data_5268 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the Antimicrobial Peptide Tachystatin A ; _BMRB_accession_number 5268 _BMRB_flat_file_name bmr5268.str _Entry_type original _Submission_date 2002-01-28 _Accession_date 2002-01-29 _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 Fujitani Naoki . . 2 Kawabata S. . . 3 Osaki T. . . 4 Kumaki Y. . . 5 Demura M. . . 6 Nitta K. . . 7 Kawano K. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 267 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-11 original BMRB . stop_ _Original_release_date 2002-01-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the Antimicrobial Peptide Tachystatin A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22075127 _PubMed_ID 11959852 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fujitani Naoki . . 2 Kawabata Shun-ichiro . . 3 Osaki Tsukasa . . 4 Kumaki Yasuhiro . . 5 Demura Makoto . . 6 Nitta Katsutoshi . . 7 Kawano Keiichi . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 277 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 23651 _Page_last 23657 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_tachystatin_A _Saveframe_category molecular_system _Mol_system_name 'tachystatin A' _Abbreviation_common 'tachystatin A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'tachystatin A' $tachystatin_A 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_tachystatin_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'tachystatin A' _Abbreviation_common 'tachystatin A' _Molecular_mass 5055.8 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 44 _Mol_residue_sequence ; YSRCQLQGFNCVVRSYGLPT IPCCRGLTCRSYFPGSTYGR CQRY ; loop_ _Residue_seq_code _Residue_label 1 TYR 2 SER 3 ARG 4 CYS 5 GLN 6 LEU 7 GLN 8 GLY 9 PHE 10 ASN 11 CYS 12 VAL 13 VAL 14 ARG 15 SER 16 TYR 17 GLY 18 LEU 19 PRO 20 THR 21 ILE 22 PRO 23 CYS 24 CYS 25 ARG 26 GLY 27 LEU 28 THR 29 CYS 30 ARG 31 SER 32 TYR 33 PHE 34 PRO 35 GLY 36 SER 37 THR 38 TYR 39 GLY 40 ARG 41 CYS 42 GLN 43 ARG 44 TYR 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 1CIX 'Three-Dimensional Structure Of Antimicrobial Peptide Tachystatin A Isolated From Horseshoe Crab' 97.73 44 100.00 100.00 6.51e-16 DBJ BAA85250 'tachystatin A2 [Tachypleus tridentatus]' 100.00 67 100.00 100.00 3.31e-17 SWISS-PROT Q9U8X3 'Tachystatin-A2 precursor' 100.00 67 100.00 100.00 3.31e-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 _Tissue _Details $tachystatin_A 'Japanese horseshoe crab' 6853 Eukaryota Metazoa Tachypleus tridentatus hemocyte 'Small garanular cell in the granular cell of hemocyte.' 