data_15094 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15094 _Entry.Title ; 1H, 13C, and 15N Chemical Shift Assignments for CutA1 from E. coli ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-01-04 _Entry.Accession_date 2007-01-04 _Entry.Last_release_date . _Entry.Original_release_date . _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 ; We applied a combined strategy of 1H and 13C detection experiments to assigne the trimeric protein CutA1 from E. coli. The CutA1 family of proteins is thought to bind divalent metal ions and are present in archaea, bacteria, plants, and animals. Their function is still unknown. In this work we demonstrate that the unique information available from 13C direct detection experiments makes it possible to assign the NMR resonances of this 37 KDa protein without the need of deuteration. ; _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 Ivano Bertini . . . 15094 2 Beatriz Jimenez . . . 15094 3 Roberta Pierattelli . . . 15094 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'CERM, University of Florence' . 15094 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 15094 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 383 15094 '15N chemical shifts' 119 15094 '1H chemical shifts' 228 15094 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2008-07-01 2007-01-04 update BMRB 'complete entry citation' 15094 1 . . 2007-10-17 2007-01-04 original author 'original release' 15094 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1NAQ . 15094 stop_ save_ ############### # Citations # ############### save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 15094 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17847095 _Citation.Full_citation . _Citation.Title 'Protonless (13)C direct detection NMR: characterization of the 37 kiloDalton trimeric protein CutA1' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Proteins _Citation.Journal_name_full . _Citation.Journal_volume 70 _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 1196 _Citation.Page_last 1205 _Citation.Year 2008 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ivano Bertini . . . 15094 1 2 Beatriz Jimenez . . . 15094 1 3 Roberta Pierattelli . . . 15094 1 4 Anthony Wedd . G. . 15094 1 5 Zhiguang Xiao . . . 15094 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID '13C direct Detection' 15094 1 CutA1 15094 1 NMR 15094 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15094 _Assembly.ID 1 _Assembly.Name homo-trimer _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'CutA1, chain 1' 1 $CutA1 A . yes native no no . . . 15094 1 2 'CutA1, chain 2' 1 $CutA1 A . yes native no no . . . 15094 1 3 'CutA1, chain 3' 1 $CutA1 A . yes native no no . . . 15094 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 1NAQ . . . . . . 15094 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CutA1 _Entity.Sf_category entity _Entity.Sf_framecode CutA1 _Entity.Entry_ID 15094 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CutA1 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MLDEKSSNTASVVVLCTAPD EATAQDLAAKVLAEKLAACA TLIPGATSLYYWEGKLEQEY EVQMILKTTVSHQQALLECL KSHHPYQTPELLVLPVTHGD TDYLSWLNASLR ; _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 112 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _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 PDB 1NAQ . "Crystal Structure Of Cuta1 From E.Coli At 1.7 A Resolution" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 2 no PDB 3AA8 . "Crystal Structure Analysis Of The Mutant Cuta1 (S11vE61V) FROM E. Coli" . . . . . 100.00 112 98.21 98.21 8.82e-72 . . . . 15094 1 3 no PDB 3AA9 . "Crystal Structure Analysis Of The Mutant Cuta1 (E61v) From E. Coli" . . . . . 100.00 112 99.11 99.11 9.95e-73 . . . . 15094 1 4 no PDB 3AH6 . "Remarkable Improvement Of The Heat Stability Of Cuta1 From E.Coli By Rational Protein Designing" . . . . . 100.00 112 99.11 99.11 6.29e-73 . . . . 15094 1 5 no PDB 3X3U . "Crystal Structure Of Wild-type Of E. Coli Cuta1" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 6 no PDB 4Y65 . "Crystal Structure Of E.coli Cuta1 C16a/c39a/c79a Mutation" . . . . . 100.00 112 97.32 97.32 6.02e-71 . . . . 15094 1 7 no DBJ BAB38541 . "divalent cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 8 no DBJ BAE78139 . "copper binding protein, copper sensitivity [Escherichia coli str. K12 substr. W3110]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 9 no DBJ BAG66863 . "copper binding protein, copper sensitivity [Escherichia coli O111:H-]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 10 no DBJ BAG79960 . "divalent cation tolerance protein [Escherichia coli SE11]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 11 no DBJ BAI28441 . "copper binding protein CutA, copper sensitivity [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 112 99.11 100.00 4.44e-73 . . . . 15094 1 12 no EMBL CAA54780 . "orf112 [Escherichia coli K-12]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 13 no EMBL CAA85374 . "periplasmic divalent cation tolerance protein [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 14 no EMBL CAP78655 . "Divalent-cation tolerance protein cutA [Escherichia coli LF82]" . . . . . 100.00 112 99.11 99.11 3.68e-73 . . . . 15094 1 15 no EMBL CAQ34486 . "copper binding protein CutA [Escherichia coli BL21(DE3)]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 16 no EMBL CAR01113 . "copper binding protein, copper sensitivity [Escherichia coli IAI1]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 17 no GB AAA97036 . "cycY [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 18 no GB AAC77097 . "divalent-cation tolerance protein, copper sensitivity [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 19 no GB AAG59336 . "divalent cation tolerance protein; cytochrome c biogenesis [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 20 no GB AAN45709 . "divalent cation tolerance protein [Shigella flexneri 2a str. 301]" . . . . . 100.00 112 99.11 99.11 3.68e-73 . . . . 15094 1 21 no GB AAN83641 . "Periplasmic divalent cation tolerance protein cutA [Escherichia coli CFT073]" . . . . . 100.00 114 99.11 99.11 2.54e-73 . . . . 15094 1 22 no REF NP_313145 . "divalent-cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 23 no REF NP_418560 . "divalent-cation tolerance protein, copper sensitivity [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 24 no REF NP_710002 . "divalent-cation tolerance protein CutA [Shigella flexneri 2a str. 301]" . . . . . 100.00 112 99.11 99.11 3.68e-73 . . . . 15094 1 25 no REF WP_000883338 . "divalent ion tolerance protein CutA [Escherichia coli]" . . . . . 100.00 112 99.11 100.00 4.44e-73 . . . . 15094 1 26 no REF WP_000883339 . "divalent ion tolerance protein CutA [Escherichia coli]" . . . . . 100.00 112 98.21 99.11 7.82e-72 . . . . 15094 1 27 no SP A7ZV06 . "RecName: Full=Divalent-cation tolerance protein CutA" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 28 no SP A8A7N3 . "RecName: Full=Divalent-cation tolerance protein CutA" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 29 no SP B1ITR1 . "RecName: Full=Divalent-cation tolerance protein CutA" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 30 no SP B1LQF8 . "RecName: Full=Divalent-cation tolerance protein CutA" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 31 no SP B1XD17 . "RecName: Full=Divalent-cation tolerance protein CutA" . . . . . 100.00 112 100.00 100.00 8.73e-74 . . . . 15094 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . MET . 15094 1 2 . LEU . 15094 1 3 . ASP . 15094 1 4 . GLU . 15094 1 5 . LYS . 15094 1 6 . SER . 15094 1 7 . SER . 15094 1 8 . ASN . 15094 1 9 . THR . 15094 1 10 . ALA . 15094 1 11 . SER . 15094 1 12 . VAL . 15094 1 13 . VAL . 15094 1 14 . VAL . 15094 1 15 . LEU . 15094 1 16 . CYS . 15094 1 17 . THR . 15094 1 18 . ALA . 15094 1 19 . PRO . 15094 1 20 . ASP . 15094 1 21 . GLU . 15094 1 22 . ALA . 15094 1 23 . THR . 15094 1 24 . ALA . 15094 1 25 . GLN . 15094 1 26 . ASP . 15094 1 27 . LEU . 15094 1 28 . ALA . 15094 1 29 . ALA . 15094 1 30 . LYS . 15094 1 31 . VAL . 15094 1 32 . LEU . 15094 1 33 . ALA . 15094 1 34 . GLU . 15094 1 35 . LYS . 15094 1 36 . LEU . 15094 1 37 . ALA . 15094 1 38 . ALA . 15094 1 39 . CYS . 15094 1 40 . ALA . 15094 1 41 . THR . 15094 1 42 . LEU . 15094 1 43 . ILE . 15094 1 44 . PRO . 15094 1 45 . GLY . 15094 1 46 . ALA . 15094 1 47 . THR . 15094 1 48 . SER . 15094 1 49 . LEU . 15094 1 50 . TYR . 15094 1 51 . TYR . 