data_4842 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of porcine peptide YY ; _BMRB_accession_number 4842 _BMRB_flat_file_name bmr4842.str _Entry_type original _Submission_date 2000-09-27 _Accession_date 2000-09-28 _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 Keire David A. . 2 Kobayashi Mitsuo . . 3 Solomon Travis E. . 4 Reeve Joseph R. Jr. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 189 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 update BMRB 'Updating non-standard residue' 2008-03-24 update BMRB . 2000-11-29 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of monomeric peptide YY supports the functional significance of the PP-fold ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20393886 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Keire David A . 2 Kobayashi Mitsuo . . 3 Solomon Travis E . 4 Reeve Joseph R. Jr. stop_ _Journal_abbreviation Biochemistry _Journal_volume 39 _Journal_issue 32 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9935 _Page_last 9942 _Year 2000 _Details . loop_ _Keyword PYY NPY PP PP-Fold '3D Structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_PYY _Saveframe_category molecular_system _Mol_system_name 'PORCINE PEPTIDE YY' _Abbreviation_common PYY _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PEPTIDE YY' $PYY stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state Monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'regulation of gastrointestinal function' 'regulation of blood pressure' 'regulation of feeding behavior' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PYY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'PEPTIDE YY' _Abbreviation_common PYY _Molecular_mass 4240 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; YPAKPEAPGEDASPEELSRY YASLRHYLNLVTRQRYX ; loop_ _Residue_seq_code _Residue_label 1 TYR 2 PRO 3 ALA 4 LYS 5 PRO 6 GLU 7 ALA 8 PRO 9 GLY 10 GLU 11 ASP 12 ALA 13 SER 14 PRO 15 GLU 16 GLU 17 LEU 18 SER 19 ARG 20 TYR 21 TYR 22 ALA 23 SER 24 LEU 25 ARG 26 HIS 27 TYR 28 LEU 29 ASN 30 LEU 31 VAL 32 THR 33 ARG 34 GLN 35 ARG 36 TYR 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 BMRB 6068 pPYY 97.22 36 100.00 100.00 3.46e-15 PDB 1QBF "Nmr Solution Structure Of Porcine Peptide Yy" 97.22 37 100.00 100.00 4.12e-15 PDB 1RU5 "Solution Structure Of Porcine Peptide Yy (Ppyy)" 97.22 37 100.00 100.00 4.12e-15 PDB 1RUU "Solution Structure Of Porcine Peptide Yy (Ppyy) Bound To Dpc Micelles" 97.22 37 100.00 100.00 4.12e-15 PDB 2OON "Structure Of Ala14-Pyy In Aqueous Solution" 97.22 37 97.14 97.14 3.44e-14 PDB 2OOP "Structure Of Tyr7-Pyy In Solution" 97.22 37 97.14 