data_6522 save_study_list _Study_list.Sf_category study_list _Study_list.Sf_framecode study_list _Study_list.Entry_ID 6522 _Study_list.ID 1 loop_ _Study.ID _Study.Name _Study.Type _Study.Details _Study.Entry_ID _Study.Study_list_ID 1 'Characterization of an amyloid fibril intermediate' 'Structure analysis' 'Data from these entries were used to assign residues for H/D exchange and stability studies at pH 4.0' 6522 1 2 'Characterization of an amyloid fibril intermediate' 'Structure analysis' 'Data from these entries were used to assign residues for H/D exchange and stability studies at pH 6.0' 6522 1 stop_ loop_ _Study_keyword.Study_ID _Study_keyword.Keyword _Study_keyword.Entry_ID _Study_keyword.Study_list_ID 1 'Amyloid fibril intermediate' 6522 1 1 'Hydrogen exchange studies' 6522 1 1 'Mutant p53 tetramerization domain' 6522 1 1 'Mutant tetramerization domain of p53 (residues 310 - 360)' 6522 1 1 'Nuclear Magnetic Resonance' 6522 1 1 R337H 6522 1 1 'Tumor suppressor protein p53 - human' 6522 1 1 p53tet-R337H 6522 1 stop_ save_ ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6522 _Entry.Title ; Characterization of an amyloid fibril intermediate ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2005-02-23 _Entry.Accession_date 2005-02-23 _Entry.Last_release_date 2005-02-23 _Entry.Original_release_date 2005-02-23 _Entry.Origination author _Entry.NMR_STAR_version 3.1.2.6 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details 'Backbone residue assignments were used for H/D exchange, pKa and stability studies of p53tet-R337H' _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.ORCID _Entry_author.Entry_ID 1 Charles Galea . A. . . 6522 2 Prentice Bowman . . . . 6522 3 Richard Kriwacki . W. . . 6522 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 6522 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 105 6522 '15N chemical shifts' 95 6522 '1H chemical shifts' 95 6522 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 . . 2007-01-29 . original BMRB . 6522 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4048 'Data were collected at a different pH for this molecular system.' 6522 BMRB 6521 'p53 tetramer' 6522 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6522 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16260757 _Citation.Full_citation . _Citation.Title ; Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 14 _Citation.Journal_issue 12 _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 2993 _Citation.Page_last 3003 _Citation.Year 2005 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Charles Galea . A. . . 6522 1 2 Prentice Bowman . . . . 6522 1 3 Richard Kriwacki . W. . . 6522 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'H/D exchange' 6522 1 'Mutant p53 tetramerization domain' 6522 1 R337H 6522 1 'amyloid fibril intermediate' 6522 1 p53tet-R337H 6522 1 'pKa studies' 6522 1 'tumor supressor protein' 6522 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 6522 _Assembly.ID 1 _Assembly.Name 'Mutant p53 tetramerization domain (p53tet-R337H)' _Assembly.BMRB_code . _Assembly.Number_of_components 4 _Assembly.Organic_ligands 0 _Assembly.Metal_ions 0 _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states no _Assembly.Ambiguous_chem_comp_sites no _Assembly.Molecules_in_chemical_exchange no _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass 24527 _Assembly.Enzyme_commission_number . _Assembly.Details Homotetramer _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID 'protein-protein complex' 6522 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 'subunit A' 1 $Mutant_p53_tetramerization_domain_polypeptide . . yes native no no 1 'oligomerization domain' . 6522 1 2 'subunit B' 1 $Mutant_p53_tetramerization_domain_polypeptide . . yes native no no 1 'oligomerization domain' . 6522 1 3 'subunit C' 1 $Mutant_p53_tetramerization_domain_polypeptide . . yes native no no 1 'oligomerization domain' . 6522 1 4 'subunit D' 1 $Mutant_p53_tetramerization_domain_polypeptide . . yes native no no 1 'oligomerization domain' . 