data_18848 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18848 _Entry.Title ; LTBP1 EGF3-cbEGF15 ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2012-11-20 _Entry.Accession_date 2012-11-20 _Entry.Last_release_date 2013-05-30 _Entry.Original_release_date 2013-05-30 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Ian Robertson . . . 18848 2 Penny Handford . . . 18848 3 Christina Redfield . . . 18848 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18848 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 291 18848 '15N chemical shifts' 95 18848 '1H chemical shifts' 373 18848 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2013-05-30 2012-11-20 original author . 18848 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18848 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23494870 _Citation.Full_citation . _Citation.Title 'Backbone (1)H, (13)C and (15)N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assignments' _Citation.Journal_name_full 'Biomolecular NMR assignments' _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year 2013 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ian Robertson . B. . 18848 1 2 Penny Handford . A. . 18848 1 3 Christina Redfield . . . 18848 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'calcium binding' 18848 1 EGF 18848 1 'epidermal growth factor-like domain' 18848 1 'latent transforming growth factor-beta binding protein' 18848 1 LTBP 18848 1 'NMR assignment' 18848 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18848 _Assembly.ID 1 _Assembly.Name LTBP1-E3cb15 _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 11966.3 _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 LTBP1-E3cb15 1 $LTBP1-E3cb15 A . yes native no no . . . 18848 1 2 'Calcium ions' 2 $entity_CA A . no native no no . . . 18848 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_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_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 LTBP1-E3cb15 1 CYS 12 12 SG . 1 LTBP1-E3cb15 1 CYS 23 23 SG . LTBP1-E3cb15 12 CYS SG . LTBP1-E3cb15 23 CYS SG 18848 1 2 disulfide single . 1 LTBP1-E3cb15 1 CYS 18 18 SG . 1 LTBP1-E3cb15 1 CYS 32 32 SG . LTBP1-E3cb15 18 CYS SG . LTBP1-E3cb15 32 CYS SG 18848 1 3 disulfide single . 1 LTBP1-E3cb15 1 CYS 34 34 SG . 1 LTBP1-E3cb15 1 CYS 47 47 SG . LTBP1-E3cb15 34 CYS SG . LTBP1-E3cb15 47 CYS SG 18848 1 4 disulfide single . 1 LTBP1-E3cb15 1 CYS 53 53 SG . 1 LTBP1-E3cb15 1 CYS 68 68 SG . LTBP1-E3cb15 53 CYS SG . LTBP1-E3cb15 68 CYS SG 18848 1 5 disulfide single . 1 LTBP1-E3cb15 1 CYS 63 63 SG . 1 LTBP1-E3cb15 1 CYS 77 77 SG . LTBP1-E3cb15 63 CYS SG . LTBP1-E3cb15 77 CYS SG 18848 1 6 disulfide single . 1 LTBP1-E3cb15 1 CYS 79 79 SG . 1 LTBP1-E3cb15 1 CYS 92 92 SG . LTBP1-E3cb15 79 CYS SG . LTBP1-E3cb15 92 CYS SG 18848 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_LTBP1-E3cb15 _Entity.Sf_category entity _Entity.Sf_framecode LTBP1-E3cb15 _Entity.Entry_ID 18848 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name LTBP1-E3cb15 _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 ; SASFEELQAEECGILNGCEN GRCVRVQEGYTCDCFDGYHL DTAKMTCVDVNECDELNNRM SLCKNAKCINTDGSYKCLCL PGYVPSDKPNYCTPLNTALN LEKDSDLE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 108 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 yes UNP Q14766 . LTBP1 . . . . . . . . . . . . . . 18848 1 2 no GB AAY15036 . "unknown [Homo sapiens]" . . . . . 98.15 150 100.00 100.00 2.03e-69 . . . . 18848 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 SER . 18848 1 2 2 ALA . 18848 1 3 3 SER . 18848 1 4 4 PHE . 18848 1 5 5 GLU . 18848 1 6 6 GLU . 18848 1 7 7 LEU . 18848 1 8 8 GLN . 18848 1 9 9 ALA . 18848 1 10 10 GLU . 18848 1 11 11 GLU . 18848 1 12 12 CYS . 18848 1 13 13 GLY . 18848 1 14 14 ILE . 18848 1 15 15 LEU . 18848 1 16 16 ASN . 18848 1 17 17 GLY . 18848 1 18 18 CYS . 18848 1 19 19 GLU . 18848 1 20 20 ASN . 18848 1 21 21 GLY . 18848 1 22 22 ARG . 18848 1 23 23 CYS . 18848 1 24 24 VAL . 18848 1 25 25 ARG . 18848 1 26 26 VAL . 18848 1 27 27 GLN . 18848 1 28 28 GLU . 18848 1 29 29 GLY . 18848 1 30 30 TYR . 18848 1 31 31 THR . 18848 1 32 32 CYS . 18848 1 33 33 ASP . 18848 1 34 34 CYS . 18848 1 35 35 PHE . 18848 1 36 36 ASP . 18848 1 37 37 GLY . 18848 1 38 38 TYR . 18848 1 39 39 HIS . 18848 1 40 40 LEU . 18848 1 41 41 ASP . 18848 1 42 42 THR . 18848 1 43 43 ALA . 18848 1 44 44 LYS . 18848 1 45 45 MET . 18848 1 46 46 THR . 18848 1 47 47 CYS . 18848 1 48 48 VAL . 18848 1 49 49 ASP . 18848 1 50 50 VAL . 18848 1 51 51 ASN . 18848 1 52 52 GLU . 18848 1 53 53 CYS . 18848 1 54 54 ASP . 18848 1 55 55 GLU . 18848 1 56 56 LEU . 18848 1 57 57 ASN . 18848 1 58 58 ASN . 18848 1 59 59 ARG . 18848 1 60 60 MET . 18848 1 61 61 SER . 18848 1 62 62 LEU . 18848 1 63 63 CYS . 18848 1 64 64 LYS . 18848 1 65 65 ASN . 18848 1 66 66 ALA . 18848 1 67 67 LYS . 18848 1 68 68 CYS . 18848 1 69 69 ILE . 18848 1 70 70 ASN . 18848 1 71 71 THR . 18848 1 72 72 ASP . 18848 1 73 73 GLY . 18848 1 74 74 SER . 18848 1 75 75 TYR . 18848 1 76 76 LYS . 18848 1 77 77 CYS . 18848 1 78 78 LEU . 18848 1 79 79 CYS . 18848 1 80 80 LEU . 18848 1 81 81 PRO . 18848 1 82 82 GLY . 18848 1 83 83 TYR . 18848 1 84 84 VAL . 18848 1 85 85 PRO . 18848 1 86 86 SER . 18848 1 87 87 ASP . 18848 1 88 88 LYS . 18848 1 89 89 PRO . 18848 1 90 90 ASN . 18848 1 91 91 TYR . 18848 1 92 92 CYS . 18848 1 93 93 THR . 18848 1 94 94 PRO . 18848 1 95 95 LEU . 18848 1 96 96 ASN . 18848 1 97 97 THR . 18848 1 98 98 ALA . 18848 1 99 99 LEU . 18848 1 100 100 ASN . 18848 1 101 101 LEU . 18848 1 102 102 GLU . 18848 1 103 103 LYS . 18848 1 104 104 ASP . 18848 1 105 105 SER . 18848 1 106 106 ASP . 18848 1 107 107 LEU . 18848 1 108 108 GLU . 18848 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 . SER 1 1 18848 1 . ALA 2 2 18848 1 . SER 3 3 18848 1 . PHE 4 4 18848 1 . GLU 5 5 18848 1 . GLU 6 6 18848 1 . LEU 7 7 18848 1 . GLN 8 8 18848 1 . ALA 9 9 18848 1 . GLU 10 10 18848 1 . GLU 11 11 18848 1 . CYS 12 12 18848 1 . GLY 13 13 18848 1 . ILE 14 14 18848 1 . LEU 15 15 18848 1 . ASN 16 16 18848 1 . GLY 17 17 18848 1 . CYS 18 18 18848 1 . GLU 19 19 18848 1 . ASN 20 20 18848 1 . GLY 21 21 18848 1 . ARG 22 22 18848 1 . CYS 23 23 18848 1 . VAL 24 24 18848 1 . ARG 25 25 18848 1 . VAL 26 26 18848 1 . GLN 27 27 18848 1 . GLU 28 28 18848 1 . GLY 29 29 18848 1 . TYR 30 30 18848 1 . THR 31 31 18848 1 . CYS 32 32 18848 1 . ASP 33 33 18848 1 . CYS 34 34 18848 1 . PHE 35 35 18848 1 . ASP 36 36 18848 1 . GLY 37 37 18848 1 . TYR 38 38 18848 1 . HIS 39 39 18848 1 . LEU 40 40 18848 1 . ASP 41 41 18848 1 . THR 42 42 18848 1 . ALA 43 43 18848 1 . LYS 44 44 18848 1 . MET 45 45 18848 1 . THR 46 46 18848 1 . CYS 47 47 18848 1 . VAL 48 48 18848 1 . ASP 49 49 18848 1 . VAL 50 50 18848 1 . ASN 51 51 18848 1 . GLU 52 52 18848 1 . CYS 53 53 18848 1 . ASP 54 54 18848 1 . GLU 55 55 18848 1 . LEU 56 56 18848 1 . ASN 57 57 18848 1 . ASN 58 58 18848 1 . ARG 59 59 18848 1 . MET 60 60 18848 1 . SER 61 61 18848 1 . LEU 62 62 18848 1 . CYS 63 63 18848 1 . LYS 64 64 18848 1 . ASN 65 65 18848 1 . ALA 66 66 18848 1 . LYS 67 67 18848 1 . CYS 68 68 18848 1 . ILE 69 69 18848 1 . ASN 70 70 18848 1 . THR 71 71 18848 1 . ASP 72 72 18848 1 . GLY 73 73 18848 1 . SER 74 74 18848 1 . TYR 75 75 18848 1 . LYS 76 76 18848 1 . CYS 77 77 18848 1 . LEU 78 78 18848 1 . CYS 79 79 18848 1 . LEU 80 80 18848 1 . PRO 81 81 18848 1 . GLY 82 82 18848 1 . TYR 83 83 18848 1 . VAL 84 84 18848 1 . PRO 85 85 18848 1 . SER 86 86 18848 1 . ASP 87 87 18848 1 . LYS 88 88 18848 1 . PRO 89 89 18848 1 . ASN 90 90 18848 1 . TYR 91 91 18848 1 . CYS 92 92 18848 1 . THR 93 93 18848 1 . PRO 94 94 18848 1 . LEU 95 95 18848 1 . ASN 96 96 18848 1 . THR 97 97 18848 1 . ALA 98 98 18848 1 . LEU 99 99 18848 1 . ASN 100 100 18848 1 . LEU 101 101 18848 1 . GLU 102 102 18848 1 . LYS 103 103 18848 1 . ASP 104 104 18848 1 . SER 105 105 18848 1 . ASP 106 106 18848 1 . LEU 107 107 18848 1 . GLU 108 108 18848 1 stop_ save_ save_entity_CA _Entity.Sf_category entity _Entity.Sf_framecode entity_CA _Entity.Entry_ID 18848 _Entity.ID 2 _Entity.BMRB_code CA _Entity.Name entity_CA _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic no. _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 40.078 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'CALCIUM ION' BMRB 18848 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'CALCIUM ION' BMRB 18848 2 CA 'Three letter code' 18848 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 CA $chem_comp_CA 18848 2 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 CA CA 18848 2 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 18848 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $LTBP1-E3cb15 . 