data_27574 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 27574 _Entry.Title ; human TGF-b2 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2018-08-11 _Entry.Accession_date 2018-08-11 _Entry.Last_release_date 2018-08-13 _Entry.Original_release_date 2018-08-13 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details 'Backbone and partial side chain assignments for human TGFb2' _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.ORCID _Entry_author.Entry_ID 1 Morkos Henen . . . . 27574 2 Pardeep Mahlawat . . . . 27574 3 Udayar Ilangovan . . . . 27574 4 Andrew Hinck . . . . 27574 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Hinck Group, Univ. Pittsburgh' . 27574 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 27574 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 383 27574 '15N chemical shifts' 92 27574 '1H chemical shifts' 499 27574 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 2 . . 2019-03-22 2018-01-01 update BMRB 'update entry citation' 27574 1 . . 2019-01-02 2018-01-01 original author 'original release' 27574 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1TFG . 27574 PDB 2TGI . 27574 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 27574 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 30598510 _Citation.Full_citation . _Citation.Title ; TGF-b2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-b and Inhibin-a ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 294 _Citation.Journal_issue 9 _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 3065 _Citation.Page_last 3080 _Citation.Year 2019 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Morkos Henen . . . . 27574 1 2 Pardeep Mahlawat . . . . 27574 1 3 Christian Zwieb . . . . 27574 1 4 Ravi Kodali . S. . . 27574 1 5 Ramsey Hanna . . . . 27574 1 6 Troy Krzysiak . C. . . 27574 1 7 Udayar Ilangovan . . . . 27574 1 8 Kristin Cano . E. . . 27574 1 9 Garrett Hinck . . . . 27574 1 10 Morkos Vonberg . . . . 27574 1 11 Megan McCabe . . . . 27574 1 12 Andrew Hinck . P. . . 27574 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'ILV methyl labeling' 27574 1 'cardiac development' 27574 1 'cell signaling' 27574 1 'cell surface receptor' 27574 1 endocrinology 27574 1 'nuclear magnetic resonance (NMR)' 27574 1 'transforming growth factor beta (TGF-b)' 27574 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 27574 _Assembly.ID 1 _Assembly.Name 'TGF-b2 homodimer' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds yes _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; TGF-b2 homodimer is formed by formation a single disulfide bond between Cys77 in each of the two component monomers. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'TGF-b2, chain 1' 1 $TGF-b2 A . yes native no no . . . 27574 1 2 'TGF-b2, chain 2' 1 $TGF-b2 B . yes native no no . . . 27574 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 77 77 SG . 2 . 1 CYS 77 77 SG . . . 77 CYS SG . . . 77 CYS SG 27574 1 2 disulfide single . 1 . 1 CYS 7 7 SG . 1 . 1 CYS 16 16 SG . . . 7 CYS SG . . . 16 CYS SG 27574 1 3 disulfide single . 1 . 1 CYS 15 15 SG . 1 . 1 CYS 78 78 SG . . . 15 CYS SG . . . 78 CYS SG 27574 1 4 disulfide single . 1 . 1 CYS 44 44 SG . 1 . 1 CYS 109 109 SG . . . 44 CYS SG . . . 109 CYS SG 27574 1 5 disulfide single . 1 . 1 CYS 48 48 SG . 1 . 1 CYS 111 111 SG . . . 48 CYS SG . . . 111 CYS SG 27574 1 6 disulfide single . 2 . 1 CYS 7 7 SG . 2 . 1 CYS 16 16 SG . . . 7 CYS SG . . . 16 CYS SG 27574 1 7 disulfide single . 2 . 1 CYS 15 15 SG . 2 . 1 CYS 78 78 SG . . . 15 CYS SG . . . 78 CYS SG 27574 1 8 disulfide single . 2 . 1 CYS 44 44 SG . 2 . 1 CYS 109 109 SG . . . 44 CYS SG . . . 109 CYS SG 27574 1 9 disulfide single . 2 . 1 CYS 48 48 SG . 2 . 1 CYS 111 111 SG . . . 48 CYS SG . . . 111 CYS SG 27574 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1tfg . . X-ray . . . 27574 1 yes PDB 2tgi . . X-ray . . . 27574 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Binds TGF-b receptors, TbRI and TbRII' 27574 1 'Cell signaling' 27574 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TGF-b2 _Entity.Sf_category entity _Entity.Sf_framecode TGF-b2 _Entity.Entry_ID 27574 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name TGF-b2 _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 ; ALDAAYCFRNVQDNCCLRPL YIDFKRDLGWKWIHEPKGYN ANFCAGACPYLWSSDTQHSK VLSLYNTINPEASASPCCVS QDLEPLTILYYIGKTPKIEQ LSNMIVKSCKCS ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details ; The sequence provided is that of the monomer, though the protein found in the NMR tube is a covalent (disulfide) linked homodimer. There is a single Arg to Lys substitution at position 60. ; _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 112 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'C-terminal growth Factor Domain of Pro-TGF-b2' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 yes NCBI NP_003229.1 . 'transforming growth factor beta-2 isoform 2 preproprotein [Homo sapiens]' . . . . . . . . . . . . . . 27574 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID Cytokine 27574 1 'Growth Factor' 27574 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 . ALA . 27574 1 2 . LEU . 27574 1 3 . ASP . 27574 1 4 . ALA . 27574 1 5 . ALA . 27574 1 6 . TYR . 27574 1 7 . CYS . 27574 1 8 . PHE . 27574 1 9 . ARG . 27574 1 10 . ASN . 27574 1 11 . VAL . 27574 1 12 . GLN . 27574 1 13 . ASP . 27574 1 14 . ASN . 27574 1 15 . CYS . 27574 1 16 . CYS . 27574 1 17 . LEU . 27574 1 18 . ARG . 27574 1 19 . PRO . 27574 1 20 . LEU . 27574 1 21 . TYR . 27574 1 22 . ILE . 27574 1 23 . ASP . 27574 1 24 . PHE . 27574 1 25 . LYS . 27574 1 26 . ARG . 27574 1 27 . ASP . 27574 1 28 . LEU . 27574 1 29 . GLY . 27574 1 30 . TRP . 27574 1 31 . LYS . 27574 1 32 . TRP . 27574 1 33 . ILE . 27574 1 34 . HIS . 27574 1 35 . GLU . 27574 1 36 . PRO . 27574 1 37 . LYS . 27574 1 38 . GLY . 27574 1 39 . TYR . 27574 1 40 . ASN . 27574 1 41 . ALA . 27574 1 42 . ASN . 27574 1 43 . PHE . 27574 1 44 . CYS . 27574 1 45 . ALA . 27574 1 46 . GLY . 27574 1 47 . ALA . 27574 1 48 . CYS . 27574 1 49 . PRO . 27574 1 50 . TYR . 27574 1 51 . LEU . 27574 1 52 . TRP . 27574 1 53 . SER . 27574 1 54 . SER . 27574 1 55 . ASP . 27574 1 56 . THR . 27574 1 57 . GLN . 27574 1 58 . HIS . 27574 1 59 . SER . 27574 1 60 . LYS . 27574 1 61 . VAL . 27574 1 62 . LEU . 27574 1 63 . SER . 27574 1 64 . LEU . 27574 1 65 . TYR . 27574 1 66 . ASN . 27574 1 67 . THR . 27574 1 68 . ILE . 27574 1 69 . ASN . 27574 1 70 . PRO . 27574 1 71 . GLU . 27574 1 72 . ALA . 27574 1 73 . SER . 27574 1 74 . ALA . 27574 1 75 . SER . 27574 1 76 . PRO . 27574 1 77 . CYS . 27574 1 78 . CYS . 27574 1 79 . VAL . 27574 1 80 . SER . 27574 1 81 . GLN . 27574 1 82 . ASP . 27574 1 83 . LEU . 27574 1 84 . GLU . 27574 1 85 . PRO . 27574 1 86 . LEU . 27574 1 87 . THR . 27574 1 88 . ILE . 27574 1 89 . LEU . 27574 1 90 . TYR . 27574 1 91 . TYR . 27574 1 92 . ILE . 27574 1 93 . GLY . 27574 1 94 . LYS . 27574 1 95 . THR . 27574 1 96 . PRO . 27574 1 97 . LYS . 27574 1 98 . ILE . 27574 1 99 . GLU . 27574 1 100 . GLN . 27574 1 101 . LEU . 27574 1 102 . SER . 27574 1 103 . ASN . 27574 1 104 . MET . 27574 1 105 . ILE . 27574 1 106 . VAL . 27574 1 107 . LYS . 27574 1 108 . SER . 27574 1 109 . CYS . 27574 1 110 . LYS . 27574 1 111 . CYS . 27574 1 112 . SER . 27574 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 . ALA 1 1 27574 1 . LEU 2 2 27574 1 . ASP 3 3 27574 1 . ALA 4 4 27574 1 . ALA 5 5 27574 1 . TYR 6 6 27574 1 . CYS 7 7 27574 1 . PHE 8 8 27574 1 . ARG 9 9 27574 1 . ASN 10 10 27574 1 . VAL 11 11 27574 1 . GLN 12 12 27574 1 . ASP 13 13 27574 1 . ASN 14 14 27574 1 . CYS 15 15 27574 1 . CYS 16 16 27574 1 . LEU 17 17 27574 1 . ARG 18 18 27574 1 . PRO 19 19 27574 1 . LEU 20 20 27574 1 . TYR 21 21 27574 1 . ILE 22 22 27574 1 . ASP 23 23 27574 1 . PHE 24 24 27574 1 . LYS 25 25 27574 1 . ARG 26 26 27574 1 . ASP 27 27 27574 1 . LEU 28 28 27574 1 . GLY 29 29 27574 1 . TRP 30 30 27574 1 . LYS 31 31 27574 1 . TRP 32 32 27574 1 . ILE 33 33 27574 1 . HIS 34 34 27574 1 . GLU 35 35 27574 1 . PRO 36 36 27574 1 . LYS 37 37 27574 1 . GLY 38 38 27574 1 . TYR 39 39 27574 1 . ASN 40 40 27574 1 . ALA 41 41 27574 1 . ASN 42 42 27574 1 . PHE 43 43 27574 1 . CYS 44 44 27574 1 . ALA 45 45 27574 1 . GLY 46 46 27574 1 . ALA 47 47 27574 1 . CYS 48 48 27574 1 . PRO 49 49 27574 1 . TYR 50 50 27574 1 . LEU 51 51 27574 1 . TRP 52 52 27574 1 . SER 53 53 27574 1 . SER 54 54 27574 1 . ASP 55 55 27574 1 . THR 56 56 27574 1 . GLN 57 57 27574 1 . HIS 58 58 27574 1 . SER 59 59 27574 1 . LYS 60 60 27574 1 . VAL 61 61 27574 1 . LEU 62 62 27574 1 . SER 63 63 27574 1 . LEU 64 64 27574 1 . TYR 65 65 27574 1 . ASN 66 66 27574 1 . THR 67 67 27574 1 . ILE 68 68 27574 1 . ASN 69 69 27574 1 . PRO 70 70 27574 1 . GLU 71 71 27574 1 . ALA 72 72 27574 1 . SER 73 73 27574 1 . ALA 74 74 27574 1 . SER 75 75 27574 1 . PRO 76 76 27574 1 . CYS 77 77 27574 1 . CYS 78 78 27574 1 . VAL 79 79 27574 1 . SER 80 80 27574 1 . GLN 81 81 27574 1 . ASP 82 82 27574 1 . LEU 83 83 27574 1 . GLU 84 84 27574 1 . PRO 85 85 27574 1 . LEU 86 86 27574 1 . THR 87 87 27574 1 . ILE 88 88 27574 1 . LEU 89 89 27574 1 . TYR 90 90 27574 1 . TYR 91 91 27574 1 . ILE 92 92 27574 1 . GLY 93 93 27574 1 . LYS 94 94 27574 1 . THR 95 95 27574 1 . PRO 96 96 27574 1 . LYS 97 97 27574 1 . ILE 98 98 27574 1 . GLU 99 99 27574 1 . GLN 100 100 27574 1 . LEU 101 101 27574 1 . SER 102 102 27574 1 . ASN 103 103 27574 1 . MET 104 104 27574 1 . ILE 105 105 27574 1 . VAL 106 106 27574 1 . LYS 107 107 27574 1 . SER 108 108 27574 1 . CYS 109 109 27574 1 . LYS 110 110 27574 1 . CYS 111 111 27574 1 . SER 112 112 27574 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 27574 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $TGF-b2 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 27574 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 27574 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $TGF-b2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . pET32a . . . 27574 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 27574 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 TGF-b2 '[U-98% 13C; U-98% 15N]' . . 1 $TGF-b2 . . 0.25 0.2 0.3 mM . . . . 27574 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 27574 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0 . M 27574 1 pH 2.7 . pH 27574 1 pressure 1 . atm 27574 1 temperature 310 . K 27574 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 27574 _Software.ID 1 _Software.Type . _Software.Name NMRView _Software.Version J _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Johnson, One Moon Scientific' . . 