data_7255 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for p53 tetramerization domain mutant Y327S T329E Q331G ; _BMRB_accession_number 7255 _BMRB_flat_file_name bmr7255.str _Entry_type original _Submission_date 2006-08-08 _Accession_date 2006-08-08 _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 Carbajo Rodrigo J. . 2 Mora Puig . . 3 'Sanchez del Pino' Manuel M. . 4 'Perez Paya' Enrique . . 5 Pineda-Lucena Antonio . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2008-02-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18076077 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mora Puig . . 2 Carbajo Rodrigo J. . 3 Pineda-Lucena Antonio . . 4 'Sanchez del Pino' Manuel M. . 5 'Perez Paya' Enrique . . stop_ _Journal_abbreviation Proteins _Journal_volume 71 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1670 _Page_last 1685 _Year 2008 _Details . loop_ _Keyword 'NMR structure' p53TD stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'p53 tetramerization domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $p53TD_Y327S_T329E_Q331G 'subunit 2' $p53TD_Y327S_T329E_Q331G 'subunit 3' $p53TD_Y327S_T329E_Q331G 'subunit 4' $p53TD_Y327S_T329E_Q331G stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'subunit 1' 1 'subunit 2' 1 'subunit 3' 1 'subunit 4' stop_ _Database_query_date . _Details 'p53 tetramerization domain (residues 326-356) mutant Y327S T329E Q331G' save_ ######################## # Monomeric polymers # ######################## save_p53TD_Y327S_T329E_Q331G _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p53TD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 31 _Mol_residue_sequence ; ESFELGIRGRERFEMFRELN EALELKDAQAG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 326 GLU 2 327 SER 3 328 PHE 4 329 GLU 5 330 LEU 6 331 GLY 7 332 ILE 8 333 ARG 9 334 GLY 10 335 ARG 11 336 GLU 12 337 ARG 13 338 PHE 14 339 GLU 15 340 MET 16 341 PHE 17 342 ARG 18 343 GLU 19 344 LEU 20 345 ASN 21 346 GLU 22 347 ALA 23 348 LEU 24 349 GLU 25 350 LEU 26 351 LYS 27 352 ASP 28 353 ALA 29 354 GLN 30 355 ALA 31 356 GLY 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 GB AAP30003 "tumor suppressor tp53 [Homo sapiens]" 80.65 35 100.00 100.00 4.77e-07 GB EAW90141 "tumor protein p53 (Li-Fraumeni syndrome), isoform CRA_b [Homo sapiens]" 54.84 54 100.00 100.00 8.23e-02 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $p53TD_Y327S_T329E_Q331G 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 $p53TD_Y327S_T329E_Q331G 'chemical synthesis' . . . . . 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 $p53TD_Y327S_T329E_Q331G 0.5 mM . 'phosphate buffer' 40 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task Processing stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Task Assignment stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'Structure calculations' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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-1H_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_1H-1H_TOCSY _Saveframe_category NMR_applied_experiment _Experiment_name '1H,1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 pH temperature 300 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 internal direct . . . 