data_4295 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4295 _Entry.Title ; Titin Module A71 from Human Cardiac Muscle ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-01-18 _Entry.Accession_date 1999-01-19 _Entry.Last_release_date 1999-02-12 _Entry.Original_release_date 1999-02-12 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _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 C. Muhle-Goll . . . 4295 2 A. Pastore . . . 4295 3 M. Nilges . . . 4295 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4295 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 101 4295 '1H chemical shifts' 731 4295 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 . . 1999-02-12 1999-01-18 original author . 4295 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4295 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98455511 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Muhle-Goll, C., Pastore, A., and Nilges, M., "The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains," Structure 6, 1291-1302 (1998). ; _Citation.Title ; The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full . _Citation.Journal_volume 6 _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 1291 _Citation.Page_last 1302 _Citation.Year 1998 _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 C. Muhle-Goll . . . 4295 1 2 A. Pastore . . . 4295 1 3 M. Nilges . . . 4295 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID connectin 4295 1 'fibronectin type III' 4295 1 titin 4295 1 stop_ save_ save_ref2 _Citation.Sf_category citations _Citation.Sf_framecode ref2 _Citation.Entry_ID 4295 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9081541 _Citation.Full_citation ; Muhle-Goll C., Nilges M., Pastore A., "1H and 15N NMR Resonance Assignments and Secondary Structure of Titin Type I domains," J. Biomol. NMR 9, (1997) ; _Citation.Title '1H and 15N NMR resonance assignments and secondary structure of titin type I domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 9 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 2 _Citation.Page_last 10 _Citation.Year 1997 _Citation.Details ; Titin/connectin is a giant muscle protein with a highly modular architecture consisting of multiple repeats of two sequence motifs, named type I and type II. Type I modules have been suggested to be intracellular members of the fibronectin type III (Fn3) domain family. Along the titin sequence they are exclusively present in the region of the molecule located in the sarcomere A-band. This region has been shown to interact with myosin and C-protein. One of the most noticeable features of type I modules is that they are particularly rich in semiconserved prolines, since these residues account for about 8% of their sequence. We have determined the secondary structure of a representative type I domain (A71) by 15N and 1H NMR. We show that the type I domains of titin have the Fn3 fold as proposed, consisting of a three- and a four-stranded beta-sheet. When the two sheets are placed on top of each other to form the beta-sandwich characteristic of the Fn3 fold, 8 out of 10 prolines are found on the same side of the molecule and form an exposed hydrophobic patch. This suggests that the semiconserved prolines might be relevant for the function of type I modules, providing a surface for binding to other A-band proteins. The secondary structure of A71 was structurally aligned to other extracellular Fn3 modules of known 3D structure. The alignment shows that titin type I modules have closest similarity to the first Fn3 domain of Drosophila neuroglian. ; 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 C Muhle-Goll C. . . 4295 2 2 M Nilges M. . . 4295 2 3 A Pastore A. . . 4295 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_Titin _Assembly.Sf_category assembly _Assembly.Sf_framecode Titin _Assembly.Entry_ID 4295 _Assembly.ID 1 _Assembly.Name 'Titin type I domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4295 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 Titin_type_I_domain-A71 1 $Titin_type_I_domain-A71 . . . native . . . . . 4295 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 . PDB 1BPV . 'Titin Module A71 From Human Cardiac Muscle, Nmr, 50 Structures' . . . . 4295 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Titin abbreviation 4295 1 'Titin type I domain' system 4295 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'muscle protein' 4295 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Titin_type_I_domain-A71 _Entity.Sf_category entity _Entity.Sf_framecode Titin_type_I_domain-A71 _Entity.Entry_ID 4295 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Titin type I domain' _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 ; MHHHHHHSSPIDPPGKPVPL NITRHTVTLKWAKPEYTGGF KITSYIVEKRDLPNGRWLKA NFSNILENEFTVSGLTEDAA YEFRVIAKNAAGAISPPSEP SDAITCRDDVEA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 112 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 12458 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1BPV . "Titin Module A71 From Human Cardiac Muscle, Nmr, 50 Structures" . . . . . 100.00 112 100.00 100.00 2.83e-76 . . . . 4295 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID Titin abbreviation 4295 1 'Titin type I domain' common 4295 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 4295 1 2 . HIS . 4295 1 3 . HIS . 4295 1 4 . HIS . 4295 1 5 . HIS . 4295 1 6 . HIS . 4295 1 7 . HIS . 4295 1 8 . SER . 4295 1 9 . SER . 4295 1 10 . PRO . 4295 1 11 . ILE . 4295 1 12 . ASP . 4295 1 13 . PRO . 4295 1 14 . PRO . 4295 1 15 . GLY . 4295 1 16 . LYS . 4295 1 17 . PRO . 4295 1 18 . VAL . 4295 1 19 . PRO . 4295 1 20 . LEU . 4295 1 21 . ASN . 4295 1 22 . ILE . 4295 1 23 . THR . 4295 1 24 . ARG . 4295 1 25 . HIS . 4295 1 26 . THR . 4295 1 27 . VAL . 4295 1 28 . THR . 4295 1 29 . LEU . 4295 1 30 . LYS . 4295 1 31 . TRP . 4295 1 32 . ALA . 4295 1 33 . LYS . 4295 1 34 . PRO . 4295 1 35 . GLU . 4295 1 36 . TYR . 4295 1 37 . THR . 4295 1 38 . GLY . 4295 1 39 . GLY . 4295 1 40 . PHE . 4295 1 41 . LYS . 4295 1 42 . ILE . 4295 1 43 . THR . 4295 1 44 . SER . 4295 1 45 . TYR . 4295 1 46 . ILE . 4295 1 47 . VAL . 4295 1 48 . GLU . 4295 1 49 . LYS . 4295 1 50 . ARG . 4295 1 51 . ASP . 4295 1 52 . LEU . 4295 1 53 . PRO . 4295 1 54 . ASN . 4295 1 55 . GLY . 4295 1 56 . ARG . 4295 1 57 . TRP . 4295 1 58 . LEU . 4295 1 59 . LYS . 4295 1 60 . ALA . 4295 1 61 . ASN . 4295 1 62 . PHE . 4295 1 63 . SER . 4295 1 64 . ASN . 4295 1 65 . ILE . 4295 1 66 . LEU . 4295 1 67 . GLU . 4295 1 68 . ASN . 4295 1 69 . GLU . 4295 1 70 . PHE . 4295 1 71 . THR . 4295 1 72 . VAL . 4295 1 73 . SER . 4295 1 74 . GLY . 4295 1 75 . LEU . 4295 1 76 . THR . 4295 1 77 . GLU . 4295 1 78 . ASP . 4295 1 79 . ALA . 4295 1 80 . ALA . 4295 1 81 . TYR . 4295 1 82 . GLU . 4295 1 83 . PHE . 4295 1 84 . ARG . 4295 1 85 . VAL . 4295 1 86 . ILE . 4295 1 87 . ALA . 4295 1 88 . LYS . 4295 1 89 . ASN . 4295 1 90 . ALA . 4295 1 91 . ALA . 4295 1 92 . GLY . 4295 1 93 . ALA . 4295 1 94 . ILE . 4295 1 95 . SER . 4295 1 96 . PRO . 4295 1 97 . PRO . 4295 1 98 . SER . 4295 1 99 . GLU . 4295 1 100 . PRO . 4295 1 101 . SER . 4295 1 102 . ASP . 4295 1 103 . ALA . 4295 1 104 . ILE . 4295 1 105 . THR . 4295 1 106 . CYS . 4295 1 107 . ARG . 4295 1 108 . ASP . 4295 1 109 . ASP . 4295 1 110 . VAL . 4295 1 111 . GLU . 4295 1 112 . ALA . 