data_3404 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A Single-Stranded Amphiphatic alpha-Helix in Aqueous Solution: Design, Structural Characterization, and Its Application for Determining alpha-Helical Propensities of Amino Acids ; _BMRB_accession_number 3404 _BMRB_flat_file_name bmr3404.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Zhou Nian E. . 2 Kay Cyril M. . 3 Sykes Brian D. . 4 Hodges Robert S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 107 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' 1996-03-25 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' 2008-03-24 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Zhou, Nian E., Kay, Cyril M., Sykes, Brian D., Hodges, Robert S., "A Single-Stranded Amphiphatic alpha-Helix in Aqueous Solution: Design, Structural Characterization, and Its Application for Determining alpha-Helical Propensities of Amino Acids," Biochem. J. 32 (24), 6190-6197 (1993). ; _Citation_title ; A Single-Stranded Amphiphatic alpha-Helix in Aqueous Solution: Design, Structural Characterization, and Its Application for Determining alpha-Helical Propensities of Amino Acids ; _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 Zhou Nian E. . 2 Kay Cyril M. . 3 Sykes Brian D. . 4 Hodges Robert S. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 32 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6190 _Page_last 6197 _Year 1993 _Details . save_ ################################## # Molecular system description # ################################## save_system_amphipathic_alpha_helix_peptide _Saveframe_category molecular_system _Mol_system_name 'amphipathic alpha helix peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'amphipathic alpha helix peptide' $amphipathic_alpha_helix_peptide stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_amphipathic_alpha_helix_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'amphipathic alpha helix peptide' _Name_variant 'synthetic design' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 19 _Mol_residue_sequence XAEKAAKEAEKAAKEAEKX loop_ _Residue_seq_code _Residue_label 1 NLG 2 ALA 3 GLU 4 LYS 5 ALA 6 ALA 7 LYS 8 GLU 9 ALA 10 GLU 11 LYS 12 ALA 13 ALA 14 LYS 15 GLU 16 ALA 17 GLU 18 LYS 19 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_NLG _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common N-ACETYL-L-GLUTAMATE _BMRB_code NLG _PDB_code NLG _Standard_residue_derivative . _Molecular_mass 189.166 _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 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CD CD C . 0 . ? CG CG C . 0 . ? H2 H2 H . 0 . ? H8C1 H8C1 H . 0 . ? H8C2 H8C2 H . 0 . ? H8C3 H8C3 H . 0 . ? HA HA H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HE2 HE2 H . 0 . ? HGC1 HGC1 H . 0 . ? HGC2 HGC2 H . 0 . ? HXT HXT H . 0 . ? N2 N2 N . 0 . ? O O O . 0 . ? O7 O7 O . 0 . ? OE1 OE1 O . 0 . ? OE2 OE2 O . 0 . ? OXT OXT 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 SING CA C ? ? SING CA CB ? ? SING CA N2 ? ? SING CA HA ? ? SING C OXT ? ? DOUB C O ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HBC1 ? ? SING CB HBC2 ? ? SING CG CD ? ? SING CG HGC1 ? ? SING CG HGC2 ? ? DOUB CD OE1 ? ? SING CD OE2 ? ? SING OE2 HE2 ? ? SING C7 C8 ? ? DOUB C7 O7 ? ? SING C7 N2 ? ? SING C8 H8C1 ? ? SING C8 H8C2 ? ? SING C8 H8C3 ? ? SING N2 H2 ? ? 