data_11032 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11032 _Entry.Title ; Solution structure of the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-03-01 _Entry.Accession_date 2008-03-02 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.100 _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 Hideaki Shimojo N. . . 11032 2 Norihiko Sano . . . 11032 3 Yoshihito Moriwaki . . . 11032 4 Masahiko Okuda . . . 11032 5 Masami Horikoshi . . . 11032 6 Yoshifumi Nishimura . . . 11032 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID chromodomain . 11032 Esa1 . 11032 HAT . 11032 'RNA binding' . 11032 'tudor domain' . 11032 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 11032 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 431 11032 '15N chemical shifts' 96 11032 '1H chemical shifts' 676 11032 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2008-07-07 2008-03-01 update BMRB 'complete entry citation' 11032 1 . . 2008-04-16 2008-03-01 original author 'original release' 11032 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 11033 'the presumed chromodomain of the yeast histone acetyl transferase protein, Esa1' 11032 EMBL CAA99465.1 'hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).' 11032 EMBL Z75152 'S.cerevisiae chromosome XV reading frame ORF YOR244w.' 11032 'NCBI Protein' NP_014887.1 ; Histone acetyltransferase catalytic subunit of the native multisubunit complex (NuA4), Esa1p [Saccharomyces cerevisiae] ; 11032 'Protein Information Resource' S67137 'hypothetical protein YOR244w - yeast (Saccharomyces cerevisiae).' 11032 'Saccharomyces Genome Database' S000005770 ESA1/YOR244W 11032 Swiss-Prot Q08649 'Histone acetyltransferase ESA1' 11032 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 11032 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18407291 _Citation.Full_citation . _Citation.Title ; Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 378 _Citation.Journal_issue 5 _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 987 _Citation.Page_last 1001 _Citation.Year 2008 _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 Hideaki Shimojo N. . . 11032 1 2 Norihiko Sano . . . 11032 1 3 Yoshihito Moriwaki . . . 11032 1 4 Masahiko Okuda . . . 11032 1 5 Masami Horikoshi . . . 11032 1 6 Yoshifumi Nishimura . . . 11032 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11032 _Assembly.ID 1 _Assembly.Name 'the knotted tudor domain' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'Residues 1-89' 1 $entity A . yes native no no . . . 11032 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 11032 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Residues 1-89' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSHMSHDGKEEPGIAKKINS VDDIIIKCQCWVQKNDEERL AEILSINTRKAPPKFYVHYV NYNKRLDEWITTDRINLDKE VLYPKLKATDED ; _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 92 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'Residues 1-89' _Entity.Mutation 'Histag -2 - 0' _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 10791.321 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 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 BMRB 11033 . "Residues 17-89" . . . . . 79.35 94 100.00 100.00 3.48e-45 . . . . 11032 1 2 no PDB 2RNZ . "Solution Structure Of The Presumed Chromodomain Of The Yeast Histone Acetyltransferase, Esa1" . . . . . 79.35 94 100.00 100.00 3.48e-45 . . . . 11032 1 3 no PDB 2RO0 . "Solution Structure Of The Knotted Tudor Domain Of The Yeast Histone Acetyltransferase, Esa1" . . . . . 100.00 92 100.00 100.00 2.64e-60 . . . . 11032 1 4 no DBJ GAA26555 . "K7_Esa1p [Saccharomyces cerevisiae Kyokai no. 7]" . . . . . 96.74 445 98.88 98.88 1.02e-52 . . . . 11032 1 5 no EMBL CAA99465 . "unnamed protein product [Saccharomyces cerevisiae]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 6 no EMBL CAY86525 . "Esa1p [Saccharomyces cerevisiae EC1118]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 7 no GB AHY77525 . "Esa1p [Saccharomyces cerevisiae YJM993]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 8 no GB AJP41755 . "Esa1p [Saccharomyces cerevisiae YJM1078]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 9 no GB AJT71177 . "Esa1p [Saccharomyces cerevisiae YJM189]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 10 no GB AJT71665 . "Esa1p [Saccharomyces cerevisiae YJM193]" . . . . . 96.74 445 100.00 100.00 4.06e-54 . . . . 11032 1 11 no GB AJT72155 . "Esa1p [Saccharomyces cerevisiae YJM195]" . . . . . 96.74 445 98.88 98.88 1.04e-52 . . . . 11032 1 12 no REF NP_014887 . "NuA4 histone acetyltransferase complex catalytic subunit ESA1 [Saccharomyces cerevisiae S288c]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 13 no SP Q08649 . "RecName: Full=Histone acetyltransferase ESA1" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 1 14 no TPG DAA11012 . "TPA: NuA4 histone acetyltransferase complex catalytic subunit ESA1 [Saccharomyces cerevisiae S288c]" . . . . . 96.74 445 100.00 100.00 4.23e-54 . . . . 11032 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 -2 GLY . 11032 1 2 -1 SER . 11032 1 3 0 HIS . 11032 1 4 1 MET . 11032 1 5 2 SER . 11032 1 6 3 HIS . 11032 1 7 4 ASP . 11032 1 8 5 GLY . 11032 1 9 6 LYS . 11032 1 10 7 GLU . 11032 1 11 8 GLU . 11032 1 12 9 PRO . 11032 1 13 10 GLY . 11032 1 14 11 ILE . 11032 1 15 12 ALA . 11032 1 16 13 LYS . 11032 1 17 14 LYS . 11032 1 18 15 ILE . 11032 1 19 16 ASN . 11032 1 20 17 SER . 11032 1 21 18 VAL . 11032 1 22 19 ASP . 11032 1 23 20 ASP . 11032 1 24 21 ILE . 11032 1 25 22 ILE . 11032 1 26 23 ILE . 11032 1 27 24 LYS . 11032 1 28 25 CYS . 11032 1 29 26 GLN . 11032 1 30 27 CYS . 11032 1 31 28 TRP . 11032 1 32 29 VAL . 11032 1 33 30 GLN . 11032 1 34 31 LYS . 11032 1 35 32 ASN . 11032 1 36 33 ASP . 11032 1 37 34 GLU . 11032 1 38 35 GLU . 11032 1 39 36 ARG . 11032 1 40 37 LEU . 11032 1 41 38 ALA . 11032 1 42 39 GLU . 11032 1 43 40 ILE . 11032 1 44 41 LEU . 11032 1 45 42 SER . 11032 1 46 43 ILE . 11032 1 47 44 ASN . 11032 1 48 45 THR . 11032 1 49 46 ARG . 11032 1 50 47 LYS . 11032 1 51 48 ALA . 11032 1 52 49 PRO . 11032 1 53 50 PRO . 11032 1 54 51 LYS . 11032 1 55 52 PHE . 11032 1 56 53 TYR . 11032 1 57 54 VAL . 11032 1 58 55 HIS . 11032 1 59 56 TYR . 11032 1 60 57 VAL . 11032 1 61 58 ASN . 11032 1 62 59 TYR . 11032 1 63 60 ASN . 11032 1 64 61 LYS . 11032 1 65 62 ARG . 11032 1 66 63 LEU . 11032 1 67 64 ASP . 11032 1 68 65 GLU . 11032 1 69 66 TRP . 11032 1 70 67 ILE . 11032 1 71 68 THR . 11032 1 72 69 THR . 11032 1 73 70 ASP . 11032 1 74 71 ARG . 11032 1 75 72 ILE . 11032 1 76 73 ASN . 11032 1 77 74 LEU . 11032 1 78 75 ASP . 11032 1 79 76 LYS . 11032 1 80 77 GLU . 11032 1 81 78 VAL . 11032 1 82 79 LEU . 11032 1 83 80 TYR . 11032 1 84 81 PRO . 11032 1 85 82 LYS . 11032 1 86 83 LEU . 11032 1 87 84 LYS . 11032 1 88 85 ALA . 11032 1 89 86 THR . 11032 1 90 87 ASP . 11032 1 91 88 GLU . 11032 1 92 89 ASP . 11032 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 . GLY 1 1 11032 1 . SER 2 2 11032 1 . HIS 3 3 11032 1 . MET 4 4 11032 1 . SER 5 5 11032 1 . HIS 6 6 11032 1 . ASP 7 7 11032 1 . GLY 8 8 11032 1 . LYS 9 9 11032 1 . GLU 10 10 11032 1 . GLU 11 11 11032 1 . PRO 12 12 11032 1 . GLY 13 13 11032 1 . ILE 14 14 11032 1 . ALA 15 15 11032 1 . LYS 16 16 11032 1 . LYS 17 17 11032 1 . ILE 18 18 11032 1 . ASN 19 19 11032 1 . SER 20 20 11032 1 . VAL 21 21 11032 1 . ASP 22 22 11032 1 . ASP 23 23 11032 1 . ILE 24 24 11032 1 . ILE 25 25 11032 1 . ILE 26 26 11032 1 . LYS 27 27 11032 1 . CYS 28 28 11032 1 . GLN 29 29 11032 1 . CYS 30 30 11032 1 . TRP 31 31 11032 1 . VAL 32 32 11032 1 . GLN 33 33 11032 1 . LYS 34 34 11032 1 . ASN 35 35 11032 1 . ASP 36 36 11032 1 . GLU 37 37 11032 1 . GLU 38 38 11032 1 . ARG 39 39 11032 1 . LEU 40 40 11032 1 . ALA 41 41 11032 1 . GLU 42 42 11032 1 . ILE 43 43 11032 1 . LEU 44 44 11032 1 . SER 45 45 11032 1 . ILE 46 46 11032 1 . ASN 47 47 11032 1 . THR 48 48 11032 1 . ARG 49 49 11032 1 . LYS 50 50 11032 1 . ALA 51 51 11032 1 . PRO 52 52 11032 1 . PRO 53 53 11032 1 . LYS 54 54 11032 1 . PHE 55 55 11032 1 . TYR 56 56 11032 1 . VAL 57 57 11032 1 . HIS 58 58 11032 1 . TYR 59 59 11032 1 . VAL 60 60 11032 1 . ASN 61 61 11032 1 . TYR 62 62 11032 1 . ASN 63 63 11032 1 . LYS 64 64 11032 1 . ARG 65 65 11032 1 . LEU 66 66 11032 1 . ASP 67 67 11032 1 . GLU 68 68 11032 1 . TRP 69 69 11032 1 . ILE 70 70 11032 1 . THR 71 71 11032 1 . THR 72 72 11032 1 . ASP 73 73 11032 1 . ARG 74 74 11032 1 . ILE 75 75 11032 1 . ASN 76 76 11032 1 . LEU 77 77 11032 1 . ASP 78 78 11032 1 . LYS 79 79 11032 1 . GLU 80 80 11032 1 . VAL 81 81 11032 1 . LEU 82 82 11032 1 . TYR 83 83 11032 1 . PRO 84 84 11032 1 . LYS 85 85 11032 1 . LEU 86 86 11032 1 . LYS 87 87 11032 1 . ALA 88 88 11032 1 . THR 89 89 11032 1 . ASP 90 90 11032 1 . GLU 91 91 11032 1 . ASP 92 92 11032 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 11032 _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 $entity . 4932 organism . 'Saccharomyces cerevisiae' 'baker's yeast' . . Eukaryota Fungi Saccharomyces cerevisiae . . . . . . . . . . . . . . . . . . . . . 11032 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 11032 _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 $entity . 'recombinant technology' 'Escherichia coli' . . 562 Escherichia coli . . . . . . . . . . . . . . . . pET . . . . . . 11032 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11032 _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 'Residues 1-89' '[U-99% 13C; U-99% 15N]' . . 1 $entity . . 0.35 . . mM . . . . 11032 1 2 'potassium phosphate' . . . . . . . 200 . . mM . . . . 11032 1 3 H2O . . . . . . . 95 . . % . . . . 11032 1 4 D2O . . . . . . . 5 . . % . . . . 11032 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 11032 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% 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 'Residues 1-89' 'natural abundance' . . 1 $entity . . 0.35 . . mM . . . . 11032 2 2 'potassium phosphate' . . . . . . . 200 . . mM . . . . 11032 2 3 D2O . . . . . . . 100 . . % . . . . 11032 2 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 11032 _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 6.8 . pH 11032 1 pressure 1 . atm 11032 1 temperature 295 . K 11032 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 11032 _Software.ID 1 _Software.Name CYANA _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'P.GUNTERT ET AL.' . . 11032 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 11032 1 stop_ save_ save_Olivia _Software.Sf_category software _Software.Sf_framecode Olivia _Software.Entry_ID 11032 _Software.ID 2 _Software.Name Olivia _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Yokochi, M., Sekiguchi, S. and Inagaki, F.' . . 11032 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 11032 2 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 11032 _Software.ID 3 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 11032 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11032 3 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 11032 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 11032 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 11032 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 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 11032 _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 DRX . 600 . . . 11032 1 2 spectrometer_2 Bruker DRX . 800 . . . 11032 1 3 spectrometer_3 Varian INOVA . 900 . . . 11032 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 11032 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 3 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 5 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 6 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11032 1 7 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 11032 1 8 '3D HCCH-TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 11032 1 9 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 11032 1 10 '3D 1H-13C NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 11032 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 11032 _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 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . . . . . . . 11032 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 11032 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 11032 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 11032 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' 1 $sample_1 isotropic 11032 1 2 '3D CBCA(CO)NH' 1 $sample_1 isotropic 11032 1 3 '3D HNCACB' 1 $sample_1 isotropic 11032 1 4 '3D HNCO' 1 $sample_1 isotropic 11032 1 5 '3D HNCA' 1 $sample_1 isotropic 11032 1 6 '3D HN(CO)CA' 1 $sample_1 isotropic 11032 1 7 '2D 1H-13C HSQC' 2 $sample_2 isotropic 11032 1 8 '3D HCCH-TOCSY' 2 $sample_2 isotropic 11032 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 GLY CA C 13 43.259 0.450 . 