data_4802 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _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) ; _BMRB_accession_number 4802 _BMRB_flat_file_name bmr4802.str _Entry_type original _Submission_date 2000-08-09 _Accession_date 2000-08-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Renzoni Debora . . 2 Esposito Diego . . 3 Pfuhl Mark . . 4 Higgins Christopher F. . 5 Driscoll Paul C. . 6 Ladbury John E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 123 "13C chemical shifts" 168 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-01-23 original author . stop_ _Original_release_date 2001-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Insight to the Oligomerisation of the Bacterial Chromatin-Structuring Protein H-N ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Renzoni Debora . . 2 Esposito Diego . . 3 Pfuhl Mark . . 4 Higgins Christopher F. . 5 Driscoll Paul C. . 6 Ladbury John E. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'nuclear magnetic resonance' 'secondary structure' coiled-coil 'general topology' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10844682 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smyth 'C. P.' P. . 2 Lundback T. . . 3 Renzoni D. . . 4 Siligardi G. . . 5 Beavil R. . . 6 Layton M. . . 7 Sidebotham 'J. M.' M. . 8 Hinton 'J. C.' C. . 9 Driscoll 'P. C.' C. . 10 Higgins 'C. F.' F. . 11 Ladbury 'J. E.' E. . stop_ _Journal_abbreviation 'Mol. Microbiol.' _Journal_name_full 'Molecular microbiology' _Journal_volume 36 _Journal_issue 4 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 962 _Page_last 972 _Year 2000 _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. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; 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 _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister 'G W' W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _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. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Boucher, W. (1996) AZARA v2.0, Department of Biochemistry, University of Cambridge, UK. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_4 _Saveframe_category citation _Citation_full ; 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 . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_H-NS(1-64) _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of H-NS' _Abbreviation_common H-NS(1-64) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'H-NS(1-64) monomer 1' $H-NS(1-64) 'H-NS(1-64) monomer 2' $H-NS(1-64) 'H-NS(1-64) monomer 3' $H-NS(1-64) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state trimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'H-NS(1-64) monomer 1' 1 'H-NS(1-64) monomer 2' 1 'H-NS(1-64) monomer 3' stop_ loop_ _Biological_function 'oligomerisation of H-NS' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_H-NS(1-64) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Oligomerisation domain of the 'histone' like nucleoid structuring protein" _Abbreviation_common H-NS(1-64) _Molecular_mass 7958 _Mol_thiol_state 'not present' _Details 'H-NS(1-64) self-associates to form a discrete trimeric state' ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; SEALKILNNIRTLRAQARES TLETLEEMLEKLEVVVNERR EEESAAAAEVEERTRKLQQY REML ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLU 3 ALA 4 LEU 5 LYS 6 ILE 7 LEU 8 ASN 9 ASN 10 ILE 11 ARG 12 THR 13 LEU 14 ARG 15 ALA 16 GLN 17 ALA 18 ARG 19 GLU 20 SER 21 THR 22 LEU 23 GLU 24 THR 25 LEU 26 GLU 27 GLU 28 MET 29 LEU 30 GLU 31 LYS 32 LEU 33 GLU 34 VAL 35 VAL 36 VAL 37 ASN 38 GLU 39 ARG 40 ARG 41 GLU 42 GLU 43 GLU 44 SER 45 ALA 46 ALA 47 ALA 48 ALA 49 GLU 50 VAL 51 GLU 52 GLU 53 ARG 54 THR 55 ARG 56 LYS 57 LEU 58 GLN 59 GLN 60 TYR 61 ARG 62 GLU 63 MET 64 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18814 H-NS 100.00 137 98.44 98.44 1.57e-31 BMRB 5390 H-NS 89.06 61 100.00 100.00 1.46e-26 PDB 1LR1 "Solution Structure Of The Oligomerization Domain Of The Bacterial Chromatin-Structuring Protein H-Ns" 89.06 61 100.00 100.00 1.46e-26 PDB 1NI8 "H-Ns Dimerization Motif" 71.88 46 97.83 97.83 9.11e-19 PDB 3NR7 "Crystal Structure Of S. Typhimurium H-Ns 1-83" 100.00 86 100.00 100.00 2.35e-32 DBJ BAA36117 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli str. K-12 substr. W3110]" 100.00 137 98.44 98.44 1.57e-31 DBJ BAB35162 "DNA-binding protein H-NS [Escherichia coli O157:H7 str. Sakai]" 100.00 137 98.44 98.44 1.57e-31 DBJ BAG76811 "DNA-binding protein [Escherichia coli SE11]" 100.00 137 98.44 98.44 1.57e-31 DBJ BAI25048 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O26:H11 str. 11368]" 100.00 137 98.44 98.44 1.57e-31 DBJ BAI30173 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O103:H2 str. 12009]" 100.00 137 98.44 98.44 1.57e-31 EMBL CAA30530 "unnamed protein product [Escherichia coli]" 100.00 137 98.44 98.44 1.57e-31 EMBL CAA31522 "unnamed protein product [Shigella flexneri]" 57.81 109 100.00 100.00 2.08e-02 EMBL CAA32549 "unnamed protein product [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 137 98.44 98.44 2.39e-31 EMBL CAA40507 "DNA-binding protein OsmZ [H-NS(H1a)] [Escherichia coli]" 100.00 137 98.44 98.44 1.57e-31 EMBL CAA42565 "histone-like protein H-NS [Escherichia coli K-12]" 100.00 137 98.44 98.44 1.57e-31 GB AAB61148 "histone H1-like protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 137 98.44 98.44 2.39e-31 GB AAC74319 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli str. K-12 substr. MG1655]" 100.00 137 98.44 98.44 1.57e-31 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 1.57e-31 GB AAL20669 "DNA-binding protein HLP-II [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 137 98.44 98.44 2.39e-31 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 1.57e-31 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 2.39e-31 PRF 1607341A "drdX gene" 100.00 137 98.44 98.44 1.57e-31 REF NP_287482 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O157:H7 str. EDL933]" 100.00 137 98.44 98.44 1.57e-31 REF NP_309766 "global DNA-binding transcriptional dual regulator H-NS [Escherichia coli O157:H7 str. Sakai]" 100.00 137 98.44 98.44 1.57e-31 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 1.57e-31 REF NP_455749 "DNA-binding protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 137 98.44 98.44 2.39e-31 REF NP_460710 "DNA-binding protein H-NS [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 137 98.44 98.44 2.39e-31 SP P09120 "RecName: Full=DNA-binding protein H-NS; AltName: Full=Pathogenesis protein KcpA [Shigella flexneri]" 100.00 137 98.44 98.44 1.57e-31 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 2.39e-31 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 2.39e-31 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 1.57e-31 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 1.57e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $H-NS(1-64) 'Salmonella typhimurium' 602 Eubacteria . Salmonella typhimurium hns stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $H-NS(1-64) 'recombinant technology' 'E. coli' Escherichia coli BL21 'lambda DE3' plasmid pET14b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $H-NS(1-64) 1.5 mM 1.0 2.0 '[U-13C; U-15N; U-2H]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task 'data processing' stop_ _Details . _Citation_label $ref_2 save_ save_AZARA _Saveframe_category software _Name AZARA _Version 2.0 _Details . _Citation_label $ref_3 save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Task 'peak assignment' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $sample_1 save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $sample_1 save_ save_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY-HSQC' _Sample_label $sample_1 save_ save_15N_TOCSY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY-HSQC' _Sample_label $sample_1 save_ save_15N-15N_HSQC-NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-15N HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_13C_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C NOESY-HSQC' _Sample_label $sample_1 save_ save_13C_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HCCH-TOCSY' _Sample_label $sample_1 save_ save_HNCA_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCOCA_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label $sample_1 save_ save_HNCACO_13 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label $sample_1 save_ save_HNCACB_14 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HNCOCACB_15 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCACB _Sample_label $sample_1 save_ save_HCCH_13C-13C_NOE_16 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH 13C-13C NOE' _Sample_label $sample_1 save_ save_The_triple_resonance_experiments_were_recorded_on_triple_labelled_samples_(2H/15N/13C)._17 _Saveframe_category NMR_applied_experiment _Experiment_name 'The triple resonance experiments were recorded on triple labelled samples (2H/15N/13C).' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated for 25 minutes under these conditions before the spectra were collected ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0 n/a temperature 298 0.4 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'H-NS(1-64) monomer 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 SER H H 8.426 . 1 2 . 1 SER HA H 4.338 . 1 3 . 1 SER C C 176.049 . 1 4 . 1 SER CA C 58.398 . 1 5 . 1 SER CB C 63.355 . 1 6 . 1 SER N N 117.04 . 1 7 . 2 GLU H H 8.419 . 1 8 . 2 GLU HA H 4.184 . 1 9 . 2 GLU C C 178.530 . 1 10 . 2 GLU CA C 57.070 . 1 11 . 2 GLU N N 122.71 . 