data_5033 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structures of the Antifungal Heliomicin ; _BMRB_accession_number 5033 _BMRB_flat_file_name bmr5033.str _Entry_type original _Submission_date 2001-03-14 _Accession_date 2001-05-29 _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 Lamberty M. . . 2 Caille A. . . 3 Landon C. . . 4 Tassin-Moindrot S. . . 5 Hetru C. . . 6 Bulet P. . . 7 Vovelle F. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 243 "coupling constants" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-01-23 original BMRB . stop_ _Original_release_date 2001-05-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structures of the Antifungal Heliomicin and a Selected Variant with both Antibacterial and Antifungal Activities ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21464431 _PubMed_ID 11580275 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lamberty M. . . 2 Caille A. . . 3 Landon C. . . 4 Tassin-Moindrot S. . . 5 Hetru C. . . 6 Bulet P. . . 7 Vovelle F. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 40 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11995 _Page_last 12003 _Year 2001 _Details . loop_ _Keyword 'CSab motif (cysteine stabilized alpha-helix beta-sheet motif)' 'alpha-beta protein' stop_ save_ ################################## # Molecular system description # ################################## save_system_DH1 _Saveframe_category molecular_system _Mol_system_name 'Defensin Heliomicin' _Abbreviation_common 'DEFENSIN HELIOMICIN' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DEFENSIN HELIOMICIN' $DH1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DH1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DEFENSIN HELIOMICIN' _Abbreviation_common 'DEFENSIN HELIOMICIN' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 44 _Mol_residue_sequence ; DKLIGSCVWGAVNYTSDCNG ECKRRGYKGGHCGSFANVNC WCET ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 LYS 3 LEU 4 ILE 5 GLY 6 SER 7 CYS 8 VAL 9 TRP 10 GLY 11 ALA 12 VAL 13 ASN 14 TYR 15 THR 16 SER 17 ASP 18 CYS 19 ASN 20 GLY 21 GLU 22 CYS 23 LYS 24 ARG 25 ARG 26 GLY 27 TYR 28 LYS 29 GLY 30 GLY 31 HIS 32 CYS 33 GLY 34 SER 35 PHE 36 ALA 37 ASN 38 VAL 39 ASN 40 CYS 41 TRP 42 CYS 43 GLU 44 THR stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1I2U 'Nmr Solution Structures Of Antifungal Heliomicin' 100.00 44 100.00 100.00 2.56e-17 SWISS-PROT P81544 'Defensin heliomicin' 100.00 44 100.00 100.00 2.56e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DH1 'Tobacco budworm' 7102 Eukaryota Metazoa Heliothis virescens 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 $DH1 'recombinant technology' Yeast Saccharomyces cerevisiae . