data_4724 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding ; _BMRB_accession_number 4724 _BMRB_flat_file_name bmr4724.str _Entry_type original _Submission_date 2000-04-20 _Accession_date 2000-04-27 _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 Montserret Roland . . 2 'Mc Leish' Michael J. . 3 Bockmann Anja . . 4 Geourjon Christophe . . 5 Penin Francois . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 "13C chemical shifts" 86 "coupling constants" 10 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4723 'acidic form' stop_ _Original_release_date 2000-05-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding ; _Citation_status submitted _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 Montserret Roland . . 2 'Mc Leish' Michael J. . 3 Bockmann Anja . . 4 Geourjon Christophe . . 5 Penin Francois . . stop_ _Journal_abbreviation Biochemistry _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 2000 _Details . loop_ _Keyword 'Circular Dichroism' 'electrostatic interactions' 'NMR spectroscopy' 'peptide structure' 'Sodium dodecyl sulfate' stop_ save_ ################################## # Molecular system description # ################################## save_system_basic _Saveframe_category molecular_system _Mol_system_name 'basic peptide' _Abbreviation_common basic _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'basic peptide' $basic stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_basic _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'basic peptide' _Abbreviation_common basic _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 15 _Mol_residue_sequence QAPAYKKAAKKLAES loop_ _Residue_seq_code _Residue_label 1 GLN 2 ALA 3 PRO 4 ALA 5 TYR 6 LYS 7 LYS 8 ALA 9 ALA 10 LYS 11 LYS 12 LEU 13 ALA 14 GLU 15 SER stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-03-03 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 PDB 1DJF 'A Chain A, Nmr Structure Of A ModelHydrophilic Amphipathic Helical Basic Peptide' 100.00 15 100 100 9.4 PDB 1DN3 'A Chain A, Nmr Structure Of A ModelHydrophilic Amphipathic Helical Basic Peptide' 100.00 15 100 100 9.4 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $basic . . . . . . 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 $basic 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Heteronuclear 1H-13C experiments were carried out with 13C nucleus in natural abundance ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $basic 10.4 mM . water 50 % . CF3CD2OH 50 % [U-2H] 'Na phosphate buffer' 10 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type b_micelles _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $basic 11.0 mM . 