data_4398 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of a neuropeptide Y Y2 agonist ; _BMRB_accession_number 4398 _BMRB_flat_file_name bmr4398.str _Entry_type original _Submission_date 1999-09-09 _Accession_date 1999-09-10 _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 Barnham K. J. . 2 Catalfamo F. . . 3 Pallaghy P. K. . 4 Howlett G. J. . 5 Norton R. S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 update BMRB 'Updating non-standard residue' 2001-11-27 update BMRB 'Addition of related BMRB entries.' 2000-03-08 original author 'Original release.' 2008-03-24 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5214 'Y2 selective analogue-I of neuropeptide Y' 5215 'Y2 selective analogue-II of neuropeptide Y' 5216 'Y2 selective analogue-III of neuropeptide Y' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Barnham, K. J., Catalfamo, F., Pallaghy, P. K., Howlett, G. J., and Norton, R. S., "Helical Structure and Self-association in a 13-residue Neuropeptide Y Y2 Receptor Agonist:Relationship to Biological Activity," Biochim. Biophys. Acta 1435, 127-137 (1999). ; _Citation_title ; Helical Structure and Self-association in a 13-residue Neuropeptide Y Y2 Receptor Agonist:Relationship to Biological Activity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20029622 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Barnham K. J. . 2 Catalfamo F. . . 3 Pallaghy P. K. . 4 Howlett G. J. . 5 Norton R. S. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et Biophysica Acta' _Journal_volume 1435 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 127 _Page_last 137 _Year 1999 _Details . loop_ _Keyword agonist helix 'neropeptide Y' stop_ save_ ################################## # Molecular system description # ################################## save_system_NPY _Saveframe_category molecular_system _Mol_system_name 'neuropeptide Y' _Abbreviation_common NPY _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'neuropeptide Y' $npy stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_npy _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'neuropeptide Y' _Name_variant 'I29L, I31L' _Abbreviation_common npy _Molecular_mass . _Mol_thiol_state . _Details ; Tyr 36 C-terminally amidated Leu 23 N-terminally acetylated ; ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence XLRHYLNLLTRQRYX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 ACE 2 25 LEU 3 26 ARG 4 27 HIS 5 28 TYR 6 29 LEU 7 30 ASN 8 31 LEU 9 32 LEU 10 33 THR 11 34 ARG 12 35 GLN 13 36 ARG 14 37 TYR 15 38 NH2 stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2003-06-19 save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'AMINO GROUP' _BMRB_code NH2 _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details . 