15094 1 52 . TRP . 15094 1 53 . GLU . 15094 1 54 . GLY . 15094 1 55 . LYS . 15094 1 56 . LEU . 15094 1 57 . GLU . 15094 1 58 . GLN . 15094 1 59 . GLU . 15094 1 60 . TYR . 15094 1 61 . GLU . 15094 1 62 . VAL . 15094 1 63 . GLN . 15094 1 64 . MET . 15094 1 65 . ILE . 15094 1 66 . LEU . 15094 1 67 . LYS . 15094 1 68 . THR . 15094 1 69 . THR . 15094 1 70 . VAL . 15094 1 71 . SER . 15094 1 72 . HIS . 15094 1 73 . GLN . 15094 1 74 . GLN . 15094 1 75 . ALA . 15094 1 76 . LEU . 15094 1 77 . LEU . 15094 1 78 . GLU . 15094 1 79 . CYS . 15094 1 80 . LEU . 15094 1 81 . LYS . 15094 1 82 . SER . 15094 1 83 . HIS . 15094 1 84 . HIS . 15094 1 85 . PRO . 15094 1 86 . TYR . 15094 1 87 . GLN . 15094 1 88 . THR . 15094 1 89 . PRO . 15094 1 90 . GLU . 15094 1 91 . LEU . 15094 1 92 . LEU . 15094 1 93 . VAL . 15094 1 94 . LEU . 15094 1 95 . PRO . 15094 1 96 . VAL . 15094 1 97 . THR . 15094 1 98 . HIS . 15094 1 99 . GLY . 15094 1 100 . ASP . 15094 1 101 . THR . 15094 1 102 . ASP . 15094 1 103 . TYR . 15094 1 104 . LEU . 15094 1 105 . SER . 15094 1 106 . TRP . 15094 1 107 . LEU . 15094 1 108 . ASN . 15094 1 109 . ALA . 15094 1 110 . SER . 15094 1 111 . LEU . 15094 1 112 . ARG . 15094 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . MET 1 1 15094 1 . LEU 2 2 15094 1 . ASP 3 3 15094 1 . GLU 4 4 15094 1 . LYS 5 5 15094 1 . SER 6 6 15094 1 . SER 7 7 15094 1 . ASN 8 8 15094 1 . THR 9 9 15094 1 . ALA 10 10 15094 1 . SER 11 11 15094 1 . VAL 12 12 15094 1 . VAL 13 13 15094 1 . VAL 14 14 15094 1 . LEU 15 15 15094 1 . CYS 16 16 15094 1 . THR 17 17 15094 1 . ALA 18 18 15094 1 . PRO 19 19 15094 1 . ASP 20 20 15094 1 . GLU 21 21 15094 1 . ALA 22 22 15094 1 . THR 23 23 15094 1 . ALA 24 24 15094 1 . GLN 25 25 15094 1 . ASP 26 26 15094 1 . LEU 27 27 15094 1 . ALA 28 28 15094 1 . ALA 29 29 15094 1 . LYS 30 30 15094 1 . VAL 31 31 15094 1 . LEU 32 32 15094 1 . ALA 33 33 15094 1 . GLU 34 34 15094 1 . LYS 35 35 15094 1 . LEU 36 36 15094 1 . ALA 37 37 15094 1 . ALA 38 38 15094 1 . CYS 39 39 15094 1 . ALA 40 40 15094 1 . THR 41 41 15094 1 . LEU 42 42 15094 1 . ILE 43 43 15094 1 . PRO 44 44 15094 1 . GLY 45 45 15094 1 . ALA 46 46 15094 1 . THR 47 47 15094 1 . SER 48 48 15094 1 . LEU 49 49 15094 1 . TYR 50 50 15094 1 . TYR 51 51 15094 1 . TRP 52 52 15094 1 . GLU 53 53 15094 1 . GLY 54 54 15094 1 . LYS 55 55 15094 1 . LEU 56 56 15094 1 . GLU 57 57 15094 1 . GLN 58 58 15094 1 . GLU 59 59 15094 1 . TYR 60 60 15094 1 . GLU 61 61 15094 1 . VAL 62 62 15094 1 . GLN 63 63 15094 1 . MET 64 64 15094 1 . ILE 65 65 15094 1 . LEU 66 66 15094 1 . LYS 67 67 15094 1 . THR 68 68 15094 1 . THR 69 69 15094 1 . VAL 70 70 15094 1 . SER 71 71 15094 1 . HIS 72 72 15094 1 . GLN 73 73 15094 1 . GLN 74 74 15094 1 . ALA 75 75 15094 1 . LEU 76 76 15094 1 . LEU 77 77 15094 1 . GLU 78 78 15094 1 . CYS 79 79 15094 1 . LEU 80 80 15094 1 . LYS 81 81 15094 1 . SER 82 82 15094 1 . HIS 83 83 15094 1 . HIS 84 84 15094 1 . PRO 85 85 15094 1 . TYR 86 86 15094 1 . GLN 87 87 15094 1 . THR 88 88 15094 1 . PRO 89 89 15094 1 . GLU 90 90 15094 1 . LEU 91 91 15094 1 . LEU 92 92 15094 1 . VAL 93 93 15094 1 . LEU 94 94 15094 1 . PRO 95 95 15094 1 . VAL 96 96 15094 1 . THR 97 97 15094 1 . HIS 98 98 15094 1 . GLY 99 99 15094 1 . ASP 100 100 15094 1 . THR 101 101 15094 1 . ASP 102 102 15094 1 . TYR 103 103 15094 1 . LEU 104 104 15094 1 . SER 105 105 15094 1 . TRP 106 106 15094 1 . LEU 107 107 15094 1 . ASN 108 108 15094 1 . ALA 109 109 15094 1 . SER 110 110 15094 1 . LEU 111 111 15094 1 . ARG 112 112 15094 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 15094 _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 $CutA1 . 562 organism . 'Escherichia coli' 'E. coli' . . Bacteria . Escherichia coli DH5a . . . . . . . . . . . . . . . . . . . . 15094 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 15094 _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 $CutA1 . 'recombinant technology' 'Escherichia coli' . . . . . BL21(DE3) . . . . . . . . . . . . . . . pET11a . . . . . . 15094 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15094 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number 2 _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 CutA1 '[U-83% 13C; U-98% 15N]' . . 1 $CutA1 . . 3.5 . . mM . . . . 15094 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 15094 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number 2 _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 CutA1 '[U-98% 15N]' . . 1 $CutA1 . . 3.5 . . mM . . . . 15094 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 15094 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.04 0.0001 M 15094 1 pH 6.5 0.01 pH 15094 1 pressure 1 . atm 15094 1 temperature 298 0.1 K 15094 1 stop_ save_ ############################ # Computer software used # ############################ save_CARA _Software.Sf_category software _Software.Sf_framecode CARA _Software.Entry_ID 15094 _Software.ID 1 _Software.Name CARA _Software.Version 1.5 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Keller and Wuthrich' . . 15094 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 15094 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 15094 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'Cryo-probe TCI' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 15094 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details 'Probe TXI' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 15094 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details 'Probe TXI' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_4 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_4 _NMR_spectrometer.Entry_ID 15094 _NMR_spectrometer.ID 4 _NMR_spectrometer.Details 'Probe TXO' _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_5 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_5 _NMR_spectrometer.Entry_ID 15094 _NMR_spectrometer.ID 5 _NMR_spectrometer.Details 'Cryo-Probe TXI' _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 15094 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 500 'Cryo-probe TCI' . . 15094 1 2 spectrometer_2 Bruker Avance . 600 'Probe TXI' . . 15094 1 3 spectrometer_3 Bruker Avance . 700 'Probe TXI' . . 15094 1 4 spectrometer_4 Bruker Avance . 700 'Probe TXO' . . 15094 1 5 spectrometer_5 Bruker Avance . 800 'Cryo-Probe TXI' . . 15094 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 15094 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 5 $spectrometer_5 . . . . . . . . . . . . . . . . 15094 1 2 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 5 $spectrometer_5 . . . . . . . . . . . . . . . . 15094 1 3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 15094 1 4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 15094 1 5 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 3 $spectrometer_3 . . . . . . . . . . . . . . . . 15094 1 6 '2D 1H-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 5 $spectrometer_5 . . . . . . . . . . . . . . . . 15094 1 7 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 5 $spectrometer_5 . . . . . . . . . . . . . . . . 15094 1 8 '2D CACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 4 $spectrometer_4 . . . . . . . . . . . . . . . . 15094 1 9 '2D CON' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 4 $spectrometer_4 . . . . . . . . . . . . . . . . 15094 1 10 '2D CBCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 4 $spectrometer_4 . . . . . . . . . . . . . . . . 15094 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 15094 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.251449530 . . . 1 $citation_1 . . 1 $citation_1 15094 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . 1 $citation_1 . . 1 $citation_1 15094 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . 1 $citation_1 . . 1 $citation_1 15094 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 15094 _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 0.07 _Assigned_chem_shift_list.Chem_shift_13C_err 0.16 _Assigned_chem_shift_list.Chem_shift_15N_err 0.39 _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 5 '3D CBCA(CO)NH' . . . 15094 1 8 '2D CACO' . . . 15094 1 9 '2D CON' . . . 15094 1 10 '2D CBCACO' . . . 15094 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 $CARA . . 15094 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 MET HA H 1 4.01 0.07 . 1 . . . . 1 MET HA . 15094 1 2 . 1 1 1 1 MET C C 13 173.17 0.16 . 1 . . . . 1 MET C . 15094 1 3 . 1 1 1 1 MET CA C 13 55.08 0.11 . 1 . . . . 1 MET CA . 15094 1 4 . 1 1 1 1 MET CB C 13 33.37 0.17 . 