data_25205 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the analgesic sea anemone peptide APETx2 ; _BMRB_accession_number 25205 _BMRB_flat_file_name bmr25205.str _Entry_type original _Submission_date 2014-09-07 _Accession_date 2014-09-07 _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 Mobli Mehdi . . 2 King Glenn F. . 3 Rosengren Johan K. . 4 Jensen Jonas E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 228 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-12-22 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6467 'Solution structure of APETx2' stop_ _Original_release_date 2014-12-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Understanding the Molecular Basis of Toxin Promiscuity: The Analgesic Sea Anemone Peptide APETx2 Interacts with Acid-Sensing Ion Channel 3 and hERG Channels via Overlapping Pharmacophores' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25337890 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jensen Jonas E. . 2 Cristofori-Armstrong Ben . . 3 Anangi Raveendra . . 4 Rosengren Johan K. . 5 Lau Carus . . 6 Mobli Mehdi . . 7 Brust Andreas . . 8 Alewood Paul F. . 9 King Glenn F. . 10 Rash Lachlan D. . stop_ _Journal_abbreviation 'J. Med. Chem.' _Journal_volume 57 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9195 _Page_last 9203 _Year 2014 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_Solution_structure_of_APETx2 _Saveframe_category citation _Citation_full . _Citation_title 'Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15987885 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chagot Benjamin . . 2 Escoubas Pierre . . 3 Diochot Sylvie . . 4 Bernard Cedric . . 5 Lazdunski Michel . . 6 Darbon Herve . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full . _Journal_volume 14 _Journal_issue . _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 2003 _Page_last 2010 _Year 2005 _Details . save_ save_APETx2_structure _Saveframe_category citation _Citation_full . _Citation_title 'Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15987885 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chagot B. . . 2 Escoubas P. . . 3 Diochot S. . . 4 Bernard C. . . 5 Lazdunski M. . . 6 Darbon H. . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full . _Journal_volume 14 _Journal_issue 8 _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 2003 _Page_last 2010 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'analgesic sea anemone peptide APETx2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $APETx2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_APETx2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common APETx2 _Molecular_mass 4571.133 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 42 _Mol_residue_sequence ; GTACSCGNSKGIYWFYRPSC PTDRGYTGSCRYFLGTCCTP AD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 THR 3 3 ALA 4 4 CYS 5 5 SER 6 6 CYS 7 7 GLY 8 8 ASN 9 9 SER 10 10 LYS 11 11 GLY 12 12 ILE 13 13 TYR 14 14 TRP 15 15 PHE 16 16 TYR 17 17 ARG 18 18 PRO 19 19 SER 20 20 CYS 21 21 PRO 22 22 THR 23 23 ASP 24 24 ARG 