data_5495 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for Psalmotoxin 1 ; _BMRB_accession_number 5495 _BMRB_flat_file_name bmr5495.str _Entry_type original _Submission_date 2002-08-07 _Accession_date 2002-08-07 _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 Escoubas Pierre . . 2 Bernard Cedric . . 3 Lambeau Gerard . . 4 Lazdunski Michel . . 5 Darbon Herve . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-07-30 original author . stop_ _Original_release_date 2003-07-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Recombinant Production and Solution Structure of PcTx1, the Specific Peptide Inhibitor of ASIC1a Proton-gated Cation Channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22709212 _PubMed_ID 12824480 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Escoubas Pierre . . 2 Bernard Cedric . . 3 Lambeau Gerard . . 4 Lazdunski Michel . . 5 Darbon Herve . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 12 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1332 _Page_last 1343 _Year 2003 _Details . loop_ _Keyword ASIC ICK 'Spider toxin' 'structure determination' stop_ save_ ################################## # Molecular system description # ################################## save_system_PcTx1 _Saveframe_category molecular_system _Mol_system_name psalmotoxin1 _Abbreviation_common PcTx1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'psalmotoxin 1' $PcTx1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PcTx1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'psalmotoxin 1' _Abbreviation_common PcTx1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; EDCIPKWKGCVNRHGDCCEG LECWKRRRSFEVCVPKTPKT ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ASP 3 CYS 4 ILE 5 PRO 6 LYS 7 TRP 8 LYS 9 GLY 10 CYS 11 VAL 12 ASN 13 ARG 14 HIS 15 GLY 16 ASP 17 CYS 18 CYS 19 GLU 20 GLY 21 LEU 22 GLU 23 CYS 24 TRP 25 LYS 26 ARG 27 ARG 28 ARG 29 SER 30 PHE 31 GLU 32 VAL 33 CYS 34 VAL 35 PRO 36 LYS 37 THR 38 PRO 39 LYS 40 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 16468 PcTx1 100.00 41 100.00 100.00 9.59e-20 BMRB 26504 TRTX-Pc1a 100.00 40 100.00 100.00 1.25e-19 PDB 1LMM "Solution Structure Of Psmalmotoxin 1, The First Characterized Specific Blocker Of Asic1a Na+ Channel" 100.00 40 100.00 100.00 1.25e-19 PDB 2KNI "High-resolution Solution Structure Of The Asic1a Blocker Pctx1" 100.00 41 100.00 100.00 9.59e-20 PDB 3S3X "Structure Of Chicken Acid-Sensing Ion Channel 1 At 3.0 A Resolution In Complex With Psalmotoxin" 92.50 37 100.00 100.00 1.27e-17 PDB 4FZ0 "Crystal Structure Of Acid-Sensing Ion Channel In Complex With Psalmotoxin 1 At Low Ph" 100.00 40 100.00 100.00 1.25e-19 PDB 4FZ1 "Crystal Structure Of Acid-Sensing Ion Channel In Complex With Psalmotoxin 1 At High Ph" 100.00 40 100.00 100.00 1.25e-19 SP P60514 "RecName: Full=Pi-theraphotoxin-Pc1a; Short=Pi-TRTX-Pc1a; AltName: Full=PcTx1; AltName: Full=Psalmotoxin-1 [Psalmopoeus cambridg" 100.00 40 100.00 100.00 1.25e-19 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PcTx1 'Psalmopoeus cambridgei' . Eukaryota Metazoa Psalmopoeus cambridgei 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 $PcTx1 'recombinant technology' . . . . . 