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 $tachystatin_A 'purified from the natural source' . . . . . 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 $tachystatin_A 2.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer JEOL _Model Alpha _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer JEOL _Model Alpha _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H DQF-COSY' _Sample_label . save_ save_2D_1H-1H_E-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H E-COSY' _Sample_label . save_ save_2D_1H-1H_HOHAHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H HOHAHA' _Sample_label . save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_exp_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 3.0 0.5 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 _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_cs1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H DQF-COSY' '2D 1H-1H E-COSY' '2D 1H-1H HOHAHA' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $exp_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'tachystatin A' _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 TYR HA H 4.20 0.02 1 2 . 1 TYR HB2 H 3.05 0.02 1 3 . 1 TYR HB3 H 3.05 0.02 1 4 . 1 TYR HD1 H 7.04 0.02 1 5 . 1 TYR HD2 H 7.04 0.02 1 6 . 1 TYR HE1 H 6.75 0.02 1 7 . 1 TYR HE2 H 6.75 0.02 1 8 . 2 SER H H 8.49 0.02 1 9 . 2 SER HA H 4.41 0.02 1 10 . 2 SER HB2 H 3.74 0.02 2 11 . 2 SER HB3 H 3.70 0.02 2 12 . 3 ARG H H 8.26 0.02 1 13 . 3 ARG HA H 4.29 0.02 1 14 . 3 ARG HB2 H 1.76 0.02 2 15 . 3 ARG HB3 H 1.69 0.02 2 16 . 3 ARG HG2 H 1.54 0.02 1 17 . 3 ARG HG3 H 1.54 0.02 1 18 . 3 ARG HD2 H 3.06 0.02 1 19 . 3 ARG HD3 H 3.06 0.02 1 20 . 3 ARG HE H 7.13 0.02 1 21 . 4 CYS H H 7.97 0.02 1 22 . 4 CYS HA H 4.91 0.02 1 23 . 4 CYS HB2 H 2.93 0.02 1 24 . 4 CYS HB3 H 2.74 0.02 1 25 . 5 GLN H H 9.14 0.02 1 26 . 5 GLN HA H 4.56 0.02 1 27 . 5 GLN HB2 H 2.01 0.02 2 28 . 5 GLN HB3 H 1.94 0.02 2 29 . 5 GLN HG2 H 2.46 0.02 1 30 . 5 GLN HG3 H 2.46 0.02 1 31 . 5 GLN HE21 H 8.03 0.02 1 32 . 5 GLN HE22 H 6.88 0.02 1 33 . 6 LEU H H 6.97 0.02 1 34 . 6 LEU HA H 3.88 0.02 1 35 . 