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DH1 4 mM . 'sodium acetate buffer' 40 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version . loop_ _Task collection stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'data analysis' stop_ _Details Bartels save_ save_DYANA _Saveframe_category software _Name DYANA _Version . loop_ _Task refinement stop_ _Details Guentert save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Task refinement stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H DQF-COSY' _Sample_label . save_ save_2D_1H_TQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H TQF-COSY' _Sample_label . save_ save_2D_1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H TOCSY' _Sample_label . save_ save_2D_1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 40 . mM pH 4.3 . n/a pressure 1 . atm temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_1 _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 H2O H 1 H ppm 4.82 internal direct 1.0 internal . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H DQF-COSY' '2D 1H TQF-COSY' '2D 1H TOCSY' '2D 1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'DEFENSIN HELIOMICIN' _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 ASP HA H 4.77 . 1 2 . 1 ASP HB2 H 2.84 . 1 3 . 1 ASP HB3 H 2.50 . 1 4 . 2 LYS H H 8.98 . 1 5 . 2 LYS HA H 4.80 . 1 6 . 2 LYS HB2 H 1.45 . 1 7 . 2 LYS HB3 H 1.32 . 1 8 . 2 LYS HG2 H 1.21 . 1 9 . 2 LYS HG3 H 1.21 . 1 10 . 2 LYS HD2 H 1.65 . 1 11 . 2 LYS HD3 H 1.65 . 1 12 . 2 LYS HE2 H 2.96 . 1 13 . 2 LYS HE3 H 2.96 . 1 14 . 3 LEU H H 8.80 . 1 15 . 3 LEU HA H 3.81 . 1 16 . 3 LEU HB2 H 1.27 . 1 17 . 3 LEU HB3 H 0.30 . 1 18 . 3 LEU HG H 0.52 . 1 19 . 3 LEU HD1 H 0.40 . 1 20 . 3 LEU HD2 H 0.01 . 1 21 . 4 ILE H H 7.98 . 1 22 . 4 ILE HA H 4.62 . 1 23 . 4 ILE HB H 1.88 . 1 24 . 4 ILE HG12 H 1.01 . 1 25 . 4 ILE HG13 H 1.01 . 1 26 . 4 ILE HG2 H 0.68 . 1 27 . 4 ILE HD1 H 0.66 . 1 28 . 5 GLY H H 6.96 . 1 29 . 5 GLY HA2 H 4.17 . 1 30 . 5 GLY HA3 H 3.94 . 1 31 . 6 SER H H 7.73 . 1 32 . 6 SER HA H 5.14 . 1 33 . 6 SER HB2 H 3.85 . 1 34 . 6 SER HB3 H 3.24 . 1 35 . 7 CYS H H 8.72 . 1 36 . 