data_18700 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18700 _Entry.Title ; The solution structure of XIAP(RING)-binding domain of human XAF1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-09-03 _Entry.Accession_date 2012-09-03 _Entry.Last_release_date 2013-02-12 _Entry.Original_release_date 2013-02-12 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 'Man Kit' Tse . . . 18700 2 'Chi Kong' Cho . . . 18700 3 Xiao Guan . . . 18700 4 'Kong Hung' Sze . . . 18700 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18700 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID XAF1 . 18700 'XIAP(RING)-binding domain' . 18700 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18700 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 237 18700 '15N chemical shifts' 57 18700 '1H chemical shifts' 382 18700 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2013-02-12 2012-09-03 original author . 18700 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LXW 'BMRB Entry Tracking System' 18700 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18700 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22811387 _Citation.Full_citation . _Citation.Title 'Domain organization of XAF1 and the identification and characterization of XIAP(RING) -binding domain of XAF1.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 21 _Citation.Journal_issue 10 _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 1418 _Citation.Page_last 1428 _Citation.Year 2012 _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 'Man Kit' Tse . . . 18700 1 2 'Chi Kong' Cho . . . 18700 1 3 'Wai Fung' Wong . . . 18700 1 4 Bing Zou . . . 18700 1 5 'Sin Kam' Hui . . . 18700 1 6 'Benjamin Chun Yu' Wong . . . 18700 1 7 'Kong Hung' Sze . . . 18700 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18700 _Assembly.ID 1 _Assembly.Name 'XIAP(RING)-binding domain of XAF1' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _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 'XIAP(RING)-binding domain of XAF1' 1 $XAF1 A . yes native no no . . . 18700 1 2 'ZINC ION' 2 $entity_ZN B . no native no no . . . 18700 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 coordinate single . 1 . 1 CYS 21 21 SG . 2 . 2 ZN 1 1 ZN 1 XAF1 21 CYS SG 2 Zinc 1 ZN ZN 18700 1 2 coordinate single . 1 . 1 CYS 24 24 SG . 2 . 2 ZN 1 1 ZN 1 XAF1 24 CYS SG 2 Zinc 1 ZN ZN 18700 1 3 coordinate single . 1 . 1 CYS 40 40 SG . 2 . 2 ZN 1 1 ZN 1 XAF1 40 CYS SG 2 Zinc 1 ZN ZN 18700 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_XAF1 _Entity.Sf_category entity _Entity.Sf_framecode XAF1 _Entity.Entry_ID 18700 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _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 ; GSEFTSSPRGDKAAYDILRR CSQCGILLPLPILNQHQEKC RWLASSKGKQVRNFS ; _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 55 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all other bound' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6202.163 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2LXW . "The Solution Structure Of Xiap(ring)-binding Domain Of Human Xaf1" . . . . . 100.00 55 100.00 100.00 1.10e-31 . . . . 18700 1 2 no DBJ BAF82965 . "unnamed protein product [Homo sapiens]" . . . . . 92.73 199 100.00 100.00 2.09e-27 . . . . 18700 1 3 no DBJ BAF85399 . "unnamed protein product [Homo sapiens]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 4 no DBJ BAF85537 . "unnamed protein product [Homo sapiens]" . . . . . 92.73 282 100.00 100.00 7.58e-27 . . . . 18700 1 5 no DBJ BAG51823 . "unnamed protein product [Homo sapiens]" . . . . . 60.00 241 100.00 100.00 1.03e-13 . . . . 18700 1 6 no GB AAH73156 . "XIAP associated factor 1 [Homo sapiens]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 7 no GB AIC51642 . "XAF1, partial [synthetic construct]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 8 no GB EAW90287 . "XIAP associated factor-1, isoform CRA_a [Homo sapiens]" . . . . . 60.00 241 100.00 100.00 9.67e-14 . . . . 18700 1 9 no GB EAW90288 . "XIAP associated factor-1, isoform CRA_b [Homo sapiens]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 10 no GB EAW90289 . "XIAP associated factor-1, isoform CRA_b [Homo sapiens]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 11 no REF NP_059993 . "XIAP-associated factor 1 isoform 1 [Homo sapiens]" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 1 12 no REF NP_954590 . "XIAP-associated factor 1 isoform 2 [Homo sapiens]" . . . . . 92.73 282 100.00 100.00 7.05e-27 . . . . 18700 1 13 no REF XP_001167990 . "PREDICTED: XIAP-associated factor 1 isoform X3 [Pan troglodytes]" . . . . . 92.73 282 98.04 98.04 1.81e-25 . . . . 18700 1 14 no REF XP_003274639 . "PREDICTED: XIAP-associated factor 1 isoform X3 [Nomascus leucogenys]" . . . . . 92.73 282 98.04 100.00 1.25e-26 . . . . 18700 1 15 no REF XP_003274640 . "PREDICTED: XIAP-associated factor 1 isoform X2 [Nomascus leucogenys]" . . . . . 92.73 301 98.04 100.00 1.25e-26 . . . . 18700 1 16 no SP Q6GPH4 . "RecName: Full=XIAP-associated factor 1; AltName: Full=BIRC4-binding protein" . . . . . 92.73 301 100.00 100.00 7.70e-27 . . . . 18700 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 . GLY . 18700 1 2 . SER . 18700 1 3 . GLU . 18700 1 4 . PHE . 18700 1 5 . THR . 18700 1 6 . SER . 18700 1 7 . SER . 18700 1 8 . PRO . 18700 1 9 . ARG . 18700 1 10 . GLY . 18700 1 11 . ASP . 18700 1 12 . LYS . 18700 1 13 . ALA . 18700 1 14 . ALA . 18700 1 15 . TYR . 18700 1 16 . ASP . 18700 1 17 . ILE . 18700 1 18 . LEU . 18700 1 19 . ARG . 18700 1 20 . ARG . 18700 1 21 . CYS . 18700 1 22 . SER . 18700 1 23 . GLN . 18700 1 24 . CYS . 18700 1 25 . GLY . 18700 1 26 . ILE . 18700 1 27 . LEU . 18700 1 28 . LEU . 18700 1 29 . PRO . 18700 1 30 . LEU . 18700 1 31 . PRO . 18700 1 32 . ILE . 18700 1 33 . LEU . 18700 1 34 . ASN . 18700 1 35 . GLN . 18700 1 36 . HIS . 18700 1 37 . GLN . 18700 1 38 . GLU . 18700 1 39 . LYS . 18700 1 40 . CYS . 18700 1 41 . ARG . 18700 1 42 . TRP . 18700 1 43 . LEU . 18700 1 44 . ALA . 18700 1 45 . SER . 18700 1 46 . SER . 18700 1 47 . LYS . 18700 1 48 . GLY . 18700 1 49 . LYS . 18700 1 50 . GLN . 18700 1 51 . VAL . 18700 1 52 . ARG . 18700 1 53 . ASN . 18700 1 54 . PHE . 18700 1 55 . SER . 18700 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 18700 1 . SER 2 2 18700 1 . GLU 3 3 18700 1 . PHE 4 4 18700 1 . THR 5 5 18700 1 . SER 6 6 18700 1 . SER 7 7 18700 1 . PRO 8 8 18700 1 . ARG 9 9 18700 1 . GLY 10 10 18700 1 . ASP 11 11 18700 1 . LYS 12 12 18700 1 . ALA 13 13 18700 1 . ALA 14 14 18700 1 . TYR 15 15 18700 1 . ASP 16 16 18700 1 . ILE 17 17 18700 1 . LEU 18 18 18700 1 . ARG 19 19 18700 1 . ARG 20 20 18700 1 . CYS 21 21 18700 1 . SER 22 22 18700 1 . GLN 23 23 18700 1 . CYS 24 24 18700 1 . GLY 25 25 18700 1 . ILE 26 26 18700 1 . LEU 27 27 18700 1 . LEU 28 28 18700 1 . PRO 29 29 18700 1 . LEU 30 30 18700 1 . PRO 31 31 18700 1 . ILE 32 32 18700 1 . LEU 33 33 18700 1 . ASN 34 34 18700 1 . GLN 35 35 18700 1 . HIS 36 36 18700 1 . GLN 37 37 18700 1 . GLU 38 38 18700 1 . LYS 39 39 18700 1 . CYS 40 40 18700 1 . ARG 41 41 18700 1 . TRP 42 42 18700 1 . LEU 43 43 18700 1 . ALA 44 44 18700 1 . SER 45 45 18700 1 . SER 46 46 18700 1 . LYS 47 47 18700 1 . GLY 48 48 18700 1 . LYS 49 49 18700 1 . GLN 50 50 18700 1 . VAL 51 51 18700 1 . ARG 52 52 18700 1 . ASN 53 53 18700 1 . PHE 54 54 18700 1 . SER 55 55 18700 1 stop_ save_ save_entity_ZN _Entity.Sf_category entity _Entity.Sf_framecode entity_ZN _Entity.Entry_ID 18700 _Entity.ID 2 _Entity.BMRB_code ZN _Entity.Name 'ZINC ION' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 65.409 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'ZINC ION' BMRB 18700 2 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'ZINC ION' BMRB 18700 2 ZN 'Three letter code' 18700 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 ZN $chem_comp_ZN 18700 2 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 ZN ZN 18700 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 18700 _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 $XAF1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18700 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 18700 _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 $XAF1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . . . . pGB1-HIS . . . 