4295 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 4295 1 . HIS 2 2 4295 1 . HIS 3 3 4295 1 . HIS 4 4 4295 1 . HIS 5 5 4295 1 . HIS 6 6 4295 1 . HIS 7 7 4295 1 . SER 8 8 4295 1 . SER 9 9 4295 1 . PRO 10 10 4295 1 . ILE 11 11 4295 1 . ASP 12 12 4295 1 . PRO 13 13 4295 1 . PRO 14 14 4295 1 . GLY 15 15 4295 1 . LYS 16 16 4295 1 . PRO 17 17 4295 1 . VAL 18 18 4295 1 . PRO 19 19 4295 1 . LEU 20 20 4295 1 . ASN 21 21 4295 1 . ILE 22 22 4295 1 . THR 23 23 4295 1 . ARG 24 24 4295 1 . HIS 25 25 4295 1 . THR 26 26 4295 1 . VAL 27 27 4295 1 . THR 28 28 4295 1 . LEU 29 29 4295 1 . LYS 30 30 4295 1 . TRP 31 31 4295 1 . ALA 32 32 4295 1 . LYS 33 33 4295 1 . PRO 34 34 4295 1 . GLU 35 35 4295 1 . TYR 36 36 4295 1 . THR 37 37 4295 1 . GLY 38 38 4295 1 . GLY 39 39 4295 1 . PHE 40 40 4295 1 . LYS 41 41 4295 1 . ILE 42 42 4295 1 . THR 43 43 4295 1 . SER 44 44 4295 1 . TYR 45 45 4295 1 . ILE 46 46 4295 1 . VAL 47 47 4295 1 . GLU 48 48 4295 1 . LYS 49 49 4295 1 . ARG 50 50 4295 1 . ASP 51 51 4295 1 . LEU 52 52 4295 1 . PRO 53 53 4295 1 . ASN 54 54 4295 1 . GLY 55 55 4295 1 . ARG 56 56 4295 1 . TRP 57 57 4295 1 . LEU 58 58 4295 1 . LYS 59 59 4295 1 . ALA 60 60 4295 1 . ASN 61 61 4295 1 . PHE 62 62 4295 1 . SER 63 63 4295 1 . ASN 64 64 4295 1 . ILE 65 65 4295 1 . LEU 66 66 4295 1 . GLU 67 67 4295 1 . ASN 68 68 4295 1 . GLU 69 69 4295 1 . PHE 70 70 4295 1 . THR 71 71 4295 1 . VAL 72 72 4295 1 . SER 73 73 4295 1 . GLY 74 74 4295 1 . LEU 75 75 4295 1 . THR 76 76 4295 1 . GLU 77 77 4295 1 . ASP 78 78 4295 1 . ALA 79 79 4295 1 . ALA 80 80 4295 1 . TYR 81 81 4295 1 . GLU 82 82 4295 1 . PHE 83 83 4295 1 . ARG 84 84 4295 1 . VAL 85 85 4295 1 . ILE 86 86 4295 1 . ALA 87 87 4295 1 . LYS 88 88 4295 1 . ASN 89 89 4295 1 . ALA 90 90 4295 1 . ALA 91 91 4295 1 . GLY 92 92 4295 1 . ALA 93 93 4295 1 . ILE 94 94 4295 1 . SER 95 95 4295 1 . PRO 96 96 4295 1 . PRO 97 97 4295 1 . SER 98 98 4295 1 . GLU 99 99 4295 1 . PRO 100 100 4295 1 . SER 101 101 4295 1 . ASP 102 102 4295 1 . ALA 103 103 4295 1 . ILE 104 104 4295 1 . THR 105 105 4295 1 . CYS 106 106 4295 1 . ARG 107 107 4295 1 . ASP 108 108 4295 1 . ASP 109 109 4295 1 . VAL 110 110 4295 1 . GLU 111 111 4295 1 . ALA 112 112 4295 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 4295 _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 $Titin_type_I_domain-A71 . 9606 . . 'Homo sapiens' Human . . . Eukaryota Homo sapiens . . . heart muscle . . . . sarcomere . . . . . . . . . . . 4295 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 4295 _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 $Titin_type_I_domain-A71 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli Bl21 . . . . . . . . . . . . plasmid . . pLysS . . . . . . 4295 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4295 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Titin type I domain' '[U-90% 15N]' . . 1 $Titin_type_I_domain-A71 . . 1.2 . . mM . . . . 4295 1 2 NaCl . . . . . . . 50 . . mM . . . . 4295 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 4295 _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 pH 5.6 0.2 na 4295 1 temperature 310 1 K 4295 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4295 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX600 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4295 _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 NMR_spectrometer Bruker AMX600 . 600 . . . 4295 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 4295 _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 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4295 1 2 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4295 1 3 HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4295 1 4 '3D NOESY-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4295 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4295 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4295 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4295 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4295 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4295 _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 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4295 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4295 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_one _Assigned_chem_shift_list.Entry_ID 4295 _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 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; Some residues showed two sets of resonances indicative of a second minor conformational species ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4295 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 9 9 SER H H 1 8.11 0.02 . 1 . . . . . . . . 4295 1 2 . 1 1 9 9 SER HA H 1 4.81 0.02 . 1 . . . . . . . . 4295 1 3 . 1 1 9 9 SER HB2 H 1 3.87 0.02 . 1 . . . . . . . . 4295 1 4 . 1 1 9 9 SER HB3 H 1 3.87 0.02 . 1 . . . . . . . . 4295 1 5 . 1 1 10 10 PRO HA H 1 4.45 0.02 . 1 . . . . . . . . 4295 1 6 . 1 1 10 10 PRO HB2 H 1 2.22 0.02 . 1 . . . . . . . . 4295 1 7 . 1 1 10 10 PRO HB3 H 1 2.22 0.02 . 1 . . . . . . . . 4295 1 8 . 1 1 10 10 PRO HG2 H 1 2.58 0.02 . 1 . . . . . . . . 4295 1 9 . 1 1 10 10 PRO HG3 H 1 2.58 0.02 . 1 . . . . . . . . 4295 1 10 . 1 1 10 10 PRO HD2 H 1 3.79 0.02 . 1 . . . . . . . . 4295 1 11 . 1 1 10 10 PRO HD3 H 1 3.79 0.02 . 1 . . . . . . . . 4295 1 12 . 1 1 11 11 ILE H H 1 7.27 0.02 . 1 . . . . . . . . 4295 1 13 . 1 1 11 11 ILE HA H 1 3.98 0.02 . 1 . . . . . . . . 4295 1 14 . 1 1 11 11 ILE HB H 1 1.30 0.02 . 1 . . . . . . . . 4295 1 15 . 1 1 11 11 ILE HG12 H 1 0.65 0.02 . 1 . . . . . . . . 4295 1 16 . 1 1 11 11 ILE HG13 H 1 0.65 0.02 . 1 . . . . . . . . 4295 1 17 . 1 1 11 11 ILE HG21 H 1 0.84 0.02 . 1 . . . . . . . . 4295 1 18 . 1 1 11 11 ILE HG22 H 1 0.84 0.02 . 1 . . . . . . . . 4295 1 19 . 1 1 11 11 ILE HG23 H 1 0.84 0.02 . 1 . . . . . . . . 4295 1 20 . 1 1 11 11 ILE HD11 H 1 0.48 0.02 . 1 . . . . . . . . 4295 1 21 . 1 1 11 11 ILE HD12 H 1 0.48 0.02 . 1 . . . . . . . . 4295 1 22 . 1 1 11 11 ILE HD13 H 1 0.48 0.02 . 1 . . . . . . . . 4295 1 23 . 1 1 11 11 ILE N N 15 115.19 0.05 . 1 . . . . . . . . 4295 1 24 . 1 1 12 12 ASP H H 1 7.98 0.02 . 1 . . . . . . . . 4295 1 25 . 1 1 12 12 ASP HA H 1 4.80 0.02 . 1 . . . . . . . . 4295 1 26 . 1 1 12 12 ASP HB2 H 1 2.89 0.02 . 2 . . . . . . . . 4295 1 27 . 1 1 12 12 ASP HB3 H 1 2.60 0.02 . 2 . . . . . . . . 4295 1 28 . 1 1 12 12 ASP N N 15 126.78 0.05 . 1 . . . . . . . . 4295 1 29 . 1 1 13 13 PRO HA H 1 4.75 0.02 . 1 . . . . . . . . 4295 1 30 . 1 1 13 13 PRO HB2 H 1 2.02 0.02 . 1 . . . . . . . . 4295 1 31 . 1 1 13 13 PRO HB3 H 1 1.74 0.02 . 1 . . . . . . . . 4295 1 32 . 1 1 13 13 PRO HG2 H 1 1.85 0.02 . 1 . . . . . . . . 4295 1 33 . 1 1 13 13 PRO HG3 H 1 1.85 0.02 . 1 . . . . . . . . 4295 1 34 . 1 1 13 13 PRO HD2 H 1 3.90 0.02 . 1 . . . . . . . . 4295 1 35 . 1 1 13 13 PRO HD3 H 1 3.61 0.02 . 1 . . . . . . . . 4295 1 36 . 1 1 14 14 PRO HA H 1 4.33 0.02 . 1 . . . . . . . . 4295 1 37 . 1 1 14 14 PRO HB2 H 1 2.38 0.02 . 2 . . . . . . . . 4295 1 38 . 1 1 14 14 PRO HB3 H 1 2.25 0.02 . 2 . . . . . . . . 4295 1 39 . 1 1 14 14 PRO HG2 H 1 1.76 0.02 . 2 . . . . . . . . 4295 1 40 . 1 1 14 14 PRO HG3 H 1 1.62 0.02 . 2 . . . . . . . . 4295 1 41 . 1 1 14 14 PRO HD2 H 1 4.09 0.02 . 2 . . . . . . . . 4295 1 42 . 1 1 14 14 PRO HD3 H 1 3.36 0.02 . 2 . . . . . . . . 4295 1 43 . 1 1 15 15 GLY H H 1 8.42 0.02 . 1 . . . . . . . . 4295 1 44 . 1 1 15 15 GLY HA2 H 1 3.98 0.02 . 1 . . . . . . . . 4295 1 45 . 1 1 15 15 GLY HA3 H 1 3.72 0.02 . 1 . . . . . . . . 4295 1 46 . 1 1 15 15 GLY N N 15 106.02 0.05 . 1 . . . . . . . . 4295 1 47 . 1 1 16 16 LYS H H 1 7.45 0.02 . 1 . . . . . . . . 4295 1 48 . 1 1 16 16 LYS HA H 1 4.43 0.02 . 1 . . . . . . . . 4295 1 49 . 1 1 16 16 LYS HB2 H 1 1.74 0.02 . 2 . . . . . . . . 4295 1 50 . 1 1 16 16 LYS HB3 H 1 1.65 0.02 . 2 . . . . . . . . 4295 1 51 . 1 1 16 16 LYS HG2 H 1 1.35 0.02 . 2 . . . . . . . . 4295 1 52 . 1 1 16 16 LYS HG3 H 1 1.17 0.02 . 2 . . . . . . . . 4295 1 53 . 1 1 16 16 LYS HD2 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 54 . 1 1 16 16 LYS HD3 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 55 . 1 1 16 16 LYS HE2 H 1 3.04 0.02 . 1 . . . . . . . . 4295 1 56 . 1 1 16 16 LYS HE3 H 1 3.04 0.02 . 1 . . . . . . . . 4295 1 57 . 1 1 16 16 LYS N N 15 118.90 0.05 . 1 . . . . . . . . 4295 1 58 . 1 1 17 17 PRO HA H 1 5.16 0.02 . 1 . . . . . . . . 4295 1 59 . 1 1 17 17 PRO HB2 H 1 2.10 0.02 . 2 . . . . . . . . 4295 1 60 . 1 1 17 17 PRO HB3 H 1 1.86 0.02 . 2 . . . . . . . . 4295 1 61 . 1 1 17 17 PRO HG2 H 1 1.99 0.02 . 2 . . . . . . . . 4295 1 62 . 1 1 17 17 PRO HG3 H 1 1.64 0.02 . 2 . . . . . . . . 4295 1 63 . 1 1 17 17 PRO HD2 H 1 4.18 0.02 . 2 . . . . . . . . 4295 1 64 . 1 1 17 17 PRO HD3 H 1 3.92 0.02 . 2 . . . . . . . . 4295 1 65 . 1 1 18 18 VAL H H 1 9.00 0.02 . 1 . . . . . . . . 4295 1 66 . 1 1 18 18 VAL HA H 1 4.75 0.02 . 1 . . . . . . . . 4295 1 67 . 1 1 18 18 VAL HB H 1 2.08 0.02 . 1 . . . . . . . . 4295 1 68 . 1 1 18 18 VAL HG11 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 69 . 1 1 18 18 VAL HG12 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 70 . 1 1 18 18 VAL HG13 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 71 . 1 1 18 18 VAL HG21 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 72 . 1 1 18 18 VAL HG22 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 73 . 1 1 18 18 VAL HG23 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 74 . 1 1 18 18 VAL N N 15 118.09 0.05 . 