data_4293 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4293 _Entry.Title ; Assignment of 1H, 13C and 15N Signals of the DNase Domain of Colicin E9 ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-01-12 _Entry.Accession_date 1999-01-19 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Sara Whittaker . . . 4293 2 Ruth Boetzel . . . 4293 3 Colin MacDonald . . . 4293 4 Lu-Yun Lian . . . 4293 5 Richard James . . . 4293 6 Colin Kleanthous . . . 4293 7 Geoffrey Moore . . . 4293 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 4293 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 460 4293 '15N chemical shifts' 161 4293 '1H chemical shifts' 580 4293 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 . . 1999-03-09 . original author 'original release' 4293 1 . . 2006-10-27 . update BMRB 'update the relationship loop' 4293 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4115 'homologous Immunity protein Im9 bound to DNase domain of colicin E9' 4293 BMRB 4116 'homologous Immunity protein Im9' 4293 BMRB 4352 'Im9 bound DNase domain of non cognate binding partner E9' 4293 BMRB 7323 'Colicin immunity protein IM2' 4293 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4293 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Whittaker, S. B.-M., Boetzel, R., MacDonald, C. J., Lian, L-Y., James, R., Kleanthous, C., and Moore, G. R., "Assignment of 1H, 13C and 15N Signals of the DNase Domain of Colicin E9," J. Biomol. NMR in preparation. ; _Citation.Title 'Assignment of 1H, 13C and 15N Signals of the DNase Domain of Colicin E9' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _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 Sara Whittaker . . . 4293 1 2 Ruth Boetzel . . . 4293 1 3 Colin MacDonald . . . 4293 1 4 Lu-Yun Lian . . . 4293 1 5 Richard James . . . 4293 1 6 Colin Kleanthous . . . 4293 1 7 Geoffrey Moore . . . 4293 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'chemical exchange' 4293 1 colicin 4293 1 EXSY 4293 1 stop_ save_ save_ref-1 _Citation.Sf_category citations _Citation.Sf_framecode ref-1 _Citation.Entry_ID 4293 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. J. Biomol. NMR 6, 277-293 (1995) ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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 F. Delaglio F. . . 4293 2 2 S. Grzesiek S. . . 4293 2 3 'G. W.' Vuister G. W. . 4293 2 4 G. Zhu G. . . 4293 2 5 J. Pfeifer J. . . 4293 2 6 A. Bax A. . . 4293 2 stop_ save_ save_ref-2 _Citation.Sf_category citations _Citation.Sf_framecode ref-2 _Citation.Entry_ID 4293 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Bartels, C., Xia, T.-H., Billeter, M., Guentert, P. & Wuethrich, K. J. Biomol. NMR 6, 1-10 (1995). ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref-3 _Citation.Sf_category citations _Citation.Sf_framecode ref-3 _Citation.Entry_ID 4293 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 2646600 _Citation.Full_citation 'Eaton, T. & James, R. Nucleic Acids Res. 17, 1761-1761 (1989).' _Citation.Title 'Complete nucleotide sequence of the colicin E9 (cei) gene.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Nucleic Acids Res.' _Citation.Journal_name_full 'Nucleic acids research' _Citation.Journal_volume 17 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0305-1048 _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 1761 _Citation.Page_last 1761 _Citation.Year 1989 _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 T. Eaton T. . . 4293 4 2 R. James R. . . 4293 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_E9_DNase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_E9_DNase _Assembly.Entry_ID 4293 _Assembly.ID 1 _Assembly.Name 'DNase domain of colicin E9' _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 no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.1.21.1 _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4293 1 stop_ 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 major_E9_DNase 1 $E9_DNase . . . native . . . . . 4293 1 2 minor_E9_DNase 1 $E9_DNase . . . native . . . . . 4293 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'DNase domain of colicin E9' system 4293 1 'E9 DNase' abbreviation 4293 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; The E9 DNase forms the cytotoxic domain of colicin E9 and is located at its C-terminus (the last 134 residues). It acts as an endonuclease and is active on both single- and double-stranded DNA but with undefined specificity. Colicins are plasmid-encoded protein antibiotics produced by, and active against, Eschericia coli and closely related bacteria. ; 4293 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_E9_DNase _Entity.Sf_category entity _Entity.Sf_framecode E9_DNase _Entity.Entry_ID 4293 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'DNase domain of colicin E9' _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 ; MESKRNKPGKATGKGKPVGD KWLDDAGKDSGAPIPDRIAD KLRDKEFKSFDDFRKAVWEE VSKDPELSKNLNPSNKSSVS KGYSPFTPKNQQVGGRKVYE LHHDKPISQGGEVYDMDNIR VTTPKRHIDIHRGK ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 134 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 15090 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; E9 DNase exists as two conformers in solution (60:40) that undergo slow chemical exchange. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 4352 . "DNase domain of colicin E9" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 2 no PDB 1BXI . "Crystal Structure Of The Escherichia Coli Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" . . . . . 99.25 134 99.25 99.25 1.43e-88 . . . . 4293 1 3 no PDB 1EMV . "Crystal Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9 (1.7 Angstroms)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 4 no PDB 1FR2 . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9(E41a)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 5 no PDB 1FSJ . "Crystal Structure Of The E9 Dnase Domain" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 6 no PDB 1V13 . "Crystal Structure Of The Mutant His103ala Of The Colicin E9 Dnase Domain In Complex With Zn+2 (2.0 Angstroms)" . . . . . 100.00 134 99.25 99.25 1.21e-89 . . . . 4293 1 7 no PDB 1V14 . "Crystal Structure Of The Colicin E9, Mutant His103ala, In Complex With Mg+2 And Dsdna (Resolution 2.9a)" . . . . . 100.00 134 99.25 99.25 1.21e-89 . . . . 4293 1 8 no PDB 1V15 . "Crystal Structure Of The Colicin E9, Mutant His103ala, In Complex With Zn+2 And Dsdna (Resolution 2.4a)" . . . . . 100.00 134 99.25 99.25 1.21e-89 . . . . 4293 1 9 no PDB 2GYK . "Crystal Structure Of The Complex Of The Colicin E9 Dnase Domain With A Mutant Immunity Protein, Imme9 (D51a)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 10 no PDB 2GZE . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55a)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 11 no PDB 2GZF . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y54f)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 12 no PDB 2GZG . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (Y55f)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 13 no PDB 2GZI . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (V34a)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 14 no PDB 2GZJ . "Crystal Structure Of The E9 Dnase Domain With A Mutant Immunity Protein Im9 (D51a)" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 15 no PDB 2K5X . "Chemical Shift Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9" . . . . . 100.00 134 100.00 100.00 7.73e-91 . . . . 4293 1 16 no PDB 2VLN . "N75a Mutant Of E9 Dnase Domain In Complex With Im9" . . . . . 100.00 134 99.25 99.25 7.57e-90 . . . . 4293 1 17 no PDB 2VLO . "K97a Mutant Of E9 Dnase Domain In Complex With Im9" . . . . . 100.00 134 99.25 99.25 3.27e-90 . . . . 4293 1 18 no PDB 2VLP . "R54a Mutant Of E9 Dnase Domain In Complex With Im9" . . . . . 100.00 134 99.25 99.25 6.94e-90 . . . . 4293 1 19 no PDB 2VLQ . "F86a Mutant Of E9 Dnase Domain In Complex With Im9" . . . . . 100.00 134 99.25 99.25 1.12e-89 . . . . 4293 1 20 no PDB 2WPT . "The Crystal Structure Of Im2 In Complex With Colicin E9 Dnase" . . . . . 100.00 134 99.25 99.25 5.17e-90 . . . . 4293 1 21 no EMBL CAA31104 . "colicin E9 [Escherichia coli str. K-12 substr. W3110]" . . . . . 99.25 582 100.00 100.00 9.43e-87 . . . . 4293 1 22 no EMBL CAA33862 . "colcinin E9 C-terminal fragment [Plasmid ColE9-J]" . . . . . 99.25 205 100.00 100.00 7.73e-91 . . . . 4293 1 23 no GB ACM07430 . "colicin E9 [Escherichia coli]" . . . . . 99.25 582 100.00 100.00 9.43e-87 . . . . 4293 1 24 no PRF 1615299E . "colicin E9" . . . . . 99.25 205 99.25 99.25 7.23e-90 . . . . 4293 1 25 no REF WP_012644886 . "colicin E9 [Escherichia coli]" . . . . . 99.25 582 100.00 100.00 9.43e-87 . . . . 4293 1 26 no REF WP_044860894 . "colicin [Escherichia coli]" . . . . . 99.25 581 100.00 100.00 1.51e-86 . . . . 4293 1 27 no REF YP_002533537 . "colicin E9 [Escherichia coli]" . . . . . 99.25 582 100.00 100.00 9.43e-87 . . . . 4293 1 28 no SP P09883 . "RecName: Full=Colicin-E9" . . . . . 99.25 582 100.00 100.00 9.43e-87 . . . . 4293 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'DNase domain of colicin E9' common 4293 1 'E9 DNase' abbreviation 4293 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 . 4293 1 2 . GLU . 4293 1 3 . SER . 4293 1 4 . LYS . 4293 1 5 . ARG . 4293 1 6 . ASN . 4293 1 7 . LYS . 4293 1 8 . PRO . 4293 1 9 . GLY . 4293 1 10 . LYS . 4293 1 11 . ALA . 4293 1 12 . THR . 4293 1 13 . GLY . 4293 1 14 . LYS . 4293 1 15 . GLY . 4293 1 16 . LYS . 4293 1 17 . PRO . 4293 1 18 . VAL . 4293 1 19 . GLY . 4293 1 20 . ASP . 4293 1 21 . LYS . 4293 1 22 . TRP . 4293 1 23 . LEU . 4293 1 24 . ASP . 4293 1 25 . ASP . 4293 1 26 . ALA . 4293 1 27 . GLY . 4293 1 28 . LYS . 4293 1 29 . ASP . 4293 1 30 . SER . 4293 1 31 . GLY . 4293 1 32 . ALA . 4293 1 33 . PRO . 4293 1 34 . ILE . 4293 1 35 . PRO . 4293 1 36 . ASP . 4293 1 37 . ARG . 4293 1 38 . ILE . 4293 1 39 . ALA . 4293 1 40 . ASP . 4293 1 41 . LYS . 4293 1 42 . LEU . 4293 1 43 . ARG . 4293 1 44 . ASP . 4293 1 45 . LYS . 4293 1 46 . GLU . 4293 1 47 . PHE . 4293 1 48 . LYS . 4293 1 49 . SER . 4293 1 50 . PHE . 4293 1 51 . ASP . 4293 1 52 . ASP . 4293 1 53 . PHE . 4293 1 54 . ARG . 4293 1 55 . LYS . 4293 1 56 . ALA . 4293 1 57 . VAL . 4293 1 58 . TRP . 4293 1 59 . GLU . 4293 1 60 . GLU . 4293 1 61 . VAL . 4293 1 62 . SER . 4293 1 63 . LYS . 4293 1 64 . ASP . 4293 1 65 . PRO . 4293 1 66 . GLU . 4293 1 67 . LEU . 4293 1 68 . SER . 4293 1 69 . LYS . 4293 1 70 . ASN . 4293 1 71 . LEU . 4293 1 72 . ASN . 4293 1 73 . PRO . 4293 1 74 . SER . 4293 1 75 . ASN . 4293 1 76 . LYS . 4293 1 77 . SER . 4293 1 78 . SER . 4293 1 79 . VAL . 4293 1 80 . SER . 4293 1 81 . LYS . 4293 1 82 . GLY . 4293 1 83 . TYR . 4293 1 84 . SER . 4293 1 85 . PRO . 4293 1 86 . PHE . 4293 1 87 . THR . 4293 1 88 . PRO . 4293 1 89 . LYS . 4293 1 90 . ASN . 4293 1 91 . GLN . 4293 1 92 . GLN . 4293 1 93 . VAL . 4293 1 94 . GLY . 4293 1 95 . GLY . 4293 1 96 . ARG . 4293 1 97 . LYS . 4293 1 98 . VAL . 4293 1 99 . TYR . 4293 1 100 . GLU . 4293 1 101 . LEU . 4293 1 102 . HIS . 4293 1 103 . HIS . 4293 1 104 . ASP . 4293 1 105 . LYS . 4293 1 106 . PRO . 4293 1 107 . ILE . 4293 1 108 . SER . 4293 1 109 . GLN . 4293 1 110 . GLY . 4293 1 111 . GLY . 4293 1 112 . GLU . 4293 1 113 . VAL . 4293 1 114 . TYR . 4293 1 115 . ASP . 4293 1 116 . MET . 4293 1 117 . ASP . 4293 1 118 . ASN . 4293 1 119 . ILE . 4293 1 120 . ARG . 4293 1 121 . VAL . 4293 1 122 . THR . 4293 1 123 . THR . 4293 1 124 . PRO . 4293 1 125 . LYS . 4293 1 126 . ARG . 4293 1 127 . HIS . 4293 1 128 . ILE . 4293 1 129 . ASP . 4293 1 130 . ILE . 4293 1 131 . HIS . 4293 1 132 . ARG . 4293 1 133 . GLY . 4293 1 134 . LYS . 