27574 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 27574 1 'data analysis' 27574 1 'peak picking' 27574 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 27574 _Software.ID 2 _Software.Type . _Software.Name NMRPipe _Software.Version . _Software.DOI . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 27574 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 27574 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 27574 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'Equipped with 5 mm TCI cryoprobe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 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 27574 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 'Equipped with 5 mm TCI cryoprobe' . . 27574 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 27574 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 3 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 5 '3D HNCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 6 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 7 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 8 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 9 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 10 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 1 11 '2D 1H-13C HSQC aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 27574 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 27574 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . 27574 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . 27574 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . 27574 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 27574 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.01 _Assigned_chem_shift_list.Chem_shift_13C_err 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 27574 1 2 '3D HNCACB' . . . 27574 1 3 '3D CBCA(CO)NH' . . . 27574 1 4 '3D HNCO' . . . 27574 1 5 '3D HNCACO' . . . 27574 1 6 '3D HNCA' . . . 27574 1 7 '3D HN(CO)CA' . . . 27574 1 8 '3D H(CCO)NH' . . . 27574 1 9 '3D HCCH-TOCSY' . . . 27574 1 10 '3D C(CO)NH' . . . 27574 1 11 '2D 1H-13C HSQC aliphatic' . . . 27574 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $NMRView . . 27574 1 2 $NMRPipe . . 27574 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.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ALA HA H 1 4.013 0.01 . 1 . . . . . 1 ALA HA . 27574 1 2 . 1 1 1 1 ALA HB1 H 1 1.446 0.01 . 1 . . . . . 1 ALA MB . 27574 1 3 . 1 1 1 1 ALA HB2 H 1 1.446 0.01 . 1 . . . . . 1 ALA MB . 27574 1 4 . 1 1 1 1 ALA HB3 H 1 1.446 0.01 . 1 . . . . . 1 ALA MB . 27574 1 5 . 1 1 1 1 ALA C C 13 173.406 0.2 . 1 . . . . . 1 ALA C . 27574 1 6 . 1 1 1 1 ALA CA C 13 51.612 0.2 . 1 . . . . . 1 ALA CA . 27574 1 7 . 1 1 1 1 ALA CB C 13 19.410 0.2 . 1 . . . . . 1 ALA CB . 27574 1 8 . 1 1 2 2 LEU H H 1 8.605 0.01 . 1 . . . . . 2 LEU H . 27574 1 9 . 1 1 2 2 LEU HA H 1 4.594 0.01 . 1 . . . . . 2 LEU HA . 27574 1 10 . 1 1 2 2 LEU HB2 H 1 1.955 0.01 . 2 . . . . . 2 LEU HB2 . 27574 1 11 . 1 1 2 2 LEU HB3 H 1 1.191 0.01 . 2 . . . . . 2 LEU HB3 . 27574 1 12 . 1 1 2 2 LEU HG H 1 1.533 0.01 . 1 . . . . . 2 LEU HG . 27574 1 13 . 1 1 2 2 LEU HD11 H 1 0.733 0.01 . 2 . . . . . 2 LEU MD1 . 27574 1 14 . 1 1 2 2 LEU HD12 H 1 0.733 0.01 . 2 . . . . . 2 LEU MD1 . 27574 1 15 . 1 1 2 2 LEU HD13 H 1 0.733 0.01 . 2 . . . . . 2 LEU MD1 . 27574 1 16 . 1 1 2 2 LEU HD21 H 1 0.803 0.01 . 2 . . . . . 2 LEU MD2 . 27574 1 17 . 1 1 2 2 LEU HD22 H 1 0.803 0.01 . 2 . . . . . 2 LEU MD2 . 27574 1 18 . 1 1 2 2 LEU HD23 H 1 0.803 0.01 . 2 . . . . . 2 LEU MD2 . 27574 1 19 . 1 1 2 2 LEU C C 13 175.279 0.2 . 1 . . . . . 2 LEU C . 27574 1 20 . 1 1 2 2 LEU CA C 13 53.686 0.2 . 1 . . . . . 2 LEU CA . 27574 1 21 . 1 1 2 2 LEU CB C 13 40.322 0.2 . 1 . . . . . 2 LEU CB . 27574 1 22 . 1 1 2 2 LEU CG C 13 26.784 0.2 . 1 . . . . . 2 LEU CG . 27574 1 23 . 1 1 2 2 LEU CD1 C 13 24.765 0.2 . 2 . . . . . 2 LEU CD1 . 27574 1 24 . 1 1 2 2 LEU CD2 C 13 22.909 0.2 . 2 . . . . . 2 LEU CD2 . 27574 1 25 . 1 1 2 2 LEU N N 15 121.220 0.3 . 1 . . . . . 2 LEU N . 27574 1 26 . 1 1 3 3 ASP H H 1 7.888 0.01 . 1 . . . . . 3 ASP H . 27574 1 27 . 1 1 3 3 ASP HA H 1 4.814 0.01 . 1 . . . . . 3 ASP HA . 27574 1 28 . 1 1 3 3 ASP HB2 H 1 3.044 0.01 . 2 . . . . . 3 ASP HB2 . 27574 1 29 . 1 1 3 3 ASP HB3 H 1 2.516 0.01 . 2 . . . . . 3 ASP HB3 . 27574 1 30 . 1 1 3 3 ASP C C 13 175.773 0.2 . 1 . . . . . 3 ASP C . 27574 1 31 . 1 1 3 3 ASP CA C 13 51.720 0.2 . 1 . . . . . 3 ASP CA . 27574 1 32 . 1 1 3 3 ASP CB C 13 41.924 0.2 . 1 . . . . . 3 ASP CB . 27574 1 33 . 1 1 3 3 ASP N N 15 121.201 0.3 . 1 . . . . . 3 ASP N . 27574 1 34 . 1 1 4 4 ALA H H 1 8.418 0.01 . 1 . . . . . 4 ALA H . 27574 1 35 . 1 1 4 4 ALA HA H 1 3.109 0.01 . 1 . . . . . 4 ALA HA . 27574 1 36 . 1 1 4 4 ALA HB1 H 1 0.879 0.01 . 1 . . . . . 4 ALA MB . 27574 1 37 . 1 1 4 4 ALA HB2 H 1 0.879 0.01 . 1 . . . . . 4 ALA MB . 27574 1 38 . 1 1 4 4 ALA HB3 H 1 0.879 0.01 . 1 . . . . . 4 ALA MB . 27574 1 39 . 1 1 4 4 ALA C C 13 178.554 0.2 . 1 . . . . . 4 ALA C . 27574 1 40 . 1 1 4 4 ALA CA C 13 54.869 0.2 . 1 . . . . . 4 ALA CA . 27574 1 41 . 1 1 4 4 ALA CB C 13 18.800 0.2 . 1 . . . . . 4 ALA CB . 27574 1 42 . 1 1 4 4 ALA N N 15 123.358 0.3 . 1 . . . . . 4 ALA N . 27574 1 43 . 1 1 5 5 ALA H H 1 7.714 0.01 . 1 . . . . . 5 ALA H . 27574 1 44 . 1 1 5 5 ALA HA H 1 3.967 0.01 . 1 . . . . . 5 ALA HA . 27574 1 45 . 1 1 5 5 ALA HB1 H 1 1.348 0.01 . 1 . . . . . 5 ALA MB . 27574 1 46 . 1 1 5 5 ALA HB2 H 1 1.348 0.01 . 1 . . . . . 5 ALA MB . 27574 1 47 . 1 1 5 5 ALA HB3 H 1 1.348 0.01 . 1 . . . . . 5 ALA MB . 27574 1 48 . 1 1 5 5 ALA C C 13 178.709 0.2 . 1 . . . . . 5 ALA C . 27574 1 49 . 1 1 5 5 ALA CA C 13 54.109 0.2 . 1 . . . . . 5 ALA CA . 27574 1 50 . 1 1 5 5 ALA CB C 13 18.268 0.2 . 1 . . . . . 5 ALA CB . 27574 1 51 . 1 1 5 5 ALA N N 15 119.903 0.3 . 1 . . . . . 5 ALA N . 27574 1 52 . 1 1 6 6 TYR H H 1 7.603 0.01 . 1 . . . . . 6 TYR H . 27574 1 53 . 1 1 6 6 TYR HA H 1 4.478 0.01 . 1 . . . . . 6 TYR HA . 27574 1 54 . 1 1 6 6 TYR HB2 H 1 3.249 0.01 . 2 . . . . . 6 TYR HB2 . 27574 1 55 . 1 1 6 6 TYR HB3 H 1 3.117 0.01 . 2 . . . . . 6 TYR HB3 . 27574 1 56 . 1 1 6 6 TYR HD1 H 1 7.144 0.01 . 3 . . . . . 6 TYR HD1 . 27574 1 57 . 1 1 6 6 TYR HD2 H 1 7.144 0.01 . 3 . . . . . 6 TYR HD2 . 27574 1 58 . 1 1 6 6 TYR HE1 H 1 6.700 0.01 . 3 . . . . . 6 TYR HE1 . 27574 1 59 . 1 1 6 6 TYR HE2 H 1 6.700 0.01 . 3 . . . . . 6 TYR HE2 . 27574 1 60 . 1 1 6 6 TYR C C 13 177.785 0.2 . 1 . . . . . 6 TYR C . 27574 1 61 . 1 1 6 6 TYR CA C 13 59.624 0.2 . 1 . . . . . 6 TYR CA . 27574 1 62 . 1 1 6 6 TYR CB C 13 40.043 0.2 . 1 . . . . . 6 TYR CB . 27574 1 63 . 1 1 6 6 TYR N N 15 116.054 0.3 . 1 . . . . . 6 TYR N . 27574 1 64 . 1 1 7 7 CYS H H 1 8.671 0.01 . 1 . . . . . 7 CYS H . 27574 1 65 . 1 1 7 7 CYS HA H 1 4.342 0.01 . 1 . . . . . 7 CYS HA . 27574 1 66 . 1 1 7 7 CYS HB2 H 1 3.349 0.01 . 2 . . . . . 7 CYS HB2 . 27574 1 67 . 1 1 7 7 CYS HB3 H 1 2.886 0.01 . 2 . . . . . 7 CYS HB3 . 27574 1 68 . 1 1 7 7 CYS C C 13 175.919 0.2 . 1 . . . . . 7 CYS C . 27574 1 69 . 1 1 7 7 CYS CA C 13 57.021 0.2 . 1 . . . . . 7 CYS CA . 27574 1 70 . 1 1 7 7 CYS CB C 13 40.632 0.2 . 1 . . . . . 7 CYS CB . 27574 1 71 . 1 1 7 7 CYS N N 15 115.700 0.3 . 1 . . . . . 7 CYS N . 27574 1 72 . 1 1 8 8 PHE H H 1 8.323 0.01 . 1 . . . . . 8 PHE H . 27574 1 73 . 1 1 8 8 PHE HA H 1 4.736 0.01 . 1 . . . . . 8 PHE HA . 27574 1 74 . 1 1 8 8 PHE HB2 H 1 3.249 0.01 . 2 . . . . . 8 PHE HB2 . 27574 1 75 . 1 1 8 8 PHE HB3 H 1 3.249 0.01 . 2 . . . . . 8 PHE HB3 . 27574 1 76 . 1 1 8 8 PHE C C 13 176.444 0.2 . 1 . . . . . 8 PHE C . 27574 1 77 . 1 1 8 8 PHE CA C 13 56.813 0.2 . 1 . . . . . 8 PHE CA . 27574 1 78 . 1 1 8 8 PHE CB C 13 36.772 0.2 . 1 . . . . . 8 PHE CB . 27574 1 79 . 1 1 8 8 PHE N N 15 118.352 0.3 . 1 . . . . . 8 PHE N . 27574 1 80 . 1 1 9 9 ARG H H 1 7.411 0.01 . 1 . . . . . 9 ARG H . 27574 1 81 . 1 1 9 9 ARG HA H 1 4.299 0.01 . 1 . . . . . 9 ARG HA . 27574 1 82 . 1 1 9 9 ARG HB2 H 1 1.802 0.01 . 2 . . . . . 9 ARG HB2 . 27574 1 83 . 1 1 9 9 ARG HB3 H 1 1.802 0.01 . 2 . . . . . 9 ARG HB3 . 27574 1 84 . 1 1 9 9 ARG C C 13 175.317 0.2 . 1 . . . . . 9 ARG C . 27574 1 85 . 1 1 9 9 ARG CA C 13 56.782 0.2 . 1 . . . . . 9 ARG CA . 27574 1 86 . 1 1 9 9 ARG CB C 13 30.868 0.2 . 1 . . . . . 9 ARG CB . 27574 1 87 . 1 1 9 9 ARG CG C 13 27.693 0.2 . 1 . . . . . 9 ARG CG . 27574 1 88 . 1 1 9 9 ARG CD C 13 43.466 0.2 . 1 . . . . . 9 ARG CD . 27574 1 89 . 1 1 9 9 ARG N N 15 117.529 0.3 . 1 . . . . . 9 ARG N . 27574 1 90 . 1 1 10 10 ASN H H 1 7.621 0.01 . 1 . . . . . 10 ASN H . 27574 1 91 . 1 1 10 10 ASN HA H 1 4.699 0.01 . 1 . . . . . 10 ASN HA . 27574 1 92 . 1 1 10 10 ASN HB2 H 1 2.611 0.01 . 2 . . . . . 10 ASN HB2 . 27574 1 93 . 1 1 10 10 ASN HB3 H 1 2.443 0.01 . 2 . . . . . 10 ASN HB3 . 27574 1 94 . 1 1 10 10 ASN C C 13 174.095 0.2 . 1 . . . . . 10 ASN C . 27574 1 95 . 1 1 10 10 ASN CA C 13 52.900 0.2 . 1 . . . . . 10 ASN CA . 27574 1 96 . 1 1 10 10 ASN CB C 13 39.302 0.2 . 1 . . . . . 10 ASN CB . 27574 1 97 . 1 1 10 10 ASN N N 15 117.850 0.3 . 1 . . . . . 10 ASN N . 27574 1 98 . 1 1 11 11 VAL H H 1 8.029 0.01 . 1 . . . . . 11 VAL H . 27574 1 99 . 1 1 11 11 VAL HA H 1 4.067 0.01 . 1 . . . . . 11 VAL HA . 27574 1 100 . 1 1 11 11 VAL HB H 1 2.041 0.01 . 1 . . . . . 11 VAL HB . 27574 1 101 . 1 1 11 11 VAL HG11 H 1 0.860 0.01 . 2 . . . . . 11 VAL MG1 . 27574 1 102 . 1 1 11 11 VAL HG12 H 1 0.860 0.01 . 2 . . . . . 11 VAL MG1 . 27574 1 103 . 1 1 11 11 VAL HG13 H 1 0.860 0.01 . 2 . . . . . 11 VAL MG1 . 27574 1 104 . 1 1 11 11 VAL HG21 H 1 0.884 0.01 . 2 . . . . . 11 VAL MG2 . 27574 1 105 . 1 1 11 11 VAL HG22 H 1 0.884 0.01 . 2 . . . . . 11 VAL MG2 . 27574 1 106 . 1 1 11 11 VAL HG23 H 1 0.884 0.01 . 2 . . . . . 11 VAL MG2 . 27574 1 107 . 1 1 11 11 VAL C C 13 176.157 0.2 . 1 . . . . . 11 VAL C . 27574 1 108 . 1 1 11 11 VAL CA C 13 63.377 0.2 . 1 . . . . . 11 VAL CA . 27574 1 109 . 1 1 11 11 VAL CB C 13 31.585 0.2 . 1 . . . . . 11 VAL CB . 27574 1 110 . 1 1 11 11 VAL CG1 C 13 21.216 0.2 . 2 . . . . . 11 VAL CG1 . 27574 1 111 . 1 1 11 11 VAL CG2 C 13 21.216 0.2 . 2 . . . . . 11 VAL CG2 . 27574 1 112 . 1 1 11 11 VAL N N 15 120.785 0.3 . 1 . . . . . 11 VAL N . 27574 1 113 . 1 1 12 12 GLN H H 1 8.350 0.01 . 1 . . . . . 12 GLN H . 27574 1 114 . 1 1 12 12 GLN HA H 1 4.581 0.01 . 1 . . . . . 12 GLN HA . 27574 1 115 . 1 1 12 12 GLN HB2 H 1 2.168 0.01 . 2 . . . . . 12 GLN HB2 . 27574 1 116 . 1 1 12 12 GLN HB3 H 1 2.168 0.01 . 2 . . . . . 12 GLN HB3 . 27574 1 117 . 