data_4684 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-Dimensional Solution Structure of the Isolated Cd4-alpha Domain of Metallothionein 2. Determination by Homonuclear and Heteronuclear Magnetic Resonance Spectroscopy ; _BMRB_accession_number 4684 _BMRB_flat_file_name bmr4684.str _Entry_type original _Submission_date 2000-03-09 _Accession_date 2000-03-09 _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 Ejnik John W. . 2 Munoz Amalia . . 3 DeRose Eugene . . 4 Shaw C. Frank III 5 Petering David H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 155 "coupling constants" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-27 original author . stop_ _Original_release_date 2003-08-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Consequences of Metallothionein Dimerization: Solution Structure of the Isolated Cd4-alpha Domain and Comparison with the Holoprotein Dimer ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22744254 _PubMed_ID 12859185 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ejnik John W. . 2 Munoz Amalia . . 3 DeRose Eugene . . 4 Shaw C. Frank III 5 Petering David H. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 42 _Journal_issue 28 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8403 _Page_last 8410 _Year 2003 _Details . loop_ _Keyword 111Cd-NMR Metallothionein Alpha-domain Isolated domain stop_ save_ ################################## # Molecular system description # ################################## save_MT _Saveframe_category molecular_system _Mol_system_name 'alpha MT' _Abbreviation_common MT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alpha domain' $alpha_domain 'Cd I' $CD 'Cd V' $CD 'Cd VI' $CD 'Cd VII' $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' 'Metal regulation' 'Metal donation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_alpha_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Metallothionein _Abbreviation_common MT _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; KKSCCSCCPPGCAKCAQGCI CKGASDKCSCCA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 30 LYS 2 31 LYS 3 32 SER 4 33 CYS 5 34 CYS 6 35 SER 7 36 CYS 8 37 CYS 9 38 PRO 10 39 PRO 11 40 GLY 12 41 CYS 13 42 ALA 14 43 LYS 15 44 CYS 16 45 ALA 17 46 GLN 18 47 GLY 19 48 CYS 20 49 ILE 21 50 CYS 22 51 LYS 23 52 GLY 24 53 ALA 25 54 SER 26 55 ASP 27 56 LYS 28 57 CYS 29 58 SER 30 59 CYS 31 60 CYS 32 61 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-24 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 