data_4802 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4802 _Entry.Title ; 1H, 13C, and 15N sequential assignment of the triple labelled N-terminal domain of the Histone like Nucleoid Structuring protein (H-NS) from Salmonella typhimurium (first 64 residues of the protein) ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-08-09 _Entry.Accession_date 2000-08-10 _Entry.Last_release_date 2001-01-23 _Entry.Original_release_date 2001-01-23 _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 Debora Renzoni . . . 4802 2 Diego Esposito . . . 4802 3 Mark Pfuhl . . . 4802 4 Christopher Higgins . F. . 4802 5 Paul Driscoll . C. . 4802 6 John Ladbury . E. . 4802 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4802 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 123 4802 '13C chemical shifts' 168 4802 '15N chemical shifts' 62 4802 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-01-23 2000-08-09 original author . 4802 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4802 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Structural Insight to the Oligomerisation of the Bacterial Chromatin-Structuring Protein H-N ; _Citation.Status 'in preparation' _Citation.Type journal _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 . 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 Debora Renzoni . . . 4802 1 2 Diego Esposito . . . 4802 1 3 Mark Pfuhl . . . 4802 1 4 Christopher Higgins . F. . 4802 1 5 Paul Driscoll . C. . 4802 1 6 John Ladbury . E. . 4802 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'nuclear magnetic resonance' 4802 1 'secondary structure' 4802 1 coiled-coil 4802 1 'general topology' 4802 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4802 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10844682 _Citation.Full_citation ; Smyth, C. P., Lundback, T., Renzoni, D., Siligardi, G., Beavil, R., Layton, M., Sidebotham, J. M., Hinton, J. C., Driscoll, P. C., Higgins, C. F. and Ladbury, J. E. (2000) Oligomerisation of the chromatin-structuring protein H-NS. Mol. Microbiol. 36, 962-972. ; _Citation.Title 'Oligomerization of the chromatin-structuring protein H-NS.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Mol. Microbiol.' _Citation.Journal_name_full 'Molecular microbiology' _Citation.Journal_volume 36 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0950-382X _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 962 _Citation.Page_last 972 _Citation.Year 2000 _Citation.Details ; H-NS is a major component of the bacterial nucleoid, involved in condensing and packaging DNA and modulating gene expression. The mechanism by which this is achieved remains unclear. Genetic data show that the biological properties of H-NS are influenced by its oligomerization properties. We have applied a variety of biophysical techniques to study the structural basis of oligomerization of the H-NS protein from Salmonella typhimurium. The N-terminal 89 amino acids are responsible for oligomerization. The first 64 residues form a trimer dominated by an alpha-helix, likely to be in coiled-coil conformation. Extending this polypeptide to 89 amino acids generated higher order, heterodisperse oligomers. Similarly, in the full-length protein no single, defined oligomeric state is adopted. The C-terminal 48 residues do not participate in oligomerization and form a monomeric, DNA-binding domain. These N- and C-terminal domains are joined via a flexible linker which enables them to function independently within the context of the full-length protein. This novel mode of oligomerization may account for the unusual binding properties of H-NS. ; 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 'C. P.' Smyth C. P. . 4802 2 2 T. Lundback T. . . 4802 2 3 D. Renzoni D. . . 4802 2 4 G. Siligardi G. . . 4802 2 5 R. Beavil R. . . 4802 2 6 M. Layton M. . . 4802 2 7 'J. M.' Sidebotham J. M. . 4802 2 8 'J. C.' Hinton J. C. . 4802 2 9 'P. C.' Driscoll P. C. . 4802 2 10 'C. F.' Higgins C. F. . 4802 2 11 'J. E.' Ladbury J. E. . 4802 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4802 _Citation.ID 3 _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 GW, Zhu G, Pfeifer J, Bax A. Related Articles NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _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. . . 4802 3 2 S Grzesiek S. . . 4802 3 3 'G W' Vuister G. W. . 4802 3 4 G Zhu G. . . 4802 3 5 J Pfeifer J. . . 4802 3 6 A Bax A. . . 4802 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4802 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Boucher, W. (1996) AZARA v2.0, Department of Biochemistry, University of Cambridge, UK. ; _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_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4802 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kraulis, P. (1989) ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive graphics. J. Magn. Reson. 