data_20028 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structures of 1-15 peptide fragment of Statherin ; _BMRB_accession_number 20028 _BMRB_flat_file_name bmr20028.str _Entry_type new _Submission_date 2008-06-29 _Accession_date 2008-06-29 _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 Guo Syuan-Ming . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-02-14 update BMRB 'PDBj annotated the coordinate file' 2010-06-03 update BMRB 'edit entity/assembly name' 2008-07-17 update author 'update the residue' 2008-07-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_1 _Saveframe_category entry_citation _Citation_full . _Citation_title . _Citation_status 'in preparation' _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 Guo Syuan-Ming . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Statherin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity entity_2 $entity entity_3 $entity entity_4 $entity entity_5 $entity entity_6 $entity entity_7 $entity entity_8 $entity entity_9 $entity entity_10 $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Statherin _Molecular_mass 1958 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence DXXEEKFLRRIGRFG loop_ _Residue_seq_code _Residue_label 1 ASP 2 SEP 3 SEP 4 GLU 5 GLU 6 LYS 7 PHE 8 LEU 9 ARG 10 ARG 11 ILE 12 GLY 13 ARG 14 PHE 15 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOSERINE _BMRB_code . _PDB_code SEP _Standard_residue_derivative SEP _Molecular_mass 185.072 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 20:49:03 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N N 0 . ? CA CA C S 0 . ? CB CB C N 0 . ? OG OG O N 0 . ? C C C N 0 . ? O O O N 0 . ? OXT OXT O N 0 . ? P P P N 0 . ? O1P O1P O N 0 . ? O2P O2P O N 0 . ? O3P O3P O N 0 . ? H H H N 0 . ? H2 H2 H N 0 . ? HA HA H N 0 . ? HB2 HB2 H N 0 . ? HB3 HB3 H N 0 . ? HXT HXT H N 0 . ? HOP2 HOP2 H N 0 . ? HOP3 HOP3 H N 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 CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 $entity 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $entity . mM 1 3 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _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_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 6 . pH stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 TMS H 1 'methyl protons' ppm 0 external 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D DQF-COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity_1 _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 1 ASP HA H 4.206 0.01 1 2 1 1 ASP HB2 H 2.847 0.01 2 3 1 1 ASP HB3 H 2.806 0.01 2 4 2 2 SEP HA H 4.443 0.01 1 5 2 2 SEP HB2 H 4.058 0.01 2 6 2 2 SEP HB3 H 4.041 0.01 2 7 3 3 SEP H H 8.816 0.01 1 8 3 3 SEP HA H 4.285 0.01 1 9 3 3 SEP HB2 H 4.044 0.01 2 10 3 3 SEP HB3 H 4.050 0.01 2 11 4 4 GLU H H 8.309 0.01 1 12 4 4 GLU HA H 4.103 0.01 1 13 4 4 GLU HB2 H 1.987 0.01 2 14 4 4 GLU HB3 H 1.975 0.01 2 15 4 4 GLU HG2 H 2.219 0.01 2 16 4 4 GLU HG3 H 2.206 0.01 2 17 5 5 GLU H H 8.092 0.01 1 18 5 5 GLU HA H 3.982 0.01 1 19 5 5 GLU HB2 H 1.940 0.01 2 20 5 5 GLU HB3 H 1.928 0.01 2 21 5 5 GLU HG2 H 2.163 0.01 2 22 5 5 GLU HG3 H 2.148 0.01 2 23 6 6 LYS H H 7.939 0.01 1 24 6 6 LYS HA H 3.929 0.01 1 25 6 6 LYS HB2 H 1.659 0.01 2 26 6 6 LYS HB3 H 1.659 0.01 2 27 6 6 LYS HD2 H 1.502 0.01 2 28 6 6 LYS HD3 H 1.502 0.01 2 29 6 6 LYS HE2 H 2.812 0.01 2 30 6 6 LYS HE3 H 2.812 0.01 2 31 6 6 LYS HG2 H 1.305 0.01 2 32 6 6 LYS HG3 H 1.204 0.01 2 33 7 7 PHE H H 7.850 0.01 1 34 7 7 PHE HA H 4.328 0.01 1 35 7 7 PHE HB2 H 3.123 0.01 2 36 7 7 PHE HB3 H 3.041 0.01 2 37 7 7 PHE HD1 H 7.139 0.01 3 38 8 8 LEU H H 8.024 0.01 1 39 8 8 LEU HA H 3.977 0.01 1 40 8 8 LEU HB2 H 1.663 0.01 2 41 8 8 LEU HB3 H 1.639 0.01 2 42 8 8 LEU HD1 H 0.780 0.01 2 43 8 8 LEU HG H 1.387 0.01 1 44 9 9 ARG H H 7.957 0.01 1 45 9 9 ARG HA H 4.097 0.01 1 46 9 9 ARG HB2 H 1.726 0.01 2 47 9 9 ARG HB3 H 1.705 0.01 2 48 9 9 ARG HD2 H 3.043 0.01 2 49 9 9 ARG HD3 H 3.043 0.01 2 50 9 9 ARG HE H 7.263 0.01 1 51 9 9 ARG HG2 H 1.476 0.01 2 52 9 9 ARG HG3 H 1.476 0.01 2 53 10 10 ARG H H 7.899 0.01 1 54 10 10 ARG HA H 4.127 0.01 1 55 10 10 ARG HB2 H 1.726 0.01 2 56 10 10 ARG HB3 H 1.696 0.01 2 57 10 10 ARG HD2 H 3.033 0.01 2 58 10 10 ARG HD3 H 3.033 0.01 2 59 10 10 ARG HE H 7.150 0.01 1 60 10 10 ARG HG2 H 1.485 0.01 2 61 10 10 ARG HG3 H 1.485 0.01 2 62 11 11 ILE H H 7.843 0.01 1 63 11 11 ILE HA H 4.069 0.01 1 64 11 11 ILE HB H 1.765 0.01 1 65 11 11 ILE HD1 H 0.724 0.01 1 66 11 11 ILE HG12 H 1.278 0.01 2 67 11 11 ILE HG13 H 1.240 0.01 2 68 11 11 ILE HG2 H 1.058 0.01 1 69 12 12 GLY H H 8.097 0.01 1 70 12 12 GLY HA2 H 3.803 0.01 2 71 12 12 GLY HA3 H 3.785 0.01 2 72 13 13 ARG H H 7.925 0.01 1 73 13 13 ARG HA H 4.140 0.01 1 74 13 13 ARG HB2 H 1.522 0.01 2 75 13 13 ARG HB3 H 1.452 0.01 2 76 13 13 ARG HD2 H 2.964 0.01 2 77 13 13 ARG HD3 H 2.964 0.01 2 78 13 13 ARG HE H 7.045 0.01 1 79 13 13 ARG HG2 H 1.270 0.01 2 80 13 13 ARG HG3 H 1.270 0.01 2 81 14 14 PHE H H 8.164 0.01 1 82 14 14 PHE HA H 4.589 0.01 1 83 14 14 PHE HB2 H 3.116 0.01 2 84 14 14 PHE HB3 H 2.798 0.01 2 85 14 14 PHE HD1 H 7.149 0.01 3 86 15 15 GLY H H 7.759 0.01 1 87 15 15 GLY HA2 H 3.677 0.01 2 88 15 15 GLY HA3 H 3.548 0.01 2 stop_ save_