data_5832 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Function and solution structure of hainantoxin-III, a potent neuronal TTX-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia hainana ; _BMRB_accession_number 5832 _BMRB_flat_file_name bmr5832.str _Entry_type original _Submission_date 2003-06-15 _Accession_date 2003-06-16 _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 Zhu Qi . . 2 Liang Songping . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 199 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'Updating non-standard residue' stop_ _Original_release_date 2003-06-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Function and solution structure of hainantoxin-III, a potent neuronal TTX-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia hainana ; _Citation_status 'in preparation' _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 Zhu Qi . . 2 Liang Songping . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_HNTX-III _Saveframe_category molecular_system _Mol_system_name hainantoxin-III _Abbreviation_common HNTX-III _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hainantoxin-III $hainantoxin-III stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Selectively acting on tetrodotoxin-sensitive voltage-gated sodium channels' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hainantoxin-III _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hainantoxin-III _Abbreviation_common HNTX-III _Molecular_mass 3607.6 _Mol_thiol_state 'all disulfide bound' _Details 'ESI-MS, the C-terminal carboxyl group is amidated.' ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; GCKGFGDSCTPGKNECCPNY ACSSKHKWCKVYX ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 CYS 3 LYS 4 GLY 5 PHE 6 GLY 7 ASP 8 SER 9 CYS 10 THR 11 PRO 12 GLY 13 LYS 14 ASN 15 GLU 16 CYS 17 CYS 18 PRO 19 ASN 20 TYR 21 ALA 22 CYS 23 SER 24 SER 25 LYS 26 HIS 27 LYS 28 TRP 29 CYS 30 LYS 31 VAL 32 TYR 33 NLW stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2008-03-03 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 2JTB 'A Chain A, Three Dimensional SolutionStructure Of Hainantoxin-Iii By 2d 1h-Nmr' 100.00 33 100 100 5e-15 SWISS-PROT P83464 'TXHA3_SELHA Hainantoxin-3 (Hainantoxin-III)(HnTx-III)' 100.00 33 100 100 5e-15 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NLW _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common L-leucinamide _BMRB_code NLW _PDB_code NLW _Standard_residue_derivative . _Molecular_mass 130.188 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CD2 CD2 C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CB CB C . 