24, 627-633. ; _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_ ############################################# # Molecular system (assembly) description # ############################################# save_system_H-NS(1-64) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_H-NS(1-64) _Assembly.Entry_ID 4802 _Assembly.ID 1 _Assembly.Name 'N-terminal domain of H-NS' _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 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID trimer 4802 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 'H-NS(1-64) monomer 1' 1 $H-NS(1-64) . . . native . . 1 . . 4802 1 2 'H-NS(1-64) monomer 2' 1 $H-NS(1-64) . . . native . . 1 . . 4802 1 3 'H-NS(1-64) monomer 3' 1 $H-NS(1-64) . . . native . . 1 . . 4802 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'N-terminal domain of H-NS' system 4802 1 H-NS(1-64) abbreviation 4802 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'oligomerisation of H-NS' 4802 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_H-NS(1-64) _Entity.Sf_category entity _Entity.Sf_framecode H-NS(1-64) _Entity.Entry_ID 4802 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name "Oligomerisation domain of the 'histone' like nucleoid structuring protein" _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 ; SEALKILNNIRTLRAQARES TLETLEEMLEKLEVVVNERR EEESAAAAEVEERTRKLQQY REML ; _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 64 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 7958 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details 'H-NS(1-64) self-associates to form a discrete trimeric state' _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 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 18814 . H-NS . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 2 no BMRB 5390 . H-NS . . . . . 89.06 61 100.00 100.00 2.67e-14 . . . . 4802 1 3 no PDB 1LR1 . "Solution Structure Of The Oligomerization Domain Of The Bacterial Chromatin-Structuring Protein H-Ns" . . . . . 89.06 61 100.00 100.00 2.67e-14 . . . . 4802 1 4 no PDB 1NI8 . "H-Ns Dimerization Motif" . . . . . 71.88 46 97.83 97.83 1.15e-18 . . . . 4802 1 5 no PDB 3NR7 . "Crystal Structure Of S. Typhimurium H-Ns 1-83" . . . . . 100.00 86 100.00 100.00 2.97e-32 . . . . 4802 1 6 no DBJ BAA36117 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 7 no DBJ BAB35162 . "DNA-binding protein H-NS [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 8 no DBJ BAG76811 . "DNA-binding protein [Escherichia coli SE11]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 9 no DBJ BAI25048 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 137 98.44 98.44 2.58e-19 . . . . 4802 1 10 no DBJ BAI30173 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 11 no EMBL CAA30530 . "unnamed protein product [Escherichia coli]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 12 no EMBL CAA31522 . "unnamed protein product [Shigella flexneri]" . . . . . 57.81 109 100.00 100.00 2.63e-02 . . . . 4802 1 13 no EMBL CAA32549 . "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 14 no EMBL CAA40507 . "DNA-binding protein OsmZ [H-NS(H1a)] [Escherichia coli]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 15 no EMBL CAA42565 . "histone-like protein H-NS [Escherichia coli K-12]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 16 no GB AAB61148 . "histone H1-like protein [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 17 no GB AAC74319 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 18 no GB AAG56094 . "DNA-binding protein HLP-II (HU, BH2, HD, NS); pleiotropic regulator [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 19 no GB AAL20669 . "DNA-binding protein HLP-II [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 20 no GB AAN42850 . "DNA-binding protein HLP-II (HU, BH2, HD, NS); pleiotropic regulator [Shigella flexneri 2a str. 301]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 21 no PIR AC0650 . "DNA-binding protein (histone-like protein Hlp-II) [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 22 no PRF 1607341A . "drdX gene" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 23 no REF NP_287482 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 24 no REF NP_309766 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 25 no REF NP_415753 . "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 26 no REF NP_455749 . "DNA-binding protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 27 no REF NP_460710 . "DNA-binding protein H-NS [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 28 no SP P09120 . "RecName: Full=DNA-binding protein H-NS; AltName: Full=Pathogenesis protein KcpA [Shigella flexneri]" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 29 no SP P0A1S2 . "RecName: Full=DNA-binding protein H-NS; AltName: Full=Histone-like protein HLP-II; AltName: Full=Protein B1; AltName: Full=Prot" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 30 no SP P0A1S3 . "RecName: Full=DNA-binding protein H-NS; AltName: Full=Histone-like protein HLP-II; AltName: Full=Protein B1; AltName: Full=Prot" . . . . . 