data_15013 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15013 _Entry.Title ; Chimer between Spc-SH3 and P41 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2006-11-02 _Entry.Accession_date 2006-11-02 _Entry.Last_release_date 2007-05-10 _Entry.Original_release_date 2007-05-10 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details 'Chimer between Spc-SH3 and decapeptide P41 starting from circular permutant S19P20s' _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 Nico 'van Nuland' . A.J. . 15013 2 Adela Candel . M. . 15013 3 Jose Martinez . C. . 15013 4 Francisco Conejero-Lara . . . 15013 5 Marta Bruix . . . 15013 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' . 15013 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID chimer . 15013 P41 . 15013 Spc-SH3 . 15013 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15013 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 282 15013 '15N chemical shifts' 78 15013 '1H chemical shifts' 527 15013 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 . . 2007-05-10 2006-11-02 original author . 15013 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1TUC . 15013 PDB 2JMA . 15013 PDB 2JMC 'BMRB Entry Tracking System' 15013 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15013 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17275816 _Citation.Full_citation . _Citation.Title 'The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full . _Citation.Journal_volume 581 _Citation.Journal_issue 4 _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 687 _Citation.Page_last 692 _Citation.Year 2007 _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 Adela Candel . M. . 15013 1 2 Francisco Conejero-Lara . . . 15013 1 3 Jose Martinez . C. . 15013 1 4 Nico 'van Nuland' . A.J. . 15013 1 5 Marta Bruix . . . 15013 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'chimeric protein' 15013 1 NMR 15013 1 'proline-rich peptide' 15013 1 'protein structure' 15013 1 SH3 15013 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15013 _Assembly.ID 1 _Assembly.Name 'SPCp41 monomer' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _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 SPCp41 1 $SPCp41 A . yes native no no . . . 15013 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1TUC . . X-ray . . . 15013 1 yes PDB 2JMA . . 'solution NMR' . . . 15013 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_SPCp41 _Entity.Sf_category entity _Entity.Sf_framecode SPCp41 _Entity.Entry_ID 15013 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name SPCp41 _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 ; GAMGPREVTMKKGDILTLLN STNKDWWKVEVNDRQGFVPA AYVKKLDSGTGKELVLALYD YQESGDNAPSYSPPPPP ; _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 77 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 8470.656 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15144 . SH3_domain_from_chicken_alpha-spectrin . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 2 no BMRB 17915 . SH3 . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 3 no PDB 1AEY . "Alpha-Spectrin Src Homology 3 Domain, Solution Nmr, 15 Structures" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 4 no PDB 1M8M . "Solid-State Mas Nmr Structure Of The A-Spectrin Sh3 Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 5 no PDB 1NEG . "Crystal Structure Analysis Of N-And C-Terminal Labeled Sh3- Domain Of Alpha-Chicken Spectrin" . . . . . 54.55 83 100.00 100.00 5.77e-21 . . . . 15013 1 6 no PDB 1QKW . "Alpha-Spectrin Src Homology 3 Domain, N47g Mutant In The Distal Loop" . . . . . 55.84 62 97.67 97.67 1.02e-20 . . . . 15013 1 7 no PDB 1SHG . "Crystal Structure Of A Src-Homology 3 (Sh3) Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 8 no PDB 1TUC . "Alpha-Spectrin Src Homology 3 Domain, Circular Permutant, Cut At S19-P20" . . . . . 79.22 63 100.00 100.00 1.04e-35 . . . . 15013 1 9 no PDB 1U06 . "Crystal Structure Of Chicken Alpha-Spectrin Sh3 Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 10 no PDB 2F2V . "Alpha-Spectrin Sh3 Domain A56g Mutant" . . . . . 55.84 62 97.67 97.67 4.64e-21 . . . . 15013 1 11 no PDB 2F2X . "Alpha-Spectrin Sh3 Domain R21g Mutant" . . . . . 55.84 62 97.67 97.67 1.96e-20 . . . . 15013 1 12 no PDB 2JMC . "Chimer Between Spc-Sh3 And P41" . . . . . 100.00 77 100.00 100.00 1.13e-47 . . . . 15013 1 13 no PDB 2LJ3 . "Pfbd: High-Throughput Strategy Of Backbone Fold Determination For Small Well-Folded Proteins In Less Than A Day" . . . . . 57.14 63 97.73 97.73 7.51e-22 . . . . 15013 1 14 no PDB 2NUZ . "Crystal Structure Of Alpha Spectrin Sh3 Domain Measured At Room Temperature" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 15 no PDB 4F16 . "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 5" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 16 no PDB 4F17 . "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 9" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1 17 no DBJ BAD52438 . "non-erythrocytic spectrin alpha [Homo sapiens]" . . . . . 55.84 2452 100.00 100.00 1.34e-20 . . . . 15013 1 18 no DBJ BAD93097 . "spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) variant [Homo sapiens]" . . . . . 55.84 2506 100.00 100.00 1.77e-20 . . . . 15013 1 19 no DBJ BAG57892 . "unnamed protein product [Homo sapiens]" . . . . . 55.84 1312 100.00 100.00 1.65e-20 . . . . 15013 1 20 no DBJ BAG62120 . "unnamed protein product [Homo sapiens]" . . . . . 55.84 1176 100.00 100.00 1.03e-20 . . . . 15013 1 21 no DBJ BAG72795 . "spectrin, alpha, non-erythrocytic 1 [synthetic construct]" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 1 22 no EMBL CAA29435 . "unnamed protein product [Xenopus laevis]" . . . . . 50.65 454 100.00 100.00 2.29e-17 . . . . 15013 1 23 no EMBL CAA32663 . "spectrin alpha chain, partial [Gallus gallus]" . . . . . 55.84 2449 100.00 100.00 1.40e-20 . . . . 15013 1 24 no EMBL CAF90367 . "unnamed protein product [Tetraodon nigroviridis]" . . . . . 55.84 1589 97.67 97.67 8.03e-19 . . . . 15013 1 25 no EMBL CDQ79062 . "unnamed protein product [Oncorhynchus mykiss]" . . . . . 55.84 2460 100.00 100.00 2.36e-20 . . . . 15013 1 26 no GB AAA51702 . "alpha-fodrin, partial [Homo sapiens]" . . . . . 55.84 920 100.00 100.00 2.62e-20 . . . . 15013 1 27 no GB AAA51790 . "nonerythroid alpha-spectrin [Homo sapiens]" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 1 28 no GB AAA52468 . "alpha-fodrin, partial [Homo sapiens]" . . . . . 55.84 920 100.00 100.00 2.62e-20 . . . . 15013 1 29 no GB AAB41498 . "alpha II spectrin [Homo sapiens]" . . . . . 55.84 2477 100.00 100.00 1.28e-20 . . . . 15013 1 30 no GB AAB60364 . "alpha II spectrin, partial [Homo sapiens]" . . . . . 55.84 719 100.00 100.00 1.79e-20 . . . . 15013 1 31 no REF NP_001036003 . "spectrin alpha chain, non-erythrocytic 1 [Gallus gallus]" . . . . . 55.84 2477 100.00 100.00 1.45e-20 . . . . 15013 1 32 no REF NP_001090674 . "spectrin alpha chain, non-erythrocytic 1 [Xenopus (Silurana) tropicalis]" . . . . . 55.84 2471 100.00 100.00 1.56e-20 . . . . 15013 1 33 no REF NP_001091958 . "spectrin alpha chain, non-erythrocytic 1 [Danio rerio]" . . . . . 55.84 2480 100.00 100.00 1.87e-20 . . . . 15013 1 34 no REF NP_001123910 . "spectrin alpha chain, non-erythrocytic 1 isoform 1 [Homo sapiens]" . . . . . 55.84 2477 100.00 100.00 1.28e-20 . . . . 15013 1 35 no REF NP_001182461 . "spectrin alpha chain, non-erythrocytic 1 isoform 3 [Homo sapiens]" . . . . . 55.84 2452 100.00 100.00 1.34e-20 . . . . 15013 1 36 no SP P07751 . "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain" . . . . . 55.84 2477 100.00 100.00 1.45e-20 . . . . 15013 1 37 no SP Q13813 . "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain; AltN" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 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 . 15013 1 2 . ALA . 15013 1 3 . MET . 15013 1 4 . GLY . 15013 1 5 . PRO . 15013 1 6 . ARG . 15013 1 7 . GLU . 15013 1 8 . VAL . 15013 1 9 . THR . 15013 1 10 . MET . 15013 1 11 . LYS . 15013 1 12 . LYS . 15013 1 13 . GLY . 15013 1 14 . ASP . 15013 1 15 . ILE . 15013 1 16 . LEU . 15013 1 17 . THR . 15013 1 18 . LEU . 15013 1 19 . LEU . 15013 1 20 . ASN . 15013 1 21 . SER . 15013 1 22 . THR . 15013 1 23 . ASN . 15013 1 24 . LYS . 15013 1 25 . ASP . 15013 1 26 . TRP . 15013 1 27 . TRP . 15013 1 28 . LYS . 15013 1 29 . VAL . 15013 1 30 . GLU . 15013 1 31 . VAL . 15013 1 32 . ASN . 15013 1 33 . ASP . 15013 1 34 . ARG . 15013 1 35 . GLN . 15013 1 36 . GLY . 15013 1 37 . PHE . 15013 1 38 . VAL . 15013 1 39 . PRO . 15013 1 40 . ALA . 15013 1 41 . ALA . 15013 1 42 . TYR . 15013 1 43 . VAL . 15013 1 44 . LYS . 15013 1 45 . LYS . 15013 1 46 . LEU . 15013 1 47 . ASP . 15013 1 48 . SER . 15013 1 49 . GLY . 15013 1 50 . THR . 15013 1 51 . GLY . 15013 1 52 . LYS . 15013 1 53 . GLU . 15013 1 54 . LEU . 15013 1 55 . VAL . 15013 1 56 . LEU . 15013 1 57 . ALA . 15013 1 58 . LEU . 15013 1 59 . TYR . 15013 1 60 . ASP . 15013 1 61 . TYR . 15013 1 62 . GLN . 15013 1 63 . GLU . 15013 1 64 . SER . 15013 1 65 . GLY . 15013 1 66 . ASP . 15013 1 67 . ASN . 15013 1 68 . ALA . 15013 1 69 . PRO . 15013 1 70 . SER . 15013 1 71 . TYR . 15013 1 72 . SER . 15013 1 73 . PRO . 15013 1 74 . PRO . 15013 1 75 . PRO . 15013 1 76 . PRO . 15013 1 77 . PRO . 