1 . . . . 1 MET CB . 15094 1 5 . 1 1 1 1 MET CG C 13 31.03 0.17 . 1 . . . . 1 MET CG . 15094 1 6 . 1 1 2 2 LEU HA H 1 4.32 0.07 . 1 . . . . 2 LEU HA . 15094 1 7 . 1 1 2 2 LEU C C 13 176.54 0.16 . 1 . . . . 2 LEU C . 15094 1 8 . 1 1 2 2 LEU CA C 13 55.29 0.11 . 1 . . . . 2 LEU CA . 15094 1 9 . 1 1 2 2 LEU CB C 13 42.21 0.17 . 1 . . . . 2 LEU CB . 15094 1 10 . 1 1 2 2 LEU CG C 13 26.93 0.17 . 1 . . . . 2 LEU CG . 15094 1 11 . 1 1 2 2 LEU CD1 C 13 24.71 0.17 . 2 . . . . 2 LEU CD1 . 15094 1 12 . 1 1 2 2 LEU CD2 C 13 23.65 0.17 . 2 . . . . 2 LEU CD2 . 15094 1 13 . 1 1 2 2 LEU N N 15 125.46 0.39 . 1 . . . . 2 LEU N . 15094 1 14 . 1 1 3 3 ASP H H 1 8.44 0.07 . 1 . . . . 3 ASP H . 15094 1 15 . 1 1 3 3 ASP HA H 1 4.57 0.07 . 1 . . . . 3 ASP HA . 15094 1 16 . 1 1 3 3 ASP HB2 H 1 2.69 0.07 . 2 . . . . 3 ASP HB2 . 15094 1 17 . 1 1 3 3 ASP HB3 H 1 2.53 0.07 . 2 . . . . 3 ASP HB3 . 15094 1 18 . 1 1 3 3 ASP C C 13 176.31 0.16 . 1 . . . . 3 ASP C . 15094 1 19 . 1 1 3 3 ASP CA C 13 53.97 0.11 . 1 . . . . 3 ASP CA . 15094 1 20 . 1 1 3 3 ASP CB C 13 41.19 0.17 . 1 . . . . 3 ASP CB . 15094 1 21 . 1 1 3 3 ASP CG C 13 180.35 0.16 . 1 . . . . 3 ASP CG . 15094 1 22 . 1 1 3 3 ASP N N 15 122.85 0.39 . 1 . . . . 3 ASP N . 15094 1 23 . 1 1 4 4 GLU H H 1 8.5 0.07 . 1 . . . . 4 GLU H . 15094 1 24 . 1 1 4 4 GLU HA H 1 4.2 0.07 . 1 . . . . 4 GLU HA . 15094 1 25 . 1 1 4 4 GLU HB2 H 1 2.24 0.07 . 2 . . . . 4 GLU HB2 . 15094 1 26 . 1 1 4 4 GLU HB3 H 1 2.02 0.07 . 2 . . . . 4 GLU HB3 . 15094 1 27 . 1 1 4 4 GLU C C 13 176.95 0.16 . 1 . . . . 4 GLU C . 15094 1 28 . 1 1 4 4 GLU CA C 13 57.01 0.11 . 1 . . . . 4 GLU CA . 15094 1 29 . 1 1 4 4 GLU CB C 13 30.17 0.17 . 1 . . . . 4 GLU CB . 15094 1 30 . 1 1 4 4 GLU CG C 13 36.35 0.17 . 1 . . . . 4 GLU CG . 15094 1 31 . 1 1 4 4 GLU CD C 13 183.98 0.16 . 1 . . . . 4 GLU CD . 15094 1 32 . 1 1 4 4 GLU N N 15 123.08 0.39 . 1 . . . . 4 GLU N . 15094 1 33 . 1 1 5 5 LYS H H 1 8.39 0.07 . 1 . . . . 5 LYS H . 15094 1 34 . 1 1 5 5 LYS HA H 1 4.28 0.07 . 1 . . . . 5 LYS HA . 15094 1 35 . 1 1 5 5 LYS HB2 H 1 1.82 0.07 . 2 . . . . 5 LYS HB2 . 15094 1 36 . 1 1 5 5 LYS HB3 H 1 1.78 0.07 . 2 . . . . 5 LYS HB3 . 15094 1 37 . 1 1 5 5 LYS HG2 H 1 1.41 0.07 . 2 . . . . 5 LYS HG2 . 15094 1 38 . 1 1 5 5 LYS C C 13 177.12 0.16 . 1 . . . . 5 LYS C . 15094 1 39 . 1 1 5 5 LYS CA C 13 56.48 0.11 . 1 . . . . 5 LYS CA . 15094 1 40 . 1 1 5 5 LYS CB C 13 32.55 0.17 . 1 . . . . 5 LYS CB . 15094 1 41 . 1 1 5 5 LYS CG C 13 24.76 0.17 . 1 . . . . 5 LYS CG . 15094 1 42 . 1 1 5 5 LYS CD C 13 29.08 0.17 . 1 . . . . 5 LYS CD . 15094 1 43 . 1 1 5 5 LYS CE C 13 41.98 0.17 . 1 . . . . 5 LYS CE . 15094 1 44 . 1 1 5 5 LYS N N 15 122.21 0.39 . 1 . . . . 5 LYS N . 15094 1 45 . 1 1 6 6 SER H H 1 8.2 0.07 . 1 . . . . 6 SER H . 15094 1 46 . 1 1 6 6 SER HA H 1 4.42 0.07 . 1 . . . . 6 SER HA . 15094 1 47 . 1 1 6 6 SER HB2 H 1 3.87 0.07 . 2 . . . . 6 SER HB2 . 15094 1 48 . 1 1 6 6 SER HB3 H 1 4.42 0.07 . 2 . . . . 6 SER HB3 . 15094 1 49 . 1 1 6 6 SER C C 13 174.8 0.16 . 1 . . . . 6 SER C . 15094 1 50 . 1 1 6 6 SER CA C 13 58.49 0.11 . 1 . . . . 6 SER CA . 15094 1 51 . 1 1 6 6 SER CB C 13 63.83 0.17 . 1 . . . . 6 SER CB . 15094 1 52 . 1 1 6 6 SER N N 15 117.03 0.39 . 1 . . . . 6 SER N . 15094 1 53 . 1 1 7 7 SER H H 1 8.29 0.07 . 1 . . . . 7 SER H . 15094 1 54 . 1 1 7 7 SER HA H 1 4.44 0.07 . 1 . . . . 7 SER HA . 15094 1 55 . 1 1 7 7 SER HB2 H 1 3.84 0.07 . 2 . . . . 7 SER HB2 . 15094 1 56 . 1 1 7 7 SER HB3 H 1 4.12 0.07 . 2 . . . . 7 SER HB3 . 15094 1 57 . 1 1 7 7 SER C C 13 174.44 0.16 . 1 . . . . 7 SER C . 15094 1 58 . 1 1 7 7 SER CA C 13 58.43 0.11 . 1 . . . . 7 SER CA . 15094 1 59 . 1 1 7 7 SER CB C 13 63.77 0.17 . 1 . . . . 7 SER CB . 15094 1 60 . 1 1 7 7 SER N N 15 118.34 0.39 . 1 . . . . 7 SER N . 15094 1 61 . 1 1 8 8 ASN H H 1 8.36 0.07 . 1 . . . . 8 ASN H . 15094 1 62 . 1 1 8 8 ASN HA H 1 4.61 0.07 . 1 . . . . 8 ASN HA . 15094 1 63 . 1 1 8 8 ASN HB2 H 1 2.64 0.07 . 2 . . . . 8 ASN HB2 . 15094 1 64 . 1 1 8 8 ASN HD21 H 1 6.91 0.07 . 2 . . . . 8 ASN HD21 . 15094 1 65 . 1 1 8 8 ASN HD22 H 1 7.59 0.07 . 2 . . . . 8 ASN HD22 . 15094 1 66 . 1 1 8 8 ASN C C 13 175.51 0.16 . 1 . . . . 8 ASN C . 15094 1 67 . 1 1 8 8 ASN CA C 13 53.47 0.11 . 1 . . . . 8 ASN CA . 15094 1 68 . 1 1 8 8 ASN CB C 13 39.12 0.17 . 1 . . . . 8 ASN CB . 15094 1 69 . 1 1 8 8 ASN CG C 13 176.58 0.16 . 1 . . . . 8 ASN CG . 15094 1 70 . 1 1 8 8 ASN N N 15 121.58 0.39 . 1 . . . . 8 ASN N . 15094 1 71 . 1 1 8 8 ASN ND2 N 15 112.98 0.39 . 1 . . . . 8 ASN ND2 . 15094 1 72 . 1 1 9 9 THR H H 1 8.12 0.07 . 1 . . . . 9 THR H . 15094 1 73 . 1 1 9 9 THR HA H 1 4.26 0.07 . 1 . . . . 9 THR HA . 15094 1 74 . 1 1 9 9 THR HB H 1 4.32 0.07 . 1 . . . . 9 THR HB . 15094 1 75 . 1 1 9 9 THR HG21 H 1 1.12 0.07 . 1 . . . . 9 THR HG2 . 15094 1 76 . 1 1 9 9 THR HG22 H 1 1.12 0.07 . 1 . . . . 9 THR HG2 . 15094 1 77 . 1 1 9 9 THR HG23 H 1 1.12 0.07 . 1 . . . . 9 THR HG2 . 15094 1 78 . 1 1 9 9 THR C C 13 174.05 0.16 . 1 . . . . 9 THR C . 15094 1 79 . 1 1 9 9 THR CA C 13 61.54 0.11 . 1 . . . . 9 THR CA . 15094 1 80 . 1 1 9 9 THR CB C 13 69.91 0.17 . 1 . . . . 9 THR CB . 15094 1 81 . 1 1 9 9 THR CG2 C 13 21.65 0.17 . 1 . . . . 9 THR CG2 . 15094 1 82 . 1 1 9 9 THR N N 15 113.95 0.39 . 1 . . . . 9 THR N . 15094 1 83 . 1 1 10 10 ALA H H 1 8.14 0.07 . 1 . . . . 10 ALA H . 15094 1 84 . 1 1 10 10 ALA HA H 1 4.31 0.07 . 1 . . . . 10 ALA HA . 15094 1 85 . 1 1 10 10 ALA C C 13 176.79 0.16 . 1 . . . . 10 ALA C . 15094 1 86 . 1 1 10 10 ALA CA C 13 52.74 0.11 . 1 . . . . 10 ALA CA . 15094 1 87 . 1 1 10 10 ALA CB C 13 19.05 0.17 . 1 . . . . 10 ALA CB . 15094 1 88 . 1 1 10 10 ALA N N 15 126.49 0.39 . 1 . . . . 10 ALA N . 15094 1 89 . 1 1 11 11 SER H H 1 8.87 0.07 . 1 . . . . 11 SER H . 15094 1 90 . 1 1 11 11 SER HB2 H 1 3.68 0.07 . 2 . . . . 11 SER HB2 . 15094 1 91 . 1 1 11 11 SER HB3 H 1 3.72 0.07 . 2 . . . . 11 SER HB3 . 15094 1 92 . 1 1 11 11 SER C C 13 173 0.16 . 1 . . . . 11 SER C . 15094 1 93 . 1 1 11 11 SER CA C 13 58.76 0.11 . 1 . . . . 11 SER CA . 15094 1 94 . 1 1 11 11 SER CB C 13 65.43 0.17 . 1 . . . . 11 SER CB . 15094 1 95 . 1 1 11 11 SER N N 15 117.94 0.39 . 1 . . . . 11 SER N . 15094 1 96 . 1 1 12 12 VAL H H 1 8.42 0.07 . 1 . . . . 12 VAL H . 15094 1 97 . 1 1 12 12 VAL C C 13 174.56 0.16 . 1 . . . . 12 VAL C . 15094 1 98 . 1 1 12 12 VAL CA C 13 59.77 0.11 . 1 . . . . 12 VAL CA . 15094 1 99 . 1 1 12 12 VAL CB C 13 36.09 0.17 . 1 . . . . 12 VAL CB . 15094 1 100 . 1 1 12 12 VAL N N 15 113.97 0.39 . 1 . . . . 12 VAL N . 15094 1 101 . 1 1 13 13 VAL H H 1 8.77 0.07 . 1 . . . . 13 VAL H . 15094 1 102 . 1 1 13 13 VAL C C 13 174.12 0.16 . 1 . . . . 13 VAL C . 15094 1 103 . 1 1 13 13 VAL CA C 13 59.98 0.11 . 1 . . . . 13 VAL CA . 15094 1 104 . 1 1 13 13 VAL CB C 13 34.67 0.17 . 1 . . . . 13 VAL CB . 15094 1 105 . 1 1 13 13 VAL N N 15 118.01 0.39 . 1 . . . . 13 VAL N . 15094 1 106 . 1 1 14 14 VAL H H 1 9.24 0.07 . 1 . . . . 14 VAL H . 15094 1 107 . 1 1 14 14 VAL C C 13 175.24 0.16 . 1 . . . . 14 VAL C . 15094 1 108 . 1 1 14 14 VAL CA C 13 59.83 0.11 . 1 . . . . 14 VAL CA . 15094 1 109 . 1 1 14 14 VAL CB C 13 34.52 0.17 . 1 . . . . 14 VAL CB . 15094 1 110 . 1 1 14 14 VAL N N 15 125.38 0.39 . 1 . . . . 14 VAL N . 15094 1 111 . 1 1 15 15 LEU H H 1 9.16 0.07 . 1 . . . . 15 LEU H . 15094 1 112 . 1 1 15 15 LEU HA H 1 4.87 0.07 . 1 . . . . 15 LEU HA . 15094 1 113 . 1 1 15 15 LEU C C 13 175.04 0.16 . 1 . . . . 15 LEU C . 15094 1 114 . 1 1 15 15 LEU CA C 13 53.3 0.11 . 1 . . . . 15 LEU CA . 15094 1 115 . 1 1 15 15 LEU CB C 13 43.19 0.17 . 1 . . . . 15 LEU CB . 15094 1 116 . 1 1 15 15 LEU N N 15 128 0.39 . 1 . . . . 15 LEU N . 15094 1 117 . 1 1 16 16 CYS H H 1 7.74 0.07 . 1 . . . . 16 CYS H . 15094 1 118 . 1 1 16 16 CYS C C 13 172.93 0.16 . 1 . . . . 16 CYS C . 15094 1 119 . 1 1 16 16 CYS CA C 13 56.34 0.11 . 1 . . . . 16 CYS CA . 15094 1 120 . 1 1 16 16 CYS CB C 13 30.14 0.17 . 1 . . . . 16 CYS CB . 15094 1 121 . 1 1 16 16 CYS N N 15 120.36 0.39 . 1 . . . . 16 CYS N . 15094 1 122 . 1 1 17 17 THR H H 1 7.55 0.07 . 1 . . . . 17 THR H . 15094 1 123 . 1 1 17 17 THR HB H 1 3.95 0.07 . 1 . . . . 17 THR HB . 15094 1 124 . 1 1 17 17 THR C C 13 173.12 0.16 . 1 . . . . 17 THR C . 15094 1 125 . 1 1 17 17 THR CA C 13 59.64 0.11 . 1 . . . . 17 THR CA . 15094 1 126 . 1 1 17 17 THR CB C 13 71.92 0.17 . 1 . . . . 17 THR CB . 15094 1 127 . 1 1 17 17 THR N N 15 117.26 0.39 . 1 . . . . 17 THR N . 15094 1 128 . 1 1 18 18 ALA H H 1 8.61 0.07 . 1 . . . . 18 ALA H . 15094 1 129 . 1 1 18 18 ALA C C 13 175.14 0.16 . 1 . . . . 18 ALA C . 15094 1 130 . 