1 12 . 3 ALA H H 8.127 . 1 13 . 3 ALA HA H 4.026 . 1 14 . 3 ALA C C 179.400 . 1 15 . 3 ALA CA C 54.242 . 1 16 . 3 ALA CB C 18.048 . 1 17 . 3 ALA N N 122.02 . 1 18 . 4 LEU H H 7.840 . 1 19 . 4 LEU HA H 4.024 . 1 20 . 4 LEU C C 178.535 . 1 21 . 4 LEU CA C 55.992 . 1 22 . 4 LEU CB C 40.470 . 1 23 . 4 LEU N N 114.95 . 1 24 . 5 LYS H H 7.530 . 1 25 . 5 LYS HA H 3.947 . 1 26 . 5 LYS C C 180.114 . 1 27 . 5 LYS CA C 58.615 . 1 28 . 5 LYS CB C 31.468 . 1 29 . 5 LYS N N 116.51 . 1 30 . 6 ILE H H 7.654 . 1 31 . 6 ILE HA H 3.874 . 1 32 . 6 ILE C C 177.006 . 1 33 . 6 ILE CA C 62.789 . 1 34 . 6 ILE CB C 37.173 . 1 35 . 6 ILE N N 118.31 . 1 36 . 7 LEU H H 7.548 . 1 37 . 7 LEU HA H 4.067 . 1 38 . 7 LEU C C 176.402 . 1 39 . 7 LEU CA C 55.028 . 1 40 . 7 LEU CB C 40.513 . 1 41 . 7 LEU N N 115.55 . 1 42 . 8 ASN H H 7.390 . 1 43 . 8 ASN HA H 4.965 . 1 44 . 8 ASN C C 175.999 . 1 45 . 8 ASN CA C 51.134 . 1 46 . 8 ASN CB C 38.109 . 1 47 . 8 ASN N N 112.56 . 1 48 . 9 ASN H H 7.752 . 1 49 . 9 ASN HA H 4.816 . 1 50 . 9 ASN C C 175.495 . 1 51 . 9 ASN CA C 51.771 . 1 52 . 9 ASN CB C 39.713 . 1 53 . 9 ASN N N 119.54 . 1 54 . 10 ILE CA C 63.457 . 1 55 . 11 ARG H H 7.950 . 1 56 . 11 ARG HA H 4.132 . 1 57 . 11 ARG C C 180.619 . 1 58 . 11 ARG CA C 58.880 . 1 59 . 11 ARG CB C 28.827 . 1 60 . 11 ARG N N 121.25 . 1 61 . 12 THR H H 7.765 . 1 62 . 12 THR HA H 4.192 . 1 63 . 12 THR C C 176.978 . 1 64 . 12 THR CA C 64.705 . 1 65 . 12 THR CB C 67.879 . 1 66 . 12 THR N N 117.16 . 1 67 . 13 LEU H H 8.681 . 1 68 . 13 LEU HA H 3.945 . 1 69 . 13 LEU C C 179.075 . 1 70 . 13 LEU CA C 57.790 . 1 71 . 13 LEU CB C 40.673 . 1 72 . 13 LEU N N 123.42 . 1 73 . 14 ARG H H 8.606 . 1 74 . 14 ARG HA H 3.794 . 1 75 . 14 ARG C C 179.43 . 1 76 . 14 ARG CA C 59.719 . 1 77 . 14 ARG CB C 29.560 . 1 78 . 14 ARG N N 117.29 . 1 79 . 15 ALA H H 7.504 . 1 80 . 15 ALA HA H 4.155 . 1 81 . 15 ALA C C 181.713 . 1 82 . 15 ALA CA C 54.348 . 1 83 . 15 ALA CB C 17.519 . 1 84 . 15 ALA N N 119.62 . 1 85 . 16 GLN H H 8.400 . 1 86 . 16 GLN HA H 4.142 . 1 87 . 16 GLN C C 179.843 . 1 88 . 16 GLN CA C 57.453 . 1 89 . 16 GLN CB C 27.307 . 1 90 . 16 GLN N N 116.87 . 1 91 . 17 ALA H H 8.905 . 1 92 . 17 ALA HA H 3.950 . 1 93 . 17 ALA C C 179.847 . 1 94 . 17 ALA CA C 53.521 . 1 95 . 17 ALA CB C 18.221 . 1 96 . 17 ALA N N 122.15 . 1 97 . 18 ARG H H 7.458 . 1 98 . 18 ARG HA H 4.062 . 1 99 . 18 ARG C C 177.72 . 1 100 . 18 ARG CA C 57.641 . 1 101 . 18 ARG CB C 29.337 . 1 102 . 18 ARG N N 117.15 . 1 103 . 19 GLU H H 7.281 . 1 104 . 19 GLU HA H 4.439 . 1 105 . 19 GLU C C 176.72 . 1 106 . 19 GLU CA C 55.147 . 1 107 . 19 GLU CB C 29.201 . 1 108 . 19 GLU N N 114.36 . 1 109 . 20 SER H H 7.637 . 1 110 . 20 SER HA H 4.937 . 1 111 . 20 SER C C 174.33 . 1 112 . 20 SER CA C 57.009 . 1 113 . 20 SER CB C 65.445 . 1 114 . 20 SER N N 115.47 . 1 115 . 21 THR H H 8.724 . 1 116 . 21 THR HA H 4.375 . 1 117 . 21 THR C C 175.83 . 1 118 . 21 THR CA C 60.085 . 1 119 . 21 THR CB C 70.159 . 1 120 . 21 THR N N 113.98 . 1 121 . 22 LEU H H 9.111 . 1 122 . 22 LEU HA H 4.064 . 1 123 . 22 LEU C C 178.487 . 1 124 . 22 LEU CA C 57.342 . 1 125 . 22 LEU CB C 39.923 . 1 126 . 22 LEU N N 123.35 . 1 127 . 23 GLU H H 8.767 . 1 128 . 23 GLU HA H 4.104 . 