'pGB1-HIS vector is modified from pET-32a vector' . . 18700 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 18700 _Chem_comp.ID ZN _Chem_comp.Provenance PDB _Chem_comp.Name 'ZINC ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code ZN _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-04-05 _Chem_comp.Modified_date 2012-04-05 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _Chem_comp.Number_atoms_all 1 _Chem_comp.Number_atoms_nh 1 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Zn/q+2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID InChI=1S/Zn/q+2 InChI InChI 1.03 18700 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 18700 ZN [Zn++] SMILES CACTVS 3.341 18700 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 18700 ZN [Zn+2] SMILES ACDLabs 10.04 18700 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 18700 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18700 ZN stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID zinc 'SYSTEMATIC NAME' ACDLabs 10.04 18700 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18700 ZN stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID ZN ZN ZN ZN . ZN . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 18700 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18700 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 XAF1 '[U-100% 13C; U-100% 15N]' . . 1 $XAF1 . . 1.2 . . mM . . . . 18700 1 2 BisTris-HCl 'natural abundance' . . . . . . 20 . . mM . . . . 18700 1 3 'sodium chloride' 'natural abundance' . . . . . . 150 . . mM . . . . 18700 1 4 DTT D10 . . . . . . 5 . . mM . . . . 18700 1 5 PMSF 'natural abundance' . . . . . . 1 . . mM . . . . 18700 1 6 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18700 1 7 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18700 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18700 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.15 . M 18700 1 pH 6.7 . pH 18700 1 pressure 1 . atm 18700 1 temperature 298 . K 18700 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 18700 _Software.ID 1 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Guntert, Mumenthaler and Wuthrich' . . 18700 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'automated peak assignments' 18700 1 'structure solution' 18700 1 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 18700 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'Equipped with a TCI cyroprobe' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18700 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 600 'Equipped with a TCI cyroprobe' . . 18700 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 18700 _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 . . . . . . . . . . . . . . . . 18700 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 3 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 4 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 5 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 6 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 7 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 8 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 9 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 10 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 11 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 1 12 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18700 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 18700 _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 TSP 'methyl protons' . . . . ppm 0 internal indirect 0.2514 . . . . . . . . . 18700 1 H 1 TSP 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . . . . . . . 18700 1 N 15 TSP 'methyl protons' . . . . ppm 0 internal indirect 0.1013 . . . . . . . . . 18700 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 18700 _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' . . . 18700 1 4 '3D CBCA(CO)NH' . . . 18700 1 5 '3D HNCACB' . . . 18700 1 6 '3D HNCA' . . . 18700 1 7 '3D HN(CO)CA' . . . 18700 1 8 '3D HCCH-TOCSY' . . . 18700 1 11 '3D 1H-15N TOCSY' . . . 18700 1 12 '3D HNCO' . . . 18700 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 HA2 H 1 3.890 0.030 . . . . . A 1 GLY HA2 . 18700 1 2 . 1 1 1 1 GLY HA3 H 1 3.890 0.030 . . . . . A 1 GLY HA3 . 18700 1 3 . 1 1 1 1 GLY CA C 13 43.543 0.300 . . . . . A 1 GLY CA . 18700 1 4 . 1 1 2 2 SER HA H 1 4.474 0.030 . . . . . A 2 SER HA . 18700 1 5 . 1 1 2 2 SER HB2 H 1 3.824 0.030 . . . . . A 2 SER HB2 . 18700 1 6 . 1 1 2 2 SER HB3 H 1 3.824 0.030 . . . . . A 2 SER HB3 . 18700 1 7 . 1 1 2 2 SER C C 13 174.533 0.300 . . . . . A 2 SER C . 18700 1 8 . 1 1 2 2 SER CA C 13 58.351 0.300 . . . . . A 2 SER CA . 18700 1 9 . 1 1 2 2 SER CB C 13 63.851 0.300 . . . . . A 2 SER CB . 18700 1 10 . 1 1 3 3 GLU H H 1 8.805 0.030 . . . . . A 3 GLU H . 18700 1 11 . 1 1 3 3 GLU HA H 1 4.236 0.030 . . . . . A 3 GLU HA . 18700 1 12 . 1 1 3 3 GLU HB2 H 1 1.835 0.030 . . . . . A 3 GLU HB2 . 18700 1 13 . 1 1 3 3 GLU HB3 H 1 1.905 0.030 . . . . . A 3 GLU HB3 . 18700 1 14 . 1 1 3 3 GLU HG2 H 1 2.078 0.030 . . . . . A 3 GLU HG2 . 18700 1 15 . 1 1 3 3 GLU HG3 H 1 2.156 0.030 . . . . . A 3 GLU HG3 . 18700 1 16 . 1 1 3 3 GLU C C 13 176.326 0.300 . . . . . A 3 GLU C . 18700 1 17 . 1 1 3 3 GLU CA C 13 57.082 0.300 . . . . . A 3 GLU CA . 18700 1 18 . 1 1 3 3 GLU CB C 13 29.955 0.300 . . . . . A 3 GLU CB . 18700 1 19 . 1 1 3 3 GLU CG C 13 35.983 0.300 . . . . . A 3 GLU CG . 18700 1 20 . 1 1 3 3 GLU N N 15 123.130 0.300 . . . . . A 3 GLU N . 18700 1 21 . 1 1 4 4 PHE H H 1 8.367 0.030 . . . . . A 4 PHE H . 18700 1 22 . 1 1 4 4 PHE HA H 1 4.709 0.030 . . . . . A 4 PHE HA . 18700 1 23 . 1 1 4 4 PHE HB2 H 1 3.018 0.030 . . . . . A 4 PHE HB2 . 18700 1 24 . 1 1 4 4 PHE HB3 H 1 3.181 0.030 . . . . . A 4 PHE HB3 . 18700 1 25 . 1 1 4 4 PHE HE1 H 1 7.332 0.030 . . . . . A 4 PHE HE1 . 18700 1 26 . 1 1 4 4 PHE HE2 H 1 7.332 0.030 . . . . . A 4 PHE HE2 . 18700 1 27 . 1 1 4 4 PHE C C 13 176.013 0.300 . . . . . A 4 PHE C . 18700 1 28 . 1 1 4 4 PHE CA C 13 57.875 0.300 . . . . . A 4 PHE CA . 18700 1 29 . 1 1 4 4 PHE CB C 13 39.610 0.300 . . . . . A 4 PHE CB . 18700 1 30 . 1 1 4 4 PHE CE1 C 13 131.637 0.300 . . . . . A 4 PHE CE1 . 18700 1 31 . 1 1 4 4 PHE CE2 C 13 131.857 0.300 . . . . . A 4 PHE CE2 . 18700 1 32 . 1 1 4 4 PHE N N 15 120.886 0.300 . . . . . A 4 PHE N . 18700 1 33 . 1 1 5 5 THR H H 1 8.079 0.030 . . . . . A 5 THR H . 18700 1 34 . 1 1 5 5 THR HA H 1 4.345 0.030 . . . . . A 5 THR HA . 18700 1 35 . 1 1 5 5 THR HB H 1 4.177 0.030 . . . . . A 5 THR HB . 18700 1 36 . 1 1 5 5 THR HG21 H 1 1.170 0.030 . . . . . A 5 THR HG21 . 18700 1 37 . 1 1 5 5 THR HG22 H 1 1.170 0.030 . . . . . A 5 THR HG22 . 18700 1 38 . 1 1 5 5 THR HG23 H 1 1.170 0.030 . . . . . A 5 THR HG23 . 18700 1 39 . 1 1 5 5 THR C C 13 174.189 0.300 . . . . . A 5 THR C . 18700 1 40 . 1 1 5 5 THR CA C 13 61.653 0.300 . . . . . A 5 THR CA . 18700 1 41 . 1 1 5 5 THR CB C 13 69.973 0.300 . . . . . A 5 THR CB . 18700 1 42 . 1 1 5 5 THR CG2 C 13 21.446 0.300 . . . . . A 5 THR CG2 . 18700 1 43 . 1 1 5 5 THR N N 15 116.070 0.300 . . . . . A 5 THR N . 