4293 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 4293 1 . GLU 2 2 4293 1 . SER 3 3 4293 1 . LYS 4 4 4293 1 . ARG 5 5 4293 1 . ASN 6 6 4293 1 . LYS 7 7 4293 1 . PRO 8 8 4293 1 . GLY 9 9 4293 1 . LYS 10 10 4293 1 . ALA 11 11 4293 1 . THR 12 12 4293 1 . GLY 13 13 4293 1 . LYS 14 14 4293 1 . GLY 15 15 4293 1 . LYS 16 16 4293 1 . PRO 17 17 4293 1 . VAL 18 18 4293 1 . GLY 19 19 4293 1 . ASP 20 20 4293 1 . LYS 21 21 4293 1 . TRP 22 22 4293 1 . LEU 23 23 4293 1 . ASP 24 24 4293 1 . ASP 25 25 4293 1 . ALA 26 26 4293 1 . GLY 27 27 4293 1 . LYS 28 28 4293 1 . ASP 29 29 4293 1 . SER 30 30 4293 1 . GLY 31 31 4293 1 . ALA 32 32 4293 1 . PRO 33 33 4293 1 . ILE 34 34 4293 1 . PRO 35 35 4293 1 . ASP 36 36 4293 1 . ARG 37 37 4293 1 . ILE 38 38 4293 1 . ALA 39 39 4293 1 . ASP 40 40 4293 1 . LYS 41 41 4293 1 . LEU 42 42 4293 1 . ARG 43 43 4293 1 . ASP 44 44 4293 1 . LYS 45 45 4293 1 . GLU 46 46 4293 1 . PHE 47 47 4293 1 . LYS 48 48 4293 1 . SER 49 49 4293 1 . PHE 50 50 4293 1 . ASP 51 51 4293 1 . ASP 52 52 4293 1 . PHE 53 53 4293 1 . ARG 54 54 4293 1 . LYS 55 55 4293 1 . ALA 56 56 4293 1 . VAL 57 57 4293 1 . TRP 58 58 4293 1 . GLU 59 59 4293 1 . GLU 60 60 4293 1 . VAL 61 61 4293 1 . SER 62 62 4293 1 . LYS 63 63 4293 1 . ASP 64 64 4293 1 . PRO 65 65 4293 1 . GLU 66 66 4293 1 . LEU 67 67 4293 1 . SER 68 68 4293 1 . LYS 69 69 4293 1 . ASN 70 70 4293 1 . LEU 71 71 4293 1 . ASN 72 72 4293 1 . PRO 73 73 4293 1 . SER 74 74 4293 1 . ASN 75 75 4293 1 . LYS 76 76 4293 1 . SER 77 77 4293 1 . SER 78 78 4293 1 . VAL 79 79 4293 1 . SER 80 80 4293 1 . LYS 81 81 4293 1 . GLY 82 82 4293 1 . TYR 83 83 4293 1 . SER 84 84 4293 1 . PRO 85 85 4293 1 . PHE 86 86 4293 1 . THR 87 87 4293 1 . PRO 88 88 4293 1 . LYS 89 89 4293 1 . ASN 90 90 4293 1 . GLN 91 91 4293 1 . GLN 92 92 4293 1 . VAL 93 93 4293 1 . GLY 94 94 4293 1 . GLY 95 95 4293 1 . ARG 96 96 4293 1 . LYS 97 97 4293 1 . VAL 98 98 4293 1 . TYR 99 99 4293 1 . GLU 100 100 4293 1 . LEU 101 101 4293 1 . HIS 102 102 4293 1 . HIS 103 103 4293 1 . ASP 104 104 4293 1 . LYS 105 105 4293 1 . PRO 106 106 4293 1 . ILE 107 107 4293 1 . SER 108 108 4293 1 . GLN 109 109 4293 1 . GLY 110 110 4293 1 . GLY 111 111 4293 1 . GLU 112 112 4293 1 . VAL 113 113 4293 1 . TYR 114 114 4293 1 . ASP 115 115 4293 1 . MET 116 116 4293 1 . ASP 117 117 4293 1 . ASN 118 118 4293 1 . ILE 119 119 4293 1 . ARG 120 120 4293 1 . VAL 121 121 4293 1 . THR 122 122 4293 1 . THR 123 123 4293 1 . PRO 124 124 4293 1 . LYS 125 125 4293 1 . ARG 126 126 4293 1 . HIS 127 127 4293 1 . ILE 128 128 4293 1 . ASP 129 129 4293 1 . ILE 130 130 4293 1 . HIS 131 131 4293 1 . ARG 132 132 4293 1 . GLY 133 133 4293 1 . LYS 134 134 4293 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 4293 _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 $E9_DNase . 562 organism . 'Escherichia coli' 'E. coli' . . Eubacteria . Escherichia coli BL21(DE3) . . . . . . . . . . . . . pRJ353 . . . . . . 4293 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 4293 _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 $E9_DNase . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . pRJ353 . . . . . . 4293 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4293 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'DNase domain of colicin E9' '[U-99% 13C; U-99% 15N]' . . 1 $E9_DNase . . 2.0 . . mM . . . . 4293 1 2 'sodium phosphate' . . . . . . . 25.0 . . mM . . . . 4293 1 3 H20 . . . . . . . 90 . . % . . . . 4293 1 4 D20 . . . . . . . 10 . . % . . . . 4293 1 5 'sodium azide' . . . . . . . 0.01 . . % . . . . 4293 1 stop_ save_ save_sample_two _Sample.Sf_category sample _Sample.Sf_framecode sample_two _Sample.Entry_ID 4293 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _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 'DNase domain of colicin E9' '[U-99% 15N]' . . 1 $E9_DNase . . 1.5 . . mM . . . . 4293 2 2 'sodium phosphate' . . . . . . . 50 . . mM . . . . 4293 2 3 H20 . . . . . . . 90 . . % . . . . 4293 2 4 D20 . . . . . . . 10 . . % . . . . 4293 2 5 'sodium azide' . . . . . . . 0.01 . . % . . . . 4293 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_one _Sample_condition_list.Entry_ID 4293 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.2 0.2 na 4293 1 temperature 293 1 K 4293 1 stop_ save_ ############################ # Computer software used # ############################ save_software_one _Software.Sf_category software _Software.Sf_framecode software_one _Software.Entry_ID 4293 _Software.ID 1 _Software.Name FELIX _Software.Version 95.0 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID ; Processing triple resonance data and peak-picking. FELIX ASSIGN: initial semi-automated assignment. In-house developed user macros for data processing. ; 4293 1 stop_ save_ save_software_two _Software.Sf_category software _Software.Sf_framecode software_two _Software.Entry_ID 4293 _Software.ID 2 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Processing 3D NOESY and TOCSY and 2D HSQC' 4293 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $ref-1 4293 2 stop_ save_ save_software_three _Software.Sf_category software _Software.Sf_framecode software_three _Software.Entry_ID 4293 _Software.ID 3 _Software.Name XEASY _Software.Version 1.2 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID ; Defining strips for 3D NOESY to aid sequential assignment. ; 4293 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref-2 4293 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4293 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_two _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_two _NMR_spectrometer.Entry_ID 4293 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4293 _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 NMR_spectrometer_one Varian INOVA . 600 . . . 4293 1 2 NMR_spectrometer_two Bruker DMX . 500 . . . 4293 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 4293 _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 '1H-15N HSQC' . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 2 '1H-15N NOESY-HSQC' . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 3 '1H-15N TOCSY-HSQC' . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 4 HNCO . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 5 HNCA . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 6 HN(CO)CA . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 7 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 8 CBCANH . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 9 HBHA(CBCACO)NH . . . . . . . . . . . . . . . . 1 $sample_conditions_one . . . . . . . . . . . . . . . . . . . . . 4293 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-15N NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-15N TOCSY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name CBCANH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 4293 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name HBHA(CBCACO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_one _Chem_shift_reference.Entry_ID 4293 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 TSP 'methyl protons' . . . . ppm 0.00 external indirect 0.25144954 External_in_the_sample cylindrical parallel_to_Bo . . . . . . 4293 1 H 1 Dioxane 'methylene protons' . . . . ppm 3.77 internal direct 1.00000000 internal cylindrical parallel_to_Bo . . . . . . 4293 1 N 15 TSP 'methyl protons' . . . . ppm 0.00 external indirect 0.10132900 External_in_the_sample cylindrical parallel_to_Bo . . . . . . 4293 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_chemical_shift_assignments_for_major_conformer_of_E9_DNase _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignments_for_major_conformer_of_E9_DNase _Assigned_chem_shift_list.Entry_ID 4293 _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_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _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 ; Assignments refer to the major conformational species of E9 DNase. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4293 1 . . 2 $sample_two . 4293 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 GLU HA H 1 4.42 . . 1 . . . . . . . . 4293 1 2 . 1 1 2 2 GLU HB2 H 1 2.02 . . 2 . . . . . . . . 4293 1 3 . 1 1 2 2 GLU C C 13 175.97 . . 1 . . . . . . . . 4293 1 4 . 1 1 2 2 GLU CA C 13 55.24 . . 1 . . . . . . . . 4293 1 5 . 1 1 2 2 GLU CB C 13 29.87 . . 1 . . . . . . . . 4293 1 6 . 1 1 3 3 SER H H 1 8.66 . . 1 . . . . . . . . 4293 1 7 . 1 1 3 3 SER HA H 1 4.45 . . 1 . . . . . . . . 4293 1 8 . 1 1 3 3 SER HB2 H 1 3.90 . . 2 . . . . . . . . 4293 1 9 . 1 1 3 3 SER C C 13 175.49 . . 1 . . . . . . . . 4293 1 10 . 1 1 3 3 SER CA C 13 57.19 . . 1 . . . . . . . . 4293 1 11 . 1 1 3 3 SER CB C 13 62.15 . . 1 . . . . . . . . 4293 1 12 . 1 1 3 3 SER N N 15 118.6 . . 1 . . . . . . . . 4293 1 13 . 1 1 4 4 LYS H H 1 8.65 . . 1 . . . . . . . . 4293 1 14 . 1 1 4 4 LYS HA H 1 4.17 . . 1 . . . . . . . . 4293 1 15 . 1 1 4 4 LYS HB2 H 1 1.75 . . 2 . . . . . . . . 4293 1 16 . 1 1 4 4 LYS C C 13 177.25 . . 1 . . . . . . . . 4293 1 17 . 1 1 4 4 LYS CA C 13 56.88 . . 1 . . . . . . . . 4293 1 18 . 1 1 4 4 LYS CB C 13 31.86 . . 1 . . . . . . . . 4293 1 19 . 1 1 4 4 LYS N N 15 124.2 . . 1 . . . . . . . . 4293 1 20 . 1 1 5 5 ARG H H 1 8.21 . . 1 . . . . . . . . 4293 1 21 . 1 1 5 5 ARG HA H 1 4.10 . . 1 . . . . . . . . 4293 1 22 . 1 1 5 5 ARG HB2 H 1 1.75 . . 2 . . . . . . . . 4293 1 23 . 1 1 5 5 ARG HG2 H 1 1.50 . . 2 . . . . . . . . 4293 1 24 . 1 1 5 5 ARG C C 13 175.35 . . 1 . . . . . . . . 4293 1 25 . 1 1 5 5 ARG CA C 13 55.76 . . 1 . . . . . . . . 4293 1 26 . 1 1 5 5 ARG CB C 13 29.61 . . 1 . . . . . . . . 4293 1 27 . 1 1 5 5 ARG N N 15 119.0 . . 1 . . . . . . . . 4293 1 28 . 1 1 6 6 ASN H H 1 8.07 . . 1 . . . . . . . . 4293 1 29 . 1 1 6 6 ASN HA H 1 4.93 . . 1 . . . . . . . . 4293 1 30 . 1 1 6 6 ASN HB2 H 1 3.09 . . 1 . . . . . . . . 4293 1 31 . 1 1 6 6 ASN HB3 H 1 2.79 . . 1 . . . . . . . . 4293 1 32 . 1 1 6 6 ASN HD21 H 1 6.99 . . 1 . . . . . . . . 4293 1 33 . 1 1 6 6 ASN HD22 H 1 7.69 . . 1 . . . . . . . . 4293 1 34 . 1 1 6 6 ASN C C 13 173.62 . . 1 . . . . . . . . 4293 1 35 . 1 1 6 6 ASN CA C 13 51.46 . . 1 . . . . . . . . 4293 1 36 . 1 1 6 6 ASN CB C 13 37.90 . . 1 . . . . . . . . 4293 1 37 . 1 1 6 6 ASN CG C 13 177.00 . . 1 . . . . . . . . 4293 1 38 . 1 1 6 6 ASN N N 15 118.2 . . 1 . . . . . . . . 4293 1 39 . 1 1 6 6 ASN ND2 N 15 113.4 . . 1 . . . . . . . . 4293 1 40 . 1 1 7 7 LYS H H 1 7.75 . . 1 . . . . . . . . 4293 1 41 . 1 1 7 7 LYS HA H 1 4.89 . . 1 . . . . . . . . 4293 1 42 . 1 1 7 7 LYS HB2 H 1 1.98 . . 1 . . . . . . . . 4293 1 43 . 1 1 7 7 LYS HB3 H 1 1.82 . . 1 . . . . . . . . 4293 1 44 . 1 1 7 7 LYS HG2 H 1 1.96 . . 2 . . . . . . . . 4293 1 45 . 1 1 7 7 LYS HD2 H 1 1.80 . . 2 . . . . . . . . 4293 1 46 . 1 1 7 7 LYS CA C 13 55.22 . . 1 . . . . . . . . 4293 1 47 . 1 1 7 7 LYS CB C 13 32.56 . . 1 . . . . . . . . 4293 1 48 . 1 1 7 7 LYS N N 15 121.7 . . 1 . . . . . . . . 4293 1 49 . 1 1 8 8 PRO HA H 1 4.93 . . 1 . . . . . . . . 4293 1 50 . 1 1 8 8 PRO HB2 H 1 2.38 . . 1 . . . . . . . . 4293 1 51 . 1 1 8 8 PRO HB3 H 1 1.90 . . 1 . . . . . . . . 4293 1 52 . 1 1 8 8 PRO C C 13 176.82 . . 1 . . . . . . . . 4293 1 53 . 1 1 8 8 PRO CA C 13 61.67 . . 1 . . . . . . . . 4293 1 54 . 1 1 8 8 PRO CB C 13 32.38 . . 1 . . . . . . . . 4293 1 55 . 1 1 9 9 GLY H H 1 8.32 . . 1 . . . . . . . . 4293 1 56 . 1 1 9 9 GLY HA2 H 1 4.16 . . 1 . . . . . . . . 4293 1 57 . 1 1 9 9 GLY HA3 H 1 3.80 . . 1 . . . . . . . . 4293 1 58 . 1 1 9 9 GLY C C 13 169.96 . . 1 . . . . . . . . 4293 1 59 . 1 1 9 9 GLY CA C 13 44.54 . . 1 . . . . . . . . 4293 1 60 . 1 1 9 9 GLY N N 15 109.6 . . 1 . . . . . . . . 4293 1 61 . 1 1 10 10 LYS H H 1 8.12 . . 1 . . . . . . . . 4293 1 62 . 1 1 10 10 LYS HA H 1 5.09 . . 1 . . . . . . . . 4293 1 63 . 1 1 10 10 LYS HB2 H 1 1.55 . . 2 . . . . . . . . 4293 1 64 . 1 1 10 10 LYS HG2 H 1 1.09 . . 2 . . . . . . . . 4293 1 65 . 1 1 10 10 LYS C C 13 175.63 . . 1 . . . . . . . . 4293 1 66 . 1 1 10 10 LYS CA C 13 52.92 . . 1 . . . . . . . . 4293 1 67 . 1 1 10 10 LYS CB C 13 34.12 . . 1 . . . . . . . . 4293 1 68 . 1 1 10 10 LYS N N 15 119.5 . . 