data_5457 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Complete 1H Chemical Shift Assignment of a 24-residue Sin Interacting Domain of hMad1 ; _BMRB_accession_number 5457 _BMRB_flat_file_name bmr5457.str _Entry_type original _Submission_date 2002-07-08 _Accession_date 2002-07-09 _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 'van Ingen' Hugo . . 2 Tessari Marco . . 3 Vuister Geerten G.W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 147 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-02 update BMRB 'update of the relationship loop' 2003-01-15 update author 'update of the system and chemical shifts' 2002-11-05 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4841 'PAH2 domain of mSin3B with Mad1-SID' 5808 'PAH2 domain of mSin3B with SID24 complex' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A 3D doubly sensitivity enhanced X-filtered TOCSY-TOCSY experiment' _Citation_status published _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 'van Ingen' Hugo . . 2 Tessari Marco . . 3 Vuister Geerten G.W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 155 _Page_last 160 _Year 2002 _Details . loop_ _Keyword MAD Sin 'Interacting Domain' PAH Sin3 stop_ save_ ################################## # Molecular system description # ################################## save_PAH2_SID _Saveframe_category molecular_system _Mol_system_name 'complex of hMad1-Sin Interacting Domain (SID) and PAH2 domain of mSin3B' _Abbreviation_common 'PAH2, SID' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PAH2 domain of mSin3B' $PAH2 'SID domain of Mad1' $SID stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SID _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Mad1 _Name_variant 'SID domain of Hs. Mad1' _Abbreviation_common SID _Molecular_mass 2973 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 24 _Mol_residue_sequence ; VRMNIQMLLEAADYLERRER EAEH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 5 VAL 2 6 ARG 3 7 MET 4 8 ASN 5 9 ILE 6 10 GLN 7 11 MET 8 12 LEU 9 13 LEU 10 14 GLU 11 15 ALA 12 16 ALA 13 17 ASP 14 18 TYR 15 19 LEU 16 20 GLU 17 21 ARG 18 22 ARG 19 23 GLU 20 24 ARG 21 25 GLU 22 26 ALA 23 27 GLU 24 28 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 4874 mSin3B-PAH2 100.00 105 100.00 100.00 2.50e-69 BMRB 6899 PAH2 100.00 105 100.00 100.00 2.50e-69 PDB 1E91 "Structure Of The Complex Of The Mad1-Sin3b Interaction Domains" 80.95 85 100.00 100.00 3.07e-54 PDB 1PD7 "Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b" 80.95 85 100.00 100.00 3.07e-54 PDB 2F05 "Solution Structure Of Free Pah2 Domain Of Msin3b" 100.00 105 99.05 99.05 9.79e-69 GB AAH51536 "Sin3b protein, partial [Mus musculus]" 100.00 190 99.05 99.05 3.20e-68 GB EDL10815 "transcriptional regulator, SIN3B (yeast), isoform CRA_c [Mus musculus]" 100.00 893 99.05 99.05 2.94e-63 GB EDL90863 "rCG38713, isoform CRA_e [Rattus norvegicus]" 100.00 231 98.10 98.10 1.55e-66 GB EDL90864 "rCG38713, isoform CRA_f [Rattus norvegicus]" 100.00 841 98.10 98.10 1.31e-62 REF XP_006751561 "PREDICTED: paired amphipathic helix protein Sin3b-like [Leptonychotes weddellii]" 82.86 342 98.85 98.85 3.37e-52 stop_ save_ save_PAH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mSin3B _Name_variant 'PAH2 domain of Mm. mSin3B' _Abbreviation_common PAH2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 105 _Mol_residue_sequence ; ESDSVEFNNAISYVNKIKTR FLDHPEIYRSFLEILHTYQK EQLHTKGRPFRGMSEEEVFT EVANLFRGQEDLLSEFGQFL PEAKRSLFTGNGSAEMNSGQ KNEEK ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 SER 3 ASP 4 SER 5 VAL 6 GLU 7 PHE 8 ASN 9 ASN 10 ALA 11 ILE 12 SER 13 TYR 14 VAL 15 ASN 16 LYS 17 ILE 18 LYS 19 THR 20 ARG 21 PHE 22 LEU 23 ASP 24 HIS 25 PRO 26 GLU 27 ILE 28 TYR 29 ARG 30 SER 31 PHE 32 LEU 33 GLU 34 ILE 35 LEU 36 HIS 37 THR 38 TYR 39 GLN 40 LYS 41 GLU 42 GLN 43 LEU 44 HIS 45 THR 46 LYS 47 GLY 48 ARG 49 PRO 50 PHE 51 ARG 52 GLY 53 MET 54 SER 55 GLU 56 GLU 57 GLU 58 VAL 59 PHE 60 THR 61 GLU 62 VAL 63 ALA 64 ASN 65 LEU 66 PHE 67 ARG 68 GLY 69 GLN 70 GLU 71 ASP 72 LEU 73 LEU 74 SER 75 GLU 76 PHE 77 GLY 78 GLN 79 PHE 80 LEU 81 PRO 82 GLU 83 ALA 84 LYS 85 ARG 86 SER 87 LEU 88 PHE 89 THR 90 GLY 91 ASN 92 GLY 93 SER 94 ALA 95 GLU 96 MET 97 ASN 98 SER 99 GLY 100 GLN 101 LYS 102 ASN 103 GLU 104 GLU 105 LYS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 GenBank EDL90864 'rCG38713, isoform CRA_f [Rattus norvegicus]' 100.00 841 98.10 98.10 1.92e-54 GenBank EDL90863 'rCG38713, isoform CRA_e [Rattus norvegicus]' 100.00 231 98.10 98.10 1.12e-53 GenBank EDL10815 'transcriptional regulator, SIN3B (yeast), isoform CRA_c [Mus musculus]' 100.00 893 99.05 99.05 4.64e-55 GenBank AAH51536 'Sin3b protein [Mus musculus]' 100.00 190 99.05 99.05 1.52e-54 PDB 2F05 'Solution Structure Of Free Pah2 Domain Of Msin3b' 100.00 105 99.05 99.05 4.80e-54 PDB 1PD7 'Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b' 80.00 85 100.00 100.00 4.32e-42 PDB 1E91 'Structure Of The Complex Of The Mad1-Sin3b Interaction Domains' 80.00 85 100.00 100.00 4.32e-42 BMRB 6899 'PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 BMRB 5808 'PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 BMRB 4874 'mSin3B-PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 BMRB 4841 'mSin3B-PAH2 domain' 100.00 105 100.00 100.00 1.69e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PAH2 'house mouse' 10090 Eukaryota Metazoa Mus musculus $SID human 9606 Eukaryota Metazoa Homo sapiens 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 $PAH2 'recombinant technology' . . . . . $SID 'solid phase synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The sample also contained trace amounts of sodiumazide and protease inhibitor' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SID 1.3 mM '[U-15N; U-13C]' $PAH2 1.3 mM . 