18700 1 44 . 1 1 6 6 SER H H 1 8.307 0.030 . . . . . A 6 SER H . 18700 1 45 . 1 1 6 6 SER HA H 1 4.472 0.030 . . . . . A 6 SER HA . 18700 1 46 . 1 1 6 6 SER HB2 H 1 3.865 0.030 . . . . . A 6 SER HB2 . 18700 1 47 . 1 1 6 6 SER HB3 H 1 3.865 0.030 . . . . . A 6 SER HB3 . 18700 1 48 . 1 1 6 6 SER C C 13 174.205 0.300 . . . . . A 6 SER C . 18700 1 49 . 1 1 6 6 SER CA C 13 58.312 0.300 . . . . . A 6 SER CA . 18700 1 50 . 1 1 6 6 SER CB C 13 63.812 0.300 . . . . . A 6 SER CB . 18700 1 51 . 1 1 6 6 SER N N 15 118.234 0.300 . . . . . A 6 SER N . 18700 1 52 . 1 1 7 7 SER H H 1 8.351 0.030 . . . . . A 7 SER H . 18700 1 53 . 1 1 7 7 SER HA H 1 4.768 0.030 . . . . . A 7 SER HA . 18700 1 54 . 1 1 7 7 SER HB2 H 1 3.854 0.030 . . . . . A 7 SER HB2 . 18700 1 55 . 1 1 7 7 SER HB3 H 1 3.854 0.030 . . . . . A 7 SER HB3 . 18700 1 56 . 1 1 7 7 SER CA C 13 56.540 0.300 . . . . . A 7 SER CA . 18700 1 57 . 1 1 7 7 SER CB C 13 63.496 0.300 . . . . . A 7 SER CB . 18700 1 58 . 1 1 7 7 SER N N 15 118.827 0.300 . . . . . A 7 SER N . 18700 1 59 . 1 1 8 8 PRO HA H 1 4.410 0.030 . . . . . A 8 PRO HA . 18700 1 60 . 1 1 8 8 PRO HB2 H 1 1.900 0.030 . . . . . A 8 PRO HB2 . 18700 1 61 . 1 1 8 8 PRO HB3 H 1 2.279 0.030 . . . . . A 8 PRO HB3 . 18700 1 62 . 1 1 8 8 PRO HG2 H 1 2.000 0.030 . . . . . A 8 PRO HG2 . 18700 1 63 . 1 1 8 8 PRO HG3 H 1 2.000 0.030 . . . . . A 8 PRO HG3 . 18700 1 64 . 1 1 8 8 PRO HD2 H 1 3.706 0.030 . . . . . A 8 PRO HD2 . 18700 1 65 . 1 1 8 8 PRO HD3 H 1 3.805 0.030 . . . . . A 8 PRO HD3 . 18700 1 66 . 1 1 8 8 PRO C C 13 177.219 0.300 . . . . . A 8 PRO C . 18700 1 67 . 1 1 8 8 PRO CA C 13 63.515 0.300 . . . . . A 8 PRO CA . 18700 1 68 . 1 1 8 8 PRO CB C 13 32.121 0.300 . . . . . A 8 PRO CB . 18700 1 69 . 1 1 8 8 PRO CG C 13 27.443 0.300 . . . . . A 8 PRO CG . 18700 1 70 . 1 1 8 8 PRO CD C 13 50.742 0.300 . . . . . A 8 PRO CD . 18700 1 71 . 1 1 9 9 ARG H H 1 8.474 0.030 . . . . . A 9 ARG H . 18700 1 72 . 1 1 9 9 ARG HA H 1 4.312 0.030 . . . . . A 9 ARG HA . 18700 1 73 . 1 1 9 9 ARG HB2 H 1 1.732 0.030 . . . . . A 9 ARG HB2 . 18700 1 74 . 1 1 9 9 ARG HB3 H 1 1.732 0.030 . . . . . A 9 ARG HB3 . 18700 1 75 . 1 1 9 9 ARG HG2 H 1 1.634 0.030 . . . . . A 9 ARG HG2 . 18700 1 76 . 1 1 9 9 ARG HG3 H 1 1.654 0.030 . . . . . A 9 ARG HG3 . 18700 1 77 . 1 1 9 9 ARG HD2 H 1 3.176 0.030 . . . . . A 9 ARG HD2 . 18700 1 78 . 1 1 9 9 ARG HD3 H 1 3.176 0.030 . . . . . A 9 ARG HD3 . 18700 1 79 . 1 1 9 9 ARG C C 13 177.116 0.300 . . . . . A 9 ARG C . 18700 1 80 . 1 1 9 9 ARG CA C 13 56.315 0.300 . . . . . A 9 ARG CA . 18700 1 81 . 1 1 9 9 ARG CB C 13 30.997 0.300 . . . . . A 9 ARG CB . 18700 1 82 . 1 1 9 9 ARG CG C 13 27.359 0.300 . . . . . A 9 ARG CG . 18700 1 83 . 1 1 9 9 ARG CD C 13 43.327 0.300 . . . . . A 9 ARG CD . 18700 1 84 . 1 1 9 9 ARG N N 15 120.954 0.300 . . . . . A 9 ARG N . 18700 1 85 . 1 1 10 10 GLY H H 1 8.390 0.030 . . . . . A 10 GLY H . 18700 1 86 . 1 1 10 10 GLY HA2 H 1 3.958 0.030 . . . . . A 10 GLY HA2 . 18700 1 87 . 1 1 10 10 GLY HA3 H 1 3.958 0.030 . . . . . A 10 GLY HA3 . 18700 1 88 . 1 1 10 10 GLY C C 13 174.092 0.300 . . . . . A 10 GLY C . 18700 1 89 . 1 1 10 10 GLY CA C 13 45.488 0.300 . . . . . A 10 GLY CA . 18700 1 90 . 1 1 10 10 GLY N N 15 109.733 0.300 . . . . . A 10 GLY N . 18700 1 91 . 1 1 11 11 ASP H H 1 8.327 0.030 . . . . . A 11 ASP H . 18700 1 92 . 1 1 11 11 ASP HA H 1 4.598 0.030 . . . . . A 11 ASP HA . 18700 1 93 . 1 1 11 11 ASP HB2 H 1 2.681 0.030 . . . . . A 11 ASP HB2 . 18700 1 94 . 1 1 11 11 ASP HB3 H 1 2.681 0.030 . . . . . A 11 ASP HB3 . 18700 1 95 . 1 1 11 11 ASP C C 13 176.751 0.300 . . . . . A 11 ASP C . 18700 1 96 . 1 1 11 11 ASP CA C 13 54.505 0.300 . . . . . A 11 ASP CA . 18700 1 97 . 1 1 11 11 ASP CB C 13 41.212 0.300 . . . . . A 11 ASP CB . 18700 1 98 . 1 1 11 11 ASP N N 15 120.653 0.300 . . . . . A 11 ASP N . 18700 1 99 . 1 1 12 12 LYS H H 1 8.297 0.030 . . . . . A 12 LYS H . 18700 1 100 . 1 1 12 12 LYS HA H 1 4.245 0.030 . . . . . A 12 LYS HA . 18700 1 101 . 1 1 12 12 LYS HB2 H 1 1.809 0.030 . . . . . A 12 LYS HB2 . 18700 1 102 . 1 1 12 12 LYS HB3 H 1 1.809 0.030 . . . . . A 12 LYS HB3 . 18700 1 103 . 1 1 12 12 LYS HG2 H 1 1.440 0.030 . . . . . A 12 LYS HG2 . 18700 1 104 . 1 1 12 12 LYS HG3 H 1 1.440 0.030 . . . . . A 12 LYS HG3 . 18700 1 105 . 1 1 12 12 LYS HD2 H 1 1.661 0.030 . . . . . A 12 LYS HD2 . 18700 1 106 . 1 1 12 12 LYS HD3 H 1 1.661 0.030 . . . . . A 12 LYS HD3 . 18700 1 107 . 1 1 12 12 LYS HE2 H 1 2.975 0.030 . . . . . A 12 LYS HE2 . 18700 1 108 . 1 1 12 12 LYS HE3 H 1 2.975 0.030 . . . . . A 12 LYS HE3 . 18700 1 109 . 1 1 12 12 LYS C C 13 177.091 0.300 . . . . . A 12 LYS C . 18700 1 110 . 1 1 12 12 LYS CA C 13 57.093 0.300 . . . . . A 12 LYS CA . 18700 1 111 . 1 1 12 12 LYS CB C 13 32.742 0.300 . . . . . A 12 LYS CB . 18700 1 112 . 1 1 12 12 LYS CG C 13 25.097 0.300 . . . . . A 12 LYS CG . 18700 1 113 . 1 1 12 12 LYS CD C 13 29.080 0.300 . . . . . A 12 LYS CD . 18700 1 114 . 1 1 12 12 LYS CE C 13 42.061 0.300 . . . . . A 12 LYS CE . 18700 1 115 . 1 1 12 12 LYS N N 15 121.545 0.300 . . . . . A 12 LYS N . 18700 1 116 . 1 1 13 13 ALA H H 1 8.300 0.030 . . . . . A 13 ALA H . 18700 1 117 . 1 1 13 13 ALA HA H 1 4.235 0.030 . . . . . A 13 ALA HA . 18700 1 118 . 1 1 13 13 ALA HB1 H 1 1.355 0.030 . . . . . A 13 ALA HB1 . 18700 1 119 . 1 1 13 13 ALA HB2 H 1 1.355 0.030 . . . . . A 13 ALA HB2 . 18700 1 120 . 1 1 13 13 ALA HB3 H 1 1.355 0.030 . . . . . A 13 ALA HB3 . 18700 1 121 . 1 1 13 13 ALA C C 13 178.328 0.300 . . . . . A 13 ALA C . 18700 1 122 . 1 1 13 13 ALA CA C 13 53.169 0.300 . . . . . A 13 ALA CA . 18700 1 123 . 1 1 13 13 ALA CB C 13 19.004 0.300 . . . . . A 13 ALA CB . 18700 1 124 . 1 1 13 13 ALA N N 15 124.017 0.300 . . . . . A 13 ALA N . 18700 1 125 . 1 1 14 14 ALA H H 1 8.088 0.030 . . . . . A 14 ALA H . 18700 1 126 . 1 1 14 14 ALA HA H 1 4.208 0.030 . . . . . A 14 ALA HA . 18700 1 127 . 1 1 14 14 ALA HB1 H 1 1.349 0.030 . . . . . A 14 ALA HB1 . 18700 1 128 . 1 1 14 14 ALA HB2 H 1 1.349 0.030 . . . . . A 14 ALA HB2 . 18700 1 129 . 1 1 14 14 ALA HB3 H 1 1.349 0.030 . . . . . A 14 ALA HB3 . 18700 1 130 . 1 1 14 14 ALA C C 13 178.028 0.300 . . . . . A 14 ALA C . 18700 1 131 . 1 1 14 14 ALA CA C 13 53.302 0.300 . . . . . A 14 ALA CA . 18700 1 132 . 1 1 14 14 ALA CB C 13 18.988 0.300 . . . . . A 14 ALA CB . 18700 1 133 . 1 1 14 14 ALA N N 15 122.114 0.300 . . . . . A 14 ALA N . 18700 1 134 . 1 1 15 15 TYR H H 1 7.894 0.030 . . . . . A 15 TYR H . 18700 1 135 . 1 1 15 15 TYR HA H 1 4.296 0.030 . . . . . A 15 TYR HA . 18700 1 136 . 1 1 15 15 TYR HB2 H 1 2.975 0.030 . . . . . A 15 TYR HB2 . 18700 1 137 . 1 1 15 15 TYR HB3 H 1 3.099 0.030 . . . . . A 15 TYR HB3 . 18700 1 138 . 1 1 15 15 TYR HD1 H 1 7.158 0.030 . . . . . A 15 TYR HD1 . 18700 1 139 . 1 1 15 15 TYR HD2 H 1 7.157 0.030 . . . . . A 15 TYR HD2 . 18700 1 140 . 1 1 15 15 TYR HE1 H 1 6.811 0.030 . . . . . A 15 TYR HE1 . 18700 1 141 . 1 1 15 15 TYR HE2 H 1 6.811 0.030 . . . . . A 15 TYR HE2 . 18700 1 142 . 1 1 15 15 TYR C C 13 175.552 0.300 . . . . . A 15 TYR C . 18700 1 143 . 1 1 15 15 TYR CA C 13 58.998 0.300 . . . . . A 15 TYR CA . 18700 1 144 . 1 1 15 15 TYR CB C 13 38.475 0.300 . . . . . A 15 TYR CB . 18700 1 145 . 1 1 15 15 TYR CD1 C 13 132.578 0.300 . . . . . A 15 TYR CD1 . 18700 1 146 . 1 1 15 15 TYR CD2 C 13 133.226 0.300 . . . . . A 15 TYR CD2 . 18700 1 147 . 1 1 15 15 TYR CE1 C 13 118.282 0.300 . . . . . A 15 TYR CE1 . 18700 1 148 . 1 1 15 15 TYR CE2 C 13 118.212 0.300 . . . . . A 15 TYR CE2 . 18700 1 149 . 1 1 15 15 TYR N N 15 116.555 0.300 . . . . . A 15 TYR N . 18700 1 150 . 1 1 16 16 ASP H H 1 8.061 0.030 . . . . . A 16 ASP H . 18700 1 151 . 1 1 16 16 ASP HA H 1 4.613 0.030 . . . . . A 16 ASP HA . 18700 1 152 . 