1 1 12 12 GLN C C 13 175.769 0.2 . 1 . . . . . 12 GLN C . 27574 1 118 . 1 1 12 12 GLN CA C 13 55.144 0.2 . 1 . . . . . 12 GLN CA . 27574 1 119 . 1 1 12 12 GLN CB C 13 30.322 0.2 . 1 . . . . . 12 GLN CB . 27574 1 120 . 1 1 12 12 GLN N N 15 123.236 0.3 . 1 . . . . . 12 GLN N . 27574 1 121 . 1 1 13 13 ASP H H 1 8.527 0.01 . 1 . . . . . 13 ASP H . 27574 1 122 . 1 1 13 13 ASP HA H 1 4.699 0.01 . 1 . . . . . 13 ASP HA . 27574 1 123 . 1 1 13 13 ASP HB2 H 1 2.790 0.01 . 2 . . . . . 13 ASP HB2 . 27574 1 124 . 1 1 13 13 ASP HB3 H 1 2.790 0.01 . 2 . . . . . 13 ASP HB3 . 27574 1 125 . 1 1 13 13 ASP C C 13 175.961 0.2 . 1 . . . . . 13 ASP C . 27574 1 126 . 1 1 13 13 ASP CA C 13 54.135 0.2 . 1 . . . . . 13 ASP CA . 27574 1 127 . 1 1 13 13 ASP CB C 13 39.428 0.2 . 1 . . . . . 13 ASP CB . 27574 1 128 . 1 1 13 13 ASP N N 15 119.604 0.3 . 1 . . . . . 13 ASP N . 27574 1 129 . 1 1 14 14 ASN H H 1 7.752 0.01 . 1 . . . . . 14 ASN H . 27574 1 130 . 1 1 14 14 ASN HA H 1 4.618 0.01 . 1 . . . . . 14 ASN HA . 27574 1 131 . 1 1 14 14 ASN CA C 13 53.361 0.2 . 1 . . . . . 14 ASN CA . 27574 1 132 . 1 1 14 14 ASN CB C 13 38.729 0.2 . 1 . . . . . 14 ASN CB . 27574 1 133 . 1 1 14 14 ASN N N 15 117.975 0.3 . 1 . . . . . 14 ASN N . 27574 1 134 . 1 1 15 15 CYS HA H 1 4.102 0.01 . 1 . . . . . 15 CYS HA . 27574 1 135 . 1 1 15 15 CYS HB2 H 1 2.880 0.01 . 2 . . . . . 15 CYS HB2 . 27574 1 136 . 1 1 15 15 CYS HB3 H 1 2.338 0.01 . 2 . . . . . 15 CYS HB3 . 27574 1 137 . 1 1 15 15 CYS C C 13 172.523 0.2 . 1 . . . . . 15 CYS C . 27574 1 138 . 1 1 15 15 CYS CA C 13 55.378 0.2 . 1 . . . . . 15 CYS CA . 27574 1 139 . 1 1 15 15 CYS CB C 13 34.783 0.2 . 1 . . . . . 15 CYS CB . 27574 1 140 . 1 1 16 16 CYS H H 1 8.204 0.01 . 1 . . . . . 16 CYS H . 27574 1 141 . 1 1 16 16 CYS C C 13 171.209 0.2 . 1 . . . . . 16 CYS C . 27574 1 142 . 1 1 16 16 CYS CA C 13 58.343 0.2 . 1 . . . . . 16 CYS CA . 27574 1 143 . 1 1 16 16 CYS CB C 13 41.198 0.2 . 1 . . . . . 16 CYS CB . 27574 1 144 . 1 1 16 16 CYS N N 15 125.332 0.3 . 1 . . . . . 16 CYS N . 27574 1 145 . 1 1 17 17 LEU H H 1 7.690 0.01 . 1 . . . . . 17 LEU H . 27574 1 146 . 1 1 17 17 LEU HA H 1 4.270 0.01 . 1 . . . . . 17 LEU HA . 27574 1 147 . 1 1 17 17 LEU HB2 H 1 1.092 0.01 . 2 . . . . . 17 LEU HB2 . 27574 1 148 . 1 1 17 17 LEU HB3 H 1 1.290 0.01 . 2 . . . . . 17 LEU HB3 . 27574 1 149 . 1 1 17 17 LEU HD11 H 1 0.448 0.01 . 2 . . . . . 17 LEU MD1 . 27574 1 150 . 1 1 17 17 LEU HD12 H 1 0.448 0.01 . 2 . . . . . 17 LEU MD1 . 27574 1 151 . 1 1 17 17 LEU HD13 H 1 0.448 0.01 . 2 . . . . . 17 LEU MD1 . 27574 1 152 . 1 1 17 17 LEU HD21 H 1 0.609 0.01 . 2 . . . . . 17 LEU MD2 . 27574 1 153 . 1 1 17 17 LEU HD22 H 1 0.609 0.01 . 2 . . . . . 17 LEU MD2 . 27574 1 154 . 1 1 17 17 LEU HD23 H 1 0.609 0.01 . 2 . . . . . 17 LEU MD2 . 27574 1 155 . 1 1 17 17 LEU C C 13 174.697 0.2 . 1 . . . . . 17 LEU C . 27574 1 156 . 1 1 17 17 LEU CA C 13 55.519 0.2 . 1 . . . . . 17 LEU CA . 27574 1 157 . 1 1 17 17 LEU CB C 13 43.988 0.2 . 1 . . . . . 17 LEU CB . 27574 1 158 . 1 1 17 17 LEU CD1 C 13 26.413 0.2 . 2 . . . . . 17 LEU CD1 . 27574 1 159 . 1 1 17 17 LEU CD2 C 13 25.425 0.2 . 2 . . . . . 17 LEU CD2 . 27574 1 160 . 1 1 17 17 LEU N N 15 124.975 0.3 . 1 . . . . . 17 LEU N . 27574 1 161 . 1 1 18 18 ARG H H 1 9.043 0.01 . 1 . . . . . 18 ARG H . 27574 1 162 . 1 1 18 18 ARG HA H 1 4.600 0.01 . 1 . . . . . 18 ARG HA . 27574 1 163 . 1 1 18 18 ARG CA C 13 51.033 0.2 . 1 . . . . . 18 ARG CA . 27574 1 164 . 1 1 18 18 ARG CB C 13 29.719 0.2 . 1 . . . . . 18 ARG CB . 27574 1 165 . 1 1 18 18 ARG N N 15 126.142 0.3 . 1 . . . . . 18 ARG N . 27574 1 166 . 1 1 19 19 PRO HA H 1 4.615 0.01 . 1 . . . . . 19 PRO HA . 27574 1 167 . 1 1 19 19 PRO HB2 H 1 1.665 0.01 . 2 . . . . . 19 PRO HB2 . 27574 1 168 . 1 1 19 19 PRO HB3 H 1 1.665 0.01 . 2 . . . . . 19 PRO HB3 . 27574 1 169 . 1 1 19 19 PRO C C 13 176.541 0.2 . 1 . . . . . 19 PRO C . 27574 1 170 . 1 1 19 19 PRO CA C 13 62.320 0.2 . 1 . . . . . 19 PRO CA . 27574 1 171 . 1 1 19 19 PRO CB C 13 31.835 0.2 . 1 . . . . . 19 PRO CB . 27574 1 172 . 1 1 19 19 PRO CG C 13 26.829 0.2 . 1 . . . . . 19 PRO CG . 27574 1 173 . 1 1 19 19 PRO CD C 13 50.141 0.2 . 1 . . . . . 19 PRO CD . 27574 1 174 . 1 1 20 20 LEU H H 1 7.686 0.01 . 1 . . . . . 20 LEU H . 27574 1 175 . 1 1 20 20 LEU HA H 1 4.279 0.01 . 1 . . . . . 20 LEU HA . 27574 1 176 . 1 1 20 20 LEU HB2 H 1 1.359 0.01 . 2 . . . . . 20 LEU HB2 . 27574 1 177 . 1 1 20 20 LEU HB3 H 1 1.883 0.01 . 2 . . . . . 20 LEU HB3 . 27574 1 178 . 1 1 20 20 LEU HD11 H 1 0.448 0.01 . 2 . . . . . 20 LEU MD1 . 27574 1 179 . 1 1 20 20 LEU HD12 H 1 0.448 0.01 . 2 . . . . . 20 LEU MD1 . 27574 1 180 . 1 1 20 20 LEU HD13 H 1 0.448 0.01 . 2 . . . . . 20 LEU MD1 . 27574 1 181 . 1 1 20 20 LEU HD21 H 1 0.664 0.01 . 2 . . . . . 20 LEU MD2 . 27574 1 182 . 1 1 20 20 LEU HD22 H 1 0.664 0.01 . 2 . . . . . 20 LEU MD2 . 27574 1 183 . 1 1 20 20 LEU HD23 H 1 0.664 0.01 . 2 . . . . . 20 LEU MD2 . 27574 1 184 . 1 1 20 20 LEU CA C 13 56.948 0.2 . 1 . . . . . 20 LEU CA . 27574 1 185 . 1 1 20 20 LEU CB C 13 44.764 0.2 . 1 . . . . . 20 LEU CB . 27574 1 186 . 1 1 20 20 LEU CG C 13 27.606 0.2 . 1 . . . . . 20 LEU CG . 27574 1 187 . 1 1 20 20 LEU CD1 C 13 26.170 0.2 . 2 . . . . . 20 LEU CD1 . 27574 1 188 . 1 1 20 20 LEU CD2 C 13 23.072 0.2 . 2 . . . . . 20 LEU CD2 . 27574 1 189 . 1 1 20 20 LEU N N 15 119.702 0.3 . 1 . . . . . 20 LEU N . 27574 1 190 . 1 1 21 21 TYR H H 1 8.589 0.01 . 1 . . . . . 21 TYR H . 27574 1 191 . 1 1 21 21 TYR HA H 1 4.743 0.01 . 1 . . . . . 21 TYR HA . 27574 1 192 . 1 1 21 21 TYR HB2 H 1 2.750 0.01 . 2 . . . . . 21 TYR HB2 . 27574 1 193 . 1 1 21 21 TYR HB3 H 1 2.750 0.01 . 2 . . . . . 21 TYR HB3 . 27574 1 194 . 1 1 21 21 TYR C C 13 173.521 0.2 . 1 . . . . . 21 TYR C . 27574 1 195 . 1 1 21 21 TYR CA C 13 57.035 0.2 . 1 . . . . . 21 TYR CA . 27574 1 196 . 1 1 21 21 TYR CB C 13 39.614 0.2 . 1 . . . . . 21 TYR CB . 27574 1 197 . 1 1 21 21 TYR N N 15 130.701 0.3 . 1 . . . . . 21 TYR N . 27574 1 198 . 1 1 22 22 ILE H H 1 7.789 0.01 . 1 . . . . . 22 ILE H . 27574 1 199 . 1 1 22 22 ILE HA H 1 3.826 0.01 . 1 . . . . . 22 ILE HA . 27574 1 200 . 1 1 22 22 ILE HB H 1 0.836 0.01 . 1 . . . . . 22 ILE HB . 27574 1 201 . 1 1 22 22 ILE HG12 H 1 0.586 0.01 . 2 . . . . . 22 ILE HG12 . 27574 1 202 . 1 1 22 22 ILE HG13 H 1 0.586 0.01 . 2 . . . . . 22 ILE HG13 . 27574 1 203 . 1 1 22 22 ILE HG21 H 1 0.260 0.01 . 1 . . . . . 22 ILE MG . 27574 1 204 . 1 1 22 22 ILE HG22 H 1 0.260 0.01 . 1 . . . . . 22 ILE MG . 27574 1 205 . 1 1 22 22 ILE HG23 H 1 0.260 0.01 . 1 . . . . . 22 ILE MG . 27574 1 206 . 1 1 22 22 ILE HD11 H 1 0.300 0.01 . 1 . . . . . 22 ILE MD . 27574 1 207 . 1 1 22 22 ILE HD12 H 1 0.300 0.01 . 1 . . . . . 22 ILE MD . 27574 1 208 . 1 1 22 22 ILE HD13 H 1 0.300 0.01 . 1 . . . . . 22 ILE MD . 27574 1 209 . 1 1 22 22 ILE C C 13 172.522 0.2 . 1 . . . . . 22 ILE C . 27574 1 210 . 1 1 22 22 ILE CA C 13 58.422 0.2 . 1 . . . . . 22 ILE CA . 27574 1 211 . 1 1 22 22 ILE CB C 13 38.646 0.2 . 1 . . . . . 22 ILE CB . 27574 1 212 . 1 1 22 22 ILE CG1 C 13 26.925 0.2 . 1 . . . . . 22 ILE CG1 . 27574 1 213 . 1 1 22 22 ILE CG2 C 13 16.761 0.2 . 1 . . . . . 22 ILE CG2 . 27574 1 214 . 1 1 22 22 ILE CD1 C 13 11.263 0.2 . 1 . . . . . 22 ILE CD1 . 27574 1 215 . 1 1 22 22 ILE N N 15 128.483 0.3 . 1 . . . . . 22 ILE N . 27574 1 216 . 1 1 23 23 ASP H H 1 8.848 0.01 . 1 . . . . . 23 ASP H . 27574 1 217 . 1 1 23 23 ASP HA H 1 4.528 0.01 . 1 . . . . . 23 ASP HA . 27574 1 218 . 1 1 23 23 ASP HB2 H 1 2.678 0.01 . 2 . . . . . 23 ASP HB2 . 27574 1 219 . 1 1 23 23 ASP HB3 H 1 2.455 0.01 . 2 . . . . . 23 ASP HB3 . 27574 1 220 . 1 1 23 23 ASP C C 13 177.392 0.2 . 1 . . . . . 23 ASP C . 27574 1 221 . 1 1 23 23 ASP CA C 13 52.627 0.2 . 1 . . . . . 23 ASP CA . 27574 1 222 . 1 1 23 23 ASP CB C 13 44.249 0.2 . 1 . . . . . 23 ASP CB . 27574 1 223 . 1 1 23 23 ASP N N 15 127.276 0.3 . 1 . . . . . 23 ASP N . 27574 1 224 . 1 1 24 24 PHE H H 1 8.260 0.01 . 1 . . . . . 24 PHE H . 27574 1 225 . 1 1 24 24 PHE HA H 1 3.947 0.01 . 1 . . . . . 24 PHE HA . 27574 1 226 . 1 1 24 24 PHE HB2 H 1 3.186 0.01 . 2 . . . . . 24 PHE HB2 . 27574 1 227 . 1 1 24 24 PHE HB3 H 1 2.908 0.01 . 2 . . . . . 24 PHE HB3 . 27574 1 228 . 1 1 24 24 PHE C C 13 177.871 0.2 . 1 . . . . . 24 PHE C . 27574 1 229 . 1 1 24 24 PHE CA C 13 63.199 0.2 . 1 . . . . . 24 PHE CA . 27574 1 230 . 1 1 24 24 PHE CB C 13 38.402 0.2 . 1 . . . . . 24 PHE CB . 27574 1 231 . 1 1 24 24 PHE N N 15 125.428 0.3 . 1 . . . . . 24 PHE N . 27574 1 232 . 1 1 25 25 LYS H H 1 8.658 0.01 . 1 . . . . . 25 LYS H . 27574 1 233 . 1 1 25 25 LYS HA H 1 3.882 0.01 . 1 . . . . . 25 LYS HA . 27574 1 234 . 1 1 25 25 LYS HB2 H 1 1.897 0.01 . 2 . . . . . 25 LYS HB2 . 27574 1 235 . 1 1 25 25 LYS HB3 H 1 1.897 0.01 . 2 . . . . . 25 LYS HB3 . 27574 1 236 . 1 1 25 25 LYS C C 13 178.400 0.2 . 1 . . . . . 25 LYS C . 27574 1 237 . 1 1 25 25 LYS CA C 13 60.572 0.2 . 1 . . . . . 25 LYS CA . 27574 1 238 . 1 1 25 25 LYS CB C 13 32.710 0.2 . 1 . . . . . 25 LYS CB . 27574 1 239 . 1 1 25 25 LYS CG C 13 26.004 0.2 . 1 . . . . . 25 LYS CG . 27574 1 240 . 1 1 25 25 LYS CD C 13 29.542 0.2 . 1 . . . . . 25 LYS CD . 27574 1 241 . 1 1 25 25 LYS CE C 13 42.220 0.2 . 1 . . . . . 25 LYS CE . 27574 1 242 . 1 1 25 25 LYS N N 15 119.569 0.3 . 1 . . . . . 25 LYS N . 27574 1 243 . 1 1 26 26 ARG H H 1 8.810 0.01 . 1 . . . . . 26 ARG H . 27574 1 244 . 1 1 26 26 ARG HA H 1 3.996 0.01 . 1 . . . . . 26 ARG HA . 27574 1 245 . 1 1 26 26 ARG HB2 H 1 1.700 0.01 . 2 . . . . . 26 ARG HB2 . 27574 1 246 . 1 1 26 26 ARG HB3 H 1 1.700 0.01 . 2 . . . . . 26 ARG HB3 . 27574 1 247 . 1 1 26 26 ARG C C 13 177.462 0.2 . 1 . . . . . 26 ARG C . 27574 1 248 . 1 1 26 26 ARG CA C 13 58.900 0.2 . 1 . . . . . 26 ARG CA . 27574 1 249 . 1 1 26 26 ARG CB C 13 31.359 0.2 . 1 . . . . . 26 ARG CB . 27574 1 250 . 1 1 26 26 ARG CG C 13 27.130 0.2 . 1 . . . . . 26 ARG CG . 27574 1 251 . 1 1 26 26 ARG CD C 13 43.480 0.2 . 1 . . . . . 26 ARG CD . 27574 1 252 . 1 1 26 26 ARG N N 15 118.819 0.3 . 1 . . . . . 26 ARG N . 27574 1 253 . 1 1 27 27 ASP H H 1 8.262 0.01 . 1 . . . . . 27 ASP H . 27574 1 254 . 1 1 27 27 ASP HA H 1 4.777 0.01 . 1 . . . . . 27 ASP HA . 27574 1 255 . 1 1 27 27 ASP CA C 13 56.086 0.2 . 1 . . . . . 27 ASP CA . 27574 1 256 . 1 1 27 27 ASP CB C 13 41.283 0.2 . 1 . . . . . 27 ASP CB . 27574 1 257 . 1 1 27 27 ASP N N 15 113.587 0.3 . 1 . . . . . 27 ASP N . 27574 1 258 . 1 1 28 28 LEU HA H 1 4.378 0.01 . 1 . . . . . 28 LEU HA . 27574 1 259 . 1 1 28 28 LEU HB2 H 1 1.363 0.01 . 2 . . . . . 28 LEU HB2 . 27574 1 260 . 1 1 28 28 LEU HB3 H 1 1.037 0.01 . 2 . . . . . 28 LEU HB3 . 