1 . . . . -2 GLY CA . 11032 1 2 . 1 1 1 1 GLY HA2 H 1 3.881 0.040 . 2 . . . . -2 GLY HA2 . 11032 1 3 . 1 1 1 1 GLY HA3 H 1 3.881 0.040 . 2 . . . . -2 GLY HA3 . 11032 1 4 . 1 1 2 2 SER CA C 13 58.275 0.450 . 1 . . . . -1 SER CA . 11032 1 5 . 1 1 2 2 SER HA H 1 4.483 0.040 . 1 . . . . -1 SER HA . 11032 1 6 . 1 1 2 2 SER CB C 13 63.784 0.450 . 1 . . . . -1 SER CB . 11032 1 7 . 1 1 2 2 SER HB2 H 1 3.815 0.040 . 2 . . . . -1 SER HB2 . 11032 1 8 . 1 1 2 2 SER HB3 H 1 3.815 0.040 . 2 . . . . -1 SER HB3 . 11032 1 9 . 1 1 2 2 SER C C 13 174.510 0.450 . 1 . . . . -1 SER C . 11032 1 10 . 1 1 3 3 HIS N N 15 121.400 0.450 . 1 . . . . 0 HIS N . 11032 1 11 . 1 1 3 3 HIS H H 1 8.745 0.040 . 1 . . . . 0 HIS H . 11032 1 12 . 1 1 3 3 HIS CA C 13 55.942 0.450 . 1 . . . . 0 HIS CA . 11032 1 13 . 1 1 3 3 HIS HA H 1 4.689 0.040 . 1 . . . . 0 HIS HA . 11032 1 14 . 1 1 3 3 HIS CB C 13 29.722 0.450 . 1 . . . . 0 HIS CB . 11032 1 15 . 1 1 3 3 HIS HB2 H 1 3.229 0.040 . 2 . . . . 0 HIS HB2 . 11032 1 16 . 1 1 3 3 HIS HB3 H 1 3.134 0.040 . 2 . . . . 0 HIS HB3 . 11032 1 17 . 1 1 3 3 HIS CD2 C 13 119.996 0.450 . 1 . . . . 0 HIS CD2 . 11032 1 18 . 1 1 3 3 HIS CE1 C 13 137.309 0.450 . 1 . . . . 0 HIS CE1 . 11032 1 19 . 1 1 3 3 HIS HD2 H 1 7.134 0.040 . 1 . . . . 0 HIS HD2 . 11032 1 20 . 1 1 3 3 HIS HE1 H 1 8.207 0.040 . 1 . . . . 0 HIS HE1 . 11032 1 21 . 1 1 3 3 HIS C C 13 174.774 0.450 . 1 . . . . 0 HIS C . 11032 1 22 . 1 1 4 4 MET N N 15 121.990 0.450 . 1 . . . . 1 MET N . 11032 1 23 . 1 1 4 4 MET H H 1 8.526 0.040 . 1 . . . . 1 MET H . 11032 1 24 . 1 1 4 4 MET CA C 13 55.263 0.450 . 1 . . . . 1 MET CA . 11032 1 25 . 1 1 4 4 MET HA H 1 4.482 0.040 . 1 . . . . 1 MET HA . 11032 1 26 . 1 1 4 4 MET CB C 13 32.966 0.450 . 1 . . . . 1 MET CB . 11032 1 27 . 1 1 4 4 MET HB2 H 1 2.009 0.040 . 2 . . . . 1 MET HB2 . 11032 1 28 . 1 1 4 4 MET HB3 H 1 1.939 0.040 . 2 . . . . 1 MET HB3 . 11032 1 29 . 1 1 4 4 MET CG C 13 31.826 0.450 . 1 . . . . 1 MET CG . 11032 1 30 . 1 1 4 4 MET HG2 H 1 2.488 0.040 . 2 . . . . 1 MET HG2 . 11032 1 31 . 1 1 4 4 MET HG3 H 1 2.449 0.040 . 2 . . . . 1 MET HG3 . 11032 1 32 . 1 1 4 4 MET HE1 H 1 2.060 0.040 . 1 . . . . 1 MET HE . 11032 1 33 . 1 1 4 4 MET HE2 H 1 2.060 0.040 . 1 . . . . 1 MET HE . 11032 1 34 . 1 1 4 4 MET HE3 H 1 2.060 0.040 . 1 . . . . 1 MET HE . 11032 1 35 . 1 1 4 4 MET CE C 13 16.893 0.450 . 1 . . . . 1 MET CE . 11032 1 36 . 1 1 4 4 MET C C 13 176.077 0.450 . 1 . . . . 1 MET C . 11032 1 37 . 1 1 5 5 SER N N 15 117.420 0.450 . 1 . . . . 2 SER N . 11032 1 38 . 1 1 5 5 SER H H 1 8.461 0.040 . 1 . . . . 2 SER H . 11032 1 39 . 1 1 5 5 SER CA C 13 58.084 0.450 . 1 . . . . 2 SER CA . 11032 1 40 . 1 1 5 5 SER HA H 1 4.435 0.040 . 1 . . . . 2 SER HA . 11032 1 41 . 1 1 5 5 SER CB C 13 63.694 0.450 . 1 . . . . 2 SER CB . 11032 1 42 . 1 1 5 5 SER HB2 H 1 3.855 0.040 . 2 . . . . 2 SER HB2 . 11032 1 43 . 1 1 5 5 SER HB3 H 1 3.855 0.040 . 2 . . . . 2 SER HB3 . 11032 1 44 . 1 1 5 5 SER C C 13 174.549 0.450 . 1 . . . . 2 SER C . 11032 1 45 . 1 1 6 6 HIS N N 15 121.469 0.450 . 1 . . . . 3 HIS N . 11032 1 46 . 1 1 6 6 HIS H H 1 8.648 0.040 . 1 . . . . 3 HIS H . 11032 1 47 . 1 1 6 6 HIS CA C 13 56.064 0.450 . 1 . . . . 3 HIS CA . 11032 1 48 . 1 1 6 6 HIS HA H 1 4.678 0.040 . 1 . . . . 3 HIS HA . 11032 1 49 . 1 1 6 6 HIS CB C 13 29.922 0.450 . 1 . . . . 3 HIS CB . 11032 1 50 . 1 1 6 6 HIS HB2 H 1 3.210 0.040 . 2 . . . . 3 HIS HB2 . 11032 1 51 . 1 1 6 6 HIS HB3 H 1 3.121 0.040 . 2 . . . . 3 HIS HB3 . 11032 1 52 . 1 1 6 6 HIS CD2 C 13 119.996 0.450 . 1 . . . . 3 HIS CD2 . 11032 1 53 . 1 1 6 6 HIS CE1 C 13 137.309 0.450 . 1 . . . . 3 HIS CE1 . 11032 1 54 . 1 1 6 6 HIS HD2 H 1 7.134 0.040 . 1 . . . . 3 HIS HD2 . 11032 1 55 . 1 1 6 6 HIS HE1 H 1 8.207 0.040 . 1 . . . . 3 HIS HE1 . 11032 1 56 . 1 1 6 6 HIS C C 13 174.769 0.450 . 1 . . . . 3 HIS C . 11032 1 57 . 1 1 7 7 ASP N N 15 121.215 0.450 . 1 . . . . 4 ASP N . 11032 1 58 . 1 1 7 7 ASP H H 1 8.393 0.040 . 1 . . . . 4 ASP H . 11032 1 59 . 1 1 7 7 ASP CA C 13 54.361 0.450 . 1 . . . . 4 ASP CA . 11032 1 60 . 1 1 7 7 ASP HA H 1 4.575 0.040 . 1 . . . . 4 ASP HA . 11032 1 61 . 1 1 7 7 ASP CB C 13 41.020 0.450 . 1 . . . . 4 ASP CB . 11032 1 62 . 1 1 7 7 ASP HB2 H 1 2.656 0.040 . 2 . . . . 4 ASP HB2 . 11032 1 63 . 1 1 7 7 ASP HB3 H 1 2.656 0.040 . 2 . . . . 4 ASP HB3 . 11032 1 64 . 1 1 7 7 ASP C C 13 176.737 0.450 . 1 . . . . 4 ASP C . 11032 1 65 . 1 1 8 8 GLY N N 15 109.480 0.450 . 1 . . . . 5 GLY N . 11032 1 66 . 1 1 8 8 GLY H H 1 8.425 0.040 . 1 . . . . 5 GLY H . 11032 1 67 . 1 1 8 8 GLY CA C 13 45.446 0.450 . 1 . . . . 5 GLY CA . 11032 1 68 . 1 1 8 8 GLY HA2 H 1 3.971 0.040 . 2 . . . . 5 GLY HA2 . 11032 1 69 . 1 1 8 8 GLY HA3 H 1 3.910 0.040 . 2 . . . . 5 GLY HA3 . 11032 1 70 . 1 1 8 8 GLY C C 13 174.320 0.450 . 1 . . . . 5 GLY C . 11032 1 71 . 1 1 9 9 LYS N N 15 120.718 0.450 . 1 . . . . 6 LYS N . 11032 1 72 . 1 1 9 9 LYS H H 1 8.131 0.040 . 1 . . . . 6 LYS H . 11032 1 73 . 1 1 9 9 LYS CA C 13 55.908 0.450 . 1 . . . . 6 LYS CA . 11032 1 74 . 1 1 9 9 LYS HA H 1 4.331 0.040 . 1 . . . . 6 LYS HA . 11032 1 75 . 1 1 9 9 LYS CB C 13 33.217 0.450 . 1 . . . . 6 LYS CB . 11032 1 76 . 1 1 9 9 LYS HB2 H 1 1.831 0.040 . 2 . . . . 6 LYS HB2 . 11032 1 77 . 1 1 9 9 LYS HB3 H 1 1.741 0.040 . 2 . . . . 6 LYS HB3 . 11032 1 78 . 1 1 9 9 LYS CG C 13 24.688 0.450 . 1 . . . . 6 LYS CG . 11032 1 79 . 1 1 9 9 LYS HG2 H 1 1.419 0.040 . 2 . . . . 6 LYS HG2 . 11032 1 80 . 1 1 9 9 LYS HG3 H 1 1.378 0.040 . 2 . . . . 6 LYS HG3 . 11032 1 81 . 1 1 9 9 LYS CD C 13 28.970 0.450 . 1 . . . . 6 LYS CD . 11032 1 82 . 1 1 9 9 LYS HD2 H 1 1.677 0.040 . 2 . . . . 6 LYS HD2 . 11032 1 83 . 1 1 9 9 LYS HD3 H 1 1.677 0.040 . 2 . . . . 6 LYS HD3 . 11032 1 84 . 1 1 9 9 LYS CE C 13 41.826 0.450 . 1 . . . . 6 LYS CE . 11032 1 85 . 1 1 9 9 LYS HE2 H 1 2.976 0.040 . 2 . . . . 6 LYS HE2 . 11032 1 86 . 1 1 9 9 LYS HE3 H 1 2.976 0.040 . 2 . . . . 6 LYS HE3 . 11032 1 87 . 1 1 9 9 LYS C C 13 176.516 0.450 . 1 . . . . 6 LYS C . 11032 1 88 . 1 1 10 10 GLU N N 15 122.236 0.450 . 1 . . . . 7 GLU N . 11032 1 89 . 1 1 10 10 GLU H H 1 8.511 0.040 . 1 . . . . 7 GLU H . 11032 1 90 . 1 1 10 10 GLU CA C 13 56.101 0.450 . 1 . . . . 7 GLU CA . 11032 1 91 . 1 1 10 10 GLU HA H 1 4.330 0.040 . 1 . . . . 7 GLU HA . 11032 1 92 . 1 1 10 10 GLU CB C 13 30.440 0.450 . 1 . . . . 7 GLU CB . 11032 1 93 . 1 1 10 10 GLU HB2 H 1 2.000 0.040 . 2 . . . . 7 GLU HB2 . 11032 1 94 . 1 1 10 10 GLU HB3 H 1 1.895 0.040 . 2 . . . . 7 GLU HB3 . 11032 1 95 . 1 1 10 10 GLU CG C 13 36.342 0.450 . 1 . . . . 7 GLU CG . 11032 1 96 . 1 1 10 10 GLU HG2 H 1 2.247 0.040 . 2 . . . . 7 GLU HG2 . 11032 1 97 . 1 1 10 10 GLU HG3 H 1 2.247 0.040 . 2 . . . . 7 GLU HG3 . 11032 1 98 . 1 1 10 10 GLU C C 13 176.293 0.450 . 1 . . . . 7 GLU C . 11032 1 99 . 1 1 11 11 GLU N N 15 124.205 0.450 . 1 . . . . 8 GLU N . 11032 1 100 . 1 1 11 11 GLU H H 1 8.556 0.040 . 1 . . . . 8 GLU H . 11032 1 101 . 1 1 11 11 GLU CA C 13 54.065 0.450 . 1 . . . . 8 GLU CA . 11032 1 102 . 1 1 11 11 GLU HA H 1 4.613 0.040 . 1 . . . . 8 GLU HA . 11032 1 103 . 1 1 11 11 GLU CB C 13 30.061 0.450 . 1 . . . . 8 GLU CB . 11032 1 104 . 1 1 11 11 GLU HB2 H 1 2.056 0.040 . 2 . . . . 8 GLU HB2 . 11032 1 105 . 1 1 11 11 GLU HB3 H 1 1.890 0.040 . 2 . . . . 8 GLU HB3 . 11032 1 106 . 1 1 11 11 GLU CG C 13 36.020 0.450 . 1 . . . . 8 GLU CG . 11032 1 107 . 1 1 11 11 GLU HG2 H 1 2.288 0.040 . 2 . . . . 8 GLU HG2 . 11032 1 108 . 1 1 11 11 GLU HG3 H 1 2.288 0.040 . 2 . . . . 8 GLU HG3 . 11032 1 109 . 1 1 12 12 PRO CD C 13 50.638 0.450 . 1 . . . . 9 PRO CD . 11032 1 110 . 1 1 12 12 PRO CA C 13 63.186 0.450 . 1 . . . . 9 PRO CA . 11032 1 111 . 1 1 12 12 PRO HA H 1 4.464 0.040 . 1 . . . . 9 PRO HA . 11032 1 112 . 1 1 12 12 PRO CB C 13 32.172 0.450 . 1 . . . . 9 PRO CB . 11032 1 113 . 1 1 12 12 PRO HB2 H 1 1.996 0.040 . 2 . . . . 9 PRO HB2 . 11032 1 114 . 1 1 12 12 PRO HB3 H 1 2.270 0.040 . 2 . . . . 9 PRO HB3 . 11032 1 115 . 1 1 12 12 PRO CG C 13 27.281 0.450 . 1 . . . . 9 PRO CG . 11032 1 116 . 1 1 12 12 PRO HG2 H 1 2.018 0.040 . 2 . . . . 9 PRO HG2 . 11032 1 117 . 1 1 12 12 PRO HG3 H 1 2.018 0.040 . 2 . . . . 9 PRO HG3 . 11032 1 118 . 1 1 12 12 PRO HD2 H 1 3.791 0.040 . 2 . . . . 9 PRO HD2 . 11032 1 119 . 1 1 12 12 PRO HD3 H 1 3.744 0.040 . 2 . . . . 9 PRO HD3 . 11032 1 120 . 1 1 12 12 PRO C C 13 177.176 0.450 . 1 . . . . 9 PRO C . 11032 1 121 . 1 1 13 13 GLY N N 15 108.077 0.450 . 1 . . . . 10 GLY N . 11032 1 122 . 1 1 13 13 GLY H H 1 8.225 0.040 . 1 . . . . 10 GLY H . 11032 1 123 . 1 1 13 13 GLY CA C 13 44.612 0.450 . 1 . . . . 10 GLY CA . 11032 1 124 . 1 1 13 13 GLY HA2 H 1 3.802 0.040 . 2 . . . . 10 GLY HA2 . 11032 1 125 . 1 1 13 13 GLY HA3 H 1 4.161 0.040 . 2 . . . . 10 GLY HA3 . 11032 1 126 . 1 1 13 13 GLY C C 13 173.003 0.450 . 1 . . . . 10 GLY C . 11032 1 127 . 1 1 14 14 ILE N N 15 120.575 0.450 . 1 . . . . 11 ILE N . 11032 1 128 . 1 1 14 14 ILE H H 1 8.513 0.040 . 1 . . . . 11 ILE H . 11032 1 129 . 1 1 14 14 ILE CA C 13 60.002 0.450 . 1 . . . . 11 ILE CA . 11032 1 130 . 1 1 14 14 ILE HA H 1 4.286 0.040 . 1 . . . . 11 ILE HA . 11032 1 131 . 1 1 14 14 ILE CB C 13 39.610 0.450 . 1 . . . . 11 ILE CB . 11032 1 132 . 1 1 14 14 ILE HB H 1 1.856 0.040 . 1 . . . . 11 ILE HB . 11032 1 133 . 1 1 14 14 ILE HG21 H 1 0.874 0.040 . 1 . . . . 11 ILE HG2 . 11032 1 134 . 1 1 14 14 ILE HG22 H 1 0.874 0.040 . 1 . . . . 11 ILE HG2 . 11032 1 135 . 1 1 14 14 ILE HG23 H 1 0.874 0.040 . 1 . . . . 11 ILE HG2 . 11032 1 136 . 1 1 14 14 ILE CG2 C 13 17.601 0.450 . 1 . . . . 11 ILE CG2 . 11032 1 137 . 1 1 14 14 ILE CG1 C 13 27.479 0.450 . 1 . . . . 11 ILE CG1 . 11032 1 138 . 1 1 14 14 ILE HG12 H 1 1.479 0.040 . 2 . . . . 11 ILE HG12 . 11032 1 139 . 1 1 14 14 ILE HG13 H 1 1.163 0.040 . 2 . . . . 11 ILE HG13 . 11032 1 140 . 1 1 14 14 ILE HD11 H 1 0.849 0.040 . 1 . . . . 11 ILE HD1 . 11032 1 141 . 1 1 14 14 ILE HD12 H 1 0.849 0.040 . 1 . . . . 11 ILE HD1 . 11032 1 142 . 1 1 14 14 ILE HD13 H 1 0.849 0.040 . 1 . . . . 11 ILE HD1 . 11032 1 143 . 1 1 14 14 ILE CD1 C 13 13.188 0.450 . 1 . . . . 11 ILE CD1 . 11032 1 144 . 1 1 14 14 ILE C C 13 175.192 0.450 . 1 . . . . 11 ILE C . 11032 1 145 . 1 1 15 15 ALA N N 15 130.084 0.450 . 1 . . . . 12 ALA N . 11032 1 146 . 1 1 15 15 ALA H H 1 8.582 0.040 . 1 . . . . 12 ALA H . 11032 1 147 . 1 1 15 15 ALA CA C 13 51.257 0.450 . 1 . . . . 12 ALA CA . 11032 1 148 . 1 1 15 15 ALA HA H 1 5.210 0.040 . 1 . . . . 12 ALA HA . 11032 1 149 . 1 1 15 15 ALA HB1 H 1 1.308 0.040 . 1 . . . . 12 ALA HB . 11032 1 150 . 1 1 15 15 ALA HB2 H 1 1.308 0.040 . 1 . . . . 12 ALA HB . 11032 1 151 . 1 1 15 15 ALA HB3 H 1 1.308 0.040 . 1 . . . . 12 ALA HB . 11032 1 152 . 1 1 15 15 ALA CB C 13 19.941 0.450 . 1 . . . . 12 ALA CB . 11032 1 153 . 1 1 15 15 ALA C C 13 177.397 0.450 . 1 . . . . 12 ALA C . 11032 1 154 . 1 1 16 16 LYS N N 15 121.502 0.450 . 1 . . . . 13 LYS N . 11032 1 155 . 1 1 16 16 LYS H H 1 9.310 0.040 . 1 . . . . 13 LYS H . 11032 1 156 . 1 1 16 16 LYS CA C 13 55.163 0.450 . 1 . . . . 13 LYS CA . 11032 1 157 . 1 1 16 16 LYS HA H 1 4.683 0.040 . 1 . . . . 13 LYS HA . 11032 1 158 . 1 1 16 16 LYS CB C 13 36.212 0.450 . 1 . . . . 13 LYS CB . 11032 1 159 . 1 1 16 16 LYS HB2 H 1 1.687 0.040 . 2 . . . . 13 LYS HB2 . 11032 1 160 . 1 1 16 16 LYS HB3 H 1 1.786 0.040 . 2 . . . . 13 LYS HB3 . 11032 1 161 . 1 1 16 16 LYS CG C 13 24.246 0.450 . 1 . . . . 13 LYS CG . 11032 1 162 . 1 1 16 16 LYS HG2 H 1 1.300 0.040 . 2 . . . . 13 LYS HG2 . 11032 1 163 . 1 1 16 16 LYS HG3 H 1 1.246 0.040 . 2 . . . . 13 LYS HG3 . 11032 1 164 . 1 1 16 16 LYS CD C 13 28.909 0.450 . 1 . . . . 13 LYS CD . 11032 1 165 . 1 1 16 16 LYS HD2 H 1 1.340 0.040 . 2 . . . . 13 LYS HD2 . 11032 1 166 . 1 1 16 16 LYS HD3 H 1 1.246 0.040 . 2 . . . . 13 LYS HD3 . 11032 1 167 . 1 1 16 16 LYS CE C 13 41.403 0.450 . 1 . . . . 13 LYS CE . 11032 1 168 . 1 1 16 16 LYS HE2 H 1 2.516 0.040 . 2 . . . . 13 LYS HE2 . 11032 1 169 . 1 1 16 16 LYS HE3 H 1 2.516 0.040 . 2 . . . . 13 LYS HE3 . 11032 1 170 . 1 1 16 16 LYS C C 13 174.540 0.450 . 1 . . . . 13 LYS C . 11032 1 171 . 1 1 17 17 LYS N N 15 123.608 0.450 . 1 . . . . 14 LYS N . 11032 1 172 . 1 1 17 17 LYS H H 1 8.609 0.040 . 1 . . . . 14 LYS H . 11032 1 173 . 1 1 17 17 LYS CA C 13 55.188 0.450 . 1 . . . . 14 LYS CA . 11032 1 174 . 1 1 17 17 LYS HA H 1 4.814 0.040 . 1 . . . . 14 LYS HA . 11032 1 175 . 1 1 17 17 LYS CB C 13 31.934 0.450 . 