374 1 210 . 1 1 24 24 ARG C C 13 176.37 0.10 . 1 . . . . . . . . 4374 1 211 . 1 1 24 24 ARG CA C 13 55.86 0.10 . 1 . . . . . . . . 4374 1 212 . 1 1 24 24 ARG CB C 13 30.71 0.10 . 1 . . . . . . . . 4374 1 213 . 1 1 24 24 ARG CD C 13 43.20 0.20 . 5 . . . . . . . . 4374 1 214 . 1 1 24 24 ARG CG C 13 27.00 0.40 . 5 . . . . . . . . 4374 1 215 . 1 1 24 24 ARG HA H 1 4.38 0.03 . 1 . . . . . . . . 4374 1 216 . 1 1 24 24 ARG HB2 H 1 1.80 0.03 . 1 . . . . . . . . 4374 1 217 . 1 1 24 24 ARG HB3 H 1 1.80 0.03 . 1 . . . . . . . . 4374 1 218 . 1 1 24 24 ARG HD2 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 219 . 1 1 24 24 ARG HD3 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 220 . 1 1 24 24 ARG HG2 H 1 1.59 0.03 . 1 . . . . . . . . 4374 1 221 . 1 1 24 24 ARG HG3 H 1 1.59 0.03 . 1 . . . . . . . . 4374 1 222 . 1 1 24 24 ARG H H 1 8.43 0.01 . 1 . . . . . . . . 4374 1 223 . 1 1 24 24 ARG N N 15 122.50 0.10 . 1 . . . . . . . . 4374 1 224 . 1 1 25 25 THR C C 13 174.60 0.10 . 1 . . . . . . . . 4374 1 225 . 1 1 25 25 THR CA C 13 62.02 0.10 . 1 . . . . . . . . 4374 1 226 . 1 1 25 25 THR CB C 13 69.64 0.10 . 1 . . . . . . . . 4374 1 227 . 1 1 25 25 THR CG2 C 13 21.61 0.30 . 5 . . . . . . . . 4374 1 228 . 1 1 25 25 THR HA H 1 4.31 0.03 . 1 . . . . . . . . 4374 1 229 . 1 1 25 25 THR HB H 1 4.16 0.03 . 1 . . . . . . . . 4374 1 230 . 1 1 25 25 THR HG21 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 231 . 1 1 25 25 THR HG22 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 232 . 1 1 25 25 THR HG23 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 233 . 1 1 25 25 THR H H 1 8.30 0.01 . 1 . . . . . . . . 4374 1 234 . 1 1 25 25 THR N N 15 116.62 0.10 . 1 . . . . . . . . 4374 1 235 . 1 1 26 26 VAL C C 13 176.31 0.10 . 1 . . . . . . . . 4374 1 236 . 1 1 26 26 VAL CA C 13 62.34 0.10 . 1 . . . . . . . . 4374 1 237 . 1 1 26 26 VAL CB C 13 32.76 0.10 . 1 . . . . . . . . 4374 1 238 . 1 1 26 26 VAL CG1 C 13 21.07 0.20 . 2 . . . . . . . . 4374 1 239 . 1 1 26 26 VAL CG2 C 13 20.41 0.20 . 2 . . . . . . . . 4374 1 240 . 1 1 26 26 VAL HA H 1 4.18 0.03 . 1 . . . . . . . . 4374 1 241 . 1 1 26 26 VAL HB H 1 2.09 0.03 . 1 . . . . . . . . 4374 1 242 . 1 1 26 26 VAL HG11 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 243 . 1 1 26 26 VAL HG12 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 244 . 1 1 26 26 VAL HG13 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 245 . 1 1 26 26 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 246 . 1 1 26 26 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 247 . 1 1 26 26 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 248 . 1 1 26 26 VAL H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 249 . 1 1 26 26 VAL N N 15 123.08 0.10 . 1 . . . . . . . . 4374 1 250 . 1 1 27 27 THR C C 13 174.65 0.10 . 1 . . . . . . . . 4374 1 251 . 1 1 27 27 THR CA C 13 61.87 0.10 . 1 . . . . . . . . 4374 1 252 . 1 1 27 27 THR CB C 13 69.70 0.10 . 1 . . . . . . . . 4374 1 253 . 1 1 27 27 THR CG2 C 13 21.61 0.30 . 5 . . . . . . . . 4374 1 254 . 1 1 27 27 THR HA H 1 4.31 0.03 . 1 . . . . . . . . 4374 1 255 . 1 1 27 27 THR HB H 1 4.25 0.03 . 1 . . . . . . . . 4374 1 256 . 1 1 27 27 THR HG21 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 257 . 1 1 27 27 THR HG22 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 258 . 1 1 27 27 THR HG23 H 1 1.18 0.03 . 1 . . . . . . . . 4374 1 259 . 1 1 27 27 THR H H 1 8.38 0.01 . 1 . . . . . . . . 4374 1 260 . 1 1 27 27 THR N N 15 118.52 0.10 . 1 . . . . . . . . 4374 1 261 . 1 1 28 28 MET C C 13 176.29 0.10 . 1 . . . . . . . . 4374 1 262 . 1 1 28 28 MET CA C 13 55.71 0.10 . 1 . . . . . . . . 4374 1 263 . 1 1 28 28 MET CB C 13 32.43 0.10 . 1 . . . . . . . . 4374 1 264 . 1 1 28 28 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 265 . 1 1 28 28 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 266 . 1 1 28 28 MET HA H 1 4.42 0.03 . 1 . . . . . . . . 4374 1 267 . 1 1 28 28 MET HB2 H 1 2.06 0.03 . 1 . . . . . . . . 4374 1 268 . 1 1 28 28 MET HB3 H 1 2.06 0.03 . 1 . . . . . . . . 4374 1 269 . 1 1 28 28 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 270 . 1 1 28 28 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 271 . 1 1 28 28 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 272 . 1 1 28 28 MET HG2 H 1 2.58 0.03 . 1 . . . . . . . . 4374 1 273 . 1 1 28 28 MET HG3 H 1 2.58 0.03 . 1 . . . . . . . . 4374 1 274 . 1 1 28 28 MET H H 1 8.56 0.01 . 1 . . . . . . . . 4374 1 275 . 1 1 28 28 MET N N 15 123.06 0.10 . 1 . . . . . . . . 4374 1 276 . 1 1 29 29 ALA C C 13 177.99 0.10 . 1 . . . . . . . . 4374 1 277 . 1 1 29 29 ALA CA C 13 52.95 0.10 . 1 . . . . . . . . 4374 1 278 . 1 1 29 29 ALA CB C 13 19.19 0.10 . 1 . . . . . . . . 4374 1 279 . 1 1 29 29 ALA HA H 1 4.20 0.03 . 1 . . . . . . . . 4374 1 280 . 1 1 29 29 ALA HB1 H 1 1.34 0.03 . 1 . . . . . . . . 4374 1 281 . 1 1 29 29 ALA HB2 H 1 1.34 0.03 . 1 . . . . . . . . 4374 1 282 . 1 1 29 29 ALA HB3 H 1 1.34 0.03 . 1 . . . . . . . . 4374 1 283 . 1 1 29 29 ALA H H 1 8.40 0.01 . 1 . . . . . . . . 4374 1 284 . 1 1 29 29 ALA N N 15 124.83 0.10 . 1 . . . . . . . . 4374 1 285 . 1 1 30 30 GLU C C 13 177.85 0.10 . 1 . . . . . . . . 4374 1 286 . 1 1 30 30 GLU CA C 13 56.82 0.10 . 1 . . . . . . . . 4374 1 287 . 1 1 30 30 GLU CB C 13 30.25 0.10 . 1 . . . . . . . . 4374 1 288 . 1 1 30 30 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 289 . 1 1 30 30 GLU HA H 1 4.15 0.03 . 1 . . . . . . . . 4374 1 290 . 1 1 30 30 GLU HB2 H 1 1.90 0.03 . 1 . . . . . . . . 4374 1 291 . 1 1 30 30 GLU HB3 H 1 1.90 0.03 . 1 . . . . . . . . 4374 1 292 . 1 1 30 30 GLU HG2 H 1 2.12 0.03 . 1 . . . . . . . . 4374 1 293 . 1 1 30 30 GLU HG3 H 1 2.12 0.03 . 1 . . . . . . . . 4374 1 294 . 1 1 30 30 GLU H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 295 . 1 1 30 30 GLU N N 15 119.49 0.10 . 1 . . . . . . . . 4374 1 296 . 1 1 31 31 PHE C C 13 175.54 0.10 . 1 . . . . . . . . 4374 1 297 . 1 1 31 31 PHE CA C 13 57.91 0.10 . 1 . . . . . . . . 4374 1 298 . 1 1 31 31 PHE CB C 13 39.37 0.10 . 1 . . . . . . . . 4374 1 299 . 1 1 31 31 PHE HA H 1 4.53 0.03 . 1 . . . . . . . . 4374 1 300 . 1 1 31 31 PHE HB2 H 1 3.08 0.03 . 1 . . . . . . . . 4374 1 301 . 1 1 31 31 PHE HB3 H 1 3.08 0.03 . 1 . . . . . . . . 4374 1 302 . 1 1 31 31 PHE HD1 H 1 7.27 0.03 . 1 . . . . . . . . 4374 1 303 . 1 1 31 31 PHE HD2 H 1 7.27 0.02 . 1 . . . . . . . . 4374 1 304 . 1 1 31 31 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 305 . 1 1 31 31 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 306 . 1 1 31 31 PHE H H 1 8.29 0.01 . 1 . . . . . . . . 4374 1 307 . 1 1 31 31 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 308 . 1 1 31 31 PHE N N 15 121.39 0.10 . 1 . . . . . . . . 4374 1 309 . 1 1 32 32 ARG C C 13 175.45 0.10 . 1 . . . . . . . . 4374 1 310 . 1 1 32 32 ARG CA C 13 55.66 0.10 . 1 . . . . . . . . 4374 1 311 . 1 1 32 32 ARG CB C 13 30.84 0.10 . 1 . . . . . . . . 4374 1 312 . 1 1 32 32 ARG CD C 13 43.20 0.20 . 5 . . . . . . . . 4374 1 313 . 1 1 32 32 ARG CG C 13 27.00 0.40 . 5 . . . . . . . . 4374 1 314 . 1 1 32 32 ARG HA H 1 4.23 0.03 . 1 . . . . . . . . 4374 1 315 . 1 1 32 32 ARG HB2 H 1 1.68 0.03 . 1 . . . . . . . . 4374 1 316 . 1 1 32 32 ARG HB3 H 1 1.68 0.03 . 1 . . . . . . . . 4374 1 317 . 1 1 32 32 ARG HD2 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 318 . 1 1 32 32 ARG HD3 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 319 . 1 1 32 32 ARG HG2 H 1 1.53 0.03 . 1 . . . . . . . . 4374 1 320 . 1 1 32 32 ARG HG3 H 1 1.53 0.03 . 1 . . . . . . . . 4374 1 321 . 1 1 32 32 ARG H H 1 8.15 0.01 . 1 . . . . . . . . 4374 1 322 . 1 1 32 32 ARG N N 15 122.90 0.10 . 1 . . . . . . . . 4374 1 323 . 1 1 33 33 ARG C C 13 176.11 0.10 . 1 . . . . . . . . 4374 1 324 . 1 1 33 33 ARG CA C 13 56.05 0.10 . 1 . . . . . . . . 4374 1 325 . 1 1 33 33 ARG CB C 13 30.59 0.10 . 1 . . . . . . . . 4374 1 326 . 1 1 33 33 ARG CD C 13 43.20 0.20 . 5 . . . . . . . . 4374 1 327 . 1 1 33 33 ARG CG C 13 27.00 0.40 . 5 . . . . . . . . 4374 1 328 . 1 1 33 33 ARG HA H 1 4.22 0.03 . 1 . . . . . . . . 4374 1 329 . 1 1 33 33 ARG HB2 H 1 1.74 0.03 . 1 . . . . . . . . 4374 1 330 . 1 1 33 33 ARG HB3 H 1 1.74 0.03 . 1 . . . . . . . . 4374 1 331 . 1 1 33 33 ARG HD2 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 332 . 1 1 33 33 ARG HD3 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 333 . 1 1 33 33 ARG HG2 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 334 . 1 1 33 33 ARG HG3 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 335 . 1 1 33 33 ARG H H 1 8.35 0.01 . 1 . . . . . . . . 4374 1 336 . 1 1 33 33 ARG N N 15 122.93 0.10 . 1 . . . . . . . . 4374 1 337 . 1 1 34 34 VAL CA C 13 59.68 0.10 . 1 . . . . . . . . 4374 1 338 . 1 1 34 34 VAL CB C 13 32.50 0.10 . 1 . . . . . . . . 4374 1 339 . 1 1 34 34 VAL CG1 C 13 20.90 0.20 . 2 . . . . . . . . 4374 1 340 . 1 1 34 34 VAL CG2 C 13 20.41 0.20 . 2 . . . . . . . . 4374 1 341 . 1 1 34 34 VAL HA H 1 4.38 0.03 . 1 . . . . . . . . 4374 1 342 . 1 1 34 34 VAL HB H 1 2.05 0.03 . 1 . . . . . . . . 4374 1 343 . 1 1 34 34 VAL HG11 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 344 . 1 1 34 34 VAL HG12 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 345 . 1 1 34 34 VAL HG13 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 346 . 1 1 34 34 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 347 . 1 1 34 34 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 348 . 1 1 34 34 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 349 . 1 1 34 34 VAL H H 1 8.26 0.01 . 1 . . . . . . . . 4374 1 350 . 1 1 34 34 VAL N N 15 123.13 0.10 . 1 . . . . . . . . 4374 1 351 . 1 1 35 35 PRO C C 13 176.49 0.10 . 