9606 organism . 'Homo sapiens' Humans . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . LTBP1 . 'C-terminus of human LTBP1 from residue 1617, inclusing the EGF3- cbEGF15 domain pair' . . 18848 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 18848 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $LTBP1-E3cb15 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pQE30 . . . 'refolded in vitro via oxido-shuffling and His tag removed by factor Xa.' . . 18848 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 18848 _Chem_comp.ID CA _Chem_comp.Provenance PDB _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code CA _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _Chem_comp.Number_atoms_all 1 _Chem_comp.Number_atoms_nh 1 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Ca/q+2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic no _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 18848 CA [Ca++] SMILES CACTVS 3.341 18848 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 18848 CA [Ca+2] SMILES ACDLabs 10.04 18848 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 18848 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18848 CA InChI=1S/Ca/q+2 InChI InChI 1.03 18848 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 18848 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18848 CA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CA CA CA CA . CA . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 18848 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18848 _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 LTBP1-E3cb15 'C13- N15' . . 1 $LTBP1-E3cb15 . . 2 . . mM . . . . 18848 1 2 'calcium chloride' 'natural abundance' . . . . . . 10 . . mM . . . . 18848 1 3 H2O 'natural abundance' . . . . . . 95 . . % . . . . 18848 1 4 D2O 'natural abundance' . . . . . . 5 . . % . . . . 18848 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 18848 _Sample_condition_list.ID 1 _Sample_condition_list.Details '10mM calcium chloride' 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' 30 . mM 18848 1 pH 5.4 0.1 pH 18848 1 pressure 1 . atm 18848 1 temperature 298 . K 18848 1 stop_ save_ ############################ # Computer software used # ############################ save_Analysis _Software.Sf_category software _Software.Sf_framecode Analysis _Software.Entry_ID 18848 _Software.ID 1 _Software.Name Analysis _Software.Version 2.2.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 18848 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18848 1 stop_ save_ save_nmrpipe _Software.Sf_category software _Software.Sf_framecode nmrpipe _Software.Entry_ID 18848 _Software.ID 2 _Software.Name NMRPipe _Software.Version 'June 2006 Sun Solaris' _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 18848 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18848 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 18848 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'with TCI CryoProbe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 18848 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details 'home-built console base on the GE-Omega data acquisition system equipped with triple-axis gradient triple resonance probe' _NMR_spectrometer.Manufacturer 'Home built' _NMR_spectrometer.Model OMEGA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18848 _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 . 500 'with TCI CryoProbe' . . 18848 1 2 spectrometer_2 'Home built' OMEGA . 600 'home-built console base on the GE-Omega data acquisition system equipped with triple-axis gradient triple resonance probe' . . 18848 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 18848 _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 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 18848 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 1 3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 1 5 '3D CBCANH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 1 6 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 1 7 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 18848 1 8 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 18848 1 9 '3D HN(CA)CO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18848 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 18848 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 water protons . . . . ppm 4.75 internal indirect 0.251449530 . . . . . . . . . 18848 1 H 1 water protons . . . . ppm 4.75 internal direct 1.0 . . . . . . . . . 18848 1 N 15 water protons . . . . ppm 4.75 internal indirect 0.101329118 . . . . . . . . . 18848 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 18848 _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 0.02 _Assigned_chem_shift_list.Chem_shift_13C_err 0.2 _Assigned_chem_shift_list.Chem_shift_15N_err 0.2 _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 'approximated from digital resolution' _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' . . . 18848 1 2 '3D CBCA(CO)NH' . . . 18848 1 3 '3D HNCO' . . . 18848 1 4 '3D HNCA' . . . 18848 1 5 '3D CBCANH' . . . 18848 1 6 '3D HBHA(CO)NH' . . . 18848 1 9 '3D HN(CA)CO' . . . 18848 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 SER C C 13 174.335 0.2 . 1 . . . . 1 SER C . 18848 1 2 . 1 1 1 1 SER CA C 13 58.437 0.2 . 1 . . . . 1 SER CA . 18848 1 3 . 1 1 1 1 SER CB C 13 63.951 0.2 . 1 . . . . 1 SER CB . 18848 1 4 . 1 1 2 2 ALA H H 1 8.714 0.02 . 1 . . . . 2 ALA H . 18848 1 5 . 1 1 2 2 ALA HA H 1 4.349 0.02 . 1 . . . . 2 ALA HA . 18848 1 6 . 1 1 2 2 ALA HB1 H 1 1.356 0.02 . 1 . . . . 2 ALA HB1 . 18848 1 7 . 1 1 2 2 ALA HB2 H 1 1.356 0.02 . 1 . . . . 2 ALA HB2 . 18848 1 8 . 1 1 2 2 ALA HB3 H 1 1.356 0.02 . 1 . . . . 2 ALA HB3 . 18848 1 9 . 1 1 2 2 ALA C C 13 177.595 0.2 . 1 . . . . 2 ALA C . 18848 1 10 . 1 1 2 2 ALA CA C 13 52.721 0.2 . 1 . . . . 2 ALA CA . 18848 1 11 . 1 1 2 2 ALA CB C 13 19.552 0.2 . 1 . . . . 2 ALA CB . 18848 1 12 . 1 1 2 2 ALA N N 15 126.313 0.2 . 1 . . . . 2 ALA N . 18848 1 13 . 1 1 3 3 SER H H 1 8.289 0.02 . 1 . . . . 3 SER H . 18848 1 14 . 1 1 3 3 SER HA H 1 4.421 0.02 . 1 . . . . 3 SER HA . 18848 1 15 . 1 1 3 3 SER HB2 H 1 3.918 0.02 . 2 . . . . 3 SER HB2 . 18848 1 16 . 1 1 3 3 SER HB3 H 1 3.838 0.02 . 2 . . . . 3 SER HB3 . 18848 1 17 . 1 1 3 3 SER C C 13 174.439 0.2 . 1 . . . . 3 SER C . 18848 1 18 . 1 1 3 3 SER CA C 13 58.258 0.2 . 1 . . . . 3 SER CA . 18848 1 19 . 1 1 3 3 SER CB C 13 64.136 0.2 . 1 . . . . 3 SER CB . 18848 1 20 . 1 1 3 3 SER N N 15 115.539 0.2 . 1 . . . . 3 SER N . 18848 1 21 . 1 1 4 4 PHE H H 1 8.285 0.02 . 1 . . . . 4 PHE H . 18848 1 22 . 1 1 4 4 PHE HA H 1 4.537 0.02 . 1 . . . . 4 PHE HA . 18848 1 23 . 1 1 4 4 PHE HB2 H 1 3.087 0.02 . 2 . . . . 4 PHE HB2 . 18848 1 24 . 1 1 4 4 PHE HB3 H 1 3.089 0.02 . 2 . . . . 4 PHE HB3 . 18848 1 25 . 1 1 4 4 PHE C C 13 176.066 0.2 . 1 . . . . 4 PHE C . 18848 1 26 . 1 1 4 4 PHE CA C 13 58.764 0.2 . 1 . . . . 4 PHE CA . 18848 1 27 . 1 1 4 4 PHE CB C 13 39.488 0.2 . 1 . . . . 4 PHE CB . 18848 1 28 . 1 1 4 4 PHE N N 15 122.287 0.2 . 1 . . . . 4 PHE N . 18848 1 29 . 1 1 5 5 GLU H H 1 8.397 0.02 . 1 . . . . 5 GLU H . 18848 1 30 . 1 1 5 5 GLU HA H 1 4.193 0.02 . 1 . . . . 5 GLU HA . 18848 1 31 . 1 1 5 5 GLU HB2 H 1 1.988 0.02 . 1 . . . . 5 GLU HB2 . 18848 1 32 . 1 1 5 5 GLU HB3 H 1 1.988 0.02 . 1 . . . . 5 GLU HB3 . 18848 1 33 . 1 1 5 5 GLU C C 13 176.763 0.2 . 1 . . . . 5 GLU C . 18848 1 34 . 1 1 5 5 GLU CA C 13 57.417 0.2 . 1 . . . . 5 GLU CA . 18848 1 35 . 1 1 5 5 GLU CB C 13 30.246 0.2 . 1 . . . . 5 GLU CB . 18848 1 36 . 1 1 5 5 GLU N N 15 121.795 0.2 . 1 . . . . 5 GLU N . 18848 1 37 . 1 1 6 6 GLU H H 1 8.230 0.02 . 1 . . . . 6 GLU H . 18848 1 38 . 1 1 6 6 GLU HA H 1 4.241 0.02 . 1 . . . . 6 GLU HA . 18848 1 39 . 1 1 6 6 GLU HB2 H 1 2.046 0.02 . 1 . . . . 6 GLU HB2 . 18848 1 40 . 1 1 6 6 GLU HB3 H 1 2.046 0.02 . 1 . . . . 6 GLU HB3 . 18848 1 41 . 1 1 6 6 GLU C C 13 176.884 0.2 . 1 . . . . 6 GLU C . 18848 1 42 . 1 1 6 6 GLU CA C 13 57.134 0.2 . 1 . . . . 6 GLU CA . 18848 1 43 . 1 1 6 6 GLU CB C 13 30.206 0.2 . 1 . . . . 6 GLU CB . 18848 1 44 . 1 1 6 6 GLU N N 15 121.987 0.2 . 1 . . . . 6 GLU N . 18848 1 45 . 1 1 7 7 LEU H H 1 8.222 0.02 . 1 . . . . 