1 . . . . 14 LYS CB . 11032 1 176 . 1 1 17 17 LYS HB2 H 1 1.893 0.040 . 2 . . . . 14 LYS HB2 . 11032 1 177 . 1 1 17 17 LYS HB3 H 1 1.705 0.040 . 2 . . . . 14 LYS HB3 . 11032 1 178 . 1 1 17 17 LYS CG C 13 25.080 0.450 . 1 . . . . 14 LYS CG . 11032 1 179 . 1 1 17 17 LYS HG2 H 1 1.431 0.040 . 2 . . . . 14 LYS HG2 . 11032 1 180 . 1 1 17 17 LYS HG3 H 1 1.341 0.040 . 2 . . . . 14 LYS HG3 . 11032 1 181 . 1 1 17 17 LYS CD C 13 28.515 0.450 . 1 . . . . 14 LYS CD . 11032 1 182 . 1 1 17 17 LYS HD2 H 1 1.732 0.040 . 2 . . . . 14 LYS HD2 . 11032 1 183 . 1 1 17 17 LYS HD3 H 1 1.637 0.040 . 2 . . . . 14 LYS HD3 . 11032 1 184 . 1 1 17 17 LYS CE C 13 41.902 0.450 . 1 . . . . 14 LYS CE . 11032 1 185 . 1 1 17 17 LYS HE2 H 1 3.052 0.040 . 2 . . . . 14 LYS HE2 . 11032 1 186 . 1 1 17 17 LYS HE3 H 1 2.956 0.040 . 2 . . . . 14 LYS HE3 . 11032 1 187 . 1 1 17 17 LYS C C 13 176.515 0.450 . 1 . . . . 14 LYS C . 11032 1 188 . 1 1 18 18 ILE N N 15 122.593 0.450 . 1 . . . . 15 ILE N . 11032 1 189 . 1 1 18 18 ILE H H 1 9.358 0.040 . 1 . . . . 15 ILE H . 11032 1 190 . 1 1 18 18 ILE CA C 13 59.892 0.450 . 1 . . . . 15 ILE CA . 11032 1 191 . 1 1 18 18 ILE HA H 1 4.724 0.040 . 1 . . . . 15 ILE HA . 11032 1 192 . 1 1 18 18 ILE CB C 13 40.676 0.450 . 1 . . . . 15 ILE CB . 11032 1 193 . 1 1 18 18 ILE HB H 1 2.251 0.040 . 1 . . . . 15 ILE HB . 11032 1 194 . 1 1 18 18 ILE HG21 H 1 1.081 0.040 . 1 . . . . 15 ILE HG2 . 11032 1 195 . 1 1 18 18 ILE HG22 H 1 1.081 0.040 . 1 . . . . 15 ILE HG2 . 11032 1 196 . 1 1 18 18 ILE HG23 H 1 1.081 0.040 . 1 . . . . 15 ILE HG2 . 11032 1 197 . 1 1 18 18 ILE CG2 C 13 18.477 0.450 . 1 . . . . 15 ILE CG2 . 11032 1 198 . 1 1 18 18 ILE CG1 C 13 25.728 0.450 . 1 . . . . 15 ILE CG1 . 11032 1 199 . 1 1 18 18 ILE HG12 H 1 1.366 0.040 . 2 . . . . 15 ILE HG12 . 11032 1 200 . 1 1 18 18 ILE HG13 H 1 1.366 0.040 . 2 . . . . 15 ILE HG13 . 11032 1 201 . 1 1 18 18 ILE HD11 H 1 0.935 0.040 . 1 . . . . 15 ILE HD1 . 11032 1 202 . 1 1 18 18 ILE HD12 H 1 0.935 0.040 . 1 . . . . 15 ILE HD1 . 11032 1 203 . 1 1 18 18 ILE HD13 H 1 0.935 0.040 . 1 . . . . 15 ILE HD1 . 11032 1 204 . 1 1 18 18 ILE CD1 C 13 14.522 0.450 . 1 . . . . 15 ILE CD1 . 11032 1 205 . 1 1 18 18 ILE C C 13 175.200 0.450 . 1 . . . . 15 ILE C . 11032 1 206 . 1 1 19 19 ASN N N 15 115.643 0.450 . 1 . . . . 16 ASN N . 11032 1 207 . 1 1 19 19 ASN H H 1 8.709 0.040 . 1 . . . . 16 ASN H . 11032 1 208 . 1 1 19 19 ASN CA C 13 53.220 0.450 . 1 . . . . 16 ASN CA . 11032 1 209 . 1 1 19 19 ASN HA H 1 4.947 0.040 . 1 . . . . 16 ASN HA . 11032 1 210 . 1 1 19 19 ASN CB C 13 40.277 0.450 . 1 . . . . 16 ASN CB . 11032 1 211 . 1 1 19 19 ASN HB2 H 1 2.835 0.040 . 2 . . . . 16 ASN HB2 . 11032 1 212 . 1 1 19 19 ASN HB3 H 1 2.787 0.040 . 2 . . . . 16 ASN HB3 . 11032 1 213 . 1 1 19 19 ASN CG C 13 176.952 0.450 . 1 . . . . 16 ASN CG . 11032 1 214 . 1 1 19 19 ASN ND2 N 15 113.639 0.450 . 1 . . . . 16 ASN ND2 . 11032 1 215 . 1 1 19 19 ASN HD21 H 1 7.704 0.040 . 2 . . . . 16 ASN HD21 . 11032 1 216 . 1 1 19 19 ASN HD22 H 1 6.934 0.040 . 2 . . . . 16 ASN HD22 . 11032 1 217 . 1 1 19 19 ASN C C 13 175.234 0.450 . 1 . . . . 16 ASN C . 11032 1 218 . 1 1 20 20 SER N N 15 112.624 0.450 . 1 . . . . 17 SER N . 11032 1 219 . 1 1 20 20 SER H H 1 7.567 0.040 . 1 . . . . 17 SER H . 11032 1 220 . 1 1 20 20 SER CA C 13 56.028 0.450 . 1 . . . . 17 SER CA . 11032 1 221 . 1 1 20 20 SER HA H 1 4.836 0.040 . 1 . . . . 17 SER HA . 11032 1 222 . 1 1 20 20 SER CB C 13 64.979 0.450 . 1 . . . . 17 SER CB . 11032 1 223 . 1 1 20 20 SER HB2 H 1 3.956 0.040 . 2 . . . . 17 SER HB2 . 11032 1 224 . 1 1 20 20 SER HB3 H 1 3.650 0.040 . 2 . . . . 17 SER HB3 . 11032 1 225 . 1 1 20 20 SER C C 13 175.509 0.450 . 1 . . . . 17 SER C . 11032 1 226 . 1 1 21 21 VAL N N 15 120.746 0.450 . 1 . . . . 18 VAL N . 11032 1 227 . 1 1 21 21 VAL H H 1 9.110 0.040 . 1 . . . . 18 VAL H . 11032 1 228 . 1 1 21 21 VAL CA C 13 64.302 0.450 . 1 . . . . 18 VAL CA . 11032 1 229 . 1 1 21 21 VAL HA H 1 3.998 0.040 . 1 . . . . 18 VAL HA . 11032 1 230 . 1 1 21 21 VAL CB C 13 31.499 0.450 . 1 . . . . 18 VAL CB . 11032 1 231 . 1 1 21 21 VAL HB H 1 2.492 0.040 . 1 . . . . 18 VAL HB . 11032 1 232 . 1 1 21 21 VAL HG11 H 1 1.203 0.040 . 2 . . . . 18 VAL HG1 . 11032 1 233 . 1 1 21 21 VAL HG12 H 1 1.203 0.040 . 2 . . . . 18 VAL HG1 . 11032 1 234 . 1 1 21 21 VAL HG13 H 1 1.203 0.040 . 2 . . . . 18 VAL HG1 . 11032 1 235 . 1 1 21 21 VAL HG21 H 1 1.167 0.040 . 2 . . . . 18 VAL HG2 . 11032 1 236 . 1 1 21 21 VAL HG22 H 1 1.167 0.040 . 2 . . . . 18 VAL HG2 . 11032 1 237 . 1 1 21 21 VAL HG23 H 1 1.167 0.040 . 2 . . . . 18 VAL HG2 . 11032 1 238 . 1 1 21 21 VAL CG1 C 13 19.032 0.450 . 1 . . . . 18 VAL CG1 . 11032 1 239 . 1 1 21 21 VAL CG2 C 13 22.064 0.450 . 1 . . . . 18 VAL CG2 . 11032 1 240 . 1 1 21 21 VAL C C 13 177.612 0.450 . 1 . . . . 18 VAL C . 11032 1 241 . 1 1 22 22 ASP N N 15 122.528 0.450 . 1 . . . . 19 ASP N . 11032 1 242 . 1 1 22 22 ASP H H 1 8.409 0.040 . 1 . . . . 19 ASP H . 11032 1 243 . 1 1 22 22 ASP CA C 13 56.430 0.450 . 1 . . . . 19 ASP CA . 11032 1 244 . 1 1 22 22 ASP HA H 1 4.501 0.040 . 1 . . . . 19 ASP HA . 11032 1 245 . 1 1 22 22 ASP CB C 13 40.097 0.450 . 1 . . . . 19 ASP CB . 11032 1 246 . 1 1 22 22 ASP HB2 H 1 2.768 0.040 . 2 . . . . 19 ASP HB2 . 11032 1 247 . 1 1 22 22 ASP HB3 H 1 2.514 0.040 . 2 . . . . 19 ASP HB3 . 11032 1 248 . 1 1 22 22 ASP C C 13 176.303 0.450 . 1 . . . . 19 ASP C . 11032 1 249 . 1 1 23 23 ASP N N 15 115.140 0.450 . 1 . . . . 20 ASP N . 11032 1 250 . 1 1 23 23 ASP H H 1 7.496 0.040 . 1 . . . . 20 ASP H . 11032 1 251 . 1 1 23 23 ASP CA C 13 54.941 0.450 . 1 . . . . 20 ASP CA . 11032 1 252 . 1 1 23 23 ASP HA H 1 4.788 0.040 . 1 . . . . 20 ASP HA . 11032 1 253 . 1 1 23 23 ASP CB C 13 41.407 0.450 . 1 . . . . 20 ASP CB . 11032 1 254 . 1 1 23 23 ASP HB2 H 1 2.951 0.040 . 2 . . . . 20 ASP HB2 . 11032 1 255 . 1 1 23 23 ASP HB3 H 1 2.840 0.040 . 2 . . . . 20 ASP HB3 . 11032 1 256 . 1 1 23 23 ASP C C 13 178.487 0.450 . 1 . . . . 20 ASP C . 11032 1 257 . 1 1 24 24 ILE N N 15 125.876 0.450 . 1 . . . . 21 ILE N . 11032 1 258 . 1 1 24 24 ILE H H 1 7.741 0.040 . 1 . . . . 21 ILE H . 11032 1 259 . 1 1 24 24 ILE CA C 13 63.589 0.450 . 1 . . . . 21 ILE CA . 11032 1 260 . 1 1 24 24 ILE HA H 1 3.727 0.040 . 1 . . . . 21 ILE HA . 11032 1 261 . 1 1 24 24 ILE CB C 13 37.111 0.450 . 1 . . . . 21 ILE CB . 11032 1 262 . 1 1 24 24 ILE HB H 1 2.108 0.040 . 1 . . . . 21 ILE HB . 11032 1 263 . 1 1 24 24 ILE HG21 H 1 0.652 0.040 . 1 . . . . 21 ILE HG2 . 11032 1 264 . 1 1 24 24 ILE HG22 H 1 0.652 0.040 . 1 . . . . 21 ILE HG2 . 11032 1 265 . 1 1 24 24 ILE HG23 H 1 0.652 0.040 . 1 . . . . 21 ILE HG2 . 11032 1 266 . 1 1 24 24 ILE CG2 C 13 18.665 0.450 . 1 . . . . 21 ILE CG2 . 11032 1 267 . 1 1 24 24 ILE CG1 C 13 29.840 0.450 . 1 . . . . 21 ILE CG1 . 11032 1 268 . 1 1 24 24 ILE HG12 H 1 0.828 0.040 . 2 . . . . 21 ILE HG12 . 11032 1 269 . 1 1 24 24 ILE HG13 H 1 1.652 0.040 . 2 . . . . 21 ILE HG13 . 11032 1 270 . 1 1 24 24 ILE HD11 H 1 0.700 0.040 . 1 . . . . 21 ILE HD1 . 11032 1 271 . 1 1 24 24 ILE HD12 H 1 0.700 0.040 . 1 . . . . 21 ILE HD1 . 11032 1 272 . 1 1 24 24 ILE HD13 H 1 0.700 0.040 . 1 . . . . 21 ILE HD1 . 11032 1 273 . 1 1 24 24 ILE CD1 C 13 13.214 0.450 . 1 . . . . 21 ILE CD1 . 11032 1 274 . 1 1 24 24 ILE C C 13 174.439 0.450 . 1 . . . . 21 ILE C . 11032 1 275 . 1 1 25 25 ILE N N 15 120.508 0.450 . 1 . . . . 22 ILE N . 11032 1 276 . 1 1 25 25 ILE H H 1 7.156 0.040 . 1 . . . . 22 ILE H . 11032 1 277 . 1 1 25 25 ILE CA C 13 59.307 0.450 . 1 . . . . 22 ILE CA . 11032 1 278 . 1 1 25 25 ILE HA H 1 4.806 0.040 . 1 . . . . 22 ILE HA . 11032 1 279 . 1 1 25 25 ILE CB C 13 42.414 0.450 . 1 . . . . 22 ILE CB . 11032 1 280 . 1 1 25 25 ILE HB H 1 2.116 0.040 . 1 . . . . 22 ILE HB . 11032 1 281 . 1 1 25 25 ILE HG21 H 1 1.023 0.040 . 1 . . . . 22 ILE HG2 . 11032 1 282 . 1 1 25 25 ILE HG22 H 1 1.023 0.040 . 1 . . . . 22 ILE HG2 . 11032 1 283 . 1 1 25 25 ILE HG23 H 1 1.023 0.040 . 1 . . . . 22 ILE HG2 . 11032 1 284 . 1 1 25 25 ILE CG2 C 13 17.616 0.450 . 1 . . . . 22 ILE CG2 . 11032 1 285 . 1 1 25 25 ILE CG1 C 13 26.471 0.450 . 1 . . . . 22 ILE CG1 . 11032 1 286 . 1 1 25 25 ILE HG12 H 1 1.556 0.040 . 2 . . . . 22 ILE HG12 . 11032 1 287 . 1 1 25 25 ILE HG13 H 1 1.078 0.040 . 2 . . . . 22 ILE HG13 . 11032 1 288 . 1 1 25 25 ILE HD11 H 1 1.057 0.040 . 1 . . . . 22 ILE HD1 . 11032 1 289 . 1 1 25 25 ILE HD12 H 1 1.057 0.040 . 1 . . . . 22 ILE HD1 . 11032 1 290 . 1 1 25 25 ILE HD13 H 1 1.057 0.040 . 1 . . . . 22 ILE HD1 . 11032 1 291 . 1 1 25 25 ILE CD1 C 13 13.963 0.450 . 1 . . . . 22 ILE CD1 . 11032 1 292 . 1 1 25 25 ILE C C 13 175.405 0.450 . 1 . . . . 22 ILE C . 11032 1 293 . 1 1 26 26 ILE N N 15 119.898 0.450 . 1 . . . . 23 ILE N . 11032 1 294 . 1 1 26 26 ILE H H 1 8.183 0.040 . 1 . . . . 23 ILE H . 11032 1 295 . 1 1 26 26 ILE CA C 13 63.817 0.450 . 1 . . . . 23 ILE CA . 11032 1 296 . 1 1 26 26 ILE HA H 1 3.479 0.040 . 1 . . . . 23 ILE HA . 11032 1 297 . 1 1 26 26 ILE CB C 13 37.603 0.450 . 1 . . . . 23 ILE CB . 11032 1 298 . 1 1 26 26 ILE HB H 1 1.777 0.040 . 1 . . . . 23 ILE HB . 11032 1 299 . 1 1 26 26 ILE HG21 H 1 1.022 0.040 . 1 . . . . 23 ILE HG2 . 11032 1 300 . 1 1 26 26 ILE HG22 H 1 1.022 0.040 . 1 . . . . 23 ILE HG2 . 11032 1 301 . 1 1 26 26 ILE HG23 H 1 1.022 0.040 . 1 . . . . 23 ILE HG2 . 11032 1 302 . 1 1 26 26 ILE CG2 C 13 17.892 0.450 . 1 . . . . 23 ILE CG2 . 11032 1 303 . 1 1 26 26 ILE CG1 C 13 28.216 0.450 . 1 . . . . 23 ILE CG1 . 11032 1 304 . 1 1 26 26 ILE HG12 H 1 1.628 0.040 . 2 . . . . 23 ILE HG12 . 11032 1 305 . 1 1 26 26 ILE HG13 H 1 1.080 0.040 . 2 . . . . 23 ILE HG13 . 11032 1 306 . 1 1 26 26 ILE HD11 H 1 0.976 0.040 . 1 . . . . 23 ILE HD1 . 11032 1 307 . 1 1 26 26 ILE HD12 H 1 0.976 0.040 . 1 . . . . 23 ILE HD1 . 11032 1 308 . 1 1 26 26 ILE HD13 H 1 0.976 0.040 . 1 . . . . 23 ILE HD1 . 11032 1 309 . 1 1 26 26 ILE CD1 C 13 13.192 0.450 . 1 . . . . 23 ILE CD1 . 11032 1 310 . 1 1 26 26 ILE C C 13 176.078 0.450 . 1 . . . . 23 ILE C . 11032 1 311 . 1 1 27 27 LYS N N 15 115.664 0.450 . 1 . . . . 24 LYS N . 11032 1 312 . 1 1 27 27 LYS H H 1 8.937 0.040 . 1 . . . . 24 LYS H . 11032 1 313 . 1 1 27 27 LYS CA C 13 59.248 0.450 . 1 . . . . 24 LYS CA . 11032 1 314 . 1 1 27 27 LYS HA H 1 3.701 0.040 . 1 . . . . 24 LYS HA . 11032 1 315 . 1 1 27 27 LYS CB C 13 29.994 0.450 . 1 . . . . 24 LYS CB . 11032 1 316 . 1 1 27 27 LYS HB2 H 1 2.486 0.040 . 2 . . . . 24 LYS HB2 . 11032 1 317 . 1 1 27 27 LYS HB3 H 1 2.051 0.040 . 2 . . . . 24 LYS HB3 . 11032 1 318 . 1 1 27 27 LYS CG C 13 26.115 0.450 . 1 . . . . 24 LYS CG . 11032 1 319 . 1 1 27 27 LYS HG2 H 1 1.538 0.040 . 2 . . . . 24 LYS HG2 . 11032 1 320 . 1 1 27 27 LYS HG3 H 1 1.538 0.040 . 2 . . . . 24 LYS HG3 . 11032 1 321 . 1 1 27 27 LYS CD C 13 28.545 0.450 . 1 . . . . 24 LYS CD . 11032 1 322 . 1 1 27 27 LYS HD2 H 1 1.680 0.040 . 2 . . . . 24 LYS HD2 . 11032 1 323 . 1 1 27 27 LYS HD3 H 1 1.642 0.040 . 2 . . . . 24 LYS HD3 . 11032 1 324 . 1 1 27 27 LYS CE C 13 41.597 0.450 . 1 . . . . 24 LYS CE . 11032 1 325 . 1 1 27 27 LYS HE2 H 1 2.965 0.040 . 2 . . . . 24 LYS HE2 . 11032 1 326 . 1 1 27 27 LYS HE3 H 1 2.965 0.040 . 2 . . . . 24 LYS HE3 . 11032 1 327 . 1 1 27 27 LYS C C 13 177.631 0.450 . 1 . . . . 24 LYS C . 11032 1 328 . 1 1 28 28 CYS N N 15 116.258 0.450 . 1 . . . . 25 CYS N . 11032 1 329 . 1 1 28 28 CYS H H 1 7.808 0.040 . 1 . . . . 25 CYS H . 11032 1 330 . 1 1 28 28 CYS CA C 13 61.565 0.450 . 1 . . . . 25 CYS CA . 11032 1 331 . 1 1 28 28 CYS HA H 1 4.766 0.040 . 1 . . . . 25 CYS HA . 11032 1 332 . 1 1 28 28 CYS CB C 13 28.187 0.450 . 1 . . . . 25 CYS CB . 11032 1 333 . 1 1 28 28 CYS HB2 H 1 2.577 0.040 . 2 . . . . 25 CYS HB2 . 11032 1 334 . 1 1 28 28 CYS HB3 H 1 2.406 0.040 . 2 . . . . 25 CYS HB3 . 11032 1 335 . 1 1 28 28 CYS C C 13 173.682 0.450 . 1 . . . . 25 CYS C . 11032 1 336 . 1 1 29 29 GLN N N 15 118.109 0.450 . 1 . . . . 26 GLN N . 11032 1 337 . 1 1 29 29 GLN H H 1 8.640 0.040 . 1 . . . . 26 GLN H . 11032 1 338 . 1 1 29 29 GLN CA C 13 53.797 0.450 . 1 . . . . 26 GLN CA . 11032 1 339 . 1 1 29 29 GLN HA H 1 5.655 0.040 . 1 . . . . 26 GLN HA . 11032 1 340 . 1 1 29 29 GLN CB C 13 30.177 0.450 . 1 . . . . 26 GLN CB . 11032 1 341 . 1 1 29 29 GLN HB2 H 1 1.800 0.040 . 2 . . . . 26 GLN HB2 . 11032 1 342 . 1 1 29 29 GLN HB3 H 1 1.653 0.040 . 2 . . . . 26 GLN HB3 . 11032 1 343 . 1 1 29 29 GLN CG C 13 33.322 0.450 . 1 . . . . 26 GLN CG . 11032 1 344 . 1 1 29 29 GLN HG2 H 1 2.319 0.040 . 2 . . . . 26 GLN HG2 . 11032 1 345 . 1 1 29 29 GLN HG3 H 1 2.319 0.040 . 2 . . . . 26 GLN HG3 . 11032 1 346 . 1 1 29 29 GLN CD C 13 178.052 0.450 . 1 . . . . 26 GLN CD . 11032 1 347 . 1 1 29 29 GLN NE2 N 15 108.072 0.450 . 