27574 1 261 . 1 1 28 28 LEU HD11 H 1 0.020 0.01 . 2 . . . . . 28 LEU MD1 . 27574 1 262 . 1 1 28 28 LEU HD12 H 1 0.020 0.01 . 2 . . . . . 28 LEU MD1 . 27574 1 263 . 1 1 28 28 LEU HD13 H 1 0.020 0.01 . 2 . . . . . 28 LEU MD1 . 27574 1 264 . 1 1 28 28 LEU HD21 H 1 0.484 0.01 . 2 . . . . . 28 LEU MD2 . 27574 1 265 . 1 1 28 28 LEU HD22 H 1 0.484 0.01 . 2 . . . . . 28 LEU MD2 . 27574 1 266 . 1 1 28 28 LEU HD23 H 1 0.484 0.01 . 2 . . . . . 28 LEU MD2 . 27574 1 267 . 1 1 28 28 LEU C C 13 177.113 0.2 . 1 . . . . . 28 LEU C . 27574 1 268 . 1 1 28 28 LEU CA C 13 54.620 0.2 . 1 . . . . . 28 LEU CA . 27574 1 269 . 1 1 28 28 LEU CB C 13 41.989 0.2 . 1 . . . . . 28 LEU CB . 27574 1 270 . 1 1 28 28 LEU CD1 C 13 24.996 0.2 . 2 . . . . . 28 LEU CD1 . 27574 1 271 . 1 1 28 28 LEU CD2 C 13 22.649 0.2 . 2 . . . . . 28 LEU CD2 . 27574 1 272 . 1 1 29 29 GLY H H 1 7.303 0.01 . 1 . . . . . 29 GLY H . 27574 1 273 . 1 1 29 29 GLY HA2 H 1 4.184 0.01 . 2 . . . . . 29 GLY HA2 . 27574 1 274 . 1 1 29 29 GLY HA3 H 1 4.002 0.01 . 2 . . . . . 29 GLY HA3 . 27574 1 275 . 1 1 29 29 GLY C C 13 175.736 0.2 . 1 . . . . . 29 GLY C . 27574 1 276 . 1 1 29 29 GLY CA C 13 46.167 0.2 . 1 . . . . . 29 GLY CA . 27574 1 277 . 1 1 29 29 GLY N N 15 106.539 0.3 . 1 . . . . . 29 GLY N . 27574 1 278 . 1 1 30 30 TRP H H 1 7.898 0.01 . 1 . . . . . 30 TRP H . 27574 1 279 . 1 1 30 30 TRP HA H 1 5.008 0.01 . 1 . . . . . 30 TRP HA . 27574 1 280 . 1 1 30 30 TRP HB2 H 1 2.908 0.01 . 2 . . . . . 30 TRP HB2 . 27574 1 281 . 1 1 30 30 TRP HB3 H 1 2.429 0.01 . 2 . . . . . 30 TRP HB3 . 27574 1 282 . 1 1 30 30 TRP C C 13 176.380 0.2 . 1 . . . . . 30 TRP C . 27574 1 283 . 1 1 30 30 TRP CA C 13 54.321 0.2 . 1 . . . . . 30 TRP CA . 27574 1 284 . 1 1 30 30 TRP N N 15 122.764 0.3 . 1 . . . . . 30 TRP N . 27574 1 285 . 1 1 31 31 LYS H H 1 8.484 0.01 . 1 . . . . . 31 LYS H . 27574 1 286 . 1 1 31 31 LYS HA H 1 4.214 0.01 . 1 . . . . . 31 LYS HA . 27574 1 287 . 1 1 31 31 LYS HB2 H 1 2.019 0.01 . 2 . . . . . 31 LYS HB2 . 27574 1 288 . 1 1 31 31 LYS HB3 H 1 1.865 0.01 . 2 . . . . . 31 LYS HB3 . 27574 1 289 . 1 1 31 31 LYS C C 13 175.724 0.2 . 1 . . . . . 31 LYS C . 27574 1 290 . 1 1 31 31 LYS CA C 13 57.586 0.2 . 1 . . . . . 31 LYS CA . 27574 1 291 . 1 1 31 31 LYS CB C 13 32.570 0.2 . 1 . . . . . 31 LYS CB . 27574 1 292 . 1 1 31 31 LYS CG C 13 25.418 0.2 . 1 . . . . . 31 LYS CG . 27574 1 293 . 1 1 31 31 LYS CD C 13 29.564 0.2 . 1 . . . . . 31 LYS CD . 27574 1 294 . 1 1 31 31 LYS CE C 13 42.183 0.2 . 1 . . . . . 31 LYS CE . 27574 1 295 . 1 1 31 31 LYS N N 15 121.056 0.3 . 1 . . . . . 31 LYS N . 27574 1 296 . 1 1 32 32 TRP H H 1 7.165 0.01 . 1 . . . . . 32 TRP H . 27574 1 297 . 1 1 32 32 TRP HA H 1 4.575 0.01 . 1 . . . . . 32 TRP HA . 27574 1 298 . 1 1 32 32 TRP HB2 H 1 3.610 0.01 . 2 . . . . . 32 TRP HB2 . 27574 1 299 . 1 1 32 32 TRP HB3 H 1 3.099 0.01 . 2 . . . . . 32 TRP HB3 . 27574 1 300 . 1 1 32 32 TRP C C 13 175.781 0.2 . 1 . . . . . 32 TRP C . 27574 1 301 . 1 1 32 32 TRP CA C 13 55.642 0.2 . 1 . . . . . 32 TRP CA . 27574 1 302 . 1 1 32 32 TRP N N 15 114.996 0.3 . 1 . . . . . 32 TRP N . 27574 1 303 . 1 1 33 33 ILE H H 1 6.660 0.01 . 1 . . . . . 33 ILE H . 27574 1 304 . 1 1 33 33 ILE HA H 1 3.531 0.01 . 1 . . . . . 33 ILE HA . 27574 1 305 . 1 1 33 33 ILE HB H 1 1.006 0.01 . 1 . . . . . 33 ILE HB . 27574 1 306 . 1 1 33 33 ILE HG12 H 1 -0.400 0.01 . 2 . . . . . 33 ILE HG12 . 27574 1 307 . 1 1 33 33 ILE HG13 H 1 -0.400 0.01 . 2 . . . . . 33 ILE HG13 . 27574 1 308 . 1 1 33 33 ILE HG21 H 1 0.429 0.01 . 1 . . . . . 33 ILE MG . 27574 1 309 . 1 1 33 33 ILE HG22 H 1 0.429 0.01 . 1 . . . . . 33 ILE MG . 27574 1 310 . 1 1 33 33 ILE HG23 H 1 0.429 0.01 . 1 . . . . . 33 ILE MG . 27574 1 311 . 1 1 33 33 ILE HD11 H 1 -0.457 0.01 . 1 . . . . . 33 ILE MD . 27574 1 312 . 1 1 33 33 ILE HD12 H 1 -0.457 0.01 . 1 . . . . . 33 ILE MD . 27574 1 313 . 1 1 33 33 ILE HD13 H 1 -0.457 0.01 . 1 . . . . . 33 ILE MD . 27574 1 314 . 1 1 33 33 ILE C C 13 175.775 0.2 . 1 . . . . . 33 ILE C . 27574 1 315 . 1 1 33 33 ILE CA C 13 62.662 0.2 . 1 . . . . . 33 ILE CA . 27574 1 316 . 1 1 33 33 ILE CB C 13 38.021 0.2 . 1 . . . . . 33 ILE CB . 27574 1 317 . 1 1 33 33 ILE CG1 C 13 27.021 0.2 . 1 . . . . . 33 ILE CG1 . 27574 1 318 . 1 1 33 33 ILE CG2 C 13 18.224 0.2 . 1 . . . . . 33 ILE CG2 . 27574 1 319 . 1 1 33 33 ILE CD1 C 13 13.164 0.2 . 1 . . . . . 33 ILE CD1 . 27574 1 320 . 1 1 33 33 ILE N N 15 122.481 0.3 . 1 . . . . . 33 ILE N . 27574 1 321 . 1 1 34 34 HIS H H 1 8.970 0.01 . 1 . . . . . 34 HIS H . 27574 1 322 . 1 1 34 34 HIS HA H 1 4.748 0.01 . 1 . . . . . 34 HIS HA . 27574 1 323 . 1 1 34 34 HIS HB2 H 1 3.297 0.01 . 2 . . . . . 34 HIS HB2 . 27574 1 324 . 1 1 34 34 HIS HB3 H 1 3.297 0.01 . 2 . . . . . 34 HIS HB3 . 27574 1 325 . 1 1 34 34 HIS C C 13 174.274 0.2 . 1 . . . . . 34 HIS C . 27574 1 326 . 1 1 34 34 HIS CA C 13 57.554 0.2 . 1 . . . . . 34 HIS CA . 27574 1 327 . 1 1 34 34 HIS CB C 13 30.021 0.2 . 1 . . . . . 34 HIS CB . 27574 1 328 . 1 1 34 34 HIS N N 15 125.916 0.3 . 1 . . . . . 34 HIS N . 27574 1 329 . 1 1 35 35 GLU H H 1 8.036 0.01 . 1 . . . . . 35 GLU H . 27574 1 330 . 1 1 35 35 GLU CA C 13 53.671 0.2 . 1 . . . . . 35 GLU CA . 27574 1 331 . 1 1 35 35 GLU CB C 13 32.470 0.2 . 1 . . . . . 35 GLU CB . 27574 1 332 . 1 1 35 35 GLU N N 15 117.134 0.3 . 1 . . . . . 35 GLU N . 27574 1 333 . 1 1 36 36 PRO HA H 1 5.051 0.01 . 1 . . . . . 36 PRO HA . 27574 1 334 . 1 1 36 36 PRO HB2 H 1 2.770 0.01 . 2 . . . . . 36 PRO HB2 . 27574 1 335 . 1 1 36 36 PRO HB3 H 1 2.770 0.01 . 2 . . . . . 36 PRO HB3 . 27574 1 336 . 1 1 36 36 PRO C C 13 175.374 0.2 . 1 . . . . . 36 PRO C . 27574 1 337 . 1 1 36 36 PRO CA C 13 62.868 0.2 . 1 . . . . . 36 PRO CA . 27574 1 338 . 1 1 36 36 PRO CB C 13 34.813 0.2 . 1 . . . . . 36 PRO CB . 27574 1 339 . 1 1 36 36 PRO CG C 13 24.926 0.2 . 1 . . . . . 36 PRO CG . 27574 1 340 . 1 1 36 36 PRO CD C 13 49.550 0.2 . 1 . . . . . 36 PRO CD . 27574 1 341 . 1 1 37 37 LYS H H 1 8.711 0.01 . 1 . . . . . 37 LYS H . 27574 1 342 . 1 1 37 37 LYS HA H 1 4.369 0.01 . 1 . . . . . 37 LYS HA . 27574 1 343 . 1 1 37 37 LYS HB2 H 1 2.058 0.01 . 2 . . . . . 37 LYS HB2 . 27574 1 344 . 1 1 37 37 LYS HB3 H 1 1.892 0.01 . 2 . . . . . 37 LYS HB3 . 27574 1 345 . 1 1 37 37 LYS C C 13 177.047 0.2 . 1 . . . . . 37 LYS C . 27574 1 346 . 1 1 37 37 LYS CA C 13 57.889 0.2 . 1 . . . . . 37 LYS CA . 27574 1 347 . 1 1 37 37 LYS CB C 13 32.711 0.2 . 1 . . . . . 37 LYS CB . 27574 1 348 . 1 1 37 37 LYS CG C 13 25.332 0.2 . 1 . . . . . 37 LYS CG . 27574 1 349 . 1 1 37 37 LYS CD C 13 29.174 0.2 . 1 . . . . . 37 LYS CD . 27574 1 350 . 1 1 37 37 LYS CE C 13 42.529 0.2 . 1 . . . . . 37 LYS CE . 27574 1 351 . 1 1 37 37 LYS N N 15 116.264 0.3 . 1 . . . . . 37 LYS N . 27574 1 352 . 1 1 38 38 GLY H H 1 7.648 0.01 . 1 . . . . . 38 GLY H . 27574 1 353 . 1 1 38 38 GLY HA2 H 1 4.065 0.01 . 2 . . . . . 38 GLY HA2 . 27574 1 354 . 1 1 38 38 GLY HA3 H 1 3.252 0.01 . 2 . . . . . 38 GLY HA3 . 27574 1 355 . 1 1 38 38 GLY C C 13 170.508 0.2 . 1 . . . . . 38 GLY C . 27574 1 356 . 1 1 38 38 GLY CA C 13 45.886 0.2 . 1 . . . . . 38 GLY CA . 27574 1 357 . 1 1 38 38 GLY N N 15 106.070 0.3 . 1 . . . . . 38 GLY N . 27574 1 358 . 1 1 39 39 TYR H H 1 8.193 0.01 . 1 . . . . . 39 TYR H . 27574 1 359 . 1 1 39 39 TYR HA H 1 4.752 0.01 . 1 . . . . . 39 TYR HA . 27574 1 360 . 1 1 39 39 TYR HB2 H 1 2.913 0.01 . 2 . . . . . 39 TYR HB2 . 27574 1 361 . 1 1 39 39 TYR HB3 H 1 2.739 0.01 . 2 . . . . . 39 TYR HB3 . 27574 1 362 . 1 1 39 39 TYR C C 13 171.714 0.2 . 1 . . . . . 39 TYR C . 27574 1 363 . 1 1 39 39 TYR CA C 13 55.630 0.2 . 1 . . . . . 39 TYR CA . 27574 1 364 . 1 1 39 39 TYR CB C 13 40.773 0.2 . 1 . . . . . 39 TYR CB . 27574 1 365 . 1 1 39 39 TYR N N 15 116.500 0.3 . 1 . . . . . 39 TYR N . 27574 1 366 . 1 1 40 40 ASN H H 1 8.592 0.01 . 1 . . . . . 40 ASN H . 27574 1 367 . 1 1 40 40 ASN HA H 1 4.964 0.01 . 1 . . . . . 40 ASN HA . 27574 1 368 . 1 1 40 40 ASN C C 13 172.425 0.2 . 1 . . . . . 40 ASN C . 27574 1 369 . 1 1 40 40 ASN CA C 13 53.062 0.2 . 1 . . . . . 40 ASN CA . 27574 1 370 . 1 1 40 40 ASN CB C 13 38.321 0.2 . 1 . . . . . 40 ASN CB . 27574 1 371 . 1 1 40 40 ASN N N 15 120.608 0.3 . 1 . . . . . 40 ASN N . 27574 1 372 . 1 1 41 41 ALA H H 1 7.209 0.01 . 1 . . . . . 41 ALA H . 27574 1 373 . 1 1 41 41 ALA HA H 1 4.205 0.01 . 1 . . . . . 41 ALA HA . 27574 1 374 . 1 1 41 41 ALA HB1 H 1 1.215 0.01 . 1 . . . . . 41 ALA MB . 27574 1 375 . 1 1 41 41 ALA HB2 H 1 1.215 0.01 . 1 . . . . . 41 ALA MB . 27574 1 376 . 1 1 41 41 ALA HB3 H 1 1.215 0.01 . 1 . . . . . 41 ALA MB . 27574 1 377 . 1 1 41 41 ALA C C 13 177.642 0.2 . 1 . . . . . 41 ALA C . 27574 1 378 . 1 1 41 41 ALA CA C 13 55.512 0.2 . 1 . . . . . 41 ALA CA . 27574 1 379 . 1 1 41 41 ALA CB C 13 21.308 0.2 . 1 . . . . . 41 ALA CB . 27574 1 380 . 1 1 41 41 ALA N N 15 129.739 0.3 . 1 . . . . . 41 ALA N . 27574 1 381 . 1 1 42 42 ASN H H 1 7.618 0.01 . 1 . . . . . 42 ASN H . 27574 1 382 . 1 1 42 42 ASN CA C 13 55.144 0.2 . 1 . . . . . 42 ASN CA . 27574 1 383 . 1 1 42 42 ASN CB C 13 40.652 0.2 . 1 . . . . . 42 ASN CB . 27574 1 384 . 1 1 42 42 ASN N N 15 103.348 0.3 . 1 . . . . . 42 ASN N . 27574 1 385 . 1 1 43 43 PHE C C 13 172.851 0.2 . 1 . . . . . 43 PHE C . 27574 1 386 . 1 1 43 43 PHE CA C 13 57.384 0.2 . 1 . . . . . 43 PHE CA . 27574 1 387 . 1 1 43 43 PHE CB C 13 40.103 0.2 . 1 . . . . . 43 PHE CB . 27574 1 388 . 1 1 44 44 CYS H H 1 8.673 0.01 . 1 . . . . . 44 CYS H . 27574 1 389 . 1 1 44 44 CYS HA H 1 5.020 0.01 . 1 . . . . . 44 CYS HA . 27574 1 390 . 1 1 44 44 CYS HB2 H 1 2.937 0.01 . 2 . . . . . 44 CYS HB2 . 27574 1 391 . 1 1 44 44 CYS HB3 H 1 2.544 0.01 . 2 . . . . . 44 CYS HB3 . 27574 1 392 . 1 1 44 44 CYS C C 13 173.418 0.2 . 1 . . . . . 44 CYS C . 27574 1 393 . 1 1 44 44 CYS CA C 13 54.520 0.2 . 1 . . . . . 44 CYS CA . 27574 1 394 . 1 1 44 44 CYS CB C 13 42.443 0.2 . 1 . . . . . 44 CYS CB . 27574 1 395 . 1 1 44 44 CYS N N 15 118.959 0.3 . 1 . . . . . 44 CYS N . 27574 1 396 . 1 1 45 45 ALA H H 1 8.078 0.01 . 1 . . . . . 45 ALA H . 27574 1 397 . 1 1 45 45 ALA HA H 1 4.581 0.01 . 1 . . . . . 45 ALA HA . 27574 1 398 . 1 1 45 45 ALA HB1 H 1 1.551 0.01 . 1 . . . . . 45 ALA MB . 27574 1 399 . 1 1 45 45 ALA HB2 H 1 1.551 0.01 . 1 . . . . . 45 ALA MB . 27574 1 400 . 1 1 45 45 ALA HB3 H 1 1.551 0.01 . 1 . . . . . 45 ALA MB . 27574 1 401 . 1 1 45 45 ALA C C 13 176.399 0.2 . 1 . . . . . 45 ALA C . 27574 1 402 . 1 1 45 45 ALA CA C 13 52.787 0.2 . 1 . . . . . 45 ALA CA . 27574 1 403 . 1 1 45 45 ALA CB C 13 23.601 0.2 . 1 . . . . . 45 ALA CB . 27574 1 404 . 1 1 45 45 ALA N N 15 121.669 0.3 . 1 . . . . . 