data_27227 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignments for mSin3B ; _BMRB_accession_number 27227 _BMRB_flat_file_name bmr27227.str _Entry_type original _Submission_date 2017-08-22 _Accession_date 2017-08-22 _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 Kurita Junichi . . 2 Hirao Yuuka . . 3 Nishimura Yoshifumi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 47 "15N chemical shifts" 46 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-10-09 original BMRB . stop_ _Original_release_date 2017-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A mimetic of the mSin3-binding helix of NRSF/REST ameliorates abnormal pain behavior in chronic pain models ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28927787 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ueda Hiroshi . . 2 Kurita Jun-Ichi I. . 3 Neyama Hiroyuki . . 4 Hirao Yuuka . . 5 Kouji Hiroyuki . . 6 Mishina Tadashi . . 7 Kasai Masaji . . 8 Nakano Hirofumi . . 9 Yoshimori Atsushi . . 10 Nishimura Yoshifumi . . stop_ _Journal_abbreviation 'Bioorg. Med. Chem. Lett.' _Journal_name_full 'Bioorganic & medicinal chemistry letters' _Journal_volume 27 _Journal_issue 20 _Journal_ISSN 1464-3405 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4705 _Page_last 4709 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'mSin3B PAH1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'mSin3B PAH domain' $mSin3B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mSin3B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mSin3B _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 84 _Mol_residue_sequence ; GSHMEKLPVHVEDALTYLDQ VKIRFGSDPATYNGFLEIMK EFKSQSIDTPGVIRRVSQLF HEHPDLIVGFNAFLPLGYRI DIPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 GLY 2 25 SER 3 26 HIS 4 27 MET 5 28 GLU 6 29 LYS 7 30 LEU 8 31 PRO 9 32 VAL 10 33 HIS 11 34 VAL 12 35 GLU 13 36 ASP 14 37 ALA 15 38 LEU 16 39 THR 17 40 TYR 18 41 LEU 19 42 ASP 20 43 GLN 21 44 VAL 22 45 LYS 23 46 ILE 24 47 ARG 25 48 PHE 26 49 GLY 27 50 SER 28 51 ASP 29 52 PRO 30 53 ALA 31 54 THR 32 55 TYR 33 56 ASN 34 57 GLY 35 58 PHE 36 59 LEU 37 60 GLU 38 61 ILE 39 62 MET 40 63 LYS 41 64 GLU 42 65 PHE 43 66 LYS 44 67 SER 45 68 GLN 46 69 SER 47 70 ILE 48 71 ASP 49 72 THR 50 73 PRO 51 74 GLY 52 75 VAL 53 76 ILE 54 77 ARG 55 78 ARG 56 79 VAL 57 80 SER 58 81 GLN 59 82 LEU 60 83 PHE 61 84 HIS 62 85 GLU 63 86 HIS 64 87 PRO 65 88 ASP 66 89 LEU 67 90 ILE 68 91 VAL 69 92 GLY 70 93 PHE 71 94 ASN 72 95 ALA 73 96 PHE 74 97 LEU 75 98 PRO 76 99 LEU 77 100 GLY 78 101 TYR 79 102 ARG 80 103 ILE 81 104 ASP 82 105 ILE 83 106 PRO 84 107 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $mSin3B Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $mSin3B 'recombinant technology' . Escherichia coli . pET28a 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 _Isotopic_labeling $mSin3B 100 uM '[U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRviewJ _Saveframe_category software _Name NMRviewJ _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCEIII _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'mSin3B PAH domain' _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 27 4 MET H H 8.211 . . 