6522 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes BMRB 4048 . . NMR . 'NMR solution structure of p53 tetramerization domain' . 6522 1 yes PDB 1A1U . . NMR . 'NMR solution structure of a mutant p53 dimerization domain' 'Mutants: M40K, F41I and L44Y' 6522 1 yes PDB 1AIE . . 'X-ray crystallography' 1.5 'Crystal structure of p53 tetramerization domain' . 6522 1 yes PDB 1C26 . . 'X-ray crystallography' 1.7 'Crystal structure of p53 tetramerization domain' . 6522 1 yes PDB 1HS5 . . NMR . 'NMR solution structure of designed p53 dimer' 'Residues 324 - 357' 6522 1 yes PDB 1OLG . . NMR . 'NMR solution structure of a mutant p53 dimerization domain' . 6522 1 yes PDB 1PES . . NMR . 'NMR solution structure of p53 tetramerization domain' . 6522 1 yes PDB 1PET . . NMR . 'NMR solution structure of p53 tetramerization domain' . 6522 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Transcription factor' 6522 1 stop_ loop_ _Assembly_keyword.Keyword _Assembly_keyword.Entry_ID _Assembly_keyword.Assembly_ID 'Mutant p53 tetramerization domain' 6522 1 R337H 6522 1 'amyloid fibril intermediate' 6522 1 p53tet-R337H 6522 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Mutant_p53_tetramerization_domain_polypeptide _Entity.Sf_category entity _Entity.Sf_framecode Mutant_p53_tetramerization_domain_polypeptide _Entity.Entry_ID 6522 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Mutant_p53_tetramerization_domain_polypeptide _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 ; GSHMNTSSSPQPKKKPLDGE YFTLQIRGRERFEMFRELNE ALELKDAQAGKEPG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'Residues 11 to 60 correspond to residues 310 to 360 of p53. Arg337 has been substituted by His.' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 54 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _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 6131.8 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'transcription factor' 6522 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Mutant p53 tetramerization domain' na 6522 1 p53tet-R337H na 6522 1 stop_ loop_ _Entity_keyword.Keyword _Entity_keyword.Entry_ID _Entity_keyword.Entity_ID 'Mutant p53 tetramerization domain' 6522 1 p53tet-R337H 6522 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 . GLY . 6522 1 2 . SER . 6522 1 3 . HIS . 6522 1 4 . MET . 6522 1 5 . ASN . 6522 1 6 . THR . 6522 1 7 . SER . 6522 1 8 . SER . 6522 1 9 . SER . 6522 1 10 . PRO . 6522 1 11 . GLN . 6522 1 12 . PRO . 6522 1 13 . LYS . 6522 1 14 . LYS . 6522 1 15 . LYS . 6522 1 16 . PRO . 6522 1 17 . LEU . 6522 1 18 . ASP . 6522 1 19 . GLY . 6522 1 20 . GLU . 6522 1 21 . TYR . 6522 1 22 . PHE . 6522 1 23 . THR . 6522 1 24 . LEU . 6522 1 25 . GLN . 6522 1 26 . ILE . 6522 1 27 . ARG . 6522 1 28 . GLY . 6522 1 29 . ARG . 6522 1 30 . GLU . 6522 1 31 . ARG . 6522 1 32 . PHE . 6522 1 33 . GLU . 6522 1 34 . MET . 6522 1 35 . PHE . 6522 1 36 . ARG . 6522 1 37 . GLU . 6522 1 38 . LEU . 6522 1 39 . ASN . 6522 1 40 . GLU . 6522 1 41 . ALA . 6522 1 42 . LEU . 6522 1 43 . GLU . 6522 1 44 . LEU . 6522 1 45 . LYS . 6522 1 46 . ASP . 6522 1 47 . ALA . 6522 1 48 . GLN . 6522 1 49 . ALA . 6522 1 50 . GLY . 6522 1 51 . LYS . 6522 1 52 . GLU . 6522 1 53 . PRO . 6522 1 54 . GLY . 6522 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 . GLY 1 1 6522 1 . SER 2 2 6522 1 . HIS 3 3 6522 1 . MET 4 4 6522 1 . ASN 5 5 6522 1 . THR 6 6 6522 1 . SER 7 7 6522 1 . SER 8 8 6522 1 . SER 9 9 6522 1 . PRO 10 10 6522 1 . GLN 11 11 6522 1 . PRO 12 12 6522 1 . LYS 13 13 6522 1 . LYS 14 14 6522 1 . LYS 15 15 6522 1 . PRO 16 16 6522 1 . LEU 17 17 6522 1 . ASP 18 18 6522 1 . GLY 19 19 6522 1 . GLU 20 20 6522 1 . TYR 21 21 6522 1 . PHE 22 22 6522 1 . THR 23 23 6522 1 . LEU 24 24 6522 1 . GLN 25 25 6522 1 . ILE 26 26 6522 1 . ARG 27 27 6522 1 . GLY 28 28 6522 1 . ARG 29 29 6522 1 . GLU 30 30 6522 1 . ARG 31 31 6522 1 . PHE 32 32 6522 1 . GLU 33 33 6522 1 . MET 34 34 6522 1 . PHE 35 35 6522 1 . ARG 36 36 6522 1 . GLU 37 37 6522 1 . LEU 38 38 6522 1 . ASN 39 39 6522 1 . GLU 40 40 6522 1 . ALA 41 41 6522 1 . LEU 42 42 6522 1 . GLU 43 43 6522 1 . LEU 44 44 6522 1 . LYS 45 45 6522 1 . ASP 46 46 6522 1 . ALA 47 47 6522 1 . GLN 48 48 6522 1 . ALA 49 49 6522 1 . GLY 50 50 6522 1 . LYS 51 51 6522 1 . GLU 52 52 6522 1 . PRO 53 53 6522 1 . GLY 54 54 6522 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 6522 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Mutant_p53_tetramerization_domain_polypeptide . 