1 129 . 23 GLU C C 179.867 . 1 130 . 23 GLU CA C 59.492 . 1 131 . 23 GLU CB C 28.473 . 1 132 . 23 GLU N N 117.04 . 1 133 . 24 THR H H 7.736 . 1 134 . 24 THR HA H 4.295 . 1 135 . 24 THR C C 176.652 . 1 136 . 24 THR CA C 65.767 . 1 137 . 24 THR CB C 68.043 . 1 138 . 24 THR N N 116.84 . 1 139 . 25 LEU H H 7.876 . 1 140 . 25 LEU HA H 4.058 . 1 141 . 25 LEU C C 179.394 . 1 142 . 25 LEU CA C 57.278 . 1 143 . 25 LEU CB C 41.201 . 1 144 . 25 LEU N N 121.61 . 1 145 . 26 GLU H H 8.848 . 1 146 . 26 GLU HA H 3.988 . 1 147 . 26 GLU C C 180.839 . 1 148 . 26 GLU CA C 59.015 . 1 149 . 26 GLU CB C 28.499 . 1 150 . 26 GLU N N 117.13 . 1 151 . 27 GLU H H 7.876 . 1 152 . 27 GLU HA H 4.139 . 1 153 . 27 GLU C C 179.568 . 1 154 . 27 GLU CA C 58.567 . 1 155 . 27 GLU CB C 28.595 . 1 156 . 27 GLU N N 120.90 . 1 157 . 28 MET H H 8.166 . 1 158 . 28 MET HA H 3.986 . 1 159 . 28 MET CB C 31.653 . 1 160 . 28 MET N N 120.21 . 1 161 . 29 LEU H H 8.285 . 1 162 . 29 LEU HA H 3.996 . 1 163 . 29 LEU C C 178.311 . 1 164 . 29 LEU CA C 57.411 . 1 165 . 29 LEU CB C 40.867 . 1 166 . 29 LEU N N 119.82 . 1 167 . 30 GLU H H 7.816 . 1 168 . 30 GLU HA H 4.066 . 1 169 . 30 GLU C C 180.12 . 1 170 . 30 GLU CA C 58.665 . 1 171 . 30 GLU CB C 28.683 . 1 172 . 30 GLU N N 118.03 . 1 173 . 31 LYS H H 7.845 . 1 174 . 31 LYS HA H 3.949 . 1 175 . 31 LYS C C 178.652 . 1 176 . 31 LYS CA C 59.315 . 1 177 . 31 LYS N N 118.08 . 1 178 . 32 LEU H H 8.594 . 1 179 . 32 LEU HA H 4.109 . 1 180 . 32 LEU C C 178.932 . 1 181 . 32 LEU CA C 56.796 . 1 182 . 32 LEU CB C 40.101 . 1 183 . 32 LEU N N 119.44 . 1 184 . 33 GLU H H 8.643 . 1 185 . 33 GLU HA H 3.792 . 1 186 . 33 GLU C C 179.660 . 1 187 . 33 GLU CA C 59.721 . 1 188 . 33 GLU CB C 28.383 . 1 189 . 33 GLU N N 118.77 . 1 190 . 34 VAL H H 7.727 . 1 191 . 34 VAL HA H 3.697 . 1 192 . 34 VAL C C 179.607 . 1 193 . 34 VAL CA C 66.107 . 1 194 . 34 VAL CB C 30.767 . 1 195 . 34 VAL N N 119.63 . 1 196 . 35 VAL H H 7.896 . 1 197 . 35 VAL HA H 3.730 . 1 198 . 35 VAL C C 179.473 . 1 199 . 35 VAL CA C 65.494 . 1 200 . 35 VAL N N 119.79 . 1 201 . 36 VAL H H 9.015 . 1 202 . 36 VAL HA H 3.418 . 1 203 . 36 VAL C C 178.402 . 1 204 . 36 VAL CA C 66.883 . 1 205 . 36 VAL CB C 30.444 . 1 206 . 36 VAL N N 121.38 . 1 207 . 37 ASN H H 8.572 . 1 208 . 37 ASN HA H 4.455 . 1 209 . 37 ASN C C 179.028 . 1 210 . 37 ASN CA C 56.355 . 1 211 . 37 ASN CB C 37.622 . 1 212 . 37 ASN N N 118.68 . 1 213 . 38 GLU H H 8.393 . 1 214 . 38 GLU HA H 4.107 . 1 215 . 38 GLU C C 180.480 . 1 216 . 38 GLU CA C 58.427 . 1 217 . 38 GLU N N 120.39 . 1 218 . 39 ARG H H 8.003 . 1 219 . 39 ARG HA H 4.268 . 1 220 . 39 ARG C C 179.362 . 1 221 . 39 ARG CA C 56.283 . 1 222 . 39 ARG CB C 27.577 . 1 223 . 39 ARG N N 120.78 . 1 224 . 40 ARG H H 8.969 . 1 225 . 40 ARG HA H 3.976 . 1 226 . 40 ARG C C 180.416 . 1 227 . 40 ARG CA C 59.152 . 1 228 . 40 ARG CB C 29.543 . 1 229 . 40 ARG N N 120.95 . 1 230 . 41 GLU H H 8.005 . 1 231 . 41 GLU HA H 4.124 . 1 232 . 41 GLU C C 179.874 . 1 233 . 41 GLU CA C 58.392 . 1 234 . 41 GLU N N 119.32 . 1 235 . 42 GLU H H 8.161 . 1 236 . 42 GLU HA H 4.140 . 1 237 . 42 GLU C C 180.168 . 1 238 . 42 GLU CA C 58.443 . 1 239 . 42 GLU N N 121.01 . 1 240 . 43 GLU H H 8.411 . 1 241 . 43 GLU HA H 4.271 . 