1 . . . . . . . . 4374 1 352 . 1 1 35 35 PRO CA C 13 62.75 0.10 . 1 . . . . . . . . 4374 1 353 . 1 1 35 35 PRO CB C 13 31.98 0.10 . 1 . . . . . . . . 4374 1 354 . 1 1 35 35 PRO CG C 13 27.35 0.20 . 5 . . . . . . . . 4374 1 355 . 1 1 35 35 PRO HA H 1 4.37 0.03 . 1 . . . . . . . . 4374 1 356 . 1 1 35 35 PRO HB2 H 1 2.23 0.03 . 4 . . . . . . . . 4374 1 357 . 1 1 35 35 PRO HB3 H 1 2.23 0.03 . 4 . . . . . . . . 4374 1 358 . 1 1 35 35 PRO HG2 H 1 1.83 0.03 . 4 . . . . . . . . 4374 1 359 . 1 1 35 35 PRO HG3 H 1 1.83 0.03 . 4 . . . . . . . . 4374 1 360 . 1 1 36 36 LEU CA C 13 52.91 0.10 . 1 . . . . . . . . 4374 1 361 . 1 1 36 36 LEU CB C 13 41.54 0.10 . 1 . . . . . . . . 4374 1 362 . 1 1 36 36 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 363 . 1 1 36 36 LEU CD2 C 13 23.34 0.10 . 2 . . . . . . . . 4374 1 364 . 1 1 36 36 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 365 . 1 1 36 36 LEU HA H 1 4.55 0.03 . 1 . . . . . . . . 4374 1 366 . 1 1 36 36 LEU HB2 H 1 1.55 0.03 . 1 . . . . . . . . 4374 1 367 . 1 1 36 36 LEU HB3 H 1 1.55 0.03 . 1 . . . . . . . . 4374 1 368 . 1 1 36 36 LEU HD11 H 1 0.95 0.03 . 2 . . . . . . . . 4374 1 369 . 1 1 36 36 LEU HD12 H 1 0.95 0.03 . 2 . . . . . . . . 4374 1 370 . 1 1 36 36 LEU HD13 H 1 0.95 0.03 . 2 . . . . . . . . 4374 1 371 . 1 1 36 36 LEU HD21 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 372 . 1 1 36 36 LEU HD22 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 373 . 1 1 36 36 LEU HD23 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 374 . 1 1 36 36 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 375 . 1 1 36 36 LEU H H 1 8.42 0.01 . 1 . . . . . . . . 4374 1 376 . 1 1 36 36 LEU N N 15 123.82 0.10 . 1 . . . . . . . . 4374 1 377 . 1 1 37 37 PRO CA C 13 61.27 0.10 . 1 . . . . . . . . 4374 1 378 . 1 1 37 37 PRO CG C 13 27.33 0.40 . 5 . . . . . . . . 4374 1 379 . 1 1 37 37 PRO HA H 1 4.66 0.03 . 1 . . . . . . . . 4374 1 380 . 1 1 37 37 PRO HG2 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 381 . 1 1 37 37 PRO HG3 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 382 . 1 1 38 38 PRO C C 13 176.98 0.10 . 1 . . . . . . . . 4374 1 383 . 1 1 38 38 PRO CA C 13 62.77 0.10 . 1 . . . . . . . . 4374 1 384 . 1 1 38 38 PRO CB C 13 31.90 0.10 . 1 . . . . . . . . 4374 1 385 . 1 1 38 38 PRO CG C 13 27.33 0.40 . 5 . . . . . . . . 4374 1 386 . 1 1 38 38 PRO HA H 1 4.38 0.03 . 5 . . . . . . . . 4374 1 387 . 1 1 38 38 PRO HG2 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 388 . 1 1 38 38 PRO HG3 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 389 . 1 1 39 39 MET C C 13 175.92 0.10 . 1 . . . . . . . . 4374 1 390 . 1 1 39 39 MET CA C 13 55.29 0.10 . 1 . . . . . . . . 4374 1 391 . 1 1 39 39 MET CB C 13 32.91 0.10 . 1 . . . . . . . . 4374 1 392 . 1 1 39 39 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 393 . 1 1 39 39 MET CG C 13 32.01 0.10 . 5 . . . . . . . . 4374 1 394 . 1 1 39 39 MET HA H 1 4.39 0.03 . 1 . . . . . . . . 4374 1 395 . 1 1 39 39 MET HB2 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 396 . 1 1 39 39 MET HB3 H 1 2.02 0.03 . 1 . . . . . . . . 4374 1 397 . 1 1 39 39 MET HE1 H 1 2.01 0.02 . 5 . . . . . . . . 4374 1 398 . 1 1 39 39 MET HE2 H 1 2.01 0.02 . 5 . . . . . . . . 4374 1 399 . 1 1 39 39 MET HE3 H 1 2.01 0.02 . 5 . . . . . . . . 4374 1 400 . 1 1 39 39 MET HG2 H 1 2.29 0.03 . 1 . . . . . . . . 4374 1 401 . 1 1 39 39 MET HG3 H 1 2.29 0.03 . 1 . . . . . . . . 4374 1 402 . 1 1 39 39 MET H H 1 8.53 0.01 . 1 . . . . . . . . 4374 1 403 . 1 1 39 39 MET N N 15 120.69 0.10 . 1 . . . . . . . . 4374 1 404 . 1 1 40 40 ALA C C 13 177.50 0.10 . 1 . . . . . . . . 4374 1 405 . 1 1 40 40 ALA CA C 13 52.25 0.10 . 1 . . . . . . . . 4374 1 406 . 1 1 40 40 ALA CB C 13 19.43 0.10 . 1 . . . . . . . . 4374 1 407 . 1 1 40 40 ALA HA H 1 4.26 0.03 . 1 . . . . . . . . 4374 1 408 . 1 1 40 40 ALA HB1 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 409 . 1 1 40 40 ALA HB2 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 410 . 1 1 40 40 ALA HB3 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 411 . 1 1 40 40 ALA H H 1 8.41 0.01 . 1 . . . . . . . . 4374 1 412 . 1 1 40 40 ALA N N 15 125.50 0.10 . 1 . . . . . . . . 4374 1 413 . 1 1 41 41 GLU C C 13 176.29 0.10 . 1 . . . . . . . . 4374 1 414 . 1 1 41 41 GLU CA C 13 56.14 0.10 . 1 . . . . . . . . 4374 1 415 . 1 1 41 41 GLU CB C 13 30.29 0.10 . 1 . . . . . . . . 4374 1 416 . 1 1 41 41 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 417 . 1 1 41 41 GLU HA H 1 4.25 0.03 . 1 . . . . . . . . 4374 1 418 . 1 1 41 41 GLU HB2 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 419 . 1 1 41 41 GLU HB3 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 420 . 1 1 41 41 GLU HG2 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 421 . 1 1 41 41 GLU HG3 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 422 . 1 1 41 41 GLU H H 1 8.49 0.01 . 1 . . . . . . . . 4374 1 423 . 1 1 41 41 GLU N N 15 120.61 0.10 . 1 . . . . . . . . 4374 1 424 . 1 1 42 42 VAL CA C 13 59.87 0.10 . 1 . . . . . . . . 4374 1 425 . 1 1 42 42 VAL CB C 13 32.43 0.10 . 1 . . . . . . . . 4374 1 426 . 1 1 42 42 VAL CG1 C 13 20.90 0.20 . 2 . . . . . . . . 4374 1 427 . 1 1 42 42 VAL CG2 C 13 20.41 0.20 . 2 . . . . . . . . 4374 1 428 . 1 1 42 42 VAL HA H 1 4.37 0.03 . 1 . . . . . . . . 4374 1 429 . 1 1 42 42 VAL HB H 1 2.06 0.03 . 1 . . . . . . . . 4374 1 430 . 1 1 42 42 VAL HG11 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 431 . 1 1 42 42 VAL HG12 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 432 . 1 1 42 42 VAL HG13 H 1 0.96 0.02 . 2 . . . . . . . . 4374 1 433 . 1 1 42 42 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 434 . 1 1 42 42 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 435 . 1 1 42 42 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 436 . 1 1 42 42 VAL H H 1 8.38 0.01 . 1 . . . . . . . . 4374 1 437 . 1 1 42 42 VAL N N 15 123.68 0.10 . 1 . . . . . . . . 4374 1 438 . 1 1 43 43 PRO C C 13 176.77 0.10 . 1 . . . . . . . . 4374 1 439 . 1 1 43 43 PRO CA C 13 63.01 0.10 . 1 . . . . . . . . 4374 1 440 . 1 1 43 43 PRO CB C 13 32.06 0.10 . 1 . . . . . . . . 4374 1 441 . 1 1 43 43 PRO CG C 13 27.33 0.40 . 5 . . . . . . . . 4374 1 442 . 1 1 43 43 PRO HA H 1 4.40 0.03 . 1 . . . . . . . . 4374 1 443 . 1 1 43 43 PRO HG2 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 444 . 1 1 43 43 PRO HG3 H 1 2.02 0.05 . 5 . . . . . . . . 4374 1 445 . 1 1 44 44 MET C C 13 176.33 0.10 . 1 . . . . . . . . 4374 1 446 . 1 1 44 44 MET CA C 13 55.40 0.10 . 1 . . . . . . . . 4374 1 447 . 1 1 44 44 MET CB C 13 32.88 0.10 . 1 . . . . . . . . 4374 1 448 . 1 1 44 44 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 449 . 1 1 44 44 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 450 . 1 1 44 44 MET HA H 1 4.42 0.03 . 1 . . . . . . . . 4374 1 451 . 1 1 44 44 MET HB2 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 452 . 1 1 44 44 MET HB3 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 453 . 1 1 44 44 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 454 . 1 1 44 44 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 455 . 1 1 44 44 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 456 . 1 1 44 44 MET HG2 H 1 2.56 0.03 . 1 . . . . . . . . 4374 1 457 . 1 1 44 44 MET HG3 H 1 2.56 0.03 . 1 . . . . . . . . 4374 1 458 . 1 1 44 44 MET H H 1 8.58 0.01 . 1 . . . . . . . . 4374 1 459 . 1 1 44 44 MET N N 15 121.31 0.10 . 1 . . . . . . . . 4374 1 460 . 1 1 45 45 LEU C C 13 177.54 0.10 . 1 . . . . . . . . 4374 1 461 . 1 1 45 45 LEU CA C 13 55.12 0.10 . 1 . . . . . . . . 4374 1 462 . 1 1 45 45 LEU CB C 13 42.27 0.10 . 1 . . . . . . . . 4374 1 463 . 1 1 45 45 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 464 . 1 1 45 45 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 465 . 1 1 45 45 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 466 . 1 1 45 45 LEU HA H 1 4.38 0.03 . 1 . . . . . . . . 4374 1 467 . 1 1 45 45 LEU HB2 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 468 . 1 1 45 45 LEU HB3 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 469 . 1 1 45 45 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 470 . 1 1 45 45 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 471 . 1 1 45 45 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 472 . 1 1 45 45 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 473 . 1 1 45 45 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 474 . 1 1 45 45 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 475 . 1 1 45 45 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 476 . 1 1 45 45 LEU H H 1 8.44 0.01 . 1 . . . . . . . . 4374 1 477 . 1 1 45 45 LEU N N 15 124.02 0.10 . 1 . . . . . . . . 4374 1 478 . 1 1 46 46 SER C C 13 175.08 0.10 . 1 . . . . . . . . 4374 1 479 . 1 1 46 46 SER CA C 13 58.22 0.10 . 1 . . . . . . . . 4374 1 480 . 1 1 46 46 SER CB C 13 63.66 0.10 . 1 . . . . . . . . 4374 1 481 . 1 1 46 46 SER HA H 1 4.48 0.03 . 1 . . . . . . . . 4374 1 482 . 1 1 46 46 SER HB2 H 1 3.89 0.03 . 1 . . . . . . . . 4374 1 483 . 1 1 46 46 SER HB3 H 1 3.89 0.03 . 1 . . . . . . . . 4374 1 484 . 1 1 46 46 SER H H 1 8.51 0.01 . 1 . . . . . . . . 4374 1 485 . 1 1 46 46 SER N N 15 116.89 0.10 . 1 . . . . . . . . 4374 1 486 . 1 1 47 47 THR C C 13 174.85 0.10 . 1 . . . . . . . . 4374 1 487 . 1 1 47 47 THR CA C 13 61.92 0.10 . 1 . . . . . . . . 4374 1 488 . 1 1 47 47 THR CB C 13 69.41 0.10 . 1 . . . . . . . . 4374 1 489 . 1 1 47 47 THR CG2 C 13 21.61 0.30 . 5 . . . . . . . . 4374 1 490 . 1 1 47 47 THR HA H 1 4.35 0.03 . 1 . . . . . . . . 4374 1 491 . 1 1 47 47 THR HB H 1 4.30 0.03 . 1 . . . . . . . . 4374 1 492 . 1 1 47 47 THR HG21 H 1 1.19 0.03 . 