25 25 GLY 26 26 TYR 27 27 THR 28 28 GLY 29 29 SER 30 30 CYS 31 31 ARG 32 32 TYR 33 33 PHE 34 34 LEU 35 35 GLY 36 36 THR 37 37 CYS 38 38 CYS 39 39 THR 40 40 PRO 41 41 ALA 42 42 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1WXN "Solution Structure Of Apetx2, A Specific Peptide Inhibitor Of Asic3 Proton-Gated Channels" 100.00 42 100.00 100.00 1.54e-20 SP P61542 "RecName: Full=Pi-actitoxin-Ael2b; Short=Pi-AITX-Ael2b; AltName: Full=Toxin APETx2" 100.00 42 100.00 100.00 1.54e-20 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $APETx2 'clonal anemone' 6110 Eukaryota Metazoa Anthopleura elegantissima 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 _Details $APETx2 'chemical synthesis' . . . . . 'See Jensen et al. (2009) Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel. Toxicon 54, 56-61' 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 $APETx2 300 uM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version + loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task processing collection stop_ _Details . save_ save_Rowland_NMR_Toolkit _Saveframe_category software _Name Rowland_NMR_Toolkit _Version 3 loop_ _Vendor _Address _Electronic_address 'J. C. Hoch & A. S. Stern' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details 'Equipped with Cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 6 . pH pressure 1 . atm 'ionic strength' 20 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 _Indirect_shift_ratio water H 1 protons ppm 4.773 internal direct . . . 1.0 water C 13 protons ppm 4.773 internal indirect . . . 0.251449530 water N 15 protons ppm 4.773 internal indirect . . . 0.101329118 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _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 2 THR H H 8.287 0.020 1 2 2 2 THR HA H 4.386 0.020 1 3 2 2 THR HB H 4.202 0.020 1 4 2 2 THR HG2 H 1.324 0.020 1 5 3 3 ALA H H 8.466 0.020 1 6 3 3 ALA HA H 4.548 0.020 1 7 3 3 ALA HB H 1.449 0.020 1 8 4 4 CYS H H 7.772 0.020 1 9 4 4 CYS HA H 4.541 0.020 1 10 4 4 CYS HB2 H 1.594 0.020 2 11 4 4 CYS HB3 H 2.493 0.020 2 12 5 5 SER H H 7.268 0.020 1 13 5 5 SER HA H 4.936 0.020 1 14 5 5 SER HB2 H 3.557 0.020 2 15 5 5 SER HB3 H 3.681 0.020 2 16 6 6 CYS H H 8.318 0.020 1 17 6 6 CYS HA H 4.892 0.020 1 18 6 6 CYS HB2 H 2.544 0.020 2 19 6 6 CYS HB3 H 3.145 0.020 2 20 7 7 GLY H H 9.043 0.020 1 21 7 7 GLY HA2 H 3.642 0.020 2 22 7 7 GLY HA3 H 3.968 0.020 2 23 8 8 ASN H H 8.919 0.020 1 24 8 8 ASN HA H 4.742 0.020 1 25 8 8 ASN HB2 H 2.932 0.020 2 26 8 8 ASN HB3 H 2.770 0.020 2 27 8 8 ASN HD21 H 7.595 0.020 2 28 8 8 ASN HD22 H 6.928 0.020 2 29 9 9 SER H H 7.987 0.020 1 30 9 9 SER HA H 4.597 0.020 1 31 9 9 SER HB2 H 3.767 0.020 2 32 9 9 SER HB3 H 3.892 0.020 2 33 10 10 LYS H H 8.620 0.020 1 34 10 10 LYS HA H 4.348 0.020 1 35 10 10 LYS HB2 H 1.978 0.020 2 36 10 10 LYS HB3 H 1.849 0.020 2 37 10 10 LYS HG2 H 1.599 0.020 2 38 10 10 LYS HG3 H 1.492 0.020 2 39 10 10 LYS HD2 H 1.693 0.020 2 40 10 10 LYS HD3 H 1.693 0.020 2 41 10 10 LYS HE2 H 2.984 0.020 2 42 10 10 LYS HE3 H 2.984 0.020 2 43 11 11 GLY H H 8.420 0.020 1 44 