data_290 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A 1H NMR Determination of the Solution Conformation of a Synthetic Peptide Analogue of Calcium-Binding Site III of Rabbit Skeletal Troponin C ; _BMRB_accession_number 290 _BMRB_flat_file_name bmr290.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Marsden Brian J. . 2 Hodges Robert S. . 3 Sykes Brian D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Marsden, Brian J., Hodges, Robert S., Sykes, Brian D., "A 1H NMR Determination of the Solution Conformation of a Synthetic Peptide Analogue of Calcium-Binding Site III of Rabbit Skeletal Troponin C," Biochemistry 28, 8839-8847 (1989). ; _Citation_title ; A 1H NMR Determination of the Solution Conformation of a Synthetic Peptide Analogue of Calcium-Binding Site III of Rabbit Skeletal Troponin C ; _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 Marsden Brian J. . 2 Hodges Robert S. . 3 Sykes Brian D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 28 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8839 _Page_last 8847 _Year 1989 _Details . save_ ################################## # Molecular system description # ################################## save_system_troponin_C _Saveframe_category molecular_system _Mol_system_name 'troponin C' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'troponin C' $troponin_C stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_troponin_C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'troponin C' _Name_variant 'residues 103-115, synthesized rabbit skeletal' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 13 _Mol_residue_sequence DRDADGYIDAEEL loop_ _Residue_seq_code _Residue_label 1 ASP 2 ARG 3 ASP 4 ALA 5 ASP 6 GLY 7 TYR 8 ILE 9 ASP 10 ALA 11 GLU 12 GLU 13 LEU stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 1999-12-06 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $troponin_C 'domestic rabbit' . . . Oryctolagus cuniculus generic 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 $troponin_C 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.75 . na temperature 279 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 DSS H . . ppm 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'troponin C' _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 ASP H H 8.64 . 1 2 . 1 ASP HA H 4.43 . 1 3 . 1 ASP HB2 H 2.58 . 2 4 . 1 ASP HB3 H 2.34 . 2 5 . 2 ARG H H 8.63 . 1 6 . 2 ARG HA H 4.49 . 1 7 . 2 ARG HB2 H 2.03 . 2 8 . 2 ARG HB3 H 1.83 . 2 9 . 2 ARG HG2 H 1.8 . 2 10 . 2 ARG HG3 H 1.7 . 2 11 . 2 ARG HD2 H 3.25 . 1 12 . 2 ARG HD3 H 3.25 . 1 13 . 2 ARG HE H 7.42 . 1 14 . 3 ASP H H 8.17 . 1 15 . 3 ASP HA H 4.73 . 1 16 . 3 ASP HB2 H 3.06 . 2 17 . 3 ASP HB3 H 2.55 . 2 18 . 4 ALA H H 8.23 . 1 19 . 4 ALA HA H 3.97 . 1 20 . 4 ALA HB H 1.34 . 1 21 . 5 ASP H H 8.18 . 1 22 . 5 ASP HA H 4.77 . 1 23 . 5 ASP HB2 H 3.21 . 2 24 . 5 ASP HB3 H 2.7 . 2 25 . 6 GLY H H 8.81 . 1 26 . 6 GLY HA2 H 4.03 . 2 27 . 6 GLY HA3 H 3.48 . 2 28 . 7 TYR H H 8.48 . 1 29 . 7 TYR HA H 4.79 . 1 30 . 7 TYR HB2 H 2.86 . 2 31 . 7 TYR HB3 H 2.78 . 2 32 . 7 TYR HD1 H 6.99 . 1 33 . 7 TYR HD2 H 6.99 . 1 34 . 7 TYR HE1 H 6.8 . 1 35 . 7 TYR HE2 H 6.8 . 1 36 . 8 ILE H H 9.3 . 1 37 . 8 ILE HA H 4.21 . 1 38 . 8 ILE HB H 1.81 . 1 39 . 8 ILE HG12 H 1.41 . 2 40 . 8 ILE HG13 H .9 . 2 41 . 8 ILE HG2 H .78 . 1 42 . 8 ILE HD1 H .87 . 1 43 . 9 ASP H H 9.3 . 1 44 . 9 ASP HB2 H 2.79 . 2 45 . 9 ASP HB3 H 2.66 . 2 46 . 10 ALA H H 8.83 . 1 47 . 10 ALA HA H 4.05 . 1 48 . 10 ALA HB H 1.47 . 1 49 . 11 GLU H H 8.95 . 1 50 . 11 GLU HA H 4.23 . 1 51 . 12 GLU H H 8.04 . 1 52 . 12 GLU HA H 4.25 . 1 53 . 12 GLU HB2 H 2.3 . 2 54 . 12 GLU HB3 H 2.06 . 2 55 . 13 LEU H H 7.68 . 1 56 . 13 LEU HA H 4.19 . 1 57 . 13 LEU HB2 H 1.72 . 2 58 . 13 LEU HB3 H 1.6 . 2 59 . 13 LEU HG H 1.62 . 1 60 . 13 LEU HD1 H .87 . 2 61 . 13 LEU HD2 H .83 . 2 stop_ save_