7 CYS HA H 5.10 . 1 37 . 7 CYS HB2 H 3.85 . 1 38 . 7 CYS HB3 H 3.24 . 1 39 . 8 VAL H H 8.77 . 1 40 . 8 VAL HA H 4.05 . 1 41 . 8 VAL HB H 2.01 . 1 42 . 8 VAL HG1 H 1.05 . 1 43 . 8 VAL HG2 H 0.93 . 1 44 . 9 TRP H H 8.59 . 1 45 . 9 TRP HA H 2.47 . 1 46 . 9 TRP HB2 H 2.87 . 1 47 . 9 TRP HB3 H 2.87 . 1 48 . 9 TRP HD1 H 6.98 . 1 49 . 9 TRP HE1 H 10.02 . 1 50 . 9 TRP HE3 H 7.13 . 1 51 . 9 TRP HZ2 H 7.40 . 1 52 . 9 TRP HZ3 H 7.07 . 1 53 . 9 TRP HH2 H 7.15 . 1 54 . 10 GLY H H 6.80 . 1 55 . 10 GLY HA2 H 3.73 . 1 56 . 10 GLY HA3 H 2.74 . 1 57 . 11 ALA H H 7.67 . 1 58 . 11 ALA HA H 4.33 . 1 59 . 11 ALA HB H 1.48 . 1 60 . 12 VAL H H 8.47 . 1 61 . 12 VAL HA H 3.74 . 1 62 . 12 VAL HB H 1.94 . 1 63 . 12 VAL HG1 H 0.96 . 1 64 . 12 VAL HG2 H 0.88 . 1 65 . 13 ASN H H 8.58 . 1 66 . 13 ASN HA H 4.58 . 1 67 . 13 ASN HB2 H 3.02 . 1 68 . 13 ASN HB3 H 2.90 . 1 69 . 13 ASN HD21 H 6.81 . 2 70 . 13 ASN HD22 H 7.62 . 2 71 . 14 TYR H H 7.35 . 1 72 . 14 TYR HA H 4.61 . 1 73 . 14 TYR HB2 H 3.26 . 1 74 . 14 TYR HB3 H 2.48 . 1 75 . 14 TYR HD1 H 6.75 . 1 76 . 14 TYR HD2 H 6.75 . 1 77 . 14 TYR HE1 H 6.71 . 1 78 . 14 TYR HE2 H 6.71 . 1 79 . 15 THR H H 8.15 . 1 80 . 15 THR HA H 4.09 . 1 81 . 15 THR HB H 3.69 . 1 82 . 15 THR HG2 H 0.84 . 1 83 . 16 SER H H 8.07 . 1 84 . 16 SER HA H 4.09 . 1 85 . 16 SER HB2 H 3.99 . 1 86 . 16 SER HB3 H 3.81 . 1 87 . 17 ASP H H 7.92 . 1 88 . 17 ASP HA H 4.72 . 1 89 . 17 ASP HB2 H 2.72 . 1 90 . 17 ASP HB3 H 2.53 . 1 91 . 18 CYS H H 8.90 . 1 92 . 18 CYS HA H 4.09 . 1 93 . 18 CYS HB2 H 2.97 . 1 94 . 18 CYS HB3 H 2.59 . 1 95 . 19 ASN H H 8.59 . 1 96 . 19 ASN HA H 3.90 . 1 97 . 19 ASN HB2 H 3.00 . 1 98 . 19 ASN HB3 H 2.71 . 1 99 . 19 ASN HD21 H 7.81 . 1 100 . 19 ASN HD22 H 6.91 . 1 101 . 20 GLY H H 8.06 . 1 102 . 20 GLY HA2 H 3.87 . 1 103 . 20 GLY HA3 H 3.61 . 1 104 . 21 GLU H H 8.88 . 1 105 . 21 GLU HA H 4.07 . 1 106 . 21 GLU HB2 H 2.07 . 1 107 . 21 GLU HB3 H 1.78 . 1 108 . 21 GLU HG2 H 2.27 . 1 109 . 21 GLU HG3 H 1.92 . 1 110 . 22 CYS H H 8.47 . 1 111 . 22 CYS HA H 4.25 . 1 112 . 22 CYS HB2 H 2.71 . 1 113 . 22 CYS HB3 H 2.51 . 1 114 . 23 LYS H H 8.07 . 1 115 . 23 LYS HA H 4.56 . 1 116 . 23 LYS HB2 H 1.81 . 1 117 . 23 LYS HB3 H 1.81 . 1 118 . 23 LYS HG2 H 1.28 . 1 119 . 23 LYS HG3 H 1.28 . 1 120 . 23 LYS HD2 H 1.58 . 1 121 . 23 LYS HD3 H 1.58 . 1 122 . 23 LYS HE2 H 2.98 . 1 123 . 23 LYS HE3 H 2.98 . 1 124 . 23 LYS HZ H 7.57 . 1 125 . 24 ARG H H 8.29 . 1 126 . 24 ARG HA H 4.00 . 1 127 . 