data_19258 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 19258 _Entry.Title ; Pin1 WW domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2013-05-22 _Entry.Accession_date 2013-05-22 _Entry.Last_release_date 2014-09-08 _Entry.Original_release_date 2014-09-08 _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 'NMR, 20 STRUCTURES' _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 Laura Luh . M. . 19258 2 Donata Kirchner . K. . 19258 3 Frank Loehr . . . 19258 4 Robert Haensel . . . 19258 5 Volker Doetsch . . . 19258 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' . 19258 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID Pin1 . 19258 'WW domain' . 19258 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 19258 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 272 19258 '13C chemical shifts' 182 19258 '15N chemical shifts' 37 19258 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 . . 2014-09-08 2013-05-22 original author . 19258 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2M8I 'BMRB Entry Tracking System' 19258 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 19258 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 23991082 _Citation.Full_citation . _Citation.Title 'In-cell NMR characterization of the secondary structure populations of a disordered conformation of -synuclein within E. coli cells.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'PLoS ONE' _Citation.Journal_name_full 'PloS one' _Citation.Journal_volume 8 _Citation.Journal_issue 8 _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 e72286 _Citation.Page_last e72286 _Citation.Year 2013 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Laura Luh . M. . 19258 1 2 Donata Kirchner . K. . 19258 1 3 Frank Loehr . . . 19258 1 4 Robert Haensel . . . 19258 1 5 Volker Doetsch . . . 19258 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 19258 _Assembly.ID 1 _Assembly.Name 'Pin1 WW 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 entity 1 $entity A . yes native no no . . . 19258 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity _Entity.Sf_category entity _Entity.Sf_framecode entity _Entity.Entry_ID 19258 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity _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 ; GLEHMADEEKLPPGWEKRMS RSSGRVYYFNHITNASQWER PSG ; _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 43 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 5043.613 _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 BMRB 16070 . Pin1_WW . . . . . 79.07 36 100.00 100.00 9.62e-16 . . . . 19258 1 2 no BMRB 16088 . Pin1_WW . . . . . 79.07 36 100.00 100.00 9.62e-16 . . . . 19258 1 3 no BMRB 17545 . "first domain of human PIN1" . . . . . 79.07 36 100.00 100.00 8.01e-16 . . . . 19258 1 4 no BMRB 19259 . Pin1 . . . . . 100.00 43 97.67 97.67 3.02e-22 . . . . 19258 1 5 no BMRB 25569 . Pin1 . . . . . 76.74 33 100.00 100.00 4.71e-15 . . . . 19258 1 6 no PDB 1I6C . "Solution Structure Of Pin1 Ww Domain" . . . . . 79.07 39 100.00 100.00 7.68e-16 . . . . 19258 1 7 no PDB 1I8G . "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" . . . . . 79.07 39 100.00 100.00 7.68e-16 . . . . 19258 1 8 no PDB 1I8H . "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" . . . . . 79.07 39 100.00 100.00 7.68e-16 . . . . 19258 1 9 no PDB 1NMV . "Solution Structure Of Human Pin1" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 10 no PDB 1PIN . "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 11 no PDB 2KCF . "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" . . . . . 79.07 36 100.00 100.00 9.62e-16 . . . . 19258 1 12 no PDB 2LB3 . "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" . . . . . 79.07 36 100.00 100.00 8.01e-16 . . . . 19258 1 13 no PDB 2M8I . "Structure Of Pin1 Ww Domain" . . . . . 100.00 43 100.00 100.00 7.07e-23 . . . . 19258 1 14 no PDB 2M8J . "Structure Of Pin1 Ww Domain Phospho-mimic S16e" . . . . . 100.00 43 97.67 97.67 3.02e-22 . . . . 19258 1 15 no PDB 2ZQS . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 100.00 100.00 1.65e-19 . . . . 19258 1 16 no PDB 2ZQT . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 100.00 100.00 1.58e-19 . . . . 19258 1 17 no PDB 2ZQU . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 97.44 97.44 4.07e-18 . . . . 19258 1 18 no PDB 2ZQV . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 97.44 97.44 2.91e-18 . . . . 19258 1 19 no PDB 2ZR4 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 97.44 100.00 3.88e-19 . . . . 19258 1 20 no PDB 2ZR5 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 100.00 100.00 1.63e-19 . . . . 19258 1 21 no PDB 2ZR6 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 90.70 163 97.44 97.44 1.56e-18 . . . . 19258 1 22 no PDB 3OOB . "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" . . . . . 90.70 163 97.44 97.44 1.56e-18 . . . . 19258 1 23 no PDB 3TC5 . "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" . . . . . 93.02 166 97.50 97.50 1.36e-19 . . . . 19258 1 24 no PDB 3TCZ . "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" . . . . . 79.07 158 97.06 97.06 8.93e-15 . . . . 19258 1 25 no PDB 3TDB . "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" . . . . . 79.07 158 97.06 97.06 8.93e-15 . . . . 19258 1 26 no PDB 3WH0 . "Structure Of Pin1 Complex With 18-crown-6" . . . . . 90.70 163 97.44 97.44 1.56e-18 . . . . 19258 1 27 no PDB 4GWT . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" . . . . . 79.07 36 100.00 100.00 9.62e-16 . . . . 19258 1 28 no PDB 4GWV . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" . . . . . 79.07 36 100.00 100.00 9.62e-16 . . . . 19258 1 29 no PDB 4QIB . "Oxidation-mediated Inhibition Of The Peptidyl-prolyl Isomerase Pin1" . . . . . 76.74 159 96.97 96.97 3.98e-14 . . . . 19258 1 30 no DBJ BAA87037 . "PIN1 [Mus sp.]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 31 no DBJ BAA87038 . "PIN1 [Mus sp.]