data_5574 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Lipid induced conformation of the tachykinin peptide Kassinin ; _BMRB_accession_number 5574 _BMRB_flat_file_name bmr5574.str _Entry_type original _Submission_date 2002-11-05 _Accession_date 2002-11-06 _Entry_origination author _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 Grace R. C. . 2 Lynn A. M. . 3 Cowsik S. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 57 "coupling constants" 8 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-27 original author . stop_ _Original_release_date 2002-12-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Lipid induced conformation of the tachykinin peptide Kassinin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11245256 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Grace R. C. . 2 Lynn A. M. . 3 Cowsik S. M. . stop_ _Journal_abbreviation 'J. Biomol. Struct. Dyn.' _Journal_volume 18 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 611 _Page_last 625 _Year 2001 _Details ; Journal of Biomolecular Structure and dynamics, Vol 18,Issue number 4(2001),611-625. ; loop_ _Keyword '3-10 helix' 'DPC micelles' 'helical core' 'lipid induced conformation' stop_ save_ ################################## # Molecular system description # ################################## save_system_KASS _Saveframe_category molecular_system _Mol_system_name KASSININ _Abbreviation_common KASS _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Kassinin $Kassinin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Stimulator of extra-vascular smooth muscle' Vasodialator stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Kassinin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Kassinin _Abbreviation_common KASS _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence DVPKSDQFVGLM loop_ _Residue_seq_code _Residue_label 1 ASP 2 VAL 3 PRO 4 LYS 5 SER 6 ASP 7 GLN 8 PHE 9 VAL 10 GLY 11 LEU 12 MET stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2002-12-29 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Kassinin 'Senegal running frog' 8415 Eukaryota Metazoa Kassina senegalensis 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 $Kassinin 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Kassinin 1.25 mg/mL . H2O 90 % . D2O 10 % . DPC 96 mM [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 95.0 loop_ _Task processing stop_ _Details MSI save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Guntert, P., and K. Wurthrich' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 5.0 0.2 n/a pressure 1 . atm temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 'methyl protons' ppm 0.00 internal direct . internal . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Kassinin _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 HA H 4.31 . 1 2 . 1 ASP HB2 H 2.83 . 1 3 . 1 ASP HB3 H 2.73 . 1 4 . 2 VAL H H 8.61 . 1 5 . 2 VAL HA H 4.41 . 1 6 . 2 VAL HB H 2.06 . 1 7 . 2 VAL HG1 H 0.98 . 1 8 . 2 VAL HG2 H 0.92 . 1 9 . 3 PRO HA H 4.39 . 1 10 . 3 PRO HB2 H 2.30 . 1 11 . 3 PRO HB3 H 1.98 . 1 12 . 3 PRO HG2 H 1.86 . 1 13 . 3 PRO HD2 H 3.85 . 1 14 . 3 PRO HD3 H 3.62 . 1 15 . 4 LYS H H 8.50 . 1 16 . 4 LYS HA H 4.22 . 1 17 . 4 LYS HB2 H 1.78 . 2 18 . 4 LYS HG2 H 1.47 . 2 19 . 4 LYS HD2 H 1.66 . 2 20 . 4 LYS HE2 H 2.97 . 2 21 . 4 LYS HZ H 7.59 . 1 22 . 5 SER H H 8.38 . 1 23 . 5 SER HA H 4.26 . 1 24 . 5 SER HB2 H 3.85 . 1 25 . 5 SER HB3 H 3.81 . 1 26 . 6 ASP H H 8.29 . 1 27 . 6 ASP HA H 4.60 . 1 28 . 6 ASP HB2 H 2.82 . 1 29 . 7 GLN H H 8.17 . 1 30 . 7 GLN HA H 4.14 . 1 31 . 7 GLN HB2 H 1.90 . 2 32 . 7 GLN HG2 H 2.16 . 2 33 . 7 GLN HE21 H 7.39 . 1 34 . 7 GLN HE22 H 6.80 . 1 35 . 8 PHE H H 8.14 . 1 36 . 8 PHE HA H 4.48 . 1 37 . 8 PHE HB2 H 3.15 . 1 38 . 8 PHE HB3 H 3.04 . 1 39 . 8 PHE HE1 H 7.21 . 3 40 . 8 PHE HE2 H 7.25 . 3 41 . 9 VAL H H 7.80 . 1 42 . 9 VAL HA H 3.86 . 1 43 . 9 VAL HB H 2.07 . 1 44 . 9 VAL HG1 H 0.92 . 2 45 . 10 GLY H H 8.18 . 1 46 . 10 GLY HA2 H 3.87 . 2 47 . 11 LEU H H 7.89 . 1 48 . 11 LEU HA H 4.20 . 1 49 . 11 LEU HB2 H 1.72 . 2 50 . 11 LEU HG H 1.56 . 1 51 . 11 LEU HD1 H 0.92 . 2 52 . 12 MET H H 7.92 . 1 53 . 12 MET HA H 4.32 . 1 54 . 12 MET HB2 H 2.07 . 1 55 . 12 MET HG2 H 2.53 . 1 56 . 12 MET HG3 H 2.42 . 1 57 . 12 MET HE H 2.00 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name Kassinin _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 2 VAL H 2 VAL HA 7.5 . . . 2 3JHNHA 3 PRO H 3 PRO HA 4.5 . . . 3 3JHNHA 4 LYS H 4 LYS HA 5.3 . . . 4 3JHNHA 5 SER H 5 SER HA 5.3 . . . 5 3JHNHA 8 PHE H 8 PHE HA 5.4 . . . 6 3JHNHA 9 VAL H 9 VAL HA 5.2 . . . 7 3JHNHA 11 LEU H 11 LEU HA 5.5 . . . 8 3JHNHA 12 MET H 12 MET HA 7.5 . . . stop_ save_