data_5487 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and 1H assignments for Tachyplesin I, tyrosine mutant ; _BMRB_accession_number 5487 _BMRB_flat_file_name bmr5487.str _Entry_type original _Submission_date 2002-08-02 _Accession_date 2002-08-02 _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 Laederach Alain . . 2 Andreotti Amy H . 3 Fulton Donald B . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 193 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-11-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5486 'Tachyplesin I, Wild type' 5488 'Tachyplesin I, phenylalanine mutant' 5489 'Tachyplesin I, alanine mutant' stop_ _Original_release_date 2002-11-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives ; _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 Laederach Alain . . 2 Andreotti Amy H . 3 Fulton Donald B . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12359 _Page_last 12368 _Year 2002 _Details . loop_ _Keyword 'Tachyplesin I' 'beta hairpin' 'antimicrobial peptide' dodecylphosphocholine NMR stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34. ; _Citation_title 'Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9882437 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rao 'A G' G. . stop_ _Journal_abbreviation 'Arch. Biochem. Biophys.' _Journal_name_full 'Archives of biochemistry and biophysics' _Journal_volume 361 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 127 _Page_last 134 _Year 1999 _Details ; Tachyplesin is a potent antimicrobial peptide isolated from the hemocytes of the horseshoe crab, Tachypleus tridentatus. Previous studies have shown that the 17-residue peptide has an intrinsic amphipathic structure conferred by two antiparallel beta-sheets held rigidly by two disulfide bonds. Taking its short length into account and the potential of such a small polypeptide to take on multiple conformational states, one may assume that the disulfide bonds are relevant determinants of function. However, in order to gain a global perspective on the tolerance of cysteine residues in tachyplesin to amino acid substitutions, a series of linear peptides have been synthesized and their physicochemical properties analyzed. In these linear peptides, the cysteines have been replaced with amino acids possessing different side-chain properties, i.e., aliphatic hydrophobic (Ala, Leu, Ile, Val, and Met), aromatic hydrophobic (Phe and Tyr), and acidic (Asp). Activity assays using natural and synthetic membranes, and conformational measurements, highlight the subtle influence and variability of the amino acid side-chain properties on peptide structure. While an unequivocal interpretation of the results will have to await more refined structural measurements, our results indicate that a rigidly held disulfide-bonded beta-pleated sheet structure may not be absolutely essential for antimicrobial activity. Furthermore, the results challenge the accepted dogma of structure-activity relationships among antimicrobial peptides and suggest that the maintenance of peptide hydrophobic-hydrophilic balance may be a critical parameter, in addition to structure, in the design of peptides with pharmaceutical relevance. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16. ; _Citation_title 'A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8490053 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tamamura H . . 