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 32 no DBJ BAB22270 . "unnamed protein product [Mus musculus]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 33 no DBJ BAB22743 . "unnamed protein product [Mus musculus]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 34 no DBJ BAC35631 . "unnamed protein product [Mus musculus]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 35 no EMBL CAG28582 . "UBL5 [Homo sapiens]" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 36 no GB AAC50492 . "Pin1 [Homo sapiens]" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 37 no GB AAF43897 . "prolyl isomerase Pin1 [Xenopus laevis]" . . . . . 86.05 159 97.30 100.00 1.56e-17 . . . . 19258 1 38 no GB AAH02899 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 39 no GB AAH38254 . "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 40 no GB AAH77447 . "Unknown (protein for IMAGE:4058360), partial [Xenopus laevis]" . . . . . 83.72 158 97.22 100.00 1.06e-16 . . . . 19258 1 41 no PRF 2209428A . "peptidyl-Pro isomerase" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 42 no REF NP_001029804 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 90.70 163 100.00 100.00 1.62e-19 . . . . 19258 1 43 no REF NP_001084236 . "prolyl isomerase Pin1 b [Xenopus laevis]" . . . . . 86.05 159 97.30 100.00 1.56e-17 . . . . 19258 1 44 no REF NP_001100171 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Rattus norvegicus]" . . . . . 86.05 165 97.30 97.30 4.95e-17 . . . . 19258 1 45 no REF NP_001231300 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" . . . . . 90.70 163 100.00 100.00 1.74e-19 . . . . 19258 1 46 no REF NP_001270625 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" . . . . . 90.70 163 97.44 97.44 1.61e-18 . . . . 19258 1 47 no SP Q13526 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 90.70 163 100.00 100.00 1.67e-19 . . . . 19258 1 48 no SP Q4R383 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 90.70 163 97.44 97.44 1.61e-18 . . . . 19258 1 49 no SP Q5BIN5 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 90.70 163 100.00 100.00 1.62e-19 . . . . 19258 1 50 no SP Q9QUR7 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 86.05 165 100.00 100.00 5.15e-18 . . . . 19258 1 51 no TPG DAA28013 . "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 90.70 163 100.00 100.00 1.62e-19 . . . . 19258 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 . 19258 1 2 . LEU . 19258 1 3 . GLU . 19258 1 4 . HIS . 19258 1 5 . MET . 19258 1 6 . ALA . 19258 1 7 . ASP . 19258 1 8 . GLU . 19258 1 9 . GLU . 19258 1 10 . LYS . 19258 1 11 . LEU . 19258 1 12 . PRO . 19258 1 13 . PRO . 19258 1 14 . GLY . 19258 1 15 . TRP . 19258 1 16 . GLU . 19258 1 17 . LYS . 19258 1 18 . ARG . 19258 1 19 . MET . 19258 1 20 . SER . 19258 1 21 . ARG . 19258 1 22 . SER . 19258 1 23 . SER . 19258 1 24 . GLY . 19258 1 25 . ARG . 19258 1 26 . VAL . 19258 1 27 . TYR . 19258 1 28 . TYR . 19258 1 29 . PHE . 19258 1 30 . ASN . 19258 1 31 . HIS . 19258 1 32 . ILE . 19258 1 33 . THR . 19258 1 34 . ASN . 19258 1 35 . ALA . 19258 1 36 . SER . 19258 1 37 . GLN . 19258 1 38 . TRP . 19258 1 39 . GLU . 19258 1 40 . ARG . 19258 1 41 . PRO . 19258 1 42 . SER . 19258 1 43 . GLY . 19258 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 19258 1 . LEU 2 2 19258 1 . GLU 3 3 19258 1 . HIS 4 4 19258 1 . MET 5 5 19258 1 . ALA 6 6 19258 1 . ASP 7 7 19258 1 . GLU 8 8 19258 1 . GLU 9 9 19258 1 . LYS 10 10 19258 1 . LEU 11 11 19258 1 . PRO 12 12 19258 1 . PRO 13 13 19258 1 . GLY 14 14 19258 1 . TRP 15 15 19258 1 . GLU 16 16 19258 1 . LYS 17 17 19258 1 . ARG 18 18 19258 1 . MET 19 19 19258 1 . SER 20 20 19258 1 . ARG 21 21 19258 1 . SER 22 22 19258 1 . SER 23 23 19258 1 . GLY 24 24 19258 1 . ARG 25 25 19258 1 . VAL 26 26 19258 1 . TYR 27 27 19258 1 . TYR 28 28 19258 1 . PHE 29 29 19258 1 . ASN 30 30 19258 1 . HIS 31 31 19258 1 . ILE 32 32 19258 1 . THR 33 33 19258 1 . ASN 34 34 19258 1 . ALA 35 35 19258 1 . SER 36 36 19258 1 . GLN 37 37 19258 1 . TRP 38 38 19258 1 . GLU 39 39 19258 1 . ARG 40 40 19258 1 . PRO 41 41 19258 1 . SER 42 42 19258 1 . GLY 43 43 19258 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 19258 _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 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 19258 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 19258 _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' . . . Escherichia coli . . . . . . . . . . . . . . . . pET29b . . . . . . 19258 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 19258 _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 entity 'natural abundance' . . 1 $entity . . . . . mM . . . . 19258 1 2 HEPES 'natural abundance' . . . . . . 25 . . mM . . . . 19258 1 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 19258 1 4 DTT 'natural abundance' . . . . . . 1 . . mM . . . . 19258 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 19258 _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 temperature 291 . K 19258 1 pH 7.5 . pH 19258 1 pressure 1 . atm 19258 1 'ionic strength' 0.05 . M 19258 1 stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 19258 _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' . . 19258 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 19258 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 19258 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 19258 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 19258 2 'data analysis' 19258 2 'peak picking' 19258 2 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 19258 _Software.ID 3 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 19258 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 19258 3 processing 19258 3 stop_ save_ save_OPAL _Software.Sf_category software _Software.Sf_framecode OPAL _Software.Entry_ID 19258 _Software.ID 4 _Software.Name OPAL _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Luginbuhl, Guntert, Billeter and Wuthrich' . . 19258 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 19258 4 stop_ save_ save_TALOS _Software.Sf_category software _Software.Sf_framecode TALOS _Software.Entry_ID 19258 _Software.ID 5 _Software.Name TALOS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Cornilescu, Delaglio and Bax' . . 