data_15704 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ca2+-S100A1-RyRP12 ; _BMRB_accession_number 15704 _BMRB_flat_file_name bmr15704.str _Entry_type new _Submission_date 2008-04-01 _Accession_date 2008-04-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'calcium loaded S100A1 bound to a peptide from the calmodulin binding domain of RyR1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wright Nathan T. . 2 Varney Kristen M. . 3 Weber David J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 77 "15N chemical shifts" 7 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-26 update BMRB 'update entity name' 2008-11-25 update BMRB 'complete entry citation' 2008-08-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'S100A1 and calmodulin compete for the same binding site on ryanodine receptor' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18650434 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wright Nathan T. . 2 Prosser Benjanmin L. . 3 Varney Kristen M. . 4 Zimmer Danna B. . 5 Schneider Martin F. . 6 Weber David J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of Biological Chemistry' _Journal_volume . _Journal_issue 283 _Journal_ASTM 39 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 26676 _Page_last 26683 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'S100A1 bound to calmodulin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label S100A1_1 $entity_1 S100A1_2 $entity_1 calmodulin_1 $entity_2 calmodulin_2 $entity_2 'CALCIUM ION_1' $CA 'CALCIUM ION_2' $CA 'CALCIUM ION_3' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S100A1 _Molecular_mass 1492.905 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence KKAVWHKLLSKQ loop_ _Residue_seq_code _Residue_label 1 LYS 2 LYS 3 ALA 4 VAL 5 TRP 6 HIS 7 LYS 8 LEU 9 LEU 10 SER 11 LYS 12 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common calmodulin _Molecular_mass 10439.711 _Mol_thiol_state 'all free' _Details . _Residue_count 93 _Mol_residue_sequence ; GSELETAMETLINVFHAHSG KEGDKYKLSKKELKDLLQTE LSSFLDVQKDADAVDKIMKE LDENGDGEVDFQEFVVLVAA LTVACNNFFWENS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 GLU 4 LEU 5 GLU 6 THR 7 ALA 8 MET 9 GLU 10 THR 11 LEU 12 ILE 13 ASN 14 VAL 15 PHE 16 HIS 17 ALA 18 HIS 19 SER 20 GLY 21 LYS 22 GLU 23 GLY 24 ASP 25 LYS 26 TYR 27 LYS 28 LEU 29 SER 30 LYS 31 LYS 32 GLU 33 LEU 34 LYS 35 ASP 36 LEU 37 LEU 38 GLN 39 THR 40 GLU 41 LEU 42 SER 43 SER 44 PHE 45 LEU 46 ASP 47 VAL 48 GLN 49 LYS 50 ASP 51 ALA 52 ASP 53 ALA 54 VAL 55 ASP 56 LYS 57 ILE 58 MET 59 LYS 60 GLU 61 LEU 62 ASP 63 GLU 64 ASN 65 GLY 66 ASP 67 GLY 68 GLU 69 VAL 70 ASP 71 PHE 72 GLN 73 GLU 74 PHE 75 VAL 76 VAL 77 LEU 78 VAL 79 ALA 80 ALA 81 LEU 82 THR 83 VAL 84 ALA 85 CYS 86 ASN 87 ASN 88 PHE 89 PHE 90 TRP 91 GLU 92 ASN 93 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 16050 S100A1 100.00 93 100.00 100.00 1.89e-58 BMRB 4285 S100A 100.00 94 100.00 100.00 1.83e-58 BMRB 6583 S100A1 100.00 94 98.92 98.92 1.76e-57 PDB 1K2H "Three-Dimensional Solution Structure Of Apo-S100a1." 100.00 93 100.00 100.00 1.89e-58 PDB 1ZFS "Solution Structure Of S100a1 Bound To Calcium" 100.00 93 100.00 100.00 1.89e-58 PDB 2K2F "Solution Structure Of Ca2+-S100a1-Ryrp12" 100.00 93 100.00 100.00 1.89e-58 PDB 2KBM "Ca-S100a1 Interacting With Trtk12" 100.00 93 100.00 100.00 1.89e-58 GB AAB20539 "S100 alpha, partial [Rattus sp.]" 90.32 84 97.62 100.00 7.68e-51 GB AAB53657 "S100A1 protein [Rattus norvegicus]" 100.00 94 100.00 100.00 1.83e-58 GB EDM00555 "rCG62688, isoform CRA_b [Rattus norvegicus]" 100.00 94 100.00 100.00 1.83e-58 REF NP_001007637 "protein S100-A1 [Rattus norvegicus]" 100.00 94 100.00 100.00 1.83e-58 REF XP_006232665 "PREDICTED: protein S100-A1 isoform X1 [Rattus norvegicus]" 100.00 94 100.00 100.00 1.83e-58 SP P35467 "RecName: Full=Protein S100-A1; AltName: Full=S-100 protein alpha chain; AltName: Full=S-100 protein subunit alpha; AltName: Ful" 100.00 94 100.00 100.00 1.83e-58 