'Na dodecyl sulfate buffer' 40 mM [U-2H] 'Na phosphate buffer' 10 mM . stop_ save_ ############################ # Computer software used # ############################ save_vnmr _Saveframe_category software _Name VNMR _Version 5.1 loop_ _Task ; processing peak assignments ; stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_clean-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name clean-TOCSY _Sample_label . save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label . save_ save_1H-13C-gHSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-gHSQC _Sample_label . save_ save_gHSQC-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name gHSQC-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name clean-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-gHSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name gHSQC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 C 13 'methyl carbons' ppm 0.0 internal direct . . . TSP H 1 'methyl protons' ppm 0.0 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'basic 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 GLN H H 8.04 0.01 1 2 . 1 GLN HA H 4.38 0.01 1 3 . 1 GLN HB2 H 2.11 0.01 1 4 . 1 GLN HB3 H 1.97 0.01 1 5 . 1 GLN HG2 H 2.37 0.01 1 6 . 1 GLN HG3 H 2.37 0.01 1 7 . 1 GLN HE21 H 7.33 0.01 1 8 . 1 GLN HE22 H 6.67 0.01 1 9 . 1 GLN CA C 57.0 0.1 1 10 . 1 GLN CB C 30.9 0.1 1 11 . 1 GLN CG C 34.9 0.1 1 12 . 2 ALA H H 8.17 0.01 1 13 . 2 ALA HA H 4.57 0.01 1 14 . 2 ALA HB H 1.46 0.01 1 15 . 2 ALA CA C 53.4 0.1 1 16 . 2 ALA CB C 18.5 0.1 1 17 . 3 PRO HA H 4.38 0.01 1 18 . 3 PRO HB2 H 2.37 0.01 1 19 . 3 PRO HB3 H 1.83 0.01 1 20 . 3 PRO HG2 H 2.09 0.01 1 21 . 3 PRO HG3 H 2.09 0.01 1 22 . 3 PRO HD2 H 3.86 0.01 1 23 . 3 PRO HD3 H 3.67 0.01 1 24 . 3 PRO CA C 65.8 0.1 1 25 . 3 PRO CB C 32.6 0.1 1 26 . 3 PRO CG C 28.7 0.1 1 27 . 3 PRO CD C 51.3 0.1 1 28 . 4 ALA H H 8.01 0.01 1 29 . 4 ALA HA H 4.16 0.01 1 30 . 4 ALA HB H 1.46 0.01 1 31 . 4 ALA CA C 55.9 0.1 1 32 . 4 ALA CB C 19.1 0.1 1 33 . 5 TYR H H 7.69 0.01 1 34 . 5 TYR HA H 4.37 0.01 1 35 . 5 TYR HB2 H 3.16 0.01 1 36 . 5 TYR HB3 H 3.16 0.01 1 37 . 5 TYR HD1 H 7.13 0.01 1 38 . 5 TYR HD2 H 7.13 0.01 1 39 . 5 TYR HE1 H 6.86 0.01 1 40 . 5 TYR HE2 H 6.86 0.01 1 41 . 5 TYR CA C 61.1 0.1 1 42 . 5 TYR CB C 38.8 0.1 1 43 . 