1 1 16 16 ASP HB2 H 1 2.682 0.030 . . . . . A 16 ASP HB2 . 18700 1 153 . 1 1 16 16 ASP HB3 H 1 2.623 0.030 . . . . . A 16 ASP HB3 . 18700 1 154 . 1 1 16 16 ASP C C 13 175.901 0.300 . . . . . A 16 ASP C . 18700 1 155 . 1 1 16 16 ASP CA C 13 54.563 0.300 . . . . . A 16 ASP CA . 18700 1 156 . 1 1 16 16 ASP CB C 13 41.204 0.300 . . . . . A 16 ASP CB . 18700 1 157 . 1 1 16 16 ASP N N 15 118.857 0.300 . . . . . A 16 ASP N . 18700 1 158 . 1 1 17 17 ILE H H 1 7.735 0.030 . . . . . A 17 ILE H . 18700 1 159 . 1 1 17 17 ILE HA H 1 4.103 0.030 . . . . . A 17 ILE HA . 18700 1 160 . 1 1 17 17 ILE HB H 1 1.962 0.030 . . . . . A 17 ILE HB . 18700 1 161 . 1 1 17 17 ILE HG12 H 1 1.186 0.030 . . . . . A 17 ILE HG12 . 18700 1 162 . 1 1 17 17 ILE HG13 H 1 1.535 0.030 . . . . . A 17 ILE HG13 . 18700 1 163 . 1 1 17 17 ILE HG21 H 1 0.883 0.030 . . . . . A 17 ILE HG21 . 18700 1 164 . 1 1 17 17 ILE HG22 H 1 0.883 0.030 . . . . . A 17 ILE HG22 . 18700 1 165 . 1 1 17 17 ILE HG23 H 1 0.883 0.030 . . . . . A 17 ILE HG23 . 18700 1 166 . 1 1 17 17 ILE HD11 H 1 0.866 0.030 . . . . . A 17 ILE HD11 . 18700 1 167 . 1 1 17 17 ILE HD12 H 1 0.866 0.030 . . . . . A 17 ILE HD12 . 18700 1 168 . 1 1 17 17 ILE HD13 H 1 0.866 0.030 . . . . . A 17 ILE HD13 . 18700 1 169 . 1 1 17 17 ILE C C 13 174.638 0.300 . . . . . A 17 ILE C . 18700 1 170 . 1 1 17 17 ILE CA C 13 61.095 0.300 . . . . . A 17 ILE CA . 18700 1 171 . 1 1 17 17 ILE CB C 13 38.344 0.300 . . . . . A 17 ILE CB . 18700 1 172 . 1 1 17 17 ILE CG1 C 13 27.337 0.300 . . . . . A 17 ILE CG1 . 18700 1 173 . 1 1 17 17 ILE CG2 C 13 17.742 0.300 . . . . . A 17 ILE CG2 . 18700 1 174 . 1 1 17 17 ILE CD1 C 13 12.958 0.300 . . . . . A 17 ILE CD1 . 18700 1 175 . 1 1 17 17 ILE N N 15 120.990 0.300 . . . . . A 17 ILE N . 18700 1 176 . 1 1 18 18 LEU H H 1 8.259 0.030 . . . . . A 18 LEU H . 18700 1 177 . 1 1 18 18 LEU HA H 1 4.790 0.030 . . . . . A 18 LEU HA . 18700 1 178 . 1 1 18 18 LEU HB2 H 1 1.062 0.030 . . . . . A 18 LEU HB2 . 18700 1 179 . 1 1 18 18 LEU HB3 H 1 1.670 0.030 . . . . . A 18 LEU HB3 . 18700 1 180 . 1 1 18 18 LEU HG H 1 1.549 0.030 . . . . . A 18 LEU HG . 18700 1 181 . 1 1 18 18 LEU HD11 H 1 0.620 0.030 . . . . . A 18 LEU HD11 . 18700 1 182 . 1 1 18 18 LEU HD12 H 1 0.620 0.030 . . . . . A 18 LEU HD12 . 18700 1 183 . 1 1 18 18 LEU HD13 H 1 0.620 0.030 . . . . . A 18 LEU HD13 . 18700 1 184 . 1 1 18 18 LEU HD21 H 1 0.834 0.030 . . . . . A 18 LEU HD21 . 18700 1 185 . 1 1 18 18 LEU HD22 H 1 0.834 0.030 . . . . . A 18 LEU HD22 . 18700 1 186 . 1 1 18 18 LEU HD23 H 1 0.834 0.030 . . . . . A 18 LEU HD23 . 18700 1 187 . 1 1 18 18 LEU C C 13 177.166 0.300 . . . . . A 18 LEU C . 18700 1 188 . 1 1 18 18 LEU CA C 13 53.797 0.300 . . . . . A 18 LEU CA . 18700 1 189 . 1 1 18 18 LEU CB C 13 43.694 0.300 . . . . . A 18 LEU CB . 18700 1 190 . 1 1 18 18 LEU CG C 13 27.240 0.300 . . . . . A 18 LEU CG . 18700 1 191 . 1 1 18 18 LEU CD1 C 13 23.043 0.300 . . . . . A 18 LEU CD1 . 18700 1 192 . 1 1 18 18 LEU CD2 C 13 25.602 0.300 . . . . . A 18 LEU CD2 . 18700 1 193 . 1 1 18 18 LEU N N 15 125.553 0.300 . . . . . A 18 LEU N . 18700 1 194 . 1 1 19 19 ARG H H 1 8.981 0.030 . . . . . A 19 ARG H . 18700 1 195 . 1 1 19 19 ARG HA H 1 4.539 0.030 . . . . . A 19 ARG HA . 18700 1 196 . 1 1 19 19 ARG HB2 H 1 1.566 0.030 . . . . . A 19 ARG HB2 . 18700 1 197 . 1 1 19 19 ARG HB3 H 1 1.741 0.030 . . . . . A 19 ARG HB3 . 18700 1 198 . 1 1 19 19 ARG HG2 H 1 1.565 0.030 . . . . . A 19 ARG HG2 . 18700 1 199 . 1 1 19 19 ARG HG3 H 1 1.565 0.030 . . . . . A 19 ARG HG3 . 18700 1 200 . 1 1 19 19 ARG HD2 H 1 3.111 0.030 . . . . . A 19 ARG HD2 . 18700 1 201 . 1 1 19 19 ARG HD3 H 1 3.308 0.030 . . . . . A 19 ARG HD3 . 18700 1 202 . 1 1 19 19 ARG C C 13 173.848 0.300 . . . . . A 19 ARG C . 18700 1 203 . 1 1 19 19 ARG CA C 13 53.838 0.300 . . . . . A 19 ARG CA . 18700 1 204 . 1 1 19 19 ARG CB C 13 34.883 0.300 . . . . . A 19 ARG CB . 18700 1 205 . 1 1 19 19 ARG CG C 13 27.338 0.300 . . . . . A 19 ARG CG . 18700 1 206 . 1 1 19 19 ARG CD C 13 43.069 0.300 . . . . . A 19 ARG CD . 18700 1 207 . 1 1 19 19 ARG N N 15 123.113 0.300 . . . . . A 19 ARG N . 18700 1 208 . 1 1 20 20 ARG H H 1 8.369 0.030 . . . . . A 20 ARG H . 18700 1 209 . 1 1 20 20 ARG HA H 1 4.905 0.030 . . . . . A 20 ARG HA . 18700 1 210 . 1 1 20 20 ARG HB2 H 1 1.360 0.030 . . . . . A 20 ARG HB2 . 18700 1 211 . 1 1 20 20 ARG HB3 H 1 1.494 0.030 . . . . . A 20 ARG HB3 . 18700 1 212 . 1 1 20 20 ARG HG2 H 1 1.294 0.030 . . . . . A 20 ARG HG2 . 18700 1 213 . 1 1 20 20 ARG HG3 H 1 1.356 0.030 . . . . . A 20 ARG HG3 . 18700 1 214 . 1 1 20 20 ARG HD2 H 1 3.055 0.030 . . . . . A 20 ARG HD2 . 18700 1 215 . 1 1 20 20 ARG HD3 H 1 3.179 0.030 . . . . . A 20 ARG HD3 . 18700 1 216 . 1 1 20 20 ARG C C 13 177.030 0.300 . . . . . A 20 ARG C . 18700 1 217 . 1 1 20 20 ARG CA C 13 55.207 0.300 . . . . . A 20 ARG CA . 18700 1 218 . 1 1 20 20 ARG CB C 13 31.916 0.300 . . . . . A 20 ARG CB . 18700 1 219 . 1 1 20 20 ARG CG C 13 28.909 0.300 . . . . . A 20 ARG CG . 18700 1 220 . 1 1 20 20 ARG CD C 13 43.329 0.300 . . . . . A 20 ARG CD . 18700 1 221 . 1 1 20 20 ARG N N 15 121.118 0.300 . . . . . A 20 ARG N . 18700 1 222 . 1 1 21 21 CYS H H 1 8.789 0.030 . . . . . A 21 CYS H . 18700 1 223 . 1 1 21 21 CYS HA H 1 4.463 0.030 . . . . . A 21 CYS HA . 18700 1 224 . 1 1 21 21 CYS HB2 H 1 2.669 0.030 . . . . . A 21 CYS HB2 . 18700 1 225 . 1 1 21 21 CYS HB3 H 1 3.199 0.030 . . . . . A 21 CYS HB3 . 18700 1 226 . 1 1 21 21 CYS C C 13 178.405 0.300 . . . . . A 21 CYS C . 18700 1 227 . 1 1 21 21 CYS CA C 13 59.826 0.300 . . . . . A 21 CYS CA . 18700 1 228 . 1 1 21 21 CYS CB C 13 30.912 0.300 . . . . . A 21 CYS CB . 18700 1 229 . 1 1 21 21 CYS N N 15 126.392 0.300 . . . . . A 21 CYS N . 18700 1 230 . 1 1 22 22 SER H H 1 9.346 0.030 . . . . . A 22 SER H . 18700 1 231 . 1 1 22 22 SER HA H 1 4.152 0.030 . . . . . A 22 SER HA . 18700 1 232 . 1 1 22 22 SER HB2 H 1 4.027 0.030 . . . . . A 22 SER HB2 . 18700 1 233 . 1 1 22 22 SER HB3 H 1 4.027 0.030 . . . . . A 22 SER HB3 . 18700 1 234 . 1 1 22 22 SER C C 13 173.983 0.300 . . . . . A 22 SER C . 18700 1 235 . 1 1 22 22 SER CA C 13 60.893 0.300 . . . . . A 22 SER CA . 18700 1 236 . 1 1 22 22 SER CB C 13 63.170 0.300 . . . . . A 22 SER CB . 18700 1 237 . 1 1 22 22 SER N N 15 128.050 0.300 . . . . . A 22 SER N . 18700 1 238 . 1 1 23 23 GLN H H 1 9.560 0.030 . . . . . A 23 GLN H . 18700 1 239 . 1 1 23 23 GLN HA H 1 4.400 0.030 . . . . . A 23 GLN HA . 18700 1 240 . 1 1 23 23 GLN HB2 H 1 2.225 0.030 . . . . . A 23 GLN HB2 . 18700 1 241 . 1 1 23 23 GLN HB3 H 1 2.225 0.030 . . . . . A 23 GLN HB3 . 18700 1 242 . 1 1 23 23 GLN HG2 H 1 2.296 0.030 . . . . . A 23 GLN HG2 . 18700 1 243 . 1 1 23 23 GLN HG3 H 1 2.296 0.030 . . . . . A 23 GLN HG3 . 18700 1 244 . 1 1 23 23 GLN HE21 H 1 7.647 0.030 . . . . . A 23 GLN HE21 . 18700 1 245 . 1 1 23 23 GLN HE22 H 1 6.964 0.030 . . . . . A 23 GLN HE22 . 18700 1 246 . 1 1 23 23 GLN C C 13 176.486 0.300 . . . . . A 23 GLN C . 18700 1 247 . 1 1 23 23 GLN CA C 13 57.309 0.300 . . . . . A 23 GLN CA . 18700 1 248 . 1 1 23 23 GLN CB C 13 29.870 0.300 . . . . . A 23 GLN CB . 18700 1 249 . 1 1 23 23 GLN CG C 13 34.166 0.300 . . . . . A 23 GLN CG . 18700 1 250 . 1 1 23 23 GLN N N 15 125.648 0.300 . . . . . A 23 GLN N . 18700 1 251 . 1 1 23 23 GLN NE2 N 15 114.105 0.300 . . . . . A 23 GLN NE2 . 18700 1 252 . 1 1 24 24 CYS H H 1 8.514 0.030 . . . . . A 24 CYS H . 18700 1 253 . 1 1 24 24 CYS HA H 1 4.895 0.030 . . . . . A 24 CYS HA . 18700 1 254 . 1 1 24 24 CYS HB2 H 1 3.094 0.030 . . . . . A 24 CYS HB2 . 18700 1 255 . 1 1 24 24 CYS HB3 H 1 3.094 0.030 . . . . . A 24 CYS HB3 . 18700 1 256 . 1 1 24 24 CYS C C 13 177.193 0.300 . . . . . A 24 CYS C . 18700 1 257 . 