100.00 137 98.44 98.44 4.43e-19 . . . . 4802 1 31 no SP P0ACF8 . "RecName: Full=DNA-binding protein H-NS; AltName: Full=Histone-like protein HLP-II; AltName: Full=Protein B1; AltName: Full=Prot" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 32 no SP P0ACF9 . "RecName: Full=DNA-binding protein H-NS; AltName: Full=Histone-like protein HLP-II; AltName: Full=Protein B1; AltName: Full=Prot" . . . . . 100.00 137 98.44 98.44 2.72e-19 . . . . 4802 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID "Oligomerisation domain of the 'histone' like nucleoid structuring protein" common 4802 1 H-NS(1-64) abbreviation 4802 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 . SER . 4802 1 2 . GLU . 4802 1 3 . ALA . 4802 1 4 . LEU . 4802 1 5 . LYS . 4802 1 6 . ILE . 4802 1 7 . LEU . 4802 1 8 . ASN . 4802 1 9 . ASN . 4802 1 10 . ILE . 4802 1 11 . ARG . 4802 1 12 . THR . 4802 1 13 . LEU . 4802 1 14 . ARG . 4802 1 15 . ALA . 4802 1 16 . GLN . 4802 1 17 . ALA . 4802 1 18 . ARG . 4802 1 19 . GLU . 4802 1 20 . SER . 4802 1 21 . THR . 4802 1 22 . LEU . 4802 1 23 . GLU . 4802 1 24 . THR . 4802 1 25 . LEU . 4802 1 26 . GLU . 4802 1 27 . GLU . 4802 1 28 . MET . 4802 1 29 . LEU . 4802 1 30 . GLU . 4802 1 31 . LYS . 4802 1 32 . LEU . 4802 1 33 . GLU . 4802 1 34 . VAL . 4802 1 35 . VAL . 4802 1 36 . VAL . 4802 1 37 . ASN . 4802 1 38 . GLU . 4802 1 39 . ARG . 4802 1 40 . ARG . 4802 1 41 . GLU . 4802 1 42 . GLU . 4802 1 43 . GLU . 4802 1 44 . SER . 4802 1 45 . ALA . 4802 1 46 . ALA . 4802 1 47 . ALA . 4802 1 48 . ALA . 4802 1 49 . GLU . 4802 1 50 . VAL . 4802 1 51 . GLU . 4802 1 52 . GLU . 4802 1 53 . ARG . 4802 1 54 . THR . 4802 1 55 . ARG . 4802 1 56 . LYS . 4802 1 57 . LEU . 4802 1 58 . GLN . 4802 1 59 . GLN . 4802 1 60 . TYR . 4802 1 61 . ARG . 4802 1 62 . GLU . 4802 1 63 . MET . 4802 1 64 . LEU . 4802 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 . SER 1 1 4802 1 . GLU 2 2 4802 1 . ALA 3 3 4802 1 . LEU 4 4 4802 1 . LYS 5 5 4802 1 . ILE 6 6 4802 1 . LEU 7 7 4802 1 . ASN 8 8 4802 1 . ASN 9 9 4802 1 . ILE 10 10 4802 1 . ARG 11 11 4802 1 . THR 12 12 4802 1 . LEU 13 13 4802 1 . ARG 14 14 4802 1 . ALA 15 15 4802 1 . GLN 16 16 4802 1 . ALA 17 17 4802 1 . ARG 18 18 4802 1 . GLU 19 19 4802 1 . SER 20 20 4802 1 . THR 21 21 4802 1 . LEU 22 22 4802 1 . GLU 23 23 4802 1 . THR 24 24 4802 1 . LEU 25 25 4802 1 . GLU 26 26 4802 1 . GLU 27 27 4802 1 . MET 28 28 4802 1 . LEU 29 29 4802 1 . GLU 30 30 4802 1 . LYS 31 31 4802 1 . LEU 32 32 4802 1 . GLU 33 33 4802 1 . VAL 34 34 4802 1 . VAL 35 35 4802 1 . VAL 36 36 4802 1 . ASN 37 37 4802 1 . GLU 38 38 4802 1 . ARG 39 39 4802 1 . ARG 40 40 4802 1 . GLU 41 41 4802 1 . GLU 42 42 4802 1 . GLU 43 43 4802 1 . SER 44 44 4802 1 . ALA 45 45 4802 1 . ALA 46 46 4802 1 . ALA 47 47 4802 1 . ALA 48 48 4802 1 . GLU 49 49 4802 1 . VAL 50 50 4802 1 . GLU 51 51 4802 1 . GLU 52 52 4802 1 . ARG 53 53 4802 1 . THR 54 54 4802 1 . ARG 55 55 4802 1 . LYS 56 56 4802 1 . LEU 57 57 4802 1 . GLN 58 58 4802 1 . GLN 59 59 4802 1 . TYR 60 60 4802 1 . ARG 61 61 4802 1 . GLU 62 62 4802 1 . MET 63 63 4802 1 . LEU 64 64 4802 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 4802 _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 $H-NS(1-64) . 602 organism . 'Salmonella typhimurium' 'Salmonella typhimurium' . . Eubacteria . Salmonella typhimurium . . . . . . . . . . . . . . . . hns . . . . 4802 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 4802 _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 $H-NS(1-64) . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 'lambda DE3' . . . . . . . . . . . plasmid . . pET14b . . . . . . 4802 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4802 _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 "Oligomerisation domain of the 'histone' like nucleoid structuring protein" '[U-13C; U-15N; U-2H]' . . 1 $H-NS(1-64) . . 1.5 1.0 2.0 mM . . . . 4802 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4802 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; The sample was equilibrated for 25 minutes under these conditions before the spectra were collected ; 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 7.0 0 n/a 4802 1 temperature 298 0.4 K 4802 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Software.Sf_category software _Software.Sf_framecode NMRPIPE _Software.Entry_ID 4802 _Software.ID 1 _Software.Name NMRPIPE _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 4802 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 4802 1 stop_ save_ save_AZARA _Software.Sf_category software _Software.Sf_framecode AZARA _Software.Entry_ID 4802 _Software.ID 2 _Software.Name AZARA _Software.Version 2.0 _Software.Details . loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_3 4802 2 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 4802 _Software.ID 3 _Software.Name ANSIG _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignment' 4802 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 5 $ref_4 4802 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4802 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITYplus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 4802 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITYplus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 4802 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4802 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian UNITYplus . 