data_5216 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Y2 selective analogue-III of neuropeptide Y ; _BMRB_accession_number 5216 _BMRB_flat_file_name bmr5216.str _Entry_type original _Submission_date 2001-11-21 _Accession_date 2001-11-26 _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 Yao Shenggen . . 2 Smith-White Margaret A. . 3 Potter Erica K. . 4 Norton Raymond S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 100 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 4398 'neuropeptide Y' 5214 'Y2 selective analogue-I of neuropeptide Y' 5215 'Y2 selective analogue-II of neuropeptide Y' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Stabilization of the Helical Structure of Y2-selective Analogues of Neuropeptide Y by Lactam Bridges ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22010296 _PubMed_ID 12014969 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yao Shenggen . . 2 Smith-White Margaret A. . 3 Potter Erica K. . 4 Norton Raymond S. . stop_ _Journal_abbreviation 'J. Med. Chem.' _Journal_volume 45 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2310 _Page_last 2318 _Year 2002 _Details . loop_ _Keyword 'neuropeptide Y' 'Y2 agonist' 'lactam bridge' helix NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_NPY _Saveframe_category molecular_system _Mol_system_name 'Y2 selective analogue III of neuropeptide Y' _Abbreviation_common NPY _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'analogue III of 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 'analog-III, L24A, I28K, T32E' _Abbreviation_common NPY _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence XARHYKNLIERQRYX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 ACE 2 24 ALA 3 25 ARG 4 26 HIS 5 27 TYR 6 28 LYS 7 29 ASN 8 30 LEU 9 31 ILE 10 32 GLU 11 33 ARG 12 34 GLN 13 35 ARG 14 36 TYR 15 36 NH2 stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-02-17 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 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? O O O . 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 . _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 Thu Jul 21 10:41:13 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_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single lactam 'analogue III of neuropeptide Y' 6 LYS NZ 'analogue III of neuropeptide Y' 10 GLU CD 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 3.0 mM . TFE 40 % . H2O 60 % . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task process stop_ _Details 'Bruker AG, Karlsruhe, Germany' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task analysis stop_ _Details 'C. Bartels et. al., J. Biomol. NMR 1995, 6, 1-10' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQFCOSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQFCOSY _Sample_label $sample_1 save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details ; Standard Bruker pulse sequences were used. Water suppression was achieved using water-gate segment. ; save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQFCOSY _BMRB_pulse_sequence_accession_number . _Details ; Standard Bruker pulse sequences were used. Water suppression was achieved using water-gate segment. ; save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details ; Standard Bruker pulse sequences were used. Water suppression was achieved using water-gate segment. ; save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details ; Standard Bruker pulse sequences were used. Water suppression was achieved using water-gate segment. ; save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 n/a temperature 308 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 DSS H 1 'methyl protons' ppm 0.0 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_analog-III_cs_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'analogue III of 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 . 