45 ALA N . 27574 1 405 . 1 1 46 46 GLY H H 1 8.940 0.01 . 1 . . . . . 46 GLY H . 27574 1 406 . 1 1 46 46 GLY CA C 13 43.713 0.2 . 1 . . . . . 46 GLY CA . 27574 1 407 . 1 1 46 46 GLY N N 15 111.052 0.3 . 1 . . . . . 46 GLY N . 27574 1 408 . 1 1 47 47 ALA HA H 1 4.045 0.01 . 1 . . . . . 47 ALA HA . 27574 1 409 . 1 1 47 47 ALA HB1 H 1 1.392 0.01 . 1 . . . . . 47 ALA MB . 27574 1 410 . 1 1 47 47 ALA HB2 H 1 1.392 0.01 . 1 . . . . . 47 ALA MB . 27574 1 411 . 1 1 47 47 ALA HB3 H 1 1.392 0.01 . 1 . . . . . 47 ALA MB . 27574 1 412 . 1 1 47 47 ALA C C 13 174.338 0.2 . 1 . . . . . 47 ALA C . 27574 1 413 . 1 1 47 47 ALA CA C 13 51.933 0.2 . 1 . . . . . 47 ALA CA . 27574 1 414 . 1 1 47 47 ALA CB C 13 19.381 0.2 . 1 . . . . . 47 ALA CB . 27574 1 415 . 1 1 48 48 CYS H H 1 8.342 0.01 . 1 . . . . . 48 CYS H . 27574 1 416 . 1 1 48 48 CYS HA H 1 4.327 0.01 . 1 . . . . . 48 CYS HA . 27574 1 417 . 1 1 48 48 CYS CA C 13 56.696 0.2 . 1 . . . . . 48 CYS CA . 27574 1 418 . 1 1 48 48 CYS CB C 13 33.058 0.2 . 1 . . . . . 48 CYS CB . 27574 1 419 . 1 1 48 48 CYS N N 15 123.500 0.3 . 1 . . . . . 48 CYS N . 27574 1 420 . 1 1 51 51 LEU HA H 1 4.215 0.01 . 1 . . . . . 51 LEU HA . 27574 1 421 . 1 1 51 51 LEU HB2 H 1 1.297 0.01 . 2 . . . . . 51 LEU HB2 . 27574 1 422 . 1 1 51 51 LEU HB3 H 1 1.297 0.01 . 2 . . . . . 51 LEU HB3 . 27574 1 423 . 1 1 51 51 LEU HD11 H 1 0.739 0.01 . 2 . . . . . 51 LEU MD1 . 27574 1 424 . 1 1 51 51 LEU HD12 H 1 0.739 0.01 . 2 . . . . . 51 LEU MD1 . 27574 1 425 . 1 1 51 51 LEU HD13 H 1 0.739 0.01 . 2 . . . . . 51 LEU MD1 . 27574 1 426 . 1 1 51 51 LEU HD21 H 1 0.670 0.01 . 2 . . . . . 51 LEU MD2 . 27574 1 427 . 1 1 51 51 LEU HD22 H 1 0.670 0.01 . 2 . . . . . 51 LEU MD2 . 27574 1 428 . 1 1 51 51 LEU HD23 H 1 0.670 0.01 . 2 . . . . . 51 LEU MD2 . 27574 1 429 . 1 1 51 51 LEU C C 13 176.063 0.2 . 1 . . . . . 51 LEU C . 27574 1 430 . 1 1 51 51 LEU CA C 13 54.678 0.2 . 1 . . . . . 51 LEU CA . 27574 1 431 . 1 1 51 51 LEU CB C 13 42.678 0.2 . 1 . . . . . 51 LEU CB . 27574 1 432 . 1 1 51 51 LEU CD1 C 13 24.994 0.2 . 2 . . . . . 51 LEU CD1 . 27574 1 433 . 1 1 51 51 LEU CD2 C 13 23.715 0.2 . 2 . . . . . 51 LEU CD2 . 27574 1 434 . 1 1 52 52 TRP H H 1 7.637 0.01 . 1 . . . . . 52 TRP H . 27574 1 435 . 1 1 52 52 TRP HA H 1 4.417 0.01 . 1 . . . . . 52 TRP HA . 27574 1 436 . 1 1 52 52 TRP HB2 H 1 3.136 0.01 . 2 . . . . . 52 TRP HB2 . 27574 1 437 . 1 1 52 52 TRP HB3 H 1 3.136 0.01 . 2 . . . . . 52 TRP HB3 . 27574 1 438 . 1 1 52 52 TRP C C 13 175.947 0.2 . 1 . . . . . 52 TRP C . 27574 1 439 . 1 1 52 52 TRP CA C 13 57.577 0.2 . 1 . . . . . 52 TRP CA . 27574 1 440 . 1 1 52 52 TRP N N 15 121.748 0.3 . 1 . . . . . 52 TRP N . 27574 1 441 . 1 1 53 53 SER H H 1 7.767 0.01 . 1 . . . . . 53 SER H . 27574 1 442 . 1 1 53 53 SER HA H 1 4.330 0.01 . 1 . . . . . 53 SER HA . 27574 1 443 . 1 1 53 53 SER HB2 H 1 3.658 0.01 . 2 . . . . . 53 SER HB2 . 27574 1 444 . 1 1 53 53 SER HB3 H 1 3.658 0.01 . 2 . . . . . 53 SER HB3 . 27574 1 445 . 1 1 53 53 SER C C 13 174.368 0.2 . 1 . . . . . 53 SER C . 27574 1 446 . 1 1 53 53 SER CA C 13 58.070 0.2 . 1 . . . . . 53 SER CA . 27574 1 447 . 1 1 53 53 SER CB C 13 64.132 0.2 . 1 . . . . . 53 SER CB . 27574 1 448 . 1 1 53 53 SER N N 15 116.468 0.3 . 1 . . . . . 53 SER N . 27574 1 449 . 1 1 54 54 SER H H 1 8.090 0.01 . 1 . . . . . 54 SER H . 27574 1 450 . 1 1 54 54 SER HA H 1 4.366 0.01 . 1 . . . . . 54 SER HA . 27574 1 451 . 1 1 54 54 SER HB2 H 1 3.842 0.01 . 2 . . . . . 54 SER HB2 . 27574 1 452 . 1 1 54 54 SER HB3 H 1 3.842 0.01 . 2 . . . . . 54 SER HB3 . 27574 1 453 . 1 1 54 54 SER C C 13 174.529 0.2 . 1 . . . . . 54 SER C . 27574 1 454 . 1 1 54 54 SER CA C 13 58.790 0.2 . 1 . . . . . 54 SER CA . 27574 1 455 . 1 1 54 54 SER CB C 13 63.954 0.2 . 1 . . . . . 54 SER CB . 27574 1 456 . 1 1 54 54 SER N N 15 117.188 0.3 . 1 . . . . . 54 SER N . 27574 1 457 . 1 1 55 55 ASP H H 1 8.254 0.01 . 1 . . . . . 55 ASP H . 27574 1 458 . 1 1 55 55 ASP HA H 1 4.694 0.01 . 1 . . . . . 55 ASP HA . 27574 1 459 . 1 1 55 55 ASP HB2 H 1 2.802 0.01 . 2 . . . . . 55 ASP HB2 . 27574 1 460 . 1 1 55 55 ASP HB3 H 1 2.802 0.01 . 2 . . . . . 55 ASP HB3 . 27574 1 461 . 1 1 55 55 ASP C C 13 176.268 0.2 . 1 . . . . . 55 ASP C . 27574 1 462 . 1 1 55 55 ASP CA C 13 53.917 0.2 . 1 . . . . . 55 ASP CA . 27574 1 463 . 1 1 55 55 ASP CB C 13 39.640 0.2 . 1 . . . . . 55 ASP CB . 27574 1 464 . 1 1 55 55 ASP N N 15 120.997 0.3 . 1 . . . . . 55 ASP N . 27574 1 465 . 1 1 56 56 THR H H 1 7.937 0.01 . 1 . . . . . 56 THR H . 27574 1 466 . 1 1 56 56 THR HA H 1 4.205 0.01 . 1 . . . . . 56 THR HA . 27574 1 467 . 1 1 56 56 THR HB H 1 4.217 0.01 . 1 . . . . . 56 THR HB . 27574 1 468 . 1 1 56 56 THR HG21 H 1 1.133 0.01 . 1 . . . . . 56 THR MG . 27574 1 469 . 1 1 56 56 THR HG22 H 1 1.133 0.01 . 1 . . . . . 56 THR MG . 27574 1 470 . 1 1 56 56 THR HG23 H 1 1.133 0.01 . 1 . . . . . 56 THR MG . 27574 1 471 . 1 1 56 56 THR C C 13 175.165 0.2 . 1 . . . . . 56 THR C . 27574 1 472 . 1 1 56 56 THR CA C 13 62.769 0.2 . 1 . . . . . 56 THR CA . 27574 1 473 . 1 1 56 56 THR CB C 13 69.604 0.2 . 1 . . . . . 56 THR CB . 27574 1 474 . 1 1 56 56 THR CG2 C 13 21.875 0.2 . 1 . . . . . 56 THR CG2 . 27574 1 475 . 1 1 56 56 THR N N 15 113.301 0.3 . 1 . . . . . 56 THR N . 27574 1 476 . 1 1 57 57 GLN H H 1 8.100 0.01 . 1 . . . . . 57 GLN H . 27574 1 477 . 1 1 57 57 GLN HA H 1 4.220 0.01 . 1 . . . . . 57 GLN HA . 27574 1 478 . 1 1 57 57 GLN HB2 H 1 1.952 0.01 . 2 . . . . . 57 GLN HB2 . 27574 1 479 . 1 1 57 57 GLN HB3 H 1 1.952 0.01 . 2 . . . . . 57 GLN HB3 . 27574 1 480 . 1 1 57 57 GLN C C 13 176.232 0.2 . 1 . . . . . 57 GLN C . 27574 1 481 . 1 1 57 57 GLN CA C 13 56.696 0.2 . 1 . . . . . 57 GLN CA . 27574 1 482 . 1 1 57 57 GLN CB C 13 29.092 0.2 . 1 . . . . . 57 GLN CB . 27574 1 483 . 1 1 57 57 GLN N N 15 120.870 0.3 . 1 . . . . . 57 GLN N . 27574 1 484 . 1 1 58 58 HIS H H 1 8.205 0.01 . 1 . . . . . 58 HIS H . 27574 1 485 . 1 1 58 58 HIS HA H 1 4.628 0.01 . 1 . . . . . 58 HIS HA . 27574 1 486 . 1 1 58 58 HIS HB2 H 1 3.220 0.01 . 2 . . . . . 58 HIS HB2 . 27574 1 487 . 1 1 58 58 HIS HB3 H 1 3.220 0.01 . 2 . . . . . 58 HIS HB3 . 27574 1 488 . 1 1 58 58 HIS C C 13 174.627 0.2 . 1 . . . . . 58 HIS C . 27574 1 489 . 1 1 58 58 HIS CA C 13 55.741 0.2 . 1 . . . . . 58 HIS CA . 27574 1 490 . 1 1 58 58 HIS CB C 13 28.398 0.2 . 1 . . . . . 58 HIS CB . 27574 1 491 . 1 1 58 58 HIS N N 15 117.632 0.3 . 1 . . . . . 58 HIS N . 27574 1 492 . 1 1 59 59 SER H H 1 8.099 0.01 . 1 . . . . . 59 SER H . 27574 1 493 . 1 1 59 59 SER HA H 1 4.379 0.01 . 1 . . . . . 59 SER HA . 27574 1 494 . 1 1 59 59 SER HB2 H 1 3.870 0.01 . 2 . . . . . 59 SER HB2 . 27574 1 495 . 1 1 59 59 SER HB3 H 1 3.870 0.01 . 2 . . . . . 59 SER HB3 . 27574 1 496 . 1 1 59 59 SER C C 13 174.565 0.2 . 1 . . . . . 59 SER C . 27574 1 497 . 1 1 59 59 SER CA C 13 59.006 0.2 . 1 . . . . . 59 SER CA . 27574 1 498 . 1 1 59 59 SER CB C 13 63.903 0.2 . 1 . . . . . 59 SER CB . 27574 1 499 . 1 1 59 59 SER N N 15 115.369 0.3 . 1 . . . . . 59 SER N . 27574 1 500 . 1 1 60 60 LYS H H 1 8.211 0.01 . 1 . . . . . 60 ARG H . 27574 1 501 . 1 1 60 60 LYS HA H 1 4.311 0.01 . 1 . . . . . 60 ARG HA . 27574 1 502 . 1 1 60 60 LYS HB2 H 1 1.797 0.01 . 2 . . . . . 60 ARG HB2 . 27574 1 503 . 1 1 60 60 LYS HB3 H 1 1.797 0.01 . 2 . . . . . 60 ARG HB3 . 27574 1 504 . 1 1 60 60 LYS C C 13 176.669 0.2 . 1 . . . . . 60 ARG C . 27574 1 505 . 1 1 60 60 LYS CA C 13 55.026 0.2 . 1 . . . . . 60 ARG CA . 27574 1 506 . 1 1 60 60 LYS CB C 13 32.813 0.2 . 1 . . . . . 60 ARG CB . 27574 1 507 . 1 1 60 60 LYS CG C 13 25.013 0.2 . 1 . . . . . 60 ARG CG . 27574 1 508 . 1 1 60 60 LYS CD C 13 29.243 0.2 . 1 . . . . . 60 ARG CD . 27574 1 509 . 1 1 60 60 LYS N N 15 122.533 0.3 . 1 . . . . . 60 ARG N . 27574 1 510 . 1 1 61 61 VAL H H 1 7.858 0.01 . 1 . . . . . 61 VAL H . 27574 1 511 . 1 1 61 61 VAL HA H 1 4.038 0.01 . 1 . . . . . 61 VAL HA . 27574 1 512 . 1 1 61 61 VAL HB H 1 2.013 0.01 . 1 . . . . . 61 VAL HB . 27574 1 513 . 1 1 61 61 VAL HG11 H 1 0.840 0.01 . 2 . . . . . 61 VAL MG1 . 27574 1 514 . 1 1 61 61 VAL HG12 H 1 0.840 0.01 . 2 . . . . . 61 VAL MG1 . 27574 1 515 . 1 1 61 61 VAL HG13 H 1 0.840 0.01 . 2 . . . . . 61 VAL MG1 . 27574 1 516 . 1 1 61 61 VAL HG21 H 1 0.900 0.01 . 2 . . . . . 61 VAL MG2 . 27574 1 517 . 1 1 61 61 VAL HG22 H 1 0.900 0.01 . 2 . . . . . 61 VAL MG2 . 27574 1 518 . 1 1 61 61 VAL HG23 H 1 0.900 0.01 . 2 . . . . . 61 VAL MG2 . 27574 1 519 . 1 1 61 61 VAL CA C 13 62.819 0.2 . 1 . . . . . 61 VAL CA . 27574 1 520 . 1 1 61 61 VAL CB C 13 32.311 0.2 . 1 . . . . . 61 VAL CB . 27574 1 521 . 1 1 61 61 VAL CG1 C 13 21.253 0.2 . 2 . . . . . 61 VAL CG1 . 27574 1 522 . 1 1 61 61 VAL CG2 C 13 21.253 0.2 . 2 . . . . . 61 VAL CG2 . 27574 1 523 . 1 1 61 61 VAL N N 15 119.447 0.3 . 1 . . . . . 61 VAL N . 27574 1 524 . 1 1 62 62 LEU H H 1 7.977 0.01 . 1 . . . . . 62 LEU H . 27574 1 525 . 1 1 62 62 LEU HA H 1 4.275 0.01 . 1 . . . . . 62 LEU HA . 27574 1 526 . 1 1 62 62 LEU HB2 H 1 1.558 0.01 . 2 . . . . . 62 LEU HB2 . 27574 1 527 . 1 1 62 62 LEU HB3 H 1 1.558 0.01 . 2 . . . . . 62 LEU HB3 . 27574 1 528 . 1 1 62 62 LEU HG H 1 1.510 0.01 . 1 . . . . . 62 LEU HG . 27574 1 529 . 1 1 62 62 LEU HD11 H 1 0.796 0.01 . 2 . . . . . 62 LEU MD1 . 27574 1 530 . 1 1 62 62 LEU HD12 H 1 0.796 0.01 . 2 . . . . . 62 LEU MD1 . 27574 1 531 . 1 1 62 62 LEU HD13 H 1 0.796 0.01 . 2 . . . . . 62 LEU MD1 . 27574 1 532 . 1 1 62 62 LEU HD21 H 1 0.744 0.01 . 2 . . . . . 62 LEU MD2 . 27574 1 533 . 1 1 62 62 LEU HD22 H 1 0.744 0.01 . 2 . . . . . 62 LEU MD2 . 27574 1 534 . 1 1 62 62 LEU HD23 H 1 0.744 0.01 . 2 . . . . . 62 LEU MD2 . 27574 1 535 . 1 1 62 62 LEU C C 13 177.249 0.2 . 1 . . . . . 62 LEU C . 27574 1 536 . 1 1 62 62 LEU CA C 13 55.566 0.2 . 1 . . . . . 62 LEU CA . 27574 1 537 . 1 1 62 62 LEU CB C 13 42.312 0.2 . 1 . . . . . 62 LEU CB . 27574 1 538 . 1 1 62 62 LEU CG C 13 27.176 0.2 . 1 . . . . . 62 LEU CG . 27574 1 539 . 1 1 62 62 LEU CD1 C 13 25.046 0.2 . 2 . . . . . 62 LEU CD1 . 27574 1 540 . 1 1 62 62 LEU CD2 C 13 23.774 0.2 . 2 . . . . . 62 LEU CD2 . 27574 1 541 . 1 1 62 62 LEU N N 15 124.072 0.3 . 1 . . . . . 62 LEU N . 27574 1 542 . 1 1 63 63 SER H H 1 7.980 0.01 . 1 . . . . . 63 SER H . 27574 1 543 . 1 1 63 63 SER HA H 1 4.379 0.01 . 1 . . . . . 63 SER HA . 27574 1 544 . 1 1 63 63 SER HB2 H 1 3.817 0.01 . 2 . . . . . 63 SER HB2 . 27574 1 545 . 1 1 63 63 SER HB3 H 1 3.817 0.01 . 2 . . . . . 63 SER HB3 . 27574 1 546 . 1 1 63 63 SER C C 13 174.578 0.2 . 1 . . . . . 63 SER C . 27574 1 547 . 1 1 63 63 SER CA C 13 58.677 0.2 . 1 . . . . . 63 SER CA . 27574 1 548 . 1 1 63 63 SER CB C 13 63.998 0.2 . 