data_391 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Characterization of the Interactions between Calmodulin and Skeletal Muscle Myosin Light Chain Kinase: Effect of Peptide (576-594)G Binding on the Ca2+-Binding Domains ; _BMRB_accession_number 391 _BMRB_flat_file_name bmr391.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 Seeholzer Steven H. . 2 Wand A. Joshua . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 102 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 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 ; Seeholzer, Steven H., Wand, A. Joshua, "Structural Characterization of the Interactions between Calmodulin and Skeletal Muscle Myosin Light Chain Kinase: Effect of Peptide (576-594)G Binding on the Ca2+-Binding Domains," Biochemistry 28 (9), 4011-4020 (1989). ; _Citation_title ; Structural Characterization of the Interactions between Calmodulin and Skeletal Muscle Myosin Light Chain Kinase: Effect of Peptide (576-594)G Binding on the Ca2+-Binding Domains ; _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 Seeholzer Steven H. . 2 Wand A. Joshua . stop_ _Journal_abbreviation Biochemistry _Journal_volume 28 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4011 _Page_last 4020 _Year 1989 _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 . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; XXXXXXXXXXXXXXXXXXXX XXGDGTITTKXXXXXXXXXX XXXXXXXXXXXXXXXXXXXN GTIDFXXXXXXXXXXXXXXX XXXXXXXXXXXXXXXGNGYI SAAXXXXXXXXXXXXXXXXX XXXXXXXXXXXGDGQVNYE ; loop_ _Residue_seq_code _Residue_label 1 X 2 X 3 X 4 X 5 X 6 X 7 X 8 X 9 X 10 X 11 X 12 X 13 X 14 X 15 X 16 X 17 X 18 X 19 X 20 X 21 X 22 X 23 GLY 24 ASP 25 GLY 26 THR 27 ILE 28 THR 29 THR 30 LYS 31 X 32 X 33 X 34 X 35 X 36 X 37 X 38 X 39 X 40 X 41 X 42 X 43 X 44 X 45 X 46 X 47 X 48 X 49 X 50 X 51 X 52 X 53 X 54 X 55 X 56 X 57 X 58 X 59 X 60 ASN 61 GLY 62 THR 63 ILE 64 ASP 65 PHE 66 X 67 X 68 X 69 X 70 X 71 X 72 X 73 X 74 X 75 X 76 X 77 X 78 X 79 X 80 X 81 X 82 X 83 X 84 X 85 X 86 X 87 X 88 X 89 X 90 X 91 X 92 X 93 X 94 X 95 X 96 GLY 97 ASN 98 GLY 99 TYR 100 ILE 101 SER 102 ALA 103 ALA 104 X 105 X 106 X 107 X 108 X 109 X 110 X 111 X 112 X 113 X 114 X 115 X 116 X 117 X 118 X 119 X 120 X 121 X 122 X 123 X 124 X 125 X 126 X 127 X 128 X 129 X 130 X 131 X 132 GLY 133 ASP 134 GLY 135 GLN 136 VAL 137 ASN 138 TYR 139 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2007-05-31 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 392 calmodulin 100.00 30 100 100 4e-10 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 cow 9909 Eukaryota Metazoa Bos primigenius 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_ ######################### # 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_ ############################# # 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 6.5 . na temperature 310 . 