19258 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 19258 5 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 19258 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 19258 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _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 19258 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 500 . . . 19258 1 2 spectrometer_2 Bruker Avance . 600 . . . 19258 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 19258 _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 . . . . . . . . . . . . . . . . . . . . . 19258 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 3 '2D 1H-13C HSQC aromatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 4 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 5 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 6 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 7 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 8 '3D HBHA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 9 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 1 10 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 19258 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 19258 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 19258 1 C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 19258 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 19258 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 19258 _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' . . . 19258 1 4 '3D HNCACB' . . . 19258 1 5 '3D HCACO' . . . 19258 1 6 '3D C(CO)NH' . . . 19258 1 7 '3D H(CCO)NH' . . . 19258 1 8 '3D HBHA(CO)NH' . . . 19258 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 2 2 LEU HA H 1 4.356 0.010 . . . . . A 2 LEU HA . 19258 1 2 . 1 1 2 2 LEU HB2 H 1 1.584 0.000 . . . . . A 2 LEU HB2 . 19258 1 3 . 1 1 2 2 LEU HB3 H 1 1.584 0.000 . . . . . A 2 LEU HB3 . 19258 1 4 . 1 1 2 2 LEU HG H 1 1.650 0.000 . . . . . A 2 LEU HG . 19258 1 5 . 1 1 2 2 LEU HD11 H 1 0.940 0.000 . . . . . A 2 LEU HD11 . 19258 1 6 . 1 1 2 2 LEU HD12 H 1 0.940 0.000 . . . . . A 2 LEU HD12 . 19258 1 7 . 1 1 2 2 LEU HD13 H 1 0.940 0.000 . . . . . A 2 LEU HD13 . 19258 1 8 . 1 1 2 2 LEU C C 13 177.736 0.000 . . . . . A 2 LEU C . 19258 1 9 . 1 1 2 2 LEU CA C 13 55.618 0.024 . . . . . A 2 LEU CA . 19258 1 10 . 1 1 2 2 LEU CB C 13 42.281 0.004 . . . . . A 2 LEU CB . 19258 1 11 . 1 1 2 2 LEU CG C 13 27.020 0.034 . . . . . A 2 LEU CG . 19258 1 12 . 1 1 2 2 LEU CD1 C 13 24.941 0.007 . . . . . A 2 LEU CD1 . 19258 1 13 . 1 1 2 2 LEU CD2 C 13 23.468 0.000 . . . . . A 2 LEU CD2 . 19258 1 14 . 1 1 3 3 GLU H H 1 8.891 0.001 . . . . . A 3 GLU H . 19258 1 15 . 1 1 3 3 GLU HA H 1 4.242 0.010 . . . . . A 3 GLU HA . 19258 1 16 . 1 1 3 3 GLU HB2 H 1 1.943 0.000 . . . . . A 3 GLU HB2 . 19258 1 17 . 1 1 3 3 GLU HB3 H 1 1.943 0.000 . . . . . A 3 GLU HB3 . 19258 1 18 . 1 1 3 3 GLU HG2 H 1 2.260 0.000 . . . . . A 3 GLU HG2 . 19258 1 19 . 1 1 3 3 GLU HG3 H 1 2.148 0.000 . . . . . A 3 GLU HG3 . 19258 1 20 . 1 1 3 3 GLU C C 13 176.304 0.004 . . . . . A 3 GLU C . 19258 1 21 . 1 1 3 3 GLU CA C 13 57.140 0.011 . . . . . A 3 GLU CA . 19258 1 22 . 1 1 3 3 GLU CB C 13 29.773 0.019 . . . . . A 3 GLU CB . 19258 1 23 . 1 1 3 3 GLU CG C 13 36.036 0.020 . . . . . A 3 GLU CG . 19258 1 24 . 1 1 3 3 GLU N N 15 121.428 0.006 . . . . . A 3 GLU N . 19258 1 25 . 1 1 4 4 HIS H H 1 8.286 0.001 . . . . . A 4 HIS H . 19258 1 26 . 1 1 4 4 HIS HA H 1 4.613 0.000 . . . . . A 4 HIS HA . 19258 1 27 . 1 1 4 4 HIS HB2 H 1 3.110 0.000 . . . . . A 4 HIS HB2 . 19258 1 28 . 1 1 4 4 HIS HB3 H 1 3.110 0.000 . . . . . A 4 HIS HB3 . 19258 1 29 . 1 1 4 4 HIS HD2 H 1 7.015 0.000 . . . . . A 4 HIS HD2 . 19258 1 30 . 1 1 4 4 HIS HE1 H 1 7.803 0.000 . . . . . A 4 HIS HE1 . 19258 1 31 . 1 1 4 4 HIS C C 13 175.467 0.007 . . . . . A 4 HIS C . 19258 1 32 . 1 1 4 4 HIS CA C 13 56.692 0.048 . . . . . A 4 HIS CA . 19258 1 33 . 1 1 4 4 HIS CB C 13 30.899 0.007 . . . . . A 4 HIS CB . 19258 1 34 . 1 1 4 4 HIS CD2 C 13 119.759 0.000 . . . . . A 4 HIS CD2 . 19258 1 35 . 1 1 4 4 HIS CE1 C 13 138.736 0.000 . . . . . A 4 HIS CE1 . 19258 1 36 . 1 1 4 4 HIS N N 15 120.267 0.006 . . . . . A 4 HIS N . 19258 1 37 . 1 1 5 5 MET H H 1 8.224 0.001 . . . . . A 5 MET H . 19258 1 38 . 1 1 5 5 MET HA H 1 4.472 0.012 . . . . . A 5 MET HA . 19258 1 39 . 1 1 5 5 MET HB2 H 1 2.077 0.017 . . . . . A 5 MET HB2 . 19258 1 40 . 1 1 5 5 MET HB3 H 1 1.972 0.015 . . . . . A 5 MET HB3 . 19258 1 41 . 1 1 5 5 MET HG2 H 1 2.545 0.000 . . . . . A 5 MET HG2 . 19258 1 42 . 1 1 5 5 MET HG3 H 1 2.458 0.000 . . . . . A 5 MET HG3 . 19258 1 43 . 1 1 5 5 MET HE1 H 1 2.083 0.000 . . . . . A 5 MET HE1 . 19258 1 44 . 1 1 5 5 MET HE2 H 1 2.083 0.000 . . . . . A 5 MET HE2 . 19258 1 45 . 1 1 5 5 MET HE3 H 1 2.083 0.000 . . . . . A 5 MET HE3 . 19258 1 46 . 1 1 5 5 MET C C 13 175.831 0.008 . . . . . A 5 MET C . 19258 1 47 . 1 1 5 5 MET CA C 13 55.348 0.013 . . . . . A 5 MET CA . 19258 1 48 . 1 1 5 5 MET CB C 13 32.911 0.015 . . . . . A 5 MET CB . 19258 1 49 . 1 1 5 5 MET CG C 13 31.971 0.036 . . . . . A 5 MET CG . 19258 1 50 . 1 1 5 5 MET CE C 13 16.991 0.000 . . . . . A 5 MET CE . 19258 1 51 . 1 1 5 5 MET N N 15 122.179 0.011 . . . . . A 5 MET N . 19258 1 52 . 1 1 6 6 ALA H H 1 8.372 0.001 . . . . . A 6 ALA H . 19258 1 53 . 1 1 6 6 ALA HA H 1 4.304 0.000 . . . . . A 6 ALA HA . 19258 1 54 . 1 1 6 6 ALA HB1 H 1 1.407 0.000 . . . . . A 6 ALA HB1 . 19258 1 55 . 1 1 6 6 ALA HB2 H 1 1.407 0.000 . . . . . A 6 ALA HB2 . 19258 1 56 . 1 1 6 6 ALA HB3 H 1 1.407 0.000 . . . . . A 6 ALA HB3 . 19258 1 57 . 1 1 6 6 ALA C C 13 177.596 0.007 . . . . . A 6 ALA C . 19258 1 58 . 1 1 6 6 ALA CA C 13 52.679 0.002 . . . . . A 6 ALA CA . 19258 1 59 . 1 1 6 6 ALA CB C 13 19.297 0.013 . . . . . A 6 ALA CB . 19258 1 60 . 1 1 6 6 ALA N N 15 125.265 0.008 . . . . . A 6 ALA N . 19258 1 61 . 1 1 7 7 ASP H H 1 8.382 0.000 . . . . . A 7 ASP H . 19258 1 62 . 1 1 7 7 ASP HA H 1 4.599 0.010 . . . . . A 7 ASP HA . 19258 1 63 . 1 1 7 7 ASP HB2 H 1 2.752 0.000 . . . . . A 7 ASP HB2 . 19258 1 64 . 1 1 7 7 ASP HB3 H 1 2.669 0.000 . . . . . A 7 ASP HB3 . 19258 1 65 . 1 1 7 7 ASP C C 13 176.400 0.135 . . . . . A 7 ASP C . 19258 1 66 . 1 1 7 7 ASP CA C 13 54.597 0.015 . . . . . A 7 ASP CA . 19258 1 67 . 1 1 7 7 ASP CB C 13 41.252 0.032 . . . . . A 7 ASP CB . 19258 1 68 . 