data_5192 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The NMR-derived Conformation of Neuropeptide F from Moniezia expansa ; _BMRB_accession_number 5192 _BMRB_flat_file_name bmr5192.str _Entry_type original _Submission_date 2001-10-29 _Accession_date 2001-10-30 _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 Miskolzie Mark . . 2 Kotovych George . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 248 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: The NMR-derived Conformation of Neuropeptide F from Moniezia expansa ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12023801 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miskolzie Mark . . 2 Kotovych George . . stop_ _Journal_abbreviation 'J. Biomol. Struct. Dyn.' _Journal_volume 19 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 991 _Page_last 998 _Year 2002 _Details . loop_ _Keyword 'Monieza expansa' 'neuropeptide F' 'NMR structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_NPF _Saveframe_category molecular_system _Mol_system_name 'neuropeptide F' _Abbreviation_common NPF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'neuropeptide F' $NPF 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_NPF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'neuropeptide F' _Abbreviation_common NPF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; PDKDFIVNPSDLVLDNKAAL RDYLRQINEYFAIIGRPRFX ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 PRO 2 -1 ASP 3 0 LYS 4 1 ASP 5 2 PHE 6 3 ILE 7 4 VAL 8 5 ASN 9 6 PRO 10 7 SER 11 8 ASP 12 9 LEU 13 10 VAL 14 11 LEU 15 12 ASP 16 13 ASN 17 14 LYS 18 15 ALA 19 16 ALA 20 17 LEU 21 18 ARG 22 19 ASP 23 20 TYR 24 21 LEU 25 22 ARG 26 23 GLN 27 24 ILE 28 25 ASN 29 26 GLU 30 27 TYR 31 28 PHE 32 29 ALA 33 30 ILE 34 31 ILE 35 32 GLY 36 33 ARG 37 34 PRO 38 35 ARG 39 36 PHE 40 37 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1K8V "The Nmr-Derived Conformation Of Neuropeptide F From Moniezia Expansa" 97.44 40 100.00 100.00 2.65e-17 SP P41967 "RecName: Full=Neuropeptide F; Short=NPF [Moniezia expansa]" 97.44 39 100.00 100.00 2.61e-17 stop_ save_ ###################### # Polymer residues # ###################### 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 $NPF 'sheep tapeworm' 28841 Eukaryota Metazoa Moniezia expansa 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 $NPF '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 $NPF 1.4 mM . CD3OH 60 '% v/v' . H2O 40 '% v/v' . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _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 4.85 0.05 n/a temperature 298.0 0.1 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 methanol H 1 'methyl protons' ppm 3.30 internal direct . internal . 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_shifts_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 'neuropeptide F' _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 PRO HA H 4.34 . 1 2 . 1 PRO HB2 H 2.45 . 1 3 . 1 PRO HB3 H 2.45 . 1 4 . 1 PRO HG2 H 2.06 . 1 5 . 1 PRO HG3 H 2.06 . 1 6 . 1 PRO HD2 H 3.44 . 2 7 . 1 PRO HD3 H 3.52 . 2 8 . 2 ASP H H 8.80 . 1 9 . 2 ASP HA H 4.56 . 1 10 . 2 ASP HB2 H 2.74 . 2 11 . 2 ASP HB3 H 2.65 . 2 12 . 3 LYS H H 8.38 . 1 13 . 3 LYS HA H 4.21 . 1 14 . 3 LYS HB2 H 1.80 . 2 15 . 3 LYS HB3 H 1.77 . 2 16 . 3 LYS HG2 H 1.39 . 1 17 . 3 LYS HG3 H 1.39 . 1 18 . 3 LYS HD2 H 1.64 . 1 19 . 3 LYS HD3 H 1.64 . 1 20 . 3 LYS HE2 H 2.96 . 1 21 . 3 LYS HE3 H 2.96 . 1 22 . 4 ASP H H 8.16 . 1 23 . 4 ASP HA H 4.52 . 1 24 . 4 ASP HB2 H 2.56 . 1 25 . 4 ASP HB3 H 2.56 . 1 26 . 5 PHE H H 7.92 . 1 27 . 5 PHE HA H 4.55 . 1 28 . 5 PHE HB2 H 3.18 . 2 29 . 5 PHE HB3 H 2.98 . 2 30 . 5 PHE HD1 H 7.23 . 1 31 . 5 PHE HD2 H 7.23 . 1 32 . 6 ILE H H 7.85 . 1 33 . 6 ILE HA H 4.13 . 1 34 . 6 ILE HB H 1.84 . 1 35 . 6 ILE HG12 H 1.47 . 2 36 . 6 ILE HG13 H 1.13 . 2 37 . 6 ILE HG2 H 0.86 . 1 38 . 6 ILE HD1 H 0.86 . 1 39 . 7 VAL H H 7.98 . 1 40 . 7 VAL HA H 4.10 . 1 41 . 7 VAL HB H 2.02 . 1 42 . 7 VAL HG1 H 0.90 . 2 43 . 7 VAL HG2 H 0.93 . 2 44 . 8 ASN H H 8.62 . 1 45 . 8 ASN HA H 4.99 . 1 46 . 8 ASN HB2 H 2.70 . 2 47 . 8 ASN HB3 H 2.96 . 2 48 . 8 ASN HD21 H 7.76 . 2 49 . 8 ASN HD22 H 6.96 . 2 50 . 9 PRO HA H 4.27 . 1 51 . 9 PRO HB2 H 2.30 . 2 52 . 9 PRO HB3 H 2.09 . 2 53 . 9 PRO HG2 H 2.00 . 1 54 . 9 PRO HG3 H 2.00 . 1 55 . 9 PRO HD2 H 3.84 . 2 56 . 9 PRO HD3 H 3.93 . 2 57 . 10 SER H H 8.16 . 1 58 . 10 SER HA H 4.22 . 1 59 . 10 SER HB2 H 3.84 . 2 60 . 10 SER HB3 H 3.89 . 2 61 . 11 ASP H H 8.02 . 1 62 . 11 ASP HA H 4.55 . 1 63 . 11 ASP HB2 H 2.76 . 2 64 . 11 ASP HB3 H 2.79 . 2 65 . 12 LEU H H 7.65 . 1 66 . 12 LEU HA H 4.22 . 1 67 . 12 LEU HB2 H 1.75 . 1 68 . 12 LEU HB3 H 1.75 . 1 69 . 12 LEU HG H 1.62 . 1 70 . 12 LEU HD1 H 0.91 . 2 71 . 12 LEU HD2 H 0.85 . 2 72 . 13 VAL H H 7.61 . 1 73 . 13 VAL HA H 3.96 . 1 74 . 13 VAL HB H 2.17 . 