97.14 3.74e-14 PDB 2RLK "Refined Solution Structure Of Porcine Peptide Yy (Pyy)" 97.22 37 100.00 100.00 4.12e-15 DBJ BAE20675 "unnamed protein product [Mus musculus]" 97.22 98 100.00 100.00 3.75e-15 DBJ BAE46747 "peptide YY [Rattus norvegicus]" 97.22 98 100.00 100.00 3.63e-15 GB AAA41222 "peptide YY precursor [Rattus sp.]" 97.22 98 100.00 100.00 3.63e-15 GB AAB19752 "peptide-YY [Rattus sp.]" 97.22 98 100.00 100.00 3.63e-15 GB AAG42908 "peptide tyrosine tyrosine PYY [Mus musculus]" 97.22 93 100.00 100.00 2.87e-15 GB AAH10821 "Peptide YY [Mus musculus]" 97.22 98 100.00 100.00 3.75e-15 GB AEY83942 "peptide YY precursor [Sus scrofa]" 97.22 97 100.00 100.00 5.00e-15 PRF 1407279A "peptide PYY" 97.22 36 100.00 100.00 4.07e-15 REF NP_001029252 "peptide YY precursor [Rattus norvegicus]" 97.22 98 100.00 100.00 3.63e-15 REF NP_001243457 "peptide YY precursor [Sus scrofa]" 97.22 97 100.00 100.00 5.00e-15 REF NP_663410 "peptide YY precursor [Mus musculus]" 97.22 98 100.00 100.00 3.75e-15 REF XP_001113958 "PREDICTED: peptide YY isoform 2 [Macaca mulatta]" 97.22 97 97.14 97.14 2.49e-14 REF XP_001491077 "PREDICTED: peptide YY [Equus caballus]" 97.22 90 97.14 97.14 4.90e-14 SP P10631 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Peptide YY(3-36); AltName" 97.22 98 100.00 100.00 3.63e-15 SP P68004 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Peptide YY(3-36) [Canis l" 97.22 36 100.00 100.00 4.07e-15 SP P68005 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Peptide YY(3-36); AltName" 97.22 36 100.00 100.00 4.07e-15 SP Q9EPS2 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Peptide YY(3-36); AltName" 97.22 98 100.00 100.00 3.75e-15 stop_ 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 Thu Jul 14 16:09:34 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_ ############# # Ligands # ############# save_NH2 _Saveframe_category ligand _Mol_type non-polymer _Name_common NH2 _Molecular_mass . _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PYY pig 9823 Eukaryota Metazoa Sus scrofa 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 $PYY '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 $PYY 1.0 mM . KCl 0.15 M . stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.0 loop_ _Task 'STRUCTURE CALCULATION' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _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 . save_ ####################### # Sample conditions # ####################### save_Condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5 0.1 n/a temperature 298 0.5 K 'ionic strength' 0.15 0.01 M 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_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external 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_chemical_shift_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 'PEPTIDE YY' _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 4.35 . 