1 . . . . . . . . 4295 1 75 . 1 1 19 19 PRO HA H 1 5.03 0.02 . 1 . . . . . . . . 4295 1 76 . 1 1 19 19 PRO HB2 H 1 1.76 0.02 . 2 . . . . . . . . 4295 1 77 . 1 1 19 19 PRO HB3 H 1 2.07 0.02 . 2 . . . . . . . . 4295 1 78 . 1 1 19 19 PRO HG2 H 1 1.86 0.02 . 2 . . . . . . . . 4295 1 79 . 1 1 19 19 PRO HG3 H 1 2.42 0.02 . 2 . . . . . . . . 4295 1 80 . 1 1 19 19 PRO HD2 H 1 3.93 0.02 . 2 . . . . . . . . 4295 1 81 . 1 1 19 19 PRO HD3 H 1 3.74 0.02 . 2 . . . . . . . . 4295 1 82 . 1 1 20 20 LEU H H 1 9.13 0.02 . 1 . . . . . . . . 4295 1 83 . 1 1 20 20 LEU HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 84 . 1 1 20 20 LEU HB2 H 1 1.46 0.02 . 2 . . . . . . . . 4295 1 85 . 1 1 20 20 LEU HB3 H 1 1.27 0.02 . 2 . . . . . . . . 4295 1 86 . 1 1 20 20 LEU HG H 1 1.27 0.02 . 1 . . . . . . . . 4295 1 87 . 1 1 20 20 LEU HD11 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 88 . 1 1 20 20 LEU HD12 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 89 . 1 1 20 20 LEU HD13 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 90 . 1 1 20 20 LEU HD21 H 1 0.70 0.02 . 2 . . . . . . . . 4295 1 91 . 1 1 20 20 LEU HD22 H 1 0.70 0.02 . 2 . . . . . . . . 4295 1 92 . 1 1 20 20 LEU HD23 H 1 0.70 0.02 . 2 . . . . . . . . 4295 1 93 . 1 1 20 20 LEU N N 15 124.69 0.05 . 1 . . . . . . . . 4295 1 94 . 1 1 21 21 ASN H H 1 7.31 0.02 . 1 . . . . . . . . 4295 1 95 . 1 1 21 21 ASN HA H 1 4.76 0.02 . 1 . . . . . . . . 4295 1 96 . 1 1 21 21 ASN HB2 H 1 2.70 0.02 . 2 . . . . . . . . 4295 1 97 . 1 1 21 21 ASN HB3 H 1 2.31 0.02 . 2 . . . . . . . . 4295 1 98 . 1 1 21 21 ASN HD21 H 1 6.68 0.02 . 2 . . . . . . . . 4295 1 99 . 1 1 21 21 ASN HD22 H 1 7.54 0.02 . 2 . . . . . . . . 4295 1 100 . 1 1 21 21 ASN N N 15 114.71 0.05 . 1 . . . . . . . . 4295 1 101 . 1 1 21 21 ASN ND2 N 15 113.42 0.02 . 1 . . . . . . . . 4295 1 102 . 1 1 22 22 ILE H H 1 8.40 0.02 . 1 . . . . . . . . 4295 1 103 . 1 1 22 22 ILE HA H 1 4.56 0.02 . 1 . . . . . . . . 4295 1 104 . 1 1 22 22 ILE HB H 1 1.70 0.02 . 1 . . . . . . . . 4295 1 105 . 1 1 22 22 ILE HG12 H 1 1.56 0.02 . 1 . . . . . . . . 4295 1 106 . 1 1 22 22 ILE HG13 H 1 1.56 0.02 . 1 . . . . . . . . 4295 1 107 . 1 1 22 22 ILE HG21 H 1 1.26 0.02 . 1 . . . . . . . . 4295 1 108 . 1 1 22 22 ILE HG22 H 1 1.26 0.02 . 1 . . . . . . . . 4295 1 109 . 1 1 22 22 ILE HG23 H 1 1.26 0.02 . 1 . . . . . . . . 4295 1 110 . 1 1 22 22 ILE HD11 H 1 0.99 0.02 . 1 . . . . . . . . 4295 1 111 . 1 1 22 22 ILE HD12 H 1 0.99 0.02 . 1 . . . . . . . . 4295 1 112 . 1 1 22 22 ILE HD13 H 1 0.99 0.02 . 1 . . . . . . . . 4295 1 113 . 1 1 22 22 ILE N N 15 127.43 0.05 . 1 . . . . . . . . 4295 1 114 . 1 1 23 23 THR H H 1 8.90 0.02 . 1 . . . . . . . . 4295 1 115 . 1 1 23 23 THR HA H 1 4.86 0.02 . 1 . . . . . . . . 4295 1 116 . 1 1 23 23 THR HB H 1 4.57 0.02 . 1 . . . . . . . . 4295 1 117 . 1 1 23 23 THR HG21 H 1 1.09 0.02 . 1 . . . . . . . . 4295 1 118 . 1 1 23 23 THR HG22 H 1 1.09 0.02 . 1 . . . . . . . . 4295 1 119 . 1 1 23 23 THR HG23 H 1 1.09 0.02 . 1 . . . . . . . . 4295 1 120 . 1 1 23 23 THR N N 15 118.73 0.05 . 1 . . . . . . . . 4295 1 121 . 1 1 24 24 ARG H H 1 7.84 0.02 . 1 . . . . . . . . 4295 1 122 . 1 1 24 24 ARG HA H 1 3.47 0.02 . 1 . . . . . . . . 4295 1 123 . 1 1 24 24 ARG HB2 H 1 1.39 0.02 . 2 . . . . . . . . 4295 1 124 . 1 1 24 24 ARG HB3 H 1 1.35 0.02 . 2 . . . . . . . . 4295 1 125 . 1 1 24 24 ARG HG2 H 1 1.23 0.02 . 2 . . . . . . . . 4295 1 126 . 1 1 24 24 ARG HG3 H 1 1.05 0.02 . 2 . . . . . . . . 4295 1 127 . 1 1 24 24 ARG HD2 H 1 3.02 0.02 . 2 . . . . . . . . 4295 1 128 . 1 1 24 24 ARG HD3 H 1 2.99 0.02 . 2 . . . . . . . . 4295 1 129 . 1 1 24 24 ARG N N 15 113.75 0.05 . 1 . . . . . . . . 4295 1 130 . 1 1 25 25 HIS H H 1 7.10 0.02 . 1 . . . . . . . . 4295 1 131 . 1 1 25 25 HIS HA H 1 5.10 0.02 . 1 . . . . . . . . 4295 1 132 . 1 1 25 25 HIS HB2 H 1 3.62 0.02 . 2 . . . . . . . . 4295 1 133 . 1 1 25 25 HIS HB3 H 1 2.89 0.02 . 2 . . . . . . . . 4295 1 134 . 1 1 25 25 HIS HE1 H 1 7.32 0.02 . 2 . . . . . . . . 4295 1 135 . 1 1 25 25 HIS HD2 H 1 8.80 0.02 . 2 . . . . . . . . 4295 1 136 . 1 1 25 25 HIS N N 15 107.15 0.05 . 1 . . . . . . . . 4295 1 137 . 1 1 26 26 THR H H 1 7.37 0.02 . 1 . . . . . . . . 4295 1 138 . 1 1 26 26 THR HA H 1 5.51 0.02 . 1 . . . . . . . . 4295 1 139 . 1 1 26 26 THR HB H 1 3.86 0.02 . 1 . . . . . . . . 4295 1 140 . 1 1 26 26 THR HG21 H 1 0.94 0.02 . 1 . . . . . . . . 4295 1 141 . 1 1 26 26 THR HG22 H 1 0.94 0.02 . 1 . . . . . . . . 4295 1 142 . 1 1 26 26 THR HG23 H 1 0.94 0.02 . 1 . . . . . . . . 4295 1 143 . 1 1 26 26 THR N N 15 110.69 0.05 . 1 . . . . . . . . 4295 1 144 . 1 1 27 27 VAL H H 1 8.03 0.02 . 1 . . . . . . . . 4295 1 145 . 1 1 27 27 VAL HA H 1 4.56 0.02 . 1 . . . . . . . . 4295 1 146 . 1 1 27 27 VAL HB H 1 1.45 0.02 . 1 . . . . . . . . 4295 1 147 . 1 1 27 27 VAL HG11 H 1 0.86 0.02 . 2 . . . . . . . . 4295 1 148 . 1 1 27 27 VAL HG12 H 1 0.86 0.02 . 2 . . . . . . . . 4295 1 149 . 1 1 27 27 VAL HG13 H 1 0.86 0.02 . 2 . . . . . . . . 4295 1 150 . 1 1 27 27 VAL HG21 H 1 0.66 0.02 . 2 . . . . . . . . 4295 1 151 . 1 1 27 27 VAL HG22 H 1 0.66 0.02 . 2 . . . . . . . . 4295 1 152 . 1 1 27 27 VAL HG23 H 1 0.66 0.02 . 2 . . . . . . . . 4295 1 153 . 1 1 27 27 VAL N N 15 116.96 0.05 . 1 . . . . . . . . 4295 1 154 . 1 1 28 28 THR H H 1 8.91 0.02 . 1 . . . . . . . . 4295 1 155 . 1 1 28 28 THR HA H 1 4.89 0.02 . 1 . . . . . . . . 4295 1 156 . 1 1 28 28 THR HB H 1 3.74 0.02 . 1 . . . . . . . . 4295 1 157 . 1 1 28 28 THR HG21 H 1 1.03 0.02 . 1 . . . . . . . . 4295 1 158 . 1 1 28 28 THR HG22 H 1 1.03 0.02 . 1 . . . . . . . . 4295 1 159 . 1 1 28 28 THR HG23 H 1 1.03 0.02 . 1 . . . . . . . . 4295 1 160 . 1 1 28 28 THR N N 15 126.14 0.05 . 1 . . . . . . . . 4295 1 161 . 1 1 29 29 LEU H H 1 9.09 0.02 . 1 . . . . . . . . 4295 1 162 . 1 1 29 29 LEU HA H 1 5.17 0.02 . 1 . . . . . . . . 4295 1 163 . 1 1 29 29 LEU HB2 H 1 1.94 0.02 . 2 . . . . . . . . 4295 1 164 . 1 1 29 29 LEU HB3 H 1 1.44 0.02 . 2 . . . . . . . . 4295 1 165 . 1 1 29 29 LEU HG H 1 1.33 0.02 . 1 . . . . . . . . 4295 1 166 . 1 1 29 29 LEU HD11 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 167 . 1 1 29 29 LEU HD12 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 168 . 1 1 29 29 LEU HD13 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 169 . 1 1 29 29 LEU HD21 H 1 0.31 0.02 . 2 . . . . . . . . 4295 1 170 . 1 1 29 29 LEU HD22 H 1 0.31 0.02 . 2 . . . . . . . . 4295 1 171 . 1 1 29 29 LEU HD23 H 1 0.31 0.02 . 2 . . . . . . . . 4295 1 172 . 1 1 29 29 LEU N N 15 130.00 0.05 . 1 . . . . . . . . 4295 1 173 . 1 1 30 30 LYS H H 1 8.53 0.02 . 1 . . . . . . . . 4295 1 174 . 1 1 30 30 LYS HA H 1 4.66 0.02 . 1 . . . . . . . . 4295 1 175 . 1 1 30 30 LYS HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 176 . 1 1 30 30 LYS HB3 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 177 . 1 1 30 30 LYS HG2 H 1 1.29 0.02 . 2 . . . . . . . . 4295 1 178 . 1 1 30 30 LYS HG3 H 1 1.20 0.02 . 2 . . . . . . . . 4295 1 179 . 1 1 30 30 LYS HD2 H 1 1.45 0.02 . 1 . . . . . . . . 4295 1 180 . 1 1 30 30 LYS HD3 H 1 1.45 0.02 . 1 . . . . . . . . 4295 1 181 . 1 1 30 30 LYS HE2 H 1 2.70 0.02 . 1 . . . . . . . . 4295 1 182 . 1 1 30 30 LYS HE3 H 1 2.70 0.02 . 1 . . . . . . . . 4295 1 183 . 1 1 30 30 LYS N N 15 118.73 0.05 . 1 . . . . . . . . 4295 1 184 . 1 1 31 31 TRP H H 1 6.97 0.02 . 1 . . . . . . . . 4295 1 185 . 1 1 31 31 TRP HA H 1 4.91 0.02 . 1 . . . . . . . . 4295 1 186 . 1 1 31 31 TRP HB2 H 1 3.07 0.02 . 2 . . . . . . . . 4295 1 187 . 1 1 31 31 TRP HB3 H 1 2.85 0.02 . 2 . . . . . . . . 4295 1 188 . 1 1 31 31 TRP HD1 H 1 6.49 0.02 . 1 . . . . . . . . 4295 1 189 . 1 1 31 31 TRP HE1 H 1 5.81 0.02 . 1 . . . . . . . . 4295 1 190 . 1 1 31 31 TRP HZ2 H 1 6.60 0.02 . 1 . . . . . . . . 4295 1 191 . 1 1 31 31 TRP HH2 H 1 6.99 0.02 . 1 . . . . . . . . 4295 1 192 . 1 1 31 31 TRP HZ3 H 1 6.59 0.02 . 1 . . . . . . . . 4295 1 193 . 1 1 31 31 TRP HE3 H 1 6.73 0.02 . 1 . . . . . . . . 4295 1 194 . 1 1 31 31 TRP N N 15 120.51 0.05 . 1 . . . . . . . . 4295 1 195 . 1 1 31 31 TRP NE1 N 15 124.69 0.02 . 1 . . . . . . . . 4295 1 196 . 1 1 32 32 ALA H H 1 8.41 0.02 . 1 . . . . . . . . 4295 1 197 . 1 1 32 32 ALA HA H 1 4.33 0.02 . 1 . . . . . . . . 4295 1 198 . 1 1 32 32 ALA HB1 H 1 1.36 0.02 . 1 . . . . . . . . 4295 1 199 . 1 1 32 32 ALA HB2 H 1 1.36 0.02 . 1 . . . . . . . . 4295 1 200 . 1 1 32 32 ALA HB3 H 1 1.36 0.02 . 1 . . . . . . . . 4295 1 201 . 1 1 32 32 ALA N N 15 122.76 0.05 . 1 . . . . . . . . 