1 1 7 7 ASP N N 15 119.846 0.009 . . . . . A 7 ASP N . 19258 1 69 . 1 1 8 8 GLU H H 1 8.417 0.001 . . . . . A 8 GLU H . 19258 1 70 . 1 1 8 8 GLU HA H 1 4.283 0.007 . . . . . A 8 GLU HA . 19258 1 71 . 1 1 8 8 GLU HB2 H 1 2.090 0.002 . . . . . A 8 GLU HB2 . 19258 1 72 . 1 1 8 8 GLU HB3 H 1 1.986 0.000 . . . . . A 8 GLU HB3 . 19258 1 73 . 1 1 8 8 GLU HG2 H 1 2.304 0.010 . . . . . A 8 GLU HG2 . 19258 1 74 . 1 1 8 8 GLU HG3 H 1 2.304 0.010 . . . . . A 8 GLU HG3 . 19258 1 75 . 1 1 8 8 GLU C C 13 176.564 0.009 . . . . . A 8 GLU C . 19258 1 76 . 1 1 8 8 GLU CA C 13 56.791 0.020 . . . . . A 8 GLU CA . 19258 1 77 . 1 1 8 8 GLU CB C 13 30.359 0.103 . . . . . A 8 GLU CB . 19258 1 78 . 1 1 8 8 GLU CG C 13 36.376 0.008 . . . . . A 8 GLU CG . 19258 1 79 . 1 1 8 8 GLU N N 15 121.200 0.013 . . . . . A 8 GLU N . 19258 1 80 . 1 1 9 9 GLU H H 1 8.425 0.001 . . . . . A 9 GLU H . 19258 1 81 . 1 1 9 9 GLU HA H 1 4.255 0.005 . . . . . A 9 GLU HA . 19258 1 82 . 1 1 9 9 GLU HB2 H 1 2.090 0.000 . . . . . A 9 GLU HB2 . 19258 1 83 . 1 1 9 9 GLU HB3 H 1 1.984 0.000 . . . . . A 9 GLU HB3 . 19258 1 84 . 1 1 9 9 GLU C C 13 176.217 0.000 . . . . . A 9 GLU C . 19258 1 85 . 1 1 9 9 GLU CA C 13 56.528 0.022 . . . . . A 9 GLU CA . 19258 1 86 . 1 1 9 9 GLU CB C 13 30.424 0.012 . . . . . A 9 GLU CB . 19258 1 87 . 1 1 9 9 GLU CG C 13 36.421 0.000 . . . . . A 9 GLU CG . 19258 1 88 . 1 1 9 9 GLU N N 15 121.984 0.007 . . . . . A 9 GLU N . 19258 1 89 . 1 1 10 10 LYS H H 1 8.355 0.001 . . . . . A 10 LYS H . 19258 1 90 . 1 1 10 10 LYS HA H 1 4.322 0.010 . . . . . A 10 LYS HA . 19258 1 91 . 1 1 10 10 LYS HB2 H 1 1.806 0.000 . . . . . A 10 LYS HB2 . 19258 1 92 . 1 1 10 10 LYS HB3 H 1 1.806 0.000 . . . . . A 10 LYS HB3 . 19258 1 93 . 1 1 10 10 LYS HG2 H 1 1.493 0.000 . . . . . A 10 LYS HG2 . 19258 1 94 . 1 1 10 10 LYS HG3 H 1 1.493 0.000 . . . . . A 10 LYS HG3 . 19258 1 95 . 1 1 10 10 LYS HD2 H 1 1.735 0.000 . . . . . A 10 LYS HD2 . 19258 1 96 . 1 1 10 10 LYS HD3 H 1 1.735 0.000 . . . . . A 10 LYS HD3 . 19258 1 97 . 1 1 10 10 LYS HE2 H 1 3.052 0.000 . . . . . A 10 LYS HE2 . 19258 1 98 . 1 1 10 10 LYS HE3 H 1 3.052 0.000 . . . . . A 10 LYS HE3 . 19258 1 99 . 1 1 10 10 LYS C C 13 176.274 0.013 . . . . . A 10 LYS C . 19258 1 100 . 1 1 10 10 LYS CA C 13 56.401 0.029 . . . . . A 10 LYS CA . 19258 1 101 . 1 1 10 10 LYS CB C 13 32.607 0.010 . . . . . A 10 LYS CB . 19258 1 102 . 1 1 10 10 LYS CG C 13 24.713 0.006 . . . . . A 10 LYS CG . 19258 1 103 . 1 1 10 10 LYS CD C 13 29.169 0.054 . . . . . A 10 LYS CD . 19258 1 104 . 1 1 10 10 LYS CE C 13 42.288 0.051 . . . . . A 10 LYS CE . 19258 1 105 . 1 1 10 10 LYS N N 15 123.894 0.004 . . . . . A 10 LYS N . 19258 1 106 . 1 1 11 11 LEU H H 1 8.631 0.000 . . . . . A 11 LEU H . 19258 1 107 . 1 1 11 11 LEU HA H 1 4.708 0.002 . . . . . A 11 LEU HA . 19258 1 108 . 1 1 11 11 LEU HB2 H 1 1.868 0.001 . . . . . A 11 LEU HB2 . 19258 1 109 . 1 1 11 11 LEU HB3 H 1 1.458 0.001 . . . . . A 11 LEU HB3 . 19258 1 110 . 1 1 11 11 LEU HG H 1 1.131 0.000 . . . . . A 11 LEU HG . 19258 1 111 . 1 1 11 11 LEU HD11 H 1 0.846 0.000 . . . . . A 11 LEU HD11 . 19258 1 112 . 1 1 11 11 LEU HD12 H 1 0.846 0.000 . . . . . A 11 LEU HD12 . 19258 1 113 . 1 1 11 11 LEU HD13 H 1 0.846 0.000 . . . . . A 11 LEU HD13 . 19258 1 114 . 1 1 11 11 LEU HD21 H 1 0.846 0.000 . . . . . A 11 LEU HD21 . 19258 1 115 . 1 1 11 11 LEU HD22 H 1 0.846 0.000 . . . . . A 11 LEU HD22 . 19258 1 116 . 1 1 11 11 LEU HD23 H 1 0.846 0.000 . . . . . A 11 LEU HD23 . 19258 1 117 . 1 1 11 11 LEU C C 13 174.153 0.000 . . . . . A 11 LEU C . 19258 1 118 . 1 1 11 11 LEU CA C 13 52.660 0.032 . . . . . A 11 LEU CA . 19258 1 119 . 1 1 11 11 LEU CB C 13 42.469 0.017 . . . . . A 11 LEU CB . 19258 1 120 . 1 1 11 11 LEU CG C 13 26.552 0.000 . . . . . A 11 LEU CG . 19258 1 121 . 1 1 11 11 LEU CD1 C 13 23.726 0.000 . . . . . A 11 LEU CD1 . 19258 1 122 . 1 1 11 11 LEU CD2 C 13 23.726 0.000 . . . . . A 11 LEU CD2 . 19258 1 123 . 1 1 11 11 LEU N N 15 125.448 0.007 . . . . . A 11 LEU N . 19258 1 124 . 1 1 12 12 PRO HA H 1 4.889 0.005 . . . . . A 12 PRO HA . 19258 1 125 . 1 1 12 12 PRO HB2 H 1 2.647 0.000 . . . . . A 12 PRO HB2 . 19258 1 126 . 1 1 12 12 PRO HB3 H 1 2.026 0.000 . . . . . A 12 PRO HB3 . 19258 1 127 . 1 1 12 12 PRO HG2 H 1 1.813 0.000 . . . . . A 12 PRO HG2 . 19258 1 128 . 1 1 12 12 PRO HG3 H 1 1.643 0.000 . . . . . A 12 PRO HG3 . 19258 1 129 . 1 1 12 12 PRO HD2 H 1 3.725 0.004 . . . . . A 12 PRO HD2 . 19258 1 130 . 1 1 12 12 PRO HD3 H 1 3.058 0.009 . . . . . A 12 PRO HD3 . 19258 1 131 . 1 1 12 12 PRO CA C 13 61.545 0.000 . . . . . A 12 PRO CA . 19258 1 132 . 1 1 12 12 PRO CB C 13 29.837 0.002 . . . . . A 12 PRO CB . 19258 1 133 . 1 1 12 12 PRO CG C 13 27.454 0.010 . . . . . A 12 PRO CG . 19258 1 134 . 1 1 12 12 PRO CD C 13 50.475 0.032 . . . . . A 12 PRO CD . 19258 1 135 . 1 1 13 13 PRO HA H 1 4.382 0.013 . . . . . A 13 PRO HA . 19258 1 136 . 1 1 13 13 PRO HB2 H 1 2.313 0.029 . . . . . A 13 PRO HB2 . 19258 1 137 . 1 1 13 13 PRO HB3 H 1 1.874 0.022 . . . . . A 13 PRO HB3 . 19258 1 138 . 1 1 13 13 PRO HG2 H 1 2.174 0.000 . . . . . A 13 PRO HG2 . 19258 1 139 . 1 1 13 13 PRO HG3 H 1 2.054 0.000 . . . . . A 13 PRO HG3 . 19258 1 140 . 1 1 13 13 PRO HD2 H 1 3.934 0.001 . . . . . A 13 PRO HD2 . 19258 1 141 . 1 1 13 13 PRO HD3 H 1 3.677 0.000 . . . . . A 13 PRO HD3 . 19258 1 142 . 1 1 13 13 PRO C C 13 177.066 0.000 . . . . . A 13 PRO C . 19258 1 143 . 1 1 13 13 PRO CA C 13 64.387 0.038 . . . . . A 13 PRO CA . 19258 1 144 . 1 1 13 13 PRO CB C 13 31.992 0.027 . . . . . A 13 PRO CB . 19258 1 145 . 1 1 13 13 PRO CG C 13 27.758 0.053 . . . . . A 13 PRO CG . 19258 1 146 . 1 1 13 13 PRO CD C 13 50.542 0.063 . . . . . A 13 PRO CD . 19258 1 147 . 1 1 14 14 GLY H H 1 8.792 0.002 . . . . . A 14 GLY H . 19258 1 148 . 1 1 14 14 GLY HA2 H 1 4.048 0.012 . . . . . A 14 GLY HA2 . 19258 1 149 . 1 1 14 14 GLY HA3 H 1 3.355 0.014 . . . . . A 14 GLY HA3 . 19258 1 150 . 1 1 14 14 GLY C C 13 172.895 0.010 . . . . . A 14 GLY C . 19258 1 151 . 1 1 14 14 GLY CA C 13 44.983 0.025 . . . . . A 14 GLY CA . 19258 1 152 . 1 1 14 14 GLY N N 15 111.904 0.011 . . . . . A 14 GLY N . 19258 1 153 . 1 1 15 15 TRP H H 1 7.403 0.001 . . . . . A 15 TRP H . 19258 1 154 . 