1 2 . 1 TYR HB2 H 2.89 . 2 3 . 1 TYR HB3 H 3.08 . 2 4 . 1 TYR HD1 H 7.10 . 2 5 . 1 TYR HE1 H 6.77 . 2 6 . 2 PRO HA H 4.40 . 1 7 . 2 PRO HB2 H 1.86 . 2 8 . 2 PRO HB3 H 2.23 . 2 9 . 2 PRO HG2 H 1.81 . 2 10 . 2 PRO HD2 H 3.11 . 2 11 . 2 PRO HD3 H 3.58 . 2 12 . 3 ALA H H 8.41 . 1 13 . 3 ALA HA H 4.23 . 1 14 . 3 ALA HB H 1.25 . 1 15 . 4 LYS H H 8.29 . 1 16 . 4 LYS HA H 3.40 . 1 17 . 4 LYS HB2 H 1.13 . 2 18 . 4 LYS HB3 H 1.24 . 2 19 . 4 LYS HG2 H 0.86 . 2 20 . 4 LYS HG3 H 1.42 . 3 21 . 4 LYS HD2 H 1.49 . 2 22 . 4 LYS HE3 H 2.81 . 2 23 . 5 PRO HA H 4.27 . 1 24 . 5 PRO HB2 H 1.78 . 2 25 . 5 PRO HB3 H 2.21 . 2 26 . 5 PRO HG2 H 1.65 . 2 27 . 5 PRO HD2 H 3.00 . 2 28 . 5 PRO HD3 H 3.36 . 2 29 . 6 GLU H H 8.49 . 1 30 . 6 GLU HA H 4.08 . 1 31 . 6 GLU HB2 H 1.72 . 2 32 . 6 GLU HG2 H 1.81 . 2 33 . 6 GLU HG3 H 2.17 . 2 34 . 7 ALA H H 8.31 . 1 35 . 7 ALA HA H 3.45 . 1 36 . 7 ALA HB H 1.00 . 1 37 . 8 PRO HA H 4.21 . 1 38 . 8 PRO HB2 H 1.65 . 2 39 . 8 PRO HB3 H 1.98 . 2 40 . 8 PRO HG2 H 1.43 . 2 41 . 8 PRO HD2 H 2.59 . 2 42 . 8 PRO HD3 H 2.64 . 2 43 . 9 GLY H H 8.30 . 1 44 . 9 GLY HA2 H 3.74 . 2 45 . 9 GLY HA3 H 3.93 . 2 46 . 10 GLU H H 8.50 . 1 47 . 10 GLU HA H 3.91 . 1 48 . 10 GLU HB2 H 1.83 . 2 49 . 10 GLU HB3 H 1.90 . 2 50 . 10 GLU HG2 H 2.16 . 2 51 . 11 ASP H H 8.44 . 1 52 . 11 ASP HA H 4.47 . 1 53 . 11 ASP HB2 H 2.58 . 2 54 . 12 ALA H H 7.16 . 1 55 . 12 ALA HA H 4.10 . 1 56 . 12 ALA HB H 1.22 . 1 57 . 13 SER H H 8.65 . 1 58 . 13 SER HA H 4.55 . 1 59 . 13 SER HB2 H 3.94 . 2 60 . 13 SER HB3 H 4.29 . 2 61 . 14 PRO HA H 3.81 . 1 62 . 15 GLU H H 8.54 . 1 63 . 15 GLU HA H 3.99 . 1 64 . 15 GLU HB2 H 1.82 . 2 65 . 15 GLU HB3 H 1.97 . 2 66 . 15 GLU HG2 H 2.17 . 2 67 . 15 GLU HG3 H 2.28 . 2 68 . 16 GLU H H 7.82 . 1 69 . 16 GLU HA H 3.83 . 1 70 . 16 GLU HB2 H 1.86 . 2 71 . 16 GLU HB3 H 2.12 . 2 72 . 16 GLU HG2 H 2.21 . 2 73 . 17 LEU H H 8.37 . 1 74 . 17 LEU HA H 3.83 . 1 75 . 17 LEU HB2 H 1.75 . 2 76 . 17 LEU HG H 1.45 . 2 77 . 17 LEU HD1 H 0.71 . 2 78 . 17 LEU HD2 H 0.75 . 2 79 . 18 SER H H 8.28 . 1 80 . 18 SER HA H 4.15 . 1 81 . 18 SER HB2 H 3.84 . 2 82 . 18 SER HB3 H 3.92 . 2 83 . 19 ARG H H 7.85 . 1 84 . 19 ARG HA H 4.02 . 1 85 . 19 ARG HB2 H 1.77 . 2 86 . 19 ARG HB3 H 1.86 . 2 87 . 19 ARG HG2 H 1.50 . 2 88 . 19 ARG HD2 H 3.07 . 2 89 . 19 ARG HD3 H 3.15 . 2 90 . 19 ARG HE H 7.41 . 1 91 . 20 TYR H H 7.96 . 1 92 . 20 TYR HA H 4.27 . 1 93 . 20 TYR HB2 H 2.86 . 2 94 . 