15013 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 15013 1 . ALA 2 2 15013 1 . MET 3 3 15013 1 . GLY 4 4 15013 1 . PRO 5 5 15013 1 . ARG 6 6 15013 1 . GLU 7 7 15013 1 . VAL 8 8 15013 1 . THR 9 9 15013 1 . MET 10 10 15013 1 . LYS 11 11 15013 1 . LYS 12 12 15013 1 . GLY 13 13 15013 1 . ASP 14 14 15013 1 . ILE 15 15 15013 1 . LEU 16 16 15013 1 . THR 17 17 15013 1 . LEU 18 18 15013 1 . LEU 19 19 15013 1 . ASN 20 20 15013 1 . SER 21 21 15013 1 . THR 22 22 15013 1 . ASN 23 23 15013 1 . LYS 24 24 15013 1 . ASP 25 25 15013 1 . TRP 26 26 15013 1 . TRP 27 27 15013 1 . LYS 28 28 15013 1 . VAL 29 29 15013 1 . GLU 30 30 15013 1 . VAL 31 31 15013 1 . ASN 32 32 15013 1 . ASP 33 33 15013 1 . ARG 34 34 15013 1 . GLN 35 35 15013 1 . GLY 36 36 15013 1 . PHE 37 37 15013 1 . VAL 38 38 15013 1 . PRO 39 39 15013 1 . ALA 40 40 15013 1 . ALA 41 41 15013 1 . TYR 42 42 15013 1 . VAL 43 43 15013 1 . LYS 44 44 15013 1 . LYS 45 45 15013 1 . LEU 46 46 15013 1 . ASP 47 47 15013 1 . SER 48 48 15013 1 . GLY 49 49 15013 1 . THR 50 50 15013 1 . GLY 51 51 15013 1 . LYS 52 52 15013 1 . GLU 53 53 15013 1 . LEU 54 54 15013 1 . VAL 55 55 15013 1 . LEU 56 56 15013 1 . ALA 57 57 15013 1 . LEU 58 58 15013 1 . TYR 59 59 15013 1 . ASP 60 60 15013 1 . TYR 61 61 15013 1 . GLN 62 62 15013 1 . GLU 63 63 15013 1 . SER 64 64 15013 1 . GLY 65 65 15013 1 . ASP 66 66 15013 1 . ASN 67 67 15013 1 . ALA 68 68 15013 1 . PRO 69 69 15013 1 . SER 70 70 15013 1 . TYR 71 71 15013 1 . SER 72 72 15013 1 . PRO 73 73 15013 1 . PRO 74 74 15013 1 . PRO 75 75 15013 1 . PRO 76 76 15013 1 . PRO 77 77 15013 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 15013 _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 $SPCp41 . . 'no natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15013 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 15013 _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 $SPCp41 . 'recombinant technology' 'Escherichia coli' . . . . . . . . . . . . . . . . . . . . . pETM11 . . . . . . 15013 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15013 _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 SPCp41 '[U-98% 13C; U-98% 15N]' . . 1 $SPCp41 . . 1 . . mM . . . . 15013 1 2 glycine . . . . . . . 20 . . mM . . . . 15013 1 3 H2O . . . . . . . 90 . . % . . . . 15013 1 4 D2O . . . . . . . 10 . . % . . . . 15013 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 15013 _Sample.ID 2 _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 SPCp41 '[U-98% 15N]' . . 1 $SPCp41 . . 1 . . mM . . . . 15013 2 2 glycine . . . . . . . 20 . . mM . . . . 15013 2 3 H2O . . . . . . . 90 . . % . . . . 15013 2 4 D2O . . . . . . . 10 . . % . . . . 15013 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 15013 _Sample.ID 3 _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 SPCp41 . . . 1 $SPCp41 . . 1 . . mM . . . . 15013 3 2 glycine . . . . . . . 20 . . mM . . . . 15013 3 3 H2O . . . . . . . 90 . . % . . . . 15013 3 4 D2O . . . . . . . 10 . . % . . . . 15013 3 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 15013 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 3.5 . pH 15013 1 pressure 1 . atm 15013 1 temperature 303 . K 15013 1 stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 15013 _Software.ID 1 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'T Goddard' . . 15013 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15013 1 'data analysis' 15013 1 'peak picking' 15013 1 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 15013 _Software.ID 2 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'P Guntert, C Mumenthaler and K Wuthrich' . . 15013 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 15013 2 stop_ save_ save_xwinnmr _Software.Sf_category software _Software.Sf_framecode xwinnmr _Software.Entry_ID 15013 _Software.ID 3 _Software.Name xwinnmr _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 15013 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 15013 3 processing 15013 3 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 15013 _Software.ID 4 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 15013 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 15013 4 processing 15013 4 stop_ save_ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 15013 _Software.ID 5 _Software.Name VNMRJ _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 15013 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 15013 5 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 15013 _Software.ID 6 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax' . . 15013 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15013 6 stop_ save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 15013 _Software.ID 7 _Software.Name NMRView _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'B Johnson, One Moon Scientific' . . 15013 7 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15013 7 'data analysis' 15013 7 'peak picking' 15013 7 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 15013 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Varian NMR System' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 15013 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 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 15013 _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_2 Bruker Avance . 800 . . . 15013 1 2 spectrometer_1 Varian 'Varian NMR System' . 600 . . . 15013 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 15013 _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 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 5 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 6 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 7 '3D 1H-15N TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 8 '2D 1H-1H NOESY' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 9 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1 10 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 15013 1 11 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 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 15013 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0 . indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 15013 1 H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 15013 1 N 15 DSS 'methyl protons' . . . . ppm 0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 15013 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 15013 _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 2 '3D HNCACB' . . . 15013 1 3 '3D HNCO' . . . 15013 1 8 '2D 1H-1H NOESY' . . . 15013 1 11 '3D HCCH-TOCSY' . . . 15013 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $SPARKY . . 15013 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 3.849 0.02 . . . . . . 1 GLY HA2 . 15013 1 2 . 1 1 1 1 GLY HA3 H 1 3.849 0.02 . . . . . . 1 GLY HA3 . 15013 1 3 . 1 1 2 2 ALA H H 1 8.587 0.002 . . . . . . 2 ALA H . 15013 1 4 . 1 1 2 2 ALA HA H 1 4.359 0.001 . . . . . . 2 ALA HA . 15013 1 5 . 1 1 2 2 ALA HB1 H 1 1.387 0.02 . . . . . . 2 ALA HB1 . 15013 1 6 . 1 1 2 2 ALA HB2 H 1 1.387 0.02 . . . . . . 2 ALA HB2 . 15013 1 7 . 1 1 2 2 ALA HB3 H 1 1.387 0.02 . . . . . . 2 ALA HB3 . 15013 1 8 . 1 1 2 2 ALA N N 15 123.863 0.05 . . . . . . 2 ALA N . 15013 1 9 . 1 1 3 3 MET H H 1 8.460 0.02 . . . . . . 3 MET H . 15013 1 10 . 1 1 3 3 MET HA H 1 4.534 0.02 . . . . . . 3 MET HA . 15013 1 11 . 1 1 3 3 MET HB2 H 1 2.015 0.002 . . . . . . 3 MET HB2 . 15013 1 12 . 1 1 3 3 MET HB3 H 1 2.101 0.02 . . . . . . 3 MET HB3 . 15013 1 13 . 1 1 3 3 MET HG2 H 1 2.568 0.02 . . . . . . 3 MET HG2 . 15013 1 14 . 1 1 3 3 MET HG3 H 1 2.621 0.02 . . . . . . 3 MET HG3 . 15013 1 15 . 1 1 3 3 MET C C 13 172.802 0.05 . . . . . . 3 MET C . 15013 1 16 . 1 1 3 3 MET CA C 13 55.423 0.05 . . . . . . 3 MET CA . 15013 1 17 . 1 1 3 3 MET CB C 13 32.969 0.05 . . . . . . 3 MET CB . 15013 1 18 . 1 1 3 3 MET CG C 13 31.107 0.041 . . . . . . 3 MET CG . 15013 1 19 . 1 1 3 3 MET N N 15 119.757 0.05 . . . . . . 3 MET N . 15013 1 20 . 1 1 4 4 GLY H H 1 8.472 0.178 . . . . . . 4 GLY H . 15013 1 21 . 1 1 4 4 GLY HA2 H 1 4.034 0.02 . . . . . . 4 GLY HA2 . 15013 1 22 . 1 1 4 4 GLY HA3 H 1 4.162 0.02 . . . . . . 4 GLY HA3 . 15013 1 23 . 1 1 4 4 GLY CA C 13 44.822 0.05 . . . . . . 4 GLY CA . 15013 1 24 . 1 1 4 4 GLY N N 15 112.111 0.008 . . . . . . 4 GLY N . 15013 1 25 . 1 1 5 5 PRO HA H 1 4.458 0.02 . . . . . . 5 PRO HA . 15013 1 26 . 1 1 5 5 PRO HB2 H 1 1.926 0.02 . . . . . . 5 PRO HB2 . 15013 1 27 . 1 1 5 5 PRO HB3 H 1 2.282 0.002 . . . . . . 5 PRO HB3 . 15013 1 28 . 1 1 5 5 PRO HG2 H 1 1.990 0.02 . . . . . . 5 PRO HG2 . 15013 1 29 . 1 1 5 5 PRO HG3 H 1 1.990 0.02 . . . . . . 5 PRO HG3 . 15013 1 30 . 1 1 5 5 PRO HD2 H 1 3.612 0.001 . . . . . . 5 PRO HD2 . 15013 1 31 . 1 1 5 5 PRO HD3 H 1 3.612 0.001 . . . . . . 5 PRO HD3 . 15013 1 32 . 1 1 5 5 PRO C C 13 177.247 0.05 . . . . . . 5 PRO C . 15013 1 33 . 1 1 5 5 PRO CA C 13 63.418 0.05 . . . . . . 5 PRO CA . 15013 1 34 . 1 1 5 5 PRO CB C 13 32.457 0.05 . . . . . . 5 PRO CB . 15013 1 35 . 1 1 5 5 PRO CG C 13 27.389 0.054 . . . . . . 5 PRO CG . 15013 1 36 . 1 1 5 5 PRO CD C 13 50.152 0.042 . . . . . . 5 PRO CD . 15013 1 37 . 1 1 6 6 ARG H H 1 8.495 0.003 . . . . . . 6 ARG H . 15013 1 38 . 1 1 6 6 ARG HA H 1 4.383 0.001 . . . . . . 6 ARG HA . 15013 1 39 . 1 1 6 6 ARG HB2 H 1 1.795 0.02 . . . . . . 6 ARG HB2 . 15013 1 40 . 1 1 6 6 ARG HB3 H 1 1.913 0.005 . . . . . . 6 ARG HB3 . 15013 1 41 . 1 1 6 6 ARG HG2 H 1 1.654 0.02 . . . . . . 6 ARG HG2 . 15013 1 42 . 1 1 6 6 ARG HG3 H 1 1.715 0.02 . . . . . . 6 ARG HG3 . 15013 1 43 . 1 1 6 6 ARG HD2 H 1 3.220 0.004 . . . . . . 6 ARG HD2 . 15013 1 44 . 1 1 6 6 ARG HD3 H 1 3.220 0.004 . . . . . . 6 ARG HD3 . 15013 1 45 . 1 1 6 6 ARG HE H 1 7.183 0.006 . . . . . . 6 ARG HE . 15013 1 46 . 1 1 6 6 ARG C C 13 176.122 0.05 . . . . . . 6 ARG C . 15013 1 47 . 1 1 6 6 ARG CA C 13 56.200 0.003 . . . . . . 6 ARG CA . 15013 1 48 . 1 1 6 6 ARG CB C 13 30.942 0.013 . . . . . . 6 ARG CB . 15013 1 49 . 1 1 6 6 ARG CG C 13 27.187 0.021 . . . . . . 6 ARG CG . 15013 1 50 . 1 1 6 6 ARG CD C 13 43.673 0.036 . . . . . . 6 ARG CD . 15013 1 51 . 1 1 6 6 ARG N N 15 120.801 0.032 . . . . . . 6 ARG N . 15013 1 52 . 1 1 6 6 ARG NE N 15 115.328 0.013 . . . . . . 6 ARG NE . 15013 1 53 . 1 1 7 7 GLU H H 1 8.078 0.001 . . . . . . 7 GLU H . 15013 1 54 . 1 1 7 7 GLU HA H 1 4.593 0.02 . . . . . . 7 GLU HA . 15013 1 55 . 1 1 7 7 GLU HB2 H 1 1.950 0.02 . . . . . . 7 GLU HB2 . 15013 1 56 . 1 1 7 7 GLU HB3 H 1 2.084 0.02 . . . . . . 7 GLU HB3 . 15013 1 57 . 1 1 7 7 GLU HG2 H 1 2.393 0.02 . . . . . . 7 GLU HG2 . 15013 1 58 . 1 1 7 7 GLU HG3 H 1 2.393 0.02 . . . . . . 7 GLU HG3 . 15013 1 59 . 1 1 7 7 GLU C C 13 176.109 0.05 . . . . . . 7 GLU C . 