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 $PcTx1 2.9 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 3.0 . n/a temperature 300 . 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 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'psalmotoxin 1' _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 GLU HA H 4.042 0.001 1 2 . 2 ASP H H 8.863 0.000 1 3 . 2 ASP HA H 4.748 0.001 1 4 . 2 ASP HB2 H 2.786 0.000 1 5 . 2 ASP HB3 H 2.573 0.000 1 6 . 3 CYS H H 8.377 0.000 1 7 . 3 CYS HA H 4.056 0.000 1 8 . 4 ILE H H 8.954 0.000 1 9 . 4 ILE HA H 4.282 0.000 1 10 . 4 ILE HB H 1.785 0.001 1 11 . 4 ILE HG2 H 0.886 0.025 1 12 . 4 ILE HD1 H 1.569 0.000 1 13 . 5 PRO HA H 4.302 0.000 1 14 . 5 PRO HG2 H 2.030 0.000 1 15 . 5 PRO HG3 H 1.754 0.000 1 16 . 5 PRO HD2 H 4.099 0.000 1 17 . 5 PRO HD3 H 3.593 0.000 1 18 . 6 LYS H H 7.619 0.000 1 19 . 6 LYS HA H 3.264 0.000 1 20 . 6 LYS HG2 H 0.649 0.000 1 21 . 6 LYS HG3 H 0.192 0.000 1 22 . 7 TRP H H 9.287 0.000 1 23 . 7 TRP HA H 4.230 0.001 1 24 . 7 TRP HD1 H 7.083 0.000 1 25 . 7 TRP HE1 H 10.206 0.001 1 26 . 7 TRP HH2 H 7.489 0.000 1 27 . 8 LYS H H 7.774 0.000 1 28 . 8 LYS HA H 4.706 0.000 1 29 . 8 LYS HB2 H 1.745 0.000 1 30 . 8 LYS HG2 H 1.502 0.000 1 31 . 8 LYS HG3 H 1.423 0.000 1 32 . 8 LYS HD2 H 2.001 0.000 1 33 . 8 LYS HD3 H 1.879 0.000 1 34 . 9 GLY H H 8.509 0.000 1 35 . 9 GLY HA2 H 4.666 0.001 1 36 . 9 GLY HA3 H 3.949 0.001 1 37 . 10 CYS H H 8.298 0.000 1 38 . 10 CYS HA H 4.900 0.000 1 39 . 10 CYS HB2 H 3.430 0.000 1 40 . 10 CYS HB3 H 3.159 0.000 1 41 . 11 VAL H H 7.900 0.000 1 42 . 11 VAL HA H 3.786 0.000 1 43 . 11 VAL HB H 1.993 0.000 1 44 . 11 VAL HG1 H 1.147 0.000 1 45 . 11 VAL HG2 H 0.922 0.000 1 46 . 12 ASN H H 8.925 0.000 1 47 . 12 ASN HA H 4.294 0.000 1 48 . 12 ASN HB2 H 3.048 0.000 1 49 . 12 ASN HB3 H 2.988 0.000 1 50 . 12 ASN HD21 H 7.613 0.000 1 51 . 12 ASN HD22 H 6.919 0.000 1 52 . 13 ARG H H 7.972 0.000 1 53 . 13 ARG HA H 4.614 0.000 1 54 . 13 ARG HG2 H 1.662 0.000 1 55 . 13 ARG HG3 H 1.486 0.000 1 56 . 13 ARG HD2 H 3.272 0.000 1 57 . 13 ARG HD3 H 3.039 0.000 1 58 . 13 ARG HE H 8.223 0.000 1 59 . 13 ARG HH21 H 6.946 0.000 1 60 . 13 ARG HH22 H 6.257 0.000 1 61 . 14 HIS H H 8.695 0.000 1 62 . 14 HIS HA H 4.595 0.001 1 63 . 14 HIS HD1 H 8.531 0.000 1 64 . 14 HIS HD2 H 7.924 0.606 1 65 . 14 HIS HE1 H 7.634 0.000 1 66 . 15 GLY H H 8.846 0.000 1 67 . 15 GLY HA2 H 4.467 0.000 1 68 . 15 GLY HA3 H 3.707 0.000 1 69 . 16 ASP H H 7.408 0.000 1 70 . 16 ASP HA H 4.917 0.000 1 71 . 16 ASP HB2 H 3.241 0.000 1 72 . 16 ASP HB3 H 2.677 0.000 1 73 . 17 CYS H H 8.618 0.000 1 74 . 17 CYS HA H 5.043 0.000 1 75 . 17 CYS HB2 H 2.966 0.000 1 76 . 17 CYS HB3 H 2.772 0.000 1 77 . 18 CYS H H 9.102 0.000 1 78 . 18 CYS HA H 4.451 0.000 1 79 . 