9606 . yes . human . . Eukaryota Metazoa homo sapiens . . . . . . . . . . . . . 6522 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 6522 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Mutant_p53_tetramerization_domain_polypeptide . 'recombinant technology' . 'E. coli' . . Escherichia coli BL21 DE3 . . . . . . . . 6522 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 6522 _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 p53tet-R337H [U-15N] 1 $assembly 1 $Mutant_p53_tetramerization_domain_polypeptide . protein 4.0 . . mM . . . . 6522 1 2 Na2HPO4 . . . . . . buffer 10.0 . . mM . . . . 6522 1 3 NaCl . . . . . . salt 50.0 . . mM . . . . 6522 1 4 NaN3 . . . . . . salt 0.02 . . % . . . . 6522 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 6522 _Sample.ID 2 _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 p53tet-R337H 'U-13C; U-15N' 1 $assembly 1 $Mutant_p53_tetramerization_domain_polypeptide . protein 4.0 . . mM . . . . 6522 2 2 Na2HPO4 . . . . . . buffer 10.0 . . mM . . . . 6522 2 3 NaCl . . . . . . salt 50.0 . . mM . . . . 6522 2 4 NaN3 . . . . . . salt 0.02 . . % . . . . 6522 2 stop_ save_ ####################### # Sample conditions # ####################### save_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_1 _Sample_condition_list.Entry_ID 6522 _Sample_condition_list.ID 1 _Sample_condition_list.Details . 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 6.0 0.05 pH 6522 1 temperature 293.0 0.1 K 6522 1 stop_ save_ save_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions_2 _Sample_condition_list.Entry_ID 6522 _Sample_condition_list.ID 2 _Sample_condition_list.Details . 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 4.0 0.05 pH 6522 2 temperature 293.0 0.1 K 6522 2 stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Software.Sf_category software _Software.Sf_framecode software_1 _Software.Entry_ID 6522 _Software.ID 1 _Software.Name Felix _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Accelrys 'Accelrys, Inc. 10188 Telesis Court, Suite 100 San Diego, CA 92121 USA Phone: +1 858 799 5000 Fax: +1 858 799 5100' http://www.accelrys.com/ 6522 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Chemical Shift Assignments' 6522 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode 600MHz_spectrometer _NMR_spectrometer.Entry_ID 6522 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'INOVA 600' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode NMR_experiment_list _Experiment_list.Entry_ID 6522 _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 1H15N_HSQC no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 2 HNCA no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 3 HN(CO)CA no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 4 HNCACB no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 5 CBCA(CO)NH no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 6 1H15N_NOESY no . . . . . . . . . . . . . . . . . . . . 1 $600MHz_spectrometer . . . . . . . . . . . . . . . . 6522 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_referencing _Chem_shift_reference.Entry_ID 6522 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 TSP 'methyl protons' . . . . ppm 0.00 external indirect . . . . . . 6522 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 6522 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _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 'Chemical shift assignments for p53tet-R337H at pH 6.0' _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 1H15N_HSQC . . isotropic 6522 1 2 HNCA . . isotropic 6522 1 3 HN(CO)CA . . isotropic 6522 1 4 HNCACB . . isotropic 6522 1 5 CBCA(CO)NH . . isotropic 6522 1 6 1H15N_NOESY . . isotropic 6522 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $software_1 . . 