data_2202 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin ; _BMRB_accession_number 2202 _BMRB_flat_file_name bmr2202.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 Precheur Benedicte . . 2 Munier Helene . . 3 Mispelter Joel . . 4 Barzu Octavian . . 5 Craescu Constantin T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 139 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-10 revision BMRB 'Updating non-standard residure' 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 ; Precheur, Benedicte, Munier, Helene, Mispelter, Joel, Barzu, Octavian, Craescu, Constantin T., "1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin," Biochemistry 31 (1), 229-236 (1992). ; _Citation_title ; 1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin ; _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 Precheur Benedicte . . 2 Munier Helene . . 3 Mispelter Joel . . 4 Barzu Octavian . . 5 Craescu Constantin T. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 31 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 229 _Page_last 236 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_amphiphilic_alpha-helix_peptide_Baa17 _Saveframe_category molecular_system _Mol_system_name 'amphiphilic alpha-helix peptide Baa17' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'amphiphilic alpha-helix peptide Baa17' $amphiphilic_alpha-helix_peptide_Baa17 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_amphiphilic_alpha-helix_peptide_Baa17 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'amphiphilic alpha-helix peptide Baa17' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence XLKWKKLLKLLKKLLKLX loop_ _Residue_seq_code _Residue_label 1 ACE 2 LEU 3 LYS 4 TRP 5 LYS 6 LYS 7 LEU 8 LEU 9 LYS 10 LEU 11 LEU 12 LYS 13 LYS 14 LEU 15 LEU 16 LYS 17 LEU 18 GM1 stop_ _Sequence_homology_query_date 2007-10-08 _Sequence_homology_query_revised_last_date 2007-10-08 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 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_GM1 _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common AMINOMETHYLAMIDE _BMRB_code GM1 _PDB_code GM1 _Standard_residue_derivative . _Molecular_mass 74.082 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? N1 N1 N . 0 . ? O1 O1 O . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 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 C1 N1 ? ? DOUB C1 O1 ? ? SING C1 C2 ? ? SING N1 HN11 ? ? SING N1 HN12 ? ? SING C2 N2 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $amphiphilic_alpha-helix_peptide_Baa17 . . . . . . 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 $amphiphilic_alpha-helix_peptide_Baa17 '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 unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' 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 6.3 . n/a 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 . 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_citation_label _Correction_value_citation_label DSS H . . ppm 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_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 'amphiphilic alpha-helix peptide Baa17' _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 . 2 LEU H H 8.22 . 1 2 . 2 LEU HA H 4.1 . 1 3 . 2 LEU HB2 H 1.5 . 1 4 . 2 LEU HB3 H 1.5 . 1 5 . 2 LEU HG H 1.37 . 1 6 . 2 LEU HD1 H .76 . 2 7 . 2 LEU HD2 H .82 . 2 8 . 3 LYS H H 8.33 . 1 9 . 3 LYS HA H 4.12 . 1 10 . 