1 . . . . . . . . 4293 1 69 . 1 1 11 11 ALA H H 1 8.33 . . 1 . . . . . . . . 4293 1 70 . 1 1 11 11 ALA HA H 1 5.15 . . 1 . . . . . . . . 4293 1 71 . 1 1 11 11 ALA HB1 H 1 1.80 . . 1 . . . . . . . . 4293 1 72 . 1 1 11 11 ALA HB2 H 1 1.80 . . 1 . . . . . . . . 4293 1 73 . 1 1 11 11 ALA HB3 H 1 1.80 . . 1 . . . . . . . . 4293 1 74 . 1 1 11 11 ALA C C 13 177.85 . . 1 . . . . . . . . 4293 1 75 . 1 1 11 11 ALA CA C 13 51.06 . . 1 . . . . . . . . 4293 1 76 . 1 1 11 11 ALA CB C 13 18.66 . . 1 . . . . . . . . 4293 1 77 . 1 1 11 11 ALA N N 15 125.6 . . 1 . . . . . . . . 4293 1 78 . 1 1 12 12 THR H H 1 8.47 . . 1 . . . . . . . . 4293 1 79 . 1 1 12 12 THR HA H 1 4.74 . . 1 . . . . . . . . 4293 1 80 . 1 1 12 12 THR HB H 1 4.31 . . 1 . . . . . . . . 4293 1 81 . 1 1 12 12 THR C C 13 172.44 . . 1 . . . . . . . . 4293 1 82 . 1 1 12 12 THR CA C 13 58.60 . . 1 . . . . . . . . 4293 1 83 . 1 1 12 12 THR CB C 13 70.86 . . 1 . . . . . . . . 4293 1 84 . 1 1 12 12 THR N N 15 115.3 . . 1 . . . . . . . . 4293 1 85 . 1 1 13 13 GLY H H 1 8.67 . . 1 . . . . . . . . 4293 1 86 . 1 1 13 13 GLY HA2 H 1 4.52 . . 1 . . . . . . . . 4293 1 87 . 1 1 13 13 GLY HA3 H 1 3.89 . . 1 . . . . . . . . 4293 1 88 . 1 1 13 13 GLY C C 13 173.26 . . 1 . . . . . . . . 4293 1 89 . 1 1 13 13 GLY CA C 13 43.33 . . 1 . . . . . . . . 4293 1 90 . 1 1 13 13 GLY N N 15 109.2 . . 1 . . . . . . . . 4293 1 91 . 1 1 14 14 LYS H H 1 9.37 . . 1 . . . . . . . . 4293 1 92 . 1 1 14 14 LYS HA H 1 4.16 . . 1 . . . . . . . . 4293 1 93 . 1 1 14 14 LYS HB2 H 1 1.97 . . 2 . . . . . . . . 4293 1 94 . 1 1 14 14 LYS HG2 H 1 1.55 . . 2 . . . . . . . . 4293 1 95 . 1 1 14 14 LYS C C 13 178.72 . . 1 . . . . . . . . 4293 1 96 . 1 1 14 14 LYS CA C 13 56.52 . . 1 . . . . . . . . 4293 1 97 . 1 1 14 14 LYS CB C 13 34.13 . . 1 . . . . . . . . 4293 1 98 . 1 1 14 14 LYS N N 15 120.1 . . 1 . . . . . . . . 4293 1 99 . 1 1 15 15 GLY H H 1 9.19 . . 1 . . . . . . . . 4293 1 100 . 1 1 15 15 GLY HA2 H 1 3.85 . . 1 . . . . . . . . 4293 1 101 . 1 1 15 15 GLY HA3 H 1 3.69 . . 1 . . . . . . . . 4293 1 102 . 1 1 15 15 GLY C C 13 173.47 . . 1 . . . . . . . . 4293 1 103 . 1 1 15 15 GLY CA C 13 43.79 . . 1 . . . . . . . . 4293 1 104 . 1 1 15 15 GLY N N 15 107.2 . . 1 . . . . . . . . 4293 1 105 . 1 1 16 16 LYS H H 1 8.13 . . 1 . . . . . . . . 4293 1 106 . 1 1 16 16 LYS HA H 1 5.03 . . 1 . . . . . . . . 4293 1 107 . 1 1 16 16 LYS HB2 H 1 1.81 . . 2 . . . . . . . . 4293 1 108 . 1 1 16 16 LYS HG2 H 1 1.35 . . 2 . . . . . . . . 4293 1 109 . 1 1 16 16 LYS CA C 13 51.55 . . 1 . . . . . . . . 4293 1 110 . 1 1 16 16 LYS CB C 13 35.28 . . 1 . . . . . . . . 4293 1 111 . 1 1 16 16 LYS N N 15 117.4 . . 1 . . . . . . . . 4293 1 112 . 1 1 17 17 PRO HA H 1 4.42 . . 1 . . . . . . . . 4293 1 113 . 1 1 17 17 PRO HB2 H 1 2.79 . . 9 . . . . . . . . 4293 1 114 . 1 1 17 17 PRO HB3 H 1 2.01 . . 1 . . . . . . . . 4293 1 115 . 1 1 17 17 PRO C C 13 178.42 . . 1 . . . . . . . . 4293 1 116 . 1 1 17 17 PRO CA C 13 61.65 . . 1 . . . . . . . . 4293 1 117 . 1 1 17 17 PRO CB C 13 30.17 . . 1 . . . . . . . . 4293 1 118 . 1 1 18 18 VAL H H 1 8.73 . . 1 . . . . . . . . 4293 1 119 . 1 1 18 18 VAL HA H 1 4.30 . . 1 . . . . . . . . 4293 1 120 . 1 1 18 18 VAL C C 13 175.7 . . 1 . . . . . . . . 4293 1 121 . 1 1 18 18 VAL CA C 13 57.74 . . 1 . . . . . . . . 4293 1 122 . 1 1 18 18 VAL CB C 13 34.6 . . 1 . . . . . . . . 4293 1 123 . 1 1 18 18 VAL N N 15 119.3 . . 1 . . . . . . . . 4293 1 124 . 1 1 19 19 GLY H H 1 8.43 . . 1 . . . . . . . . 4293 1 125 . 1 1 19 19 GLY HA2 H 1 4.54 . . 1 . . . . . . . . 4293 1 126 . 1 1 19 19 GLY HA3 H 1 3.86 . . 1 . . . . . . . . 4293 1 127 . 1 1 19 19 GLY C C 13 174.38 . . 1 . . . . . . . . 4293 1 128 . 1 1 19 19 GLY CA C 13 43.03 . . 1 . . . . . . . . 4293 1 129 . 1 1 19 19 GLY N N 15 111.0 . . 1 . . . . . . . . 4293 1 130 . 1 1 20 20 ASP H H 1 8.44 . . 1 . . . . . . . . 4293 1 131 . 1 1 20 20 ASP HA H 1 4.47 . . 1 . . . . . . . . 4293 1 132 . 1 1 20 20 ASP HB2 H 1 2.79 . . 2 . . . . . . . . 4293 1 133 . 1 1 20 20 ASP C C 13 178.30 . . 1 . . . . . . . . 4293 1 134 . 1 1 20 20 ASP CA C 13 54.77 . . 1 . . . . . . . . 4293 1 135 . 1 1 20 20 ASP CB C 13 40.15 . . 1 . . . . . . . . 4293 1 136 . 1 1 20 20 ASP N N 15 119.4 . . 1 . . . . . . . . 4293 1 137 . 1 1 21 21 LYS H H 1 8.37 . . 1 . . . . . . . . 4293 1 138 . 1 1 21 21 LYS HA H 1 4.64 . . 1 . . . . . . . . 4293 1 139 . 1 1 21 21 LYS HB2 H 1 1.71 . . 2 . . . . . . . . 4293 1 140 . 1 1 21 21 LYS C C 13 175.73 . . 1 . . . . . . . . 4293 1 141 . 1 1 21 21 LYS CA C 13 53.99 . . 1 . . . . . . . . 4293 1 142 . 1 1 21 21 LYS CB C 13 29.84 . . 1 . . . . . . . . 4293 1 143 . 1 1 21 21 LYS N N 15 120.1 . . 1 . . . . . . . . 4293 1 144 . 1 1 22 22 TRP H H 1 7.58 . . 1 . . . . . . . . 4293 1 145 . 1 1 22 22 TRP HA H 1 4.38 . . 1 . . . . . . . . 4293 1 146 . 1 1 22 22 TRP HE1 H 1 10.8 . . 1 . . . . . . . . 4293 1 147 . 1 1 22 22 TRP C C 13 176.56 . . 1 . . . . . . . . 4293 1 148 . 1 1 22 22 TRP CA C 13 59.40 . . 1 . . . . . . . . 4293 1 149 . 1 1 22 22 TRP CB C 13 28.54 . . 1 . . . . . . . . 4293 1 150 . 1 1 22 22 TRP N N 15 122.3 . . 1 . . . . . . . . 4293 1 151 . 1 1 22 22 TRP NE1 N 15 129.7 . . 1 . . . . . . . . 4293 1 152 . 1 1 23 23 LEU H H 1 8.30 . . 1 . . . . . . . . 4293 1 153 . 1 1 23 23 LEU HA H 1 3.26 . . 1 . . . . . . . . 4293 1 154 . 1 1 23 23 LEU C C 13 180.63 . . 1 . . . . . . . . 4293 1 155 . 1 1 23 23 LEU CA C 13 55.16 . . 1 . . . . . . . . 4293 1 156 . 1 1 23 23 LEU CB C 13 38.44 . . 1 . . . . . . . . 4293 1 157 . 1 1 23 23 LEU N N 15 113.3 . . 1 . . . . . . . . 4293 1 158 . 1 1 24 24 ASP H H 1 8.16 . . 1 . . . . . . . . 4293 1 159 . 1 1 24 24 ASP HA H 1 4.33 . . 1 . . . . . . . . 4293 1 160 . 1 1 24 24 ASP HB2 H 1 2.93 . . 1 . . . . . . . . 4293 1 161 . 1 1 24 24 ASP HB3 H 1 2.69 . . 1 . . . . . . . . 4293 1 162 . 1 1 24 24 ASP CA C 13 56.23 . . 1 . . . . . . . . 4293 1 163 . 1 1 24 24 ASP CB C 13 38.62 . . 1 . . . . . . . . 4293 1 164 . 1 1 24 24 ASP N N 15 123.7 . . 1 . . . . . . . . 4293 1 165 . 1 1 25 25 ASP H H 1 7.91 . . 1 . . . . . . . . 4293 1 166 . 1 1 25 25 ASP HA H 1 4.46 . . 1 . . . . . . . . 4293 1 167 . 1 1 25 25 ASP HB2 H 1 3.01 . . 2 . . . . . . . . 4293 1 168 . 1 1 25 25 ASP C C 13 177.13 . . 1 . . . . . . . . 4293 1 169 . 1 1 25 25 ASP CA C 13 56.31 . . 1 . . . . . . . . 4293 1 170 . 1 1 25 25 ASP CB C 13 38.27 . . 1 . . . . . . . . 4293 1 171 . 1 1 25 25 ASP N N 15 119.6 . . 1 . . . . . . . . 4293 1 172 . 1 1 26 26 ALA H H 1 7.58 . . 1 . . . . . . . . 4293 1 173 . 1 1 26 26 ALA HA H 1 4.47 . . 1 . . . . . . . . 4293 1 174 . 1 1 26 26 ALA HB1 H 1 1.40 . . 1 . . . . . . . . 4293 1 175 . 1 1 26 26 ALA HB2 H 1 1.40 . . 1 . . . . . . . . 4293 1 176 . 1 1 26 26 ALA HB3 H 1 1.40 . . 1 . . . . . . . . 4293 1 177 . 1 1 26 26 ALA C C 13 176.99 . . 1 . . . . . . . . 4293 1 178 . 1 1 26 26 ALA CA C 13 53.20 . . 1 . . . . . . . . 4293 1 179 . 1 1 26 26 ALA CB C 13 18.06 . . 1 . . . . . . . . 4293 1 180 . 1 1 26 26 ALA N N 15 120.4 . . 1 . . . . . . . . 4293 1 181 . 1 1 27 27 GLY H H 1 7.53 . . 1 . . . . . . . . 4293 1 182 . 1 1 27 27 GLY HA2 H 1 4.56 . . 1 . . . . . . . . 4293 1 183 . 1 1 27 27 GLY HA3 H 1 3.69 . . 1 . . . . . . . . 4293 1 184 . 1 1 27 27 GLY C C 13 173.11 . . 1 . . . . . . . . 4293 1 185 . 1 1 27 27 GLY CA C 13 43.43 . . 1 . . . . . . . . 4293 1 186 . 1 1 27 27 GLY N N 15 102.5 . . 1 . . . . . . . . 4293 1 187 . 1 1 28 28 LYS H H 1 7.57 . . 1 . . . . . . . . 4293 1 188 . 1 1 28 28 LYS HA H 1 4.66 . . 1 . . . . . . . . 4293 1 189 . 1 1 28 28 LYS HB2 H 1 1.86 . . 1 . . . . . . . . 4293 1 190 . 1 1 28 28 LYS HB3 H 1 1.75 . . 1 . . . . . . . . 4293 1 191 . 1 1 28 28 LYS HG2 H 1 1.39 . . 2 . . . . . . . . 4293 1 192 . 1 1 28 28 LYS C C 13 173.8 . . 1 . . . . . . . . 4293 1 193 . 1 1 28 28 LYS CA C 13 53.24 . . 1 . . . . . . . . 4293 1 194 . 1 1 28 28 LYS CB C 13 35.24 . . 1 . . . . . . . . 4293 1 195 . 1 1 28 28 LYS N N 15 120.0 . . 1 . . . . . . . . 4293 1 196 . 1 1 29 29 ASP H H 1 8.95 . . 1 . . . . . . . . 4293 1 197 . 1 1 29 29 ASP HA H 1 4.20 . . 1 . . . . . . . . 4293 1 198 . 1 1 29 29 ASP HB2 H 1 2.91 . . 2 . . . . . . . . 4293 1 199 . 1 1 29 29 ASP C C 13 176.22 . . 1 . . . . . . . . 4293 1 200 . 1 1 29 29 ASP CA C 13 55.34 . . 1 . . . . . . . . 4293 1 201 . 1 1 29 29 ASP CB C 13 38.94 . . 1 . . . . . . . . 4293 1 202 . 1 1 29 29 ASP N N 15 119.9 . . 1 . . . . . . . . 4293 1 203 . 1 1 30 30 SER H H 1 8.29 . . 1 . . . . . . . . 4293 1 204 . 1 1 30 30 SER HA H 1 4.57 . . 1 . . . . . . . . 4293 1 205 . 1 1 30 30 SER HB2 H 1 3.95 . . 2 . . . . . . . . 4293 1 206 . 1 1 30 30 SER C C 13 173.97 . . 1 . . . . . . . . 4293 1 207 . 1 1 30 30 SER CA C 13 57.07 . . 1 . . . . . . . . 4293 1 208 . 1 1 30 30 SER CB C 13 61.97 . . 1 . . . . . . . . 4293 1 209 . 1 1 30 30 SER N N 15 117.8 . . 1 . . . . . . . . 4293 1 210 . 1 1 31 31 GLY H H 1 8.39 . . 1 . . . . . . . . 4293 1 211 . 1 1 31 31 GLY HA2 H 1 4.42 . . 1 . . . . . . . . 4293 1 212 . 1 1 31 31 GLY HA3 H 1 4.20 . . 1 . . . . . . . . 4293 1 213 . 1 1 31 31 GLY C C 13 171.53 . . 1 . . . . . . . . 4293 1 214 . 1 1 31 31 GLY CA C 13 43.20 . . 1 . . . . . . . . 4293 1 215 . 1 1 31 31 GLY N N 15 108.7 . . 1 . . . . . . . . 4293 1 216 . 1 1 32 32 ALA H H 1 9.38 . . 1 . . . . . . . . 4293 1 217 . 1 1 32 32 ALA HA H 1 4.94 . . 1 . . . . . . . . 4293 1 218 . 1 1 32 32 ALA HB1 H 1 1.24 . . 1 . . . . . . . . 4293 1 219 . 1 1 32 32 ALA HB2 H 1 1.24 . . 1 . . . . . . . . 4293 1 220 . 1 1 32 32 ALA HB3 H 1 1.24 . . 1 . . . . . . . . 4293 1 221 . 1 1 32 32 ALA CA C 13 47.72 . . 1 . . . . . . . . 4293 1 222 . 1 1 32 32 ALA CB C 13 19.17 . . 1 . . . . . . . . 4293 1 223 . 1 1 32 32 ALA N N 15 124.2 . . 1 . . . . . . . . 4293 1 224 . 1 1 33 33 PRO HA H 1 4.44 . . 1 . . . . . . . . 4293 1 225 . 1 1 33 33 PRO HB2 H 1 2.29 . . 9 . . . . . . . . 4293 1 226 . 1 1 33 33 PRO HB3 H 1 1.89 . . 9 . . . . . . . . 4293 1 227 . 1 1 33 33 PRO C C 13 176.7 . . 1 . . . . . . . . 4293 1 228 . 1 1 33 33 PRO CA C 13 61.67 . . 1 . . . . . . . . 4293 1 229 . 1 1 33 33 PRO CB C 13 31.31 . . 1 . . . . . . . . 4293 1 230 . 1 1 34 34 ILE H H 1 8.30 . . 1 . . . . . . . . 4293 1 231 . 1 1 34 34 ILE HA H 1 4.14 . . 1 . . . . . . . . 4293 1 232 . 1 1 34 34 ILE HB H 1 1.83 . . 1 . . . . . . . . 4293 1 233 . 1 1 34 34 ILE HG12 H 1 1.48 . . 1 . . . . . . . . 4293 1 234 . 1 1 34 34 ILE HG13 H 1 1.19 . . 1 . . . . . . . . 4293 1 235 . 1 1 34 34 ILE HG21 H 1 0.56 . . 1 . . . . . . . . 4293 1 236 . 1 1 34 34 ILE HG22 H 1 0.56 . . 1 . . . . . . . . 4293 1 237 . 1 1 34 34 ILE HG23 H 1 0.56 . . 1 . . . . . . . . 4293 1 238 . 1 1 34 34 ILE HD11 H 1 0.46 . . 1 . . . . . . . . 4293 1 239 . 1 1 34 34 ILE HD12 H 1 0.46 . . 1 . . . . . . . . 4293 1 240 . 1 1 34 34 ILE HD13 H 1 0.46 . . 1 . . . . . . . . 4293 1 241 . 1 1 34 34 ILE CA C 13 60.10 . . 1 . . . . . . . . 4293 1 242 . 1 1 34 34 ILE CB C 13 34.29 . . 1 . . . . . . . . 4293 1 243 . 1 1 34 34 ILE N N 15 121.8 . . 1 . . . . . . . . 4293 1 244 . 1 1 35 35 PRO HA H 1 4.72 . . 1 . . . . . . . . 4293 1 245 . 1 1 35 35 PRO C C 13 177.03 . . 1 . . . . . . . . 4293 1 246 . 1 1 35 35 PRO CA C 13 59.90 . . 1 . . . . . . . . 4293 1 247 . 1 1 35 35 PRO CB C 13 31.15 . . 1 . . . . . . . . 4293 1 248 . 1 1 36 36 ASP H H 1 8.77 . . 1 . . . . . . . . 4293 1 249 . 1 1 36 36 ASP C C 13 178.33 . . 1 . . . . . . . . 4293 1 250 . 1 1 36 36 ASP CA C 13 55.11 . . 1 . . . . . . . . 4293 1 251 . 1 1 36 36 ASP CB C 13 36.81 . . 1 . . . . . . . . 4293 1 252 . 1 1 36 36 ASP N N 15 130.9 . . 1 . . . . . . . . 4293 1 253 . 1 1 37 37 ARG H H 1 8.68 . . 1 . . . . . . . . 4293 1 254 . 1 1 37 37 ARG HA H 1 4.10 . . 1 . . . . . . . . 4293 1 255 . 1 1 37 37 ARG C C 13 178.66 . . 1 . . . . . . . . 4293 1 256 . 1 1 37 37 ARG CA C 13 57.28 . . 1 . . . . . . . . 4293 1 257 . 1 1 37 37 ARG CB C 13 30.41 . . 1 . . . . . . . . 4293 1 258 . 1 1 37 37 ARG N N 15 118.9 . . 1 . . . . . . . . 4293 1 259 . 1 1 38 38 ILE H H 1 6.97 . . 1 . . . . . . . . 4293 1 260 . 1 1 38 38 ILE HA H 1 3.70 . . 