500 . . . 4802 1 2 spectrometer_2 Varian UNITYplus . 600 . . . 4802 1 3 spectrometer_3 Bruker AVANCE . 800 . . . 4802 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 4802 _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-1H NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 2 '1H-1H TOCSY' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 3 '1H-15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 4 '15N NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 5 '15N TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 6 '15N-15N HSQC-NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 7 HNHA . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 8 '13C NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 9 '13C HCCH-TOCSY' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 10 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 11 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 12 HNCOCA . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 13 HNCACO . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 14 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 15 HNCOCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 16 'HCCH 13C-13C NOE' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 17 'The triple resonance experiments were recorded on triple labelled samples (2H/15N/13C).' . . . . . . . . . . . 1 $sample_1 . . . 1 $Ex-cond_1 . . . . . . . . . . . . . . . . . . . . . 4802 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4802 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 4802 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4802 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4802 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_shift_set1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set1 _Assigned_chem_shift_list.Entry_ID 4802 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4802 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 SER H H 1 8.426 . . 1 . . . . . . . . 4802 1 2 . 1 1 1 1 SER HA H 1 4.338 . . 1 . . . . . . . . 4802 1 3 . 1 1 1 1 SER C C 13 176.049 . . 1 . . . . . . . . 4802 1 4 . 1 1 1 1 SER CA C 13 58.398 . . 1 . . . . . . . . 4802 1 5 . 1 1 1 1 SER CB C 13 63.355 . . 1 . . . . . . . . 4802 1 6 . 1 1 1 1 SER N N 15 117.04 . . 1 . . . . . . . . 4802 1 7 . 1 1 2 2 GLU H H 1 8.419 . . 1 . . . . . . . . 4802 1 8 . 1 1 2 2 GLU HA H 1 4.184 . . 1 . . . . . . . . 4802 1 9 . 1 1 2 2 GLU C C 13 178.530 . . 1 . . . . . . . . 4802 1 10 . 1 1 2 2 GLU CA C 13 57.070 . . 1 . . . . . . . . 4802 1 11 . 1 1 2 2 GLU N N 15 122.71 . . 1 . . . . . . . . 4802 1 12 . 1 1 3 3 ALA H H 1 8.127 . . 1 . . . . . . . . 4802 1 13 . 1 1 3 3 ALA HA H 1 4.026 . . 1 . . . . . . . . 4802 1 14 . 1 1 3 3 ALA C C 13 179.400 . . 1 . . . . . . . . 4802 1 15 . 1 1 3 3 ALA CA C 13 54.242 . . 1 . . . . . . . . 4802 1 16 . 1 1 3 3 ALA CB C 13 18.048 . . 1 . . . . . . . . 4802 1 17 . 1 1 3 3 ALA N N 15 122.02 . . 1 . . . . . . . . 4802 1 18 . 1 1 4 4 LEU H H 1 7.840 . . 1 . . . . . . . . 4802 1 19 . 1 1 4 4 LEU HA H 1 4.024 . . 1 . . . . . . . . 4802 1 20 . 1 1 4 4 LEU C C 13 178.535 . . 1 . . . . . . . . 4802 1 21 . 1 1 4 4 LEU CA C 13 55.992 . . 1 . . . . . . . . 4802 1 22 . 1 1 4 4 LEU CB C 13 40.470 . . 1 . . . . . . . . 4802 1 23 . 1 1 4 4 LEU N N 15 114.95 . . 1 . . . . . . . . 4802 1 24 . 1 1 5 5 LYS H H 1 7.530 . . 1 . . . . . . . . 4802 1 25 . 1 1 5 5 LYS HA H 1 3.947 . . 1 . . . . . . . . 4802 1 26 . 1 1 5 5 LYS C C 13 180.114 . . 1 . . . . . . . . 4802 1 27 . 1 1 5 5 LYS CA C 13 58.615 . . 1 . . . . . . . . 4802 1 28 . 1 1 5 5 LYS CB C 13 31.468 . . 1 . . . . . . . . 4802 1 29 . 1 1 5 5 LYS N N 15 116.51 . . 1 . . . . . . . . 4802 1 30 . 1 1 6 6 ILE H H 1 7.654 . . 1 . . . . . . . . 4802 1 31 . 1 1 6 6 ILE HA H 1 3.874 . . 1 . . . . . . . . 4802 1 32 . 1 1 6 6 ILE C C 13 177.006 . . 1 . . . . . . . . 4802 1 33 . 1 1 6 6 ILE CA C 13 62.789 . . 1 . . . . . . . . 4802 1 34 . 1 1 6 6 ILE CB C 13 37.173 . . 1 . . . . . . . . 4802 1 35 . 1 1 6 6 ILE N N 15 118.31 . . 1 . . . . . . . . 4802 1 36 . 1 1 7 7 LEU H H 1 7.548 . . 1 . . . . . . . . 4802 1 37 . 1 1 7 7 LEU HA H 1 4.067 . . 1 . . . . . . . . 4802 1 38 . 1 1 7 7 LEU C C 13 176.402 . . 1 . . . . . . . . 4802 1 39 . 1 1 7 7 LEU CA C 13 55.028 . . 1 . . . . . . . . 4802 1 40 . 1 1 7 7 LEU CB C 13 40.513 . . 