7 LEU H . 18848 1 46 . 1 1 7 7 LEU HA H 1 4.327 0.02 . 1 . . . . 7 LEU HA . 18848 1 47 . 1 1 7 7 LEU HB2 H 1 1.692 0.02 . 2 . . . . 7 LEU HB2 . 18848 1 48 . 1 1 7 7 LEU HB3 H 1 1.563 0.02 . 2 . . . . 7 LEU HB3 . 18848 1 49 . 1 1 7 7 LEU C C 13 177.757 0.2 . 1 . . . . 7 LEU C . 18848 1 50 . 1 1 7 7 LEU CA C 13 55.421 0.2 . 1 . . . . 7 LEU CA . 18848 1 51 . 1 1 7 7 LEU CB C 13 42.437 0.2 . 1 . . . . 7 LEU CB . 18848 1 52 . 1 1 7 7 LEU N N 15 123.313 0.2 . 1 . . . . 7 LEU N . 18848 1 53 . 1 1 8 8 GLN H H 1 8.337 0.02 . 1 . . . . 8 GLN H . 18848 1 54 . 1 1 8 8 GLN HA H 1 4.264 0.02 . 1 . . . . 8 GLN HA . 18848 1 55 . 1 1 8 8 GLN HB2 H 1 1.985 0.02 . 2 . . . . 8 GLN HB2 . 18848 1 56 . 1 1 8 8 GLN HB3 H 1 2.117 0.02 . 2 . . . . 8 GLN HB3 . 18848 1 57 . 1 1 8 8 GLN C C 13 176.154 0.2 . 1 . . . . 8 GLN C . 18848 1 58 . 1 1 8 8 GLN CA C 13 56.114 0.2 . 1 . . . . 8 GLN CA . 18848 1 59 . 1 1 8 8 GLN CB C 13 29.436 0.2 . 1 . . . . 8 GLN CB . 18848 1 60 . 1 1 8 8 GLN N N 15 121.202 0.2 . 1 . . . . 8 GLN N . 18848 1 61 . 1 1 9 9 ALA H H 1 8.229 0.02 . 1 . . . . 9 ALA H . 18848 1 62 . 1 1 9 9 ALA HA H 1 4.265 0.02 . 1 . . . . 9 ALA HA . 18848 1 63 . 1 1 9 9 ALA HB1 H 1 1.425 0.02 . 1 . . . . 9 ALA HB1 . 18848 1 64 . 1 1 9 9 ALA HB2 H 1 1.425 0.02 . 1 . . . . 9 ALA HB2 . 18848 1 65 . 1 1 9 9 ALA HB3 H 1 1.425 0.02 . 1 . . . . 9 ALA HB3 . 18848 1 66 . 1 1 9 9 ALA C C 13 178.196 0.2 . 1 . . . . 9 ALA C . 18848 1 67 . 1 1 9 9 ALA CA C 13 53.295 0.2 . 1 . . . . 9 ALA CA . 18848 1 68 . 1 1 9 9 ALA CB C 13 19.242 0.2 . 1 . . . . 9 ALA CB . 18848 1 69 . 1 1 9 9 ALA N N 15 125.008 0.2 . 1 . . . . 9 ALA N . 18848 1 70 . 1 1 10 10 GLU H H 1 8.408 0.02 . 1 . . . . 10 GLU H . 18848 1 71 . 1 1 10 10 GLU HA H 1 4.266 0.02 . 1 . . . . 10 GLU HA . 18848 1 72 . 1 1 10 10 GLU HB2 H 1 2.004 0.02 . 2 . . . . 10 GLU HB2 . 18848 1 73 . 1 1 10 10 GLU HB3 H 1 2.093 0.02 . 2 . . . . 10 GLU HB3 . 18848 1 74 . 1 1 10 10 GLU C C 13 176.783 0.2 . 1 . . . . 10 GLU C . 18848 1 75 . 1 1 10 10 GLU CA C 13 57.144 0.2 . 1 . . . . 10 GLU CA . 18848 1 76 . 1 1 10 10 GLU CB C 13 30.219 0.2 . 1 . . . . 10 GLU CB . 18848 1 77 . 1 1 10 10 GLU N N 15 119.867 0.2 . 1 . . . . 10 GLU N . 18848 1 78 . 1 1 11 11 GLU H H 1 8.252 0.02 . 1 . . . . 11 GLU H . 18848 1 79 . 1 1 11 11 GLU HA H 1 4.228 0.02 . 1 . . . . 11 GLU HA . 18848 1 80 . 1 1 11 11 GLU HB2 H 1 1.931 0.02 . 2 . . . . 11 GLU HB2 . 18848 1 81 . 1 1 11 11 GLU HB3 H 1 2.021 0.02 . 2 . . . . 11 GLU HB3 . 18848 1 82 . 1 1 11 11 GLU C C 13 176.071 0.2 . 1 . . . . 11 GLU C . 18848 1 83 . 1 1 11 11 GLU N N 15 121.339 0.2 . 1 . . . . 11 GLU N . 18848 1 84 . 1 1 12 12 CYS H H 1 8.198 0.02 . 1 . . . . 12 CYS H . 18848 1 85 . 1 1 12 12 CYS HA H 1 4.164 0.02 . 1 . . . . 12 CYS HA . 18848 1 86 . 1 1 12 12 CYS HB3 H 1 2.987 0.02 . 1 . . . . 12 CYS HB3 . 18848 1 87 . 1 1 12 12 CYS N N 15 119.003 0.2 . 1 . . . . 12 CYS N . 18848 1 88 . 1 1 13 13 GLY HA2 H 1 3.787 0.02 . 2 . . . . 13 GLY HA2 . 18848 1 89 . 1 1 13 13 GLY HA3 H 1 3.492 0.02 . 2 . . . . 13 GLY HA3 . 18848 1 90 . 1 1 13 13 GLY C C 13 173.998 0.2 . 1 . . . . 11 GLU N . 18848 1 91 . 1 1 13 13 GLY CA C 13 46.310 0.2 . 1 . . . . 11 GLU N . 18848 1 92 . 1 1 14 14 ILE H H 1 7.438 0.02 . 1 . . . . 14 ILE H . 18848 1 93 . 1 1 14 14 ILE HA H 1 4.108 0.02 . 1 . . . . 14 ILE HA . 18848 1 94 . 1 1 14 14 ILE HB H 1 1.768 0.02 . 1 . . . . 14 ILE HB . 18848 1 95 . 1 1 14 14 ILE C C 13 176.467 0.2 . 1 . . . . 11 GLU N . 18848 1 96 . 1 1 14 14 ILE CA C 13 61.317 0.2 . 1 . . . . 14 ILE CA . 18848 1 97 . 1 1 14 14 ILE CB C 13 38.764 0.2 . 1 . . . . 14 ILE CB . 18848 1 98 . 1 1 14 14 ILE N N 15 120.774 0.2 . 1 . . . . 14 ILE N . 18848 1 99 . 1 1 15 15 LEU H H 1 8.210 0.02 . 1 . . . . 15 LEU H . 18848 1 100 . 1 1 15 15 LEU HA H 1 4.189 0.02 . 1 . . . . 15 LEU HA . 18848 1 101 . 1 1 15 15 LEU HB3 H 1 1.619 0.02 . 1 . . . . 15 LEU HB3 . 18848 1 102 . 1 1 15 15 LEU C C 13 177.293 0.2 . 1 . . . . 15 LEU C . 18848 1 103 . 1 1 15 15 LEU CA C 13 56.334 0.2 . 1 . . . . 15 LEU CA . 18848 1 104 . 1 1 15 15 LEU N N 15 126.441 0.2 . 1 . . . . 15 LEU N . 18848 1 105 . 1 1 16 16 ASN H H 1 8.378 0.02 . 1 . . . . 16 ASN H . 18848 1 106 . 1 1 16 16 ASN HA H 1 4.553 0.02 . 1 . . . . 16 ASN HA . 18848 1 107 . 1 1 16 16 ASN HB2 H 1 2.855 0.02 . 2 . . . . 16 ASN HB2 . 18848 1 108 . 1 1 16 16 ASN HB3 H 1 2.752 0.02 . 2 . . . . 16 ASN HB3 . 18848 1 109 . 1 1 16 16 ASN C C 13 175.315 0.2 . 1 . . . . 16 ASN C . 18848 1 110 . 1 1 16 16 ASN CA C 13 53.924 0.2 . 1 . . . . 16 ASN CA . 18848 1 111 . 1 1 16 16 ASN CB C 13 38.598 0.2 . 1 . . . . 16 ASN CB . 18848 1 112 . 1 1 16 16 ASN N N 15 117.954 0.2 . 1 . . . . 16 ASN N . 18848 1 113 . 1 1 17 17 GLY H H 1 7.970 0.02 . 1 . . . . 17 GLY H . 18848 1 114 . 1 1 17 17 GLY HA2 H 1 3.913 0.02 . 1 . . . . 17 GLY HA2 . 18848 1 115 . 1 1 17 17 GLY HA3 H 1 3.913 0.02 . 1 . . . . 17 GLY HA3 . 18848 1 116 . 1 1 17 17 GLY C C 13 173.439 0.2 . 1 . . . . 17 GLY C . 18848 1 117 . 1 1 17 17 GLY CA C 13 45.603 0.2 . 1 . . . . 17 GLY CA . 18848 1 118 . 1 1 17 17 GLY N N 15 107.458 0.2 . 1 . . . . 17 GLY N . 18848 1 119 . 1 1 18 18 CYS H H 1 8.488 0.02 . 1 . . . . 18 CYS H . 18848 1 120 . 1 1 18 18 CYS HA H 1 4.358 0.02 . 1 . . . . 18 CYS HA . 18848 1 121 . 1 1 18 18 CYS HB2 H 1 2.632 0.02 . 2 . . . . 18 CYS HB2 . 18848 1 122 . 1 1 18 18 CYS HB3 H 1 2.463 0.02 . 2 . . . . 18 CYS HB3 . 18848 1 123 . 1 1 18 18 CYS C C 13 173.860 0.2 . 1 . . . . 18 CYS C . 18848 1 124 . 1 1 18 18 CYS CA C 13 55.040 0.2 . 1 . . . . 18 CYS CA . 18848 1 125 . 1 1 18 18 CYS N N 15 115.970 0.2 . 1 . . . . 18 CYS N . 18848 1 126 . 1 1 19 19 GLU HA H 1 4.016 0.02 . 1 . . . . 19 GLU HA . 18848 1 127 . 1 1 19 19 GLU HB2 H 1 1.898 0.02 . 1 . . . . 19 GLU HB2 . 18848 1 128 . 1 1 19 19 GLU C C 13 176.181 0.2 . 1 . . . . 19 GLU C . 18848 1 129 . 1 1 19 19 GLU CA C 13 57.573 0.2 . 1 . . . . 19 GLU CA . 18848 1 130 . 1 1 20 20 ASN H H 1 8.653 0.02 . 1 . . . . 20 ASN H . 18848 1 131 . 1 1 20 20 ASN HA H 1 3.823 0.02 . 1 . . . . 20 ASN HA . 18848 1 132 . 1 1 20 20 ASN HB2 H 1 1.143 0.02 . 2 . . . . 20 ASN HB2 . 18848 1 133 . 1 1 20 20 ASN HB3 H 1 2.179 0.02 . 2 . . . . 20 ASN HB3 . 18848 1 134 . 1 1 20 20 ASN C C 13 172.208 0.2 . 1 . . . . 20 ASN C . 18848 1 135 . 1 1 20 20 ASN CA C 13 54.352 0.2 . 1 . . . . 20 ASN CA . 18848 1 136 . 1 1 20 20 ASN CB C 13 36.574 0.2 . 1 . . . . 20 ASN CB . 18848 1 137 . 1 1 20 20 ASN N N 15 117.413 0.2 . 1 . . . . 20 ASN N . 18848 1 138 . 1 1 21 21 GLY H H 1 6.840 0.02 . 1 . . . . 21 GLY H . 18848 1 139 . 1 1 21 21 GLY HA2 H 1 3.325 0.02 . 2 . . . . 21 GLY HA2 . 18848 1 140 . 1 1 21 21 GLY HA3 H 1 2.891 0.02 . 2 . . . . 21 GLY HA3 . 18848 1 141 . 1 1 21 21 GLY C C 13 170.550 0.2 . 1 . . . . 21 GLY C . 18848 1 142 . 1 1 21 21 GLY CA C 13 45.751 0.2 . 1 . . . . 21 GLY CA . 18848 1 143 . 1 1 21 21 GLY N N 15 104.570 0.2 . 1 . . . . 21 GLY N . 18848 1 144 . 1 1 22 22 ARG H H 1 7.924 0.02 . 1 . . . . 22 ARG H . 18848 1 145 . 1 1 22 22 ARG HA H 1 4.678 0.02 . 1 . . . . 22 ARG HA . 18848 1 146 . 1 1 22 22 ARG HB2 H 1 1.754 0.02 . 2 . . . . 22 ARG HB2 . 18848 1 147 . 1 1 22 22 ARG HB3 H 1 1.810 0.02 . 2 . . . . 22 ARG HB3 . 18848 1 148 . 1 1 22 22 ARG C C 13 174.707 0.2 . 1 . . . . 22 ARG C . 18848 1 149 . 1 1 22 22 ARG CA C 13 53.802 0.2 . 1 . . . . 22 ARG CA . 18848 1 150 . 1 1 22 22 ARG CB C 13 33.505 0.2 . 1 . . . . 22 ARG CB . 18848 1 151 . 1 1 22 22 ARG N N 15 118.018 0.2 . 1 . . . . 22 ARG N . 18848 1 152 . 1 1 23 23 CYS H H 1 9.058 0.02 . 1 . . . . 23 CYS H . 18848 1 153 . 1 1 23 23 CYS HA H 1 5.121 0.02 . 1 . . . . 23 CYS HA . 18848 1 154 . 1 1 23 23 CYS HB2 H 1 3.354 0.02 . 2 . . . . 23 CYS HB2 . 18848 1 155 . 1 1 23 23 CYS HB3 H 1 2.889 0.02 . 2 . . . . 23 CYS HB3 . 18848 1 156 . 1 1 23 23 CYS C C 13 173.957 0.2 . 1 . . . . 23 CYS C . 18848 1 157 . 1 1 23 23 CYS CA C 13 56.366 0.2 . 1 . . . . 23 CYS CA . 18848 1 158 . 1 1 23 23 CYS CB C 13 42.754 0.2 . 1 . . . . 23 CYS CB . 18848 1 159 . 1 1 23 23 CYS N N 15 125.912 0.2 . 1 . . . . 23 CYS N . 18848 1 160 . 1 1 24 24 VAL H H 1 8.950 0.02 . 1 . . . . 24 VAL H . 18848 1 161 . 1 1 24 24 VAL HA H 1 4.599 0.02 . 1 . . . . 24 VAL HA . 18848 1 162 . 1 1 24 24 VAL HB H 1 1.946 0.02 . 1 . . . . 24 VAL HB . 18848 1 163 . 1 1 24 24 VAL C C 13 174.094 0.2 . 1 . . . . 24 VAL C . 18848 1 164 . 1 1 24 24 VAL CA C 13 60.563 0.2 . 1 . . . . 24 VAL CA . 18848 1 165 . 1 1 24 24 VAL CB C 13 35.710 0.2 . 1 . . . . 24 VAL CB . 18848 1 166 . 1 1 24 24 VAL N N 15 125.920 0.2 . 1 . . . . 24 VAL N . 