1.0 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'subunit 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 1 GLU H H 8.31 0.01 1 2 1 1 GLU HA H 4.16 0.01 1 3 1 1 GLU HB2 H 1.86 0.01 1 4 1 1 GLU HB3 H 1.86 0.01 1 5 1 1 GLU HG2 H 2.07 0.01 2 6 1 1 GLU HG3 H 2.18 0.01 2 7 2 2 SER H H 7.86 0.01 1 8 2 2 SER HA H 4.90 0.01 1 9 2 2 SER HB2 H 3.51 0.01 2 10 2 2 SER HB3 H 3.56 0.01 2 11 3 3 PHE H H 9.01 0.01 1 12 3 3 PHE HA H 4.31 0.01 1 13 3 3 PHE HB2 H 1.95 0.01 2 14 3 3 PHE HB3 H 2.14 0.01 2 15 3 3 PHE HD1 H 6.72 0.01 1 16 3 3 PHE HD2 H 6.72 0.01 1 17 3 3 PHE HE1 H 6.97 0.01 1 18 3 3 PHE HE2 H 6.97 0.01 1 19 3 3 PHE HZ H 7.09 0.01 1 20 4 4 GLU H H 8.27 0.01 1 21 4 4 GLU HA H 5.02 0.01 1 22 4 4 GLU HB2 H 1.71 0.01 2 23 4 4 GLU HB3 H 1.85 0.01 2 24 4 4 GLU HG2 H 2.03 0.01 1 25 4 4 GLU HG3 H 2.03 0.01 1 26 5 5 LEU H H 9.05 0.01 1 27 5 5 LEU HA H 4.81 0.01 1 28 5 5 LEU HB3 H 1.91 0.01 2 29 5 5 LEU HG H 1.35 0.01 1 30 5 5 LEU HD1 H 0.42 0.01 2 31 5 5 LEU HD2 H 0.87 0.01 2 32 6 6 GLY H H 8.72 0.01 1 33 6 6 GLY HA2 H 3.48 0.01 2 34 6 6 GLY HA3 H 4.61 0.01 2 35 7 7 ILE H H 8.96 0.01 1 36 7 7 ILE HA H 4.31 0.01 1 37 7 7 ILE HB H 1.73 0.01 1 38 7 7 ILE HG12 H 1.01 0.01 2 39 7 7 ILE HG13 H 1.40 0.01 2 40 7 7 ILE HG2 H 0.93 0.01 1 41 7 7 ILE HD1 H 0.69 0.01 1 42 8 8 ARG H H 9.65 0.01 1 43 8 8 ARG HA H 4.71 0.01 1 44 8 8 ARG HB2 H 1.74 0.01 2 45 8 8 ARG HB3 H 1.77 0.01 2 46 8 8 ARG HG2 H 1.50 0.01 2 47 8 8 ARG HG3 H 1.62 0.01 2 48 8 8 ARG HD2 H 3.13 0.01 1 49 8 8 ARG HD3 H 3.13 0.01 1 50 9 9 GLY H H 8.62 0.01 1 51 9 9 GLY HA2 H 3.80 0.01 2 52 9 9 GLY HA3 H 4.73 0.01 2 53 10 10 ARG H H 8.97 0.01 1 54 10 10 ARG HA H 3.35 0.01 1 55 10 10 ARG HB2 H 1.74 0.01 2 56 10 10 ARG HB3 H 1.90 0.01 2 57 10 10 ARG HG2 H 1.39 0.01 2 58 10 10 ARG HG3 H 1.56 0.01 2 59 10 10 ARG HD2 H 3.00 0.01 2 60 10 10 ARG HD3 H 3.08 0.01 2 61 11 11 GLU H H 8.90 0.01 1 62 11 11 GLU HA H 3.90 0.01 1 63 11 11 GLU HB2 H 1.94 0.01 2 64 11 11 GLU HB3 H 2.05 0.01 2 65 11 11 GLU HG2 H 2.26 0.01 2 66 11 11 GLU HG3 H 2.39 0.01 2 67 12 12 ARG H H 7.93 0.01 1 68 12 12 ARG HA H 3.86 0.01 1 69 12 12 ARG HB2 H 1.96 0.01 2 70 12 12 ARG HB3 H 2.01 0.01 2 71 12 12 ARG HG2 H 1.65 0.01 2 72 12 12 ARG HD2 H 3.47 0.01 2 73 12 12 ARG HD3 H 3.65 0.01 2 74 13 13 PHE H H 8.37 0.01 1 75 13 13 PHE HA H 4.11 0.01 1 76 13 13 PHE HB2 H 2.72 0.01 2 77 13 13 PHE HB3 H 2.78 0.01 2 78 13 13 PHE HD1 H 6.73 0.01 1 79 13 13 PHE HD2 H 6.73 0.01 1 80 13 13 PHE HE1 H 7.13 0.01 1 81 13 13 PHE HE2 H 7.13 0.01 1 82 13 13 PHE HZ H 7.34 0.01 1 83 14 14 GLU H H 8.55 0.01 1 84 14 14 GLU HA H 3.48 0.01 1 85 14 14 GLU HB2 H 1.91 0.01 2 86 14 14 GLU HB3 H 1.94 0.01 2 87 14 14 GLU HG2 H 2.25 0.01 2 88 14 14 GLU HG3 H 2.45 0.01 2 89 15 15 MET H H 7.61 0.01 1 90 15 15 MET HA H 4.07 0.01 1 91 15 15 MET HB2 H 1.91 0.01 2 92 15 15 MET HB3 H 2.21 0.01 2 93 15 15 MET HG2 H 1.96 0.01 2 94 15 15 MET