4295 1 202 . 1 1 33 33 LYS H H 1 8.40 0.02 . 1 . . . . . . . . 4295 1 203 . 1 1 33 33 LYS HA H 1 4.36 0.02 . 1 . . . . . . . . 4295 1 204 . 1 1 33 33 LYS HB2 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 205 . 1 1 33 33 LYS HB3 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 206 . 1 1 33 33 LYS HG2 H 1 1.34 0.02 . 2 . . . . . . . . 4295 1 207 . 1 1 33 33 LYS HG3 H 1 1.18 0.02 . 2 . . . . . . . . 4295 1 208 . 1 1 33 33 LYS HD2 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 209 . 1 1 33 33 LYS HD3 H 1 1.58 0.02 . 1 . . . . . . . . 4295 1 210 . 1 1 33 33 LYS HE2 H 1 3.06 0.02 . 1 . . . . . . . . 4295 1 211 . 1 1 33 33 LYS HE3 H 1 3.06 0.02 . 1 . . . . . . . . 4295 1 212 . 1 1 33 33 LYS N N 15 122.92 0.05 . 1 . . . . . . . . 4295 1 213 . 1 1 34 34 PRO HA H 1 4.26 0.02 . 1 . . . . . . . . 4295 1 214 . 1 1 34 34 PRO HB2 H 1 2.38 0.02 . 1 . . . . . . . . 4295 1 215 . 1 1 34 34 PRO HB3 H 1 2.38 0.02 . 1 . . . . . . . . 4295 1 216 . 1 1 34 34 PRO HD2 H 1 4.11 0.02 . 2 . . . . . . . . 4295 1 217 . 1 1 34 34 PRO HD3 H 1 3.47 0.02 . 2 . . . . . . . . 4295 1 218 . 1 1 35 35 GLU H H 1 8.65 0.02 . 1 . . . . . . . . 4295 1 219 . 1 1 35 35 GLU HA H 1 4.05 0.02 . 1 . . . . . . . . 4295 1 220 . 1 1 35 35 GLU HB2 H 1 2.07 0.02 . 1 . . . . . . . . 4295 1 221 . 1 1 35 35 GLU HB3 H 1 2.07 0.02 . 1 . . . . . . . . 4295 1 222 . 1 1 35 35 GLU HG2 H 1 2.31 0.02 . 2 . . . . . . . . 4295 1 223 . 1 1 35 35 GLU HG3 H 1 2.19 0.02 . 2 . . . . . . . . 4295 1 224 . 1 1 35 35 GLU N N 15 124.85 0.05 . 1 . . . . . . . . 4295 1 225 . 1 1 36 36 TYR H H 1 8.19 0.02 . 1 . . . . . . . . 4295 1 226 . 1 1 36 36 TYR HA H 1 4.79 0.02 . 1 . . . . . . . . 4295 1 227 . 1 1 36 36 TYR HB2 H 1 2.95 0.02 . 2 . . . . . . . . 4295 1 228 . 1 1 36 36 TYR HB3 H 1 2.85 0.02 . 2 . . . . . . . . 4295 1 229 . 1 1 36 36 TYR HD1 H 1 7.10 0.02 . 1 . . . . . . . . 4295 1 230 . 1 1 36 36 TYR HD2 H 1 7.10 0.02 . 1 . . . . . . . . 4295 1 231 . 1 1 36 36 TYR HE1 H 1 6.75 0.02 . 1 . . . . . . . . 4295 1 232 . 1 1 36 36 TYR HE2 H 1 6.75 0.02 . 1 . . . . . . . . 4295 1 233 . 1 1 36 36 TYR N N 15 119.86 0.05 . 1 . . . . . . . . 4295 1 234 . 1 1 37 37 THR H H 1 8.29 0.02 . 1 . . . . . . . . 4295 1 235 . 1 1 37 37 THR HA H 1 4.37 0.02 . 1 . . . . . . . . 4295 1 236 . 1 1 37 37 THR HB H 1 4.66 0.02 . 1 . . . . . . . . 4295 1 237 . 1 1 37 37 THR HG21 H 1 0.96 0.02 . 1 . . . . . . . . 4295 1 238 . 1 1 37 37 THR HG22 H 1 0.96 0.02 . 1 . . . . . . . . 4295 1 239 . 1 1 37 37 THR HG23 H 1 0.96 0.02 . 1 . . . . . . . . 4295 1 240 . 1 1 37 37 THR N N 15 116.80 0.05 . 1 . . . . . . . . 4295 1 241 . 1 1 38 38 GLY H H 1 5.94 0.02 . 1 . . . . . . . . 4295 1 242 . 1 1 38 38 GLY HA2 H 1 3.85 0.02 . 1 . . . . . . . . 4295 1 243 . 1 1 38 38 GLY HA3 H 1 3.53 0.02 . 1 . . . . . . . . 4295 1 244 . 1 1 38 38 GLY N N 15 109.40 0.05 . 1 . . . . . . . . 4295 1 245 . 1 1 39 39 GLY H H 1 7.94 0.02 . 1 . . . . . . . . 4295 1 246 . 1 1 39 39 GLY HA2 H 1 3.87 0.02 . 1 . . . . . . . . 4295 1 247 . 1 1 39 39 GLY HA3 H 1 3.35 0.02 . 1 . . . . . . . . 4295 1 248 . 1 1 39 39 GLY N N 15 106.83 0.05 . 1 . . . . . . . . 4295 1 249 . 1 1 40 40 PHE H H 1 6.73 0.02 . 1 . . . . . . . . 4295 1 250 . 1 1 40 40 PHE HA H 1 4.70 0.02 . 1 . . . . . . . . 4295 1 251 . 1 1 40 40 PHE HB2 H 1 3.10 0.02 . 2 . . . . . . . . 4295 1 252 . 1 1 40 40 PHE HB3 H 1 2.52 0.02 . 2 . . . . . . . . 4295 1 253 . 1 1 40 40 PHE HD1 H 1 7.13 0.02 . 1 . . . . . . . . 4295 1 254 . 1 1 40 40 PHE HD2 H 1 7.13 0.02 . 1 . . . . . . . . 4295 1 255 . 1 1 40 40 PHE HE1 H 1 7.28 0.02 . 1 . . . . . . . . 4295 1 256 . 1 1 40 40 PHE HE2 H 1 7.28 0.02 . 1 . . . . . . . . 4295 1 257 . 1 1 40 40 PHE HZ H 1 7.35 0.02 . 1 . . . . . . . . 4295 1 258 . 1 1 40 40 PHE N N 15 116.32 0.05 . 1 . . . . . . . . 4295 1 259 . 1 1 41 41 LYS H H 1 8.74 0.02 . 1 . . . . . . . . 4295 1 260 . 1 1 41 41 LYS HA H 1 4.17 0.02 . 1 . . . . . . . . 4295 1 261 . 1 1 41 41 LYS HB2 H 1 1.73 0.02 . 1 . . . . . . . . 4295 1 262 . 1 1 41 41 LYS HB3 H 1 1.73 0.02 . 1 . . . . . . . . 4295 1 263 . 1 1 41 41 LYS HG2 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 264 . 1 1 41 41 LYS HG3 H 1 1.41 0.02 . 1 . . . . . . . . 4295 1 265 . 1 1 41 41 LYS HD2 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 266 . 1 1 41 41 LYS HD3 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 267 . 1 1 41 41 LYS HE2 H 1 2.94 0.02 . 1 . . . . . . . . 4295 1 268 . 1 1 41 41 LYS HE3 H 1 2.94 0.02 . 1 . . . . . . . . 4295 1 269 . 1 1 41 41 LYS N N 15 122.28 0.05 . 1 . . . . . . . . 4295 1 270 . 1 1 42 42 ILE H H 1 8.54 0.02 . 1 . . . . . . . . 4295 1 271 . 1 1 42 42 ILE HA H 1 4.13 0.02 . 1 . . . . . . . . 4295 1 272 . 1 1 42 42 ILE HB H 1 1.93 0.02 . 1 . . . . . . . . 4295 1 273 . 1 1 42 42 ILE HG12 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 274 . 1 1 42 42 ILE HG13 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 275 . 1 1 42 42 ILE HG21 H 1 0.39 0.02 . 1 . . . . . . . . 4295 1 276 . 1 1 42 42 ILE HG22 H 1 0.39 0.02 . 1 . . . . . . . . 4295 1 277 . 1 1 42 42 ILE HG23 H 1 0.39 0.02 . 1 . . . . . . . . 4295 1 278 . 1 1 42 42 ILE HD11 H 1 0.66 0.02 . 1 . . . . . . . . 4295 1 279 . 1 1 42 42 ILE HD12 H 1 0.66 0.02 . 1 . . . . . . . . 4295 1 280 . 1 1 42 42 ILE HD13 H 1 0.66 0.02 . 1 . . . . . . . . 4295 1 281 . 1 1 42 42 ILE N N 15 122.44 0.05 . 1 . . . . . . . . 4295 1 282 . 1 1 43 43 THR H H 1 8.55 0.02 . 1 . . . . . . . . 4295 1 283 . 1 1 43 43 THR HA H 1 4.30 0.02 . 1 . . . . . . . . 4295 1 284 . 1 1 43 43 THR HB H 1 4.03 0.02 . 1 . . . . . . . . 4295 1 285 . 1 1 43 43 THR HG21 H 1 1.00 0.02 . 1 . . . . . . . . 4295 1 286 . 1 1 43 43 THR HG22 H 1 1.00 0.02 . 1 . . . . . . . . 4295 1 287 . 1 1 43 43 THR HG23 H 1 1.00 0.02 . 1 . . . . . . . . 4295 1 288 . 1 1 43 43 THR N N 15 120.02 0.05 . 1 . . . . . . . . 4295 1 289 . 1 1 44 44 SER H H 1 7.25 0.02 . 1 . . . . . . . . 4295 1 290 . 1 1 44 44 SER HA H 1 4.79 0.02 . 1 . . . . . . . . 4295 1 291 . 1 1 44 44 SER HB2 H 1 3.75 0.02 . 2 . . . . . . . . 4295 1 292 . 1 1 44 44 SER HB3 H 1 3.57 0.02 . 2 . . . . . . . . 4295 1 293 . 1 1 44 44 SER N N 15 114.07 0.05 . 1 . . . . . . . . 4295 1 294 . 1 1 45 45 TYR H H 1 8.53 0.02 . 1 . . . . . . . . 4295 1 295 . 1 1 45 45 TYR HA H 1 5.40 0.02 . 1 . . . . . . . . 4295 1 296 . 1 1 45 45 TYR HB2 H 1 2.64 0.02 . 2 . . . . . . . . 4295 1 297 . 1 1 45 45 TYR HB3 H 1 2.53 0.02 . 2 . . . . . . . . 4295 1 298 . 1 1 45 45 TYR HD1 H 1 6.72 0.02 . 1 . . . . . . . . 4295 1 299 . 1 1 45 45 TYR HD2 H 1 6.72 0.02 . 1 . . . . . . . . 4295 1 300 . 1 1 45 45 TYR HE1 H 1 7.01 0.02 . 1 . . . . . . . . 4295 1 301 . 1 1 45 45 TYR HE2 H 1 7.01 0.02 . 1 . . . . . . . . 4295 1 302 . 1 1 45 45 TYR N N 15 118.73 0.05 . 1 . . . . . . . . 4295 1 303 . 1 1 46 46 ILE H H 1 9.13 0.02 . 1 . . . . . . . . 4295 1 304 . 1 1 46 46 ILE HA H 1 4.18 0.02 . 1 . . . . . . . . 4295 1 305 . 1 1 46 46 ILE HB H 1 1.47 0.02 . 1 . . . . . . . . 4295 1 306 . 1 1 46 46 ILE HG21 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 307 . 1 1 46 46 ILE HG22 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 308 . 1 1 46 46 ILE HG23 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 309 . 1 1 46 46 ILE HG12 H 1 1.31 0.02 . 1 . . . . . . . . 4295 1 310 . 1 1 46 46 ILE HG13 H 1 0.97 0.02 . 1 . . . . . . . . 4295 1 311 . 1 1 46 46 ILE HD11 H 1 0.65 0.02 . 1 . . . . . . . . 4295 1 312 . 1 1 46 46 ILE HD12 H 1 0.65 0.02 . 1 . . . . . . . . 4295 1 313 . 1 1 46 46 ILE HD13 H 1 0.65 0.02 . 1 . . . . . . . . 4295 1 314 . 1 1 46 46 ILE N N 15 123.08 0.05 . 1 . . . . . . . . 4295 1 315 . 1 1 47 47 VAL H H 1 8.03 0.02 . 1 . . . . . . . . 4295 1 316 . 1 1 47 47 VAL HA H 1 4.44 0.02 . 1 . . . . . . . . 4295 1 317 . 1 1 47 47 VAL HB H 1 1.47 0.02 . 1 . . . . . . . . 4295 1 318 . 1 1 47 47 VAL HG11 H 1 0.80 0.02 . 2 . . . . . . . . 4295 1 319 . 1 1 47 47 VAL HG12 H 1 0.80 0.02 . 2 . . . . . . . . 4295 1 320 . 1 1 47 47 VAL HG13 H 1 0.80 0.02 . 2 . . . . . . . . 4295 1 321 . 1 1 47 47 VAL HG21 H 1 0.37 0.02 . 2 . . . . . . . . 4295 1 322 . 1 1 47 47 VAL HG22 H 1 0.37 0.02 . 2 . . . . . . . . 4295 1 323 . 1 1 47 47 VAL HG23 H 1 0.37 0.02 . 2 . . . . . . . . 4295 1 324 . 1 1 47 47 VAL N N 15 126.62 0.05 . 1 . . . . . . . . 4295 1 325 . 1 1 48 48 GLU H H 1 9.07 0.02 . 1 . . . . . . . . 4295 1 326 . 1 1 48 48 GLU HA H 1 5.26 0.02 . 1 . . . . . . . . 4295 1 327 . 1 1 48 48 GLU HB2 H 1 1.72 0.02 . 2 . . . . . . . . 4295 1 328 . 1 1 48 48 GLU HB3 H 1 1.46 0.02 . 