24 ARG HB2 H 2.01 . 1 128 . 24 ARG HB3 H 1.93 . 1 129 . 24 ARG HG2 H 1.75 . 1 130 . 24 ARG HG3 H 1.58 . 1 131 . 24 ARG HD2 H 3.20 . 1 132 . 24 ARG HD3 H 3.20 . 1 133 . 24 ARG HE H 7.44 . 1 134 . 25 ARG H H 7.59 . 1 135 . 25 ARG HA H 4.25 . 1 136 . 25 ARG HB2 H 2.23 . 1 137 . 25 ARG HB3 H 1.98 . 1 138 . 25 ARG HG2 H 1.96 . 1 139 . 25 ARG HG3 H 1.69 . 1 140 . 25 ARG HD2 H 3.36 . 1 141 . 25 ARG HD3 H 2.94 . 1 142 . 25 ARG HE H 8.38 . 1 143 . 26 GLY H H 7.77 . 1 144 . 26 GLY HA2 H 4.08 . 1 145 . 26 GLY HA3 H 3.61 . 1 146 . 27 TYR H H 7.93 . 1 147 . 27 TYR HA H 4.77 . 1 148 . 27 TYR HB2 H 3.63 . 1 149 . 27 TYR HB3 H 2.44 . 1 150 . 27 TYR HD1 H 7.32 . 1 151 . 27 TYR HD2 H 7.32 . 1 152 . 27 TYR HE1 H 6.61 . 1 153 . 27 TYR HE2 H 6.61 . 1 154 . 28 LYS H H 8.86 . 1 155 . 28 LYS HA H 4.09 . 1 156 . 28 LYS HB2 H 1.79 . 1 157 . 28 LYS HB3 H 1.79 . 1 158 . 28 LYS HG2 H 1.45 . 1 159 . 28 LYS HG3 H 1.45 . 1 160 . 28 LYS HD2 H 1.62 . 1 161 . 28 LYS HD3 H 1.62 . 1 162 . 28 LYS HE2 H 2.93 . 1 163 . 28 LYS HE3 H 2.93 . 1 164 . 28 LYS HZ H 7.56 . 1 165 . 29 GLY H H 7.32 . 1 166 . 29 GLY HA2 H 4.30 . 1 167 . 29 GLY HA3 H 3.79 . 1 168 . 30 GLY H H 9.20 . 1 169 . 30 GLY HA2 H 4.98 . 1 170 . 30 GLY HA3 H 4.38 . 1 171 . 31 HIS H H 8.95 . 1 172 . 31 HIS HA H 4.83 . 1 173 . 31 HIS HB2 H 3.28 . 1 174 . 31 HIS HB3 H 3.17 . 1 175 . 31 HIS HD2 H 7.06 . 3 176 . 31 HIS HE1 H 8.50 . 3 177 . 32 CYS H H 9.05 . 1 178 . 32 CYS HA H 5.52 . 1 179 . 32 CYS HB2 H 3.34 . 1 180 . 32 CYS HB3 H 2.97 . 1 181 . 33 GLY H H 10.02 . 1 182 . 33 GLY HA2 H 5.01 . 1 183 . 33 GLY HA3 H 4.20 . 1 184 . 34 SER H H 8.31 . 1 185 . 34 SER HA H 4.81 . 1 186 . 34 SER HB2 H 4.46 . 1 187 . 34 SER HB3 H 4.39 . 1 188 . 35 PHE H H 8.50 . 1 189 . 35 PHE HA H 4.24 . 1 190 . 35 PHE HB2 H 3.18 . 1 191 . 35 PHE HB3 H 3.01 . 1 192 . 35 PHE HD1 H 7.29 . 1 193 . 35 PHE HD2 H 7.29 . 1 194 . 35 PHE HE1 H 7.37 . 1 195 . 35 PHE HE2 H 7.37 . 1 196 . 36 ALA H H 8.35 . 1 197 . 36 ALA HA H 3.53 . 1 198 . 36 ALA HB H 1.18 . 1 199 . 37 ASN H H 8.64 . 1 200 . 37 ASN HA H 4.07 . 1 201 . 37 ASN HB2 H 2.89 . 1 202 . 37 ASN HB3 H 2.71 . 1 203 . 37 ASN HD21 H 7.42 . 1 204 . 37 ASN HD22 H 6.76 . 1 205 . 38 VAL H H 6.52 . 1 206 . 38 VAL HA H 3.97 . 1 207 . 38 VAL HB H 2.28 . 1 208 . 38 VAL HG1 H 0.98 . 1 209 . 38 VAL HG2 H 0.95 . 1 210 . 39 ASN H H 8.72 . 1 211 . 39 ASN HA H 5.30 . 1 212 . 39 ASN HB2 H 2.50 . 1 213 . 39 ASN HB3 H 1.71 . 1 214 . 39 ASN HD21 H 7.69 . 