1 75 . 13 VAL HG1 H 0.99 . 2 76 . 13 VAL HG2 H 0.94 . 2 77 . 14 LEU H H 7.96 . 1 78 . 14 LEU HA H 4.26 . 1 79 . 14 LEU HB2 H 1.73 . 1 80 . 14 LEU HB3 H 1.73 . 1 81 . 14 LEU HG H 1.59 . 1 82 . 14 LEU HD1 H 0.91 . 2 83 . 14 LEU HD2 H 0.87 . 2 84 . 15 ASP H H 8.19 . 1 85 . 15 ASP HA H 4.59 . 1 86 . 15 ASP HB2 H 2.75 . 2 87 . 15 ASP HB3 H 2.80 . 2 88 . 16 ASN H H 8.38 . 1 89 . 16 ASN HA H 4.60 . 1 90 . 16 ASN HB2 H 2.84 . 2 91 . 16 ASN HB3 H 2.91 . 2 92 . 16 ASN HD21 H 7.70 . 2 93 . 16 ASN HD22 H 6.91 . 2 94 . 17 LYS H H 8.36 . 1 95 . 17 LYS HA H 4.13 . 1 96 . 17 LYS HB2 H 1.98 . 2 97 . 17 LYS HB3 H 1.92 . 2 98 . 17 LYS HG2 H 1.47 . 2 99 . 17 LYS HG3 H 1.53 . 2 100 . 17 LYS HD2 H 1.73 . 2 101 . 17 LYS HD3 H 1.63 . 2 102 . 17 LYS HE2 H 2.99 . 1 103 . 17 LYS HE3 H 2.99 . 1 104 . 18 ALA H H 8.12 . 1 105 . 18 ALA HA H 4.02 . 1 106 . 18 ALA HB H 1.52 . 1 107 . 19 ALA H H 8.13 . 1 108 . 19 ALA HA H 4.19 . 1 109 . 19 ALA HB H 1.49 . 1 110 . 20 LEU H H 7.94 . 1 111 . 20 LEU HA H 4.20 . 1 112 . 20 LEU HB2 H 1.75 . 2 113 . 20 LEU HB3 H 1.83 . 2 114 . 20 LEU HG H 1.72 . 1 115 . 20 LEU HD1 H 1.00 . 2 116 . 20 LEU HD2 H 0.93 . 2 117 . 21 ARG H H 8.12 . 1 118 . 21 ARG HA H 3.96 . 1 119 . 21 ARG HB2 H 2.00 . 2 120 . 21 ARG HB3 H 2.05 . 2 121 . 21 ARG HG2 H 1.89 . 2 122 . 21 ARG HG3 H 1.55 . 2 123 . 21 ARG HD2 H 3.23 . 1 124 . 21 ARG HD3 H 3.23 . 1 125 . 21 ARG HE H 7.45 . 1 126 . 22 ASP H H 8.23 . 1 127 . 22 ASP HA H 4.53 . 1 128 . 22 ASP HB2 H 2.72 . 2 129 . 22 ASP HB3 H 2.79 . 2 130 . 23 TYR H H 8.26 . 1 131 . 23 TYR HA H 4.27 . 1 132 . 23 TYR HB2 H 3.21 . 1 133 . 23 TYR HB3 H 3.21 . 1 134 . 23 TYR HD1 H 7.01 . 1 135 . 23 TYR HD2 H 7.01 . 1 136 . 23 TYR HE1 H 6.68 . 1 137 . 23 TYR HE2 H 6.68 . 1 138 . 24 LEU H H 8.40 . 1 139 . 24 LEU HA H 3.90 . 1 140 . 24 LEU HB2 H 1.94 . 1 141 . 24 LEU HB3 H 1.94 . 1 142 . 24 LEU HG H 1.48 . 1 143 . 24 LEU HD1 H 0.92 . 1 144 . 24 LEU HD2 H 0.92 . 1 145 . 25 ARG H H 8.12 . 1 146 . 25 ARG HA H 4.07 . 1 147 . 25 ARG HB2 H 2.16 . 2 148 . 25 ARG HB3 H 1.81 . 2 149 . 25 ARG HG2 H 1.61 . 1 150 . 25 ARG HG3 H 1.61 . 1 151 . 25 ARG HD2 H 3.29 . 2 152 . 25 ARG HD3 H 3.18 . 2 153 . 25 ARG HE H 7.60 . 1 154 . 26 GLN H H 8.08 . 1 155 . 26 GLN HA H 4.00 . 1 156 . 26 GLN HB2 H 2.24 . 2 157 . 26 GLN HB3 H 2.11 . 2 158 . 26 GLN HG2 H 2.57 . 2 159 . 26 GLN HG3 H 2.29 . 2 160 . 26 GLN HE21 H 7.31 . 2 161 . 26 GLN HE22 H 6.73 . 2 162 . 27 ILE H H 8.19 . 