6 LEU HB2 H 1.45 0.02 1 36 . 6 LEU HB3 H 1.45 0.02 1 37 . 6 LEU HG H 1.05 0.02 1 38 . 6 LEU HD1 H 0.74 0.02 1 39 . 6 LEU HD2 H 0.74 0.02 1 40 . 7 GLN H H 8.14 0.02 1 41 . 7 GLN HA H 3.56 0.02 1 42 . 7 GLN HB2 H 1.93 0.02 2 43 . 7 GLN HB3 H 1.87 0.02 2 44 . 7 GLN HG2 H 2.34 0.02 2 45 . 7 GLN HG3 H 2.23 0.02 2 46 . 7 GLN HE21 H 7.51 0.02 1 47 . 7 GLN HE22 H 6.86 0.02 1 48 . 8 GLY H H 9.55 0.02 1 49 . 8 GLY HA2 H 4.25 0.02 2 50 . 8 GLY HA3 H 3.44 0.02 2 51 . 9 PHE H H 7.97 0.02 1 52 . 9 PHE HA H 3.56 0.02 1 53 . 9 PHE HB2 H 1.87 0.02 2 54 . 9 PHE HB3 H 1.93 0.02 2 55 . 9 PHE HD1 H 2.46 0.02 1 56 . 9 PHE HD2 H 2.46 0.02 1 57 . 9 PHE HE1 H 7.34 0.02 1 58 . 9 PHE HE2 H 7.34 0.02 1 59 . 9 PHE HZ H 7.31 0.02 1 60 . 10 ASN H H 8.59 0.02 1 61 . 10 ASN HA H 5.19 0.02 1 62 . 10 ASN HB2 H 2.75 0.02 1 63 . 10 ASN HB3 H 2.75 0.02 1 64 . 10 ASN HD21 H 6.50 0.02 1 65 . 10 ASN HD22 H 7.56 0.02 1 66 . 11 CYS H H 8.59 0.02 1 67 . 11 CYS HA H 5.01 0.02 1 68 . 11 CYS HB2 H 2.94 0.02 1 69 . 11 CYS HB3 H 3.17 0.02 1 70 . 12 VAL H H 8.70 0.02 1 71 . 12 VAL HA H 4.11 0.02 1 72 . 12 VAL HB H 1.81 0.02 1 73 . 12 VAL HG1 H 0.65 0.02 1 74 . 12 VAL HG2 H 0.91 0.02 1 75 . 13 VAL H H 8.29 0.02 1 76 . 13 VAL HA H 3.41 0.02 1 77 . 13 VAL HB H 1.68 0.02 1 78 . 13 VAL HG1 H 0.50 0.02 2 79 . 13 VAL HG2 H 0.75 0.02 2 80 . 14 ARG H H 7.71 0.02 1 81 . 14 ARG HA H 4.32 0.02 1 82 . 14 ARG HB2 H 1.41 0.02 2 83 . 14 ARG HB3 H 1.48 0.02 2 84 . 14 ARG HG2 H 1.24 0.02 1 85 . 14 ARG HG3 H 1.24 0.02 1 86 . 14 ARG HD2 H 2.96 0.02 1 87 . 14 ARG HD3 H 2.96 0.02 1 88 . 14 ARG HE H 6.94 0.02 1 89 . 15 SER H H 8.22 0.02 1 90 . 15 SER HA H 4.16 0.02 1 91 . 15 SER HB2 H 3.61 0.02 2 92 . 15 SER HB3 H 3.89 0.02 2 93 . 16 TYR H H 8.32 0.02 1 94 . 16 TYR HA H 4.32 0.02 1 95 . 16 TYR HB2 H 2.93 0.02 2 96 . 16 TYR HB3 H 3.04 0.02 2 97 . 16 TYR HD1 H 6.98 0.02 1 98 . 16 TYR HD2 H 6.98 0.02 1 99 . 16 TYR HE1 H 6.89 0.02 1 100 . 16 TYR HE2 H 6.89 0.02 1 101 . 17 GLY H H 8.20 0.02 1 102 . 17 GLY HA2 H 3.58 0.02 2 103 . 17 GLY HA3 H 4.02 0.02 2 104 . 18 LEU H H 7.63 0.02 1 105 . 18 LEU HA H 4.60 0.02 1 106 . 18 LEU HB2 H 1.59 0.02 1 107 . 18 LEU HB3 H 1.59 0.02 1 108 . 18 LEU HG H 1.46 0.02 1 109 . 18 LEU HD1 H 0.85 0.02 2 110 . 18 LEU HD2 H 0.88 0.02 2 111 . 19 PRO HA H 4.40 0.02 1 112 . 19 PRO HB2 H 2.19 0.02 2 113 . 19 PRO HB3 H 1.97 0.02 2 114 . 19 PRO HG2 H 1.80 0.02 1 115 . 