1 . . . . . . . . 4374 1 493 . 1 1 47 47 THR HG22 H 1 1.19 0.03 . 1 . . . . . . . . 4374 1 494 . 1 1 47 47 THR HG23 H 1 1.19 0.03 . 1 . . . . . . . . 4374 1 495 . 1 1 47 47 THR H H 1 8.28 0.01 . 1 . . . . . . . . 4374 1 496 . 1 1 47 47 THR N N 15 115.51 0.10 . 1 . . . . . . . . 4374 1 497 . 1 1 48 48 GLN C C 13 175.86 0.10 . 1 . . . . . . . . 4374 1 498 . 1 1 48 48 GLN CA C 13 56.05 0.10 . 1 . . . . . . . . 4374 1 499 . 1 1 48 48 GLN CB C 13 29.25 0.10 . 1 . . . . . . . . 4374 1 500 . 1 1 48 48 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 501 . 1 1 48 48 GLN HA H 1 4.30 0.03 . 1 . . . . . . . . 4374 1 502 . 1 1 48 48 GLN HB2 H 1 2.00 0.03 . 1 . . . . . . . . 4374 1 503 . 1 1 48 48 GLN HB3 H 1 2.00 0.03 . 1 . . . . . . . . 4374 1 504 . 1 1 48 48 GLN HG2 H 1 2.34 0.03 . 1 . . . . . . . . 4374 1 505 . 1 1 48 48 GLN HG3 H 1 2.34 0.03 . 1 . . . . . . . . 4374 1 506 . 1 1 48 48 GLN H H 1 8.42 0.01 . 1 . . . . . . . . 4374 1 507 . 1 1 48 48 GLN N N 15 122.11 0.10 . 1 . . . . . . . . 4374 1 508 . 1 1 49 49 ASN C C 13 175.49 0.10 . 1 . . . . . . . . 4374 1 509 . 1 1 49 49 ASN CA C 13 53.23 0.10 . 1 . . . . . . . . 4374 1 510 . 1 1 49 49 ASN CB C 13 38.75 0.10 . 1 . . . . . . . . 4374 1 511 . 1 1 49 49 ASN HA H 1 4.72 0.03 . 1 . . . . . . . . 4374 1 512 . 1 1 49 49 ASN HB2 H 1 2.78 0.03 . 1 . . . . . . . . 4374 1 513 . 1 1 49 49 ASN HB3 H 1 2.78 0.03 . 1 . . . . . . . . 4374 1 514 . 1 1 49 49 ASN H H 1 8.55 0.01 . 1 . . . . . . . . 4374 1 515 . 1 1 49 49 ASN N N 15 119.72 0.10 . 1 . . . . . . . . 4374 1 516 . 1 1 50 50 SER C C 13 174.90 0.10 . 1 . . . . . . . . 4374 1 517 . 1 1 50 50 SER CA C 13 58.67 0.10 . 1 . . . . . . . . 4374 1 518 . 1 1 50 50 SER CB C 13 63.53 0.10 . 1 . . . . . . . . 4374 1 519 . 1 1 50 50 SER HA H 1 4.42 0.03 . 1 . . . . . . . . 4374 1 520 . 1 1 50 50 SER HB2 H 1 3.88 0.03 . 1 . . . . . . . . 4374 1 521 . 1 1 50 50 SER HB3 H 1 3.88 0.03 . 1 . . . . . . . . 4374 1 522 . 1 1 50 50 SER H H 1 8.44 0.01 . 1 . . . . . . . . 4374 1 523 . 1 1 50 50 SER N N 15 116.48 0.10 . 1 . . . . . . . . 4374 1 524 . 1 1 51 51 MET C C 13 176.99 0.10 . 1 . . . . . . . . 4374 1 525 . 1 1 51 51 MET CA C 13 55.68 0.10 . 1 . . . . . . . . 4374 1 526 . 1 1 51 51 MET CB C 13 32.23 0.10 . 1 . . . . . . . . 4374 1 527 . 1 1 51 51 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 528 . 1 1 51 51 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 529 . 1 1 51 51 MET HA H 1 4.50 0.03 . 1 . . . . . . . . 4374 1 530 . 1 1 51 51 MET HB2 H 1 2.12 0.03 . 1 . . . . . . . . 4374 1 531 . 1 1 51 51 MET HB3 H 1 2.12 0.03 . 1 . . . . . . . . 4374 1 532 . 1 1 51 51 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 533 . 1 1 51 51 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 534 . 1 1 51 51 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 535 . 1 1 51 51 MET HG2 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 536 . 1 1 51 51 MET HG3 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 537 . 1 1 51 51 MET H H 1 8.51 0.01 . 1 . . . . . . . . 4374 1 538 . 1 1 51 51 MET N N 15 121.85 0.10 . 1 . . . . . . . . 4374 1 539 . 1 1 52 52 GLY C C 13 174.26 0.10 . 1 . . . . . . . . 4374 1 540 . 1 1 52 52 GLY CA C 13 45.21 0.10 . 1 . . . . . . . . 4374 1 541 . 1 1 52 52 GLY HA2 H 1 3.97 0.03 . 1 . . . . . . . . 4374 1 542 . 1 1 52 52 GLY HA3 H 1 3.97 0.03 . 1 . . . . . . . . 4374 1 543 . 1 1 52 52 GLY H H 1 8.45 0.01 . 1 . . . . . . . . 4374 1 544 . 1 1 52 52 GLY N N 15 109.80 0.10 . 1 . . . . . . . . 4374 1 545 . 1 1 53 53 SER C C 13 174.91 0.10 . 1 . . . . . . . . 4374 1 546 . 1 1 53 53 SER CA C 13 58.19 0.10 . 1 . . . . . . . . 4374 1 547 . 1 1 53 53 SER CB C 13 63.90 0.10 . 1 . . . . . . . . 4374 1 548 . 1 1 53 53 SER HA H 1 4.49 0.03 . 1 . . . . . . . . 4374 1 549 . 1 1 53 53 SER HB2 H 1 3.95 0.03 . 1 . . . . . . . . 4374 1 550 . 1 1 53 53 SER HB3 H 1 3.95 0.03 . 1 . . . . . . . . 4374 1 551 . 1 1 53 53 SER H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 552 . 1 1 53 53 SER N N 15 115.73 0.10 . 1 . . . . . . . . 4374 1 553 . 1 1 54 54 SER C C 13 174.54 0.10 . 1 . . . . . . . . 4374 1 554 . 1 1 54 54 SER CA C 13 58.43 0.10 . 1 . . . . . . . . 4374 1 555 . 1 1 54 54 SER CB C 13 63.67 0.10 . 1 . . . . . . . . 4374 1 556 . 1 1 54 54 SER HA H 1 4.46 0.03 . 1 . . . . . . . . 4374 1 557 . 1 1 54 54 SER HB2 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 558 . 1 1 54 54 SER HB3 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 559 . 1 1 54 54 SER H H 1 8.55 0.01 . 1 . . . . . . . . 4374 1 560 . 1 1 54 54 SER N N 15 118.09 0.10 . 1 . . . . . . . . 4374 1 561 . 1 1 55 55 ALA C C 13 178.07 0.10 . 1 . . . . . . . . 4374 1 562 . 1 1 55 55 ALA CA C 13 52.73 0.10 . 1 . . . . . . . . 4374 1 563 . 1 1 55 55 ALA CB C 13 19.18 0.10 . 1 . . . . . . . . 4374 1 564 . 1 1 55 55 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4374 1 565 . 1 1 55 55 ALA HB1 H 1 1.39 0.03 . 1 . . . . . . . . 4374 1 566 . 1 1 55 55 ALA HB2 H 1 1.39 0.03 . 1 . . . . . . . . 4374 1 567 . 1 1 55 55 ALA HB3 H 1 1.39 0.03 . 1 . . . . . . . . 4374 1 568 . 1 1 55 55 ALA H H 1 8.45 0.01 . 1 . . . . . . . . 4374 1 569 . 1 1 55 55 ALA N N 15 125.98 0.10 . 1 . . . . . . . . 4374 1 570 . 1 1 56 56 SER C C 13 174.60 0.10 . 1 . . . . . . . . 4374 1 571 . 1 1 56 56 SER CA C 13 58.33 0.10 . 1 . . . . . . . . 4374 1 572 . 1 1 56 56 SER CB C 13 63.67 0.10 . 1 . . . . . . . . 4374 1 573 . 1 1 56 56 SER HA H 1 4.39 0.03 . 1 . . . . . . . . 4374 1 574 . 1 1 56 56 SER HB2 H 1 3.87 0.03 . 1 . . . . . . . . 4374 1 575 . 1 1 56 56 SER HB3 H 1 3.87 0.03 . 1 . . . . . . . . 4374 1 576 . 1 1 56 56 SER H H 1 8.32 0.01 . 1 . . . . . . . . 4374 1 577 . 1 1 56 56 SER N N 15 114.89 0.10 . 1 . . . . . . . . 4374 1 578 . 1 1 57 57 ALA C C 13 178.01 0.10 . 1 . . . . . . . . 4374 1 579 . 1 1 57 57 ALA CA C 13 52.70 0.10 . 1 . . . . . . . . 4374 1 580 . 1 1 57 57 ALA CB C 13 19.21 0.10 . 1 . . . . . . . . 4374 1 581 . 1 1 57 57 ALA HA H 1 4.33 0.03 . 1 . . . . . . . . 4374 1 582 . 1 1 57 57 ALA HB1 H 1 1.40 0.03 . 1 . . . . . . . . 4374 1 583 . 1 1 57 57 ALA HB2 H 1 1.40 0.03 . 1 . . . . . . . . 4374 1 584 . 1 1 57 57 ALA HB3 H 1 1.40 0.03 . 1 . . . . . . . . 4374 1 585 . 1 1 57 57 ALA H H 1 8.39 0.01 . 1 . . . . . . . . 4374 1 586 . 1 1 57 57 ALA N N 15 126.20 0.10 . 1 . . . . . . . . 4374 1 587 . 1 1 58 58 SER C C 13 174.59 0.10 . 1 . . . . . . . . 4374 1 588 . 1 1 58 58 SER CA C 13 58.28 0.10 . 1 . . . . . . . . 4374 1 589 . 1 1 58 58 SER CB C 13 63.74 0.10 . 1 . . . . . . . . 4374 1 590 . 1 1 58 58 SER HA H 1 4.40 0.03 . 1 . . . . . . . . 4374 1 591 . 1 1 58 58 SER HB2 H 1 3.88 0.03 . 1 . . . . . . . . 4374 1 592 . 1 1 58 58 SER HB3 H 1 3.88 0.03 . 1 . . . . . . . . 4374 1 593 . 1 1 58 58 SER H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 594 . 1 1 58 58 SER N N 15 115.00 0.10 . 1 . . . . . . . . 4374 1 595 . 1 1 59 59 ALA C C 13 178.26 0.10 . 1 . . . . . . . . 4374 1 596 . 1 1 59 59 ALA CA C 13 52.92 0.10 . 1 . . . . . . . . 4374 1 597 . 1 1 59 59 ALA CB C 13 19.17 0.10 . 1 . . . . . . . . 4374 1 598 . 1 1 59 59 ALA HA H 1 4.31 0.03 . 1 . . . . . . . . 4374 1 599 . 1 1 59 59 ALA HB1 H 1 1.41 0.03 . 1 . . . . . . . . 4374 1 600 . 1 1 59 59 ALA HB2 H 1 1.41 0.03 . 1 . . . . . . . . 4374 1 601 . 1 1 59 59 ALA HB3 H 1 1.41 0.03 . 1 . . . . . . . . 4374 1 602 . 1 1 59 59 ALA H H 1 8.43 0.01 . 1 . . . . . . . . 4374 1 603 . 1 1 59 59 ALA N N 15 125.96 0.10 . 1 . . . . . . . . 4374 1 604 . 1 1 60 60 SER C C 13 175.00 0.10 . 1 . . . . . . . . 4374 1 605 . 1 1 60 60 SER CA C 13 58.56 0.10 . 1 . . . . . . . . 4374 1 606 . 1 1 60 60 SER CB C 13 63.66 0.10 . 1 . . . . . . . . 4374 1 607 . 1 1 60 60 SER HA H 1 4.42 0.03 . 1 . . . . . . . . 4374 1 608 . 1 1 60 60 SER HB2 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 609 . 1 1 60 60 SER HB3 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 610 . 1 1 60 60 SER H H 1 8.41 0.01 . 1 . . . . . . . . 4374 1 611 . 1 1 60 60 SER N N 15 114.82 0.10 . 1 . . . . . . . . 4374 1 612 . 1 1 61 61 SER C C 13 175.04 0.10 . 1 . . . . . . . . 4374 1 613 . 1 1 61 61 SER CA C 13 58.90 0.10 . 1 . . . . . . . . 4374 1 614 . 1 1 61 61 SER CB C 13 63.49 0.10 . 1 . . . . . . . . 4374 1 615 . 1 1 61 61 SER HA H 1 4.41 0.03 . 1 . . . . . . . . 4374 1 616 . 1 1 61 61 SER HB2 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 617 . 1 1 61 61 SER HB3 H 1 3.90 0.03 . 1 . . . . . . . . 4374 1 618 . 1 1 61 61 SER H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 619 . 1 1 61 61 SER N N 15 118.03 0.10 . 1 . . . . . . . . 4374 1 620 . 1 1 62 62 LEU C C 13 177.98 0.10 . 1 . . . . . . . . 4374 1 621 . 1 1 62 62 LEU CA C 13 55.81 0.10 . 1 . . . . . . . . 4374 1 622 . 1 1 62 62 LEU CB C 13 42.00 0.10 . 1 . . . . . . . . 4374 1 623 . 1 1 62 62 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 624 . 1 1 62 62 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 625 . 1 1 62 62 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 626 . 1 1 62 62 LEU HA H 1 4.28 0.03 . 1 . . . . . . . . 4374 1 627 . 1 1 62 62 LEU HB2 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 628 . 1 1 62 62 LEU HB3 H 1 1.61 0.03 . 1 . . . . . . . . 4374 1 629 . 1 1 62 62 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 630 . 1 1 62 62 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 631 . 1 1 62 62 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 632 . 1 1 62 62 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 633 . 1 1 62 62 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 634 . 1 1 62 62 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 635 . 1 1 62 62 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 636 . 1 1 62 62 LEU H H 1 8.26 0.01 . 