1 . . . . . 63 SER CB . 27574 1 549 . 1 1 63 63 SER N N 15 115.415 0.3 . 1 . . . . . 63 SER N . 27574 1 550 . 1 1 64 64 LEU H H 1 7.854 0.01 . 1 . . . . . 64 LEU H . 27574 1 551 . 1 1 64 64 LEU HA H 1 4.090 0.01 . 1 . . . . . 64 LEU HA . 27574 1 552 . 1 1 64 64 LEU HB2 H 1 1.336 0.01 . 2 . . . . . 64 LEU HB2 . 27574 1 553 . 1 1 64 64 LEU HB3 H 1 1.230 0.01 . 2 . . . . . 64 LEU HB3 . 27574 1 554 . 1 1 64 64 LEU CA C 13 55.905 0.2 . 1 . . . . . 64 LEU CA . 27574 1 555 . 1 1 64 64 LEU CB C 13 42.262 0.2 . 1 . . . . . 64 LEU CB . 27574 1 556 . 1 1 64 64 LEU CD1 C 13 24.530 0.2 . 2 . . . . . 64 LEU CD1 . 27574 1 557 . 1 1 64 64 LEU CD2 C 13 24.530 0.2 . 2 . . . . . 64 LEU CD2 . 27574 1 558 . 1 1 64 64 LEU N N 15 122.800 0.3 . 1 . . . . . 64 LEU N . 27574 1 559 . 1 1 65 65 TYR HA H 1 4.328 0.01 . 1 . . . . . 65 TYR HA . 27574 1 560 . 1 1 65 65 TYR HB2 H 1 2.808 0.01 . 2 . . . . . 65 TYR HB2 . 27574 1 561 . 1 1 65 65 TYR HB3 H 1 2.993 0.01 . 2 . . . . . 65 TYR HB3 . 27574 1 562 . 1 1 65 65 TYR CA C 13 58.121 0.2 . 1 . . . . . 65 TYR CA . 27574 1 563 . 1 1 65 65 TYR CB C 13 38.412 0.2 . 1 . . . . . 65 TYR CB . 27574 1 564 . 1 1 66 66 ASN HA H 1 4.614 0.01 . 1 . . . . . 66 ASN HA . 27574 1 565 . 1 1 66 66 ASN HB2 H 1 2.728 0.01 . 2 . . . . . 66 ASN HB2 . 27574 1 566 . 1 1 66 66 ASN HB3 H 1 2.728 0.01 . 2 . . . . . 66 ASN HB3 . 27574 1 567 . 1 1 66 66 ASN C C 13 174.822 0.2 . 1 . . . . . 66 ASN C . 27574 1 568 . 1 1 66 66 ASN CA C 13 53.580 0.2 . 1 . . . . . 66 ASN CA . 27574 1 569 . 1 1 66 66 ASN CB C 13 38.920 0.2 . 1 . . . . . 66 ASN CB . 27574 1 570 . 1 1 67 67 THR H H 1 7.780 0.01 . 1 . . . . . 67 THR H . 27574 1 571 . 1 1 67 67 THR HA H 1 4.302 0.01 . 1 . . . . . 67 THR HA . 27574 1 572 . 1 1 67 67 THR HB H 1 4.217 0.01 . 1 . . . . . 67 THR HB . 27574 1 573 . 1 1 67 67 THR HG21 H 1 1.100 0.01 . 1 . . . . . 67 THR MG . 27574 1 574 . 1 1 67 67 THR HG22 H 1 1.100 0.01 . 1 . . . . . 67 THR MG . 27574 1 575 . 1 1 67 67 THR HG23 H 1 1.100 0.01 . 1 . . . . . 67 THR MG . 27574 1 576 . 1 1 67 67 THR C C 13 174.102 0.2 . 1 . . . . . 67 THR C . 27574 1 577 . 1 1 67 67 THR CA C 13 62.218 0.2 . 1 . . . . . 67 THR CA . 27574 1 578 . 1 1 67 67 THR CB C 13 69.826 0.2 . 1 . . . . . 67 THR CB . 27574 1 579 . 1 1 67 67 THR CG2 C 13 21.725 0.2 . 1 . . . . . 67 THR CG2 . 27574 1 580 . 1 1 67 67 THR N N 15 112.681 0.3 . 1 . . . . . 67 THR N . 27574 1 581 . 1 1 68 68 ILE H H 1 7.820 0.01 . 1 . . . . . 68 ILE H . 27574 1 582 . 1 1 68 68 ILE CB C 13 38.929 0.2 . 1 . . . . . 68 ILE CB . 27574 1 583 . 1 1 68 68 ILE N N 15 120.829 0.3 . 1 . . . . . 68 ILE N . 27574 1 584 . 1 1 70 70 PRO HA H 1 4.423 0.01 . 1 . . . . . 70 PRO HA . 27574 1 585 . 1 1 70 70 PRO HB2 H 1 2.257 0.01 . 2 . . . . . 70 PRO HB2 . 27574 1 586 . 1 1 70 70 PRO HB3 H 1 1.953 0.01 . 2 . . . . . 70 PRO HB3 . 27574 1 587 . 1 1 70 70 PRO C C 13 177.048 0.2 . 1 . . . . . 70 PRO C . 27574 1 588 . 1 1 70 70 PRO CA C 13 64.145 0.2 . 1 . . . . . 70 PRO CA . 27574 1 589 . 1 1 70 70 PRO CB C 13 32.191 0.2 . 1 . . . . . 70 PRO CB . 27574 1 590 . 1 1 70 70 PRO CG C 13 27.378 0.2 . 1 . . . . . 70 PRO CG . 27574 1 591 . 1 1 70 70 PRO CD C 13 50.748 0.2 . 1 . . . . . 70 PRO CD . 27574 1 592 . 1 1 71 71 GLU H H 1 8.018 0.01 . 1 . . . . . 71 GLU H . 27574 1 593 . 1 1 71 71 GLU HA H 1 4.312 0.01 . 1 . . . . . 71 GLU HA . 27574 1 594 . 1 1 71 71 GLU HB2 H 1 2.124 0.01 . 2 . . . . . 71 GLU HB2 . 27574 1 595 . 1 1 71 71 GLU HB3 H 1 1.939 0.01 . 2 . . . . . 71 GLU HB3 . 27574 1 596 . 1 1 71 71 GLU C C 13 175.893 0.2 . 1 . . . . . 71 GLU C . 27574 1 597 . 1 1 71 71 GLU CA C 13 55.746 0.2 . 1 . . . . . 71 GLU CA . 27574 1 598 . 1 1 71 71 GLU CB C 13 28.529 0.2 . 1 . . . . . 71 GLU CB . 27574 1 599 . 1 1 71 71 GLU N N 15 117.228 0.3 . 1 . . . . . 71 GLU N . 27574 1 600 . 1 1 72 72 ALA H H 1 7.906 0.01 . 1 . . . . . 72 ALA H . 27574 1 601 . 1 1 72 72 ALA HA H 1 4.289 0.01 . 1 . . . . . 72 ALA HA . 27574 1 602 . 1 1 72 72 ALA HB1 H 1 1.369 0.01 . 1 . . . . . 72 ALA MB . 27574 1 603 . 1 1 72 72 ALA HB2 H 1 1.369 0.01 . 1 . . . . . 72 ALA MB . 27574 1 604 . 1 1 72 72 ALA HB3 H 1 1.369 0.01 . 1 . . . . . 72 ALA MB . 27574 1 605 . 1 1 72 72 ALA C C 13 178.025 0.2 . 1 . . . . . 72 ALA C . 27574 1 606 . 1 1 72 72 ALA CA C 13 52.792 0.2 . 1 . . . . . 72 ALA CA . 27574 1 607 . 1 1 72 72 ALA CB C 13 19.201 0.2 . 1 . . . . . 72 ALA CB . 27574 1 608 . 1 1 72 72 ALA N N 15 123.198 0.3 . 1 . . . . . 72 ALA N . 27574 1 609 . 1 1 73 73 SER H H 1 8.062 0.01 . 1 . . . . . 73 SER H . 27574 1 610 . 1 1 73 73 SER HA H 1 4.422 0.01 . 1 . . . . . 73 SER HA . 27574 1 611 . 1 1 73 73 SER HB2 H 1 3.862 0.01 . 2 . . . . . 73 SER HB2 . 27574 1 612 . 1 1 73 73 SER HB3 H 1 3.862 0.01 . 2 . . . . . 73 SER HB3 . 27574 1 613 . 1 1 73 73 SER C C 13 173.701 0.2 . 1 . . . . . 73 SER C . 27574 1 614 . 1 1 73 73 SER CA C 13 58.559 0.2 . 1 . . . . . 73 SER CA . 27574 1 615 . 1 1 73 73 SER CB C 13 64.226 0.2 . 1 . . . . . 73 SER CB . 27574 1 616 . 1 1 73 73 SER N N 15 114.332 0.3 . 1 . . . . . 73 SER N . 27574 1 617 . 1 1 74 74 ALA H H 1 7.952 0.01 . 1 . . . . . 74 ALA H . 27574 1 618 . 1 1 74 74 ALA HB1 H 1 1.493 0.01 . 1 . . . . . 74 ALA MB . 27574 1 619 . 1 1 74 74 ALA HB2 H 1 1.493 0.01 . 1 . . . . . 74 ALA MB . 27574 1 620 . 1 1 74 74 ALA HB3 H 1 1.493 0.01 . 1 . . . . . 74 ALA MB . 27574 1 621 . 1 1 74 74 ALA C C 13 177.046 0.2 . 1 . . . . . 74 ALA C . 27574 1 622 . 1 1 74 74 ALA CA C 13 51.844 0.2 . 1 . . . . . 74 ALA CA . 27574 1 623 . 1 1 74 74 ALA CB C 13 21.116 0.2 . 1 . . . . . 74 ALA CB . 27574 1 624 . 1 1 74 74 ALA N N 15 124.538 0.3 . 1 . . . . . 74 ALA N . 27574 1 625 . 1 1 75 75 SER H H 1 8.374 0.01 . 1 . . . . . 75 SER H . 27574 1 626 . 1 1 75 75 SER CA C 13 57.235 0.2 . 1 . . . . . 75 SER CA . 27574 1 627 . 1 1 75 75 SER CB C 13 63.725 0.2 . 1 . . . . . 75 SER CB . 27574 1 628 . 1 1 75 75 SER N N 15 116.420 0.3 . 1 . . . . . 75 SER N . 27574 1 629 . 1 1 76 76 PRO C C 13 175.210 0.2 . 1 . . . . . 76 PRO C . 27574 1 630 . 1 1 76 76 PRO CA C 13 63.161 0.2 . 1 . . . . . 76 PRO CA . 27574 1 631 . 1 1 76 76 PRO CB C 13 32.526 0.2 . 1 . . . . . 76 PRO CB . 27574 1 632 . 1 1 76 76 PRO CG C 13 27.236 0.2 . 1 . . . . . 76 PRO CG . 27574 1 633 . 1 1 76 76 PRO CD C 13 50.815 0.2 . 1 . . . . . 76 PRO CD . 27574 1 634 . 1 1 77 77 CYS H H 1 8.787 0.01 . 1 . . . . . 77 CYS H . 27574 1 635 . 1 1 77 77 CYS C C 13 172.857 0.2 . 1 . . . . . 77 CYS C . 27574 1 636 . 1 1 77 77 CYS CA C 13 53.461 0.2 . 1 . . . . . 77 CYS CA . 27574 1 637 . 1 1 77 77 CYS CB C 13 42.490 0.2 . 1 . . . . . 77 CYS CB . 27574 1 638 . 1 1 77 77 CYS N N 15 120.913 0.3 . 1 . . . . . 77 CYS N . 27574 1 639 . 1 1 78 78 CYS H H 1 8.649 0.01 . 1 . . . . . 78 CYS H . 27574 1 640 . 1 1 78 78 CYS HA H 1 4.978 0.01 . 1 . . . . . 78 CYS HA . 27574 1 641 . 1 1 78 78 CYS HB2 H 1 1.904 0.01 . 2 . . . . . 78 CYS HB2 . 27574 1 642 . 1 1 78 78 CYS HB3 H 1 1.904 0.01 . 2 . . . . . 78 CYS HB3 . 27574 1 643 . 1 1 78 78 CYS C C 13 173.197 0.2 . 1 . . . . . 78 CYS C . 27574 1 644 . 1 1 78 78 CYS CA C 13 55.198 0.2 . 1 . . . . . 78 CYS CA . 27574 1 645 . 1 1 78 78 CYS CB C 13 36.682 0.2 . 1 . . . . . 78 CYS CB . 27574 1 646 . 1 1 78 78 CYS N N 15 125.733 0.3 . 1 . . . . . 78 CYS N . 27574 1 647 . 1 1 79 79 VAL H H 1 9.207 0.01 . 1 . . . . . 79 VAL H . 27574 1 648 . 1 1 79 79 VAL HA H 1 4.873 0.01 . 1 . . . . . 79 VAL HA . 27574 1 649 . 1 1 79 79 VAL HB H 1 2.344 0.01 . 1 . . . . . 79 VAL HB . 27574 1 650 . 1 1 79 79 VAL HG11 H 1 0.877 0.01 . 2 . . . . . 79 VAL MG1 . 27574 1 651 . 1 1 79 79 VAL HG12 H 1 0.877 0.01 . 2 . . . . . 79 VAL MG1 . 27574 1 652 . 1 1 79 79 VAL HG13 H 1 0.877 0.01 . 2 . . . . . 79 VAL MG1 . 27574 1 653 . 1 1 79 79 VAL HG21 H 1 0.805 0.01 . 2 . . . . . 79 VAL MG2 . 27574 1 654 . 1 1 79 79 VAL HG22 H 1 0.805 0.01 . 2 . . . . . 79 VAL MG2 . 27574 1 655 . 1 1 79 79 VAL HG23 H 1 0.805 0.01 . 2 . . . . . 79 VAL MG2 . 27574 1 656 . 1 1 79 79 VAL C C 13 174.695 0.2 . 1 . . . . . 79 VAL C . 27574 1 657 . 1 1 79 79 VAL CA C 13 59.240 0.2 . 1 . . . . . 79 VAL CA . 27574 1 658 . 1 1 79 79 VAL CB C 13 36.302 0.2 . 1 . . . . . 79 VAL CB . 27574 1 659 . 1 1 79 79 VAL N N 15 122.918 0.3 . 1 . . . . . 79 VAL N . 27574 1 660 . 1 1 80 80 SER H H 1 8.240 0.01 . 1 . . . . . 80 SER H . 27574 1 661 . 1 1 80 80 SER HA H 1 4.804 0.01 . 1 . . . . . 80 SER HA . 27574 1 662 . 1 1 80 80 SER HB2 H 1 3.814 0.01 . 2 . . . . . 80 SER HB2 . 27574 1 663 . 1 1 80 80 SER HB3 H 1 3.814 0.01 . 2 . . . . . 80 SER HB3 . 27574 1 664 . 1 1 80 80 SER C C 13 173.742 0.2 . 1 . . . . . 80 SER C . 27574 1 665 . 1 1 80 80 SER CA C 13 59.226 0.2 . 1 . . . . . 80 SER CA . 27574 1 666 . 1 1 80 80 SER CB C 13 64.791 0.2 . 1 . . . . . 80 SER CB . 27574 1 667 . 1 1 80 80 SER N N 15 114.501 0.3 . 1 . . . . . 80 SER N . 27574 1 668 . 1 1 81 81 GLN H H 1 8.667 0.01 . 1 . . . . . 81 GLN H . 27574 1 669 . 1 1 81 81 GLN HA H 1 4.502 0.01 . 1 . . . . . 81 GLN HA . 27574 1 670 . 1 1 81 81 GLN HB2 H 1 1.932 0.01 . 2 . . . . . 81 GLN HB2 . 27574 1 671 . 1 1 81 81 GLN HB3 H 1 1.399 0.01 . 2 . . . . . 81 GLN HB3 . 27574 1 672 . 1 1 81 81 GLN C C 13 173.715 0.2 . 1 . . . . . 81 GLN C . 27574 1 673 . 1 1 81 81 GLN CA C 13 56.110 0.2 . 1 . . . . . 81 GLN CA . 27574 1 674 . 1 1 81 81 GLN CB C 13 29.477 0.2 . 1 . . . . . 81 GLN CB . 27574 1 675 . 1 1 81 81 GLN N N 15 122.226 0.3 . 1 . . . . . 81 GLN N . 27574 1 676 . 1 1 82 82 ASP H H 1 7.355 0.01 . 1 . . . . . 82 ASP H . 27574 1 677 . 1 1 82 82 ASP HA H 1 4.865 0.01 . 1 . . . . . 82 ASP HA . 27574 1 678 . 1 1 82 82 ASP HB2 H 1 2.678 0.01 . 2 . . . . . 82 ASP HB2 . 27574 1 679 . 1 1 82 82 ASP HB3 H 1 2.678 0.01 . 2 . . . . . 82 ASP HB3 . 27574 1 680 . 1 1 82 82 ASP C C 13 173.915 0.2 . 1 . . . . . 82 ASP C . 27574 1 681 . 1 1 82 82 ASP CA C 13 53.835 0.2 . 1 . . . . . 82 ASP CA . 27574 1 682 . 1 1 82 82 ASP CB C 13 41.275 0.2 . 1 . . . . . 82 ASP CB . 27574 1 683 . 1 1 82 82 ASP N N 15 117.469 0.3 . 1 . . . . . 82 ASP N . 27574 1 684 . 1 1 83 83 LEU H H 1 8.400 0.01 . 1 . . . . . 83 LEU H . 27574 1 685 . 1 1 83 83 LEU HA H 1 5.512 0.01 . 1 . . . . . 83 LEU HA . 27574 1 686 . 1 1 83 83 LEU HB2 H 1 1.726 0.01 . 2 . . . . . 83 LEU HB2 . 27574 1 687 . 1 1 83 83 LEU HB3 H 1 1.206 0.01 . 2 . . . . . 83 LEU HB3 . 27574 1 688 . 1 1 83 83 LEU C C 13 176.594 0.2 . 1 . . . . . 83 LEU C . 27574 1 689 . 1 1 83 83 LEU CA C 13 53.403 0.2 . 1 . . . . . 83 LEU CA . 27574 1 690 . 1 1 83 83 LEU CB C 13 46.101 0.2 . 1 . . . . . 83 LEU CB . 27574 1 691 . 1 1 83 83 LEU CD1 C 13 25.814 0.2 . 2 . . . . . 83 LEU CD1 . 27574 1 692 . 1 1 83 83 LEU CD2 C 13 25.814 0.2 . 