11 11 GLY HA2 H 4.594 0.020 2 45 11 11 GLY HA3 H 3.421 0.020 2 46 12 12 ILE H H 8.740 0.020 1 47 12 12 ILE HA H 4.726 0.020 1 48 12 12 ILE HB H 1.919 0.020 1 49 12 12 ILE HG12 H 1.452 0.020 2 50 12 12 ILE HG13 H 1.846 0.020 2 51 12 12 ILE HG2 H 0.727 0.020 1 52 12 12 ILE HD1 H 0.807 0.020 1 53 13 13 TYR H H 8.682 0.020 1 54 13 13 TYR HA H 4.754 0.020 1 55 13 13 TYR HB2 H 2.237 0.020 2 56 13 13 TYR HB3 H 2.678 0.020 2 57 13 13 TYR HD1 H 6.684 0.020 3 58 13 13 TYR HD2 H 6.684 0.020 3 59 13 13 TYR HE1 H 7.023 0.020 3 60 13 13 TYR HE2 H 7.023 0.020 3 61 14 14 TRP H H 9.276 0.020 1 62 14 14 TRP HA H 4.278 0.020 1 63 14 14 TRP HB2 H 2.981 0.020 2 64 14 14 TRP HB3 H 3.051 0.020 2 65 14 14 TRP HD1 H 7.042 0.020 1 66 14 14 TRP HE1 H 9.659 0.020 1 67 14 14 TRP HE3 H 7.736 0.020 1 68 14 14 TRP HZ2 H 7.669 0.020 1 69 14 14 TRP HZ3 H 7.242 0.020 1 70 14 14 TRP HH2 H 7.289 0.020 1 71 15 15 PHE H H 7.794 0.020 1 72 15 15 PHE HA H 3.836 0.020 1 73 15 15 PHE HB2 H 2.765 0.020 2 74 15 15 PHE HB3 H 2.452 0.020 2 75 15 15 PHE HD1 H 6.955 0.020 3 76 15 15 PHE HD2 H 6.955 0.020 3 77 15 15 PHE HE1 H 7.126 0.020 3 78 15 15 PHE HE2 H 7.126 0.020 3 79 16 16 TYR H H 8.599 0.020 1 80 16 16 TYR HA H 4.244 0.020 1 81 16 16 TYR HB2 H 3.288 0.020 2 82 16 16 TYR HB3 H 2.767 0.020 2 83 16 16 TYR HD1 H 7.037 0.020 3 84 16 16 TYR HD2 H 7.037 0.020 3 85 16 16 TYR HE1 H 6.819 0.020 3 86 16 16 TYR HE2 H 6.819 0.020 3 87 17 17 ARG H H 7.355 0.020 1 88 17 17 ARG HA H 5.002 0.020 1 89 17 17 ARG HB2 H 2.068 0.020 2 90 17 17 ARG HB3 H 1.854 0.020 2 91 17 17 ARG HG2 H 1.811 0.020 2 92 17 17 ARG HG3 H 1.811 0.020 2 93 17 17 ARG HD2 H 3.383 0.020 2 94 17 17 ARG HD3 H 3.253 0.020 2 95 17 17 ARG HE H 7.228 0.020 1 96 18 18 PRO HA H 4.424 0.020 1 97 18 18 PRO HB2 H 2.117 0.020 2 98 18 18 PRO HB3 H 2.063 0.020 2 99 18 18 PRO HG2 H 1.909 0.020 2 100 18 18 PRO HG3 H 2.053 0.020 2 101 18 18 PRO HD2 H 3.888 0.020 2 102 18 18 PRO HD3 H 3.789 0.020 2 103 19 19 SER H H 7.154 0.020 1 104 19 19 SER HA H 4.489 0.020 1 105 19 19 SER HB2 H 3.752 0.020 2 106 19 19 SER HB3 H 3.752 0.020 2 107 20 20 CYS H H 8.697 0.020 1 108 20 20 CYS HA H 4.088 0.020 1 109 20 20 CYS HB2 H 2.778 0.020 2 110 20 20 CYS HB3 H 2.827 0.020 2 111 21 21 PRO HA H 4.349 0.020 1 112 21 21 PRO HB2 H 2.111 0.020 2 113 21 21 PRO HB3 H 1.595 0.020 2 114 21 21 PRO HG2 H 0.722 0.020 2 115 21 21 PRO HG3 H 0.812 0.020 2 116 21 21 PRO HD2 H 2.763 0.020 2 117 21 21 PRO HD3 H 2.492 0.020 2 118 22 22 THR H H 8.515 0.020 1 119 22 22 THR HA H 4.215 0.020 1 120 22 22 THR HB H 4.490 0.020 1 121 22 22 THR HG2 H 1.177 0.020 1 122 23 23 ASP H H 8.576 0.020 1 123 23 23 ASP HA H 4.649 0.020 1 124 23 23 ASP HB2 H 2.945 0.020 2 125 23 23 ASP HB3 H 2.518 0.020 2 126 24 24 ARG H H 8.134 0.020 1 127 24 24 ARG HA H 4.379 0.020 1 128 24 24 ARG HB2 H 1.567 0.020 2 129 24 24 ARG HB3 H 0.724 0.020 2 130 24 24 ARG HG2 H 1.313 0.020 2 131 24 24 ARG HG3 H 1.441 0.020 2 132 24 24 ARG HD2 H 3.215 0.020 2 133 24 24 ARG HD3 H 3.189 0.020 2 134 24 24 ARG HE H 7.929 0.020 1 135 25 25 GLY H H 8.262 0.020 1 136 25 25 GLY HA2 H 3.604 0.020 2 137 25 25 