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 18:14:40 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA N 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $entity_1 Rat 10116 Eukaryota Metazoa Rattus norvegicus 'S100A1 protein derived from Rat' $entity_2 Human 9606 Eukaryota Metazoa Homo sapiens 'peptide from the RyR1 of human' 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 $entity_1 'recombinant technology' . . . HMS(DE3) pET14b $entity_2 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'S100A1-RyRP12 solution for NMR' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CA 10-15 mM 'natural abundance' $entity_1 1-3 mM '[U-100% 13C; U-100% 15N]' $entity_2 2-6 mM 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task 'chemical shift assignment' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'equipped with cryoprobe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details 'equipped with cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_13C_ed_12C_filt_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C ed 12C filt NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 310 . K pH 7.2 . pH pressure 1 . atm 'ionic strength' 45 5 mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 TSP H 1 protons ppm 0 external direct . . . 1 TSP N 15 protons ppm 0 external indirect . . . 0.10132905 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '3D 13C ed 12C filt NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name S100A1_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 LYS HA H 4.28 0.02 1 2 1 1 LYS HB2 H 1.81 0.02 2 3 1 1 LYS HB3 H 1.81 0.02 2 4 1 1 LYS HD2 H 1.70 0.02 2 5 1 1 LYS HD3 H 1.70 0.02 2 6 1 1 LYS HE2 H 2.93 0.02 2 7 1 1 LYS HE3 H 2.93 0.02 2 8 1 1 LYS HG2 H 1.42 0.02 2 9 1 1 LYS HG3 H 1.42 0.02 2 10 2 2 LYS HA H 4.05 0.02 1 11 2 2 LYS HB2 H 1.75 0.02 2 12 2 2 LYS HB3 H 1.75 0.02 2 13 2 2 LYS HD2 H 1.63 0.02 2 14 2 2 LYS HD3 H 1.63 0.02 2 15 2 2 LYS HE2 H 2.93 0.02 2 16 2 2 LYS HE3 H 2.93 0.02 2 17 2 2 LYS HG2 H 1.30 0.02 2 18 2 2 LYS HG3 H 1.30 0.02 2 19 3 3 ALA HA H 3.96 0.02 1 20 3 3 ALA HB H 1.20 0.02 1 21 4 4 VAL H H 7.93 0.02 1 22 4 4 VAL HA H 4.04 0.02 1 23 4 4 VAL HB H 1.94 0.02 1 24 4 4 VAL HG1 H 0.84 0.02 2 25 4 4 VAL HG2 H 0.78 0.02 2 26 4 4 VAL N N 119.6 0.1 1 27 5 5 TRP HA H 4.53 0.02 1 28 5 5 TRP HB2 H 3.01 0.02 2 29 5 5 TRP HB3 H 3.01 0.02 2 30 5 5 TRP HZ2 H 7.30 0.02 1 31 5 5 TRP HZ3 H 7.30 0.02 1 32 6 6 HIS HA H 3.62 0.02 1 33 6 6 HIS HB2 H 3.12 0.02 2 34 6 6 HIS HB3 H 3.12 0.02 2 35 6 6 HIS HD2 H 7.95 0.02 1 36 6 6 HIS HE1 H 8.32 0.02 1 37 7 7 LYS H H 7.56 0.02 1 38 7 7 LYS HA H 3.87 0.02 1 39 7 7 LYS HB2 H 1.86 0.02 2 40 7 7 LYS HB3 H 1.86 0.02 2 41 7 7 LYS HD2 H 1.62 0.02 2 42 7 7 LYS HD3 H 1.62 0.02 2 43 7 7 LYS HE2 H 3.00 0.02 2 44 7 7 LYS HE3 H 3.00 0.02 2 45 7 7 LYS HG2 H 1.69 0.02 2 46 7 7 LYS HG3 H 1.69 0.02 2 47 7 7 LYS N N 122 0.1 1 48 8 8 LEU H H 7.62 0.02 1 49 8 8 LEU HA H 3.91 0.02 1 50 8 8 LEU HB2 H 1.68 0.02 2 51 8 8 LEU HB3 H 1.68 0.02 2 52 8 8 LEU HD1 H 0.75 0.02 2 53 8 8 LEU HD2 H 0.68 0.02 2 54 8 8 LEU N N 119.3 0.1 1 55 9 9 LEU H H 7.81 0.02 1 56 9 9 LEU HA H 3.86 0.02 1 57 9 9 LEU HB2 H 1.65 0.02 2 58 9 9 LEU HB3 H 1.65 0.02 2 59 9 9 LEU HD1 H 0.79 0.02 2 60 9 9 LEU HD2 H 0.76 0.02 2 61 9 9 LEU N N 120.9 0.1 1 62 10 10 SER H H 7.84 0.02 1 63 10 10 SER HA H 4.44 0.02 1 64 10 10 SER HB2 H 3.83 0.02 2 65 10 10 SER HB3 H 3.83 0.02 2 66 10 10 SER N N 116.3 0.1 1 67 11 11 LYS H H 7.60 0.02 1 68 11 11 LYS HA H 4.18 0.02 1 69 11 11 LYS HB2 H 1.81 0.02 2 70 11 11 LYS HB3 H 1.81 0.02 2 71 11 11 LYS HD2 H 1.71 0.02 2 72 11 11 LYS HD3 H 1.71 0.02 2 73 11 11 LYS HE2 H 2.99 0.02 2 74 11 11 LYS HE3 H 2.99 0.02 2 75 11 11 LYS HG2 H 1.42 0.02 2 76 11 11 LYS HG3 H 1.42 0.02 2 77 11 11 LYS N N 120.3 0.1 1 78 12 12 GLN H H 7.84 0.02 1 79 12 12 GLN HA H 4.28 0.02 1 80 12 12 GLN HB2 H 1.94 0.02 2 81 12 12 GLN HB3 H 2.09 0.02 2 82 12 12 GLN HG2 H 2.34 0.02 2 83 12 12 GLN HG3 H 2.34 0.02 2 84 12 12 GLN N N 127.3 0.1 1 stop_ save_