1 . . . . . . . . 4374 1 637 . 1 1 62 62 LEU N N 15 123.74 0.10 . 1 . . . . . . . . 4374 1 638 . 1 1 63 63 GLU C C 13 176.03 0.10 . 1 . . . . . . . . 4374 1 639 . 1 1 63 63 GLU CA C 13 55.85 0.10 . 1 . . . . . . . . 4374 1 640 . 1 1 63 63 GLU CB C 13 29.29 0.10 . 1 . . . . . . . . 4374 1 641 . 1 1 63 63 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 642 . 1 1 63 63 GLU HA H 1 4.18 0.03 . 1 . . . . . . . . 4374 1 643 . 1 1 63 63 GLU HB2 H 1 1.99 0.03 . 1 . . . . . . . . 4374 1 644 . 1 1 63 63 GLU HB3 H 1 1.99 0.03 . 1 . . . . . . . . 4374 1 645 . 1 1 63 63 GLU H H 1 8.41 0.01 . 1 . . . . . . . . 4374 1 646 . 1 1 63 63 GLU N N 15 120.36 0.10 . 1 . . . . . . . . 4374 1 647 . 1 1 64 64 MET C C 13 176.97 0.10 . 1 . . . . . . . . 4374 1 648 . 1 1 64 64 MET CA C 13 56.55 0.10 . 1 . . . . . . . . 4374 1 649 . 1 1 64 64 MET CB C 13 32.11 0.10 . 1 . . . . . . . . 4374 1 650 . 1 1 64 64 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 651 . 1 1 64 64 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 652 . 1 1 64 64 MET HA H 1 4.28 0.03 . 1 . . . . . . . . 4374 1 653 . 1 1 64 64 MET HB2 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 654 . 1 1 64 64 MET HB3 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 655 . 1 1 64 64 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 656 . 1 1 64 64 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 657 . 1 1 64 64 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 658 . 1 1 64 64 MET HG2 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 659 . 1 1 64 64 MET HG3 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 660 . 1 1 64 64 MET H H 1 8.52 0.01 . 1 . . . . . . . . 4374 1 661 . 1 1 64 64 MET N N 15 121.60 0.10 . 1 . . . . . . . . 4374 1 662 . 1 1 65 65 TRP C C 13 177.24 0.10 . 1 . . . . . . . . 4374 1 663 . 1 1 65 65 TRP CA C 13 58.32 0.10 . 1 . . . . . . . . 4374 1 664 . 1 1 65 65 TRP CB C 13 29.04 0.10 . 1 . . . . . . . . 4374 1 665 . 1 1 65 65 TRP HA H 1 4.59 0.03 . 1 . . . . . . . . 4374 1 666 . 1 1 65 65 TRP HB2 H 1 3.35 0.03 . 1 . . . . . . . . 4374 1 667 . 1 1 65 65 TRP HB3 H 1 3.35 0.03 . 1 . . . . . . . . 4374 1 668 . 1 1 65 65 TRP HD1 H 1 7.25 0.03 . 1 . . . . . . . . 4374 1 669 . 1 1 65 65 TRP HE1 H 1 10.24 0.02 . 1 . . . . . . . . 4374 1 670 . 1 1 65 65 TRP HE3 H 1 7.62 0.02 . 1 . . . . . . . . 4374 1 671 . 1 1 65 65 TRP HH2 H 1 7.22 0.02 . 1 . . . . . . . . 4374 1 672 . 1 1 65 65 TRP H H 1 8.09 0.01 . 1 . . . . . . . . 4374 1 673 . 1 1 65 65 TRP HZ2 H 1 7.48 0.02 . 1 . . . . . . . . 4374 1 674 . 1 1 65 65 TRP HZ3 H 1 7.15 0.02 . 1 . . . . . . . . 4374 1 675 . 1 1 65 65 TRP N N 15 120.84 0.10 . 1 . . . . . . . . 4374 1 676 . 1 1 66 66 GLU C C 13 177.55 0.10 . 1 . . . . . . . . 4374 1 677 . 1 1 66 66 GLU CA C 13 57.58 0.10 . 1 . . . . . . . . 4374 1 678 . 1 1 66 66 GLU CB C 13 29.94 0.10 . 1 . . . . . . . . 4374 1 679 . 1 1 66 66 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 680 . 1 1 66 66 GLU HA H 1 3.97 0.03 . 1 . . . . . . . . 4374 1 681 . 1 1 66 66 GLU HB2 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 682 . 1 1 66 66 GLU HB3 H 1 1.92 0.03 . 1 . . . . . . . . 4374 1 683 . 1 1 66 66 GLU HG2 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 684 . 1 1 66 66 GLU HG3 H 1 2.04 0.03 . 1 . . . . . . . . 4374 1 685 . 1 1 66 66 GLU H H 1 8.22 0.01 . 1 . . . . . . . . 4374 1 686 . 1 1 66 66 GLU N N 15 120.95 0.10 . 1 . . . . . . . . 4374 1 687 . 1 1 67 67 LYS C C 13 177.36 0.10 . 1 . . . . . . . . 4374 1 688 . 1 1 67 67 LYS CA C 13 57.54 0.10 . 1 . . . . . . . . 4374 1 689 . 1 1 67 67 LYS CB C 13 32.56 0.10 . 1 . . . . . . . . 4374 1 690 . 1 1 67 67 LYS CD C 13 28.99 0.20 . 5 . . . . . . . . 4374 1 691 . 1 1 67 67 LYS CE C 13 40.15 0.20 . 5 . . . . . . . . 4374 1 692 . 1 1 67 67 LYS CG C 13 24.64 0.30 . 5 . . . . . . . . 4374 1 693 . 1 1 67 67 LYS HA H 1 4.11 0.03 . 1 . . . . . . . . 4374 1 694 . 1 1 67 67 LYS HB2 H 1 1.81 0.03 . 1 . . . . . . . . 4374 1 695 . 1 1 67 67 LYS HB3 H 1 1.81 0.03 . 1 . . . . . . . . 4374 1 696 . 1 1 67 67 LYS HD2 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 697 . 1 1 67 67 LYS HD3 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 698 . 1 1 67 67 LYS HE2 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 699 . 1 1 67 67 LYS HE3 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 700 . 1 1 67 67 LYS HG2 H 1 1.44 0.03 . 1 . . . . . . . . 4374 1 701 . 1 1 67 67 LYS HG3 H 1 1.44 0.03 . 1 . . . . . . . . 4374 1 702 . 1 1 67 67 LYS H H 1 8.03 0.01 . 1 . . . . . . . . 4374 1 703 . 1 1 67 67 LYS N N 15 121.26 0.10 . 1 . . . . . . . . 4374 1 704 . 1 1 68 68 ASP C C 13 177.23 0.10 . 1 . . . . . . . . 4374 1 705 . 1 1 68 68 ASP CA C 13 55.49 0.10 . 1 . . . . . . . . 4374 1 706 . 1 1 68 68 ASP CB C 13 40.72 0.10 . 1 . . . . . . . . 4374 1 707 . 1 1 68 68 ASP HA H 1 4.47 0.03 . 1 . . . . . . . . 4374 1 708 . 1 1 68 68 ASP HB2 H 1 2.70 0.03 . 1 . . . . . . . . 4374 1 709 . 1 1 68 68 ASP HB3 H 1 2.70 0.03 . 1 . . . . . . . . 4374 1 710 . 1 1 68 68 ASP H H 1 8.30 0.01 . 1 . . . . . . . . 4374 1 711 . 1 1 68 68 ASP N N 15 120.33 0.10 . 1 . . . . . . . . 4374 1 712 . 1 1 69 69 LEU C C 13 178.24 0.10 . 1 . . . . . . . . 4374 1 713 . 1 1 69 69 LEU CA C 13 56.79 0.10 . 1 . . . . . . . . 4374 1 714 . 1 1 69 69 LEU CB C 13 41.81 0.10 . 1 . . . . . . . . 4374 1 715 . 1 1 69 69 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 716 . 1 1 69 69 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 717 . 1 1 69 69 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 718 . 1 1 69 69 LEU HA H 1 4.06 0.03 . 1 . . . . . . . . 4374 1 719 . 1 1 69 69 LEU HB2 H 1 1.57 0.03 . 1 . . . . . . . . 4374 1 720 . 1 1 69 69 LEU HB3 H 1 1.57 0.03 . 1 . . . . . . . . 4374 1 721 . 1 1 69 69 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 722 . 1 1 69 69 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 723 . 1 1 69 69 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 724 . 1 1 69 69 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 725 . 1 1 69 69 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 726 . 1 1 69 69 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 727 . 1 1 69 69 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 728 . 1 1 69 69 LEU H H 1 8.00 0.01 . 1 . . . . . . . . 4374 1 729 . 1 1 69 69 LEU N N 15 121.39 0.10 . 1 . . . . . . . . 4374 1 730 . 1 1 70 70 GLU C C 13 177.80 0.10 . 1 . . . . . . . . 4374 1 731 . 1 1 70 70 GLU CA C 13 57.98 0.10 . 1 . . . . . . . . 4374 1 732 . 1 1 70 70 GLU CB C 13 29.70 0.10 . 1 . . . . . . . . 4374 1 733 . 1 1 70 70 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 734 . 1 1 70 70 GLU HA H 1 4.04 0.03 . 1 . . . . . . . . 4374 1 735 . 1 1 70 70 GLU HB2 H 1 2.03 0.03 . 1 . . . . . . . . 4374 1 736 . 1 1 70 70 GLU HB3 H 1 2.03 0.03 . 1 . . . . . . . . 4374 1 737 . 1 1 70 70 GLU HG2 H 1 2.26 0.03 . 1 . . . . . . . . 4374 1 738 . 1 1 70 70 GLU HG3 H 1 2.26 0.03 . 1 . . . . . . . . 4374 1 739 . 1 1 70 70 GLU H H 1 8.19 0.01 . 1 . . . . . . . . 4374 1 740 . 1 1 70 70 GLU N N 15 119.70 0.10 . 1 . . . . . . . . 4374 1 741 . 1 1 71 71 GLU C C 13 178.00 0.10 . 1 . . . . . . . . 4374 1 742 . 1 1 71 71 GLU CA C 13 57.78 0.10 . 1 . . . . . . . . 4374 1 743 . 1 1 71 71 GLU CB C 13 29.69 0.10 . 1 . . . . . . . . 4374 1 744 . 1 1 71 71 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 745 . 1 1 71 71 GLU HA H 1 4.13 0.03 . 1 . . . . . . . . 4374 1 746 . 1 1 71 71 GLU HB2 H 1 2.03 0.03 . 1 . . . . . . . . 4374 1 747 . 1 1 71 71 GLU HB3 H 1 2.03 0.03 . 1 . . . . . . . . 4374 1 748 . 1 1 71 71 GLU HG2 H 1 2.33 0.03 . 1 . . . . . . . . 4374 1 749 . 1 1 71 71 GLU HG3 H 1 2.33 0.03 . 1 . . . . . . . . 4374 1 750 . 1 1 71 71 GLU H H 1 8.25 0.01 . 1 . . . . . . . . 4374 1 751 . 1 1 71 71 GLU N N 15 120.13 0.10 . 1 . . . . . . . . 4374 1 752 . 1 1 72 72 ARG C C 13 176.44 0.10 . 1 . . . . . . . . 4374 1 753 . 1 1 72 72 ARG CA C 13 57.31 0.10 . 1 . . . . . . . . 4374 1 754 . 1 1 72 72 ARG CB C 13 30.25 0.10 . 1 . . . . . . . . 4374 1 755 . 1 1 72 72 ARG CD C 13 43.20 0.20 . 5 . . . . . . . . 4374 1 756 . 1 1 72 72 ARG CG C 13 27.00 0.40 . 5 . . . . . . . . 4374 1 757 . 1 1 72 72 ARG HA H 1 4.20 0.03 . 1 . . . . . . . . 4374 1 758 . 1 1 72 72 ARG HB2 H 1 1.84 0.03 . 1 . . . . . . . . 4374 1 759 . 1 1 72 72 ARG HB3 H 1 1.84 0.03 . 1 . . . . . . . . 4374 1 760 . 1 1 72 72 ARG HD2 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 761 . 1 1 72 72 ARG HD3 H 1 3.16 0.03 . 5 . . . . . . . . 4374 1 762 . 1 1 72 72 ARG HG2 H 1 1.58 0.03 . 1 . . . . . . . . 4374 1 763 . 1 1 72 72 ARG HG3 H 1 1.58 0.03 . 1 . . . . . . . . 4374 1 764 . 1 1 72 72 ARG H H 1 8.24 0.01 . 1 . . . . . . . . 4374 1 765 . 1 1 72 72 ARG N N 15 120.84 0.10 . 1 . . . . . . . . 4374 1 766 . 1 1 73 73 LEU C C 13 178.09 0.10 . 1 . . . . . . . . 4374 1 767 . 1 1 73 73 LEU CA C 13 56.08 0.10 . 1 . . . . . . . . 4374 1 768 . 1 1 73 73 LEU CB C 13 41.78 0.10 . 1 . . . . . . . . 4374 1 769 . 1 1 73 73 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 770 . 1 1 73 73 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 771 . 1 1 73 73 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 772 . 1 1 73 73 LEU HA H 1 4.20 0.03 . 1 . . . . . . . . 4374 1 773 . 1 1 73 73 LEU HB2 H 1 1.71 0.03 . 1 . . . . . . . . 4374 1 774 . 1 1 73 73 LEU HB3 H 1 1.71 0.03 . 1 . . . . . . . . 4374 1 775 . 1 1 73 73 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 776 . 1 1 73 73 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 777 . 1 1 73 73 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 778 . 1 1 73 73 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 779 . 1 1 73 73 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 780 . 