1 1 18 18 ALA CA C 13 48.57 0.11 . 1 . . . . 18 ALA CA . 15094 1 131 . 1 1 18 18 ALA CB C 13 21.75 0.17 . 1 . . . . 18 ALA CB . 15094 1 132 . 1 1 18 18 ALA N N 15 122.93 0.39 . 1 . . . . 18 ALA N . 15094 1 133 . 1 1 19 19 PRO C C 13 174.96 0.16 . 1 . . . . 19 PRO C . 15094 1 134 . 1 1 19 19 PRO CA C 13 64.35 0.11 . 1 . . . . 19 PRO CA . 15094 1 135 . 1 1 19 19 PRO CB C 13 32.26 0.17 . 1 . . . . 19 PRO CB . 15094 1 136 . 1 1 19 19 PRO N N 15 129.89 0.39 . 1 . . . . 19 PRO N . 15094 1 137 . 1 1 20 20 ASP H H 1 6.91 0.07 . 1 . . . . 20 ASP H . 15094 1 138 . 1 1 20 20 ASP HA H 1 4.56 0.07 . 1 . . . . 20 ASP HA . 15094 1 139 . 1 1 20 20 ASP C C 13 175.5 0.16 . 1 . . . . 20 ASP C . 15094 1 140 . 1 1 20 20 ASP CA C 13 52.37 0.11 . 1 . . . . 20 ASP CA . 15094 1 141 . 1 1 20 20 ASP CB C 13 41.98 0.17 . 1 . . . . 20 ASP CB . 15094 1 142 . 1 1 20 20 ASP CG C 13 179.62 0.16 . 1 . . . . 20 ASP CG . 15094 1 143 . 1 1 20 20 ASP N N 15 109.66 0.39 . 1 . . . . 20 ASP N . 15094 1 144 . 1 1 21 21 GLU H H 1 9.28 0.07 . 1 . . . . 21 GLU H . 15094 1 145 . 1 1 21 21 GLU C C 13 177.58 0.16 . 1 . . . . 21 GLU C . 15094 1 146 . 1 1 21 21 GLU CA C 13 61.06 0.11 . 1 . . . . 21 GLU CA . 15094 1 147 . 1 1 21 21 GLU CB C 13 29.92 0.17 . 1 . . . . 21 GLU CB . 15094 1 148 . 1 1 21 21 GLU CG C 13 38.34 0.17 . 1 . . . . 21 GLU CG . 15094 1 149 . 1 1 21 21 GLU CD C 13 182.97 0.16 . 1 . . . . 21 GLU CD . 15094 1 150 . 1 1 21 21 GLU N N 15 121.72 0.39 . 1 . . . . 21 GLU N . 15094 1 151 . 1 1 22 22 ALA H H 1 8.48 0.07 . 1 . . . . 22 ALA H . 15094 1 152 . 1 1 22 22 ALA HB1 H 1 0.66 0.07 . 1 . . . . 22 ALA HB . 15094 1 153 . 1 1 22 22 ALA HB2 H 1 0.66 0.07 . 1 . . . . 22 ALA HB . 15094 1 154 . 1 1 22 22 ALA HB3 H 1 0.66 0.07 . 1 . . . . 22 ALA HB . 15094 1 155 . 1 1 22 22 ALA C C 13 180.92 0.16 . 1 . . . . 22 ALA C . 15094 1 156 . 1 1 22 22 ALA CA C 13 55.33 0.11 . 1 . . . . 22 ALA CA . 15094 1 157 . 1 1 22 22 ALA CB C 13 17.67 0.17 . 1 . . . . 22 ALA CB . 15094 1 158 . 1 1 22 22 ALA N N 15 123.81 0.39 . 1 . . . . 22 ALA N . 15094 1 159 . 1 1 23 23 THR H H 1 8.74 0.07 . 1 . . . . 23 THR H . 15094 1 160 . 1 1 23 23 THR HA H 1 3.82 0.07 . 1 . . . . 23 THR HA . 15094 1 161 . 1 1 23 23 THR HB H 1 3.73 0.07 . 1 . . . . 23 THR HB . 15094 1 162 . 1 1 23 23 THR C C 13 176.21 0.16 . 1 . . . . 23 THR C . 15094 1 163 . 1 1 23 23 THR CA C 13 66.43 0.11 . 1 . . . . 23 THR CA . 15094 1 164 . 1 1 23 23 THR CB C 13 67.77 0.17 . 1 . . . . 23 THR CB . 15094 1 165 . 1 1 23 23 THR N N 15 116.68 0.39 . 1 . . . . 23 THR N . 15094 1 166 . 1 1 24 24 ALA H H 1 8.02 0.07 . 1 . . . . 24 ALA H . 15094 1 167 . 1 1 24 24 ALA HA H 1 3.79 0.07 . 1 . . . . 24 ALA HA . 15094 1 168 . 1 1 24 24 ALA C C 13 178.61 0.16 . 1 . . . . 24 ALA C . 15094 1 169 . 1 1 24 24 ALA CA C 13 55.49 0.11 . 1 . . . . 24 ALA CA . 15094 1 170 . 1 1 24 24 ALA CB C 13 19.35 0.17 . 1 . . . . 24 ALA CB . 15094 1 171 . 1 1 24 24 ALA N N 15 124.01 0.39 . 1 . . . . 24 ALA N . 15094 1 172 . 1 1 25 25 GLN H H 1 8.49 0.07 . 1 . . . . 25 GLN H . 15094 1 173 . 1 1 25 25 GLN HA H 1 3.58 0.07 . 1 . . . . 25 GLN HA . 15094 1 174 . 1 1 25 25 GLN HE21 H 1 6.64 0.07 . 2 . . . . 25 GLN HE21 . 15094 1 175 . 1 1 25 25 GLN HE22 H 1 7.35 0.07 . 2 . . . . 25 GLN HE22 . 15094 1 176 . 1 1 25 25 GLN C C 13 177.76 0.16 . 1 . . . . 25 GLN C . 15094 1 177 . 1 1 25 25 GLN CA C 13 59.74 0.11 . 1 . . . . 25 GLN CA . 15094 1 178 . 1 1 25 25 GLN CB C 13 27.43 0.17 . 1 . . . . 25 GLN CB . 15094 1 179 . 1 1 25 25 GLN CG C 13 34.18 0.17 . 1 . . . . 25 GLN CG . 15094 1 180 . 1 1 25 25 GLN CD C 13 179.19 0.16 . 1 . . . . 25 GLN CD . 15094 1 181 . 1 1 25 25 GLN N N 15 116.97 0.39 . 1 . . . . 25 GLN N . 15094 1 182 . 1 1 25 25 GLN NE2 N 15 110.32 0.39 . 1 . . . . 25 GLN NE2 . 15094 1 183 . 1 1 26 26 ASP H H 1 7.88 0.07 . 1 . . . . 26 ASP H . 15094 1 184 . 1 1 26 26 ASP C C 13 178.91 0.16 . 1 . . . . 26 ASP C . 15094 1 185 . 1 1 26 26 ASP CA C 13 57.5 0.11 . 1 . . . . 26 ASP CA . 15094 1 186 . 1 1 26 26 ASP CB C 13 41.45 0.17 . 1 . . . . 26 ASP CB . 15094 1 187 . 1 1 26 26 ASP CG C 13 179.22 0.16 . 1 . . . . 26 ASP CG . 15094 1 188 . 1 1 26 26 ASP N N 15 121.41 0.39 . 1 . . . . 26 ASP N . 15094 1 189 . 1 1 27 27 LEU H H 1 8.43 0.07 . 1 . . . . 27 LEU H . 15094 1 190 . 1 1 27 27 LEU C C 13 178.67 0.16 . 1 . . . . 27 LEU C . 15094 1 191 . 1 1 27 27 LEU CA C 13 57.69 0.11 . 1 . . . . 27 LEU CA . 15094 1 192 . 1 1 27 27 LEU CB C 13 42.56 0.17 . 1 . . . . 27 LEU CB . 15094 1 193 . 1 1 27 27 LEU N N 15 119.87 0.39 . 1 . . . . 27 LEU N . 15094 1 194 . 1 1 28 28 ALA H H 1 8.09 0.07 . 1 . . . . 28 ALA H . 15094 1 195 . 1 1 28 28 ALA C C 13 177.98 0.16 . 1 . . . . 28 ALA C . 15094 1 196 . 1 1 28 28 ALA CA C 13 54.57 0.11 . 1 . . . . 28 ALA CA . 15094 1 197 . 1 1 28 28 ALA CB C 13 18.83 0.17 . 1 . . . . 28 ALA CB . 15094 1 198 . 1 1 28 28 ALA N N 15 119.02 0.39 . 1 . . . . 28 ALA N . 15094 1 199 . 1 1 29 29 ALA H H 1 8.65 0.07 . 1 . . . . 29 ALA H . 15094 1 200 . 1 1 29 29 ALA C C 13 180.76 0.16 . 1 . . . . 29 ALA C . 15094 1 201 . 1 1 29 29 ALA CA C 13 55.6 0.11 . 1 . . . . 29 ALA CA . 15094 1 202 . 1 1 29 29 ALA CB C 13 17.79 0.17 . 1 . . . . 29 ALA CB . 15094 1 203 . 1 1 29 29 ALA N N 15 119.22 0.39 . 1 . . . . 29 ALA N . 15094 1 204 . 1 1 30 30 LYS H H 1 7.76 0.07 . 1 . . . . 30 LYS H . 15094 1 205 . 1 1 30 30 LYS HA H 1 4.69 0.07 . 1 . . . . 30 LYS HA . 15094 1 206 . 1 1 30 30 LYS C C 13 178.73 0.16 . 1 . . . . 30 LYS C . 15094 1 207 . 1 1 30 30 LYS CA C 13 59.06 0.11 . 1 . . . . 30 LYS CA . 15094 1 208 . 1 1 30 30 LYS CB C 13 31.8 0.17 . 1 . . . . 30 LYS CB . 15094 1 209 . 1 1 30 30 LYS N N 15 118.52 0.39 . 1 . . . . 30 LYS N . 15094 1 210 . 1 1 31 31 VAL H H 1 7.6 0.07 . 1 . . . . 31 VAL H . 15094 1 211 . 1 1 31 31 VAL HA H 1 3.92 0.07 . 1 . . . . 31 VAL HA . 15094 1 212 . 1 1 31 31 VAL C C 13 178.34 0.16 . 1 . . . . 31 VAL C . 15094 1 213 . 1 1 31 31 VAL CA C 13 64.7 0.11 . 1 . . . . 31 VAL CA . 15094 1 214 . 1 1 31 31 VAL CB C 13 30.89 0.17 . 1 . . . . 31 VAL CB . 15094 1 215 . 1 1 31 31 VAL N N 15 111.22 0.39 . 1 . . . . 31 VAL N . 15094 1 216 . 1 1 32 32 LEU H H 1 8.28 0.07 . 1 . . . . 32 LEU H . 15094 1 217 . 1 1 32 32 LEU HA H 1 5.55 0.07 . 1 . . . . 32 LEU HA . 15094 1 218 . 1 1 32 32 LEU C C 13 181.1 0.16 . 1 . . . . 32 LEU C . 15094 1 219 . 1 1 32 32 LEU CA C 13 57.36 0.11 . 1 . . . . 32 LEU CA . 15094 1 220 . 1 1 32 32 LEU CB C 13 41 0.17 . 1 . . . . 32 LEU CB . 15094 1 221 . 1 1 32 32 LEU N N 15 123.08 0.39 . 1 . . . . 32 LEU N . 15094 1 222 . 1 1 33 33 ALA H H 1 8.18 0.07 . 1 . . . . 33 ALA H . 15094 1 223 . 1 1 33 33 ALA HA H 1 4.44 0.07 . 1 . . . . 33 ALA HA . 15094 1 224 . 1 1 33 33 ALA HB1 H 1 1.34 0.07 . 1 . . . . 33 ALA HB . 15094 1 225 . 1 1 33 33 ALA HB2 H 1 1.34 0.07 . 1 . . . . 33 ALA HB . 15094 1 226 . 1 1 33 33 ALA HB3 H 1 1.34 0.07 . 1 . . . . 33 ALA HB . 15094 1 227 . 1 1 33 33 ALA C C 13 180.03 0.16 . 1 . . . . 33 ALA C . 15094 1 228 . 1 1 33 33 ALA CA C 13 55.09 0.11 . 1 . . . . 33 ALA CA . 15094 1 229 . 1 1 33 33 ALA CB C 13 17.78 0.17 . 1 . . . . 33 ALA CB . 15094 1 230 . 1 1 33 33 ALA N N 15 125.25 0.39 . 1 . . . . 33 ALA N . 15094 1 231 . 1 1 34 34 GLU H H 1 7.31 0.07 . 1 . . . . 34 GLU H . 15094 1 232 . 1 1 34 34 GLU C C 13 174.75 0.16 . 1 . . . . 34 GLU C . 15094 1 233 . 1 1 34 34 GLU CA C 13 56 0.11 . 1 . . . . 34 GLU CA . 15094 1 234 . 1 1 34 34 GLU CB C 13 30.15 0.17 . 1 . . . . 34 GLU CB . 15094 1 235 . 1 1 34 34 GLU CG C 13 36.2 0.17 . 1 . . . . 34 GLU CG . 15094 1 236 . 1 1 34 34 GLU CD C 13 183.09 0.16 . 1 . . . . 34 GLU CD . 15094 1 237 . 1 1 34 34 GLU N N 15 114.77 0.39 . 1 . . . . 34 GLU N . 15094 1 238 . 1 1 35 35 LYS H H 1 7.74 0.07 . 1 . . . . 35 LYS H . 15094 1 239 . 1 1 35 35 LYS C C 13 174.73 0.16 . 1 . . . . 35 LYS C . 15094 1 240 . 1 1 35 35 LYS CA C 13 57.54 0.11 . 1 . . . . 35 LYS CA . 15094 1 241 . 1 1 35 35 LYS CB C 13 28.94 0.17 . 1 . . . . 35 LYS CB . 15094 1 242 . 1 1 35 35 LYS N N 15 114.65 0.39 . 1 . . . . 35 LYS N . 15094 1 243 . 1 1 36 36 LEU H H 1 7.86 0.07 . 1 . . . . 36 LEU H . 15094 1 244 . 1 1 36 36 LEU C C 13 176.32 0.16 . 1 . . . . 36 LEU C . 15094 1 245 . 1 1 36 36 LEU CA C 13 54.24 0.11 . 1 . . . . 36 LEU CA . 15094 1 246 . 1 1 36 36 LEU CB C 13 44.92 0.17 . 1 . . . . 36 LEU CB . 15094 1 247 . 1 1 36 36 LEU N N 15 113.05 0.39 . 1 . . . . 36 LEU N . 15094 1 248 . 1 1 37 37 ALA H H 1 7.35 0.07 . 1 . . . . 37 ALA H . 15094 1 249 . 1 1 37 37 ALA HA H 1 4.39 0.07 . 1 . . . . 37 ALA HA . 15094 1 250 . 1 1 37 37 ALA C C 13 174.19 0.16 . 1 . . . . 37 ALA C . 15094 1 251 . 