18848 1 167 . 1 1 25 25 ARG H H 1 8.637 0.02 . 1 . . . . 25 ARG H . 18848 1 168 . 1 1 25 25 ARG HA H 1 4.286 0.02 . 1 . . . . 25 ARG HA . 18848 1 169 . 1 1 25 25 ARG HB2 H 1 1.523 0.02 . 1 . . . . 25 ARG HB2 . 18848 1 170 . 1 1 25 25 ARG C C 13 176.181 0.2 . 1 . . . . 25 ARG C . 18848 1 171 . 1 1 25 25 ARG CA C 13 56.032 0.2 . 1 . . . . 25 ARG CA . 18848 1 172 . 1 1 25 25 ARG N N 15 125.608 0.2 . 1 . . . . 25 ARG N . 18848 1 173 . 1 1 26 26 VAL H H 1 8.211 0.02 . 1 . . . . 26 VAL H . 18848 1 174 . 1 1 26 26 VAL HA H 1 4.429 0.02 . 1 . . . . 26 VAL HA . 18848 1 175 . 1 1 26 26 VAL HB H 1 2.193 0.02 . 1 . . . . 26 VAL HB . 18848 1 176 . 1 1 26 26 VAL C C 13 175.929 0.2 . 1 . . . . 26 VAL C . 18848 1 177 . 1 1 26 26 VAL CA C 13 60.239 0.2 . 1 . . . . 26 VAL CA . 18848 1 178 . 1 1 26 26 VAL CB C 13 33.985 0.2 . 1 . . . . 26 VAL CB . 18848 1 179 . 1 1 26 26 VAL N N 15 122.471 0.2 . 1 . . . . 26 VAL N . 18848 1 180 . 1 1 27 27 GLN H H 1 8.717 0.02 . 1 . . . . 27 GLN H . 18848 1 181 . 1 1 27 27 GLN HA H 1 3.847 0.02 . 1 . . . . 27 GLN HA . 18848 1 182 . 1 1 27 27 GLN HB2 H 1 2.172 0.02 . 2 . . . . 27 GLN HB2 . 18848 1 183 . 1 1 27 27 GLN HB3 H 1 2.072 0.02 . 2 . . . . 27 GLN HB3 . 18848 1 184 . 1 1 27 27 GLN C C 13 177.052 0.2 . 1 . . . . 27 GLN C . 18848 1 185 . 1 1 27 27 GLN CA C 13 59.481 0.2 . 1 . . . . 27 GLN CA . 18848 1 186 . 1 1 27 27 GLN CB C 13 27.696 0.2 . 1 . . . . 27 GLN CB . 18848 1 187 . 1 1 27 27 GLN N N 15 123.006 0.2 . 1 . . . . 27 GLN N . 18848 1 188 . 1 1 28 28 GLU H H 1 8.525 0.02 . 1 . . . . 28 GLU H . 18848 1 189 . 1 1 28 28 GLU HA H 1 4.317 0.02 . 1 . . . . 28 GLU HA . 18848 1 190 . 1 1 28 28 GLU HB2 H 1 2.185 0.02 . 2 . . . . 28 GLU HB2 . 18848 1 191 . 1 1 28 28 GLU HB3 H 1 1.954 0.02 . 2 . . . . 28 GLU HB3 . 18848 1 192 . 1 1 28 28 GLU C C 13 175.755 0.2 . 1 . . . . 28 GLU C . 18848 1 193 . 1 1 28 28 GLU CA C 13 56.813 0.2 . 1 . . . . 28 GLU CA . 18848 1 194 . 1 1 28 28 GLU CB C 13 29.270 0.2 . 1 . . . . 28 GLU CB . 18848 1 195 . 1 1 28 28 GLU N N 15 117.421 0.2 . 1 . . . . 28 GLU N . 18848 1 196 . 1 1 29 29 GLY H H 1 7.621 0.02 . 1 . . . . 29 GLY H . 18848 1 197 . 1 1 29 29 GLY HA2 H 1 3.871 0.02 . 2 . . . . 29 GLY HA2 . 18848 1 198 . 1 1 29 29 GLY HA3 H 1 4.169 0.02 . 2 . . . . 29 GLY HA3 . 18848 1 199 . 1 1 29 29 GLY C C 13 171.805 0.2 . 1 . . . . 29 GLY C . 18848 1 200 . 1 1 29 29 GLY CA C 13 45.273 0.2 . 1 . . . . 29 GLY CA . 18848 1 201 . 1 1 29 29 GLY N N 15 109.639 0.2 . 1 . . . . 29 GLY N . 18848 1 202 . 1 1 30 30 TYR H H 1 8.411 0.02 . 1 . . . . 30 TYR H . 18848 1 203 . 1 1 30 30 TYR HA H 1 5.375 0.02 . 1 . . . . 30 TYR HA . 18848 1 204 . 1 1 30 30 TYR HB2 H 1 2.984 0.02 . 2 . . . . 30 TYR HB2 . 18848 1 205 . 1 1 30 30 TYR HB3 H 1 2.741 0.02 . 2 . . . . 30 TYR HB3 . 18848 1 206 . 1 1 30 30 TYR C C 13 174.829 0.2 . 1 . . . . 30 TYR C . 18848 1 207 . 1 1 30 30 TYR CA C 13 57.392 0.2 . 1 . . . . 30 TYR CA . 18848 1 208 . 1 1 30 30 TYR CB C 13 42.048 0.2 . 1 . . . . 30 TYR CB . 18848 1 209 . 1 1 30 30 TYR N N 15 120.842 0.2 . 1 . . . . 30 TYR N . 18848 1 210 . 1 1 31 31 THR H H 1 9.126 0.02 . 1 . . . . 31 THR H . 18848 1 211 . 1 1 31 31 THR HA H 1 4.605 0.02 . 1 . . . . 31 THR HA . 18848 1 212 . 1 1 31 31 THR HB H 1 3.960 0.02 . 1 . . . . 31 THR HB . 18848 1 213 . 1 1 31 31 THR HG21 H 1 0.784 0.02 . 1 . . . . 31 THR HG21 . 18848 1 214 . 1 1 31 31 THR HG22 H 1 0.784 0.02 . 1 . . . . 31 THR HG22 . 18848 1 215 . 1 1 31 31 THR HG23 H 1 0.784 0.02 . 1 . . . . 31 THR HG23 . 18848 1 216 . 1 1 31 31 THR C C 13 172.146 0.2 . 1 . . . . 31 THR C . 18848 1 217 . 1 1 31 31 THR CA C 13 59.571 0.2 . 1 . . . . 31 THR CA . 18848 1 218 . 1 1 31 31 THR CB C 13 69.874 0.2 . 1 . . . . 31 THR CB . 18848 1 219 . 1 1 31 31 THR N N 15 116.268 0.2 . 1 . . . . 31 THR N . 18848 1 220 . 1 1 32 32 CYS H H 1 7.728 0.02 . 1 . . . . 32 CYS H . 18848 1 221 . 1 1 32 32 CYS HA H 1 5.427 0.02 . 1 . . . . 32 CYS HA . 18848 1 222 . 1 1 32 32 CYS HB2 H 1 2.477 0.02 . 2 . . . . 32 CYS HB2 . 18848 1 223 . 1 1 32 32 CYS HB3 H 1 2.359 0.02 . 2 . . . . 32 CYS HB3 . 18848 1 224 . 1 1 32 32 CYS C C 13 173.192 0.2 . 1 . . . . 32 CYS C . 18848 1 225 . 1 1 32 32 CYS CA C 13 52.266 0.2 . 1 . . . . 32 CYS CA . 18848 1 226 . 1 1 32 32 CYS CB C 13 40.366 0.2 . 1 . . . . 32 CYS CB . 18848 1 227 . 1 1 32 32 CYS N N 15 118.076 0.2 . 1 . . . . 32 CYS N . 18848 1 228 . 1 1 33 33 ASP H H 1 9.176 0.02 . 1 . . . . 33 ASP H . 18848 1 229 . 1 1 33 33 ASP HA H 1 4.847 0.02 . 1 . . . . 33 ASP HA . 18848 1 230 . 1 1 33 33 ASP HB2 H 1 2.448 0.02 . 2 . . . . 33 ASP HB2 . 18848 1 231 . 1 1 33 33 ASP HB3 H 1 2.762 0.02 . 2 . . . . 33 ASP HB3 . 18848 1 232 . 1 1 33 33 ASP C C 13 176.646 0.2 . 1 . . . . 33 ASP C . 18848 1 233 . 1 1 33 33 ASP CA C 13 52.826 0.2 . 1 . . . . 33 ASP CA . 18848 1 234 . 1 1 33 33 ASP CB C 13 41.738 0.2 . 1 . . . . 33 ASP CB . 18848 1 235 . 1 1 33 33 ASP N N 15 126.117 0.2 . 1 . . . . 33 ASP N . 18848 1 236 . 1 1 34 34 CYS H H 1 8.471 0.02 . 1 . . . . 34 CYS H . 18848 1 237 . 1 1 34 34 CYS HB3 H 1 2.711 0.02 . 1 . . . . 34 CYS HB3 . 18848 1 238 . 1 1 34 34 CYS C C 13 175.448 0.2 . 1 . . . . 34 CYS C . 18848 1 239 . 1 1 34 34 CYS CA C 13 53.737 0.2 . 1 . . . . 34 CYS CA . 18848 1 240 . 1 1 34 34 CYS CB C 13 37.520 0.2 . 1 . . . . 34 CYS CB . 18848 1 241 . 1 1 34 34 CYS N N 15 123.982 0.2 . 1 . . . . 34 CYS N . 18848 1 242 . 1 1 35 35 PHE H H 1 8.470 0.02 . 1 . . . . 35 PHE H . 18848 1 243 . 1 1 35 35 PHE HA H 1 4.969 0.02 . 1 . . . . 35 PHE HA . 18848 1 244 . 1 1 35 35 PHE HB2 H 1 3.596 0.02 . 2 . . . . 35 PHE HB2 . 18848 1 245 . 1 1 35 35 PHE HB3 H 1 2.840 0.02 . 2 . . . . 35 PHE HB3 . 18848 1 246 . 1 1 35 35 PHE C C 13 175.324 0.2 . 1 . . . . 35 PHE C . 18848 1 247 . 1 1 35 35 PHE CA C 13 55.000 0.2 . 1 . . . . 35 PHE CA . 18848 1 248 . 1 1 35 35 PHE CB C 13 38.532 0.2 . 1 . . . . 35 PHE CB . 18848 1 249 . 1 1 35 35 PHE N N 15 123.068 0.2 . 1 . . . . 35 PHE N . 18848 1 250 . 1 1 36 36 ASP H H 1 8.602 0.02 . 1 . . . . 36 ASP H . 18848 1 251 . 1 1 36 36 ASP HA H 1 4.572 0.02 . 1 . . . . 36 ASP HA . 18848 1 252 . 1 1 36 36 ASP HB2 H 1 2.743 0.02 . 1 . . . . 36 ASP HB2 . 18848 1 253 . 1 1 36 36 ASP HB3 H 1 2.743 0.02 . 1 . . . . 36 ASP HB3 . 18848 1 254 . 1 1 36 36 ASP C C 13 176.618 0.2 . 1 . . . . 36 ASP C . 18848 1 255 . 1 1 36 36 ASP CA C 13 56.558 0.2 . 1 . . . . 36 ASP CA . 18848 1 256 . 1 1 36 36 ASP CB C 13 40.861 0.2 . 1 . . . . 36 ASP CB . 18848 1 257 . 1 1 36 36 ASP N N 15 120.469 0.2 . 1 . . . . 36 ASP N . 18848 1 258 . 1 1 37 37 GLY H H 1 8.743 0.02 . 1 . . . . 37 GLY H . 18848 1 259 . 1 1 37 37 GLY HA2 H 1 4.441 0.02 . 2 . . . . 37 GLY HA2 . 18848 1 260 . 1 1 37 37 GLY HA3 H 1 3.354 0.02 . 2 . . . . 37 GLY HA3 . 18848 1 261 . 1 1 37 37 GLY C C 13 173.481 0.2 . 1 . . . . 37 GLY C . 18848 1 262 . 1 1 37 37 GLY CA C 13 44.693 0.2 . 1 . . . . 37 GLY CA . 18848 1 263 . 1 1 37 37 GLY N N 15 111.124 0.2 . 1 . . . . 37 GLY N . 18848 1 264 . 1 1 38 38 TYR H H 1 8.424 0.02 . 1 . . . . 38 TYR H . 18848 1 265 . 1 1 38 38 TYR HA H 1 5.294 0.02 . 1 . . . . 38 TYR HA . 18848 1 266 . 1 1 38 38 TYR HB2 H 1 2.682 0.02 . 2 . . . . 38 TYR HB2 . 18848 1 267 . 1 1 38 38 TYR HB3 H 1 3.206 0.02 . 2 . . . . 38 TYR HB3 . 18848 1 268 . 1 1 38 38 TYR C C 13 174.671 0.2 . 1 . . . . 38 TYR C . 18848 1 269 . 1 1 38 38 TYR CA C 13 56.978 0.2 . 1 . . . . 38 TYR CA . 18848 1 270 . 1 1 38 38 TYR CB C 13 41.966 0.2 . 1 . . . . 38 TYR CB . 18848 1 271 . 1 1 38 38 TYR N N 15 118.037 0.2 . 1 . . . . 38 TYR N . 18848 1 272 . 1 1 39 39 HIS H H 1 9.781 0.02 . 1 . . . . 39 HIS H . 18848 1 273 . 1 1 39 39 HIS HA H 1 5.055 0.02 . 1 . . . . 39 HIS HA . 18848 1 274 . 1 1 39 39 HIS HB2 H 1 3.262 0.02 . 2 . . . . 39 HIS HB2 . 18848 1 275 . 1 1 39 39 HIS HB3 H 1 3.118 0.02 . 2 . . . . 39 HIS HB3 . 18848 1 276 . 1 1 39 39 HIS C C 13 173.550 0.2 . 1 . . . . 39 HIS C . 18848 1 277 . 1 1 39 39 HIS CA C 13 53.597 0.2 . 1 . . . . 39 HIS CA . 18848 1 278 . 1 1 39 39 HIS CB C 13 32.184 0.2 . 1 . . . . 39 HIS CB . 18848 1 279 . 1 1 39 39 HIS N N 15 116.632 0.2 . 1 . . . . 39 HIS N . 18848 1 280 . 1 1 40 40 LEU H H 1 8.759 0.02 . 1 . . . . 40 LEU H . 18848 1 281 . 1 1 40 40 LEU C C 13 176.189 0.2 . 1 . . . . 40 LEU C . 18848 1 282 . 1 1 40 40 LEU CA C 13 56.253 0.2 . 1 . . . . 40 LEU CA . 18848 1 283 . 1 1 40 40 LEU N N 15 126.633 0.2 . 1 . . . . 40 LEU N . 18848 1 284 . 1 1 41 41 ASP HA H 1 4.851 0.02 . 1 . . . . 41 ASP HA . 18848 1 285 . 1 1 41 41 ASP HB2 H 1 2.563 0.02 . 2 . . . . 41 ASP HB2 . 18848 1 286 . 