2 27 4 MET N N 121.993 . . 3 28 5 GLU H H 8.396 . . 4 28 5 GLU N N 121.589 . . 5 29 6 LYS H H 8.283 . . 6 29 6 LYS N N 122.025 . . 7 30 7 LEU H H 8.232 . . 8 30 7 LEU N N 124.606 . . 9 36 13 ASP H H 8.162 . . 10 36 13 ASP N N 120.345 . . 11 38 15 LEU H H 8.105 . . 12 38 15 LEU N N 118.022 . . 13 39 16 THR H H 8.276 . . 14 39 16 THR N N 116.000 . . 15 46 23 ILE H H 7.910 . . 16 46 23 ILE N N 118.052 . . 17 48 25 PHE H H 7.333 . . 18 48 25 PHE N N 112.714 . . 19 49 26 GLY H H 7.505 . . 20 49 26 GLY N N 110.016 . . 21 51 28 ASP H H 7.751 . . 22 51 28 ASP N N 120.549 . . 23 53 30 ALA H H 8.288 . . 24 54 31 THR H H 7.657 . . 25 54 31 THR N N 117.675 . . 26 56 33 ASN H H 8.988 . . 27 56 33 ASN N N 116.107 . . 28 57 34 GLY H H 7.968 . . 29 57 34 GLY N N 108.624 . . 30 59 36 LEU H H 7.965 . . 31 59 36 LEU N N 118.893 . . 32 61 38 ILE H H 7.485 . . 33 61 38 ILE N N 120.006 . . 34 62 39 MET H H 7.696 . . 35 62 39 MET N N 117.300 . . 36 63 40 LYS H H 7.929 . . 37 63 40 LYS N N 121.317 . . 38 65 42 PHE H H 8.600 . . 39 65 42 PHE N N 120.500 . . 40 66 43 LYS H H 8.470 . . 41 66 43 LYS N N 120.597 . . 42 67 44 SER H H 7.760 . . 43 67 44 SER N N 112.203 . . 44 68 45 GLN H H 7.912 . . 45 68 45 GLN N N 115.615 . . 46 69 46 SER H H 8.447 . . 47 69 46 SER N N 113.871 . . 48 70 47 ILE H H 7.262 . . 49 70 47 ILE N N 116.419 . . 50 71 48 ASP H H 7.959 . . 51 71 48 ASP N N 123.129 . . 52 72 49 THR H H 8.617 . . 53 72 49 THR N N 115.503 . . 54 74 51 GLY H H 7.997 . . 55 74 51 GLY N N 107.393 . . 56 75 52 VAL H H 8.531 . . 57 75 52 VAL N N 124.827 . . 58 76 53 ILE H H 7.994 . . 59 76 53 ILE N N 120.609 . . 60 77 54 ARG H H 8.046 . . 61 77 54 ARG N N 120.443 . . 62 78 55 ARG H H 7.917 . . 63 78 55 ARG N N 118.546 . . 64 79 56 VAL H H 8.690 . . 65 79 56 VAL N N 121.492 . . 66 80 57 SER H H 8.089 . . 67 80 57 SER N N 114.743 . . 68 81 58 GLN H H 7.330 . . 69 81 58 GLN N N 118.245 . . 70 83 60 PHE H H 8.282 . . 71 83 60 PHE N N 113.855 . . 72 84 61 HIS H H 7.178 . . 73 84 61 HIS N N 118.492 . . 74 86 63 HIS H H 8.267 . . 75 86 63 HIS N N 117.648 . . 76 88 65 ASP H H 8.792 . . 77 88 65 ASP N N 115.809 . . 78 89 66 LEU H H 7.859 . . 79 89 66 LEU N N 121.691 . . 80 92 69 GLY H H 7.998 . . 81 92 69 GLY N N 105.865 . . 82 95 72 ALA H H 7.108 . . 83 95 72 ALA N N 119.471 . . 84 96 73 PHE H H 7.397 . . 85 96 73 PHE N N 115.213 . . 86 101 78 TYR H H 7.825 . . 87 101 78 TYR N N 117.772 . . 88 104 81 ASP H H 8.494 . . 89 104 81 ASP N N 126.268 . . 90 105 82 ILE H H 8.203 . . 91 105 82 ILE N N 123.177 . . 92 107 84 LYS H H 7.952 . . 93 107 84 LYS N N 126.792 . . stop_ save_