1 1 37 37 ALA CA C 13 49.91 0.11 . 1 . . . . 37 ALA CA . 15094 1 252 . 1 1 37 37 ALA CB C 13 22 0.17 . 1 . . . . 37 ALA CB . 15094 1 253 . 1 1 37 37 ALA N N 15 118.42 0.39 . 1 . . . . 37 ALA N . 15094 1 254 . 1 1 38 38 ALA H H 1 8.46 0.07 . 1 . . . . 38 ALA H . 15094 1 255 . 1 1 38 38 ALA HA H 1 4.15 0.07 . 1 . . . . 38 ALA HA . 15094 1 256 . 1 1 38 38 ALA C C 13 175.96 0.16 . 1 . . . . 38 ALA C . 15094 1 257 . 1 1 38 38 ALA CA C 13 52.73 0.11 . 1 . . . . 38 ALA CA . 15094 1 258 . 1 1 38 38 ALA CB C 13 21.77 0.17 . 1 . . . . 38 ALA CB . 15094 1 259 . 1 1 38 38 ALA N N 15 122.29 0.39 . 1 . . . . 38 ALA N . 15094 1 260 . 1 1 39 39 CYS H H 1 7.26 0.07 . 1 . . . . 39 CYS H . 15094 1 261 . 1 1 39 39 CYS C C 13 172.61 0.16 . 1 . . . . 39 CYS C . 15094 1 262 . 1 1 39 39 CYS CA C 13 55.64 0.11 . 1 . . . . 39 CYS CA . 15094 1 263 . 1 1 39 39 CYS CB C 13 29.69 0.17 . 1 . . . . 39 CYS CB . 15094 1 264 . 1 1 39 39 CYS N N 15 109.57 0.39 . 1 . . . . 39 CYS N . 15094 1 265 . 1 1 40 40 ALA H H 1 9.14 0.07 . 1 . . . . 40 ALA H . 15094 1 266 . 1 1 40 40 ALA HA H 1 5.28 0.07 . 1 . . . . 40 ALA HA . 15094 1 267 . 1 1 40 40 ALA C C 13 174.35 0.16 . 1 . . . . 40 ALA C . 15094 1 268 . 1 1 40 40 ALA CA C 13 50.52 0.11 . 1 . . . . 40 ALA CA . 15094 1 269 . 1 1 40 40 ALA CB C 13 23.28 0.17 . 1 . . . . 40 ALA CB . 15094 1 270 . 1 1 40 40 ALA N N 15 127.28 0.39 . 1 . . . . 40 ALA N . 15094 1 271 . 1 1 41 41 THR H H 1 9.24 0.07 . 1 . . . . 41 THR H . 15094 1 272 . 1 1 41 41 THR HB H 1 3.86 0.07 . 1 . . . . 41 THR HB . 15094 1 273 . 1 1 41 41 THR C C 13 172.81 0.16 . 1 . . . . 41 THR C . 15094 1 274 . 1 1 41 41 THR CA C 13 62.08 0.11 . 1 . . . . 41 THR CA . 15094 1 275 . 1 1 41 41 THR CB C 13 70.86 0.17 . 1 . . . . 41 THR CB . 15094 1 276 . 1 1 41 41 THR N N 15 121.5 0.39 . 1 . . . . 41 THR N . 15094 1 277 . 1 1 42 42 LEU H H 1 9.78 0.07 . 1 . . . . 42 LEU H . 15094 1 278 . 1 1 42 42 LEU HA H 1 5.04 0.07 . 1 . . . . 42 LEU HA . 15094 1 279 . 1 1 42 42 LEU C C 13 175.84 0.16 . 1 . . . . 42 LEU C . 15094 1 280 . 1 1 42 42 LEU CA C 13 53.19 0.11 . 1 . . . . 42 LEU CA . 15094 1 281 . 1 1 42 42 LEU CB C 13 43.32 0.17 . 1 . . . . 42 LEU CB . 15094 1 282 . 1 1 42 42 LEU N N 15 129.28 0.39 . 1 . . . . 42 LEU N . 15094 1 283 . 1 1 43 43 ILE H H 1 9.18 0.07 . 1 . . . . 43 ILE H . 15094 1 284 . 1 1 43 43 ILE C C 13 172.85 0.16 . 1 . . . . 43 ILE C . 15094 1 285 . 1 1 43 43 ILE CA C 13 58.47 0.11 . 1 . . . . 43 ILE CA . 15094 1 286 . 1 1 43 43 ILE CB C 13 39.87 0.17 . 1 . . . . 43 ILE CB . 15094 1 287 . 1 1 43 43 ILE N N 15 122.6 0.39 . 1 . . . . 43 ILE N . 15094 1 288 . 1 1 44 44 PRO C C 13 175.59 0.16 . 1 . . . . 44 PRO C . 15094 1 289 . 1 1 44 44 PRO CA C 13 62.17 0.11 . 1 . . . . 44 PRO CA . 15094 1 290 . 1 1 44 44 PRO CB C 13 32.78 0.17 . 1 . . . . 44 PRO CB . 15094 1 291 . 1 1 44 44 PRO N N 15 136.52 0.39 . 1 . . . . 44 PRO N . 15094 1 292 . 1 1 45 45 GLY H H 1 8.01 0.07 . 1 . . . . 45 GLY H . 15094 1 293 . 1 1 45 45 GLY HA2 H 1 3.73 0.07 . 2 . . . . 45 GLY HA2 . 15094 1 294 . 1 1 45 45 GLY HA3 H 1 4.08 0.07 . 2 . . . . 45 GLY HA3 . 15094 1 295 . 1 1 45 45 GLY C C 13 174.59 0.16 . 1 . . . . 45 GLY C . 15094 1 296 . 1 1 45 45 GLY CA C 13 46.02 0.11 . 1 . . . . 45 GLY CA . 15094 1 297 . 1 1 45 45 GLY N N 15 103.76 0.39 . 1 . . . . 45 GLY N . 15094 1 298 . 1 1 46 46 ALA H H 1 7.75 0.07 . 1 . . . . 46 ALA H . 15094 1 299 . 1 1 46 46 ALA HA H 1 5.07 0.07 . 1 . . . . 46 ALA HA . 15094 1 300 . 1 1 46 46 ALA C C 13 176.87 0.16 . 1 . . . . 46 ALA C . 15094 1 301 . 1 1 46 46 ALA CA C 13 50.73 0.11 . 1 . . . . 46 ALA CA . 15094 1 302 . 1 1 46 46 ALA CB C 13 20.11 0.17 . 1 . . . . 46 ALA CB . 15094 1 303 . 1 1 46 46 ALA N N 15 123.11 0.39 . 1 . . . . 46 ALA N . 15094 1 304 . 1 1 47 47 THR H H 1 8.79 0.07 . 1 . . . . 47 THR H . 15094 1 305 . 1 1 47 47 THR HB H 1 3.81 0.07 . 1 . . . . 47 THR HB . 15094 1 306 . 1 1 47 47 THR C C 13 173.71 0.16 . 1 . . . . 47 THR C . 15094 1 307 . 1 1 47 47 THR CA C 13 61.73 0.11 . 1 . . . . 47 THR CA . 15094 1 308 . 1 1 47 47 THR CB C 13 71.92 0.17 . 1 . . . . 47 THR CB . 15094 1 309 . 1 1 47 47 THR N N 15 116.6 0.39 . 1 . . . . 47 THR N . 15094 1 310 . 1 1 48 48 SER H H 1 9.51 0.07 . 1 . . . . 48 SER H . 15094 1 311 . 1 1 48 48 SER C C 13 172.91 0.16 . 1 . . . . 48 SER C . 15094 1 312 . 1 1 48 48 SER CA C 13 56.68 0.11 . 1 . . . . 48 SER CA . 15094 1 313 . 1 1 48 48 SER CB C 13 65.13 0.17 . 1 . . . . 48 SER CB . 15094 1 314 . 1 1 48 48 SER N N 15 123.56 0.39 . 1 . . . . 48 SER N . 15094 1 315 . 1 1 49 49 LEU H H 1 9.17 0.07 . 1 . . . . 49 LEU H . 15094 1 316 . 1 1 49 49 LEU C C 13 175.32 0.16 . 1 . . . . 49 LEU C . 15094 1 317 . 1 1 49 49 LEU CA C 13 54.41 0.11 . 1 . . . . 49 LEU CA . 15094 1 318 . 1 1 49 49 LEU CB C 13 45.82 0.17 . 1 . . . . 49 LEU CB . 15094 1 319 . 1 1 49 49 LEU N N 15 125.28 0.39 . 1 . . . . 49 LEU N . 15094 1 320 . 1 1 50 50 TYR H H 1 8.12 0.07 . 1 . . . . 50 TYR H . 15094 1 321 . 1 1 50 50 TYR C C 13 172.56 0.16 . 1 . . . . 50 TYR C . 15094 1 322 . 1 1 50 50 TYR CA C 13 56.58 0.11 . 1 . . . . 50 TYR CA . 15094 1 323 . 1 1 50 50 TYR CB C 13 39.64 0.17 . 1 . . . . 50 TYR CB . 15094 1 324 . 1 1 50 50 TYR N N 15 117.36 0.39 . 1 . . . . 50 TYR N . 15094 1 325 . 1 1 51 51 TYR H H 1 9.66 0.07 . 1 . . . . 51 TYR H . 15094 1 326 . 1 1 51 51 TYR C C 13 176.34 0.16 . 1 . . . . 51 TYR C . 15094 1 327 . 1 1 51 51 TYR CA C 13 57.8 0.11 . 1 . . . . 51 TYR CA . 15094 1 328 . 1 1 51 51 TYR CB C 13 40.93 0.17 . 1 . . . . 51 TYR CB . 15094 1 329 . 1 1 51 51 TYR N N 15 122.55 0.39 . 1 . . . . 51 TYR N . 15094 1 330 . 1 1 52 52 TRP H H 1 9.09 0.07 . 1 . . . . 52 TRP H . 15094 1 331 . 1 1 52 52 TRP HD1 H 1 7.28 0.07 . 1 . . . . 52 TRP HD1 . 15094 1 332 . 1 1 52 52 TRP HE1 H 1 10.04 0.07 . 1 . . . . 52 TRP HE1 . 15094 1 333 . 1 1 52 52 TRP HZ2 H 1 7.41 0.07 . 1 . . . . 52 TRP HZ2 . 15094 1 334 . 1 1 52 52 TRP HH2 H 1 7.12 0.07 . 1 . . . . 52 TRP HH2 . 15094 1 335 . 1 1 52 52 TRP C C 13 175.72 0.16 . 1 . . . . 52 TRP C . 15094 1 336 . 1 1 52 52 TRP CA C 13 56.8 0.11 . 1 . . . . 52 TRP CA . 15094 1 337 . 1 1 52 52 TRP CB C 13 32.26 0.17 . 1 . . . . 52 TRP CB . 15094 1 338 . 1 1 52 52 TRP N N 15 124.53 0.39 . 1 . . . . 52 TRP N . 15094 1 339 . 1 1 52 52 TRP NE1 N 15 130.37 0.39 . 1 . . . . 52 TRP NE1 . 15094 1 340 . 1 1 53 53 GLU H H 1 9 0.07 . 1 . . . . 53 GLU H . 15094 1 341 . 1 1 53 53 GLU C C 13 176.61 0.16 . 1 . . . . 53 GLU C . 15094 1 342 . 1 1 53 53 GLU CA C 13 56.74 0.11 . 1 . . . . 53 GLU CA . 15094 1 343 . 1 1 53 53 GLU CB C 13 27.24 0.17 . 1 . . . . 53 GLU CB . 15094 1 344 . 1 1 53 53 GLU CG C 13 35.62 0.17 . 1 . . . . 53 GLU CG . 15094 1 345 . 1 1 53 53 GLU CD C 13 184.36 0.16 . 1 . . . . 53 GLU CD . 15094 1 346 . 1 1 53 53 GLU N N 15 127.35 0.39 . 1 . . . . 53 GLU N . 15094 1 347 . 1 1 54 54 GLY H H 1 8.31 0.07 . 1 . . . . 54 GLY H . 15094 1 348 . 1 1 54 54 GLY HA2 H 1 3.57 0.07 . 2 . . . . 54 GLY HA2 . 15094 1 349 . 1 1 54 54 GLY HA3 H 1 4.06 0.07 . 2 . . . . 54 GLY HA3 . 15094 1 350 . 1 1 54 54 GLY C C 13 173.55 0.16 . 1 . . . . 54 GLY C . 15094 1 351 . 1 1 54 54 GLY CA C 13 45.39 0.11 . 1 . . . . 54 GLY CA . 15094 1 352 . 1 1 54 54 GLY N N 15 103.5 0.39 . 1 . . . . 54 GLY N . 15094 1 353 . 1 1 55 55 LYS H H 1 7.69 0.07 . 1 . . . . 55 LYS H . 15094 1 354 . 1 1 55 55 LYS HA H 1 4.52 0.07 . 1 . . . . 55 LYS HA . 15094 1 355 . 1 1 55 55 LYS HB2 H 1 1.76 0.07 . 2 . . . . 55 LYS HB2 . 15094 1 356 . 1 1 55 55 LYS C C 13 173.93 0.16 . 1 . . . . 55 LYS C . 15094 1 357 . 1 1 55 55 LYS CA C 13 54.37 0.11 . 1 . . . . 55 LYS CA . 15094 1 358 . 1 1 55 55 LYS CB C 13 35.23 0.17 . 1 . . . . 55 LYS CB . 15094 1 359 . 1 1 55 55 LYS CG C 13 24.38 0.17 . 1 . . . . 55 LYS CG . 15094 1 360 . 1 1 55 55 LYS CD C 13 29.09 0.17 . 1 . . . . 55 LYS CD . 15094 1 361 . 1 1 55 55 LYS CE C 13 42.29 0.17 . 1 . . . . 55 LYS CE . 15094 1 362 . 1 1 55 55 LYS N N 15 121.69 0.39 . 1 . . . . 55 LYS N . 15094 1 363 . 1 1 56 56 LEU H H 1 8.22 0.07 . 1 . . . . 56 LEU H . 15094 1 364 . 1 1 56 56 LEU HA H 1 4.41 0.07 . 1 . . . . 56 LEU HA . 15094 1 365 . 1 1 56 56 LEU HB2 H 1 1.42 0.07 . 2 . . . . 56 LEU HB2 . 15094 1 366 . 1 1 56 56 LEU C C 13 175.71 0.16 . 1 . . . . 56 LEU C . 15094 1 367 . 1 1 56 56 LEU CA C 13 55.03 0.11 . 1 . . . . 56 LEU CA . 15094 1 368 . 1 1 56 56 LEU CB C 13 41.72 0.17 . 1 . . . . 56 LEU CB . 15094 1 369 . 1 1 56 56 LEU N N 15 125.46 0.39 . 1 . . . . 56 LEU N . 15094 1 370 . 1 1 57 57 GLU H H 1 9.04 0.07 . 1 . . . . 57 GLU H . 15094 1 371 . 1 1 57 57 GLU C C 13 173.9 0.16 . 1 . . . . 57 GLU C . 15094 1 372 . 1 1 57 57 GLU CA C 13 54.51 0.11 . 