HG3 H 2.50 0.01 2 95 15 15 MET HE H 1.43 0.01 1 96 16 16 PHE H H 8.04 0.01 1 97 16 16 PHE HA H 4.08 0.01 1 98 16 16 PHE HB2 H 2.60 0.01 2 99 16 16 PHE HB3 H 2.83 0.01 2 100 16 16 PHE HD1 H 7.08 0.01 1 101 16 16 PHE HD2 H 7.08 0.01 1 102 16 16 PHE HE1 H 7.27 0.01 1 103 16 16 PHE HE2 H 7.27 0.01 1 104 16 16 PHE HZ H 6.87 0.01 1 105 17 17 ARG H H 9.18 0.01 1 106 17 17 ARG HA H 3.62 0.01 1 107 17 17 ARG HB2 H 1.46 0.01 1 108 17 17 ARG HB3 H 1.51 0.01 1 109 17 17 ARG HG2 H 1.36 0.01 1 110 17 17 ARG HG3 H 1.36 0.01 1 111 17 17 ARG HD2 H 2.75 0.01 1 112 17 17 ARG HD3 H 2.75 0.01 1 113 18 18 GLU H H 7.81 0.01 1 114 18 18 GLU HA H 3.97 0.01 1 115 18 18 GLU HB2 H 2.05 0.01 1 116 18 18 GLU HB3 H 2.05 0.01 1 117 18 18 GLU HG2 H 2.13 0.01 2 118 18 18 GLU HG3 H 2.22 0.01 2 119 19 19 LEU H H 7.79 0.01 1 120 19 19 LEU HA H 4.02 0.01 1 121 19 19 LEU HB2 H 1.51 0.01 2 122 19 19 LEU HB3 H 2.20 0.01 2 123 19 19 LEU HG H 2.00 0.01 1 124 19 19 LEU HD1 H 0.75 0.01 2 125 19 19 LEU HD2 H 0.87 0.01 2 126 20 20 ASN H H 8.75 0.01 1 127 20 20 ASN HA H 4.49 0.01 1 128 20 20 ASN HB2 H 2.33 0.01 2 129 20 20 ASN HB3 H 2.73 0.01 2 130 20 20 ASN HD21 H 6.28 0.01 2 131 20 20 ASN HD22 H 7.61 0.01 2 132 21 21 GLU H H 8.75 0.01 1 133 21 21 GLU HA H 3.96 0.01 1 134 21 21 GLU HB2 H 2.03 0.01 2 135 21 21 GLU HB3 H 2.14 0.01 2 136 21 21 GLU HG2 H 2.18 0.01 2 137 21 21 GLU HG3 H 2.46 0.01 2 138 22 22 ALA H H 8.13 0.01 1 139 22 22 ALA HA H 4.03 0.01 1 140 22 22 ALA HB H 1.49 0.01 1 141 23 23 LEU H H 8.05 0.01 1 142 23 23 LEU HA H 3.99 0.01 1 143 23 23 LEU HB2 H 1.37 0.01 2 144 23 23 LEU HB3 H 2.14 0.01 2 145 23 23 LEU HG H 1.99 0.01 1 146 23 23 LEU HD1 H 0.83 0.01 2 147 23 23 LEU HD2 H 0.95 0.01 2 148 24 24 GLU H H 8.38 0.01 1 149 24 24 GLU HA H 4.16 0.01 1 150 24 24 GLU HB2 H 2.02 0.01 2 151 24 24 GLU HB3 H 2.14 0.01 2 152 24 24 GLU HG2 H 2.72 0.01 2 153 25 25 LEU H H 8.20 0.01 1 154 25 25 LEU HA H 4.21 0.01 1 155 25 25 LEU HB2 H 1.76 0.01 2 156 25 25 LEU HB3 H 1.91 0.01 2 157 25 25 LEU HG H 1.66 0.01 1 158 25 25 LEU HD1 H 0.85 0.01 2 159 25 25 LEU HD2 H 0.91 0.01 2 160 26 26 LYS H H 7.91 0.01 1 161 26 26 LYS HA H 3.91 0.01 1 162 26 26 LYS HB2 H 1.76 0.01 2 163 26 26 LYS HB3 H 2.30 0.01 2 164 26 26 LYS HG2 H 1.47 0.01 2 165 26 26 LYS HG3 H 1.54 0.01 2 166 26 26 LYS HD2 H 1.59 0.01 2 167 26 26 LYS HD3 H 1.65 0.01 2 168 26 26 LYS HE2 H 2.96 0.01 1 169 26 26 LYS HE3 H 2.96 0.01 1 170 27 27 ASP H H 8.21 0.01 1 171 27 27 ASP HA H 4.33 0.01 1 172 27 27 ASP HB2 H 2.71 0.01 2 173 27 27 ASP HB3 H 2.94 0.01 2 174 28 28 ALA H H 7.68 0.01 1 175 28 28 ALA HA H 4.22 0.01 1 176 28 28 ALA HB H 1.54 0.01 1 177 29 29 GLN H H 7.87 0.01 1 178 29 29 GLN HA H 4.22 0.01 1 179 29 29 GLN HB2 H 2.07 0.01 2 180 29 29 GLN HB3 H 2.23 0.01 2 181 29 29 GLN HG2 H 2.48 0.01 1 182 29 29 GLN HG3 H 2.48 0.01 1 183 29 29 GLN HE21 H 6.90 0.01 2 184 29 29 GLN HE22 H 7.44 0.01 2 185 30 30 ALA H H 7.93 0.01 1 186 30 30 ALA HA H 4.30 0.01 1 187 30 30 ALA HB H 1.46 0.01 1 188 31 31 GLY H H 8.13 0.01 1 189 31 31 GLY HA2 H 3.90 0.01 1 190 31 31 GLY HA3 H 3.90 0.01 1 stop_ save_