1 1 73 73 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 781 . 1 1 73 73 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 782 . 1 1 73 73 LEU H H 1 8.30 0.01 . 1 . . . . . . . . 4374 1 783 . 1 1 73 73 LEU N N 15 121.32 0.10 . 1 . . . . . . . . 4374 1 784 . 1 1 74 74 ASN C C 13 175.58 0.10 . 1 . . . . . . . . 4374 1 785 . 1 1 74 74 ASN CA C 13 53.62 0.10 . 1 . . . . . . . . 4374 1 786 . 1 1 74 74 ASN CB C 13 38.73 0.10 . 1 . . . . . . . . 4374 1 787 . 1 1 74 74 ASN HA H 1 4.70 0.03 . 1 . . . . . . . . 4374 1 788 . 1 1 74 74 ASN HB2 H 1 2.81 0.03 . 1 . . . . . . . . 4374 1 789 . 1 1 74 74 ASN HB3 H 1 2.81 0.03 . 1 . . . . . . . . 4374 1 790 . 1 1 74 74 ASN H H 1 8.28 0.01 . 1 . . . . . . . . 4374 1 791 . 1 1 74 74 ASN N N 15 117.95 0.10 . 1 . . . . . . . . 4374 1 792 . 1 1 75 75 SER C C 13 174.89 0.10 . 1 . . . . . . . . 4374 1 793 . 1 1 75 75 SER CA C 13 58.79 0.10 . 1 . . . . . . . . 4374 1 794 . 1 1 75 75 SER CB C 13 63.64 0.10 . 1 . . . . . . . . 4374 1 795 . 1 1 75 75 SER HA H 1 4.41 0.03 . 1 . . . . . . . . 4374 1 796 . 1 1 75 75 SER HB2 H 1 3.91 0.03 . 1 . . . . . . . . 4374 1 797 . 1 1 75 75 SER HB3 H 1 3.91 0.03 . 1 . . . . . . . . 4374 1 798 . 1 1 75 75 SER H H 1 8.11 0.01 . 1 . . . . . . . . 4374 1 799 . 1 1 75 75 SER N N 15 115.71 0.10 . 1 . . . . . . . . 4374 1 800 . 1 1 76 76 ILE C C 13 176.20 0.10 . 1 . . . . . . . . 4374 1 801 . 1 1 76 76 ILE CA C 13 61.76 0.10 . 1 . . . . . . . . 4374 1 802 . 1 1 76 76 ILE CB C 13 38.51 0.10 . 1 . . . . . . . . 4374 1 803 . 1 1 76 76 ILE CD1 C 13 13.17 0.10 . 1 . . . . . . . . 4374 1 804 . 1 1 76 76 ILE CG1 C 13 27.35 0.10 . 1 . . . . . . . . 4374 1 805 . 1 1 76 76 ILE CG2 C 13 17.27 0.10 . 1 . . . . . . . . 4374 1 806 . 1 1 76 76 ILE HA H 1 4.11 0.03 . 1 . . . . . . . . 4374 1 807 . 1 1 76 76 ILE HB H 1 1.85 0.03 . 1 . . . . . . . . 4374 1 808 . 1 1 76 76 ILE HD11 H 1 0.85 0.03 . 1 . . . . . . . . 4374 1 809 . 1 1 76 76 ILE HD12 H 1 0.85 0.03 . 1 . . . . . . . . 4374 1 810 . 1 1 76 76 ILE HD13 H 1 0.85 0.03 . 1 . . . . . . . . 4374 1 811 . 1 1 76 76 ILE HG12 H 1 1.47 0.02 . 2 . . . . . . . . 4374 1 812 . 1 1 76 76 ILE HG13 H 1 1.16 0.02 . 2 . . . . . . . . 4374 1 813 . 1 1 76 76 ILE HG21 H 1 0.84 0.03 . 1 . . . . . . . . 4374 1 814 . 1 1 76 76 ILE HG22 H 1 0.84 0.03 . 1 . . . . . . . . 4374 1 815 . 1 1 76 76 ILE HG23 H 1 0.84 0.03 . 1 . . . . . . . . 4374 1 816 . 1 1 76 76 ILE H H 1 8.09 0.01 . 1 . . . . . . . . 4374 1 817 . 1 1 76 76 ILE N N 15 122.07 0.10 . 1 . . . . . . . . 4374 1 818 . 1 1 77 77 ASP C C 13 176.39 0.10 . 1 . . . . . . . . 4374 1 819 . 1 1 77 77 ASP CA C 13 54.40 0.10 . 1 . . . . . . . . 4374 1 820 . 1 1 77 77 ASP CB C 13 40.90 0.10 . 1 . . . . . . . . 4374 1 821 . 1 1 77 77 ASP HA H 1 4.54 0.03 . 1 . . . . . . . . 4374 1 822 . 1 1 77 77 ASP HB2 H 1 2.63 0.03 . 1 . . . . . . . . 4374 1 823 . 1 1 77 77 ASP HB3 H 1 2.63 0.03 . 1 . . . . . . . . 4374 1 824 . 1 1 77 77 ASP H H 1 8.32 0.01 . 1 . . . . . . . . 4374 1 825 . 1 1 77 77 ASP N N 15 122.84 0.10 . 1 . . . . . . . . 4374 1 826 . 1 1 78 78 HIS C C 13 175.01 0.10 . 1 . . . . . . . . 4374 1 827 . 1 1 78 78 HIS CA C 13 56.40 0.10 . 1 . . . . . . . . 4374 1 828 . 1 1 78 78 HIS CB C 13 29.70 0.10 . 1 . . . . . . . . 4374 1 829 . 1 1 78 78 HIS HA H 1 4.55 0.03 . 1 . . . . . . . . 4374 1 830 . 1 1 78 78 HIS HB2 H 1 3.16 0.03 . 1 . . . . . . . . 4374 1 831 . 1 1 78 78 HIS HB3 H 1 3.16 0.03 . 1 . . . . . . . . 4374 1 832 . 1 1 78 78 HIS H H 1 8.33 0.01 . 1 . . . . . . . . 4374 1 833 . 1 1 78 78 HIS N N 15 119.44 0.10 . 1 . . . . . . . . 4374 1 834 . 1 1 79 79 ASP C C 13 176.95 0.10 . 1 . . . . . . . . 4374 1 835 . 1 1 79 79 ASP CA C 13 54.64 0.10 . 1 . . . . . . . . 4374 1 836 . 1 1 79 79 ASP CB C 13 40.85 0.10 . 1 . . . . . . . . 4374 1 837 . 1 1 79 79 ASP HA H 1 4.55 0.03 . 1 . . . . . . . . 4374 1 838 . 1 1 79 79 ASP HB2 H 1 2.69 0.03 . 1 . . . . . . . . 4374 1 839 . 1 1 79 79 ASP HB3 H 1 2.69 0.03 . 1 . . . . . . . . 4374 1 840 . 1 1 79 79 ASP H H 1 8.47 0.01 . 1 . . . . . . . . 4374 1 841 . 1 1 79 79 ASP N N 15 120.85 0.10 . 1 . . . . . . . . 4374 1 842 . 1 1 80 80 MET C C 13 176.77 0.10 . 1 . . . . . . . . 4374 1 843 . 1 1 80 80 MET CA C 13 56.05 0.10 . 1 . . . . . . . . 4374 1 844 . 1 1 80 80 MET CB C 13 31.97 0.10 . 1 . . . . . . . . 4374 1 845 . 1 1 80 80 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 846 . 1 1 80 80 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 847 . 1 1 80 80 MET HA H 1 4.37 0.03 . 1 . . . . . . . . 4374 1 848 . 1 1 80 80 MET HB2 H 1 2.06 0.03 . 1 . . . . . . . . 4374 1 849 . 1 1 80 80 MET HB3 H 1 2.06 0.03 . 1 . . . . . . . . 4374 1 850 . 1 1 80 80 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 851 . 1 1 80 80 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 852 . 1 1 80 80 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 853 . 1 1 80 80 MET HG2 H 1 2.53 0.03 . 1 . . . . . . . . 4374 1 854 . 1 1 80 80 MET HG3 H 1 2.53 0.03 . 1 . . . . . . . . 4374 1 855 . 1 1 80 80 MET H H 1 8.43 0.01 . 1 . . . . . . . . 4374 1 856 . 1 1 80 80 MET N N 15 120.86 0.10 . 1 . . . . . . . . 4374 1 857 . 1 1 81 81 ASN C C 13 175.21 0.10 . 1 . . . . . . . . 4374 1 858 . 1 1 81 81 ASN CA C 13 53.65 0.10 . 1 . . . . . . . . 4374 1 859 . 1 1 81 81 ASN CB C 13 38.62 0.10 . 1 . . . . . . . . 4374 1 860 . 1 1 81 81 ASN HA H 1 4.66 0.03 . 1 . . . . . . . . 4374 1 861 . 1 1 81 81 ASN HB2 H 1 2.78 0.03 . 1 . . . . . . . . 4374 1 862 . 1 1 81 81 ASN HB3 H 1 2.78 0.03 . 1 . . . . . . . . 4374 1 863 . 1 1 81 81 ASN H H 1 8.49 0.01 . 1 . . . . . . . . 4374 1 864 . 1 1 81 81 ASN N N 15 118.38 0.10 . 1 . . . . . . . . 4374 1 865 . 1 1 82 82 ASN C C 13 175.11 0.10 . 1 . . . . . . . . 4374 1 866 . 1 1 82 82 ASN CA C 13 53.44 0.10 . 1 . . . . . . . . 4374 1 867 . 1 1 82 82 ASN CB C 13 38.53 0.10 . 1 . . . . . . . . 4374 1 868 . 1 1 82 82 ASN HA H 1 4.65 0.03 . 1 . . . . . . . . 4374 1 869 . 1 1 82 82 ASN HB2 H 1 2.73 0.03 . 1 . . . . . . . . 4374 1 870 . 1 1 82 82 ASN HB3 H 1 2.73 0.03 . 1 . . . . . . . . 4374 1 871 . 1 1 82 82 ASN H H 1 8.29 0.01 . 1 . . . . . . . . 4374 1 872 . 1 1 82 82 ASN N N 15 118.61 0.10 . 1 . . . . . . . . 4374 1 873 . 1 1 83 83 ASN C C 13 175.44 0.10 . 1 . . . . . . . . 4374 1 874 . 1 1 83 83 ASN CA C 13 53.37 0.10 . 1 . . . . . . . . 4374 1 875 . 1 1 83 83 ASN CB C 13 38.47 0.10 . 1 . . . . . . . . 4374 1 876 . 1 1 83 83 ASN HA H 1 4.63 0.03 . 1 . . . . . . . . 4374 1 877 . 1 1 83 83 ASN HB2 H 1 2.75 0.03 . 1 . . . . . . . . 4374 1 878 . 1 1 83 83 ASN HB3 H 1 2.75 0.03 . 1 . . . . . . . . 4374 1 879 . 1 1 83 83 ASN H H 1 8.40 0.01 . 1 . . . . . . . . 4374 1 880 . 1 1 83 83 ASN N N 15 118.87 0.10 . 1 . . . . . . . . 4374 1 881 . 1 1 84 84 LYS C C 13 176.60 0.10 . 1 . . . . . . . . 4374 1 882 . 1 1 84 84 LYS CA C 13 56.55 0.10 . 1 . . . . . . . . 4374 1 883 . 1 1 84 84 LYS CB C 13 32.58 0.10 . 1 . . . . . . . . 4374 1 884 . 1 1 84 84 LYS CD C 13 28.92 0.20 . 5 . . . . . . . . 4374 1 885 . 1 1 84 84 LYS CE C 13 40.15 0.20 . 5 . . . . . . . . 4374 1 886 . 1 1 84 84 LYS CG C 13 24.64 0.30 . 5 . . . . . . . . 4374 1 887 . 1 1 84 84 LYS HA H 1 4.18 0.03 . 1 . . . . . . . . 4374 1 888 . 1 1 84 84 LYS HB2 H 1 1.60 0.03 . 1 . . . . . . . . 4374 1 889 . 1 1 84 84 LYS HB3 H 1 1.60 0.03 . 1 . . . . . . . . 4374 1 890 . 1 1 84 84 LYS HD2 H 1 1.57 0.03 . 1 . . . . . . . . 4374 1 891 . 1 1 84 84 LYS HD3 H 1 1.57 0.03 . 1 . . . . . . . . 4374 1 892 . 1 1 84 84 LYS HE2 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 893 . 1 1 84 84 LYS HE3 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 894 . 1 1 84 84 LYS HG2 H 1 1.19 0.03 . 1 . . . . . . . . 4374 1 895 . 1 1 84 84 LYS HG3 H 1 1.19 0.03 . 1 . . . . . . . . 4374 1 896 . 1 1 84 84 LYS H H 1 8.25 0.01 . 1 . . . . . . . . 4374 1 897 . 1 1 84 84 LYS N N 15 121.10 0.10 . 1 . . . . . . . . 4374 1 898 . 1 1 85 85 PHE C C 13 176.53 0.10 . 1 . . . . . . . . 4374 1 899 . 1 1 85 85 PHE CA C 13 57.70 0.10 . 1 . . . . . . . . 4374 1 900 . 1 1 85 85 PHE CB C 13 39.28 0.10 . 1 . . . . . . . . 4374 1 901 . 1 1 85 85 PHE HA H 1 4.61 0.03 . 1 . . . . . . . . 4374 1 902 . 1 1 85 85 PHE HB2 H 1 3.22 0.03 . 1 . . . . . . . . 4374 1 903 . 1 1 85 85 PHE HB3 H 1 3.22 0.03 . 1 . . . . . . . . 4374 1 904 . 1 1 85 85 PHE HD1 H 1 7.27 0.03 . 1 . . . . . . . . 4374 1 905 . 1 1 85 85 PHE HD2 H 1 7.27 0.02 . 1 . . . . . . . . 4374 1 906 . 1 1 85 85 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 907 . 1 1 85 85 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 908 . 1 1 85 85 PHE H H 1 8.32 0.01 . 1 . . . . . . . . 4374 1 909 . 1 1 85 85 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 910 . 1 1 85 85 PHE N N 15 120.21 0.10 . 1 . . . . . . . . 4374 1 911 . 1 1 86 86 GLY C C 13 174.32 0.10 . 1 . . . . . . . . 4374 1 912 . 1 1 86 86 GLY CA C 13 45.22 0.10 . 1 . . . . . . . . 4374 1 913 . 1 1 86 86 GLY HA2 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 914 . 1 1 86 86 GLY HA3 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 915 . 1 1 86 86 GLY H H 1 8.40 0.01 . 1 . . . . . . . . 4374 1 916 . 1 1 86 86 GLY N N 15 110.54 0.10 . 1 . . . . . . . . 4374 1 917 . 1 1 87 87 SER C C 13 175.40 0.10 . 1 . . . . . . . . 4374 1 918 . 1 1 87 87 SER CA C 13 58.60 0.10 . 1 . . . . . . . . 4374 1 919 . 1 1 87 87 SER CB C 13 63.78 0.10 . 1 . . . . . . . . 4374 1 920 . 1 1 87 87 SER HA H 1 4.43 0.03 . 1 . . . . . . . . 4374 1 921 . 1 1 87 87 SER HB2 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 922 . 1 1 87 87 SER HB3 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 923 . 1 1 87 87 SER H H 1 8.42 0.01 . 1 . . . . . . . . 4374 1 924 . 1 1 87 87 SER N N 15 115.70 0.10 . 1 . . . . . . . . 4374 1 925 . 