1MRB "Three-Dimensional Structure Of Rabbit Liver Cd7 Metallothionein-2a In Aqueous Solution Determined By Nuclear Magnetic Resonance" 71.88 31 100.00 100.00 3.01e-01 GB AAB21306 "MT-2A, metallothionein 2A [rabbits, liver, Peptide, 62 aa]" 100.00 62 100.00 100.00 4.13e-09 GB ELW66183 "Metallothionein-2 [Tupaia chinensis]" 56.25 130 100.00 100.00 1.33e+00 REF XP_002711575 "PREDICTED: metallothionein-2A [Oryctolagus cuniculus]" 100.00 89 100.00 100.00 1.90e-09 REF XP_004057727 "PREDICTED: metallothionein-2-like [Gorilla gorilla gorilla]" 62.50 61 100.00 100.00 1.35e-01 REF XP_006148462 "PREDICTED: metallothionein-1E-like [Tupaia chinensis]" 56.25 61 100.00 100.00 1.17e+00 REF XP_006179841 "PREDICTED: metallothionein-1D-like [Camelus ferus]" 62.50 61 100.00 100.00 1.22e-01 REF XP_006179844 "PREDICTED: metallothionein-4 isoform X1 [Camelus ferus]" 59.38 62 100.00 100.00 4.16e-01 SP P18055 "RecName: Full=Metallothionein-2A; Short=MT-2A; AltName: Full=Metallothionein-IIA; Short=MT-IIA" 100.00 62 100.00 100.00 4.50e-09 SP P80290 "RecName: Full=Metallothionein-2C; Short=MT-2C; AltName: Full=Metallothionein-IIC; Short=MT-IIC" 100.00 62 100.00 100.00 4.13e-09 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 Thu Aug 25 10:27:49 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 $alpha_domain 'New Zeland White Rabbit' 9986 Eukaryota Metazoa Oryctolagus cuniculus kidney 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 $alpha_domain '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 $alpha_domain 3 mM '[U-99.5% 111Cd]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2.3 loop_ _Task 'processing and peak assignments' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model GN _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'DQF COSY' _Sample_label $sample_1 save_ save_PE_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'PE COSY' _Sample_label $sample_1 save_ save_TOCSY_MLEV-17_(41_ms_and_80_ms)_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY MLEV-17 (41 ms and 80 ms)' _Sample_label $sample_1 save_ save_1H-111Cd_HMQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-111Cd HMQC' _Sample_label $sample_1 save_ save_NOESY_(60_ms,120_ms_and_250_ms)_for_10%_D2O_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY (60 ms,120 ms and 250 ms) for 10% D2O' _Sample_label $sample_1 save_ save_NOESY_(50_ms_and_100_ms)_for_100%_D2O_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY (50 ms and 100 ms) for 100% D2O' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 pH temperature 298 0.1 K pressure 1 . atm 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_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.8 internal 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'alpha domain' _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 4.38 0.03 1 2 . 