2 Kuroda M . . 3 Masuda M . . 4 Otaka A . . 5 Funakoshi S . . 6 Nakashima H . . 7 Yamamoto N . . 8 Waki M . . 9 Matsumoto A . . 10 Lancelin 'J M' M. . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et biophysica acta' _Journal_volume 1163 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 209 _Page_last 216 _Year 1993 _Details ; The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity. ; save_ ################################## # Molecular system description # ################################## save_system_TP _Saveframe_category molecular_system _Mol_system_name 'Tachyplesin I, tyrosine mutant' _Abbreviation_common TP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Tachyplesin I, tyrosine mutant' $TP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state Monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'antimicrobial peptide' stop_ _Database_query_date . _Details 'Solution structures were not computed for TPF4 and TPA4.' save_ ######################## # Monomeric polymers # ######################## save_TP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Tachyplesin I, tyrosine mutant' _Abbreviation_common TP _Molecular_mass . _Mol_thiol_state 'not present' _Details ; Wild type, has two disulfide bridges (C3-C16, and C7-C12). Wild Type, TPY4 and TPF4 adopt beta-hairpins. TPY4, TPF4 and TPA4 are mutants in which the four Cyteine residues are uniformly mutated to tyrosine, phenylalanine, and alanine, respectively. ; ############################## # Polymer residue sequence # ############################## _Residue_count 17 _Mol_residue_sequence KWYFRVYYRGIYYRRYR loop_ _Residue_seq_code _Residue_label 1 LYS 2 TRP 3 TYR 4 PHE 5 ARG 6 VAL 7 TYR 8 TYR 9 ARG 10 GLY 11 ILE 12 TYR 13 TYR 14 ARG 15 ARG 16 TYR 17 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1MA4 "Solution Structure Of Tachyplesin I Mutant Tpy4 In Water" 100.00 17 100.00 100.00 1.15e+00 PDB 1MA6 "Tpy4 Tachyplesin I Tyrosine Mutant In The Presence Of Dodecylphosphocholine Micelles (300 Mm)" 100.00 17 100.00 100.00 1.15e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $TP . . . . . . 'The peptide was synthetic and is not in any natural source.' 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 $TP 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_water_sample _Saveframe_category sample _Sample_type solution _Details 'All experiments in water were done in these conditions.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $TP . mM 0.5 1.0 . TFA 0.15 % . . . stop_ save_ save_DPC_micelle_sample _Saveframe_category sample _Sample_type Bi_cell _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TP 0.5 mM . TFA 0.15 % . Dodecylphosphocholine 320 mM '[U-98% D]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label . save_ save_2D_1H-1H_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H ROESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H ROESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_Water_4C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.0 0.2 n/a temperature 277 1 K 'ionic strength' 0.0015 0.0001 % stop_ save_ save_condition_DPC_40C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.0 0.2 n/a temperature 313 1 K 'ionic strength' 0.0015 0.0001 % 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_Shift_tyrosine_mutant_in_water _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $water_sample stop_ _Sample_conditions_label $condition_Water_4C _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Tachyplesin I, tyrosine mutant' _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 LYS HA H 3.964 0.001 1 2 . 