1 1 24 24 CYS CA C 13 58.965 0.300 . . . . . A 24 CYS CA . 18700 1 258 . 1 1 24 24 CYS CB C 13 32.723 0.300 . . . . . A 24 CYS CB . 18700 1 259 . 1 1 24 24 CYS N N 15 117.093 0.300 . . . . . A 24 CYS N . 18700 1 260 . 1 1 25 25 GLY H H 1 7.795 0.030 . . . . . A 25 GLY H . 18700 1 261 . 1 1 25 25 GLY HA2 H 1 3.800 0.030 . . . . . A 25 GLY HA2 . 18700 1 262 . 1 1 25 25 GLY HA3 H 1 4.136 0.030 . . . . . A 25 GLY HA3 . 18700 1 263 . 1 1 25 25 GLY C C 13 173.584 0.300 . . . . . A 25 GLY C . 18700 1 264 . 1 1 25 25 GLY CA C 13 46.280 0.300 . . . . . A 25 GLY CA . 18700 1 265 . 1 1 25 25 GLY N N 15 112.635 0.300 . . . . . A 25 GLY N . 18700 1 266 . 1 1 26 26 ILE H H 1 8.111 0.030 . . . . . A 26 ILE H . 18700 1 267 . 1 1 26 26 ILE HA H 1 4.095 0.030 . . . . . A 26 ILE HA . 18700 1 268 . 1 1 26 26 ILE HB H 1 1.841 0.030 . . . . . A 26 ILE HB . 18700 1 269 . 1 1 26 26 ILE HG12 H 1 1.117 0.030 . . . . . A 26 ILE HG12 . 18700 1 270 . 1 1 26 26 ILE HG13 H 1 1.242 0.030 . . . . . A 26 ILE HG13 . 18700 1 271 . 1 1 26 26 ILE HG21 H 1 0.629 0.030 . . . . . A 26 ILE HG21 . 18700 1 272 . 1 1 26 26 ILE HG22 H 1 0.629 0.030 . . . . . A 26 ILE HG22 . 18700 1 273 . 1 1 26 26 ILE HG23 H 1 0.629 0.030 . . . . . A 26 ILE HG23 . 18700 1 274 . 1 1 26 26 ILE HD11 H 1 0.638 0.030 . . . . . A 26 ILE HD11 . 18700 1 275 . 1 1 26 26 ILE HD12 H 1 0.638 0.030 . . . . . A 26 ILE HD12 . 18700 1 276 . 1 1 26 26 ILE HD13 H 1 0.638 0.030 . . . . . A 26 ILE HD13 . 18700 1 277 . 1 1 26 26 ILE C C 13 173.868 0.300 . . . . . A 26 ILE C . 18700 1 278 . 1 1 26 26 ILE CA C 13 62.686 0.300 . . . . . A 26 ILE CA . 18700 1 279 . 1 1 26 26 ILE CB C 13 38.435 0.300 . . . . . A 26 ILE CB . 18700 1 280 . 1 1 26 26 ILE CG1 C 13 27.472 0.300 . . . . . A 26 ILE CG1 . 18700 1 281 . 1 1 26 26 ILE CG2 C 13 17.211 0.300 . . . . . A 26 ILE CG2 . 18700 1 282 . 1 1 26 26 ILE CD1 C 13 13.824 0.300 . . . . . A 26 ILE CD1 . 18700 1 283 . 1 1 26 26 ILE N N 15 121.921 0.300 . . . . . A 26 ILE N . 18700 1 284 . 1 1 27 27 LEU H H 1 7.961 0.030 . . . . . A 27 LEU H . 18700 1 285 . 1 1 27 27 LEU HA H 1 4.459 0.030 . . . . . A 27 LEU HA . 18700 1 286 . 1 1 27 27 LEU HB2 H 1 1.437 0.030 . . . . . A 27 LEU HB2 . 18700 1 287 . 1 1 27 27 LEU HB3 H 1 1.437 0.030 . . . . . A 27 LEU HB3 . 18700 1 288 . 1 1 27 27 LEU HG H 1 1.383 0.030 . . . . . A 27 LEU HG . 18700 1 289 . 1 1 27 27 LEU HD11 H 1 0.698 0.030 . . . . . A 27 LEU HD11 . 18700 1 290 . 1 1 27 27 LEU HD12 H 1 0.698 0.030 . . . . . A 27 LEU HD12 . 18700 1 291 . 1 1 27 27 LEU HD13 H 1 0.698 0.030 . . . . . A 27 LEU HD13 . 18700 1 292 . 1 1 27 27 LEU HD21 H 1 0.736 0.030 . . . . . A 27 LEU HD21 . 18700 1 293 . 1 1 27 27 LEU HD22 H 1 0.736 0.030 . . . . . A 27 LEU HD22 . 18700 1 294 . 1 1 27 27 LEU HD23 H 1 0.736 0.030 . . . . . A 27 LEU HD23 . 18700 1 295 . 1 1 27 27 LEU C C 13 176.643 0.300 . . . . . A 27 LEU C . 18700 1 296 . 1 1 27 27 LEU CA C 13 54.371 0.300 . . . . . A 27 LEU CA . 18700 1 297 . 1 1 27 27 LEU CB C 13 43.517 0.300 . . . . . A 27 LEU CB . 18700 1 298 . 1 1 27 27 LEU CG C 13 27.034 0.300 . . . . . A 27 LEU CG . 18700 1 299 . 1 1 27 27 LEU CD1 C 13 24.969 0.300 . . . . . A 27 LEU CD1 . 18700 1 300 . 1 1 27 27 LEU CD2 C 13 24.983 0.300 . . . . . A 27 LEU CD2 . 18700 1 301 . 1 1 27 27 LEU N N 15 124.429 0.300 . . . . . A 27 LEU N . 18700 1 302 . 1 1 28 28 LEU H H 1 8.847 0.030 . . . . . A 28 LEU H . 18700 1 303 . 1 1 28 28 LEU HA H 1 4.924 0.030 . . . . . A 28 LEU HA . 18700 1 304 . 1 1 28 28 LEU HB2 H 1 1.226 0.030 . . . . . A 28 LEU HB2 . 18700 1 305 . 1 1 28 28 LEU HB3 H 1 1.379 0.030 . . . . . A 28 LEU HB3 . 18700 1 306 . 1 1 28 28 LEU HG H 1 1.298 0.030 . . . . . A 28 LEU HG . 18700 1 307 . 1 1 28 28 LEU HD11 H 1 0.420 0.030 . . . . . A 28 LEU HD11 . 18700 1 308 . 1 1 28 28 LEU HD12 H 1 0.420 0.030 . . . . . A 28 LEU HD12 . 18700 1 309 . 1 1 28 28 LEU HD13 H 1 0.420 0.030 . . . . . A 28 LEU HD13 . 18700 1 310 . 1 1 28 28 LEU HD21 H 1 0.781 0.030 . . . . . A 28 LEU HD21 . 18700 1 311 . 1 1 28 28 LEU HD22 H 1 0.781 0.030 . . . . . A 28 LEU HD22 . 18700 1 312 . 1 1 28 28 LEU HD23 H 1 0.781 0.030 . . . . . A 28 LEU HD23 . 18700 1 313 . 1 1 28 28 LEU CA C 13 51.921 0.300 . . . . . A 28 LEU CA . 18700 1 314 . 1 1 28 28 LEU CB C 13 46.326 0.300 . . . . . A 28 LEU CB . 18700 1 315 . 1 1 28 28 LEU CG C 13 26.457 0.300 . . . . . A 28 LEU CG . 18700 1 316 . 1 1 28 28 LEU CD1 C 13 26.303 0.300 . . . . . A 28 LEU CD1 . 18700 1 317 . 1 1 28 28 LEU CD2 C 13 23.140 0.300 . . . . . A 28 LEU CD2 . 18700 1 318 . 1 1 28 28 LEU N N 15 125.778 0.300 . . . . . A 28 LEU N . 18700 1 319 . 1 1 29 29 PRO HA H 1 4.714 0.030 . . . . . A 29 PRO HA . 18700 1 320 . 1 1 29 29 PRO HB2 H 1 2.494 0.030 . . . . . A 29 PRO HB2 . 18700 1 321 . 1 1 29 29 PRO HB3 H 1 1.788 0.030 . . . . . A 29 PRO HB3 . 18700 1 322 . 1 1 29 29 PRO HG2 H 1 2.159 0.030 . . . . . A 29 PRO HG2 . 18700 1 323 . 1 1 29 29 PRO HG3 H 1 1.953 0.030 . . . . . A 29 PRO HG3 . 18700 1 324 . 1 1 29 29 PRO HD2 H 1 3.399 0.030 . . . . . A 29 PRO HD2 . 18700 1 325 . 1 1 29 29 PRO HD3 H 1 3.856 0.030 . . . . . A 29 PRO HD3 . 18700 1 326 . 1 1 29 29 PRO C C 13 178.244 0.300 . . . . . A 29 PRO C . 18700 1 327 . 1 1 29 29 PRO CA C 13 62.424 0.300 . . . . . A 29 PRO CA . 18700 1 328 . 1 1 29 29 PRO CB C 13 33.239 0.300 . . . . . A 29 PRO CB . 18700 1 329 . 1 1 29 29 PRO CG C 13 28.135 0.300 . . . . . A 29 PRO CG . 18700 1 330 . 1 1 29 29 PRO CD C 13 50.615 0.300 . . . . . A 29 PRO CD . 18700 1 331 . 1 1 30 30 LEU H H 1 8.889 0.030 . . . . . A 30 LEU H . 18700 1 332 . 1 1 30 30 LEU HA H 1 4.078 0.030 . . . . . A 30 LEU HA . 18700 1 333 . 1 1 30 30 LEU HB2 H 1 1.579 0.030 . . . . . A 30 LEU HB2 . 18700 1 334 . 1 1 30 30 LEU HB3 H 1 1.846 0.030 . . . . . A 30 LEU HB3 . 18700 1 335 . 1 1 30 30 LEU HG H 1 1.657 0.030 . . . . . A 30 LEU HG . 18700 1 336 . 1 1 30 30 LEU HD11 H 1 0.885 0.030 . . . . . A 30 LEU HD11 . 18700 1 337 . 1 1 30 30 LEU HD12 H 1 0.885 0.030 . . . . . A 30 LEU HD12 . 18700 1 338 . 1 1 30 30 LEU HD13 H 1 0.885 0.030 . . . . . A 30 LEU HD13 . 18700 1 339 . 1 1 30 30 LEU HD21 H 1 0.934 0.030 . . . . . A 30 LEU HD21 . 18700 1 340 . 1 1 30 30 LEU HD22 H 1 0.934 0.030 . . . . . A 30 LEU HD22 . 18700 1 341 . 1 1 30 30 LEU HD23 H 1 0.934 0.030 . . . . . A 30 LEU HD23 . 18700 1 342 . 1 1 30 30 LEU CA C 13 59.748 0.300 . . . . . A 30 LEU CA . 18700 1 343 . 1 1 30 30 LEU CB C 13 39.913 0.300 . . . . . A 30 LEU CB . 18700 1 344 . 1 1 30 30 LEU CG C 13 27.227 0.300 . . . . . A 30 LEU CG . 18700 1 345 . 1 1 30 30 LEU CD1 C 13 24.883 0.300 . . . . . A 30 LEU CD1 . 18700 1 346 . 1 1 30 30 LEU CD2 C 13 24.493 0.300 . . . . . A 30 LEU CD2 . 18700 1 347 . 1 1 30 30 LEU N N 15 124.813 0.300 . . . . . A 30 LEU N . 18700 1 348 . 1 1 31 31 PRO HA H 1 4.354 0.030 . . . . . A 31 PRO HA . 18700 1 349 . 1 1 31 31 PRO HB2 H 1 2.369 0.030 . . . . . A 31 PRO HB2 . 18700 1 350 . 1 1 31 31 PRO HB3 H 1 1.607 0.030 . . . . . A 31 PRO HB3 . 18700 1 351 . 1 1 31 31 PRO HG2 H 1 1.768 0.030 . . . . . A 31 PRO HG2 . 18700 1 352 . 1 1 31 31 PRO HG3 H 1 1.544 0.030 . . . . . A 31 PRO HG3 . 18700 1 353 . 1 1 31 31 PRO HD2 H 1 3.141 0.030 . . . . . A 31 PRO HD2 . 18700 1 354 . 1 1 31 31 PRO HD3 H 1 3.809 0.030 . . . . . A 31 PRO HD3 . 18700 1 355 . 1 1 31 31 PRO C C 13 178.305 0.300 . . . . . A 31 PRO C . 18700 1 356 . 1 1 31 31 PRO CA C 13 65.870 0.300 . . . . . A 31 PRO CA . 18700 1 357 . 1 1 31 31 PRO CB C 13 31.742 0.300 . . . . . A 31 PRO CB . 18700 1 358 . 1 1 31 31 PRO CG C 13 28.360 0.300 . . . . . A 31 PRO CG . 18700 1 359 . 1 1 31 31 PRO CD C 13 50.542 0.300 . . . . . A 31 PRO CD . 18700 1 360 . 1 1 32 32 ILE H H 1 7.289 0.030 . . . . . A 32 ILE H . 18700 1 361 . 1 1 32 32 ILE HA H 1 4.504 0.030 . . . . . A 32 ILE HA . 