1 . . . . 57 GLU CA . 15094 1 373 . 1 1 57 57 GLU CB C 13 31.37 0.17 . 1 . . . . 57 GLU CB . 15094 1 374 . 1 1 57 57 GLU CG C 13 34.96 0.17 . 1 . . . . 57 GLU CG . 15094 1 375 . 1 1 57 57 GLU CD C 13 183.21 0.16 . 1 . . . . 57 GLU CD . 15094 1 376 . 1 1 57 57 GLU N N 15 131.43 0.39 . 1 . . . . 57 GLU N . 15094 1 377 . 1 1 58 58 GLN H H 1 8.12 0.07 . 1 . . . . 58 GLN H . 15094 1 378 . 1 1 58 58 GLN HA H 1 5.35 0.07 . 1 . . . . 58 GLN HA . 15094 1 379 . 1 1 58 58 GLN HE21 H 1 6.57 0.07 . 2 . . . . 58 GLN HE21 . 15094 1 380 . 1 1 58 58 GLN HE22 H 1 7.14 0.07 . 2 . . . . 58 GLN HE22 . 15094 1 381 . 1 1 58 58 GLN C C 13 175.12 0.16 . 1 . . . . 58 GLN C . 15094 1 382 . 1 1 58 58 GLN CA C 13 53.75 0.11 . 1 . . . . 58 GLN CA . 15094 1 383 . 1 1 58 58 GLN CB C 13 31.69 0.17 . 1 . . . . 58 GLN CB . 15094 1 384 . 1 1 58 58 GLN CG C 13 33.39 0.17 . 1 . . . . 58 GLN CG . 15094 1 385 . 1 1 58 58 GLN CD C 13 180.12 0.16 . 1 . . . . 58 GLN CD . 15094 1 386 . 1 1 58 58 GLN N N 15 118.99 0.39 . 1 . . . . 58 GLN N . 15094 1 387 . 1 1 58 58 GLN NE2 N 15 110.88 0.39 . 1 . . . . 58 GLN NE2 . 15094 1 388 . 1 1 59 59 GLU H H 1 8.94 0.07 . 1 . . . . 59 GLU H . 15094 1 389 . 1 1 59 59 GLU C C 13 174.87 0.16 . 1 . . . . 59 GLU C . 15094 1 390 . 1 1 59 59 GLU CA C 13 54.18 0.11 . 1 . . . . 59 GLU CA . 15094 1 391 . 1 1 59 59 GLU CB C 13 33.63 0.17 . 1 . . . . 59 GLU CB . 15094 1 392 . 1 1 59 59 GLU CG C 13 35.36 0.17 . 1 . . . . 59 GLU CG . 15094 1 393 . 1 1 59 59 GLU CD C 13 183.72 0.16 . 1 . . . . 59 GLU CD . 15094 1 394 . 1 1 59 59 GLU N N 15 123.69 0.39 . 1 . . . . 59 GLU N . 15094 1 395 . 1 1 60 60 TYR H H 1 8.76 0.07 . 1 . . . . 60 TYR H . 15094 1 396 . 1 1 60 60 TYR C C 13 175.61 0.16 . 1 . . . . 60 TYR C . 15094 1 397 . 1 1 60 60 TYR CA C 13 58.34 0.11 . 1 . . . . 60 TYR CA . 15094 1 398 . 1 1 60 60 TYR CB C 13 38.59 0.17 . 1 . . . . 60 TYR CB . 15094 1 399 . 1 1 60 60 TYR N N 15 126.03 0.39 . 1 . . . . 60 TYR N . 15094 1 400 . 1 1 61 61 GLU H H 1 8.29 0.07 . 1 . . . . 61 GLU H . 15094 1 401 . 1 1 61 61 GLU HB2 H 1 2.65 0.07 . 2 . . . . 61 GLU HB2 . 15094 1 402 . 1 1 61 61 GLU C C 13 173.63 0.16 . 1 . . . . 61 GLU C . 15094 1 403 . 1 1 61 61 GLU CA C 13 54.36 0.11 . 1 . . . . 61 GLU CA . 15094 1 404 . 1 1 61 61 GLU CB C 13 34.49 0.17 . 1 . . . . 61 GLU CB . 15094 1 405 . 1 1 61 61 GLU N N 15 121.85 0.39 . 1 . . . . 61 GLU N . 15094 1 406 . 1 1 62 62 VAL H H 1 8.76 0.07 . 1 . . . . 62 VAL H . 15094 1 407 . 1 1 62 62 VAL C C 13 176.66 0.16 . 1 . . . . 62 VAL C . 15094 1 408 . 1 1 62 62 VAL CA C 13 60.38 0.11 . 1 . . . . 62 VAL CA . 15094 1 409 . 1 1 62 62 VAL CB C 13 34.47 0.17 . 1 . . . . 62 VAL CB . 15094 1 410 . 1 1 62 62 VAL CG1 C 13 20.6 0.17 . 1 . . . . 62 VAL CG1 . 15094 1 411 . 1 1 62 62 VAL N N 15 118.26 0.39 . 1 . . . . 62 VAL N . 15094 1 412 . 1 1 63 63 GLN H H 1 8.59 0.07 . 1 . . . . 63 GLN H . 15094 1 413 . 1 1 63 63 GLN C C 13 174.09 0.16 . 1 . . . . 63 GLN C . 15094 1 414 . 1 1 63 63 GLN CA C 13 55.04 0.11 . 1 . . . . 63 GLN CA . 15094 1 415 . 1 1 63 63 GLN CB C 13 30.52 0.17 . 1 . . . . 63 GLN CB . 15094 1 416 . 1 1 63 63 GLN N N 15 127.54 0.39 . 1 . . . . 63 GLN N . 15094 1 417 . 1 1 64 64 MET H H 1 9.35 0.07 . 1 . . . . 64 MET H . 15094 1 418 . 1 1 64 64 MET C C 13 176.27 0.16 . 1 . . . . 64 MET C . 15094 1 419 . 1 1 64 64 MET CA C 13 54.3 0.11 . 1 . . . . 64 MET CA . 15094 1 420 . 1 1 64 64 MET CB C 13 35.83 0.17 . 1 . . . . 64 MET CB . 15094 1 421 . 1 1 64 64 MET N N 15 126.52 0.39 . 1 . . . . 64 MET N . 15094 1 422 . 1 1 65 65 ILE H H 1 9.22 0.07 . 1 . . . . 65 ILE H . 15094 1 423 . 1 1 65 65 ILE C C 13 176.41 0.16 . 1 . . . . 65 ILE C . 15094 1 424 . 1 1 65 65 ILE CA C 13 61.15 0.11 . 1 . . . . 65 ILE CA . 15094 1 425 . 1 1 65 65 ILE CB C 13 40.17 0.17 . 1 . . . . 65 ILE CB . 15094 1 426 . 1 1 65 65 ILE CG1 C 13 32.77 0.17 . 1 . . . . 65 ILE CG1 . 15094 1 427 . 1 1 65 65 ILE N N 15 122.63 0.39 . 1 . . . . 65 ILE N . 15094 1 428 . 1 1 66 66 LEU H H 1 10.1 0.07 . 1 . . . . 66 LEU H . 15094 1 429 . 1 1 66 66 LEU C C 13 175.29 0.16 . 1 . . . . 66 LEU C . 15094 1 430 . 1 1 66 66 LEU CA C 13 54.5 0.11 . 1 . . . . 66 LEU CA . 15094 1 431 . 1 1 66 66 LEU CB C 13 44.36 0.17 . 1 . . . . 66 LEU CB . 15094 1 432 . 1 1 66 66 LEU CD1 C 13 26.53 0.17 . 2 . . . . 66 LEU CD1 . 15094 1 433 . 1 1 66 66 LEU CD2 C 13 23.52 0.17 . 2 . . . . 66 LEU CD2 . 15094 1 434 . 1 1 66 66 LEU N N 15 128.56 0.39 . 1 . . . . 66 LEU N . 15094 1 435 . 1 1 67 67 LYS H H 1 8.04 0.07 . 1 . . . . 67 LYS H . 15094 1 436 . 1 1 67 67 LYS C C 13 175.55 0.16 . 1 . . . . 67 LYS C . 15094 1 437 . 1 1 67 67 LYS CA C 13 56.36 0.11 . 1 . . . . 67 LYS CA . 15094 1 438 . 1 1 67 67 LYS CB C 13 33.09 0.17 . 1 . . . . 67 LYS CB . 15094 1 439 . 1 1 67 67 LYS N N 15 122.05 0.39 . 1 . . . . 67 LYS N . 15094 1 440 . 1 1 68 68 THR H H 1 8.34 0.07 . 1 . . . . 68 THR H . 15094 1 441 . 1 1 68 68 THR HA H 1 4.5 0.07 . 1 . . . . 68 THR HA . 15094 1 442 . 1 1 68 68 THR C C 13 171.86 0.16 . 1 . . . . 68 THR C . 15094 1 443 . 1 1 68 68 THR CA C 13 59.92 0.11 . 1 . . . . 68 THR CA . 15094 1 444 . 1 1 68 68 THR CB C 13 68.7 0.17 . 1 . . . . 68 THR CB . 15094 1 445 . 1 1 68 68 THR CG2 C 13 21.87 0.17 . 1 . . . . 68 THR CG2 . 15094 1 446 . 1 1 68 68 THR N N 15 119.34 0.39 . 1 . . . . 68 THR N . 15094 1 447 . 1 1 69 69 THR H H 1 8.06 0.07 . 1 . . . . 69 THR H . 15094 1 448 . 1 1 69 69 THR HB H 1 4.54 0.07 . 1 . . . . 69 THR HB . 15094 1 449 . 1 1 69 69 THR C C 13 177.07 0.16 . 1 . . . . 69 THR C . 15094 1 450 . 1 1 69 69 THR CA C 13 58.87 0.11 . 1 . . . . 69 THR CA . 15094 1 451 . 1 1 69 69 THR CB C 13 72.22 0.17 . 1 . . . . 69 THR CB . 15094 1 452 . 1 1 69 69 THR CG2 C 13 21.07 0.17 . 1 . . . . 69 THR CG2 . 15094 1 453 . 1 1 69 69 THR N N 15 110.57 0.39 . 1 . . . . 69 THR N . 15094 1 454 . 1 1 70 70 VAL H H 1 8.86 0.07 . 1 . . . . 70 VAL H . 15094 1 455 . 1 1 70 70 VAL HA H 1 3.62 0.07 . 1 . . . . 70 VAL HA . 15094 1 456 . 1 1 70 70 VAL C C 13 178.51 0.16 . 1 . . . . 70 VAL C . 15094 1 457 . 1 1 70 70 VAL CA C 13 65.75 0.11 . 1 . . . . 70 VAL CA . 15094 1 458 . 1 1 70 70 VAL CB C 13 31.8 0.17 . 1 . . . . 70 VAL CB . 15094 1 459 . 1 1 70 70 VAL CG1 C 13 22.09 0.17 . 2 . . . . 70 VAL CG1 . 15094 1 460 . 1 1 70 70 VAL N N 15 121.58 0.39 . 1 . . . . 70 VAL N . 15094 1 461 . 1 1 71 71 SER H H 1 7.98 0.07 . 1 . . . . 71 SER H . 15094 1 462 . 1 1 71 71 SER HA H 1 4.74 0.07 . 1 . . . . 71 SER HA . 15094 1 463 . 1 1 71 71 SER C C 13 175.31 0.16 . 1 . . . . 71 SER C . 15094 1 464 . 1 1 71 71 SER CA C 13 60.31 0.11 . 1 . . . . 71 SER CA . 15094 1 465 . 1 1 71 71 SER CB C 13 62.94 0.17 . 1 . . . . 71 SER CB . 15094 1 466 . 1 1 71 71 SER N N 15 114.16 0.39 . 1 . . . . 71 SER N . 15094 1 467 . 1 1 72 72 HIS H H 1 7.66 0.07 . 1 . . . . 72 HIS H . 15094 1 468 . 1 1 72 72 HIS C C 13 175.63 0.16 . 1 . . . . 72 HIS C . 15094 1 469 . 1 1 72 72 HIS CA C 13 56.33 0.11 . 1 . . . . 72 HIS CA . 15094 1 470 . 1 1 72 72 HIS CB C 13 31.14 0.17 . 1 . . . . 72 HIS CB . 15094 1 471 . 1 1 72 72 HIS N N 15 118.31 0.39 . 1 . . . . 72 HIS N . 15094 1 472 . 1 1 73 73 GLN H H 1 7.52 0.07 . 1 . . . . 73 GLN H . 15094 1 473 . 1 1 73 73 GLN HE21 H 1 5.92 0.07 . 2 . . . . 73 GLN HE21 . 15094 1 474 . 1 1 73 73 GLN HE22 H 1 6.89 0.07 . 2 . . . . 73 GLN HE22 . 15094 1 475 . 1 1 73 73 GLN C C 13 175.64 0.16 . 1 . . . . 73 GLN C . 15094 1 476 . 1 1 73 73 GLN CA C 13 60.21 0.11 . 1 . . . . 73 GLN CA . 15094 1 477 . 1 1 73 73 GLN CB C 13 27.28 0.17 . 1 . . . . 73 GLN CB . 15094 1 478 . 1 1 73 73 GLN CG C 13 31.82 0.17 . 1 . . . . 73 GLN CG . 15094 1 479 . 1 1 73 73 GLN CD C 13 177.12 0.16 . 1 . . . . 73 GLN CD . 15094 1 480 . 1 1 73 73 GLN N N 15 120.19 0.39 . 1 . . . . 73 GLN N . 15094 1 481 . 1 1 73 73 GLN NE2 N 15 106.39 0.39 . 1 . . . . 73 GLN NE2 . 15094 1 482 . 1 1 74 74 GLN H H 1 8.41 0.07 . 1 . . . . 74 GLN H . 15094 1 483 . 1 1 74 74 GLN HA H 1 4.74 0.07 . 1 . . . . 74 GLN HA . 15094 1 484 . 1 1 74 74 GLN HE21 H 1 6.89 0.07 . 2 . . . . 74 GLN HE21 . 15094 1 485 . 1 1 74 74 GLN HE22 H 1 7.91 0.07 . 2 . . . . 74 GLN HE22 . 15094 1 486 . 1 1 74 74 GLN C C 13 177.93 0.16 . 1 . . . . 74 GLN C . 15094 1 487 . 1 1 74 74 GLN CA C 13 59.06 0.11 . 1 . . . . 74 GLN CA . 15094 1 488 . 1 1 74 74 GLN CB C 13 27.61 0.17 . 1 . . . . 74 GLN CB . 15094 1 489 . 1 1 74 74 GLN CG C 13 33.28 0.17 . 1 . . . . 74 GLN CG . 15094 1 490 . 1 1 74 74 GLN CD C 13 180.08 0.16 . 1 . . . . 74 GLN CD . 15094 1 491 . 1 1 74 74 GLN N N 15 121.83 0.39 . 1 . . . . 74 GLN N . 15094 1 492 . 1 1 74 74 GLN NE2 N 15 113.69 0.39 . 1 . . . . 74 GLN NE2 . 