1 1 15 15 TRP HA H 1 5.325 0.010 . . . . . A 15 TRP HA . 19258 1 155 . 1 1 15 15 TRP HB2 H 1 3.273 0.009 . . . . . A 15 TRP HB2 . 19258 1 156 . 1 1 15 15 TRP HB3 H 1 2.990 0.011 . . . . . A 15 TRP HB3 . 19258 1 157 . 1 1 15 15 TRP HD1 H 1 6.980 0.000 . . . . . A 15 TRP HD1 . 19258 1 158 . 1 1 15 15 TRP HE1 H 1 10.613 0.000 . . . . . A 15 TRP HE1 . 19258 1 159 . 1 1 15 15 TRP HE3 H 1 7.417 0.000 . . . . . A 15 TRP HE3 . 19258 1 160 . 1 1 15 15 TRP HZ2 H 1 7.468 0.000 . . . . . A 15 TRP HZ2 . 19258 1 161 . 1 1 15 15 TRP HZ3 H 1 6.934 0.000 . . . . . A 15 TRP HZ3 . 19258 1 162 . 1 1 15 15 TRP HH2 H 1 7.016 0.000 . . . . . A 15 TRP HH2 . 19258 1 163 . 1 1 15 15 TRP C C 13 176.565 0.007 . . . . . A 15 TRP C . 19258 1 164 . 1 1 15 15 TRP CA C 13 57.194 0.045 . . . . . A 15 TRP CA . 19258 1 165 . 1 1 15 15 TRP CB C 13 32.583 0.009 . . . . . A 15 TRP CB . 19258 1 166 . 1 1 15 15 TRP CD1 C 13 128.038 0.000 . . . . . A 15 TRP CD1 . 19258 1 167 . 1 1 15 15 TRP CE3 C 13 120.434 0.000 . . . . . A 15 TRP CE3 . 19258 1 168 . 1 1 15 15 TRP CZ2 C 13 114.901 0.000 . . . . . A 15 TRP CZ2 . 19258 1 169 . 1 1 15 15 TRP CZ3 C 13 122.782 0.000 . . . . . A 15 TRP CZ3 . 19258 1 170 . 1 1 15 15 TRP CH2 C 13 125.235 0.000 . . . . . A 15 TRP CH2 . 19258 1 171 . 1 1 15 15 TRP N N 15 117.202 0.005 . . . . . A 15 TRP N . 19258 1 172 . 1 1 15 15 TRP NE1 N 15 129.898 0.000 . . . . . A 15 TRP NE1 . 19258 1 173 . 1 1 16 16 GLU H H 1 9.855 0.001 . . . . . A 16 GLU H . 19258 1 174 . 1 1 16 16 GLU HA H 1 4.879 0.008 . . . . . A 16 GLU HA . 19258 1 175 . 1 1 16 16 GLU HB2 H 1 2.247 0.010 . . . . . A 16 GLU HB2 . 19258 1 176 . 1 1 16 16 GLU HB3 H 1 2.247 0.010 . . . . . A 16 GLU HB3 . 19258 1 177 . 1 1 16 16 GLU HG2 H 1 2.530 0.000 . . . . . A 16 GLU HG2 . 19258 1 178 . 1 1 16 16 GLU HG3 H 1 2.359 0.000 . . . . . A 16 GLU HG3 . 19258 1 179 . 1 1 16 16 GLU C C 13 174.084 0.005 . . . . . A 16 GLU C . 19258 1 180 . 1 1 16 16 GLU CA C 13 54.808 0.030 . . . . . A 16 GLU CA . 19258 1 181 . 1 1 16 16 GLU CB C 13 34.707 0.026 . . . . . A 16 GLU CB . 19258 1 182 . 1 1 16 16 GLU CG C 13 36.531 0.025 . . . . . A 16 GLU CG . 19258 1 183 . 1 1 16 16 GLU N N 15 120.928 0.008 . . . . . A 16 GLU N . 19258 1 184 . 1 1 17 17 LYS H H 1 8.981 0.001 . . . . . A 17 LYS H . 19258 1 185 . 1 1 17 17 LYS HA H 1 4.457 0.006 . . . . . A 17 LYS HA . 19258 1 186 . 1 1 17 17 LYS HB2 H 1 1.786 0.012 . . . . . A 17 LYS HB2 . 19258 1 187 . 1 1 17 17 LYS HB3 H 1 1.639 0.008 . . . . . A 17 LYS HB3 . 19258 1 188 . 1 1 17 17 LYS HG2 H 1 1.095 0.000 . . . . . A 17 LYS HG2 . 19258 1 189 . 1 1 17 17 LYS HG3 H 1 1.095 0.000 . . . . . A 17 LYS HG3 . 19258 1 190 . 1 1 17 17 LYS HD2 H 1 1.744 0.000 . . . . . A 17 LYS HD2 . 19258 1 191 . 1 1 17 17 LYS HD3 H 1 1.744 0.000 . . . . . A 17 LYS HD3 . 19258 1 192 . 1 1 17 17 LYS HE2 H 1 2.981 0.000 . . . . . A 17 LYS HE2 . 19258 1 193 . 1 1 17 17 LYS HE3 H 1 2.981 0.000 . . . . . A 17 LYS HE3 . 19258 1 194 . 1 1 17 17 LYS C C 13 175.463 0.006 . . . . . A 17 LYS C . 19258 1 195 . 1 1 17 17 LYS CA C 13 56.121 0.034 . . . . . A 17 LYS CA . 19258 1 196 . 1 1 17 17 LYS CB C 13 34.015 0.033 . . . . . A 17 LYS CB . 19258 1 197 . 1 1 17 17 LYS CG C 13 25.231 0.009 . . . . . A 17 LYS CG . 19258 1 198 . 1 1 17 17 LYS CD C 13 29.900 0.000 . . . . . A 17 LYS CD . 19258 1 199 . 1 1 17 17 LYS CE C 13 42.079 0.024 . . . . . A 17 LYS CE . 19258 1 200 . 1 1 17 17 LYS N N 15 125.558 0.006 . . . . . A 17 LYS N . 19258 1 201 . 1 1 18 18 ARG H H 1 8.823 0.001 . . . . . A 18 ARG H . 19258 1 202 . 1 1 18 18 ARG HA H 1 4.473 0.009 . . . . . A 18 ARG HA . 19258 1 203 . 1 1 18 18 ARG HB2 H 1 1.335 0.009 . . . . . A 18 ARG HB2 . 19258 1 204 . 1 1 18 18 ARG HB3 H 1 0.122 0.012 . . . . . A 18 ARG HB3 . 19258 1 205 . 1 1 18 18 ARG HG2 H 1 1.426 0.000 . . . . . A 18 ARG HG2 . 19258 1 206 . 1 1 18 18 ARG HG3 H 1 1.275 0.000 . . . . . A 18 ARG HG3 . 19258 1 207 . 1 1 18 18 ARG HD2 H 1 2.920 0.000 . . . . . A 18 ARG HD2 . 19258 1 208 . 1 1 18 18 ARG HD3 H 1 2.632 0.001 . . . . . A 18 ARG HD3 . 19258 1 209 . 1 1 18 18 ARG C C 13 173.197 0.007 . . . . . A 18 ARG C . 19258 1 210 . 1 1 18 18 ARG CA C 13 54.534 0.036 . . . . . A 18 ARG CA . 19258 1 211 . 1 1 18 18 ARG CB C 13 34.633 0.088 . . . . . A 18 ARG CB . 19258 1 212 . 1 1 18 18 ARG CG C 13 28.090 0.001 . . . . . A 18 ARG CG . 19258 1 213 . 1 1 18 18 ARG CD C 13 43.704 0.021 . . . . . A 18 ARG CD . 19258 1 214 . 1 1 18 18 ARG N N 15 126.826 0.008 . . . . . A 18 ARG N . 19258 1 215 . 1 1 19 19 MET H H 1 8.257 0.001 . . . . . A 19 MET H . 19258 1 216 . 1 1 19 19 MET HA H 1 4.948 0.006 . . . . . A 19 MET HA . 19258 1 217 . 1 1 19 19 MET HB2 H 1 1.884 0.011 . . . . . A 19 MET HB2 . 19258 1 218 . 1 1 19 19 MET HB3 H 1 1.884 0.011 . . . . . A 19 MET HB3 . 19258 1 219 . 1 1 19 19 MET HG2 H 1 2.470 0.000 . . . . . A 19 MET HG2 . 19258 1 220 . 1 1 19 19 MET HG3 H 1 2.315 0.000 . . . . . A 19 MET HG3 . 19258 1 221 . 1 1 19 19 MET HE1 H 1 2.023 0.000 . . . . . A 19 MET HE1 . 19258 1 222 . 1 1 19 19 MET HE2 H 1 2.023 0.000 . . . . . A 19 MET HE2 . 19258 1 223 . 1 1 19 19 MET HE3 H 1 2.023 0.000 . . . . . A 19 MET HE3 . 19258 1 224 . 1 1 19 19 MET C C 13 176.693 0.006 . . . . . A 19 MET C . 19258 1 225 . 1 1 19 19 MET CA C 13 54.110 0.071 . . . . . A 19 MET CA . 19258 1 226 . 1 1 19 19 MET CB C 13 34.442 0.035 . . . . . A 19 MET CB . 19258 1 227 . 1 1 19 19 MET CG C 13 31.867 0.023 . . . . . A 19 MET CG . 19258 1 228 . 1 1 19 19 MET CE C 13 16.805 0.000 . . . . . A 19 MET CE . 19258 1 229 . 1 1 19 19 MET N N 15 117.434 0.006 . . . . . A 19 MET N . 19258 1 230 . 1 1 20 20 SER H H 1 9.065 0.001 . . . . . A 20 SER H . 19258 1 231 . 1 1 20 20 SER HA H 1 4.788 0.005 . . . . . A 20 SER HA . 19258 1 232 . 1 1 20 20 SER HB2 H 1 4.340 0.006 . . . . . A 20 SER HB2 . 19258 1 233 . 1 1 20 20 SER HB3 H 1 4.215 0.006 . . . . . A 20 SER HB3 . 19258 1 234 . 1 1 20 20 SER C C 13 176.191 0.000 . . . . . A 20 SER C . 19258 1 235 . 1 1 20 20 SER CA C 13 57.775 0.041 . . . . . A 20 SER CA . 19258 1 236 . 1 1 20 20 SER CB C 13 63.433 0.030 . . . . . A 20 SER CB . 19258 1 237 . 1 1 20 20 SER N N 15 121.115 0.009 . . . . . A 20 SER N . 19258 1 238 . 1 1 21 21 ARG HA H 1 4.199 0.007 . . . . . A 21 ARG HA . 