1 1 41 41 ASP HB3 H 1 2.980 0.02 . 2 . . . . 41 ASP HB3 . 18848 1 287 . 1 1 41 41 ASP CA C 13 53.060 0.2 . 1 . . . . 41 ASP CA . 18848 1 288 . 1 1 42 42 THR H H 1 8.558 0.02 . 1 . . . . 42 THR H . 18848 1 289 . 1 1 42 42 THR HA H 1 4.054 0.02 . 1 . . . . 42 THR HA . 18848 1 290 . 1 1 42 42 THR CA C 13 64.699 0.2 . 1 . . . . 42 THR CA . 18848 1 291 . 1 1 42 42 THR N N 15 118.036 0.2 . 1 . . . . 42 THR N . 18848 1 292 . 1 1 47 47 CYS HA H 1 5.166 0.02 . 1 . . . . 47 CYS HA . 18848 1 293 . 1 1 47 47 CYS HB2 H 1 2.428 0.02 . 2 . . . . 47 CYS HB2 . 18848 1 294 . 1 1 47 47 CYS HB3 H 1 3.454 0.02 . 2 . . . . 47 CYS HB3 . 18848 1 295 . 1 1 47 47 CYS C C 13 174.108 0.2 . 1 . . . . 47 CYS C . 18848 1 296 . 1 1 47 47 CYS CA C 13 55.524 0.2 . 1 . . . . 47 CYS CA . 18848 1 297 . 1 1 47 47 CYS CB C 13 42.428 0.2 . 1 . . . . 47 CYS CB . 18848 1 298 . 1 1 48 48 VAL H H 1 9.379 0.02 . 1 . . . . 48 VAL H . 18848 1 299 . 1 1 48 48 VAL HA H 1 4.867 0.02 . 1 . . . . 48 VAL HA . 18848 1 300 . 1 1 48 48 VAL HB H 1 2.322 0.02 . 1 . . . . 48 VAL HB . 18848 1 301 . 1 1 48 48 VAL C C 13 175.841 0.2 . 1 . . . . 48 VAL C . 18848 1 302 . 1 1 48 48 VAL CA C 13 59.626 0.2 . 1 . . . . 48 VAL CA . 18848 1 303 . 1 1 48 48 VAL CB C 13 35.203 0.2 . 1 . . . . 48 VAL CB . 18848 1 304 . 1 1 48 48 VAL N N 15 120.979 0.2 . 1 . . . . 48 VAL N . 18848 1 305 . 1 1 49 49 ASP H H 1 9.098 0.02 . 1 . . . . 49 ASP H . 18848 1 306 . 1 1 49 49 ASP HA H 1 4.223 0.02 . 1 . . . . 49 ASP HA . 18848 1 307 . 1 1 49 49 ASP HB2 H 1 2.366 0.02 . 2 . . . . 49 ASP HB2 . 18848 1 308 . 1 1 49 49 ASP HB3 H 1 2.884 0.02 . 2 . . . . 49 ASP HB3 . 18848 1 309 . 1 1 49 49 ASP C C 13 176.045 0.2 . 1 . . . . 49 ASP C . 18848 1 310 . 1 1 49 49 ASP CA C 13 56.354 0.2 . 1 . . . . 49 ASP CA . 18848 1 311 . 1 1 49 49 ASP CB C 13 43.155 0.2 . 1 . . . . 49 ASP CB . 18848 1 312 . 1 1 49 49 ASP N N 15 124.297 0.2 . 1 . . . . 49 ASP N . 18848 1 313 . 1 1 50 50 VAL H H 1 7.803 0.02 . 1 . . . . 50 VAL H . 18848 1 314 . 1 1 50 50 VAL HA H 1 3.654 0.02 . 1 . . . . 50 VAL HA . 18848 1 315 . 1 1 50 50 VAL HB H 1 1.596 0.02 . 1 . . . . 50 VAL HB . 18848 1 316 . 1 1 50 50 VAL C C 13 174.073 0.2 . 1 . . . . 50 VAL C . 18848 1 317 . 1 1 50 50 VAL CA C 13 62.010 0.2 . 1 . . . . 50 VAL CA . 18848 1 318 . 1 1 50 50 VAL CB C 13 33.418 0.2 . 1 . . . . 50 VAL CB . 18848 1 319 . 1 1 50 50 VAL N N 15 127.111 0.2 . 1 . . . . 50 VAL N . 18848 1 320 . 1 1 51 51 ASN H H 1 9.129 0.02 . 1 . . . . 51 ASN H . 18848 1 321 . 1 1 51 51 ASN HA H 1 4.973 0.02 . 1 . . . . 51 ASN HA . 18848 1 322 . 1 1 51 51 ASN HB2 H 1 3.162 0.02 . 2 . . . . 51 ASN HB2 . 18848 1 323 . 1 1 51 51 ASN HB3 H 1 2.650 0.02 . 2 . . . . 51 ASN HB3 . 18848 1 324 . 1 1 51 51 ASN C C 13 175.826 0.2 . 1 . . . . 51 ASN C . 18848 1 325 . 1 1 51 51 ASN CA C 13 50.389 0.2 . 1 . . . . 51 ASN CA . 18848 1 326 . 1 1 51 51 ASN CB C 13 36.560 0.2 . 1 . . . . 51 ASN CB . 18848 1 327 . 1 1 51 51 ASN N N 15 126.912 0.2 . 1 . . . . 51 ASN N . 18848 1 328 . 1 1 52 52 GLU H H 1 9.782 0.02 . 1 . . . . 52 GLU H . 18848 1 329 . 1 1 52 52 GLU HA H 1 3.522 0.02 . 1 . . . . 52 GLU HA . 18848 1 330 . 1 1 52 52 GLU HB2 H 1 1.224 0.02 . 2 . . . . 52 GLU HB2 . 18848 1 331 . 1 1 52 52 GLU HB3 H 1 1.474 0.02 . 2 . . . . 52 GLU HB3 . 18848 1 332 . 1 1 52 52 GLU C C 13 176.594 0.2 . 1 . . . . 52 GLU C . 18848 1 333 . 1 1 52 52 GLU CA C 13 61.713 0.2 . 1 . . . . 52 GLU CA . 18848 1 334 . 1 1 52 52 GLU CB C 13 28.246 0.2 . 1 . . . . 52 GLU CB . 18848 1 335 . 1 1 52 52 GLU N N 15 127.466 0.2 . 1 . . . . 52 GLU N . 18848 1 336 . 1 1 53 53 CYS H H 1 7.512 0.02 . 1 . . . . 53 CYS H . 18848 1 337 . 1 1 53 53 CYS HA H 1 4.361 0.02 . 1 . . . . 53 CYS HA . 18848 1 338 . 1 1 53 53 CYS HB2 H 1 3.310 0.02 . 2 . . . . 53 CYS HB2 . 18848 1 339 . 1 1 53 53 CYS HB3 H 1 2.960 0.02 . 2 . . . . 53 CYS HB3 . 18848 1 340 . 1 1 53 53 CYS C C 13 175.705 0.2 . 1 . . . . 53 CYS C . 18848 1 341 . 1 1 53 53 CYS CA C 13 53.137 0.2 . 1 . . . . 53 CYS CA . 18848 1 342 . 1 1 53 53 CYS CB C 13 35.757 0.2 . 1 . . . . 53 CYS CB . 18848 1 343 . 1 1 53 53 CYS N N 15 111.907 0.2 . 1 . . . . 53 CYS N . 18848 1 344 . 1 1 54 54 ASP H H 1 7.051 0.02 . 1 . . . . 54 ASP H . 18848 1 345 . 1 1 54 54 ASP HA H 1 4.622 0.02 . 1 . . . . 54 ASP HA . 18848 1 346 . 1 1 54 54 ASP HB2 H 1 2.745 0.02 . 2 . . . . 54 ASP HB2 . 18848 1 347 . 1 1 54 54 ASP HB3 H 1 2.478 0.02 . 2 . . . . 54 ASP HB3 . 18848 1 348 . 1 1 54 54 ASP C C 13 176.595 0.2 . 1 . . . . 54 ASP C . 18848 1 349 . 1 1 54 54 ASP CA C 13 54.662 0.2 . 1 . . . . 54 ASP CA . 18848 1 350 . 1 1 54 54 ASP CB C 13 41.524 0.2 . 1 . . . . 54 ASP CB . 18848 1 351 . 1 1 54 54 ASP N N 15 119.783 0.2 . 1 . . . . 54 ASP N . 18848 1 352 . 1 1 55 55 GLU H H 1 8.008 0.02 . 1 . . . . 55 GLU H . 18848 1 353 . 1 1 55 55 GLU HA H 1 4.244 0.02 . 1 . . . . 55 GLU HA . 18848 1 354 . 1 1 55 55 GLU HB2 H 1 1.884 0.02 . 2 . . . . 55 GLU HB2 . 18848 1 355 . 1 1 55 55 GLU HB3 H 1 2.036 0.02 . 2 . . . . 55 GLU HB3 . 18848 1 356 . 1 1 55 55 GLU C C 13 177.334 0.2 . 1 . . . . 55 GLU C . 18848 1 357 . 1 1 55 55 GLU CA C 13 57.702 0.2 . 1 . . . . 55 GLU CA . 18848 1 358 . 1 1 55 55 GLU CB C 13 30.455 0.2 . 1 . . . . 55 GLU CB . 18848 1 359 . 1 1 55 55 GLU N N 15 121.154 0.2 . 1 . . . . 55 GLU N . 18848 1 360 . 1 1 56 56 LEU H H 1 8.179 0.02 . 1 . . . . 56 LEU H . 18848 1 361 . 1 1 56 56 LEU HA H 1 4.235 0.02 . 1 . . . . 56 LEU HA . 18848 1 362 . 1 1 56 56 LEU HB2 H 1 1.567 0.02 . 2 . . . . 56 LEU HB2 . 18848 1 363 . 1 1 56 56 LEU HB3 H 1 1.703 0.02 . 2 . . . . 56 LEU HB3 . 18848 1 364 . 1 1 56 56 LEU C C 13 178.158 0.2 . 1 . . . . 56 LEU C . 18848 1 365 . 1 1 56 56 LEU CA C 13 56.433 0.2 . 1 . . . . 56 LEU CA . 18848 1 366 . 1 1 56 56 LEU CB C 13 42.045 0.2 . 1 . . . . 56 LEU CB . 18848 1 367 . 1 1 56 56 LEU N N 15 121.569 0.2 . 1 . . . . 56 LEU N . 18848 1 368 . 1 1 57 57 ASN H H 1 8.292 0.02 . 1 . . . . 57 ASN H . 18848 1 369 . 1 1 57 57 ASN HA H 1 4.593 0.02 . 1 . . . . 57 ASN HA . 18848 1 370 . 1 1 57 57 ASN HB2 H 1 2.734 0.02 . 2 . . . . 57 ASN HB2 . 18848 1 371 . 1 1 57 57 ASN HB3 H 1 2.838 0.02 . 2 . . . . 57 ASN HB3 . 18848 1 372 . 1 1 57 57 ASN C C 13 175.755 0.2 . 1 . . . . 57 ASN C . 18848 1 373 . 1 1 57 57 ASN CA C 13 54.578 0.2 . 1 . . . . 57 ASN CA . 18848 1 374 . 1 1 57 57 ASN CB C 13 38.896 0.2 . 1 . . . . 57 ASN CB . 18848 1 375 . 1 1 57 57 ASN N N 15 117.864 0.2 . 1 . . . . 57 ASN N . 18848 1 376 . 1 1 58 58 ASN H H 1 8.210 0.02 . 1 . . . . 58 ASN H . 18848 1 377 . 1 1 58 58 ASN HA H 1 4.637 0.02 . 1 . . . . 58 ASN HA . 18848 1 378 . 1 1 58 58 ASN HB2 H 1 2.824 0.02 . 1 . . . . 58 ASN HB2 . 18848 1 379 . 1 1 58 58 ASN HB3 H 1 2.824 0.02 . 1 . . . . 58 ASN HB3 . 18848 1 380 . 1 1 58 58 ASN C C 13 175.899 0.2 . 1 . . . . 58 ASN C . 18848 1 381 . 1 1 58 58 ASN CA C 13 54.023 0.2 . 1 . . . . 58 ASN CA . 18848 1 382 . 1 1 58 58 ASN CB C 13 38.382 0.2 . 1 . . . . 58 ASN CB . 18848 1 383 . 1 1 58 58 ASN N N 15 117.714 0.2 . 1 . . . . 58 ASN N . 18848 1 384 . 1 1 59 59 ARG H H 1 8.051 0.02 . 1 . . . . 59 ARG H . 18848 1 385 . 1 1 59 59 ARG HA H 1 4.173 0.02 . 1 . . . . 59 ARG HA . 18848 1 386 . 1 1 59 59 ARG HB2 H 1 1.890 0.02 . 1 . . . . 59 ARG HB2 . 18848 1 387 . 1 1 59 59 ARG HB3 H 1 1.890 0.02 . 1 . . . . 59 ARG HB3 . 18848 1 388 . 1 1 59 59 ARG C C 13 176.650 0.2 . 1 . . . . 59 ARG C . 18848 1 389 . 1 1 59 59 ARG CA C 13 57.738 0.2 . 1 . . . . 59 ARG CA . 18848 1 390 . 1 1 59 59 ARG CB C 13 30.076 0.2 . 1 . . . . 59 ARG CB . 18848 1 391 . 1 1 59 59 ARG N N 15 119.570 0.2 . 1 . . . . 59 ARG N . 18848 1 392 . 1 1 60 60 MET H H 1 8.160 0.02 . 1 . . . . 60 MET H . 18848 1 393 . 1 1 60 60 MET HA H 1 4.509 0.02 . 1 . . . . 60 MET HA . 18848 1 394 . 1 1 60 60 MET HB2 H 1 1.995 0.02 . 2 . . . . 60 MET HB2 . 18848 1 395 . 1 1 60 60 MET HB3 H 1 2.122 0.02 . 2 . . . . 60 MET HB3 . 18848 1 396 . 1 1 60 60 MET C C 13 175.864 0.2 . 1 . . . . 60 MET C . 18848 1 397 . 1 1 60 60 MET CA C 13 55.627 0.2 . 1 . . . . 60 MET CA . 18848 1 398 . 1 1 60 60 MET CB C 13 32.622 0.2 . 1 . . . . 60 MET CB . 18848 1 399 . 1 1 60 60 MET N N 15 117.937 0.2 . 1 . . . . 60 MET N . 18848 1 400 . 1 1 61 61 SER H H 1 8.112 0.02 . 1 . . . . 61 SER H . 18848 1 401 . 1 1 61 61 SER HA H 1 4.406 0.02 . 1 . . . . 61 SER HA . 18848 1 402 . 1 1 61 61 SER HB2 H 1 3.854 0.02 . 1 . . . . 61 SER HB2 . 18848 1 403 . 1 1 61 61 SER HB3 H 1 3.854 0.02 . 1 . . . . 61 SER HB3 . 18848 1 404 . 1 1 61 61 SER C C 13 174.727 0.2 . 1 . . . . 61 SER C . 18848 1 405 . 1 1 61 61 SER CA C 13 58.321 0.2 . 