15013 1 60 . 1 1 7 7 GLU CA C 13 55.792 0.005 . . . . . . 7 GLU CA . 15013 1 61 . 1 1 7 7 GLU CB C 13 30.050 0.001 . . . . . . 7 GLU CB . 15013 1 62 . 1 1 7 7 GLU CG C 13 33.743 0.013 . . . . . . 7 GLU CG . 15013 1 63 . 1 1 7 7 GLU N N 15 120.603 0.033 . . . . . . 7 GLU N . 15013 1 64 . 1 1 8 8 VAL H H 1 8.296 0.005 . . . . . . 8 VAL H . 15013 1 65 . 1 1 8 8 VAL HA H 1 4.096 0.001 . . . . . . 8 VAL HA . 15013 1 66 . 1 1 8 8 VAL HB H 1 1.920 0.02 . . . . . . 8 VAL HB . 15013 1 67 . 1 1 8 8 VAL HG11 H 1 0.753 0.02 . . . . . . 8 VAL HG11 . 15013 1 68 . 1 1 8 8 VAL HG12 H 1 0.753 0.02 . . . . . . 8 VAL HG12 . 15013 1 69 . 1 1 8 8 VAL HG13 H 1 0.753 0.02 . . . . . . 8 VAL HG13 . 15013 1 70 . 1 1 8 8 VAL HG21 H 1 0.828 0.02 . . . . . . 8 VAL HG21 . 15013 1 71 . 1 1 8 8 VAL HG22 H 1 0.828 0.02 . . . . . . 8 VAL HG22 . 15013 1 72 . 1 1 8 8 VAL HG23 H 1 0.828 0.02 . . . . . . 8 VAL HG23 . 15013 1 73 . 1 1 8 8 VAL C C 13 174.660 0.05 . . . . . . 8 VAL C . 15013 1 74 . 1 1 8 8 VAL CA C 13 62.866 0.001 . . . . . . 8 VAL CA . 15013 1 75 . 1 1 8 8 VAL CB C 13 33.474 0.003 . . . . . . 8 VAL CB . 15013 1 76 . 1 1 8 8 VAL CG1 C 13 21.125 0.099 . . . . . . 8 VAL CG1 . 15013 1 77 . 1 1 8 8 VAL CG2 C 13 21.861 0.079 . . . . . . 8 VAL CG2 . 15013 1 78 . 1 1 8 8 VAL N N 15 121.939 0.016 . . . . . . 8 VAL N . 15013 1 79 . 1 1 9 9 THR H H 1 7.972 0.023 . . . . . . 9 THR H . 15013 1 80 . 1 1 9 9 THR HA H 1 4.803 0.02 . . . . . . 9 THR HA . 15013 1 81 . 1 1 9 9 THR HB H 1 4.063 0.001 . . . . . . 9 THR HB . 15013 1 82 . 1 1 9 9 THR HG21 H 1 1.136 0.02 . . . . . . 9 THR HG21 . 15013 1 83 . 1 1 9 9 THR HG22 H 1 1.136 0.02 . . . . . . 9 THR HG22 . 15013 1 84 . 1 1 9 9 THR HG23 H 1 1.136 0.02 . . . . . . 9 THR HG23 . 15013 1 85 . 1 1 9 9 THR C C 13 173.345 0.05 . . . . . . 9 THR C . 15013 1 86 . 1 1 9 9 THR CA C 13 61.409 0.010 . . . . . . 9 THR CA . 15013 1 87 . 1 1 9 9 THR CB C 13 70.989 0.002 . . . . . . 9 THR CB . 15013 1 88 . 1 1 9 9 THR CG2 C 13 24.631 0.05 . . . . . . 9 THR CG2 . 15013 1 89 . 1 1 9 9 THR N N 15 120.018 0.036 . . . . . . 9 THR N . 15013 1 90 . 1 1 10 10 MET H H 1 9.097 0.023 . . . . . . 10 MET H . 15013 1 91 . 1 1 10 10 MET HA H 1 4.667 0.006 . . . . . . 10 MET HA . 15013 1 92 . 1 1 10 10 MET HB2 H 1 1.992 0.009 . . . . . . 10 MET HB2 . 15013 1 93 . 1 1 10 10 MET HB3 H 1 2.240 0.022 . . . . . . 10 MET HB3 . 15013 1 94 . 1 1 10 10 MET HG2 H 1 2.458 0.02 . . . . . . 10 MET HG2 . 15013 1 95 . 1 1 10 10 MET HG3 H 1 2.655 0.002 . . . . . . 10 MET HG3 . 15013 1 96 . 1 1 10 10 MET C C 13 173.829 0.05 . . . . . . 10 MET C . 15013 1 97 . 1 1 10 10 MET CA C 13 55.224 0.031 . . . . . . 10 MET CA . 15013 1 98 . 1 1 10 10 MET CB C 13 36.409 0.05 . . . . . . 10 MET CB . 15013 1 99 . 1 1 10 10 MET CG C 13 32.477 0.030 . . . . . . 10 MET CG . 15013 1 100 . 1 1 10 10 MET N N 15 122.967 0.038 . . . . . . 10 MET N . 15013 1 101 . 1 1 11 11 LYS H H 1 8.688 0.059 . . . . . . 11 LYS H . 15013 1 102 . 1 1 11 11 LYS HA H 1 4.871 0.001 . . . . . . 11 LYS HA . 15013 1 103 . 1 1 11 11 LYS HB2 H 1 1.671 0.02 . . . . . . 11 LYS HB2 . 15013 1 104 . 1 1 11 11 LYS HB3 H 1 1.704 0.02 . . . . . . 11 LYS HB3 . 15013 1 105 . 1 1 11 11 LYS HG2 H 1 1.382 0.02 . . . . . . 11 LYS HG2 . 15013 1 106 . 1 1 11 11 LYS HG3 H 1 1.406 0.02 . . . . . . 11 LYS HG3 . 15013 1 107 . 1 1 11 11 LYS C C 13 175.497 0.05 . . . . . . 11 LYS C . 15013 1 108 . 1 1 11 11 LYS CA C 13 53.481 0.025 . . . . . . 11 LYS CA . 15013 1 109 . 1 1 11 11 LYS CB C 13 34.507 0.007 . . . . . . 11 LYS CB . 15013 1 110 . 1 1 11 11 LYS CG C 13 24.763 0.041 . . . . . . 11 LYS CG . 15013 1 111 . 1 1 11 11 LYS CD C 13 29.089 0.030 . . . . . . 11 LYS CD . 15013 1 112 . 1 1 11 11 LYS CE C 13 41.979 0.026 . . . . . . 11 LYS CE . 15013 1 113 . 1 1 11 11 LYS N N 15 126.398 0.032 . . . . . . 11 LYS N . 15013 1 114 . 1 1 12 12 LYS H H 1 8.501 0.022 . . . . . . 12 LYS H . 15013 1 115 . 1 1 12 12 LYS HA H 1 3.295 0.002 . . . . . . 12 LYS HA . 15013 1 116 . 1 1 12 12 LYS HB2 H 1 1.456 0.02 . . . . . . 12 LYS HB2 . 15013 1 117 . 1 1 12 12 LYS HB3 H 1 1.610 0.02 . . . . . . 12 LYS HB3 . 15013 1 118 . 1 1 12 12 LYS HG2 H 1 1.100 0.02 . . . . . . 12 LYS HG2 . 15013 1 119 . 1 1 12 12 LYS HG3 H 1 1.166 0.02 . . . . . . 12 LYS HG3 . 15013 1 120 . 1 1 12 12 LYS HD2 H 1 1.654 0.02 . . . . . . 12 LYS HD2 . 15013 1 121 . 1 1 12 12 LYS HD3 H 1 1.654 0.02 . . . . . . 12 LYS HD3 . 15013 1 122 . 1 1 12 12 LYS C C 13 177.341 0.05 . . . . . . 12 LYS C . 15013 1 123 . 1 1 12 12 LYS CA C 13 58.620 0.016 . . . . . . 12 LYS CA . 15013 1 124 . 1 1 12 12 LYS CB C 13 32.722 0.014 . . . . . . 12 LYS CB . 15013 1 125 . 1 1 12 12 LYS CG C 13 24.545 0.032 . . . . . . 12 LYS CG . 15013 1 126 . 1 1 12 12 LYS CD C 13 29.750 0.060 . . . . . . 12 LYS CD . 15013 1 127 . 1 1 12 12 LYS CE C 13 42.320 0.050 . . . . . . 12 LYS CE . 15013 1 128 . 1 1 12 12 LYS N N 15 121.424 0.030 . . . . . . 12 LYS N . 15013 1 129 . 1 1 13 13 GLY H H 1 8.834 0.005 . . . . . . 13 GLY H . 15013 1 130 . 1 1 13 13 GLY HA2 H 1 3.522 0.001 . . . . . . 13 GLY HA2 . 15013 1 131 . 1 1 13 13 GLY HA3 H 1 4.482 0.001 . . . . . . 13 GLY HA3 . 15013 1 132 . 1 1 13 13 GLY C C 13 174.350 0.05 . . . . . . 13 GLY C . 15013 1 133 . 1 1 13 13 GLY CA C 13 45.024 0.002 . . . . . . 13 GLY CA . 15013 1 134 . 1 1 13 13 GLY N N 15 115.551 0.021 . . . . . . 13 GLY N . 15013 1 135 . 1 1 14 14 ASP H H 1 8.489 0.007 . . . . . . 14 ASP H . 15013 1 136 . 1 1 14 14 ASP HA H 1 4.564 0.001 . . . . . . 14 ASP HA . 15013 1 137 . 1 1 14 14 ASP HB2 H 1 2.615 0.02 . . . . . . 14 ASP HB2 . 15013 1 138 . 1 1 14 14 ASP HB3 H 1 2.857 0.02 . . . . . . 14 ASP HB3 . 15013 1 139 . 1 1 14 14 ASP C C 13 174.595 0.05 . . . . . . 14 ASP C . 15013 1 140 . 1 1 14 14 ASP CA C 13 55.453 0.003 . . . . . . 14 ASP CA . 15013 1 141 . 1 1 14 14 ASP CB C 13 41.349 0.004 . . . . . . 14 ASP CB . 15013 1 142 . 1 1 14 14 ASP N N 15 121.772 0.019 . . . . . . 14 ASP N . 15013 1 143 . 1 1 15 15 ILE H H 1 8.118 0.018 . . . . . . 15 ILE H . 15013 1 144 . 1 1 15 15 ILE HA H 1 5.071 0.02 . . . . . . 15 ILE HA . 15013 1 145 . 1 1 15 15 ILE HB H 1 1.766 0.02 . . . . . . 15 ILE HB . 15013 1 146 . 1 1 15 15 ILE HG12 H 1 1.103 0.02 . . . . . . 15 ILE HG12 . 15013 1 147 . 1 1 15 15 ILE HG13 H 1 1.669 0.02 . . . . . . 15 ILE HG13 . 15013 1 148 . 1 1 15 15 ILE HG21 H 1 0.888 0.02 . . . . . . 15 ILE HG21 . 15013 1 149 . 1 1 15 15 ILE HG22 H 1 0.888 0.02 . . . . . . 15 ILE HG22 . 15013 1 150 . 1 1 15 15 ILE HG23 H 1 0.888 0.02 . . . . . . 15 ILE HG23 . 15013 1 151 . 1 1 15 15 ILE HD11 H 1 0.847 0.02 . . . . . . 15 ILE HD11 . 15013 1 152 . 1 1 15 15 ILE HD12 H 1 0.847 0.02 . . . . . . 15 ILE HD12 . 15013 1 153 . 1 1 15 15 ILE HD13 H 1 0.847 0.02 . . . . . . 15 ILE HD13 . 15013 1 154 . 1 1 15 15 ILE C C 13 176.683 0.05 . . . . . . 15 ILE C . 15013 1 155 . 1 1 15 15 ILE CA C 13 60.407 0.012 . . . . . . 15 ILE CA . 15013 1 156 . 1 1 15 15 ILE CB C 13 38.623 0.020 . . . . . . 15 ILE CB . 15013 1 157 . 1 1 15 15 ILE CG1 C 13 28.160 0.051 . . . . . . 15 ILE CG1 . 15013 1 158 . 1 1 15 15 ILE CG2 C 13 19.021 0.034 . . . . . . 15 ILE CG2 . 15013 1 159 . 1 1 15 15 ILE CD1 C 13 12.954 0.05 . . . . . . 15 ILE CD1 . 15013 1 160 . 1 1 15 15 ILE N N 15 120.153 0.034 . . . . . . 15 ILE N . 15013 1 161 . 1 1 16 16 LEU H H 1 9.280 0.007 . . . . . . 16 LEU H . 15013 1 162 . 1 1 16 16 LEU HA H 1 4.996 0.001 . . . . . . 16 LEU HA . 15013 1 163 . 1 1 16 16 LEU HB2 H 1 1.425 0.02 . . . . . . 16 LEU HB2 . 15013 1 164 . 1 1 16 16 LEU HB3 H 1 1.645 0.02 . . . . . . 16 LEU HB3 . 15013 1 165 . 1 1 16 16 LEU HG H 1 1.584 0.02 . . . . . . 16 LEU HG . 15013 1 166 . 1 1 16 16 LEU HD11 H 1 0.865 0.02 . . . . . . 16 LEU HD11 . 15013 1 167 . 1 1 16 16 LEU HD12 H 1 0.865 0.02 . . . . . . 16 LEU HD12 . 15013 1 168 . 1 1 16 16 LEU HD13 H 1 0.865 0.02 . . . . . . 16 LEU HD13 . 15013 1 169 . 1 1 16 16 LEU HD21 H 1 0.893 0.02 . . . . . . 16 LEU HD21 . 15013 1 170 . 1 1 16 16 LEU HD22 H 1 0.893 0.02 . . . . . . 16 LEU HD22 . 15013 1 171 . 1 1 16 16 LEU HD23 H 1 0.893 0.02 . . . . . . 16 LEU HD23 . 15013 1 172 . 1 1 16 16 LEU C C 13 175.911 0.05 . . . . . . 16 LEU C . 15013 1 173 . 1 1 16 16 LEU CA C 13 54.216 0.038 . . . . . . 16 LEU CA . 15013 1 174 . 1 1 16 16 LEU CB C 13 44.419 0.006 . . . . . . 16 LEU CB . 15013 1 175 . 1 1 16 16 LEU CG C 13 28.602 0.018 . . . . . . 16 LEU CG . 15013 1 176 . 1 1 16 16 LEU CD2 C 13 27.891 0.05 . . . . . . 16 LEU CD2 . 15013 1 177 . 1 1 16 16 LEU N N 15 126.959 0.018 . . . . . . 16 LEU N . 15013 1 178 . 1 1 17 17 THR H H 1 8.477 0.002 . . . . . . 17 THR H . 15013 1 179 . 1 1 17 17 THR HA H 1 4.569 0.001 . . . . . . 17 THR HA . 15013 1 180 . 1 1 17 17 THR HB H 1 4.099 0.003 . . . . . . 17 THR HB . 15013 1 181 . 1 1 17 17 THR HG21 H 1 1.154 0.02 . . . . . . 17 THR HG21 . 15013 1 182 . 1 1 17 17 THR HG22 H 1 1.154 0.02 . . . . . . 17 THR HG22 . 15013 1 183 . 1 1 17 17 THR HG23 H 1 1.154 0.02 . . . . . . 17 THR HG23 . 15013 1 184 . 1 1 17 17 THR C C 13 173.933 0.05 . . . . . . 17 THR C . 15013 1 185 . 1 1 17 17 THR CA C 13 63.734 0.018 . . . . . . 17 THR CA . 15013 1 186 . 1 1 17 17 THR CB C 13 69.962 0.005 . . . . . . 17 THR CB . 15013 1 187 . 1 1 17 17 THR N N 15 117.328 0.005 . . . . . . 17 THR N . 15013 1 188 . 1 1 18 18 LEU H H 1 8.787 0.004 . . . . . . 18 LEU H . 15013 1 189 . 1 1 18 18 LEU HA H 1 4.407 0.002 . . . . . . 18 LEU HA . 15013 1 190 . 1 1 18 18 LEU HB2 H 1 1.122 0.02 . . . . . . 18 LEU HB2 . 15013 1 191 . 1 1 18 18 LEU HB3 H 1 1.770 0.02 . . . . . . 18 LEU HB3 . 15013 1 192 . 1 1 18 18 LEU HG H 1 1.146 0.02 . . . . . . 18 LEU HG . 15013 1 193 . 1 1 18 18 LEU HD11 H 1 0.391 0.02 . . . . . . 18 LEU HD11 . 15013 1 194 . 1 1 18 18 LEU HD12 H 1 0.391 0.02 . . . . . . 18 LEU HD12 . 15013 1 195 . 1 1 18 18 LEU HD13 H 1 0.391 0.02 . . . . . . 18 LEU HD13 . 15013 1 196 . 1 1 18 18 LEU HD21 H 1 0.682 0.02 . . . . . . 18 LEU HD21 . 15013 1 197 . 1 1 18 18 LEU HD22 H 1 0.682 0.02 . . . . . . 18 LEU HD22 . 15013 1 198 . 1 1 18 18 LEU HD23 H 1 0.682 0.02 . . . . . . 18 LEU HD23 . 15013 1 199 . 