1 . . . . . . . . 4293 1 261 . 1 1 38 38 ILE HB H 1 1.94 . . 1 . . . . . . . . 4293 1 262 . 1 1 38 38 ILE HG12 H 1 1.48 . . 1 . . . . . . . . 4293 1 263 . 1 1 38 38 ILE HG13 H 1 1.14 . . 1 . . . . . . . . 4293 1 264 . 1 1 38 38 ILE HG21 H 1 0.56 . . 1 . . . . . . . . 4293 1 265 . 1 1 38 38 ILE HG22 H 1 0.56 . . 1 . . . . . . . . 4293 1 266 . 1 1 38 38 ILE HG23 H 1 0.56 . . 1 . . . . . . . . 4293 1 267 . 1 1 38 38 ILE HD11 H 1 0.46 . . 1 . . . . . . . . 4293 1 268 . 1 1 38 38 ILE HD12 H 1 0.46 . . 1 . . . . . . . . 4293 1 269 . 1 1 38 38 ILE HD13 H 1 0.46 . . 1 . . . . . . . . 4293 1 270 . 1 1 38 38 ILE C C 13 177.36 . . 1 . . . . . . . . 4293 1 271 . 1 1 38 38 ILE CA C 13 60.66 . . 1 . . . . . . . . 4293 1 272 . 1 1 38 38 ILE CB C 13 34.29 . . 1 . . . . . . . . 4293 1 273 . 1 1 38 38 ILE N N 15 116.8 . . 1 . . . . . . . . 4293 1 274 . 1 1 39 39 ALA H H 1 8.31 . . 1 . . . . . . . . 4293 1 275 . 1 1 39 39 ALA HA H 1 3.95 . . 1 . . . . . . . . 4293 1 276 . 1 1 39 39 ALA HB1 H 1 1.14 . . 1 . . . . . . . . 4293 1 277 . 1 1 39 39 ALA HB2 H 1 1.14 . . 1 . . . . . . . . 4293 1 278 . 1 1 39 39 ALA HB3 H 1 1.14 . . 1 . . . . . . . . 4293 1 279 . 1 1 39 39 ALA C C 13 179.47 . . 1 . . . . . . . . 4293 1 280 . 1 1 39 39 ALA CA C 13 54.80 . . 1 . . . . . . . . 4293 1 281 . 1 1 39 39 ALA CB C 13 15.69 . . 1 . . . . . . . . 4293 1 282 . 1 1 39 39 ALA N N 15 124.9 . . 1 . . . . . . . . 4293 1 283 . 1 1 40 40 ASP H H 1 8.33 . . 1 . . . . . . . . 4293 1 284 . 1 1 40 40 ASP HA H 1 4.30 . . 1 . . . . . . . . 4293 1 285 . 1 1 40 40 ASP HB2 H 1 2.64 . . 2 . . . . . . . . 4293 1 286 . 1 1 40 40 ASP C C 13 178.31 . . 1 . . . . . . . . 4293 1 287 . 1 1 40 40 ASP CA C 13 55.72 . . 1 . . . . . . . . 4293 1 288 . 1 1 40 40 ASP CB C 13 39.46 . . 1 . . . . . . . . 4293 1 289 . 1 1 40 40 ASP N N 15 115.3 . . 1 . . . . . . . . 4293 1 290 . 1 1 41 41 LYS H H 1 7.14 . . 1 . . . . . . . . 4293 1 291 . 1 1 41 41 LYS HA H 1 4.20 . . 1 . . . . . . . . 4293 1 292 . 1 1 41 41 LYS HB2 H 1 1.92 . . 2 . . . . . . . . 4293 1 293 . 1 1 41 41 LYS HG2 H 1 1.61 . . 2 . . . . . . . . 4293 1 294 . 1 1 41 41 LYS HD2 H 1 1.72 . . 2 . . . . . . . . 4293 1 295 . 1 1 41 41 LYS C C 13 177.73 . . 1 . . . . . . . . 4293 1 296 . 1 1 41 41 LYS CA C 13 55.73 . . 1 . . . . . . . . 4293 1 297 . 1 1 41 41 LYS CB C 13 31.77 . . 1 . . . . . . . . 4293 1 298 . 1 1 41 41 LYS N N 15 117.2 . . 1 . . . . . . . . 4293 1 299 . 1 1 42 42 LEU H H 1 7.49 . . 1 . . . . . . . . 4293 1 300 . 1 1 42 42 LEU HA H 1 4.42 . . 1 . . . . . . . . 4293 1 301 . 1 1 42 42 LEU HB2 H 1 1.66 . . 2 . . . . . . . . 4293 1 302 . 1 1 42 42 LEU C C 13 176.04 . . 1 . . . . . . . . 4293 1 303 . 1 1 42 42 LEU CA C 13 53.79 . . 1 . . . . . . . . 4293 1 304 . 1 1 42 42 LEU CB C 13 42.16 . . 1 . . . . . . . . 4293 1 305 . 1 1 42 42 LEU N N 15 117.5 . . 1 . . . . . . . . 4293 1 306 . 1 1 43 43 ARG H H 1 7.94 . . 1 . . . . . . . . 4293 1 307 . 1 1 43 43 ARG HA H 1 3.50 . . 1 . . . . . . . . 4293 1 308 . 1 1 43 43 ARG HB2 H 1 1.97 . . 2 . . . . . . . . 4293 1 309 . 1 1 43 43 ARG C C 13 176.36 . . 1 . . . . . . . . 4293 1 310 . 1 1 43 43 ARG CA C 13 57.79 . . 1 . . . . . . . . 4293 1 311 . 1 1 43 43 ARG CB C 13 28.41 . . 1 . . . . . . . . 4293 1 312 . 1 1 43 43 ARG N N 15 119.9 . . 1 . . . . . . . . 4293 1 313 . 1 1 44 44 ASP H H 1 9.11 . . 1 . . . . . . . . 4293 1 314 . 1 1 44 44 ASP HA H 1 4.23 . . 1 . . . . . . . . 4293 1 315 . 1 1 44 44 ASP HB2 H 1 3.15 . . 1 . . . . . . . . 4293 1 316 . 1 1 44 44 ASP HB3 H 1 2.91 . . 1 . . . . . . . . 4293 1 317 . 1 1 44 44 ASP C C 13 174.3 . . 1 . . . . . . . . 4293 1 318 . 1 1 44 44 ASP CA C 13 56.01 . . 1 . . . . . . . . 4293 1 319 . 1 1 44 44 ASP CB C 13 38.37 . . 1 . . . . . . . . 4293 1 320 . 1 1 44 44 ASP N N 15 118.9 . . 1 . . . . . . . . 4293 1 321 . 1 1 45 45 LYS H H 1 8.08 . . 1 . . . . . . . . 4293 1 322 . 1 1 45 45 LYS HA H 1 4.21 . . 1 . . . . . . . . 4293 1 323 . 1 1 45 45 LYS HB2 H 1 1.40 . . 2 . . . . . . . . 4293 1 324 . 1 1 45 45 LYS C C 13 174.46 . . 1 . . . . . . . . 4293 1 325 . 1 1 45 45 LYS CA C 13 55.24 . . 1 . . . . . . . . 4293 1 326 . 1 1 45 45 LYS CB C 13 31.7 . . 1 . . . . . . . . 4293 1 327 . 1 1 45 45 LYS N N 15 121.1 . . 1 . . . . . . . . 4293 1 328 . 1 1 46 46 GLU H H 1 7.98 . . 1 . . . . . . . . 4293 1 329 . 1 1 46 46 GLU HA H 1 4.57 . . 1 . . . . . . . . 4293 1 330 . 1 1 46 46 GLU HB2 H 1 1.82 . . 1 . . . . . . . . 4293 1 331 . 1 1 46 46 GLU HB3 H 1 1.63 . . 1 . . . . . . . . 4293 1 332 . 1 1 46 46 GLU HG2 H 1 2.01 . . 2 . . . . . . . . 4293 1 333 . 1 1 46 46 GLU C C 13 175.23 . . 1 . . . . . . . . 4293 1 334 . 1 1 46 46 GLU CA C 13 53.80 . . 1 . . . . . . . . 4293 1 335 . 1 1 46 46 GLU CB C 13 30.48 . . 1 . . . . . . . . 4293 1 336 . 1 1 46 46 GLU N N 15 120.4 . . 1 . . . . . . . . 4293 1 337 . 1 1 47 47 PHE H H 1 8.63 . . 1 . . . . . . . . 4293 1 338 . 1 1 47 47 PHE HA H 1 4.68 . . 1 . . . . . . . . 4293 1 339 . 1 1 47 47 PHE HB2 H 1 3.18 . . 1 . . . . . . . . 4293 1 340 . 1 1 47 47 PHE HB3 H 1 2.27 . . 1 . . . . . . . . 4293 1 341 . 1 1 47 47 PHE C C 13 175.2 . . 1 . . . . . . . . 4293 1 342 . 1 1 47 47 PHE CA C 13 56.21 . . 1 . . . . . . . . 4293 1 343 . 1 1 47 47 PHE CB C 13 42.5 . . 1 . . . . . . . . 4293 1 344 . 1 1 47 47 PHE N N 15 122.7 . . 1 . . . . . . . . 4293 1 345 . 1 1 48 48 LYS H H 1 9.52 . . 1 . . . . . . . . 4293 1 346 . 1 1 48 48 LYS HA H 1 4.09 . . 1 . . . . . . . . 4293 1 347 . 1 1 48 48 LYS HB2 H 1 1.92 . . 2 . . . . . . . . 4293 1 348 . 1 1 48 48 LYS HG2 H 1 1.58 . . 1 . . . . . . . . 4293 1 349 . 1 1 48 48 LYS HG3 H 1 1.51 . . 1 . . . . . . . . 4293 1 350 . 1 1 48 48 LYS HD2 H 1 1.71 . . 2 . . . . . . . . 4293 1 351 . 1 1 48 48 LYS C C 13 175.0 . . 1 . . . . . . . . 4293 1 352 . 1 1 48 48 LYS CA C 13 56.36 . . 1 . . . . . . . . 4293 1 353 . 1 1 48 48 LYS CB C 13 32.10 . . 1 . . . . . . . . 4293 1 354 . 1 1 48 48 LYS N N 15 120.4 . . 1 . . . . . . . . 4293 1 355 . 1 1 49 49 SER H H 1 7.71 . . 1 . . . . . . . . 4293 1 356 . 1 1 49 49 SER HA H 1 4.58 . . 1 . . . . . . . . 4293 1 357 . 1 1 49 49 SER HB2 H 1 4.33 . . 1 . . . . . . . . 4293 1 358 . 1 1 49 49 SER HB3 H 1 4.09 . . 9 . . . . . . . . 4293 1 359 . 1 1 49 49 SER C C 13 175.48 . . 1 . . . . . . . . 4293 1 360 . 1 1 49 49 SER CA C 13 56.51 . . 1 . . . . . . . . 4293 1 361 . 1 1 49 49 SER CB C 13 64.52 . . 1 . . . . . . . . 4293 1 362 . 1 1 49 49 SER N N 15 109.4 . . 1 . . . . . . . . 4293 1 363 . 1 1 50 50 PHE H H 1 9.32 . . 1 . . . . . . . . 4293 1 364 . 1 1 50 50 PHE HA H 1 4.49 . . 1 . . . . . . . . 4293 1 365 . 1 1 50 50 PHE HB2 H 1 3.09 . . 2 . . . . . . . . 4293 1 366 . 1 1 50 50 PHE C C 13 177.07 . . 1 . . . . . . . . 4293 1 367 . 1 1 50 50 PHE CA C 13 60.84 . . 1 . . . . . . . . 4293 1 368 . 1 1 50 50 PHE CB C 13 37.89 . . 1 . . . . . . . . 4293 1 369 . 1 1 50 50 PHE N N 15 122.7 . . 1 . . . . . . . . 4293 1 370 . 1 1 51 51 ASP H H 1 8.47 . . 1 . . . . . . . . 4293 1 371 . 1 1 51 51 ASP HA H 1 4.43 . . 1 . . . . . . . . 4293 1 372 . 1 1 51 51 ASP HB2 H 1 2.76 . . 1 . . . . . . . . 4293 1 373 . 1 1 51 51 ASP HB3 H 1 2.66 . . 1 . . . . . . . . 4293 1 374 . 1 1 51 51 ASP C C 13 177.96 . . 1 . . . . . . . . 4293 1 375 . 1 1 51 51 ASP CA C 13 56.73 . . 1 . . . . . . . . 4293 1 376 . 1 1 51 51 ASP CB C 13 40.15 . . 1 . . . . . . . . 4293 1 377 . 1 1 51 51 ASP N N 15 118.9 . . 1 . . . . . . . . 4293 1 378 . 1 1 52 52 ASP H H 1 7.83 . . 1 . . . . . . . . 4293 1 379 . 1 1 52 52 ASP HA H 1 4.52 . . 1 . . . . . . . . 4293 1 380 . 1 1 52 52 ASP HB2 H 1 3.15 . . 1 . . . . . . . . 4293 1 381 . 1 1 52 52 ASP HB3 H 1 3.08 . . 1 . . . . . . . . 4293 1 382 . 1 1 52 52 ASP C C 13 178.53 . . 1 . . . . . . . . 4293 1 383 . 1 1 52 52 ASP CA C 13 56.10 . . 1 . . . . . . . . 4293 1 384 . 1 1 52 52 ASP CB C 13 40.44 . . 1 . . . . . . . . 4293 1 385 . 1 1 52 52 ASP N N 15 120.1 . . 1 . . . . . . . . 4293 1 386 . 1 1 53 53 PHE H H 1 7.55 . . 1 . . . . . . . . 4293 1 387 . 1 1 53 53 PHE HB2 H 1 3.32 . . 1 . . . . . . . . 4293 1 388 . 1 1 53 53 PHE HB3 H 1 2.91 . . 1 . . . . . . . . 4293 1 389 . 1 1 53 53 PHE C C 13 174.31 . . 1 . . . . . . . . 4293 1 390 . 1 1 53 53 PHE CA C 13 59.63 . . 1 . . . . . . . . 4293 1 391 . 1 1 53 53 PHE CB C 13 37.34 . . 1 . . . . . . . . 4293 1 392 . 1 1 53 53 PHE N N 15 123.2 . . 1 . . . . . . . . 4293 1 393 . 1 1 54 54 ARG H H 1 8.25 . . 1 . . . . . . . . 4293 1 394 . 1 1 54 54 ARG HA H 1 3.11 . . 1 . . . . . . . . 4293 1 395 . 1 1 54 54 ARG HB2 H 1 1.66 . . 1 . . . . . . . . 4293 1 396 . 1 1 54 54 ARG C C 13 176.46 . . 1 . . . . . . . . 4293 1 397 . 1 1 54 54 ARG CA C 13 58.03 . . 1 . . . . . . . . 4293 1 398 . 1 1 54 54 ARG CB C 13 37.34 . . 1 . . . . . . . . 4293 1 399 . 1 1 54 54 ARG N N 15 120.6 . . 1 . . . . . . . . 4293 1 400 . 1 1 55 55 LYS H H 1 7.48 . . 1 . . . . . . . . 4293 1 401 . 1 1 55 55 LYS HA H 1 4.38 . . 1 . . . . . . . . 4293 1 402 . 1 1 55 55 LYS HB2 H 1 1.93 . . 2 . . . . . . . . 4293 1 403 . 1 1 55 55 LYS HG2 H 1 1.44 . . 2 . . . . . . . . 4293 1 404 . 1 1 55 55 LYS C C 13 177.25 . . 1 . . . . . . . . 4293 1 405 . 1 1 55 55 LYS CA C 13 57.92 . . 1 . . . . . . . . 4293 1 406 . 1 1 55 55 LYS CB C 13 32.25 . . 1 . . . . . . . . 4293 1 407 . 1 1 55 55 LYS N N 15 116.9 . . 1 . . . . . . . . 4293 1 408 . 1 1 56 56 ALA H H 1 7.18 . . 1 . . . . . . . . 4293 1 409 . 1 1 56 56 ALA HA H 1 4.14 . . 1 . . . . . . . . 4293 1 410 . 1 1 56 56 ALA HB1 H 1 1.49 . . 1 . . . . . . . . 4293 1 411 . 1 1 56 56 ALA HB2 H 1 1.49 . . 1 . . . . . . . . 4293 1 412 . 1 1 56 56 ALA HB3 H 1 1.49 . . 1 . . . . . . . . 4293 1 413 . 1 1 56 56 ALA C C 13 179.89 . . 1 . . . . . . . . 4293 1 414 . 1 1 56 56 ALA CA C 13 53.57 . . 1 . . . . . . . . 4293 1 415 . 1 1 56 56 ALA CB C 13 18.22 . . 1 . . . . . . . . 4293 1 416 . 1 1 56 56 ALA N N 15 120.5 . . 1 . . . . . . . . 4293 1 417 . 1 1 57 57 VAL H H 1 7.72 . . 1 . . . . . . . . 4293 1 418 . 1 1 57 57 VAL HA H 1 2.81 . . 1 . . . . . . . . 4293 1 419 . 1 1 57 57 VAL HB H 1 1.41 . . 1 . . . . . . . . 4293 1 420 . 1 1 57 57 VAL HG11 H 1 -0.24 . . 2 . . . . . . . . 4293 1 421 . 1 1 57 57 VAL HG12 H 1 -0.24 . . 2 . . . . . . . . 4293 1 422 . 1 1 57 57 VAL HG13 H 1 -0.24 . . 2 . . . . . . . . 4293 1 423 . 1 1 57 57 VAL C C 13 177.49 . . 1 . . . . . . . . 4293 1 424 . 1 1 57 57 VAL CA C 13 65.64 . . 1 . . . . . . . . 4293 1 425 . 1 1 57 57 VAL CB C 13 29.6 . . 1 . . . . . . . . 4293 1 426 . 1 1 57 57 VAL N N 15 118.7 . . 1 . . . . . . . . 4293 1 427 . 1 1 58 58 TRP H H 1 7.28 . . 1 . . . . . . . . 4293 1 428 . 1 1 58 58 TRP HA H 1 4.62 . . 1 . . . . . . . . 4293 1 429 . 1 1 58 58 TRP HB2 H 1 3.27 . . 2 . . . . . . . . 4293 1 430 . 1 1 58 58 TRP HE1 H 1 10.1 . . 1 . . . . . . . . 4293 1 431 . 1 1 58 58 TRP C C 13 178.4 . . 1 . . . . . . . . 4293 1 432 . 1 1 58 58 TRP CA C 13 58.62 . . 1 . . . . . . . . 4293 1 433 . 1 1 58 58 TRP CB C 13 27.62 . . 1 . . . . . . . . 4293 1 434 . 1 1 58 58 TRP N N 15 118.1 . . 1 . . . . . . . . 4293 1 435 . 1 1 58 58 TRP NE1 N 15 129.5 . . 1 . . . . . . . . 4293 1 436 . 1 1 59 59 GLU H H 1 8.71 . . 1 . . . . . . . . 4293 1 437 . 1 1 59 59 GLU HA H 1 4.11 . . 1 . . . . . . . . 4293 1 438 . 1 1 59 59 GLU C C 13 181.12 . . 1 . . . . . . . . 4293 1 439 . 1 1 59 59 GLU CA C 13 58.58 . . 1 . . . . . . . . 4293 1 440 . 1 1 59 59 GLU CB C 13 28.81 . . 1 . . . . . . . . 4293 1 441 . 1 1 59 59 GLU N N 15 120.2 . . 1 . . . . . . . . 4293 1 442 . 1 1 60 60 GLU H H 1 8.32 . . 1 . . . . . . . . 4293 1 443 . 1 1 60 60 GLU HA H 1 4.08 . . 1 . . . . . . . . 4293 1 444 . 1 1 60 60 GLU HB2 H 1 2.01 . . 2 . . . . . . . . 4293 1 445 . 1 1 60 60 GLU C C 13 180.64 . . 1 . . . . . . . . 4293 1 446 . 1 1 60 60 GLU CA C 13 57.49 . . 1 . . . . . . . . 4293 1 447 . 1 1 60 60 GLU CB C 13 27.42 . . 1 . . . . . . . . 4293 1 448 . 1 1 60 60 GLU N N 15 119.3 . . 1 . . . . . . . . 4293 1 449 . 1 1 61 61 VAL H H 1 8.63 . . 1 . . . . . . . . 4293 1 450 . 1 1 61 61 VAL HA H 1 3.42 . . 1 . . . . . . . . 4293 1 451 . 1 1 61 61 VAL C C 13 177.74 . . 