1 LYS HB2 H 1.75 0.03 2 3 . 1 LYS HB3 H 1.84 0.03 2 4 . 1 LYS HG2 H 1.47 0.03 1 5 . 1 LYS HG3 H 1.47 0.03 1 6 . 1 LYS HD2 H 1.71 0.03 1 7 . 1 LYS HD3 H 1.71 0.03 1 8 . 1 LYS HE2 H 3.01 0.03 1 9 . 1 LYS HE3 H 3.01 0.03 1 10 . 2 LYS HA H 4.46 0.03 1 11 . 2 LYS HB2 H 1.79 0.03 2 12 . 2 LYS HB3 H 1.88 0.03 2 13 . 2 LYS HG2 H 1.51 0.03 1 14 . 2 LYS HG3 H 1.51 0.03 1 15 . 2 LYS HD2 H 1.72 0.03 1 16 . 2 LYS HD3 H 1.72 0.03 1 17 . 2 LYS HE2 H 3.03 0.03 1 18 . 2 LYS HE3 H 3.03 0.03 1 19 . 3 SER HA H 4.61 0.03 1 20 . 3 SER HB2 H 3.75 0.03 2 21 . 3 SER HB3 H 4.05 0.03 2 22 . 4 CYS H H 8.22 0.03 1 23 . 4 CYS HA H 4.51 0.03 1 24 . 4 CYS HB2 H 3.25 0.03 2 25 . 4 CYS HB3 H 3.27 0.03 2 26 . 5 CYS H H 8.37 0.03 1 27 . 5 CYS HA H 5.08 0.03 1 28 . 5 CYS HB2 H 3.55 0.03 2 29 . 5 CYS HB3 H 3.62 0.03 2 30 . 6 SER HA H 4.46 0.03 1 31 . 6 SER HB2 H 3.88 0.03 2 32 . 6 SER HB3 H 4.00 0.03 2 33 . 7 CYS H H 8.54 0.03 1 34 . 7 CYS HA H 4.51 0.03 1 35 . 7 CYS HB2 H 2.77 0.03 2 36 . 7 CYS HB3 H 3.18 0.03 2 37 . 8 CYS H H 7.20 0.03 1 38 . 8 CYS HA H 5.16 0.03 1 39 . 8 CYS HB2 H 3.06 0.03 1 40 . 8 CYS HB3 H 3.06 0.03 1 41 . 9 PRO HA H 4.91 0.03 1 42 . 9 PRO HB2 H 2.02 0.03 3 43 . 9 PRO HB3 H 2.39 0.03 3 44 . 9 PRO HG2 H 1.95 0.03 3 45 . 9 PRO HG3 H 2.11 0.03 3 46 . 9 PRO HD2 H 3.80 0.03 3 47 . 9 PRO HD3 H 3.88 0.03 3 48 . 10 PRO HA H 4.39 0.03 3 49 . 10 PRO HB2 H 1.84 0.03 3 50 . 10 PRO HB3 H 2.16 0.03 3 51 . 10 PRO HG2 H 2.00 0.03 3 52 . 10 PRO HG3 H 2.17 0.03 3 53 . 10 PRO HD2 H 3.69 0.03 3 54 . 10 PRO HD3 H 3.91 0.03 3 55 . 11 GLY HA2 H 3.71 0.03 2 56 . 11 GLY HA3 H 4.03 0.03 2 57 . 12 CYS H H 7.00 0.03 1 58 . 12 CYS HA H 4.08 0.03 1 59 . 12 CYS HB2 H 3.17 0.03 1 60 . 12 CYS HB3 H 3.17 0.03 1 61 . 13 ALA H H 9.38 0.03 1 62 . 13 ALA HA H 4.16 0.03 1 63 . 13 ALA HB H 1.57 0.03 1 64 . 14 LYS H H 8.34 0.03 1 65 . 14 LYS HA H 4.23 0.03 1 66 . 14 LYS HB2 H 2.09 0.03 1 67 . 14 LYS HB3 H 2.09 0.03 1 68 . 14 LYS HG2 H 1.56 0.03 1 69 . 14 LYS HG3 H 1.56 0.03 1 70 . 14 LYS HD2 H 1.72 0.03 1 71 . 14 LYS HD3 H 1.72 0.03 1 72 . 14 LYS HE2 H 3.06 0.03 1 73 . 14 LYS HE3 H 3.06 0.03 1 74 . 15 CYS H H 7.56 0.03 1 75 . 15 CYS HA H 4.67 0.03 1 76 . 15 CYS HB2 H 2.62 0.03 2 77 . 15 CYS HB3 H 3.77 0.03 2 78 . 