1 1 18 18 LEU C C 13 174.874 0.05 . . . . . . 18 LEU C . 15013 1 200 . 1 1 18 18 LEU CA C 13 54.703 0.016 . . . . . . 18 LEU CA . 15013 1 201 . 1 1 18 18 LEU CB C 13 43.415 0.028 . . . . . . 18 LEU CB . 15013 1 202 . 1 1 18 18 LEU CG C 13 26.964 0.030 . . . . . . 18 LEU CG . 15013 1 203 . 1 1 18 18 LEU CD1 C 13 25.507 0.049 . . . . . . 18 LEU CD1 . 15013 1 204 . 1 1 18 18 LEU CD2 C 13 24.015 0.041 . . . . . . 18 LEU CD2 . 15013 1 205 . 1 1 18 18 LEU N N 15 129.268 0.022 . . . . . . 18 LEU N . 15013 1 206 . 1 1 19 19 LEU H H 1 8.973 0.003 . . . . . . 19 LEU H . 15013 1 207 . 1 1 19 19 LEU HA H 1 4.494 0.001 . . . . . . 19 LEU HA . 15013 1 208 . 1 1 19 19 LEU HB2 H 1 1.155 0.02 . . . . . . 19 LEU HB2 . 15013 1 209 . 1 1 19 19 LEU HB3 H 1 1.411 0.02 . . . . . . 19 LEU HB3 . 15013 1 210 . 1 1 19 19 LEU HG H 1 1.407 0.001 . . . . . . 19 LEU HG . 15013 1 211 . 1 1 19 19 LEU HD11 H 1 0.746 0.02 . . . . . . 19 LEU HD11 . 15013 1 212 . 1 1 19 19 LEU HD12 H 1 0.746 0.02 . . . . . . 19 LEU HD12 . 15013 1 213 . 1 1 19 19 LEU HD13 H 1 0.746 0.02 . . . . . . 19 LEU HD13 . 15013 1 214 . 1 1 19 19 LEU HD21 H 1 0.704 0.02 . . . . . . 19 LEU HD21 . 15013 1 215 . 1 1 19 19 LEU HD22 H 1 0.704 0.02 . . . . . . 19 LEU HD22 . 15013 1 216 . 1 1 19 19 LEU HD23 H 1 0.704 0.02 . . . . . . 19 LEU HD23 . 15013 1 217 . 1 1 19 19 LEU C C 13 177.750 0.05 . . . . . . 19 LEU C . 15013 1 218 . 1 1 19 19 LEU CA C 13 55.406 0.035 . . . . . . 19 LEU CA . 15013 1 219 . 1 1 19 19 LEU CB C 13 43.213 0.017 . . . . . . 19 LEU CB . 15013 1 220 . 1 1 19 19 LEU CG C 13 27.092 0.028 . . . . . . 19 LEU CG . 15013 1 221 . 1 1 19 19 LEU CD1 C 13 25.978 0.027 . . . . . . 19 LEU CD1 . 15013 1 222 . 1 1 19 19 LEU CD2 C 13 22.292 0.045 . . . . . . 19 LEU CD2 . 15013 1 223 . 1 1 19 19 LEU N N 15 126.111 0.069 . . . . . . 19 LEU N . 15013 1 224 . 1 1 20 20 ASN H H 1 7.526 0.003 . . . . . . 20 ASN H . 15013 1 225 . 1 1 20 20 ASN HA H 1 4.710 0.02 . . . . . . 20 ASN HA . 15013 1 226 . 1 1 20 20 ASN HB2 H 1 2.651 0.02 . . . . . . 20 ASN HB2 . 15013 1 227 . 1 1 20 20 ASN HB3 H 1 2.795 0.02 . . . . . . 20 ASN HB3 . 15013 1 228 . 1 1 20 20 ASN HD21 H 1 7.184 0.02 . . . . . . 20 ASN HD21 . 15013 1 229 . 1 1 20 20 ASN HD22 H 1 7.916 0.02 . . . . . . 20 ASN HD22 . 15013 1 230 . 1 1 20 20 ASN C C 13 174.573 0.05 . . . . . . 20 ASN C . 15013 1 231 . 1 1 20 20 ASN CA C 13 54.701 0.015 . . . . . . 20 ASN CA . 15013 1 232 . 1 1 20 20 ASN CB C 13 41.354 0.021 . . . . . . 20 ASN CB . 15013 1 233 . 1 1 20 20 ASN N N 15 114.046 0.012 . . . . . . 20 ASN N . 15013 1 234 . 1 1 20 20 ASN ND2 N 15 114.763 0.05 . . . . . . 20 ASN ND2 . 15013 1 235 . 1 1 21 21 SER H H 1 9.063 0.006 . . . . . . 21 SER H . 15013 1 236 . 1 1 21 21 SER HA H 1 3.950 0.001 . . . . . . 21 SER HA . 15013 1 237 . 1 1 21 21 SER HB2 H 1 2.032 0.02 . . . . . . 21 SER HB2 . 15013 1 238 . 1 1 21 21 SER HB3 H 1 2.878 0.02 . . . . . . 21 SER HB3 . 15013 1 239 . 1 1 21 21 SER C C 13 173.723 0.05 . . . . . . 21 SER C . 15013 1 240 . 1 1 21 21 SER CA C 13 57.066 0.005 . . . . . . 21 SER CA . 15013 1 241 . 1 1 21 21 SER CB C 13 62.415 0.053 . . . . . . 21 SER CB . 15013 1 242 . 1 1 21 21 SER N N 15 123.165 0.024 . . . . . . 21 SER N . 15013 1 243 . 1 1 22 22 THR H H 1 8.166 0.011 . . . . . . 22 THR H . 15013 1 244 . 1 1 22 22 THR HA H 1 3.973 0.001 . . . . . . 22 THR HA . 15013 1 245 . 1 1 22 22 THR HB H 1 4.273 0.02 . . . . . . 22 THR HB . 15013 1 246 . 1 1 22 22 THR HG21 H 1 1.307 0.02 . . . . . . 22 THR HG21 . 15013 1 247 . 1 1 22 22 THR HG22 H 1 1.307 0.02 . . . . . . 22 THR HG22 . 15013 1 248 . 1 1 22 22 THR HG23 H 1 1.307 0.02 . . . . . . 22 THR HG23 . 15013 1 249 . 1 1 22 22 THR C C 13 175.474 0.05 . . . . . . 22 THR C . 15013 1 250 . 1 1 22 22 THR CA C 13 65.615 0.008 . . . . . . 22 THR CA . 15013 1 251 . 1 1 22 22 THR CB C 13 69.709 0.026 . . . . . . 22 THR CB . 15013 1 252 . 1 1 22 22 THR N N 15 115.378 0.007 . . . . . . 22 THR N . 15013 1 253 . 1 1 23 23 ASN H H 1 8.622 0.009 . . . . . . 23 ASN H . 15013 1 254 . 1 1 23 23 ASN HA H 1 4.832 0.001 . . . . . . 23 ASN HA . 15013 1 255 . 1 1 23 23 ASN HB2 H 1 2.853 0.02 . . . . . . 23 ASN HB2 . 15013 1 256 . 1 1 23 23 ASN HB3 H 1 3.832 0.001 . . . . . . 23 ASN HB3 . 15013 1 257 . 1 1 23 23 ASN HD21 H 1 7.484 0.02 . . . . . . 23 ASN HD21 . 15013 1 258 . 1 1 23 23 ASN HD22 H 1 7.930 0.02 . . . . . . 23 ASN HD22 . 15013 1 259 . 1 1 23 23 ASN C C 13 174.922 0.05 . . . . . . 23 ASN C . 15013 1 260 . 1 1 23 23 ASN CA C 13 53.471 0.005 . . . . . . 23 ASN CA . 15013 1 261 . 1 1 23 23 ASN CB C 13 40.374 0.016 . . . . . . 23 ASN CB . 15013 1 262 . 1 1 23 23 ASN N N 15 122.914 0.019 . . . . . . 23 ASN N . 15013 1 263 . 1 1 23 23 ASN ND2 N 15 114.775 0.05 . . . . . . 23 ASN ND2 . 15013 1 264 . 1 1 24 24 LYS H H 1 8.485 0.006 . . . . . . 24 LYS H . 15013 1 265 . 1 1 24 24 LYS HA H 1 4.265 0.02 . . . . . . 24 LYS HA . 15013 1 266 . 1 1 24 24 LYS HB2 H 1 1.796 0.02 . . . . . . 24 LYS HB2 . 15013 1 267 . 1 1 24 24 LYS HB3 H 1 1.841 0.02 . . . . . . 24 LYS HB3 . 15013 1 268 . 1 1 24 24 LYS HG2 H 1 1.442 0.001 . . . . . . 24 LYS HG2 . 15013 1 269 . 1 1 24 24 LYS HG3 H 1 1.442 0.001 . . . . . . 24 LYS HG3 . 15013 1 270 . 1 1 24 24 LYS HD2 H 1 1.695 0.02 . . . . . . 24 LYS HD2 . 15013 1 271 . 1 1 24 24 LYS HD3 H 1 1.695 0.02 . . . . . . 24 LYS HD3 . 15013 1 272 . 1 1 24 24 LYS HE2 H 1 3.037 0.02 . . . . . . 24 LYS HE2 . 15013 1 273 . 1 1 24 24 LYS HE3 H 1 3.037 0.02 . . . . . . 24 LYS HE3 . 15013 1 274 . 1 1 24 24 LYS C C 13 176.547 0.05 . . . . . . 24 LYS C . 15013 1 275 . 1 1 24 24 LYS CA C 13 58.469 0.022 . . . . . . 24 LYS CA . 15013 1 276 . 1 1 24 24 LYS CB C 13 32.784 0.002 . . . . . . 24 LYS CB . 15013 1 277 . 1 1 24 24 LYS CG C 13 24.519 0.030 . . . . . . 24 LYS CG . 15013 1 278 . 1 1 24 24 LYS CD C 13 29.544 0.061 . . . . . . 24 LYS CD . 15013 1 279 . 1 1 24 24 LYS CE C 13 42.422 0.053 . . . . . . 24 LYS CE . 15013 1 280 . 1 1 24 24 LYS N N 15 121.275 0.020 . . . . . . 24 LYS N . 15013 1 281 . 1 1 25 25 ASP H H 1 8.326 0.017 . . . . . . 25 ASP H . 15013 1 282 . 1 1 25 25 ASP HA H 1 4.524 0.002 . . . . . . 25 ASP HA . 15013 1 283 . 1 1 25 25 ASP HB2 H 1 1.955 0.02 . . . . . . 25 ASP HB2 . 15013 1 284 . 1 1 25 25 ASP HB3 H 1 2.801 0.001 . . . . . . 25 ASP HB3 . 15013 1 285 . 1 1 25 25 ASP C C 13 176.916 0.05 . . . . . . 25 ASP C . 15013 1 286 . 1 1 25 25 ASP CA C 13 55.596 0.015 . . . . . . 25 ASP CA . 15013 1 287 . 1 1 25 25 ASP CB C 13 43.386 0.002 . . . . . . 25 ASP CB . 15013 1 288 . 1 1 25 25 ASP N N 15 115.342 0.011 . . . . . . 25 ASP N . 15013 1 289 . 1 1 26 26 TRP H H 1 8.104 0.005 . . . . . . 26 TRP H . 15013 1 290 . 1 1 26 26 TRP HA H 1 5.132 0.02 . . . . . . 26 TRP HA . 15013 1 291 . 1 1 26 26 TRP HB2 H 1 2.865 0.001 . . . . . . 26 TRP HB2 . 15013 1 292 . 1 1 26 26 TRP HB3 H 1 2.972 0.02 . . . . . . 26 TRP HB3 . 15013 1 293 . 1 1 26 26 TRP HD1 H 1 7.139 0.02 . . . . . . 26 TRP HD1 . 15013 1 294 . 1 1 26 26 TRP HE1 H 1 9.925 0.02 . . . . . . 26 TRP HE1 . 15013 1 295 . 1 1 26 26 TRP HE3 H 1 6.950 0.02 . . . . . . 26 TRP HE3 . 15013 1 296 . 1 1 26 26 TRP HZ2 H 1 7.057 0.02 . . . . . . 26 TRP HZ2 . 15013 1 297 . 1 1 26 26 TRP HZ3 H 1 6.756 0.02 . . . . . . 26 TRP HZ3 . 15013 1 298 . 1 1 26 26 TRP HH2 H 1 7.235 0.001 . . . . . . 26 TRP HH2 . 15013 1 299 . 1 1 26 26 TRP C C 13 174.490 0.05 . . . . . . 26 TRP C . 15013 1 300 . 1 1 26 26 TRP CA C 13 55.890 0.052 . . . . . . 26 TRP CA . 15013 1 301 . 1 1 26 26 TRP CB C 13 33.085 0.045 . . . . . . 26 TRP CB . 15013 1 302 . 1 1 26 26 TRP N N 15 121.794 0.025 . . . . . . 26 TRP N . 15013 1 303 . 1 1 26 26 TRP NE1 N 15 128.806 0.05 . . . . . . 26 TRP NE1 . 15013 1 304 . 1 1 27 27 TRP H H 1 9.530 0.004 . . . . . . 27 TRP H . 15013 1 305 . 1 1 27 27 TRP HA H 1 5.511 0.002 . . . . . . 27 TRP HA . 15013 1 306 . 1 1 27 27 TRP HB2 H 1 2.804 0.002 . . . . . . 27 TRP HB2 . 15013 1 307 . 1 1 27 27 TRP HB3 H 1 2.967 0.02 . . . . . . 27 TRP HB3 . 15013 1 308 . 1 1 27 27 TRP HD1 H 1 7.555 0.02 . . . . . . 27 TRP HD1 . 15013 1 309 . 1 1 27 27 TRP HE1 H 1 9.272 0.02 . . . . . . 27 TRP HE1 . 15013 1 310 . 1 1 27 27 TRP HE3 H 1 7.091 0.002 . . . . . . 27 TRP HE3 . 15013 1 311 . 1 1 27 27 TRP HZ2 H 1 7.547 0.02 . . . . . . 27 TRP HZ2 . 15013 1 312 . 1 1 27 27 TRP HZ3 H 1 6.715 0.02 . . . . . . 27 TRP HZ3 . 15013 1 313 . 1 1 27 27 TRP HH2 H 1 7.211 0.02 . . . . . . 27 TRP HH2 . 15013 1 314 . 1 1 27 27 TRP C C 13 174.485 0.05 . . . . . . 27 TRP C . 15013 1 315 . 1 1 27 27 TRP CA C 13 54.170 0.004 . . . . . . 27 TRP CA . 15013 1 316 . 1 1 27 27 TRP CB C 13 31.848 0.001 . . . . . . 27 TRP CB . 15013 1 317 . 1 1 27 27 TRP N N 15 124.771 0.023 . . . . . . 27 TRP N . 15013 1 318 . 1 1 27 27 TRP NE1 N 15 129.396 0.05 . . . . . . 27 TRP NE1 . 15013 1 319 . 1 1 28 28 LYS H H 1 8.723 0.002 . . . . . . 28 LYS H . 15013 1 320 . 1 1 28 28 LYS HA H 1 4.415 0.001 . . . . . . 28 LYS HA . 15013 1 321 . 1 1 28 28 LYS HB2 H 1 1.104 0.02 . . . . . . 28 LYS HB2 . 15013 1 322 . 1 1 28 28 LYS HB3 H 1 1.498 0.002 . . . . . . 28 LYS HB3 . 15013 1 323 . 1 1 28 28 LYS HG2 H 1 0.305 0.001 . . . . . . 28 LYS HG2 . 15013 1 324 . 1 1 28 28 LYS HG3 H 1 0.948 0.02 . . . . . . 28 LYS HG3 . 15013 1 325 . 1 1 28 28 LYS HD2 H 1 1.394 0.02 . . . . . . 28 LYS HD2 . 15013 1 326 . 1 1 28 28 LYS HD3 H 1 1.394 0.02 . . . . . . 28 LYS HD3 . 15013 1 327 . 1 1 28 28 LYS HE2 H 1 2.614 0.02 . . . . . . 28 LYS HE2 . 15013 1 328 . 1 1 28 28 LYS HE3 H 1 2.684 0.02 . . . . . . 28 LYS HE3 . 15013 1 329 . 1 1 28 28 LYS C C 13 175.913 0.05 . . . . . . 28 LYS C . 15013 1 330 . 1 1 28 28 LYS CA C 13 55.430 0.004 . . . . . . 28 LYS CA . 15013 1 331 . 1 1 28 28 LYS CB C 13 34.684 0.017 . . . . . . 28 LYS CB . 15013 1 332 . 1 1 28 28 LYS CG C 13 25.991 0.060 . . . . . . 28 LYS CG . 15013 1 333 . 1 1 28 28 LYS CD C 13 29.562 0.052 . . . . . . 28 LYS CD . 15013 1 334 . 1 1 28 28 LYS N N 15 124.270 0.061 . . . . . . 28 LYS N . 15013 1 335 . 1 1 29 29 VAL H H 1 9.176 0.004 . . . . . . 29 VAL H . 15013 1 336 . 1 1 29 29 VAL HA H 1 5.334 0.02 . . . . . . 29 VAL HA . 