1 . . . . 26 GLN NE2 . 11032 1 348 . 1 1 29 29 GLN HE21 H 1 7.463 0.040 . 2 . . . . 26 GLN HE21 . 11032 1 349 . 1 1 29 29 GLN HE22 H 1 6.401 0.040 . 2 . . . . 26 GLN HE22 . 11032 1 350 . 1 1 29 29 GLN C C 13 175.195 0.450 . 1 . . . . 26 GLN C . 11032 1 351 . 1 1 30 30 CYS N N 15 118.734 0.450 . 1 . . . . 27 CYS N . 11032 1 352 . 1 1 30 30 CYS H H 1 9.205 0.040 . 1 . . . . 27 CYS H . 11032 1 353 . 1 1 30 30 CYS CA C 13 54.510 0.450 . 1 . . . . 27 CYS CA . 11032 1 354 . 1 1 30 30 CYS HA H 1 4.886 0.040 . 1 . . . . 27 CYS HA . 11032 1 355 . 1 1 30 30 CYS CB C 13 31.756 0.450 . 1 . . . . 27 CYS CB . 11032 1 356 . 1 1 30 30 CYS HB2 H 1 2.789 0.040 . 2 . . . . 27 CYS HB2 . 11032 1 357 . 1 1 30 30 CYS HB3 H 1 2.764 0.040 . 2 . . . . 27 CYS HB3 . 11032 1 358 . 1 1 30 30 CYS C C 13 171.247 0.450 . 1 . . . . 27 CYS C . 11032 1 359 . 1 1 31 31 TRP N N 15 124.551 0.450 . 1 . . . . 28 TRP N . 11032 1 360 . 1 1 31 31 TRP H H 1 9.398 0.040 . 1 . . . . 28 TRP H . 11032 1 361 . 1 1 31 31 TRP CA C 13 56.784 0.450 . 1 . . . . 28 TRP CA . 11032 1 362 . 1 1 31 31 TRP HA H 1 4.629 0.040 . 1 . . . . 28 TRP HA . 11032 1 363 . 1 1 31 31 TRP CB C 13 29.253 0.450 . 1 . . . . 28 TRP CB . 11032 1 364 . 1 1 31 31 TRP HB2 H 1 3.107 0.040 . 2 . . . . 28 TRP HB2 . 11032 1 365 . 1 1 31 31 TRP HB3 H 1 3.130 0.040 . 2 . . . . 28 TRP HB3 . 11032 1 366 . 1 1 31 31 TRP CD1 C 13 128.227 0.450 . 1 . . . . 28 TRP CD1 . 11032 1 367 . 1 1 31 31 TRP CE3 C 13 119.262 0.450 . 1 . . . . 28 TRP CE3 . 11032 1 368 . 1 1 31 31 TRP NE1 N 15 129.751 0.450 . 1 . . . . 28 TRP NE1 . 11032 1 369 . 1 1 31 31 TRP HD1 H 1 7.449 0.040 . 1 . . . . 28 TRP HD1 . 11032 1 370 . 1 1 31 31 TRP HE3 H 1 7.183 0.040 . 1 . . . . 28 TRP HE3 . 11032 1 371 . 1 1 31 31 TRP CZ3 C 13 122.024 0.450 . 1 . . . . 28 TRP CZ3 . 11032 1 372 . 1 1 31 31 TRP CZ2 C 13 114.934 0.450 . 1 . . . . 28 TRP CZ2 . 11032 1 373 . 1 1 31 31 TRP HE1 H 1 10.204 0.040 . 1 . . . . 28 TRP HE1 . 11032 1 374 . 1 1 31 31 TRP HZ3 H 1 7.138 0.040 . 1 . . . . 28 TRP HZ3 . 11032 1 375 . 1 1 31 31 TRP CH2 C 13 124.385 0.450 . 1 . . . . 28 TRP CH2 . 11032 1 376 . 1 1 31 31 TRP HZ2 H 1 7.527 0.040 . 1 . . . . 28 TRP HZ2 . 11032 1 377 . 1 1 31 31 TRP HH2 H 1 7.238 0.040 . 1 . . . . 28 TRP HH2 . 11032 1 378 . 1 1 31 31 TRP C C 13 175.202 0.450 . 1 . . . . 28 TRP C . 11032 1 379 . 1 1 32 32 VAL N N 15 122.449 0.450 . 1 . . . . 29 VAL N . 11032 1 380 . 1 1 32 32 VAL H H 1 9.161 0.040 . 1 . . . . 29 VAL H . 11032 1 381 . 1 1 32 32 VAL CA C 13 59.628 0.450 . 1 . . . . 29 VAL CA . 11032 1 382 . 1 1 32 32 VAL HA H 1 4.971 0.040 . 1 . . . . 29 VAL HA . 11032 1 383 . 1 1 32 32 VAL CB C 13 35.745 0.450 . 1 . . . . 29 VAL CB . 11032 1 384 . 1 1 32 32 VAL HB H 1 1.994 0.040 . 1 . . . . 29 VAL HB . 11032 1 385 . 1 1 32 32 VAL HG11 H 1 0.962 0.040 . 2 . . . . 29 VAL HG1 . 11032 1 386 . 1 1 32 32 VAL HG12 H 1 0.962 0.040 . 2 . . . . 29 VAL HG1 . 11032 1 387 . 1 1 32 32 VAL HG13 H 1 0.962 0.040 . 2 . . . . 29 VAL HG1 . 11032 1 388 . 1 1 32 32 VAL HG21 H 1 0.756 0.040 . 2 . . . . 29 VAL HG2 . 11032 1 389 . 1 1 32 32 VAL HG22 H 1 0.756 0.040 . 2 . . . . 29 VAL HG2 . 11032 1 390 . 1 1 32 32 VAL HG23 H 1 0.756 0.040 . 2 . . . . 29 VAL HG2 . 11032 1 391 . 1 1 32 32 VAL CG1 C 13 22.559 0.450 . 1 . . . . 29 VAL CG1 . 11032 1 392 . 1 1 32 32 VAL CG2 C 13 23.229 0.450 . 1 . . . . 29 VAL CG2 . 11032 1 393 . 1 1 32 32 VAL C C 13 175.640 0.450 . 1 . . . . 29 VAL C . 11032 1 394 . 1 1 33 33 GLN N N 15 125.695 0.450 . 1 . . . . 30 GLN N . 11032 1 395 . 1 1 33 33 GLN H H 1 9.059 0.040 . 1 . . . . 30 GLN H . 11032 1 396 . 1 1 33 33 GLN CA C 13 56.315 0.450 . 1 . . . . 30 GLN CA . 11032 1 397 . 1 1 33 33 GLN HA H 1 4.588 0.040 . 1 . . . . 30 GLN HA . 11032 1 398 . 1 1 33 33 GLN CB C 13 29.048 0.450 . 1 . . . . 30 GLN CB . 11032 1 399 . 1 1 33 33 GLN HB2 H 1 2.137 0.040 . 2 . . . . 30 GLN HB2 . 11032 1 400 . 1 1 33 33 GLN HB3 H 1 2.078 0.040 . 2 . . . . 30 GLN HB3 . 11032 1 401 . 1 1 33 33 GLN CG C 13 33.328 0.450 . 1 . . . . 30 GLN CG . 11032 1 402 . 1 1 33 33 GLN HG2 H 1 2.400 0.040 . 2 . . . . 30 GLN HG2 . 11032 1 403 . 1 1 33 33 GLN HG3 H 1 2.400 0.040 . 2 . . . . 30 GLN HG3 . 11032 1 404 . 1 1 33 33 GLN CD C 13 179.810 0.450 . 1 . . . . 30 GLN CD . 11032 1 405 . 1 1 33 33 GLN NE2 N 15 111.037 0.450 . 1 . . . . 30 GLN NE2 . 11032 1 406 . 1 1 33 33 GLN HE21 H 1 7.529 0.040 . 2 . . . . 30 GLN HE21 . 11032 1 407 . 1 1 33 33 GLN HE22 H 1 6.715 0.040 . 2 . . . . 30 GLN HE22 . 11032 1 408 . 1 1 33 33 GLN C C 13 175.198 0.450 . 1 . . . . 30 GLN C . 11032 1 409 . 1 1 34 34 LYS N N 15 128.774 0.450 . 1 . . . . 31 LYS N . 11032 1 410 . 1 1 34 34 LYS H H 1 8.906 0.040 . 1 . . . . 31 LYS H . 11032 1 411 . 1 1 34 34 LYS CA C 13 54.427 0.450 . 1 . . . . 31 LYS CA . 11032 1 412 . 1 1 34 34 LYS HA H 1 4.415 0.040 . 1 . . . . 31 LYS HA . 11032 1 413 . 1 1 34 34 LYS CB C 13 33.550 0.450 . 1 . . . . 31 LYS CB . 11032 1 414 . 1 1 34 34 LYS HB2 H 1 1.402 0.040 . 2 . . . . 31 LYS HB2 . 11032 1 415 . 1 1 34 34 LYS HB3 H 1 1.402 0.040 . 2 . . . . 31 LYS HB3 . 11032 1 416 . 1 1 34 34 LYS CG C 13 24.209 0.450 . 1 . . . . 31 LYS CG . 11032 1 417 . 1 1 34 34 LYS HG2 H 1 0.924 0.040 . 2 . . . . 31 LYS HG2 . 11032 1 418 . 1 1 34 34 LYS HG3 H 1 0.615 0.040 . 2 . . . . 31 LYS HG3 . 11032 1 419 . 1 1 34 34 LYS CD C 13 28.174 0.450 . 1 . . . . 31 LYS CD . 11032 1 420 . 1 1 34 34 LYS HD2 H 1 1.463 0.040 . 2 . . . . 31 LYS HD2 . 11032 1 421 . 1 1 34 34 LYS HD3 H 1 1.378 0.040 . 2 . . . . 31 LYS HD3 . 11032 1 422 . 1 1 34 34 LYS CE C 13 41.792 0.450 . 1 . . . . 31 LYS CE . 11032 1 423 . 1 1 34 34 LYS HE2 H 1 2.632 0.040 . 2 . . . . 31 LYS HE2 . 11032 1 424 . 1 1 34 34 LYS HE3 H 1 2.558 0.040 . 2 . . . . 31 LYS HE3 . 11032 1 425 . 1 1 34 34 LYS C C 13 174.320 0.450 . 1 . . . . 31 LYS C . 11032 1 426 . 1 1 35 35 ASN N N 15 125.636 0.450 . 1 . . . . 32 ASN N . 11032 1 427 . 1 1 35 35 ASN H H 1 9.541 0.040 . 1 . . . . 32 ASN H . 11032 1 428 . 1 1 35 35 ASN CA C 13 55.158 0.450 . 1 . . . . 32 ASN CA . 11032 1 429 . 1 1 35 35 ASN HA H 1 4.219 0.040 . 1 . . . . 32 ASN HA . 11032 1 430 . 1 1 35 35 ASN CB C 13 36.930 0.450 . 1 . . . . 32 ASN CB . 11032 1 431 . 1 1 35 35 ASN HB2 H 1 2.972 0.040 . 2 . . . . 32 ASN HB2 . 11032 1 432 . 1 1 35 35 ASN HB3 H 1 2.948 0.040 . 2 . . . . 32 ASN HB3 . 11032 1 433 . 1 1 35 35 ASN CG C 13 177.392 0.450 . 1 . . . . 32 ASN CG . 11032 1 434 . 1 1 35 35 ASN ND2 N 15 112.973 0.450 . 1 . . . . 32 ASN ND2 . 11032 1 435 . 1 1 35 35 ASN HD21 H 1 7.605 0.040 . 2 . . . . 32 ASN HD21 . 11032 1 436 . 1 1 35 35 ASN HD22 H 1 7.039 0.040 . 2 . . . . 32 ASN HD22 . 11032 1 437 . 1 1 35 35 ASN C C 13 174.330 0.450 . 1 . . . . 32 ASN C . 11032 1 438 . 1 1 36 36 ASP N N 15 118.173 0.450 . 1 . . . . 33 ASP N . 11032 1 439 . 1 1 36 36 ASP H H 1 8.658 0.040 . 1 . . . . 33 ASP H . 11032 1 440 . 1 1 36 36 ASP CA C 13 55.007 0.450 . 1 . . . . 33 ASP CA . 11032 1 441 . 1 1 36 36 ASP HA H 1 4.556 0.040 . 1 . . . . 33 ASP HA . 11032 1 442 . 1 1 36 36 ASP CB C 13 40.075 0.450 . 1 . . . . 33 ASP CB . 11032 1 443 . 1 1 36 36 ASP HB2 H 1 2.814 0.040 . 2 . . . . 33 ASP HB2 . 11032 1 444 . 1 1 36 36 ASP HB3 H 1 2.814 0.040 . 2 . . . . 33 ASP HB3 . 11032 1 445 . 1 1 36 36 ASP C C 13 174.637 0.450 . 1 . . . . 33 ASP C . 11032 1 446 . 1 1 37 37 GLU N N 15 118.754 0.450 . 1 . . . . 34 GLU N . 11032 1 447 . 1 1 37 37 GLU H H 1 7.934 0.040 . 1 . . . . 34 GLU H . 11032 1 448 . 1 1 37 37 GLU CA C 13 54.451 0.450 . 1 . . . . 34 GLU CA . 11032 1 449 . 1 1 37 37 GLU HA H 1 4.737 0.040 . 1 . . . . 34 GLU HA . 11032 1 450 . 1 1 37 37 GLU CB C 13 33.169 0.450 . 1 . . . . 34 GLU CB . 11032 1 451 . 1 1 37 37 GLU HB2 H 1 2.052 0.040 . 2 . . . . 34 GLU HB2 . 11032 1 452 . 1 1 37 37 GLU HB3 H 1 2.052 0.040 . 2 . . . . 34 GLU HB3 . 11032 1 453 . 1 1 37 37 GLU CG C 13 35.710 0.450 . 1 . . . . 34 GLU CG . 11032 1 454 . 1 1 37 37 GLU HG2 H 1 2.328 0.040 . 2 . . . . 34 GLU HG2 . 11032 1 455 . 1 1 37 37 GLU HG3 H 1 2.168 0.040 . 2 . . . . 34 GLU HG3 . 11032 1 456 . 1 1 37 37 GLU C C 13 174.591 0.450 . 1 . . . . 34 GLU C . 11032 1 457 . 1 1 38 38 GLU N N 15 120.143 0.450 . 1 . . . . 35 GLU N . 11032 1 458 . 1 1 38 38 GLU H H 1 8.461 0.040 . 1 . . . . 35 GLU H . 11032 1 459 . 1 1 38 38 GLU CA C 13 55.461 0.450 . 1 . . . . 35 GLU CA . 11032 1 460 . 1 1 38 38 GLU HA H 1 5.262 0.040 . 1 . . . . 35 GLU HA . 11032 1 461 . 1 1 38 38 GLU CB C 13 32.532 0.450 . 1 . . . . 35 GLU CB . 11032 1 462 . 1 1 38 38 GLU HB2 H 1 2.108 0.040 . 2 . . . . 35 GLU HB2 . 11032 1 463 . 1 1 38 38 GLU HB3 H 1 1.936 0.040 . 2 . . . . 35 GLU HB3 . 11032 1 464 . 1 1 38 38 GLU CG C 13 37.119 0.450 . 1 . . . . 35 GLU CG . 11032 1 465 . 1 1 38 38 GLU HG2 H 1 2.287 0.040 . 2 . . . . 35 GLU HG2 . 11032 1 466 . 1 1 38 38 GLU HG3 H 1 2.147 0.040 . 2 . . . . 35 GLU HG3 . 11032 1 467 . 1 1 38 38 GLU C C 13 176.099 0.450 . 1 . . . . 35 GLU C . 11032 1 468 . 1 1 39 39 ARG N N 15 122.266 0.450 . 1 . . . . 36 ARG N . 11032 1 469 . 1 1 39 39 ARG H H 1 9.493 0.040 . 1 . . . . 36 ARG H . 11032 1 470 . 1 1 39 39 ARG CA C 13 54.293 0.450 . 1 . . . . 36 ARG CA . 11032 1 471 . 1 1 39 39 ARG HA H 1 4.967 0.040 . 1 . . . . 36 ARG HA . 11032 1 472 . 1 1 39 39 ARG CB C 13 35.709 0.450 . 1 . . . . 36 ARG CB . 11032 1 473 . 1 1 39 39 ARG HB2 H 1 1.872 0.040 . 2 . . . . 36 ARG HB2 . 11032 1 474 . 1 1 39 39 ARG HB3 H 1 1.504 0.040 . 2 . . . . 36 ARG HB3 . 11032 1 475 . 1 1 39 39 ARG CG C 13 26.814 0.450 . 1 . . . . 36 ARG CG . 11032 1 476 . 1 1 39 39 ARG HG2 H 1 1.649 0.040 . 2 . . . . 36 ARG HG2 . 11032 1 477 . 1 1 39 39 ARG HG3 H 1 1.373 0.040 . 2 . . . . 36 ARG HG3 . 11032 1 478 . 1 1 39 39 ARG CD C 13 43.046 0.450 . 1 . . . . 36 ARG CD . 11032 1 479 . 1 1 39 39 ARG HD2 H 1 2.263 0.040 . 2 . . . . 36 ARG HD2 . 11032 1 480 . 1 1 39 39 ARG HD3 H 1 1.862 0.040 . 2 . . . . 36 ARG HD3 . 11032 1 481 . 1 1 39 39 ARG C C 13 174.314 0.450 . 1 . . . . 36 ARG C . 11032 1 482 . 1 1 40 40 LEU N N 15 125.818 0.450 . 1 . . . . 37 LEU N . 11032 1 483 . 1 1 40 40 LEU H H 1 8.075 0.040 . 1 . . . . 37 LEU H . 11032 1 484 . 1 1 40 40 LEU CA C 13 54.882 0.450 . 1 . . . . 37 LEU CA . 11032 1 485 . 1 1 40 40 LEU HA H 1 3.550 0.040 . 1 . . . . 37 LEU HA . 11032 1 486 . 1 1 40 40 LEU CB C 13 41.554 0.450 . 1 . . . . 37 LEU CB . 11032 1 487 . 1 1 40 40 LEU HB2 H 1 1.210 0.040 . 2 . . . . 37 LEU HB2 . 11032 1 488 . 1 1 40 40 LEU HB3 H 1 0.083 0.040 . 2 . . . . 37 LEU HB3 . 11032 1 489 . 1 1 40 40 LEU CG C 13 25.999 0.450 . 1 . . . . 37 LEU CG . 11032 1 490 . 1 1 40 40 LEU HG H 1 0.733 0.040 . 1 . . . . 37 LEU HG . 11032 1 491 . 1 1 40 40 LEU HD11 H 1 -0.172 0.040 . 2 . . . . 37 LEU HD1 . 11032 1 492 . 1 1 40 40 LEU HD12 H 1 -0.172 0.040 . 2 . . . . 37 LEU HD1 . 11032 1 493 . 1 1 40 40 LEU HD13 H 1 -0.172 0.040 . 2 . . . . 37 LEU HD1 . 11032 1 494 . 1 1 40 40 LEU HD21 H 1 0.475 0.040 . 2 . . . . 37 LEU HD2 . 11032 1 495 . 1 1 40 40 LEU HD22 H 1 0.475 0.040 . 2 . . . . 37 LEU HD2 . 11032 1 496 . 1 1 40 40 LEU HD23 H 1 0.475 0.040 . 2 . . . . 37 LEU HD2 . 11032 1 497 . 1 1 40 40 LEU CD1 C 13 21.388 0.450 . 1 . . . . 37 LEU CD1 . 11032 1 498 . 1 1 40 40 LEU CD2 C 13 25.145 0.450 . 1 . . . . 37 LEU CD2 . 11032 1 499 . 1 1 40 40 LEU C C 13 176.078 0.450 . 1 . . . . 37 LEU C . 11032 1 500 . 1 1 41 41 ALA N N 15 131.692 0.450 . 1 . . . . 38 ALA N . 11032 1 501 . 1 1 41 41 ALA H H 1 9.466 0.040 . 1 . . . . 38 ALA H . 11032 1 502 . 1 1 41 41 ALA CA C 13 50.098 0.450 . 1 . . . . 38 ALA CA . 11032 1 503 . 1 1 41 41 ALA HA H 1 5.040 0.040 . 1 . . . . 38 ALA HA . 11032 1 504 . 1 1 41 41 ALA HB1 H 1 0.858 0.040 . 1 . . . . 38 ALA HB . 11032 1 505 . 1 1 41 41 ALA HB2 H 1 0.858 0.040 . 1 . . . . 38 ALA HB . 11032 1 506 . 1 1 41 41 ALA HB3 H 1 0.858 0.040 . 1 . . . . 38 ALA HB . 11032 1 507 . 1 1 41 41 ALA CB C 13 22.545 0.450 . 1 . . . . 38 ALA CB . 11032 1 508 . 1 1 41 41 ALA C C 13 174.540 0.450 . 1 . . . . 38 ALA C . 11032 1 509 . 1 1 42 42 GLU N N 15 121.238 0.450 . 1 . . . . 39 GLU N . 11032 1 510 . 1 1 42 42 GLU H H 1 9.325 0.040 . 1 . . . . 39 GLU H . 11032 1 511 . 1 1 42 42 GLU CA C 13 53.835 0.450 . 1 . . . . 39 GLU CA . 11032 1 512 . 1 1 42 42 GLU HA H 1 4.881 0.040 . 1 . . . . 39 GLU HA . 11032 1 513 . 1 1 42 42 GLU CB C 13 33.160 0.450 . 1 . . . . 39 GLU CB . 11032 1 514 . 1 1 42 42 GLU HB2 H 1 1.708 0.040 . 2 . . . . 39 GLU HB2 . 11032 1 515 . 1 1 42 42 GLU HB3 H 1 1.914 0.040 . 2 . . . . 39 GLU HB3 . 11032 1 516 . 1 1 42 42 GLU CG C 13 37.019 0.450 . 1 . . . . 39 GLU CG . 11032 1 517 . 1 1 42 42 GLU HG2 H 1 1.919 0.040 . 2 . . . . 39 GLU HG2 . 11032 1 518 . 1 1 42 42 GLU HG3 H 1 1.849 0.040 . 2 . . . . 39 GLU HG3 . 11032 1 519 . 1 1 42 42 GLU C C 13 175.661 0.450 . 