20 TYR HB3 H 3.07 . 2 95 . 20 TYR HD1 H 6.59 . 2 96 . 20 TYR HE1 H 6.39 . 2 97 . 21 TYR H H 8.65 . 1 98 . 21 TYR HA H 3.84 . 1 99 . 21 TYR HB2 H 2.84 . 2 100 . 21 TYR HB3 H 2.96 . 2 101 . 21 TYR HD1 H 6.94 . 2 102 . 21 TYR HE1 H 6.72 . 2 103 . 22 ALA H H 7.89 . 1 104 . 22 ALA HA H 4.03 . 1 105 . 22 ALA HB H 1.44 . 1 106 . 23 SER H H 8.17 . 1 107 . 23 SER HA H 4.22 . 1 108 . 23 SER HB2 H 3.86 . 2 109 . 23 SER HB3 H 3.96 . 2 110 . 24 LEU H H 8.72 . 1 111 . 24 LEU HA H 3.90 . 1 112 . 24 LEU HB2 H 1.52 . 2 113 . 24 LEU HG H 1.37 . 2 114 . 24 LEU HD1 H 0.76 . 2 115 . 24 LEU HD2 H 1.12 . 2 116 . 25 ARG H H 8.03 . 1 117 . 25 ARG HA H 3.80 . 1 118 . 25 ARG HB2 H 1.79 . 2 119 . 25 ARG HG2 H 1.45 . 2 120 . 25 ARG HG3 H 1.64 . 2 121 . 25 ARG HD2 H 3.05 . 2 122 . 25 ARG HD3 H 3.12 . 2 123 . 25 ARG HE H 7.18 . 1 124 . 26 HIS H H 7.77 . 1 125 . 26 HIS HA H 4.28 . 1 126 . 26 HIS HB2 H 3.15 . 2 127 . 26 HIS HB3 H 3.22 . 2 128 . 26 HIS HD1 H 8.16 . 1 129 . 26 HIS HE2 H 7.12 . 1 130 . 27 TYR H H 8.11 . 1 131 . 27 TYR HA H 3.96 . 1 132 . 27 TYR HB2 H 3.01 . 2 133 . 27 TYR HB3 H 3.08 . 2 134 . 27 TYR HD1 H 6.88 . 2 135 . 27 TYR HE1 H 6.60 . 2 136 . 28 LEU H H 8.55 . 1 137 . 28 LEU HA H 3.70 . 1 138 . 28 LEU HB2 H 1.69 . 2 139 . 28 LEU HG H 1.36 . 1 140 . 28 LEU HD1 H 0.75 . 2 141 . 29 ASN H H 7.88 . 1 142 . 29 ASN HA H 4.28 . 1 143 . 29 ASN HB2 H 2.69 . 2 144 . 29 ASN HB3 H 2.78 . 2 145 . 29 ASN HD21 H 6.83 . 2 146 . 29 ASN HD22 H 7.57 . 2 147 . 30 LEU H H 7.62 . 1 148 . 30 LEU HA H 3.94 . 1 149 . 30 LEU HB2 H 1.58 . 2 150 . 30 LEU HD1 H 1.30 . 2 151 . 30 LEU HD2 H 1.36 . 2 152 . 30 LEU HG H 0.64 . 1 153 . 31 VAL H H 7.80 . 1 154 . 31 VAL HA H 3.69 . 1 155 . 31 VAL HB H 1.81 . 1 156 . 32 THR H H 7.64 . 1 157 . 32 THR HA H 4.04 . 1 158 . 32 THR HB H 4.14 . 1 159 . 32 THR HG2 H 1.10 . 1 160 . 33 ARG H H 7.77 . 1 161 . 33 ARG HA H 4.09 . 1 162 . 33 ARG HB2 H 1.72 . 2 163 . 33 ARG HB3 H 1.77 . 2 164 . 33 ARG HG2 H 1.54 . 2 165 . 33 ARG HD2 H 3.04 . 2 166 . 33 ARG HD3 H 3.14 . 2 167 . 33 ARG HE H 7.09 . 1 168 . 34 GLN H H 8.04 . 1 169 . 34 GLN HA H 4.06 . 1 170 . 34 GLN HB2 H 1.86 . 2 171 . 34 GLN HG2 H 1.91 . 2 172 . 34 GLN HG3 H 2.21 . 2 173 . 34 GLN HE21 H 6.73 . 2 174 . 34 GLN HE22 H 7.37 . 2 175 . 35 ARG H H 8.07 . 1 176 . 35 ARG HA H 4.06 . 1 177 . 35 ARG HB2 H 1.55 . 2 178 . 35 ARG HG2 H 1.26 . 2 179 . 35 ARG HG3 H 1.34 . 2 180 . 35 ARG HD2 H 2.97 . 2 181 . 35 ARG HE H 7.03 . 1 182 . 36 TYR H H 8.00 . 1 183 . 36 TYR HA H 4.41 . 1 184 . 36 TYR HB2 H 2.77 . 2 185 . 36 TYR HB3 H 3.00 . 2 186 . 36 TYR HD1 H 7.03 . 2 187 . 36 TYR HE1 H 6.70 . 2 188 . 37 NH2 HN1 H 7.05 . 1 189 . 37 NH2 HN2 H 7.57 . 1 stop_ save_