15013 1 337 . 1 1 29 29 VAL HB H 1 2.114 0.02 . . . . . . 29 VAL HB . 15013 1 338 . 1 1 29 29 VAL HG11 H 1 0.753 0.02 . . . . . . 29 VAL HG11 . 15013 1 339 . 1 1 29 29 VAL HG12 H 1 0.753 0.02 . . . . . . 29 VAL HG12 . 15013 1 340 . 1 1 29 29 VAL HG13 H 1 0.753 0.02 . . . . . . 29 VAL HG13 . 15013 1 341 . 1 1 29 29 VAL HG21 H 1 0.835 0.02 . . . . . . 29 VAL HG21 . 15013 1 342 . 1 1 29 29 VAL HG22 H 1 0.835 0.02 . . . . . . 29 VAL HG22 . 15013 1 343 . 1 1 29 29 VAL HG23 H 1 0.835 0.02 . . . . . . 29 VAL HG23 . 15013 1 344 . 1 1 29 29 VAL C C 13 173.995 0.05 . . . . . . 29 VAL C . 15013 1 345 . 1 1 29 29 VAL CA C 13 59.048 0.013 . . . . . . 29 VAL CA . 15013 1 346 . 1 1 29 29 VAL CB C 13 36.757 0.008 . . . . . . 29 VAL CB . 15013 1 347 . 1 1 29 29 VAL CG1 C 13 18.876 0.028 . . . . . . 29 VAL CG1 . 15013 1 348 . 1 1 29 29 VAL CG2 C 13 21.878 0.021 . . . . . . 29 VAL CG2 . 15013 1 349 . 1 1 29 29 VAL N N 15 121.453 0.035 . . . . . . 29 VAL N . 15013 1 350 . 1 1 30 30 GLU H H 1 8.666 0.003 . . . . . . 30 GLU H . 15013 1 351 . 1 1 30 30 GLU HA H 1 5.332 0.02 . . . . . . 30 GLU HA . 15013 1 352 . 1 1 30 30 GLU HB2 H 1 1.861 0.02 . . . . . . 30 GLU HB2 . 15013 1 353 . 1 1 30 30 GLU HB3 H 1 1.861 0.02 . . . . . . 30 GLU HB3 . 15013 1 354 . 1 1 30 30 GLU HG2 H 1 2.292 0.02 . . . . . . 30 GLU HG2 . 15013 1 355 . 1 1 30 30 GLU HG3 H 1 2.292 0.02 . . . . . . 30 GLU HG3 . 15013 1 356 . 1 1 30 30 GLU C C 13 174.821 0.05 . . . . . . 30 GLU C . 15013 1 357 . 1 1 30 30 GLU CA C 13 54.514 0.035 . . . . . . 30 GLU CA . 15013 1 358 . 1 1 30 30 GLU CB C 13 32.215 0.040 . . . . . . 30 GLU CB . 15013 1 359 . 1 1 30 30 GLU CG C 13 33.431 0.05 . . . . . . 30 GLU CG . 15013 1 360 . 1 1 30 30 GLU N N 15 118.996 0.047 . . . . . . 30 GLU N . 15013 1 361 . 1 1 31 31 VAL H H 1 8.657 0.008 . . . . . . 31 VAL H . 15013 1 362 . 1 1 31 31 VAL HA H 1 4.453 0.02 . . . . . . 31 VAL HA . 15013 1 363 . 1 1 31 31 VAL HB H 1 2.115 0.001 . . . . . . 31 VAL HB . 15013 1 364 . 1 1 31 31 VAL HG11 H 1 0.929 0.02 . . . . . . 31 VAL HG11 . 15013 1 365 . 1 1 31 31 VAL HG12 H 1 0.929 0.02 . . . . . . 31 VAL HG12 . 15013 1 366 . 1 1 31 31 VAL HG13 H 1 0.929 0.02 . . . . . . 31 VAL HG13 . 15013 1 367 . 1 1 31 31 VAL HG21 H 1 1.045 0.02 . . . . . . 31 VAL HG21 . 15013 1 368 . 1 1 31 31 VAL HG22 H 1 1.045 0.02 . . . . . . 31 VAL HG22 . 15013 1 369 . 1 1 31 31 VAL HG23 H 1 1.045 0.02 . . . . . . 31 VAL HG23 . 15013 1 370 . 1 1 31 31 VAL C C 13 174.801 0.05 . . . . . . 31 VAL C . 15013 1 371 . 1 1 31 31 VAL CA C 13 61.217 0.002 . . . . . . 31 VAL CA . 15013 1 372 . 1 1 31 31 VAL CB C 13 33.928 0.005 . . . . . . 31 VAL CB . 15013 1 373 . 1 1 31 31 VAL CG1 C 13 19.733 0.050 . . . . . . 31 VAL CG1 . 15013 1 374 . 1 1 31 31 VAL CG2 C 13 21.563 0.019 . . . . . . 31 VAL CG2 . 15013 1 375 . 1 1 31 31 VAL N N 15 124.548 0.045 . . . . . . 31 VAL N . 15013 1 376 . 1 1 32 32 ASN H H 1 9.425 0.011 . . . . . . 32 ASN H . 15013 1 377 . 1 1 32 32 ASN HA H 1 4.334 0.02 . . . . . . 32 ASN HA . 15013 1 378 . 1 1 32 32 ASN HB2 H 1 2.861 0.02 . . . . . . 32 ASN HB2 . 15013 1 379 . 1 1 32 32 ASN HB3 H 1 3.063 0.02 . . . . . . 32 ASN HB3 . 15013 1 380 . 1 1 32 32 ASN HD21 H 1 7.042 0.02 . . . . . . 32 ASN HD21 . 15013 1 381 . 1 1 32 32 ASN HD22 H 1 7.586 0.02 . . . . . . 32 ASN HD22 . 15013 1 382 . 1 1 32 32 ASN C C 13 174.402 0.05 . . . . . . 32 ASN C . 15013 1 383 . 1 1 32 32 ASN CA C 13 55.247 0.007 . . . . . . 32 ASN CA . 15013 1 384 . 1 1 32 32 ASN CB C 13 37.740 0.014 . . . . . . 32 ASN CB . 15013 1 385 . 1 1 32 32 ASN N N 15 126.251 0.038 . . . . . . 32 ASN N . 15013 1 386 . 1 1 32 32 ASN ND2 N 15 113.211 0.05 . . . . . . 32 ASN ND2 . 15013 1 387 . 1 1 33 33 ASP H H 1 8.748 0.008 . . . . . . 33 ASP H . 15013 1 388 . 1 1 33 33 ASP HA H 1 4.418 0.003 . . . . . . 33 ASP HA . 15013 1 389 . 1 1 33 33 ASP HB2 H 1 2.960 0.02 . . . . . . 33 ASP HB2 . 15013 1 390 . 1 1 33 33 ASP HB3 H 1 3.077 0.02 . . . . . . 33 ASP HB3 . 15013 1 391 . 1 1 33 33 ASP C C 13 174.748 0.05 . . . . . . 33 ASP C . 15013 1 392 . 1 1 33 33 ASP CA C 13 54.934 0.014 . . . . . . 33 ASP CA . 15013 1 393 . 1 1 33 33 ASP CB C 13 38.682 0.006 . . . . . . 33 ASP CB . 15013 1 394 . 1 1 33 33 ASP N N 15 112.100 0.032 . . . . . . 33 ASP N . 15013 1 395 . 1 1 34 34 ARG H H 1 8.106 0.004 . . . . . . 34 ARG H . 15013 1 396 . 1 1 34 34 ARG HA H 1 4.691 0.001 . . . . . . 34 ARG HA . 15013 1 397 . 1 1 34 34 ARG HB2 H 1 1.795 0.02 . . . . . . 34 ARG HB2 . 15013 1 398 . 1 1 34 34 ARG HB3 H 1 1.917 0.02 . . . . . . 34 ARG HB3 . 15013 1 399 . 1 1 34 34 ARG HG2 H 1 1.654 0.02 . . . . . . 34 ARG HG2 . 15013 1 400 . 1 1 34 34 ARG HG3 H 1 1.716 0.02 . . . . . . 34 ARG HG3 . 15013 1 401 . 1 1 34 34 ARG HD2 H 1 3.218 0.001 . . . . . . 34 ARG HD2 . 15013 1 402 . 1 1 34 34 ARG HD3 H 1 3.218 0.001 . . . . . . 34 ARG HD3 . 15013 1 403 . 1 1 34 34 ARG HE H 1 7.199 0.004 . . . . . . 34 ARG HE . 15013 1 404 . 1 1 34 34 ARG C C 13 175.030 0.05 . . . . . . 34 ARG C . 15013 1 405 . 1 1 34 34 ARG CA C 13 55.131 0.007 . . . . . . 34 ARG CA . 15013 1 406 . 1 1 34 34 ARG CB C 13 32.315 0.012 . . . . . . 34 ARG CB . 15013 1 407 . 1 1 34 34 ARG CG C 13 27.393 0.009 . . . . . . 34 ARG CG . 15013 1 408 . 1 1 34 34 ARG CD C 13 43.617 0.05 . . . . . . 34 ARG CD . 15013 1 409 . 1 1 34 34 ARG N N 15 119.743 0.047 . . . . . . 34 ARG N . 15013 1 410 . 1 1 34 34 ARG NE N 15 114.751 0.001 . . . . . . 34 ARG NE . 15013 1 411 . 1 1 35 35 GLN H H 1 8.465 0.010 . . . . . . 35 GLN H . 15013 1 412 . 1 1 35 35 GLN HA H 1 5.333 0.001 . . . . . . 35 GLN HA . 15013 1 413 . 1 1 35 35 GLN HB2 H 1 1.739 0.02 . . . . . . 35 GLN HB2 . 15013 1 414 . 1 1 35 35 GLN HB3 H 1 1.890 0.02 . . . . . . 35 GLN HB3 . 15013 1 415 . 1 1 35 35 GLN HG2 H 1 2.109 0.02 . . . . . . 35 GLN HG2 . 15013 1 416 . 1 1 35 35 GLN HG3 H 1 2.253 0.038 . . . . . . 35 GLN HG3 . 15013 1 417 . 1 1 35 35 GLN HE21 H 1 6.713 0.02 . . . . . . 35 GLN HE21 . 15013 1 418 . 1 1 35 35 GLN HE22 H 1 7.304 0.02 . . . . . . 35 GLN HE22 . 15013 1 419 . 1 1 35 35 GLN C C 13 175.915 0.05 . . . . . . 35 GLN C . 15013 1 420 . 1 1 35 35 GLN CA C 13 54.287 0.05 . . . . . . 35 GLN CA . 15013 1 421 . 1 1 35 35 GLN CB C 13 31.572 0.002 . . . . . . 35 GLN CB . 15013 1 422 . 1 1 35 35 GLN CG C 13 33.845 0.032 . . . . . . 35 GLN CG . 15013 1 423 . 1 1 35 35 GLN N N 15 119.853 0.022 . . . . . . 35 GLN N . 15013 1 424 . 1 1 35 35 GLN NE2 N 15 110.590 0.05 . . . . . . 35 GLN NE2 . 15013 1 425 . 1 1 36 36 GLY H H 1 8.434 0.004 . . . . . . 36 GLY H . 15013 1 426 . 1 1 36 36 GLY HA2 H 1 4.129 0.001 . . . . . . 36 GLY HA2 . 15013 1 427 . 1 1 36 36 GLY HA3 H 1 4.129 0.001 . . . . . . 36 GLY HA3 . 15013 1 428 . 1 1 36 36 GLY C C 13 170.828 0.05 . . . . . . 36 GLY C . 15013 1 429 . 1 1 36 36 GLY CA C 13 45.554 0.012 . . . . . . 36 GLY CA . 15013 1 430 . 1 1 36 36 GLY N N 15 107.483 0.049 . . . . . . 36 GLY N . 15013 1 431 . 1 1 37 37 PHE H H 1 8.492 0.014 . . . . . . 37 PHE H . 15013 1 432 . 1 1 37 37 PHE HA H 1 5.592 0.02 . . . . . . 37 PHE HA . 15013 1 433 . 1 1 37 37 PHE HB2 H 1 2.761 0.02 . . . . . . 37 PHE HB2 . 15013 1 434 . 1 1 37 37 PHE HB3 H 1 2.761 0.02 . . . . . . 37 PHE HB3 . 15013 1 435 . 1 1 37 37 PHE HD1 H 1 7.024 0.001 . . . . . . 37 PHE HD1 . 15013 1 436 . 1 1 37 37 PHE HD2 H 1 7.024 0.001 . . . . . . 37 PHE HD2 . 15013 1 437 . 1 1 37 37 PHE HE1 H 1 7.387 0.02 . . . . . . 37 PHE HE1 . 15013 1 438 . 1 1 37 37 PHE HE2 H 1 7.387 0.02 . . . . . . 37 PHE HE2 . 15013 1 439 . 1 1 37 37 PHE C C 13 175.924 0.05 . . . . . . 37 PHE C . 15013 1 440 . 1 1 37 37 PHE CA C 13 57.997 0.027 . . . . . . 37 PHE CA . 15013 1 441 . 1 1 37 37 PHE CB C 13 42.204 0.002 . . . . . . 37 PHE CB . 15013 1 442 . 1 1 37 37 PHE N N 15 117.750 0.011 . . . . . . 37 PHE N . 15013 1 443 . 1 1 38 38 VAL H H 1 9.262 0.001 . . . . . . 38 VAL H . 15013 1 444 . 1 1 38 38 VAL HA H 1 4.919 0.001 . . . . . . 38 VAL HA . 15013 1 445 . 1 1 38 38 VAL HB H 1 1.825 0.02 . . . . . . 38 VAL HB . 15013 1 446 . 1 1 38 38 VAL HG11 H 1 0.711 0.02 . . . . . . 38 VAL HG11 . 15013 1 447 . 1 1 38 38 VAL HG12 H 1 0.711 0.02 . . . . . . 38 VAL HG12 . 15013 1 448 . 1 1 38 38 VAL HG13 H 1 0.711 0.02 . . . . . . 38 VAL HG13 . 15013 1 449 . 1 1 38 38 VAL HG21 H 1 1.048 0.02 . . . . . . 38 VAL HG21 . 15013 1 450 . 1 1 38 38 VAL HG22 H 1 1.048 0.02 . . . . . . 38 VAL HG22 . 15013 1 451 . 1 1 38 38 VAL HG23 H 1 1.048 0.02 . . . . . . 38 VAL HG23 . 15013 1 452 . 1 1 38 38 VAL CA C 13 57.311 0.05 . . . . . . 38 VAL CA . 15013 1 453 . 1 1 38 38 VAL CB C 13 33.096 0.05 . . . . . . 38 VAL CB . 15013 1 454 . 1 1 38 38 VAL CG1 C 13 17.975 0.079 . . . . . . 38 VAL CG1 . 15013 1 455 . 1 1 38 38 VAL CG2 C 13 21.538 0.103 . . . . . . 38 VAL CG2 . 15013 1 456 . 1 1 38 38 VAL N N 15 113.319 0.043 . . . . . . 38 VAL N . 15013 1 457 . 1 1 39 39 PRO HA H 1 3.846 0.001 . . . . . . 39 PRO HA . 15013 1 458 . 1 1 39 39 PRO HB2 H 1 1.045 0.02 . . . . . . 39 PRO HB2 . 15013 1 459 . 1 1 39 39 PRO HB3 H 1 1.327 0.02 . . . . . . 39 PRO HB3 . 15013 1 460 . 1 1 39 39 PRO HG2 H 1 0.104 0.001 . . . . . . 39 PRO HG2 . 15013 1 461 . 1 1 39 39 PRO HG3 H 1 0.715 0.02 . . . . . . 39 PRO HG3 . 15013 1 462 . 1 1 39 39 PRO HD2 H 1 2.097 0.02 . . . . . . 39 PRO HD2 . 15013 1 463 . 1 1 39 39 PRO HD3 H 1 2.391 0.002 . . . . . . 39 PRO HD3 . 15013 1 464 . 1 1 39 39 PRO C C 13 177.902 0.05 . . . . . . 39 PRO C . 15013 1 465 . 1 1 39 39 PRO CA C 13 61.946 0.05 . . . . . . 39 PRO CA . 15013 1 466 . 1 1 39 39 PRO CB C 13 31.143 0.05 . . . . . . 39 PRO CB . 15013 1 467 . 1 1 39 39 PRO CG C 13 27.733 0.051 . . . . . . 39 PRO CG . 15013 1 468 . 1 1 39 39 PRO CD C 13 50.297 0.042 . . . . . . 39 PRO CD . 15013 1 469 . 1 1 40 40 ALA H H 1 7.651 0.002 . . . . . . 40 ALA H . 15013 1 470 . 1 1 40 40 ALA HA H 1 2.629 0.004 . . . . . . 40 ALA HA . 15013 1 471 . 1 1 40 40 ALA HB1 H 1 -0.068 0.02 . . . . . . 40 ALA HB1 . 15013 1 472 . 1 1 40 40 ALA HB2 H 1 -0.068 0.02 . . . . . . 40 ALA HB2 . 15013 1 473 . 1 1 40 40 ALA HB3 H 1 -0.068 0.02 . . . . . . 40 ALA HB3 . 15013 1 474 . 1 1 40 40 ALA C C 13 178.861 0.05 . . . . . . 