1 . . . . 39 GLU C . 11032 1 520 . 1 1 43 43 ILE N N 15 124.167 0.450 . 1 . . . . 40 ILE N . 11032 1 521 . 1 1 43 43 ILE H H 1 8.550 0.040 . 1 . . . . 40 ILE H . 11032 1 522 . 1 1 43 43 ILE CA C 13 59.516 0.450 . 1 . . . . 40 ILE CA . 11032 1 523 . 1 1 43 43 ILE HA H 1 3.876 0.040 . 1 . . . . 40 ILE HA . 11032 1 524 . 1 1 43 43 ILE CB C 13 35.361 0.450 . 1 . . . . 40 ILE CB . 11032 1 525 . 1 1 43 43 ILE HB H 1 2.179 0.040 . 1 . . . . 40 ILE HB . 11032 1 526 . 1 1 43 43 ILE HG21 H 1 0.757 0.040 . 1 . . . . 40 ILE HG2 . 11032 1 527 . 1 1 43 43 ILE HG22 H 1 0.757 0.040 . 1 . . . . 40 ILE HG2 . 11032 1 528 . 1 1 43 43 ILE HG23 H 1 0.757 0.040 . 1 . . . . 40 ILE HG2 . 11032 1 529 . 1 1 43 43 ILE CG2 C 13 18.605 0.450 . 1 . . . . 40 ILE CG2 . 11032 1 530 . 1 1 43 43 ILE CG1 C 13 26.186 0.450 . 1 . . . . 40 ILE CG1 . 11032 1 531 . 1 1 43 43 ILE HG12 H 1 1.413 0.040 . 2 . . . . 40 ILE HG12 . 11032 1 532 . 1 1 43 43 ILE HG13 H 1 1.006 0.040 . 2 . . . . 40 ILE HG13 . 11032 1 533 . 1 1 43 43 ILE HD11 H 1 0.330 0.040 . 1 . . . . 40 ILE HD1 . 11032 1 534 . 1 1 43 43 ILE HD12 H 1 0.330 0.040 . 1 . . . . 40 ILE HD1 . 11032 1 535 . 1 1 43 43 ILE HD13 H 1 0.330 0.040 . 1 . . . . 40 ILE HD1 . 11032 1 536 . 1 1 43 43 ILE CD1 C 13 9.260 0.450 . 1 . . . . 40 ILE CD1 . 11032 1 537 . 1 1 43 43 ILE C C 13 175.858 0.450 . 1 . . . . 40 ILE C . 11032 1 538 . 1 1 44 44 LEU N N 15 129.595 0.450 . 1 . . . . 41 LEU N . 11032 1 539 . 1 1 44 44 LEU H H 1 9.475 0.040 . 1 . . . . 41 LEU H . 11032 1 540 . 1 1 44 44 LEU CA C 13 55.695 0.450 . 1 . . . . 41 LEU CA . 11032 1 541 . 1 1 44 44 LEU HA H 1 4.549 0.040 . 1 . . . . 41 LEU HA . 11032 1 542 . 1 1 44 44 LEU CB C 13 43.394 0.450 . 1 . . . . 41 LEU CB . 11032 1 543 . 1 1 44 44 LEU HB2 H 1 1.674 0.040 . 2 . . . . 41 LEU HB2 . 11032 1 544 . 1 1 44 44 LEU HB3 H 1 1.521 0.040 . 2 . . . . 41 LEU HB3 . 11032 1 545 . 1 1 44 44 LEU CG C 13 26.944 0.450 . 1 . . . . 41 LEU CG . 11032 1 546 . 1 1 44 44 LEU HG H 1 1.553 0.040 . 1 . . . . 41 LEU HG . 11032 1 547 . 1 1 44 44 LEU HD11 H 1 0.703 0.040 . 2 . . . . 41 LEU HD1 . 11032 1 548 . 1 1 44 44 LEU HD12 H 1 0.703 0.040 . 2 . . . . 41 LEU HD1 . 11032 1 549 . 1 1 44 44 LEU HD13 H 1 0.703 0.040 . 2 . . . . 41 LEU HD1 . 11032 1 550 . 1 1 44 44 LEU HD21 H 1 0.648 0.040 . 2 . . . . 41 LEU HD2 . 11032 1 551 . 1 1 44 44 LEU HD22 H 1 0.648 0.040 . 2 . . . . 41 LEU HD2 . 11032 1 552 . 1 1 44 44 LEU HD23 H 1 0.648 0.040 . 2 . . . . 41 LEU HD2 . 11032 1 553 . 1 1 44 44 LEU CD1 C 13 22.098 0.450 . 1 . . . . 41 LEU CD1 . 11032 1 554 . 1 1 44 44 LEU CD2 C 13 25.701 0.450 . 1 . . . . 41 LEU CD2 . 11032 1 555 . 1 1 44 44 LEU C C 13 177.690 0.450 . 1 . . . . 41 LEU C . 11032 1 556 . 1 1 45 45 SER N N 15 110.494 0.450 . 1 . . . . 42 SER N . 11032 1 557 . 1 1 45 45 SER H H 1 7.716 0.040 . 1 . . . . 42 SER H . 11032 1 558 . 1 1 45 45 SER CA C 13 57.679 0.450 . 1 . . . . 42 SER CA . 11032 1 559 . 1 1 45 45 SER HA H 1 4.541 0.040 . 1 . . . . 42 SER HA . 11032 1 560 . 1 1 45 45 SER CB C 13 64.975 0.450 . 1 . . . . 42 SER CB . 11032 1 561 . 1 1 45 45 SER HB2 H 1 3.686 0.040 . 2 . . . . 42 SER HB2 . 11032 1 562 . 1 1 45 45 SER HB3 H 1 3.607 0.040 . 2 . . . . 42 SER HB3 . 11032 1 563 . 1 1 45 45 SER C C 13 172.123 0.450 . 1 . . . . 42 SER C . 11032 1 564 . 1 1 46 46 ILE N N 15 123.887 0.450 . 1 . . . . 43 ILE N . 11032 1 565 . 1 1 46 46 ILE H H 1 8.651 0.040 . 1 . . . . 43 ILE H . 11032 1 566 . 1 1 46 46 ILE CA C 13 61.397 0.450 . 1 . . . . 43 ILE CA . 11032 1 567 . 1 1 46 46 ILE HA H 1 4.603 0.040 . 1 . . . . 43 ILE HA . 11032 1 568 . 1 1 46 46 ILE CB C 13 41.784 0.450 . 1 . . . . 43 ILE CB . 11032 1 569 . 1 1 46 46 ILE HB H 1 1.675 0.040 . 1 . . . . 43 ILE HB . 11032 1 570 . 1 1 46 46 ILE HG21 H 1 0.674 0.040 . 1 . . . . 43 ILE HG2 . 11032 1 571 . 1 1 46 46 ILE HG22 H 1 0.674 0.040 . 1 . . . . 43 ILE HG2 . 11032 1 572 . 1 1 46 46 ILE HG23 H 1 0.674 0.040 . 1 . . . . 43 ILE HG2 . 11032 1 573 . 1 1 46 46 ILE CG2 C 13 17.138 0.450 . 1 . . . . 43 ILE CG2 . 11032 1 574 . 1 1 46 46 ILE CG1 C 13 27.109 0.450 . 1 . . . . 43 ILE CG1 . 11032 1 575 . 1 1 46 46 ILE HG12 H 1 0.973 0.040 . 2 . . . . 43 ILE HG12 . 11032 1 576 . 1 1 46 46 ILE HG13 H 1 1.377 0.040 . 2 . . . . 43 ILE HG13 . 11032 1 577 . 1 1 46 46 ILE HD11 H 1 0.883 0.040 . 1 . . . . 43 ILE HD1 . 11032 1 578 . 1 1 46 46 ILE HD12 H 1 0.883 0.040 . 1 . . . . 43 ILE HD1 . 11032 1 579 . 1 1 46 46 ILE HD13 H 1 0.883 0.040 . 1 . . . . 43 ILE HD1 . 11032 1 580 . 1 1 46 46 ILE CD1 C 13 14.115 0.450 . 1 . . . . 43 ILE CD1 . 11032 1 581 . 1 1 46 46 ILE C C 13 174.983 0.450 . 1 . . . . 43 ILE C . 11032 1 582 . 1 1 47 47 ASN N N 15 125.536 0.450 . 1 . . . . 44 ASN N . 11032 1 583 . 1 1 47 47 ASN H H 1 9.161 0.040 . 1 . . . . 44 ASN H . 11032 1 584 . 1 1 47 47 ASN CA C 13 51.602 0.450 . 1 . . . . 44 ASN CA . 11032 1 585 . 1 1 47 47 ASN HA H 1 5.164 0.040 . 1 . . . . 44 ASN HA . 11032 1 586 . 1 1 47 47 ASN CB C 13 39.116 0.450 . 1 . . . . 44 ASN CB . 11032 1 587 . 1 1 47 47 ASN HB2 H 1 2.576 0.040 . 2 . . . . 44 ASN HB2 . 11032 1 588 . 1 1 47 47 ASN HB3 H 1 2.727 0.040 . 2 . . . . 44 ASN HB3 . 11032 1 589 . 1 1 47 47 ASN CG C 13 176.070 0.450 . 1 . . . . 44 ASN CG . 11032 1 590 . 1 1 47 47 ASN ND2 N 15 109.903 0.450 . 1 . . . . 44 ASN ND2 . 11032 1 591 . 1 1 47 47 ASN HD21 H 1 6.992 0.040 . 2 . . . . 44 ASN HD21 . 11032 1 592 . 1 1 47 47 ASN HD22 H 1 6.695 0.040 . 2 . . . . 44 ASN HD22 . 11032 1 593 . 1 1 47 47 ASN C C 13 176.080 0.450 . 1 . . . . 44 ASN C . 11032 1 594 . 1 1 48 48 THR N N 15 115.175 0.450 . 1 . . . . 45 THR N . 11032 1 595 . 1 1 48 48 THR H H 1 8.740 0.040 . 1 . . . . 45 THR H . 11032 1 596 . 1 1 48 48 THR CA C 13 60.792 0.450 . 1 . . . . 45 THR CA . 11032 1 597 . 1 1 48 48 THR HA H 1 4.407 0.040 . 1 . . . . 45 THR HA . 11032 1 598 . 1 1 48 48 THR CB C 13 68.262 0.450 . 1 . . . . 45 THR CB . 11032 1 599 . 1 1 48 48 THR HB H 1 4.612 0.040 . 1 . . . . 45 THR HB . 11032 1 600 . 1 1 48 48 THR HG21 H 1 1.162 0.040 . 1 . . . . 45 THR HG2 . 11032 1 601 . 1 1 48 48 THR HG22 H 1 1.162 0.040 . 1 . . . . 45 THR HG2 . 11032 1 602 . 1 1 48 48 THR HG23 H 1 1.162 0.040 . 1 . . . . 45 THR HG2 . 11032 1 603 . 1 1 48 48 THR CG2 C 13 21.842 0.450 . 1 . . . . 45 THR CG2 . 11032 1 604 . 1 1 48 48 THR C C 13 175.199 0.450 . 1 . . . . 45 THR C . 11032 1 605 . 1 1 49 49 ARG N N 15 122.313 0.450 . 1 . . . . 46 ARG N . 11032 1 606 . 1 1 49 49 ARG H H 1 8.320 0.040 . 1 . . . . 46 ARG H . 11032 1 607 . 1 1 49 49 ARG CA C 13 58.244 0.450 . 1 . . . . 46 ARG CA . 11032 1 608 . 1 1 49 49 ARG HA H 1 4.063 0.040 . 1 . . . . 46 ARG HA . 11032 1 609 . 1 1 49 49 ARG CB C 13 29.778 0.450 . 1 . . . . 46 ARG CB . 11032 1 610 . 1 1 49 49 ARG HB2 H 1 1.905 0.040 . 2 . . . . 46 ARG HB2 . 11032 1 611 . 1 1 49 49 ARG HB3 H 1 1.859 0.040 . 2 . . . . 46 ARG HB3 . 11032 1 612 . 1 1 49 49 ARG CG C 13 27.783 0.450 . 1 . . . . 46 ARG CG . 11032 1 613 . 1 1 49 49 ARG HG2 H 1 1.721 0.040 . 2 . . . . 46 ARG HG2 . 11032 1 614 . 1 1 49 49 ARG HG3 H 1 1.622 0.040 . 2 . . . . 46 ARG HG3 . 11032 1 615 . 1 1 49 49 ARG CD C 13 42.942 0.450 . 1 . . . . 46 ARG CD . 11032 1 616 . 1 1 49 49 ARG HD2 H 1 3.185 0.040 . 2 . . . . 46 ARG HD2 . 11032 1 617 . 1 1 49 49 ARG HD3 H 1 3.185 0.040 . 2 . . . . 46 ARG HD3 . 11032 1 618 . 1 1 49 49 ARG C C 13 176.950 0.450 . 1 . . . . 46 ARG C . 11032 1 619 . 1 1 50 50 LYS N N 15 116.589 0.450 . 1 . . . . 47 LYS N . 11032 1 620 . 1 1 50 50 LYS H H 1 7.230 0.040 . 1 . . . . 47 LYS H . 11032 1 621 . 1 1 50 50 LYS CA C 13 54.094 0.450 . 1 . . . . 47 LYS CA . 11032 1 622 . 1 1 50 50 LYS HA H 1 4.335 0.040 . 1 . . . . 47 LYS HA . 11032 1 623 . 1 1 50 50 LYS CB C 13 34.709 0.450 . 1 . . . . 47 LYS CB . 11032 1 624 . 1 1 50 50 LYS HB2 H 1 1.711 0.040 . 2 . . . . 47 LYS HB2 . 11032 1 625 . 1 1 50 50 LYS HB3 H 1 1.490 0.040 . 2 . . . . 47 LYS HB3 . 11032 1 626 . 1 1 50 50 LYS CG C 13 24.458 0.450 . 1 . . . . 47 LYS CG . 11032 1 627 . 1 1 50 50 LYS HG2 H 1 1.239 0.040 . 2 . . . . 47 LYS HG2 . 11032 1 628 . 1 1 50 50 LYS HG3 H 1 1.239 0.040 . 2 . . . . 47 LYS HG3 . 11032 1 629 . 1 1 50 50 LYS CD C 13 28.469 0.450 . 1 . . . . 47 LYS CD . 11032 1 630 . 1 1 50 50 LYS HD2 H 1 1.600 0.040 . 2 . . . . 47 LYS HD2 . 11032 1 631 . 1 1 50 50 LYS HD3 H 1 1.537 0.040 . 2 . . . . 47 LYS HD3 . 11032 1 632 . 1 1 50 50 LYS CE C 13 41.409 0.450 . 1 . . . . 47 LYS CE . 11032 1 633 . 1 1 50 50 LYS HE2 H 1 2.863 0.040 . 2 . . . . 47 LYS HE2 . 11032 1 634 . 1 1 50 50 LYS HE3 H 1 2.838 0.040 . 2 . . . . 47 LYS HE3 . 11032 1 635 . 1 1 50 50 LYS C C 13 173.662 0.450 . 1 . . . . 47 LYS C . 11032 1 636 . 1 1 51 51 ALA N N 15 123.569 0.450 . 1 . . . . 48 ALA N . 11032 1 637 . 1 1 51 51 ALA H H 1 8.158 0.040 . 1 . . . . 48 ALA H . 11032 1 638 . 1 1 51 51 ALA CA C 13 48.844 0.450 . 1 . . . . 48 ALA CA . 11032 1 639 . 1 1 51 51 ALA HA H 1 4.413 0.040 . 1 . . . . 48 ALA HA . 11032 1 640 . 1 1 51 51 ALA HB1 H 1 1.268 0.040 . 1 . . . . 48 ALA HB . 11032 1 641 . 1 1 51 51 ALA HB2 H 1 1.268 0.040 . 1 . . . . 48 ALA HB . 11032 1 642 . 1 1 51 51 ALA HB3 H 1 1.268 0.040 . 1 . . . . 48 ALA HB . 11032 1 643 . 1 1 51 51 ALA CB C 13 19.620 0.450 . 1 . . . . 48 ALA CB . 11032 1 644 . 1 1 52 52 PRO CD C 13 50.172 0.450 . 1 . . . . 49 PRO CD . 11032 1 645 . 1 1 52 52 PRO CA C 13 61.960 0.450 . 1 . . . . 49 PRO CA . 11032 1 646 . 1 1 52 52 PRO HA H 1 4.961 0.040 . 1 . . . . 49 PRO HA . 11032 1 647 . 1 1 52 52 PRO CB C 13 32.580 0.450 . 1 . . . . 49 PRO CB . 11032 1 648 . 1 1 52 52 PRO HB2 H 1 2.578 0.040 . 2 . . . . 49 PRO HB2 . 11032 1 649 . 1 1 52 52 PRO HB3 H 1 2.340 0.040 . 2 . . . . 49 PRO HB3 . 11032 1 650 . 1 1 52 52 PRO CG C 13 25.093 0.450 . 1 . . . . 49 PRO CG . 11032 1 651 . 1 1 52 52 PRO HG2 H 1 2.015 0.040 . 2 . . . . 49 PRO HG2 . 11032 1 652 . 1 1 52 52 PRO HG3 H 1 2.015 0.040 . 2 . . . . 49 PRO HG3 . 11032 1 653 . 1 1 52 52 PRO HD2 H 1 3.586 0.040 . 2 . . . . 49 PRO HD2 . 11032 1 654 . 1 1 52 52 PRO HD3 H 1 3.564 0.040 . 2 . . . . 49 PRO HD3 . 11032 1 655 . 1 1 53 53 PRO CD C 13 50.336 0.450 . 1 . . . . 50 PRO CD . 11032 1 656 . 1 1 53 53 PRO CA C 13 62.909 0.450 . 1 . . . . 50 PRO CA . 11032 1 657 . 1 1 53 53 PRO HA H 1 4.553 0.040 . 1 . . . . 50 PRO HA . 11032 1 658 . 1 1 53 53 PRO CB C 13 32.438 0.450 . 1 . . . . 50 PRO CB . 11032 1 659 . 1 1 53 53 PRO HB2 H 1 1.990 0.040 . 2 . . . . 50 PRO HB2 . 11032 1 660 . 1 1 53 53 PRO HB3 H 1 1.385 0.040 . 2 . . . . 50 PRO HB3 . 11032 1 661 . 1 1 53 53 PRO CG C 13 27.413 0.450 . 1 . . . . 50 PRO CG . 11032 1 662 . 1 1 53 53 PRO HG2 H 1 2.007 0.040 . 2 . . . . 50 PRO HG2 . 11032 1 663 . 1 1 53 53 PRO HG3 H 1 1.943 0.040 . 2 . . . . 50 PRO HG3 . 11032 1 664 . 1 1 53 53 PRO HD2 H 1 3.697 0.040 . 2 . . . . 50 PRO HD2 . 11032 1 665 . 1 1 53 53 PRO HD3 H 1 3.796 0.040 . 2 . . . . 50 PRO HD3 . 11032 1 666 . 1 1 53 53 PRO C C 13 175.647 0.450 . 1 . . . . 50 PRO C . 11032 1 667 . 1 1 54 54 LYS N N 15 115.089 0.450 . 1 . . . . 51 LYS N . 11032 1 668 . 1 1 54 54 LYS H H 1 7.485 0.040 . 1 . . . . 51 LYS H . 11032 1 669 . 1 1 54 54 LYS CA C 13 54.603 0.450 . 1 . . . . 51 LYS CA . 11032 1 670 . 1 1 54 54 LYS HA H 1 5.184 0.040 . 1 . . . . 51 LYS HA . 11032 1 671 . 1 1 54 54 LYS CB C 13 37.252 0.450 . 1 . . . . 51 LYS CB . 11032 1 672 . 1 1 54 54 LYS HB2 H 1 1.547 0.040 . 2 . . . . 51 LYS HB2 . 11032 1 673 . 1 1 54 54 LYS HB3 H 1 2.102 0.040 . 2 . . . . 51 LYS HB3 . 11032 1 674 . 1 1 54 54 LYS CG C 13 25.626 0.450 . 1 . . . . 51 LYS CG . 11032 1 675 . 1 1 54 54 LYS HG2 H 1 1.589 0.040 . 2 . . . . 51 LYS HG2 . 11032 1 676 . 1 1 54 54 LYS HG3 H 1 1.424 0.040 . 2 . . . . 51 LYS HG3 . 11032 1 677 . 1 1 54 54 LYS CD C 13 29.621 0.450 . 1 . . . . 51 LYS CD . 11032 1 678 . 1 1 54 54 LYS HD2 H 1 1.503 0.040 . 2 . . . . 51 LYS HD2 . 11032 1 679 . 1 1 54 54 LYS HD3 H 1 1.503 0.040 . 2 . . . . 51 LYS HD3 . 11032 1 680 . 1 1 54 54 LYS CE C 13 41.374 0.450 . 1 . . . . 51 LYS CE . 11032 1 681 . 1 1 54 54 LYS HE2 H 1 2.729 0.040 . 2 . . . . 51 LYS HE2 . 11032 1 682 . 1 1 54 54 LYS HE3 H 1 2.678 0.040 . 2 . . . . 51 LYS HE3 . 11032 1 683 . 1 1 54 54 LYS C C 13 175.199 0.450 . 1 . . . . 51 LYS C . 11032 1 684 . 1 1 55 55 PHE N N 15 118.341 0.450 . 1 . . . . 52 PHE N . 11032 1 685 . 1 1 55 55 PHE H H 1 8.854 0.040 . 1 . . . . 52 PHE H . 11032 1 686 . 1 1 55 55 PHE CA C 13 56.156 0.450 . 1 . . . . 52 PHE CA . 11032 1 687 . 1 1 55 55 PHE HA H 1 5.317 0.040 . 1 . . . . 52 PHE HA . 11032 1 688 . 1 1 55 55 PHE CB C 13 41.344 0.450 . 1 . . . . 52 PHE CB . 11032 1 689 . 1 1 55 55 PHE HB2 H 1 2.662 0.040 . 2 . . . . 52 PHE HB2 . 11032 1 690 . 1 1 55 55 PHE HB3 H 1 2.732 0.040 . 2 . . . . 52 PHE HB3 . 11032 1 691 . 1 1 55 55 PHE CD1 C 13 131.613 0.450 . 