1 . . . . . . . . 4802 1 41 . 1 1 7 7 LEU N N 15 115.55 . . 1 . . . . . . . . 4802 1 42 . 1 1 8 8 ASN H H 1 7.390 . . 1 . . . . . . . . 4802 1 43 . 1 1 8 8 ASN HA H 1 4.965 . . 1 . . . . . . . . 4802 1 44 . 1 1 8 8 ASN C C 13 175.999 . . 1 . . . . . . . . 4802 1 45 . 1 1 8 8 ASN CA C 13 51.134 . . 1 . . . . . . . . 4802 1 46 . 1 1 8 8 ASN CB C 13 38.109 . . 1 . . . . . . . . 4802 1 47 . 1 1 8 8 ASN N N 15 112.56 . . 1 . . . . . . . . 4802 1 48 . 1 1 9 9 ASN H H 1 7.752 . . 1 . . . . . . . . 4802 1 49 . 1 1 9 9 ASN HA H 1 4.816 . . 1 . . . . . . . . 4802 1 50 . 1 1 9 9 ASN C C 13 175.495 . . 1 . . . . . . . . 4802 1 51 . 1 1 9 9 ASN CA C 13 51.771 . . 1 . . . . . . . . 4802 1 52 . 1 1 9 9 ASN CB C 13 39.713 . . 1 . . . . . . . . 4802 1 53 . 1 1 9 9 ASN N N 15 119.54 . . 1 . . . . . . . . 4802 1 54 . 1 1 10 10 ILE CA C 13 63.457 . . 1 . . . . . . . . 4802 1 55 . 1 1 11 11 ARG H H 1 7.950 . . 1 . . . . . . . . 4802 1 56 . 1 1 11 11 ARG HA H 1 4.132 . . 1 . . . . . . . . 4802 1 57 . 1 1 11 11 ARG C C 13 180.619 . . 1 . . . . . . . . 4802 1 58 . 1 1 11 11 ARG CA C 13 58.880 . . 1 . . . . . . . . 4802 1 59 . 1 1 11 11 ARG CB C 13 28.827 . . 1 . . . . . . . . 4802 1 60 . 1 1 11 11 ARG N N 15 121.25 . . 1 . . . . . . . . 4802 1 61 . 1 1 12 12 THR H H 1 7.765 . . 1 . . . . . . . . 4802 1 62 . 1 1 12 12 THR HA H 1 4.192 . . 1 . . . . . . . . 4802 1 63 . 1 1 12 12 THR C C 13 176.978 . . 1 . . . . . . . . 4802 1 64 . 1 1 12 12 THR CA C 13 64.705 . . 1 . . . . . . . . 4802 1 65 . 1 1 12 12 THR CB C 13 67.879 . . 1 . . . . . . . . 4802 1 66 . 1 1 12 12 THR N N 15 117.16 . . 1 . . . . . . . . 4802 1 67 . 1 1 13 13 LEU H H 1 8.681 . . 1 . . . . . . . . 4802 1 68 . 1 1 13 13 LEU HA H 1 3.945 . . 1 . . . . . . . . 4802 1 69 . 1 1 13 13 LEU C C 13 179.075 . . 1 . . . . . . . . 4802 1 70 . 1 1 13 13 LEU CA C 13 57.790 . . 1 . . . . . . . . 4802 1 71 . 1 1 13 13 LEU CB C 13 40.673 . . 1 . . . . . . . . 4802 1 72 . 1 1 13 13 LEU N N 15 123.42 . . 1 . . . . . . . . 4802 1 73 . 1 1 14 14 ARG H H 1 8.606 . . 1 . . . . . . . . 4802 1 74 . 1 1 14 14 ARG HA H 1 3.794 . . 1 . . . . . . . . 4802 1 75 . 1 1 14 14 ARG C C 13 179.43 . . 1 . . . . . . . . 4802 1 76 . 1 1 14 14 ARG CA C 13 59.719 . . 1 . . . . . . . . 4802 1 77 . 1 1 14 14 ARG CB C 13 29.560 . . 1 . . . . . . . . 4802 1 78 . 1 1 14 14 ARG N N 15 117.29 . . 1 . . . . . . . . 4802 1 79 . 1 1 15 15 ALA H H 1 7.504 . . 1 . . . . . . . . 4802 1 80 . 1 1 15 15 ALA HA H 1 4.155 . . 1 . . . . . . . . 4802 1 81 . 1 1 15 15 ALA C C 13 181.713 . . 1 . . . . . . . . 4802 1 82 . 1 1 15 15 ALA CA C 13 54.348 . . 1 . . . . . . . . 4802 1 83 . 1 1 15 15 ALA CB C 13 17.519 . . 1 . . . . . . . . 4802 1 84 . 1 1 15 15 ALA N N 15 119.62 . . 1 . . . . . . . . 4802 1 85 . 1 1 16 16 GLN H H 1 8.400 . . 1 . . . . . . . . 4802 1 86 . 1 1 16 16 GLN HA H 1 4.142 . . 1 . . . . . . . . 4802 1 87 . 1 1 16 16 GLN C C 13 179.843 . . 1 . . . . . . . . 4802 1 88 . 1 1 16 16 GLN CA C 13 57.453 . . 1 . . . . . . . . 4802 1 89 . 1 1 16 16 GLN CB C 13 27.307 . . 1 . . . . . . . . 4802 1 90 . 1 1 16 16 GLN N N 15 116.87 . . 1 . . . . . . . . 4802 1 91 . 1 1 17 17 ALA H H 1 8.905 . . 1 . . . . . . . . 4802 1 92 . 1 1 17 17 ALA HA H 1 3.950 . . 1 . . . . . . . . 4802 1 93 . 1 1 17 17 ALA C C 13 179.847 . . 1 . . . . . . . . 4802 1 94 . 1 1 17 17 ALA CA C 13 53.521 . . 1 . . . . . . . . 4802 1 95 . 1 1 17 17 ALA CB C 13 18.221 . . 1 . . . . . . . . 4802 1 96 . 1 1 17 17 ALA N N 15 122.15 . . 1 . . . . . . . . 4802 1 97 . 1 1 18 18 ARG H H 1 7.458 . . 1 . . . . . . . . 4802 1 98 . 1 1 18 18 ARG HA H 1 4.062 . . 1 . . . . . . . . 4802 1 99 . 1 1 18 18 ARG C C 13 177.72 . . 1 . . . . . . . . 4802 1 100 . 1 1 18 18 ARG CA C 13 57.641 . . 1 . . . . . . . . 4802 1 101 . 1 1 18 18 ARG CB C 13 29.337 . . 1 . . . . . . . . 4802 1 102 . 1 1 18 18 ARG N N 15 117.15 . . 1 . . . . . . . . 4802 1 103 . 1 1 19 19 GLU H H 1 7.281 . . 1 . . . . . . . . 4802 1 104 . 1 1 19 19 GLU HA H 1 4.439 . . 1 . . . . . . . . 4802 1 105 . 1 1 19 19 GLU C C 13 176.72 . . 1 . . . . . . . . 4802 1 106 . 1 1 19 19 GLU CA C 13 55.147 . . 1 . . . . . . . . 4802 1 107 . 1 1 19 19 GLU CB C 13 29.201 . . 1 . . . . . . . . 4802 1 108 . 1 1 19 19 GLU N N 15 114.36 . . 1 . . . . . . . . 4802 1 109 . 1 1 20 20 SER H H 1 7.637 . . 1 . . . . . . . . 4802 1 110 . 1 1 20 20 SER HA H 1 4.937 . . 1 . . . . . . . . 4802 1 111 . 1 1 20 20 SER C C 13 174.33 . . 1 . . . . . . . . 4802 1 112 . 1 1 20 20 SER CA C 13 57.009 . . 1 . . . . . . . . 4802 1 113 . 1 1 20 20 SER CB C 13 65.445 . . 1 . . . . . . . . 4802 1 114 . 1 1 20 20 SER N N 15 115.47 . . 1 . . . . . . . . 4802 1 115 . 1 1 21 21 THR H H 1 8.724 . . 1 . . . . . . . . 4802 1 116 . 1 1 21 21 THR HA H 1 4.375 . . 1 . . . . . . . . 4802 1 117 . 1 1 21 21 THR C C 13 175.83 . . 1 . . . . . . . . 4802 1 118 . 1 1 21 21 THR CA C 13 60.085 . . 1 . . . . . . . . 4802 1 119 . 1 1 21 21 THR CB C 13 70.159 . . 1 . . . . . . . . 