data_7005 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The PP-fold Solution Structure of Human Polypeptide YY and Human Polypeptide YY 3-36 as Determined by NMR ; _BMRB_accession_number 7005 _BMRB_flat_file_name bmr7005.str _Entry_type original _Submission_date 2006-02-28 _Accession_date 2006-02-28 _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 Nygaard R. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 178 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-10-19 original author . stop_ _Original_release_date 2006-10-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The PP-Fold Solution Structure of Human Polypeptide YY and Human PYY3-36 As Determined by NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16819834 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nygaard R. . . 2 Nielbo S. . . 3 Schwartz T. W. . 4 Poulsen F. M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8350 _Page_last 8357 _Year 2006 _Details . loop_ _Keyword amphipathic helix neuropeptide peptide PP-fold PYY stop_ save_ ################################## # Molecular system description # ################################## save_system_Peptide_YY _Saveframe_category molecular_system _Mol_system_name 'Peptide YY' _Abbreviation_common 'Peptide YY' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Peptide YY' $Peptide_YY 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_Peptide_YY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Peptide YY' _Abbreviation_common 'Peptide YY' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; IKPEAPGEDASPEELNRYYA SLRHYLNLVTRQRYX ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 LYS 3 PRO 4 GLU 5 ALA 6 PRO 7 GLY 8 GLU 9 ASP 10 ALA 11 SER 12 PRO 13 GLU 14 GLU 15 LEU 16 ASN 17 ARG 18 TYR 19 TYR 20 ALA 21 SER 22 LEU 23 ARG 24 HIS 25 TYR 26 LEU 27 ASN 28 LEU 29 VAL 30 THR 31 ARG 32 GLN 33 ARG 34 TYR 35 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 7006 YY 97.06 36 100.00 100.00 5.29e-14 PDB 2DEZ "Structure Of Human Pyy" 97.06 37 100.00 100.00 5.66e-14 PDB 2DF0 "Solution Structure Of Human Pyy3-36" 97.06 35 100.00 100.00 3.91e-14 DBJ BAA02997 "peptide YY precursor [Homo sapiens]" 97.06 97 100.00 100.00 7.88e-14 DBJ BAA02998 "peptide YY precursor variant [Homo sapiens]" 97.06 90 100.00 100.00 6.69e-14 DBJ BAA03000 "peptide YY precursor [Homo sapiens]" 97.06 97 100.00 100.00 8.86e-14 DBJ BAA03002 "peptide YY precursor [Homo sapiens]" 97.06 90 100.00 100.00 6.69e-14 EMBL CAG46926 "PYY [Homo sapiens]" 97.06 90 100.00 100.00 7.52e-14 GB AAA36433 "peptide YY [Homo sapiens]" 97.06 97 100.00 100.00 7.88e-14 GB AAB32641 "peptide YY, PYY(1-36) [rabbits, intestinal mucosa, Peptide, 36 aa]" 94.12 36 100.00 100.00 2.95e-13 GB AAB32642 "peptide YY, PYY(3-36) [rabbits, intestinal mucosa, Peptide, 34 aa]" 94.12 34 100.00 100.00 2.16e-13 GB AAH41057 "Peptide YY [Homo sapiens]" 97.06 97 100.00 100.00 8.86e-14 GB AIC59196 "PYY, partial [synthetic construct]" 97.06 97 100.00 100.00 8.86e-14 REF NP_004151 "peptide YY preproprotein [Homo sapiens]" 97.06 97 100.00 100.00 7.88e-14 REF XP_001113958 "PREDICTED: peptide YY isoform 2 [Macaca mulatta]" 97.06 97 96.97 100.00 4.12e-13 REF XP_002719223 "PREDICTED: peptide YY isoform X1 [Oryctolagus