1 . . . . 52 PHE CD1 . 11032 1 692 . 1 1 55 55 PHE HD1 H 1 7.019 0.040 . 1 . . . . 52 PHE HD1 . 11032 1 693 . 1 1 55 55 PHE CE1 C 13 131.574 0.450 . 1 . . . . 52 PHE CE1 . 11032 1 694 . 1 1 55 55 PHE HE1 H 1 7.201 0.040 . 1 . . . . 52 PHE HE1 . 11032 1 695 . 1 1 55 55 PHE CZ C 13 129.444 0.450 . 1 . . . . 52 PHE CZ . 11032 1 696 . 1 1 55 55 PHE HZ H 1 7.138 0.040 . 1 . . . . 52 PHE HZ . 11032 1 697 . 1 1 55 55 PHE CE2 C 13 131.574 0.450 . 1 . . . . 52 PHE CE2 . 11032 1 698 . 1 1 55 55 PHE HE2 H 1 7.201 0.040 . 1 . . . . 52 PHE HE2 . 11032 1 699 . 1 1 55 55 PHE CD2 C 13 131.613 0.450 . 1 . . . . 52 PHE CD2 . 11032 1 700 . 1 1 55 55 PHE HD2 H 1 7.019 0.040 . 1 . . . . 52 PHE HD2 . 11032 1 701 . 1 1 55 55 PHE C C 13 172.973 0.450 . 1 . . . . 52 PHE C . 11032 1 702 . 1 1 56 56 TYR N N 15 129.145 0.450 . 1 . . . . 53 TYR N . 11032 1 703 . 1 1 56 56 TYR H H 1 8.725 0.040 . 1 . . . . 53 TYR H . 11032 1 704 . 1 1 56 56 TYR CA C 13 56.381 0.450 . 1 . . . . 53 TYR CA . 11032 1 705 . 1 1 56 56 TYR HA H 1 4.369 0.040 . 1 . . . . 53 TYR HA . 11032 1 706 . 1 1 56 56 TYR CB C 13 37.707 0.450 . 1 . . . . 53 TYR CB . 11032 1 707 . 1 1 56 56 TYR HB2 H 1 1.950 0.040 . 2 . . . . 53 TYR HB2 . 11032 1 708 . 1 1 56 56 TYR HB3 H 1 -0.030 0.040 . 2 . . . . 53 TYR HB3 . 11032 1 709 . 1 1 56 56 TYR CD1 C 13 132.425 0.450 . 1 . . . . 53 TYR CD1 . 11032 1 710 . 1 1 56 56 TYR HD1 H 1 5.646 0.040 . 1 . . . . 53 TYR HD1 . 11032 1 711 . 1 1 56 56 TYR CE1 C 13 116.767 0.450 . 1 . . . . 53 TYR CE1 . 11032 1 712 . 1 1 56 56 TYR HE1 H 1 6.444 0.040 . 1 . . . . 53 TYR HE1 . 11032 1 713 . 1 1 56 56 TYR CE2 C 13 116.767 0.450 . 1 . . . . 53 TYR CE2 . 11032 1 714 . 1 1 56 56 TYR HE2 H 1 6.444 0.040 . 1 . . . . 53 TYR HE2 . 11032 1 715 . 1 1 56 56 TYR CD2 C 13 132.425 0.450 . 1 . . . . 53 TYR CD2 . 11032 1 716 . 1 1 56 56 TYR HD2 H 1 5.646 0.040 . 1 . . . . 53 TYR HD2 . 11032 1 717 . 1 1 56 56 TYR C C 13 175.421 0.450 . 1 . . . . 53 TYR C . 11032 1 718 . 1 1 57 57 VAL N N 15 119.533 0.450 . 1 . . . . 54 VAL N . 11032 1 719 . 1 1 57 57 VAL H H 1 8.294 0.040 . 1 . . . . 54 VAL H . 11032 1 720 . 1 1 57 57 VAL CA C 13 57.709 0.450 . 1 . . . . 54 VAL CA . 11032 1 721 . 1 1 57 57 VAL HA H 1 5.158 0.040 . 1 . . . . 54 VAL HA . 11032 1 722 . 1 1 57 57 VAL CB C 13 34.818 0.450 . 1 . . . . 54 VAL CB . 11032 1 723 . 1 1 57 57 VAL HB H 1 1.404 0.040 . 1 . . . . 54 VAL HB . 11032 1 724 . 1 1 57 57 VAL HG11 H 1 0.515 0.040 . 2 . . . . 54 VAL HG1 . 11032 1 725 . 1 1 57 57 VAL HG12 H 1 0.515 0.040 . 2 . . . . 54 VAL HG1 . 11032 1 726 . 1 1 57 57 VAL HG13 H 1 0.515 0.040 . 2 . . . . 54 VAL HG1 . 11032 1 727 . 1 1 57 57 VAL HG21 H 1 0.195 0.040 . 2 . . . . 54 VAL HG2 . 11032 1 728 . 1 1 57 57 VAL HG22 H 1 0.195 0.040 . 2 . . . . 54 VAL HG2 . 11032 1 729 . 1 1 57 57 VAL HG23 H 1 0.195 0.040 . 2 . . . . 54 VAL HG2 . 11032 1 730 . 1 1 57 57 VAL CG1 C 13 21.187 0.450 . 1 . . . . 54 VAL CG1 . 11032 1 731 . 1 1 57 57 VAL CG2 C 13 17.192 0.450 . 1 . . . . 54 VAL CG2 . 11032 1 732 . 1 1 57 57 VAL C C 13 172.278 0.450 . 1 . . . . 54 VAL C . 11032 1 733 . 1 1 58 58 HIS N N 15 115.772 0.450 . 1 . . . . 55 HIS N . 11032 1 734 . 1 1 58 58 HIS H H 1 8.030 0.040 . 1 . . . . 55 HIS H . 11032 1 735 . 1 1 58 58 HIS CA C 13 52.507 0.450 . 1 . . . . 55 HIS CA . 11032 1 736 . 1 1 58 58 HIS HA H 1 4.896 0.040 . 1 . . . . 55 HIS HA . 11032 1 737 . 1 1 58 58 HIS CB C 13 31.460 0.450 . 1 . . . . 55 HIS CB . 11032 1 738 . 1 1 58 58 HIS HB2 H 1 2.975 0.040 . 2 . . . . 55 HIS HB2 . 11032 1 739 . 1 1 58 58 HIS HB3 H 1 2.707 0.040 . 2 . . . . 55 HIS HB3 . 11032 1 740 . 1 1 58 58 HIS CD2 C 13 119.311 0.450 . 1 . . . . 55 HIS CD2 . 11032 1 741 . 1 1 58 58 HIS CE1 C 13 135.926 0.450 . 1 . . . . 55 HIS CE1 . 11032 1 742 . 1 1 58 58 HIS HD2 H 1 7.081 0.040 . 1 . . . . 55 HIS HD2 . 11032 1 743 . 1 1 58 58 HIS HE1 H 1 7.491 0.040 . 1 . . . . 55 HIS HE1 . 11032 1 744 . 1 1 58 58 HIS C C 13 174.318 0.450 . 1 . . . . 55 HIS C . 11032 1 745 . 1 1 59 59 TYR N N 15 127.663 0.450 . 1 . . . . 56 TYR N . 11032 1 746 . 1 1 59 59 TYR H H 1 8.211 0.040 . 1 . . . . 56 TYR H . 11032 1 747 . 1 1 59 59 TYR CA C 13 58.913 0.450 . 1 . . . . 56 TYR CA . 11032 1 748 . 1 1 59 59 TYR HA H 1 4.281 0.040 . 1 . . . . 56 TYR HA . 11032 1 749 . 1 1 59 59 TYR CB C 13 36.403 0.450 . 1 . . . . 56 TYR CB . 11032 1 750 . 1 1 59 59 TYR HB2 H 1 2.485 0.040 . 2 . . . . 56 TYR HB2 . 11032 1 751 . 1 1 59 59 TYR HB3 H 1 2.485 0.040 . 2 . . . . 56 TYR HB3 . 11032 1 752 . 1 1 59 59 TYR CD1 C 13 132.913 0.450 . 1 . . . . 56 TYR CD1 . 11032 1 753 . 1 1 59 59 TYR HD1 H 1 6.741 0.040 . 1 . . . . 56 TYR HD1 . 11032 1 754 . 1 1 59 59 TYR CE1 C 13 117.138 0.450 . 1 . . . . 56 TYR CE1 . 11032 1 755 . 1 1 59 59 TYR HE1 H 1 6.494 0.040 . 1 . . . . 56 TYR HE1 . 11032 1 756 . 1 1 59 59 TYR CE2 C 13 117.138 0.450 . 1 . . . . 56 TYR CE2 . 11032 1 757 . 1 1 59 59 TYR HE2 H 1 6.494 0.040 . 1 . . . . 56 TYR HE2 . 11032 1 758 . 1 1 59 59 TYR CD2 C 13 132.913 0.450 . 1 . . . . 56 TYR CD2 . 11032 1 759 . 1 1 59 59 TYR HD2 H 1 6.741 0.040 . 1 . . . . 56 TYR HD2 . 11032 1 760 . 1 1 60 60 VAL CA C 13 65.183 0.450 . 1 . . . . 57 VAL CA . 11032 1 761 . 1 1 60 60 VAL HA H 1 3.357 0.040 . 1 . . . . 57 VAL HA . 11032 1 762 . 1 1 60 60 VAL CB C 13 31.181 0.450 . 1 . . . . 57 VAL CB . 11032 1 763 . 1 1 60 60 VAL HB H 1 1.695 0.040 . 1 . . . . 57 VAL HB . 11032 1 764 . 1 1 60 60 VAL HG11 H 1 0.884 0.040 . 2 . . . . 57 VAL HG1 . 11032 1 765 . 1 1 60 60 VAL HG12 H 1 0.884 0.040 . 2 . . . . 57 VAL HG1 . 11032 1 766 . 1 1 60 60 VAL HG13 H 1 0.884 0.040 . 2 . . . . 57 VAL HG1 . 11032 1 767 . 1 1 60 60 VAL HG21 H 1 0.786 0.040 . 2 . . . . 57 VAL HG2 . 11032 1 768 . 1 1 60 60 VAL HG22 H 1 0.786 0.040 . 2 . . . . 57 VAL HG2 . 11032 1 769 . 1 1 60 60 VAL HG23 H 1 0.786 0.040 . 2 . . . . 57 VAL HG2 . 11032 1 770 . 1 1 60 60 VAL CG1 C 13 20.497 0.450 . 1 . . . . 57 VAL CG1 . 11032 1 771 . 1 1 60 60 VAL CG2 C 13 20.909 0.450 . 1 . . . . 57 VAL CG2 . 11032 1 772 . 1 1 60 60 VAL C C 13 177.832 0.450 . 1 . . . . 57 VAL C . 11032 1 773 . 1 1 61 61 ASN N N 15 118.666 0.450 . 1 . . . . 58 ASN N . 11032 1 774 . 1 1 61 61 ASN H H 1 9.158 0.040 . 1 . . . . 58 ASN H . 11032 1 775 . 1 1 61 61 ASN CA C 13 55.359 0.450 . 1 . . . . 58 ASN CA . 11032 1 776 . 1 1 61 61 ASN CG C 13 177.606 0.450 . 1 . . . . 58 ASN CG . 11032 1 777 . 1 1 61 61 ASN ND2 N 15 113.570 0.450 . 1 . . . . 58 ASN ND2 . 11032 1 778 . 1 1 61 61 ASN HD21 H 1 7.555 0.040 . 2 . . . . 58 ASN HD21 . 11032 1 779 . 1 1 61 61 ASN HD22 H 1 6.964 0.040 . 2 . . . . 58 ASN HD22 . 11032 1 780 . 1 1 61 61 ASN C C 13 174.523 0.450 . 1 . . . . 58 ASN C . 11032 1 781 . 1 1 62 62 TYR N N 15 118.289 0.450 . 1 . . . . 59 TYR N . 11032 1 782 . 1 1 62 62 TYR H H 1 8.228 0.040 . 1 . . . . 59 TYR H . 11032 1 783 . 1 1 62 62 TYR CA C 13 57.225 0.450 . 1 . . . . 59 TYR CA . 11032 1 784 . 1 1 62 62 TYR HA H 1 4.670 0.040 . 1 . . . . 59 TYR HA . 11032 1 785 . 1 1 62 62 TYR CB C 13 40.994 0.450 . 1 . . . . 59 TYR CB . 11032 1 786 . 1 1 62 62 TYR HB2 H 1 3.006 0.040 . 2 . . . . 59 TYR HB2 . 11032 1 787 . 1 1 62 62 TYR HB3 H 1 3.006 0.040 . 2 . . . . 59 TYR HB3 . 11032 1 788 . 1 1 62 62 TYR CD1 C 13 133.689 0.450 . 1 . . . . 59 TYR CD1 . 11032 1 789 . 1 1 62 62 TYR HD1 H 1 7.011 0.040 . 1 . . . . 59 TYR HD1 . 11032 1 790 . 1 1 62 62 TYR CE1 C 13 117.396 0.450 . 1 . . . . 59 TYR CE1 . 11032 1 791 . 1 1 62 62 TYR HE1 H 1 6.740 0.040 . 1 . . . . 59 TYR HE1 . 11032 1 792 . 1 1 62 62 TYR CE2 C 13 117.396 0.450 . 1 . . . . 59 TYR CE2 . 11032 1 793 . 1 1 62 62 TYR HE2 H 1 6.740 0.040 . 1 . . . . 59 TYR HE2 . 11032 1 794 . 1 1 62 62 TYR CD2 C 13 133.689 0.450 . 1 . . . . 59 TYR CD2 . 11032 1 795 . 1 1 62 62 TYR HD2 H 1 7.011 0.040 . 1 . . . . 59 TYR HD2 . 11032 1 796 . 1 1 62 62 TYR C C 13 175.424 0.450 . 1 . . . . 59 TYR C . 11032 1 797 . 1 1 63 63 ASN N N 15 119.626 0.450 . 1 . . . . 60 ASN N . 11032 1 798 . 1 1 63 63 ASN H H 1 8.749 0.040 . 1 . . . . 60 ASN H . 11032 1 799 . 1 1 63 63 ASN CA C 13 54.557 0.450 . 1 . . . . 60 ASN CA . 11032 1 800 . 1 1 63 63 ASN HA H 1 4.634 0.040 . 1 . . . . 60 ASN HA . 11032 1 801 . 1 1 63 63 ASN CB C 13 40.181 0.450 . 1 . . . . 60 ASN CB . 11032 1 802 . 1 1 63 63 ASN HB2 H 1 3.007 0.040 . 2 . . . . 60 ASN HB2 . 11032 1 803 . 1 1 63 63 ASN HB3 H 1 2.668 0.040 . 2 . . . . 60 ASN HB3 . 11032 1 804 . 1 1 63 63 ASN CG C 13 176.736 0.450 . 1 . . . . 60 ASN CG . 11032 1 805 . 1 1 63 63 ASN ND2 N 15 115.349 0.450 . 1 . . . . 60 ASN ND2 . 11032 1 806 . 1 1 63 63 ASN HD21 H 1 8.128 0.040 . 2 . . . . 60 ASN HD21 . 11032 1 807 . 1 1 63 63 ASN HD22 H 1 7.218 0.040 . 2 . . . . 60 ASN HD22 . 11032 1 808 . 1 1 63 63 ASN C C 13 177.131 0.450 . 1 . . . . 60 ASN C . 11032 1 809 . 1 1 64 64 LYS N N 15 125.718 0.450 . 1 . . . . 61 LYS N . 11032 1 810 . 1 1 64 64 LYS H H 1 9.068 0.040 . 1 . . . . 61 LYS H . 11032 1 811 . 1 1 64 64 LYS CA C 13 58.133 0.450 . 1 . . . . 61 LYS CA . 11032 1 812 . 1 1 64 64 LYS HA H 1 4.551 0.040 . 1 . . . . 61 LYS HA . 11032 1 813 . 1 1 64 64 LYS CB C 13 32.189 0.450 . 1 . . . . 61 LYS CB . 11032 1 814 . 1 1 64 64 LYS HB2 H 1 1.981 0.040 . 2 . . . . 61 LYS HB2 . 11032 1 815 . 1 1 64 64 LYS HB3 H 1 1.834 0.040 . 2 . . . . 61 LYS HB3 . 11032 1 816 . 1 1 64 64 LYS CG C 13 24.317 0.450 . 1 . . . . 61 LYS CG . 11032 1 817 . 1 1 64 64 LYS HG2 H 1 1.497 0.040 . 2 . . . . 61 LYS HG2 . 11032 1 818 . 1 1 64 64 LYS HG3 H 1 1.431 0.040 . 2 . . . . 61 LYS HG3 . 11032 1 819 . 1 1 64 64 LYS CD C 13 29.263 0.450 . 1 . . . . 61 LYS CD . 11032 1 820 . 1 1 64 64 LYS HD2 H 1 1.663 0.040 . 2 . . . . 61 LYS HD2 . 11032 1 821 . 1 1 64 64 LYS HD3 H 1 1.663 0.040 . 2 . . . . 61 LYS HD3 . 11032 1 822 . 1 1 64 64 LYS CE C 13 41.445 0.450 . 1 . . . . 61 LYS CE . 11032 1 823 . 1 1 64 64 LYS HE2 H 1 2.968 0.040 . 2 . . . . 61 LYS HE2 . 11032 1 824 . 1 1 64 64 LYS HE3 H 1 2.968 0.040 . 2 . . . . 61 LYS HE3 . 11032 1 825 . 1 1 64 64 LYS C C 13 177.841 0.450 . 1 . . . . 61 LYS C . 11032 1 826 . 1 1 65 65 ARG N N 15 121.445 0.450 . 1 . . . . 62 ARG N . 11032 1 827 . 1 1 65 65 ARG H H 1 9.330 0.040 . 1 . . . . 62 ARG H . 11032 1 828 . 1 1 65 65 ARG CA C 13 58.249 0.450 . 1 . . . . 62 ARG CA . 11032 1 829 . 1 1 65 65 ARG HA H 1 4.279 0.040 . 1 . . . . 62 ARG HA . 11032 1 830 . 1 1 65 65 ARG CB C 13 29.312 0.450 . 1 . . . . 62 ARG CB . 11032 1 831 . 1 1 65 65 ARG HB2 H 1 1.935 0.040 . 2 . . . . 62 ARG HB2 . 11032 1 832 . 1 1 65 65 ARG HB3 H 1 1.871 0.040 . 2 . . . . 62 ARG HB3 . 11032 1 833 . 1 1 65 65 ARG CG C 13 27.591 0.450 . 1 . . . . 62 ARG CG . 11032 1 834 . 1 1 65 65 ARG HG2 H 1 1.680 0.040 . 2 . . . . 62 ARG HG2 . 11032 1 835 . 1 1 65 65 ARG HG3 H 1 1.680 0.040 . 2 . . . . 62 ARG HG3 . 11032 1 836 . 1 1 65 65 ARG CD C 13 43.031 0.450 . 1 . . . . 62 ARG CD . 11032 1 837 . 1 1 65 65 ARG HD2 H 1 3.225 0.040 . 2 . . . . 62 ARG HD2 . 11032 1 838 . 1 1 65 65 ARG HD3 H 1 3.189 0.040 . 2 . . . . 62 ARG HD3 . 11032 1 839 . 1 1 65 65 ARG C C 13 177.176 0.450 . 1 . . . . 62 ARG C . 11032 1 840 . 1 1 66 66 LEU N N 15 118.911 0.450 . 1 . . . . 63 LEU N . 11032 1 841 . 1 1 66 66 LEU H H 1 7.824 0.040 . 1 . . . . 63 LEU H . 11032 1 842 . 1 1 66 66 LEU CA C 13 54.575 0.450 . 1 . . . . 63 LEU CA . 11032 1 843 . 1 1 66 66 LEU HA H 1 4.423 0.040 . 1 . . . . 63 LEU HA . 11032 1 844 . 1 1 66 66 LEU CB C 13 42.177 0.450 . 1 . . . . 63 LEU CB . 11032 1 845 . 1 1 66 66 LEU HB2 H 1 2.116 0.040 . 2 . . . . 63 LEU HB2 . 11032 1 846 . 1 1 66 66 LEU HB3 H 1 1.771 0.040 . 2 . . . . 63 LEU HB3 . 11032 1 847 . 1 1 66 66 LEU CG C 13 27.911 0.450 . 1 . . . . 63 LEU CG . 11032 1 848 . 1 1 66 66 LEU HG H 1 1.672 0.040 . 1 . . . . 63 LEU HG . 11032 1 849 . 1 1 66 66 LEU HD11 H 1 0.996 0.040 . 2 . . . . 63 LEU HD1 . 11032 1 850 . 1 1 66 66 LEU HD12 H 1 0.996 0.040 . 2 . . . . 63 LEU HD1 . 11032 1 851 . 1 1 66 66 LEU HD13 H 1 0.996 0.040 . 2 . . . . 63 LEU HD1 . 11032 1 852 . 1 1 66 66 LEU HD21 H 1 0.829 0.040 . 2 . . . . 63 LEU HD2 . 11032 1 853 . 1 1 66 66 LEU HD22 H 1 0.829 0.040 . 2 . . . . 63 LEU HD2 . 11032 1 854 . 1 1 66 66 LEU HD23 H 1 0.829 0.040 . 2 . . . . 63 LEU HD2 . 11032 1 855 . 1 1 66 66 LEU CD1 C 13 25.879 0.450 . 1 . . . . 63 LEU CD1 . 11032 1 856 . 1 1 66 66 LEU CD2 C 13 23.051 0.450 . 1 . . . . 63 LEU CD2 . 11032 1 857 . 1 1 66 66 LEU C C 13 176.079 0.450 . 1 . . . . 63 LEU C . 11032 1 858 . 1 1 67 67 ASP N N 15 122.191 0.450 . 1 . . . . 64 ASP N . 11032 1 859 . 1 1 67 67 ASP H H 1 7.636 0.040 . 1 . . . . 64 ASP H . 11032 1 860 . 1 1 67 67 ASP CA C 13 55.736 0.450 . 1 . . . . 64 ASP CA . 11032 1 861 . 1 1 67 67 ASP HA H 1 4.466 0.040 . 1 . . . . 64 ASP HA . 11032 1 862 . 1 1 67 67 ASP CB C 13 38.724 0.450 . 1 . . . . 64 ASP CB . 