data_6870 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Probing the conformation and dynamics of allatostatin neuropeptides: a structural model for functional differences. ; _BMRB_accession_number 6870 _BMRB_flat_file_name bmr6870.str _Entry_type original _Submission_date 2005-10-20 _Accession_date 2005-11-10 _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 Meyerowitz E. . . 2 Zubkov S. . . 3 Mohanty S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 46 "13C chemical shifts" 27 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-05-21 update BMRB 'update entry citation' 2008-09-19 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Probing the conformation and dynamics of allatostatin neuropeptides: a structural model for functional differences.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18191874 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banerjee Monimoy . . 2 Meyerowitz Eric . . 3 Huang Chengdong . . 4 Mohanty Smita . . stop_ _Journal_abbreviation Peptides _Journal_name_full Peptides _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 375 _Page_last 385 _Year 2008 _Details . loop_ _Keyword 'bend / loose alpha turn among residues Ser3-Phe7' stop_ save_ ################################## # Molecular system description # ################################## save_system_Dip-AST5_peptide _Saveframe_category molecular_system _Mol_system_name 'Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2)' _Abbreviation_common 'Dip-AST8: 9 residue peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2)' $Dip-AST_peptide stop_ _System_molecular_weight . _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Dip-AST_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2)' _Abbreviation_common 'Dip-AST8: 9 residue peptide' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 10 _Mol_residue_sequence GGSLYSFGLX loop_ _Residue_seq_code _Residue_label 1 GLY 2 GLY 3 SER 4 LEU 5 TYR 6 SER 7 PHE 8 GLY 9 LEU 10 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 13:59:18 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Dip-AST_peptide Cockroach 6984 Eukaryota Metazoa Diploptera punctata 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 $Dip-AST_peptide 'from a vendor' . . . . . 'Peptide obtained as 95% pure powder from Genemed 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 $Dip-AST_peptide . mM . 'SDS (sodium dodecyl sulfate)' 30 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 'CYANA 1.0.6' loop_ _Task refinement stop_ _Details 'Guntert et al.' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 97.027.12.56 loop_ _Task processing stop_ _Details 'Delaglio et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _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 pH 7 . pH temperature 303 . K 'ionic strength' 30 . mM pressure 1 . atm 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 . H 1 . ppm . . . . . . . C 13 . ppm . . . . . . 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 'Dip-AST8: 9 residue peptide (GGSLYSFGL-NH2)' _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 GLY CA C 43.391 0.000 . 2 . 1 GLY HA3 H 3.924 0.000 . 3 . 1 GLY HA2 H 3.948 0.000 . 4 . 2 GLY H H 8.462 0.000 . 5 . 2 GLY CA C 45.493 0.000 . 6 . 2 GLY HA3 H 4.075 0.000 . 7 . 2 GLY HA2 H 4.082 0.000 . 8 . 3 SER H H 8.215 0.000 . 9 . 3 SER CA C 58.866 0.000 . 10 . 3 SER HA H 4.469 0.000 . 11 . 3 SER CB C 63.933 0.000 . 12 . 3 SER HB2 H 3.884 0.000 . 13 . 3 SER HB3 H 3.884 0.000 . 14 . 4 LEU H H 8.239 0.000 . 15 . 4 LEU CA C 56.621 0.000 . 16 . 4 LEU HA H 4.201 0.000 . 17 . 4 LEU CB C 42.210 0.000 . 18 . 4 LEU HB2 H 1.617 0.000 . 19 . 4 LEU HB3 H 1.624 0.000 . 20 . 4 LEU CG C 27.225 0.000 . 21 . 4 LEU HG H 1.449 0.000 . 22 . 4 LEU CD1 C 25.082 0.000 . 23 . 4 LEU HD1 H 0.904 0.000 . 24 . 4 LEU CD2 C 24.066 0.000 . 25 . 4 LEU HD2 H 0.839 0.000 . 26 . 5 TYR H H 7.706 0.000 . 27 . 5 TYR CA C 58.391 0.000 . 28 . 5 TYR HA H 4.427 0.000 . 29 . 5 TYR CB C 39.021 0.000 . 30 . 5 TYR HB2 H 2.888 0.000 . 31 . 5 TYR HB3 H 2.889 0.000 . 32 . 5 TYR CD1 C 133.142 0.000 . 33 . 5 TYR HD1 H 6.996 0.000 . 34 . 5 TYR HE1 H 6.766 0.000 . 35 . 5 TYR HE2 H 6.767 0.000 . 36 . 5 TYR CD2 C 133.142 0.000 . 37 . 5 TYR HD2 H 6.996 0.000 . 38 . 6 SER H H 7.734 0.000 . 39 . 6 SER CA C 58.536 0.000 . 40 . 6 SER HA H 4.362 0.000 . 41 . 6 SER CB C 63.573 0.000 . 42 . 6 SER HB2 H 3.756 0.000 . 43 . 6 SER HB3 H 3.707 0.000 . 44 . 7 PHE H H 7.840 0.000 . 45 . 7 PHE CA C 58.474 0.000 . 46 . 7 PHE HA H 4.547 0.000 . 47 . 7 PHE CB C 39.564 0.000 . 48 . 7 PHE HB2 H 3.081 0.000 . 49 . 7 PHE HB3 H 3.245 0.000 . 50 . 7 PHE CD1 C 131.978 0.000 . 51 . 7 PHE HD1 H 7.293 0.000 . 52 . 7 PHE CE1 C 129.589 0.000 . 53 . 7 PHE HE1 H 7.173 0.000 . 54 . 7 PHE CE2 C 131.299 0.000 . 55 . 7 PHE HE2 H 7.173 0.000 . 56 . 7 PHE CD2 C 131.987 0.000 . 57 . 7 PHE HD2 H 7.292 0.000 . 58 . 8 GLY H H 8.076 0.000 . 59 . 8 GLY CA C 45.844 0.000 . 60 . 8 GLY HA3 H 3.898 0.000 . 61 . 8 GLY HA2 H 3.903 0.000 . 62 . 9 LEU H H 7.693 0.000 . 63 . 9 LEU CA C 55.004 0.000 . 64 . 9 LEU HA H 4.296 0.000 . 65 . 9 LEU CB C 42.820 0.000 . 66 . 9 LEU HB2 H 1.705 0.000 . 67 . 9 LEU HB3 H 1.699 0.000 . 68 . 9 LEU CG C 27.266 0.000 . 69 . 9 LEU HG H 1.560 0.000 . 70 . 9 LEU CD1 C 25.554 0.000 . 71 . 9 LEU HD1 H 0.934 0.000 . 72 . 9 LEU CD2 C 23.536 0.000 . 73 . 9 LEU HD2 H 0.892 0.000 . stop_ save_