6522 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 4 4 MET H H 1 8.313 . . . . . . . 10 MET H . 6522 1 2 . 1 1 4 4 MET CA C 13 55.11147 . . . . . . . 10 MET CA . 6522 1 3 . 1 1 4 4 MET N N 15 123.176 . . . . . . . 10 MET N . 6522 1 4 . 1 1 5 5 ASN H H 1 8.469 . . . . . . . 11 ASN H . 6522 1 5 . 1 1 5 5 ASN CA C 13 52.97075 . . . . . . . 11 ASN CA . 6522 1 6 . 1 1 5 5 ASN N N 15 121.892 . . . . . . . 11 ASN N . 6522 1 7 . 1 1 6 6 THR H H 1 8.064 . . . . . . . 12 THR H . 6522 1 8 . 1 1 6 6 THR CA C 13 61.20434 . . . . . . . 12 THR CA . 6522 1 9 . 1 1 6 6 THR N N 15 115.726 . . . . . . . 12 THR N . 6522 1 10 . 1 1 7 7 SER H H 1 8.135 . . . . . . . 13 SER H . 6522 1 11 . 1 1 7 7 SER CA C 13 57.95821 . . . . . . . 13 SER CA . 6522 1 12 . 1 1 7 7 SER N N 15 119.074 . . . . . . . 13 SER N . 6522 1 13 . 1 1 8 8 SER H H 1 8.195 . . . . . . . 14 SER H . 6522 1 14 . 1 1 8 8 SER CA C 13 57.85863 . . . . . . . 14 SER CA . 6522 1 15 . 1 1 8 8 SER N N 15 118.953 . . . . . . . 14 SER N . 6522 1 16 . 1 1 9 9 SER H H 1 8.117 . . . . . . . 15 SER H . 6522 1 17 . 1 1 9 9 SER CA C 13 56.04787 . . . . . . . 15 SER CA . 6522 1 18 . 1 1 9 9 SER N N 15 120.146 . . . . . . . 15 SER N . 6522 1 19 . 1 1 10 10 PRO CA C 13 63.13255 . . . . . . . 16 PRO H . 6522 1 20 . 1 1 11 11 GLN H H 1 7.934 . . . . . . . 17 GLN H . 6522 1 21 . 1 1 11 11 GLN CA C 13 52.77706 . . . . . . . 17 GLN CA . 6522 1 22 . 1 1 11 11 GLN N N 15 120.431 . . . . . . . 17 GLN N . 6522 1 23 . 1 1 12 12 PRO CA C 13 62.80736 . . . . . . . 18 PRO H . 6522 1 24 . 1 1 13 13 LYS H H 1 8.27 . . . . . . . 19 LYS H . 6522 1 25 . 1 1 13 13 LYS CA C 13 56.26735 . . . . . . . 19 LYS CA . 6522 1 26 . 1 1 13 13 LYS N N 15 123.212 . . . . . . . 19 LYS N . 6522 1 27 . 1 1 14 14 LYS H H 1 8.181 . . . . . . . 20 LYS H . 6522 1 28 . 1 1 14 14 LYS CA C 13 56 . . . . . . . 20 LYS CA . 6522 1 29 . 1 1 14 14 LYS N N 15 124.416 . . . . . . . 20 LYS N . 6522 1 30 . 1 1 15 15 LYS H H 1 8.281 . . . . . . . 21 LYS H . 6522 1 31 . 1 1 15 15 LYS CA C 13 53.94794 . . . . . . . 21 LYS CA . 6522 1 32 . 1 1 15 15 LYS N N 15 126.174 . . . . . . . 21 LYS N . 6522 1 33 . 1 1 16 16 PRO CA C 13 62.80927 . . . . . . . 22 PRO H . 6522 1 34 . 1 1 17 17 LEU H H 1 8.22 . . . . . . . 23 LEU H . 6522 1 35 . 1 1 17 17 LEU CA C 13 54.79747 . . . . . . . 23 LEU CA . 6522 1 36 . 1 1 17 17 LEU N N 15 123.325 . . . . . . . 23 LEU N . 6522 1 37 . 1 1 18 18 ASP H H 1 8.13 . . . . . . . 24 ASP H . 6522 1 38 . 1 1 18 18 ASP CA C 13 53.85928 . . . . . . . 24 ASP CA . 6522 1 39 . 1 1 18 18 ASP N N 15 122.758 . . . . . . . 24 ASP N . 6522 1 40 . 1 1 19 19 GLY H H 1 8.086 . . . . . . . 25 GLY H . 6522 1 41 . 1 1 19 19 GLY CA C 13 44.61739 . . . . . . . 25 GLY CA . 6522 1 42 . 1 1 19 19 GLY N N 15 110.413 . . . . . . . 25 GLY N . 6522 1 43 . 1 1 20 20 GLU H H 1 7.84 . . . . . . . 26 GLU H . 6522 1 44 . 1 1 20 20 GLU CA C 13 56.67536 . . . . . . . 26 GLU CA . 6522 1 45 . 1 1 20 20 GLU N N 15 122.063 . . . . . . . 26 GLU N . 6522 1 46 . 1 1 21 21 TYR H H 1 7.911 . . . . . . . 27 TYR H . 6522 1 47 . 1 1 21 21 TYR CA C 13 57.03203 . . . . . . . 27 TYR CA . 6522 1 48 . 1 1 21 21 TYR N N 15 121.631 . . . . . . . 27 TYR N . 6522 1 49 . 1 1 22 22 PHE H H 1 9.067 . . . . . . . 28 PHE H . 6522 1 50 . 1 1 22 22 PHE CA C 13 56.24717 . . . . . . . 28 PHE CA . 6522 1 51 . 1 1 22 22 PHE N N 15 122.586 . . . . . . . 28 PHE N . 6522 1 52 . 1 1 23 23 THR H H 1 8.324 . . . . . . . 29 THR H . 6522 1 53 . 1 1 23 23 THR CA C 13 61.1375 . . . . . . . 29 THR CA . 6522 1 54 . 1 1 23 23 THR N N 15 116.38 . . . . . . . 29 THR N . 6522 1 55 . 1 1 24 24 LEU H H 1 8.812 . . . . . . . 30 LEU H . 6522 1 56 . 1 1 24 24 LEU CA C 13 53.01972 . . . . . . . 30 LEU CA . 6522 1 57 . 1 1 24 24 LEU N N 15 128.06 . . . . . . . 30 LEU N . 6522 1 58 . 1 1 25 25 GLN H H 1 8.502 . . . . . . . 31 GLN H . 6522 1 59 . 1 1 25 25 GLN CA C 13 54.6095 . . . . . . . 31 GLN CA . 6522 1 60 . 1 1 25 25 GLN N N 15 125.88 . . . . . . . 31 GLN N . 6522 1 61 . 