19 PRO HG3 H 1.80 0.02 1 116 . 19 PRO HD2 H 3.54 0.02 2 117 . 19 PRO HD3 H 3.77 0.02 2 118 . 20 THR H H 8.08 0.02 1 119 . 20 THR HA H 4.43 0.02 1 120 . 20 THR HB H 4.03 0.02 1 121 . 20 THR HG2 H 1.01 0.02 1 122 . 21 ILE H H 8.16 0.02 1 123 . 21 ILE HA H 4.38 0.02 1 124 . 21 ILE HB H 1.72 0.02 1 125 . 21 ILE HD1 H 0.68 0.02 1 126 . 21 ILE HG12 H 1.08 0.02 2 127 . 21 ILE HG13 H 1.45 0.02 2 128 . 21 ILE HG2 H 0.80 0.02 1 129 . 22 PRO HA H 4.06 0.02 1 130 . 22 PRO HB2 H 1.72 0.02 2 131 . 22 PRO HB3 H 2.14 0.02 2 132 . 22 PRO HG2 H 1.45 0.02 2 133 . 22 PRO HG3 H 1.58 0.02 2 134 . 22 PRO HD2 H 3.53 0.02 2 135 . 22 PRO HD3 H 3.78 0.02 2 136 . 23 CYS H H 8.87 0.02 1 137 . 23 CYS HA H 4.84 0.02 1 138 . 23 CYS HB2 H 2.41 0.02 1 139 . 23 CYS HB3 H 2.93 0.02 1 140 . 24 CYS H H 9.23 0.02 1 141 . 24 CYS HA H 4.36 0.02 1 142 . 24 CYS HB2 H 2.45 0.02 1 143 . 24 CYS HB3 H 3.30 0.02 1 144 . 25 ARG H H 8.07 0.02 1 145 . 25 ARG HA H 4.01 0.02 1 146 . 25 ARG HB2 H 1.64 0.02 2 147 . 25 ARG HB3 H 1.77 0.02 2 148 . 25 ARG HG2 H 1.54 0.02 1 149 . 25 ARG HG3 H 1.54 0.02 1 150 . 25 ARG HD2 H 3.14 0.02 1 151 . 25 ARG HD3 H 3.14 0.02 1 152 . 25 ARG HE H 7.12 0.02 1 153 . 26 GLY H H 8.84 0.02 1 154 . 26 GLY HA2 H 3.53 0.02 2 155 . 26 GLY HA3 H 4.16 0.02 2 156 . 27 LEU H H 7.87 0.02 1 157 . 27 LEU HA H 4.90 0.02 1 158 . 27 LEU HB2 H 1.26 0.02 2 159 . 27 LEU HB3 H 2.09 0.02 2 160 . 27 LEU HG H 0.91 0.02 1 161 . 27 LEU HD1 H 0.52 0.02 2 162 . 27 LEU HD2 H 0.70 0.02 2 163 . 28 THR H H 9.13 0.02 1 164 . 28 THR HA H 4.42 0.02 1 165 . 28 THR HB H 3.58 0.02 1 166 . 28 THR HG2 H 0.88 0.02 1 167 . 29 CYS H H 8.77 0.02 1 168 . 29 CYS HA H 4.41 0.02 1 169 . 29 CYS HB2 H 2.81 0.02 1 170 . 29 CYS HB3 H 2.86 0.02 1 171 . 30 ARG H H 8.34 0.02 1 172 . 30 ARG HA H 4.47 0.02 1 173 . 30 ARG HB2 H 1.60 0.02 2 174 . 30 ARG HB3 H 1.74 0.02 2 175 . 30 ARG HG2 H 1.48 0.02 1 176 . 30 ARG HG3 H 1.48 0.02 1 177 . 30 ARG HD2 H 3.01 0.02 1 178 . 30 ARG HD3 H 3.01 0.02 1 179 . 30 ARG HE H 7.26 0.02 1 180 . 31 SER H H 8.64 0.02 1 181 . 31 SER HA H 3.95 0.02 1 182 . 31 SER HB2 H 3.71 0.02 1 183 . 31 SER HB3 H 3.71 0.02 1 184 . 32 TYR H H 7.90 0.02 1 185 . 32 TYR HA H 4.26 0.02 1 186 . 32 TYR HB2 H 2.60 0.02 2 187 . 32 TYR HB3 H 3.17 0.02 2 188 . 32 TYR HD1 H 7.02 0.02 1 189 . 32 TYR HD2 H 7.02 0.02 1 190 . 32 TYR HE1 H 6.67 0.02 1 191 . 32 TYR HE2 H 6.67 0.02 1 192 . 