'potassium phosphate' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . _Details . save_ save_Xeasy _Saveframe_category software _Name Xeasy _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_The_use_of_a_3D_TOCSY-TOCSY_was_required_to_solve_high_degree_of_overlap_in_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'The use of a 3D TOCSY-TOCSY was required to solve high degree of overlap in' _Sample_label $sample_1 save_ save_the_2D_TOCSY_spectrum._The_overlap_is_caused_by_the_highly_redundant_amino_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'the 2D TOCSY spectrum. The overlap is caused by the highly redundant amino' _Sample_label $sample_1 save_ save_acid_composition_of_the_C-terminal_part_of_the_SID_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'acid composition of the C-terminal part of the SID' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 293 0.5 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation 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_set_1 _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 'SID domain of Mad1' _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 . 2 ARG H H 8.498 0.01 1 2 . 2 ARG HA H 4.373 0.01 1 3 . 2 ARG HB2 H 1.730 0.01 2 4 . 2 ARG HB3 H 1.800 0.01 2 5 . 2 ARG HG2 H 1.628 0.01 1 6 . 2 ARG HG3 H 1.628 0.01 1 7 . 2 ARG HD2 H 3.197 0.01 1 8 . 2 ARG HD3 H 3.197 0.01 1 9 . 2 ARG HE H 7.329 0.01 1 10 . 3 MET H H 8.495 0.01 1 11 . 3 MET HA H 4.497 0.01 1 12 . 3 MET HB2 H 1.754 0.01 2 13 . 3 MET HB3 H 1.803 0.01 2 14 . 3 MET HG2 H 2.322 0.01 2 15 . 3 MET HG3 H 2.439 0.01 2 16 . 4 ASN H H 7.375 0.01 1 17 . 4 ASN HA H 5.382 0.01 1 18 . 4 ASN HB2 H 2.983 0.01 2 19 . 4 ASN HB3 H 3.476 0.01 2 20 . 4 ASN HD21 H 7.625 0.01 2 21 . 4 ASN HD22 H 6.908 0.01 2 22 . 5 ILE H H 8.485 0.01 1 23 . 5 ILE HA H 3.745 0.01 1 24 . 5 ILE HB H 2.062 0.01 1 25 . 5 ILE HG2 H 0.974 0.01 1 26 . 5 ILE HG12 H 1.264 0.01 2 27 . 5 ILE HG13 H 1.645 0.01 2 28 . 5 ILE HD1 H 0.551 0.01 1 29 . 6 GLN H H 8.349 0.01 1 30 . 6 GLN HA H 3.926 0.01 1 31 . 6 GLN HB2 H 2.083 0.01 2 32 . 6 GLN HB3 H 2.196 0.01 2 33 . 6 GLN HG2 H 2.424 0.01 2 34 . 6 GLN HG3 H 2.395 0.01 2 35 . 6 GLN HE21 H 6.817 0.01 2 36 . 6 GLN HE22 H 7.832 0.01 2 37 . 7 MET H H 8.132 0.01 1 38 . 7 MET HA H 4.302 0.01 1 39 . 7 MET HB2 H 2.308 0.01 2 40 . 7 MET HB3 H 2.394 0.01 2 41 . 7 MET HG2 H 2.584 0.01 2 42 . 7 MET HG3 H 2.905 0.01 2 43 . 8 LEU H H 7.659 0.01 1 44 . 8 LEU HA H 3.928 0.01 1 45 . 8 LEU HB2 H 1.226 0.01 2 46 . 8 LEU HB3 H 2.110 0.01 2 47 . 8 LEU HG H 1.473 0.01 1 48 . 8 LEU HD1 H 0.278 0.01 2 49 . 8 LEU HD2 H 0.777 0.01 2 50 . 9 LEU H H 7.901 0.01 1 51 . 9 LEU HA H 3.951 0.01 1 52 . 9 LEU HB2 H 1.423 0.01 2 53 . 9 LEU HB3 H 1.985 0.01 2 54 . 9 LEU HG H 1.539 0.01 1 55 . 9 LEU HD1 H 0.456 0.01 2 56 . 