2 . . . . . . . . 4295 1 329 . 1 1 48 48 GLU HG2 H 1 1.93 0.02 . 2 . . . . . . . . 4295 1 330 . 1 1 48 48 GLU HG3 H 1 1.75 0.02 . 2 . . . . . . . . 4295 1 331 . 1 1 48 48 GLU N N 15 125.98 0.05 . 1 . . . . . . . . 4295 1 332 . 1 1 49 49 LYS H H 1 9.56 0.02 . 1 . . . . . . . . 4295 1 333 . 1 1 49 49 LYS HA H 1 5.56 0.02 . 1 . . . . . . . . 4295 1 334 . 1 1 49 49 LYS HB2 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 335 . 1 1 49 49 LYS HB3 H 1 1.56 0.02 . 1 . . . . . . . . 4295 1 336 . 1 1 49 49 LYS HG2 H 1 1.40 0.02 . 1 . . . . . . . . 4295 1 337 . 1 1 49 49 LYS HG3 H 1 1.38 0.02 . 1 . . . . . . . . 4295 1 338 . 1 1 49 49 LYS HD2 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 339 . 1 1 49 49 LYS HD3 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 340 . 1 1 49 49 LYS HE2 H 1 2.97 0.02 . 1 . . . . . . . . 4295 1 341 . 1 1 49 49 LYS HE3 H 1 2.97 0.02 . 1 . . . . . . . . 4295 1 342 . 1 1 49 49 LYS N N 15 120.18 0.05 . 1 . . . . . . . . 4295 1 343 . 1 1 50 50 ARG H H 1 8.43 0.02 . 1 . . . . . . . . 4295 1 344 . 1 1 50 50 ARG HA H 1 4.28 0.02 . 1 . . . . . . . . 4295 1 345 . 1 1 50 50 ARG HB2 H 1 0.43 0.02 . 2 . . . . . . . . 4295 1 346 . 1 1 50 50 ARG HB3 H 1 -0.25 0.02 . 2 . . . . . . . . 4295 1 347 . 1 1 50 50 ARG HG2 H 1 0.14 0.02 . 2 . . . . . . . . 4295 1 348 . 1 1 50 50 ARG HG3 H 1 0.23 0.02 . 2 . . . . . . . . 4295 1 349 . 1 1 50 50 ARG HD2 H 1 2.14 0.02 . 2 . . . . . . . . 4295 1 350 . 1 1 50 50 ARG HD3 H 1 0.72 0.02 . 2 . . . . . . . . 4295 1 351 . 1 1 50 50 ARG HH11 H 1 6.30 0.02 . 1 . . . . . . . . 4295 1 352 . 1 1 50 50 ARG HH12 H 1 6.30 0.02 . 1 . . . . . . . . 4295 1 353 . 1 1 50 50 ARG HH21 H 1 6.11 0.02 . 1 . . . . . . . . 4295 1 354 . 1 1 50 50 ARG HH22 H 1 6.11 0.02 . 1 . . . . . . . . 4295 1 355 . 1 1 50 50 ARG HE H 1 6.93 0.02 . 1 . . . . . . . . 4295 1 356 . 1 1 50 50 ARG N N 15 122.76 0.05 . 1 . . . . . . . . 4295 1 357 . 1 1 50 50 ARG NE N 15 108.60 0.02 . 1 . . . . . . . . 4295 1 358 . 1 1 51 51 ASP H H 1 8.57 0.02 . 1 . . . . . . . . 4295 1 359 . 1 1 51 51 ASP HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 360 . 1 1 51 51 ASP HB2 H 1 2.45 0.02 . 2 . . . . . . . . 4295 1 361 . 1 1 51 51 ASP HB3 H 1 2.29 0.02 . 2 . . . . . . . . 4295 1 362 . 1 1 51 51 ASP N N 15 125.33 0.05 . 1 . . . . . . . . 4295 1 363 . 1 1 52 52 LEU H H 1 7.71 0.02 . 1 . . . . . . . . 4295 1 364 . 1 1 52 52 LEU HA H 1 4.18 0.02 . 1 . . . . . . . . 4295 1 365 . 1 1 52 52 LEU HB2 H 1 1.24 0.02 . 2 . . . . . . . . 4295 1 366 . 1 1 52 52 LEU HB3 H 1 1.09 0.02 . 2 . . . . . . . . 4295 1 367 . 1 1 52 52 LEU HG H 1 1.24 0.02 . 1 . . . . . . . . 4295 1 368 . 1 1 52 52 LEU HD11 H 1 0.59 0.02 . 2 . . . . . . . . 4295 1 369 . 1 1 52 52 LEU HD12 H 1 0.59 0.02 . 2 . . . . . . . . 4295 1 370 . 1 1 52 52 LEU HD13 H 1 0.59 0.02 . 2 . . . . . . . . 4295 1 371 . 1 1 52 52 LEU HD21 H 1 0.46 0.02 . 2 . . . . . . . . 4295 1 372 . 1 1 52 52 LEU HD22 H 1 0.46 0.02 . 2 . . . . . . . . 4295 1 373 . 1 1 52 52 LEU HD23 H 1 0.46 0.02 . 2 . . . . . . . . 4295 1 374 . 1 1 52 52 LEU N N 15 122.60 0.05 . 1 . . . . . . . . 4295 1 375 . 1 1 53 53 PRO HA H 1 4.30 0.02 . 1 . . . . . . . . 4295 1 376 . 1 1 53 53 PRO HB2 H 1 2.24 0.02 . 1 . . . . . . . . 4295 1 377 . 1 1 53 53 PRO HB3 H 1 2.24 0.02 . 1 . . . . . . . . 4295 1 378 . 1 1 53 53 PRO HG2 H 1 1.87 0.02 . 2 . . . . . . . . 4295 1 379 . 1 1 53 53 PRO HG3 H 1 1.72 0.02 . 2 . . . . . . . . 4295 1 380 . 1 1 53 53 PRO HD2 H 1 3.49 0.02 . 2 . . . . . . . . 4295 1 381 . 1 1 53 53 PRO HD3 H 1 3.39 0.02 . 2 . . . . . . . . 4295 1 382 . 1 1 54 54 ASN H H 1 8.34 0.02 . 1 . . . . . . . . 4295 1 383 . 1 1 54 54 ASN HA H 1 4.95 0.02 . 1 . . . . . . . . 4295 1 384 . 1 1 54 54 ASN HB2 H 1 2.94 0.02 . 2 . . . . . . . . 4295 1 385 . 1 1 54 54 ASN HB3 H 1 2.58 0.02 . 2 . . . . . . . . 4295 1 386 . 1 1 54 54 ASN HD21 H 1 7.53 0.02 . 2 . . . . . . . . 4295 1 387 . 1 1 54 54 ASN HD22 H 1 6.91 0.02 . 2 . . . . . . . . 4295 1 388 . 1 1 54 54 ASN N N 15 119.38 0.05 . 1 . . . . . . . . 4295 1 389 . 1 1 54 54 ASN ND2 N 15 114.07 0.02 . 1 . . . . . . . . 4295 1 390 . 1 1 55 55 GLY H H 1 8.07 0.02 . 1 . . . . . . . . 4295 1 391 . 1 1 55 55 GLY HA2 H 1 4.01 0.02 . 1 . . . . . . . . 4295 1 392 . 1 1 55 55 GLY HA3 H 1 4.01 0.02 . 1 . . . . . . . . 4295 1 393 . 1 1 55 55 GLY N N 15 110.20 0.05 . 1 . . . . . . . . 4295 1 394 . 1 1 56 56 ARG H H 1 8.04 0.02 . 1 . . . . . . . . 4295 1 395 . 1 1 56 56 ARG HA H 1 4.44 0.02 . 1 . . . . . . . . 4295 1 396 . 1 1 56 56 ARG HB2 H 1 1.82 0.02 . 1 . . . . . . . . 4295 1 397 . 1 1 56 56 ARG HB3 H 1 1.82 0.02 . 1 . . . . . . . . 4295 1 398 . 1 1 56 56 ARG HG2 H 1 1.66 0.02 . 1 . . . . . . . . 4295 1 399 . 1 1 56 56 ARG HG3 H 1 1.66 0.02 . 1 . . . . . . . . 4295 1 400 . 1 1 56 56 ARG HD2 H 1 3.19 0.02 . 1 . . . . . . . . 4295 1 401 . 1 1 56 56 ARG HD3 H 1 3.19 0.02 . 1 . . . . . . . . 4295 1 402 . 1 1 56 56 ARG N N 15 120.02 0.05 . 1 . . . . . . . . 4295 1 403 . 1 1 57 57 TRP H H 1 7.89 0.02 . 1 . . . . . . . . 4295 1 404 . 1 1 57 57 TRP HA H 1 4.43 0.02 . 1 . . . . . . . . 4295 1 405 . 1 1 57 57 TRP HB2 H 1 2.95 0.02 . 2 . . . . . . . . 4295 1 406 . 1 1 57 57 TRP HB3 H 1 2.85 0.02 . 2 . . . . . . . . 4295 1 407 . 1 1 57 57 TRP HD1 H 1 7.25 0.02 . 1 . . . . . . . . 4295 1 408 . 1 1 57 57 TRP HE1 H 1 9.93 0.02 . 1 . . . . . . . . 4295 1 409 . 1 1 57 57 TRP HZ2 H 1 7.33 0.02 . 1 . . . . . . . . 4295 1 410 . 1 1 57 57 TRP HH2 H 1 6.71 0.02 . 1 . . . . . . . . 4295 1 411 . 1 1 57 57 TRP HZ3 H 1 6.78 0.02 . 1 . . . . . . . . 4295 1 412 . 1 1 57 57 TRP HE3 H 1 7.08 0.02 . 1 . . . . . . . . 4295 1 413 . 1 1 57 57 TRP N N 15 122.28 0.05 . 1 . . . . . . . . 4295 1 414 . 1 1 57 57 TRP NE1 N 15 130.00 0.02 . 1 . . . . . . . . 4295 1 415 . 1 1 58 58 LEU H H 1 9.20 0.02 . 1 . . . . . . . . 4295 1 416 . 1 1 58 58 LEU HA H 1 4.81 0.02 . 1 . . . . . . . . 4295 1 417 . 1 1 58 58 LEU HB2 H 1 1.74 0.02 . 2 . . . . . . . . 4295 1 418 . 1 1 58 58 LEU HB3 H 1 1.63 0.02 . 2 . . . . . . . . 4295 1 419 . 1 1 58 58 LEU HG H 1 1.74 0.02 . 1 . . . . . . . . 4295 1 420 . 1 1 58 58 LEU HD11 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 421 . 1 1 58 58 LEU HD12 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 422 . 1 1 58 58 LEU HD13 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 423 . 1 1 58 58 LEU HD21 H 1 0.88 0.02 . 2 . . . . . . . . 4295 1 424 . 1 1 58 58 LEU HD22 H 1 0.88 0.02 . 2 . . . . . . . . 4295 1 425 . 1 1 58 58 LEU HD23 H 1 0.88 0.02 . 2 . . . . . . . . 4295 1 426 . 1 1 58 58 LEU N N 15 126.14 0.05 . 1 . . . . . . . . 4295 1 427 . 1 1 59 59 LYS H H 1 8.54 0.02 . 1 . . . . . . . . 4295 1 428 . 1 1 59 59 LYS HA H 1 4.17 0.02 . 1 . . . . . . . . 4295 1 429 . 1 1 59 59 LYS HB2 H 1 1.73 0.02 . 2 . . . . . . . . 4295 1 430 . 1 1 59 59 LYS HB3 H 1 1.65 0.02 . 2 . . . . . . . . 4295 1 431 . 1 1 59 59 LYS HG2 H 1 1.46 0.02 . 2 . . . . . . . . 4295 1 432 . 1 1 59 59 LYS HG3 H 1 1.41 0.02 . 2 . . . . . . . . 4295 1 433 . 1 1 59 59 LYS HD2 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 434 . 1 1 59 59 LYS HD3 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 435 . 1 1 59 59 LYS HE2 H 1 2.94 0.02 . 1 . . . . . . . . 4295 1 436 . 1 1 59 59 LYS HE3 H 1 2.94 0.02 . 1 . . . . . . . . 4295 1 437 . 1 1 59 59 LYS N N 15 124.69 0.05 . 1 . . . . . . . . 4295 1 438 . 1 1 60 60 ALA H H 1 9.61 0.02 . 1 . . . . . . . . 4295 1 439 . 1 1 60 60 ALA HA H 1 4.61 0.02 . 1 . . . . . . . . 4295 1 440 . 1 1 60 60 ALA HB1 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 441 . 1 1 60 60 ALA HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 442 . 1 1 60 60 ALA HB3 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 443 . 1 1 60 60 ALA N N 15 126.94 0.05 . 1 . . . . . . . . 4295 1 444 . 1 1 61 61 ASN H H 1 7.94 0.02 . 1 . . . . . . . . 4295 1 445 . 1 1 61 61 ASN HA H 1 4.91 0.02 . 1 . . . . . . . . 4295 1 446 . 1 1 61 61 ASN HB2 H 1 2.56 0.02 . 2 . . . . . . . . 4295 1 447 . 1 1 61 61 ASN HB3 H 1 1.89 0.02 . 2 . . . . . . . . 4295 1 448 . 1 1 61 61 ASN HD21 H 1 7.49 0.02 . 2 . . . . . . . . 4295 1 449 . 1 1 61 61 ASN HD22 H 1 6.17 0.02 . 2 . . . . . . . . 4295 1 450 . 1 1 61 61 ASN N N 15 114.39 0.05 . 1 . . . . . . . . 4295 1 451 . 1 1 61 61 ASN ND2 N 15 115.19 0.02 . 1 . . . . . . . . 4295 1 452 . 1 1 62 62 PHE HA H 1 4.66 0.02 . 1 . . . . . . . . 4295 1 453 . 1 1 62 62 PHE HB2 H 1 3.31 0.02 . 2 . . . . . . . . 4295 1 454 . 1 1 62 62 PHE HB3 H 1 2.98 0.02 . 2 . . . . . . . . 4295 1 455 . 