2 . . . . . 83 LEU CD2 . 27574 1 693 . 1 1 83 83 LEU N N 15 124.422 0.3 . 1 . . . . . 83 LEU N . 27574 1 694 . 1 1 84 84 GLU H H 1 9.520 0.01 . 1 . . . . . 84 GLU H . 27574 1 695 . 1 1 84 84 GLU HA H 1 5.013 0.01 . 1 . . . . . 84 GLU HA . 27574 1 696 . 1 1 84 84 GLU HB2 H 1 1.754 0.01 . 2 . . . . . 84 GLU HB2 . 27574 1 697 . 1 1 84 84 GLU HB3 H 1 2.278 0.01 . 2 . . . . . 84 GLU HB3 . 27574 1 698 . 1 1 84 84 GLU CA C 13 52.761 0.2 . 1 . . . . . 84 GLU CA . 27574 1 699 . 1 1 84 84 GLU CB C 13 31.776 0.2 . 1 . . . . . 84 GLU CB . 27574 1 700 . 1 1 84 84 GLU N N 15 120.380 0.3 . 1 . . . . . 84 GLU N . 27574 1 701 . 1 1 85 85 PRO HA H 1 5.108 0.01 . 1 . . . . . 85 PRO HA . 27574 1 702 . 1 1 85 85 PRO HB2 H 1 1.727 0.01 . 2 . . . . . 85 PRO HB2 . 27574 1 703 . 1 1 85 85 PRO HB3 H 1 1.727 0.01 . 2 . . . . . 85 PRO HB3 . 27574 1 704 . 1 1 85 85 PRO C C 13 174.619 0.2 . 1 . . . . . 85 PRO C . 27574 1 705 . 1 1 85 85 PRO CA C 13 62.317 0.2 . 1 . . . . . 85 PRO CA . 27574 1 706 . 1 1 85 85 PRO CB C 13 34.169 0.2 . 1 . . . . . 85 PRO CB . 27574 1 707 . 1 1 85 85 PRO CG C 13 26.543 0.2 . 1 . . . . . 85 PRO CG . 27574 1 708 . 1 1 85 85 PRO CD C 13 50.970 0.2 . 1 . . . . . 85 PRO CD . 27574 1 709 . 1 1 86 86 LEU H H 1 8.419 0.01 . 1 . . . . . 86 LEU H . 27574 1 710 . 1 1 86 86 LEU HA H 1 4.670 0.01 . 1 . . . . . 86 LEU HA . 27574 1 711 . 1 1 86 86 LEU HB2 H 1 1.525 0.01 . 2 . . . . . 86 LEU HB2 . 27574 1 712 . 1 1 86 86 LEU HB3 H 1 1.001 0.01 . 2 . . . . . 86 LEU HB3 . 27574 1 713 . 1 1 86 86 LEU HD11 H 1 0.185 0.01 . 2 . . . . . 86 LEU MD1 . 27574 1 714 . 1 1 86 86 LEU HD12 H 1 0.185 0.01 . 2 . . . . . 86 LEU MD1 . 27574 1 715 . 1 1 86 86 LEU HD13 H 1 0.185 0.01 . 2 . . . . . 86 LEU MD1 . 27574 1 716 . 1 1 86 86 LEU HD21 H 1 0.850 0.01 . 2 . . . . . 86 LEU MD2 . 27574 1 717 . 1 1 86 86 LEU HD22 H 1 0.850 0.01 . 2 . . . . . 86 LEU MD2 . 27574 1 718 . 1 1 86 86 LEU HD23 H 1 0.850 0.01 . 2 . . . . . 86 LEU MD2 . 27574 1 719 . 1 1 86 86 LEU C C 13 175.394 0.2 . 1 . . . . . 86 LEU C . 27574 1 720 . 1 1 86 86 LEU CA C 13 53.511 0.2 . 1 . . . . . 86 LEU CA . 27574 1 721 . 1 1 86 86 LEU CB C 13 47.396 0.2 . 1 . . . . . 86 LEU CB . 27574 1 722 . 1 1 86 86 LEU CD1 C 13 26.663 0.2 . 2 . . . . . 86 LEU CD1 . 27574 1 723 . 1 1 86 86 LEU CD2 C 13 23.335 0.2 . 2 . . . . . 86 LEU CD2 . 27574 1 724 . 1 1 86 86 LEU N N 15 118.803 0.3 . 1 . . . . . 86 LEU N . 27574 1 725 . 1 1 87 87 THR H H 1 8.485 0.01 . 1 . . . . . 87 THR H . 27574 1 726 . 1 1 87 87 THR HA H 1 4.888 0.01 . 1 . . . . . 87 THR HA . 27574 1 727 . 1 1 87 87 THR HB H 1 3.970 0.01 . 1 . . . . . 87 THR HB . 27574 1 728 . 1 1 87 87 THR HG21 H 1 1.093 0.01 . 1 . . . . . 87 THR MG . 27574 1 729 . 1 1 87 87 THR HG22 H 1 1.093 0.01 . 1 . . . . . 87 THR MG . 27574 1 730 . 1 1 87 87 THR HG23 H 1 1.093 0.01 . 1 . . . . . 87 THR MG . 27574 1 731 . 1 1 87 87 THR C C 13 173.896 0.2 . 1 . . . . . 87 THR C . 27574 1 732 . 1 1 87 87 THR CA C 13 63.269 0.2 . 1 . . . . . 87 THR CA . 27574 1 733 . 1 1 87 87 THR CB C 13 69.186 0.2 . 1 . . . . . 87 THR CB . 27574 1 734 . 1 1 87 87 THR CG2 C 13 22.532 0.2 . 1 . . . . . 87 THR CG2 . 27574 1 735 . 1 1 87 87 THR N N 15 124.605 0.3 . 1 . . . . . 87 THR N . 27574 1 736 . 1 1 88 88 ILE H H 1 8.985 0.01 . 1 . . . . . 88 ILE H . 27574 1 737 . 1 1 88 88 ILE HA H 1 5.016 0.01 . 1 . . . . . 88 ILE HA . 27574 1 738 . 1 1 88 88 ILE HB H 1 1.840 0.01 . 1 . . . . . 88 ILE HB . 27574 1 739 . 1 1 88 88 ILE HG12 H 1 1.565 0.01 . 2 . . . . . 88 ILE HG12 . 27574 1 740 . 1 1 88 88 ILE HG13 H 1 1.000 0.01 . 2 . . . . . 88 ILE HG13 . 27574 1 741 . 1 1 88 88 ILE HG21 H 1 0.724 0.01 . 1 . . . . . 88 ILE MG . 27574 1 742 . 1 1 88 88 ILE HG22 H 1 0.724 0.01 . 1 . . . . . 88 ILE MG . 27574 1 743 . 1 1 88 88 ILE HG23 H 1 0.724 0.01 . 1 . . . . . 88 ILE MG . 27574 1 744 . 1 1 88 88 ILE HD11 H 1 0.756 0.01 . 1 . . . . . 88 ILE MD . 27574 1 745 . 1 1 88 88 ILE HD12 H 1 0.756 0.01 . 1 . . . . . 88 ILE MD . 27574 1 746 . 1 1 88 88 ILE HD13 H 1 0.756 0.01 . 1 . . . . . 88 ILE MD . 27574 1 747 . 1 1 88 88 ILE C C 13 173.115 0.2 . 1 . . . . . 88 ILE C . 27574 1 748 . 1 1 88 88 ILE CA C 13 59.124 0.2 . 1 . . . . . 88 ILE CA . 27574 1 749 . 1 1 88 88 ILE CB C 13 42.402 0.2 . 1 . . . . . 88 ILE CB . 27574 1 750 . 1 1 88 88 ILE CG1 C 13 26.816 0.2 . 1 . . . . . 88 ILE CG1 . 27574 1 751 . 1 1 88 88 ILE CG2 C 13 19.455 0.2 . 1 . . . . . 88 ILE CG2 . 27574 1 752 . 1 1 88 88 ILE CD1 C 13 15.774 0.2 . 1 . . . . . 88 ILE CD1 . 27574 1 753 . 1 1 88 88 ILE N N 15 120.979 0.3 . 1 . . . . . 88 ILE N . 27574 1 754 . 1 1 89 89 LEU H H 1 8.702 0.01 . 1 . . . . . 89 LEU H . 27574 1 755 . 1 1 89 89 LEU HA H 1 5.464 0.01 . 1 . . . . . 89 LEU HA . 27574 1 756 . 1 1 89 89 LEU HB2 H 1 1.704 0.01 . 2 . . . . . 89 LEU HB2 . 27574 1 757 . 1 1 89 89 LEU HB3 H 1 1.591 0.01 . 2 . . . . . 89 LEU HB3 . 27574 1 758 . 1 1 89 89 LEU HD11 H 1 0.752 0.01 . 2 . . . . . 89 LEU MD1 . 27574 1 759 . 1 1 89 89 LEU HD12 H 1 0.752 0.01 . 2 . . . . . 89 LEU MD1 . 27574 1 760 . 1 1 89 89 LEU HD13 H 1 0.752 0.01 . 2 . . . . . 89 LEU MD1 . 27574 1 761 . 1 1 89 89 LEU HD21 H 1 0.715 0.01 . 2 . . . . . 89 LEU MD2 . 27574 1 762 . 1 1 89 89 LEU HD22 H 1 0.715 0.01 . 2 . . . . . 89 LEU MD2 . 27574 1 763 . 1 1 89 89 LEU HD23 H 1 0.715 0.01 . 2 . . . . . 89 LEU MD2 . 27574 1 764 . 1 1 89 89 LEU C C 13 175.955 0.2 . 1 . . . . . 89 LEU C . 27574 1 765 . 1 1 89 89 LEU CA C 13 54.044 0.2 . 1 . . . . . 89 LEU CA . 27574 1 766 . 1 1 89 89 LEU CB C 13 45.960 0.2 . 1 . . . . . 89 LEU CB . 27574 1 767 . 1 1 89 89 LEU CG C 13 28.189 0.2 . 1 . . . . . 89 LEU CG . 27574 1 768 . 1 1 89 89 LEU CD1 C 13 25.991 0.2 . 2 . . . . . 89 LEU CD1 . 27574 1 769 . 1 1 89 89 LEU CD2 C 13 24.838 0.2 . 2 . . . . . 89 LEU CD2 . 27574 1 770 . 1 1 89 89 LEU N N 15 122.395 0.3 . 1 . . . . . 89 LEU N . 27574 1 771 . 1 1 90 90 TYR H H 1 9.302 0.01 . 1 . . . . . 90 TYR H . 27574 1 772 . 1 1 90 90 TYR HA H 1 5.004 0.01 . 1 . . . . . 90 TYR HA . 27574 1 773 . 1 1 90 90 TYR HB2 H 1 3.593 0.01 . 2 . . . . . 90 TYR HB2 . 27574 1 774 . 1 1 90 90 TYR HB3 H 1 3.047 0.01 . 2 . . . . . 90 TYR HB3 . 27574 1 775 . 1 1 90 90 TYR C C 13 170.779 0.2 . 1 . . . . . 90 TYR C . 27574 1 776 . 1 1 90 90 TYR CA C 13 55.685 0.2 . 1 . . . . . 90 TYR CA . 27574 1 777 . 1 1 90 90 TYR CB C 13 41.316 0.2 . 1 . . . . . 90 TYR CB . 27574 1 778 . 1 1 90 90 TYR N N 15 126.149 0.3 . 1 . . . . . 90 TYR N . 27574 1 779 . 1 1 91 91 TYR H H 1 8.904 0.01 . 1 . . . . . 91 TYR H . 27574 1 780 . 1 1 91 91 TYR HA H 1 4.897 0.01 . 1 . . . . . 91 TYR HA . 27574 1 781 . 1 1 91 91 TYR HB2 H 1 2.813 0.01 . 2 . . . . . 91 TYR HB2 . 27574 1 782 . 1 1 91 91 TYR HB3 H 1 2.637 0.01 . 2 . . . . . 91 TYR HB3 . 27574 1 783 . 1 1 91 91 TYR C C 13 176.383 0.2 . 1 . . . . . 91 TYR C . 27574 1 784 . 1 1 91 91 TYR CA C 13 57.397 0.2 . 1 . . . . . 91 TYR CA . 27574 1 785 . 1 1 91 91 TYR CB C 13 40.990 0.2 . 1 . . . . . 91 TYR CB . 27574 1 786 . 1 1 91 91 TYR N N 15 118.632 0.3 . 1 . . . . . 91 TYR N . 27574 1 787 . 1 1 92 92 ILE H H 1 8.303 0.01 . 1 . . . . . 92 ILE H . 27574 1 788 . 1 1 92 92 ILE HA H 1 4.254 0.01 . 1 . . . . . 92 ILE HA . 27574 1 789 . 1 1 92 92 ILE HB H 1 1.677 0.01 . 1 . . . . . 92 ILE HB . 27574 1 790 . 1 1 92 92 ILE HG12 H 1 1.375 0.01 . 2 . . . . . 92 ILE HG12 . 27574 1 791 . 1 1 92 92 ILE HG13 H 1 1.068 0.01 . 2 . . . . . 92 ILE HG13 . 27574 1 792 . 1 1 92 92 ILE HG21 H 1 0.848 0.01 . 1 . . . . . 92 ILE MG . 27574 1 793 . 1 1 92 92 ILE HG22 H 1 0.848 0.01 . 1 . . . . . 92 ILE MG . 27574 1 794 . 1 1 92 92 ILE HG23 H 1 0.848 0.01 . 1 . . . . . 92 ILE MG . 27574 1 795 . 1 1 92 92 ILE HD11 H 1 0.832 0.01 . 1 . . . . . 92 ILE MD . 27574 1 796 . 1 1 92 92 ILE HD12 H 1 0.832 0.01 . 1 . . . . . 92 ILE MD . 27574 1 797 . 1 1 92 92 ILE HD13 H 1 0.832 0.01 . 1 . . . . . 92 ILE MD . 27574 1 798 . 1 1 92 92 ILE C C 13 177.176 0.2 . 1 . . . . . 92 ILE C . 27574 1 799 . 1 1 92 92 ILE CA C 13 60.643 0.2 . 1 . . . . . 92 ILE CA . 27574 1 800 . 1 1 92 92 ILE CB C 13 38.023 0.2 . 1 . . . . . 92 ILE CB . 27574 1 801 . 1 1 92 92 ILE CG1 C 13 27.288 0.2 . 1 . . . . . 92 ILE CG1 . 27574 1 802 . 1 1 92 92 ILE CG2 C 13 17.383 0.2 . 1 . . . . . 92 ILE CG2 . 27574 1 803 . 1 1 92 92 ILE CD1 C 13 13.211 0.2 . 1 . . . . . 92 ILE CD1 . 27574 1 804 . 1 1 92 92 ILE N N 15 122.610 0.3 . 1 . . . . . 92 ILE N . 27574 1 805 . 1 1 93 93 GLY H H 1 8.796 0.01 . 1 . . . . . 93 GLY H . 27574 1 806 . 1 1 93 93 GLY HA2 H 1 4.038 0.01 . 2 . . . . . 93 GLY HA2 . 27574 1 807 . 1 1 93 93 GLY HA3 H 1 3.647 0.01 . 2 . . . . . 93 GLY HA3 . 27574 1 808 . 1 1 93 93 GLY C C 13 174.878 0.2 . 1 . . . . . 93 GLY C . 27574 1 809 . 1 1 93 93 GLY CA C 13 47.107 0.2 . 1 . . . . . 93 GLY CA . 27574 1 810 . 1 1 93 93 GLY N N 15 117.857 0.3 . 1 . . . . . 93 GLY N . 27574 1 811 . 1 1 94 94 LYS H H 1 8.725 0.01 . 1 . . . . . 94 LYS H . 27574 1 812 . 1 1 94 94 LYS HA H 1 4.359 0.01 . 1 . . . . . 94 LYS HA . 27574 1 813 . 1 1 94 94 LYS HB2 H 1 1.993 0.01 . 2 . . . . . 94 LYS HB2 . 27574 1 814 . 1 1 94 94 LYS HB3 H 1 1.774 0.01 . 2 . . . . . 94 LYS HB3 . 27574 1 815 . 1 1 94 94 LYS C C 13 176.485 0.2 . 1 . . . . . 94 LYS C . 27574 1 816 . 1 1 94 94 LYS CA C 13 56.191 0.2 . 1 . . . . . 94 LYS CA . 27574 1 817 . 1 1 94 94 LYS CB C 13 32.653 0.2 . 1 . . . . . 94 LYS CB . 27574 1 818 . 1 1 94 94 LYS N N 15 125.950 0.3 . 1 . . . . . 94 LYS N . 27574 1 819 . 1 1 95 95 THR H H 1 8.244 0.01 . 1 . . . . . 95 THR H . 27574 1 820 . 1 1 95 95 THR HA H 1 4.576 0.01 . 1 . . . . . 95 THR HA . 27574 1 821 . 1 1 95 95 THR HB H 1 4.214 0.01 . 1 . . . . . 95 THR HB . 27574 1 822 . 1 1 95 95 THR HG21 H 1 1.155 0.01 . 1 . . . . . 95 THR MG . 27574 1 823 . 1 1 95 95 THR HG22 H 1 1.155 0.01 . 1 . . . . . 95 THR MG . 27574 1 824 . 1 1 95 95 THR HG23 H 1 1.155 0.01 . 1 . . . . . 95 THR MG . 27574 1 825 . 1 1 95 95 THR CA C 13 60.472 0.2 . 1 . . . . . 95 THR CA . 27574 1 826 . 1 1 95 95 THR CB C 13 70.630 0.2 . 1 . . . . . 95 THR CB . 27574 1 827 . 1 1 95 95 THR CG2 C 13 21.500 0.2 . 1 . . . . . 95 THR CG2 . 27574 1 828 . 1 1 95 95 THR N N 15 119.419 0.3 . 1 . . . . . 95 THR N . 27574 1 829 . 1 1 96 96 PRO HA H 1 3.798 0.01 . 1 . . . . . 96 PRO HA . 27574 1 830 . 1 1 96 96 PRO HB2 H 1 1.539 0.01 . 2 . . . . . 96 PRO HB2 . 27574 1 831 . 1 1 96 96 PRO HB3 H 1 1.539 0.01 . 2 . . . . . 96 PRO HB3 . 27574 1 832 . 1 1 96 96 PRO C C 13 175.728 0.2 . 1 . . . . . 96 PRO C . 27574 1 833 . 1 1 96 96 PRO CA C 13 61.837 0.2 . 1 . . . . . 96 PRO CA . 27574 1 834 . 1 1 96 96 PRO CB C 13 32.085 0.2 . 1 . . . . . 96 PRO CB . 27574 1 835 . 1 1 96 96 PRO CG C 13 26.711 0.2 . 