0 . ? CA CA C . 0 . ? N N N . 0 . ? C C C . 0 . ? O O O . 0 . ? NH2 NH2 N . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? H6 H6 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H9 H9 H . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H14 H14 H . 0 . ? H15 H15 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CD1 CG ? ? SING CG CD2 ? ? SING CG CB ? ? SING CB CA ? ? SING N CA ? ? SING CA C ? ? SING C NH2 ? ? DOUB C O ? ? SING CD2 H1 ? ? SING CD2 H2 ? ? SING CD2 H3 ? ? SING CG H4 ? ? SING CD1 H5 ? ? SING CD1 H6 ? ? SING CD1 H7 ? ? SING CB H8 ? ? SING CB H9 ? ? SING CA H10 ? ? SING N H11 ? ? SING N H12 ? ? SING NH2 H14 ? ? SING NH2 H15 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Secretion $hainantoxin-III 'chinese bird spider' 209901 Eukaryota Metazoa Selenocosmia hainana 'venomous gland' 'venomous gland' 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 $hainantoxin-III '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 $hainantoxin-III 4.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name FELIX _Version 98.0 loop_ _Task 'manual peak 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_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $sample_1 save_ save_1H-1H_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label $sample_1 save_ save_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _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 4.5 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 TSP 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_set_1 _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 hainantoxin-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 GLY HA2 H 4.14 0.02 2 2 . 1 GLY HA3 H 3.72 0.02 2 3 . 2 CYS H H 8.60 0.02 1 4 . 2 CYS HA H 4.98 0.02 1 5 . 2 CYS HB2 H 3.10 0.02 2 6 . 2 CYS HB3 H 3.26 0.02 2 7 . 3 LYS H H 8.66 0.02 1 8 . 3 LYS HA H 4.38 0.02 1 9 . 3 LYS HB2 H 1.94 0.02 2 10 . 3 LYS HB3 H 1.76 0.02 2 11 . 3 LYS HG2 H 1.45 0.02 1 12 . 3 LYS HG3 H 1.45 0.02 1 13 . 3 LYS HD2 H 1.82 0.02 2 14 . 3 LYS HD3 H 1.57 0.02 2 15 . 3 LYS HE2 H 2.98 0.02 1 16 . 3 LYS HE3 H 2.98 0.02 1 17 . 3 LYS HZ H 7.44 0.02 2 18 . 4 GLY H H 8.44 0.02 1 19 . 4 GLY HA2 H 3.91 0.02 2 20 . 4 GLY HA3 H 3.49 0.02 2 21 . 5 PHE H H 7.83 0.02 1 22 . 5 PHE HA H 3.59 0.02 1 23 . 5 PHE HB2 H 2.98 0.02 2 24 . 5 PHE HB3 H 2.76 0.02 2 25 . 5 PHE HD1 H 7.17 0.02 1 26 . 5 PHE HD2 H 7.17 0.02 1 27 . 5 PHE HE1 H 7.45 0.02 1 28 . 5 PHE HE2 H 7.45 0.02 1 29 . 6 GLY H H 8.53 0.02 1 30 . 