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 . 23 GLY H H 7.7 . 1 2 . 24 ASP H H 8.41 . 1 3 . 25 GLY H H 10.62 . 1 4 . 25 GLY HA2 H 4.39 . 2 5 . 25 GLY HA3 H 3.72 . 2 6 . 26 THR H H 8.17 . 1 7 . 26 THR HA H 5.33 . 1 8 . 26 THR HB H 3.87 . 1 9 . 26 THR HG2 H 1.07 . 1 10 . 27 ILE H H 9.8 . 1 11 . 27 ILE HA H 4.98 . 1 12 . 27 ILE HB H 1.82 . 1 13 . 28 THR H H 8.52 . 1 14 . 28 THR HA H 4.85 . 1 15 . 28 THR HB H 4.83 . 1 16 . 28 THR HG2 H 1.33 . 1 17 . 29 THR H H 9.01 . 1 18 . 29 THR HA H 4 . 1 19 . 29 THR HB H 4.12 . 1 20 . 29 THR HG2 H 1.36 . 1 21 . 30 LYS H H 8.68 . 1 22 . 60 ASN H H 8.11 . 1 23 . 60 ASN HA H 4.7 . 1 24 . 61 GLY H H 10.58 . 1 25 . 61 GLY HA2 H 3.51 . 2 26 . 61 GLY HA3 H 4.22 . 2 27 . 62 THR H H 7.7 . 1 28 . 62 THR HA H 4.79 . 1 29 . 62 THR HB H 4.03 . 1 30 . 62 THR HG2 H 1.13 . 1 31 . 63 ILE H H 8.91 . 1 32 . 63 ILE HA H 5.18 . 1 33 . 63 ILE HB H 2.09 . 1 34 . 63 ILE HG2 H 1.25 . 1 35 . 64 ASP H H 8.91 . 1 36 . 64 ASP HA H 5.4 . 1 37 . 64 ASP HB2 H 2.86 . 2 38 . 64 ASP HB3 H 3.1 . 2 39 . 65 PHE H H 8.99 . 1 40 . 65 PHE HA H 4.04 . 1 41 . 65 PHE HB2 H 2.41 . 2 42 . 65 PHE HB3 H 2.85 . 2 43 . 65 PHE HD1 H 6.64 . 1 44 . 65 PHE HD2 H 6.64 . 1 45 . 65 PHE HE1 H 7.04 . 1 46 . 65 PHE HE2 H 7.04 . 1 47 . 65 PHE HZ H 7.23 . 1 48 . 96 GLY H H 7.79 . 1 49 . 97 ASN H H 8.35 . 1 50 . 97 ASN HA H 4.67 . 1 51 . 98 GLY H H 10.64 . 1 52 . 98 GLY HA2 H 3.46 . 2 53 . 98 GLY HA3 H 4.08 . 2 54 . 99 TYR H H 7.63 . 1 55 . 99 TYR HA H 5.07 . 1 56 . 99 TYR HB2 H 2.5 . 2 57 . 99 TYR HB3 H 2.54 . 2 58 . 99 TYR HD1 H 6.78 . 1 59 . 99 TYR HD2 H 6.78 . 1 60 . 99 TYR HE1 H 6.95 . 1 61 . 99 TYR HE2 H 6.95 . 1 62 . 100 ILE H H 10.16 . 1 63 . 100 ILE HA H 4.84 . 1 64 . 100 ILE HB H 1.9 . 1 65 . 100 ILE HG2 H .98 . 1 66 . 101 SER H H 9.01 . 1 67 . 101 SER HA H 4.88 . 1 68 . 101 SER HB2 H 4.46 . 1 69 . 101 SER HB3 H 4.46 . 1 70 . 102 ALA H H 9.21 . 1 71 . 102 ALA HA H 3.95 . 1 72 . 102 ALA HB H 1.51 . 1 73 . 103 ALA H H 8.22 . 1 74 . 103 ALA HA H 4.07 . 1 75 . 103 ALA HB H 1.45 . 1 76 . 132 GLY H H 7.6 . 1 77 . 132 GLY HA2 H 4.01 . 2 78 . 132 GLY HA3 H 3.98 . 2 79 . 133 ASP H H 8.36 . 1 80 . 133 ASP HA H 4.5 . 1 81 . 134 GLY H H 10.35 . 1 82 . 134 GLY HA2 H 4.06 . 2 83 . 134 GLY HA3 H 3.45 . 2 84 . 135 GLN H H 7.98 . 1 85 . 135 GLN HA H 4.9 . 1 86 . 135 GLN HB2 H 1.72 . 1 87 . 135 GLN HB3 H 1.72 . 1 88 . 136 VAL H H 9.14 . 1 89 . 136 VAL HA H 5.22 . 1 90 . 136 VAL HB H 2.33 . 1 91 . 136 VAL HG1 H .94 . 2 92 . 136 VAL HG2 H 1.3 . 2 93 . 137 ASN H H 9.6 . 1 94 . 137 ASN HA H 5.25 . 1 95 . 137 ASN HB2 H 3.27 . 1 96 . 137 ASN HB3 H 3.27 . 1 97 . 138 TYR H H 8.43 . 1 98 . 138 TYR HA H 3.96 . 1 99 . 138 TYR HD1 H 6.32 . 1 100 . 138 TYR HD2 H 6.32 . 1 101 . 138 TYR HE1 H 6.53 . 1 102 . 138 TYR HE2 H 6.53 . 1 stop_ save_