18700 1 362 . 1 1 32 32 ILE HB H 1 2.155 0.030 . . . . . A 32 ILE HB . 18700 1 363 . 1 1 32 32 ILE HG12 H 1 1.446 0.030 . . . . . A 32 ILE HG12 . 18700 1 364 . 1 1 32 32 ILE HG13 H 1 1.248 0.030 . . . . . A 32 ILE HG13 . 18700 1 365 . 1 1 32 32 ILE HG21 H 1 1.008 0.030 . . . . . A 32 ILE HG21 . 18700 1 366 . 1 1 32 32 ILE HG22 H 1 1.008 0.030 . . . . . A 32 ILE HG22 . 18700 1 367 . 1 1 32 32 ILE HG23 H 1 1.008 0.030 . . . . . A 32 ILE HG23 . 18700 1 368 . 1 1 32 32 ILE HD11 H 1 0.936 0.030 . . . . . A 32 ILE HD11 . 18700 1 369 . 1 1 32 32 ILE HD12 H 1 0.936 0.030 . . . . . A 32 ILE HD12 . 18700 1 370 . 1 1 32 32 ILE HD13 H 1 0.936 0.030 . . . . . A 32 ILE HD13 . 18700 1 371 . 1 1 32 32 ILE C C 13 177.366 0.300 . . . . . A 32 ILE C . 18700 1 372 . 1 1 32 32 ILE CA C 13 60.981 0.300 . . . . . A 32 ILE CA . 18700 1 373 . 1 1 32 32 ILE CB C 13 38.468 0.300 . . . . . A 32 ILE CB . 18700 1 374 . 1 1 32 32 ILE CG1 C 13 27.471 0.300 . . . . . A 32 ILE CG1 . 18700 1 375 . 1 1 32 32 ILE CG2 C 13 18.152 0.300 . . . . . A 32 ILE CG2 . 18700 1 376 . 1 1 32 32 ILE CD1 C 13 12.957 0.300 . . . . . A 32 ILE CD1 . 18700 1 377 . 1 1 32 32 ILE N N 15 110.885 0.300 . . . . . A 32 ILE N . 18700 1 378 . 1 1 33 33 LEU H H 1 8.132 0.030 . . . . . A 33 LEU H . 18700 1 379 . 1 1 33 33 LEU HA H 1 3.999 0.030 . . . . . A 33 LEU HA . 18700 1 380 . 1 1 33 33 LEU HB2 H 1 1.940 0.030 . . . . . A 33 LEU HB2 . 18700 1 381 . 1 1 33 33 LEU HB3 H 1 1.470 0.030 . . . . . A 33 LEU HB3 . 18700 1 382 . 1 1 33 33 LEU HG H 1 1.564 0.030 . . . . . A 33 LEU HG . 18700 1 383 . 1 1 33 33 LEU HD11 H 1 0.861 0.030 . . . . . A 33 LEU HD11 . 18700 1 384 . 1 1 33 33 LEU HD12 H 1 0.861 0.030 . . . . . A 33 LEU HD12 . 18700 1 385 . 1 1 33 33 LEU HD13 H 1 0.861 0.030 . . . . . A 33 LEU HD13 . 18700 1 386 . 1 1 33 33 LEU HD21 H 1 0.835 0.030 . . . . . A 33 LEU HD21 . 18700 1 387 . 1 1 33 33 LEU HD22 H 1 0.835 0.030 . . . . . A 33 LEU HD22 . 18700 1 388 . 1 1 33 33 LEU HD23 H 1 0.835 0.030 . . . . . A 33 LEU HD23 . 18700 1 389 . 1 1 33 33 LEU C C 13 178.588 0.300 . . . . . A 33 LEU C . 18700 1 390 . 1 1 33 33 LEU CA C 13 58.528 0.300 . . . . . A 33 LEU CA . 18700 1 391 . 1 1 33 33 LEU CB C 13 41.641 0.300 . . . . . A 33 LEU CB . 18700 1 392 . 1 1 33 33 LEU CG C 13 27.229 0.300 . . . . . A 33 LEU CG . 18700 1 393 . 1 1 33 33 LEU CD1 C 13 23.036 0.300 . . . . . A 33 LEU CD1 . 18700 1 394 . 1 1 33 33 LEU CD2 C 13 25.604 0.300 . . . . . A 33 LEU CD2 . 18700 1 395 . 1 1 33 33 LEU N N 15 124.452 0.300 . . . . . A 33 LEU N . 18700 1 396 . 1 1 34 34 ASN H H 1 8.708 0.030 . . . . . A 34 ASN H . 18700 1 397 . 1 1 34 34 ASN HA H 1 4.438 0.030 . . . . . A 34 ASN HA . 18700 1 398 . 1 1 34 34 ASN HB2 H 1 2.814 0.030 . . . . . A 34 ASN HB2 . 18700 1 399 . 1 1 34 34 ASN HB3 H 1 2.814 0.030 . . . . . A 34 ASN HB3 . 18700 1 400 . 1 1 34 34 ASN HD21 H 1 7.657 0.030 . . . . . A 34 ASN HD21 . 18700 1 401 . 1 1 34 34 ASN HD22 H 1 6.888 0.030 . . . . . A 34 ASN HD22 . 18700 1 402 . 1 1 34 34 ASN C C 13 177.791 0.300 . . . . . A 34 ASN C . 18700 1 403 . 1 1 34 34 ASN CA C 13 57.101 0.300 . . . . . A 34 ASN CA . 18700 1 404 . 1 1 34 34 ASN CB C 13 37.642 0.300 . . . . . A 34 ASN CB . 18700 1 405 . 1 1 34 34 ASN N N 15 117.092 0.300 . . . . . A 34 ASN N . 18700 1 406 . 1 1 34 34 ASN ND2 N 15 111.534 0.309 . . . . . A 34 ASN ND2 . 18700 1 407 . 1 1 35 35 GLN H H 1 8.118 0.030 . . . . . A 35 GLN H . 18700 1 408 . 1 1 35 35 GLN HA H 1 4.190 0.030 . . . . . A 35 GLN HA . 18700 1 409 . 1 1 35 35 GLN HB2 H 1 2.163 0.030 . . . . . A 35 GLN HB2 . 18700 1 410 . 1 1 35 35 GLN HB3 H 1 2.163 0.030 . . . . . A 35 GLN HB3 . 18700 1 411 . 1 1 35 35 GLN HG2 H 1 2.474 0.030 . . . . . A 35 GLN HG2 . 18700 1 412 . 1 1 35 35 GLN HG3 H 1 2.515 0.030 . . . . . A 35 GLN HG3 . 18700 1 413 . 1 1 35 35 GLN HE21 H 1 7.621 0.030 . . . . . A 35 GLN HE21 . 18700 1 414 . 1 1 35 35 GLN HE22 H 1 6.952 0.030 . . . . . A 35 GLN HE22 . 18700 1 415 . 1 1 35 35 GLN C C 13 178.483 0.300 . . . . . A 35 GLN C . 18700 1 416 . 1 1 35 35 GLN CA C 13 58.552 0.300 . . . . . A 35 GLN CA . 18700 1 417 . 1 1 35 35 GLN CB C 13 28.608 0.300 . . . . . A 35 GLN CB . 18700 1 418 . 1 1 35 35 GLN CG C 13 34.041 0.300 . . . . . A 35 GLN CG . 18700 1 419 . 1 1 35 35 GLN N N 15 118.707 0.300 . . . . . A 35 GLN N . 18700 1 420 . 1 1 35 35 GLN NE2 N 15 111.648 0.300 . . . . . A 35 GLN NE2 . 18700 1 421 . 1 1 36 36 HIS H H 1 8.036 0.030 . . . . . A 36 HIS H . 18700 1 422 . 1 1 36 36 HIS HA H 1 4.280 0.030 . . . . . A 36 HIS HA . 18700 1 423 . 1 1 36 36 HIS HB2 H 1 3.260 0.030 . . . . . A 36 HIS HB2 . 18700 1 424 . 1 1 36 36 HIS HB3 H 1 3.374 0.030 . . . . . A 36 HIS HB3 . 18700 1 425 . 1 1 36 36 HIS HD2 H 1 7.081 0.030 . . . . . A 36 HIS HD2 . 18700 1 426 . 1 1 36 36 HIS HE1 H 1 7.933 0.030 . . . . . A 36 HIS HE1 . 18700 1 427 . 1 1 36 36 HIS C C 13 177.431 0.300 . . . . . A 36 HIS C . 18700 1 428 . 1 1 36 36 HIS CA C 13 59.949 0.300 . . . . . A 36 HIS CA . 18700 1 429 . 1 1 36 36 HIS CB C 13 28.673 0.300 . . . . . A 36 HIS CB . 18700 1 430 . 1 1 36 36 HIS CD2 C 13 127.998 0.300 . . . . . A 36 HIS CD2 . 18700 1 431 . 1 1 36 36 HIS CE1 C 13 139.233 0.300 . . . . . A 36 HIS CE1 . 18700 1 432 . 1 1 36 36 HIS N N 15 118.674 0.300 . . . . . A 36 HIS N . 18700 1 433 . 1 1 37 37 GLN H H 1 9.230 0.030 . . . . . A 37 GLN H . 18700 1 434 . 1 1 37 37 GLN HA H 1 4.068 0.030 . . . . . A 37 GLN HA . 18700 1 435 . 1 1 37 37 GLN HB2 H 1 2.353 0.030 . . . . . A 37 GLN HB2 . 18700 1 436 . 1 1 37 37 GLN HB3 H 1 2.223 0.030 . . . . . A 37 GLN HB3 . 18700 1 437 . 1 1 37 37 GLN HG2 H 1 2.875 0.030 . . . . . A 37 GLN HG2 . 18700 1 438 . 1 1 37 37 GLN HG3 H 1 2.743 0.030 . . . . . A 37 GLN HG3 . 18700 1 439 . 1 1 37 37 GLN HE21 H 1 7.565 0.030 . . . . . A 37 GLN HE21 . 18700 1 440 . 1 1 37 37 GLN HE22 H 1 6.895 0.030 . . . . . A 37 GLN HE22 . 18700 1 441 . 1 1 37 37 GLN C C 13 177.499 0.300 . . . . . A 37 GLN C . 18700 1 442 . 1 1 37 37 GLN CA C 13 59.987 0.300 . . . . . A 37 GLN CA . 18700 1 443 . 1 1 37 37 GLN CB C 13 30.456 0.300 . . . . . A 37 GLN CB . 18700 1 444 . 1 1 37 37 GLN CG C 13 35.710 0.300 . . . . . A 37 GLN CG . 18700 1 445 . 1 1 37 37 GLN N N 15 118.973 0.300 . . . . . A 37 GLN N . 18700 1 446 . 1 1 37 37 GLN NE2 N 15 109.910 0.300 . . . . . A 37 GLN NE2 . 18700 1 447 . 1 1 38 38 GLU H H 1 7.964 0.030 . . . . . A 38 GLU H . 18700 1 448 . 1 1 38 38 GLU HA H 1 4.065 0.030 . . . . . A 38 GLU HA . 18700 1 449 . 1 1 38 38 GLU HB2 H 1 2.090 0.030 . . . . . A 38 GLU HB2 . 18700 1 450 . 1 1 38 38 GLU HB3 H 1 2.043 0.030 . . . . . A 38 GLU HB3 . 18700 1 451 . 1 1 38 38 GLU HG2 H 1 2.384 0.030 . . . . . A 38 GLU HG2 . 18700 1 452 . 1 1 38 38 GLU HG3 H 1 2.276 0.030 . . . . . A 38 GLU HG3 . 18700 1 453 . 1 1 38 38 GLU C C 13 178.495 0.300 . . . . . A 38 GLU C . 18700 1 454 . 1 1 38 38 GLU CA C 13 59.380 0.300 . . . . . A 38 GLU CA . 18700 1 455 . 1 1 38 38 GLU CB C 13 29.625 0.300 . . . . . A 38 GLU CB . 18700 1 456 . 1 1 38 38 GLU CG C 13 36.211 0.300 . . . . . A 38 GLU CG . 18700 1 457 . 1 1 38 38 GLU N N 15 117.628 0.300 . . . . . A 38 GLU N . 18700 1 458 . 1 1 39 39 LYS H H 1 7.020 0.030 . . . . . A 39 LYS H . 18700 1 459 . 1 1 39 39 LYS HA H 1 4.269 0.030 . . . . . A 39 LYS HA . 18700 1 460 . 1 1 39 39 LYS HB2 H 1 1.801 0.030 . . . . . A 39 LYS HB2 . 18700 1 461 . 1 1 39 39 LYS HB3 H 1 1.801 0.030 . . . . . A 39 LYS HB3 . 18700 1 462 . 1 1 39 39 LYS HG2 H 1 1.421 0.030 . . . . . A 39 LYS HG2 . 18700 1 463 . 1 1 39 39 LYS HG3 H 1 1.421 0.030 . . . . . A 39 LYS HG3 . 18700 1 464 . 1 1 39 39 LYS HD2 H 1 1.651 0.030 . . . . . A 39 LYS HD2 . 18700 1 465 . 1 1 39 39 LYS HD3 H 1 1.651 0.030 . . . . . A 39 LYS HD3 . 18700 1 466 . 1 1 39 39 LYS HE2 H 1 2.958 0.030 . . . . . A 39 LYS HE2 . 