4802 1 120 . 1 1 21 21 THR N N 15 113.98 . . 1 . . . . . . . . 4802 1 121 . 1 1 22 22 LEU H H 1 9.111 . . 1 . . . . . . . . 4802 1 122 . 1 1 22 22 LEU HA H 1 4.064 . . 1 . . . . . . . . 4802 1 123 . 1 1 22 22 LEU C C 13 178.487 . . 1 . . . . . . . . 4802 1 124 . 1 1 22 22 LEU CA C 13 57.342 . . 1 . . . . . . . . 4802 1 125 . 1 1 22 22 LEU CB C 13 39.923 . . 1 . . . . . . . . 4802 1 126 . 1 1 22 22 LEU N N 15 123.35 . . 1 . . . . . . . . 4802 1 127 . 1 1 23 23 GLU H H 1 8.767 . . 1 . . . . . . . . 4802 1 128 . 1 1 23 23 GLU HA H 1 4.104 . . 1 . . . . . . . . 4802 1 129 . 1 1 23 23 GLU C C 13 179.867 . . 1 . . . . . . . . 4802 1 130 . 1 1 23 23 GLU CA C 13 59.492 . . 1 . . . . . . . . 4802 1 131 . 1 1 23 23 GLU CB C 13 28.473 . . 1 . . . . . . . . 4802 1 132 . 1 1 23 23 GLU N N 15 117.04 . . 1 . . . . . . . . 4802 1 133 . 1 1 24 24 THR H H 1 7.736 . . 1 . . . . . . . . 4802 1 134 . 1 1 24 24 THR HA H 1 4.295 . . 1 . . . . . . . . 4802 1 135 . 1 1 24 24 THR C C 13 176.652 . . 1 . . . . . . . . 4802 1 136 . 1 1 24 24 THR CA C 13 65.767 . . 1 . . . . . . . . 4802 1 137 . 1 1 24 24 THR CB C 13 68.043 . . 1 . . . . . . . . 4802 1 138 . 1 1 24 24 THR N N 15 116.84 . . 1 . . . . . . . . 4802 1 139 . 1 1 25 25 LEU H H 1 7.876 . . 1 . . . . . . . . 4802 1 140 . 1 1 25 25 LEU HA H 1 4.058 . . 1 . . . . . . . . 4802 1 141 . 1 1 25 25 LEU C C 13 179.394 . . 1 . . . . . . . . 4802 1 142 . 1 1 25 25 LEU CA C 13 57.278 . . 1 . . . . . . . . 4802 1 143 . 1 1 25 25 LEU CB C 13 41.201 . . 1 . . . . . . . . 4802 1 144 . 1 1 25 25 LEU N N 15 121.61 . . 1 . . . . . . . . 4802 1 145 . 1 1 26 26 GLU H H 1 8.848 . . 1 . . . . . . . . 4802 1 146 . 1 1 26 26 GLU HA H 1 3.988 . . 1 . . . . . . . . 4802 1 147 . 1 1 26 26 GLU C C 13 180.839 . . 1 . . . . . . . . 4802 1 148 . 1 1 26 26 GLU CA C 13 59.015 . . 1 . . . . . . . . 4802 1 149 . 1 1 26 26 GLU CB C 13 28.499 . . 1 . . . . . . . . 4802 1 150 . 1 1 26 26 GLU N N 15 117.13 . . 1 . . . . . . . . 4802 1 151 . 1 1 27 27 GLU H H 1 7.876 . . 1 . . . . . . . . 4802 1 152 . 1 1 27 27 GLU HA H 1 4.139 . . 1 . . . . . . . . 4802 1 153 . 1 1 27 27 GLU C C 13 179.568 . . 1 . . . . . . . . 4802 1 154 . 1 1 27 27 GLU CA C 13 58.567 . . 1 . . . . . . . . 4802 1 155 . 1 1 27 27 GLU CB C 13 28.595 . . 1 . . . . . . . . 4802 1 156 . 1 1 27 27 GLU N N 15 120.90 . . 1 . . . . . . . . 4802 1 157 . 1 1 28 28 MET H H 1 8.166 . . 1 . . . . . . . . 4802 1 158 . 1 1 28 28 MET HA H 1 3.986 . . 1 . . . . . . . . 4802 1 159 . 1 1 28 28 MET CB C 13 31.653 . . 1 . . . . . . . . 4802 1 160 . 1 1 28 28 MET N N 15 120.21 . . 1 . . . . . . . . 4802 1 161 . 1 1 29 29 LEU H H 1 8.285 . . 1 . . . . . . . . 4802 1 162 . 1 1 29 29 LEU HA H 1 3.996 . . 1 . . . . . . . . 4802 1 163 . 1 1 29 29 LEU C C 13 178.311 . . 1 . . . . . . . . 4802 1 164 . 1 1 29 29 LEU CA C 13 57.411 . . 1 . . . . . . . . 4802 1 165 . 1 1 29 29 LEU CB C 13 40.867 . . 1 . . . . . . . . 4802 1 166 . 1 1 29 29 LEU N N 15 119.82 . . 1 . . . . . . . . 4802 1 167 . 1 1 30 30 GLU H H 1 7.816 . . 1 . . . . . . . . 4802 1 168 . 1 1 30 30 GLU HA H 1 4.066 . . 1 . . . . . . . . 4802 1 169 . 1 1 30 30 GLU C C 13 180.12 . . 1 . . . . . . . . 4802 1 170 . 1 1 30 30 GLU CA C 13 58.665 . . 1 . . . . . . . . 4802 1 171 . 1 1 30 30 GLU CB C 13 28.683 . . 1 . . . . . . . . 4802 1 172 . 1 1 30 30 GLU N N 15 118.03 . . 1 . . . . . . . . 4802 1 173 . 1 1 31 31 LYS H H 1 7.845 . . 1 . . . . . . . . 4802 1 174 . 1 1 31 31 LYS HA H 1 3.949 . . 1 . . . . . . . . 4802 1 175 . 1 1 31 31 LYS C C 13 178.652 . . 1 . . . . . . . . 4802 1 176 . 1 1 31 31 LYS CA C 13 59.315 . . 1 . . . . . . . . 4802 1 177 . 1 1 31 31 LYS N N 15 118.08 . . 1 . . . . . . . . 4802 1 178 . 1 1 32 32 LEU H H 1 8.594 . . 1 . . . . . . . . 4802 1 179 . 1 1 32 32 LEU HA H 1 4.109 . . 1 . . . . . . . . 4802 1 180 . 1 1 32 32 LEU C C 13 178.932 . . 1 . . . . . . . . 4802 1 181 . 1 1 32 32 LEU CA C 13 56.796 . . 1 . . . . . . . . 4802 1 182 . 1 1 32 32 LEU CB C 13 40.101 . . 1 . . . . . . . . 4802 1 183 . 1 1 32 32 LEU N N 15 119.44 . . 1 . . . . . . . . 4802 1 184 . 1 1 33 33 GLU H H 1 8.643 . . 1 . . . . . . . . 4802 1 185 . 1 1 33 33 GLU HA H 1 3.792 . . 1 . . . . . . . . 4802 1 186 . 1 1 33 33 GLU C C 13 179.660 . . 1 . . . . . . . . 4802 1 187 . 1 1 33 33 GLU CA C 13 59.721 . . 1 . . . . . . . . 4802 1 188 . 1 1 33 33 GLU CB C 13 28.383 . . 1 . . . . . . . . 4802 1 189 . 1 1 33 33 GLU N N 15 118.77 . . 1 . . . . . . . . 4802 1 190 . 1 1 34 34 VAL H H 1 7.727 . . 1 . . . . . . . . 4802 1 191 . 1 1 34 34 VAL HA H 1 3.697 . . 1 . . . . . . . . 4802 1 192 . 1 1 34 34 VAL C C 13 179.607 . . 1 . . . . . . . . 4802 1 193 . 1 1 34 34 VAL CA C 13 66.107 . . 1 . . . . . . . . 4802 1 194 . 1 1 34 34 VAL CB C 13 30.767 . . 1 . . . . . . . . 4802 1 195 . 1 1 34 34 VAL N N 15 119.63 . . 1 . . . . . . . . 4802 1 196 . 1 1 35 35 VAL H H 1 7.896 . . 1 . . . . . . . . 4802 1 197 . 1 1 35 35 VAL HA H 1 3.730 . . 1 . . . . . . . . 