1 . . . . . . . . 4293 1 452 . 1 1 61 61 VAL CA C 13 66.51 . . 1 . . . . . . . . 4293 1 453 . 1 1 61 61 VAL N N 15 124.1 . . 1 . . . . . . . . 4293 1 454 . 1 1 62 62 SER H H 1 8.04 . . 1 . . . . . . . . 4293 1 455 . 1 1 62 62 SER HB2 H 1 3.95 . . 2 . . . . . . . . 4293 1 456 . 1 1 62 62 SER C C 13 174.55 . . 1 . . . . . . . . 4293 1 457 . 1 1 62 62 SER CA C 13 60.27 . . 1 . . . . . . . . 4293 1 458 . 1 1 62 62 SER CB C 13 62.43 . . 1 . . . . . . . . 4293 1 459 . 1 1 62 62 SER N N 15 113.1 . . 1 . . . . . . . . 4293 1 460 . 1 1 63 63 LYS H H 1 7.06 . . 1 . . . . . . . . 4293 1 461 . 1 1 63 63 LYS HA H 1 4.22 . . 1 . . . . . . . . 4293 1 462 . 1 1 63 63 LYS HB2 H 1 1.70 . . 2 . . . . . . . . 4293 1 463 . 1 1 63 63 LYS HG2 H 1 1.44 . . 2 . . . . . . . . 4293 1 464 . 1 1 63 63 LYS C C 13 175.14 . . 1 . . . . . . . . 4293 1 465 . 1 1 63 63 LYS CA C 13 55.23 . . 1 . . . . . . . . 4293 1 466 . 1 1 63 63 LYS CB C 13 32.69 . . 1 . . . . . . . . 4293 1 467 . 1 1 63 63 LYS N N 15 119.1 . . 1 . . . . . . . . 4293 1 468 . 1 1 64 64 ASP H H 1 7.66 . . 1 . . . . . . . . 4293 1 469 . 1 1 64 64 ASP HA H 1 5.03 . . 1 . . . . . . . . 4293 1 470 . 1 1 64 64 ASP HB2 H 1 3.14 . . 1 . . . . . . . . 4293 1 471 . 1 1 64 64 ASP HB3 H 1 2.33 . . 1 . . . . . . . . 4293 1 472 . 1 1 64 64 ASP CA C 13 50.24 . . 1 . . . . . . . . 4293 1 473 . 1 1 64 64 ASP CB C 13 42.54 . . 1 . . . . . . . . 4293 1 474 . 1 1 64 64 ASP N N 15 124.1 . . 1 . . . . . . . . 4293 1 475 . 1 1 65 65 PRO HA H 1 4.24 . . 1 . . . . . . . . 4293 1 476 . 1 1 65 65 PRO HB2 H 1 2.39 . . 1 . . . . . . . . 4293 1 477 . 1 1 65 65 PRO HB3 H 1 2.05 . . 9 . . . . . . . . 4293 1 478 . 1 1 65 65 PRO C C 13 178.1 . . 1 . . . . . . . . 4293 1 479 . 1 1 65 65 PRO CA C 13 63.71 . . 1 . . . . . . . . 4293 1 480 . 1 1 65 65 PRO CB C 13 31.4 . . 1 . . . . . . . . 4293 1 481 . 1 1 66 66 GLU H H 1 7.82 . . 1 . . . . . . . . 4293 1 482 . 1 1 66 66 GLU HA H 1 4.31 . . 1 . . . . . . . . 4293 1 483 . 1 1 66 66 GLU HB2 H 1 2.04 . . 1 . . . . . . . . 4293 1 484 . 1 1 66 66 GLU HB3 H 1 1.92 . . 1 . . . . . . . . 4293 1 485 . 1 1 66 66 GLU HG2 H 1 2.33 . . 1 . . . . . . . . 4293 1 486 . 1 1 66 66 GLU HG3 H 1 2.19 . . 1 . . . . . . . . 4293 1 487 . 1 1 66 66 GLU C C 13 178.46 . . 1 . . . . . . . . 4293 1 488 . 1 1 66 66 GLU CA C 13 57.12 . . 1 . . . . . . . . 4293 1 489 . 1 1 66 66 GLU CB C 13 29.30 . . 1 . . . . . . . . 4293 1 490 . 1 1 66 66 GLU N N 15 116.0 . . 1 . . . . . . . . 4293 1 491 . 1 1 67 67 LEU H H 1 8.42 . . 1 . . . . . . . . 4293 1 492 . 1 1 67 67 LEU HA H 1 4.32 . . 1 . . . . . . . . 4293 1 493 . 1 1 67 67 LEU C C 13 179.33 . . 1 . . . . . . . . 4293 1 494 . 1 1 67 67 LEU CA C 13 55.27 . . 1 . . . . . . . . 4293 1 495 . 1 1 67 67 LEU CB C 13 40.77 . . 1 . . . . . . . . 4293 1 496 . 1 1 67 67 LEU N N 15 116.9 . . 1 . . . . . . . . 4293 1 497 . 1 1 68 68 SER H H 1 8.27 . . 1 . . . . . . . . 4293 1 498 . 1 1 68 68 SER HA H 1 4.48 . . 1 . . . . . . . . 4293 1 499 . 1 1 68 68 SER HB2 H 1 4.21 . . 1 . . . . . . . . 4293 1 500 . 1 1 68 68 SER HB3 H 1 4.16 . . 1 . . . . . . . . 4293 1 501 . 1 1 68 68 SER C C 13 176.48 . . 1 . . . . . . . . 4293 1 502 . 1 1 68 68 SER CA C 13 58.86 . . 1 . . . . . . . . 4293 1 503 . 1 1 68 68 SER CB C 13 62.36 . . 1 . . . . . . . . 4293 1 504 . 1 1 68 68 SER N N 15 111.7 . . 1 . . . . . . . . 4293 1 505 . 1 1 69 69 LYS H H 1 7.22 . . 1 . . . . . . . . 4293 1 506 . 1 1 69 69 LYS HA H 1 4.15 . . 1 . . . . . . . . 4293 1 507 . 1 1 69 69 LYS HB2 H 1 1.96 . . 2 . . . . . . . . 4293 1 508 . 1 1 69 69 LYS HG2 H 1 1.54 . . 1 . . . . . . . . 4293 1 509 . 1 1 69 69 LYS HG3 H 1 1.44 . . 1 . . . . . . . . 4293 1 510 . 1 1 69 69 LYS HD2 H 1 1.77 . . 2 . . . . . . . . 4293 1 511 . 1 1 69 69 LYS C C 13 177.05 . . 1 . . . . . . . . 4293 1 512 . 1 1 69 69 LYS CA C 13 58.04 . . 1 . . . . . . . . 4293 1 513 . 1 1 69 69 LYS CB C 13 31.35 . . 1 . . . . . . . . 4293 1 514 . 1 1 69 69 LYS N N 15 122.1 . . 1 . . . . . . . . 4293 1 515 . 1 1 70 70 ASN H H 1 8.05 . . 1 . . . . . . . . 4293 1 516 . 1 1 70 70 ASN HA H 1 4.89 . . 1 . . . . . . . . 4293 1 517 . 1 1 70 70 ASN HB2 H 1 3.06 . . 1 . . . . . . . . 4293 1 518 . 1 1 70 70 ASN HB3 H 1 2.78 . . 1 . . . . . . . . 4293 1 519 . 1 1 70 70 ASN HD21 H 1 6.87 . . 1 . . . . . . . . 4293 1 520 . 1 1 70 70 ASN HD22 H 1 7.55 . . 1 . . . . . . . . 4293 1 521 . 1 1 70 70 ASN C C 13 175.12 . . 1 . . . . . . . . 4293 1 522 . 1 1 70 70 ASN CA C 13 52.22 . . 1 . . . . . . . . 4293 1 523 . 1 1 70 70 ASN CB C 13 38.23 . . 1 . . . . . . . . 4293 1 524 . 1 1 70 70 ASN CG C 13 176.8 . . 1 . . . . . . . . 4293 1 525 . 1 1 70 70 ASN N N 15 114.8 . . 1 . . . . . . . . 4293 1 526 . 1 1 70 70 ASN ND2 N 15 113.1 . . 1 . . . . . . . . 4293 1 527 . 1 1 71 71 LEU H H 1 7.50 . . 1 . . . . . . . . 4293 1 528 . 1 1 71 71 LEU HA H 1 4.56 . . 1 . . . . . . . . 4293 1 529 . 1 1 71 71 LEU HB2 H 1 1.99 . . 2 . . . . . . . . 4293 1 530 . 1 1 71 71 LEU HD11 H 1 0.87 . . 1 . . . . . . . . 4293 1 531 . 1 1 71 71 LEU HD12 H 1 0.87 . . 1 . . . . . . . . 4293 1 532 . 1 1 71 71 LEU HD13 H 1 0.87 . . 1 . . . . . . . . 4293 1 533 . 1 1 71 71 LEU HD21 H 1 0.78 . . 1 . . . . . . . . 4293 1 534 . 1 1 71 71 LEU HD22 H 1 0.78 . . 1 . . . . . . . . 4293 1 535 . 1 1 71 71 LEU HD23 H 1 0.78 . . 1 . . . . . . . . 4293 1 536 . 1 1 71 71 LEU C C 13 176.22 . . 1 . . . . . . . . 4293 1 537 . 1 1 71 71 LEU CA C 13 53.03 . . 1 . . . . . . . . 4293 1 538 . 1 1 71 71 LEU CB C 13 41.45 . . 1 . . . . . . . . 4293 1 539 . 1 1 71 71 LEU N N 15 120.2 . . 1 . . . . . . . . 4293 1 540 . 1 1 72 72 ASN H H 1 8.68 . . 1 . . . . . . . . 4293 1 541 . 1 1 72 72 ASN CA C 13 50.76 . . 1 . . . . . . . . 4293 1 542 . 1 1 72 72 ASN CB C 13 35.29 . . 1 . . . . . . . . 4293 1 543 . 1 1 72 72 ASN N N 15 122.4 . . 1 . . . . . . . . 4293 1 544 . 1 1 73 73 PRO HA H 1 4.21 . . 9 . . . . . . . . 4293 1 545 . 1 1 73 73 PRO HB2 H 1 2.45 . . 9 . . . . . . . . 4293 1 546 . 1 1 73 73 PRO HB3 H 1 1.92 . . 9 . . . . . . . . 4293 1 547 . 1 1 73 73 PRO C C 13 179.39 . . 1 . . . . . . . . 4293 1 548 . 1 1 73 73 PRO CA C 13 65.67 . . 1 . . . . . . . . 4293 1 549 . 1 1 73 73 PRO CB C 13 31.14 . . 1 . . . . . . . . 4293 1 550 . 1 1 74 74 SER H H 1 8.29 . . 1 . . . . . . . . 4293 1 551 . 1 1 74 74 SER HA H 1 4.32 . . 1 . . . . . . . . 4293 1 552 . 1 1 74 74 SER HB2 H 1 3.93 . . 2 . . . . . . . . 4293 1 553 . 1 1 74 74 SER C C 13 174.24 . . 1 . . . . . . . . 4293 1 554 . 1 1 74 74 SER CA C 13 59.74 . . 1 . . . . . . . . 4293 1 555 . 1 1 74 74 SER CB C 13 61.12 . . 1 . . . . . . . . 4293 1 556 . 1 1 74 74 SER N N 15 114.3 . . 1 . . . . . . . . 4293 1 557 . 1 1 75 75 ASN H H 1 8.49 . . 1 . . . . . . . . 4293 1 558 . 1 1 75 75 ASN HA H 1 4.92 . . 1 . . . . . . . . 4293 1 559 . 1 1 75 75 ASN HB2 H 1 3.04 . . 1 . . . . . . . . 4293 1 560 . 1 1 75 75 ASN HB3 H 1 2.55 . . 1 . . . . . . . . 4293 1 561 . 1 1 75 75 ASN C C 13 177.4 . . 1 . . . . . . . . 4293 1 562 . 1 1 75 75 ASN CA C 13 53.04 . . 1 . . . . . . . . 4293 1 563 . 1 1 75 75 ASN CB C 13 38.12 . . 1 . . . . . . . . 4293 1 564 . 1 1 75 75 ASN N N 15 121.7 . . 1 . . . . . . . . 4293 1 565 . 1 1 76 76 LYS H H 1 8.76 . . 1 . . . . . . . . 4293 1 566 . 1 1 76 76 LYS HA H 1 4.04 . . 1 . . . . . . . . 4293 1 567 . 1 1 76 76 LYS HB2 H 1 1.90 . . 2 . . . . . . . . 4293 1 568 . 1 1 76 76 LYS C C 13 178.8 . . 1 . . . . . . . . 4293 1 569 . 1 1 76 76 LYS CA C 13 58.75 . . 1 . . . . . . . . 4293 1 570 . 1 1 76 76 LYS CB C 13 31.61 . . 1 . . . . . . . . 4293 1 571 . 1 1 76 76 LYS N N 15 122.7 . . 1 . . . . . . . . 4293 1 572 . 1 1 77 77 SER H H 1 8.05 . . 1 . . . . . . . . 4293 1 573 . 1 1 77 77 SER HA H 1 4.44 . . 1 . . . . . . . . 4293 1 574 . 1 1 77 77 SER HB2 H 1 3.95 . . 2 . . . . . . . . 4293 1 575 . 1 1 77 77 SER C C 13 177.46 . . 1 . . . . . . . . 4293 1 576 . 1 1 77 77 SER CA C 13 59.40 . . 1 . . . . . . . . 4293 1 577 . 1 1 77 77 SER CB C 13 61.28 . . 1 . . . . . . . . 4293 1 578 . 1 1 77 77 SER N N 15 115.3 . . 1 . . . . . . . . 4293 1 579 . 1 1 78 78 SER H H 1 8.18 . . 1 . . . . . . . . 4293 1 580 . 1 1 78 78 SER HA H 1 4.25 . . 1 . . . . . . . . 4293 1 581 . 1 1 78 78 SER HB2 H 1 3.95 . . 1 . . . . . . . . 4293 1 582 . 1 1 78 78 SER HB3 H 1 3.71 . . 1 . . . . . . . . 4293 1 583 . 1 1 78 78 SER C C 13 176.56 . . 1 . . . . . . . . 4293 1 584 . 1 1 78 78 SER CA C 13 61.45 . . 1 . . . . . . . . 4293 1 585 . 1 1 78 78 SER N N 15 118.4 . . 1 . . . . . . . . 4293 1 586 . 1 1 79 79 VAL H H 1 8.23 . . 1 . . . . . . . . 4293 1 587 . 1 1 79 79 VAL HA H 1 4.57 . . 1 . . . . . . . . 4293 1 588 . 1 1 79 79 VAL C C 13 179.02 . . 1 . . . . . . . . 4293 1 589 . 1 1 79 79 VAL CA C 13 63.42 . . 1 . . . . . . . . 4293 1 590 . 1 1 79 79 VAL CB C 13 29.3 . . 1 . . . . . . . . 4293 1 591 . 1 1 79 79 VAL N N 15 117.5 . . 1 . . . . . . . . 4293 1 592 . 1 1 80 80 SER H H 1 7.72 . . 1 . . . . . . . . 4293 1 593 . 1 1 80 80 SER HA H 1 4.48 . . 1 . . . . . . . . 4293 1 594 . 1 1 80 80 SER HB2 H 1 4.06 . . 2 . . . . . . . . 4293 1 595 . 1 1 80 80 SER C C 13 175.29 . . 1 . . . . . . . . 4293 1 596 . 1 1 80 80 SER CA C 13 59.90 . . 1 . . . . . . . . 4293 1 597 . 1 1 80 80 SER CB C 13 61.69 . . 1 . . . . . . . . 4293 1 598 . 1 1 80 80 SER N N 15 117.0 . . 1 . . . . . . . . 4293 1 599 . 1 1 81 81 LYS H H 1 7.30 . . 1 . . . . . . . . 4293 1 600 . 1 1 81 81 LYS HA H 1 4.43 . . 1 . . . . . . . . 4293 1 601 . 1 1 81 81 LYS HB2 H 1 1.71 . . 2 . . . . . . . . 4293 1 602 . 1 1 81 81 LYS C C 13 176.13 . . 1 . . . . . . . . 4293 1 603 . 1 1 81 81 LYS CA C 13 54.29 . . 1 . . . . . . . . 4293 1 604 . 1 1 81 81 LYS CB C 13 32.36 . . 1 . . . . . . . . 4293 1 605 . 1 1 81 81 LYS N N 15 119.8 . . 1 . . . . . . . . 4293 1 606 . 1 1 82 82 GLY H H 1 8.20 . . 1 . . . . . . . . 4293 1 607 . 1 1 82 82 GLY HA2 H 1 4.20 . . 1 . . . . . . . . 4293 1 608 . 1 1 82 82 GLY HA3 H 1 3.82 . . 1 . . . . . . . . 4293 1 609 . 1 1 82 82 GLY C C 13 172.85 . . 1 . . . . . . . . 4293 1 610 . 1 1 82 82 GLY CA C 13 44.80 . . 1 . . . . . . . . 4293 1 611 . 1 1 82 82 GLY N N 15 108.7 . . 1 . . . . . . . . 4293 1 612 . 1 1 83 83 TYR H H 1 7.73 . . 1 . . . . . . . . 4293 1 613 . 1 1 83 83 TYR HA H 1 4.42 . . 1 . . . . . . . . 4293 1 614 . 1 1 83 83 TYR HB2 H 1 2.91 . . 1 . . . . . . . . 4293 1 615 . 1 1 83 83 TYR HB3 H 1 2.55 . . 1 . . . . . . . . 4293 1 616 . 1 1 83 83 TYR C C 13 173.4 . . 1 . . . . . . . . 4293 1 617 . 1 1 83 83 TYR CA C 13 55.23 . . 1 . . . . . . . . 4293 1 618 . 1 1 83 83 TYR CB C 13 37.09 . . 1 . . . . . . . . 4293 1 619 . 1 1 83 83 TYR N N 15 119.9 . . 1 . . . . . . . . 4293 1 620 . 1 1 84 84 SER H H 1 7.85 . . 1 . . . . . . . . 4293 1 621 . 1 1 84 84 SER CA C 13 53.30 . . 1 . . . . . . . . 4293 1 622 . 1 1 84 84 SER N N 15 115.3 . . 1 . . . . . . . . 4293 1 623 . 1 1 85 85 PRO C C 13 175.35 . . 1 . . . . . . . . 4293 1 624 . 1 1 85 85 PRO CA C 13 60.62 . . 1 . . . . . . . . 4293 1 625 . 1 1 85 85 PRO CB C 13 29.75 . . 1 . . . . . . . . 4293 1 626 . 1 1 86 86 PHE H H 1 8.34 . . 1 . . . . . . . . 4293 1 627 . 1 1 86 86 PHE HA H 1 4.76 . . 1 . . . . . . . . 4293 1 628 . 1 1 86 86 PHE HB2 H 1 3.04 . . 1 . . . . . . . . 4293 1 629 . 1 1 86 86 PHE HB3 H 1 2.91 . . 1 . . . . . . . . 4293 1 630 . 1 1 86 86 PHE C C 13 177.39 . . 1 . . . . . . . . 4293 1 631 . 1 1 86 86 PHE CA C 13 57.23 . . 1 . . . . . . . . 4293 1 632 . 1 1 86 86 PHE CB C 13 38.67 . . 1 . . . . . . . . 4293 1 633 . 1 1 86 86 PHE N N 15 117.1 . . 1 . . . . . . . . 4293 1 634 . 1 1 87 87 THR H H 1 8.26 . . 1 . . . . . . . . 4293 1 635 . 1 1 87 87 THR HA H 1 4.31 . . 1 . . . . . . . . 4293 1 636 . 1 1 87 87 THR CA C 13 58.98 . . 1 . . . . . . . . 4293 1 637 . 1 1 87 87 THR N N 15 112.3 . . 1 . . . . . . . . 4293 1 638 . 1 1 89 89 LYS C C 13 178.23 . . 1 . . . . . . . . 4293 1 639 . 1 1 89 89 LYS CA C 13 59.36 . . 1 . . . . . . . . 4293 1 640 . 1 1 89 89 LYS CB C 13 31.31 . . 1 . . . . . . . . 4293 1 641 . 1 1 90 90 ASN H H 1 8.68 . . 1 . . . . . . . . 4293 1 642 . 1 1 90 90 ASN HA H 1 4.51 . . 1 . . . . . . . . 4293 1 643 . 