16 ALA H H 7.11 0.03 1 79 . 16 ALA HA H 4.14 0.03 1 80 . 16 ALA HB H 1.52 0.03 1 81 . 17 GLN H H 8.16 0.03 1 82 . 17 GLN HA H 4.58 0.03 1 83 . 17 GLN HB2 H 1.99 0.03 2 84 . 17 GLN HB3 H 2.43 0.03 2 85 . 17 GLN HG2 H 2.39 0.03 1 86 . 17 GLN HG3 H 2.39 0.03 1 87 . 17 GLN HE21 H 6.88 0.03 2 88 . 17 GLN HE22 H 7.56 0.03 2 89 . 18 GLY H H 7.38 0.03 1 90 . 18 GLY HA2 H 3.61 0.03 2 91 . 18 GLY HA3 H 4.40 0.03 2 92 . 19 CYS HA H 4.36 0.03 1 93 . 19 CYS HB2 H 2.93 0.03 2 94 . 19 CYS HB3 H 3.00 0.03 2 95 . 20 ILE H H 7.21 0.03 1 96 . 20 ILE HA H 4.73 0.03 1 97 . 20 ILE HB H 2.27 0.03 1 98 . 20 ILE HG12 H 1.03 0.03 2 99 . 20 ILE HG13 H 1.06 0.03 2 100 . 20 ILE HG2 H 0.96 0.03 1 101 . 20 ILE HD1 H 0.96 0.03 1 102 . 21 CYS H H 9.12 0.03 1 103 . 21 CYS HA H 4.45 0.03 1 104 . 21 CYS HB2 H 2.65 0.03 2 105 . 21 CYS HB3 H 3.13 0.03 2 106 . 22 LYS H H 8.53 0.03 1 107 . 22 LYS HA H 4.32 0.03 1 108 . 22 LYS HB2 H 1.84 0.03 1 109 . 22 LYS HB3 H 1.84 0.03 1 110 . 22 LYS HG2 H 1.51 0.03 2 111 . 22 LYS HG3 H 1.72 0.03 2 112 . 22 LYS HD2 H 1.72 0.03 1 113 . 22 LYS HD3 H 1.72 0.03 1 114 . 22 LYS HE2 H 3.03 0.03 1 115 . 22 LYS HE3 H 3.03 0.03 1 116 . 23 GLY HA2 H 3.89 0.03 2 117 . 23 GLY HA3 H 4.09 0.03 2 118 . 24 ALA HA H 4.49 0.03 1 119 . 24 ALA HB H 1.46 0.03 1 120 . 25 SER H H 8.18 0.03 1 121 . 25 SER HA H 4.64 0.03 1 122 . 25 SER HB2 H 3.88 0.03 1 123 . 25 SER HB3 H 3.92 0.03 1 124 . 26 ASP H H 8.55 0.03 1 125 . 26 ASP HA H 4.40 0.03 1 126 . 26 ASP HB2 H 2.72 0.03 2 127 . 26 ASP HB3 H 2.77 0.03 2 128 . 27 LYS H H 7.87 0.03 1 129 . 27 LYS HA H 4.73 0.03 1 130 . 27 LYS HB2 H 1.75 0.03 2 131 . 27 LYS HB3 H 1.82 0.03 2 132 . 27 LYS HG2 H 1.44 0.03 1 133 . 27 LYS HG3 H 1.44 0.03 1 134 . 27 LYS HD2 H 1.71 0.03 1 135 . 27 LYS HD3 H 1.71 0.03 1 136 . 27 LYS HE2 H 3.04 0.03 1 137 . 27 LYS HE3 H 3.04 0.03 1 138 . 28 CYS H H 8.50 0.03 1 139 . 28 CYS HA H 5.20 0.03 1 140 . 28 CYS HB2 H 3.60 0.03 1 141 . 28 CYS HB3 H 3.60 0.03 1 142 . 29 SER HA H 4.68 0.03 1 143 . 29 SER HB2 H 3.91 0.03 2 144 . 29 SER HB3 H 3.98 0.03 2 145 . 30 CYS H H 8.39 0.03 1 146 . 30 CYS HA H 4.60 0.03 1 147 . 30 CYS HB2 H 3.24 0.03 2 148 . 30 CYS HB3 H 3.31 0.03 2 149 . 31 CYS H H 7.71 0.03 1 150 . 31 CYS HA H 4.75 0.03 1 151 . 31 CYS HB2 H 2.69 0.03 2 152 . 31 CYS HB3 H 2.83 0.03 2 153 . 32 ALA H H 7.14 0.03 1 154 . 32 ALA HA H 4.14 0.03 1 155 . 32 ALA HB H 1.42 0.03 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'alpha domain' _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 7.8 . . . 