1 1 26 26 ILE H H 1 9.29 . . . . . . . 32 ILE H . 6522 1 62 . 1 1 26 26 ILE CA C 13 59.0805 . . . . . . . 32 ILE CA . 6522 1 63 . 1 1 26 26 ILE N N 15 127.644 . . . . . . . 32 ILE N . 6522 1 64 . 1 1 27 27 ARG H H 1 9.513 . . . . . . . 33 ARG H . 6522 1 65 . 1 1 27 27 ARG CA C 13 55.81449 . . . . . . . 33 ARG CA . 6522 1 66 . 1 1 27 27 ARG N N 15 130.477 . . . . . . . 33 ARG N . 6522 1 67 . 1 1 28 28 GLY H H 1 8.842 . . . . . . . 34 GLY H . 6522 1 68 . 1 1 28 28 GLY CA C 13 44.61617 . . . . . . . 34 GLY CA . 6522 1 69 . 1 1 28 28 GLY N N 15 118.23 . . . . . . . 34 GLY N . 6522 1 70 . 1 1 29 29 ARG H H 1 8.627 . . . . . . . 35 ARG H . 6522 1 71 . 1 1 29 29 ARG CA C 13 58.61677 . . . . . . . 35 ARG CA . 6522 1 72 . 1 1 29 29 ARG N N 15 125.516 . . . . . . . 35 ARG N . 6522 1 73 . 1 1 30 30 GLU H H 1 8.702 . . . . . . . 36 GLU H . 6522 1 74 . 1 1 30 30 GLU CA C 13 60.10957 . . . . . . . 36 GLU CA . 6522 1 75 . 1 1 30 30 GLU N N 15 120.007 . . . . . . . 36 GLU N . 6522 1 76 . 1 1 31 31 ARG H H 1 8.918 . . . . . . . 37 ARG H . 6522 1 77 . 1 1 31 31 ARG CA C 13 55.90561 . . . . . . . 37 ARG CA . 6522 1 78 . 1 1 31 31 ARG N N 15 118.612 . . . . . . . 37 ARG N . 6522 1 79 . 1 1 32 32 PHE H H 1 8.058 . . . . . . . 38 PHE H . 6522 1 80 . 1 1 32 32 PHE CA C 13 61.6898 . . . . . . . 38 PHE CA . 6522 1 81 . 1 1 32 32 PHE N N 15 122.598 . . . . . . . 38 PHE N . 6522 1 82 . 1 1 33 33 GLU H H 1 8.47 . . . . . . . 39 GLU H . 6522 1 83 . 1 1 33 33 GLU CA C 13 58.7117 . . . . . . . 39 GLU CA . 6522 1 84 . 1 1 33 33 GLU N N 15 118.893 . . . . . . . 39 GLU N . 6522 1 85 . 1 1 34 34 MET H H 1 7.246 . . . . . . . 40 MET H . 6522 1 86 . 1 1 34 34 MET CA C 13 58.66151 . . . . . . . 40 MET CA . 6522 1 87 . 1 1 34 34 MET N N 15 121.086 . . . . . . . 40 MET N . 6522 1 88 . 1 1 35 35 PHE H H 1 7.822 . . . . . . . 41 PHE H . 6522 1 89 . 1 1 35 35 PHE CA C 13 60.47758 . . . . . . . 41 PHE CA . 6522 1 90 . 1 1 35 35 PHE N N 15 118.118 . . . . . . . 41 PHE N . 6522 1 91 . 1 1 36 36 ARG H H 1 8.938 . . . . . . . 42 ARG H . 6522 1 92 . 1 1 36 36 ARG CA C 13 59.54486 . . . . . . . 42 ARG CA . 6522 1 93 . 1 1 36 36 ARG N N 15 122.555 . . . . . . . 42 ARG N . 6522 1 94 . 1 1 37 37 GLU H H 1 7.438 . . . . . . . 43 GLU H . 6522 1 95 . 1 1 37 37 GLU CA C 13 59.17438 . . . . . . . 43 GLU CA . 6522 1 96 . 1 1 37 37 GLU N N 15 121.298 . . . . . . . 43 GLU N . 6522 1 97 . 1 1 38 38 LEU H H 1 7.699 . . . . . . . 44 LEU H . 6522 1 98 . 1 1 38 38 LEU CA C 13 57.68349 . . . . . . . 44 LEU CA . 6522 1 99 . 1 1 38 38 LEU N N 15 118.892 . . . . . . . 44 LEU N . 6522 1 100 . 1 1 39 39 ASN H H 1 8.78 . . . . . . . 45 ASN H . 6522 1 101 . 1 1 39 39 ASN CA C 13 56.933 . . . . . . . 45 ASN CA . 6522 1 102 . 1 1 39 39 ASN N N 15 119.109 . . . . . . . 45 ASN N . 6522 1 103 . 1 1 40 40 GLU H H 1 8.259 . . . . . . . 46 GLU H . 6522 1 104 . 1 1 40 40 GLU CA C 13 58.99051 . . . . . . . 46 GLU CA . 6522 1 105 . 1 1 40 40 GLU N N 15 119.582 . . . . . . . 46 GLU N . 6522 1 106 . 1 1 41 41 ALA H H 1 7.946 . . . . . . . 47 ALA H . 6522 1 107 . 1 1 41 41 ALA CA C 13 54.97206 . . . . . . . 47 ALA CA . 6522 1 108 . 1 1 41 41 ALA N N 15 122.503 . . . . . . . 47 ALA N . 6522 1 109 . 1 1 42 42 LEU H H 1 8.192 . . . . . . . 48 LEU H . 6522 1 110 . 1 1 42 42 LEU CA C 13 57.63275 . . . . . . . 48 LEU CA . 6522 1 111 . 1 1 42 42 LEU N N 15 120.827 . . . . . . . 48 LEU N . 6522 1 112 . 1 1 43 43 GLU H H 1 8.209 . . . . . . . 49 GLU H . 6522 1 113 . 1 1 43 43 GLU CA C 13 59.48402 . . . . . . . 49 GLU CA . 6522 1 114 . 1 1 43 43 GLU N N 15 119.756 . . . . . . . 49 GLU N . 6522 1 115 . 1 1 44 44 LEU CA C 13 57.43578 . . . . . . . 50 LEU H . 6522 1 116 . 1 1 45 45 LYS H H 1 7.986 . . . . . . . 51 LYS H . 6522 1 117 . 1 1 45 45 LYS CA C 13 59.17493 . . . . . . . 51 LYS CA . 6522 1 118 . 1 1 45 45 LYS N N 15 122.187 . . . . . . . 51 LYS N . 6522 1 119 . 1 1 46 46 ASP H H 1 8.309 . . . . . . . 52 ASP H . 6522 1 120 . 1 1 46 46 ASP CA C 13 56.46623 . . . . . . . 52 ASP CA . 6522 1 121 . 1 1 46 46 ASP N N 15 121.246 . . . . . . . 52 ASP N . 6522 1 122 . 1 1 47 47 ALA H H 1 7.749 . . . . . . . 