data_1445 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance ; _BMRB_accession_number 1445 _BMRB_flat_file_name bmr1445.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _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 Bradley Erin K. . 2 Thomason John F. . 3 Cohen Fred E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 revision BMRB 'updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Bradley, Erin K., Thomason, John F., Cohen, Fred E., "Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance," J. Mol. Biol. 215, 607-622 (1990). ; _Citation_title ; Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance ; _Citation_status published _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 Bradley Erin K. . 2 Thomason John F. . 3 Cohen Fred E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 215 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 607 _Page_last 622 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_designed_helical_protein _Saveframe_category molecular_system _Mol_system_name 'designed helical protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'designed helical protein' $designed_helical_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_designed_helical_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'designed helical protein' _Name_variant 'N,C-terminal-blocked (i+4) designed helical protein' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 19 _Mol_residue_sequence XETGTKAELLAKYEATHKX loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ACE 2 2 GLU 3 3 THR 4 4 GLY 5 5 THR 6 6 LYS 7 7 ALA 8 8 GLU 9 9 LEU 10 10 LEU 11 11 ALA 12 12 LYS 13 13 TYR 14 14 GLU 15 15 ALA 16 16 THR 17 17 HIS 18 18 LYS 19 19 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2007-10-08 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 1446 'designed helical protein' 100.00 17 100 100 2.9 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYL GROUP' _BMRB_code ACE _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? O O O . 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ 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 HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? N N 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 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 $designed_helical_protein . . . . . . 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 $designed_helical_protein 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength . _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2 . na temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_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 . . ppm 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'designed helical protein' _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 ACE H1 H 2.04 . 1 2 . 1 ACE H2 H 2.04 . 1 3 . 1 ACE H3 H 2.04 . 1 4 . 2 GLU H H 8.55 . 1 5 . 2 GLU HA H 4.4 . 1 6 . 2 GLU HB2 H 2.14 . 2 7 . 2 GLU HB3 H 2.05 . 2 8 . 2 GLU HG2 H 2.52 . 1 9 . 2 GLU HG3 H 2.52 . 1 10 . 3 THR H H 8.38 . 1 11 . 3 THR HA H 4.41 . 1 12 . 3 THR HB H 4.28 . 1 13 . 3 THR HG2 H 1.23 . 1 14 . 4 GLY H H 8.54 . 1 15 . 4 GLY HA2 H 4.07 . 1 16 . 4 GLY HA3 H 4.07 . 1 17 . 5 THR H H 8.06 . 1 18 . 5 THR HA H 4.31 . 1 19 . 5 THR HB H 4.42 . 1 20 . 5 THR HG2 H 1.26 . 1 21 . 6 LYS H H 8.68 . 1 22 . 6 LYS HA H 4.07 . 1 23 . 6 LYS HB2 H 1.86 . 1 24 . 6 LYS HB3 H 1.86 . 1 25 . 6 LYS HG2 H 1.42 . 1 26 . 6 LYS HG3 H 1.42 . 1 27 . 6 LYS HD2 H 1.72 . 1 28 . 6 LYS HD3 H 1.72 . 1 29 . 6 LYS HE2 H 3 . 1 30 . 6 LYS HE3 H 3 . 1 31 . 6 LYS HZ H 7.62 . 1 32 . 7 ALA H H 8.43 . 1 33 . 7 ALA HA H 4.16 . 1 34 . 7 ALA HB H 1.42 . 1 35 . 8 GLU H H 8.08 . 1 36 . 8 GLU HA H 4.19 . 1 37 . 8 GLU HB2 H 2.18 . 1 38 . 8 GLU HB3 H 2.18 . 1 39 . 8 GLU HG2 H 2.55 . 1 40 . 8 GLU HG3 H 2.55 . 1 41 . 9 LEU H H 8.36 . 1 42 . 9 LEU HA H 4.14 . 1 43 . 9 LEU HB2 H 1.56 . 2 44 . 9 LEU HB3 H 1.83 . 2 45 . 9 LEU HG H 1.73 . 1 46 . 9 LEU HD1 H 0.89 . 1 47 . 9 LEU HD2 H 0.89 . 1 48 . 10 LEU H H 8.13 . 1 49 . 10 LEU HA H 4.32 . 1 50 . 10 LEU HB2 H 1.74 . 1 51 . 10 LEU HB3 H 1.74 . 1 52 . 10 LEU HG H 1.67 . 1 53 . 10 LEU HD1 H 0.89 . 2 54 . 10 LEU HD2 H 0.95 . 2 55 . 11 ALA H H 8.05 . 1 56 . 11 ALA HA H 4.19 . 1 57 . 11 ALA HB H 1.49 . 1 58 . 12 LYS H H 8.05 . 1 59 . 12 LYS HA H 4.19 . 1 60 . 12 LYS HB2 H 1.91 . 1 61 . 12 LYS HB3 H 1.91 . 1 62 . 12 LYS HG2 H 1.44 . 1 63 . 12 LYS HG3 H 1.44 . 1 64 . 12 LYS HD2 H 1.71 . 1 65 . 12 LYS HD3 H 1.71 . 1 66 . 12 LYS HE2 H 2.99 . 1 67 . 12 LYS HE3 H 2.99 . 1 68 . 12 LYS HZ H 7.64 . 1 69 . 13 TYR H H 8.23 . 1 70 . 13 TYR HA H 4.31 . 1 71 . 13 TYR HB2 H 3.16 . 2 72 . 13 TYR HB3 H 3.24 . 2 73 . 13 TYR HD1 H 7.04 . 1 74 . 13 TYR HD2 H 7.04 . 1 75 . 13 TYR HE1 H 6.62 . 1 76 . 13 TYR HE2 H 6.62 . 1 77 . 14 GLU H H 8.73 . 1 78 . 14 GLU HA H 4.14 . 1 79 . 14 GLU HB2 H 2.16 . 1 80 . 14 GLU HB3 H 2.16 . 1 81 . 14 GLU HG2 H 2.67 . 1 82 . 14 GLU HG3 H 2.67 . 1 83 . 15 ALA H H 8.01 . 1 84 . 15 ALA HA H 4.24 . 1 85 . 15 ALA HB H 1.53 . 1 86 . 16 THR H H 7.73 . 1 87 . 16 THR HA H 4.31 . 1 88 . 16 THR HB H 4.21 . 1 89 . 16 THR HG2 H 1.19 . 1 90 . 17 HIS H H 7.96 . 1 91 . 17 HIS HA H 4.63 . 1 92 . 17 HIS HB2 H 2.75 . 2 93 . 17 HIS HB3 H 3.17 . 2 94 . 17 HIS HD2 H 7.16 . 1 95 . 17 HIS HE1 H 8.41 . 1 96 . 18 LYS H H 8.32 . 1 97 . 18 LYS HA H 4.28 . 1 98 . 18 LYS HB2 H 1.84 . 2 99 . 18 LYS HB3 H 1.78 . 2 100 . 18 LYS HG2 H 1.46 . 1 101 . 18 LYS HG3 H 1.46 . 1 102 . 18 LYS HD2 H 1.7 . 1 103 . 18 LYS HD3 H 1.7 . 1 104 . 18 LYS HE2 H 3 . 1 105 . 18 LYS HE3 H 3 . 1 106 . 18 LYS HZ H 7.58 . 1 stop_ save_