data_4179 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for the Peptide H1a ; _BMRB_accession_number 4179 _BMRB_flat_file_name bmr4179.str _Entry_type original _Submission_date 1998-08-12 _Accession_date 1998-08-12 _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 Spector Shari . . 2 Rosconi Michael . . 3 Raleigh Daniel P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-23 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4180 'Loop peptide from the peripheral subunit-binding domain' stop_ _Original_release_date 1999-12-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformational Analysis of Peptide Fragments Derived from the Peripheral Subunit-binding Domain from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus: Evidence for Non-random Structure in the Unfolded State ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99169414 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Spector Shari . . 2 Rosconi Michael . . 3 Raleigh Daniel P. . stop_ _Journal_abbreviation Biopolymers _Journal_name_full Biopolymers _Journal_volume 49 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 29 _Page_last 40 _Year 1999 _Details . save_ ################################## # Molecular system description # ################################## save_system_H1a _Saveframe_category molecular_system _Mol_system_name 'helix1 from the peripheral subunit binding domain' _Abbreviation_common H1a _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'H1a trans' $H1a 'H1a cis' $H1a stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; This peptide is N-terminally acetylated and C-terminally amidated. The first residue is proline, and there is cis-trans isomerization about the acetyl-proline peptide bond. ; save_ ######################## # Monomeric polymers # ######################## save_H1a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'helix1 from the peripheral subunit binding domain' _Abbreviation_common H1a _Molecular_mass . _Mol_thiol_state . _Details ; N-terminal Proline is acetylated C-terminal Valine is amidated ; ############################## # Polymer residue sequence # ############################## _Residue_count 12 _Mol_residue_sequence PSVRKYAREKGV loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 5 PRO 2 6 SER 3 7 VAL 4 8 ARG 5 9 LYS 6 10 TYR 7 11 ALA 8 12 ARG 9 13 GLU 10 14 LYS 11 15 GLY 12 16 VAL stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2001-05-09 save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $H1a 'Bacillus stearothermophilus' 1422 Eubacteria . Bacillus stearothermophilus 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 _Details $H1a 'chemical synthesis' . . . . . 'H1a was prepared by solid phase peptide synthesis using standard Fmoc chemistry.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details 'D2O:10%/H2O:90%' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $H1a 8 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_ROESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 n/a temperature 300 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 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_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; There was a minor conformer present due to cis-trans isomerization about the N-acetyl-proline peptide bond. Chemical shifts of the NH and alpha protons are reported for Pro5-Tyr10 of the minor conformer and for the beta proton of Ser6. The remaining protons appeared to have the same chemical shift as in both the cis and the trans conformers or they were not assigned. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'H1a trans' _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 4.61 . 1 2 . 1 PRO HB2 H 1.95 . 2 3 . 1 PRO HB3 H 1.86 . 2 4 . 1 PRO HG2 H 2.10 . 1 5 . 1 PRO HG3 H 2.10 . 1 6 . 1 PRO HD2 H 2.40 . 1 7 . 1 PRO HD3 H 2.40 . 1 8 . 2 SER H H 8.38 . 1 9 . 2 SER HA H 4.35 . 1 10 . 2 SER HB2 H 3.82 . 1 11 . 2 SER HB3 H 3.82 . 1 12 . 3 VAL H H 8.03 . 1 13 . 3 VAL HA H 4.07 . 1 14 . 3 VAL HB H 2.08 . 1 15 . 3 VAL HG1 H 0.92 . 1 16 . 3 VAL HG2 H 0.92 . 1 17 . 4 ARG H H 8.31 . 1 18 . 4 ARG HA H 4.18 . 1 19 . 4 ARG HB2 H 1.57 . 2 20 . 4 ARG HB3 H 1.52 . 2 21 . 4 ARG HG2 H 1.70 . 1 22 . 4 ARG HG3 H 1.70 . 1 23 . 4 ARG HD2 H 3.14 . 2 24 . 4 ARG HD3 H 3.90 . 2 25 . 5 LYS H H 8.25 . 1 26 . 5 LYS HA H 4.17 . 1 27 . 5 LYS HB2 H 1.32 . 2 28 . 5 LYS HB3 H 1.23 . 2 29 . 5 LYS HG2 H 1.65 . 1 30 . 5 LYS HG3 H 1.65 . 1 31 . 5 LYS HD2 H 2.93 . 1 32 . 5 LYS HD3 H 2.93 . 1 33 . 6 TYR H H 8.19 . 1 34 . 6 TYR HA H 4.41 . 1 35 . 6 TYR HB2 H 3.05 . 2 36 . 6 TYR HB3 H 2.89 . 2 37 . 7 ALA H H 8.20 . 1 38 . 7 ALA HA H 4.21 . 1 39 . 7 ALA HB H 1.36 . 1 40 . 8 ARG H H 8.24 . 1 41 . 8 ARG HA H 4.18 . 1 42 . 8 ARG HB2 H 1.63 . 1 43 . 8 ARG HB3 H 1.63 . 1 44 . 8 ARG HG2 H 1.83 . 2 45 . 8 ARG HG3 H 1.76 . 2 46 . 8 ARG HD2 H 4.08 . 2 47 . 8 ARG HD3 H 3.19 . 2 48 . 8 ARG HE H 7.20 . 1 49 . 9 GLU H H 8.48 . 1 50 . 9 GLU HA H 4.23 . 1 51 . 9 GLU HB2 H 1.97 . 1 52 . 9 GLU HB3 H 1.97 . 1 53 . 9 GLU HG2 H 2.29 . 2 54 . 9 GLU HG3 H 2.06 . 2 55 . 10 LYS H H 8.40 . 1 56 . 10 LYS HA H 4.21 . 1 57 . 10 LYS HB2 H 1.80 . 1 58 . 10 LYS HB3 H 1.80 . 1 59 . 10 LYS HG2 H 1.67 . 2 60 . 10 LYS HG3 H 1.44 . 2 61 . 10 LYS HD2 H 2.97 . 1 62 . 10 LYS HD3 H 2.97 . 1 63 . 10 LYS HE2 H 3.92 . 1 64 . 10 LYS HE3 H 3.92 . 1 65 . 11 GLY H H 8.41 . 1 66 . 11 GLY HA2 H 3.93 . 1 67 . 11 GLY HA3 H 3.93 . 1 68 . 12 VAL H H 7.97 . 1 69 . 12 VAL HA H 4.07 . 1 70 . 12 VAL HB H 2.09 . 1 71 . 12 VAL HG1 H 0.94 . 1 72 . 12 VAL HG2 H 0.94 . 1 stop_ save_ save_assigned_chemical_shifts_two _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'H1a cis' _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 3.53 . 1 2 . 1 PRO HB2 H 1.95 . 2 3 . 1 PRO HB3 H 1.86 . 2 4 . 1 PRO HG2 H 2.10 . 1 5 . 1 PRO HG3 H 2.10 . 1 6 . 1 PRO HD2 H 2.40 . 1 7 . 1 PRO HD3 H 2.40 . 1 8 . 2 SER H H 8.56 . 1 9 . 2 SER HA H 4.40 . 1 10 . 2 SER HB2 H 3.84 . 1 11 . 2 SER HB3 H 3.84 . 1 12 . 3 VAL H H 8.22 . 1 13 . 3 VAL HA H 4.09 . 1 14 . 4 ARG H H 8.37 . 1 15 . 4 ARG HA H 4.21 . 1 16 . 5 LYS H H 8.28 . 1 17 . 5 LYS HA H 4.19 . 1 18 . 6 TYR H H 8.21 . 1 19 . 6 TYR HA H 4.43 . 1 stop_ save_