1 ACE H1 H 2.08 0.01 1 2 . 1 ACE H2 H 2.08 0.01 1 3 . 1 ACE H3 H 2.08 0.01 1 4 . 2 ALA H H 8.12 0.01 1 5 . 2 ALA HA H 4.22 0.01 1 6 . 2 ALA HB H 1.39 0.01 1 7 . 3 ARG H H 8.18 0.01 1 8 . 3 ARG HA H 4.16 0.01 1 9 . 3 ARG HB2 H 1.73 0.01 1 10 . 3 ARG HB3 H 1.73 0.01 1 11 . 3 ARG HG2 H 1.57 0.01 1 12 . 3 ARG HG3 H 1.57 0.01 1 13 . 3 ARG HD2 H 3.17 0.01 1 14 . 3 ARG HD3 H 3.17 0.01 1 15 . 3 ARG HE H 7.15 0.01 1 16 . 4 HIS H H 8.04 0.01 1 17 . 4 HIS HA H 4.56 0.01 1 18 . 4 HIS HB2 H 3.14 0.01 1 19 . 4 HIS HB3 H 3.14 0.01 1 20 . 4 HIS HD2 H 7.00 0.01 1 21 . 4 HIS HE1 H 8.31 0.01 1 22 . 5 TYR H H 7.89 0.01 1 23 . 5 TYR HA H 4.46 0.01 1 24 . 5 TYR HB2 H 2.94 0.01 2 25 . 5 TYR HB3 H 3.11 0.01 2 26 . 5 TYR HD1 H 7.10 0.01 1 27 . 5 TYR HD2 H 7.10 0.01 1 28 . 5 TYR HE1 H 6.80 0.01 1 29 . 5 TYR HE2 H 6.80 0.01 1 30 . 6 LYS H H 8.21 0.01 1 31 . 6 LYS HA H 4.03 0.01 1 32 . 6 LYS HB2 H 1.74 0.01 2 33 . 6 LYS HB3 H 2.00 0.01 2 34 . 6 LYS HG2 H 1.37 0.01 2 35 . 6 LYS HG3 H 1.41 0.01 2 36 . 6 LYS HD2 H 1.49 0.01 2 37 . 6 LYS HD3 H 1.53 0.01 2 38 . 6 LYS HE2 H 2.98 0.01 2 39 . 6 LYS HE3 H 3.39 0.01 2 40 . 6 LYS HZ H 7.43 0.01 1 41 . 7 ASN H H 7.93 0.01 1 42 . 7 ASN HA H 4.48 0.01 1 43 . 7 ASN HB2 H 2.94 0.01 1 44 . 7 ASN HB3 H 2.94 0.01 1 45 . 7 ASN HD21 H 6.72 0.01 2 46 . 7 ASN HD22 H 7.59 0.01 2 47 . 8 LEU H H 7.92 0.01 1 48 . 8 LEU HA H 4.09 0.01 1 49 . 8 LEU HB2 H 1.77 0.01 1 50 . 8 LEU HB3 H 1.77 0.01 1 51 . 8 LEU HG H 1.66 0.01 1 52 . 8 LEU HD1 H 0.88 0.01 2 53 . 8 LEU HD2 H 0.91 0.01 2 54 . 9 ILE H H 7.90 0.01 1 55 . 9 ILE HA H 3.87 0.01 1 56 . 9 ILE HB H 1.94 0.01 1 57 . 9 ILE HG2 H 0.88 0.01 1 58 . 9 ILE HG12 H 1.19 0.01 2 59 . 9 ILE HG13 H 1.51 0.01 2 60 . 9 ILE HD1 H 0.81 0.01 1 61 . 10 GLU H H 7.94 0.01 1 62 . 10 GLU HA H 4.10 0.01 1 63 . 10 GLU HB2 H 2.20 0.01 1 64 . 10 GLU HB3 H 2.20 0.01 1 65 . 10 GLU HG2 H 2.47 0.01 1 66 . 10 GLU HG3 H 2.47 0.01 1 67 . 11 ARG H H 7.87 0.01 1 68 . 11 ARG HA H 3.92 0.01 1 69 . 11 ARG HB2 H 1.80 0.01 2 70 . 11 ARG HB3 H 1.94 0.01 2 71 . 11 ARG HG2 H 1.64 0.01 1 72 . 11 ARG HG3 H 1.64 0.01 1 73 . 11 ARG HD2 H 3.14 0.01 1 74 . 11 ARG HD3 H 3.14 0.01 1 75 . 11 ARG HE H 7.22 0.01 1 76 . 12 GLN H H 8.05 0.01 1 77 . 12 GLN HA H 4.14 0.01 1 78 . 12 GLN HB2 H 2.13 0.01 1 79 . 12 GLN HB3 H 2.13 0.01 1 80 . 12 GLN HG2 H 2.39 0.01 2 81 . 12 GLN HG3 H 2.46 0.01 2 82 . 12 GLN HE21 H 6.60 0.01 2 83 . 12 GLN HE22 H 7.15 0.01 2 84 . 13 ARG H H 7.99 0.01 1 85 . 13 ARG HA H 4.15 0.01 1 86 . 13 ARG HB2 H 1.63 0.01 2 87 . 13 ARG HB3 H 1.67 0.01 2 88 . 13 ARG HG2 H 1.41 0.01 2 89 . 13 ARG HG3 H 1.46 0.01 2 90 . 13 ARG HD2 H 3.06 0.01 1 91 . 13 ARG HD3 H 3.06 0.01 1 92 . 13 ARG HE H 7.08 0.01 1 93 . 14 TYR H H 7.89 0.01 1 94 . 14 TYR HA H 4.61 0.01 1 95 . 14 TYR HB2 H 2.91 0.01 2 96 . 14 TYR HB3 H 3.23 0.01 2 97 . 14 TYR HD1 H 7.21 0.01 1 98 . 14 TYR HD2 H 7.21 0.01 1 99 . 14 TYR HE1 H 6.83 0.01 1 100 . 14 TYR HE2 H 6.83 0.01 1 stop_ save_