1 1 90 90 ASN HB2 H 1 3.12 . . 9 . . . . . . . . 4293 1 644 . 1 1 90 90 ASN HB3 H 1 2.83 . . 9 . . . . . . . . 4293 1 645 . 1 1 90 90 ASN HD21 H 1 6.73 . . 1 . . . . . . . . 4293 1 646 . 1 1 90 90 ASN HD22 H 1 7.59 . . 1 . . . . . . . . 4293 1 647 . 1 1 90 90 ASN C C 13 175.91 . . 1 . . . . . . . . 4293 1 648 . 1 1 90 90 ASN CA C 13 52.96 . . 1 . . . . . . . . 4293 1 649 . 1 1 90 90 ASN CB C 13 35.64 . . 1 . . . . . . . . 4293 1 650 . 1 1 90 90 ASN CG C 13 176.7 . . 1 . . . . . . . . 4293 1 651 . 1 1 90 90 ASN N N 15 114.7 . . 1 . . . . . . . . 4293 1 652 . 1 1 90 90 ASN ND2 N 15 111.1 . . 1 . . . . . . . . 4293 1 653 . 1 1 91 91 GLN H H 1 7.72 . . 1 . . . . . . . . 4293 1 654 . 1 1 91 91 GLN HA H 1 4.26 . . 9 . . . . . . . . 4293 1 655 . 1 1 91 91 GLN HB2 H 1 2.10 . . 1 . . . . . . . . 4293 1 656 . 1 1 91 91 GLN HB3 H 1 1.96 . . 1 . . . . . . . . 4293 1 657 . 1 1 91 91 GLN C C 13 173.97 . . 1 . . . . . . . . 4293 1 658 . 1 1 91 91 GLN CA C 13 53.02 . . 1 . . . . . . . . 4293 1 659 . 1 1 91 91 GLN CB C 13 28.72 . . 1 . . . . . . . . 4293 1 660 . 1 1 91 91 GLN N N 15 117.0 . . 1 . . . . . . . . 4293 1 661 . 1 1 92 92 GLN H H 1 7.20 . . 1 . . . . . . . . 4293 1 662 . 1 1 92 92 GLN HA H 1 4.15 . . 1 . . . . . . . . 4293 1 663 . 1 1 92 92 GLN HB2 H 1 2.06 . . 2 . . . . . . . . 4293 1 664 . 1 1 92 92 GLN C C 13 175.85 . . 1 . . . . . . . . 4293 1 665 . 1 1 92 92 GLN CA C 13 54.08 . . 1 . . . . . . . . 4293 1 666 . 1 1 92 92 GLN CB C 13 27.74 . . 1 . . . . . . . . 4293 1 667 . 1 1 92 92 GLN N N 15 119.0 . . 1 . . . . . . . . 4293 1 668 . 1 1 93 93 VAL H H 1 8.22 . . 1 . . . . . . . . 4293 1 669 . 1 1 93 93 VAL HA H 1 4.11 . . 1 . . . . . . . . 4293 1 670 . 1 1 93 93 VAL HB H 1 2.09 . . 1 . . . . . . . . 4293 1 671 . 1 1 93 93 VAL C C 13 176.6 . . 1 . . . . . . . . 4293 1 672 . 1 1 93 93 VAL CA C 13 61.32 . . 1 . . . . . . . . 4293 1 673 . 1 1 93 93 VAL CB C 13 31.77 . . 1 . . . . . . . . 4293 1 674 . 1 1 93 93 VAL N N 15 121.9 . . 1 . . . . . . . . 4293 1 675 . 1 1 94 94 GLY H H 1 8.55 . . 1 . . . . . . . . 4293 1 676 . 1 1 94 94 GLY HA2 H 1 3.96 . . 2 . . . . . . . . 4293 1 677 . 1 1 94 94 GLY C C 13 174.39 . . 1 . . . . . . . . 4293 1 678 . 1 1 94 94 GLY CA C 13 44.13 . . 1 . . . . . . . . 4293 1 679 . 1 1 94 94 GLY N N 15 113.4 . . 1 . . . . . . . . 4293 1 680 . 1 1 95 95 GLY H H 1 8.27 . . 1 . . . . . . . . 4293 1 681 . 1 1 95 95 GLY HA2 H 1 3.94 . . 2 . . . . . . . . 4293 1 682 . 1 1 95 95 GLY C C 13 173.86 . . 1 . . . . . . . . 4293 1 683 . 1 1 95 95 GLY CA C 13 44.13 . . 1 . . . . . . . . 4293 1 684 . 1 1 95 95 GLY N N 15 109.3 . . 1 . . . . . . . . 4293 1 685 . 1 1 96 96 ARG H H 1 8.38 . . 1 . . . . . . . . 4293 1 686 . 1 1 96 96 ARG HA H 1 4.25 . . 1 . . . . . . . . 4293 1 687 . 1 1 96 96 ARG HB2 H 1 2.21 . . 2 . . . . . . . . 4293 1 688 . 1 1 96 96 ARG C C 13 176.06 . . 1 . . . . . . . . 4293 1 689 . 1 1 96 96 ARG CA C 13 55.00 . . 1 . . . . . . . . 4293 1 690 . 1 1 96 96 ARG CB C 13 29.12 . . 1 . . . . . . . . 4293 1 691 . 1 1 96 96 ARG N N 15 121.1 . . 1 . . . . . . . . 4293 1 692 . 1 1 97 97 LYS H H 1 8.40 . . 1 . . . . . . . . 4293 1 693 . 1 1 97 97 LYS HA H 1 4.27 . . 1 . . . . . . . . 4293 1 694 . 1 1 97 97 LYS HB2 H 1 1.66 . . 2 . . . . . . . . 4293 1 695 . 1 1 97 97 LYS HG2 H 1 1.32 . . 2 . . . . . . . . 4293 1 696 . 1 1 97 97 LYS C C 13 176.11 . . 9 . . . . . . . . 4293 1 697 . 1 1 97 97 LYS CA C 13 55.07 . . 1 . . . . . . . . 4293 1 698 . 1 1 97 97 LYS CB C 13 31.9 . . 1 . . . . . . . . 4293 1 699 . 1 1 97 97 LYS N N 15 123.5 . . 1 . . . . . . . . 4293 1 700 . 1 1 98 98 VAL H H 1 8.08 . . 1 . . . . . . . . 4293 1 701 . 1 1 98 98 VAL HA H 1 4.03 . . 1 . . . . . . . . 4293 1 702 . 1 1 98 98 VAL HB H 1 1.97 . . 1 . . . . . . . . 4293 1 703 . 1 1 98 98 VAL C C 13 175.53 . . 1 . . . . . . . . 4293 1 704 . 1 1 98 98 VAL CA C 13 61.13 . . 1 . . . . . . . . 4293 1 705 . 1 1 98 98 VAL CB C 13 31.67 . . 1 . . . . . . . . 4293 1 706 . 1 1 98 98 VAL N N 15 121.2 . . 1 . . . . . . . . 4293 1 707 . 1 1 99 99 TYR H H 1 8.14 . . 1 . . . . . . . . 4293 1 708 . 1 1 99 99 TYR HA H 1 4.56 . . 1 . . . . . . . . 4293 1 709 . 1 1 99 99 TYR HB2 H 1 2.99 . . 1 . . . . . . . . 4293 1 710 . 1 1 99 99 TYR HB3 H 1 2.90 . . 1 . . . . . . . . 4293 1 711 . 1 1 99 99 TYR CA C 13 56.34 . . 1 . . . . . . . . 4293 1 712 . 1 1 99 99 TYR CB C 13 38.33 . . 1 . . . . . . . . 4293 1 713 . 1 1 99 99 TYR N N 15 123.3 . . 1 . . . . . . . . 4293 1 714 . 1 1 100 100 GLU C C 13 178.26 . . 1 . . . . . . . . 4293 1 715 . 1 1 100 100 GLU CA C 13 53.30 . . 1 . . . . . . . . 4293 1 716 . 1 1 100 100 GLU CB C 13 32.45 . . 1 . . . . . . . . 4293 1 717 . 1 1 101 101 LEU H H 1 8.48 . . 1 . . . . . . . . 4293 1 718 . 1 1 101 101 LEU HA H 1 5.29 . . 1 . . . . . . . . 4293 1 719 . 1 1 101 101 LEU HB2 H 1 1.79 . . 2 . . . . . . . . 4293 1 720 . 1 1 101 101 LEU C C 13 175.49 . . 1 . . . . . . . . 4293 1 721 . 1 1 101 101 LEU CA C 13 52.80 . . 1 . . . . . . . . 4293 1 722 . 1 1 101 101 LEU CB C 13 41.95 . . 1 . . . . . . . . 4293 1 723 . 1 1 101 101 LEU N N 15 121.6 . . 1 . . . . . . . . 4293 1 724 . 1 1 102 102 HIS H H 1 9.05 . . 1 . . . . . . . . 4293 1 725 . 1 1 102 102 HIS HA H 1 5.04 . . 1 . . . . . . . . 4293 1 726 . 1 1 102 102 HIS HB2 H 1 3.58 . . 1 . . . . . . . . 4293 1 727 . 1 1 102 102 HIS HB3 H 1 2.70 . . 1 . . . . . . . . 4293 1 728 . 1 1 102 102 HIS C C 13 172.97 . . 1 . . . . . . . . 4293 1 729 . 1 1 102 102 HIS CA C 13 52.74 . . 1 . . . . . . . . 4293 1 730 . 1 1 102 102 HIS CB C 13 32.65 . . 1 . . . . . . . . 4293 1 731 . 1 1 102 102 HIS N N 15 119.8 . . 1 . . . . . . . . 4293 1 732 . 1 1 103 103 HIS H H 1 9.87 . . 1 . . . . . . . . 4293 1 733 . 1 1 103 103 HIS HA H 1 5.17 . . 1 . . . . . . . . 4293 1 734 . 1 1 103 103 HIS HB2 H 1 3.00 . . 2 . . . . . . . . 4293 1 735 . 1 1 103 103 HIS C C 13 175.24 . . 1 . . . . . . . . 4293 1 736 . 1 1 103 103 HIS CA C 13 55.88 . . 1 . . . . . . . . 4293 1 737 . 1 1 103 103 HIS CB C 13 29.36 . . 1 . . . . . . . . 4293 1 738 . 1 1 103 103 HIS N N 15 120.7 . . 1 . . . . . . . . 4293 1 739 . 1 1 104 104 ASP H H 1 8.26 . . 1 . . . . . . . . 4293 1 740 . 1 1 104 104 ASP HA H 1 4.41 . . 1 . . . . . . . . 4293 1 741 . 1 1 104 104 ASP HB2 H 1 2.86 . . 1 . . . . . . . . 4293 1 742 . 1 1 104 104 ASP HB3 H 1 2.43 . . 1 . . . . . . . . 4293 1 743 . 1 1 104 104 ASP C C 13 175.67 . . 1 . . . . . . . . 4293 1 744 . 1 1 104 104 ASP CA C 13 55.61 . . 1 . . . . . . . . 4293 1 745 . 1 1 104 104 ASP CB C 13 40.66 . . 1 . . . . . . . . 4293 1 746 . 1 1 104 104 ASP N N 15 125.5 . . 1 . . . . . . . . 4293 1 747 . 1 1 105 105 LYS H H 1 9.52 . . 1 . . . . . . . . 4293 1 748 . 1 1 105 105 LYS HA H 1 4.75 . . 1 . . . . . . . . 4293 1 749 . 1 1 105 105 LYS HB2 H 1 1.76 . . 2 . . . . . . . . 4293 1 750 . 1 1 105 105 LYS CA C 13 51.85 . . 1 . . . . . . . . 4293 1 751 . 1 1 105 105 LYS CB C 13 31.38 . . 1 . . . . . . . . 4293 1 752 . 1 1 105 105 LYS N N 15 122.2 . . 1 . . . . . . . . 4293 1 753 . 1 1 106 106 PRO HA H 1 4.33 . . 1 . . . . . . . . 4293 1 754 . 1 1 106 106 PRO HB2 H 1 2.43 . . 1 . . . . . . . . 4293 1 755 . 1 1 106 106 PRO HB3 H 1 1.80 . . 1 . . . . . . . . 4293 1 756 . 1 1 106 106 PRO C C 13 178.61 . . 1 . . . . . . . . 4293 1 757 . 1 1 106 106 PRO CA C 13 61.41 . . 1 . . . . . . . . 4293 1 758 . 1 1 106 106 PRO CB C 13 31.66 . . 1 . . . . . . . . 4293 1 759 . 1 1 107 107 ILE H H 1 8.69 . . 1 . . . . . . . . 4293 1 760 . 1 1 107 107 ILE HA H 1 4.04 . . 1 . . . . . . . . 4293 1 761 . 1 1 107 107 ILE C C 13 179.32 . . 1 . . . . . . . . 4293 1 762 . 1 1 107 107 ILE CA C 13 61.38 . . 1 . . . . . . . . 4293 1 763 . 1 1 107 107 ILE CB C 13 35.86 . . 1 . . . . . . . . 4293 1 764 . 1 1 107 107 ILE N N 15 125.5 . . 1 . . . . . . . . 4293 1 765 . 1 1 108 108 SER H H 1 8.49 . . 1 . . . . . . . . 4293 1 766 . 1 1 108 108 SER C C 13 174.98 . . 1 . . . . . . . . 4293 1 767 . 1 1 108 108 SER CA C 13 58.60 . . 1 . . . . . . . . 4293 1 768 . 1 1 108 108 SER CB C 13 61.60 . . 1 . . . . . . . . 4293 1 769 . 1 1 108 108 SER N N 15 115.9 . . 1 . . . . . . . . 4293 1 770 . 1 1 109 109 GLN H H 1 7.52 . . 1 . . . . . . . . 4293 1 771 . 1 1 109 109 GLN HA H 1 4.55 . . 1 . . . . . . . . 4293 1 772 . 1 1 109 109 GLN HB2 H 1 2.45 . . 1 . . . . . . . . 4293 1 773 . 1 1 109 109 GLN HB3 H 1 1.67 . . 1 . . . . . . . . 4293 1 774 . 1 1 109 109 GLN C C 13 175.36 . . 1 . . . . . . . . 4293 1 775 . 1 1 109 109 GLN CA C 13 53.31 . . 1 . . . . . . . . 4293 1 776 . 1 1 109 109 GLN CB C 13 28.30 . . 1 . . . . . . . . 4293 1 777 . 1 1 109 109 GLN N N 15 120.1 . . 1 . . . . . . . . 4293 1 778 . 1 1 110 110 GLY H H 1 7.88 . . 1 . . . . . . . . 4293 1 779 . 1 1 110 110 GLY HA2 H 1 4.31 . . 1 . . . . . . . . 4293 1 780 . 1 1 110 110 GLY HA3 H 1 3.69 . . 1 . . . . . . . . 4293 1 781 . 1 1 110 110 GLY C C 13 175.23 . . 1 . . . . . . . . 4293 1 782 . 1 1 110 110 GLY CA C 13 44.10 . . 1 . . . . . . . . 4293 1 783 . 1 1 110 110 GLY N N 15 107.8 . . 1 . . . . . . . . 4293 1 784 . 1 1 111 111 GLY H H 1 8.10 . . 1 . . . . . . . . 4293 1 785 . 1 1 111 111 GLY HA2 H 1 3.79 . . 1 . . . . . . . . 4293 1 786 . 1 1 111 111 GLY HA3 H 1 3.43 . . 1 . . . . . . . . 4293 1 787 . 1 1 111 111 GLY C C 13 172.40 . . 1 . . . . . . . . 4293 1 788 . 1 1 111 111 GLY CA C 13 43.59 . . 1 . . . . . . . . 4293 1 789 . 1 1 111 111 GLY N N 15 110.1 . . 1 . . . . . . . . 4293 1 790 . 1 1 112 112 GLU H H 1 8.71 . . 1 . . . . . . . . 4293 1 791 . 1 1 112 112 GLU HA H 1 4.43 . . 1 . . . . . . . . 4293 1 792 . 1 1 112 112 GLU HB2 H 1 2.02 . . 2 . . . . . . . . 4293 1 793 . 1 1 112 112 GLU C C 13 177.99 . . 1 . . . . . . . . 4293 1 794 . 1 1 112 112 GLU CA C 13 54.59 . . 1 . . . . . . . . 4293 1 795 . 1 1 112 112 GLU CB C 13 30.03 . . 1 . . . . . . . . 4293 1 796 . 1 1 112 112 GLU N N 15 122.3 . . 1 . . . . . . . . 4293 1 797 . 1 1 113 113 VAL H H 1 8.39 . . 1 . . . . . . . . 4293 1 798 . 1 1 113 113 VAL HA H 1 2.94 . . 1 . . . . . . . . 4293 1 799 . 1 1 113 113 VAL HB H 1 1.55 . . 1 . . . . . . . . 4293 1 800 . 1 1 113 113 VAL C C 13 177.19 . . 1 . . . . . . . . 4293 1 801 . 1 1 113 113 VAL CA C 13 63.73 . . 1 . . . . . . . . 4293 1 802 . 1 1 113 113 VAL CB C 13 31.65 . . 1 . . . . . . . . 4293 1 803 . 1 1 113 113 VAL N N 15 121.9 . . 1 . . . . . . . . 4293 1 804 . 1 1 114 114 TYR H H 1 8.55 . . 1 . . . . . . . . 4293 1 805 . 1 1 114 114 TYR HA H 1 4.16 . . 1 . . . . . . . . 4293 1 806 . 1 1 114 114 TYR HB2 H 1 2.88 . . 1 . . . . . . . . 4293 1 807 . 1 1 114 114 TYR HB3 H 1 2.61 . . 1 . . . . . . . . 4293 1 808 . 1 1 114 114 TYR C C 13 173.35 . . 1 . . . . . . . . 4293 1 809 . 1 1 114 114 TYR CA C 13 55.17 . . 1 . . . . . . . . 4293 1 810 . 1 1 114 114 TYR CB C 13 36.26 . . 1 . . . . . . . . 4293 1 811 . 1 1 114 114 TYR N N 15 116.2 . . 1 . . . . . . . . 4293 1 812 . 1 1 115 115 ASP H H 1 6.18 . . 1 . . . . . . . . 4293 1 813 . 1 1 115 115 ASP HA H 1 4.79 . . 1 . . . . . . . . 4293 1 814 . 1 1 115 115 ASP HB2 H 1 2.70 . . 1 . . . . . . . . 4293 1 815 . 1 1 115 115 ASP HB3 H 1 2.57 . . 1 . . . . . . . . 4293 1 816 . 1 1 115 115 ASP C C 13 177.62 . . 1 . . . . . . . . 4293 1 817 . 1 1 115 115 ASP CA C 13 50.93 . . 1 . . . . . . . . 4293 1 818 . 1 1 115 115 ASP CB C 13 40.89 . . 1 . . . . . . . . 4293 1 819 . 1 1 115 115 ASP N N 15 116.3 . . 1 . . . . . . . . 4293 1 820 . 1 1 116 116 MET H H 1 9.94 . . 1 . . . . . . . . 4293 1 821 . 1 1 116 116 MET HA H 1 3.89 . . 1 . . . . . . . . 4293 1 822 . 1 1 116 116 MET HB2 H 1 2.14 . . 1 . . . . . . . . 4293 1 823 . 1 1 116 116 MET HB3 H 1 1.98 . . 1 . . . . . . . . 4293 1 824 . 1 1 116 116 MET C C 13 176.86 . . 1 . . . . . . . . 4293 1 825 . 1 1 116 116 MET CA C 13 58.24 . . 1 . . . . . . . . 4293 1 826 . 1 1 116 116 MET CB C 13 32.17 . . 1 . . . . . . . . 4293 1 827 . 1 1 116 116 MET N N 15 126.4 . . 1 . . . . . . . . 4293 1 828 . 1 1 117 117 ASP H H 1 8.73 . . 1 . . . . . . . . 4293 1 829 . 1 1 117 117 ASP HA H 1 4.93 . . 1 . . . . . . . . 4293 1 830 . 1 1 117 117 ASP HB2 H 1 2.96 . . 