data_18354 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High-resolution solution NMR structure of the rho-conotoxin TIA. ; _BMRB_accession_number 18354 _BMRB_flat_file_name bmr18354.str _Entry_type original _Submission_date 2012-03-27 _Accession_date 2012-03-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Refined solution NMR structure of the rho-conotoxin TIA.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rosengren 'K. Johan' . . 2 Lewis Richard J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 131 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-14 update BMRB 'update entry citation' 2012-04-30 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Conopeptide -TIA defines a new allosteric site on the extracellular surface of the 1B-adrenoceptor.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23184947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ragnarsson Lotten . . 2 Wang 'Ching-I Anderson' . . 3 Andersson Asa . . 4 Fajarningsih Dewi . . 5 Monks Thea . . 6 Brust Andreas . . 7 Rosengren 'K. Johan' . . 8 Lewis Richard J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1814 _Page_last 1827 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name conotoxin_TIA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label conotoxin_TIA $conotoxin_TIA 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_conotoxin_TIA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common conotoxin_TIA _Molecular_mass 2401.951 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 19 _Mol_residue_sequence FNWRCCLIPACRRNHKKFC loop_ _Residue_seq_code _Residue_label 1 PHE 2 ASN 3 TRP 4 ARG 5 CYS 6 CYS 7 LEU 8 ILE 9 PRO 10 ALA 11 CYS 12 ARG 13 ARG 14 ASN 15 HIS 16 LYS 17 LYS 18 PHE 19 CYS 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 PDB 1IEN "Solution Structure Of Tia" 100.00 20 100.00 100.00 4.18e-04 PDB 2LR9 "High-Resolution Solution Nmr Structure Of The Rho-Conotoxin Tia" 100.00 20 100.00 100.00 4.18e-04 GB ADN79119 "rho conotoxin A-superfamily protein [Conus tulipa]" 100.00 62 100.00 100.00 2.17e-05 SP P58811 "RecName: Full=Rho-conotoxin TIA; Short=Rho-TIA; Flags: Precursor [Conus tulipa]" 100.00 58 100.00 100.00 2.32e-05 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $conotoxin_TIA 'tulip cone' 6495 Eukaryota Metazoa Conus tulipa 'This sequence occurs naturally in Conus tulipa.' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $conotoxin_TIA 'chemical synthesis' . not applicable . 'not applicable' 'not applicable' 'Peptide was made synthetically through solid phase peptide chemistry.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'lyophylized sample dissolved in distilled water.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $conotoxin_TIA 1 mg/ml 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H 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 'ionic strength' 0 . M pH 4.5 . pH pressure 1 . atm temperature 298 . K 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 water H 1 protons ppm 4.69 internal direct . . . 1.0 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D DQF-COSY' '2D 1H-1H TOCSY' '2D 1H-1H 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 conotoxin_TIA _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 PHE HA H 3.845 0.000 . 2 1 1 PHE HB2 H 2.449 0.000 . 3 1 1 PHE HB3 H 2.679 0.000 . 4 1 1 PHE HD1 H 6.434 0.000 . 5 1 1 PHE HD2 H 6.434 0.000 . 6 1 1 PHE HE1 H 6.647 0.000 . 7 1 1 PHE HE2 H 6.647 0.000 . 8 2 2 ASN H H 7.684 0.003 . 9 2 2 ASN HA H 4.529 0.000 . 10 2 2 ASN HB2 H 2.548 0.000 . 11 2 2 ASN HB3 H 2.548 0.000 . 12 2 2 ASN HD21 H 6.647 0.000 . 13 2 2 ASN HD22 H 7.444 0.000 . 14 3 3 TRP H H 8.207 0.000 . 15 3 3 TRP HA H 4.212 0.000 . 16 3 3 TRP HB2 H 3.263 0.000 . 