1 1 62 62 PHE HD1 H 1 7.28 0.02 . 1 . . . . . . . . 4295 1 456 . 1 1 62 62 PHE HD2 H 1 7.28 0.02 . 1 . . . . . . . . 4295 1 457 . 1 1 62 62 PHE HE1 H 1 7.35 0.02 . 1 . . . . . . . . 4295 1 458 . 1 1 62 62 PHE HE2 H 1 7.35 0.02 . 1 . . . . . . . . 4295 1 459 . 1 1 63 63 SER H H 1 7.83 0.02 . 1 . . . . . . . . 4295 1 460 . 1 1 63 63 SER HA H 1 4.64 0.02 . 1 . . . . . . . . 4295 1 461 . 1 1 63 63 SER HB2 H 1 3.94 0.02 . 1 . . . . . . . . 4295 1 462 . 1 1 63 63 SER HB3 H 1 3.94 0.02 . 1 . . . . . . . . 4295 1 463 . 1 1 63 63 SER N N 15 115.52 0.05 . 1 . . . . . . . . 4295 1 464 . 1 1 64 64 ASN H H 1 8.59 0.02 . 1 . . . . . . . . 4295 1 465 . 1 1 64 64 ASN HA H 1 4.64 0.02 . 1 . . . . . . . . 4295 1 466 . 1 1 64 64 ASN HB2 H 1 2.74 0.02 . 2 . . . . . . . . 4295 1 467 . 1 1 64 64 ASN HB3 H 1 2.60 0.02 . 2 . . . . . . . . 4295 1 468 . 1 1 64 64 ASN HD21 H 1 7.48 0.02 . 2 . . . . . . . . 4295 1 469 . 1 1 64 64 ASN HD22 H 1 6.82 0.02 . 2 . . . . . . . . 4295 1 470 . 1 1 64 64 ASN ND2 N 15 113.58 0.02 . 1 . . . . . . . . 4295 1 471 . 1 1 65 65 ILE H H 1 8.00 0.02 . 1 . . . . . . . . 4295 1 472 . 1 1 65 65 ILE HA H 1 4.34 0.02 . 1 . . . . . . . . 4295 1 473 . 1 1 65 65 ILE HB H 1 2.05 0.02 . 1 . . . . . . . . 4295 1 474 . 1 1 65 65 ILE HG12 H 1 1.38 0.02 . 1 . . . . . . . . 4295 1 475 . 1 1 65 65 ILE HG13 H 1 0.68 0.02 . 1 . . . . . . . . 4295 1 476 . 1 1 65 65 ILE HG21 H 1 1.38 0.02 . 1 . . . . . . . . 4295 1 477 . 1 1 65 65 ILE HG22 H 1 1.38 0.02 . 1 . . . . . . . . 4295 1 478 . 1 1 65 65 ILE HG23 H 1 1.38 0.02 . 1 . . . . . . . . 4295 1 479 . 1 1 65 65 ILE HD11 H 1 0.10 0.02 . 1 . . . . . . . . 4295 1 480 . 1 1 65 65 ILE HD12 H 1 0.10 0.02 . 1 . . . . . . . . 4295 1 481 . 1 1 65 65 ILE HD13 H 1 0.10 0.02 . 1 . . . . . . . . 4295 1 482 . 1 1 65 65 ILE N N 15 124.53 0.05 . 1 . . . . . . . . 4295 1 483 . 1 1 66 66 LEU H H 1 8.74 0.02 . 1 . . . . . . . . 4295 1 484 . 1 1 66 66 LEU HA H 1 4.56 0.02 . 1 . . . . . . . . 4295 1 485 . 1 1 66 66 LEU HB2 H 1 1.75 0.02 . 2 . . . . . . . . 4295 1 486 . 1 1 66 66 LEU HB3 H 1 1.71 0.02 . 2 . . . . . . . . 4295 1 487 . 1 1 66 66 LEU HG H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 488 . 1 1 66 66 LEU HD11 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 489 . 1 1 66 66 LEU HD12 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 490 . 1 1 66 66 LEU HD13 H 1 0.94 0.02 . 2 . . . . . . . . 4295 1 491 . 1 1 66 66 LEU HD21 H 1 1.09 0.02 . 2 . . . . . . . . 4295 1 492 . 1 1 66 66 LEU HD22 H 1 1.09 0.02 . 2 . . . . . . . . 4295 1 493 . 1 1 66 66 LEU HD23 H 1 1.09 0.02 . 2 . . . . . . . . 4295 1 494 . 1 1 66 66 LEU N N 15 126.94 0.05 . 1 . . . . . . . . 4295 1 495 . 1 1 67 67 GLU H H 1 7.64 0.02 . 1 . . . . . . . . 4295 1 496 . 1 1 67 67 GLU HA H 1 4.67 0.02 . 1 . . . . . . . . 4295 1 497 . 1 1 67 67 GLU HB2 H 1 1.98 0.02 . 1 . . . . . . . . 4295 1 498 . 1 1 67 67 GLU HB3 H 1 1.98 0.02 . 1 . . . . . . . . 4295 1 499 . 1 1 67 67 GLU HG2 H 1 2.32 0.02 . 2 . . . . . . . . 4295 1 500 . 1 1 67 67 GLU HG3 H 1 2.15 0.02 . 2 . . . . . . . . 4295 1 501 . 1 1 67 67 GLU N N 15 119.06 0.05 . 1 . . . . . . . . 4295 1 502 . 1 1 68 68 ASN H H 1 7.98 0.02 . 1 . . . . . . . . 4295 1 503 . 1 1 68 68 ASN HA H 1 3.64 0.02 . 1 . . . . . . . . 4295 1 504 . 1 1 68 68 ASN HB2 H 1 2.16 0.02 . 2 . . . . . . . . 4295 1 505 . 1 1 68 68 ASN HB3 H 1 1.82 0.02 . 2 . . . . . . . . 4295 1 506 . 1 1 68 68 ASN HD21 H 1 7.54 0.02 . 2 . . . . . . . . 4295 1 507 . 1 1 68 68 ASN HD22 H 1 6.45 0.02 . 2 . . . . . . . . 4295 1 508 . 1 1 68 68 ASN N N 15 116.48 0.05 . 1 . . . . . . . . 4295 1 509 . 1 1 68 68 ASN ND2 N 15 112.62 0.02 . 1 . . . . . . . . 4295 1 510 . 1 1 69 69 GLU H H 1 6.61 0.02 . 1 . . . . . . . . 4295 1 511 . 1 1 69 69 GLU HA H 1 4.53 0.02 . 1 . . . . . . . . 4295 1 512 . 1 1 69 69 GLU HB2 H 1 1.57 0.02 . 2 . . . . . . . . 4295 1 513 . 1 1 69 69 GLU HB3 H 1 1.51 0.02 . 2 . . . . . . . . 4295 1 514 . 1 1 69 69 GLU HG2 H 1 1.85 0.02 . 1 . . . . . . . . 4295 1 515 . 1 1 69 69 GLU HG3 H 1 1.85 0.02 . 1 . . . . . . . . 4295 1 516 . 1 1 69 69 GLU N N 15 115.36 0.05 . 1 . . . . . . . . 4295 1 517 . 1 1 70 70 PHE H H 1 8.53 0.02 . 1 . . . . . . . . 4295 1 518 . 1 1 70 70 PHE HA H 1 4.79 0.02 . 1 . . . . . . . . 4295 1 519 . 1 1 70 70 PHE HB2 H 1 2.71 0.02 . 2 . . . . . . . . 4295 1 520 . 1 1 70 70 PHE HB3 H 1 2.57 0.02 . 2 . . . . . . . . 4295 1 521 . 1 1 70 70 PHE HD1 H 1 7.15 0.02 . 1 . . . . . . . . 4295 1 522 . 1 1 70 70 PHE HD2 H 1 7.15 0.02 . 1 . . . . . . . . 4295 1 523 . 1 1 70 70 PHE HE1 H 1 7.26 0.02 . 1 . . . . . . . . 4295 1 524 . 1 1 70 70 PHE HE2 H 1 7.26 0.02 . 1 . . . . . . . . 4295 1 525 . 1 1 70 70 PHE HZ H 1 7.45 0.02 . 1 . . . . . . . . 4295 1 526 . 1 1 70 70 PHE N N 15 121.31 0.05 . 1 . . . . . . . . 4295 1 527 . 1 1 71 71 THR H H 1 7.53 0.02 . 1 . . . . . . . . 4295 1 528 . 1 1 71 71 THR HA H 1 4.74 0.02 . 1 . . . . . . . . 4295 1 529 . 1 1 71 71 THR HB H 1 3.61 0.02 . 1 . . . . . . . . 4295 1 530 . 1 1 71 71 THR HG21 H 1 0.77 0.02 . 1 . . . . . . . . 4295 1 531 . 1 1 71 71 THR HG22 H 1 0.77 0.02 . 1 . . . . . . . . 4295 1 532 . 1 1 71 71 THR HG23 H 1 0.77 0.02 . 1 . . . . . . . . 4295 1 533 . 1 1 71 71 THR N N 15 125.98 0.05 . 1 . . . . . . . . 4295 1 534 . 1 1 72 72 VAL H H 1 8.74 0.02 . 1 . . . . . . . . 4295 1 535 . 1 1 72 72 VAL HA H 1 3.78 0.02 . 1 . . . . . . . . 4295 1 536 . 1 1 72 72 VAL HB H 1 1.83 0.02 . 1 . . . . . . . . 4295 1 537 . 1 1 72 72 VAL HG11 H 1 1.08 0.02 . 2 . . . . . . . . 4295 1 538 . 1 1 72 72 VAL HG12 H 1 1.08 0.02 . 2 . . . . . . . . 4295 1 539 . 1 1 72 72 VAL HG13 H 1 1.08 0.02 . 2 . . . . . . . . 4295 1 540 . 1 1 72 72 VAL HG21 H 1 0.85 0.02 . 2 . . . . . . . . 4295 1 541 . 1 1 72 72 VAL HG22 H 1 0.85 0.02 . 2 . . . . . . . . 4295 1 542 . 1 1 72 72 VAL HG23 H 1 0.85 0.02 . 2 . . . . . . . . 4295 1 543 . 1 1 72 72 VAL N N 15 129.84 0.05 . 1 . . . . . . . . 4295 1 544 . 1 1 73 73 SER H H 1 8.21 0.02 . 1 . . . . . . . . 4295 1 545 . 1 1 73 73 SER HA H 1 5.15 0.02 . 1 . . . . . . . . 4295 1 546 . 1 1 73 73 SER HB2 H 1 3.89 0.02 . 2 . . . . . . . . 4295 1 547 . 1 1 73 73 SER HB3 H 1 3.62 0.02 . 2 . . . . . . . . 4295 1 548 . 1 1 73 73 SER N N 15 121.79 0.05 . 1 . . . . . . . . 4295 1 549 . 1 1 74 74 GLY H H 1 8.41 0.02 . 1 . . . . . . . . 4295 1 550 . 1 1 74 74 GLY HA2 H 1 3.92 0.02 . 1 . . . . . . . . 4295 1 551 . 1 1 74 74 GLY HA3 H 1 3.74 0.02 . 1 . . . . . . . . 4295 1 552 . 1 1 74 74 GLY N N 15 107.95 0.05 . 1 . . . . . . . . 4295 1 553 . 1 1 75 75 LEU H H 1 8.15 0.02 . 1 . . . . . . . . 4295 1 554 . 1 1 75 75 LEU HA H 1 4.34 0.02 . 1 . . . . . . . . 4295 1 555 . 1 1 75 75 LEU HB2 H 1 1.47 0.02 . 2 . . . . . . . . 4295 1 556 . 1 1 75 75 LEU HB3 H 1 1.39 0.02 . 2 . . . . . . . . 4295 1 557 . 1 1 75 75 LEU HG H 1 1.09 0.02 . 1 . . . . . . . . 4295 1 558 . 1 1 75 75 LEU HD11 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 559 . 1 1 75 75 LEU HD12 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 560 . 1 1 75 75 LEU HD13 H 1 0.39 0.02 . 2 . . . . . . . . 4295 1 561 . 1 1 75 75 LEU HD21 H 1 0.08 0.02 . 2 . . . . . . . . 4295 1 562 . 1 1 75 75 LEU HD22 H 1 0.08 0.02 . 2 . . . . . . . . 4295 1 563 . 1 1 75 75 LEU HD23 H 1 0.08 0.02 . 2 . . . . . . . . 4295 1 564 . 1 1 75 75 LEU N N 15 120.99 0.05 . 1 . . . . . . . . 4295 1 565 . 1 1 76 76 THR H H 1 8.59 0.02 . 1 . . . . . . . . 4295 1 566 . 1 1 76 76 THR HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 567 . 1 1 76 76 THR HB H 1 4.13 0.02 . 1 . . . . . . . . 4295 1 568 . 1 1 76 76 THR HG21 H 1 1.34 0.02 . 1 . . . . . . . . 4295 1 569 . 1 1 76 76 THR HG22 H 1 1.34 0.02 . 1 . . . . . . . . 4295 1 570 . 1 1 76 76 THR HG23 H 1 1.34 0.02 . 1 . . . . . . . . 4295 1 571 . 1 1 76 76 THR N N 15 121.31 0.05 . 1 . . . . . . . . 4295 1 572 . 1 1 77 77 GLU H H 1 8.57 0.02 . 1 . . . . . . . . 4295 1 573 . 1 1 77 77 GLU HA H 1 4.34 0.02 . 1 . . . . . . . . 4295 1 574 . 1 1 77 77 GLU HB2 H 1 1.87 0.02 . 2 . . . . . . . . 4295 1 575 . 1 1 77 77 GLU HB3 H 1 1.75 0.02 . 2 . . . . . . . . 4295 1 576 . 1 1 77 77 GLU HG2 H 1 2.29 0.02 . 2 . . . . . . . . 4295 1 577 . 1 1 77 77 GLU HG3 H 1 2.13 0.02 . 2 . . . . . . . . 4295 1 578 . 1 1 77 77 GLU N N 15 129.03 0.05 . 1 . . . . . . . . 4295 1 579 . 1 1 78 78 ASP H H 1 9.25 0.02 . 1 . . . . . . . . 4295 1 580 . 1 1 78 78 ASP HA H 1 4.07 0.02 . 1 . . . . . . . . 4295 1 581 . 1 1 78 78 ASP HB2 H 1 2.96 0.02 . 2 . . . . . . . . 4295 1 582 . 1 1 78 78 ASP HB3 H 1 2.85 0.02 . 