33 PHE H H 7.45 0.02 1 193 . 33 PHE HA H 4.88 0.02 1 194 . 33 PHE HB2 H 3.06 0.02 2 195 . 33 PHE HB3 H 3.23 0.02 2 196 . 33 PHE HD1 H 7.11 0.02 1 197 . 33 PHE HD2 H 7.11 0.02 1 198 . 33 PHE HE1 H 7.28 0.02 1 199 . 33 PHE HE2 H 7.28 0.02 1 200 . 33 PHE HZ H 7.04 0.02 1 201 . 34 PRO HA H 4.28 0.02 1 202 . 34 PRO HB2 H 2.15 0.02 2 203 . 34 PRO HB3 H 2.26 0.02 2 204 . 34 PRO HG2 H 1.93 0.02 1 205 . 34 PRO HG3 H 1.93 0.02 1 206 . 34 PRO HD2 H 3.68 0.02 2 207 . 34 PRO HD3 H 3.86 0.02 2 208 . 35 GLY H H 8.72 0.02 1 209 . 35 GLY HA2 H 3.61 0.02 2 210 . 35 GLY HA3 H 4.19 0.02 2 211 . 36 SER H H 8.06 0.02 1 212 . 36 SER HA H 3.96 0.02 1 213 . 36 SER HB2 H 3.38 0.02 1 214 . 36 SER HB3 H 3.38 0.02 1 215 . 37 THR H H 8.56 0.02 1 216 . 37 THR HA H 3.81 0.02 1 217 . 37 THR HB H 3.81 0.02 1 218 . 37 THR HG2 H 0.75 0.02 1 219 . 38 TYR H H 7.94 0.02 1 220 . 38 TYR HA H 5.11 0.02 1 221 . 38 TYR HB2 H 2.91 0.02 2 222 . 38 TYR HB3 H 3.39 0.02 2 223 . 38 TYR HD1 H 7.14 0.02 1 224 . 38 TYR HD2 H 7.14 0.02 1 225 . 38 TYR HE1 H 6.77 0.02 1 226 . 38 TYR HE2 H 6.77 0.02 1 227 . 39 GLY H H 8.82 0.02 1 228 . 39 GLY HA2 H 3.21 0.02 2 229 . 39 GLY HA3 H 3.51 0.02 2 230 . 40 ARG H H 7.72 0.02 1 231 . 40 ARG HA H 5.13 0.02 1 232 . 40 ARG HB2 H 1.47 0.02 1 233 . 40 ARG HB3 H 1.47 0.02 1 234 . 40 ARG HG2 H 1.41 0.02 1 235 . 40 ARG HG3 H 1.41 0.02 1 236 . 40 ARG HD2 H 2.95 0.02 2 237 . 40 ARG HD3 H 3.10 0.02 2 238 . 40 ARG HE H 7.04 0.02 1 239 . 41 CYS H H 8.41 0.02 1 240 . 41 CYS HA H 4.87 0.02 1 241 . 41 CYS HB2 H 2.55 0.02 1 242 . 41 CYS HB3 H 3.07 0.02 1 243 . 42 GLN H H 9.40 0.02 1 244 . 42 GLN HA H 4.94 0.02 1 245 . 42 GLN HB2 H 1.67 0.02 2 246 . 42 GLN HB3 H 2.09 0.02 2 247 . 42 GLN HG2 H 2.25 0.02 2 248 . 42 GLN HG3 H 2.33 0.02 2 249 . 42 GLN HE21 H 6.87 0.02 2 250 . 42 GLN HE22 H 7.24 0.02 2 251 . 43 ARG H H 8.89 0.02 1 252 . 43 ARG HA H 4.30 0.02 1 253 . 43 ARG HB2 H 1.59 0.02 2 254 . 43 ARG HB3 H 1.75 0.02 2 255 . 43 ARG HG2 H 1.45 0.02 2 256 . 43 ARG HG3 H 1.52 0.02 2 257 . 43 ARG HD2 H 3.09 0.02 1 258 . 43 ARG HD3 H 3.09 0.02 1 259 . 43 ARG HE H 7.09 0.02 1 260 . 44 TYR H H 7.52 0.02 1 261 . 44 TYR HA H 4.31 0.02 1 262 . 44 TYR HB2 H 2.86 0.02 1 263 . 44 TYR HB3 H 2.86 0.02 1 264 . 44 TYR HD1 H 6.96 0.02 1 265 . 44 TYR HD2 H 6.96 0.02 1 266 . 44 TYR HE1 H 6.65 0.02 1 267 . 44 TYR HE2 H 6.65 0.02 1 stop_ save_