53 ALA H . 6522 1 123 . 1 1 47 47 ALA CA C 13 53.60693 . . . . . . . 53 ALA CA . 6522 1 124 . 1 1 47 47 ALA N N 15 123.27 . . . . . . . 53 ALA N . 6522 1 125 . 1 1 48 48 GLN H H 1 7.725 . . . . . . . 54 GLN H . 6522 1 126 . 1 1 48 48 GLN CA C 13 56.23407 . . . . . . . 54 GLN CA . 6522 1 127 . 1 1 48 48 GLN N N 15 118.02 . . . . . . . 54 GLN N . 6522 1 128 . 1 1 49 49 ALA H H 1 7.69 . . . . . . . 55 ALA H . 6522 1 129 . 1 1 49 49 ALA CA C 13 52.82521 . . . . . . . 55 ALA CA . 6522 1 130 . 1 1 49 49 ALA N N 15 123.99 . . . . . . . 55 ALA N . 6522 1 131 . 1 1 50 50 GLY H H 1 8.061 . . . . . . . 56 GLY H . 6522 1 132 . 1 1 50 50 GLY CA C 13 45.08553 . . . . . . . 56 GLY CA . 6522 1 133 . 1 1 50 50 GLY N N 15 108.675 . . . . . . . 56 GLY N . 6522 1 134 . 1 1 51 51 LYS H H 1 7.772 . . . . . . . 57 LYS H . 6522 1 135 . 1 1 51 51 LYS CA C 13 55.54168 . . . . . . . 57 LYS CA . 6522 1 136 . 1 1 51 51 LYS N N 15 121.654 . . . . . . . 57 LYS N . 6522 1 137 . 1 1 52 52 GLU H H 1 8.325 . . . . . . . 58 GLU H . 6522 1 138 . 1 1 52 52 GLU CA C 13 54.04124 . . . . . . . 58 GLU CA . 6522 1 139 . 1 1 52 52 GLU N N 15 125.135 . . . . . . . 58 GLU N . 6522 1 140 . 1 1 53 53 PRO CA C 13 62.90543 . . . . . . . 59 PRO H . 6522 1 141 . 1 1 54 54 GLY H H 1 8.025 . . . . . . . 60 GLY H . 6522 1 142 . 1 1 54 54 GLY CA C 13 46.0188 . . . . . . . 60 GLY CA . 6522 1 143 . 1 1 54 54 GLY N N 15 118.225 . . . . . . . 60 GLY N . 6522 1 stop_ save_ save_chem_shift_list_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_list_2 _Assigned_chem_shift_list.Entry_ID 6522 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $conditions_2 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_referencing _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 'Chemical shift assignments for p53tet-R337H at pH 4.0' _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 1H15N_HSQC . . isotropic 6522 2 2 HNCA . . isotropic 6522 2 3 HN(CO)CA . . isotropic 6522 2 4 HNCACB . . isotropic 6522 2 5 CBCA(CO)NH . . isotropic 6522 2 6 1H15N_NOESY . . isotropic 6522 2 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $software_1 . . 6522 2 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 GLY CA C 13 43.32244 . . . . . . . 6 GLY CA . 6522 2 2 . 1 1 2 2 SER H H 1 8.494 . . . . . . . 7 SER H . 6522 2 3 . 1 1 2 2 SER CA C 13 58.2537 . . . . . . . 7 SER CA . 6522 2 4 . 1 1 2 2 SER N N 15 116.78 . . . . . . . 7 SER N . 6522 2 5 . 1 1 3 3 HIS H H 1 8.56 . . . . . . . 8 HIS H . 6522 2 6 . 1 1 3 3 HIS CA C 13 55.34199 . . . . . . . 8 HIS CA . 6522 2 7 . 1 1 3 3 HIS N N 15 121.816 . . . . . . . 8 HIS N . 6522 2 8 . 1 1 4 4 MET H H 1 8.305 . . . . . . . 9 MET H . 6522 2 9 . 1 1 4 4 MET CA C 13 55.45112 . . . . . . . 9 MET CA . 6522 2 10 . 1 1 4 4 MET N N 15 123.232 . . . . . . . 9 MET N . 6522 2 11 . 1 1 5 5 ASN H H 1 8.481 . . . . . . . 10 ASN H . 6522 2 12 . 1 1 5 5 ASN CA C 13 53.21523 . . . . . . . 10 ASN CA . 6522 2 13 . 1 1 5 5 ASN N N 15 122.078 . . . . . . . 10 ASN N . 6522 2 14 . 1 1 6 6 THR H H 1 8.065 . . . . . . . 12 THR H . 6522 2 15 . 1 1 6 6 THR CA C 13 61.70045 . . . . . . . 12 THR CA . 6522 2 16 . 1 1 6 6 THR N N 15 115.85 . . . . . . . 12 THR N . 6522 2 17 . 1 1 7 7 SER H H 1 8.195 . . . . . . . 13 SER H . 6522 2 18 . 1 1 7 7 SER CA C 13 58.44032 . . . . . . . 13 SER CA . 6522 2 19 . 1 1 7 7 SER N N 15 119.041 . . . . . . . 13 SER N . 6522 2 20 . 1 1 8 8 SER H H 1 8.156 . . . . . . . 14 SER H . 6522 2 21 . 1 1 8 8 SER CA C 13 58.24934 . . . . . . . 14 SER CA . 6522 2 22 . 1 1 8 8 SER N N 15 119.129 . . . . . . . 14 SER N . 6522 2 23 . 1 1 9 9 SER H H 1 8.131 . . . . . . . 15 SER H . 6522 2 24 . 1 1 9 9 SER CA C 13 56.57248 . . . . . . . 15 SER CA . 6522 2 25 . 1 1 9 9 SER N N 15 120.24 . . . . . . . 15 SER N . 6522 2 26 . 1 1 10 10 PRO CA C 13 63.4758 . . . . . . . 16 PRO CA . 6522 2 27 . 1 1 11 11 GLN H H 1 7.934 . . . . . . . 17 GLN H . 6522 2 28 . 1 1 11 11 GLN CA C 13 52.89492 . . . . . . . 17 GLN CA . 6522 2 29 . 1 1 11 11 GLN N N 15 120.543 . . . . . . . 17 GLN N . 6522 2 30 . 1 1 12 12 PRO CA C 13 62.91949 . . . . . . . 