2 . . . . . . . . 4295 1 583 . 1 1 78 78 ASP N N 15 120.67 0.05 . 1 . . . . . . . . 4295 1 584 . 1 1 79 79 ALA H H 1 7.75 0.02 . 1 . . . . . . . . 4295 1 585 . 1 1 79 79 ALA HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 586 . 1 1 79 79 ALA HB1 H 1 1.27 0.02 . 1 . . . . . . . . 4295 1 587 . 1 1 79 79 ALA HB2 H 1 1.27 0.02 . 1 . . . . . . . . 4295 1 588 . 1 1 79 79 ALA HB3 H 1 1.27 0.02 . 1 . . . . . . . . 4295 1 589 . 1 1 79 79 ALA N N 15 124.69 0.05 . 1 . . . . . . . . 4295 1 590 . 1 1 80 80 ALA H H 1 7.64 0.02 . 1 . . . . . . . . 4295 1 591 . 1 1 80 80 ALA HA H 1 5.48 0.02 . 1 . . . . . . . . 4295 1 592 . 1 1 80 80 ALA HB1 H 1 1.06 0.02 . 1 . . . . . . . . 4295 1 593 . 1 1 80 80 ALA HB2 H 1 1.06 0.02 . 1 . . . . . . . . 4295 1 594 . 1 1 80 80 ALA HB3 H 1 1.06 0.02 . 1 . . . . . . . . 4295 1 595 . 1 1 80 80 ALA N N 15 121.63 0.05 . 1 . . . . . . . . 4295 1 596 . 1 1 81 81 TYR H H 1 8.90 0.02 . 1 . . . . . . . . 4295 1 597 . 1 1 81 81 TYR HA H 1 5.12 0.02 . 1 . . . . . . . . 4295 1 598 . 1 1 81 81 TYR HB2 H 1 2.19 0.02 . 2 . . . . . . . . 4295 1 599 . 1 1 81 81 TYR HB3 H 1 2.12 0.02 . 2 . . . . . . . . 4295 1 600 . 1 1 81 81 TYR HD1 H 1 6.87 0.02 . 1 . . . . . . . . 4295 1 601 . 1 1 81 81 TYR HD2 H 1 6.87 0.02 . 1 . . . . . . . . 4295 1 602 . 1 1 81 81 TYR HE1 H 1 6.97 0.02 . 1 . . . . . . . . 4295 1 603 . 1 1 81 81 TYR HE2 H 1 6.97 0.02 . 1 . . . . . . . . 4295 1 604 . 1 1 81 81 TYR N N 15 119.54 0.05 . 1 . . . . . . . . 4295 1 605 . 1 1 82 82 GLU H H 1 7.92 0.02 . 1 . . . . . . . . 4295 1 606 . 1 1 82 82 GLU HA H 1 4.45 0.02 . 1 . . . . . . . . 4295 1 607 . 1 1 82 82 GLU HB2 H 1 2.27 0.02 . 1 . . . . . . . . 4295 1 608 . 1 1 82 82 GLU HB3 H 1 2.27 0.02 . 1 . . . . . . . . 4295 1 609 . 1 1 82 82 GLU N N 15 115.52 0.05 . 1 . . . . . . . . 4295 1 610 . 1 1 83 83 PHE H H 1 8.31 0.02 . 1 . . . . . . . . 4295 1 611 . 1 1 83 83 PHE HA H 1 6.09 0.02 . 1 . . . . . . . . 4295 1 612 . 1 1 83 83 PHE HB2 H 1 3.01 0.02 . 2 . . . . . . . . 4295 1 613 . 1 1 83 83 PHE HB3 H 1 2.43 0.02 . 2 . . . . . . . . 4295 1 614 . 1 1 83 83 PHE HD1 H 1 7.22 0.02 . 1 . . . . . . . . 4295 1 615 . 1 1 83 83 PHE HD2 H 1 7.22 0.02 . 1 . . . . . . . . 4295 1 616 . 1 1 83 83 PHE HE1 H 1 6.70 0.02 . 1 . . . . . . . . 4295 1 617 . 1 1 83 83 PHE HE2 H 1 6.70 0.02 . 1 . . . . . . . . 4295 1 618 . 1 1 83 83 PHE HZ H 1 6.97 0.02 . 1 . . . . . . . . 4295 1 619 . 1 1 83 83 PHE N N 15 115.52 0.05 . 1 . . . . . . . . 4295 1 620 . 1 1 84 84 ARG H H 1 9.13 0.02 . 1 . . . . . . . . 4295 1 621 . 1 1 84 84 ARG HA H 1 4.44 0.02 . 1 . . . . . . . . 4295 1 622 . 1 1 84 84 ARG HB2 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 623 . 1 1 84 84 ARG HB3 H 1 1.71 0.02 . 1 . . . . . . . . 4295 1 624 . 1 1 84 84 ARG HG2 H 1 1.64 0.02 . 1 . . . . . . . . 4295 1 625 . 1 1 84 84 ARG HG3 H 1 1.64 0.02 . 1 . . . . . . . . 4295 1 626 . 1 1 84 84 ARG HD2 H 1 2.95 0.02 . 1 . . . . . . . . 4295 1 627 . 1 1 84 84 ARG HD3 H 1 2.95 0.02 . 1 . . . . . . . . 4295 1 628 . 1 1 84 84 ARG HE H 1 6.64 0.02 . 1 . . . . . . . . 4295 1 629 . 1 1 84 84 ARG N N 15 118.25 0.05 . 1 . . . . . . . . 4295 1 630 . 1 1 85 85 VAL H H 1 8.22 0.02 . 1 . . . . . . . . 4295 1 631 . 1 1 85 85 VAL HA H 1 4.83 0.02 . 1 . . . . . . . . 4295 1 632 . 1 1 85 85 VAL HB H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 633 . 1 1 85 85 VAL HG11 H 1 -0.19 0.02 . 2 . . . . . . . . 4295 1 634 . 1 1 85 85 VAL HG12 H 1 -0.19 0.02 . 2 . . . . . . . . 4295 1 635 . 1 1 85 85 VAL HG13 H 1 -0.19 0.02 . 2 . . . . . . . . 4295 1 636 . 1 1 85 85 VAL HG21 H 1 -0.42 0.02 . 2 . . . . . . . . 4295 1 637 . 1 1 85 85 VAL HG22 H 1 -0.42 0.02 . 2 . . . . . . . . 4295 1 638 . 1 1 85 85 VAL HG23 H 1 -0.42 0.02 . 2 . . . . . . . . 4295 1 639 . 1 1 85 85 VAL N N 15 119.70 0.05 . 1 . . . . . . . . 4295 1 640 . 1 1 86 86 ILE H H 1 8.91 0.02 . 1 . . . . . . . . 4295 1 641 . 1 1 86 86 ILE HA H 1 3.80 0.02 . 1 . . . . . . . . 4295 1 642 . 1 1 86 86 ILE HB H 1 1.32 0.02 . 1 . . . . . . . . 4295 1 643 . 1 1 86 86 ILE HG12 H 1 0.91 0.02 . 2 . . . . . . . . 4295 1 644 . 1 1 86 86 ILE HG13 H 1 0.63 0.02 . 2 . . . . . . . . 4295 1 645 . 1 1 86 86 ILE HG21 H 1 0.81 0.02 . 1 . . . . . . . . 4295 1 646 . 1 1 86 86 ILE HG22 H 1 0.81 0.02 . 1 . . . . . . . . 4295 1 647 . 1 1 86 86 ILE HG23 H 1 0.81 0.02 . 1 . . . . . . . . 4295 1 648 . 1 1 86 86 ILE HD11 H 1 0.52 0.02 . 1 . . . . . . . . 4295 1 649 . 1 1 86 86 ILE HD12 H 1 0.52 0.02 . 1 . . . . . . . . 4295 1 650 . 1 1 86 86 ILE HD13 H 1 0.52 0.02 . 1 . . . . . . . . 4295 1 651 . 1 1 86 86 ILE N N 15 128.71 0.05 . 1 . . . . . . . . 4295 1 652 . 1 1 87 87 ALA H H 1 8.71 0.02 . 1 . . . . . . . . 4295 1 653 . 1 1 87 87 ALA HA H 1 4.96 0.02 . 1 . . . . . . . . 4295 1 654 . 1 1 87 87 ALA HB1 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 655 . 1 1 87 87 ALA HB2 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 656 . 1 1 87 87 ALA HB3 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 657 . 1 1 87 87 ALA N N 15 129.03 0.05 . 1 . . . . . . . . 4295 1 658 . 1 1 88 88 LYS H H 1 8.24 0.02 . 1 . . . . . . . . 4295 1 659 . 1 1 88 88 LYS HA H 1 5.28 0.02 . 1 . . . . . . . . 4295 1 660 . 1 1 88 88 LYS HB2 H 1 1.63 0.02 . 2 . . . . . . . . 4295 1 661 . 1 1 88 88 LYS HB3 H 1 1.29 0.02 . 2 . . . . . . . . 4295 1 662 . 1 1 88 88 LYS HG2 H 1 1.39 0.02 . 2 . . . . . . . . 4295 1 663 . 1 1 88 88 LYS HG3 H 1 1.11 0.02 . 2 . . . . . . . . 4295 1 664 . 1 1 88 88 LYS HD2 H 1 1.39 0.02 . 1 . . . . . . . . 4295 1 665 . 1 1 88 88 LYS HD3 H 1 1.39 0.02 . 1 . . . . . . . . 4295 1 666 . 1 1 88 88 LYS HE2 H 1 2.72 0.02 . 2 . . . . . . . . 4295 1 667 . 1 1 88 88 LYS HE3 H 1 2.66 0.02 . 2 . . . . . . . . 4295 1 668 . 1 1 88 88 LYS N N 15 120.99 0.05 . 1 . . . . . . . . 4295 1 669 . 1 1 89 89 ASN H H 1 8.36 0.02 . 1 . . . . . . . . 4295 1 670 . 1 1 89 89 ASN HA H 1 5.52 0.02 . 1 . . . . . . . . 4295 1 671 . 1 1 89 89 ASN HB2 H 1 3.25 0.02 . 2 . . . . . . . . 4295 1 672 . 1 1 89 89 ASN HB3 H 1 2.39 0.02 . 2 . . . . . . . . 4295 1 673 . 1 1 89 89 ASN HD21 H 1 7.61 0.02 . 2 . . . . . . . . 4295 1 674 . 1 1 89 89 ASN HD22 H 1 7.75 0.02 . 2 . . . . . . . . 4295 1 675 . 1 1 89 89 ASN N N 15 121.47 0.05 . 1 . . . . . . . . 4295 1 676 . 1 1 89 89 ASN ND2 N 15 113.26 0.02 . 1 . . . . . . . . 4295 1 677 . 1 1 90 90 ALA H H 1 8.25 0.02 . 1 . . . . . . . . 4295 1 678 . 1 1 90 90 ALA HA H 1 4.01 0.02 . 1 . . . . . . . . 4295 1 679 . 1 1 90 90 ALA HB1 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 680 . 1 1 90 90 ALA HB2 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 681 . 1 1 90 90 ALA HB3 H 1 1.46 0.02 . 1 . . . . . . . . 4295 1 682 . 1 1 90 90 ALA N N 15 119.06 0.05 . 1 . . . . . . . . 4295 1 683 . 1 1 91 91 ALA H H 1 6.76 0.02 . 1 . . . . . . . . 4295 1 684 . 1 1 91 91 ALA HA H 1 3.98 0.02 . 1 . . . . . . . . 4295 1 685 . 1 1 91 91 ALA HB1 H 1 0.37 0.02 . 1 . . . . . . . . 4295 1 686 . 1 1 91 91 ALA HB2 H 1 0.37 0.02 . 1 . . . . . . . . 4295 1 687 . 1 1 91 91 ALA HB3 H 1 0.37 0.02 . 1 . . . . . . . . 4295 1 688 . 1 1 91 91 ALA N N 15 119.06 0.05 . 1 . . . . . . . . 4295 1 689 . 1 1 92 92 GLY H H 1 7.94 0.02 . 1 . . . . . . . . 4295 1 690 . 1 1 92 92 GLY HA2 H 1 4.14 0.02 . 1 . . . . . . . . 4295 1 691 . 1 1 92 92 GLY HA3 H 1 3.37 0.02 . 1 . . . . . . . . 4295 1 692 . 1 1 92 92 GLY N N 15 107.63 0.05 . 1 . . . . . . . . 4295 1 693 . 1 1 93 93 ALA H H 1 7.38 0.02 . 1 . . . . . . . . 4295 1 694 . 1 1 93 93 ALA HA H 1 4.22 0.02 . 1 . . . . . . . . 4295 1 695 . 1 1 93 93 ALA HB1 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 696 . 1 1 93 93 ALA HB2 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 697 . 1 1 93 93 ALA HB3 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 698 . 1 1 93 93 ALA N N 15 124.53 0.05 . 1 . . . . . . . . 4295 1 699 . 1 1 94 94 ILE H H 1 7.87 0.02 . 1 . . . . . . . . 4295 1 700 . 1 1 94 94 ILE HA H 1 4.85 0.02 . 1 . . . . . . . . 4295 1 701 . 1 1 94 94 ILE HB H 1 1.56 0.02 . 1 . . . . . . . . 4295 1 702 . 1 1 94 94 ILE HG12 H 1 1.43 0.02 . 2 . . . . . . . . 4295 1 703 . 1 1 94 94 ILE HG13 H 1 0.90 0.02 . 2 . . . . . . . . 4295 1 704 . 1 1 94 94 ILE HG21 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 705 . 1 1 94 94 ILE HG22 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 706 . 1 1 94 94 ILE HG23 H 1 0.80 0.02 . 1 . . . . . . . . 4295 1 707 . 1 1 94 94 ILE HD11 H 1 0.72 0.02 . 1 . . . . . . . . 4295 1 708 . 1 1 94 94 ILE HD12 H 1 0.72 0.02 . 1 . . . . . . . . 