40 ALA C . 15013 1 475 . 1 1 40 40 ALA CA C 13 55.137 0.034 . . . . . . 40 ALA CA . 15013 1 476 . 1 1 40 40 ALA CB C 13 16.049 0.007 . . . . . . 40 ALA CB . 15013 1 477 . 1 1 40 40 ALA N N 15 130.254 0.031 . . . . . . 40 ALA N . 15013 1 478 . 1 1 41 41 ALA H H 1 8.148 0.003 . . . . . . 41 ALA H . 15013 1 479 . 1 1 41 41 ALA HA H 1 4.113 0.002 . . . . . . 41 ALA HA . 15013 1 480 . 1 1 41 41 ALA HB1 H 1 1.323 0.02 . . . . . . 41 ALA HB1 . 15013 1 481 . 1 1 41 41 ALA HB2 H 1 1.323 0.02 . . . . . . 41 ALA HB2 . 15013 1 482 . 1 1 41 41 ALA HB3 H 1 1.323 0.02 . . . . . . 41 ALA HB3 . 15013 1 483 . 1 1 41 41 ALA C C 13 177.864 0.05 . . . . . . 41 ALA C . 15013 1 484 . 1 1 41 41 ALA CA C 13 52.897 0.003 . . . . . . 41 ALA CA . 15013 1 485 . 1 1 41 41 ALA CB C 13 18.002 0.003 . . . . . . 41 ALA CB . 15013 1 486 . 1 1 41 41 ALA N N 15 113.328 0.031 . . . . . . 41 ALA N . 15013 1 487 . 1 1 42 42 TYR H H 1 7.920 0.006 . . . . . . 42 TYR H . 15013 1 488 . 1 1 42 42 TYR HA H 1 4.793 0.003 . . . . . . 42 TYR HA . 15013 1 489 . 1 1 42 42 TYR HB2 H 1 3.163 0.003 . . . . . . 42 TYR HB2 . 15013 1 490 . 1 1 42 42 TYR HB3 H 1 3.336 0.02 . . . . . . 42 TYR HB3 . 15013 1 491 . 1 1 42 42 TYR HD1 H 1 6.830 0.02 . . . . . . 42 TYR HD1 . 15013 1 492 . 1 1 42 42 TYR HD2 H 1 6.830 0.02 . . . . . . 42 TYR HD2 . 15013 1 493 . 1 1 42 42 TYR HE1 H 1 6.754 0.02 . . . . . . 42 TYR HE1 . 15013 1 494 . 1 1 42 42 TYR HE2 H 1 6.754 0.02 . . . . . . 42 TYR HE2 . 15013 1 495 . 1 1 42 42 TYR C C 13 174.736 0.05 . . . . . . 42 TYR C . 15013 1 496 . 1 1 42 42 TYR CA C 13 57.157 0.027 . . . . . . 42 TYR CA . 15013 1 497 . 1 1 42 42 TYR CB C 13 37.725 0.002 . . . . . . 42 TYR CB . 15013 1 498 . 1 1 42 42 TYR N N 15 116.511 0.003 . . . . . . 42 TYR N . 15013 1 499 . 1 1 43 43 VAL H H 1 7.472 0.001 . . . . . . 43 VAL H . 15013 1 500 . 1 1 43 43 VAL HA H 1 5.483 0.001 . . . . . . 43 VAL HA . 15013 1 501 . 1 1 43 43 VAL HB H 1 1.937 0.02 . . . . . . 43 VAL HB . 15013 1 502 . 1 1 43 43 VAL HG11 H 1 0.775 0.02 . . . . . . 43 VAL HG11 . 15013 1 503 . 1 1 43 43 VAL HG12 H 1 0.775 0.02 . . . . . . 43 VAL HG12 . 15013 1 504 . 1 1 43 43 VAL HG13 H 1 0.775 0.02 . . . . . . 43 VAL HG13 . 15013 1 505 . 1 1 43 43 VAL HG21 H 1 0.794 0.02 . . . . . . 43 VAL HG21 . 15013 1 506 . 1 1 43 43 VAL HG22 H 1 0.794 0.02 . . . . . . 43 VAL HG22 . 15013 1 507 . 1 1 43 43 VAL HG23 H 1 0.794 0.02 . . . . . . 43 VAL HG23 . 15013 1 508 . 1 1 43 43 VAL C C 13 173.648 0.05 . . . . . . 43 VAL C . 15013 1 509 . 1 1 43 43 VAL CA C 13 58.391 0.016 . . . . . . 43 VAL CA . 15013 1 510 . 1 1 43 43 VAL CB C 13 36.427 0.019 . . . . . . 43 VAL CB . 15013 1 511 . 1 1 43 43 VAL CG2 C 13 22.828 0.019 . . . . . . 43 VAL CG2 . 15013 1 512 . 1 1 43 43 VAL N N 15 110.912 0.039 . . . . . . 43 VAL N . 15013 1 513 . 1 1 44 44 LYS H H 1 8.739 0.002 . . . . . . 44 LYS H . 15013 1 514 . 1 1 44 44 LYS HA H 1 4.835 0.002 . . . . . . 44 LYS HA . 15013 1 515 . 1 1 44 44 LYS HB2 H 1 1.720 0.02 . . . . . . 44 LYS HB2 . 15013 1 516 . 1 1 44 44 LYS HB3 H 1 1.720 0.02 . . . . . . 44 LYS HB3 . 15013 1 517 . 1 1 44 44 LYS HG2 H 1 1.373 0.004 . . . . . . 44 LYS HG2 . 15013 1 518 . 1 1 44 44 LYS HG3 H 1 1.459 0.02 . . . . . . 44 LYS HG3 . 15013 1 519 . 1 1 44 44 LYS HD2 H 1 1.642 0.02 . . . . . . 44 LYS HD2 . 15013 1 520 . 1 1 44 44 LYS HD3 H 1 1.642 0.02 . . . . . . 44 LYS HD3 . 15013 1 521 . 1 1 44 44 LYS HE2 H 1 2.958 0.02 . . . . . . 44 LYS HE2 . 15013 1 522 . 1 1 44 44 LYS HE3 H 1 2.958 0.02 . . . . . . 44 LYS HE3 . 15013 1 523 . 1 1 44 44 LYS C C 13 176.280 0.05 . . . . . . 44 LYS C . 15013 1 524 . 1 1 44 44 LYS CA C 13 54.240 0.005 . . . . . . 44 LYS CA . 15013 1 525 . 1 1 44 44 LYS CB C 13 37.042 0.020 . . . . . . 44 LYS CB . 15013 1 526 . 1 1 44 44 LYS CD C 13 30.018 0.058 . . . . . . 44 LYS CD . 15013 1 527 . 1 1 44 44 LYS N N 15 118.908 0.023 . . . . . . 44 LYS N . 15013 1 528 . 1 1 45 45 LYS H H 1 9.190 0.012 . . . . . . 45 LYS H . 15013 1 529 . 1 1 45 45 LYS HA H 1 4.500 0.001 . . . . . . 45 LYS HA . 15013 1 530 . 1 1 45 45 LYS HB2 H 1 1.838 0.02 . . . . . . 45 LYS HB2 . 15013 1 531 . 1 1 45 45 LYS HB3 H 1 1.997 0.02 . . . . . . 45 LYS HB3 . 15013 1 532 . 1 1 45 45 LYS HG2 H 1 1.433 0.001 . . . . . . 45 LYS HG2 . 15013 1 533 . 1 1 45 45 LYS HG3 H 1 1.712 0.006 . . . . . . 45 LYS HG3 . 15013 1 534 . 1 1 45 45 LYS HD2 H 1 1.642 0.001 . . . . . . 45 LYS HD2 . 15013 1 535 . 1 1 45 45 LYS HD3 H 1 1.719 0.02 . . . . . . 45 LYS HD3 . 15013 1 536 . 1 1 45 45 LYS HE2 H 1 2.758 0.001 . . . . . . 45 LYS HE2 . 15013 1 537 . 1 1 45 45 LYS HE3 H 1 2.846 0.003 . . . . . . 45 LYS HE3 . 15013 1 538 . 1 1 45 45 LYS CA C 13 58.683 0.017 . . . . . . 45 LYS CA . 15013 1 539 . 1 1 45 45 LYS CB C 13 33.291 0.007 . . . . . . 45 LYS CB . 15013 1 540 . 1 1 45 45 LYS CG C 13 26.100 0.048 . . . . . . 45 LYS CG . 15013 1 541 . 1 1 45 45 LYS CD C 13 29.649 0.05 . . . . . . 45 LYS CD . 15013 1 542 . 1 1 45 45 LYS N N 15 126.137 0.051 . . . . . . 45 LYS N . 15013 1 543 . 1 1 46 46 LEU H H 1 8.320 0.004 . . . . . . 46 LEU H . 15013 1 544 . 1 1 46 46 LEU HA H 1 4.573 0.002 . . . . . . 46 LEU HA . 15013 1 545 . 1 1 46 46 LEU HB2 H 1 1.498 0.02 . . . . . . 46 LEU HB2 . 15013 1 546 . 1 1 46 46 LEU HB3 H 1 1.565 0.02 . . . . . . 46 LEU HB3 . 15013 1 547 . 1 1 46 46 LEU HG H 1 1.643 0.02 . . . . . . 46 LEU HG . 15013 1 548 . 1 1 46 46 LEU HD11 H 1 0.867 0.02 . . . . . . 46 LEU HD11 . 15013 1 549 . 1 1 46 46 LEU HD12 H 1 0.867 0.02 . . . . . . 46 LEU HD12 . 15013 1 550 . 1 1 46 46 LEU HD13 H 1 0.867 0.02 . . . . . . 46 LEU HD13 . 15013 1 551 . 1 1 46 46 LEU HD21 H 1 0.867 0.02 . . . . . . 46 LEU HD21 . 15013 1 552 . 1 1 46 46 LEU HD22 H 1 0.867 0.02 . . . . . . 46 LEU HD22 . 15013 1 553 . 1 1 46 46 LEU HD23 H 1 0.867 0.02 . . . . . . 46 LEU HD23 . 15013 1 554 . 1 1 46 46 LEU C C 13 176.707 0.322 . . . . . . 46 LEU C . 15013 1 555 . 1 1 46 46 LEU CA C 13 54.088 0.019 . . . . . . 46 LEU CA . 15013 1 556 . 1 1 46 46 LEU CB C 13 43.729 0.027 . . . . . . 46 LEU CB . 15013 1 557 . 1 1 46 46 LEU CG C 13 27.201 0.066 . . . . . . 46 LEU CG . 15013 1 558 . 1 1 46 46 LEU CD1 C 13 25.963 0.061 . . . . . . 46 LEU CD1 . 15013 1 559 . 1 1 46 46 LEU CD2 C 13 25.963 0.061 . . . . . . 46 LEU CD2 . 15013 1 560 . 1 1 46 46 LEU N N 15 125.332 0.039 . . . . . . 46 LEU N . 15013 1 561 . 1 1 47 47 ASP H H 1 8.619 0.020 . . . . . . 47 ASP H . 15013 1 562 . 1 1 47 47 ASP HA H 1 4.832 0.02 . . . . . . 47 ASP HA . 15013 1 563 . 1 1 47 47 ASP HB2 H 1 2.747 0.02 . . . . . . 47 ASP HB2 . 15013 1 564 . 1 1 47 47 ASP HB3 H 1 2.881 0.02 . . . . . . 47 ASP HB3 . 15013 1 565 . 1 1 47 47 ASP C C 13 175.795 0.05 . . . . . . 47 ASP C . 15013 1 566 . 1 1 47 47 ASP CA C 13 53.777 0.009 . . . . . . 47 ASP CA . 15013 1 567 . 1 1 47 47 ASP CB C 13 39.717 0.001 . . . . . . 47 ASP CB . 15013 1 568 . 1 1 47 47 ASP N N 15 121.309 0.040 . . . . . . 47 ASP N . 15013 1 569 . 1 1 48 48 SER H H 1 8.312 0.007 . . . . . . 48 SER H . 15013 1 570 . 1 1 48 48 SER HA H 1 4.560 0.003 . . . . . . 48 SER HA . 15013 1 571 . 1 1 48 48 SER HB2 H 1 3.817 0.02 . . . . . . 48 SER HB2 . 15013 1 572 . 1 1 48 48 SER HB3 H 1 3.951 0.02 . . . . . . 48 SER HB3 . 15013 1 573 . 1 1 48 48 SER C C 13 175.436 0.05 . . . . . . 48 SER C . 15013 1 574 . 1 1 48 48 SER CA C 13 58.373 0.015 . . . . . . 48 SER CA . 15013 1 575 . 1 1 48 48 SER CB C 13 64.689 0.042 . . . . . . 48 SER CB . 15013 1 576 . 1 1 48 48 SER N N 15 116.622 0.006 . . . . . . 48 SER N . 15013 1 577 . 1 1 49 49 GLY H H 1 8.587 0.005 . . . . . . 49 GLY H . 15013 1 578 . 1 1 49 49 GLY HA2 H 1 4.071 0.002 . . . . . . 49 GLY HA2 . 15013 1 579 . 1 1 49 49 GLY HA3 H 1 4.071 0.002 . . . . . . 49 GLY HA3 . 15013 1 580 . 1 1 49 49 GLY C C 13 174.886 0.05 . . . . . . 49 GLY C . 15013 1 581 . 1 1 49 49 GLY CA C 13 45.844 0.012 . . . . . . 49 GLY CA . 15013 1 582 . 1 1 49 49 GLY N N 15 111.630 0.046 . . . . . . 49 GLY N . 15013 1 583 . 1 1 50 50 THR H H 1 8.145 0.004 . . . . . . 50 THR H . 15013 1 584 . 1 1 50 50 THR HA H 1 4.408 0.02 . . . . . . 50 THR HA . 15013 1 585 . 1 1 50 50 THR HB H 1 4.364 0.02 . . . . . . 50 THR HB . 15013 1 586 . 1 1 50 50 THR HG21 H 1 1.196 0.02 . . . . . . 50 THR HG21 . 15013 1 587 . 1 1 50 50 THR HG22 H 1 1.196 0.02 . . . . . . 50 THR HG22 . 15013 1 588 . 1 1 50 50 THR HG23 H 1 1.196 0.02 . . . . . . 50 THR HG23 . 15013 1 589 . 1 1 50 50 THR C C 13 175.580 0.05 . . . . . . 50 THR C . 15013 1 590 . 1 1 50 50 THR CA C 13 61.973 0.001 . . . . . . 50 THR CA . 15013 1 591 . 1 1 50 50 THR CB C 13 70.121 0.012 . . . . . . 50 THR CB . 15013 1 592 . 1 1 50 50 THR N N 15 112.104 0.012 . . . . . . 50 THR N . 15013 1 593 . 1 1 51 51 GLY H H 1 8.424 0.003 . . . . . . 51 GLY H . 15013 1 594 . 1 1 51 51 GLY HA2 H 1 3.853 0.003 . . . . . . 51 GLY HA2 . 15013 1 595 . 1 1 51 51 GLY HA3 H 1 4.085 0.001 . . . . . . 51 GLY HA3 . 15013 1 596 . 1 1 51 51 GLY C C 13 174.068 0.05 . . . . . . 51 GLY C . 15013 1 597 . 1 1 51 51 GLY CA C 13 45.602 0.002 . . . . . . 51 GLY CA . 15013 1 598 . 1 1 51 51 GLY N N 15 110.990 0.027 . . . . . . 51 GLY N . 15013 1 599 . 1 1 52 52 LYS H H 1 7.724 0.011 . . . . . . 52 LYS H . 15013 1 600 . 1 1 52 52 LYS HA H 1 4.343 0.002 . . . . . . 52 LYS HA . 15013 1 601 . 1 1 52 52 LYS HB2 H 1 1.649 0.02 . . . . . . 52 LYS HB2 . 15013 1 602 . 1 1 52 52 LYS HB3 H 1 1.722 0.02 . . . . . . 52 LYS HB3 . 15013 1 603 . 1 1 52 52 LYS HG2 H 1 1.344 0.02 . . . . . . 52 LYS HG2 . 15013 1 604 . 1 1 52 52 LYS HG3 H 1 1.381 0.02 . . . . . . 52 LYS HG3 . 15013 1 605 . 1 1 52 52 LYS HD2 H 1 1.628 0.02 . . . . . . 52 LYS HD2 . 15013 1 606 . 1 1 52 52 LYS HD3 H 1 1.628 0.02 . . . . . . 52 LYS HD3 . 15013 1 607 . 1 1 52 52 LYS HE2 H 1 2.965 0.02 . . . . . . 52 LYS HE2 . 15013 1 608 . 1 1 52 52 LYS HE3 H 1 2.965 0.02 . . . . . . 52 LYS HE3 . 15013 1 609 . 1 1 52 52 LYS C C 13 175.851 0.05 . . . . . . 52 LYS C . 15013 1 610 . 1 1 52 52 LYS CA C 13 55.855 0.038 . . . . . . 52 LYS CA . 15013 1 611 . 1 1 52 52 LYS CB C 13 33.698 0.006 . . . . . . 52 LYS CB . 15013 1 612 . 1 1 52 52 LYS CD C 13 29.452 0.062 . . . . . . 