1 1 88 88 GLY C C 13 174.26 0.10 . 1 . . . . . . . . 4374 1 926 . 1 1 88 88 GLY CA C 13 45.29 0.10 . 1 . . . . . . . . 4374 1 927 . 1 1 88 88 GLY HA2 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 928 . 1 1 88 88 GLY HA3 H 1 3.94 0.03 . 1 . . . . . . . . 4374 1 929 . 1 1 88 88 GLY H H 1 8.64 0.01 . 1 . . . . . . . . 4374 1 930 . 1 1 88 88 GLY N N 15 111.08 0.10 . 1 . . . . . . . . 4374 1 931 . 1 1 89 89 GLU C C 13 176.70 0.10 . 1 . . . . . . . . 4374 1 932 . 1 1 89 89 GLU CA C 13 56.50 0.10 . 1 . . . . . . . . 4374 1 933 . 1 1 89 89 GLU CB C 13 30.15 0.10 . 1 . . . . . . . . 4374 1 934 . 1 1 89 89 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 935 . 1 1 89 89 GLU HA H 1 4.22 0.03 . 1 . . . . . . . . 4374 1 936 . 1 1 89 89 GLU HB2 H 1 1.97 0.03 . 1 . . . . . . . . 4374 1 937 . 1 1 89 89 GLU HB3 H 1 1.97 0.03 . 1 . . . . . . . . 4374 1 938 . 1 1 89 89 GLU HG2 H 1 2.23 0.03 . 1 . . . . . . . . 4374 1 939 . 1 1 89 89 GLU HG3 H 1 2.23 0.03 . 1 . . . . . . . . 4374 1 940 . 1 1 89 89 GLU H H 1 8.33 0.01 . 1 . . . . . . . . 4374 1 941 . 1 1 89 89 GLU N N 15 120.69 0.10 . 1 . . . . . . . . 4374 1 942 . 1 1 90 90 LEU C C 13 177.61 0.10 . 1 . . . . . . . . 4374 1 943 . 1 1 90 90 LEU CA C 13 55.33 0.10 . 1 . . . . . . . . 4374 1 944 . 1 1 90 90 LEU CB C 13 41.96 0.10 . 1 . . . . . . . . 4374 1 945 . 1 1 90 90 LEU CD1 C 13 24.80 0.30 . 2 . . . . . . . . 4374 1 946 . 1 1 90 90 LEU CD2 C 13 23.48 0.30 . 2 . . . . . . . . 4374 1 947 . 1 1 90 90 LEU CG C 13 27.00 0.30 . 5 . . . . . . . . 4374 1 948 . 1 1 90 90 LEU HA H 1 4.29 0.03 . 1 . . . . . . . . 4374 1 949 . 1 1 90 90 LEU HB2 H 1 1.62 0.03 . 1 . . . . . . . . 4374 1 950 . 1 1 90 90 LEU HB3 H 1 1.62 0.03 . 1 . . . . . . . . 4374 1 951 . 1 1 90 90 LEU HD11 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 952 . 1 1 90 90 LEU HD12 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 953 . 1 1 90 90 LEU HD13 H 1 0.91 0.03 . 2 . . . . . . . . 4374 1 954 . 1 1 90 90 LEU HD21 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 955 . 1 1 90 90 LEU HD22 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 956 . 1 1 90 90 LEU HD23 H 1 0.84 0.03 . 2 . . . . . . . . 4374 1 957 . 1 1 90 90 LEU HG H 1 1.60 0.05 . 5 . . . . . . . . 4374 1 958 . 1 1 90 90 LEU H H 1 8.39 0.01 . 1 . . . . . . . . 4374 1 959 . 1 1 90 90 LEU N N 15 123.26 0.10 . 1 . . . . . . . . 4374 1 960 . 1 1 91 91 LYS C C 13 176.74 0.10 . 1 . . . . . . . . 4374 1 961 . 1 1 91 91 LYS CA C 13 56.38 0.10 . 1 . . . . . . . . 4374 1 962 . 1 1 91 91 LYS CB C 13 32.78 0.10 . 1 . . . . . . . . 4374 1 963 . 1 1 91 91 LYS CD C 13 28.99 0.20 . 5 . . . . . . . . 4374 1 964 . 1 1 91 91 LYS CE C 13 40.15 0.20 . 5 . . . . . . . . 4374 1 965 . 1 1 91 91 LYS CG C 13 24.64 0.30 . 5 . . . . . . . . 4374 1 966 . 1 1 91 91 LYS HA H 1 4.26 0.03 . 1 . . . . . . . . 4374 1 967 . 1 1 91 91 LYS HB2 H 1 1.77 0.03 . 1 . . . . . . . . 4374 1 968 . 1 1 91 91 LYS HB3 H 1 1.77 0.03 . 1 . . . . . . . . 4374 1 969 . 1 1 91 91 LYS HD2 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 970 . 1 1 91 91 LYS HD3 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 971 . 1 1 91 91 LYS HE2 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 972 . 1 1 91 91 LYS HE3 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 973 . 1 1 91 91 LYS HG2 H 1 1.38 0.03 . 1 . . . . . . . . 4374 1 974 . 1 1 91 91 LYS HG3 H 1 1.38 0.03 . 1 . . . . . . . . 4374 1 975 . 1 1 91 91 LYS H H 1 8.39 0.01 . 1 . . . . . . . . 4374 1 976 . 1 1 91 91 LYS N N 15 122.10 0.10 . 1 . . . . . . . . 4374 1 977 . 1 1 92 92 SER C C 13 174.86 0.10 . 1 . . . . . . . . 4374 1 978 . 1 1 92 92 SER CA C 13 58.28 0.10 . 1 . . . . . . . . 4374 1 979 . 1 1 92 92 SER CB C 13 63.68 0.10 . 1 . . . . . . . . 4374 1 980 . 1 1 92 92 SER HA H 1 4.37 0.03 . 1 . . . . . . . . 4374 1 981 . 1 1 92 92 SER HB2 H 1 3.83 0.03 . 1 . . . . . . . . 4374 1 982 . 1 1 92 92 SER HB3 H 1 3.83 0.03 . 1 . . . . . . . . 4374 1 983 . 1 1 92 92 SER H H 1 8.35 0.01 . 1 . . . . . . . . 4374 1 984 . 1 1 92 92 SER N N 15 116.37 0.10 . 1 . . . . . . . . 4374 1 985 . 1 1 93 93 MET C C 13 176.19 0.10 . 1 . . . . . . . . 4374 1 986 . 1 1 93 93 MET CA C 13 55.59 0.10 . 1 . . . . . . . . 4374 1 987 . 1 1 93 93 MET CB C 13 32.32 0.10 . 1 . . . . . . . . 4374 1 988 . 1 1 93 93 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 989 . 1 1 93 93 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 990 . 1 1 93 93 MET HA H 1 4.39 0.03 . 1 . . . . . . . . 4374 1 991 . 1 1 93 93 MET HB2 H 1 1.95 0.03 . 1 . . . . . . . . 4374 1 992 . 1 1 93 93 MET HB3 H 1 1.95 0.03 . 1 . . . . . . . . 4374 1 993 . 1 1 93 93 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 994 . 1 1 93 93 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 995 . 1 1 93 93 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 996 . 1 1 93 93 MET HG2 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 997 . 1 1 93 93 MET HG3 H 1 2.36 0.03 . 1 . . . . . . . . 4374 1 998 . 1 1 93 93 MET H H 1 8.41 0.01 . 1 . . . . . . . . 4374 1 999 . 1 1 93 93 MET N N 15 121.87 0.10 . 1 . . . . . . . . 4374 1 1000 . 1 1 94 94 PHE C C 13 175.61 0.10 . 1 . . . . . . . . 4374 1 1001 . 1 1 94 94 PHE CA C 13 57.74 0.10 . 1 . . . . . . . . 4374 1 1002 . 1 1 94 94 PHE CB C 13 39.39 0.10 . 1 . . . . . . . . 4374 1 1003 . 1 1 94 94 PHE HA H 1 4.58 0.03 . 1 . . . . . . . . 4374 1 1004 . 1 1 94 94 PHE HB2 H 1 3.12 0.03 . 1 . . . . . . . . 4374 1 1005 . 1 1 94 94 PHE HB3 H 1 3.12 0.03 . 1 . . . . . . . . 4374 1 1006 . 1 1 94 94 PHE HD1 H 1 7.27 0.03 . 1 . . . . . . . . 4374 1 1007 . 1 1 94 94 PHE HD2 H 1 7.27 0.02 . 1 . . . . . . . . 4374 1 1008 . 1 1 94 94 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 1009 . 1 1 94 94 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . 4374 1 1010 . 1 1 94 94 PHE H H 1 8.25 0.01 . 1 . . . . . . . . 4374 1 1011 . 1 1 94 94 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 1012 . 1 1 94 94 PHE N N 15 120.46 0.10 . 1 . . . . . . . . 4374 1 1013 . 1 1 95 95 ASN C C 13 175.03 0.10 . 1 . . . . . . . . 4374 1 1014 . 1 1 95 95 ASN CA C 13 53.06 0.10 . 1 . . . . . . . . 4374 1 1015 . 1 1 95 95 ASN CB C 13 38.61 0.10 . 1 . . . . . . . . 4374 1 1016 . 1 1 95 95 ASN HA H 1 4.60 0.03 . 1 . . . . . . . . 4374 1 1017 . 1 1 95 95 ASN HB2 H 1 2.77 0.03 . 2 . . . . . . . . 4374 1 1018 . 1 1 95 95 ASN HB3 H 1 2.67 0.03 . 2 . . . . . . . . 4374 1 1019 . 1 1 95 95 ASN H H 1 8.43 0.01 . 1 . . . . . . . . 4374 1 1020 . 1 1 95 95 ASN N N 15 120.46 0.10 . 1 . . . . . . . . 4374 1 1021 . 1 1 96 96 GLN C C 13 176.38 0.10 . 1 . . . . . . . . 4374 1 1022 . 1 1 96 96 GLN CA C 13 56.06 0.10 . 1 . . . . . . . . 4374 1 1023 . 1 1 96 96 GLN CB C 13 29.11 0.10 . 1 . . . . . . . . 4374 1 1024 . 1 1 96 96 GLN CG C 13 33.66 0.50 . 5 . . . . . . . . 4374 1 1025 . 1 1 96 96 GLN HA H 1 4.21 0.03 . 1 . . . . . . . . 4374 1 1026 . 1 1 96 96 GLN HB2 H 1 1.86 0.03 . 1 . . . . . . . . 4374 1 1027 . 1 1 96 96 GLN HB3 H 1 1.86 0.03 . 1 . . . . . . . . 4374 1 1028 . 1 1 96 96 GLN HG2 H 1 2.25 0.03 . 1 . . . . . . . . 4374 1 1029 . 1 1 96 96 GLN HG3 H 1 2.25 0.03 . 1 . . . . . . . . 4374 1 1030 . 1 1 96 96 GLN H H 1 8.41 0.01 . 1 . . . . . . . . 4374 1 1031 . 1 1 96 96 GLN N N 15 120.30 0.10 . 1 . . . . . . . . 4374 1 1032 . 1 1 97 97 GLY C C 13 173.70 0.10 . 1 . . . . . . . . 4374 1 1033 . 1 1 97 97 GLY CA C 13 45.06 0.10 . 1 . . . . . . . . 4374 1 1034 . 1 1 97 97 GLY HA2 H 1 3.91 0.03 . 1 . . . . . . . . 4374 1 1035 . 1 1 97 97 GLY HA3 H 1 3.91 0.03 . 1 . . . . . . . . 4374 1 1036 . 1 1 97 97 GLY H H 1 8.47 0.01 . 1 . . . . . . . . 4374 1 1037 . 1 1 97 97 GLY N N 15 109.69 0.10 . 1 . . . . . . . . 4374 1 1038 . 1 1 98 98 LYS C C 13 176.61 0.10 . 1 . . . . . . . . 4374 1 1039 . 1 1 98 98 LYS CA C 13 55.94 0.10 . 1 . . . . . . . . 4374 1 1040 . 1 1 98 98 LYS CB C 13 33.11 0.10 . 1 . . . . . . . . 4374 1 1041 . 1 1 98 98 LYS CD C 13 28.99 0.20 . 5 . . . . . . . . 4374 1 1042 . 1 1 98 98 LYS CE C 13 40.15 0.20 . 5 . . . . . . . . 4374 1 1043 . 1 1 98 98 LYS CG C 13 24.64 0.30 . 5 . . . . . . . . 4374 1 1044 . 1 1 98 98 LYS HA H 1 4.34 0.03 . 1 . . . . . . . . 4374 1 1045 . 1 1 98 98 LYS HB2 H 1 1.74 0.03 . 1 . . . . . . . . 4374 1 1046 . 1 1 98 98 LYS HB3 H 1 1.74 0.03 . 1 . . . . . . . . 4374 1 1047 . 1 1 98 98 LYS HD2 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 1048 . 1 1 98 98 LYS HD3 H 1 1.64 0.03 . 1 . . . . . . . . 4374 1 1049 . 1 1 98 98 LYS HE2 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 1050 . 1 1 98 98 LYS HE3 H 1 3.10 0.05 . 5 . . . . . . . . 4374 1 1051 . 1 1 98 98 LYS HG2 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 1052 . 1 1 98 98 LYS HG3 H 1 1.36 0.03 . 1 . . . . . . . . 4374 1 1053 . 1 1 98 98 LYS H H 1 8.17 0.01 . 1 . . . . . . . . 4374 1 1054 . 1 1 98 98 LYS N N 15 121.21 0.10 . 1 . . . . . . . . 4374 1 1055 . 1 1 99 99 VAL C C 13 176.29 0.10 . 1 . . . . . . . . 4374 1 1056 . 1 1 99 99 VAL CA C 13 62.46 0.10 . 1 . . . . . . . . 4374 1 1057 . 1 1 99 99 VAL CB C 13 32.56 0.10 . 1 . . . . . . . . 4374 1 1058 . 1 1 99 99 VAL CG1 C 13 21.07 0.20 . 2 . . . . . . . . 4374 1 1059 . 1 1 99 99 VAL CG2 C 13 20.41 0.20 . 2 . . . . . . . . 4374 1 1060 . 1 1 99 99 VAL HA H 1 4.07 0.03 . 1 . . . . . . . . 4374 1 1061 . 1 1 99 99 VAL HB H 1 2.05 0.03 . 1 . . . . . . . . 4374 1 1062 . 1 1 99 99 VAL HG11 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 1063 . 1 1 99 99 VAL HG12 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 1064 . 1 1 99 99 VAL HG13 H 1 0.92 0.02 . 2 . . . . . . . . 4374 1 1065 . 1 1 99 99 VAL HG21 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 1066 . 1 1 99 99 VAL HG22 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 1067 . 