18 PRO CA . 6522 2 31 . 1 1 13 13 LYS H H 1 8.273 . . . . . . . 19 LYS H . 6522 2 32 . 1 1 13 13 LYS CA C 13 56.20251 . . . . . . . 19 LYS CA . 6522 2 33 . 1 1 13 13 LYS N N 15 123.285 . . . . . . . 19 LYS N . 6522 2 34 . 1 1 14 14 LYS H H 1 8.169 . . . . . . . 20 LYS H . 6522 2 35 . 1 1 14 14 LYS CA C 13 56.01453 . . . . . . . 20 LYS CA . 6522 2 36 . 1 1 14 14 LYS N N 15 124.404 . . . . . . . 20 LYS N . 6522 2 37 . 1 1 15 15 LYS H H 1 8.273 . . . . . . . 21 LYS H . 6522 2 38 . 1 1 15 15 LYS CA C 13 54.33304 . . . . . . . 21 LYS CA . 6522 2 39 . 1 1 15 15 LYS N N 15 126.183 . . . . . . . 21 LYS N . 6522 2 40 . 1 1 16 16 PRO CA C 13 63.10583 . . . . . . . 22 PRO CA . 6522 2 41 . 1 1 17 17 LEU H H 1 8.207 . . . . . . . 23 LEU H . 6522 2 42 . 1 1 17 17 LEU CA C 13 55.26614 . . . . . . . 23 LEU CA . 6522 2 43 . 1 1 17 17 LEU N N 15 123.499 . . . . . . . 23 LEU N . 6522 2 44 . 1 1 18 18 ASP H H 1 8.176 . . . . . . . 24 ASP H . 6522 2 45 . 1 1 18 18 ASP CA C 13 54.14478 . . . . . . . 24 ASP CA . 6522 2 46 . 1 1 18 18 ASP N N 15 122.243 . . . . . . . 24 ASP N . 6522 2 47 . 1 1 19 19 GLY H H 1 8.091 . . . . . . . 25 GLY H . 6522 2 48 . 1 1 19 19 GLY CA C 13 45.09724 . . . . . . . 25 GLY CA . 6522 2 49 . 1 1 19 19 GLY N N 15 110.445 . . . . . . . 25 GLY N . 6522 2 50 . 1 1 20 20 GLU H H 1 7.791 . . . . . . . 26 GLU H . 6522 2 51 . 1 1 20 20 GLU CA C 13 55.82436 . . . . . . . 26 GLU CA . 6522 2 52 . 1 1 20 20 GLU N N 15 121.368 . . . . . . . 26 GLU N . 6522 2 53 . 1 1 21 21 TYR H H 1 7.87 . . . . . . . 27 TYR H . 6522 2 54 . 1 1 21 21 TYR CA C 13 57.40764 . . . . . . . 27 TYR CA . 6522 2 55 . 1 1 21 21 TYR N N 15 121.173 . . . . . . . 27 TYR N . 6522 2 56 . 1 1 22 22 PHE H H 1 8.997 . . . . . . . 28 PHE H . 6522 2 57 . 1 1 22 22 PHE CA C 13 56.57576 . . . . . . . 28 PHE CA . 6522 2 58 . 1 1 22 22 PHE N N 15 122.563 . . . . . . . 28 PHE N . 6522 2 59 . 1 1 23 23 THR H H 1 8.329 . . . . . . . 29 THR H . 6522 2 60 . 1 1 23 23 THR CA C 13 61.60469 . . . . . . . 29 THR CA . 6522 2 61 . 1 1 23 23 THR N N 15 116.528 . . . . . . . 29 THR N . 6522 2 62 . 1 1 24 24 LEU H H 1 8.792 . . . . . . . 30 LEU H . 6522 2 63 . 1 1 24 24 LEU CA C 13 53.39939 . . . . . . . 30 LEU CA . 6522 2 64 . 1 1 24 24 LEU N N 15 127.918 . . . . . . . 30 LEU N . 6522 2 65 . 1 1 25 25 GLN H H 1 8.482 . . . . . . . 31 GLN H . 6522 2 66 . 1 1 25 25 GLN CA C 13 55.07897 . . . . . . . 31 GLN CA . 6522 2 67 . 1 1 25 25 GLN N N 15 126.063 . . . . . . . 31 GLN N . 6522 2 68 . 1 1 26 26 ILE H H 1 9.262 . . . . . . . 32 ILE H . 6522 2 69 . 1 1 26 26 ILE CA C 13 59.37342 . . . . . . . 32 ILE CA . 6522 2 70 . 1 1 26 26 ILE N N 15 127.659 . . . . . . . 32 ILE N . 6522 2 71 . 1 1 27 27 ARG H H 1 9.192 . . . . . . . 33 ARG H . 6522 2 72 . 1 1 27 27 ARG CA C 13 56.0099 . . . . . . . 33 ARG CA . 6522 2 73 . 1 1 27 27 ARG N N 15 130.085 . . . . . . . 33 ARG N . 6522 2 74 . 1 1 28 28 GLY H H 1 8.826 . . . . . . . 34 GLY H . 6522 2 75 . 1 1 28 28 GLY CA C 13 45.00147 . . . . . . . 34 GLY CA . 6522 2 76 . 1 1 28 28 GLY N N 15 117.952 . . . . . . . 34 GLY N . 6522 2 77 . 1 1 29 29 ARG H H 1 8.632 . . . . . . . 35 ARG H . 6522 2 78 . 1 1 29 29 ARG CA C 13 59.36088 . . . . . . . 35 ARG CA . 6522 2 79 . 1 1 29 29 ARG N N 15 126.461 . . . . . . . 35 ARG N . 6522 2 80 . 1 1 30 30 GLU H H 1 8.598 . . . . . . . 36 GLU H . 6522 2 81 . 1 1 30 30 GLU CA C 13 60.121 . . . . . . . 36 GLU CA . 6522 2 82 . 1 1 30 30 GLU N N 15 120.186 . . . . . . . 36 GLU N . 6522 2 83 . 1 1 31 31 ARG H H 1 8.687 . . . . . . . 37 ARG H . 6522 2 84 . 1 1 31 31 ARG CA C 13 56.56675 . . . . . . . 37 ARG CA . 6522 2 85 . 1 1 31 31 ARG N N 15 118.556 . . . . . . . 37 ARG N . 6522 2 86 . 1 1 32 32 PHE H H 1 8.092 . . . . . . . 38 PHE H . 6522 2 87 . 1 1 32 32 PHE CA C 13 61.79622 . . . . . . . 38 PHE CA . 6522 2 88 . 1 1 32 32 PHE N N 15 122.301 . . . . . . . 38 PHE N . 6522 2 89 . 1 1 33 33 GLU H H 1 8.409 . . . . . . . 39 GLU H . 6522 2 90 . 1 1 33 33 GLU CA C 13 58.99855 . . . . . . . 39 GLU CA . 6522 2 91 . 1 1 33 33 GLU N N 15 118.863 . . . . . . . 39 GLU N . 6522 2 92 . 