6 LYS H H 7.79 0.01 1 44 . 6 LYS HA H 4.07 0.01 1 45 . 6 LYS HB2 H 1.89 0.01 1 46 . 6 LYS HB3 H 1.89 0.01 1 47 . 6 LYS HG2 H 1.53 0.01 1 48 . 6 LYS HG3 H 1.44 0.01 1 49 . 6 LYS HD2 H 1.74 0.01 1 50 . 6 LYS HD3 H 1.74 0.01 1 51 . 6 LYS HE2 H 3.05 0.01 1 52 . 6 LYS HE3 H 3.05 0.01 1 53 . 6 LYS CA C 60.5 0.1 1 54 . 6 LYS CB C 33.4 0.1 1 55 . 6 LYS CG C 26.5 0.1 1 56 . 6 LYS CD C 30.5 0.1 1 57 . 6 LYS CE C 43.3 0.1 1 58 . 7 LYS H H 7.83 0.01 1 59 . 7 LYS HA H 4.06 0.01 1 60 . 7 LYS HB2 H 1.93 0.01 1 61 . 7 LYS HB3 H 1.93 0.01 1 62 . 7 LYS HG2 H 1.60 0.01 1 63 . 7 LYS HG3 H 1.46 0.01 1 64 . 7 LYS HD2 H 1.74 0.01 1 65 . 7 LYS HD3 H 1.74 0.01 1 66 . 7 LYS HE2 H 3.01 0.01 1 67 . 7 LYS HE3 H 3.01 0.01 1 68 . 7 LYS CA C 60.5 0.1 1 69 . 7 LYS CB C 33.5 0.1 1 70 . 7 LYS CG C 26.3 0.1 1 71 . 7 LYS CD C 30.5 0.1 1 72 . 7 LYS CE C 43.3 0.1 1 73 . 8 ALA H H 7.97 0.01 1 74 . 8 ALA HA H 4.13 0.01 1 75 . 8 ALA HB H 1.50 0.01 1 76 . 8 ALA CA C 56.0 0.1 1 77 . 8 ALA CB C 18.7 0.1 1 78 . 9 ALA H H 8.15 0.01 1 79 . 9 ALA HA H 4.07 0.01 1 80 . 9 ALA HB H 1.48 0.01 1 81 . 9 ALA CA C 56.2 0.1 1 82 . 9 ALA CB C 18.7 0.1 1 83 . 10 LYS H H 7.86 0.01 1 84 . 10 LYS HA H 4.09 0.01 1 85 . 10 LYS HB2 H 1.98 0.01 1 86 . 10 LYS HB3 H 1.98 0.01 1 87 . 10 LYS HG2 H 1.53 0.01 1 88 . 10 LYS HG3 H 1.49 0.01 1 89 . 10 LYS HD2 H 1.73 0.01 1 90 . 10 LYS HD3 H 1.73 0.01 1 91 . 10 LYS HE2 H 3.05 0.01 1 92 . 10 LYS HE3 H 3.05 0.01 1 93 . 10 LYS CA C 60.3 0.1 1 94 . 10 LYS CB C 33.8 0.1 1 95 . 10 LYS CG C 25.7 0.1 1 96 . 10 LYS CD C 30.5 0.1 1 97 . 10 LYS CE C 43.3 0.1 1 98 . 11 LYS H H 7.89 0.01 1 99 . 11 LYS HA H 4.18 0.01 1 100 . 11 LYS HB2 H 2.01 0.01 1 101 . 11 LYS HB3 H 2.01 0.01 1 102 . 11 LYS HG2 H 1.53 0.01 1 103 . 11 LYS HG3 H 1.53 0.01 1 104 . 11 LYS HD2 H 1.76 0.01 1 105 . 11 LYS HD3 H 1.76 0.01 1 106 . 11 LYS HE2 H 3.01 0.01 1 107 . 11 LYS HE3 H 3.01 0.01 1 108 . 11 LYS CA C 59.5 0.1 1 109 . 11 LYS CB C 33.6 0.1 1 110 . 11 LYS CG C 25.5 0.1 1 111 . 11 LYS CD C 29.7 0.1 1 112 . 11 LYS CE C 43.3 0.1 1 113 . 12 LEU H H 8.38 0.01 1 114 . 12 LEU HA H 4.14 0.01 1 115 . 12 LEU HB2 H 1.87 0.01 1 116 . 12 LEU HB3 H 1.68 0.01 1 117 . 12 LEU HG H 1.78 0.01 1 118 . 12 LEU HD1 H 0.93 0.01 1 119 . 12 LEU HD2 H 0.93 0.01 1 120 . 12 LEU CA C 59.0 0.1 1 121 . 12 LEU CB C 42.8 0.1 1 122 . 12 LEU CG C 28.0 0.1 1 123 . 12 LEU CD1 C 25.0 0.1 1 124 . 12 LEU CD2 C 24.0 0.1 1 125 . 13 ALA H H 8.19 0.01 1 126 . 13 ALA HA H 4.20 0.01 1 127 . 13 ALA HB H 1.58 0.01 1 128 . 13 ALA CA C 55.7 0.1 1 129 . 