11032 1 863 . 1 1 67 67 ASP HB2 H 1 2.637 0.040 . 2 . . . . 64 ASP HB2 . 11032 1 864 . 1 1 67 67 ASP HB3 H 1 2.203 0.040 . 2 . . . . 64 ASP HB3 . 11032 1 865 . 1 1 67 67 ASP C C 13 176.509 0.450 . 1 . . . . 64 ASP C . 11032 1 866 . 1 1 68 68 GLU N N 15 115.669 0.450 . 1 . . . . 65 GLU N . 11032 1 867 . 1 1 68 68 GLU H H 1 7.522 0.040 . 1 . . . . 65 GLU H . 11032 1 868 . 1 1 68 68 GLU CA C 13 54.793 0.450 . 1 . . . . 65 GLU CA . 11032 1 869 . 1 1 68 68 GLU HA H 1 4.842 0.040 . 1 . . . . 65 GLU HA . 11032 1 870 . 1 1 68 68 GLU CB C 13 32.207 0.450 . 1 . . . . 65 GLU CB . 11032 1 871 . 1 1 68 68 GLU HB2 H 1 2.154 0.040 . 2 . . . . 65 GLU HB2 . 11032 1 872 . 1 1 68 68 GLU HB3 H 1 2.154 0.040 . 2 . . . . 65 GLU HB3 . 11032 1 873 . 1 1 68 68 GLU CG C 13 33.571 0.450 . 1 . . . . 65 GLU CG . 11032 1 874 . 1 1 68 68 GLU HG2 H 1 2.405 0.040 . 2 . . . . 65 GLU HG2 . 11032 1 875 . 1 1 68 68 GLU HG3 H 1 2.405 0.040 . 2 . . . . 65 GLU HG3 . 11032 1 876 . 1 1 68 68 GLU C C 13 174.319 0.450 . 1 . . . . 65 GLU C . 11032 1 877 . 1 1 69 69 TRP N N 15 120.329 0.450 . 1 . . . . 66 TRP N . 11032 1 878 . 1 1 69 69 TRP H H 1 8.802 0.040 . 1 . . . . 66 TRP H . 11032 1 879 . 1 1 69 69 TRP CA C 13 56.785 0.450 . 1 . . . . 66 TRP CA . 11032 1 880 . 1 1 69 69 TRP HA H 1 5.450 0.040 . 1 . . . . 66 TRP HA . 11032 1 881 . 1 1 69 69 TRP CB C 13 30.215 0.450 . 1 . . . . 66 TRP CB . 11032 1 882 . 1 1 69 69 TRP HB2 H 1 3.307 0.040 . 2 . . . . 66 TRP HB2 . 11032 1 883 . 1 1 69 69 TRP HB3 H 1 3.036 0.040 . 2 . . . . 66 TRP HB3 . 11032 1 884 . 1 1 69 69 TRP CD1 C 13 128.255 0.450 . 1 . . . . 66 TRP CD1 . 11032 1 885 . 1 1 69 69 TRP CE3 C 13 120.370 0.450 . 1 . . . . 66 TRP CE3 . 11032 1 886 . 1 1 69 69 TRP NE1 N 15 131.585 0.450 . 1 . . . . 66 TRP NE1 . 11032 1 887 . 1 1 69 69 TRP HD1 H 1 7.533 0.040 . 1 . . . . 66 TRP HD1 . 11032 1 888 . 1 1 69 69 TRP HE3 H 1 7.412 0.040 . 1 . . . . 66 TRP HE3 . 11032 1 889 . 1 1 69 69 TRP CZ3 C 13 122.448 0.450 . 1 . . . . 66 TRP CZ3 . 11032 1 890 . 1 1 69 69 TRP CZ2 C 13 115.464 0.450 . 1 . . . . 66 TRP CZ2 . 11032 1 891 . 1 1 69 69 TRP HE1 H 1 10.169 0.040 . 1 . . . . 66 TRP HE1 . 11032 1 892 . 1 1 69 69 TRP HZ3 H 1 6.795 0.040 . 1 . . . . 66 TRP HZ3 . 11032 1 893 . 1 1 69 69 TRP CH2 C 13 123.988 0.450 . 1 . . . . 66 TRP CH2 . 11032 1 894 . 1 1 69 69 TRP HZ2 H 1 7.290 0.040 . 1 . . . . 66 TRP HZ2 . 11032 1 895 . 1 1 69 69 TRP HH2 H 1 7.048 0.040 . 1 . . . . 66 TRP HH2 . 11032 1 896 . 1 1 69 69 TRP C C 13 177.216 0.450 . 1 . . . . 66 TRP C . 11032 1 897 . 1 1 70 70 ILE N N 15 117.384 0.450 . 1 . . . . 67 ILE N . 11032 1 898 . 1 1 70 70 ILE H H 1 10.074 0.040 . 1 . . . . 67 ILE H . 11032 1 899 . 1 1 70 70 ILE CA C 13 59.192 0.450 . 1 . . . . 67 ILE CA . 11032 1 900 . 1 1 70 70 ILE HA H 1 5.101 0.040 . 1 . . . . 67 ILE HA . 11032 1 901 . 1 1 70 70 ILE CB C 13 42.507 0.450 . 1 . . . . 67 ILE CB . 11032 1 902 . 1 1 70 70 ILE HB H 1 1.938 0.040 . 1 . . . . 67 ILE HB . 11032 1 903 . 1 1 70 70 ILE HG21 H 1 0.923 0.040 . 1 . . . . 67 ILE HG2 . 11032 1 904 . 1 1 70 70 ILE HG22 H 1 0.923 0.040 . 1 . . . . 67 ILE HG2 . 11032 1 905 . 1 1 70 70 ILE HG23 H 1 0.923 0.040 . 1 . . . . 67 ILE HG2 . 11032 1 906 . 1 1 70 70 ILE CG2 C 13 18.133 0.450 . 1 . . . . 67 ILE CG2 . 11032 1 907 . 1 1 70 70 ILE CG1 C 13 26.353 0.450 . 1 . . . . 67 ILE CG1 . 11032 1 908 . 1 1 70 70 ILE HG12 H 1 1.580 0.040 . 2 . . . . 67 ILE HG12 . 11032 1 909 . 1 1 70 70 ILE HG13 H 1 1.305 0.040 . 2 . . . . 67 ILE HG13 . 11032 1 910 . 1 1 70 70 ILE HD11 H 1 0.703 0.040 . 1 . . . . 67 ILE HD1 . 11032 1 911 . 1 1 70 70 ILE HD12 H 1 0.703 0.040 . 1 . . . . 67 ILE HD1 . 11032 1 912 . 1 1 70 70 ILE HD13 H 1 0.703 0.040 . 1 . . . . 67 ILE HD1 . 11032 1 913 . 1 1 70 70 ILE CD1 C 13 15.897 0.450 . 1 . . . . 67 ILE CD1 . 11032 1 914 . 1 1 70 70 ILE C C 13 175.207 0.450 . 1 . . . . 67 ILE C . 11032 1 915 . 1 1 71 71 THR N N 15 109.497 0.450 . 1 . . . . 68 THR N . 11032 1 916 . 1 1 71 71 THR H H 1 7.331 0.040 . 1 . . . . 68 THR H . 11032 1 917 . 1 1 71 71 THR CA C 13 59.916 0.450 . 1 . . . . 68 THR CA . 11032 1 918 . 1 1 71 71 THR HA H 1 5.014 0.040 . 1 . . . . 68 THR HA . 11032 1 919 . 1 1 71 71 THR CB C 13 70.215 0.450 . 1 . . . . 68 THR CB . 11032 1 920 . 1 1 71 71 THR HB H 1 4.654 0.040 . 1 . . . . 68 THR HB . 11032 1 921 . 1 1 71 71 THR HG21 H 1 1.366 0.040 . 1 . . . . 68 THR HG2 . 11032 1 922 . 1 1 71 71 THR HG22 H 1 1.366 0.040 . 1 . . . . 68 THR HG2 . 11032 1 923 . 1 1 71 71 THR HG23 H 1 1.366 0.040 . 1 . . . . 68 THR HG2 . 11032 1 924 . 1 1 71 71 THR CG2 C 13 22.878 0.450 . 1 . . . . 68 THR CG2 . 11032 1 925 . 1 1 71 71 THR C C 13 176.737 0.450 . 1 . . . . 68 THR C . 11032 1 926 . 1 1 72 72 THR N N 15 114.999 0.450 . 1 . . . . 69 THR N . 11032 1 927 . 1 1 72 72 THR H H 1 9.002 0.040 . 1 . . . . 69 THR H . 11032 1 928 . 1 1 72 72 THR CA C 13 67.000 0.450 . 1 . . . . 69 THR CA . 11032 1 929 . 1 1 72 72 THR HA H 1 3.848 0.040 . 1 . . . . 69 THR HA . 11032 1 930 . 1 1 72 72 THR CB C 13 69.294 0.450 . 1 . . . . 69 THR CB . 11032 1 931 . 1 1 72 72 THR HB H 1 4.292 0.040 . 1 . . . . 69 THR HB . 11032 1 932 . 1 1 72 72 THR HG21 H 1 1.277 0.040 . 1 . . . . 69 THR HG2 . 11032 1 933 . 1 1 72 72 THR HG22 H 1 1.277 0.040 . 1 . . . . 69 THR HG2 . 11032 1 934 . 1 1 72 72 THR HG23 H 1 1.277 0.040 . 1 . . . . 69 THR HG2 . 11032 1 935 . 1 1 72 72 THR CG2 C 13 22.349 0.450 . 1 . . . . 69 THR CG2 . 11032 1 936 . 1 1 72 72 THR C C 13 175.904 0.450 . 1 . . . . 69 THR C . 11032 1 937 . 1 1 73 73 ASP N N 15 117.509 0.450 . 1 . . . . 70 ASP N . 11032 1 938 . 1 1 73 73 ASP H H 1 8.541 0.040 . 1 . . . . 70 ASP H . 11032 1 939 . 1 1 73 73 ASP CA C 13 55.265 0.450 . 1 . . . . 70 ASP CA . 11032 1 940 . 1 1 73 73 ASP HA H 1 4.446 0.040 . 1 . . . . 70 ASP HA . 11032 1 941 . 1 1 73 73 ASP CB C 13 39.851 0.450 . 1 . . . . 70 ASP CB . 11032 1 942 . 1 1 73 73 ASP HB2 H 1 2.783 0.040 . 2 . . . . 70 ASP HB2 . 11032 1 943 . 1 1 73 73 ASP HB3 H 1 2.741 0.040 . 2 . . . . 70 ASP HB3 . 11032 1 944 . 1 1 73 73 ASP C C 13 176.297 0.450 . 1 . . . . 70 ASP C . 11032 1 945 . 1 1 74 74 ARG N N 15 116.471 0.450 . 1 . . . . 71 ARG N . 11032 1 946 . 1 1 74 74 ARG H H 1 7.589 0.040 . 1 . . . . 71 ARG H . 11032 1 947 . 1 1 74 74 ARG CA C 13 55.987 0.450 . 1 . . . . 71 ARG CA . 11032 1 948 . 1 1 74 74 ARG HA H 1 4.367 0.040 . 1 . . . . 71 ARG HA . 11032 1 949 . 1 1 74 74 ARG CB C 13 30.784 0.450 . 1 . . . . 71 ARG CB . 11032 1 950 . 1 1 74 74 ARG HB2 H 1 1.991 0.040 . 2 . . . . 71 ARG HB2 . 11032 1 951 . 1 1 74 74 ARG HB3 H 1 2.443 0.040 . 2 . . . . 71 ARG HB3 . 11032 1 952 . 1 1 74 74 ARG CG C 13 26.840 0.450 . 1 . . . . 71 ARG CG . 11032 1 953 . 1 1 74 74 ARG HG2 H 1 1.805 0.040 . 2 . . . . 71 ARG HG2 . 11032 1 954 . 1 1 74 74 ARG HG3 H 1 1.939 0.040 . 2 . . . . 71 ARG HG3 . 11032 1 955 . 1 1 74 74 ARG CD C 13 43.449 0.450 . 1 . . . . 71 ARG CD . 11032 1 956 . 1 1 74 74 ARG HD2 H 1 3.287 0.040 . 2 . . . . 71 ARG HD2 . 11032 1 957 . 1 1 74 74 ARG HD3 H 1 3.406 0.040 . 2 . . . . 71 ARG HD3 . 11032 1 958 . 1 1 74 74 ARG NE N 15 82.937 0.450 . 1 . . . . 71 ARG NE . 11032 1 959 . 1 1 74 74 ARG HE H 1 7.159 0.040 . 1 . . . . 71 ARG HE . 11032 1 960 . 1 1 74 74 ARG CZ C 13 159.906 0.450 . 1 . . . . 71 ARG CZ . 11032 1 961 . 1 1 74 74 ARG C C 13 176.298 0.450 . 1 . . . . 71 ARG C . 11032 1 962 . 1 1 75 75 ILE N N 15 119.917 0.450 . 1 . . . . 72 ILE N . 11032 1 963 . 1 1 75 75 ILE H H 1 7.518 0.040 . 1 . . . . 72 ILE H . 11032 1 964 . 1 1 75 75 ILE CA C 13 61.888 0.450 . 1 . . . . 72 ILE CA . 11032 1 965 . 1 1 75 75 ILE HA H 1 4.157 0.040 . 1 . . . . 72 ILE HA . 11032 1 966 . 1 1 75 75 ILE CB C 13 38.214 0.450 . 1 . . . . 72 ILE CB . 11032 1 967 . 1 1 75 75 ILE HB H 1 1.798 0.040 . 1 . . . . 72 ILE HB . 11032 1 968 . 1 1 75 75 ILE HG21 H 1 0.671 0.040 . 1 . . . . 72 ILE HG2 . 11032 1 969 . 1 1 75 75 ILE HG22 H 1 0.671 0.040 . 1 . . . . 72 ILE HG2 . 11032 1 970 . 1 1 75 75 ILE HG23 H 1 0.671 0.040 . 1 . . . . 72 ILE HG2 . 11032 1 971 . 1 1 75 75 ILE CG2 C 13 17.224 0.450 . 1 . . . . 72 ILE CG2 . 11032 1 972 . 1 1 75 75 ILE CG1 C 13 28.333 0.450 . 1 . . . . 72 ILE CG1 . 11032 1 973 . 1 1 75 75 ILE HG12 H 1 1.511 0.040 . 2 . . . . 72 ILE HG12 . 11032 1 974 . 1 1 75 75 ILE HG13 H 1 0.695 0.040 . 2 . . . . 72 ILE HG13 . 11032 1 975 . 1 1 75 75 ILE HD11 H 1 0.269 0.040 . 1 . . . . 72 ILE HD1 . 11032 1 976 . 1 1 75 75 ILE HD12 H 1 0.269 0.040 . 1 . . . . 72 ILE HD1 . 11032 1 977 . 1 1 75 75 ILE HD13 H 1 0.269 0.040 . 1 . . . . 72 ILE HD1 . 11032 1 978 . 1 1 75 75 ILE CD1 C 13 13.225 0.450 . 1 . . . . 72 ILE CD1 . 11032 1 979 . 1 1 75 75 ILE C C 13 175.185 0.450 . 1 . . . . 72 ILE C . 11032 1 980 . 1 1 76 76 ASN N N 15 126.244 0.450 . 1 . . . . 73 ASN N . 11032 1 981 . 1 1 76 76 ASN H H 1 9.045 0.040 . 1 . . . . 73 ASN H . 11032 1 982 . 1 1 76 76 ASN CA C 13 51.652 0.450 . 1 . . . . 73 ASN CA . 11032 1 983 . 1 1 76 76 ASN HA H 1 4.843 0.040 . 1 . . . . 73 ASN HA . 11032 1 984 . 1 1 76 76 ASN CB C 13 37.028 0.450 . 1 . . . . 73 ASN CB . 11032 1 985 . 1 1 76 76 ASN HB2 H 1 3.140 0.040 . 2 . . . . 73 ASN HB2 . 11032 1 986 . 1 1 76 76 ASN HB3 H 1 2.621 0.040 . 2 . . . . 73 ASN HB3 . 11032 1 987 . 1 1 76 76 ASN CG C 13 177.394 0.450 . 1 . . . . 73 ASN CG . 11032 1 988 . 1 1 76 76 ASN ND2 N 15 112.467 0.450 . 1 . . . . 73 ASN ND2 . 11032 1 989 . 1 1 76 76 ASN HD21 H 1 8.820 0.040 . 2 . . . . 73 ASN HD21 . 11032 1 990 . 1 1 76 76 ASN HD22 H 1 7.089 0.040 . 2 . . . . 73 ASN HD22 . 11032 1 991 . 1 1 76 76 ASN C C 13 175.858 0.450 . 1 . . . . 73 ASN C . 11032 1 992 . 1 1 77 77 LEU N N 15 124.765 0.450 . 1 . . . . 74 LEU N . 11032 1 993 . 1 1 77 77 LEU H H 1 8.598 0.040 . 1 . . . . 74 LEU H . 11032 1 994 . 1 1 77 77 LEU CA C 13 55.051 0.450 . 1 . . . . 74 LEU CA . 11032 1 995 . 1 1 77 77 LEU HA H 1 4.484 0.040 . 1 . . . . 74 LEU HA . 11032 1 996 . 1 1 77 77 LEU CB C 13 40.115 0.450 . 1 . . . . 74 LEU CB . 11032 1 997 . 1 1 77 77 LEU HB2 H 1 1.844 0.040 . 2 . . . . 74 LEU HB2 . 11032 1 998 . 1 1 77 77 LEU HB3 H 1 1.728 0.040 . 2 . . . . 74 LEU HB3 . 11032 1 999 . 1 1 77 77 LEU CG C 13 26.484 0.450 . 1 . . . . 74 LEU CG . 11032 1 1000 . 1 1 77 77 LEU HG H 1 1.618 0.040 . 1 . . . . 74 LEU HG . 11032 1 1001 . 1 1 77 77 LEU HD11 H 1 0.765 0.040 . 2 . . . . 74 LEU HD1 . 11032 1 1002 . 1 1 77 77 LEU HD12 H 1 0.765 0.040 . 2 . . . . 74 LEU HD1 . 11032 1 1003 . 1 1 77 77 LEU HD13 H 1 0.765 0.040 . 2 . . . . 74 LEU HD1 . 11032 1 1004 . 1 1 77 77 LEU HD21 H 1 0.671 0.040 . 2 . . . . 74 LEU HD2 . 11032 1 1005 . 1 1 77 77 LEU HD22 H 1 0.671 0.040 . 2 . . . . 74 LEU HD2 . 11032 1 1006 . 1 1 77 77 LEU HD23 H 1 0.671 0.040 . 2 . . . . 74 LEU HD2 . 11032 1 1007 . 1 1 77 77 LEU CD1 C 13 25.516 0.450 . 1 . . . . 74 LEU CD1 . 11032 1 1008 . 1 1 77 77 LEU CD2 C 13 22.570 0.450 . 1 . . . . 74 LEU CD2 . 11032 1 1009 . 1 1 77 77 LEU C C 13 178.052 0.450 . 1 . . . . 74 LEU C . 11032 1 1010 . 1 1 78 78 ASP N N 15 118.323 0.450 . 1 . . . . 75 ASP N . 11032 1 1011 . 1 1 78 78 ASP H H 1 8.524 0.040 . 1 . . . . 75 ASP H . 11032 1 1012 . 1 1 78 78 ASP CA C 13 55.636 0.450 . 1 . . . . 75 ASP CA . 11032 1 1013 . 1 1 78 78 ASP HA H 1 4.631 0.040 . 1 . . . . 75 ASP HA . 11032 1 1014 . 1 1 78 78 ASP CB C 13 40.849 0.450 . 1 . . . . 75 ASP CB . 11032 1 1015 . 1 1 78 78 ASP HB2 H 1 2.872 0.040 . 2 . . . . 75 ASP HB2 . 11032 1 1016 . 1 1 78 78 ASP HB3 H 1 2.707 0.040 . 2 . . . . 75 ASP HB3 . 11032 1 1017 . 1 1 78 78 ASP C C 13 176.731 0.450 . 1 . . . . 75 ASP C . 11032 1 1018 . 1 1 79 79 LYS N N 15 118.512 0.450 . 1 . . . . 76 LYS N . 11032 1 1019 . 1 1 79 79 LYS H H 1 6.980 0.040 . 1 . . . . 76 LYS H . 11032 1 1020 . 1 1 79 79 LYS CA C 13 54.714 0.450 . 1 . . . . 76 LYS CA . 11032 1 1021 . 1 1 79 79 LYS HA H 1 4.378 0.040 . 1 . . . . 76 LYS HA . 11032 1 1022 . 1 1 79 79 LYS CB C 13 35.772 0.450 . 1 . . . . 76 LYS CB . 11032 1 1023 . 1 1 79 79 LYS HB2 H 1 1.671 0.040 . 2 . . . . 76 LYS HB2 . 11032 1 1024 . 1 1 79 79 LYS HB3 H 1 1.869 0.040 . 2 . . . . 76 LYS HB3 . 11032 1 1025 . 1 1 79 79 LYS CG C 13 26.358 0.450 . 1 . . . . 76 LYS CG . 11032 1 1026 . 1 1 79 79 LYS HG2 H 1 1.216 0.040 . 2 . . . . 76 LYS HG2 . 11032 1 1027 . 1 1 79 79 LYS HG3 H 1 1.082 0.040 . 2 . . . . 76 LYS HG3 . 11032 1 1028 . 1 1 79 79 LYS CD C 13 28.759 0.450 . 1 . . . . 76 LYS CD . 11032 1 1029 . 1 1 79 79 LYS HD2 H 1 1.107 0.040 . 2 . . . . 76 LYS HD2 . 11032 1 1030 . 1 1 79 79 LYS HD3 H 1 0.738 0.040 . 2 . . . . 76 LYS HD3 . 11032 1 1031 . 1 1 79 79 LYS CE C 13 41.258 0.450 . 1 . . . . 76 LYS CE . 11032 1 1032 . 1 1 79 79 LYS HE2 H 1 2.389 0.040 . 2 . . . . 76 LYS HE2 . 11032 1 1033 . 1 1 79 79 LYS HE3 H 1 2.246 0.040 . 2 . . . . 76 LYS HE3 . 11032 1 1034 . 