1 . . . . . 96 PRO CG . 27574 1 836 . 1 1 96 96 PRO CD C 13 51.063 0.2 . 1 . . . . . 96 PRO CD . 27574 1 837 . 1 1 97 97 LYS H H 1 8.726 0.01 . 1 . . . . . 97 LYS H . 27574 1 838 . 1 1 97 97 LYS HA H 1 4.254 0.01 . 1 . . . . . 97 LYS HA . 27574 1 839 . 1 1 97 97 LYS HB2 H 1 1.033 0.01 . 2 . . . . . 97 LYS HB2 . 27574 1 840 . 1 1 97 97 LYS HB3 H 1 0.546 0.01 . 2 . . . . . 97 LYS HB3 . 27574 1 841 . 1 1 97 97 LYS C C 13 173.489 0.2 . 1 . . . . . 97 LYS C . 27574 1 842 . 1 1 97 97 LYS CA C 13 53.983 0.2 . 1 . . . . . 97 LYS CA . 27574 1 843 . 1 1 97 97 LYS CB C 13 34.274 0.2 . 1 . . . . . 97 LYS CB . 27574 1 844 . 1 1 97 97 LYS CG C 13 24.377 0.2 . 1 . . . . . 97 LYS CG . 27574 1 845 . 1 1 97 97 LYS CD C 13 28.570 0.2 . 1 . . . . . 97 LYS CD . 27574 1 846 . 1 1 97 97 LYS CE C 13 42.398 0.2 . 1 . . . . . 97 LYS CE . 27574 1 847 . 1 1 97 97 LYS N N 15 123.646 0.3 . 1 . . . . . 97 LYS N . 27574 1 848 . 1 1 98 98 ILE H H 1 7.855 0.01 . 1 . . . . . 98 ILE H . 27574 1 849 . 1 1 98 98 ILE HA H 1 5.143 0.01 . 1 . . . . . 98 ILE HA . 27574 1 850 . 1 1 98 98 ILE HB H 1 1.587 0.01 . 1 . . . . . 98 ILE HB . 27574 1 851 . 1 1 98 98 ILE HG12 H 1 1.417 0.01 . 2 . . . . . 98 ILE HG12 . 27574 1 852 . 1 1 98 98 ILE HG13 H 1 1.003 0.01 . 2 . . . . . 98 ILE HG13 . 27574 1 853 . 1 1 98 98 ILE HG21 H 1 0.778 0.01 . 1 . . . . . 98 ILE MG . 27574 1 854 . 1 1 98 98 ILE HG22 H 1 0.778 0.01 . 1 . . . . . 98 ILE MG . 27574 1 855 . 1 1 98 98 ILE HG23 H 1 0.778 0.01 . 1 . . . . . 98 ILE MG . 27574 1 856 . 1 1 98 98 ILE HD11 H 1 0.762 0.01 . 1 . . . . . 98 ILE MD . 27574 1 857 . 1 1 98 98 ILE HD12 H 1 0.762 0.01 . 1 . . . . . 98 ILE MD . 27574 1 858 . 1 1 98 98 ILE HD13 H 1 0.762 0.01 . 1 . . . . . 98 ILE MD . 27574 1 859 . 1 1 98 98 ILE C C 13 176.868 0.2 . 1 . . . . . 98 ILE C . 27574 1 860 . 1 1 98 98 ILE CA C 13 59.373 0.2 . 1 . . . . . 98 ILE CA . 27574 1 861 . 1 1 98 98 ILE CB C 13 39.948 0.2 . 1 . . . . . 98 ILE CB . 27574 1 862 . 1 1 98 98 ILE CG1 C 13 28.152 0.2 . 1 . . . . . 98 ILE CG1 . 27574 1 863 . 1 1 98 98 ILE CG2 C 13 17.776 0.2 . 1 . . . . . 98 ILE CG2 . 27574 1 864 . 1 1 98 98 ILE CD1 C 13 13.126 0.2 . 1 . . . . . 98 ILE CD1 . 27574 1 865 . 1 1 98 98 ILE N N 15 121.796 0.3 . 1 . . . . . 98 ILE N . 27574 1 866 . 1 1 99 99 GLU H H 1 8.836 0.01 . 1 . . . . . 99 GLU H . 27574 1 867 . 1 1 99 99 GLU HA H 1 4.788 0.01 . 1 . . . . . 99 GLU HA . 27574 1 868 . 1 1 99 99 GLU HB2 H 1 2.267 0.01 . 2 . . . . . 99 GLU HB2 . 27574 1 869 . 1 1 99 99 GLU HB3 H 1 2.267 0.01 . 2 . . . . . 99 GLU HB3 . 27574 1 870 . 1 1 99 99 GLU C C 13 173.270 0.2 . 1 . . . . . 99 GLU C . 27574 1 871 . 1 1 99 99 GLU CA C 13 54.138 0.2 . 1 . . . . . 99 GLU CA . 27574 1 872 . 1 1 99 99 GLU CB C 13 32.496 0.2 . 1 . . . . . 99 GLU CB . 27574 1 873 . 1 1 99 99 GLU N N 15 124.534 0.3 . 1 . . . . . 99 GLU N . 27574 1 874 . 1 1 100 100 GLN H H 1 8.598 0.01 . 1 . . . . . 100 GLN H . 27574 1 875 . 1 1 100 100 GLN HA H 1 5.002 0.01 . 1 . . . . . 100 GLN HA . 27574 1 876 . 1 1 100 100 GLN HB2 H 1 1.926 0.01 . 2 . . . . . 100 GLN HB2 . 27574 1 877 . 1 1 100 100 GLN HB3 H 1 1.806 0.01 . 2 . . . . . 100 GLN HB3 . 27574 1 878 . 1 1 100 100 GLN C C 13 175.350 0.2 . 1 . . . . . 100 GLN C . 27574 1 879 . 1 1 100 100 GLN CA C 13 55.088 0.2 . 1 . . . . . 100 GLN CA . 27574 1 880 . 1 1 100 100 GLN CB C 13 30.398 0.2 . 1 . . . . . 100 GLN CB . 27574 1 881 . 1 1 100 100 GLN N N 15 121.603 0.3 . 1 . . . . . 100 GLN N . 27574 1 882 . 1 1 101 101 LEU H H 1 9.094 0.01 . 1 . . . . . 101 LEU H . 27574 1 883 . 1 1 101 101 LEU HA H 1 4.668 0.01 . 1 . . . . . 101 LEU HA . 27574 1 884 . 1 1 101 101 LEU HB2 H 1 1.815 0.01 . 2 . . . . . 101 LEU HB2 . 27574 1 885 . 1 1 101 101 LEU HB3 H 1 1.651 0.01 . 2 . . . . . 101 LEU HB3 . 27574 1 886 . 1 1 101 101 LEU HD11 H 1 0.932 0.01 . 2 . . . . . 101 LEU MD1 . 27574 1 887 . 1 1 101 101 LEU HD12 H 1 0.932 0.01 . 2 . . . . . 101 LEU MD1 . 27574 1 888 . 1 1 101 101 LEU HD13 H 1 0.932 0.01 . 2 . . . . . 101 LEU MD1 . 27574 1 889 . 1 1 101 101 LEU HD21 H 1 0.885 0.01 . 2 . . . . . 101 LEU MD2 . 27574 1 890 . 1 1 101 101 LEU HD22 H 1 0.885 0.01 . 2 . . . . . 101 LEU MD2 . 27574 1 891 . 1 1 101 101 LEU HD23 H 1 0.885 0.01 . 2 . . . . . 101 LEU MD2 . 27574 1 892 . 1 1 101 101 LEU C C 13 176.335 0.2 . 1 . . . . . 101 LEU C . 27574 1 893 . 1 1 101 101 LEU CA C 13 53.476 0.2 . 1 . . . . . 101 LEU CA . 27574 1 894 . 1 1 101 101 LEU CB C 13 42.802 0.2 . 1 . . . . . 101 LEU CB . 27574 1 895 . 1 1 101 101 LEU CD1 C 13 26.080 0.2 . 2 . . . . . 101 LEU CD1 . 27574 1 896 . 1 1 101 101 LEU CD2 C 13 23.144 0.2 . 2 . . . . . 101 LEU CD2 . 27574 1 897 . 1 1 101 101 LEU N N 15 126.928 0.3 . 1 . . . . . 101 LEU N . 27574 1 898 . 1 1 102 102 SER H H 1 8.498 0.01 . 1 . . . . . 102 SER H . 27574 1 899 . 1 1 102 102 SER HA H 1 4.079 0.01 . 1 . . . . . 102 SER HA . 27574 1 900 . 1 1 102 102 SER HB2 H 1 3.793 0.01 . 2 . . . . . 102 SER HB2 . 27574 1 901 . 1 1 102 102 SER HB3 H 1 3.793 0.01 . 2 . . . . . 102 SER HB3 . 27574 1 902 . 1 1 102 102 SER C C 13 174.478 0.2 . 1 . . . . . 102 SER C . 27574 1 903 . 1 1 102 102 SER CA C 13 59.282 0.2 . 1 . . . . . 102 SER CA . 27574 1 904 . 1 1 102 102 SER CB C 13 64.020 0.2 . 1 . . . . . 102 SER CB . 27574 1 905 . 1 1 102 102 SER N N 15 118.761 0.3 . 1 . . . . . 102 SER N . 27574 1 906 . 1 1 103 103 ASN H H 1 8.726 0.01 . 1 . . . . . 103 ASN H . 27574 1 907 . 1 1 103 103 ASN HA H 1 4.592 0.01 . 1 . . . . . 103 ASN HA . 27574 1 908 . 1 1 103 103 ASN CA C 13 51.763 0.2 . 1 . . . . . 103 ASN CA . 27574 1 909 . 1 1 103 103 ASN CB C 13 36.302 0.2 . 1 . . . . . 103 ASN CB . 27574 1 910 . 1 1 103 103 ASN N N 15 115.913 0.3 . 1 . . . . . 103 ASN N . 27574 1 911 . 1 1 104 104 MET H H 1 7.251 0.01 . 1 . . . . . 104 MET H . 27574 1 912 . 1 1 104 104 MET N N 15 113.929 0.3 . 1 . . . . . 104 MET N . 27574 1 913 . 1 1 105 105 ILE HB H 1 1.629 0.01 . 1 . . . . . 105 ILE HB . 27574 1 914 . 1 1 105 105 ILE HG12 H 1 1.344 0.01 . 2 . . . . . 105 ILE HG12 . 27574 1 915 . 1 1 105 105 ILE HG13 H 1 1.442 0.01 . 2 . . . . . 105 ILE HG13 . 27574 1 916 . 1 1 105 105 ILE HG21 H 1 0.900 0.01 . 1 . . . . . 105 ILE MG . 27574 1 917 . 1 1 105 105 ILE HG22 H 1 0.900 0.01 . 1 . . . . . 105 ILE MG . 27574 1 918 . 1 1 105 105 ILE HG23 H 1 0.900 0.01 . 1 . . . . . 105 ILE MG . 27574 1 919 . 1 1 105 105 ILE HD11 H 1 0.953 0.01 . 1 . . . . . 105 ILE MD . 27574 1 920 . 1 1 105 105 ILE HD12 H 1 0.953 0.01 . 1 . . . . . 105 ILE MD . 27574 1 921 . 1 1 105 105 ILE HD13 H 1 0.953 0.01 . 1 . . . . . 105 ILE MD . 27574 1 922 . 1 1 105 105 ILE CG2 C 13 16.909 0.2 . 1 . . . . . 105 ILE CG2 . 27574 1 923 . 1 1 105 105 ILE CD1 C 13 14.399 0.2 . 1 . . . . . 105 ILE CD1 . 27574 1 924 . 1 1 106 106 VAL C C 13 174.878 0.2 . 1 . . . . . 106 VAL C . 27574 1 925 . 1 1 106 106 VAL CA C 13 63.243 0.2 . 1 . . . . . 106 VAL CA . 27574 1 926 . 1 1 106 106 VAL CB C 13 31.662 0.2 . 1 . . . . . 106 VAL CB . 27574 1 927 . 1 1 107 107 LYS H H 1 8.754 0.01 . 1 . . . . . 107 LYS H . 27574 1 928 . 1 1 107 107 LYS HA H 1 4.467 0.01 . 1 . . . . . 107 LYS HA . 27574 1 929 . 1 1 107 107 LYS HB2 H 1 1.767 0.01 . 2 . . . . . 107 LYS HB2 . 27574 1 930 . 1 1 107 107 LYS HB3 H 1 1.602 0.01 . 2 . . . . . 107 LYS HB3 . 27574 1 931 . 1 1 107 107 LYS C C 13 176.021 0.2 . 1 . . . . . 107 LYS C . 27574 1 932 . 1 1 107 107 LYS CA C 13 55.694 0.2 . 1 . . . . . 107 LYS CA . 27574 1 933 . 1 1 107 107 LYS CB C 13 34.819 0.2 . 1 . . . . . 107 LYS CB . 27574 1 934 . 1 1 107 107 LYS CG C 13 24.993 0.2 . 1 . . . . . 107 LYS CG . 27574 1 935 . 1 1 107 107 LYS CD C 13 29.141 0.2 . 1 . . . . . 107 LYS CD . 27574 1 936 . 1 1 107 107 LYS CE C 13 42.062 0.2 . 1 . . . . . 107 LYS CE . 27574 1 937 . 1 1 107 107 LYS N N 15 125.755 0.3 . 1 . . . . . 107 LYS N . 27574 1 938 . 1 1 108 108 SER H H 1 7.814 0.01 . 1 . . . . . 108 SER H . 27574 1 939 . 1 1 108 108 SER HA H 1 5.000 0.01 . 1 . . . . . 108 SER HA . 27574 1 940 . 1 1 108 108 SER HB2 H 1 4.000 0.01 . 2 . . . . . 108 SER HB2 . 27574 1 941 . 1 1 108 108 SER HB3 H 1 3.854 0.01 . 2 . . . . . 108 SER HB3 . 27574 1 942 . 1 1 108 108 SER C C 13 173.540 0.2 . 1 . . . . . 108 SER C . 27574 1 943 . 1 1 108 108 SER CA C 13 57.470 0.2 . 1 . . . . . 108 SER CA . 27574 1 944 . 1 1 108 108 SER CB C 13 65.561 0.2 . 1 . . . . . 108 SER CB . 27574 1 945 . 1 1 108 108 SER N N 15 110.267 0.3 . 1 . . . . . 108 SER N . 27574 1 946 . 1 1 109 109 CYS H H 1 8.123 0.01 . 1 . . . . . 109 CYS H . 27574 1 947 . 1 1 109 109 CYS HA H 1 5.444 0.01 . 1 . . . . . 109 CYS HA . 27574 1 948 . 1 1 109 109 CYS HB2 H 1 2.200 0.01 . 2 . . . . . 109 CYS HB2 . 27574 1 949 . 1 1 109 109 CYS HB3 H 1 2.893 0.01 . 2 . . . . . 109 CYS HB3 . 27574 1 950 . 1 1 109 109 CYS C C 13 172.279 0.2 . 1 . . . . . 109 CYS C . 27574 1 951 . 1 1 109 109 CYS CA C 13 53.763 0.2 . 1 . . . . . 109 CYS CA . 27574 1 952 . 1 1 109 109 CYS CB C 13 44.112 0.2 . 1 . . . . . 109 CYS CB . 27574 1 953 . 1 1 109 109 CYS N N 15 118.004 0.3 . 1 . . . . . 109 CYS N . 27574 1 954 . 1 1 110 110 LYS H H 1 9.381 0.01 . 1 . . . . . 110 LYS H . 27574 1 955 . 1 1 110 110 LYS HA H 1 4.601 0.01 . 1 . . . . . 110 LYS HA . 27574 1 956 . 1 1 110 110 LYS C C 13 173.331 0.2 . 1 . . . . . 110 LYS C . 27574 1 957 . 1 1 110 110 LYS CA C 13 55.330 0.2 . 1 . . . . . 110 LYS CA . 27574 1 958 . 1 1 110 110 LYS CB C 13 35.397 0.2 . 1 . . . . . 110 LYS CB . 27574 1 959 . 1 1 110 110 LYS CG C 13 24.000 0.2 . 1 . . . . . 110 LYS CG . 27574 1 960 . 1 1 110 110 LYS CD C 13 29.826 0.2 . 1 . . . . . 110 LYS CD . 27574 1 961 . 1 1 110 110 LYS CE C 13 42.464 0.2 . 1 . . . . . 110 LYS CE . 27574 1 962 . 1 1 110 110 LYS N N 15 117.671 0.3 . 1 . . . . . 110 LYS N . 27574 1 963 . 1 1 111 111 CYS H H 1 8.310 0.01 . 1 . . . . . 111 CYS H . 27574 1 964 . 1 1 111 111 CYS HA H 1 5.200 0.01 . 1 . . . . . 111 CYS HA . 27574 1 965 . 1 1 111 111 CYS HB2 H 1 2.924 0.01 . 2 . . . . . 111 CYS HB2 . 27574 1 966 . 1 1 111 111 CYS HB3 H 1 2.800 0.01 . 2 . . . . . 111 CYS HB3 . 27574 1 967 . 1 1 111 111 CYS C C 13 175.325 0.2 . 1 . . . . . 111 CYS C . 27574 1 968 . 1 1 111 111 CYS CA C 13 56.281 0.2 . 1 . . . . . 111 CYS CA . 27574 1 969 . 1 1 111 111 CYS CB C 13 43.313 0.2 . 1 . . . . . 111 CYS CB . 27574 1 970 . 1 1 111 111 CYS N N 15 118.550 0.3 . 1 . . . . . 111 CYS N . 27574 1 971 . 1 1 112 112 SER H H 1 9.206 0.01 . 1 . . . . . 112 SER H . 27574 1 972 . 1 1 112 112 SER HA H 1 4.312 0.01 . 1 . . . . . 112 SER HA . 27574 1 973 . 1 1 112 112 SER CA C 13 59.286 0.2 . 1 . . . . . 112 SER CA . 27574 1 974 . 1 1 112 112 SER CB C 13 65.441 0.2 . 1 . . . . . 112 SER CB . 27574 1 stop_ save_