6 GLY HA2 H 3.63 0.02 2 31 . 6 GLY HA3 H 2.75 0.02 2 32 . 7 ASP H H 7.99 0.02 1 33 . 7 ASP HA H 4.68 0.02 1 34 . 7 ASP HB2 H 2.85 0.02 2 35 . 7 ASP HB3 H 2.61 0.02 2 36 . 8 SER H H 8.63 0.02 1 37 . 8 SER HA H 4.83 0.02 1 38 . 8 SER HB2 H 3.96 0.02 1 39 . 8 SER HB3 H 3.96 0.02 1 40 . 9 CYS H H 8.12 0.02 1 41 . 9 CYS HA H 4.98 0.02 1 42 . 9 CYS HB2 H 3.29 0.02 2 43 . 9 CYS HB3 H 2.99 0.02 2 44 . 10 THR H H 9.03 0.02 1 45 . 10 THR HA H 4.63 0.02 1 46 . 10 THR HB H 3.81 0.02 1 47 . 10 THR HG2 H 1.19 0.02 1 48 . 11 PRO HA H 3.98 0.02 1 49 . 11 PRO HB2 H 2.11 0.02 2 50 . 11 PRO HB3 H 2.22 0.02 2 51 . 11 PRO HG2 H 1.92 0.02 2 52 . 11 PRO HG3 H 1.71 0.02 2 53 . 11 PRO HD2 H 4.07 0.02 2 54 . 11 PRO HD3 H 3.81 0.02 2 55 . 12 GLY H H 8.77 0.02 1 56 . 12 GLY HA2 H 4.34 0.02 2 57 . 12 GLY HA3 H 3.77 0.02 2 58 . 13 LYS H H 7.49 0.02 1 59 . 13 LYS HA H 4.55 0.02 1 60 . 13 LYS HB2 H 2.00 0.02 2 61 . 13 LYS HB3 H 1.84 0.02 2 62 . 13 LYS HG2 H 1.42 0.02 2 63 . 13 LYS HG3 H 1.28 0.02 2 64 . 13 LYS HD2 H 1.62 0.02 1 65 . 13 LYS HD3 H 1.62 0.02 1 66 . 13 LYS HE2 H 2.99 0.02 1 67 . 13 LYS HE3 H 2.99 0.02 1 68 . 13 LYS HZ H 7.55 0.02 2 69 . 14 ASN H H 8.61 0.02 1 70 . 14 ASN HA H 4.77 0.02 1 71 . 14 ASN HB2 H 3.03 0.02 2 72 . 14 ASN HB3 H 2.72 0.02 2 73 . 14 ASN HD21 H 7.66 0.02 1 74 . 14 ASN HD22 H 7.66 0.02 1 75 . 15 GLU H H 8.70 0.02 1 76 . 15 GLU HA H 4.30 0.02 1 77 . 15 GLU HB2 H 2.23 0.02 2 78 . 15 GLU HB3 H 2.07 0.02 2 79 . 15 GLU HG2 H 2.22 0.02 1 80 . 15 GLU HG3 H 2.22 0.02 1 81 . 16 CYS H H 8.48 0.02 1 82 . 16 CYS HA H 5.07 0.02 1 83 . 16 CYS HB2 H 3.13 0.02 2 84 . 16 CYS HB3 H 2.88 0.02 2 85 . 17 CYS H H 9.89 0.02 1 86 . 17 CYS HA H 4.84 0.02 1 87 . 17 CYS HB2 H 3.54 0.02 2 88 . 17 CYS HB3 H 2.52 0.02 2 89 . 18 PRO HA H 4.43 0.02 1 90 . 18 PRO HB2 H 2.38 0.02 2 91 . 18 PRO HB3 H 2.14 0.02 2 92 . 18 PRO HG2 H 2.08 0.02 2 93 . 18 PRO HG3 H 1.82 0.02 2 94 . 18 PRO HD2 H 3.98 0.02 2 95 . 18 PRO HD3 H 3.69 0.02 2 96 . 19 ASN H H 8.63 0.02 1 97 . 19 ASN HA H 4.28 0.02 1 98 . 19 ASN HB2 H 2.88 0.02 2 99 . 19 ASN HB3 H 2.67 0.02 2 100 . 19 ASN HD21 H 7.26 0.02 2 101 . 19 ASN HD22 H 6.80 0.02 2 102 . 20 TYR H H 8.51 0.02 1 103 . 20 TYR HA H 5.34 0.02 1 104 . 20 TYR HB2 H 3.23 0.02 2 105 . 20 TYR HB3 H 2.92 0.02 2 106 . 20 TYR HD1 H 6.90 0.02 1 107 . 20 TYR HD2 H 6.90 0.02 1 108 . 20 TYR HE1 H 6.82 0.02 1 109 . 20 TYR HE2 H 6.82 0.02 1 110 . 21 ALA H H 9.36 0.02 1 111 . 21 ALA HA H 4.69 0.02 1 112 . 21 ALA HB H 1.34 0.02 1 113 . 22 CYS H H 8.91 0.02 1 114 . 22 CYS HA H 4.72 0.02 1 115 . 22 CYS HB2 H 3.12 0.02 2 116 . 22 CYS HB3 H 3.00 0.02 2 117 . 