2 3JHNHA 5 CYS H 5 CYS HA 8.4 . . . 3 3JHNHA 7 CYS H 7 CYS HA 9.2 . . . 4 3JHNHA 8 CYS H 8 CYS HA 10.1 . . . 5 3JHNHA 14 LYS H 14 LYS HA 7.2 . . . 6 3JHNHA 15 CYS H 15 CYS HA 9.8 . . . 7 3JHNHA 16 ALA H 16 ALA HA 6.5 . . . 8 3JHNHA 17 GLN H 17 GLN HA 12.7 . . . 9 3JHNHA 18 GLY H 18 GLY HA 10.2 . . . 10 3JHNHA 20 ILE H 20 ILE HA 9.9 . . . 11 3JHNHA 21 CYS H 21 CYS HA 8.1 . . . 12 3JHNHA 25 SER H 25 SER HA 9.5 . . . 13 3JHNHA 27 LYS H 27 LYS HA 8.5 . . . 14 3JHNHA 28 CYS H 28 CYS HA 9.8 . . . 15 3JHNHA 30 CYS H 30 CYS HA 8.7 . . . 16 3JHNHA 31 CYS H 31 CYS HA 10.6 . . . 17 3JHNHA 32 ALA H 32 ALA HA 8.1 . . . stop_ save_ save_coupling_constants_2 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'alpha domain' _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 3JHAHB 2 LYS HA 2 LYS HB2 7.4 . . . 2 3JHAHB 2 LYS HA 2 LYS HB3 6.2 . . . 3 3JHAHB 3 SER HA 3 SER HB2 10.0 . . . 4 3JHAHB 3 SER HA 3 SER HB3 5.6 . . . 5 3JHAHB 4 CYS HA 4 CYS HB2 6.2 . . . 6 3JHAHB 4 CYS HA 4 CYS HB3 2.0 . . . 7 3JHAHB 5 CYS HA 5 CYS HB2 5.8 . . . 8 3JHAHB 5 CYS HA 5 CYS HB3 2.0 . . . 9 3JHAHB 6 SER HA 6 SER HB2 5.2 . . . 10 3JHAHB 6 SER HA 6 SER HB3 2.7 . . . 11 3JHAHB 7 CYS HA 7 CYS HB2 7.7 . . . 12 3JHAHB 7 CYS HA 7 CYS HB3 2.3 . . . 13 3JHAHB 9 PRO HA 9 PRO HB2 9.3 . . . 14 3JHAHB 9 PRO HA 9 PRO HB3 5.6 . . . 15 3JHAHB 10 PRO HA 10 PRO HB2 7.6 . . . 16 3JHAHB 10 PRO HA 10 PRO HB3 7.5 . . . 17 3JHAHB 12 CYS HA 12 CYS HB2 10.9 . . . 18 3JHAHB 12 CYS HA 12 CYS HB3 7.0 . . . 19 3JHAHB 14 LYS HA 14 LYS HB2 10.5 . . . 20 3JHAHB 14 LYS HA 14 LYS HB3 3.6 . . . 21 3JHAHB 15 CYS HA 15 CYS HB2 10.6 . . . 22 3JHAHB 15 CYS HA 15 CYS HB3 6.5 . . . 23 3JHAHB 17 GLN HA 17 GLN HB2 11.3 . . . 24 3JHAHB 17 GLN HA 17 GLN HB3 5.0 . . . 25 3JHAHB 19 CYS HA 19 CYS HB2 11.8 . . . 26 3JHAHB 19 CYS HA 19 CYS HB3 5.0 . . . 27 3JHAHB 20 ILE HA 20 ILE HB2 5.8 . . . 28 3JHAHB 21 CYS HA 21 CYS HB2 12.5 . . . 29 3JHAHB 21 CYS HA 21 CYS HB3 5.5 . . . 30 3JHAHB 22 LYS HA 22 LYS HB2 8.4 . . . 31 3JHAHB 22 LYS HA 22 LYS HB3 5.6 . . . 32 3JHAHB 25 SER HA 25 SER HB2 5.0 . . . 33 3JHAHB 25 SER HA 25 SER HB3 5.3 . . . 34 3JHAHB 26 ASP HA 26 ASP HB2 6.2 . . . 35 3JHAHB 26 ASP HA 26 ASP HB3 5.4 . . . 36 3JHAHB 27 LYS HA 27 LYS HB2 6.8 . . . 37 3JHAHB 27 LYS HA 27 LYS HB3 6.3 . . . 38 3JHAHB 29 SER HA 29 SER HB2 4.6 . . . 39 3JHAHB 29 SER HA 29 SER HB3 4.0 . . . 40 3JHAHB 30 CYS HA 30 CYS HB2 6.9 . . . 41 3JHAHB 30 CYS HA 30 CYS HB3 2.5 . . . 42 3JHAHB 31 CYS HA 31 CYS HB2 12.3 . . . 43 3JHAHB 31 CYS HA 31 CYS HB3 4.3 . . . stop_ save_