52 LYS CD . 15013 1 613 . 1 1 52 52 LYS CE C 13 42.530 0.05 . . . . . . 52 LYS CE . 15013 1 614 . 1 1 52 52 LYS N N 15 120.068 0.009 . . . . . . 52 LYS N . 15013 1 615 . 1 1 53 53 GLU H H 1 8.649 0.010 . . . . . . 53 GLU H . 15013 1 616 . 1 1 53 53 GLU HA H 1 4.534 0.001 . . . . . . 53 GLU HA . 15013 1 617 . 1 1 53 53 GLU HB2 H 1 2.010 0.010 . . . . . . 53 GLU HB2 . 15013 1 618 . 1 1 53 53 GLU HB3 H 1 2.122 0.02 . . . . . . 53 GLU HB3 . 15013 1 619 . 1 1 53 53 GLU HG2 H 1 2.350 0.02 . . . . . . 53 GLU HG2 . 15013 1 620 . 1 1 53 53 GLU HG3 H 1 2.461 0.02 . . . . . . 53 GLU HG3 . 15013 1 621 . 1 1 53 53 GLU C C 13 174.641 0.05 . . . . . . 53 GLU C . 15013 1 622 . 1 1 53 53 GLU CA C 13 55.780 0.05 . . . . . . 53 GLU CA . 15013 1 623 . 1 1 53 53 GLU CB C 13 29.538 0.011 . . . . . . 53 GLU CB . 15013 1 624 . 1 1 53 53 GLU CG C 13 33.837 0.012 . . . . . . 53 GLU CG . 15013 1 625 . 1 1 53 53 GLU N N 15 122.758 0.025 . . . . . . 53 GLU N . 15013 1 626 . 1 1 54 54 LEU H H 1 8.438 0.008 . . . . . . 54 LEU H . 15013 1 627 . 1 1 54 54 LEU HA H 1 5.412 0.001 . . . . . . 54 LEU HA . 15013 1 628 . 1 1 54 54 LEU HB2 H 1 1.375 0.02 . . . . . . 54 LEU HB2 . 15013 1 629 . 1 1 54 54 LEU HB3 H 1 1.671 0.02 . . . . . . 54 LEU HB3 . 15013 1 630 . 1 1 54 54 LEU HG H 1 1.566 0.02 . . . . . . 54 LEU HG . 15013 1 631 . 1 1 54 54 LEU HD11 H 1 0.795 0.02 . . . . . . 54 LEU HD11 . 15013 1 632 . 1 1 54 54 LEU HD12 H 1 0.795 0.02 . . . . . . 54 LEU HD12 . 15013 1 633 . 1 1 54 54 LEU HD13 H 1 0.795 0.02 . . . . . . 54 LEU HD13 . 15013 1 634 . 1 1 54 54 LEU HD21 H 1 0.837 0.02 . . . . . . 54 LEU HD21 . 15013 1 635 . 1 1 54 54 LEU HD22 H 1 0.837 0.02 . . . . . . 54 LEU HD22 . 15013 1 636 . 1 1 54 54 LEU HD23 H 1 0.837 0.02 . . . . . . 54 LEU HD23 . 15013 1 637 . 1 1 54 54 LEU C C 13 177.384 0.05 . . . . . . 54 LEU C . 15013 1 638 . 1 1 54 54 LEU CA C 13 53.436 0.017 . . . . . . 54 LEU CA . 15013 1 639 . 1 1 54 54 LEU CB C 13 46.225 0.025 . . . . . . 54 LEU CB . 15013 1 640 . 1 1 54 54 LEU CD1 C 13 23.625 0.048 . . . . . . 54 LEU CD1 . 15013 1 641 . 1 1 54 54 LEU CD2 C 13 25.645 0.035 . . . . . . 54 LEU CD2 . 15013 1 642 . 1 1 54 54 LEU N N 15 124.029 0.037 . . . . . . 54 LEU N . 15013 1 643 . 1 1 55 55 VAL H H 1 9.106 0.002 . . . . . . 55 VAL H . 15013 1 644 . 1 1 55 55 VAL HA H 1 5.239 0.001 . . . . . . 55 VAL HA . 15013 1 645 . 1 1 55 55 VAL HB H 1 2.008 0.02 . . . . . . 55 VAL HB . 15013 1 646 . 1 1 55 55 VAL HG11 H 1 0.804 0.02 . . . . . . 55 VAL HG11 . 15013 1 647 . 1 1 55 55 VAL HG12 H 1 0.804 0.02 . . . . . . 55 VAL HG12 . 15013 1 648 . 1 1 55 55 VAL HG13 H 1 0.804 0.02 . . . . . . 55 VAL HG13 . 15013 1 649 . 1 1 55 55 VAL HG21 H 1 1.057 0.02 . . . . . . 55 VAL HG21 . 15013 1 650 . 1 1 55 55 VAL HG22 H 1 1.057 0.02 . . . . . . 55 VAL HG22 . 15013 1 651 . 1 1 55 55 VAL HG23 H 1 1.057 0.02 . . . . . . 55 VAL HG23 . 15013 1 652 . 1 1 55 55 VAL C C 13 172.848 0.05 . . . . . . 55 VAL C . 15013 1 653 . 1 1 55 55 VAL CA C 13 58.106 0.002 . . . . . . 55 VAL CA . 15013 1 654 . 1 1 55 55 VAL CB C 13 36.203 0.006 . . . . . . 55 VAL CB . 15013 1 655 . 1 1 55 55 VAL CG1 C 13 20.140 0.023 . . . . . . 55 VAL CG1 . 15013 1 656 . 1 1 55 55 VAL CG2 C 13 24.276 0.011 . . . . . . 55 VAL CG2 . 15013 1 657 . 1 1 55 55 VAL N N 15 111.440 0.013 . . . . . . 55 VAL N . 15013 1 658 . 1 1 56 56 LEU H H 1 9.015 0.002 . . . . . . 56 LEU H . 15013 1 659 . 1 1 56 56 LEU HA H 1 5.106 0.001 . . . . . . 56 LEU HA . 15013 1 660 . 1 1 56 56 LEU HB2 H 1 1.388 0.02 . . . . . . 56 LEU HB2 . 15013 1 661 . 1 1 56 56 LEU HB3 H 1 1.726 0.02 . . . . . . 56 LEU HB3 . 15013 1 662 . 1 1 56 56 LEU HG H 1 1.264 0.02 . . . . . . 56 LEU HG . 15013 1 663 . 1 1 56 56 LEU HD11 H 1 0.803 0.02 . . . . . . 56 LEU HD11 . 15013 1 664 . 1 1 56 56 LEU HD12 H 1 0.803 0.02 . . . . . . 56 LEU HD12 . 15013 1 665 . 1 1 56 56 LEU HD13 H 1 0.803 0.02 . . . . . . 56 LEU HD13 . 15013 1 666 . 1 1 56 56 LEU HD21 H 1 0.846 0.02 . . . . . . 56 LEU HD21 . 15013 1 667 . 1 1 56 56 LEU HD22 H 1 0.846 0.02 . . . . . . 56 LEU HD22 . 15013 1 668 . 1 1 56 56 LEU HD23 H 1 0.846 0.02 . . . . . . 56 LEU HD23 . 15013 1 669 . 1 1 56 56 LEU C C 13 176.869 0.05 . . . . . . 56 LEU C . 15013 1 670 . 1 1 56 56 LEU CA C 13 52.793 0.097 . . . . . . 56 LEU CA . 15013 1 671 . 1 1 56 56 LEU CB C 13 46.801 0.001 . . . . . . 56 LEU CB . 15013 1 672 . 1 1 56 56 LEU CD1 C 13 26.541 0.097 . . . . . . 56 LEU CD1 . 15013 1 673 . 1 1 56 56 LEU CD2 C 13 24.357 0.057 . . . . . . 56 LEU CD2 . 15013 1 674 . 1 1 56 56 LEU N N 15 123.355 0.036 . . . . . . 56 LEU N . 15013 1 675 . 1 1 57 57 ALA H H 1 9.214 0.003 . . . . . . 57 ALA H . 15013 1 676 . 1 1 57 57 ALA HA H 1 4.549 0.001 . . . . . . 57 ALA HA . 15013 1 677 . 1 1 57 57 ALA HB1 H 1 1.611 0.02 . . . . . . 57 ALA HB1 . 15013 1 678 . 1 1 57 57 ALA HB2 H 1 1.611 0.02 . . . . . . 57 ALA HB2 . 15013 1 679 . 1 1 57 57 ALA HB3 H 1 1.611 0.02 . . . . . . 57 ALA HB3 . 15013 1 680 . 1 1 57 57 ALA C C 13 178.476 0.05 . . . . . . 57 ALA C . 15013 1 681 . 1 1 57 57 ALA CA C 13 52.957 0.05 . . . . . . 57 ALA CA . 15013 1 682 . 1 1 57 57 ALA CB C 13 19.754 0.046 . . . . . . 57 ALA CB . 15013 1 683 . 1 1 57 57 ALA N N 15 127.357 0.016 . . . . . . 57 ALA N . 15013 1 684 . 1 1 58 58 LEU H H 1 9.238 0.006 . . . . . . 58 LEU H . 15013 1 685 . 1 1 58 58 LEU HA H 1 3.912 0.001 . . . . . . 58 LEU HA . 15013 1 686 . 1 1 58 58 LEU HB2 H 1 0.526 0.02 . . . . . . 58 LEU HB2 . 15013 1 687 . 1 1 58 58 LEU HB3 H 1 1.076 0.02 . . . . . . 58 LEU HB3 . 15013 1 688 . 1 1 58 58 LEU HG H 1 1.324 0.02 . . . . . . 58 LEU HG . 15013 1 689 . 1 1 58 58 LEU HD11 H 1 0.593 0.02 . . . . . . 58 LEU HD11 . 15013 1 690 . 1 1 58 58 LEU HD12 H 1 0.593 0.02 . . . . . . 58 LEU HD12 . 15013 1 691 . 1 1 58 58 LEU HD13 H 1 0.593 0.02 . . . . . . 58 LEU HD13 . 15013 1 692 . 1 1 58 58 LEU HD21 H 1 0.648 0.02 . . . . . . 58 LEU HD21 . 15013 1 693 . 1 1 58 58 LEU HD22 H 1 0.648 0.02 . . . . . . 58 LEU HD22 . 15013 1 694 . 1 1 58 58 LEU HD23 H 1 0.648 0.02 . . . . . . 58 LEU HD23 . 15013 1 695 . 1 1 58 58 LEU C C 13 175.258 0.05 . . . . . . 58 LEU C . 15013 1 696 . 1 1 58 58 LEU CA C 13 55.756 0.028 . . . . . . 58 LEU CA . 15013 1 697 . 1 1 58 58 LEU CB C 13 43.079 0.003 . . . . . . 58 LEU CB . 15013 1 698 . 1 1 58 58 LEU CD1 C 13 21.950 0.065 . . . . . . 58 LEU CD1 . 15013 1 699 . 1 1 58 58 LEU CD2 C 13 25.551 0.045 . . . . . . 58 LEU CD2 . 15013 1 700 . 1 1 58 58 LEU N N 15 126.607 0.014 . . . . . . 58 LEU N . 15013 1 701 . 1 1 59 59 TYR H H 1 7.033 0.001 . . . . . . 59 TYR H . 15013 1 702 . 1 1 59 59 TYR HA H 1 4.691 0.001 . . . . . . 59 TYR HA . 15013 1 703 . 1 1 59 59 TYR HB2 H 1 2.082 0.02 . . . . . . 59 TYR HB2 . 15013 1 704 . 1 1 59 59 TYR HB3 H 1 3.075 0.002 . . . . . . 59 TYR HB3 . 15013 1 705 . 1 1 59 59 TYR HD1 H 1 6.640 0.02 . . . . . . 59 TYR HD1 . 15013 1 706 . 1 1 59 59 TYR HD2 H 1 6.640 0.02 . . . . . . 59 TYR HD2 . 15013 1 707 . 1 1 59 59 TYR HE1 H 1 6.586 0.02 . . . . . . 59 TYR HE1 . 15013 1 708 . 1 1 59 59 TYR HE2 H 1 6.586 0.02 . . . . . . 59 TYR HE2 . 15013 1 709 . 1 1 59 59 TYR C C 13 173.398 0.05 . . . . . . 59 TYR C . 15013 1 710 . 1 1 59 59 TYR CA C 13 54.556 0.015 . . . . . . 59 TYR CA . 15013 1 711 . 1 1 59 59 TYR CB C 13 43.302 0.047 . . . . . . 59 TYR CB . 15013 1 712 . 1 1 59 59 TYR N N 15 111.462 0.023 . . . . . . 59 TYR N . 15013 1 713 . 1 1 60 60 ASP H H 1 8.281 0.026 . . . . . . 60 ASP H . 15013 1 714 . 1 1 60 60 ASP HA H 1 4.920 0.02 . . . . . . 60 ASP HA . 15013 1 715 . 1 1 60 60 ASP HB2 H 1 2.742 0.02 . . . . . . 60 ASP HB2 . 15013 1 716 . 1 1 60 60 ASP HB3 H 1 2.888 0.02 . . . . . . 60 ASP HB3 . 15013 1 717 . 1 1 60 60 ASP C C 13 176.991 0.05 . . . . . . 60 ASP C . 15013 1 718 . 1 1 60 60 ASP CA C 13 54.128 0.026 . . . . . . 60 ASP CA . 15013 1 719 . 1 1 60 60 ASP CB C 13 41.044 0.008 . . . . . . 60 ASP CB . 15013 1 720 . 1 1 60 60 ASP N N 15 117.786 0.015 . . . . . . 60 ASP N . 15013 1 721 . 1 1 61 61 TYR H H 1 8.877 0.002 . . . . . . 61 TYR H . 15013 1 722 . 1 1 61 61 TYR HA H 1 4.732 0.02 . . . . . . 61 TYR HA . 15013 1 723 . 1 1 61 61 TYR HB2 H 1 2.751 0.001 . . . . . . 61 TYR HB2 . 15013 1 724 . 1 1 61 61 TYR HB3 H 1 3.354 0.001 . . . . . . 61 TYR HB3 . 15013 1 725 . 1 1 61 61 TYR HD1 H 1 7.125 0.02 . . . . . . 61 TYR HD1 . 15013 1 726 . 1 1 61 61 TYR HD2 H 1 7.125 0.02 . . . . . . 61 TYR HD2 . 15013 1 727 . 1 1 61 61 TYR HE1 H 1 6.987 0.02 . . . . . . 61 TYR HE1 . 15013 1 728 . 1 1 61 61 TYR HE2 H 1 6.987 0.02 . . . . . . 61 TYR HE2 . 15013 1 729 . 1 1 61 61 TYR C C 13 173.155 0.05 . . . . . . 61 TYR C . 15013 1 730 . 1 1 61 61 TYR CA C 13 60.027 0.023 . . . . . . 61 TYR CA . 15013 1 731 . 1 1 61 61 TYR CB C 13 43.365 0.006 . . . . . . 61 TYR CB . 15013 1 732 . 1 1 61 61 TYR N N 15 119.377 0.011 . . . . . . 61 TYR N . 15013 1 733 . 1 1 62 62 GLN H H 1 7.660 0.003 . . . . . . 62 GLN H . 15013 1 734 . 1 1 62 62 GLN HA H 1 4.673 0.003 . . . . . . 62 GLN HA . 15013 1 735 . 1 1 62 62 GLN HB2 H 1 1.916 0.02 . . . . . . 62 GLN HB2 . 15013 1 736 . 1 1 62 62 GLN HB3 H 1 1.916 0.02 . . . . . . 62 GLN HB3 . 15013 1 737 . 1 1 62 62 GLN HG2 H 1 1.994 0.02 . . . . . . 62 GLN HG2 . 15013 1 738 . 1 1 62 62 GLN HG3 H 1 1.994 0.02 . . . . . . 62 GLN HG3 . 15013 1 739 . 1 1 62 62 GLN HE21 H 1 6.759 0.02 . . . . . . 62 GLN HE21 . 15013 1 740 . 1 1 62 62 GLN HE22 H 1 7.432 0.02 . . . . . . 62 GLN HE22 . 15013 1 741 . 1 1 62 62 GLN C C 13 173.764 0.05 . . . . . . 62 GLN C . 15013 1 742 . 1 1 62 62 GLN CA C 13 54.838 0.001 . . . . . . 62 GLN CA . 15013 1 743 . 1 1 62 62 GLN CB C 13 30.599 0.001 . . . . . . 62 GLN CB . 15013 1 744 . 1 1 62 62 GLN N N 15 126.124 0.054 . . . . . . 62 GLN N . 15013 1 745 . 1 1 62 62 GLN NE2 N 15 112.103 0.05 . . . . . . 62 GLN NE2 . 15013 1 746 . 1 1 63 63 GLU H H 1 8.180 0.033 . . . . . . 63 GLU H . 15013 1 747 . 1 1 63 63 GLU HA H 1 4.380 0.001 . . . . . . 63 GLU HA . 15013 1 748 . 1 1 63 63 GLU HB2 H 1 2.145 0.02 . . . . . . 63 GLU HB2 . 15013 1 749 . 1 1 63 63 GLU HB3 H 1 2.236 0.02 . . . . . . 63 GLU HB3 . 15013 1 750 . 