23 SER H H 8.28 0.02 1 118 . 23 SER HA H 4.57 0.02 1 119 . 23 SER HB2 H 4.15 0.02 2 120 . 23 SER HB3 H 3.83 0.02 2 121 . 24 SER H H 9.05 0.02 1 122 . 24 SER HA H 4.04 0.02 1 123 . 24 SER HB2 H 3.92 0.02 1 124 . 24 SER HB3 H 3.92 0.02 1 125 . 25 LYS H H 7.75 0.02 1 126 . 25 LYS HA H 4.12 0.02 1 127 . 25 LYS HB2 H 1.52 0.02 2 128 . 25 LYS HB3 H 1.36 0.02 2 129 . 25 LYS HG2 H 1.15 0.02 2 130 . 25 LYS HG3 H 1.02 0.02 2 131 . 25 LYS HD2 H 1.51 0.02 1 132 . 25 LYS HD3 H 1.51 0.02 1 133 . 25 LYS HE2 H 2.89 0.02 1 134 . 25 LYS HE3 H 2.89 0.02 1 135 . 25 LYS HZ H 7.50 0.02 1 136 . 26 HIS H H 7.50 0.02 1 137 . 26 HIS HA H 4.38 0.02 1 138 . 26 HIS HB2 H 1.88 0.02 2 139 . 26 HIS HB3 H 1.76 0.02 2 140 . 26 HIS HD1 H 6.90 0.02 1 141 . 26 HIS HE1 H 7.60 0.02 1 142 . 27 LYS H H 8.32 0.02 1 143 . 27 LYS HA H 4.04 0.02 1 144 . 27 LYS HB2 H 1.86 0.02 2 145 . 27 LYS HB3 H 1.72 0.02 2 146 . 27 LYS HG2 H 1.65 0.02 1 147 . 27 LYS HG3 H 1.65 0.02 1 148 . 27 LYS HD2 H 1.21 0.02 2 149 . 27 LYS HD3 H 1.27 0.02 2 150 . 27 LYS HE2 H 2.35 0.02 2 151 . 27 LYS HE3 H 2.99 0.02 2 152 . 27 LYS HZ H 7.55 0.02 1 153 . 28 TRP H H 7.39 0.02 1 154 . 28 TRP HA H 5.56 0.02 1 155 . 28 TRP HB2 H 3.06 0.02 2 156 . 28 TRP HB3 H 2.57 0.02 2 157 . 28 TRP HD1 H 6.95 0.02 1 158 . 28 TRP HE1 H 10.17 0.02 1 159 . 28 TRP HE3 H 7.04 0.02 1 160 . 28 TRP HZ2 H 7.35 0.02 1 161 . 28 TRP HZ3 H 7.18 0.02 1 162 . 28 TRP HH2 H 7.46 0.02 1 163 . 29 CYS H H 8.58 0.02 1 164 . 29 CYS HA H 4.99 0.02 1 165 . 29 CYS HB2 H 3.27 0.02 2 166 . 29 CYS HB3 H 2.57 0.02 2 167 . 30 LYS H H 9.28 0.02 1 168 . 30 LYS HA H 5.05 0.02 1 169 . 30 LYS HB2 H 2.03 0.02 2 170 . 30 LYS HB3 H 1.98 0.02 2 171 . 30 LYS HG2 H 1.49 0.02 2 172 . 30 LYS HG3 H 1.40 0.02 2 173 . 30 LYS HD2 H 1.65 0.02 1 174 . 30 LYS HD3 H 1.65 0.02 1 175 . 30 LYS HE2 H 2.74 0.02 2 176 . 30 LYS HE3 H 2.83 0.02 2 177 . 30 LYS HZ H 7.57 0.02 1 178 . 31 VAL H H 8.72 0.02 1 179 . 31 VAL HA H 3.99 0.02 1 180 . 31 VAL HB H 2.04 0.02 1 181 . 31 VAL HG1 H 1.01 0.02 2 182 . 31 VAL HG2 H 0.91 0.02 2 183 . 32 TYR H H 8.54 0.02 1 184 . 32 TYR HA H 4.58 0.02 1 185 . 32 TYR HB2 H 2.83 0.02 2 186 . 32 TYR HB3 H 2.75 0.02 2 187 . 32 TYR HD1 H 7.08 0.02 1 188 . 32 TYR HD2 H 7.08 0.02 1 189 . 32 TYR HE1 H 6.80 0.02 1 190 . 32 TYR HE2 H 6.80 0.02 1 191 . 33 NLW H H 8.12 0.02 1 192 . 33 NLW HA H 4.20 0.02 1 193 . 33 NLW HB2 H 1.48 0.02 1 194 . 33 NLW HB3 H 1.48 0.02 1 195 . 33 NLW HG H 1.43 0.02 1 196 . 33 NLW HD1 H 0.77 0.02 2 197 . 33 NLW HD2 H 0.88 0.02 2 198 . 33 NLW HT1 H 7.18 0.02 2 199 . 33 NLW HT2 H 8.60 0.02 2 stop_ save_