data_2435 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change ; _BMRB_accession_number 2435 _BMRB_flat_file_name bmr2435.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _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 Ikura Mitsuhiko . . 2 Hiraoki Toshifumi . . 3 Hikichi Kunio . . 4 Mikuni Toshiaki . . 5 Yazawa Michio . . 6 Yagi Koichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 6 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-10-03 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, "Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change," Biochemistry 22 (10), 2573-2579 (1983). ; _Citation_title 'Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change' _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 Ikura Mitsuhiko . . 2 Hiraoki Toshifumi . . 3 Hikichi Kunio . . 4 Mikuni Toshiaki . . 5 Yazawa Michio . . 6 Yagi Koichi . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 22 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2573 _Page_last 2579 _Year 1983 _Details . save_ ################################## # Molecular system description # ################################## save_system_calmodulin _Saveframe_category molecular_system _Mol_system_name calmodulin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label calmodulin $calmodulin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_calmodulin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common calmodulin _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 143 _Mol_residue_sequence ; XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXXFX XXXXXXHXXXXXXXXXXXXX XXXXXXXXXXXXXXXXXYXX XXT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 X 2 2 X 3 3 X 4 4 X 5 5 X 6 6 X 7 7 X 8 8 X 9 9 X 10 10 X 11 11 X 12 12 X 13 13 X 14 14 X 15 15 X 16 16 X 17 17 X 18 18 X 19 19 X 20 20 X 21 21 X 22 22 X 23 23 X 24 24 X 25 25 X 26 26 X 27 27 X 28 28 X 29 29 X 30 30 X 31 31 X 32 32 X 33 33 X 34 34 X 35 35 X 36 36 X 37 37 X 38 38 X 39 39 X 40 40 X 41 41 X 42 42 X 43 43 X 44 44 X 45 45 X 46 46 X 47 47 X 48 48 X 49 49 X 50 50 X 51 51 X 52 52 X 53 53 X 54 54 X 55 55 X 56 56 X 57 57 X 58 58 X 59 59 X 60 60 X 61 61 X 62 62 X 63 63 X 64 64 X 65 65 X 66 66 X 67 67 X 68 68 X 69 69 X 70 70 X 71 71 X 72 72 X 73 73 X 74 74 X 75 75 X 76 76 X 77 77 X 78 78 X 79 79 X 80 80 X 81 81 X 82 82 X 83 83 X 84 84 X 85 85 X 86 86 X 87 87 X 88 88 X 89 89 X 90 90 X 91 91 X 92 92 X 93 93 X 94 94 X 95 95 X 96 96 X 97 97 X 98 98 X 99 99 PHE 100 100 X 101 101 X 102 102 X 103 103 X 104 104 X 105 105 X 106 106 X 107 107 HIS 108 108 X 109 109 X 110 110 X 111 111 X 112 112 X 113 113 X 114 114 X 115 115 M3L 116 116 X 117 117 X 118 118 X 119 119 X 120 120 X 121 121 X 122 122 X 123 123 X 124 124 X 125 125 X 126 126 X 127 127 X 128 128 X 129 129 X 130 130 X 131 131 X 132 132 X 133 133 X 134 134 X 135 135 X 136 136 X 137 137 X 138 138 TYR 139 139 X 140 140 X 141 141 X 142 142 X 143 143 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_M3L _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-TRIMETHYLLYSINE _BMRB_code M3L _PDB_code M3L _Standard_residue_derivative . _Molecular_mass 189.275 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? NZ NZ N . 1 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CM1 CM1 C . 0 . ? CM2 CM2 C . 0 . ? CM3 CM3 C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? HXT HXT H . 0 . ? HM11 HM11 H . 0 . ? HM12 HM12 H . 0 . ? HM13 HM13 H . 0 . ? HM21 HM21 H . 0 . ? HM22 HM22 H . 0 . ? HM23 HM23 H . 0 . ? HM31 HM31 H . 0 . ? HM32 HM32 H . 0 . ? HM33 HM33 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE NZ ? ? SING CE HE2 ? ? SING CE HE3 ? ? SING NZ CM1 ? ? SING NZ CM2 ? ? SING NZ CM3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CM1 HM11 ? ? SING CM1 HM12 ? ? SING CM1 HM13 ? ? SING CM2 HM21 ? ? SING CM2 HM22 ? ? SING CM2 HM23 ? ? SING CM3 HM31 ? ? SING CM3 HM32 ? ? SING CM3 HM33 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Tissue $calmodulin scallop . . . Patinopecten yessoensis generic testis 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 $calmodulin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one 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 8.8 . na temperature 296 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H . . ppm 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_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 calmodulin _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 . 107 HIS HD2 H 6.81 . 1 2 . 107 HIS HE1 H 7.71 . 1 3 . 138 TYR HD1 H 6.73 . 1 4 . 138 TYR HD2 H 6.73 . 1 5 . 138 TYR HE1 H 6.67 . 1 6 . 138 TYR HE2 H 6.67 . 1 stop_ save_