1 1 79 79 LYS C C 13 175.421 0.450 . 1 . . . . 76 LYS C . 11032 1 1035 . 1 1 80 80 GLU N N 15 118.897 0.450 . 1 . . . . 77 GLU N . 11032 1 1036 . 1 1 80 80 GLU H H 1 8.727 0.040 . 1 . . . . 77 GLU H . 11032 1 1037 . 1 1 80 80 GLU CA C 13 57.821 0.450 . 1 . . . . 77 GLU CA . 11032 1 1038 . 1 1 80 80 GLU HA H 1 4.017 0.040 . 1 . . . . 77 GLU HA . 11032 1 1039 . 1 1 80 80 GLU CB C 13 30.091 0.450 . 1 . . . . 77 GLU CB . 11032 1 1040 . 1 1 80 80 GLU HB2 H 1 1.961 0.040 . 2 . . . . 77 GLU HB2 . 11032 1 1041 . 1 1 80 80 GLU HB3 H 1 1.847 0.040 . 2 . . . . 77 GLU HB3 . 11032 1 1042 . 1 1 80 80 GLU CG C 13 36.707 0.450 . 1 . . . . 77 GLU CG . 11032 1 1043 . 1 1 80 80 GLU HG2 H 1 2.253 0.040 . 2 . . . . 77 GLU HG2 . 11032 1 1044 . 1 1 80 80 GLU HG3 H 1 2.253 0.040 . 2 . . . . 77 GLU HG3 . 11032 1 1045 . 1 1 80 80 GLU C C 13 175.447 0.450 . 1 . . . . 77 GLU C . 11032 1 1046 . 1 1 81 81 VAL N N 15 122.746 0.450 . 1 . . . . 78 VAL N . 11032 1 1047 . 1 1 81 81 VAL H H 1 8.898 0.040 . 1 . . . . 78 VAL H . 11032 1 1048 . 1 1 81 81 VAL CA C 13 61.336 0.450 . 1 . . . . 78 VAL CA . 11032 1 1049 . 1 1 81 81 VAL HA H 1 4.434 0.040 . 1 . . . . 78 VAL HA . 11032 1 1050 . 1 1 81 81 VAL CB C 13 34.347 0.450 . 1 . . . . 78 VAL CB . 11032 1 1051 . 1 1 81 81 VAL HB H 1 2.132 0.040 . 1 . . . . 78 VAL HB . 11032 1 1052 . 1 1 81 81 VAL HG11 H 1 0.697 0.040 . 2 . . . . 78 VAL HG1 . 11032 1 1053 . 1 1 81 81 VAL HG12 H 1 0.697 0.040 . 2 . . . . 78 VAL HG1 . 11032 1 1054 . 1 1 81 81 VAL HG13 H 1 0.697 0.040 . 2 . . . . 78 VAL HG1 . 11032 1 1055 . 1 1 81 81 VAL HG21 H 1 1.085 0.040 . 2 . . . . 78 VAL HG2 . 11032 1 1056 . 1 1 81 81 VAL HG22 H 1 1.085 0.040 . 2 . . . . 78 VAL HG2 . 11032 1 1057 . 1 1 81 81 VAL HG23 H 1 1.085 0.040 . 2 . . . . 78 VAL HG2 . 11032 1 1058 . 1 1 81 81 VAL CG1 C 13 21.963 0.450 . 1 . . . . 78 VAL CG1 . 11032 1 1059 . 1 1 81 81 VAL CG2 C 13 21.829 0.450 . 1 . . . . 78 VAL CG2 . 11032 1 1060 . 1 1 81 81 VAL C C 13 174.759 0.450 . 1 . . . . 78 VAL C . 11032 1 1061 . 1 1 82 82 LEU N N 15 126.518 0.450 . 1 . . . . 79 LEU N . 11032 1 1062 . 1 1 82 82 LEU H H 1 8.875 0.040 . 1 . . . . 79 LEU H . 11032 1 1063 . 1 1 82 82 LEU CA C 13 53.671 0.450 . 1 . . . . 79 LEU CA . 11032 1 1064 . 1 1 82 82 LEU HA H 1 4.946 0.040 . 1 . . . . 79 LEU HA . 11032 1 1065 . 1 1 82 82 LEU CB C 13 42.895 0.450 . 1 . . . . 79 LEU CB . 11032 1 1066 . 1 1 82 82 LEU HB2 H 1 1.437 0.040 . 2 . . . . 79 LEU HB2 . 11032 1 1067 . 1 1 82 82 LEU HB3 H 1 1.678 0.040 . 2 . . . . 79 LEU HB3 . 11032 1 1068 . 1 1 82 82 LEU CG C 13 27.293 0.450 . 1 . . . . 79 LEU CG . 11032 1 1069 . 1 1 82 82 LEU HG H 1 1.570 0.040 . 1 . . . . 79 LEU HG . 11032 1 1070 . 1 1 82 82 LEU HD11 H 1 0.857 0.040 . 2 . . . . 79 LEU HD1 . 11032 1 1071 . 1 1 82 82 LEU HD12 H 1 0.857 0.040 . 2 . . . . 79 LEU HD1 . 11032 1 1072 . 1 1 82 82 LEU HD13 H 1 0.857 0.040 . 2 . . . . 79 LEU HD1 . 11032 1 1073 . 1 1 82 82 LEU HD21 H 1 0.804 0.040 . 2 . . . . 79 LEU HD2 . 11032 1 1074 . 1 1 82 82 LEU HD22 H 1 0.804 0.040 . 2 . . . . 79 LEU HD2 . 11032 1 1075 . 1 1 82 82 LEU HD23 H 1 0.804 0.040 . 2 . . . . 79 LEU HD2 . 11032 1 1076 . 1 1 82 82 LEU CD1 C 13 24.370 0.450 . 1 . . . . 79 LEU CD1 . 11032 1 1077 . 1 1 82 82 LEU CD2 C 13 24.014 0.450 . 1 . . . . 79 LEU CD2 . 11032 1 1078 . 1 1 82 82 LEU C C 13 177.174 0.450 . 1 . . . . 79 LEU C . 11032 1 1079 . 1 1 83 83 TYR N N 15 127.272 0.450 . 1 . . . . 80 TYR N . 11032 1 1080 . 1 1 83 83 TYR H H 1 9.385 0.040 . 1 . . . . 80 TYR H . 11032 1 1081 . 1 1 83 83 TYR CA C 13 56.008 0.450 . 1 . . . . 80 TYR CA . 11032 1 1082 . 1 1 83 83 TYR HA H 1 4.816 0.040 . 1 . . . . 80 TYR HA . 11032 1 1083 . 1 1 83 83 TYR CB C 13 38.797 0.450 . 1 . . . . 80 TYR CB . 11032 1 1084 . 1 1 83 83 TYR HB2 H 1 3.074 0.040 . 2 . . . . 80 TYR HB2 . 11032 1 1085 . 1 1 83 83 TYR HB3 H 1 3.034 0.040 . 2 . . . . 80 TYR HB3 . 11032 1 1086 . 1 1 83 83 TYR CD1 C 13 132.952 0.450 . 1 . . . . 80 TYR CD1 . 11032 1 1087 . 1 1 83 83 TYR HD1 H 1 7.236 0.040 . 1 . . . . 80 TYR HD1 . 11032 1 1088 . 1 1 83 83 TYR CE1 C 13 117.988 0.450 . 1 . . . . 80 TYR CE1 . 11032 1 1089 . 1 1 83 83 TYR HE1 H 1 6.707 0.040 . 1 . . . . 80 TYR HE1 . 11032 1 1090 . 1 1 83 83 TYR CE2 C 13 117.988 0.450 . 1 . . . . 80 TYR CE2 . 11032 1 1091 . 1 1 83 83 TYR HE2 H 1 6.707 0.040 . 1 . . . . 80 TYR HE2 . 11032 1 1092 . 1 1 83 83 TYR CD2 C 13 132.952 0.450 . 1 . . . . 80 TYR CD2 . 11032 1 1093 . 1 1 83 83 TYR HD2 H 1 7.236 0.040 . 1 . . . . 80 TYR HD2 . 11032 1 1094 . 1 1 84 84 PRO CD C 13 50.672 0.450 . 1 . . . . 81 PRO CD . 11032 1 1095 . 1 1 84 84 PRO CA C 13 62.163 0.450 . 1 . . . . 81 PRO CA . 11032 1 1096 . 1 1 84 84 PRO HA H 1 4.523 0.040 . 1 . . . . 81 PRO HA . 11032 1 1097 . 1 1 84 84 PRO CB C 13 32.142 0.450 . 1 . . . . 81 PRO CB . 11032 1 1098 . 1 1 84 84 PRO HB2 H 1 2.152 0.040 . 2 . . . . 81 PRO HB2 . 11032 1 1099 . 1 1 84 84 PRO HB3 H 1 1.953 0.040 . 2 . . . . 81 PRO HB3 . 11032 1 1100 . 1 1 84 84 PRO CG C 13 27.147 0.450 . 1 . . . . 81 PRO CG . 11032 1 1101 . 1 1 84 84 PRO HG2 H 1 2.061 0.040 . 2 . . . . 81 PRO HG2 . 11032 1 1102 . 1 1 84 84 PRO HG3 H 1 2.061 0.040 . 2 . . . . 81 PRO HG3 . 11032 1 1103 . 1 1 84 84 PRO HD2 H 1 3.746 0.040 . 2 . . . . 81 PRO HD2 . 11032 1 1104 . 1 1 84 84 PRO HD3 H 1 3.478 0.040 . 2 . . . . 81 PRO HD3 . 11032 1 1105 . 1 1 84 84 PRO C C 13 176.528 0.450 . 1 . . . . 81 PRO C . 11032 1 1106 . 1 1 85 85 LYS N N 15 121.567 0.450 . 1 . . . . 82 LYS N . 11032 1 1107 . 1 1 85 85 LYS H H 1 8.516 0.040 . 1 . . . . 82 LYS H . 11032 1 1108 . 1 1 85 85 LYS CA C 13 56.467 0.450 . 1 . . . . 82 LYS CA . 11032 1 1109 . 1 1 85 85 LYS HA H 1 4.205 0.040 . 1 . . . . 82 LYS HA . 11032 1 1110 . 1 1 85 85 LYS CB C 13 33.003 0.450 . 1 . . . . 82 LYS CB . 11032 1 1111 . 1 1 85 85 LYS HB2 H 1 1.790 0.040 . 2 . . . . 82 LYS HB2 . 11032 1 1112 . 1 1 85 85 LYS HB3 H 1 1.680 0.040 . 2 . . . . 82 LYS HB3 . 11032 1 1113 . 1 1 85 85 LYS CG C 13 24.932 0.450 . 1 . . . . 82 LYS CG . 11032 1 1114 . 1 1 85 85 LYS HG2 H 1 1.426 0.040 . 2 . . . . 82 LYS HG2 . 11032 1 1115 . 1 1 85 85 LYS HG3 H 1 1.392 0.040 . 2 . . . . 82 LYS HG3 . 11032 1 1116 . 1 1 85 85 LYS CD C 13 29.020 0.450 . 1 . . . . 82 LYS CD . 11032 1 1117 . 1 1 85 85 LYS HD2 H 1 1.675 0.040 . 2 . . . . 82 LYS HD2 . 11032 1 1118 . 1 1 85 85 LYS HD3 H 1 1.675 0.040 . 2 . . . . 82 LYS HD3 . 11032 1 1119 . 1 1 85 85 LYS CE C 13 41.809 0.450 . 1 . . . . 82 LYS CE . 11032 1 1120 . 1 1 85 85 LYS HE2 H 1 2.976 0.040 . 2 . . . . 82 LYS HE2 . 11032 1 1121 . 1 1 85 85 LYS HE3 H 1 2.976 0.040 . 2 . . . . 82 LYS HE3 . 11032 1 1122 . 1 1 85 85 LYS C C 13 176.368 0.450 . 1 . . . . 82 LYS C . 11032 1 1123 . 1 1 86 86 LEU N N 15 125.609 0.450 . 1 . . . . 83 LEU N . 11032 1 1124 . 1 1 86 86 LEU H H 1 8.382 0.040 . 1 . . . . 83 LEU H . 11032 1 1125 . 1 1 86 86 LEU CA C 13 54.744 0.450 . 1 . . . . 83 LEU CA . 11032 1 1126 . 1 1 86 86 LEU HA H 1 4.392 0.040 . 1 . . . . 83 LEU HA . 11032 1 1127 . 1 1 86 86 LEU CB C 13 42.575 0.450 . 1 . . . . 83 LEU CB . 11032 1 1128 . 1 1 86 86 LEU HB2 H 1 1.634 0.040 . 2 . . . . 83 LEU HB2 . 11032 1 1129 . 1 1 86 86 LEU HB3 H 1 1.555 0.040 . 2 . . . . 83 LEU HB3 . 11032 1 1130 . 1 1 86 86 LEU CG C 13 26.875 0.450 . 1 . . . . 83 LEU CG . 11032 1 1131 . 1 1 86 86 LEU HG H 1 1.643 0.040 . 1 . . . . 83 LEU HG . 11032 1 1132 . 1 1 86 86 LEU HD11 H 1 0.925 0.040 . 2 . . . . 83 LEU HD1 . 11032 1 1133 . 1 1 86 86 LEU HD12 H 1 0.925 0.040 . 2 . . . . 83 LEU HD1 . 11032 1 1134 . 1 1 86 86 LEU HD13 H 1 0.925 0.040 . 2 . . . . 83 LEU HD1 . 11032 1 1135 . 1 1 86 86 LEU HD21 H 1 0.870 0.040 . 2 . . . . 83 LEU HD2 . 11032 1 1136 . 1 1 86 86 LEU HD22 H 1 0.870 0.040 . 2 . . . . 83 LEU HD2 . 11032 1 1137 . 1 1 86 86 LEU HD23 H 1 0.870 0.040 . 2 . . . . 83 LEU HD2 . 11032 1 1138 . 1 1 86 86 LEU CD1 C 13 24.931 0.450 . 1 . . . . 83 LEU CD1 . 11032 1 1139 . 1 1 86 86 LEU CD2 C 13 23.460 0.450 . 1 . . . . 83 LEU CD2 . 11032 1 1140 . 1 1 86 86 LEU C C 13 177.146 0.450 . 1 . . . . 83 LEU C . 11032 1 1141 . 1 1 87 87 LYS N N 15 123.080 0.450 . 1 . . . . 84 LYS N . 11032 1 1142 . 1 1 87 87 LYS H H 1 8.399 0.040 . 1 . . . . 84 LYS H . 11032 1 1143 . 1 1 87 87 LYS CA C 13 56.021 0.450 . 1 . . . . 84 LYS CA . 11032 1 1144 . 1 1 87 87 LYS HA H 1 4.328 0.040 . 1 . . . . 84 LYS HA . 11032 1 1145 . 1 1 87 87 LYS CB C 13 33.244 0.450 . 1 . . . . 84 LYS CB . 11032 1 1146 . 1 1 87 87 LYS HB2 H 1 1.824 0.040 . 2 . . . . 84 LYS HB2 . 11032 1 1147 . 1 1 87 87 LYS HB3 H 1 1.741 0.040 . 2 . . . . 84 LYS HB3 . 11032 1 1148 . 1 1 87 87 LYS CG C 13 24.707 0.450 . 1 . . . . 84 LYS CG . 11032 1 1149 . 1 1 87 87 LYS HG2 H 1 1.436 0.040 . 2 . . . . 84 LYS HG2 . 11032 1 1150 . 1 1 87 87 LYS HG3 H 1 1.414 0.040 . 2 . . . . 84 LYS HG3 . 11032 1 1151 . 1 1 87 87 LYS CD C 13 29.246 0.450 . 1 . . . . 84 LYS CD . 11032 1 1152 . 1 1 87 87 LYS HD2 H 1 1.679 0.040 . 2 . . . . 84 LYS HD2 . 11032 1 1153 . 1 1 87 87 LYS HD3 H 1 1.679 0.040 . 2 . . . . 84 LYS HD3 . 11032 1 1154 . 1 1 87 87 LYS CE C 13 42.020 0.450 . 1 . . . . 84 LYS CE . 11032 1 1155 . 1 1 87 87 LYS HE2 H 1 2.987 0.040 . 2 . . . . 84 LYS HE2 . 11032 1 1156 . 1 1 87 87 LYS HE3 H 1 2.987 0.040 . 2 . . . . 84 LYS HE3 . 11032 1 1157 . 1 1 87 87 LYS C C 13 176.298 0.450 . 1 . . . . 84 LYS C . 11032 1 1158 . 1 1 88 88 ALA N N 15 126.653 0.450 . 1 . . . . 85 ALA N . 11032 1 1159 . 1 1 88 88 ALA H H 1 8.590 0.040 . 1 . . . . 85 ALA H . 11032 1 1160 . 1 1 88 88 ALA CA C 13 52.525 0.450 . 1 . . . . 85 ALA CA . 11032 1 1161 . 1 1 88 88 ALA HA H 1 4.381 0.040 . 1 . . . . 85 ALA HA . 11032 1 1162 . 1 1 88 88 ALA HB1 H 1 1.432 0.040 . 1 . . . . 85 ALA HB . 11032 1 1163 . 1 1 88 88 ALA HB2 H 1 1.432 0.040 . 1 . . . . 85 ALA HB . 11032 1 1164 . 1 1 88 88 ALA HB3 H 1 1.432 0.040 . 1 . . . . 85 ALA HB . 11032 1 1165 . 1 1 88 88 ALA CB C 13 19.337 0.450 . 1 . . . . 85 ALA CB . 11032 1 1166 . 1 1 88 88 ALA C C 13 178.051 0.450 . 1 . . . . 85 ALA C . 11032 1 1167 . 1 1 89 89 THR N N 15 112.572 0.450 . 1 . . . . 86 THR N . 11032 1 1168 . 1 1 89 89 THR H H 1 8.195 0.040 . 1 . . . . 86 THR H . 11032 1 1169 . 1 1 89 89 THR CA C 13 61.514 0.450 . 1 . . . . 86 THR CA . 11032 1 1170 . 1 1 89 89 THR HA H 1 4.353 0.040 . 1 . . . . 86 THR HA . 11032 1 1171 . 1 1 89 89 THR CB C 13 69.782 0.450 . 1 . . . . 86 THR CB . 11032 1 1172 . 1 1 89 89 THR HB H 1 4.278 0.040 . 1 . . . . 86 THR HB . 11032 1 1173 . 1 1 89 89 THR HG21 H 1 1.212 0.040 . 1 . . . . 86 THR HG2 . 11032 1 1174 . 1 1 89 89 THR HG22 H 1 1.212 0.040 . 1 . . . . 86 THR HG2 . 11032 1 1175 . 1 1 89 89 THR HG23 H 1 1.212 0.040 . 1 . . . . 86 THR HG2 . 11032 1 1176 . 1 1 89 89 THR CG2 C 13 21.493 0.450 . 1 . . . . 86 THR CG2 . 11032 1 1177 . 1 1 89 89 THR C C 13 174.546 0.450 . 1 . . . . 86 THR C . 11032 1 1178 . 1 1 90 90 ASP N N 15 121.744 0.450 . 1 . . . . 87 ASP N . 11032 1 1179 . 1 1 90 90 ASP H H 1 8.375 0.040 . 1 . . . . 87 ASP H . 11032 1 1180 . 1 1 90 90 ASP CA C 13 55.428 0.450 . 1 . . . . 87 ASP CA . 11032 1 1181 . 1 1 90 90 ASP HA H 1 4.628 0.040 . 1 . . . . 87 ASP HA . 11032 1 1182 . 1 1 90 90 ASP CB C 13 40.955 0.450 . 1 . . . . 87 ASP CB . 11032 1 1183 . 1 1 90 90 ASP HB2 H 1 2.708 0.040 . 2 . . . . 87 ASP HB2 . 11032 1 1184 . 1 1 90 90 ASP HB3 H 1 2.708 0.040 . 2 . . . . 87 ASP HB3 . 11032 1 1185 . 1 1 90 90 ASP C C 13 176.024 0.450 . 1 . . . . 87 ASP C . 11032 1 1186 . 1 1 91 91 GLU N N 15 120.663 0.450 . 1 . . . . 88 GLU N . 11032 1 1187 . 1 1 91 91 GLU H H 1 8.160 0.040 . 1 . . . . 88 GLU H . 11032 1 1188 . 1 1 91 91 GLU CA C 13 56.189 0.450 . 1 . . . . 88 GLU CA . 11032 1 1189 . 1 1 91 91 GLU HA H 1 4.336 0.040 . 1 . . . . 88 GLU HA . 11032 1 1190 . 1 1 91 91 GLU CB C 13 30.487 0.450 . 1 . . . . 88 GLU CB . 11032 1 1191 . 1 1 91 91 GLU HB2 H 1 2.104 0.040 . 2 . . . . 88 GLU HB2 . 11032 1 1192 . 1 1 91 91 GLU HB3 H 1 1.887 0.040 . 2 . . . . 88 GLU HB3 . 11032 1 1193 . 1 1 91 91 GLU CG C 13 36.358 0.450 . 1 . . . . 88 GLU CG . 11032 1 1194 . 1 1 91 91 GLU HG2 H 1 2.246 0.040 . 2 . . . . 88 GLU HG2 . 11032 1 1195 . 1 1 91 91 GLU HG3 H 1 2.246 0.040 . 2 . . . . 88 GLU HG3 . 11032 1 1196 . 1 1 91 91 GLU C C 13 175.417 0.450 . 1 . . . . 88 GLU C . 11032 1 1197 . 1 1 92 92 ASP N N 15 127.010 0.450 . 1 . . . . 89 ASP N . 11032 1 1198 . 1 1 92 92 ASP H H 1 8.020 0.040 . 1 . . . . 89 ASP H . 11032 1 1199 . 1 1 92 92 ASP CA C 13 56.103 0.450 . 1 . . . . 89 ASP CA . 11032 1 1200 . 1 1 92 92 ASP HA H 1 4.365 0.040 . 1 . . . . 89 ASP HA . 11032 1 1201 . 1 1 92 92 ASP CB C 13 42.192 0.450 . 1 . . . . 89 ASP CB . 11032 1 1202 . 1 1 92 92 ASP HB2 H 1 2.666 0.040 . 2 . . . . 89 ASP HB2 . 11032 1 1203 . 1 1 92 92 ASP HB3 H 1 2.557 0.040 . 2 . . . . 89 ASP HB3 . 11032 1 stop_ save_