1 1 63 63 GLU HG2 H 1 2.575 0.02 . . . . . . 63 GLU HG2 . 15013 1 751 . 1 1 63 63 GLU HG3 H 1 2.652 0.02 . . . . . . 63 GLU HG3 . 15013 1 752 . 1 1 63 63 GLU C C 13 175.621 0.05 . . . . . . 63 GLU C . 15013 1 753 . 1 1 63 63 GLU CA C 13 56.131 0.007 . . . . . . 63 GLU CA . 15013 1 754 . 1 1 63 63 GLU CB C 13 30.130 0.035 . . . . . . 63 GLU CB . 15013 1 755 . 1 1 63 63 GLU CG C 13 33.383 0.047 . . . . . . 63 GLU CG . 15013 1 756 . 1 1 63 63 GLU N N 15 122.776 0.036 . . . . . . 63 GLU N . 15013 1 757 . 1 1 64 64 SER H H 1 8.453 0.008 . . . . . . 64 SER H . 15013 1 758 . 1 1 64 64 SER HA H 1 4.668 0.002 . . . . . . 64 SER HA . 15013 1 759 . 1 1 64 64 SER HB2 H 1 3.869 0.02 . . . . . . 64 SER HB2 . 15013 1 760 . 1 1 64 64 SER HB3 H 1 3.869 0.02 . . . . . . 64 SER HB3 . 15013 1 761 . 1 1 64 64 SER C C 13 174.943 0.05 . . . . . . 64 SER C . 15013 1 762 . 1 1 64 64 SER CA C 13 58.191 0.009 . . . . . . 64 SER CA . 15013 1 763 . 1 1 64 64 SER CB C 13 64.582 0.025 . . . . . . 64 SER CB . 15013 1 764 . 1 1 64 64 SER N N 15 117.598 0.011 . . . . . . 64 SER N . 15013 1 765 . 1 1 65 65 GLY H H 1 8.360 0.002 . . . . . . 65 GLY H . 15013 1 766 . 1 1 65 65 GLY HA2 H 1 4.063 0.001 . . . . . . 65 GLY HA2 . 15013 1 767 . 1 1 65 65 GLY HA3 H 1 4.220 0.001 . . . . . . 65 GLY HA3 . 15013 1 768 . 1 1 65 65 GLY C C 13 173.929 0.05 . . . . . . 65 GLY C . 15013 1 769 . 1 1 65 65 GLY CA C 13 45.286 0.05 . . . . . . 65 GLY CA . 15013 1 770 . 1 1 65 65 GLY N N 15 111.496 0.031 . . . . . . 65 GLY N . 15013 1 771 . 1 1 66 66 ASP H H 1 8.435 0.016 . . . . . . 66 ASP H . 15013 1 772 . 1 1 66 66 ASP HA H 1 4.890 0.02 . . . . . . 66 ASP HA . 15013 1 773 . 1 1 66 66 ASP HB2 H 1 2.812 0.001 . . . . . . 66 ASP HB2 . 15013 1 774 . 1 1 66 66 ASP HB3 H 1 2.812 0.001 . . . . . . 66 ASP HB3 . 15013 1 775 . 1 1 66 66 ASP C C 13 175.372 0.05 . . . . . . 66 ASP C . 15013 1 776 . 1 1 66 66 ASP CA C 13 53.966 0.019 . . . . . . 66 ASP CA . 15013 1 777 . 1 1 66 66 ASP CB C 13 40.248 0.004 . . . . . . 66 ASP CB . 15013 1 778 . 1 1 66 66 ASP N N 15 117.852 0.013 . . . . . . 66 ASP N . 15013 1 779 . 1 1 67 67 ASN H H 1 8.053 0.006 . . . . . . 67 ASN H . 15013 1 780 . 1 1 67 67 ASN HA H 1 4.723 0.02 . . . . . . 67 ASN HA . 15013 1 781 . 1 1 67 67 ASN HB2 H 1 2.566 0.02 . . . . . . 67 ASN HB2 . 15013 1 782 . 1 1 67 67 ASN HB3 H 1 2.620 0.02 . . . . . . 67 ASN HB3 . 15013 1 783 . 1 1 67 67 ASN HD21 H 1 6.856 0.02 . . . . . . 67 ASN HD21 . 15013 1 784 . 1 1 67 67 ASN HD22 H 1 7.432 0.02 . . . . . . 67 ASN HD22 . 15013 1 785 . 1 1 67 67 ASN C C 13 174.159 0.05 . . . . . . 67 ASN C . 15013 1 786 . 1 1 67 67 ASN CA C 13 52.331 0.004 . . . . . . 67 ASN CA . 15013 1 787 . 1 1 67 67 ASN CB C 13 40.204 0.060 . . . . . . 67 ASN CB . 15013 1 788 . 1 1 67 67 ASN N N 15 117.060 0.006 . . . . . . 67 ASN N . 15013 1 789 . 1 1 67 67 ASN ND2 N 15 113.444 0.05 . . . . . . 67 ASN ND2 . 15013 1 790 . 1 1 68 68 ALA H H 1 7.960 0.013 . . . . . . 68 ALA H . 15013 1 791 . 1 1 68 68 ALA HA H 1 3.151 0.02 . . . . . . 68 ALA HA . 15013 1 792 . 1 1 68 68 ALA HB1 H 1 0.708 0.02 . . . . . . 68 ALA HB1 . 15013 1 793 . 1 1 68 68 ALA HB2 H 1 0.708 0.02 . . . . . . 68 ALA HB2 . 15013 1 794 . 1 1 68 68 ALA HB3 H 1 0.708 0.02 . . . . . . 68 ALA HB3 . 15013 1 795 . 1 1 68 68 ALA CA C 13 50.551 0.05 . . . . . . 68 ALA CA . 15013 1 796 . 1 1 68 68 ALA CB C 13 17.177 0.05 . . . . . . 68 ALA CB . 15013 1 797 . 1 1 68 68 ALA N N 15 125.697 0.025 . . . . . . 68 ALA N . 15013 1 798 . 1 1 69 69 PRO HA H 1 3.716 0.001 . . . . . . 69 PRO HA . 15013 1 799 . 1 1 69 69 PRO HB2 H 1 0.415 0.02 . . . . . . 69 PRO HB2 . 15013 1 800 . 1 1 69 69 PRO HB3 H 1 1.027 0.02 . . . . . . 69 PRO HB3 . 15013 1 801 . 1 1 69 69 PRO HG2 H 1 0.901 0.02 . . . . . . 69 PRO HG2 . 15013 1 802 . 1 1 69 69 PRO HG3 H 1 0.901 0.02 . . . . . . 69 PRO HG3 . 15013 1 803 . 1 1 69 69 PRO C C 13 176.218 0.05 . . . . . . 69 PRO C . 15013 1 804 . 1 1 69 69 PRO CA C 13 62.623 0.05 . . . . . . 69 PRO CA . 15013 1 805 . 1 1 69 69 PRO CB C 13 31.648 0.05 . . . . . . 69 PRO CB . 15013 1 806 . 1 1 69 69 PRO CG C 13 27.569 0.075 . . . . . . 69 PRO CG . 15013 1 807 . 1 1 69 69 PRO CD C 13 49.121 0.040 . . . . . . 69 PRO CD . 15013 1 808 . 1 1 70 70 SER H H 1 8.067 0.016 . . . . . . 70 SER H . 15013 1 809 . 1 1 70 70 SER HA H 1 4.316 0.02 . . . . . . 70 SER HA . 15013 1 810 . 1 1 70 70 SER HB2 H 1 3.745 0.002 . . . . . . 70 SER HB2 . 15013 1 811 . 1 1 70 70 SER HB3 H 1 3.888 0.001 . . . . . . 70 SER HB3 . 15013 1 812 . 1 1 70 70 SER C C 13 173.872 0.05 . . . . . . 70 SER C . 15013 1 813 . 1 1 70 70 SER CA C 13 58.165 0.012 . . . . . . 70 SER CA . 15013 1 814 . 1 1 70 70 SER CB C 13 63.753 0.005 . . . . . . 70 SER CB . 15013 1 815 . 1 1 70 70 SER N N 15 114.298 0.017 . . . . . . 70 SER N . 15013 1 816 . 1 1 71 71 TYR H H 1 6.883 0.007 . . . . . . 71 TYR H . 15013 1 817 . 1 1 71 71 TYR HA H 1 4.866 0.001 . . . . . . 71 TYR HA . 15013 1 818 . 1 1 71 71 TYR HB2 H 1 3.043 0.001 . . . . . . 71 TYR HB2 . 15013 1 819 . 1 1 71 71 TYR HB3 H 1 3.253 0.003 . . . . . . 71 TYR HB3 . 15013 1 820 . 1 1 71 71 TYR HD1 H 1 7.196 0.02 . . . . . . 71 TYR HD1 . 15013 1 821 . 1 1 71 71 TYR HD2 H 1 7.196 0.02 . . . . . . 71 TYR HD2 . 15013 1 822 . 1 1 71 71 TYR HE1 H 1 6.844 0.02 . . . . . . 71 TYR HE1 . 15013 1 823 . 1 1 71 71 TYR HE2 H 1 6.844 0.02 . . . . . . 71 TYR HE2 . 15013 1 824 . 1 1 71 71 TYR C C 13 174.887 0.05 . . . . . . 71 TYR C . 15013 1 825 . 1 1 71 71 TYR CA C 13 55.083 0.019 . . . . . . 71 TYR CA . 15013 1 826 . 1 1 71 71 TYR CB C 13 39.672 0.007 . . . . . . 71 TYR CB . 15013 1 827 . 1 1 71 71 TYR N N 15 118.415 0.014 . . . . . . 71 TYR N . 15013 1 828 . 1 1 72 72 SER H H 1 8.554 0.014 . . . . . . 72 SER H . 15013 1 829 . 1 1 72 72 SER HA H 1 4.719 0.02 . . . . . . 72 SER HA . 15013 1 830 . 1 1 72 72 SER HB2 H 1 3.817 0.02 . . . . . . 72 SER HB2 . 15013 1 831 . 1 1 72 72 SER HB3 H 1 3.941 0.02 . . . . . . 72 SER HB3 . 15013 1 832 . 1 1 72 72 SER CA C 13 57.367 0.05 . . . . . . 72 SER CA . 15013 1 833 . 1 1 72 72 SER CB C 13 62.951 0.05 . . . . . . 72 SER CB . 15013 1 834 . 1 1 72 72 SER N N 15 116.950 0.019 . . . . . . 72 SER N . 15013 1 835 . 1 1 73 73 PRO HA H 1 4.532 0.02 . . . . . . 73 PRO HA . 15013 1 836 . 1 1 73 73 PRO HB2 H 1 0.661 0.007 . . . . . . 73 PRO HB2 . 15013 1 837 . 1 1 73 73 PRO HB3 H 1 1.322 0.02 . . . . . . 73 PRO HB3 . 15013 1 838 . 1 1 73 73 PRO HG2 H 1 1.161 0.02 . . . . . . 73 PRO HG2 . 15013 1 839 . 1 1 73 73 PRO HG3 H 1 1.686 0.02 . . . . . . 73 PRO HG3 . 15013 1 840 . 1 1 73 73 PRO HD2 H 1 3.302 0.001 . . . . . . 73 PRO HD2 . 15013 1 841 . 1 1 73 73 PRO HD3 H 1 3.567 0.001 . . . . . . 73 PRO HD3 . 15013 1 842 . 1 1 73 73 PRO CA C 13 61.507 0.088 . . . . . . 73 PRO CA . 15013 1 843 . 1 1 73 73 PRO CB C 13 29.776 0.049 . . . . . . 73 PRO CB . 15013 1 844 . 1 1 73 73 PRO CG C 13 26.859 0.054 . . . . . . 73 PRO CG . 15013 1 845 . 1 1 73 73 PRO CD C 13 50.001 0.079 . . . . . . 73 PRO CD . 15013 1 846 . 1 1 74 74 PRO HA H 1 4.741 0.02 . . . . . . 74 PRO HA . 15013 1 847 . 1 1 74 74 PRO HB2 H 1 1.999 0.02 . . . . . . 74 PRO HB2 . 15013 1 848 . 1 1 74 74 PRO HB3 H 1 2.330 0.001 . . . . . . 74 PRO HB3 . 15013 1 849 . 1 1 74 74 PRO HG2 H 1 2.001 0.02 . . . . . . 74 PRO HG2 . 15013 1 850 . 1 1 74 74 PRO HG3 H 1 2.196 0.002 . . . . . . 74 PRO HG3 . 15013 1 851 . 1 1 74 74 PRO HD2 H 1 3.189 0.002 . . . . . . 74 PRO HD2 . 15013 1 852 . 1 1 74 74 PRO HD3 H 1 3.871 0.001 . . . . . . 74 PRO HD3 . 15013 1 853 . 1 1 74 74 PRO CA C 13 61.690 0.041 . . . . . . 74 PRO CA . 15013 1 854 . 1 1 74 74 PRO CB C 13 30.166 0.010 . . . . . . 74 PRO CB . 15013 1 855 . 1 1 74 74 PRO CG C 13 27.776 0.031 . . . . . . 74 PRO CG . 15013 1 856 . 1 1 74 74 PRO CD C 13 50.617 0.035 . . . . . . 74 PRO CD . 15013 1 857 . 1 1 75 75 PRO HA H 1 4.659 0.02 . . . . . . 75 PRO HA . 15013 1 858 . 1 1 75 75 PRO HB2 H 1 1.839 0.02 . . . . . . 75 PRO HB2 . 15013 1 859 . 1 1 75 75 PRO HB3 H 1 2.274 0.004 . . . . . . 75 PRO HB3 . 15013 1 860 . 1 1 75 75 PRO HG2 H 1 1.938 0.02 . . . . . . 75 PRO HG2 . 15013 1 861 . 1 1 75 75 PRO HG3 H 1 2.001 0.02 . . . . . . 75 PRO HG3 . 15013 1 862 . 1 1 75 75 PRO HD2 H 1 3.607 0.003 . . . . . . 75 PRO HD2 . 15013 1 863 . 1 1 75 75 PRO HD3 H 1 3.731 0.02 . . . . . . 75 PRO HD3 . 15013 1 864 . 1 1 75 75 PRO CA C 13 61.405 0.05 . . . . . . 75 PRO CA . 15013 1 865 . 1 1 75 75 PRO CB C 13 30.547 0.015 . . . . . . 75 PRO CB . 15013 1 866 . 1 1 75 75 PRO CD C 13 50.256 0.011 . . . . . . 75 PRO CD . 15013 1 867 . 1 1 76 76 PRO HA H 1 3.906 0.001 . . . . . . 76 PRO HA . 15013 1 868 . 1 1 76 76 PRO HB2 H 1 1.401 0.001 . . . . . . 76 PRO HB2 . 15013 1 869 . 1 1 76 76 PRO HB3 H 1 1.504 0.02 . . . . . . 76 PRO HB3 . 15013 1 870 . 1 1 76 76 PRO HG2 H 1 1.672 0.001 . . . . . . 76 PRO HG2 . 15013 1 871 . 1 1 76 76 PRO HG3 H 1 1.965 0.001 . . . . . . 76 PRO HG3 . 15013 1 872 . 1 1 76 76 PRO HD2 H 1 3.494 0.002 . . . . . . 76 PRO HD2 . 15013 1 873 . 1 1 76 76 PRO HD3 H 1 3.703 0.001 . . . . . . 76 PRO HD3 . 15013 1 874 . 1 1 76 76 PRO CA C 13 61.578 0.086 . . . . . . 76 PRO CA . 15013 1 875 . 1 1 76 76 PRO CB C 13 30.252 0.051 . . . . . . 76 PRO CB . 15013 1 876 . 1 1 76 76 PRO CG C 13 27.719 0.056 . . . . . . 76 PRO CG . 15013 1 877 . 1 1 76 76 PRO CD C 13 50.441 0.080 . . . . . . 76 PRO CD . 15013 1 878 . 1 1 77 77 PRO HA H 1 4.225 0.02 . . . . . . 77 PRO HA . 15013 1 879 . 1 1 77 77 PRO HB2 H 1 1.875 0.02 . . . . . . 77 PRO HB2 . 15013 1 880 . 1 1 77 77 PRO HB3 H 1 2.153 0.02 . . . . . . 77 PRO HB3 . 15013 1 881 . 1 1 77 77 PRO HG2 H 1 1.725 0.02 . . . . . . 77 PRO HG2 . 15013 1 882 . 1 1 77 77 PRO HG3 H 1 1.877 0.02 . . . . . . 77 PRO HG3 . 15013 1 883 . 1 1 77 77 PRO HD2 H 1 2.055 0.02 . . . . . . 77 PRO HD2 . 15013 1 884 . 1 1 77 77 PRO HD3 H 1 3.019 0.001 . . . . . . 77 PRO HD3 . 15013 1 885 . 1 1 77 77 PRO CB C 13 31.700 0.009 . . . . . . 77 PRO CB . 15013 1 886 . 1 1 77 77 PRO CG C 13 26.906 0.086 . . . . . . 77 PRO CG . 15013 1 887 . 1 1 77 77 PRO CD C 13 50.136 0.059 . . . . . . 77 PRO CD . 15013 1 stop_ save_