1 215 . 39 ASN HD22 H 7.11 . 1 216 . 40 CYS H H 8.61 . 1 217 . 40 CYS HA H 4.65 . 1 218 . 40 CYS HB2 H 2.63 . 1 219 . 40 CYS HB3 H 1.85 . 1 220 . 41 TRP H H 8.23 . 1 221 . 41 TRP HA H 4.80 . 1 222 . 41 TRP HB2 H 2.65 . 1 223 . 41 TRP HB3 H 2.48 . 1 224 . 41 TRP HD1 H 6.71 . 1 225 . 41 TRP HE1 H 10.04 . 1 226 . 41 TRP HE3 H 7.00 . 1 227 . 41 TRP HZ2 H 7.43 . 1 228 . 41 TRP HZ3 H 7.02 . 1 229 . 41 TRP HH2 H 7.24 . 1 230 . 42 CYS H H 9.41 . 1 231 . 42 CYS HA H 5.37 . 1 232 . 42 CYS HB2 H 2.31 . 1 233 . 42 CYS HB3 H 1.44 . 1 234 . 43 GLU H H 8.67 . 1 235 . 43 GLU HA H 4.36 . 1 236 . 43 GLU HB2 H 2.03 . 1 237 . 43 GLU HB3 H 1.82 . 1 238 . 43 GLU HG2 H 2.50 . 1 239 . 43 GLU HG3 H 2.26 . 1 240 . 44 THR H H 8.08 . 1 241 . 44 THR HA H 4.37 . 1 242 . 44 THR HB H 4.48 . 1 243 . 44 THR HG2 H 1.17 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_J-values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '2D 1H DQF-COSY' '2D 1H TQF-COSY' '2D 1H TOCSY' '2D 1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'DEFENSIN HELIOMICIN' _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 2 LYS H 2 LYS HA 10.0 . . . 2 3JHNHA 3 LEU H 3 LEU HA 6.2 . . . 3 3JHNHA 4 ILE H 4 ILE HA 10.4 . . . 4 3JHNHA 6 SER H 6 SER HA 10.2 . . . 5 3JHNHA 7 CYS H 7 CYS HA 10.3 . . . 6 3JHNHA 8 VAL H 8 VAL HA 9.2 . . . 7 3JHNHA 9 TRP H 9 TRP HA 2.8 . . . 8 3JHNHA 11 ALA H 11 ALA HA 6.5 . . . 9 3JHNHA 12 VAL H 12 VAL HA 3.5 . . . 10 3JHNHA 13 ASN H 13 ASN HA 9.8 . . . 11 3JHNHA 14 TYR H 14 TYR HA 3.5 . . . 12 3JHNHA 15 THR H 15 THR HA 10.5 . . . 13 3JHNHA 16 SER H 16 SER HA 6.4 . . . 14 3JHNHA 17 ASP H 17 ASP HA 9.2 . . . 15 3JHNHA 18 CYS H 18 CYS HA 3.1 . . . 16 3JHNHA 19 ASN H 19 ASN HA 3.4 . . . 17 3JHNHA 21 GLU H 21 GLU HA 4.7 . . . 18 3JHNHA 22 CYS H 22 CYS HA 3.7 . . . 19 3JHNHA 23 LYS H 23 LYS HA 6.1 . . . 20 3JHNHA 24 ARG H 24 ARG HA 4.1 . . . 21 3JHNHA 25 ARG H 25 ARG HA 7.9 . . . 22 3JHNHA 27 TYR H 27 TYR HA 9.4 . . . 23 3JHNHA 28 LYS H 28 LYS HA 4.4 . . . 24 3JHNHA 31 HIS H 31 HIS HA 7.6 . . . 25 3JHNHA 32 CYS H 32 CYS HA 7.2 . . . 26 3JHNHA 34 SER H 34 SER HA 6.6 . . . 27 3JHNHA 35 PHE H 35 PHE HA 3.4 . . . 28 3JHNHA 36 ALA H 36 ALA HA 8.2 . . . 29 3JHNHA 39 ASN H 39 ASN HA 9.9 . . . 30 3JHNHA 40 CYS H 40 CYS HA 9.0 . . . 31 3JHNHA 41 TRP H 41 TRP HA 10.2 . . . 32 3JHNHA 42 CYS H 42 CYS HA 9.4 . . . 33 3JHNHA 43 GLU H 43 GLU HA 7.3 . . . 34 3JHNHA 44 THR H 44 THR HA 9.6 . . . stop_ save_