1 1 99 99 VAL HG23 H 1 0.93 0.02 . 2 . . . . . . . . 4374 1 1068 . 1 1 99 99 VAL H H 1 8.42 0.01 . 1 . . . . . . . . 4374 1 1069 . 1 1 99 99 VAL N N 15 123.17 0.10 . 1 . . . . . . . . 4374 1 1070 . 1 1 100 100 GLU C C 13 176.31 0.10 . 1 . . . . . . . . 4374 1 1071 . 1 1 100 100 GLU CA C 13 56.36 0.10 . 1 . . . . . . . . 4374 1 1072 . 1 1 100 100 GLU CB C 13 30.09 0.10 . 1 . . . . . . . . 4374 1 1073 . 1 1 100 100 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 1074 . 1 1 100 100 GLU HA H 1 4.26 0.03 . 1 . . . . . . . . 4374 1 1075 . 1 1 100 100 GLU HB2 H 1 2.02 0.03 . 2 . . . . . . . . 4374 1 1076 . 1 1 100 100 GLU HB3 H 1 1.89 0.03 . 2 . . . . . . . . 4374 1 1077 . 1 1 100 100 GLU HG2 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 1078 . 1 1 100 100 GLU HG3 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 1079 . 1 1 100 100 GLU H H 1 8.70 0.01 . 1 . . . . . . . . 4374 1 1080 . 1 1 100 100 GLU N N 15 124.95 0.10 . 1 . . . . . . . . 4374 1 1081 . 1 1 101 101 GLU C C 13 176.31 0.10 . 1 . . . . . . . . 4374 1 1082 . 1 1 101 101 GLU CA C 13 56.41 0.10 . 1 . . . . . . . . 4374 1 1083 . 1 1 101 101 GLU CB C 13 30.13 0.10 . 1 . . . . . . . . 4374 1 1084 . 1 1 101 101 GLU CG C 13 36.18 0.50 . 5 . . . . . . . . 4374 1 1085 . 1 1 101 101 GLU HA H 1 4.22 0.03 . 1 . . . . . . . . 4374 1 1086 . 1 1 101 101 GLU HB2 H 1 2.00 0.03 . 2 . . . . . . . . 4374 1 1087 . 1 1 101 101 GLU HB3 H 1 1.91 0.03 . 2 . . . . . . . . 4374 1 1088 . 1 1 101 101 GLU HG2 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 1089 . 1 1 101 101 GLU HG3 H 1 2.24 0.03 . 1 . . . . . . . . 4374 1 1090 . 1 1 101 101 GLU H H 1 8.53 0.01 . 1 . . . . . . . . 4374 1 1091 . 1 1 101 101 GLU N N 15 122.11 0.10 . 1 . . . . . . . . 4374 1 1092 . 1 1 102 102 MET C C 13 175.60 0.10 . 1 . . . . . . . . 4374 1 1093 . 1 1 102 102 MET CA C 13 55.09 0.10 . 1 . . . . . . . . 4374 1 1094 . 1 1 102 102 MET CB C 13 33.06 0.10 . 1 . . . . . . . . 4374 1 1095 . 1 1 102 102 MET CE C 13 16.85 0.30 . 5 . . . . . . . . 4374 1 1096 . 1 1 102 102 MET CG C 13 31.93 0.30 . 5 . . . . . . . . 4374 1 1097 . 1 1 102 102 MET HA H 1 4.45 0.03 . 1 . . . . . . . . 4374 1 1098 . 1 1 102 102 MET HB2 H 1 1.94 0.03 . 1 . . . . . . . . 4374 1 1099 . 1 1 102 102 MET HB3 H 1 1.94 0.03 . 1 . . . . . . . . 4374 1 1100 . 1 1 102 102 MET HE1 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 1101 . 1 1 102 102 MET HE2 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 1102 . 1 1 102 102 MET HE3 H 1 2.07 0.03 . 5 . . . . . . . . 4374 1 1103 . 1 1 102 102 MET HG2 H 1 2.48 0.03 . 1 . . . . . . . . 4374 1 1104 . 1 1 102 102 MET HG3 H 1 2.48 0.03 . 1 . . . . . . . . 4374 1 1105 . 1 1 102 102 MET H H 1 8.43 0.01 . 1 . . . . . . . . 4374 1 1106 . 1 1 102 102 MET N N 15 121.09 0.10 . 1 . . . . . . . . 4374 1 1107 . 1 1 103 103 ASP C C 13 174.72 0.10 . 1 . . . . . . . . 4374 1 1108 . 1 1 103 103 ASP CA C 13 54.11 0.10 . 1 . . . . . . . . 4374 1 1109 . 1 1 103 103 ASP CB C 13 41.00 0.10 . 1 . . . . . . . . 4374 1 1110 . 1 1 103 103 ASP HA H 1 4.59 0.03 . 1 . . . . . . . . 4374 1 1111 . 1 1 103 103 ASP HB2 H 1 2.54 0.03 . 1 . . . . . . . . 4374 1 1112 . 1 1 103 103 ASP HB3 H 1 2.54 0.03 . 1 . . . . . . . . 4374 1 1113 . 1 1 103 103 ASP H H 1 8.36 0.01 . 1 . . . . . . . . 4374 1 1114 . 1 1 103 103 ASP N N 15 121.77 0.10 . 1 . . . . . . . . 4374 1 1115 . 1 1 104 104 PHE CA C 13 58.90 0.10 . 1 . . . . . . . . 4374 1 1116 . 1 1 104 104 PHE CB C 13 40.21 0.10 . 1 . . . . . . . . 4374 1 1117 . 1 1 104 104 PHE HA H 1 4.40 0.03 . 1 . . . . . . . . 4374 1 1118 . 1 1 104 104 PHE HB2 H 1 3.14 0.03 . 2 . . . . . . . . 4374 1 1119 . 1 1 104 104 PHE HB3 H 1 3.00 0.03 . 2 . . . . . . . . 4374 1 1120 . 1 1 104 104 PHE HD1 H 1 7.11 0.02 . 1 . . . . . . . . 4374 1 1121 . 1 1 104 104 PHE HD2 H 1 7.11 0.02 . 1 . . . . . . . . 4374 1 1122 . 1 1 104 104 PHE HE1 H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 1123 . 1 1 104 104 PHE HE2 H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 1124 . 1 1 104 104 PHE H H 1 7.68 0.01 . 1 . . . . . . . . 4374 1 1125 . 1 1 104 104 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . 4374 1 1126 . 1 1 104 104 PHE N N 15 124.74 0.10 . 1 . . . . . . . . 4374 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 195 4374 1 1 196 4374 1 2 201 4374 1 2 202 4374 1 2 203 4374 1 2 204 4374 1 2 205 4374 1 2 206 4374 1 3 238 4374 1 3 239 4374 1 4 242 4374 1 4 243 4374 1 4 244 4374 1 4 245 4374 1 4 246 4374 1 4 247 4374 1 5 339 4374 1 5 340 4374 1 6 343 4374 1 6 344 4374 1 6 345 4374 1 6 346 4374 1 6 347 4374 1 6 348 4374 1 7 362 4374 1 7 363 4374 1 8 368 4374 1 8 369 4374 1 8 370 4374 1 8 371 4374 1 8 372 4374 1 8 373 4374 1 9 426 4374 1 9 427 4374 1 10 430 4374 1 10 431 4374 1 10 432 4374 1 10 433 4374 1 10 434 4374 1 10 435 4374 1 11 463 4374 1 11 464 4374 1 12 469 4374 1 12 470 4374 1 12 471 4374 1 12 472 4374 1 12 473 4374 1 12 474 4374 1 13 475 4374 1 13 476 4374 1 14 623 4374 1 14 624 4374 1 15 629 4374 1 15 630 4374 1 15 631 4374 1 15 632 4374 1 15 633 4374 1 15 634 4374 1 16 715 4374 1 16 716 4374 1 17 721 4374 1 17 722 4374 1 17 723 4374 1 17 724 4374 1 17 725 4374 1 17 726 4374 1 18 769 4374 1 18 770 4374 1 19 775 4374 1 19 776 4374 1 19 777 4374 1 19 778 4374 1 19 779 4374 1 19 780 4374 1 20 811 4374 1 20 812 4374 1 21 945 4374 1 21 946 4374 1 22 951 4374 1 22 952 4374 1 22 953 4374 1 22 954 4374 1 22 955 4374 1 22 956 4374 1 23 1017 4374 1 23 1018 4374 1 24 1058 4374 1 24 1059 4374 1 25 1062 4374 1 25 1063 4374 1 25 1064 4374 1 25 1065 4374 1 25 1066 4374 1 25 1067 4374 1 26 1075 4374 1 26 1076 4374 1 27 1118 4374 1 27 1119 4374 1 28 4 4374 1 28 25 4374 1 28 88 4374 1 28 117 4374 1 28 128 4374 1 28 139 4374 1 28 150 4374 1 28 500 4374 1 28 1024 4374 1 29 136 4374 1 29 147 4374 1 30 137 4374 1 30 148 4374 1 31 138 4374 1 31 149 4374 1 32 140 4374 1 32 151 4374 1 33 141 4374 1 33 142 4374 1 33 152 4374 1 33 153 4374 1 34 143 4374 1 34 144 4374 1 34 154 4374 1 34 155 4374 1 35 145 4374 1 35 156 4374 1 36 146 4374 1 36 157 4374 1 37 169 4374 1 37 354 4374 1 37 378 4374 1 37 385 4374 1 37 441 4374 1 38 170 4374 1 38 386 4374 1 39 171 4374 1 39 172 4374 1 39 380 4374 1 39 381 4374 1 39 387 4374 1 39 388 4374 1 39 443 4374 1 39 444 4374 1 40 184 4374 1 40 227 4374 1 40 253 4374 1 40 489 4374 1 41 197 4374 1 41 364 4374 1 41 465 4374 1 41 625 4374 1 41 717 4374 1 41 771 4374 1 41 947 4374 1 42 207 4374 1 42 374 4374 1 42 475 4374 1 42 635 4374 1 42 727 4374 1 42 781 4374 1 42 957 4374 1 43 213 4374 1 43 312 4374 1 43 326 4374 1 43 755 4374 1 44 214 4374 1 44 313 4374 1 44 327 4374 1 44 756 4374 1 45 218 4374 1 45 219 4374 1 45 317 4374 1 45 318 4374 1 45 331 4374 1 45 332 4374 1 45 760 4374 1 45 761 4374 1 46 264 4374 1 46 392 4374 1 46 448 4374 1 46 527 4374 1 46 650 4374 1 46 845 4374 1 46 988 4374 1 46 1095 4374 1 47 265 4374 1 47 393 4374 1 47 449 4374 1 47 528 4374 1 47 651 4374 1 47 846 4374 1 47 989 4374 1 47 1096 4374 1 48 269 4374 1 48 270 4374 1 48 271 4374 1 48 397 4374 1 48 398 4374 1 48 399 4374 1 48 453 4374 1 48 454 4374 1 48 455 4374 1 48 532 4374 1 48 533 4374 1 48 534 4374 1 48 655 4374 1 48 656 4374 1 48 657 4374 1 48 850 4374 1 48 851 4374 1 48 852 4374 1 48 993 4374 1 48 994 4374 1 48 995 4374 1 48 1100 4374 1 48 1101 4374 1 48 1102 4374 1 49 288 4374 1 49 416 4374 1 49 641 4374 1 49 679 4374 1 49 733 4374 1 49 744 4374 1 49 934 4374 1 49 1073 4374 1 49 1084 4374 1 50 356 4374 1 50 357 4374 1 50 358 4374 1 50 359 4374 1 51 690 4374 1 51 884 4374 1 51 963 4374 1 51 1041 4374 1 52 691 4374 1 52 885 4374 1 52 964 4374 1 52 1042 4374 1 53 692 4374 1 53 886 4374 1 53 965 4374 1 53 1043 4374 1 54 698 4374 1 54 699 4374 1 54 892 4374 1 54 893 4374 1 54 971 4374 1 54 972 4374 1 54 1049 4374 1 54 1050 4374 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_label _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode coupling_constants_label _Coupling_constant_list.Entry_ID 4374 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $conditions_1 _Coupling_constant_list.Spectrometer_frequency_1H . _Coupling_constant_list.Details ; # about the data. Quantitative coupling constants 3J(HNHalpha) (Hz) as measured by a 3D HNHA experiment on the [U-15N] labeled sample. Software used: UXNMR (processing), XEASY (analysis, peak integration) Remarks: - For Gly52,Gly86,Gly88 and Gly97 the average value 3JHNHA for both the overlapping HA2 and HA3 signals (indicated by HA*) is given. - Gln17 and Gln18 have near-identical HN, N and HA resonance frequencies. 3JHNHA of Gln17 and Gln18 are therefore indistinguishable from one another. The average value for both residues is listed instead. - 3JHNHA of residues Met1 and Gln2 are not given, because of missing amide proton signals in the proton dimension of the 3D HNHA spectrum. - In the case of overlapping diagonal peaks in the HNHA spectrum, an average intensity for the reference diagonal peak was taken as best approximation. - For residues 95,97-104 the 3J(HNHalpha) coupling constant was determined directly by taking slices through the amide proton signals from a high-resolution 15N-1H HSQC, recorded on the [U-15N]-labeled sample. - Comparison of the 3JHNHA values derived directly and calculated from the HNHA measurement show on average an absolute error of about 0.5 Hz in the determination of the 3JHNHA coupling constant. ; _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_one . 4374 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 3 3 ASN H . . . . 1 1 3 3 ASN HA . . . 6.53 . . 0.5 . . . . . . . . . . . 4374 1 2 3JHNHA . 1 1 4 4 SER H . . . . 1 1 4 4 SER HA . . . 4.88 . . 0.5 . . . . . . . . . . . 