1 163 . 27 ILE HA H 3.74 . 1 164 . 27 ILE HB H 1.80 . 1 165 . 27 ILE HG12 H 1.25 . 2 166 . 27 ILE HG13 H 1.00 . 2 167 . 27 ILE HG2 H 0.81 . 1 168 . 27 ILE HD1 H 0.58 . 1 169 . 28 ASN H H 8.15 . 1 170 . 28 ASN HA H 4.58 . 1 171 . 28 ASN HB2 H 2.77 . 2 172 . 28 ASN HB3 H 2.98 . 2 173 . 28 ASN HD21 H 7.64 . 2 174 . 28 ASN HD22 H 6.90 . 2 175 . 29 GLU H H 8.41 . 1 176 . 29 GLU HA H 4.04 . 1 177 . 29 GLU HB2 H 2.21 . 2 178 . 29 GLU HB3 H 2.07 . 2 179 . 29 GLU HG2 H 2.52 . 2 180 . 29 GLU HG3 H 2.28 . 2 181 . 30 TYR H H 8.09 . 1 182 . 30 TYR HA H 3.90 . 1 183 . 30 TYR HB2 H 3.06 . 1 184 . 30 TYR HB3 H 3.06 . 1 185 . 30 TYR HD1 H 6.60 . 1 186 . 30 TYR HD2 H 6.60 . 1 187 . 30 TYR HE1 H 6.54 . 1 188 . 30 TYR HE2 H 6.54 . 1 189 . 31 PHE H H 8.26 . 1 190 . 31 PHE HA H 4.17 . 1 191 . 31 PHE HB2 H 3.22 . 2 192 . 31 PHE HB3 H 3.10 . 2 193 . 31 PHE HD1 H 7.38 . 1 194 . 31 PHE HD2 H 7.38 . 1 195 . 31 PHE HE1 H 7.31 . 1 196 . 31 PHE HE2 H 7.31 . 1 197 . 31 PHE HZ H 7.28 . 1 198 . 32 ALA H H 8.03 . 1 199 . 32 ALA HA H 4.12 . 1 200 . 32 ALA HB H 1.54 . 1 201 . 33 ILE H H 7.86 . 1 202 . 33 ILE HA H 3.87 . 1 203 . 33 ILE HB H 1.95 . 1 204 . 33 ILE HG12 H 1.72 . 2 205 . 33 ILE HG13 H 1.19 . 2 206 . 33 ILE HG2 H 0.86 . 1 207 . 33 ILE HD1 H 0.86 . 1 208 . 34 ILE H H 7.74 . 1 209 . 34 ILE HA H 4.05 . 1 210 . 34 ILE HB H 1.80 . 1 211 . 34 ILE HG12 H 1.20 . 2 212 . 34 ILE HG13 H 1.10 . 2 213 . 34 ILE HG2 H 0.70 . 1 214 . 34 ILE HD1 H 0.67 . 1 215 . 35 GLY H H 7.87 . 1 216 . 35 GLY HA2 H 3.82 . 2 217 . 35 GLY HA3 H 3.93 . 2 218 . 36 ARG H H 7.67 . 1 219 . 36 ARG HA H 4.57 . 1 220 . 36 ARG HB2 H 1.82 . 2 221 . 36 ARG HB3 H 1.72 . 2 222 . 36 ARG HG2 H 1.67 . 2 223 . 36 ARG HG3 H 1.65 . 2 224 . 36 ARG HD2 H 3.14 . 1 225 . 36 ARG HD3 H 3.14 . 1 226 . 36 ARG HE H 7.34 . 1 227 . 37 PRO HA H 4.33 . 1 228 . 37 PRO HB2 H 2.20 . 2 229 . 37 PRO HB3 H 1.77 . 2 230 . 37 PRO HG2 H 2.00 . 2 231 . 37 PRO HG3 H 1.95 . 2 232 . 37 PRO HD2 H 3.58 . 2 233 . 37 PRO HD3 H 3.76 . 2 234 . 38 ARG H H 8.31 . 1 235 . 38 ARG HA H 4.20 . 1 236 . 38 ARG HB2 H 1.64 . 2 237 . 38 ARG HB3 H 1.70 . 2 238 . 38 ARG HG2 H 1.50 . 2 239 . 38 ARG HG3 H 1.54 . 2 240 . 38 ARG HD2 H 3.10 . 1 241 . 38 ARG HD3 H 3.10 . 1 242 . 38 ARG HE H 7.30 . 1 243 . 39 PHE H H 7.96 . 1 244 . 39 PHE HA H 4.59 . 1 245 . 39 PHE HB2 H 2.94 . 2 246 . 39 PHE HB3 H 3.13 . 2 247 . 40 NH2 HN1 H 7.54 . 2 248 . 40 NH2 HN2 H 7.05 . 2 stop_ save_