19258 1 239 . 1 1 21 21 ARG HB2 H 1 1.977 0.000 . . . . . A 21 ARG HB2 . 19258 1 240 . 1 1 21 21 ARG HB3 H 1 1.977 0.000 . . . . . A 21 ARG HB3 . 19258 1 241 . 1 1 21 21 ARG HG2 H 1 1.818 0.000 . . . . . A 21 ARG HG2 . 19258 1 242 . 1 1 21 21 ARG HG3 H 1 1.764 0.000 . . . . . A 21 ARG HG3 . 19258 1 243 . 1 1 21 21 ARG HD2 H 1 3.270 0.007 . . . . . A 21 ARG HD2 . 19258 1 244 . 1 1 21 21 ARG HD3 H 1 3.270 0.007 . . . . . A 21 ARG HD3 . 19258 1 245 . 1 1 21 21 ARG CA C 13 58.504 0.000 . . . . . A 21 ARG CA . 19258 1 246 . 1 1 21 21 ARG CB C 13 30.032 0.000 . . . . . A 21 ARG CB . 19258 1 247 . 1 1 21 21 ARG CG C 13 27.426 0.004 . . . . . A 21 ARG CG . 19258 1 248 . 1 1 21 21 ARG CD C 13 43.203 0.007 . . . . . A 21 ARG CD . 19258 1 249 . 1 1 22 22 SER HA H 1 4.418 0.005 . . . . . A 22 SER HA . 19258 1 250 . 1 1 22 22 SER HB2 H 1 3.947 0.000 . . . . . A 22 SER HB2 . 19258 1 251 . 1 1 22 22 SER HB3 H 1 3.947 0.000 . . . . . A 22 SER HB3 . 19258 1 252 . 1 1 22 22 SER CA C 13 59.979 0.014 . . . . . A 22 SER CA . 19258 1 253 . 1 1 22 22 SER CB C 13 62.892 0.000 . . . . . A 22 SER CB . 19258 1 254 . 1 1 23 23 SER HA H 1 4.672 0.008 . . . . . A 23 SER HA . 19258 1 255 . 1 1 23 23 SER HB2 H 1 4.013 0.009 . . . . . A 23 SER HB2 . 19258 1 256 . 1 1 23 23 SER HB3 H 1 3.886 0.010 . . . . . A 23 SER HB3 . 19258 1 257 . 1 1 23 23 SER C C 13 175.707 0.000 . . . . . A 23 SER C . 19258 1 258 . 1 1 23 23 SER CA C 13 58.279 0.021 . . . . . A 23 SER CA . 19258 1 259 . 1 1 23 23 SER CB C 13 65.694 0.073 . . . . . A 23 SER CB . 19258 1 260 . 1 1 24 24 GLY H H 1 8.170 0.002 . . . . . A 24 GLY H . 19258 1 261 . 1 1 24 24 GLY HA2 H 1 4.117 0.000 . . . . . A 24 GLY HA2 . 19258 1 262 . 1 1 24 24 GLY HA3 H 1 3.941 0.000 . . . . . A 24 GLY HA3 . 19258 1 263 . 1 1 24 24 GLY C C 13 173.424 0.011 . . . . . A 24 GLY C . 19258 1 264 . 1 1 24 24 GLY CA C 13 46.317 0.017 . . . . . A 24 GLY CA . 19258 1 265 . 1 1 24 24 GLY N N 15 112.205 0.006 . . . . . A 24 GLY N . 19258 1 266 . 1 1 25 25 ARG H H 1 7.695 0.001 . . . . . A 25 ARG H . 19258 1 267 . 1 1 25 25 ARG HA H 1 4.514 0.010 . . . . . A 25 ARG HA . 19258 1 268 . 1 1 25 25 ARG HB2 H 1 1.966 0.006 . . . . . A 25 ARG HB2 . 19258 1 269 . 1 1 25 25 ARG HB3 H 1 1.765 0.014 . . . . . A 25 ARG HB3 . 19258 1 270 . 1 1 25 25 ARG HG2 H 1 1.781 0.005 . . . . . A 25 ARG HG2 . 19258 1 271 . 1 1 25 25 ARG HG3 H 1 1.710 0.002 . . . . . A 25 ARG HG3 . 19258 1 272 . 1 1 25 25 ARG HD2 H 1 2.878 0.004 . . . . . A 25 ARG HD2 . 19258 1 273 . 1 1 25 25 ARG HD3 H 1 2.527 0.004 . . . . . A 25 ARG HD3 . 19258 1 274 . 1 1 25 25 ARG C C 13 176.089 0.005 . . . . . A 25 ARG C . 19258 1 275 . 1 1 25 25 ARG CA C 13 56.111 0.035 . . . . . A 25 ARG CA . 19258 1 276 . 1 1 25 25 ARG CB C 13 32.780 0.021 . . . . . A 25 ARG CB . 19258 1 277 . 1 1 25 25 ARG CG C 13 26.920 0.023 . . . . . A 25 ARG CG . 19258 1 278 . 1 1 25 25 ARG CD C 13 43.496 0.023 . . . . . A 25 ARG CD . 19258 1 279 . 1 1 25 25 ARG N N 15 119.359 0.008 . . . . . A 25 ARG N . 19258 1 280 . 1 1 26 26 VAL H H 1 8.570 0.001 . . . . . A 26 VAL H . 19258 1 281 . 1 1 26 26 VAL HA H 1 4.750 0.008 . . . . . A 26 VAL HA . 19258 1 282 . 1 1 26 26 VAL HB H 1 2.015 0.010 . . . . . A 26 VAL HB . 19258 1 283 . 1 1 26 26 VAL HG11 H 1 1.063 0.001 . . . . . A 26 VAL HG11 . 19258 1 284 . 1 1 26 26 VAL HG12 H 1 1.063 0.001 . . . . . A 26 VAL HG12 . 19258 1 285 . 1 1 26 26 VAL HG13 H 1 1.063 0.001 . . . . . A 26 VAL HG13 . 19258 1 286 . 1 1 26 26 VAL HG21 H 1 0.840 0.000 . . . . . A 26 VAL HG21 . 19258 1 287 . 1 1 26 26 VAL HG22 H 1 0.840 0.000 . . . . . A 26 VAL HG22 . 19258 1 288 . 1 1 26 26 VAL HG23 H 1 0.840 0.000 . . . . . A 26 VAL HG23 . 19258 1 289 . 1 1 26 26 VAL C C 13 175.248 0.007 . . . . . A 26 VAL C . 19258 1 290 . 1 1 26 26 VAL CA C 13 62.247 0.027 . . . . . A 26 VAL CA . 19258 1 291 . 1 1 26 26 VAL CB C 13 33.016 0.086 . . . . . A 26 VAL CB . 19258 1 292 . 1 1 26 26 VAL CG1 C 13 21.802 0.090 . . . . . A 26 VAL CG1 . 19258 1 293 . 1 1 26 26 VAL CG2 C 13 21.802 0.090 . . . . . A 26 VAL CG2 . 19258 1 294 . 1 1 26 26 VAL N N 15 124.995 0.007 . . . . . A 26 VAL N . 19258 1 295 . 1 1 27 27 TYR H H 1 8.756 0.001 . . . . . A 27 TYR H . 19258 1 296 . 1 1 27 27 TYR HA H 1 4.931 0.006 . . . . . A 27 TYR HA . 19258 1 297 . 1 1 27 27 TYR HB2 H 1 2.938 0.004 . . . . . A 27 TYR HB2 . 19258 1 298 . 1 1 27 27 TYR HB3 H 1 2.532 0.007 . . . . . A 27 TYR HB3 . 19258 1 299 . 1 1 27 27 TYR HD1 H 1 6.896 0.000 . . . . . A 27 TYR HD1 . 19258 1 300 . 1 1 27 27 TYR HD2 H 1 6.896 0.000 . . . . . A 27 TYR HD2 . 19258 1 301 . 1 1 27 27 TYR HE1 H 1 6.430 0.000 . . . . . A 27 TYR HE1 . 19258 1 302 . 1 1 27 27 TYR HE2 H 1 6.430 0.000 . . . . . A 27 TYR HE2 . 19258 1 303 . 1 1 27 27 TYR C C 13 170.738 0.006 . . . . . A 27 TYR C . 19258 1 304 . 1 1 27 27 TYR CA C 13 55.484 0.044 . . . . . A 27 TYR CA . 19258 1 305 . 1 1 27 27 TYR CB C 13 39.898 0.013 . . . . . A 27 TYR CB . 19258 1 306 . 1 1 27 27 TYR CD1 C 13 134.114 0.000 . . . . . A 27 TYR CD1 . 19258 1 307 . 1 1 27 27 TYR CE1 C 13 117.449 0.000 . . . . . A 27 TYR CE1 . 19258 1 308 . 1 1 27 27 TYR N N 15 121.587 0.005 . . . . . A 27 TYR N . 19258 1 309 . 1 1 28 28 TYR H H 1 9.024 0.001 . . . . . A 28 TYR H . 19258 1 310 . 1 1 28 28 TYR HA H 1 5.279 0.009 . . . . . A 28 TYR HA . 19258 1 311 . 1 1 28 28 TYR HB2 H 1 2.931 0.011 . . . . . A 28 TYR HB2 . 19258 1 312 . 1 1 28 28 TYR HB3 H 1 2.687 0.011 . . . . . A 28 TYR HB3 . 19258 1 313 . 1 1 28 28 TYR HD1 H 1 6.839 0.000 . . . . . A 28 TYR HD1 . 19258 1 314 . 1 1 28 28 TYR HD2 H 1 6.839 0.000 . . . . . A 28 TYR HD2 . 19258 1 315 . 1 1 28 28 TYR HE1 H 1 6.772 0.000 . . . . . A 28 TYR HE1 . 19258 1 316 . 1 1 28 28 TYR HE2 H 1 6.772 0.000 . . . . . A 28 TYR HE2 . 19258 1 317 . 1 1 28 28 TYR C C 13 174.276 0.007 . . . . . A 28 TYR C . 19258 1 318 . 1 1 28 28 TYR CA C 13 57.193 0.036 . . . . . A 28 TYR CA . 19258 1 319 . 1 1 28 28 TYR CB C 13 41.315 0.014 . . . . . A 28 TYR CB . 19258 1 320 . 1 1 28 28 TYR CD2 C 13 133.711 0.000 . . . . . A 28 TYR CD2 . 19258 1 321 . 1 1 28 28 TYR CE2 C 13 117.203 0.000 . . . . . A 28 TYR CE2 . 19258 1 322 . 1 1 28 28 TYR N N 15 117.065 0.004 . . . . . A 28 TYR N . 19258 1 323 . 