data_200 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton NMR and CD solution conformation determination and opioid receptor binding studies of a dynorphin A(1-17) model peptide ; _BMRB_accession_number 200 _BMRB_flat_file_name bmr200.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Vaughn Joseph B. . 2 Taylor John W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Vaughn, Joseph B., Jr., Taylor, John W., "Proton NMR and CD solution conformation determination and opioid receptor binding studies of a dynorphin A(1-17) model peptide," Biochim. Biophys. Acta 999, 135-146 (1989). ; _Citation_title ; Proton NMR and CD solution conformation determination and opioid receptor binding studies of a dynorphin A(1-17) model peptide ; _Citation_status published _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 Vaughn Joseph B. . 2 Taylor John W. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_volume 999 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 135 _Page_last 146 _Year 1989 _Details . save_ ################################## # Molecular system description # ################################## save_system_dynorphin_analogue _Saveframe_category molecular_system _Mol_system_name 'dynorphin analogue' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dynorphin analogue' $dynorphin_analogue stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_dynorphin_analogue _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'dynorphin analogue' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 17 _Mol_residue_sequence YGGFLKKVKPKVKVKSS loop_ _Residue_seq_code _Residue_label 1 TYR 2 GLY 3 GLY 4 PHE 5 LEU 6 LYS 7 LYS 8 VAL 9 LYS 10 PRO 11 LYS 12 VAL 13 LYS 14 VAL 15 LYS 16 SER 17 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2005-12-09 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $dynorphin_analogue . . . . . . 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 $dynorphin_analogue 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.42 . na temperature 299 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 DSS H . . ppm 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_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'dynorphin analogue' _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 TYR HA H 4.22 . 1 2 . 1 TYR HB2 H 3.14 . 1 3 . 1 TYR HB3 H 3.14 . 1 4 . 1 TYR HD1 H 7.16 . 1 5 . 1 TYR HD2 H 7.16 . 1 6 . 1 TYR HE1 H 6.87 . 1 7 . 1 TYR HE2 H 6.87 . 1 8 . 2 GLY H H 8.66 . 1 9 . 2 GLY HA2 H 3.87 . 2 10 . 2 GLY HA3 H 3.92 . 2 11 . 3 GLY H H 8.04 . 1 12 . 3 GLY HA2 H 3.85 . 2 13 . 3 GLY HA3 H 3.88 . 2 14 . 4 PHE H H 8.18 . 1 15 . 4 PHE HA H 4.6 . 1 16 . 4 PHE HB2 H 2.98 . 2 17 . 