18 CYS HB2 H 3.418 0.000 1 80 . 18 CYS HB3 H 2.499 0.000 1 81 . 19 GLU H H 8.221 0.000 1 82 . 19 GLU HA H 4.064 0.000 1 83 . 20 GLY H H 8.887 0.000 1 84 . 20 GLY HA2 H 4.243 0.000 1 85 . 20 GLY HA3 H 3.661 0.000 1 86 . 21 LEU H H 7.820 0.000 1 87 . 21 LEU HA H 5.135 0.000 1 88 . 21 LEU HB2 H 2.082 0.000 1 89 . 21 LEU HB3 H 0.965 0.000 1 90 . 21 LEU HG H 1.250 0.000 1 91 . 21 LEU HD1 H 0.650 0.000 1 92 . 21 LEU HD2 H 0.374 0.000 1 93 . 22 GLU H H 9.377 0.000 1 94 . 22 GLU HA H 4.670 0.000 1 95 . 22 GLU HB2 H 1.962 0.000 1 96 . 22 GLU HB3 H 1.813 0.000 1 97 . 23 CYS H H 8.935 0.000 1 98 . 23 CYS HA H 4.769 0.000 1 99 . 23 CYS HB2 H 3.144 0.000 1 100 . 23 CYS HB3 H 2.755 0.000 1 101 . 24 TRP H H 9.403 0.000 1 102 . 24 TRP HA H 4.872 0.000 1 103 . 24 TRP HB2 H 3.406 0.000 1 104 . 24 TRP HB3 H 3.019 0.000 1 105 . 24 TRP HD1 H 7.121 0.001 1 106 . 24 TRP HE1 H 10.179 0.000 1 107 . 24 TRP HZ2 H 7.147 0.000 1 108 . 24 TRP HH2 H 7.556 0.000 1 109 . 25 LYS H H 8.086 0.000 1 110 . 25 LYS HA H 4.184 0.001 1 111 . 26 ARG H H 7.601 0.000 1 112 . 26 ARG HA H 3.985 0.001 1 113 . 26 ARG HE H 7.016 0.000 1 114 . 27 ARG H H 8.381 0.000 1 115 . 27 ARG HA H 4.345 0.001 1 116 . 27 ARG HB2 H 1.874 0.004 1 117 . 27 ARG HB3 H 1.788 0.007 1 118 . 29 SER H H 8.023 0.000 1 119 . 29 SER HA H 4.373 0.000 1 120 . 29 SER HB2 H 3.756 0.000 1 121 . 29 SER HB3 H 3.613 0.002 1 122 . 30 PHE H H 7.862 0.000 1 123 . 30 PHE HA H 4.778 0.000 1 124 . 30 PHE HB2 H 3.178 0.003 1 125 . 30 PHE HB3 H 3.049 0.001 1 126 . 30 PHE HZ H 7.293 0.000 1 127 . 31 GLU H H 8.579 0.000 1 128 . 31 GLU HA H 4.279 0.000 1 129 . 31 GLU HG2 H 1.636 0.001 1 130 . 31 GLU HG3 H 1.446 0.001 1 131 . 32 VAL H H 8.365 0.001 1 132 . 32 VAL HA H 5.053 0.000 1 133 . 32 VAL HB H 1.776 0.000 1 134 . 32 VAL HG1 H 0.893 0.000 1 135 . 32 VAL HG2 H 0.825 0.000 1 136 . 33 CYS H H 8.219 0.000 1 137 . 33 CYS HA H 5.121 0.000 1 138 . 33 CYS HB2 H 2.960 0.000 1 139 . 33 CYS HB3 H 2.537 0.000 1 140 . 34 VAL H H 9.563 0.000 1 141 . 34 VAL HA H 4.503 0.004 1 142 . 34 VAL HB H 2.159 0.005 1 143 . 34 VAL HG1 H 1.031 0.003 1 144 . 34 VAL HG2 H 0.831 0.003 1 145 . 35 PRO HA H 4.362 0.000 1 146 . 35 PRO HB2 H 2.239 0.000 1 147 . 35 PRO HB3 H 1.803 0.000 1 148 . 35 PRO HG2 H 2.093 0.000 1 149 . 35 PRO HG3 H 1.561 0.001 1 150 . 35 PRO HD2 H 3.447 0.000 1 151 . 35 PRO HD3 H 2.768 0.000 1 152 . 36 LYS H H 8.024 0.000 1 153 . 36 LYS HA H 4.141 0.000 1 154 . 36 LYS HB2 H 1.660 0.000 1 155 . 36 LYS HB3 H 1.441 0.001 1 156 . 36 LYS HG2 H 1.248 0.000 1 157 . 36 LYS HG3 H 1.162 0.000 1 158 . 37 THR H H 8.277 0.000 1 159 . 37 THR HA H 4.509 0.001 1 160 . 37 THR HB H 4.079 0.000 1 161 . 37 THR HG2 H 1.173 0.000 1 162 . 38 PRO HA H 4.389 0.001 1 163 . 38 PRO HD2 H 3.820 0.000 1 164 . 38 PRO HD3 H 3.656 0.000 1 165 . 39 LYS H H 8.523 0.000 1 166 . 39 LYS HA H 4.062 0.005 1 167 . 40 THR H H 7.772 0.000 1 168 . 40 THR HA H 4.228 0.000 1 169 . 40 THR HB H 4.167 0.000 1 170 . 40 THR HG2 H 1.140 0.000 1 stop_ save_