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 $npy 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 $npy '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 $npy . mM . TFE-d3 40 % . H2O 60 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details ; NOESY COSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.6 0.2 n/a pressure 1 . atm temperature 293 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo . $entry_citation $entry_citation 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_Panpy.bmrb _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 'neuropeptide Y' _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 . 2 LEU H H 8.13 . 1 2 . 2 LEU HA H 4.22 . 1 3 . 2 LEU HB2 H 1.71 . 2 4 . 2 LEU HB3 H 1.65 . 2 5 . 2 LEU HD1 H 1.01 . 2 6 . 2 LEU HD2 H 0.94 . 2 7 . 3 ARG H H 8.50 . 1 8 . 3 ARG HA H 3.98 . 1 9 . 3 ARG HB2 H 1.83 . 2 10 . 3 ARG HB3 H 1.70 . 2 11 . 3 ARG HG2 H 1.66 . 1 12 . 3 ARG HG3 H 1.66 . 1 13 . 3 ARG HD2 H 3.19 . 1 14 . 3 ARG HD3 H 3.19 . 1 15 . 3 ARG HE H 7.20 . 1 16 . 3 ARG HH21 H 7.20 . 2 17 . 4 HIS H H 7.98 . 1 18 . 4 HIS HA H 4.43 . 1 19 . 4 HIS HB2 H 3.30 . 2 20 . 4 HIS HB3 H 3.28 . 2 21 . 4 HIS HD2 H 7.06 . 1 22 . 4 HIS HE1 H 8.55 . 1 23 . 5 TYR H H 7.99 . 1 24 . 5 TYR HA H 4.27 . 1 25 . 5 TYR HB2 H 3.20 . 2 26 . 5 TYR HB3 H 3.12 . 2 27 . 5 TYR HD1 H 7.07 . 1 28 . 5 TYR HD2 H 7.07 . 1 29 . 5 TYR HE1 H 6.79 . 1 30 . 5 TYR HE2 H 6.79 . 1 31 . 6 LEU H H 8.59 . 1 32 . 6 LEU HA H 4.02 . 1 33 . 6 LEU HB2 H 1.87 . 2 34 . 6 LEU HB3 H 1.50 . 2 35 . 6 LEU HD1 H 0.89 . 2 36 . 6 LEU HD2 H 0.77 . 2 37 . 7 ASN H H 8.15 . 1 38 . 7 ASN HA H 4.39 . 1 39 . 7 ASN HB2 H 3.00 . 2 40 . 7 ASN HB3 H 2.80 . 2 41 . 7 ASN HD21 H 6.76 . 2 42 . 7 ASN HD22 H 7.49 . 2 43 . 8 LEU H H 7.76 . 1 44 . 8 LEU HA H 4.05 . 1 45 . 8 LEU HB2 H 1.81 . 2 46 . 8 LEU HB3 H 1.63 . 2 47 . 8 LEU HD1 H 0.86 . 1 48 . 8 LEU HD2 H 0.86 . 1 49 . 9 LEU H H 8.32 . 1 50 . 9 LEU HA H 4.01 . 1 51 . 9 LEU HB2 H 1.67 . 2 52 . 9 LEU HB3 H 1.52 . 2 53 . 9 LEU HD1 H 0.86 . 2 54 . 9 LEU HD2 H 0.78 . 2 55 . 10 THR H H 8.02 . 1 56 . 10 THR HA H 4.39 . 1 57 . 10 THR HB H 4.02 . 1 58 . 10 THR HG2 H 1.32 . 1 59 . 11 ARG H H 7.82 . 1 60 . 11 ARG HA H 4.14 . 1 61 . 11 ARG HB2 H 1.97 . 1 62 . 11 ARG HB3 H 1.97 . 1 63 . 11 ARG HG2 H 1.79 . 2 64 . 11 ARG HG3 H 1.72 . 2 65 . 11 ARG HD2 H 3.17 . 1 66 . 11 ARG HD3 H 3.17 . 1 67 . 11 ARG HE H 7.22 . 1 68 . 12 GLN H H 8.12 . 1 69 . 12 GLN HA H 4.13 . 1 70 . 12 GLN HB2 H 2.46 . 2 71 . 12 GLN HB3 H 2.38 . 2 72 . 12 GLN HG2 H 2.38 . 2 73 . 12 GLN HG3 H 2.45 . 2 74 . 12 GLN HE21 H 6.57 . 2 75 . 12 GLN HE22 H 7.18 . 2 76 . 13 ARG H H 7.97 . 1 77 . 13 ARG HA H 4.12 . 1 78 . 13 ARG HB2 H 1.71 . 2 79 . 13 ARG HB3 H 1.64 . 2 80 . 13 ARG HG2 H 1.33 . 2 81 . 13 ARG HG3 H 1.37 . 2 82 . 13 ARG HD2 H 3.03 . 1 83 . 13 ARG HD3 H 3.03 . 1 84 . 13 ARG HE H 7.06 . 1 85 . 14 TYR H H 7.90 . 1 86 . 14 TYR HA H 4.58 . 1 87 . 14 TYR HB2 H 3.20 . 2 88 . 14 TYR HB3 H 2.88 . 2 89 . 14 TYR HD1 H 7.21 . 1 90 . 14 TYR HD2 H 7.21 . 1 91 . 14 TYR HE1 H 6.81 . 1 92 . 14 TYR HE2 H 6.81 . 1 stop_ save_