9 LEU HD2 H 0.575 0.01 2 57 . 10 GLU H H 8.487 0.01 1 58 . 10 GLU HA H 4.238 0.01 1 59 . 10 GLU HB2 H 2.392 0.01 2 60 . 10 GLU HB3 H 2.247 0.01 2 61 . 10 GLU HG2 H 2.630 0.01 1 62 . 10 GLU HG3 H 2.630 0.01 1 63 . 11 ALA H H 8.826 0.01 1 64 . 11 ALA HA H 4.098 0.01 1 65 . 11 ALA HB H 1.287 0.01 1 66 . 12 ALA H H 8.556 0.01 1 67 . 12 ALA HA H 4.158 0.01 1 68 . 12 ALA HB H 1.654 0.01 1 69 . 13 ASP H H 8.184 0.01 1 70 . 13 ASP HA H 4.503 0.01 1 71 . 13 ASP HB2 H 2.804 0.01 2 72 . 13 ASP HB3 H 2.915 0.01 2 73 . 14 TYR H H 8.356 0.01 1 74 . 14 TYR HA H 4.153 0.01 1 75 . 14 TYR HB2 H 3.403 0.01 2 76 . 14 TYR HB3 H 3.538 0.01 2 77 . 14 TYR HD1 H 7.133 0.01 1 78 . 14 TYR HD2 H 7.133 0.01 1 79 . 14 TYR HE1 H 6.845 0.01 1 80 . 14 TYR HE2 H 6.845 0.01 1 81 . 15 LEU H H 8.469 0.01 1 82 . 15 LEU HA H 3.894 0.01 1 83 . 15 LEU HB2 H 1.970 0.01 1 84 . 15 LEU HB3 H 1.970 0.01 1 85 . 15 LEU HG H 1.581 0.01 1 86 . 15 LEU HD1 H 0.936 0.01 1 87 . 15 LEU HD2 H 0.936 0.01 1 88 . 16 GLU H H 7.984 0.01 1 89 . 16 GLU HA H 4.096 0.01 1 90 . 16 GLU HB2 H 2.201 0.01 1 91 . 16 GLU HB3 H 2.201 0.01 1 92 . 16 GLU HG2 H 2.378 0.01 1 93 . 16 GLU HG3 H 2.378 0.01 1 94 . 17 ARG H H 8.090 0.01 1 95 . 17 ARG HA H 3.954 0.01 1 96 . 17 ARG HB2 H 1.810 0.01 2 97 . 17 ARG HB3 H 1.852 0.01 2 98 . 17 ARG HG2 H 1.528 0.01 2 99 . 17 ARG HG3 H 1.755 0.01 2 100 . 17 ARG HD2 H 3.135 0.01 2 101 . 17 ARG HD3 H 3.202 0.01 2 102 . 17 ARG HE H 7.450 0.01 1 103 . 18 ARG H H 8.003 0.01 1 104 . 18 ARG HA H 3.966 0.01 1 105 . 18 ARG HB2 H 1.640 0.01 2 106 . 18 ARG HB3 H 1.774 0.01 2 107 . 18 ARG HG2 H 1.448 0.01 2 108 . 18 ARG HG3 H 1.482 0.01 2 109 . 18 ARG HD2 H 2.949 0.01 2 110 . 18 ARG HD3 H 3.033 0.01 2 111 . 18 ARG HE H 7.238 0.01 1 112 . 19 GLU H H 7.885 0.01 1 113 . 19 GLU HA H 4.066 0.01 1 114 . 19 GLU HB2 H 2.082 0.01 1 115 . 19 GLU HB3 H 2.082 0.01 1 116 . 19 GLU HG2 H 2.222 0.01 2 117 . 19 GLU HG3 H 2.363 0.01 2 118 . 20 ARG H H 7.929 0.01 1 119 . 20 ARG HA H 4.189 0.01 1 120 . 20 ARG HB2 H 1.900 0.01 1 121 . 20 ARG HB3 H 1.900 0.01 1 122 . 20 ARG HG2 H 1.689 0.01 2 123 . 20 ARG HG3 H 1.741 0.01 2 124 . 20 ARG HD2 H 3.195 0.01 1 125 . 20 ARG HD3 H 3.195 0.01 1 126 . 20 ARG HE H 7.439 0.01 1 127 . 21 GLU H H 8.056 0.01 1 128 . 21 GLU HA H 4.095 0.01 1 129 . 21 GLU HB2 H 2.010 0.01 1 130 . 21 GLU HB3 H 2.010 0.01 1 131 . 21 GLU HG2 H 2.251 0.01 2 132 . 21 GLU HG3 H 2.390 0.01 2 133 . 22 ALA H H 7.810 0.01 1 134 . 22 ALA HA H 4.198 0.01 1 135 . 22 ALA HB H 1.404 0.01 1 136 . 23 GLU H H 7.972 0.01 1 137 . 23 GLU HA H 4.118 0.01 1 138 . 23 GLU HB2 H 1.946 0.01 1 139 . 23 GLU HB3 H 1.946 0.01 1 140 . 23 GLU HG2 H 2.261 0.01 2 141 . 23 GLU HG3 H 2.139 0.01 2 142 . 24 HIS H H 8.181 0.01 1 143 . 24 HIS HA H 4.629 0.01 1 144 . 24 HIS HB2 H 3.132 0.01 2 145 . 24 HIS HB3 H 3.271 0.01 2 146 . 24 HIS HD2 H 7.215 0.01 3 147 . 24 HIS HE1 H 7.470 0.01 3 stop_ save_