data_4725 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Determination of the three dimensional structure and HN--S hydrogen bonding of the synthetic 113Cd3-beta-N domain of lobster MT-1 by Nuclear Magnetic Resonance ; _BMRB_accession_number 4725 _BMRB_flat_file_name bmr4725.str _Entry_type original _Submission_date 2000-04-25 _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 Munoz Amalia . . 2 Forsterling F. Holger . 3 Shaw C. Frank III 4 Petering David H . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 4 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 "13C chemical shifts" 41 "coupling constants" 34 "113Cd chemical shifts" 3 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-03 original author . stop_ _Original_release_date 2002-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the 113Cd3 Beta Domains from Homarus americanus Metallothionein-1: Hydrogen bonding and Solvent Accessibility of Sulfur Atoms ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22191392 _PubMed_ID 12203008 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Munoz Amalia . . 2 Forsterling F. Holger . 3 Shaw C. Frank III 4 Petering David H . stop_ _Journal_abbreviation 'J. Biol. Inorg. Chem.' _Journal_volume 7 _Journal_issue 7-8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 713 _Page_last 724 _Year 2002 _Details . loop_ _Keyword lobster metallothionein 2D-NMR beta-domain H-bonding stop_ save_ ################################## # Molecular system description # ################################## save_MT _Saveframe_category molecular_system _Mol_system_name metallothionein _Abbreviation_common MT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'beta n' $beta_n 'Cd II' $CD 'Cd III' $CD 'Cd V' $CD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function ; metal detoxification Cu-regulation ; stop_ _Database_query_date . _Details ; Cadmium numbering was done according to the 113Cd chemical shifts within the whole protein (i.e. Cd_II has the same chemical shift than Cd(II) of the holoprotein). ; save_ ######################## # Monomeric polymers # ######################## save_beta_n _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'beta n' _Name_variant 'beta n' _Abbreviation_common 'beta n' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 28 _Mol_residue_sequence ; PGPCCKDKCECAEGGCKTGC KCTSCRCA ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 GLY 3 PRO 4 CYS 5 CYS 6 LYS 7 ASP 8 LYS 9 CYS 10 GLU 11 CYS 12 ALA 13 GLU 14 GLY 15 GLY 16 CYS 17 LYS 18 THR 19 GLY 20 CYS 21 LYS 22 CYS 23 THR 24 SER 25 CYS 26 ARG 27 CYS 28 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-29 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 1J5M "Solution Structure Of The Synthetic 113cd_3 Beta_n Domain Of Lobster Metallothionein-1" 96.43 28 100.00 100.00 6.87e-07 EMBL CAC42504 "metallothionein [Homarus americanus]" 100.00 58 100.00 100.00 2.21e-07 EMBL CAC80859 "metallothionein [Homarus americanus]" 100.00 58 100.00 100.00 2.21e-07 SP P29499 "RecName: Full=Metallothionein-1; AltName: Full=CuMT-1" 100.00 58 100.00 100.00 2.28e-07 stop_ save_ ############# # Ligands # ############# save_CD _Saveframe_category ligand _Mol_type non-polymer _Name_common "CD (CADMIUM ION)" _BMRB_code . _PDB_code CD _Molecular_mass 112.411 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jul 19 10:41:15 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CD CD CD . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $beta_n Lobster 6706 Eukaryota Metazoa Homarus americanus hepatopancreas 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 $beta_n '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 $beta_n 4.0 mM '[U-99% 113Cd]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 loop_ _Task 'resonance assignments' stop_ _Details . 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_TOCSY_(278,_283,_298_and_313_K),_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY (278, 283, 298 and 313 K),' _Sample_label $sample_1 save_ save_NOESY_(60_and_150_ms_at_278_and_298_K)_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY (60 and 150 ms at 278 and 298 K)' _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_P.E._COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'P.E. COSY' _Sample_label $sample_1 save_ save_1H-113Cd-HSQC-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-113Cd-HSQC-TOCSY _Sample_label $sample_1 save_ save_HSED_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSED _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY (278, 283, 298 and 313 K),' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY (60 and 150 ms at 278 and 298 K)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'P.E. COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-113Cd-HSQC-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSED _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 298 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.78 internal direct . internal . . $entry_citation $entry_citation DSS C 13 'methyl protons' ppm . external indirect . . . 0.25144954 $entry_citation $entry_citation Cd(ClO4)2 Cd 113 cadmium ppm 0.0 external direct . . . . $entry_citation $entry_citation 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 ; 113Cd chemical shifts at 298K are: 648.6 ppm for Cd(II), 646.3 ppm for Cd(III) and 640.8 ppm for Cd(V) ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'beta n' _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 PRO HA H 4.54 0.03 1 2 . 1 PRO HB2 H 2.31 0.03 2 3 . 1 PRO HB3 H 2.11 0.03 2 4 . 1 PRO HD2 H 3.52 0.03 2 5 . 1 PRO HD3 H 3.42 0.03 2 6 . 2 GLY HA2 H 4.08 0.03 2 7 . 2 GLY HA3 H 3.92 0.03 2 8 . 2 GLY CA C 42.18 0.3 1 9 . 3 PRO HA H 4.44 0.03 1 10 . 3 PRO HB2 H 2.165 0.03 2 11 . 3 PRO HD2 H 3.79 0.03 2 12 . 3 PRO HD3 H 3.38 0.03 2 13 . 4 CYS H H 7.59 0.03 1 14 . 4 CYS HA H 4.92 0.03 1 15 . 