4374 1 3 3JHNHA . 1 1 5 5 GLN H . . . . 1 1 5 5 GLN HA . . . 6.79 . . 0.5 . . . . . . . . . . . 4374 1 4 3JHNHA . 1 1 6 6 ASP H . . . . 1 1 6 6 ASP HA . . . 6.17 . . 0.5 . . . . . . . . . . . 4374 1 5 3JHNHA . 1 1 7 7 TYR H . . . . 1 1 7 7 TYR HA . . . 6.22 . . 0.5 . . . . . . . . . . . 4374 1 6 3JHNHA . 1 1 8 8 PHE H . . . . 1 1 8 8 PHE HA . . . 5.99 . . 0.5 . . . . . . . . . . . 4374 1 7 3JHNHA . 1 1 9 9 TYR H . . . . 1 1 9 9 TYR HA . . . 6.21 . . 0.5 . . . . . . . . . . . 4374 1 8 3JHNHA . 1 1 10 10 ALA H . . . . 1 1 10 10 ALA HA . . . 5.17 . . 0.5 . . . . . . . . . . . 4374 1 9 3JHNHA . 1 1 11 11 GLN H . . . . 1 1 11 11 GLN HA . . . 5.94 . . 1.0 . . . . . . . . . . . 4374 1 10 3JHNHA . 1 1 12 12 ASN H . . . . 1 1 12 12 ASN HA . . . 7.82 . . 1.0 . . . . . . . . . . . 4374 1 11 3JHNHA . 1 1 13 13 ARG H . . . . 1 1 13 13 ARG HA . . . 6.87 . . 0.5 . . . . . . . . . . . 4374 1 12 3JHNHA . 1 1 14 14 CYS H . . . . 1 1 14 14 CYS HA . . . 4.35 . . 0.5 . . . . . . . . . . . 4374 1 13 3JHNHA . 1 1 15 15 GLN H . . . . 1 1 15 15 GLN HA . . . 6.01 . . 0.5 . . . . . . . . . . . 4374 1 14 3JHNHA . 1 1 16 16 GLN H . . . . 1 1 16 16 GLN HA . . . 6.16 . . 0.5 . . . . . . . . . . . 4374 1 15 3JHNHA . 1 1 17 17 GLN H . . . . 1 1 17 17 GLN HA . . . 7.23 . . 0.5 . . . . . . . . . . . 4374 1 16 3JHNHA . 1 1 18 18 GLN H . . . . 1 1 18 18 GLN HA . . . 7.23 . . 0.5 . . . . . . . . . . . 4374 1 17 3JHNHA . 1 1 19 19 ALA H . . . . 1 1 19 19 ALA HA . . . 5.01 . . 0.5 . . . . . . . . . . . 4374 1 18 3JHNHA . 1 1 21 21 SER H . . . . 1 1 21 21 SER HA . . . 6.32 . . 0.5 . . . . . . . . . . . 4374 1 19 3JHNHA . 1 1 22 22 THR H . . . . 1 1 22 22 THR HA . . . 8.00 . . 0.5 . . . . . . . . . . . 4374 1 20 3JHNHA . 1 1 23 23 LEU H . . . . 1 1 23 23 LEU HA . . . 6.33 . . 0.5 . . . . . . . . . . . 4374 1 21 3JHNHA . 1 1 24 24 ARG H . . . . 1 1 24 24 ARG HA . . . 6.39 . . 0.5 . . . . . . . . . . . 4374 1 22 3JHNHA . 1 1 25 25 THR H . . . . 1 1 25 25 THR HA . . . 7.26 . . 0.5 . . . . . . . . . . . 4374 1 23 3JHNHA . 1 1 26 26 VAL H . . . . 1 1 26 26 VAL HA . . . 6.85 . . 0.5 . . . . . . . . . . . 4374 1 24 3JHNHA . 1 1 27 27 THR H . . . . 1 1 27 27 THR HA . . . 7.44 . . 0.5 . . . . . . . . . . . 4374 1 25 3JHNHA . 1 1 28 28 MET H . . . . 1 1 28 28 MET HA . . . 5.67 . . 0.5 . . . . . . . . . . . 4374 1 26 3JHNHA . 1 1 29 29 ALA H . . . . 1 1 29 29 ALA HA . . . 5.03 . . 0.5 . . . . . . . . . . . 4374 1 27 3JHNHA . 1 1 30 30 GLU H . . . . 1 1 30 30 GLU HA . . . 5.17 . . 0.5 . . . . . . . . . . . 4374 1 28 3JHNHA . 1 1 31 31 PHE H . . . . 1 1 31 31 PHE HA . . . 6.13 . . 0.5 . . . . . . . . . . . 4374 1 29 3JHNHA . 1 1 32 32 ARG H . . . . 1 1 32 32 ARG HA . . . 7.37 . . 0.5 . . . . . . . . . . . 4374 1 30 3JHNHA . 1 1 33 33 ARG H . . . . 1 1 33 33 ARG HA . . . 6.55 . . 0.5 . . . . . . . . . . . 4374 1 31 3JHNHA . 1 1 34 34 VAL H . . . . 1 1 34 34 VAL HA . . . 7.38 . . 0.5 . . . . . . . . . . . 4374 1 32 3JHNHA . 1 1 36 36 LEU H . . . . 1 1 36 36 LEU HA . . . 5.87 . . 0.5 . . . . . . . . . . . 4374 1 33 3JHNHA . 1 1 39 39 MET H . . . . 1 1 39 39 MET HA . . . 5.94 . . 0.5 . . . . . . . . . . . 4374 1 34 3JHNHA . 1 1 40 40 ALA H . . . . 1 1 40 40 ALA HA . . . 6.14 . . 0.5 . . . . . . . . . . . 4374 1 35 3JHNHA . 1 1 41 41 GLU H . . . . 1 1 41 41 GLU HA . . . 6.36 . . 0.5 . . . . . . . . . . . 4374 1 36 3JHNHA . 1 1 42 42 VAL H . . . . 1 1 42 42 VAL HA . . . 7.72 . . 0.5 . . . . . . . . . . . 4374 1 37 3JHNHA . 1 1 44 44 MET H . . . . 1 1 44 44 MET HA . . . 6.37 . . 0.5 . . . . . . . . . . . 4374 1 38 3JHNHA . 1 1 45 45 LEU H . . . . 1 1 45 45 LEU HA . . . 6.63 . . 0.5 . . . . . . . . . . . 4374 1 39 3JHNHA . 1 1 46 46 SER H . . . . 1 1 46 46 SER HA . . . 5.97 . . 0.5 . . . . . . . . . . . 4374 1 40 3JHNHA . 1 1 47 47 THR H . . . . 1 1 47 47 THR HA . . . 7.47 . . 0.5 . . . . . . . . . . . 4374 1 41 3JHNHA . 1 1 48 48 GLN H . . . . 1 1 48 48 GLN HA . . . 5.96 . . 0.5 . . . . . . . . . . . 4374 1 42 3JHNHA . 1 1 49 49 ASN H . . . . 1 1 49 49 ASN HA . . . 7.18 . . 0.5 . . . . . . . . . . . 4374 1 43 3JHNHA . 1 1 50 50 SER H . . . . 1 1 50 50 SER HA . . . 6.31 . . 0.5 . . . . . . . . . . . 4374 1 44 3JHNHA . 1 1 51 51 MET H . . . . 1 1 51 51 MET HA . . . 7.20 . . 0.5 . . . . . . . . . . . 4374 1 45 3JHNHA . 1 1 52 52 GLY H . . . . 1 1 52 52 GLY HA* . . . 5.17 . . 0.5 . . . . . . . . . . . 4374 1 46 3JHNHA . 1 1 53 53 SER H . . . . 1 1 53 53 SER HA . . . 6.55 . . 0.5 . . . . . . . . . . . 4374 1 47 3JHNHA . 1 1 54 54 SER H . . . . 1 1 54 54 SER HA . . . 6.09 . . 0.5 . . . . . . . . . . . 4374 1 48 3JHNHA . 1 1 55 55 ALA H . . . . 1 1 55 55 ALA HA . . . 5.48 . . 0.5 . . . . . . . . . . . 4374 1 49 3JHNHA . 1 1 56 56 SER H . . . . 1 1 56 56 SER HA . . . 6.65 . . 0.5 . . . . . . . . . . . 4374 1 50 3JHNHA . 1 1 57 57 ALA H . . . . 1 1 57 57 ALA HA . . . 5.94 . . 0.5 . . . . . . . . . . . 4374 1 51 3JHNHA . 1 1 58 58 SER H . . . . 1 1 58 58 SER HA . . . 6.38 . . 0.5 . . . . . . . . . . . 4374 1 52 3JHNHA . 1 1 59 59 ALA H . . . . 1 1 59 59 ALA HA . . . 5.71 . . 0.5 . . . . . . . . . . . 4374 1 53 3JHNHA . 1 1 60 60 SER H . . . . 1 1 60 60 SER HA . . . 6.20 . . 0.5 . . . . . . . . . . . 4374 1 54 3JHNHA . 1 1 61 61 SER H . . . . 1 1 61 61 SER HA . . . 6.29 . . 0.5 . . . . . . . . . . . 4374 1 55 3JHNHA . 1 1 62 62 LEU H . . . . 1 1 62 62 LEU HA . . . 5.78 . . 0.5 . . . . . . . . . . . 4374 1 56 3JHNHA . 1 1 63 63 GLU H . . . . 1 1 63 63 GLU HA . . . 5.84 . . 0.5 . . . . . . . . . . . 4374 1 57 3JHNHA . 1 1 64 64 MET H . . . . 1 1 64 64 MET HA . . . 6.55 . . 0.5 . . . . . . . . . . . 4374 1 58 3JHNHA . 1 1 65 65 TRP H . . . . 1 1 65 65 TRP HA . . . 5.20 . . 0.5 . . . . . . . . . . . 4374 1 59 3JHNHA . 1 1 66 66 GLU H . . . . 1 1 66 66 GLU HA . . . 3.90 . . 0.5 . . . . . . . . . . . 4374 1 60 3JHNHA . 1 1 67 67 LYS H . . . . 1 1 67 67 LYS HA . . . 5.25 . . 0.5 . . . . . . . . . . . 4374 1 61 3JHNHA . 1 1 68 68 ASP H . . . . 1 1 68 68 ASP HA . . . 4.68 . . 0.5 . . . . . . . . . . . 4374 1 62 3JHNHA . 1 1 69 69 LEU H . . . . 1 1 69 69 LEU HA . . . 4.60 . . 0.5 . . . . . . . . . . . 4374 1 63 3JHNHA . 1 1 70 70 GLU H . . . . 1 1 70 70 GLU HA . . . 5.41 . . 0.5 . . . . . . . . . . . 4374 1 64 3JHNHA . 1 1 71 71 GLU H . . . . 1 1 71 71 GLU HA . . . 5.37 . . 0.5 . . . . . . . . . . . 4374 1 65 3JHNHA . 1 1 72 72 ARG H . . . . 1 1 72 72 ARG HA . . . 5.48 . . 0.5 . . . . . . . . . . . 4374 1 66 3JHNHA . 1 1 73 73 LEU H . . . . 1 1 73 73 LEU HA . . . 6.00 . . 0.5 . . . . . . . . . . . 4374 1 67 3JHNHA . 1 1 74 74 ASN H . . . . 1 1 74 74 ASN HA . . . 6.38 . . 0.5 . . . . . . . . . . . 4374 1 68 3JHNHA . 1 1 75 75 SER H . . . . 1 1 75 75 SER HA . . . 6.31 . . 0.5 . . . . . . . . . . . 4374 1 69 3JHNHA . 1 1 76 76 ILE H . . . . 1 1 76 76 ILE HA . . . 6.66 . . 0.5 . . . . . . . . . . . 4374 1 70 3JHNHA . 1 1 77 77 ASP H . . . . 1 1 77 77 ASP HA . . . 6.60 . . 0.5 . . . . . . . . . . . 4374 1 71 3JHNHA . 1 1 78 78 HIS H . . . . 1 1 78 78 HIS HA . . . 6.69 . . 0.5 . . . . . . . . . . . 4374 1 72 3JHNHA . 1 1 79 79 ASP H . . . . 1 1 79 79 ASP HA . . . 6.17 . . 0.5 . . . . . . . . . . . 4374 1 73 3JHNHA . 1 1 80 80 MET H . . . . 1 1 80 80 MET HA . . . 5.66 . . 0.5 . . . . . . . . . . . 4374 1 74 3JHNHA . 1 1 81 81 ASN H . . . . 1 1 81 81 ASN HA . . . 7.14 . . 0.5 . . . . . . . . . . . 4374 1 75 3JHNHA . 1 1 82 82 ASN H . . . . 1 1 82 82 ASN HA . . . 7.48 . . 0.5 . . . . . . . . . . . 4374 1 76 3JHNHA . 1 1 83 83 ASN H . . . . 1 1 83 83 ASN HA . . . 7.19 . . 0.5 . . . . . . . . . . . 4374 1 77 3JHNHA . 1 1 84 84 LYS H . . . . 1 1 84 84 LYS HA . . . 6.47 . . 0.5 . . . . . . . . . . . 4374 1 78 3JHNHA . 1 1 85 85 PHE H . . . . 1 1 85 85 PHE HA . . . 6.32 . . 0.5 . . . . . . . . . . . 4374 1 79 3JHNHA . 1 1 86 86 GLY H . . . . 1 1 86 86 GLY HA* . . . 7.36 . . 0.5 . . . . . . . . . . . 4374 1 80 3JHNHA . 1 1 87 87 SER H . . . . 1 1 87 87 SER HA . . . 6.22 . . 0.5 . . . . . . . . . . . 4374 1 81 3JHNHA . 1 1 88 88 GLY H . . . . 1 1 88 88 GLY HA* . . . 7.13 . . 0.5 . . . . . . . . . . . 4374 1 82 3JHNHA . 1 1 89 89 GLU H . . . . 1 1 89 89 GLU HA . . . 6.36 . . 0.5 . . . . . . . . . . . 4374 1 83 3JHNHA . 1 1 90 90 LEU H . . . . 1 1 90 90 LEU HA . . . 6.05 . . 0.5 . . . . . . . . . . . 4374 1 84 3JHNHA . 1 1 91 91 LYS H . . . . 1 1 91 91 LYS HA . . . 7.45 . . 0.5 . . . . . . . . . . . 4374 1 85 3JHNHA . 1 1 92 92 SER H . . . . 1 1 92 92 SER HA . . . 6.21 . . 0.5 . . . . . . . . . . . 4374 1 86 3JHNHA . 1 1 93 93 MET H . . . . 1 1 93 93 MET HA . . . 6.00 . . 0.5 . . . . . . . . . . . 4374 1 87 3JHNHA . 1 1 94 94 PHE H . . . . 1 1 94 94 PHE HA . . . 6.30 . . 0.5 . . . . . . . . . . . 4374 1 88 3JHNHA . 1 1 95 95 ASN H . . . . 1 1 95 95 ASN HA . . . 5.74 . . 0.5 . . . . . . . . . . . 4374 1 89 3JHNHA . 1 1 96 96 GLN H . . . . 1 1 96 96 GLN HA . . . 5.84 . . 0.5 . . . . . . . . . . . 4374 1 90 3JHNHA . 1 1 97 97 GLY H . . . . 1 1 97 97 GLY HA* . . . 7.44 . . 0.5 . . . . . . . . . . . 4374 1 91 3JHNHA . 1 1 98 98 LYS H . . . . 1 1 98 98 LYS HA . . . 6.80 . . 0.5 . . . . . . . . . . . 4374 1 92 3JHNHA . 1 1 99 99 VAL H . . . . 1 1 99 99 VAL HA . . . 7.35 . . 0.5 . . . . . . . . . . . 4374 1 93 3JHNHA . 1 1 100 100 GLU H . . . . 1 1 100 100 GLU HA . . . 6.30 . . 0.5 . . . . . . . . . . . 4374 1 94 3JHNHA . 1 1 101 101 GLU H . . . . 1 1 101 101 GLU HA . . . 6.96 . . 0.5 . . . . . . . . . . . 4374 1 95 3JHNHA . 1 1 102 102 MET H . . . . 1 1 102 102 MET HA . . . 7.48 . . 0.5 . . . . . . . . . . . 4374 1 96 3JHNHA . 1 1 103 103 ASP H . . . . 1 1 103 103 ASP HA . . . 7.62 . . 0.5 . . . . . . . . . . . 4374 1 97 3JHNHA . 1 1 104 104 PHE H . . . . 1 1 104 104 PHE HA . . . 7.93 . . 0.5 . . . . . . . . . . . 4374 1 stop_ save_