2 . . . . . . . . 4293 1 831 . 1 1 117 117 ASP C C 13 175.60 . . 1 . . . . . . . . 4293 1 832 . 1 1 117 117 ASP CA C 13 55.22 . . 1 . . . . . . . . 4293 1 833 . 1 1 117 117 ASP CB C 13 38.94 . . 1 . . . . . . . . 4293 1 834 . 1 1 117 117 ASP N N 15 117.8 . . 1 . . . . . . . . 4293 1 835 . 1 1 118 118 ASN H H 1 8.32 . . 1 . . . . . . . . 4293 1 836 . 1 1 118 118 ASN HA H 1 5.25 . . 1 . . . . . . . . 4293 1 837 . 1 1 118 118 ASN HB2 H 1 3.12 . . 1 . . . . . . . . 4293 1 838 . 1 1 118 118 ASN HB3 H 1 2.72 . . 1 . . . . . . . . 4293 1 839 . 1 1 118 118 ASN HD21 H 1 7.38 . . 1 . . . . . . . . 4293 1 840 . 1 1 118 118 ASN HD22 H 1 7.78 . . 1 . . . . . . . . 4293 1 841 . 1 1 118 118 ASN C C 13 173.68 . . 1 . . . . . . . . 4293 1 842 . 1 1 118 118 ASN CA C 13 50.78 . . 1 . . . . . . . . 4293 1 843 . 1 1 118 118 ASN CB C 13 40.07 . . 1 . . . . . . . . 4293 1 844 . 1 1 118 118 ASN CG C 13 178.1 . . 1 . . . . . . . . 4293 1 845 . 1 1 118 118 ASN N N 15 119.4 . . 1 . . . . . . . . 4293 1 846 . 1 1 118 118 ASN ND2 N 15 111.3 . . 1 . . . . . . . . 4293 1 847 . 1 1 119 119 ILE H H 1 6.77 . . 1 . . . . . . . . 4293 1 848 . 1 1 119 119 ILE HA H 1 4.72 . . 1 . . . . . . . . 4293 1 849 . 1 1 119 119 ILE HB H 1 1.54 . . 1 . . . . . . . . 4293 1 850 . 1 1 119 119 ILE C C 13 173.80 . . 1 . . . . . . . . 4293 1 851 . 1 1 119 119 ILE CA C 13 58.35 . . 1 . . . . . . . . 4293 1 852 . 1 1 119 119 ILE CB C 13 39.65 . . 1 . . . . . . . . 4293 1 853 . 1 1 119 119 ILE N N 15 119.9 . . 1 . . . . . . . . 4293 1 854 . 1 1 120 120 ARG H H 1 8.96 . . 1 . . . . . . . . 4293 1 855 . 1 1 120 120 ARG HA H 1 5.10 . . 1 . . . . . . . . 4293 1 856 . 1 1 120 120 ARG HB2 H 1 1.63 . . 2 . . . . . . . . 4293 1 857 . 1 1 120 120 ARG C C 13 174.84 . . 1 . . . . . . . . 4293 1 858 . 1 1 120 120 ARG CA C 13 51.05 . . 1 . . . . . . . . 4293 1 859 . 1 1 120 120 ARG CB C 13 32.90 . . 1 . . . . . . . . 4293 1 860 . 1 1 120 120 ARG N N 15 125.4 . . 1 . . . . . . . . 4293 1 861 . 1 1 121 121 VAL H H 1 9.88 . . 1 . . . . . . . . 4293 1 862 . 1 1 121 121 VAL HA H 1 5.08 . . 1 . . . . . . . . 4293 1 863 . 1 1 121 121 VAL HB H 1 1.83 . . 1 . . . . . . . . 4293 1 864 . 1 1 121 121 VAL HG11 H 1 0.82 . . 2 . . . . . . . . 4293 1 865 . 1 1 121 121 VAL HG12 H 1 0.82 . . 2 . . . . . . . . 4293 1 866 . 1 1 121 121 VAL HG13 H 1 0.82 . . 2 . . . . . . . . 4293 1 867 . 1 1 121 121 VAL C C 13 176.73 . . 1 . . . . . . . . 4293 1 868 . 1 1 121 121 VAL CA C 13 59.42 . . 1 . . . . . . . . 4293 1 869 . 1 1 121 121 VAL CB C 13 31.50 . . 1 . . . . . . . . 4293 1 870 . 1 1 121 121 VAL N N 15 123.4 . . 1 . . . . . . . . 4293 1 871 . 1 1 122 122 THR H H 1 9.74 . . 1 . . . . . . . . 4293 1 872 . 1 1 122 122 THR HA H 1 6.07 . . 1 . . . . . . . . 4293 1 873 . 1 1 122 122 THR HB H 1 4.45 . . 1 . . . . . . . . 4293 1 874 . 1 1 122 122 THR HG21 H 1 1.22 . . 1 . . . . . . . . 4293 1 875 . 1 1 122 122 THR HG22 H 1 1.22 . . 1 . . . . . . . . 4293 1 876 . 1 1 122 122 THR HG23 H 1 1.22 . . 1 . . . . . . . . 4293 1 877 . 1 1 122 122 THR C C 13 175.69 . . 1 . . . . . . . . 4293 1 878 . 1 1 122 122 THR CA C 13 58.36 . . 1 . . . . . . . . 4293 1 879 . 1 1 122 122 THR CB C 13 70.70 . . 1 . . . . . . . . 4293 1 880 . 1 1 122 122 THR N N 15 117.2 . . 1 . . . . . . . . 4293 1 881 . 1 1 123 123 THR H H 1 7.61 . . 1 . . . . . . . . 4293 1 882 . 1 1 123 123 THR HA H 1 4.59 . . 1 . . . . . . . . 4293 1 883 . 1 1 123 123 THR CA C 13 58.32 . . 1 . . . . . . . . 4293 1 884 . 1 1 123 123 THR CB C 13 66.58 . . 1 . . . . . . . . 4293 1 885 . 1 1 123 123 THR N N 15 111.7 . . 1 . . . . . . . . 4293 1 886 . 1 1 124 124 PRO HA H 1 4.24 . . 1 . . . . . . . . 4293 1 887 . 1 1 124 124 PRO HB2 H 1 2.34 . . 2 . . . . . . . . 4293 1 888 . 1 1 124 124 PRO C C 13 177.10 . . 1 . . . . . . . . 4293 1 889 . 1 1 124 124 PRO CA C 13 64.25 . . 1 . . . . . . . . 4293 1 890 . 1 1 124 124 PRO CB C 13 31.69 . . 1 . . . . . . . . 4293 1 891 . 1 1 125 125 LYS H H 1 7.57 . . 1 . . . . . . . . 4293 1 892 . 1 1 125 125 LYS HA H 1 3.73 . . 1 . . . . . . . . 4293 1 893 . 1 1 125 125 LYS C C 13 177.08 . . 1 . . . . . . . . 4293 1 894 . 1 1 125 125 LYS CA C 13 58.14 . . 1 . . . . . . . . 4293 1 895 . 1 1 125 125 LYS CB C 13 31.91 . . 1 . . . . . . . . 4293 1 896 . 1 1 125 125 LYS N N 15 114.3 . . 1 . . . . . . . . 4293 1 897 . 1 1 126 126 ARG H H 1 7.71 . . 1 . . . . . . . . 4293 1 898 . 1 1 126 126 ARG HA H 1 4.29 . . 1 . . . . . . . . 4293 1 899 . 1 1 126 126 ARG N N 15 117.0 . . 1 . . . . . . . . 4293 1 900 . 1 1 130 130 ILE CA C 13 63.50 . . 1 . . . . . . . . 4293 1 901 . 1 1 130 130 ILE CB C 13 37.40 . . 1 . . . . . . . . 4293 1 902 . 1 1 131 131 HIS H H 1 7.48 . . 1 . . . . . . . . 4293 1 903 . 1 1 131 131 HIS HA H 1 4.38 . . 1 . . . . . . . . 4293 1 904 . 1 1 131 131 HIS HB2 H 1 3.28 . . 1 . . . . . . . . 4293 1 905 . 1 1 131 131 HIS HB3 H 1 2.75 . . 1 . . . . . . . . 4293 1 906 . 1 1 131 131 HIS C C 13 174.52 . . 1 . . . . . . . . 4293 1 907 . 1 1 131 131 HIS CA C 13 55.75 . . 1 . . . . . . . . 4293 1 908 . 1 1 131 131 HIS CB C 13 27.85 . . 1 . . . . . . . . 4293 1 909 . 1 1 131 131 HIS N N 15 117.5 . . 1 . . . . . . . . 4293 1 910 . 1 1 132 132 ARG H H 1 7.77 . . 1 . . . . . . . . 4293 1 911 . 1 1 132 132 ARG HA H 1 4.31 . . 1 . . . . . . . . 4293 1 912 . 1 1 132 132 ARG HB2 H 1 1.90 . . 2 . . . . . . . . 4293 1 913 . 1 1 132 132 ARG HG2 H 1 1.72 . . 2 . . . . . . . . 4293 1 914 . 1 1 132 132 ARG HD2 H 1 3.21 . . 2 . . . . . . . . 4293 1 915 . 1 1 132 132 ARG C C 13 176.64 . . 1 . . . . . . . . 4293 1 916 . 1 1 132 132 ARG CA C 13 55.80 . . 1 . . . . . . . . 4293 1 917 . 1 1 132 132 ARG CB C 13 29.29 . . 1 . . . . . . . . 4293 1 918 . 1 1 132 132 ARG N N 15 121.3 . . 1 . . . . . . . . 4293 1 919 . 1 1 133 133 GLY H H 1 8.31 . . 1 . . . . . . . . 4293 1 920 . 1 1 133 133 GLY HA2 H 1 3.94 . . 2 . . . . . . . . 4293 1 921 . 1 1 133 133 GLY C C 13 173.06 . . 1 . . . . . . . . 4293 1 922 . 1 1 133 133 GLY CA C 13 44.34 . . 1 . . . . . . . . 4293 1 923 . 1 1 133 133 GLY N N 15 110.5 . . 1 . . . . . . . . 4293 1 924 . 1 1 134 134 LYS H H 1 7.80 . . 1 . . . . . . . . 4293 1 925 . 1 1 134 134 LYS HA H 1 4.20 . . 1 . . . . . . . . 4293 1 926 . 1 1 134 134 LYS HB2 H 1 1.87 . . 2 . . . . . . . . 4293 1 927 . 1 1 134 134 LYS HG2 H 1 1.36 . . 2 . . . . . . . . 4293 1 928 . 1 1 134 134 LYS HD2 H 1 1.66 . . 2 . . . . . . . . 4293 1 929 . 1 1 134 134 LYS CA C 13 55.89 . . 1 . . . . . . . . 4293 1 930 . 1 1 134 134 LYS CB C 13 32.69 . . 1 . . . . . . . . 4293 1 931 . 1 1 134 134 LYS N N 15 126.1 . . 1 . . . . . . . . 4293 1 stop_ save_ save_chemical_shift_assignments_for_minor_conformer_of_E9_DNase _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignments_for_minor_conformer_of_E9_DNase _Assigned_chem_shift_list.Entry_ID 4293 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_one _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 ; Assignments refer to the minor conformational species of E9 DNase. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4293 2 . . 2 $sample_two . 4293 2 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 . 2 1 10 10 LYS C C 13 176.20 . . 1 . . . . . . . . 4293 2 2 . 2 1 10 10 LYS CA C 13 54.98 . . 1 . . . . . . . . 4293 2 3 . 2 1 10 10 LYS CB C 13 32.27 . . 1 . . . . . . . . 4293 2 4 . 2 1 11 11 ALA H H 1 8.45 . . 1 . . . . . . . . 4293 2 5 . 2 1 11 11 ALA CA C 13 51.36 . . 1 . . . . . . . . 4293 2 6 . 2 1 11 11 ALA CB C 13 18.53 . . 1 . . . . . . . . 4293 2 7 . 2 1 11 11 ALA N N 15 126.1 . . 1 . . . . . . . . 4293 2 8 . 2 1 15 15 GLY H H 1 9.07 . . 1 . . . . . . . . 4293 2 9 . 2 1 15 15 GLY HA2 H 1 3.85 . . 1 . . . . . . . . 4293 2 10 . 2 1 15 15 GLY HA3 H 1 3.69 . . 1 . . . . . . . . 4293 2 11 . 2 1 15 15 GLY C C 13 173.47 . . 1 . . . . . . . . 4293 2 12 . 2 1 15 15 GLY CA C 13 43.79 . . 1 . . . . . . . . 4293 2 13 . 2 1 15 15 GLY N N 15 107.2 . . 1 . . . . . . . . 4293 2 14 . 2 1 18 18 VAL H H 1 8.67 . . 1 . . . . . . . . 4293 2 15 . 2 1 18 18 VAL HA H 1 4.30 . . 1 . . . . . . . . 4293 2 16 . 2 1 18 18 VAL CA C 13 57.80 . . 1 . . . . . . . . 4293 2 17 . 2 1 18 18 VAL CB C 13 34.1 . . 1 . . . . . . . . 4293 2 18 . 2 1 18 18 VAL N N 15 119.3 . . 1 . . . . . . . . 4293 2 19 . 2 1 19 19 GLY H H 1 8.41 . . 1 . . . . . . . . 4293 2 20 . 2 1 19 19 GLY HA2 H 1 4.54 . . 1 . . . . . . . . 4293 2 21 . 2 1 19 19 GLY HA3 H 1 3.86 . . 1 . . . . . . . . 4293 2 22 . 2 1 19 19 GLY C C 13 174.25 . . 1 . . . . . . . . 4293 2 23 . 2 1 19 19 GLY CA C 13 42.82 . . 1 . . . . . . . . 4293 2 24 . 2 1 19 19 GLY N N 15 109.4 . . 1 . . . . . . . . 4293 2 25 . 2 1 20 20 ASP H H 1 8.37 . . 1 . . . . . . . . 4293 2 26 . 2 1 20 20 ASP HA H 1 4.47 . . 1 . . . . . . . . 4293 2 27 . 2 1 20 20 ASP HB2 H 1 2.79 . . 2 . . . . . . . . 4293 2 28 . 2 1 20 20 ASP C C 13 177.16 . . 1 . . . . . . . . 4293 2 29 . 2 1 20 20 ASP CA C 13 55.16 . . 1 . . . . . . . . 4293 2 30 . 2 1 20 20 ASP CB C 13 39.89 . . 1 . . . . . . . . 4293 2 31 . 2 1 20 20 ASP N N 15 116.2 . . 1 . . . . . . . . 4293 2 32 . 2 1 21 21 LYS H H 1 8.47 . . 1 . . . . . . . . 4293 2 33 . 2 1 21 21 LYS HA H 1 4.64 . . 1 . . . . . . . . 4293 2 34 . 2 1 21 21 LYS HB2 H 1 1.71 . . 2 . . . . . . . . 4293 2 35 . 2 1 21 21 LYS C C 13 175.83 . . 1 . . . . . . . . 4293 2 36 . 2 1 21 21 LYS CA C 13 54.71 . . 1 . . . . . . . . 4293 2 37 . 2 1 21 21 LYS CB C 13 29.54 . . 1 . . . . . . . . 4293 2 38 . 2 1 21 21 LYS N N 15 122.4 . . 1 . . . . . . . . 4293 2 39 . 2 1 22 22 TRP H H 1 7.80 . . 1 . . . . . . . . 4293 2 40 . 2 1 22 22 TRP HA H 1 4.38 . . 1 . . . . . . . . 4293 2 41 . 2 1 22 22 TRP HE1 H 1 10.5 . . 1 . . . . . . . . 4293 2 42 . 2 1 22 22 TRP C C 13 176.86 . . 1 . . . . . . . . 4293 2 43 . 2 1 22 22 TRP CA C 13 59.22 . . 1 . . . . . . . . 4293 2 44 . 2 1 22 22 TRP CB C 13 26.47 . . 1 . . . . . . . . 4293 2 45 . 2 1 22 22 TRP N N 15 122.1 . . 1 . . . . . . . . 4293 2 46 . 2 1 22 22 TRP NE1 N 15 129.9 . . 1 . . . . . . . . 4293 2 47 . 2 1 23 23 LEU H H 1 7.48 . . 1 . . . . . . . . 4293 2 48 . 2 1 23 23 LEU HA H 1 3.26 . . 1 . . . . . . . . 4293 2 49 . 2 1 23 23 LEU C C 13 180.80 . . 1 . . . . . . . . 4293 2 50 . 2 1 23 23 LEU CA C 13 55.21 . . 1 . . . . . . . . 4293 2 51 . 2 1 23 23 LEU CB C 13 38.05 . . 1 . . . . . . . . 4293 2 52 . 2 1 23 23 LEU N N 15 119.1 . . 1 . . . . . . . . 4293 2 53 . 2 1 24 24 ASP H H 1 8.42 . . 1 . . . . . . . . 4293 2 54 . 2 1 24 24 ASP HA H 1 4.34 . . 1 . . . . . . . . 4293 2 55 . 2 1 24 24 ASP HB2 H 1 2.95 . . 1 . . . . . . . . 4293 2 56 . 2 1 24 24 ASP HB3 H 1 2.70 . . 1 . . . . . . . . 4293 2 57 . 2 1 24 24 ASP CA C 13 56.24 . . 1 . . . . . . . . 4293 2 58 . 2 1 24 24 ASP CB C 13 38.52 . . 1 . . . . . . . . 4293 2 59 . 2 1 24 24 ASP N N 15 124.3 . . 1 . . . . . . . . 4293 2 60 . 2 1 25 25 ASP H H 1 7.56 . . 1 . . . . . . . . 4293 2 61 . 2 1 25 25 ASP HA H 1 4.46 . . 1 . . . . . . . . 4293 2 62 . 2 1 25 25 ASP HB2 H 1 2.99 . . 2 . . . . . . . . 4293 2 63 . 2 1 25 25 ASP C C 13 177.28 . . 1 . . . . . . . . 4293 2 64 . 2 1 25 25 ASP CA C 13 55.09 . . 1 . . . . . . . . 4293 2 65 . 2 1 25 25 ASP CB C 13 38.59 . . 1 . . . . . . . . 4293 2 66 . 2 1 25 25 ASP N N 15 119.6 . . 1 . . . . . . . . 4293 2 67 . 2 1 26 26 ALA H H 1 7.48 . . 1 . . . . . . . . 4293 2 68 . 2 1 26 26 ALA HA H 1 4.53 . . 1 . . . . . . . . 4293 2 69 . 2 1 26 26 ALA HB1 H 1 1.39 . . 1 . . . . . . . . 4293 2 70 . 2 1 26 26 ALA HB2 H 1 1.39 . . 1 . . . . . . . . 4293 2 71 . 2 1 26 26 ALA HB3 H 1 1.39 . . 1 . . . . . . . . 4293 2 72 . 2 1 26 26 ALA C C 13 176.97 . . 1 . . . . . . . . 4293 2 73 . 2 1 26 26 ALA CA C 13 53.20 . . 1 . . . . . . . . 4293 2 74 . 2 1 26 26 ALA CB C 13 18.06 . . 1 . . . . . . . . 4293 2 75 . 2 1 26 26 ALA N N 15 120.4 . . 1 . . . . . . . . 4293 2 76 . 2 1 27 27 GLY H H 1 7.46 . . 1 . . . . . . . . 4293 2 77 . 2 1 27 27 GLY HA2 H 1 4.56 . . 1 . . . . . . . . 4293 2 78 . 2 1 27 27 GLY HA3 H 1 3.69 . . 1 . . . . . . . . 4293 2 79 . 2 1 27 27 GLY C C 13 173.11 . . 1 . . . . . . . . 4293 2 80 . 2 1 27 27 GLY CA C 13 43.30 . . 