4 CYS HB2 H 3.12 0.03 2 16 . 4 CYS HB3 H 3.00 0.03 2 17 . 4 CYS CA C 54.33 0.3 1 18 . 4 CYS CB C 30.45 0.3 1 19 . 5 CYS H H 10.08 0.03 1 20 . 5 CYS HA H 4.60 0.03 1 21 . 5 CYS CA C 58.09 0.3 1 22 . 5 CYS CB C 25.72 0.3 1 23 . 6 LYS H H 8.45 0.03 1 24 . 6 LYS HA H 3.84 0.03 1 25 . 6 LYS HB2 H 1.67 0.03 2 26 . 6 LYS HB3 H 1.59 0.03 2 27 . 6 LYS CA C 57.70 0.3 1 28 . 6 LYS CB C 30.02 0.3 1 29 . 6 LYS CG C 22.95 0.3 1 30 . 7 ASP H H 8.74 0.03 1 31 . 7 ASP HA H 4.65 0.03 1 32 . 7 ASP HB2 H 2.63 0.03 2 33 . 7 ASP HB3 H 2.47 0.03 2 34 . 8 LYS H H 7.68 0.03 1 35 . 8 LYS HA H 4.29 0.03 1 36 . 8 LYS HB2 H 1.86 0.03 2 37 . 8 LYS HB3 H 1.63 0.03 2 38 . 8 LYS HG2 H 1.26 0.03 2 39 . 8 LYS HG3 H 0.90 0.03 2 40 . 8 LYS CA C 52.18 0.3 1 41 . 8 LYS CB C 31.15 0.3 1 42 . 8 LYS CG C 20.56 0.3 1 43 . 8 LYS CD C 26.82 0.3 1 44 . 8 LYS CE C 39.75 0.3 1 45 . 9 CYS H H 8.77 0.03 1 46 . 9 CYS HA H 4.26 0.03 1 47 . 9 CYS HB2 H 2.76 0.03 2 48 . 9 CYS HB3 H 2.84 0.03 2 49 . 10 GLU H H 8.68 0.03 1 50 . 10 GLU HA H 4.63 0.03 1 51 . 10 GLU HB2 H 2.19 0.03 2 52 . 10 GLU HG2 H 2.37 0.03 2 53 . 10 GLU HG3 H 2.11 0.03 2 54 . 10 GLU CA C 53.90 0.3 1 55 . 11 CYS H H 8.22 0.03 1 56 . 11 CYS HA H 4.60 0.03 1 57 . 11 CYS HB2 H 2.52 0.03 2 58 . 11 CYS HB3 H 2.81 0.03 2 59 . 11 CYS CA C 63.95 0.3 1 60 . 12 ALA H H 8.83 0.03 1 61 . 12 ALA HA H 4.14 0.03 1 62 . 12 ALA HB H 1.34 0.03 1 63 . 12 ALA CB C 15.44 0.3 1 64 . 13 GLU H H 7.72 0.03 1 65 . 13 GLU HA H 4.33 0.03 1 66 . 13 GLU HB2 H 2.16 0.03 2 67 . 13 GLU HB3 H 2.05 0.03 2 68 . 13 GLU CA C 53.79 0.3 1 69 . 13 GLU CB C 27.48 0.3 1 70 . 13 GLU CG C 34.05 0.3 1 71 . 14 GLY H H 7.91 0.03 1 72 . 14 GLY HA2 H 4.12 0.03 1 73 . 14 GLY CA C 44.17 0.3 1 74 . 15 GLY H H 8.18 0.03 1 75 . 15 GLY HA2 H 4.27 0.03 2 76 . 15 GLY HA3 H 3.72 0.03 2 77 . 15 GLY CA C 43.23 0.3 1 78 . 16 CYS H H 8.65 0.03 1 79 . 16 CYS HA H 4.78 0.03 1 80 . 16 CYS HB2 H 3.13 0.03 2 81 . 16 CYS HB3 H 3.05 0.03 2 82 . 16 CYS CA C 60.71 0.3 1 83 . 16 CYS CB C 29.51 0.3 1 84 . 17 LYS H H 9.40 0.03 1 85 . 17 LYS HA H 4.70 0.03 1 86 . 17 LYS HB2 H 1.97 0.03 2 87 . 17 LYS HB3 H 1.40 0.03 2 88 . 17 LYS CA C 50.93 0.3 1 89 . 17 LYS CB C 33.97 0.3 1 90 . 18 THR H H 8.71 0.03 1 91 . 18 THR HA H 3.87 0.03 1 92 . 18 THR HB H 3.89 0.03 1 93 . 18 THR HG2 H 1.17 0.03 1 94 . 18 THR CA C 62.70 0.3 1 95 . 18 THR CB C 66.53 0.3 1 96 . 19 GLY H H 9.42 0.03 1 97 . 19 GLY HA2 H 4.19 0.03 2 98 . 19 GLY HA3 H 3.53 0.03 2 99 . 20 CYS H H 7.23 0.03 1 100 . 20 CYS HA H 3.92 0.03 1 101 . 20 CYS HB2 H 2.85 0.03 2 102 . 20 CYS HB3 H 3.11 0.03 2 103 . 21 LYS H H 9.61 0.03 1 104 . 21 LYS HA H 4.53 0.03 1 105 . 21 LYS HB2 H 2.07 0.03 2 106 . 21 LYS CA C 52.61 0.3 1 107 . 21 LYS CB C 31.58 0.3 1 108 . 22 CYS H H 9.27 0.03 1 109 . 22 CYS HA H 4.30 0.03 1 110 . 22 CYS HB2 H 2.79 0.03 2 111 . 22 CYS HB3 H 3.06 0.03 2 112 . 22 CYS CA C 58.09 0.3 1 113 . 22 CYS CB C 30.18 0.3 1 114 . 23 THR H H 8.92 0.03 1 115 . 23 THR HA H 4.60 0.03 1 116 . 