13 ALA CB C 19.2 0.1 1 130 . 14 GLU H H 8.10 0.01 1 131 . 14 GLU HA H 4.24 0.01 1 132 . 14 GLU HB2 H 2.21 0.01 1 133 . 14 GLU HB3 H 2.21 0.01 1 134 . 14 GLU HG2 H 2.62 0.01 1 135 . 14 GLU HG3 H 2.41 0.01 1 136 . 14 GLU CA C 58.7 0.1 1 137 . 14 GLU CB C 31.0 0.1 1 138 . 14 GLU CG C 37.7 0.1 1 139 . 15 SER H H 7.88 0.01 1 140 . 15 SER HA H 4.46 0.01 1 141 . 15 SER HB2 H 4.07 0.01 1 142 . 15 SER HB3 H 4.07 0.01 1 143 . 15 SER CA C 60.6 0.1 1 144 . 15 SER CB C 65.2 0.1 1 stop_ save_ save_chemical_shifts_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'basic 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 GLN H H 8.27 0.01 1 2 . 1 GLN HA H 4.34 0.01 1 3 . 1 GLN HB2 H 2.09 0.01 1 4 . 1 GLN HB3 H 1.97 0.01 1 5 . 1 GLN HG2 H 2.39 0.01 1 6 . 1 GLN HG3 H 2.39 0.01 1 7 . 1 GLN HE21 H 7.56 0.01 1 8 . 1 GLN HE22 H 6.88 0.01 1 9 . 1 GLN CA C 55.9 0.1 1 10 . 1 GLN CB C 30.1 0.1 1 11 . 1 GLN CG C 34.0 0.1 1 12 . 2 ALA H H 8.38 0.01 1 13 . 2 ALA HA H 4.59 0.01 1 14 . 2 ALA HB H 1.40 0.01 1 15 . 2 ALA CA C 51.5 0.1 1 16 . 2 ALA CB C 18.2 0.1 1 17 . 3 PRO HA H 4.39 0.01 1 18 . 3 PRO HB2 H 2.40 0.01 1 19 . 3 PRO HB3 H 1.74 0.01 1 20 . 3 PRO HG2 H 2.08 0.01 1 21 . 3 PRO HG3 H 2.08 0.01 1 22 . 3 PRO HD2 H 3.84 0.01 1 23 . 3 PRO HD3 H 3.62 0.01 1 24 . 3 PRO CA C 64.0 0.1 1 25 . 3 PRO CB C 32.3 0.1 1 26 . 3 PRO CG C 27.9 0.1 1 27 . 3 PRO CD C 50.6 0.1 1 28 . 4 ALA H H 8.49 0.01 1 29 . 4 ALA HA H 4.16 0.01 1 30 . 4 ALA HB H 1.49 0.01 1 31 . 4 ALA CA C 54.9 0.1 1 32 . 4 ALA CB C 18.6 0.1 1 33 . 5 TYR H H 7.91 0.01 1 34 . 5 TYR HA H 4.29 0.01 1 35 . 5 TYR HB2 H 3.08 0.01 1 36 . 5 TYR HB3 H 3.08 0.01 1 37 . 5 TYR HD1 H 7.10 0.01 1 38 . 5 TYR HD2 H 7.10 0.01 1 39 . 5 TYR HE1 H 6.82 0.01 1 40 . 5 TYR HE2 H 6.82 0.01 1 41 . 5 TYR CA C 60.5 0.1 1 42 . 5 TYR CB C 37.8 0.1 1 43 . 6 LYS H H 7.48 0.01 1 44 . 6 LYS HA H 3.96 0.01 1 45 . 6 LYS HB2 H 1.86 0.01 1 46 . 6 LYS HB3 H 1.86 0.01 1 47 . 6 LYS HG2 H 1.32 0.01 1 48 . 6 LYS HG3 H 1.32 0.01 1 49 . 6 LYS HD2 H 1.72 0.01 1 50 . 6 LYS HD3 H 1.72 0.01 1 51 . 6 LYS HE2 H 3.04 0.01 1 52 . 6 LYS HE3 H 3.04 0.01 1 53 . 6 LYS CA C 59.3 0.1 1 54 . 6 LYS CE C 42.2 0.1 1 55 . 7 LYS H H 7.78 0.01 1 56 . 7 LYS HA H 4.03 0.01 1 57 . 7 LYS HB2 H 1.92 0.01 1 58 . 7 LYS HB3 H 1.92 0.01 1 59 . 7 LYS HG2 H 1.50 0.01 1 60 . 7 LYS HG3 H 1.50 0.01 1 61 . 7 LYS HD2 H 1.75 0.01 1 62 . 7 LYS HD3 H 1.75 0.01 1 63 . 7 LYS HE2 H 3.00 0.01 1 64 . 7 LYS HE3 H 3.00 0.01 1 65 . 7 LYS CA C 59.3 0.1 1 66 . 7 LYS CE C 42.2 0.1 1 67 . 