3 LYS HB2 H 1.61 . 1 11 . 3 LYS HB3 H 1.61 . 1 12 . 3 LYS HG2 H 1.12 . 2 13 . 3 LYS HG3 H 1.17 . 2 14 . 3 LYS HD2 H 1.47 . 1 15 . 3 LYS HD3 H 1.47 . 1 16 . 3 LYS HE2 H 2.78 . 1 17 . 3 LYS HE3 H 2.78 . 1 18 . 4 TRP H H 7.9 . 1 19 . 4 TRP HA H 4.3 . 1 20 . 4 TRP HB2 H 3.19 . 1 21 . 4 TRP HB3 H 3.19 . 1 22 . 4 TRP HD1 H 7.23 . 1 23 . 4 TRP HE1 H 10.24 . 1 24 . 4 TRP HE3 H 7.3 . 1 25 . 4 TRP HZ2 H 7.33 . 1 26 . 4 TRP HZ3 H 6.75 . 1 27 . 4 TRP HH2 H 6.94 . 1 28 . 5 LYS H H 7.95 . 1 29 . 5 LYS HA H 3.76 . 1 30 . 5 LYS HB2 H 1.75 . 1 31 . 5 LYS HB3 H 1.75 . 1 32 . 5 LYS HG2 H 1.2 . 2 33 . 5 LYS HG3 H 1.34 . 2 34 . 5 LYS HD2 H 1.6 . 1 35 . 5 LYS HD3 H 1.6 . 1 36 . 5 LYS HE2 H 2.9 . 1 37 . 5 LYS HE3 H 2.9 . 1 38 . 6 LYS H H 7.63 . 1 39 . 6 LYS HA H 3.92 . 1 40 . 6 LYS HB2 H 1.83 . 2 41 . 6 LYS HB3 H 1.74 . 2 42 . 6 LYS HG2 H 1.3 . 2 43 . 6 LYS HG3 H 1.47 . 2 44 . 6 LYS HD2 H 1.58 . 1 45 . 6 LYS HD3 H 1.58 . 1 46 . 6 LYS HE2 H 2.85 . 1 47 . 6 LYS HE3 H 2.85 . 1 48 . 7 LEU H H 7.77 . 1 49 . 7 LEU HA H 3.93 . 1 50 . 7 LEU HB2 H 1.75 . 1 51 . 7 LEU HB3 H 1.75 . 1 52 . 7 LEU HG H 1.52 . 1 53 . 7 LEU HD1 H .7 . 2 54 . 7 LEU HD2 H .77 . 2 55 . 8 LEU H H 8.19 . 1 56 . 8 LEU HA H 3.77 . 1 57 . 8 LEU HB2 H 1.55 . 1 58 . 8 LEU HB3 H 1.55 . 1 59 . 8 LEU HG H 1.51 . 1 60 . 8 LEU HD1 H .72 . 2 61 . 8 LEU HD2 H .76 . 2 62 . 9 LYS H H 7.55 . 1 63 . 9 LYS HA H 3.81 . 1 64 . 9 LYS HB2 H 1.83 . 1 65 . 9 LYS HB3 H 1.83 . 1 66 . 9 LYS HG2 H 1.31 . 2 67 . 9 LYS HG3 H 1.51 . 2 68 . 9 LYS HD2 H 1.6 . 1 69 . 9 LYS HD3 H 1.6 . 1 70 . 9 LYS HE2 H 2.88 . 1 71 . 9 LYS HE3 H 2.88 . 1 72 . 10 LEU H H 7.64 . 1 73 . 10 LEU HA H 4.02 . 1 74 . 10 LEU HB2 H 1.75 . 1 75 . 10 LEU HB3 H 1.75 . 1 76 . 10 LEU HG H 1.6 . 1 77 . 10 LEU HD1 H .78 . 2 78 . 10 LEU HD2 H .82 . 2 79 . 11 LEU H H 8.44 . 1 80 . 11 LEU HA H 3.83 . 1 81 . 11 LEU HB2 H 1.71 . 2 82 . 11 LEU HB3 H 1.75 . 2 83 . 11 LEU HG H 1.39 . 1 84 . 11 LEU HD1 H .71 . 2 85 . 11 LEU HD2 H .74 . 2 86 . 12 LYS H H 8.16 . 1 87 . 12 LYS HA H 3.68 . 1 88 . 12 LYS HB2 H 1.72 . 2 89 . 12 LYS HB3 H 1.67 . 2 90 . 12 LYS HG2 H 1.39 . 2 91 . 12 LYS HG3 H 1.09 . 2 92 . 12 LYS HD2 H 1.47 . 1 93 . 12 LYS HD3 H 1.47 . 1 94 . 12 LYS HE2 H 2.92 . 1 95 . 12 LYS HE3 H 2.92 . 1 96 . 13 LYS H H 7.47 . 1 97 . 13 LYS HA H 4.01 . 1 98 . 13 LYS HB2 H 1.88 . 1 99 . 13 LYS HB3 H 1.88 . 1 100 . 13 LYS HG2 H 1.5 . 2 101 . 13 LYS HG3 H 1.34 . 2 102 . 13 LYS HD2 H 1.59 . 1 103 . 13 LYS HD3 H 1.59 . 1 104 . 13 LYS HE2 H 2.86 . 1 105 . 13 LYS HE3 H 2.86 . 1 106 . 14 LEU H H 8.16 . 1 107 . 14 LEU HA H 3.99 . 1 108 . 14 LEU HB2 H 1.7 . 1 109 . 14 LEU HB3 H 1.7 . 1 110 . 14 LEU HG H 1.47 . 1 111 . 14 LEU HD1 H .7 . 2 112 . 14 LEU HD2 H .73 . 2 113 . 15 LEU H H 7.89 . 1 114 . 15 LEU HA H 4.11 . 1 115 . 15 LEU HB2 H 1.68 . 1 116 . 15 LEU HB3 H 1.68 . 1 117 . 15 LEU HG H 1.68 . 1 118 . 15 LEU HD1 H .69 . 2 119 . 15 LEU HD2 H .74 . 2 120 . 16 LYS H H 7.53 . 1 121 . 16 LYS HA H 4.07 . 1 122 . 16 LYS HB2 H 1.87 . 1 123 . 16 LYS HB3 H 1.87 . 1 124 . 16 LYS HG2 H 1.41 . 2 125 . 16 LYS HG3 H 1.35 . 2 126 . 16 LYS HD2 H 1.61 . 1 127 . 16 LYS HD3 H 1.61 . 1 128 . 16 LYS HE2 H 2.94 . 1 129 . 16 LYS HE3 H 2.94 . 1 130 . 17 LEU H H 7.89 . 1 131 . 17 LEU HA H 3.68 . 1 132 . 17 LEU HB2 H 1.59 . 1 133 . 17 LEU HB3 H 1.59 . 1 134 . 17 LEU HG H 1.58 . 1 135 . 17 LEU HD1 H .76 . 2 136 . 17 LEU HD2 H .69 . 2 137 . 18 GM1 HN11 H 7.77 . 1 138 . 18 GM1 H21 H 3.62 . 2 139 . 18 GM1 H22 H 3.69 . 2 stop_ save_