cuniculus]" 94.12 188 100.00 100.00 1.30e-12 REF XP_002748087 "PREDICTED: peptide YY [Callithrix jacchus]" 97.06 97 96.97 100.00 2.76e-13 REF XP_003786336 "PREDICTED: peptide YY [Otolemur garnettii]" 97.06 88 96.97 96.97 1.55e-13 SP P10082 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=PYY-I; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Pept" 97.06 97 96.97 96.97 1.96e-12 SP Q9TR93 "RecName: Full=Peptide YY; Short=PYY; AltName: Full=PYY-I; AltName: Full=Peptide tyrosine tyrosine; Contains: RecName: Full=Pept" 94.12 36 100.00 100.00 2.95e-13 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 Mon Jun 20 13:59:18 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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Peptide_YY 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 $Peptide_YY '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 $Peptide_YY 1 mM . NaOH . mM . HCl . mM . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_Pronto3D _Saveframe_category software _Name Pronto3D _Version . loop_ _Task 'data analysis' stop_ _Details 'Kjaer, M.' save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0 loop_ _Task 'structure solution' stop_ _Details 'Guntert, P.' save_ save_XPLOR-NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.9 loop_ _Task 'structure solution' stop_ _Details 'Schwieters, C.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF COSY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _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 4.6 . pH temperature 298 . 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 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 $sample_cond_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 ILE HA H 3.87 . 1 2 . 1 ILE HB H 1.93 . 1 3 . 1 ILE HG13 H 1.19 . 2 4 . 1 ILE HG2 H 0.96 . 1 5 . 1 ILE HG12 H 1.45 . 2 6 . 1 ILE HD1 H 0.89 . 1 7 . 2 LYS H H 8.59 . 1 8 . 2 LYS HA H 4.33 . 1 9 . 2 LYS HB3 H 1.74 . 2 10 . 2 LYS HB2 H 1.64 . 2 11 . 2 LYS HG3 H 1.38 . 2 12 . 2 LYS HG2 H 1.31 . 2 13 . 2 LYS HD2 H 1.66 . 2 14 . 2 LYS HE2 H 2.97 . 2 15 . 3 PRO HD3 H 3.67 . 2 16 . 3 PRO HA H 4.39 . 1 17 . 3 PRO HD2 H 3.46 . 2 18 . 3 PRO HB2 H 2.28 . 2 19 . 3 PRO HG3 H 1.90 . 2 20 . 3 PRO HG2 H 1.93 . 2 21 . 4 GLU H H 8.46 . 1 22 . 4 GLU HA H 4.25 . 1 23 . 4 GLU HB3 H 1.87 . 2 24 . 4 GLU HB2 H 1.96 . 2 25 . 4 GLU HG3 H 2.28 . 2 26 . 5 ALA H H 8.30 . 1 27 . 5 ALA HA H 4.04 . 1 28 . 5 ALA HB H 1.20 . 1 29 . 6 PRO HB3 H 2.14 . 2 30 . 6 PRO HA H 4.33 . 1 31 . 6 PRO HB2 H 1.80 . 2 32 . 6 PRO HG3 H 1.74 . 2 33 . 7 GLY H H 8.38 . 1 34 . 7 GLY HA3 H 4.03 . 2 35 . 7 GLY HA2 H 3.88 . 2 36 . 8 GLU H H 8.37 . 1 37 . 8 GLU HA H 4.16 . 1 38 . 8 GLU HB3 H 1.96 . 2 39 . 8 GLU HB2 H 2.05 . 2 40 . 8 GLU HG2 H 2.32 . 2 41 . 9 ASP H H 8.49 . 1 42 . 9 ASP HA H 4.62 . 1 43 . 9 ASP HB3 H 2.72 . 2 44 . 9 ASP HB2 H 2.69 . 2 45 . 10 ALA H H 7.64 . 1 46 . 10 ALA HA H 4.30 . 1 47 . 10 ALA HB H 1.33 . 1 48 . 11 SER H H 8.51 . 1 49 . 11 SER HA H 4.72 . 1 50 . 11 SER HB3 H 4.30 . 2 51 . 11 SER HB2 H 4.01 . 2 52 . 12 PRO HG3 H 2.03 . 2 53 . 12 PRO HD3 H 3.88 . 2 54 . 12 PRO HD2 H 3.92 . 2 55 . 12 PRO HG2 H 2.18 . 2 56 . 12 PRO HB3 H 1.95 . 2 57 . 12 PRO HA H 4.26 . 1 58 . 12 PRO HB2 H 2.37 . 2 59 . 13 GLU H H 8.46 . 1 60 . 