1 1 29 29 PHE H H 1 9.442 0.002 . . . . . A 29 PHE H . 19258 1 324 . 1 1 29 29 PHE HA H 1 5.625 0.007 . . . . . A 29 PHE HA . 19258 1 325 . 1 1 29 29 PHE HB2 H 1 2.909 0.007 . . . . . A 29 PHE HB2 . 19258 1 326 . 1 1 29 29 PHE HB3 H 1 2.603 0.013 . . . . . A 29 PHE HB3 . 19258 1 327 . 1 1 29 29 PHE HD1 H 1 6.900 0.000 . . . . . A 29 PHE HD1 . 19258 1 328 . 1 1 29 29 PHE HD2 H 1 6.900 0.000 . . . . . A 29 PHE HD2 . 19258 1 329 . 1 1 29 29 PHE HE1 H 1 6.994 0.000 . . . . . A 29 PHE HE1 . 19258 1 330 . 1 1 29 29 PHE HE2 H 1 6.994 0.000 . . . . . A 29 PHE HE2 . 19258 1 331 . 1 1 29 29 PHE HZ H 1 7.310 0.000 . . . . . A 29 PHE HZ . 19258 1 332 . 1 1 29 29 PHE C C 13 172.638 0.005 . . . . . A 29 PHE C . 19258 1 333 . 1 1 29 29 PHE CA C 13 55.977 0.037 . . . . . A 29 PHE CA . 19258 1 334 . 1 1 29 29 PHE CB C 13 44.449 0.029 . . . . . A 29 PHE CB . 19258 1 335 . 1 1 29 29 PHE CD2 C 13 131.624 0.000 . . . . . A 29 PHE CD2 . 19258 1 336 . 1 1 29 29 PHE CE2 C 13 130.904 0.000 . . . . . A 29 PHE CE2 . 19258 1 337 . 1 1 29 29 PHE CZ C 13 130.126 0.000 . . . . . A 29 PHE CZ . 19258 1 338 . 1 1 29 29 PHE N N 15 124.816 0.005 . . . . . A 29 PHE N . 19258 1 339 . 1 1 30 30 ASN H H 1 8.123 0.001 . . . . . A 30 ASN H . 19258 1 340 . 1 1 30 30 ASN HA H 1 4.450 0.012 . . . . . A 30 ASN HA . 19258 1 341 . 1 1 30 30 ASN HB2 H 1 1.999 0.009 . . . . . A 30 ASN HB2 . 19258 1 342 . 1 1 30 30 ASN HB3 H 1 -0.627 0.000 . . . . . A 30 ASN HB3 . 19258 1 343 . 1 1 30 30 ASN C C 13 174.648 0.006 . . . . . A 30 ASN C . 19258 1 344 . 1 1 30 30 ASN CA C 13 50.619 0.033 . . . . . A 30 ASN CA . 19258 1 345 . 1 1 30 30 ASN CB C 13 38.193 0.006 . . . . . A 30 ASN CB . 19258 1 346 . 1 1 30 30 ASN N N 15 128.938 0.007 . . . . . A 30 ASN N . 19258 1 347 . 1 1 31 31 HIS H H 1 8.201 0.007 . . . . . A 31 HIS H . 19258 1 348 . 1 1 31 31 HIS HA H 1 4.110 0.009 . . . . . A 31 HIS HA . 19258 1 349 . 1 1 31 31 HIS HB2 H 1 3.244 0.011 . . . . . A 31 HIS HB2 . 19258 1 350 . 1 1 31 31 HIS HB3 H 1 3.058 0.016 . . . . . A 31 HIS HB3 . 19258 1 351 . 1 1 31 31 HIS HD2 H 1 6.962 0.000 . . . . . A 31 HIS HD2 . 19258 1 352 . 1 1 31 31 HIS HE1 H 1 7.751 0.000 . . . . . A 31 HIS HE1 . 19258 1 353 . 1 1 31 31 HIS C C 13 176.224 0.007 . . . . . A 31 HIS C . 19258 1 354 . 1 1 31 31 HIS CA C 13 57.889 0.056 . . . . . A 31 HIS CA . 19258 1 355 . 1 1 31 31 HIS CB C 13 30.487 0.023 . . . . . A 31 HIS CB . 19258 1 356 . 1 1 31 31 HIS CD2 C 13 121.352 0.000 . . . . . A 31 HIS CD2 . 19258 1 357 . 1 1 31 31 HIS CE1 C 13 138.479 0.000 . . . . . A 31 HIS CE1 . 19258 1 358 . 1 1 31 31 HIS N N 15 121.514 0.011 . . . . . A 31 HIS N . 19258 1 359 . 1 1 32 32 ILE H H 1 8.260 0.001 . . . . . A 32 ILE H . 19258 1 360 . 1 1 32 32 ILE HA H 1 3.852 0.009 . . . . . A 32 ILE HA . 19258 1 361 . 1 1 32 32 ILE HB H 1 2.000 0.016 . . . . . A 32 ILE HB . 19258 1 362 . 1 1 32 32 ILE HG12 H 1 1.328 0.000 . . . . . A 32 ILE HG12 . 19258 1 363 . 1 1 32 32 ILE HG13 H 1 1.012 0.000 . . . . . A 32 ILE HG13 . 19258 1 364 . 1 1 32 32 ILE HG21 H 1 0.790 0.000 . . . . . A 32 ILE HG21 . 19258 1 365 . 1 1 32 32 ILE HG22 H 1 0.790 0.000 . . . . . A 32 ILE HG22 . 19258 1 366 . 1 1 32 32 ILE HG23 H 1 0.790 0.000 . . . . . A 32 ILE HG23 . 19258 1 367 . 1 1 32 32 ILE HD11 H 1 0.755 0.000 . . . . . A 32 ILE HD11 . 19258 1 368 . 1 1 32 32 ILE HD12 H 1 0.755 0.000 . . . . . A 32 ILE HD12 . 19258 1 369 . 1 1 32 32 ILE HD13 H 1 0.755 0.000 . . . . . A 32 ILE HD13 . 19258 1 370 . 1 1 32 32 ILE C C 13 178.171 0.009 . . . . . A 32 ILE C . 19258 1 371 . 1 1 32 32 ILE CA C 13 63.409 0.007 . . . . . A 32 ILE CA . 19258 1 372 . 1 1 32 32 ILE CB C 13 37.191 0.014 . . . . . A 32 ILE CB . 19258 1 373 . 1 1 32 32 ILE CG1 C 13 27.987 0.035 . . . . . A 32 ILE CG1 . 19258 1 374 . 1 1 32 32 ILE CG2 C 13 17.120 0.002 . . . . . A 32 ILE CG2 . 19258 1 375 . 1 1 32 32 ILE CD1 C 13 12.156 0.007 . . . . . A 32 ILE CD1 . 19258 1 376 . 1 1 32 32 ILE N N 15 121.479 0.011 . . . . . A 32 ILE N . 19258 1 377 . 1 1 33 33 THR H H 1 7.424 0.001 . . . . . A 33 THR H . 19258 1 378 . 1 1 33 33 THR HA H 1 4.106 0.006 . . . . . A 33 THR HA . 19258 1 379 . 1 1 33 33 THR HB H 1 4.246 0.006 . . . . . A 33 THR HB . 19258 1 380 . 1 1 33 33 THR HG21 H 1 0.961 0.005 . . . . . A 33 THR HG21 . 19258 1 381 . 1 1 33 33 THR HG22 H 1 0.961 0.005 . . . . . A 33 THR HG22 . 19258 1 382 . 1 1 33 33 THR HG23 H 1 0.961 0.005 . . . . . A 33 THR HG23 . 19258 1 383 . 1 1 33 33 THR C C 13 176.108 0.009 . . . . . A 33 THR C . 19258 1 384 . 1 1 33 33 THR CA C 13 61.293 0.038 . . . . . A 33 THR CA . 19258 1 385 . 1 1 33 33 THR CB C 13 70.098 0.005 . . . . . A 33 THR CB . 19258 1 386 . 1 1 33 33 THR CG2 C 13 21.208 0.005 . . . . . A 33 THR CG2 . 19258 1 387 . 1 1 33 33 THR N N 15 107.936 0.008 . . . . . A 33 THR N . 19258 1 388 . 1 1 34 34 ASN H H 1 8.088 0.001 . . . . . A 34 ASN H . 19258 1 389 . 1 1 34 34 ASN HA H 1 4.131 0.006 . . . . . A 34 ASN HA . 19258 1 390 . 1 1 34 34 ASN HB2 H 1 3.152 0.009 . . . . . A 34 ASN HB2 . 19258 1 391 . 1 1 34 34 ASN HB3 H 1 2.924 0.009 . . . . . A 34 ASN HB3 . 19258 1 392 . 1 1 34 34 ASN C C 13 173.368 0.009 . . . . . A 34 ASN C . 19258 1 393 . 1 1 34 34 ASN CA C 13 55.065 0.035 . . . . . A 34 ASN CA . 19258 1 394 . 1 1 34 34 ASN CB C 13 37.599 0.050 . . . . . A 34 ASN CB . 19258 1 395 . 1 1 34 34 ASN N N 15 118.213 0.008 . . . . . A 34 ASN N . 19258 1 396 . 1 1 35 35 ALA H H 1 7.142 0.001 . . . . . A 35 ALA H . 19258 1 397 . 1 1 35 35 ALA HA H 1 4.454 0.008 . . . . . A 35 ALA HA . 19258 1 398 . 1 1 35 35 ALA HB1 H 1 1.259 0.010 . . . . . A 35 ALA HB1 . 19258 1 399 . 1 1 35 35 ALA HB2 H 1 1.259 0.010 . . . . . A 35 ALA HB2 . 19258 1 400 . 1 1 35 35 ALA HB3 H 1 1.259 0.010 . . . . . A 35 ALA HB3 . 19258 1 401 . 1 1 35 35 ALA C C 13 175.462 0.007 . . . . . A 35 ALA C . 19258 1 402 . 1 1 35 35 ALA CA C 13 52.112 0.016 . . . . . A 35 ALA CA . 19258 1 403 . 1 1 35 35 ALA CB C 13 20.897 0.021 . . . . . A 35 ALA CB . 19258 1 404 . 1 1 35 35 ALA N N 15 121.789 0.006 . . . . . A 35 ALA N . 19258 1 405 . 1 1 36 36 SER H H 1 8.290 0.001 . . . . . A 36 SER H . 19258 1 406 . 1 1 36 36 SER HA H 1 6.041 0.008 . . . . . A 36 SER HA . 19258 1 407 . 1 1 36 36 SER HB2 H 1 3.877 0.000 . . . . . A 36 SER HB2 . 