1 . . . . 61 SER CA . 18848 1 406 . 1 1 61 61 SER CB C 13 63.689 0.2 . 1 . . . . 61 SER CB . 18848 1 407 . 1 1 61 61 SER N N 15 115.765 0.2 . 1 . . . . 61 SER N . 18848 1 408 . 1 1 62 62 LEU H H 1 8.085 0.02 . 1 . . . . 62 LEU H . 18848 1 409 . 1 1 62 62 LEU HA H 1 4.129 0.02 . 1 . . . . 62 LEU HA . 18848 1 410 . 1 1 62 62 LEU HB2 H 1 1.458 0.02 . 1 . . . . 62 LEU HB2 . 18848 1 411 . 1 1 62 62 LEU HB3 H 1 1.458 0.02 . 1 . . . . 62 LEU HB3 . 18848 1 412 . 1 1 62 62 LEU C C 13 177.321 0.2 . 1 . . . . 62 LEU C . 18848 1 413 . 1 1 62 62 LEU CA C 13 57.125 0.2 . 1 . . . . 62 LEU CA . 18848 1 414 . 1 1 62 62 LEU CB C 13 42.677 0.2 . 1 . . . . 62 LEU CB . 18848 1 415 . 1 1 62 62 LEU N N 15 124.576 0.2 . 1 . . . . 62 LEU N . 18848 1 416 . 1 1 63 63 CYS H H 1 8.004 0.02 . 1 . . . . 63 CYS H . 18848 1 417 . 1 1 63 63 CYS HA H 1 5.120 0.02 . 1 . . . . 63 CYS HA . 18848 1 418 . 1 1 63 63 CYS HB2 H 1 2.522 0.02 . 2 . . . . 63 CYS HB2 . 18848 1 419 . 1 1 63 63 CYS HB3 H 1 2.664 0.02 . 2 . . . . 63 CYS HB3 . 18848 1 420 . 1 1 63 63 CYS C C 13 174.012 0.2 . 1 . . . . 63 CYS C . 18848 1 421 . 1 1 63 63 CYS CA C 13 52.001 0.2 . 1 . . . . 63 CYS CA . 18848 1 422 . 1 1 63 63 CYS CB C 13 39.970 0.2 . 1 . . . . 63 CYS CB . 18848 1 423 . 1 1 63 63 CYS N N 15 114.769 0.2 . 1 . . . . 63 CYS N . 18848 1 424 . 1 1 64 64 LYS H H 1 8.407 0.02 . 1 . . . . 64 LYS H . 18848 1 425 . 1 1 64 64 LYS HA H 1 4.482 0.02 . 1 . . . . 64 LYS HA . 18848 1 426 . 1 1 64 64 LYS HB2 H 1 1.651 0.02 . 1 . . . . 64 LYS HB2 . 18848 1 427 . 1 1 64 64 LYS HB3 H 1 1.651 0.02 . 1 . . . . 64 LYS HB3 . 18848 1 428 . 1 1 64 64 LYS C C 13 175.327 0.2 . 1 . . . . 64 LYS C . 18848 1 429 . 1 1 64 64 LYS CA C 13 55.758 0.2 . 1 . . . . 64 LYS CA . 18848 1 430 . 1 1 64 64 LYS CB C 13 34.328 0.2 . 1 . . . . 64 LYS CB . 18848 1 431 . 1 1 64 64 LYS N N 15 123.136 0.2 . 1 . . . . 64 LYS N . 18848 1 432 . 1 1 65 65 ASN H H 1 9.033 0.02 . 1 . . . . 65 ASN H . 18848 1 433 . 1 1 65 65 ASN HA H 1 3.736 0.02 . 1 . . . . 65 ASN HA . 18848 1 434 . 1 1 65 65 ASN HB2 H 1 2.763 0.02 . 2 . . . . 65 ASN HB2 . 18848 1 435 . 1 1 65 65 ASN HB3 H 1 1.290 0.02 . 2 . . . . 65 ASN HB3 . 18848 1 436 . 1 1 65 65 ASN C C 13 172.948 0.2 . 1 . . . . 65 ASN C . 18848 1 437 . 1 1 65 65 ASN CA C 13 53.967 0.2 . 1 . . . . 65 ASN CA . 18848 1 438 . 1 1 65 65 ASN CB C 13 36.467 0.2 . 1 . . . . 65 ASN CB . 18848 1 439 . 1 1 65 65 ASN N N 15 122.861 0.2 . 1 . . . . 65 ASN N . 18848 1 440 . 1 1 66 66 ALA H H 1 7.136 0.02 . 1 . . . . 66 ALA H . 18848 1 441 . 1 1 66 66 ALA HA H 1 4.696 0.02 . 1 . . . . 66 ALA HA . 18848 1 442 . 1 1 66 66 ALA HB1 H 1 1.038 0.02 . 1 . . . . 66 ALA HB1 . 18848 1 443 . 1 1 66 66 ALA HB2 H 1 1.038 0.02 . 1 . . . . 66 ALA HB2 . 18848 1 444 . 1 1 66 66 ALA HB3 H 1 1.038 0.02 . 1 . . . . 66 ALA HB3 . 18848 1 445 . 1 1 66 66 ALA C C 13 174.419 0.2 . 1 . . . . 66 ALA C . 18848 1 446 . 1 1 66 66 ALA CA C 13 50.814 0.2 . 1 . . . . 66 ALA CA . 18848 1 447 . 1 1 66 66 ALA CB C 13 24.146 0.2 . 1 . . . . 66 ALA CB . 18848 1 448 . 1 1 66 66 ALA N N 15 115.739 0.2 . 1 . . . . 66 ALA N . 18848 1 449 . 1 1 67 67 LYS H H 1 8.865 0.02 . 1 . . . . 67 LYS H . 18848 1 450 . 1 1 67 67 LYS HA H 1 4.485 0.02 . 1 . . . . 67 LYS HA . 18848 1 451 . 1 1 67 67 LYS HB2 H 1 1.769 0.02 . 2 . . . . 67 LYS HB2 . 18848 1 452 . 1 1 67 67 LYS HB3 H 1 1.714 0.02 . 2 . . . . 67 LYS HB3 . 18848 1 453 . 1 1 67 67 LYS C C 13 174.469 0.2 . 1 . . . . 67 LYS C . 18848 1 454 . 1 1 67 67 LYS CA C 13 54.427 0.2 . 1 . . . . 67 LYS CA . 18848 1 455 . 1 1 67 67 LYS CB C 13 35.104 0.2 . 1 . . . . 67 LYS CB . 18848 1 456 . 1 1 67 67 LYS N N 15 121.078 0.2 . 1 . . . . 67 LYS N . 18848 1 457 . 1 1 68 68 CYS H H 1 8.741 0.02 . 1 . . . . 68 CYS H . 18848 1 458 . 1 1 68 68 CYS HA H 1 5.164 0.02 . 1 . . . . 68 CYS HA . 18848 1 459 . 1 1 68 68 CYS HB2 H 1 2.640 0.02 . 2 . . . . 68 CYS HB2 . 18848 1 460 . 1 1 68 68 CYS HB3 H 1 3.192 0.02 . 2 . . . . 68 CYS HB3 . 18848 1 461 . 1 1 68 68 CYS C C 13 174.177 0.2 . 1 . . . . 68 CYS C . 18848 1 462 . 1 1 68 68 CYS CA C 13 57.917 0.2 . 1 . . . . 68 CYS CA . 18848 1 463 . 1 1 68 68 CYS CB C 13 36.029 0.2 . 1 . . . . 68 CYS CB . 18848 1 464 . 1 1 68 68 CYS N N 15 126.579 0.2 . 1 . . . . 68 CYS N . 18848 1 465 . 1 1 69 69 ILE H H 1 9.680 0.02 . 1 . . . . 69 ILE H . 18848 1 466 . 1 1 69 69 ILE HA H 1 4.409 0.02 . 1 . . . . 69 ILE HA . 18848 1 467 . 1 1 69 69 ILE HB H 1 1.879 0.02 . 1 . . . . 69 ILE HB . 18848 1 468 . 1 1 69 69 ILE C C 13 174.680 0.2 . 1 . . . . 69 ILE C . 18848 1 469 . 1 1 69 69 ILE CA C 13 59.612 0.2 . 1 . . . . 69 ILE CA . 18848 1 470 . 1 1 69 69 ILE CB C 13 39.485 0.2 . 1 . . . . 69 ILE CB . 18848 1 471 . 1 1 69 69 ILE N N 15 132.154 0.2 . 1 . . . . 69 ILE N . 18848 1 472 . 1 1 70 70 ASN H H 1 9.044 0.02 . 1 . . . . 70 ASN H . 18848 1 473 . 1 1 70 70 ASN HA H 1 4.919 0.02 . 1 . . . . 70 ASN HA . 18848 1 474 . 1 1 70 70 ASN HB2 H 1 2.867 0.02 . 2 . . . . 70 ASN HB2 . 18848 1 475 . 1 1 70 70 ASN HB3 H 1 2.666 0.02 . 2 . . . . 70 ASN HB3 . 18848 1 476 . 1 1 70 70 ASN C C 13 175.081 0.2 . 1 . . . . 70 ASN C . 18848 1 477 . 1 1 70 70 ASN CA C 13 54.365 0.2 . 1 . . . . 70 ASN CA . 18848 1 478 . 1 1 70 70 ASN CB C 13 39.521 0.2 . 1 . . . . 70 ASN CB . 18848 1 479 . 1 1 70 70 ASN N N 15 127.594 0.2 . 1 . . . . 70 ASN N . 18848 1 480 . 1 1 71 71 THR H H 1 7.897 0.02 . 1 . . . . 71 THR H . 18848 1 481 . 1 1 71 71 THR HA H 1 4.727 0.02 . 1 . . . . 71 THR HA . 18848 1 482 . 1 1 71 71 THR HB H 1 4.249 0.02 . 1 . . . . 71 THR HB . 18848 1 483 . 1 1 71 71 THR C C 13 173.751 0.2 . 1 . . . . 71 THR C . 18848 1 484 . 1 1 71 71 THR CA C 13 59.665 0.2 . 1 . . . . 71 THR CA . 18848 1 485 . 1 1 71 71 THR CB C 13 70.854 0.2 . 1 . . . . 71 THR CB . 18848 1 486 . 1 1 71 71 THR N N 15 117.429 0.2 . 1 . . . . 71 THR N . 18848 1 487 . 1 1 72 72 ASP H H 1 8.734 0.02 . 1 . . . . 72 ASP H . 18848 1 488 . 1 1 72 72 ASP HA H 1 4.303 0.02 . 1 . . . . 72 ASP HA . 18848 1 489 . 1 1 72 72 ASP HB2 H 1 2.868 0.02 . 2 . . . . 72 ASP HB2 . 18848 1 490 . 1 1 72 72 ASP HB3 H 1 2.630 0.02 . 2 . . . . 72 ASP HB3 . 18848 1 491 . 1 1 72 72 ASP C C 13 175.594 0.2 . 1 . . . . 72 ASP C . 18848 1 492 . 1 1 72 72 ASP CA C 13 55.723 0.2 . 1 . . . . 72 ASP CA . 18848 1 493 . 1 1 72 72 ASP CB C 13 40.297 0.2 . 1 . . . . 72 ASP CB . 18848 1 494 . 1 1 72 72 ASP N N 15 123.765 0.2 . 1 . . . . 72 ASP N . 18848 1 495 . 1 1 73 73 GLY H H 1 9.230 0.02 . 1 . . . . 73 GLY H . 18848 1 496 . 1 1 73 73 GLY HA2 H 1 4.272 0.02 . 2 . . . . 73 GLY HA2 . 18848 1 497 . 1 1 73 73 GLY HA3 H 1 2.958 0.02 . 2 . . . . 73 GLY HA3 . 18848 1 498 . 1 1 73 73 GLY C C 13 174.225 0.2 . 1 . . . . 73 GLY C . 18848 1 499 . 1 1 73 73 GLY CA C 13 46.372 0.2 . 1 . . . . 73 GLY CA . 18848 1 500 . 1 1 73 73 GLY N N 15 119.827 0.2 . 1 . . . . 73 GLY N . 18848 1 501 . 1 1 74 74 SER H H 1 6.645 0.02 . 1 . . . . 74 SER H . 18848 1 502 . 1 1 74 74 SER HA H 1 4.386 0.02 . 1 . . . . 74 SER HA . 18848 1 503 . 1 1 74 74 SER HB2 H 1 3.873 0.02 . 2 . . . . 74 SER HB2 . 18848 1 504 . 1 1 74 74 SER HB3 H 1 3.398 0.02 . 2 . . . . 74 SER HB3 . 18848 1 505 . 1 1 74 74 SER C C 13 173.549 0.2 . 1 . . . . 74 SER C . 18848 1 506 . 1 1 74 74 SER CA C 13 56.184 0.2 . 1 . . . . 74 SER CA . 18848 1 507 . 1 1 74 74 SER CB C 13 63.041 0.2 . 1 . . . . 74 SER CB . 18848 1 508 . 1 1 74 74 SER N N 15 113.308 0.2 . 1 . . . . 74 SER N . 18848 1 509 . 1 1 75 75 TYR H H 1 9.045 0.02 . 1 . . . . 75 TYR H . 18848 1 510 . 1 1 75 75 TYR HA H 1 5.053 0.02 . 1 . . . . 75 TYR HA . 18848 1 511 . 1 1 75 75 TYR HB2 H 1 2.965 0.02 . 2 . . . . 75 TYR HB2 . 18848 1 512 . 1 1 75 75 TYR HB3 H 1 3.548 0.02 . 2 . . . . 75 TYR HB3 . 18848 1 513 . 1 1 75 75 TYR C C 13 172.703 0.2 . 1 . . . . 75 TYR C . 18848 1 514 . 1 1 75 75 TYR CA C 13 57.478 0.2 . 1 . . . . 75 TYR CA . 18848 1 515 . 1 1 75 75 TYR CB C 13 39.123 0.2 . 1 . . . . 75 TYR CB . 18848 1 516 . 1 1 75 75 TYR N N 15 118.680 0.2 . 1 . . . . 75 TYR N . 18848 1 517 . 1 1 76 76 LYS H H 1 9.662 0.02 . 1 . . . . 76 LYS H . 18848 1 518 . 1 1 76 76 LYS HA H 1 4.508 0.02 . 1 . . . . 76 LYS HA . 18848 1 519 . 1 1 76 76 LYS HB2 H 1 1.672 0.02 . 1 . . . . 76 LYS HB2 . 18848 1 520 . 1 1 76 76 LYS HB3 H 1 1.672 0.02 . 1 . . . . 76 LYS HB3 . 18848 1 521 . 1 1 76 76 LYS C C 13 174.126 0.2 . 1 . . . . 76 LYS C . 18848 1 522 . 1 1 76 76 LYS CA C 13 54.611 0.2 . 1 . . . . 76 LYS CA . 18848 1 523 . 1 1 76 76 LYS CB C 13 36.504 0.2 . 1 . . . . 76 LYS CB . 18848 1 524 . 1 1 76 76 LYS N N 15 120.160 0.2 . 1 . . . . 