1 1 34 34 MET H H 1 7.316 . . . . . . . 40 MET H . 6522 2 93 . 1 1 34 34 MET CA C 13 58.99964 . . . . . . . 40 MET CA . 6522 2 94 . 1 1 34 34 MET N N 15 120.733 . . . . . . . 40 MET N . 6522 2 95 . 1 1 35 35 PHE H H 1 7.885 . . . . . . . 41 PHE H . 6522 2 96 . 1 1 35 35 PHE CA C 13 61.05301 . . . . . . . 41 PHE CA . 6522 2 97 . 1 1 35 35 PHE N N 15 118.263 . . . . . . . 41 PHE N . 6522 2 98 . 1 1 36 36 ARG H H 1 8.855 . . . . . . . 42 ARG H . 6522 2 99 . 1 1 36 36 ARG CA C 13 60.02578 . . . . . . . 42 ARG CA . 6522 2 100 . 1 1 36 36 ARG N N 15 122.603 . . . . . . . 42 ARG N . 6522 2 101 . 1 1 37 37 GLU H H 1 7.497 . . . . . . . 43 GLU H . 6522 2 102 . 1 1 37 37 GLU CA C 13 59.36633 . . . . . . . 43 GLU CA . 6522 2 103 . 1 1 37 37 GLU N N 15 120.826 . . . . . . . 43 GLU N . 6522 2 104 . 1 1 38 38 LEU H H 1 7.79 . . . . . . . 44 LEU H . 6522 2 105 . 1 1 38 38 LEU CA C 13 58.0649 . . . . . . . 44 LEU CA . 6522 2 106 . 1 1 38 38 LEU N N 15 119.342 . . . . . . . 44 LEU N . 6522 2 107 . 1 1 39 39 ASN H H 1 8.765 . . . . . . . 45 ASN H . 6522 2 108 . 1 1 39 39 ASN CA C 13 57.31487 . . . . . . . 45 ASN CA . 6522 2 109 . 1 1 39 39 ASN N N 15 119.31 . . . . . . . 45 ASN N . 6522 2 110 . 1 1 40 40 GLU H H 1 8.234 . . . . . . . 46 GLU H . 6522 2 111 . 1 1 40 40 GLU CA C 13 59.09022 . . . . . . . 46 GLU CA . 6522 2 112 . 1 1 40 40 GLU N N 15 119.019 . . . . . . . 46 GLU N . 6522 2 113 . 1 1 41 41 ALA H H 1 7.882 . . . . . . . 47 ALA H . 6522 2 114 . 1 1 41 41 ALA CA C 13 55.35836 . . . . . . . 47 ALA CA . 6522 2 115 . 1 1 41 41 ALA N N 15 122.631 . . . . . . . 47 ALA N . 6522 2 116 . 1 1 42 42 LEU H H 1 8.195 . . . . . . . 48 LEU H . 6522 2 117 . 1 1 42 42 LEU CA C 13 58.44169 . . . . . . . 48 LEU CA . 6522 2 118 . 1 1 42 42 LEU N N 15 120.666 . . . . . . . 48 LEU N . 6522 2 119 . 1 1 43 43 GLU H H 1 8.156 . . . . . . . 49 GLU H . 6522 2 120 . 1 1 43 43 GLU CA C 13 59.55786 . . . . . . . 49 GLU CA . 6522 2 121 . 1 1 43 43 GLU N N 15 119.402 . . . . . . . 49 GLU N . 6522 2 122 . 1 1 44 44 LEU H H 1 7.655 . . . . . . . 50 LEU H . 6522 2 123 . 1 1 44 44 LEU CA C 13 57.87473 . . . . . . . 50 LEU CA . 6522 2 124 . 1 1 44 44 LEU N N 15 122.912 . . . . . . . 50 LEU N . 6522 2 125 . 1 1 45 45 LYS H H 1 7.959 . . . . . . . 51 LYS H . 6522 2 126 . 1 1 45 45 LYS CA C 13 59.3707 . . . . . . . 51 LYS CA . 6522 2 127 . 1 1 45 45 LYS N N 15 122.036 . . . . . . . 51 LYS N . 6522 2 128 . 1 1 46 46 ASP H H 1 8.339 . . . . . . . 52 ASP H . 6522 2 129 . 1 1 46 46 ASP CA C 13 56.57412 . . . . . . . 52 ASP CA . 6522 2 130 . 1 1 46 46 ASP N N 15 120.768 . . . . . . . 52 ASP N . 6522 2 131 . 1 1 47 47 ALA H H 1 7.723 . . . . . . . 53 ALA H . 6522 2 132 . 1 1 47 47 ALA CA C 13 53.95816 . . . . . . . 53 ALA CA . 6522 2 133 . 1 1 47 47 ALA N N 15 123.535 . . . . . . . 53 ALA N . 6522 2 134 . 1 1 48 48 GLN H H 1 7.758 . . . . . . . 54 GLN H . 6522 2 135 . 1 1 48 48 GLN CA C 13 56.75992 . . . . . . . 54 GLN CA . 6522 2 136 . 1 1 48 48 GLN N N 15 118.46 . . . . . . . 54 GLN N . 6522 2 137 . 1 1 49 49 ALA H H 1 7.737 . . . . . . . 55 ALA H . 6522 2 138 . 1 1 49 49 ALA CA C 13 53.21605 . . . . . . . 55 ALA CA . 6522 2 139 . 1 1 49 49 ALA N N 15 123.947 . . . . . . . 55 ALA N . 6522 2 140 . 1 1 50 50 GLY H H 1 8.026 . . . . . . . 56 GLY H . 6522 2 141 . 1 1 50 50 GLY CA C 13 45.5627 . . . . . . . 56 GLY CA . 6522 2 142 . 1 1 50 50 GLY N N 15 108.689 . . . . . . . 56 GLY N . 6522 2 143 . 1 1 51 51 LYS H H 1 7.804 . . . . . . . 57 LYS H . 6522 2 144 . 1 1 51 51 LYS CA C 13 55.82791 . . . . . . . 57 LYS CA . 6522 2 145 . 1 1 51 51 LYS N N 15 121.477 . . . . . . . 57 LYS N . 6522 2 146 . 1 1 52 52 GLU H H 1 8.245 . . . . . . . 58 GLU H . 6522 2 147 . 1 1 52 52 GLU CA C 13 53.96034 . . . . . . . 58 GLU CA . 6522 2 148 . 1 1 52 52 GLU N N 15 124.209 . . . . . . . 58 GLU N . 6522 2 149 . 1 1 53 53 PRO CA C 13 63.28536 . . . . . . . 59 PRO CA . 6522 2 150 . 1 1 54 54 GLY H H 1 8.039 . . . . . . . 60 GLY H . 6522 2 151 . 1 1 54 54 GLY CA C 13 46.12011 . . . . . . . 60 GLY CA . 6522 2 152 . 1 1 54 54 GLY N N 15 116.673 . . . . . . . 60 GLY N . 6522 2 stop_ save_