17 3 3 TRP HB3 H 3.263 0.000 . 18 3 3 TRP HD1 H 7.337 0.003 . 19 3 3 TRP HE1 H 10.080 0.000 . 20 3 3 TRP HE3 H 7.470 0.000 . 21 3 3 TRP HZ2 H 7.367 0.006 . 22 3 3 TRP HZ3 H 7.043 0.003 . 23 3 3 TRP HH2 H 7.080 0.009 . 24 4 4 ARG H H 7.655 0.000 . 25 4 4 ARG HA H 3.621 0.001 . 26 4 4 ARG HB2 H 1.336 0.000 . 27 4 4 ARG HB3 H 1.529 0.000 . 28 4 4 ARG HG2 H 0.843 0.000 . 29 4 4 ARG HG3 H 0.887 0.000 . 30 4 4 ARG HD2 H 2.862 0.000 . 31 4 4 ARG HD3 H 2.862 0.000 . 32 4 4 ARG HE H 7.026 0.000 . 33 5 5 CYS H H 7.635 0.000 . 34 5 5 CYS HA H 4.057 0.002 . 35 5 5 CYS HB2 H 2.458 0.000 . 36 5 5 CYS HB3 H 3.059 0.000 . 37 6 6 CYS H H 7.614 0.000 . 38 6 6 CYS HA H 4.259 0.005 . 39 6 6 CYS HB2 H 2.729 0.000 . 40 6 6 CYS HB3 H 3.295 0.002 . 41 7 7 LEU H H 7.636 0.000 . 42 7 7 LEU HA H 4.284 0.000 . 43 7 7 LEU HB2 H 1.702 0.000 . 44 7 7 LEU HB3 H 1.749 0.000 . 45 7 7 LEU HG H 1.596 0.000 . 46 7 7 LEU HD1 H 0.891 0.000 . 47 7 7 LEU HD2 H 0.816 0.000 . 48 8 8 ILE H H 7.756 0.000 . 49 8 8 ILE HA H 4.510 0.000 . 50 8 8 ILE HB H 2.014 0.004 . 51 8 8 ILE HG12 H 1.021 0.000 . 52 8 8 ILE HG13 H 1.507 0.000 . 53 8 8 ILE HG2 H 0.915 0.007 . 54 8 8 ILE HD1 H 0.695 0.001 . 55 9 9 PRO HA H 3.959 0.002 . 56 9 9 PRO HB2 H 2.282 0.000 . 57 9 9 PRO HB3 H 1.926 0.000 . 58 9 9 PRO HG2 H 1.940 0.000 . 59 9 9 PRO HG3 H 2.156 0.000 . 60 9 9 PRO HD2 H 3.830 0.002 . 61 9 9 PRO HD3 H 4.051 0.000 . 62 10 10 ALA H H 8.534 0.000 . 63 10 10 ALA HA H 3.919 0.000 . 64 10 10 ALA HB H 1.276 0.000 . 65 11 11 CYS H H 7.321 0.000 . 66 11 11 CYS HA H 4.470 0.000 . 67 11 11 CYS HB2 H 3.090 0.000 . 68 11 11 CYS HB3 H 4.278 0.000 . 69 12 12 ARG H H 8.933 0.000 . 70 12 12 ARG HA H 3.851 0.007 . 71 12 12 ARG HB2 H 1.783 0.001 . 72 12 12 ARG HB3 H 1.916 0.005 . 73 12 12 ARG HG2 H 1.524 0.001 . 74 12 12 ARG HG3 H 1.524 0.001 . 75 12 12 ARG HD2 H 3.208 0.000 . 76 12 12 ARG HD3 H 3.208 0.000 . 77 12 12 ARG HE H 7.271 0.000 . 78 13 13 ARG H H 7.755 0.000 . 79 13 13 ARG HA H 3.955 0.000 . 80 13 13 ARG HB2 H 1.696 0.000 . 81 13 13 ARG HB3 H 1.831 0.000 . 82 13 13 ARG HG2 H 1.535 0.000 . 83 13 13 ARG HG3 H 1.535 0.000 . 84 13 13 ARG HD2 H 3.081 0.000 . 85 13 13 ARG HD3 H 3.081 0.000 . 86 13 13 ARG HE H 7.093 0.000 . 87 14 14 ASN H H 7.171 0.000 . 88 14 14 ASN HA H 4.766 0.007 . 89 14 14 ASN HB2 H 2.578 0.000 . 90 14 14 ASN HB3 H 2.578 0.000 . 91 14 14 ASN HD21 H 6.793 0.000 . 92 14 14 ASN HD22 H 7.443 0.000 . 93 15 15 HIS H H 7.815 0.000 . 94 15 15 HIS HA H 4.865 0.000 . 95 15 15 HIS HB2 H 2.775 0.000 . 96 15 15 HIS HB3 H 3.288 0.000 . 97 15 15 HIS HD2 H 7.244 0.000 . 98 15 15 HIS HE1 H 8.620 0.000 . 99 16 16 LYS H H 8.086 0.001 . 100 16 16 LYS HA H 3.777 0.004 . 101 16 16 LYS HB2 H 1.698 0.000 . 102 16 16 LYS HB3 H 1.698 0.000 . 103 16 16 LYS HG2 H 1.322 0.000 . 104 16 16 LYS HG3 H 1.468 0.000 . 105 16 16 LYS HD2 H 1.597 0.000 . 106 16 16 LYS HD3 H 1.597 0.000 . 107 16 16 LYS HE2 H 2.930 0.000 . 108 16 16 LYS HE3 H 2.930 0.000 . 109 17 17 LYS H H 8.377 0.000 . 110 17 17 LYS HA H 3.920 0.000 . 111 17 17 LYS HB2 H 1.557 0.000 . 112 17 17 LYS HB3 H 1.643 0.000 . 113 17 17 LYS HG2 H 1.125 0.000 . 114 17 17 LYS HG3 H 1.188 0.000 . 115 17 17 LYS HD2 H 1.486 0.000 . 116 17 17 LYS HD3 H 1.486 0.000 . 117 17 17 LYS HE2 H 2.796 0.000 . 118 17 17 LYS HE3 H 2.796 0.000 . 119 18 18 PHE H H 7.704 0.000 . 120 18 18 PHE HA H 4.268 0.000 . 121 18 18 PHE HB2 H 2.629 0.000 . 122 18 18 PHE HB3 H 2.723 0.000 . 123 18 18 PHE HD1 H 6.855 0.000 . 124 18 18 PHE HD2 H 6.855 0.000 . 125 18 18 PHE HE1 H 7.147 0.000 . 126 18 18 PHE HE2 H 7.147 0.000 . 127 18 18 PHE HZ H 7.098 0.000 . 128 19 19 CYS H H 7.833 0.000 . 129 19 19 CYS HA H 4.704 0.000 . 130 19 19 CYS HB2 H 2.625 0.003 . 131 19 19 CYS HB3 H 3.160 0.004 . stop_ save_