76 LYS N . 18848 1 525 . 1 1 77 77 CYS H H 1 8.517 0.02 . 1 . . . . 77 CYS H . 18848 1 526 . 1 1 77 77 CYS HA H 1 5.509 0.02 . 1 . . . . 77 CYS HA . 18848 1 527 . 1 1 77 77 CYS HB2 H 1 2.521 0.02 . 2 . . . . 77 CYS HB2 . 18848 1 528 . 1 1 77 77 CYS HB3 H 1 2.822 0.02 . 2 . . . . 77 CYS HB3 . 18848 1 529 . 1 1 77 77 CYS C C 13 173.898 0.2 . 1 . . . . 77 CYS C . 18848 1 530 . 1 1 77 77 CYS CA C 13 52.165 0.2 . 1 . . . . 77 CYS CA . 18848 1 531 . 1 1 77 77 CYS CB C 13 39.187 0.2 . 1 . . . . 77 CYS CB . 18848 1 532 . 1 1 77 77 CYS N N 15 119.056 0.2 . 1 . . . . 77 CYS N . 18848 1 533 . 1 1 78 78 LEU H H 1 9.085 0.02 . 1 . . . . 78 LEU H . 18848 1 534 . 1 1 78 78 LEU HA H 1 4.713 0.02 . 1 . . . . 78 LEU HA . 18848 1 535 . 1 1 78 78 LEU HB2 H 1 1.720 0.02 . 2 . . . . 78 LEU HB2 . 18848 1 536 . 1 1 78 78 LEU HB3 H 1 1.466 0.02 . 2 . . . . 78 LEU HB3 . 18848 1 537 . 1 1 78 78 LEU C C 13 176.152 0.2 . 1 . . . . 78 LEU C . 18848 1 538 . 1 1 78 78 LEU CA C 13 53.199 0.2 . 1 . . . . 78 LEU CA . 18848 1 539 . 1 1 78 78 LEU CB C 13 43.596 0.2 . 1 . . . . 78 LEU CB . 18848 1 540 . 1 1 78 78 LEU N N 15 126.998 0.2 . 1 . . . . 78 LEU N . 18848 1 541 . 1 1 79 79 CYS H H 1 8.711 0.02 . 1 . . . . 79 CYS H . 18848 1 542 . 1 1 79 79 CYS HA H 1 4.567 0.02 . 1 . . . . 79 CYS HA . 18848 1 543 . 1 1 79 79 CYS HB2 H 1 2.738 0.02 . 2 . . . . 79 CYS HB2 . 18848 1 544 . 1 1 79 79 CYS HB3 H 1 3.110 0.02 . 2 . . . . 79 CYS HB3 . 18848 1 545 . 1 1 79 79 CYS C C 13 175.217 0.2 . 1 . . . . 79 CYS C . 18848 1 546 . 1 1 79 79 CYS CA C 13 53.803 0.2 . 1 . . . . 79 CYS CA . 18848 1 547 . 1 1 79 79 CYS CB C 13 37.877 0.2 . 1 . . . . 79 CYS CB . 18848 1 548 . 1 1 79 79 CYS N N 15 124.073 0.2 . 1 . . . . 79 CYS N . 18848 1 549 . 1 1 80 80 LEU H H 1 7.659 0.02 . 1 . . . . 80 LEU H . 18848 1 550 . 1 1 80 80 LEU C C 13 173.692 0.2 . 1 . . . . 80 LEU C . 18848 1 551 . 1 1 80 80 LEU CA C 13 53.729 0.2 . 1 . . . . 80 LEU CA . 18848 1 552 . 1 1 80 80 LEU CB C 13 40.706 0.2 . 1 . . . . 80 LEU CB . 18848 1 553 . 1 1 80 80 LEU N N 15 124.168 0.2 . 1 . . . . 80 LEU N . 18848 1 554 . 1 1 81 81 PRO HA H 1 4.457 0.02 . 1 . . . . 81 PRO HA . 18848 1 555 . 1 1 81 81 PRO HB2 H 1 1.894 0.02 . 2 . . . . 81 PRO HB2 . 18848 1 556 . 1 1 81 81 PRO HB3 H 1 2.365 0.02 . 2 . . . . 81 PRO HB3 . 18848 1 557 . 1 1 81 81 PRO C C 13 178.080 0.2 . 1 . . . . 81 PRO C . 18848 1 558 . 1 1 81 81 PRO CA C 13 64.367 0.2 . 1 . . . . 81 PRO CA . 18848 1 559 . 1 1 81 81 PRO CB C 13 31.604 0.2 . 1 . . . . 81 PRO CB . 18848 1 560 . 1 1 82 82 GLY H H 1 8.837 0.02 . 1 . . . . 82 GLY H . 18848 1 561 . 1 1 82 82 GLY HA2 H 1 3.520 0.02 . 2 . . . . 82 GLY HA2 . 18848 1 562 . 1 1 82 82 GLY HA3 H 1 4.183 0.02 . 2 . . . . 82 GLY HA3 . 18848 1 563 . 1 1 82 82 GLY C C 13 173.496 0.2 . 1 . . . . 82 GLY C . 18848 1 564 . 1 1 82 82 GLY CA C 13 44.997 0.2 . 1 . . . . 82 GLY CA . 18848 1 565 . 1 1 82 82 GLY N N 15 112.104 0.2 . 1 . . . . 82 GLY N . 18848 1 566 . 1 1 83 83 TYR H H 1 8.444 0.02 . 1 . . . . 83 TYR H . 18848 1 567 . 1 1 83 83 TYR HA H 1 5.167 0.02 . 1 . . . . 83 TYR HA . 18848 1 568 . 1 1 83 83 TYR HB2 H 1 3.146 0.02 . 2 . . . . 83 TYR HB2 . 18848 1 569 . 1 1 83 83 TYR HB3 H 1 2.603 0.02 . 2 . . . . 83 TYR HB3 . 18848 1 570 . 1 1 83 83 TYR C C 13 174.551 0.2 . 1 . . . . 83 TYR C . 18848 1 571 . 1 1 83 83 TYR CA C 13 56.436 0.2 . 1 . . . . 83 TYR CA . 18848 1 572 . 1 1 83 83 TYR CB C 13 40.876 0.2 . 1 . . . . 83 TYR CB . 18848 1 573 . 1 1 83 83 TYR N N 15 120.930 0.2 . 1 . . . . 83 TYR N . 18848 1 574 . 1 1 84 84 VAL H H 1 9.395 0.02 . 1 . . . . 84 VAL H . 18848 1 575 . 1 1 84 84 VAL HA H 1 5.042 0.02 . 1 . . . . 84 VAL HA . 18848 1 576 . 1 1 84 84 VAL C C 13 173.772 0.2 . 1 . . . . 84 VAL C . 18848 1 577 . 1 1 84 84 VAL CA C 13 58.721 0.2 . 1 . . . . 84 VAL CA . 18848 1 578 . 1 1 84 84 VAL CB C 13 33.308 0.2 . 1 . . . . 84 VAL CB . 18848 1 579 . 1 1 84 84 VAL N N 15 114.694 0.2 . 1 . . . . 84 VAL N . 18848 1 580 . 1 1 85 85 PRO HA H 1 4.529 0.02 . 1 . . . . 85 PRO HA . 18848 1 581 . 1 1 85 85 PRO HB2 H 1 1.974 0.02 . 2 . . . . 85 PRO HB2 . 18848 1 582 . 1 1 85 85 PRO HB3 H 1 2.523 0.02 . 2 . . . . 85 PRO HB3 . 18848 1 583 . 1 1 85 85 PRO C C 13 176.793 0.2 . 1 . . . . 85 PRO C . 18848 1 584 . 1 1 85 85 PRO CA C 13 64.604 0.2 . 1 . . . . 85 PRO CA . 18848 1 585 . 1 1 85 85 PRO CB C 13 32.559 0.2 . 1 . . . . 85 PRO CB . 18848 1 586 . 1 1 86 86 SER H H 1 8.534 0.02 . 1 . . . . 86 SER H . 18848 1 587 . 1 1 86 86 SER HA H 1 5.003 0.02 . 1 . . . . 86 SER HA . 18848 1 588 . 1 1 86 86 SER HB2 H 1 3.983 0.02 . 2 . . . . 86 SER HB2 . 18848 1 589 . 1 1 86 86 SER HB3 H 1 4.395 0.02 . 2 . . . . 86 SER HB3 . 18848 1 590 . 1 1 86 86 SER C C 13 173.486 0.2 . 1 . . . . 86 SER C . 18848 1 591 . 1 1 86 86 SER CA C 13 57.362 0.2 . 1 . . . . 86 SER CA . 18848 1 592 . 1 1 86 86 SER CB C 13 66.744 0.2 . 1 . . . . 86 SER CB . 18848 1 593 . 1 1 86 86 SER N N 15 119.606 0.2 . 1 . . . . 86 SER N . 18848 1 594 . 1 1 87 87 ASP H H 1 8.721 0.02 . 1 . . . . 87 ASP H . 18848 1 595 . 1 1 87 87 ASP HA H 1 4.498 0.02 . 1 . . . . 87 ASP HA . 18848 1 596 . 1 1 87 87 ASP HB2 H 1 2.725 0.02 . 2 . . . . 87 ASP HB2 . 18848 1 597 . 1 1 87 87 ASP HB3 H 1 2.813 0.02 . 2 . . . . 87 ASP HB3 . 18848 1 598 . 1 1 87 87 ASP C C 13 175.987 0.2 . 1 . . . . 87 ASP C . 18848 1 599 . 1 1 87 87 ASP CA C 13 55.325 0.2 . 1 . . . . 87 ASP CA . 18848 1 600 . 1 1 87 87 ASP CB C 13 40.072 0.2 . 1 . . . . 87 ASP CB . 18848 1 601 . 1 1 87 87 ASP N N 15 118.346 0.2 . 1 . . . . 87 ASP N . 18848 1 602 . 1 1 88 88 LYS H H 1 8.507 0.02 . 1 . . . . 88 LYS H . 18848 1 603 . 1 1 88 88 LYS C C 13 174.960 0.2 . 1 . . . . 88 LYS C . 18848 1 604 . 1 1 88 88 LYS CA C 13 52.930 0.2 . 1 . . . . 88 LYS CA . 18848 1 605 . 1 1 88 88 LYS CB C 13 33.474 0.2 . 1 . . . . 88 LYS CB . 18848 1 606 . 1 1 88 88 LYS N N 15 122.864 0.2 . 1 . . . . 88 LYS N . 18848 1 607 . 1 1 89 89 PRO HA H 1 4.343 0.02 . 1 . . . . 89 PRO HA . 18848 1 608 . 1 1 89 89 PRO HB2 H 1 2.331 0.02 . 2 . . . . 89 PRO HB2 . 18848 1 609 . 1 1 89 89 PRO HB3 H 1 1.913 0.02 . 2 . . . . 89 PRO HB3 . 18848 1 610 . 1 1 89 89 PRO C C 13 176.531 0.2 . 1 . . . . 89 PRO C . 18848 1 611 . 1 1 89 89 PRO CA C 13 64.289 0.2 . 1 . . . . 89 PRO CA . 18848 1 612 . 1 1 89 89 PRO CB C 13 32.058 0.2 . 1 . . . . 89 PRO CB . 18848 1 613 . 1 1 90 90 ASN H H 1 8.290 0.02 . 1 . . . . 90 ASN H . 18848 1 614 . 1 1 90 90 ASN HA H 1 4.589 0.02 . 1 . . . . 90 ASN HA . 18848 1 615 . 1 1 90 90 ASN HB2 H 1 3.464 0.02 . 2 . . . . 90 ASN HB2 . 18848 1 616 . 1 1 90 90 ASN HB3 H 1 3.256 0.02 . 2 . . . . 90 ASN HB3 . 18848 1 617 . 1 1 90 90 ASN C C 13 173.403 0.2 . 1 . . . . 90 ASN C . 18848 1 618 . 1 1 90 90 ASN CA C 13 54.105 0.2 . 1 . . . . 90 ASN CA . 18848 1 619 . 1 1 90 90 ASN CB C 13 37.642 0.2 . 1 . . . . 90 ASN CB . 18848 1 620 . 1 1 90 90 ASN N N 15 114.376 0.2 . 1 . . . . 90 ASN N . 18848 1 621 . 1 1 91 91 TYR H H 1 7.749 0.02 . 1 . . . . 91 TYR H . 18848 1 622 . 1 1 91 91 TYR HA H 1 5.095 0.02 . 1 . . . . 91 TYR HA . 18848 1 623 . 1 1 91 91 TYR HB2 H 1 2.915 0.02 . 1 . . . . 91 TYR HB2 . 18848 1 624 . 1 1 91 91 TYR HB3 H 1 2.915 0.02 . 1 . . . . 91 TYR HB3 . 18848 1 625 . 1 1 91 91 TYR C C 13 175.285 0.2 . 1 . . . . 91 TYR C . 18848 1 626 . 1 1 91 91 TYR CA C 13 56.679 0.2 . 1 . . . . 91 TYR CA . 18848 1 627 . 1 1 91 91 TYR CB C 13 40.363 0.2 . 1 . . . . 91 TYR CB . 18848 1 628 . 1 1 91 91 TYR N N 15 120.107 0.2 . 1 . . . . 91 TYR N . 18848 1 629 . 1 1 92 92 CYS H H 1 7.717 0.02 . 1 . . . . 92 CYS H . 18848 1 630 . 1 1 92 92 CYS HA H 1 5.432 0.02 . 1 . . . . 92 CYS HA . 18848 1 631 . 1 1 92 92 CYS HB2 H 1 2.787 0.02 . 2 . . . . 92 CYS HB2 . 18848 1 632 . 1 1 92 92 CYS HB3 H 1 3.610 0.02 . 2 . . . . 92 CYS HB3 . 18848 1 633 . 1 1 92 92 CYS C C 13 172.120 0.2 . 1 . . . . 92 CYS C . 18848 1 634 . 1 1 92 92 CYS CA C 13 56.642 0.2 . 1 . . . . 92 CYS CA . 18848 1 635 . 1 1 92 92 CYS CB C 13 46.977 0.2 . 1 . . . . 92 CYS CB . 18848 1 636 . 1 1 92 92 CYS N N 15 125.055 0.2 . 1 . . . . 92 CYS N . 18848 1 637 . 1 1 93 93 THR H H 1 9.627 0.02 . 1 . . . . 93 THR H . 18848 1 638 . 1 1 93 93 THR HA H 1 5.023 0.02 . 1 . . . . 93 THR HA . 18848 1 639 . 1 1 93 93 THR C C 13 172.102 0.2 . 1 . . . . 93 THR C . 18848 1 640 . 1 1 93 93 THR CA C 13 58.591 0.2 . 1 . . . . 93 THR CA . 18848 1 641 . 1 1 93 93 THR CB C 13 71.675 0.2 . 1 . . . . 93 THR CB . 18848 1 642 . 1 1 93 93 THR N N 15 118.812 0.2 . 1 . . . . 93 THR N . 18848 1 643 . 1 1 94 94 PRO HA H 1 4.095 0.02 . 1 . . . . 94 PRO HA . 