19258 1 408 . 1 1 36 36 SER HB3 H 1 3.800 0.000 . . . . . A 36 SER HB3 . 19258 1 409 . 1 1 36 36 SER C C 13 174.028 0.007 . . . . . A 36 SER C . 19258 1 410 . 1 1 36 36 SER CA C 13 56.962 0.034 . . . . . A 36 SER CA . 19258 1 411 . 1 1 36 36 SER CB C 13 66.789 0.040 . . . . . A 36 SER CB . 19258 1 412 . 1 1 36 36 SER N N 15 112.101 0.010 . . . . . A 36 SER N . 19258 1 413 . 1 1 37 37 GLN H H 1 9.377 0.001 . . . . . A 37 GLN H . 19258 1 414 . 1 1 37 37 GLN HA H 1 4.856 0.000 . . . . . A 37 GLN HA . 19258 1 415 . 1 1 37 37 GLN HB2 H 1 2.549 0.000 . . . . . A 37 GLN HB2 . 19258 1 416 . 1 1 37 37 GLN HB3 H 1 2.237 0.000 . . . . . A 37 GLN HB3 . 19258 1 417 . 1 1 37 37 GLN C C 13 174.644 0.005 . . . . . A 37 GLN C . 19258 1 418 . 1 1 37 37 GLN CA C 13 54.723 0.029 . . . . . A 37 GLN CA . 19258 1 419 . 1 1 37 37 GLN CB C 13 32.099 0.024 . . . . . A 37 GLN CB . 19258 1 420 . 1 1 37 37 GLN N N 15 116.631 0.010 . . . . . A 37 GLN N . 19258 1 421 . 1 1 38 38 TRP H H 1 8.631 0.001 . . . . . A 38 TRP H . 19258 1 422 . 1 1 38 38 TRP HA H 1 5.025 0.008 . . . . . A 38 TRP HA . 19258 1 423 . 1 1 38 38 TRP HB2 H 1 3.634 0.014 . . . . . A 38 TRP HB2 . 19258 1 424 . 1 1 38 38 TRP HB3 H 1 3.212 0.011 . . . . . A 38 TRP HB3 . 19258 1 425 . 1 1 38 38 TRP HD1 H 1 7.492 0.000 . . . . . A 38 TRP HD1 . 19258 1 426 . 1 1 38 38 TRP HE1 H 1 10.125 0.000 . . . . . A 38 TRP HE1 . 19258 1 427 . 1 1 38 38 TRP HE3 H 1 8.210 0.000 . . . . . A 38 TRP HE3 . 19258 1 428 . 1 1 38 38 TRP HZ2 H 1 7.398 0.000 . . . . . A 38 TRP HZ2 . 19258 1 429 . 1 1 38 38 TRP HZ3 H 1 6.900 0.000 . . . . . A 38 TRP HZ3 . 19258 1 430 . 1 1 38 38 TRP HH2 H 1 7.109 0.000 . . . . . A 38 TRP HH2 . 19258 1 431 . 1 1 38 38 TRP C C 13 177.164 0.006 . . . . . A 38 TRP C . 19258 1 432 . 1 1 38 38 TRP CA C 13 58.855 0.028 . . . . . A 38 TRP CA . 19258 1 433 . 1 1 38 38 TRP CB C 13 30.786 0.017 . . . . . A 38 TRP CB . 19258 1 434 . 1 1 38 38 TRP CD1 C 13 128.409 0.000 . . . . . A 38 TRP CD1 . 19258 1 435 . 1 1 38 38 TRP CE3 C 13 121.995 0.000 . . . . . A 38 TRP CE3 . 19258 1 436 . 1 1 38 38 TRP CZ2 C 13 114.616 0.000 . . . . . A 38 TRP CZ2 . 19258 1 437 . 1 1 38 38 TRP CZ3 C 13 122.714 0.000 . . . . . A 38 TRP CZ3 . 19258 1 438 . 1 1 38 38 TRP CH2 C 13 124.198 0.000 . . . . . A 38 TRP CH2 . 19258 1 439 . 1 1 38 38 TRP N N 15 120.543 0.008 . . . . . A 38 TRP N . 19258 1 440 . 1 1 38 38 TRP NE1 N 15 128.708 0.000 . . . . . A 38 TRP NE1 . 19258 1 441 . 1 1 39 39 GLU H H 1 8.129 0.001 . . . . . A 39 GLU H . 19258 1 442 . 1 1 39 39 GLU HA H 1 4.416 0.004 . . . . . A 39 GLU HA . 19258 1 443 . 1 1 39 39 GLU HB2 H 1 1.895 0.000 . . . . . A 39 GLU HB2 . 19258 1 444 . 1 1 39 39 GLU HB3 H 1 1.895 0.000 . . . . . A 39 GLU HB3 . 19258 1 445 . 1 1 39 39 GLU HG2 H 1 2.383 0.000 . . . . . A 39 GLU HG2 . 19258 1 446 . 1 1 39 39 GLU HG3 H 1 2.295 0.000 . . . . . A 39 GLU HG3 . 19258 1 447 . 1 1 39 39 GLU C C 13 175.723 0.008 . . . . . A 39 GLU C . 19258 1 448 . 1 1 39 39 GLU CA C 13 55.965 0.046 . . . . . A 39 GLU CA . 19258 1 449 . 1 1 39 39 GLU CB C 13 30.292 0.014 . . . . . A 39 GLU CB . 19258 1 450 . 1 1 39 39 GLU CG C 13 36.482 0.000 . . . . . A 39 GLU CG . 19258 1 451 . 1 1 39 39 GLU N N 15 117.041 0.005 . . . . . A 39 GLU N . 19258 1 452 . 1 1 40 40 ARG H H 1 8.535 0.001 . . . . . A 40 ARG H . 19258 1 453 . 1 1 40 40 ARG HA H 1 2.647 0.006 . . . . . A 40 ARG HA . 19258 1 454 . 1 1 40 40 ARG HB2 H 1 1.410 0.007 . . . . . A 40 ARG HB2 . 19258 1 455 . 1 1 40 40 ARG HB3 H 1 1.410 0.007 . . . . . A 40 ARG HB3 . 19258 1 456 . 1 1 40 40 ARG HG2 H 1 1.236 0.009 . . . . . A 40 ARG HG2 . 19258 1 457 . 1 1 40 40 ARG HG3 H 1 1.015 0.006 . . . . . A 40 ARG HG3 . 19258 1 458 . 1 1 40 40 ARG HD2 H 1 3.055 0.006 . . . . . A 40 ARG HD2 . 19258 1 459 . 1 1 40 40 ARG HD3 H 1 3.055 0.006 . . . . . A 40 ARG HD3 . 19258 1 460 . 1 1 40 40 ARG C C 13 174.617 0.000 . . . . . A 40 ARG C . 19258 1 461 . 1 1 40 40 ARG CA C 13 54.192 0.027 . . . . . A 40 ARG CA . 19258 1 462 . 1 1 40 40 ARG CB C 13 30.062 0.038 . . . . . A 40 ARG CB . 19258 1 463 . 1 1 40 40 ARG CG C 13 26.862 0.015 . . . . . A 40 ARG CG . 19258 1 464 . 1 1 40 40 ARG CD C 13 43.566 0.002 . . . . . A 40 ARG CD . 19258 1 465 . 1 1 40 40 ARG N N 15 125.150 0.006 . . . . . A 40 ARG N . 19258 1 466 . 1 1 41 41 PRO HA H 1 3.926 0.007 . . . . . A 41 PRO HA . 19258 1 467 . 1 1 41 41 PRO HB2 H 1 0.872 0.003 . . . . . A 41 PRO HB2 . 19258 1 468 . 1 1 41 41 PRO HB3 H 1 0.688 0.009 . . . . . A 41 PRO HB3 . 19258 1 469 . 1 1 41 41 PRO HG2 H 1 0.597 0.000 . . . . . A 41 PRO HG2 . 19258 1 470 . 1 1 41 41 PRO HG3 H 1 -0.053 0.001 . . . . . A 41 PRO HG3 . 19258 1 471 . 1 1 41 41 PRO HD2 H 1 2.443 0.000 . . . . . A 41 PRO HD2 . 19258 1 472 . 1 1 41 41 PRO HD3 H 1 2.332 0.000 . . . . . A 41 PRO HD3 . 19258 1 473 . 1 1 41 41 PRO C C 13 175.438 0.000 . . . . . A 41 PRO C . 19258 1 474 . 1 1 41 41 PRO CA C 13 61.917 0.046 . . . . . A 41 PRO CA . 19258 1 475 . 1 1 41 41 PRO CB C 13 31.366 0.017 . . . . . A 41 PRO CB . 19258 1 476 . 1 1 41 41 PRO CG C 13 25.721 0.007 . . . . . A 41 PRO CG . 19258 1 477 . 1 1 41 41 PRO CD C 13 50.053 0.045 . . . . . A 41 PRO CD . 19258 1 478 . 1 1 42 42 SER H H 1 8.196 0.002 . . . . . A 42 SER H . 19258 1 479 . 1 1 42 42 SER HA H 1 4.323 0.008 . . . . . A 42 SER HA . 19258 1 480 . 1 1 42 42 SER HB2 H 1 3.831 0.000 . . . . . A 42 SER HB2 . 19258 1 481 . 1 1 42 42 SER HB3 H 1 3.756 0.000 . . . . . A 42 SER HB3 . 19258 1 482 . 1 1 42 42 SER C C 13 173.810 0.011 . . . . . A 42 SER C . 19258 1 483 . 1 1 42 42 SER CA C 13 57.902 0.030 . . . . . A 42 SER CA . 19258 1 484 . 1 1 42 42 SER CB C 13 64.522 0.055 . . . . . A 42 SER CB . 19258 1 485 . 1 1 42 42 SER N N 15 115.552 0.008 . . . . . A 42 SER N . 19258 1 486 . 1 1 43 43 GLY H H 1 7.932 0.001 . . . . . A 43 GLY H . 19258 1 487 . 1 1 43 43 GLY HA2 H 1 3.769 0.000 . . . . . A 43 GLY HA2 . 19258 1 488 . 1 1 43 43 GLY HA3 H 1 3.769 0.000 . . . . . A 43 GLY HA3 . 19258 1 489 . 1 1 43 43 GLY C C 13 178.372 0.000 . . . . . A 43 GLY C . 19258 1 490 . 1 1 43 43 GLY CA C 13 46.182 0.017 . . . . . A 43 GLY CA . 19258 1 491 . 1 1 43 43 GLY N N 15 116.616 0.010 . . . . . A 43 GLY N . 19258 1 stop_ save_