4802 1 198 . 1 1 35 35 VAL C C 13 179.473 . . 1 . . . . . . . . 4802 1 199 . 1 1 35 35 VAL CA C 13 65.494 . . 1 . . . . . . . . 4802 1 200 . 1 1 35 35 VAL N N 15 119.79 . . 1 . . . . . . . . 4802 1 201 . 1 1 36 36 VAL H H 1 9.015 . . 1 . . . . . . . . 4802 1 202 . 1 1 36 36 VAL HA H 1 3.418 . . 1 . . . . . . . . 4802 1 203 . 1 1 36 36 VAL C C 13 178.402 . . 1 . . . . . . . . 4802 1 204 . 1 1 36 36 VAL CA C 13 66.883 . . 1 . . . . . . . . 4802 1 205 . 1 1 36 36 VAL CB C 13 30.444 . . 1 . . . . . . . . 4802 1 206 . 1 1 36 36 VAL N N 15 121.38 . . 1 . . . . . . . . 4802 1 207 . 1 1 37 37 ASN H H 1 8.572 . . 1 . . . . . . . . 4802 1 208 . 1 1 37 37 ASN HA H 1 4.455 . . 1 . . . . . . . . 4802 1 209 . 1 1 37 37 ASN C C 13 179.028 . . 1 . . . . . . . . 4802 1 210 . 1 1 37 37 ASN CA C 13 56.355 . . 1 . . . . . . . . 4802 1 211 . 1 1 37 37 ASN CB C 13 37.622 . . 1 . . . . . . . . 4802 1 212 . 1 1 37 37 ASN N N 15 118.68 . . 1 . . . . . . . . 4802 1 213 . 1 1 38 38 GLU H H 1 8.393 . . 1 . . . . . . . . 4802 1 214 . 1 1 38 38 GLU HA H 1 4.107 . . 1 . . . . . . . . 4802 1 215 . 1 1 38 38 GLU C C 13 180.480 . . 1 . . . . . . . . 4802 1 216 . 1 1 38 38 GLU CA C 13 58.427 . . 1 . . . . . . . . 4802 1 217 . 1 1 38 38 GLU N N 15 120.39 . . 1 . . . . . . . . 4802 1 218 . 1 1 39 39 ARG H H 1 8.003 . . 1 . . . . . . . . 4802 1 219 . 1 1 39 39 ARG HA H 1 4.268 . . 1 . . . . . . . . 4802 1 220 . 1 1 39 39 ARG C C 13 179.362 . . 1 . . . . . . . . 4802 1 221 . 1 1 39 39 ARG CA C 13 56.283 . . 1 . . . . . . . . 4802 1 222 . 1 1 39 39 ARG CB C 13 27.577 . . 1 . . . . . . . . 4802 1 223 . 1 1 39 39 ARG N N 15 120.78 . . 1 . . . . . . . . 4802 1 224 . 1 1 40 40 ARG H H 1 8.969 . . 1 . . . . . . . . 4802 1 225 . 1 1 40 40 ARG HA H 1 3.976 . . 1 . . . . . . . . 4802 1 226 . 1 1 40 40 ARG C C 13 180.416 . . 1 . . . . . . . . 4802 1 227 . 1 1 40 40 ARG CA C 13 59.152 . . 1 . . . . . . . . 4802 1 228 . 1 1 40 40 ARG CB C 13 29.543 . . 1 . . . . . . . . 4802 1 229 . 1 1 40 40 ARG N N 15 120.95 . . 1 . . . . . . . . 4802 1 230 . 1 1 41 41 GLU H H 1 8.005 . . 1 . . . . . . . . 4802 1 231 . 1 1 41 41 GLU HA H 1 4.124 . . 1 . . . . . . . . 4802 1 232 . 1 1 41 41 GLU C C 13 179.874 . . 1 . . . . . . . . 4802 1 233 . 1 1 41 41 GLU CA C 13 58.392 . . 1 . . . . . . . . 4802 1 234 . 1 1 41 41 GLU N N 15 119.32 . . 1 . . . . . . . . 4802 1 235 . 1 1 42 42 GLU H H 1 8.161 . . 1 . . . . . . . . 4802 1 236 . 1 1 42 42 GLU HA H 1 4.140 . . 1 . . . . . . . . 4802 1 237 . 1 1 42 42 GLU C C 13 180.168 . . 1 . . . . . . . . 4802 1 238 . 1 1 42 42 GLU CA C 13 58.443 . . 1 . . . . . . . . 4802 1 239 . 1 1 42 42 GLU N N 15 121.01 . . 1 . . . . . . . . 4802 1 240 . 1 1 43 43 GLU H H 1 8.411 . . 1 . . . . . . . . 4802 1 241 . 1 1 43 43 GLU HA H 1 4.271 . . 1 . . . . . . . . 4802 1 242 . 1 1 43 43 GLU C C 13 179.749 . . 1 . . . . . . . . 4802 1 243 . 1 1 43 43 GLU CA C 13 57.957 . . 1 . . . . . . . . 4802 1 244 . 1 1 43 43 GLU CB C 13 28.216 . . 1 . . . . . . . . 4802 1 245 . 1 1 43 43 GLU N N 15 118.61 . . 1 . . . . . . . . 4802 1 246 . 1 1 44 44 SER H H 1 8.153 . . 1 . . . . . . . . 4802 1 247 . 1 1 44 44 SER HA H 1 4.378 . . 1 . . . . . . . . 4802 1 248 . 1 1 44 44 SER C C 13 177.125 . . 1 . . . . . . . . 4802 1 249 . 1 1 44 44 SER CA C 13 60.019 . . 1 . . . . . . . . 4802 1 250 . 1 1 44 44 SER CB C 13 62.592 . . 1 . . . . . . . . 4802 1 251 . 1 1 44 44 SER N N 15 116.02 . . 1 . . . . . . . . 4802 1 252 . 1 1 45 45 ALA H H 1 8.140 . . 1 . . . . . . . . 4802 1 253 . 1 1 45 45 ALA HA H 1 4.300 . . 1 . . . . . . . . 4802 1 254 . 1 1 45 45 ALA C C 13 180.139 . . 1 . . . . . . . . 4802 1 255 . 1 1 45 45 ALA CA C 13 53.460 . . 1 . . . . . . . . 4802 1 256 . 1 1 45 45 ALA CB C 13 17.656 . . 1 . . . . . . . . 4802 1 257 . 1 1 45 45 ALA N N 15 125.18 . . 1 . . . . . . . . 4802 1 258 . 1 1 46 46 ALA H H 1 8.049 . . 1 . . . . . . . . 4802 1 259 . 1 1 46 46 ALA HA H 1 4.277 . . 1 . . . . . . . . 4802 1 260 . 1 1 46 46 ALA C C 13 180.004 . . 1 . . . . . . . . 4802 1 261 . 1 1 46 46 ALA CA C 13 53.177 . . 1 . . . . . . . . 4802 1 262 . 1 1 46 46 ALA N N 15 121.92 . . 1 . . . . . . . . 4802 1 263 . 1 1 47 47 ALA H H 1 8.026 . . 1 . . . . . . . . 4802 1 264 . 1 1 47 47 ALA HA H 1 4.272 . . 1 . . . . . . . . 4802 1 265 . 1 1 47 47 ALA C C 13 179.597 . . 1 . . . . . . . . 4802 1 266 . 1 1 47 47 ALA CA C 13 53.312 . . 1 . . . . . . . . 4802 1 267 . 1 1 47 47 ALA N N 15 121.79 . . 1 . . . . . . . . 4802 1 268 . 1 1 48 48 ALA H H 1 8.030 . . 1 . . . . . . . . 4802 1 269 . 1 1 48 48 ALA HA H 1 4.256 . . 1 . . . . . . . . 4802 1 270 . 1 1 48 48 ALA C C 13 179.996 . . 1 . . . . . . . . 4802 1 271 . 1 1 48 48 ALA CA C 13 53.102 . . 1 . . . . . . . . 4802 1 272 . 1 1 48 48 ALA CB C 13 17.946 . . 1 . . . . . . . . 4802 1 273 . 1 1 48 48 ALA N N 15 121.71 . . 1 . . . . . . . . 4802 1 274 . 1 1 49 49 GLU H H 1 8.025 . . 1 . . . . . . . . 4802 1 275 . 1 1 49 49 GLU HA H 1 4.253 . . 1 . . . . . . . . 4802 1 276 . 