8 ALA H H 8.07 0.01 1 68 . 8 ALA HA H 4.10 0.01 1 69 . 8 ALA HB H 1.51 0.01 1 70 . 8 ALA CA C 54.9 0.1 1 71 . 8 ALA CB C 18.6 0.1 1 72 . 9 ALA H H 8.20 0.01 1 73 . 9 ALA HA H 4.00 0.01 1 74 . 9 ALA HB H 1.52 0.01 1 75 . 9 ALA CA C 55.3 0.1 1 76 . 9 ALA CB C 18.4 0.1 1 77 . 10 LYS H H 7.90 0.01 1 78 . 10 LYS HA H 4.04 0.01 1 79 . 10 LYS HB2 H 1.94 0.01 1 80 . 10 LYS HB3 H 1.94 0.01 1 81 . 10 LYS HG2 H 1.49 0.01 1 82 . 10 LYS HG3 H 1.49 0.01 1 83 . 10 LYS HD2 H 1.72 0.01 1 84 . 10 LYS HD3 H 1.72 0.01 1 85 . 10 LYS HE2 H 3.04 0.01 1 86 . 10 LYS HE3 H 3.04 0.01 1 87 . 10 LYS CA C 59.2 0.1 1 88 . 10 LYS CE C 42.2 0.1 1 89 . 11 LYS H H 7.78 0.01 1 90 . 11 LYS HA H 4.17 0.01 1 91 . 11 LYS HB2 H 1.98 0.01 1 92 . 11 LYS HB3 H 1.98 0.01 1 93 . 11 LYS HG2 H 1.50 0.01 1 94 . 11 LYS HG3 H 1.50 0.01 1 95 . 11 LYS HD2 H 1.76 0.01 1 96 . 11 LYS HD3 H 1.76 0.01 1 97 . 11 LYS HE2 H 3.00 0.01 1 98 . 11 LYS HE3 H 3.00 0.01 1 99 . 11 LYS CA C 58.5 0.1 1 100 . 11 LYS CE C 42.2 0.1 1 101 . 12 LEU H H 8.16 0.01 1 102 . 12 LEU HA H 4.14 0.01 1 103 . 12 LEU HB2 H 1.82 0.01 1 104 . 12 LEU HB3 H 1.67 0.01 1 105 . 12 LEU HG H 1.80 0.01 1 106 . 12 LEU HD1 H 0.93 0.01 1 107 . 12 LEU HD2 H 0.93 0.01 1 108 . 12 LEU CA C 57.7 0.1 1 109 . 12 LEU CB C 41.9 0.1 1 110 . 12 LEU CG C 27.3 0.1 1 111 . 12 LEU CD1 C 25.2 0.1 1 112 . 12 LEU CD2 C 24.4 0.1 1 113 . 13 ALA H H 8.13 0.01 1 114 . 13 ALA HA H 4.17 0.01 1 115 . 13 ALA HB H 1.54 0.01 1 116 . 13 ALA CA C 54.6 0.1 1 117 . 13 ALA CB C 18.7 0.1 1 118 . 14 GLU H H 7.97 0.01 1 119 . 14 GLU HA H 4.24 0.01 1 120 . 14 GLU HB2 H 2.15 0.01 1 121 . 14 GLU HB3 H 2.15 0.01 1 122 . 14 GLU HG2 H 2.54 0.01 1 123 . 14 GLU HG3 H 2.35 0.01 1 124 . 14 GLU CA C 57.6 0.1 1 125 . 14 GLU CB C 30.1 0.1 1 126 . 14 GLU CG C 36.6 0.1 1 127 . 15 SER H H 7.91 0.01 1 128 . 15 SER HA H 4.41 0.01 1 129 . 15 SER HB2 H 4.03 0.01 1 130 . 15 SER HB3 H 4.03 0.01 1 131 . 15 SER CA C 59.6 0.1 1 132 . 15 SER CB C 64.2 0.1 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'basic peptide' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 4 ALA H 4 ALA HA 3.40 . . 0.05 2 3JHNHA 5 TYR H 5 TYR HA 4.75 . . 0.05 3 3JHNHA 6 LYS H 6 LYS HA 4.75 . . 0.05 4 3JHNHA 7 LYS H 7 LYS HA 4.45 . . 0.05 5 3JHNHA 8 ALA H 8 ALA HA 3.95 . . 0.05 6 3JHNHA 9 ALA H 9 ALA HA 3.00 . . 0.05 7 3JHNHA 10 LYS H 10 LYS HA 4.70 . . 0.05 8 3JHNHA 11 LYS H 11 LYS HA 4.30 . . 0.05 9 3JHNHA 12 LEU H 12 LEU HA 3.95 . . 0.05 10 3JHNHA 13 ALA H 13 ALA HA 3.90 . . 0.05 stop_ save_