1 242 . 43 GLU C C 179.749 . 1 243 . 43 GLU CA C 57.957 . 1 244 . 43 GLU CB C 28.216 . 1 245 . 43 GLU N N 118.61 . 1 246 . 44 SER H H 8.153 . 1 247 . 44 SER HA H 4.378 . 1 248 . 44 SER C C 177.125 . 1 249 . 44 SER CA C 60.019 . 1 250 . 44 SER CB C 62.592 . 1 251 . 44 SER N N 116.02 . 1 252 . 45 ALA H H 8.140 . 1 253 . 45 ALA HA H 4.300 . 1 254 . 45 ALA C C 180.139 . 1 255 . 45 ALA CA C 53.460 . 1 256 . 45 ALA CB C 17.656 . 1 257 . 45 ALA N N 125.18 . 1 258 . 46 ALA H H 8.049 . 1 259 . 46 ALA HA H 4.277 . 1 260 . 46 ALA C C 180.004 . 1 261 . 46 ALA CA C 53.177 . 1 262 . 46 ALA N N 121.92 . 1 263 . 47 ALA H H 8.026 . 1 264 . 47 ALA HA H 4.272 . 1 265 . 47 ALA C C 179.597 . 1 266 . 47 ALA CA C 53.312 . 1 267 . 47 ALA N N 121.79 . 1 268 . 48 ALA H H 8.030 . 1 269 . 48 ALA HA H 4.256 . 1 270 . 48 ALA C C 179.996 . 1 271 . 48 ALA CA C 53.102 . 1 272 . 48 ALA CB C 17.946 . 1 273 . 48 ALA N N 121.71 . 1 274 . 49 GLU H H 8.025 . 1 275 . 49 GLU HA H 4.253 . 1 276 . 49 GLU C C 178.753 . 1 277 . 49 GLU CA C 57.375 . 1 278 . 49 GLU CB C 29.043 . 1 279 . 49 GLU N N 119.68 . 1 280 . 50 VAL H H 7.904 . 1 281 . 50 VAL HA H 3.864 . 1 282 . 50 VAL C C 178.645 . 1 283 . 50 VAL CA C 64.006 . 1 284 . 50 VAL CB C 31.457 . 1 285 . 50 VAL N N 120.12 . 1 286 . 51 GLU H H 8.260 . 1 287 . 51 GLU HA H 4.161 . 1 288 . 51 GLU CA C 57.678 . 1 289 . 51 GLU N N 122.69 . 1 290 . 52 GLU H H 8.272 . 1 291 . 52 GLU HA H 4.163 . 1 292 . 52 GLU C C 178.620 . 1 293 . 52 GLU CA C 57.590 . 1 294 . 52 GLU N N 120.70 . 1 295 . 53 ARG H H 8.228 . 1 296 . 53 ARG HA H 4.179 . 1 297 . 53 ARG C C 178.834 . 1 298 . 53 ARG CA C 57.660 . 1 299 . 53 ARG CB C 29.518 . 1 300 . 53 ARG N N 120.09 . 1 301 . 54 THR H H 8.143 . 1 302 . 54 THR HA H 4.304 . 1 303 . 54 THR C C 176.363 . 1 304 . 54 THR CA C 63.717 . 1 305 . 54 THR CB C 68.664 . 1 306 . 54 THR N N 114.23 . 1 307 . 55 ARG H H 8.113 . 1 308 . 55 ARG HA H 4.185 . 1 309 . 55 ARG C C 178.388 . 1 310 . 55 ARG CA C 57.260 . 1 311 . 55 ARG N N 122.64 . 1 312 . 56 LYS CA C 56.900 . 1 313 . 57 LEU H H 8.009 . 1 314 . 57 LEU CA C 55.400 . 1 315 . 57 LEU CB C 41.148 . 1 316 . 57 LEU N N 120.78 . 1 317 . 58 GLN H H 8.135 . 1 318 . 58 GLN HA H 4.226 . 1 319 . 58 GLN CA C 55.890 . 1 320 . 58 GLN N N 119.48 . 1 321 . 59 GLN H H 8.156 . 1 322 . 59 GLN HA H 4.267 . 1 323 . 59 GLN CA C 55.220 . 1 324 . 59 GLN N N 119.78 . 1 325 . 60 TYR H H 8.106 . 1 326 . 60 TYR HA H 4.563 . 1 327 . 60 TYR CA C 57.594 . 1 328 . 60 TYR CB C 37.835 . 1 329 . 60 TYR N N 120.43 . 1 330 . 61 ARG H H 8.011 . 1 331 . 61 ARG HA H 4.260 . 1 332 . 61 ARG C C 176.634 . 1 333 . 61 ARG CA C 55.514 . 1 334 . 61 ARG CB C 30.180 . 1 335 . 61 ARG N N 121.96 . 1 336 . 62 GLU H H 8.283 . 1 337 . 62 GLU HA H 4.231 . 1 338 . 62 GLU C C 176.854 . 1 339 . 62 GLU CA C 55.968 . 1 340 . 62 GLU CB C 29.450 . 1 341 . 62 GLU N N 121.10 . 1 342 . 63 MET H H 8.222 . 1 343 . 63 MET HA H 4.505 . 1 344 . 63 MET C C 175.679 . 1 345 . 63 MET CA C 54.580 . 1 346 . 63 MET CB C 32.125 . 1 347 . 63 MET N N 121.51 . 1 348 . 64 LEU H H 7.793 . 1 349 . 64 LEU HA H 4.186 . 1 350 . 64 LEU C C 183.104 . 1 351 . 64 LEU CA C 55.997 . 1 352 . 64 LEU CB C 42.341 . 1 353 . 64 LEU N N 128.98 . 1 stop_ save_