1 1 49 49 GLU C C 13 178.753 . . 1 . . . . . . . . 4802 1 277 . 1 1 49 49 GLU CA C 13 57.375 . . 1 . . . . . . . . 4802 1 278 . 1 1 49 49 GLU CB C 13 29.043 . . 1 . . . . . . . . 4802 1 279 . 1 1 49 49 GLU N N 15 119.68 . . 1 . . . . . . . . 4802 1 280 . 1 1 50 50 VAL H H 1 7.904 . . 1 . . . . . . . . 4802 1 281 . 1 1 50 50 VAL HA H 1 3.864 . . 1 . . . . . . . . 4802 1 282 . 1 1 50 50 VAL C C 13 178.645 . . 1 . . . . . . . . 4802 1 283 . 1 1 50 50 VAL CA C 13 64.006 . . 1 . . . . . . . . 4802 1 284 . 1 1 50 50 VAL CB C 13 31.457 . . 1 . . . . . . . . 4802 1 285 . 1 1 50 50 VAL N N 15 120.12 . . 1 . . . . . . . . 4802 1 286 . 1 1 51 51 GLU H H 1 8.260 . . 1 . . . . . . . . 4802 1 287 . 1 1 51 51 GLU HA H 1 4.161 . . 1 . . . . . . . . 4802 1 288 . 1 1 51 51 GLU CA C 13 57.678 . . 1 . . . . . . . . 4802 1 289 . 1 1 51 51 GLU N N 15 122.69 . . 1 . . . . . . . . 4802 1 290 . 1 1 52 52 GLU H H 1 8.272 . . 1 . . . . . . . . 4802 1 291 . 1 1 52 52 GLU HA H 1 4.163 . . 1 . . . . . . . . 4802 1 292 . 1 1 52 52 GLU C C 13 178.620 . . 1 . . . . . . . . 4802 1 293 . 1 1 52 52 GLU CA C 13 57.590 . . 1 . . . . . . . . 4802 1 294 . 1 1 52 52 GLU N N 15 120.70 . . 1 . . . . . . . . 4802 1 295 . 1 1 53 53 ARG H H 1 8.228 . . 1 . . . . . . . . 4802 1 296 . 1 1 53 53 ARG HA H 1 4.179 . . 1 . . . . . . . . 4802 1 297 . 1 1 53 53 ARG C C 13 178.834 . . 1 . . . . . . . . 4802 1 298 . 1 1 53 53 ARG CA C 13 57.660 . . 1 . . . . . . . . 4802 1 299 . 1 1 53 53 ARG CB C 13 29.518 . . 1 . . . . . . . . 4802 1 300 . 1 1 53 53 ARG N N 15 120.09 . . 1 . . . . . . . . 4802 1 301 . 1 1 54 54 THR H H 1 8.143 . . 1 . . . . . . . . 4802 1 302 . 1 1 54 54 THR HA H 1 4.304 . . 1 . . . . . . . . 4802 1 303 . 1 1 54 54 THR C C 13 176.363 . . 1 . . . . . . . . 4802 1 304 . 1 1 54 54 THR CA C 13 63.717 . . 1 . . . . . . . . 4802 1 305 . 1 1 54 54 THR CB C 13 68.664 . . 1 . . . . . . . . 4802 1 306 . 1 1 54 54 THR N N 15 114.23 . . 1 . . . . . . . . 4802 1 307 . 1 1 55 55 ARG H H 1 8.113 . . 1 . . . . . . . . 4802 1 308 . 1 1 55 55 ARG HA H 1 4.185 . . 1 . . . . . . . . 4802 1 309 . 1 1 55 55 ARG C C 13 178.388 . . 1 . . . . . . . . 4802 1 310 . 1 1 55 55 ARG CA C 13 57.260 . . 1 . . . . . . . . 4802 1 311 . 1 1 55 55 ARG N N 15 122.64 . . 1 . . . . . . . . 4802 1 312 . 1 1 56 56 LYS CA C 13 56.900 . . 1 . . . . . . . . 4802 1 313 . 1 1 57 57 LEU H H 1 8.009 . . 1 . . . . . . . . 4802 1 314 . 1 1 57 57 LEU CA C 13 55.400 . . 1 . . . . . . . . 4802 1 315 . 1 1 57 57 LEU CB C 13 41.148 . . 1 . . . . . . . . 4802 1 316 . 1 1 57 57 LEU N N 15 120.78 . . 1 . . . . . . . . 4802 1 317 . 1 1 58 58 GLN H H 1 8.135 . . 1 . . . . . . . . 4802 1 318 . 1 1 58 58 GLN HA H 1 4.226 . . 1 . . . . . . . . 4802 1 319 . 1 1 58 58 GLN CA C 13 55.890 . . 1 . . . . . . . . 4802 1 320 . 1 1 58 58 GLN N N 15 119.48 . . 1 . . . . . . . . 4802 1 321 . 1 1 59 59 GLN H H 1 8.156 . . 1 . . . . . . . . 4802 1 322 . 1 1 59 59 GLN HA H 1 4.267 . . 1 . . . . . . . . 4802 1 323 . 1 1 59 59 GLN CA C 13 55.220 . . 1 . . . . . . . . 4802 1 324 . 1 1 59 59 GLN N N 15 119.78 . . 1 . . . . . . . . 4802 1 325 . 1 1 60 60 TYR H H 1 8.106 . . 1 . . . . . . . . 4802 1 326 . 1 1 60 60 TYR HA H 1 4.563 . . 1 . . . . . . . . 4802 1 327 . 1 1 60 60 TYR CA C 13 57.594 . . 1 . . . . . . . . 4802 1 328 . 1 1 60 60 TYR CB C 13 37.835 . . 1 . . . . . . . . 4802 1 329 . 1 1 60 60 TYR N N 15 120.43 . . 1 . . . . . . . . 4802 1 330 . 1 1 61 61 ARG H H 1 8.011 . . 1 . . . . . . . . 4802 1 331 . 1 1 61 61 ARG HA H 1 4.260 . . 1 . . . . . . . . 4802 1 332 . 1 1 61 61 ARG C C 13 176.634 . . 1 . . . . . . . . 4802 1 333 . 1 1 61 61 ARG CA C 13 55.514 . . 1 . . . . . . . . 4802 1 334 . 1 1 61 61 ARG CB C 13 30.180 . . 1 . . . . . . . . 4802 1 335 . 1 1 61 61 ARG N N 15 121.96 . . 1 . . . . . . . . 4802 1 336 . 1 1 62 62 GLU H H 1 8.283 . . 1 . . . . . . . . 4802 1 337 . 1 1 62 62 GLU HA H 1 4.231 . . 1 . . . . . . . . 4802 1 338 . 1 1 62 62 GLU C C 13 176.854 . . 1 . . . . . . . . 4802 1 339 . 1 1 62 62 GLU CA C 13 55.968 . . 1 . . . . . . . . 4802 1 340 . 1 1 62 62 GLU CB C 13 29.450 . . 1 . . . . . . . . 4802 1 341 . 1 1 62 62 GLU N N 15 121.10 . . 1 . . . . . . . . 4802 1 342 . 1 1 63 63 MET H H 1 8.222 . . 1 . . . . . . . . 4802 1 343 . 1 1 63 63 MET HA H 1 4.505 . . 1 . . . . . . . . 4802 1 344 . 1 1 63 63 MET C C 13 175.679 . . 1 . . . . . . . . 4802 1 345 . 1 1 63 63 MET CA C 13 54.580 . . 1 . . . . . . . . 4802 1 346 . 1 1 63 63 MET CB C 13 32.125 . . 1 . . . . . . . . 4802 1 347 . 1 1 63 63 MET N N 15 121.51 . . 1 . . . . . . . . 4802 1 348 . 1 1 64 64 LEU H H 1 7.793 . . 1 . . . . . . . . 4802 1 349 . 1 1 64 64 LEU HA H 1 4.186 . . 1 . . . . . . . . 4802 1 350 . 1 1 64 64 LEU C C 13 183.104 . . 1 . . . . . . . . 4802 1 351 . 1 1 64 64 LEU CA C 13 55.997 . . 1 . . . . . . . . 4802 1 352 . 1 1 64 64 LEU CB C 13 42.341 . . 1 . . . . . . . . 4802 1 353 . 1 1 64 64 LEU N N 15 128.98 . . 1 . . . . . . . . 4802 1 stop_ save_