18700 1 467 . 1 1 39 39 LYS HE3 H 1 2.958 0.030 . . . . . A 39 LYS HE3 . 18700 1 468 . 1 1 39 39 LYS C C 13 176.738 0.300 . . . . . A 39 LYS C . 18700 1 469 . 1 1 39 39 LYS CA C 13 57.514 0.300 . . . . . A 39 LYS CA . 18700 1 470 . 1 1 39 39 LYS CB C 13 32.832 0.300 . . . . . A 39 LYS CB . 18700 1 471 . 1 1 39 39 LYS CG C 13 24.846 0.300 . . . . . A 39 LYS CG . 18700 1 472 . 1 1 39 39 LYS CD C 13 29.030 0.300 . . . . . A 39 LYS CD . 18700 1 473 . 1 1 39 39 LYS CE C 13 42.069 0.300 . . . . . A 39 LYS CE . 18700 1 474 . 1 1 39 39 LYS N N 15 117.698 0.300 . . . . . A 39 LYS N . 18700 1 475 . 1 1 40 40 CYS H H 1 8.126 0.030 . . . . . A 40 CYS H . 18700 1 476 . 1 1 40 40 CYS HA H 1 3.765 0.030 . . . . . A 40 CYS HA . 18700 1 477 . 1 1 40 40 CYS HB2 H 1 2.632 0.030 . . . . . A 40 CYS HB2 . 18700 1 478 . 1 1 40 40 CYS HB3 H 1 2.154 0.030 . . . . . A 40 CYS HB3 . 18700 1 479 . 1 1 40 40 CYS C C 13 178.133 0.300 . . . . . A 40 CYS C . 18700 1 480 . 1 1 40 40 CYS CA C 13 63.295 0.300 . . . . . A 40 CYS CA . 18700 1 481 . 1 1 40 40 CYS CB C 13 29.413 0.300 . . . . . A 40 CYS CB . 18700 1 482 . 1 1 40 40 CYS N N 15 124.171 0.300 . . . . . A 40 CYS N . 18700 1 483 . 1 1 41 41 ARG H H 1 8.381 0.030 . . . . . A 41 ARG H . 18700 1 484 . 1 1 41 41 ARG HA H 1 4.107 0.030 . . . . . A 41 ARG HA . 18700 1 485 . 1 1 41 41 ARG HB2 H 1 1.776 0.030 . . . . . A 41 ARG HB2 . 18700 1 486 . 1 1 41 41 ARG HB3 H 1 1.858 0.030 . . . . . A 41 ARG HB3 . 18700 1 487 . 1 1 41 41 ARG HG2 H 1 1.628 0.030 . . . . . A 41 ARG HG2 . 18700 1 488 . 1 1 41 41 ARG HG3 H 1 1.628 0.030 . . . . . A 41 ARG HG3 . 18700 1 489 . 1 1 41 41 ARG HD2 H 1 3.108 0.030 . . . . . A 41 ARG HD2 . 18700 1 490 . 1 1 41 41 ARG HD3 H 1 3.108 0.030 . . . . . A 41 ARG HD3 . 18700 1 491 . 1 1 41 41 ARG C C 13 177.886 0.300 . . . . . A 41 ARG C . 18700 1 492 . 1 1 41 41 ARG CA C 13 58.166 0.300 . . . . . A 41 ARG CA . 18700 1 493 . 1 1 41 41 ARG CB C 13 30.563 0.300 . . . . . A 41 ARG CB . 18700 1 494 . 1 1 41 41 ARG CG C 13 27.259 0.300 . . . . . A 41 ARG CG . 18700 1 495 . 1 1 41 41 ARG CD C 13 43.388 0.300 . . . . . A 41 ARG CD . 18700 1 496 . 1 1 41 41 ARG N N 15 119.660 0.300 . . . . . A 41 ARG N . 18700 1 497 . 1 1 42 42 TRP H H 1 7.811 0.030 . . . . . A 42 TRP H . 18700 1 498 . 1 1 42 42 TRP HA H 1 4.385 0.030 . . . . . A 42 TRP HA . 18700 1 499 . 1 1 42 42 TRP HB2 H 1 3.363 0.030 . . . . . A 42 TRP HB2 . 18700 1 500 . 1 1 42 42 TRP HB3 H 1 3.390 0.030 . . . . . A 42 TRP HB3 . 18700 1 501 . 1 1 42 42 TRP HD1 H 1 7.280 0.030 . . . . . A 42 TRP HD1 . 18700 1 502 . 1 1 42 42 TRP HE1 H 1 10.156 0.030 . . . . . A 42 TRP HE1 . 18700 1 503 . 1 1 42 42 TRP HE3 H 1 7.587 0.030 . . . . . A 42 TRP HE3 . 18700 1 504 . 1 1 42 42 TRP HZ2 H 1 7.469 0.030 . . . . . A 42 TRP HZ2 . 18700 1 505 . 1 1 42 42 TRP HZ3 H 1 7.263 0.030 . . . . . A 42 TRP HZ3 . 18700 1 506 . 1 1 42 42 TRP HH2 H 1 7.212 0.030 . . . . . A 42 TRP HH2 . 18700 1 507 . 1 1 42 42 TRP C C 13 178.302 0.300 . . . . . A 42 TRP C . 18700 1 508 . 1 1 42 42 TRP CA C 13 60.137 0.300 . . . . . A 42 TRP CA . 18700 1 509 . 1 1 42 42 TRP CB C 13 29.325 0.300 . . . . . A 42 TRP CB . 18700 1 510 . 1 1 42 42 TRP CD1 C 13 129.835 0.300 . . . . . A 42 TRP CD1 . 18700 1 511 . 1 1 42 42 TRP CE3 C 13 121.016 0.300 . . . . . A 42 TRP CE3 . 18700 1 512 . 1 1 42 42 TRP CZ2 C 13 114.636 0.300 . . . . . A 42 TRP CZ2 . 18700 1 513 . 1 1 42 42 TRP CZ3 C 13 127.332 0.300 . . . . . A 42 TRP CZ3 . 18700 1 514 . 1 1 42 42 TRP CH2 C 13 124.469 0.300 . . . . . A 42 TRP CH2 . 18700 1 515 . 1 1 42 42 TRP N N 15 121.625 0.300 . . . . . A 42 TRP N . 18700 1 516 . 1 1 42 42 TRP NE1 N 15 129.513 0.300 . . . . . A 42 TRP NE1 . 18700 1 517 . 1 1 43 43 LEU H H 1 8.483 0.030 . . . . . A 43 LEU H . 18700 1 518 . 1 1 43 43 LEU HA H 1 3.923 0.030 . . . . . A 43 LEU HA . 18700 1 519 . 1 1 43 43 LEU HB2 H 1 1.545 0.030 . . . . . A 43 LEU HB2 . 18700 1 520 . 1 1 43 43 LEU HB3 H 1 1.791 0.030 . . . . . A 43 LEU HB3 . 18700 1 521 . 1 1 43 43 LEU HG H 1 1.741 0.030 . . . . . A 43 LEU HG . 18700 1 522 . 1 1 43 43 LEU HD11 H 1 0.922 0.030 . . . . . A 43 LEU HD11 . 18700 1 523 . 1 1 43 43 LEU HD12 H 1 0.922 0.030 . . . . . A 43 LEU HD12 . 18700 1 524 . 1 1 43 43 LEU HD13 H 1 0.922 0.030 . . . . . A 43 LEU HD13 . 18700 1 525 . 1 1 43 43 LEU HD21 H 1 0.908 0.030 . . . . . A 43 LEU HD21 . 18700 1 526 . 1 1 43 43 LEU HD22 H 1 0.908 0.030 . . . . . A 43 LEU HD22 . 18700 1 527 . 1 1 43 43 LEU HD23 H 1 0.908 0.030 . . . . . A 43 LEU HD23 . 18700 1 528 . 1 1 43 43 LEU C C 13 178.529 0.300 . . . . . A 43 LEU C . 18700 1 529 . 1 1 43 43 LEU CA C 13 56.747 0.300 . . . . . A 43 LEU CA . 18700 1 530 . 1 1 43 43 LEU CB C 13 42.198 0.300 . . . . . A 43 LEU CB . 18700 1 531 . 1 1 43 43 LEU CG C 13 26.976 0.300 . . . . . A 43 LEU CG . 18700 1 532 . 1 1 43 43 LEU CD1 C 13 25.170 0.300 . . . . . A 43 LEU CD1 . 18700 1 533 . 1 1 43 43 LEU CD2 C 13 23.617 0.300 . . . . . A 43 LEU CD2 . 18700 1 534 . 1 1 43 43 LEU N N 15 122.158 0.300 . . . . . A 43 LEU N . 18700 1 535 . 1 1 44 44 ALA H H 1 7.846 0.030 . . . . . A 44 ALA H . 18700 1 536 . 1 1 44 44 ALA HA H 1 4.121 0.030 . . . . . A 44 ALA HA . 18700 1 537 . 1 1 44 44 ALA HB1 H 1 1.405 0.030 . . . . . A 44 ALA HB1 . 18700 1 538 . 1 1 44 44 ALA HB2 H 1 1.405 0.030 . . . . . A 44 ALA HB2 . 18700 1 539 . 1 1 44 44 ALA HB3 H 1 1.405 0.030 . . . . . A 44 ALA HB3 . 18700 1 540 . 1 1 44 44 ALA C C 13 179.065 0.300 . . . . . A 44 ALA C . 18700 1 541 . 1 1 44 44 ALA CA C 13 53.885 0.300 . . . . . A 44 ALA CA . 18700 1 542 . 1 1 44 44 ALA CB C 13 18.771 0.300 . . . . . A 44 ALA CB . 18700 1 543 . 1 1 44 44 ALA N N 15 121.923 0.300 . . . . . A 44 ALA N . 18700 1 544 . 1 1 45 45 SER H H 1 7.996 0.030 . . . . . A 45 SER H . 18700 1 545 . 1 1 45 45 SER HA H 1 4.341 0.030 . . . . . A 45 SER HA . 18700 1 546 . 1 1 45 45 SER HB2 H 1 3.904 0.030 . . . . . A 45 SER HB2 . 18700 1 547 . 1 1 45 45 SER HB3 H 1 3.904 0.030 . . . . . A 45 SER HB3 . 18700 1 548 . 1 1 45 45 SER C C 13 175.670 0.300 . . . . . A 45 SER C . 18700 1 549 . 1 1 45 45 SER CA C 13 59.448 0.300 . . . . . A 45 SER CA . 18700 1 550 . 1 1 45 45 SER CB C 13 63.658 0.300 . . . . . A 45 SER CB . 18700 1 551 . 1 1 45 45 SER N N 15 113.586 0.300 . . . . . A 45 SER N . 18700 1 552 . 1 1 46 46 SER H H 1 8.082 0.030 . . . . . A 46 SER H . 18700 1 553 . 1 1 46 46 SER HA H 1 4.239 0.030 . . . . . A 46 SER HA . 18700 1 554 . 1 1 46 46 SER HB2 H 1 3.548 0.030 . . . . . A 46 SER HB2 . 18700 1 555 . 1 1 46 46 SER HB3 H 1 3.712 0.030 . . . . . A 46 SER HB3 . 18700 1 556 . 1 1 46 46 SER C C 13 175.125 0.300 . . . . . A 46 SER C . 18700 1 557 . 1 1 46 46 SER CA C 13 59.437 0.300 . . . . . A 46 SER CA . 18700 1 558 . 1 1 46 46 SER CB C 13 63.378 0.300 . . . . . A 46 SER CB . 18700 1 559 . 1 1 46 46 SER N N 15 117.311 0.300 . . . . . A 46 SER N . 18700 1 560 . 1 1 47 47 LYS H H 1 7.908 0.030 . . . . . A 47 LYS H . 18700 1 561 . 1 1 47 47 LYS HA H 1 4.238 0.030 . . . . . A 47 LYS HA . 18700 1 562 . 1 1 47 47 LYS HB2 H 1 1.830 0.030 . . . . . A 47 LYS HB2 . 18700 1 563 . 1 1 47 47 LYS HB3 H 1 1.830 0.030 . . . . . A 47 LYS HB3 . 18700 1 564 . 1 1 47 47 LYS HG2 H 1 1.426 0.030 . . . . . A 47 LYS HG2 . 18700 1 565 . 1 1 47 47 LYS HG3 H 1 1.426 0.030 . . . . . A 47 LYS HG3 . 18700 1 566 . 1 1 47 47 LYS HD2 H 1 1.648 0.030 . . . . . A 47 LYS HD2 . 18700 1 567 . 1 1 47 47 LYS HD3 H 1 1.648 0.030 . . . . . A 47 LYS HD3 . 18700 1 568 . 1 1 47 47 LYS HE2 H 1 2.954 0.030 . . . . . A 47 LYS HE2 . 18700 1 569 . 1 1 47 47 LYS HE3 H 1 2.954 0.030 . . . . . A 47 LYS HE3 . 18700 1 570 . 1 1 47 47 LYS C C 13 177.311 0.300 . . . . . A 47 LYS C . 18700 1 571 . 1 1 47 47 LYS CA C 13 56.840 0.300 . . . . . A 47 LYS CA . 18700 1 572 . 