GLY HA3 H 3.786 0.020 2 138 26 26 TYR H H 7.786 0.020 1 139 26 26 TYR HA H 4.835 0.020 1 140 26 26 TYR HB2 H 2.754 0.020 2 141 26 26 TYR HB3 H 3.380 0.020 2 142 26 26 TYR HD1 H 7.105 0.020 3 143 26 26 TYR HD2 H 7.105 0.020 3 144 26 26 TYR HE1 H 6.682 0.020 3 145 26 26 TYR HE2 H 6.682 0.020 3 146 27 27 THR H H 9.713 0.020 1 147 27 27 THR HA H 4.573 0.020 1 148 27 27 THR HB H 4.510 0.020 1 149 27 27 THR HG2 H 1.218 0.020 1 150 28 28 GLY H H 8.365 0.020 1 151 28 28 GLY HA2 H 4.474 0.020 2 152 28 28 GLY HA3 H 3.690 0.020 2 153 29 29 SER H H 8.085 0.020 1 154 29 29 SER HA H 5.548 0.020 1 155 29 29 SER HB2 H 3.616 0.020 2 156 29 29 SER HB3 H 4.209 0.020 2 157 29 29 SER HG H 5.549 0.020 1 158 30 30 CYS H H 8.745 0.020 1 159 30 30 CYS HA H 4.944 0.020 1 160 30 30 CYS HB2 H 3.427 0.020 2 161 30 30 CYS HB3 H 3.139 0.020 2 162 31 31 ARG H H 8.694 0.020 1 163 31 31 ARG HA H 4.448 0.020 1 164 31 31 ARG HB2 H 1.752 0.020 2 165 31 31 ARG HB3 H 1.729 0.020 2 166 31 31 ARG HG2 H 1.787 0.020 2 167 31 31 ARG HG3 H 1.650 0.020 2 168 31 31 ARG HD2 H 3.209 0.020 2 169 31 31 ARG HD3 H 3.209 0.020 2 170 31 31 ARG HE H 7.130 0.020 1 171 32 32 TYR H H 8.230 0.020 1 172 32 32 TYR HA H 4.486 0.020 1 173 32 32 TYR HB2 H 2.657 0.020 2 174 32 32 TYR HB3 H 2.820 0.020 2 175 32 32 TYR HD1 H 6.766 0.020 3 176 32 32 TYR HD2 H 6.766 0.020 3 177 32 32 TYR HE1 H 6.688 0.020 3 178 32 32 TYR HE2 H 6.688 0.020 3 179 33 33 PHE H H 8.581 0.020 1 180 33 33 PHE HA H 4.038 0.020 1 181 33 33 PHE HB2 H 2.989 0.020 2 182 33 33 PHE HB3 H 3.032 0.020 2 183 33 33 PHE HD1 H 6.827 0.020 3 184 33 33 PHE HD2 H 6.827 0.020 3 185 33 33 PHE HE1 H 7.215 0.020 3 186 33 33 PHE HE2 H 7.215 0.020 3 187 34 34 LEU H H 7.972 0.020 1 188 34 34 LEU HA H 4.523 0.020 1 189 34 34 LEU HB2 H 1.742 0.020 2 190 34 34 LEU HB3 H 1.787 0.020 2 191 34 34 LEU HG H 1.382 0.020 1 192 34 34 LEU HD1 H 0.952 0.020 2 193 34 34 LEU HD2 H 0.840 0.020 2 194 35 35 GLY H H 8.290 0.020 1 195 35 35 GLY HA2 H 4.347 0.020 2 196 35 35 GLY HA3 H 4.347 0.020 2 197 36 36 THR H H 8.408 0.020 1 198 36 36 THR HA H 4.792 0.020 1 199 36 36 THR HB H 3.532 0.020 1 200 36 36 THR HG1 H 5.592 0.020 1 201 36 36 THR HG2 H 1.076 0.020 1 202 37 37 CYS H H 9.382 0.020 1 203 37 37 CYS HA H 5.070 0.020 1 204 37 37 CYS HB2 H 2.143 0.020 2 205 37 37 CYS HB3 H 3.342 0.020 2 206 38 38 CYS H H 8.664 0.020 1 207 38 38 CYS HA H 4.626 0.020 1 208 38 38 CYS HB2 H 2.051 0.020 2 209 38 38 CYS HB3 H 1.143 0.020 2 210 39 39 THR H H 8.337 0.020 1 211 39 39 THR HA H 4.707 0.020 1 212 39 39 THR HB H 4.001 0.020 1 213 39 39 THR HG1 H 5.547 0.020 1 214 39 39 THR HG2 H 0.590 0.020 1 215 40 40 PRO HA H 4.947 0.020 1 216 40 40 PRO HB2 H 2.523 0.020 2 217 40 40 PRO HB3 H 2.295 0.020 2 218 40 40 PRO HG2 H 2.024 0.020 2 219 40 40 PRO HG3 H 1.971 0.020 2 220 40 40 PRO HD2 H 4.048 0.020 2 221 40 40 PRO HD3 H 3.926 0.020 2 222 41 41 ALA H H 7.610 0.020 1 223 41 41 ALA HA H 4.209 0.020 1 224 41 41 ALA HB H 1.276 0.020 1 225 42 42 ASP H H 8.273 0.020 1 226 42 42 ASP HA H 4.387 0.020 1 227 42 42 ASP HB2 H 2.708 0.020 2 228 42 42 ASP HB3 H 2.708 0.020 2 stop_ save_