4 PHE HB3 H 3.11 . 2 18 . 4 PHE HD1 H 7.24 . 1 19 . 4 PHE HD2 H 7.24 . 1 20 . 4 PHE HE1 H 7.36 . 1 21 . 4 PHE HE2 H 7.36 . 1 22 . 4 PHE HZ H 7.32 . 1 23 . 5 LEU H H 8.27 . 1 24 . 5 LEU HA H 4.29 . 1 25 . 5 LEU HB2 H 1.68 . 2 26 . 5 LEU HB3 H 1.64 . 2 27 . 5 LEU HG H 1.51 . 1 28 . 5 LEU HD1 H .84 . 2 29 . 5 LEU HD2 H .91 . 2 30 . 6 LYS H H 8.37 . 1 31 . 6 LYS HA H 4.36 . 1 32 . 6 LYS HB2 H 1.8 . 1 33 . 6 LYS HB3 H 1.8 . 1 34 . 6 LYS HG2 H 1.44 . 1 35 . 6 LYS HG3 H 1.44 . 1 36 . 6 LYS HD2 H 1.69 . 1 37 . 6 LYS HD3 H 1.69 . 1 38 . 6 LYS HE2 H 3 . 1 39 . 6 LYS HE3 H 3 . 1 40 . 7 LYS H H 8.27 . 1 41 . 7 LYS HA H 4.24 . 1 42 . 7 LYS HB2 H 1.73 . 2 43 . 7 LYS HB3 H 1.76 . 2 44 . 7 LYS HG2 H 1.41 . 1 45 . 7 LYS HG3 H 1.41 . 1 46 . 7 LYS HD2 H 1.69 . 1 47 . 7 LYS HD3 H 1.69 . 1 48 . 7 LYS HE2 H 3 . 1 49 . 7 LYS HE3 H 3 . 1 50 . 8 VAL H H 8.21 . 1 51 . 8 VAL HA H 4.08 . 1 52 . 8 VAL HB H 2.01 . 1 53 . 8 VAL HG1 H .89 . 2 54 . 8 VAL HG2 H .9 . 2 55 . 9 LYS H H 8.56 . 1 56 . 9 LYS HA H 4.59 . 1 57 . 9 LYS HB2 H 1.71 . 2 58 . 9 LYS HB3 H 1.73 . 2 59 . 9 LYS HG2 H 1.62 . 1 60 . 9 LYS HG3 H 1.62 . 1 61 . 9 LYS HD2 H 1.69 . 1 62 . 9 LYS HD3 H 1.69 . 1 63 . 9 LYS HE2 H 3 . 1 64 . 9 LYS HE3 H 3 . 1 65 . 10 PRO HA H 4.41 . 1 66 . 10 PRO HB2 H 1.87 . 2 67 . 10 PRO HB3 H 2.3 . 2 68 . 10 PRO HG2 H 2.05 . 1 69 . 10 PRO HG3 H 2.05 . 1 70 . 10 PRO HD2 H 3.62 . 2 71 . 10 PRO HD3 H 3.86 . 2 72 . 11 LYS H H 8.51 . 1 73 . 11 LYS HA H 4.34 . 1 74 . 11 LYS HB2 H 1.37 . 2 75 . 11 LYS HB3 H 1.38 . 2 76 . 11 LYS HG2 H 1.41 . 1 77 . 11 LYS HG3 H 1.41 . 1 78 . 11 LYS HD2 H 1.69 . 1 79 . 11 LYS HD3 H 1.69 . 1 80 . 11 LYS HE2 H 3 . 1 81 . 11 LYS HE3 H 3 . 1 82 . 12 VAL H H 8.24 . 1 83 . 12 VAL HA H 4.09 . 1 84 . 12 VAL HB H 2.01 . 1 85 . 12 VAL HG1 H .93 . 2 86 . 12 VAL HG2 H .94 . 2 87 . 13 LYS H H 8.54 . 1 88 . 13 LYS HA H 4.25 . 1 89 . 13 LYS HB2 H 1.52 . 2 90 . 13 LYS HB3 H 1.54 . 2 91 . 13 LYS HG2 H 1.45 . 1 92 . 13 LYS HG3 H 1.45 . 1 93 . 13 LYS HD2 H 1.69 . 1 94 . 13 LYS HD3 H 1.69 . 1 95 . 13 LYS HE2 H 3 . 1 96 . 13 LYS HE3 H 3 . 1 97 . 14 VAL H H 8.31 . 1 98 . 14 VAL HA H 4.1 . 1 99 . 14 VAL HB H 2.01 . 1 100 . 14 VAL HG1 H .93 . 2 101 . 14 VAL HG2 H .94 . 2 102 . 15 LYS H H 8.56 . 1 103 . 15 LYS HA H 4.32 . 1 104 . 15 LYS HB2 H 1.73 . 2 105 . 15 LYS HB3 H 1.75 . 2 106 . 15 LYS HG2 H 1.41 . 1 107 . 15 LYS HG3 H 1.41 . 1 108 . 15 LYS HD2 H 1.69 . 1 109 . 15 LYS HD3 H 1.69 . 1 110 . 15 LYS HE2 H 3 . 1 111 . 15 LYS HE3 H 3 . 1 112 . 16 SER H H 8.51 . 1 113 . 16 SER HA H 4.49 . 1 114 . 16 SER HB2 H 3.92 . 2 115 . 16 SER HB3 H 3.97 . 2 116 . 17 SER H H 8.39 . 1 117 . 17 SER HA H 4.51 . 1 118 . 17 SER HB2 H 3.92 . 2 119 . 17 SER HB3 H 3.97 . 2 stop_ save_