4295 1 709 . 1 1 94 94 ILE HD13 H 1 0.72 0.02 . 1 . . . . . . . . 4295 1 710 . 1 1 94 94 ILE N N 15 118.41 0.05 . 1 . . . . . . . . 4295 1 711 . 1 1 95 95 SER H H 1 9.13 0.02 . 1 . . . . . . . . 4295 1 712 . 1 1 95 95 SER HA H 1 4.50 0.02 . 1 . . . . . . . . 4295 1 713 . 1 1 95 95 SER HB2 H 1 4.20 0.02 . 2 . . . . . . . . 4295 1 714 . 1 1 95 95 SER HB3 H 1 3.47 0.02 . 2 . . . . . . . . 4295 1 715 . 1 1 95 95 SER HG H 1 5.21 0.02 . 1 . . . . . . . . 4295 1 716 . 1 1 95 95 SER N N 15 126.14 0.05 . 1 . . . . . . . . 4295 1 717 . 1 1 96 96 PRO HA H 1 4.79 0.02 . 1 . . . . . . . . 4295 1 718 . 1 1 96 96 PRO HB2 H 1 2.01 0.02 . 1 . . . . . . . . 4295 1 719 . 1 1 96 96 PRO HB3 H 1 2.01 0.02 . 1 . . . . . . . . 4295 1 720 . 1 1 96 96 PRO HG2 H 1 1.73 0.02 . 1 . . . . . . . . 4295 1 721 . 1 1 96 96 PRO HG3 H 1 1.73 0.02 . 1 . . . . . . . . 4295 1 722 . 1 1 96 96 PRO HD2 H 1 3.94 0.02 . 2 . . . . . . . . 4295 1 723 . 1 1 96 96 PRO HD3 H 1 3.41 0.02 . 2 . . . . . . . . 4295 1 724 . 1 1 97 97 PRO HA H 1 4.37 0.02 . 1 . . . . . . . . 4295 1 725 . 1 1 97 97 PRO HB2 H 1 2.45 0.02 . 2 . . . . . . . . 4295 1 726 . 1 1 97 97 PRO HB3 H 1 1.52 0.02 . 2 . . . . . . . . 4295 1 727 . 1 1 97 97 PRO HG2 H 1 1.76 0.02 . 2 . . . . . . . . 4295 1 728 . 1 1 97 97 PRO HG3 H 1 1.58 0.02 . 2 . . . . . . . . 4295 1 729 . 1 1 97 97 PRO HD2 H 1 3.67 0.02 . 2 . . . . . . . . 4295 1 730 . 1 1 97 97 PRO HD3 H 1 3.43 0.02 . 2 . . . . . . . . 4295 1 731 . 1 1 98 98 SER H H 1 8.70 0.02 . 1 . . . . . . . . 4295 1 732 . 1 1 98 98 SER HA H 1 4.13 0.02 . 1 . . . . . . . . 4295 1 733 . 1 1 98 98 SER HB2 H 1 4.00 0.02 . 2 . . . . . . . . 4295 1 734 . 1 1 98 98 SER HB3 H 1 3.47 0.02 . 2 . . . . . . . . 4295 1 735 . 1 1 98 98 SER N N 15 116.00 0.05 . 1 . . . . . . . . 4295 1 736 . 1 1 99 99 GLU H H 1 8.49 0.02 . 1 . . . . . . . . 4295 1 737 . 1 1 99 99 GLU HA H 1 4.41 0.02 . 1 . . . . . . . . 4295 1 738 . 1 1 99 99 GLU HB2 H 1 2.02 0.02 . 2 . . . . . . . . 4295 1 739 . 1 1 99 99 GLU HB3 H 1 1.88 0.02 . 2 . . . . . . . . 4295 1 740 . 1 1 99 99 GLU HG2 H 1 2.43 0.02 . 1 . . . . . . . . 4295 1 741 . 1 1 99 99 GLU HG3 H 1 2.43 0.02 . 1 . . . . . . . . 4295 1 742 . 1 1 99 99 GLU N N 15 121.79 0.05 . 1 . . . . . . . . 4295 1 743 . 1 1 100 100 PRO HA H 1 4.93 0.02 . 1 . . . . . . . . 4295 1 744 . 1 1 100 100 PRO HB2 H 1 2.27 0.02 . 1 . . . . . . . . 4295 1 745 . 1 1 100 100 PRO HB3 H 1 2.27 0.02 . 1 . . . . . . . . 4295 1 746 . 1 1 100 100 PRO HG2 H 1 2.01 0.02 . 1 . . . . . . . . 4295 1 747 . 1 1 100 100 PRO HG3 H 1 2.01 0.02 . 1 . . . . . . . . 4295 1 748 . 1 1 100 100 PRO HD2 H 1 3.86 0.02 . 2 . . . . . . . . 4295 1 749 . 1 1 100 100 PRO HD3 H 1 3.71 0.02 . 2 . . . . . . . . 4295 1 750 . 1 1 101 101 SER H H 1 9.50 0.02 . 1 . . . . . . . . 4295 1 751 . 1 1 101 101 SER HA H 1 4.32 0.02 . 1 . . . . . . . . 4295 1 752 . 1 1 101 101 SER HB2 H 1 4.60 0.02 . 2 . . . . . . . . 4295 1 753 . 1 1 101 101 SER HB3 H 1 3.99 0.02 . 2 . . . . . . . . 4295 1 754 . 1 1 101 101 SER HG H 1 5.26 0.02 . 1 . . . . . . . . 4295 1 755 . 1 1 101 101 SER N N 15 115.19 0.05 . 1 . . . . . . . . 4295 1 756 . 1 1 102 102 ASP H H 1 8.65 0.02 . 1 . . . . . . . . 4295 1 757 . 1 1 102 102 ASP HA H 1 4.64 0.02 . 1 . . . . . . . . 4295 1 758 . 1 1 102 102 ASP HB2 H 1 2.88 0.02 . 2 . . . . . . . . 4295 1 759 . 1 1 102 102 ASP HB3 H 1 2.46 0.02 . 2 . . . . . . . . 4295 1 760 . 1 1 102 102 ASP N N 15 119.70 0.05 . 1 . . . . . . . . 4295 1 761 . 1 1 103 103 ALA H H 1 8.37 0.02 . 1 . . . . . . . . 4295 1 762 . 1 1 103 103 ALA HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 763 . 1 1 103 103 ALA HB1 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 764 . 1 1 103 103 ALA HB2 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 765 . 1 1 103 103 ALA HB3 H 1 1.17 0.02 . 1 . . . . . . . . 4295 1 766 . 1 1 103 103 ALA N N 15 125.01 0.05 . 1 . . . . . . . . 4295 1 767 . 1 1 104 104 ILE H H 1 9.31 0.02 . 1 . . . . . . . . 4295 1 768 . 1 1 104 104 ILE HA H 1 4.35 0.02 . 1 . . . . . . . . 4295 1 769 . 1 1 104 104 ILE HB H 1 1.93 0.02 . 1 . . . . . . . . 4295 1 770 . 1 1 104 104 ILE HG21 H 1 1.24 0.02 . 1 . . . . . . . . 4295 1 771 . 1 1 104 104 ILE HG22 H 1 1.24 0.02 . 1 . . . . . . . . 4295 1 772 . 1 1 104 104 ILE HG23 H 1 1.24 0.02 . 1 . . . . . . . . 4295 1 773 . 1 1 104 104 ILE HD11 H 1 1.04 0.02 . 1 . . . . . . . . 4295 1 774 . 1 1 104 104 ILE HD12 H 1 1.04 0.02 . 1 . . . . . . . . 4295 1 775 . 1 1 104 104 ILE HD13 H 1 1.04 0.02 . 1 . . . . . . . . 4295 1 776 . 1 1 104 104 ILE N N 15 127.75 0.05 . 1 . . . . . . . . 4295 1 777 . 1 1 105 105 THR H H 1 8.29 0.02 . 1 . . . . . . . . 4295 1 778 . 1 1 105 105 THR HA H 1 5.11 0.02 . 1 . . . . . . . . 4295 1 779 . 1 1 105 105 THR HB H 1 3.79 0.02 . 1 . . . . . . . . 4295 1 780 . 1 1 105 105 THR HG21 H 1 0.91 0.02 . 1 . . . . . . . . 4295 1 781 . 1 1 105 105 THR HG22 H 1 0.91 0.02 . 1 . . . . . . . . 4295 1 782 . 1 1 105 105 THR HG23 H 1 0.91 0.02 . 1 . . . . . . . . 4295 1 783 . 1 1 105 105 THR N N 15 123.40 0.05 . 1 . . . . . . . . 4295 1 784 . 1 1 106 106 CYS H H 1 8.30 0.02 . 1 . . . . . . . . 4295 1 785 . 1 1 106 106 CYS HA H 1 4.00 0.02 . 1 . . . . . . . . 4295 1 786 . 1 1 106 106 CYS HB2 H 1 3.26 0.02 . 2 . . . . . . . . 4295 1 787 . 1 1 106 106 CYS HB3 H 1 2.77 0.02 . 2 . . . . . . . . 4295 1 788 . 1 1 106 106 CYS N N 15 127.43 0.05 . 1 . . . . . . . . 4295 1 789 . 1 1 107 107 ARG H H 1 6.93 0.02 . 1 . . . . . . . . 4295 1 790 . 1 1 107 107 ARG HA H 1 4.36 0.02 . 1 . . . . . . . . 4295 1 791 . 1 1 107 107 ARG HB2 H 1 1.96 0.02 . 2 . . . . . . . . 4295 1 792 . 1 1 107 107 ARG HB3 H 1 1.62 0.02 . 2 . . . . . . . . 4295 1 793 . 1 1 107 107 ARG HG2 H 1 1.54 0.02 . 2 . . . . . . . . 4295 1 794 . 1 1 107 107 ARG HG3 H 1 1.34 0.02 . 2 . . . . . . . . 4295 1 795 . 1 1 107 107 ARG HD2 H 1 3.08 0.02 . 1 . . . . . . . . 4295 1 796 . 1 1 107 107 ARG HD3 H 1 3.08 0.02 . 1 . . . . . . . . 4295 1 797 . 1 1 107 107 ARG HE H 1 7.36 0.02 . 1 . . . . . . . . 4295 1 798 . 1 1 107 107 ARG N N 15 123.88 0.05 . 1 . . . . . . . . 4295 1 799 . 1 1 107 107 ARG NE N 15 108.11 0.02 . 1 . . . . . . . . 4295 1 800 . 1 1 108 108 ASP H H 1 8.55 0.02 . 1 . . . . . . . . 4295 1 801 . 1 1 108 108 ASP HA H 1 4.77 0.02 . 1 . . . . . . . . 4295 1 802 . 1 1 108 108 ASP HB2 H 1 2.72 0.02 . 2 . . . . . . . . 4295 1 803 . 1 1 108 108 ASP HB3 H 1 2.63 0.02 . 2 . . . . . . . . 4295 1 804 . 1 1 108 108 ASP N N 15 120.83 0.05 . 1 . . . . . . . . 4295 1 805 . 1 1 109 109 ASP H H 1 8.41 0.02 . 1 . . . . . . . . 4295 1 806 . 1 1 109 109 ASP HA H 1 4.60 0.02 . 1 . . . . . . . . 4295 1 807 . 1 1 109 109 ASP HB2 H 1 2.69 0.02 . 2 . . . . . . . . 4295 1 808 . 1 1 109 109 ASP HB3 H 1 2.51 0.02 . 2 . . . . . . . . 4295 1 809 . 1 1 109 109 ASP N N 15 122.28 0.05 . 1 . . . . . . . . 4295 1 810 . 1 1 110 110 VAL H H 1 7.92 0.02 . 1 . . . . . . . . 4295 1 811 . 1 1 110 110 VAL HA H 1 4.10 0.02 . 1 . . . . . . . . 4295 1 812 . 1 1 110 110 VAL HB H 1 2.07 0.02 . 1 . . . . . . . . 4295 1 813 . 1 1 110 110 VAL HG11 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 814 . 1 1 110 110 VAL HG12 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 815 . 1 1 110 110 VAL HG13 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 816 . 1 1 110 110 VAL HG21 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 817 . 1 1 110 110 VAL HG22 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 818 . 1 1 110 110 VAL HG23 H 1 0.88 0.02 . 1 . . . . . . . . 4295 1 819 . 1 1 110 110 VAL N N 15 120.51 0.05 . 1 . . . . . . . . 4295 1 820 . 1 1 111 111 GLU H H 1 8.28 0.02 . 1 . . . . . . . . 4295 1 821 . 1 1 111 111 GLU HA H 1 4.28 0.02 . 1 . . . . . . . . 4295 1 822 . 1 1 111 111 GLU HB2 H 1 2.06 0.02 . 2 . . . . . . . . 4295 1 823 . 1 1 111 111 GLU HB3 H 1 1.89 0.02 . 2 . . . . . . . . 4295 1 824 . 1 1 111 111 GLU HG2 H 1 2.26 0.02 . 1 . . . . . . . . 4295 1 825 . 1 1 111 111 GLU HG3 H 1 2.26 0.02 . 1 . . . . . . . . 4295 1 826 . 1 1 111 111 GLU N N 15 125.66 0.05 . 1 . . . . . . . . 4295 1 827 . 1 1 112 112 ALA H H 1 7.80 0.02 . 1 . . . . . . . . 4295 1 828 . 1 1 112 112 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . 4295 1 829 . 1 1 112 112 ALA HB1 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 830 . 1 1 112 112 ALA HB2 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 831 . 1 1 112 112 ALA HB3 H 1 1.28 0.02 . 1 . . . . . . . . 4295 1 832 . 1 1 112 112 ALA N N 15 131.93 0.05 . 1 . . . . . . . . 4295 1 stop_ save_