18848 1 644 . 1 1 94 94 PRO HB2 H 1 1.803 0.02 . 2 . . . . 94 PRO HB2 . 18848 1 645 . 1 1 94 94 PRO HB3 H 1 1.970 0.02 . 2 . . . . 94 PRO HB3 . 18848 1 646 . 1 1 94 94 PRO C C 13 177.271 0.2 . 1 . . . . 94 PRO C . 18848 1 647 . 1 1 94 94 PRO CA C 13 63.594 0.2 . 1 . . . . 94 PRO CA . 18848 1 648 . 1 1 94 94 PRO CB C 13 31.800 0.2 . 1 . . . . 94 PRO CB . 18848 1 649 . 1 1 95 95 LEU H H 1 8.064 0.02 . 1 . . . . 95 LEU H . 18848 1 650 . 1 1 95 95 LEU HA H 1 4.149 0.02 . 1 . . . . 95 LEU HA . 18848 1 651 . 1 1 95 95 LEU HB2 H 1 1.402 0.02 . 2 . . . . 95 LEU HB2 . 18848 1 652 . 1 1 95 95 LEU HB3 H 1 1.475 0.02 . 2 . . . . 95 LEU HB3 . 18848 1 653 . 1 1 95 95 LEU C C 13 176.963 0.2 . 1 . . . . 95 LEU C . 18848 1 654 . 1 1 95 95 LEU CA C 13 56.155 0.2 . 1 . . . . 95 LEU CA . 18848 1 655 . 1 1 95 95 LEU CB C 13 42.901 0.2 . 1 . . . . 95 LEU CB . 18848 1 656 . 1 1 95 95 LEU N N 15 124.230 0.2 . 1 . . . . 95 LEU N . 18848 1 657 . 1 1 96 96 ASN H H 1 8.465 0.02 . 1 . . . . 96 ASN H . 18848 1 658 . 1 1 96 96 ASN HA H 1 4.749 0.02 . 1 . . . . 96 ASN HA . 18848 1 659 . 1 1 96 96 ASN HB2 H 1 2.845 0.02 . 2 . . . . 96 ASN HB2 . 18848 1 660 . 1 1 96 96 ASN HB3 H 1 2.750 0.02 . 2 . . . . 96 ASN HB3 . 18848 1 661 . 1 1 96 96 ASN C C 13 175.535 0.2 . 1 . . . . 96 ASN C . 18848 1 662 . 1 1 96 96 ASN CA C 13 53.281 0.2 . 1 . . . . 96 ASN CA . 18848 1 663 . 1 1 96 96 ASN CB C 13 38.599 0.2 . 1 . . . . 96 ASN CB . 18848 1 664 . 1 1 96 96 ASN N N 15 119.926 0.2 . 1 . . . . 96 ASN N . 18848 1 665 . 1 1 97 97 THR H H 1 8.046 0.02 . 1 . . . . 97 THR H . 18848 1 666 . 1 1 97 97 THR HA H 1 4.275 0.02 . 1 . . . . 97 THR HA . 18848 1 667 . 1 1 97 97 THR HB H 1 4.275 0.02 . 1 . . . . 97 THR HB . 18848 1 668 . 1 1 97 97 THR C C 13 174.511 0.2 . 1 . . . . 97 THR C . 18848 1 669 . 1 1 97 97 THR CA C 13 62.291 0.2 . 1 . . . . 97 THR CA . 18848 1 670 . 1 1 97 97 THR CB C 13 69.540 0.2 . 1 . . . . 97 THR CB . 18848 1 671 . 1 1 97 97 THR N N 15 115.102 0.2 . 1 . . . . 97 THR N . 18848 1 672 . 1 1 98 98 ALA H H 1 8.159 0.02 . 1 . . . . 98 ALA H . 18848 1 673 . 1 1 98 98 ALA HA H 1 4.336 0.02 . 1 . . . . 98 ALA HA . 18848 1 674 . 1 1 98 98 ALA HB1 H 1 1.401 0.02 . 1 . . . . 98 ALA HB1 . 18848 1 675 . 1 1 98 98 ALA HB2 H 1 1.401 0.02 . 1 . . . . 98 ALA HB2 . 18848 1 676 . 1 1 98 98 ALA HB3 H 1 1.401 0.02 . 1 . . . . 98 ALA HB3 . 18848 1 677 . 1 1 98 98 ALA C C 13 177.714 0.2 . 1 . . . . 98 ALA C . 18848 1 678 . 1 1 98 98 ALA CA C 13 52.808 0.2 . 1 . . . . 98 ALA CA . 18848 1 679 . 1 1 98 98 ALA CB C 13 19.178 0.2 . 1 . . . . 98 ALA CB . 18848 1 680 . 1 1 98 98 ALA N N 15 126.186 0.2 . 1 . . . . 98 ALA N . 18848 1 681 . 1 1 99 99 LEU H H 1 7.980 0.02 . 1 . . . . 99 LEU H . 18848 1 682 . 1 1 99 99 LEU HA H 1 4.299 0.02 . 1 . . . . 99 LEU HA . 18848 1 683 . 1 1 99 99 LEU HB2 H 1 1.600 0.02 . 1 . . . . 99 LEU HB2 . 18848 1 684 . 1 1 99 99 LEU HB3 H 1 1.600 0.02 . 1 . . . . 99 LEU HB3 . 18848 1 685 . 1 1 99 99 LEU C C 13 177.025 0.2 . 1 . . . . 99 LEU C . 18848 1 686 . 1 1 99 99 LEU CA C 13 55.376 0.2 . 1 . . . . 99 LEU CA . 18848 1 687 . 1 1 99 99 LEU CB C 13 42.575 0.2 . 1 . . . . 99 LEU CB . 18848 1 688 . 1 1 99 99 LEU N N 15 120.837 0.2 . 1 . . . . 99 LEU N . 18848 1 689 . 1 1 100 100 ASN H H 1 8.310 0.02 . 1 . . . . 100 ASN H . 18848 1 690 . 1 1 100 100 ASN HA H 1 4.710 0.02 . 1 . . . . 100 ASN HA . 18848 1 691 . 1 1 100 100 ASN HB2 H 1 2.755 0.02 . 2 . . . . 100 ASN HB2 . 18848 1 692 . 1 1 100 100 ASN HB3 H 1 2.864 0.02 . 2 . . . . 100 ASN HB3 . 18848 1 693 . 1 1 100 100 ASN C C 13 175.028 0.2 . 1 . . . . 100 ASN C . 18848 1 694 . 1 1 100 100 ASN CA C 13 53.298 0.2 . 1 . . . . 100 ASN CA . 18848 1 695 . 1 1 100 100 ASN CB C 13 38.715 0.2 . 1 . . . . 100 ASN CB . 18848 1 696 . 1 1 100 100 ASN N N 15 119.570 0.2 . 1 . . . . 100 ASN N . 18848 1 697 . 1 1 101 101 LEU H H 1 8.192 0.02 . 1 . . . . 101 LEU H . 18848 1 698 . 1 1 101 101 LEU HA H 1 4.341 0.02 . 1 . . . . 101 LEU HA . 18848 1 699 . 1 1 101 101 LEU HB2 H 1 1.636 0.02 . 1 . . . . 101 LEU HB2 . 18848 1 700 . 1 1 101 101 LEU HB3 H 1 1.636 0.02 . 1 . . . . 101 LEU HB3 . 18848 1 701 . 1 1 101 101 LEU C C 13 177.529 0.2 . 1 . . . . 101 LEU C . 18848 1 702 . 1 1 101 101 LEU CA C 13 55.339 0.2 . 1 . . . . 101 LEU CA . 18848 1 703 . 1 1 101 101 LEU CB C 13 42.419 0.2 . 1 . . . . 101 LEU CB . 18848 1 704 . 1 1 101 101 LEU N N 15 123.093 0.2 . 1 . . . . 101 LEU N . 18848 1 705 . 1 1 102 102 GLU H H 1 8.328 0.02 . 1 . . . . 102 GLU H . 18848 1 706 . 1 1 102 102 GLU HA H 1 4.293 0.02 . 1 . . . . 102 GLU HA . 18848 1 707 . 1 1 102 102 GLU HB2 H 1 1.984 0.02 . 2 . . . . 102 GLU HB2 . 18848 1 708 . 1 1 102 102 GLU HB3 H 1 2.076 0.02 . 2 . . . . 102 GLU HB3 . 18848 1 709 . 1 1 102 102 GLU C C 13 176.470 0.2 . 1 . . . . 102 GLU C . 18848 1 710 . 1 1 102 102 GLU CA C 13 56.721 0.2 . 1 . . . . 102 GLU CA . 18848 1 711 . 1 1 102 102 GLU CB C 13 30.198 0.2 . 1 . . . . 102 GLU CB . 18848 1 712 . 1 1 102 102 GLU N N 15 121.740 0.2 . 1 . . . . 102 GLU N . 18848 1 713 . 1 1 103 103 LYS H H 1 8.240 0.02 . 1 . . . . 103 LYS H . 18848 1 714 . 1 1 103 103 LYS HA H 1 4.341 0.02 . 1 . . . . 103 LYS HA . 18848 1 715 . 1 1 103 103 LYS HB2 H 1 1.791 0.02 . 2 . . . . 103 LYS HB2 . 18848 1 716 . 1 1 103 103 LYS HB3 H 1 1.835 0.02 . 2 . . . . 103 LYS HB3 . 18848 1 717 . 1 1 103 103 LYS C C 13 176.331 0.2 . 1 . . . . 103 LYS C . 18848 1 718 . 1 1 103 103 LYS CA C 13 56.367 0.2 . 1 . . . . 103 LYS CA . 18848 1 719 . 1 1 103 103 LYS CB C 13 33.423 0.2 . 1 . . . . 103 LYS CB . 18848 1 720 . 1 1 103 103 LYS N N 15 122.612 0.2 . 1 . . . . 103 LYS N . 18848 1 721 . 1 1 104 104 ASP H H 1 8.433 0.02 . 1 . . . . 104 ASP H . 18848 1 722 . 1 1 104 104 ASP HA H 1 4.636 0.02 . 1 . . . . 104 ASP HA . 18848 1 723 . 1 1 104 104 ASP HB2 H 1 2.776 0.02 . 2 . . . . 104 ASP HB2 . 18848 1 724 . 1 1 104 104 ASP HB3 H 1 2.664 0.02 . 2 . . . . 104 ASP HB3 . 18848 1 725 . 1 1 104 104 ASP C C 13 176.440 0.2 . 1 . . . . 104 ASP C . 18848 1 726 . 1 1 104 104 ASP CA C 13 54.687 0.2 . 1 . . . . 104 ASP CA . 18848 1 727 . 1 1 104 104 ASP CB C 13 41.210 0.2 . 1 . . . . 104 ASP CB . 18848 1 728 . 1 1 104 104 ASP N N 15 122.392 0.2 . 1 . . . . 104 ASP N . 18848 1 729 . 1 1 105 105 SER H H 1 8.230 0.02 . 1 . . . . 105 SER H . 18848 1 730 . 1 1 105 105 SER HA H 1 4.444 0.02 . 1 . . . . 105 SER HA . 18848 1 731 . 1 1 105 105 SER HB2 H 1 3.870 0.02 . 2 . . . . 105 SER HB2 . 18848 1 732 . 1 1 105 105 SER HB3 H 1 3.921 0.02 . 2 . . . . 105 SER HB3 . 18848 1 733 . 1 1 105 105 SER C C 13 174.404 0.2 . 1 . . . . 105 SER C . 18848 1 734 . 1 1 105 105 SER CA C 13 58.712 0.2 . 1 . . . . 105 SER CA . 18848 1 735 . 1 1 105 105 SER CB C 13 64.095 0.2 . 1 . . . . 105 SER CB . 18848 1 736 . 1 1 105 105 SER N N 15 116.554 0.2 . 1 . . . . 105 SER N . 18848 1 737 . 1 1 106 106 ASP H H 1 8.441 0.02 . 1 . . . . 106 ASP H . 18848 1 738 . 1 1 106 106 ASP HA H 1 4.679 0.02 . 1 . . . . 106 ASP HA . 18848 1 739 . 1 1 106 106 ASP HB2 H 1 2.766 0.02 . 2 . . . . 106 ASP HB2 . 18848 1 740 . 1 1 106 106 ASP HB3 H 1 2.701 0.02 . 2 . . . . 106 ASP HB3 . 18848 1 741 . 1 1 106 106 ASP C C 13 176.084 0.2 . 1 . . . . 106 ASP C . 18848 1 742 . 1 1 106 106 ASP CA C 13 54.559 0.2 . 1 . . . . 106 ASP CA . 18848 1 743 . 1 1 106 106 ASP CB C 13 41.051 0.2 . 1 . . . . 106 ASP CB . 18848 1 744 . 1 1 106 106 ASP N N 15 122.726 0.2 . 1 . . . . 106 ASP N . 18848 1 745 . 1 1 107 107 LEU H H 1 8.048 0.02 . 1 . . . . 107 LEU H . 18848 1 746 . 1 1 107 107 LEU HA H 1 4.372 0.02 . 1 . . . . 107 LEU HA . 18848 1 747 . 1 1 107 107 LEU HB2 H 1 1.657 0.02 . 1 . . . . 107 LEU HB2 . 18848 1 748 . 1 1 107 107 LEU HB3 H 1 1.657 0.02 . 1 . . . . 107 LEU HB3 . 18848 1 749 . 1 1 107 107 LEU C C 13 176.575 0.2 . 1 . . . . 107 LEU C . 18848 1 750 . 1 1 107 107 LEU CA C 13 55.323 0.2 . 1 . . . . 107 LEU CA . 18848 1 751 . 1 1 107 107 LEU CB C 13 42.629 0.2 . 1 . . . . 107 LEU CB . 18848 1 752 . 1 1 107 107 LEU N N 15 122.433 0.2 . 1 . . . . 107 LEU N . 18848 1 753 . 1 1 108 108 GLU H H 1 7.849 0.02 . 1 . . . . 108 GLU H . 18848 1 754 . 1 1 108 108 GLU HA H 1 4.138 0.02 . 1 . . . . 108 GLU HA . 18848 1 755 . 1 1 108 108 GLU HB2 H 1 1.903 0.02 . 1 . . . . 108 GLU HB2 . 18848 1 756 . 1 1 108 108 GLU C C 13 181.229 0.2 . 1 . . . . 108 GLU C . 18848 1 757 . 1 1 108 108 GLU CA C 13 58.058 0.2 . 1 . . . . 108 GLU CA . 18848 1 758 . 1 1 108 108 GLU CB C 13 31.239 0.2 . 1 . . . . 108 GLU CB . 18848 1 759 . 1 1 108 108 GLU N N 15 126.542 0.2 . 1 . . . . 108 GLU N . 18848 1 stop_ save_