1 LYS HB3 H 1.927 0.001 2 3 . 1 LYS HB2 H 1.899 0.001 2 4 . 2 TRP H H 8.776 0.001 1 5 . 2 TRP HA H 4.690 0.001 1 6 . 2 TRP HB3 H 2.967 0.001 2 7 . 2 TRP HB2 H 3.141 0.001 2 8 . 2 TRP HD1 H 7.139 0.001 1 9 . 2 TRP HE1 H 10.123 0.001 2 10 . 2 TRP HZ2 H 7.473 0.001 2 11 . 2 TRP HH2 H 7.210 0.001 1 12 . 2 TRP HZ3 H 6.938 0.001 2 13 . 2 TRP HE3 H 7.553 0.001 2 14 . 3 TYR H H 7.969 0.001 1 15 . 3 TYR HA H 4.619 0.001 1 16 . 3 TYR HB3 H 2.589 0.001 2 17 . 3 TYR HB2 H 2.705 0.001 2 18 . 3 TYR HD1 H 6.558 0.001 2 19 . 3 TYR HE1 H 6.711 0.001 2 20 . 4 PHE H H 8.456 0.001 1 21 . 4 PHE HA H 4.479 0.001 1 22 . 4 PHE HB2 H 2.989 0.001 2 23 . 4 PHE HD1 H 7.190 0.001 2 24 . 4 PHE HE1 H 7.278 0.001 2 25 . 5 ARG H H 8.321 0.001 1 26 . 5 ARG HA H 4.588 0.001 1 27 . 5 ARG HB3 H 1.487 0.001 2 28 . 5 ARG HB2 H 1.658 0.001 2 29 . 5 ARG HG3 H 1.408 0.001 2 30 . 5 ARG HG2 H 1.387 0.001 2 31 . 5 ARG HD2 H 2.874 0.001 2 32 . 6 VAL H H 8.585 0.001 1 33 . 6 VAL HA H 4.227 0.001 1 34 . 6 VAL HB H 1.919 0.001 1 35 . 6 VAL HG2 H 0.894 0.001 4 36 . 7 TYR H H 8.672 0.001 1 37 . 7 TYR HA H 4.710 0.001 1 38 . 7 TYR HB3 H 2.757 0.001 2 39 . 7 TYR HB2 H 2.948 0.001 2 40 . 7 TYR HD1 H 6.620 0.001 2 41 . 7 TYR HE1 H 6.609 0.001 2 42 . 8 TYR H H 8.748 0.001 1 43 . 8 TYR HA H 4.541 0.001 1 44 . 8 TYR HB2 H 2.878 0.001 2 45 . 8 TYR HD1 H 7.079 0.001 2 46 . 8 TYR HE1 H 6.900 0.001 2 47 . 9 ARG H H 8.788 0.001 1 48 . 9 ARG HA H 3.830 0.001 1 49 . 9 ARG HB3 H 1.433 0.001 2 50 . 9 ARG HB2 H 1.744 0.001 2 51 . 9 ARG HG3 H 1.302 0.001 2 52 . 9 ARG HG2 H 1.750 0.001 2 53 . 10 GLY H H 7.397 0.001 1 54 . 10 GLY HA3 H 3.721 0.001 2 55 . 10 GLY HA2 H 3.906 0.001 2 56 . 11 ILE H H 7.695 0.001 1 57 . 11 ILE HA H 5.269 0.001 1 58 . 11 ILE HB H 1.751 0.001 1 59 . 11 ILE HD1 H 0.546 0.001 1 60 . 11 ILE HG12 H 1.061 0.001 4 61 . 11 ILE HG13 H 0.811 0.001 4 62 . 11 ILE HG2 H 1.279 0.001 4 63 . 12 TYR H H 8.409 0.001 1 64 . 12 TYR HA H 4.767 0.001 1 65 . 12 TYR HB3 H 2.735 0.001 2 66 . 12 TYR HB2 H 2.799 0.001 2 67 . 12 TYR HD1 H 6.956 0.001 2 68 . 12 TYR HE1 H 6.736 0.001 2 69 . 13 TYR H H 8.705 0.001 1 70 . 13 TYR HA H 4.527 0.001 1 71 . 13 TYR HB2 H 2.800 0.001 2 72 . 13 TYR HD1 H 7.100 0.001 2 73 . 13 TYR HE1 H 6.873 0.001 2 74 . 14 ARG H H 8.519 0.001 1 75 . 14 ARG HA H 4.255 0.001 1 76 . 14 ARG HB3 H 1.607 0.001 2 77 . 14 ARG HB2 H 1.793 0.001 2 78 . 14 ARG HG2 H 1.468 0.001 2 79 . 14 ARG HD2 H 2.678 0.001 2 80 . 15 ARG H H 8.484 0.001 1 81 . 15 ARG HA H 4.381 0.001 1 82 . 15 ARG HG2 H 1.374 0.001 2 83 . 16 TYR H H 8.499 0.001 1 84 . 16 TYR HA H 4.742 0.001 1 85 . 16 TYR HB3 H 2.777 0.001 2 86 . 16 TYR HB2 H 2.966 0.001 2 87 . 16 TYR HD1 H 7.017 0.001 2 88 . 16 TYR HE1 H 6.759 0.001 2 89 . 17 ARG H H 8.396 0.001 1 90 . 17 ARG HA H 4.219 0.001 1 91 . 17 ARG HB3 H 1.555 0.001 2 92 . 17 ARG HB2 H 1.761 0.001 2 93 . 17 ARG HG2 H 0.907 0.001 2 94 . 