15094 1 493 . 1 1 75 75 ALA H H 1 8.49 0.07 . 1 . . . . 75 ALA H . 15094 1 494 . 1 1 75 75 ALA HA H 1 4.74 0.07 . 1 . . . . 75 ALA HA . 15094 1 495 . 1 1 75 75 ALA C C 13 181.46 0.16 . 1 . . . . 75 ALA C . 15094 1 496 . 1 1 75 75 ALA CA C 13 54.57 0.11 . 1 . . . . 75 ALA CA . 15094 1 497 . 1 1 75 75 ALA CB C 13 18.61 0.17 . 1 . . . . 75 ALA CB . 15094 1 498 . 1 1 75 75 ALA N N 15 123.28 0.39 . 1 . . . . 75 ALA N . 15094 1 499 . 1 1 76 76 LEU H H 1 8.67 0.07 . 1 . . . . 76 LEU H . 15094 1 500 . 1 1 76 76 LEU C C 13 177.85 0.16 . 1 . . . . 76 LEU C . 15094 1 501 . 1 1 76 76 LEU CA C 13 58.57 0.11 . 1 . . . . 76 LEU CA . 15094 1 502 . 1 1 76 76 LEU CB C 13 39.87 0.17 . 1 . . . . 76 LEU CB . 15094 1 503 . 1 1 76 76 LEU N N 15 120.19 0.39 . 1 . . . . 76 LEU N . 15094 1 504 . 1 1 77 77 LEU H H 1 8.1 0.07 . 1 . . . . 77 LEU H . 15094 1 505 . 1 1 77 77 LEU C C 13 179.17 0.16 . 1 . . . . 77 LEU C . 15094 1 506 . 1 1 77 77 LEU CA C 13 59.38 0.11 . 1 . . . . 77 LEU CA . 15094 1 507 . 1 1 77 77 LEU CB C 13 40.25 0.17 . 1 . . . . 77 LEU CB . 15094 1 508 . 1 1 77 77 LEU CD1 C 13 27.99 0.17 . 2 . . . . 77 LEU CD1 . 15094 1 509 . 1 1 77 77 LEU CD2 C 13 21.83 0.17 . 2 . . . . 77 LEU CD2 . 15094 1 510 . 1 1 77 77 LEU N N 15 120.38 0.39 . 1 . . . . 77 LEU N . 15094 1 511 . 1 1 78 78 GLU H H 1 8.2 0.07 . 1 . . . . 78 GLU H . 15094 1 512 . 1 1 78 78 GLU HA H 1 4.33 0.07 . 1 . . . . 78 GLU HA . 15094 1 513 . 1 1 78 78 GLU C C 13 178.96 0.16 . 1 . . . . 78 GLU C . 15094 1 514 . 1 1 78 78 GLU CA C 13 59.27 0.11 . 1 . . . . 78 GLU CA . 15094 1 515 . 1 1 78 78 GLU CB C 13 29.39 0.17 . 1 . . . . 78 GLU CB . 15094 1 516 . 1 1 78 78 GLU CG C 13 36.55 0.17 . 1 . . . . 78 GLU CG . 15094 1 517 . 1 1 78 78 GLU CD C 13 183.48 0.16 . 1 . . . . 78 GLU CD . 15094 1 518 . 1 1 78 78 GLU N N 15 117.99 0.39 . 1 . . . . 78 GLU N . 15094 1 519 . 1 1 79 79 CYS H H 1 8.11 0.07 . 1 . . . . 79 CYS H . 15094 1 520 . 1 1 79 79 CYS C C 13 178.07 0.16 . 1 . . . . 79 CYS C . 15094 1 521 . 1 1 79 79 CYS CA C 13 62.63 0.11 . 1 . . . . 79 CYS CA . 15094 1 522 . 1 1 79 79 CYS CB C 13 27.44 0.17 . 1 . . . . 79 CYS CB . 15094 1 523 . 1 1 79 79 CYS N N 15 122.13 0.39 . 1 . . . . 79 CYS N . 15094 1 524 . 1 1 80 80 LEU H H 1 8.46 0.07 . 1 . . . . 80 LEU H . 15094 1 525 . 1 1 80 80 LEU C C 13 178.32 0.16 . 1 . . . . 80 LEU C . 15094 1 526 . 1 1 80 80 LEU CA C 13 58.41 0.11 . 1 . . . . 80 LEU CA . 15094 1 527 . 1 1 80 80 LEU N N 15 119.43 0.39 . 1 . . . . 80 LEU N . 15094 1 528 . 1 1 81 81 LYS H H 1 8.42 0.07 . 1 . . . . 81 LYS H . 15094 1 529 . 1 1 81 81 LYS C C 13 179.04 0.16 . 1 . . . . 81 LYS C . 15094 1 530 . 1 1 81 81 LYS CA C 13 59.79 0.11 . 1 . . . . 81 LYS CA . 15094 1 531 . 1 1 81 81 LYS CB C 13 33.61 0.17 . 1 . . . . 81 LYS CB . 15094 1 532 . 1 1 81 81 LYS N N 15 118.2 0.39 . 1 . . . . 81 LYS N . 15094 1 533 . 1 1 82 82 SER H H 1 7.97 0.07 . 1 . . . . 82 SER H . 15094 1 534 . 1 1 82 82 SER HA H 1 4.13 0.07 . 1 . . . . 82 SER HA . 15094 1 535 . 1 1 82 82 SER C C 13 175.39 0.16 . 1 . . . . 82 SER C . 15094 1 536 . 1 1 82 82 SER CA C 13 60.96 0.11 . 1 . . . . 82 SER CA . 15094 1 537 . 1 1 82 82 SER CB C 13 63.17 0.17 . 1 . . . . 82 SER CB . 15094 1 538 . 1 1 82 82 SER N N 15 112 0.39 . 1 . . . . 82 SER N . 15094 1 539 . 1 1 83 83 HIS H H 1 7.28 0.07 . 1 . . . . 83 HIS H . 15094 1 540 . 1 1 83 83 HIS HA H 1 3.49 0.07 . 1 . . . . 83 HIS HA . 15094 1 541 . 1 1 83 83 HIS C C 13 173.63 0.16 . 1 . . . . 83 HIS C . 15094 1 542 . 1 1 83 83 HIS CA C 13 56.67 0.11 . 1 . . . . 83 HIS CA . 15094 1 543 . 1 1 83 83 HIS CB C 13 30.72 0.17 . 1 . . . . 83 HIS CB . 15094 1 544 . 1 1 83 83 HIS N N 15 116.72 0.39 . 1 . . . . 83 HIS N . 15094 1 545 . 1 1 84 84 HIS H H 1 7.84 0.07 . 1 . . . . 84 HIS H . 15094 1 546 . 1 1 84 84 HIS C C 13 174.68 0.16 . 1 . . . . 84 HIS C . 15094 1 547 . 1 1 84 84 HIS CA C 13 56.58 0.11 . 1 . . . . 84 HIS CA . 15094 1 548 . 1 1 84 84 HIS CB C 13 31.54 0.17 . 1 . . . . 84 HIS CB . 15094 1 549 . 1 1 84 84 HIS N N 15 126.27 0.39 . 1 . . . . 84 HIS N . 15094 1 550 . 1 1 85 85 PRO C C 13 178.44 0.16 . 1 . . . . 85 PRO C . 15094 1 551 . 1 1 85 85 PRO CA C 13 63.76 0.11 . 1 . . . . 85 PRO CA . 15094 1 552 . 1 1 85 85 PRO CB C 13 32.01 0.17 . 1 . . . . 85 PRO CB . 15094 1 553 . 1 1 85 85 PRO N N 15 136.19 0.39 . 1 . . . . 85 PRO N . 15094 1 554 . 1 1 86 86 TYR H H 1 10.82 0.07 . 1 . . . . 86 TYR H . 15094 1 555 . 1 1 86 86 TYR C C 13 176.17 0.16 . 1 . . . . 86 TYR C . 15094 1 556 . 1 1 86 86 TYR CA C 13 54.04 0.11 . 1 . . . . 86 TYR CA . 15094 1 557 . 1 1 86 86 TYR CB C 13 37.05 0.17 . 1 . . . . 86 TYR CB . 15094 1 558 . 1 1 86 86 TYR N N 15 124.39 0.39 . 1 . . . . 86 TYR N . 15094 1 559 . 1 1 87 87 GLN H H 1 8.3 0.07 . 1 . . . . 87 GLN H . 15094 1 560 . 1 1 87 87 GLN HA H 1 4.25 0.07 . 1 . . . . 87 GLN HA . 15094 1 561 . 1 1 87 87 GLN HB2 H 1 2.34 0.07 . 2 . . . . 87 GLN HB2 . 15094 1 562 . 1 1 87 87 GLN HB3 H 1 1.94 0.07 . 2 . . . . 87 GLN HB3 . 15094 1 563 . 1 1 87 87 GLN HE21 H 1 6.79 0.07 . 2 . . . . 87 GLN HE21 . 15094 1 564 . 1 1 87 87 GLN HE22 H 1 7.5 0.07 . 2 . . . . 87 GLN HE22 . 15094 1 565 . 1 1 87 87 GLN C C 13 177.19 0.16 . 1 . . . . 87 GLN C . 15094 1 566 . 1 1 87 87 GLN CA C 13 58.22 0.11 . 1 . . . . 87 GLN CA . 15094 1 567 . 1 1 87 87 GLN CB C 13 29.23 0.17 . 1 . . . . 87 GLN CB . 15094 1 568 . 1 1 87 87 GLN CG C 13 33.96 0.17 . 1 . . . . 87 GLN CG . 15094 1 569 . 1 1 87 87 GLN CD C 13 180.67 0.16 . 1 . . . . 87 GLN CD . 15094 1 570 . 1 1 87 87 GLN N N 15 120.39 0.39 . 1 . . . . 87 GLN N . 15094 1 571 . 1 1 87 87 GLN NE2 N 15 113.53 0.39 . 1 . . . . 87 GLN NE2 . 15094 1 572 . 1 1 88 88 THR H H 1 7.75 0.07 . 1 . . . . 88 THR H . 15094 1 573 . 1 1 88 88 THR HA H 1 4.28 0.07 . 1 . . . . 88 THR HA . 15094 1 574 . 1 1 88 88 THR HB H 1 3.62 0.07 . 1 . . . . 88 THR HB . 15094 1 575 . 1 1 88 88 THR HG21 H 1 -0.84 0.07 . 1 . . . . 88 THR HG2 . 15094 1 576 . 1 1 88 88 THR HG22 H 1 -0.84 0.07 . 1 . . . . 88 THR HG2 . 15094 1 577 . 1 1 88 88 THR HG23 H 1 -0.84 0.07 . 1 . . . . 88 THR HG2 . 15094 1 578 . 1 1 88 88 THR C C 13 171.31 0.16 . 1 . . . . 88 THR C . 15094 1 579 . 1 1 88 88 THR CA C 13 58.02 0.11 . 1 . . . . 88 THR CA . 15094 1 580 . 1 1 88 88 THR CB C 13 68.88 0.17 . 1 . . . . 88 THR CB . 15094 1 581 . 1 1 88 88 THR CG2 C 13 21.83 0.17 . 1 . . . . 88 THR CG2 . 15094 1 582 . 1 1 88 88 THR N N 15 112.93 0.39 . 1 . . . . 88 THR N . 15094 1 583 . 1 1 89 89 PRO HA H 1 3.89 0.07 . 1 . . . . 89 PRO HA . 15094 1 584 . 1 1 89 89 PRO C C 13 175.33 0.16 . 1 . . . . 89 PRO C . 15094 1 585 . 1 1 89 89 PRO CA C 13 61.63 0.11 . 1 . . . . 89 PRO CA . 15094 1 586 . 1 1 89 89 PRO CB C 13 30.9 0.17 . 1 . . . . 89 PRO CB . 15094 1 587 . 1 1 89 89 PRO CG C 13 27.75 0.17 . 1 . . . . 89 PRO CG . 15094 1 588 . 1 1 89 89 PRO N N 15 137.43 0.39 . 1 . . . . 89 PRO N . 15094 1 589 . 1 1 90 90 GLU H H 1 8.15 0.07 . 1 . . . . 90 GLU H . 15094 1 590 . 1 1 90 90 GLU HA H 1 4.58 0.07 . 1 . . . . 90 GLU HA . 15094 1 591 . 1 1 90 90 GLU HB2 H 1 3.03 0.07 . 1 . . . . 90 GLU HB2 . 15094 1 592 . 1 1 90 90 GLU HB3 H 1 2.88 0.07 . 1 . . . . 90 GLU HB3 . 15094 1 593 . 1 1 90 90 GLU C C 13 174.86 0.16 . 1 . . . . 90 GLU C . 15094 1 594 . 1 1 90 90 GLU CA C 13 56.46 0.11 . 1 . . . . 90 GLU CA . 15094 1 595 . 1 1 90 90 GLU N N 15 121.23 0.39 . 1 . . . . 90 GLU N . 15094 1 596 . 1 1 91 91 LEU C C 13 175.11 0.16 . 1 . . . . 91 LEU C . 15094 1 597 . 1 1 91 91 LEU CA C 13 53.52 0.11 . 1 . . . . 91 LEU CA . 15094 1 598 . 1 1 91 91 LEU CB C 13 46.02 0.17 . 1 . . . . 91 LEU CB . 15094 1 599 . 1 1 92 92 LEU H H 1 7.99 0.07 . 1 . . . . 92 LEU H . 15094 1 600 . 1 1 92 92 LEU HA H 1 4.22 0.07 . 1 . . . . 92 LEU HA . 15094 1 601 . 1 1 92 92 LEU C C 13 174.17 0.16 . 1 . . . . 92 LEU C . 15094 1 602 . 1 1 92 92 LEU CA C 13 53.28 0.11 . 1 . . . . 92 LEU CA . 15094 1 603 . 1 1 92 92 LEU CB C 13 47.48 0.17 . 1 . . . . 92 LEU CB . 15094 1 604 . 1 1 92 92 LEU N N 15 122.17 0.39 . 1 . . . . 92 LEU N . 15094 1 605 . 1 1 93 93 VAL H H 1 8.58 0.07 . 1 . . . . 93 VAL H . 15094 1 606 . 1 1 93 93 VAL HA H 1 4.71 0.07 . 1 . . . . 93 VAL HA . 15094 1 607 . 1 1 93 93 VAL C C 13 173.68 0.16 . 1 . . . . 93 VAL C . 15094 1 608 . 1 1 93 93 VAL CA C 13 61.75 0.11 . 1 . . . . 93 VAL CA . 15094 1 609 . 1 1 93 93 VAL CB C 13 32.71 0.17 . 1 . . . . 93 VAL CB . 15094 1 610 . 1 1 93 93 VAL N N 15 121.74 0.39 . 1 . . . . 93 VAL N . 15094 1 611 . 1 1 94 94 LEU H H 1 9.67 0.07 . 1 . . . . 94 LEU H . 15094 1 612 . 1 1 94 94 LEU HA H 1 5.4 0.07 . 1 . . . . 94 LEU HA . 15094 1 613 . 1 1 94 94 LEU C C 13 174.11 0.16 . 1 . . . . 94 LEU C . 