23 THR HG2 H 1.24 0.03 1 117 . 23 THR CB C 66.57 0.3 1 118 . 24 SER H H 9.57 0.03 1 119 . 24 SER HA H 4.53 0.03 1 120 . 24 SER HB2 H 3.90 0.03 2 121 . 24 SER HB3 H 3.76 0.03 2 122 . 24 SER CA C 57.66 0.3 1 123 . 24 SER CB C 61.72 0.3 1 124 . 25 CYS H H 7.38 0.03 1 125 . 25 CYS HA H 4.97 0.03 1 126 . 25 CYS HB2 H 3.57 0.03 2 127 . 25 CYS HB3 H 2.97 0.03 2 128 . 25 CYS CA C 52.73 0.3 1 129 . 25 CYS CB C 32.87 0.3 1 130 . 26 ARG H H 8.65 0.03 1 131 . 26 ARG HA H 5.02 0.03 1 132 . 26 ARG HB2 H 1.71 0.03 2 133 . 26 ARG HB3 H 1.63 0.03 2 134 . 26 ARG HG2 H 1.57 0.03 2 135 . 26 ARG HG3 H 1.47 0.03 2 136 . 26 ARG CA C 55.90 0.3 1 137 . 27 CYS H H 8.36 0.03 1 138 . 27 CYS HA H 3.51 0.03 1 139 . 27 CYS HB2 H 2.49 0.03 2 140 . 27 CYS HB3 H 2.88 0.03 2 141 . 27 CYS CA C 59.54 0.3 1 142 . 27 CYS CB C 28.22 0.3 1 143 . 28 ALA H H 8.11 0.03 1 144 . 28 ALA HA H 4.00 0.03 1 145 . 28 ALA HB H 1.26 0.03 1 146 . 28 ALA CA C 51.48 0.3 1 147 . 28 ALA CB C 18.06 0.3 1 stop_ save_ save_chemical_shifts_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Cd II' _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 CD Cd Cd 648.6 . 1 stop_ save_ save_chemical_shifts_3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Cd III' _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 CD Cd Cd 646.3 . 1 stop_ save_ save_chemical_shifts_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Cd V' _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 CD Cd Cd 640.8 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'beta n' _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 CYS H 4 CYS HA 8.3 . . 2 2 3JHNHA 5 CYS H 5 CYS HA 8.6 . . 2 3 3JHNHA 6 LYS H 6 LYS HA 7.5 . . 2 4 3JHNHA 7 ASP H 7 ASP HA 10.9 . . 2 5 3JHNHA 8 LYS H 8 LYS HA 8.7 . . 2 6 3JHNHA 9 CYS H 9 CYS HA 8.0 . . 2 7 3JHNHA 10 GLU H 10 GLU HA 11.2 . . 2 8 3JHNHA 11 CYS H 11 CYS HA 7.3 . . 2 9 3JHNHA 12 ALA H 12 ALA HA 8.8 . . 2 10 3JHNHA 13 GLU H 13 GLU HA 9.9 . . 2 11 3JHNHA 16 CYS H 16 CYS HA 7.1 . . 2 12 3JHNHA 17 LYS H 17 LYS HA 10.3 . . 2 13 3JHNHA 18 THR H 18 THR HA 8.32 . . 2 14 3JHNHA 20 CYS H 20 CYS HA 5.3 . . 2 15 3JHNHA 21 LYS H 21 LYS HA 10.9 . . 2 16 3JHNHA 22 CYS H 22 CYS HA 5.9 . . 2 17 3JHNHA 23 THR H 23 THR HA 9.6 . . 2 18 3JHNHA 24 SER H 24 SER HA 8.5 . . 2 19 3JHNHA 25 CYS H 25 CYS HA 9.6 . . 2 20 3JHNHA 26 ARG H 26 ARG HA 14.0 . . 2 21 3JHNHA 27 CYS H 27 CYS HA 11.0 . . 2 22 3JHNHA 28 ALA H 28 ALA HA 8.1 . . 2 23 3JHAHB2 9 CYS HA 9 CYS HB2 11.0 . . 2 24 3JHAHB3 9 CYS HA 9 CYS HB3 6.0 . . 2 25 3JHAHB 11 CYS HA 11 CYS HB2 9.0 . . 2 26 3JHAHB 11 CYS HA 11 CYS HB3 3.0 . . 2 27 3JHAHB 20 CYS HA 20 CYS HB2 5.3 . . 2 28 3JHAHB 20 CYS HA 20 CYS HB3 7.0 . . 2 29 3JHAHB2 22 CYS HA 22 CYS HB2 12.0 . . 2 30 3JHAHB3 22 CYS HA 22 CYS HB3 5.2 . . 2 31 3JHAHB2 25 CYS HA 25 CYS HB2 5.0 . . 2 32 3JHAHB3 25 CYS HA 25 CYS HB3 3.0 . . 2 33 3JHAHB2 27 CYS HA 27 CYS HB2 4.0 . . 2 34 3JHAHB3 27 CYS HA 27 CYS HB3 11.0 . . 1 stop_ save_