17 ARG HD2 H 3.154 0.001 2 stop_ loop_ _Atom_shift_assign_ID_ambiguity 35 '35,35' '62,62,62,61,60' stop_ save_ save_Shift_tyrosine_mutant_in_DPC_micelles _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $DPC_micelle_sample stop_ _Sample_conditions_label $condition_DPC_40C _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Tachyplesin I, tyrosine mutant' _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 LYS HA H 3.920 0.001 1 2 . 1 LYS HB2 H 1.597 0.001 2 3 . 1 LYS HG2 H 1.241 0.001 2 4 . 1 LYS HZ H 7.606 0.001 1 5 . 2 TRP H H 8.044 0.001 1 6 . 2 TRP HA H 4.266 0.001 1 7 . 2 TRP HB3 H 2.983 0.001 2 8 . 2 TRP HB2 H 3.142 0.001 2 9 . 2 TRP HD1 H 7.130 0.001 1 10 . 2 TRP HE1 H 8.858 0.001 2 11 . 2 TRP HZ2 H 7.418 0.001 2 12 . 2 TRP HH2 H 7.074 0.001 1 13 . 2 TRP HZ3 H 6.967 0.001 2 14 . 2 TRP HE3 H 7.488 0.001 2 15 . 3 TYR H H 7.878 0.001 1 16 . 3 TYR HA H 4.245 0.001 1 17 . 3 TYR HB3 H 2.885 0.001 2 18 . 3 TYR HB2 H 3.013 0.001 2 19 . 3 TYR HD1 H 6.712 0.001 2 20 . 3 TYR HE1 H 6.681 0.001 2 21 . 4 PHE H H 7.648 0.001 1 22 . 4 PHE HA H 4.406 0.001 1 23 . 4 PHE HB3 H 3.015 0.001 2 24 . 4 PHE HB2 H 3.139 0.001 2 25 . 4 PHE HD1 H 7.181 0.001 2 26 . 4 PHE HE1 H 7.223 0.001 2 27 . 5 ARG H H 7.943 0.001 1 28 . 5 ARG HA H 4.025 0.001 1 29 . 5 ARG HB2 H 2.114 0.001 2 30 . 5 ARG HG2 H 1.609 0.001 2 31 . 5 ARG HD2 H 3.161 0.001 2 32 . 5 ARG HE H 7.470 0.001 1 33 . 6 VAL H H 7.577 0.001 1 34 . 6 VAL HA H 3.804 0.001 1 35 . 6 VAL HB H 2.066 0.001 1 36 . 6 VAL HG2 H 0.852 0.001 4 37 . 6 VAL HG1 H 0.979 0.001 4 38 . 7 TYR H H 7.650 0.001 1 39 . 7 TYR HA H 4.348 0.001 1 40 . 7 TYR HB2 H 2.963 0.001 2 41 . 7 TYR HD1 H 6.829 0.001 2 42 . 7 TYR HE1 H 6.714 0.001 2 43 . 8 TYR H H 7.956 0.001 1 44 . 8 TYR HA H 4.260 0.001 1 45 . 8 TYR HB3 H 3.003 0.001 2 46 . 8 TYR HB2 H 3.028 0.001 2 47 . 8 TYR HD1 H 7.097 0.001 2 48 . 8 TYR HE1 H 6.791 0.001 2 49 . 9 ARG H H 7.920 0.001 1 50 . 9 ARG HA H 4.070 0.001 1 51 . 9 ARG HB2 H 2.278 0.001 2 52 . 9 ARG HG2 H 1.627 0.001 2 53 . 9 ARG HD2 H 3.121 0.001 2 54 . 9 ARG HE H 7.407 0.001 1 55 . 10 GLY H H 7.987 0.001 1 56 . 10 GLY HA2 H 3.871 0.001 2 57 . 11 ILE H H 7.771 0.001 1 58 . 11 ILE HA H 3.884 0.001 1 59 . 11 ILE HB H 1.840 0.001 1 60 . 11 ILE HG12 H 1.437 0.001 4 61 . 11 ILE HD1 H 0.806 0.001 1 62 . 11 ILE HG13 H 1.587 0.001 4 63 . 11 ILE HG2 H 1.119 0.001 4 64 . 12 TYR H H 7.881 0.001 1 65 . 12 TYR HA H 4.511 0.001 1 66 . 12 TYR HB3 H 3.041 0.001 2 67 . 12 TYR HB2 H 2.708 0.001 2 68 . 12 TYR HD1 H 6.976 0.001 2 69 . 12 TYR HE1 H 6.732 0.001 2 70 . 13 TYR H H 7.900 0.001 1 71 . 13 TYR HA H 4.277 0.001 1 72 . 13 TYR HB2 H 2.987 0.001 2 73 . 13 TYR HD1 H 7.023 0.001 2 74 . 13 TYR HE1 H 6.831 0.001 2 75 . 14 ARG H H 7.801 0.001 1 76 . 14 ARG HA H 4.047 0.001 1 77 . 14 ARG HB2 H 2.256 0.001 2 78 . 14 ARG HG2 H 1.587 0.001 2 79 . 14 ARG HD2 H 3.126 0.001 2 80 . 14 ARG HE H 7.367 0.001 1 81 . 15 ARG H H 7.702 0.001 1 82 . 15 ARG HA H 4.111 0.001 1 83 . 15 ARG HB2 H 1.718 0.001 2 84 . 15 ARG HG2 H 1.293 0.001 2 85 . 15 ARG HD2 H 2.984 0.001 2 86 . 15 ARG HE H 7.146 0.001 1 87 . 16 TYR H H 7.878 0.001 1 88 . 16 TYR HA H 4.231 0.001 1 89 . 16 TYR HB3 H 2.885 0.001 2 90 . 16 TYR HB2 H 3.003 0.001 2 91 . 16 TYR HD1 H 6.755 0.001 2 92 . 16 TYR HE1 H 6.648 0.001 2 93 . 17 ARG H H 7.822 0.001 1 94 . 17 ARG HA H 4.089 0.001 1 95 . 17 ARG HB3 H 1.715 0.001 2 96 . 17 ARG HB2 H 1.833 0.001 2 97 . 17 ARG HG2 H 1.526 0.001 2 98 . 17 ARG HD2 H 3.121 0.001 2 99 . 17 ARG HE H 7.270 0.001 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 37 '37,37,36,36,36' '63,63,63,62,60' stop_ save_