15094 1 614 . 1 1 94 94 LEU CA C 13 51.77 0.11 . 1 . . . . 94 LEU CA . 15094 1 615 . 1 1 94 94 LEU N N 15 128.84 0.39 . 1 . . . . 94 LEU N . 15094 1 616 . 1 1 95 95 PRO C C 13 173.86 0.16 . 1 . . . . 95 PRO C . 15094 1 617 . 1 1 95 95 PRO CA C 13 62.44 0.11 . 1 . . . . 95 PRO CA . 15094 1 618 . 1 1 95 95 PRO CB C 13 32.41 0.17 . 1 . . . . 95 PRO CB . 15094 1 619 . 1 1 95 95 PRO N N 15 132.94 0.39 . 1 . . . . 95 PRO N . 15094 1 620 . 1 1 96 96 VAL H H 1 7.1 0.07 . 1 . . . . 96 VAL H . 15094 1 621 . 1 1 96 96 VAL C C 13 179.05 0.16 . 1 . . . . 96 VAL C . 15094 1 622 . 1 1 96 96 VAL CA C 13 60.6 0.11 . 1 . . . . 96 VAL CA . 15094 1 623 . 1 1 96 96 VAL CB C 13 32.89 0.17 . 1 . . . . 96 VAL CB . 15094 1 624 . 1 1 96 96 VAL CG1 C 13 21.46 0.17 . 1 . . . . 96 VAL CG1 . 15094 1 625 . 1 1 96 96 VAL CG2 C 13 21.46 0.17 . 1 . . . . 96 VAL CG2 . 15094 1 626 . 1 1 96 96 VAL N N 15 117.03 0.39 . 1 . . . . 96 VAL N . 15094 1 627 . 1 1 97 97 THR H H 1 8.98 0.07 . 1 . . . . 97 THR H . 15094 1 628 . 1 1 97 97 THR C C 13 175.26 0.16 . 1 . . . . 97 THR C . 15094 1 629 . 1 1 97 97 THR CA C 13 62.63 0.11 . 1 . . . . 97 THR CA . 15094 1 630 . 1 1 97 97 THR CB C 13 68.45 0.17 . 1 . . . . 97 THR CB . 15094 1 631 . 1 1 97 97 THR N N 15 120.08 0.39 . 1 . . . . 97 THR N . 15094 1 632 . 1 1 98 98 HIS H H 1 7.84 0.07 . 1 . . . . 98 HIS H . 15094 1 633 . 1 1 98 98 HIS HA H 1 4.12 0.07 . 1 . . . . 98 HIS HA . 15094 1 634 . 1 1 98 98 HIS C C 13 171.8 0.16 . 1 . . . . 98 HIS C . 15094 1 635 . 1 1 98 98 HIS CA C 13 55.69 0.11 . 1 . . . . 98 HIS CA . 15094 1 636 . 1 1 98 98 HIS CB C 13 32.95 0.17 . 1 . . . . 98 HIS CB . 15094 1 637 . 1 1 98 98 HIS N N 15 120.26 0.39 . 1 . . . . 98 HIS N . 15094 1 638 . 1 1 99 99 GLY H H 1 7.15 0.07 . 1 . . . . 99 GLY H . 15094 1 639 . 1 1 99 99 GLY HA2 H 1 3.75 0.07 . 2 . . . . 99 GLY HA2 . 15094 1 640 . 1 1 99 99 GLY HA3 H 1 4.2 0.07 . 2 . . . . 99 GLY HA3 . 15094 1 641 . 1 1 99 99 GLY C C 13 170.7 0.16 . 1 . . . . 99 GLY C . 15094 1 642 . 1 1 99 99 GLY CA C 13 44.7 0.11 . 1 . . . . 99 GLY CA . 15094 1 643 . 1 1 99 99 GLY N N 15 108.27 0.39 . 1 . . . . 99 GLY N . 15094 1 644 . 1 1 100 100 ASP H H 1 7.49 0.07 . 1 . . . . 100 ASP H . 15094 1 645 . 1 1 100 100 ASP C C 13 176.53 0.16 . 1 . . . . 100 ASP C . 15094 1 646 . 1 1 100 100 ASP CA C 13 54.56 0.11 . 1 . . . . 100 ASP CA . 15094 1 647 . 1 1 100 100 ASP CB C 13 45.98 0.17 . 1 . . . . 100 ASP CB . 15094 1 648 . 1 1 100 100 ASP N N 15 119.72 0.39 . 1 . . . . 100 ASP N . 15094 1 649 . 1 1 101 101 THR H H 1 8.79 0.07 . 1 . . . . 101 THR H . 15094 1 650 . 1 1 101 101 THR HB H 1 4.17 0.07 . 1 . . . . 101 THR HB . 15094 1 651 . 1 1 101 101 THR C C 13 176.44 0.16 . 1 . . . . 101 THR C . 15094 1 652 . 1 1 101 101 THR CA C 13 66.54 0.11 . 1 . . . . 101 THR CA . 15094 1 653 . 1 1 101 101 THR CB C 13 68.67 0.17 . 1 . . . . 101 THR CB . 15094 1 654 . 1 1 101 101 THR CG2 C 13 21.94 0.17 . 1 . . . . 101 THR CG2 . 15094 1 655 . 1 1 101 101 THR N N 15 123.67 0.39 . 1 . . . . 101 THR N . 15094 1 656 . 1 1 102 102 ASP H H 1 8.14 0.07 . 1 . . . . 102 ASP H . 15094 1 657 . 1 1 102 102 ASP C C 13 179.12 0.16 . 1 . . . . 102 ASP C . 15094 1 658 . 1 1 102 102 ASP CA C 13 57.62 0.11 . 1 . . . . 102 ASP CA . 15094 1 659 . 1 1 102 102 ASP CB C 13 40.25 0.17 . 1 . . . . 102 ASP CB . 15094 1 660 . 1 1 102 102 ASP CG C 13 179.59 0.16 . 1 . . . . 102 ASP CG . 15094 1 661 . 1 1 102 102 ASP N N 15 123.52 0.39 . 1 . . . . 102 ASP N . 15094 1 662 . 1 1 103 103 TYR H H 1 8.67 0.07 . 1 . . . . 103 TYR H . 15094 1 663 . 1 1 103 103 TYR HA H 1 3.82 0.07 . 1 . . . . 103 TYR HA . 15094 1 664 . 1 1 103 103 TYR C C 13 177.35 0.16 . 1 . . . . 103 TYR C . 15094 1 665 . 1 1 103 103 TYR CA C 13 63.03 0.11 . 1 . . . . 103 TYR CA . 15094 1 666 . 1 1 103 103 TYR CB C 13 38.24 0.17 . 1 . . . . 103 TYR CB . 15094 1 667 . 1 1 103 103 TYR N N 15 125.42 0.39 . 1 . . . . 103 TYR N . 15094 1 668 . 1 1 104 104 LEU H H 1 8.71 0.07 . 1 . . . . 104 LEU H . 15094 1 669 . 1 1 104 104 LEU C C 13 180.34 0.16 . 1 . . . . 104 LEU C . 15094 1 670 . 1 1 104 104 LEU CA C 13 58.06 0.11 . 1 . . . . 104 LEU CA . 15094 1 671 . 1 1 104 104 LEU CB C 13 40.7 0.17 . 1 . . . . 104 LEU CB . 15094 1 672 . 1 1 104 104 LEU N N 15 118.6 0.39 . 1 . . . . 104 LEU N . 15094 1 673 . 1 1 105 105 SER H H 1 8.35 0.07 . 1 . . . . 105 SER H . 15094 1 674 . 1 1 105 105 SER C C 13 176.74 0.16 . 1 . . . . 105 SER C . 15094 1 675 . 1 1 105 105 SER CA C 13 61.85 0.11 . 1 . . . . 105 SER CA . 15094 1 676 . 1 1 105 105 SER CB C 13 66.95 0.17 . 1 . . . . 105 SER CB . 15094 1 677 . 1 1 105 105 SER N N 15 117.03 0.39 . 1 . . . . 105 SER N . 15094 1 678 . 1 1 106 106 TRP H H 1 7.95 0.07 . 1 . . . . 106 TRP H . 15094 1 679 . 1 1 106 106 TRP HA H 1 4.13 0.07 . 1 . . . . 106 TRP HA . 15094 1 680 . 1 1 106 106 TRP HB2 H 1 3.396 0.07 . 2 . . . . 106 TRP HB2 . 15094 1 681 . 1 1 106 106 TRP HB3 H 1 3.155 0.07 . 2 . . . . 106 TRP HB3 . 15094 1 682 . 1 1 106 106 TRP HD1 H 1 7.22 0.07 . 1 . . . . 106 TRP HD1 . 15094 1 683 . 1 1 106 106 TRP HE1 H 1 9.9 0.07 . 1 . . . . 106 TRP HE1 . 15094 1 684 . 1 1 106 106 TRP HZ2 H 1 7.57 0.07 . 1 . . . . 106 TRP HZ2 . 15094 1 685 . 1 1 106 106 TRP HH2 H 1 6.99 0.07 . 1 . . . . 106 TRP HH2 . 15094 1 686 . 1 1 106 106 TRP C C 13 178.28 0.16 . 1 . . . . 106 TRP C . 15094 1 687 . 1 1 106 106 TRP CA C 13 61.71 0.11 . 1 . . . . 106 TRP CA . 15094 1 688 . 1 1 106 106 TRP CB C 13 27.5 0.17 . 1 . . . . 106 TRP CB . 15094 1 689 . 1 1 106 106 TRP N N 15 126.3 0.39 . 1 . . . . 106 TRP N . 15094 1 690 . 1 1 106 106 TRP NE1 N 15 131.01 0.39 . 1 . . . . 106 TRP NE1 . 15094 1 691 . 1 1 107 107 LEU H H 1 8.56 0.07 . 1 . . . . 107 LEU H . 15094 1 692 . 1 1 107 107 LEU HA H 1 4.15 0.07 . 1 . . . . 107 LEU HA . 15094 1 693 . 1 1 107 107 LEU HB2 H 1 2.12 0.07 . 2 . . . . 107 LEU HB2 . 15094 1 694 . 1 1 107 107 LEU HB3 H 1 1.83 0.07 . 2 . . . . 107 LEU HB3 . 15094 1 695 . 1 1 107 107 LEU C C 13 178.21 0.16 . 1 . . . . 107 LEU C . 15094 1 696 . 1 1 107 107 LEU CA C 13 58.5 0.11 . 1 . . . . 107 LEU CA . 15094 1 697 . 1 1 107 107 LEU CB C 13 42.21 0.17 . 1 . . . . 107 LEU CB . 15094 1 698 . 1 1 107 107 LEU N N 15 123.73 0.39 . 1 . . . . 107 LEU N . 15094 1 699 . 1 1 108 108 ASN H H 1 7.55 0.07 . 1 . . . . 108 ASN H . 15094 1 700 . 1 1 108 108 ASN HD21 H 1 6.97 0.07 . 2 . . . . 108 ASN HD21 . 15094 1 701 . 1 1 108 108 ASN HD22 H 1 7.39 0.07 . 2 . . . . 108 ASN HD22 . 15094 1 702 . 1 1 108 108 ASN C C 13 178.11 0.16 . 1 . . . . 108 ASN C . 15094 1 703 . 1 1 108 108 ASN CA C 13 56.66 0.11 . 1 . . . . 108 ASN CA . 15094 1 704 . 1 1 108 108 ASN CB C 13 39.57 0.17 . 1 . . . . 108 ASN CB . 15094 1 705 . 1 1 108 108 ASN CG C 13 176.34 0.16 . 1 . . . . 108 ASN CG . 15094 1 706 . 1 1 108 108 ASN N N 15 114.75 0.39 . 1 . . . . 108 ASN N . 15094 1 707 . 1 1 108 108 ASN ND2 N 15 112.72 0.39 . 1 . . . . 108 ASN ND2 . 15094 1 708 . 1 1 109 109 ALA H H 1 8.17 0.07 . 1 . . . . 109 ALA H . 15094 1 709 . 1 1 109 109 ALA HA H 1 4.07 0.07 . 1 . . . . 109 ALA HA . 15094 1 710 . 1 1 109 109 ALA HB1 H 1 0.85 0.07 . 1 . . . . 109 ALA HB . 15094 1 711 . 1 1 109 109 ALA HB2 H 1 0.85 0.07 . 1 . . . . 109 ALA HB . 15094 1 712 . 1 1 109 109 ALA HB3 H 1 0.85 0.07 . 1 . . . . 109 ALA HB . 15094 1 713 . 1 1 109 109 ALA C C 13 179.78 0.16 . 1 . . . . 109 ALA C . 15094 1 714 . 1 1 109 109 ALA CA C 13 54.5 0.11 . 1 . . . . 109 ALA CA . 15094 1 715 . 1 1 109 109 ALA CB C 13 17.94 0.17 . 1 . . . . 109 ALA CB . 15094 1 716 . 1 1 109 109 ALA N N 15 122.25 0.39 . 1 . . . . 109 ALA N . 15094 1 717 . 1 1 110 110 SER H H 1 7.56 0.07 . 1 . . . . 110 SER H . 15094 1 718 . 1 1 110 110 SER C C 13 173.7 0.16 . 1 . . . . 110 SER C . 15094 1 719 . 1 1 110 110 SER CA C 13 60.6 0.11 . 1 . . . . 110 SER CA . 15094 1 720 . 1 1 110 110 SER CB C 13 63.09 0.17 . 1 . . . . 110 SER CB . 15094 1 721 . 1 1 110 110 SER N N 15 114.05 0.39 . 1 . . . . 110 SER N . 15094 1 722 . 1 1 111 111 LEU H H 1 6.69 0.07 . 1 . . . . 111 LEU H . 15094 1 723 . 1 1 111 111 LEU HA H 1 4.69 0.07 . 1 . . . . 111 LEU HA . 15094 1 724 . 1 1 111 111 LEU C C 13 176.31 0.16 . 1 . . . . 111 LEU C . 15094 1 725 . 1 1 111 111 LEU CA C 13 53.56 0.11 . 1 . . . . 111 LEU CA . 15094 1 726 . 1 1 111 111 LEU CB C 13 42.06 0.17 . 1 . . . . 111 LEU CB . 15094 1 727 . 1 1 111 111 LEU N N 15 119.08 0.39 . 1 . . . . 111 LEU N . 15094 1 728 . 1 1 112 112 ARG H H 1 7.44 0.07 . 1 . . . . 112 ARG H . 15094 1 729 . 1 1 112 112 ARG CA C 13 58.45 0.11 . 1 . . . . 112 ARG CA . 15094 1 730 . 1 1 112 112 ARG N N 15 125.8 0.39 . 1 . . . . 112 ARG N . 15094 1 stop_ save_