1 1 47 47 LYS CB C 13 32.644 0.300 . . . . . A 47 LYS CB . 18700 1 573 . 1 1 47 47 LYS CG C 13 24.687 0.300 . . . . . A 47 LYS CG . 18700 1 574 . 1 1 47 47 LYS CD C 13 28.976 0.300 . . . . . A 47 LYS CD . 18700 1 575 . 1 1 47 47 LYS CE C 13 42.154 0.300 . . . . . A 47 LYS CE . 18700 1 576 . 1 1 47 47 LYS N N 15 121.877 0.300 . . . . . A 47 LYS N . 18700 1 577 . 1 1 48 48 GLY H H 1 8.184 0.030 . . . . . A 48 GLY H . 18700 1 578 . 1 1 48 48 GLY HA2 H 1 3.900 0.030 . . . . . A 48 GLY HA2 . 18700 1 579 . 1 1 48 48 GLY HA3 H 1 3.900 0.030 . . . . . A 48 GLY HA3 . 18700 1 580 . 1 1 48 48 GLY C C 13 174.353 0.300 . . . . . A 48 GLY C . 18700 1 581 . 1 1 48 48 GLY CA C 13 45.487 0.300 . . . . . A 48 GLY CA . 18700 1 582 . 1 1 48 48 GLY N N 15 108.912 0.300 . . . . . A 48 GLY N . 18700 1 583 . 1 1 49 49 LYS H H 1 8.031 0.030 . . . . . A 49 LYS H . 18700 1 584 . 1 1 49 49 LYS HA H 1 4.302 0.030 . . . . . A 49 LYS HA . 18700 1 585 . 1 1 49 49 LYS HB2 H 1 1.766 0.030 . . . . . A 49 LYS HB2 . 18700 1 586 . 1 1 49 49 LYS HB3 H 1 1.766 0.030 . . . . . A 49 LYS HB3 . 18700 1 587 . 1 1 49 49 LYS HG2 H 1 1.383 0.030 . . . . . A 49 LYS HG2 . 18700 1 588 . 1 1 49 49 LYS HG3 H 1 1.383 0.030 . . . . . A 49 LYS HG3 . 18700 1 589 . 1 1 49 49 LYS HD2 H 1 1.645 0.030 . . . . . A 49 LYS HD2 . 18700 1 590 . 1 1 49 49 LYS HD3 H 1 1.645 0.030 . . . . . A 49 LYS HD3 . 18700 1 591 . 1 1 49 49 LYS HE2 H 1 2.956 0.030 . . . . . A 49 LYS HE2 . 18700 1 592 . 1 1 49 49 LYS HE3 H 1 2.956 0.030 . . . . . A 49 LYS HE3 . 18700 1 593 . 1 1 49 49 LYS C C 13 176.616 0.300 . . . . . A 49 LYS C . 18700 1 594 . 1 1 49 49 LYS CA C 13 56.109 0.300 . . . . . A 49 LYS CA . 18700 1 595 . 1 1 49 49 LYS CB C 13 32.962 0.300 . . . . . A 49 LYS CB . 18700 1 596 . 1 1 49 49 LYS CG C 13 24.824 0.300 . . . . . A 49 LYS CG . 18700 1 597 . 1 1 49 49 LYS CD C 13 29.011 0.300 . . . . . A 49 LYS CD . 18700 1 598 . 1 1 49 49 LYS CE C 13 42.141 0.300 . . . . . A 49 LYS CE . 18700 1 599 . 1 1 49 49 LYS N N 15 120.301 0.300 . . . . . A 49 LYS N . 18700 1 600 . 1 1 50 50 GLN H H 1 8.392 0.030 . . . . . A 50 GLN H . 18700 1 601 . 1 1 50 50 GLN HA H 1 4.309 0.030 . . . . . A 50 GLN HA . 18700 1 602 . 1 1 50 50 GLN HB2 H 1 2.022 0.030 . . . . . A 50 GLN HB2 . 18700 1 603 . 1 1 50 50 GLN HB3 H 1 2.022 0.030 . . . . . A 50 GLN HB3 . 18700 1 604 . 1 1 50 50 GLN HG2 H 1 2.331 0.030 . . . . . A 50 GLN HG2 . 18700 1 605 . 1 1 50 50 GLN HG3 H 1 2.331 0.030 . . . . . A 50 GLN HG3 . 18700 1 606 . 1 1 50 50 GLN HE21 H 1 7.539 0.030 . . . . . A 50 GLN HE21 . 18700 1 607 . 1 1 50 50 GLN HE22 H 1 6.894 0.030 . . . . . A 50 GLN HE22 . 18700 1 608 . 1 1 50 50 GLN C C 13 176.066 0.300 . . . . . A 50 GLN C . 18700 1 609 . 1 1 50 50 GLN CA C 13 55.995 0.300 . . . . . A 50 GLN CA . 18700 1 610 . 1 1 50 50 GLN CB C 13 29.513 0.300 . . . . . A 50 GLN CB . 18700 1 611 . 1 1 50 50 GLN CG C 13 33.841 0.300 . . . . . A 50 GLN CG . 18700 1 612 . 1 1 50 50 GLN N N 15 121.384 0.300 . . . . . A 50 GLN N . 18700 1 613 . 1 1 50 50 GLN NE2 N 15 112.346 0.300 . . . . . A 50 GLN NE2 . 18700 1 614 . 1 1 51 51 VAL H H 1 8.298 0.030 . . . . . A 51 VAL H . 18700 1 615 . 1 1 51 51 VAL HA H 1 4.086 0.030 . . . . . A 51 VAL HA . 18700 1 616 . 1 1 51 51 VAL HB H 1 2.033 0.030 . . . . . A 51 VAL HB . 18700 1 617 . 1 1 51 51 VAL HG11 H 1 0.906 0.030 . . . . . A 51 VAL HG11 . 18700 1 618 . 1 1 51 51 VAL HG12 H 1 0.906 0.030 . . . . . A 51 VAL HG12 . 18700 1 619 . 1 1 51 51 VAL HG13 H 1 0.906 0.030 . . . . . A 51 VAL HG13 . 18700 1 620 . 1 1 51 51 VAL HG21 H 1 0.924 0.030 . . . . . A 51 VAL HG21 . 18700 1 621 . 1 1 51 51 VAL HG22 H 1 0.924 0.030 . . . . . A 51 VAL HG22 . 18700 1 622 . 1 1 51 51 VAL HG23 H 1 0.924 0.030 . . . . . A 51 VAL HG23 . 18700 1 623 . 1 1 51 51 VAL C C 13 176.076 0.300 . . . . . A 51 VAL C . 18700 1 624 . 1 1 51 51 VAL CA C 13 62.525 0.300 . . . . . A 51 VAL CA . 18700 1 625 . 1 1 51 51 VAL CB C 13 32.771 0.300 . . . . . A 51 VAL CB . 18700 1 626 . 1 1 51 51 VAL CG1 C 13 21.287 0.300 . . . . . A 51 VAL CG1 . 18700 1 627 . 1 1 51 51 VAL CG2 C 13 20.711 0.300 . . . . . A 51 VAL CG2 . 18700 1 628 . 1 1 51 51 VAL N N 15 122.558 0.300 . . . . . A 51 VAL N . 18700 1 629 . 1 1 52 52 ARG H H 1 8.439 0.030 . . . . . A 52 ARG H . 18700 1 630 . 1 1 52 52 ARG HA H 1 4.301 0.030 . . . . . A 52 ARG HA . 18700 1 631 . 1 1 52 52 ARG HB2 H 1 1.681 0.030 . . . . . A 52 ARG HB2 . 18700 1 632 . 1 1 52 52 ARG HB3 H 1 1.681 0.030 . . . . . A 52 ARG HB3 . 18700 1 633 . 1 1 52 52 ARG HG2 H 1 1.483 0.030 . . . . . A 52 ARG HG2 . 18700 1 634 . 1 1 52 52 ARG HG3 H 1 1.483 0.030 . . . . . A 52 ARG HG3 . 18700 1 635 . 1 1 52 52 ARG HD2 H 1 3.110 0.030 . . . . . A 52 ARG HD2 . 18700 1 636 . 1 1 52 52 ARG HD3 H 1 3.110 0.030 . . . . . A 52 ARG HD3 . 18700 1 637 . 1 1 52 52 ARG C C 13 175.496 0.300 . . . . . A 52 ARG C . 18700 1 638 . 1 1 52 52 ARG CA C 13 55.931 0.300 . . . . . A 52 ARG CA . 18700 1 639 . 1 1 52 52 ARG CB C 13 31.021 0.300 . . . . . A 52 ARG CB . 18700 1 640 . 1 1 52 52 ARG CG C 13 27.222 0.300 . . . . . A 52 ARG CG . 18700 1 641 . 1 1 52 52 ARG CD C 13 43.364 0.300 . . . . . A 52 ARG CD . 18700 1 642 . 1 1 52 52 ARG N N 15 125.087 0.300 . . . . . A 52 ARG N . 18700 1 643 . 1 1 53 53 ASN H H 1 8.417 0.030 . . . . . A 53 ASN H . 18700 1 644 . 1 1 53 53 ASN HA H 1 4.660 0.030 . . . . . A 53 ASN HA . 18700 1 645 . 1 1 53 53 ASN HB2 H 1 2.657 0.030 . . . . . A 53 ASN HB2 . 18700 1 646 . 1 1 53 53 ASN HB3 H 1 2.714 0.030 . . . . . A 53 ASN HB3 . 18700 1 647 . 1 1 53 53 ASN HD21 H 1 7.588 0.030 . . . . . A 53 ASN HD21 . 18700 1 648 . 1 1 53 53 ASN HD22 H 1 6.900 0.030 . . . . . A 53 ASN HD22 . 18700 1 649 . 1 1 53 53 ASN C C 13 174.667 0.300 . . . . . A 53 ASN C . 18700 1 650 . 1 1 53 53 ASN CA C 13 53.181 0.300 . . . . . A 53 ASN CA . 18700 1 651 . 1 1 53 53 ASN CB C 13 39.165 0.300 . . . . . A 53 ASN CB . 18700 1 652 . 1 1 53 53 ASN N N 15 120.409 0.300 . . . . . A 53 ASN N . 18700 1 653 . 1 1 53 53 ASN ND2 N 15 112.611 0.300 . . . . . A 53 ASN ND2 . 18700 1 654 . 1 1 54 54 PHE H H 1 8.277 0.030 . . . . . A 54 PHE H . 18700 1 655 . 1 1 54 54 PHE HA H 1 4.672 0.030 . . . . . A 54 PHE HA . 18700 1 656 . 1 1 54 54 PHE HB2 H 1 3.003 0.030 . . . . . A 54 PHE HB2 . 18700 1 657 . 1 1 54 54 PHE HB3 H 1 3.178 0.030 . . . . . A 54 PHE HB3 . 18700 1 658 . 1 1 54 54 PHE HD1 H 1 7.248 0.030 . . . . . A 54 PHE HD1 . 18700 1 659 . 1 1 54 54 PHE HD2 H 1 7.248 0.030 . . . . . A 54 PHE HD2 . 18700 1 660 . 1 1 54 54 PHE HE1 H 1 7.248 0.030 . . . . . A 54 PHE HE1 . 18700 1 661 . 1 1 54 54 PHE HE2 H 1 7.247 0.030 . . . . . A 54 PHE HE2 . 18700 1 662 . 1 1 54 54 PHE C C 13 174.918 0.300 . . . . . A 54 PHE C . 18700 1 663 . 1 1 54 54 PHE CA C 13 57.795 0.300 . . . . . A 54 PHE CA . 18700 1 664 . 1 1 54 54 PHE CB C 13 39.661 0.300 . . . . . A 54 PHE CB . 18700 1 665 . 1 1 54 54 PHE CD1 C 13 132.615 0.300 . . . . . A 54 PHE CD1 . 18700 1 666 . 1 1 54 54 PHE CD2 C 13 133.102 0.300 . . . . . A 54 PHE CD2 . 18700 1 667 . 1 1 54 54 PHE CE1 C 13 131.706 0.300 . . . . . A 54 PHE CE1 . 18700 1 668 . 1 1 54 54 PHE CE2 C 13 131.462 0.300 . . . . . A 54 PHE CE2 . 18700 1 669 . 1 1 54 54 PHE N N 15 120.884 0.300 . . . . . A 54 PHE N . 18700 1 670 . 1 1 55 55 SER H H 1 7.939 0.030 . . . . . A 55 SER H . 18700 1 671 . 1 1 55 55 SER HA H 1 4.218 0.030 . . . . . A 55 SER HA . 18700 1 672 . 1 1 55 55 SER HB2 H 1 3.828 0.030 . . . . . A 55 SER HB2 . 18700 1 673 . 1 1 55 55 SER HB3 H 1 3.828 0.030 . . . . . A 55 SER HB3 . 18700 1 674 . 1 1 55 55 SER CA C 13 60.074 0.300 . . . . . A 55 SER CA . 18700 1 675 . 1 1 55 55 SER CB C 13 64.923 0.300 . . . . . A 55 SER CB . 18700 1 676 . 1 1 55 55 SER N N 15 122.368 0.300 . . . . . A 55 SER N . 18700 1 stop_ save_