1 . . . . . . . . 4293 2 81 . 2 1 27 27 GLY N N 15 102.2 . . 1 . . . . . . . . 4293 2 82 . 2 1 28 28 LYS H H 1 7.63 . . 1 . . . . . . . . 4293 2 83 . 2 1 28 28 LYS HA H 1 4.66 . . 1 . . . . . . . . 4293 2 84 . 2 1 28 28 LYS HB2 H 1 1.86 . . 1 . . . . . . . . 4293 2 85 . 2 1 28 28 LYS HB3 H 1 1.75 . . 1 . . . . . . . . 4293 2 86 . 2 1 28 28 LYS HG2 H 1 1.39 . . 2 . . . . . . . . 4293 2 87 . 2 1 28 28 LYS C C 13 173.8 . . 1 . . . . . . . . 4293 2 88 . 2 1 28 28 LYS CA C 13 53.29 . . 1 . . . . . . . . 4293 2 89 . 2 1 28 28 LYS CB C 13 35.04 . . 1 . . . . . . . . 4293 2 90 . 2 1 28 28 LYS N N 15 120.0 . . 1 . . . . . . . . 4293 2 91 . 2 1 30 30 SER H H 1 8.28 . . 1 . . . . . . . . 4293 2 92 . 2 1 30 30 SER HA H 1 4.57 . . 1 . . . . . . . . 4293 2 93 . 2 1 30 30 SER HB2 H 1 3.95 . . 2 . . . . . . . . 4293 2 94 . 2 1 30 30 SER C C 13 173.97 . . 1 . . . . . . . . 4293 2 95 . 2 1 30 30 SER CA C 13 57.07 . . 1 . . . . . . . . 4293 2 96 . 2 1 30 30 SER CB C 13 61.97 . . 1 . . . . . . . . 4293 2 97 . 2 1 30 30 SER N N 15 118.3 . . 1 . . . . . . . . 4293 2 98 . 2 1 36 36 ASP H H 1 8.69 . . 1 . . . . . . . . 4293 2 99 . 2 1 36 36 ASP C C 13 178.33 . . 1 . . . . . . . . 4293 2 100 . 2 1 36 36 ASP CA C 13 55.11 . . 1 . . . . . . . . 4293 2 101 . 2 1 36 36 ASP CB C 13 36.81 . . 1 . . . . . . . . 4293 2 102 . 2 1 36 36 ASP N N 15 130.9 . . 1 . . . . . . . . 4293 2 103 . 2 1 37 37 ARG H H 1 8.30 . . 1 . . . . . . . . 4293 2 104 . 2 1 37 37 ARG HA H 1 4.10 . . 1 . . . . . . . . 4293 2 105 . 2 1 37 37 ARG N N 15 118.9 . . 1 . . . . . . . . 4293 2 106 . 2 1 39 39 ALA H H 1 8.14 . . 1 . . . . . . . . 4293 2 107 . 2 1 39 39 ALA HA H 1 3.95 . . 1 . . . . . . . . 4293 2 108 . 2 1 39 39 ALA HB1 H 1 1.15 . . 1 . . . . . . . . 4293 2 109 . 2 1 39 39 ALA HB2 H 1 1.15 . . 1 . . . . . . . . 4293 2 110 . 2 1 39 39 ALA HB3 H 1 1.15 . . 1 . . . . . . . . 4293 2 111 . 2 1 39 39 ALA CA C 13 53.84 . . 1 . . . . . . . . 4293 2 112 . 2 1 39 39 ALA CB C 13 15.84 . . 1 . . . . . . . . 4293 2 113 . 2 1 39 39 ALA N N 15 124.8 . . 1 . . . . . . . . 4293 2 114 . 2 1 42 42 LEU H H 1 7.41 . . 1 . . . . . . . . 4293 2 115 . 2 1 42 42 LEU HA H 1 4.42 . . 1 . . . . . . . . 4293 2 116 . 2 1 42 42 LEU HB2 H 1 1.66 . . 2 . . . . . . . . 4293 2 117 . 2 1 42 42 LEU CA C 13 53.80 . . 1 . . . . . . . . 4293 2 118 . 2 1 42 42 LEU CB C 13 42.16 . . 1 . . . . . . . . 4293 2 119 . 2 1 42 42 LEU N N 15 117.7 . . 1 . . . . . . . . 4293 2 120 . 2 1 61 61 VAL H H 1 8.59 . . 1 . . . . . . . . 4293 2 121 . 2 1 61 61 VAL HA H 1 3.42 . . 1 . . . . . . . . 4293 2 122 . 2 1 61 61 VAL C C 13 177.91 . . 1 . . . . . . . . 4293 2 123 . 2 1 61 61 VAL CA C 13 66.44 . . 1 . . . . . . . . 4293 2 124 . 2 1 61 61 VAL N N 15 124.0 . . 1 . . . . . . . . 4293 2 125 . 2 1 62 62 SER H H 1 8.06 . . 1 . . . . . . . . 4293 2 126 . 2 1 62 62 SER HB2 H 1 3.95 . . 2 . . . . . . . . 4293 2 127 . 2 1 62 62 SER C C 13 174.50 . . 1 . . . . . . . . 4293 2 128 . 2 1 62 62 SER CA C 13 60.21 . . 1 . . . . . . . . 4293 2 129 . 2 1 62 62 SER CB C 13 62.35 . . 1 . . . . . . . . 4293 2 130 . 2 1 62 62 SER N N 15 113.4 . . 1 . . . . . . . . 4293 2 131 . 2 1 63 63 LYS H H 1 6.99 . . 1 . . . . . . . . 4293 2 132 . 2 1 63 63 LYS HA H 1 4.22 . . 1 . . . . . . . . 4293 2 133 . 2 1 63 63 LYS HB2 H 1 1.70 . . 2 . . . . . . . . 4293 2 134 . 2 1 63 63 LYS HG2 H 1 1.44 . . 2 . . . . . . . . 4293 2 135 . 2 1 63 63 LYS C C 13 175.37 . . 1 . . . . . . . . 4293 2 136 . 2 1 63 63 LYS CA C 13 55.21 . . 1 . . . . . . . . 4293 2 137 . 2 1 63 63 LYS CB C 13 32.71 . . 1 . . . . . . . . 4293 2 138 . 2 1 63 63 LYS N N 15 119.2 . . 1 . . . . . . . . 4293 2 139 . 2 1 64 64 ASP H H 1 7.70 . . 1 . . . . . . . . 4293 2 140 . 2 1 64 64 ASP HA H 1 5.03 . . 1 . . . . . . . . 4293 2 141 . 2 1 64 64 ASP HB2 H 1 3.14 . . 1 . . . . . . . . 4293 2 142 . 2 1 64 64 ASP HB3 H 1 2.33 . . 1 . . . . . . . . 4293 2 143 . 2 1 64 64 ASP CA C 13 50.24 . . 1 . . . . . . . . 4293 2 144 . 2 1 64 64 ASP CB C 13 42.54 . . 1 . . . . . . . . 4293 2 145 . 2 1 64 64 ASP N N 15 123.7 . . 1 . . . . . . . . 4293 2 146 . 2 1 66 66 GLU C C 13 178.79 . . 1 . . . . . . . . 4293 2 147 . 2 1 66 66 GLU CA C 13 57.20 . . 1 . . . . . . . . 4293 2 148 . 2 1 66 66 GLU CB C 13 29.60 . . 1 . . . . . . . . 4293 2 149 . 2 1 67 67 LEU H H 1 8.70 . . 1 . . . . . . . . 4293 2 150 . 2 1 67 67 LEU HA H 1 4.32 . . 1 . . . . . . . . 4293 2 151 . 2 1 67 67 LEU C C 13 179.51 . . 1 . . . . . . . . 4293 2 152 . 2 1 67 67 LEU CA C 13 55.36 . . 1 . . . . . . . . 4293 2 153 . 2 1 67 67 LEU CB C 13 40.85 . . 1 . . . . . . . . 4293 2 154 . 2 1 67 67 LEU N N 15 118.8 . . 1 . . . . . . . . 4293 2 155 . 2 1 68 68 SER H H 1 8.07 . . 1 . . . . . . . . 4293 2 156 . 2 1 68 68 SER HA H 1 4.47 . . 1 . . . . . . . . 4293 2 157 . 2 1 68 68 SER HB2 H 1 4.21 . . 1 . . . . . . . . 4293 2 158 . 2 1 68 68 SER HB3 H 1 4.16 . . 1 . . . . . . . . 4293 2 159 . 2 1 68 68 SER C C 13 175.49 . . 1 . . . . . . . . 4293 2 160 . 2 1 68 68 SER CA C 13 57.39 . . 1 . . . . . . . . 4293 2 161 . 2 1 68 68 SER CB C 13 63.49 . . 1 . . . . . . . . 4293 2 162 . 2 1 68 68 SER N N 15 110.8 . . 1 . . . . . . . . 4293 2 163 . 2 1 69 69 LYS H H 1 7.21 . . 1 . . . . . . . . 4293 2 164 . 2 1 69 69 LYS HA H 1 4.15 . . 1 . . . . . . . . 4293 2 165 . 2 1 69 69 LYS HB2 H 1 1.96 . . 2 . . . . . . . . 4293 2 166 . 2 1 69 69 LYS HG2 H 1 1.54 . . 1 . . . . . . . . 4293 2 167 . 2 1 69 69 LYS HG3 H 1 1.44 . . 1 . . . . . . . . 4293 2 168 . 2 1 69 69 LYS HD2 H 1 1.77 . . 2 . . . . . . . . 4293 2 169 . 2 1 69 69 LYS C C 13 177.14 . . 1 . . . . . . . . 4293 2 170 . 2 1 69 69 LYS CA C 13 58.82 . . 1 . . . . . . . . 4293 2 171 . 2 1 69 69 LYS CB C 13 32.13 . . 1 . . . . . . . . 4293 2 172 . 2 1 69 69 LYS N N 15 123.9 . . 1 . . . . . . . . 4293 2 173 . 2 1 70 70 ASN H H 1 8.74 . . 1 . . . . . . . . 4293 2 174 . 2 1 70 70 ASN HA H 1 4.91 . . 1 . . . . . . . . 4293 2 175 . 2 1 70 70 ASN HB2 H 1 3.06 . . 1 . . . . . . . . 4293 2 176 . 2 1 70 70 ASN HB3 H 1 2.79 . . 1 . . . . . . . . 4293 2 177 . 2 1 70 70 ASN CA C 13 52.07 . . 1 . . . . . . . . 4293 2 178 . 2 1 70 70 ASN CB C 13 38.03 . . 1 . . . . . . . . 4293 2 179 . 2 1 70 70 ASN N N 15 114.1 . . 1 . . . . . . . . 4293 2 180 . 2 1 71 71 LEU H H 1 7.39 . . 1 . . . . . . . . 4293 2 181 . 2 1 71 71 LEU HA H 1 4.52 . . 1 . . . . . . . . 4293 2 182 . 2 1 71 71 LEU HB2 H 1 1.99 . . 2 . . . . . . . . 4293 2 183 . 2 1 71 71 LEU HD11 H 1 0.87 . . 1 . . . . . . . . 4293 2 184 . 2 1 71 71 LEU HD12 H 1 0.87 . . 1 . . . . . . . . 4293 2 185 . 2 1 71 71 LEU HD13 H 1 0.87 . . 1 . . . . . . . . 4293 2 186 . 2 1 71 71 LEU HD21 H 1 0.78 . . 1 . . . . . . . . 4293 2 187 . 2 1 71 71 LEU HD22 H 1 0.78 . . 1 . . . . . . . . 4293 2 188 . 2 1 71 71 LEU HD23 H 1 0.78 . . 1 . . . . . . . . 4293 2 189 . 2 1 71 71 LEU CA C 13 53.30 . . 1 . . . . . . . . 4293 2 190 . 2 1 71 71 LEU CB C 13 41.50 . . 1 . . . . . . . . 4293 2 191 . 2 1 71 71 LEU N N 15 120.1 . . 1 . . . . . . . . 4293 2 192 . 2 1 76 76 LYS H H 1 8.91 . . 1 . . . . . . . . 4293 2 193 . 2 1 76 76 LYS HA H 1 4.04 . . 1 . . . . . . . . 4293 2 194 . 2 1 76 76 LYS HB2 H 1 1.90 . . 2 . . . . . . . . 4293 2 195 . 2 1 76 76 LYS C C 13 178.8 . . 1 . . . . . . . . 4293 2 196 . 2 1 76 76 LYS CA C 13 58.75 . . 1 . . . . . . . . 4293 2 197 . 2 1 76 76 LYS CB C 13 31.61 . . 1 . . . . . . . . 4293 2 198 . 2 1 76 76 LYS N N 15 122.7 . . 1 . . . . . . . . 4293 2 199 . 2 1 78 78 SER H H 1 8.13 . . 1 . . . . . . . . 4293 2 200 . 2 1 78 78 SER HA H 1 4.25 . . 1 . . . . . . . . 4293 2 201 . 2 1 78 78 SER HB2 H 1 3.95 . . 1 . . . . . . . . 4293 2 202 . 2 1 78 78 SER HB3 H 1 3.71 . . 1 . . . . . . . . 4293 2 203 . 2 1 78 78 SER C C 13 176.56 . . 1 . . . . . . . . 4293 2 204 . 2 1 78 78 SER CA C 13 61.45 . . 1 . . . . . . . . 4293 2 205 . 2 1 78 78 SER N N 15 118.4 . . 1 . . . . . . . . 4293 2 206 . 2 1 80 80 SER H H 1 7.81 . . 1 . . . . . . . . 4293 2 207 . 2 1 80 80 SER HA H 1 4.48 . . 1 . . . . . . . . 4293 2 208 . 2 1 80 80 SER HB2 H 1 4.06 . . 2 . . . . . . . . 4293 2 209 . 2 1 80 80 SER C C 13 175.29 . . 1 . . . . . . . . 4293 2 210 . 2 1 80 80 SER CA C 13 59.90 . . 1 . . . . . . . . 4293 2 211 . 2 1 80 80 SER CB C 13 61.69 . . 1 . . . . . . . . 4293 2 212 . 2 1 80 80 SER N N 15 116.7 . . 1 . . . . . . . . 4293 2 213 . 2 1 81 81 LYS H H 1 7.25 . . 1 . . . . . . . . 4293 2 214 . 2 1 81 81 LYS HA H 1 4.43 . . 1 . . . . . . . . 4293 2 215 . 2 1 81 81 LYS HB2 H 1 1.71 . . 2 . . . . . . . . 4293 2 216 . 2 1 81 81 LYS C C 13 176.13 . . 1 . . . . . . . . 4293 2 217 . 2 1 81 81 LYS CA C 13 54.29 . . 1 . . . . . . . . 4293 2 218 . 2 1 81 81 LYS CB C 13 32.36 . . 1 . . . . . . . . 4293 2 219 . 2 1 81 81 LYS N N 15 119.8 . . 1 . . . . . . . . 4293 2 220 . 2 1 87 87 THR H H 1 8.20 . . 1 . . . . . . . . 4293 2 221 . 2 1 87 87 THR HA H 1 4.31 . . 1 . . . . . . . . 4293 2 222 . 2 1 87 87 THR CA C 13 58.98 . . 1 . . . . . . . . 4293 2 223 . 2 1 87 87 THR N N 15 112.1 . . 1 . . . . . . . . 4293 2 224 . 2 1 96 96 ARG H H 1 8.15 . . 1 . . . . . . . . 4293 2 225 . 2 1 96 96 ARG HA H 1 4.25 . . 1 . . . . . . . . 4293 2 226 . 2 1 96 96 ARG HB2 H 1 2.21 . . 2 . . . . . . . . 4293 2 227 . 2 1 96 96 ARG C C 13 176.06 . . 1 . . . . . . . . 4293 2 228 . 2 1 96 96 ARG CA C 13 55.00 . . 1 . . . . . . . . 4293 2 229 . 2 1 96 96 ARG CB C 13 29.83 . . 1 . . . . . . . . 4293 2 230 . 2 1 96 96 ARG N N 15 121.1 . . 1 . . . . . . . . 4293 2 231 . 2 1 99 99 TYR H H 1 8.22 . . 1 . . . . . . . . 4293 2 232 . 2 1 99 99 TYR CA C 13 56.08 . . 1 . . . . . . . . 4293 2 233 . 2 1 99 99 TYR CB C 13 38.09 . . 1 . . . . . . . . 4293 2 234 . 2 1 99 99 TYR N N 15 124.3 . . 1 . . . . . . . . 4293 2 235 . 2 1 121 121 VAL H H 1 9.99 . . 1 . . . . . . . . 4293 2 236 . 2 1 121 121 VAL HA H 1 5.09 . . 1 . . . . . . . . 4293 2 237 . 2 1 121 121 VAL HB H 1 1.83 . . 1 . . . . . . . . 4293 2 238 . 2 1 121 121 VAL HG11 H 1 0.83 . . 2 . . . . . . . . 4293 2 239 . 2 1 121 121 VAL HG12 H 1 0.83 . . 2 . . . . . . . . 4293 2 240 . 2 1 121 121 VAL HG13 H 1 0.83 . . 2 . . . . . . . . 4293 2 241 . 2 1 121 121 VAL C C 13 176.73 . . 1 . . . . . . . . 4293 2 242 . 2 1 121 121 VAL CA C 13 59.42 . . 1 . . . . . . . . 4293 2 243 . 2 1 121 121 VAL CB C 13 31.50 . . 1 . . . . . . . . 4293 2 244 . 2 1 121 121 VAL N N 15 123.6 . . 1 . . . . . . . . 4293 2 245 . 2 1 122 122 THR H H 1 9.70 . . 1 . . . . . . . . 4293 2 246 . 2 1 122 122 THR HA H 1 6.07 . . 1 . . . . . . . . 4293 2 247 . 2 1 122 122 THR HB H 1 4.45 . . 1 . . . . . . . . 4293 2 248 . 2 1 122 122 THR HG21 H 1 1.22 . . 1 . . . . . . . . 4293 2 249 . 2 1 122 122 THR HG22 H 1 1.22 . . 1 . . . . . . . . 4293 2 250 . 2 1 122 122 THR HG23 H 1 1.22 . . 1 . . . . . . . . 4293 2 251 . 2 1 122 122 THR C C 13 175.69 . . 1 . . . . . . . . 4293 2 252 . 2 1 122 122 THR CA C 13 58.36 . . 1 . . . . . . . . 4293 2 253 . 2 1 122 122 THR CB C 13 70.70 . . 1 . . . . . . . . 4293 2 254 . 2 1 122 122 THR N N 15 117.2 . . 1 . . . . . . . . 4293 2 255 . 2 1 132 132 ARG C C 13 176.37 . . 1 . . . . . . . . 4293 2 256 . 2 1 132 132 ARG CA C 13 55.18 . . 1 . . . . . . . . 4293 2 257 . 2 1 132 132 ARG CB C 13 29.82 . . 1 . . . . . . . . 4293 2 258 . 2 1 133 133 GLY H H 1 8.41 . . 1 . . . . . . . . 4293 2 259 . 2 1 133 133 GLY HA2 H 1 3.94 . . 2 . . . . . . . . 4293 2 260 . 2 1 133 133 GLY C C 13 172.84 . . 1 . . . . . . . . 4293 2 261 . 2 1 133 133 GLY CA C 13 43.99 . . 1 . . . . . . . . 4293 2 262 . 2 1 133 133 GLY N N 15 111.2 . . 1 . . . . . . . . 4293 2 263 . 2 1 134 134 LYS H H 1 7.84 . . 1 . . . . . . . . 4293 2 264 . 2 1 134 134 LYS HA H 1 4.20 . . 1 . . . . . . . . 4293 2 265 . 2 1 134 134 LYS HB2 H 1 1.87 . . 2 . . . . . . . . 4293 2 266 . 2 1 134 134 LYS HG2 H 1 1.36 . . 2 . . . . . . . . 4293 2 267 . 2 1 134 134 LYS HD2 H 1 1.66 . . 2 . . . . . . . . 4293 2 268 . 2 1 134 134 LYS CA C 13 55.89 . . 1 . . . . . . . . 4293 2 269 . 2 1 134 134 LYS CB C 13 32.69 . . 1 . . . . . . . . 4293 2 270 . 2 1 134 134 LYS N N 15 126.1 . . 1 . . . . . . . . 4293 2 stop_ save_