13 GLU HA H 4.13 . 1 61 . 13 GLU HB2 H 2.07 . 2 62 . 13 GLU HG2 H 2.38 . 2 63 . 14 GLU H H 7.90 . 1 64 . 14 GLU HA H 4.00 . 1 65 . 14 GLU HB3 H 2.22 . 2 66 . 14 GLU HB2 H 2.01 . 2 67 . 14 GLU HG2 H 2.35 . 2 68 . 14 GLU HG3 H 2.27 . 2 69 . 15 LEU HG H 1.58 . 1 70 . 15 LEU HD1 H 0.82 . 2 71 . 15 LEU HD2 H 0.85 . 2 72 . 15 LEU HB2 H 1.81 . 2 73 . 15 LEU HA H 3.98 . 1 74 . 15 LEU H H 7.95 . 1 75 . 16 ASN H H 8.34 . 1 76 . 16 ASN HA H 4.55 . 1 77 . 16 ASN HB3 H 2.92 . 2 78 . 16 ASN HB2 H 2.85 . 2 79 . 16 ASN HD21 H 7.65 . 1 80 . 16 ASN HD22 H 6.93 . 1 81 . 17 ARG H H 8.19 . 1 82 . 17 ARG HA H 4.19 . 1 83 . 17 ARG HD2 H 3.08 . 2 84 . 17 ARG HB2 H 1.66 . 2 85 . 17 ARG HG2 H 1.47 . 2 86 . 17 ARG HG3 H 1.40 . 2 87 . 18 TYR H H 8.10 . 1 88 . 18 TYR HA H 4.32 . 1 89 . 18 TYR HB3 H 3.10 . 2 90 . 18 TYR HB2 H 2.96 . 2 91 . 18 TYR HD1 H 6.70 . 3 92 . 18 TYR HE1 H 6.58 . 3 93 . 19 TYR H H 8.59 . 1 94 . 19 TYR HA H 4.08 . 1 95 . 19 TYR HB2 H 2.97 . 2 96 . 19 TYR HB3 H 3.10 . 2 97 . 19 TYR HD1 H 7.10 . 3 98 . 19 TYR HE1 H 6.82 . 3 99 . 20 ALA H H 8.10 . 1 100 . 20 ALA HA H 4.11 . 1 101 . 20 ALA HB H 1.51 . 1 102 . 21 SER H H 8.06 . 1 103 . 21 SER HA H 4.31 . 1 104 . 21 SER HB3 H 4.02 . 2 105 . 21 SER HB2 H 3.96 . 2 106 . 22 LEU H H 8.18 . 1 107 . 22 LEU HA H 4.08 . 1 108 . 22 LEU HB3 H 1.42 . 2 109 . 22 LEU HB2 H 1.61 . 2 110 . 22 LEU HG H 1.49 . 1 111 . 22 LEU HD1 H 0.81 . 2 112 . 23 ARG H H 7.95 . 1 113 . 23 ARG HA H 4.10 . 1 114 . 23 ARG HB2 H 1.94 . 2 115 . 23 ARG HG2 H 1.59 . 2 116 . 23 ARG HE H 7.41 . 1 117 . 23 ARG HD2 H 3.18 . 2 118 . 23 ARG HD3 H 3.22 . 2 119 . 23 ARG HB3 H 1.88 . 2 120 . 23 ARG HG3 H 1.79 . 2 121 . 24 HIS H H 7.96 . 1 122 . 24 HIS HA H 4.45 . 1 123 . 24 HIS HB3 H 3.31 . 2 124 . 24 HIS HB2 H 3.24 . 2 125 . 25 TYR H H 8.15 . 1 126 . 25 TYR HA H 4.24 . 1 127 . 25 TYR HB2 H 3.07 . 2 128 . 25 TYR HD1 H 7.03 . 3 129 . 25 TYR HE1 H 6.76 . 3 130 . 26 LEU H H 8.37 . 1 131 . 26 LEU HA H 4.01 . 1 132 . 26 LEU HB2 H 1.71 . 2 133 . 26 LEU HG H 1.49 . 1 134 . 26 LEU HD1 H 0.83 . 2 135 . 27 ASN H H 8.04 . 1 136 . 27 ASN HA H 4.50 . 1 137 . 27 ASN HB2 H 2.81 . 2 138 . 27 ASN HD21 H 7.56 . 1 139 . 27 ASN HD22 H 6.89 . 1 140 . 28 LEU H H 7.77 . 1 141 . 28 LEU HA H 4.16 . 1 142 . 28 LEU HG H 1.65 . 1 143 . 28 LEU HB2 H 1.53 . 2 144 . 28 LEU HD1 H 0.78 . 2 145 . 28 LEU HD2 H 0.82 . 2 146 . 29 VAL H H 7.92 . 1 147 . 29 VAL HA H 3.97 . 1 148 . 29 VAL HB H 2.03 . 1 149 . 29 VAL HG1 H 0.80 . 1 150 . 30 THR H H 7.90 . 1 151 . 30 THR HA H 4.22 . 1 152 . 30 THR HG2 H 1.20 . 1 153 . 31 ARG H H 8.00 . 1 154 . 31 ARG HA H 4.23 . 1 155 . 31 ARG HE H 7.16 . 1 156 . 31 ARG HD2 H 3.15 . 2 157 . 31 ARG HB2 H 1.80 . 2 158 . 31 ARG HB3 H 1.85 . 2 159 . 32 GLN H H 8.19 . 1 160 . 32 GLN HA H 4.20 . 1 161 . 32 GLN HG2 H 2.31 . 2 162 . 32 GLN HB3 H 2.00 . 2 163 . 32 GLN HB2 H 1.95 . 2 164 . 32 GLN HE21 H 7.45 . 1 165 . 32 GLN HE22 H 6.82 . 1 166 . 33 ARG H H 8.30 . 1 167 . 33 ARG HA H 3.99 . 1 168 . 33 ARG HE H 7.22 . 1 169 . 33 ARG HD2 H 3.16 . 2 170 . 33 ARG HD3 H 3.12 . 2 171 . 33 ARG HB2 H 1.80 . 2 172 . 33 ARG HG2 H 1.54 . 2 173 . 34 TYR H H 8.09 . 1 174 . 34 TYR HA H 4.56 . 1 175 . 34 TYR HB3 H 3.10 . 2 176 . 34 TYR HB2 H 2.87 . 2 177 . 34 TYR HD1 H 7.13 . 3 178 . 34 TYR HE1 H 6.79 . 3 stop_ save_