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 $amphipathic_alpha_helix_peptide . . . . . . 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 $amphipathic_alpha_helix_peptide '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_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details 'The chemical shift reference is not available at this time.' 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 . H 1 . ppm . . . . . . 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 'amphipathic alpha helix peptide' _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 NLG H2 H 8.46 . 1 2 . 1 NLG HA H 4.15 . 1 3 . 1 NLG HBC1 H 2.13 . 2 4 . 1 NLG HBC2 H 2.05 . 2 5 . 1 NLG HGC1 H 2.42 . 1 6 . 1 NLG HGC2 H 2.42 . 1 7 . 2 ALA H H 8.43 . 1 8 . 2 ALA HA H 4.19 . 1 9 . 2 ALA HB H 1.48 . 1 10 . 3 GLU H H 8.29 . 1 11 . 3 GLU HA H 4.11 . 1 12 . 3 GLU HB2 H 2.16 . 2 13 . 3 GLU HB3 H 2.09 . 2 14 . 3 GLU HG2 H 2.38 . 1 15 . 3 GLU HG3 H 2.38 . 1 16 . 4 LYS H H 7.84 . 1 17 . 4 LYS HA H 4.05 . 1 18 . 4 LYS HB2 H 1.97 . 1 19 . 4 LYS HB3 H 1.97 . 1 20 . 4 LYS HG2 H 1.76 . 1 21 . 4 LYS HG3 H 1.76 . 1 22 . 4 LYS HD2 H 1.58 . 2 23 . 4 LYS HD3 H 1.46 . 2 24 . 4 LYS HE2 H 3.01 . 1 25 . 4 LYS HE3 H 3.01 . 1 26 . 5 ALA H H 8.14 . 1 27 . 5 ALA HA H 4.16 . 1 28 . 5 ALA HB H 1.54 . 1 29 . 6 ALA H H 8.09 . 1 30 . 6 ALA HA H 4.19 . 1 31 . 6 ALA HB H 1.57 . 1 32 . 7 LYS H H 8.11 . 1 33 . 7 LYS HA H 4.15 . 1 34 . 7 LYS HB2 H 2.09 . 2 35 . 7 LYS HB3 H 1.96 . 2 36 . 7 LYS HG2 H 1.76 . 1 37 . 7 LYS HG3 H 1.76 . 1 38 . 7 LYS HD2 H 1.58 . 1 39 . 7 LYS HD3 H 1.58 . 1 40 . 7 LYS HE2 H 3.01 . 1 41 . 7 LYS HE3 H 3.01 . 1 42 . 8 GLU H H 8.35 . 1 43 . 8 GLU HA H 4.14 . 1 44 . 8 GLU HB2 H 2.23 . 1 45 . 8 GLU HB3 H 2.23 . 1 46 . 8 GLU HG2 H 2.51 . 2 47 . 8 GLU HG3 H 2.43 . 2 48 . 9 ALA H H 8.25 . 1 49 . 9 ALA HA H 4.21 . 1 50 . 9 ALA HB H 1.58 . 1 51 . 10 GLU H H 8.12 . 1 52 . 10 GLU HA H 4.06 . 1 53 . 10 GLU HB2 H 2.24 . 1 54 . 10 GLU HB3 H 2.24 . 1 55 . 10 GLU HG2 H 2.5 . 1 56 . 10 GLU HG3 H 2.5 . 1 57 . 11 LYS H H 8 . 1 58 . 11 LYS HA H 4.01 . 1 59 . 11 LYS HB2 H 2.02 . 1 60 . 11 LYS HB3 H 2.02 . 1 61 . 11 LYS HG2 H 1.63 . 1 62 . 11 LYS HG3 H 1.63 . 1 63 . 11 LYS HD2 H 1.47 . 1 64 . 11 LYS HD3 H 1.47 . 1 65 . 11 LYS HE2 H 3.01 . 1 66 . 11 LYS HE3 H 3.01 . 1 67 . 12 ALA H H 8.19 . 1 68 . 12 ALA HA H 4.17 . 1 69 . 12 ALA HB H 1.57 . 1 70 . 13 ALA H H 8.12 . 1 71 . 13 ALA HA H 4.16 . 1 72 . 13 ALA HB H 1.55 . 1 73 . 14 LYS H H 8.11 . 1 74 . 14 LYS HA H 4.15 . 1 75 . 14 LYS HB2 H 2.05 . 2 76 . 14 LYS HB3 H 1.97 . 2 77 . 14 LYS HG2 H 1.76 . 1 78 . 14 LYS HG3 H 1.76 . 1 79 . 14 LYS HD2 H 1.62 . 2 80 . 14 LYS HD3 H 1.46 . 2 81 . 14 LYS HE2 H 3.01 . 1 82 . 14 LYS HE3 H 3.01 . 1 83 . 15 GLU H H 8.22 . 1 84 . 15 GLU HA H 4.15 . 1 85 . 15 GLU HB2 H 2.18 . 1 86 . 15 GLU HB3 H 2.18 . 1 87 . 15 GLU HG2 H 2.51 . 2 88 . 15 GLU HG3 H 2.41 . 2 89 . 16 ALA H H 8 . 1 90 . 16 ALA HA H 4.23 . 1 91 . 16 ALA HB H 1.56 . 1 92 . 17 GLU H H 7.87 . 1 93 . 17 GLU HA H 4.2 . 1 94 . 17 GLU HB2 H 2.2 . 1 95 . 17 GLU HB3 H 2.2 . 1 96 . 17 GLU HG2 H 2.53 . 2 97 . 17 GLU HG3 H 2.41 . 2 98 . 18 LYS H H 7.76 . 1 99 . 18 LYS HA H 4.25 . 1 100 . 18 LYS HB2 H 1.94 . 1 101 . 18 LYS HB3 H 1.94 . 1 102 . 18 LYS HG2 H 1.76 . 1 103 . 18 LYS HG3 H 1.76 . 1 104 . 18 LYS HD2 H 1.63 . 2 105 . 18 LYS HD3 H 1.54 . 2 106 . 18 LYS HE2 H 3.01 . 1 107 . 18 LYS HE3 H 3.01 . 1 stop_ save_