data_19933 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Membrane induced structure of novel human tachykinin Hemokinin-1 (hHK1) ; _BMRB_accession_number 19933 _BMRB_flat_file_name bmr19933.str _Entry_type original _Submission_date 2014-04-24 _Accession_date 2014-04-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR solution structure of Hemokinin-1 in SDS Micelles' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ganjiwale Anjali . . 2 Cowsik 'Sudha M' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 46 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-05-26 original BMRB . stop_ _Original_release_date 2015-05-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Membrane induced structure of novel human tachykinin Hemokinin-1 ; _Citation_status 'in preparation' _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 Ganjiwale Anjali . . 2 Cowsik 'Sudha M' . . stop_ _Journal_abbreviation Biopolymers _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'novel human tachykinin Hemokinin-1 (hHK1)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 2356.776 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 11 _Mol_residue_sequence ; TGKASQFFGLM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 THR 2 2 GLY 3 3 LYS 4 4 ALA 5 5 SER 6 6 GLN 7 7 PHE 8 8 PHE 9 9 GLY 10 10 LEU 11 11 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity Human 9606 Eukaryota Metazoa Homo sapiens 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 _Details $entity 'chemical synthesis' . . . . . 'Custom synthesized peptide with >99% purity' 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 $entity 4.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % [U-2H] SDS 300 mM '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'data analysis' refinement 'structure solution' stop_ _Details 'NMR structure calculation' save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task 'chemical shift calculation' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _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 pH 3.5 . pH pressure 1 . atm temperature 305 . 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 4.7 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_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '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 entity _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 THR HA H 4.15 . . 2 2 2 GLY H H 8.67 . . 3 2 2 GLY HA2 H 4.26 . . 4 2 2 GLY HA3 H 4.20 . . 5 3 3 LYS H H 8.33 . . 6 3 3 LYS HA H 4.20 . . 7 3 3 LYS HB2 H 1.92 . . 8 3 3 LYS HB3 H 1.84 . . 9 3 3 LYS HG2 H 1.75 . . 10 3 3 LYS HG3 H 1.58 . . 11 3 3 LYS HD2 H 1.50 . . 12 4 4 ALA H H 8.48 . . 13 4 4 ALA HA H 4.17 . . 14 4 4 ALA HB H 1.53 . . 15 5 5 SER H H 8.17 . . 16 5 5 SER HA H 4.29 . . 17 5 5 SER HB2 H 3.78 . . 18 5 5 SER HB3 H 3.75 . . 19 6 6 GLN H H 7.90 . . 20 6 6 GLN HA H 4.18 . . 21 6 6 GLN HB2 H 2.24 . . 22 6 6 GLN HB3 H 2.07 . . 23 6 6 GLN HE21 H 6.99 . . 24 6 6 GLN HE22 H 7.21 . . 25 7 7 PHE H H 7.99 . . 26 7 7 PHE HA H 4.36 . . 27 7 7 PHE HB2 H 3.05 . . 28 7 7 PHE HZ H 7.00 . . 29 8 8 PHE H H 8.08 . . 30 8 8 PHE HA H 4.41 . . 31 8 8 PHE HB2 H 3.37 . . 32 8 8 PHE HB3 H 3.10 . . 33 8 8 PHE HZ H 7.36 . . 34 9 9 GLY H H 8.13 . . 35 9 9 GLY HA2 H 3.98 . . 36 10 10 LEU H H 7.72 . . 37 10 10 LEU HA H 4.34 . . 38 10 10 LEU HB2 H 1.85 . . 39 10 10 LEU HB3 H 1.62 . . 40 10 10 LEU HD1 H 0.97 . . 41 11 11 MET H H 7.72 . . 42 11 11 MET HA H 4.36 . . 43 11 11 MET HB2 H 2.12 . . 44 11 11 MET HB3 H 2.05 . . 45 11 11 MET HG2 H 2.51 . . 46 11 11 MET HG3 H 2.45 . . stop_ save_