data_5495 #Corrected using PDB structure: 1LMMA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 6 K HA 3.17 4.21 # 9 G HA 4.21 3.37 # 17 C HA 4.94 4.07 # 21 L HA 5.04 4.29 # 31 E HA 4.18 5.32 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.10 N/A N/A N/A N/A -0.16 # #bmr5495.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5495.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.06 N/A N/A N/A N/A +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.431 N/A N/A N/A N/A 0.468 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.183 N/A N/A N/A N/A 0.302 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for Psalmotoxin 1 ; 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_ _BMRB_accession_number 5495 _BMRB_flat_file_name bmr5495.str _Entry_type new _Submission_date 2002-08-07 _Accession_date 2002-08-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 170 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _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 _Page_first 1332 _Page_last 1343 _Year 2003 loop_ _Keyword "Spider toxin" "structure determination" ICK ASIC 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_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1LMM ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_PcTx1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "psalmotoxin 1" _Name_variant . _Abbreviation_common PcTx1 _Mol_thiol_state 'all disulfide bound' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-03-18 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 1LMM "A Chain A, Solution Structure OfPsmalmotoxin 1, The First Characterized SpecificBlocker Of Asic1a Na+ Channel" 100.00 40 100 100 2e-20 SWISS-PROT P60514 "TXP1_PSACA Psalmotoxin 1 (PcTx1)" 100.00 40 100 100 2e-20 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "psalmotoxin 1" 3 CYS SG "psalmotoxin 1" 18 CYS SG single disulfide "psalmotoxin 1" 10 CYS SG "psalmotoxin 1" 23 CYS SG single disulfide "psalmotoxin 1" 17 CYS SG "psalmotoxin 1" 33 CYS SG 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 loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PcTx1 2.9 mM . stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions 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 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts 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" loop_ _Atom_shift_assign_ID _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 4.04 0.001 1 2 2 ASP H H 8.86 0.000 1 3 2 ASP HA H 4.75 0.001 1 4 2 ASP HB2 H 2.79 0.000 1 5 2 ASP HB3 H 2.57 0.000 1 6 3 CYS H H 8.38 0.000 1 7 3 CYS HA H 4.06 0.000 1 8 4 ILE H H 8.95 0.000 1 9 4 ILE HA H 4.28 0.000 1 10 4 ILE HB H 1.78 0.001 1 11 4 ILE HG2 H 0.89 0.025 1 12 4 ILE HD1 H 1.57 0.000 1 13 5 PRO HA H 4.30 0.000 1 14 5 PRO HG2 H 2.03 0.000 1 15 5 PRO HG3 H 1.75 0.000 1 16 5 PRO HD2 H 4.10 0.000 1 17 5 PRO HD3 H 3.59 0.000 1 18 6 LYS H H 7.62 0.000 1 19 6 LYS HA H 3.26 0.000 1 20 6 LYS HG2 H 0.65 0.000 1 21 6 LYS HG3 H 0.19 0.000 1 22 7 TRP H H 9.29 0.000 1 23 7 TRP HA H 4.23 0.001 1 24 7 TRP HD1 H 7.08 0.000 1 25 7 TRP HE1 H 10.21 0.001 1 26 7 TRP HH2 H 7.49 0.000 1 27 8 LYS H H 7.77 0.000 1 28 8 LYS HA H 4.71 0.000 1 29 8 LYS HB2 H 1.75 0.000 1 30 8 LYS HG2 H 1.50 0.000 1 31 8 LYS HG3 H 1.42 0.000 1 32 8 LYS HD2 H 2.00 0.000 1 33 8 LYS HD3 H 1.88 0.000 1 34 9 GLY H H 8.51 0.000 1 35 9 GLY HA2 H 4.67 0.001 1 36 9 GLY HA3 H 3.95 0.001 1 37 10 CYS H H 8.30 0.000 1 38 10 CYS HA H 4.90 0.000 1 39 10 CYS HB2 H 3.43 0.000 1 40 10 CYS HB3 H 3.16 0.000 1 41 11 VAL H H 7.90 0.000 1 42 11 VAL HA H 3.79 0.000 1 43 11 VAL HB H 1.99 0.000 1 44 11 VAL HG1 H 1.15 0.000 1 45 11 VAL HG2 H 0.92 0.000 1 46 12 ASN H H 8.93 0.000 1 47 12 ASN HA H 4.29 0.000 1 48 12 ASN HB2 H 3.05 0.000 1 49 12 ASN HB3 H 2.99 0.000 1 50 12 ASN HD21 H 7.61 0.000 1 51 12 ASN HD22 H 6.92 0.000 1 52 13 ARG H H 7.97 0.000 1 53 13 ARG HA H 4.61 0.000 1 54 13 ARG HG2 H 1.66 0.000 1 55 13 ARG HG3 H 1.49 0.000 1 56 13 ARG HD2 H 3.27 0.000 1 57 13 ARG HD3 H 3.04 0.000 1 58 13 ARG HE H 8.22 0.000 1 59 13 ARG HH21 H 6.95 0.000 1 60 13 ARG HH22 H 6.26 0.000 1 61 14 HIS H H 8.70 0.000 1 62 14 HIS HA H 4.59 0.001 1 63 14 HIS HD1 H 8.53 0.000 1 64 14 HIS HD2 H 7.92 0.606 1 65 14 HIS HE1 H 7.63 0.000 1 66 15 GLY H H 8.85 0.000 1 67 15 GLY HA2 H 4.47 0.000 1 68 15 GLY HA3 H 3.71 0.000 1 69 16 ASP H H 7.41 0.000 1 70 16 ASP HA H 4.92 0.000 1 71 16 ASP HB2 H 3.24 0.000 1 72 16 ASP HB3 H 2.68 0.000 1 73 17 CYS H H 8.62 0.000 1 74 17 CYS HA H 5.04 0.000 1 75 17 CYS HB2 H 2.97 0.000 1 76 17 CYS HB3 H 2.77 0.000 1 77 18 CYS H H 9.10 0.000 1 78 18 CYS HA H 4.45 0.000 1 79 18 CYS HB2 H 3.42 0.000 1 80 18 CYS HB3 H 2.50 0.000 1 81 19 GLU H H 8.22 0.000 1 82 19 GLU HA H 4.06 0.000 1 83 20 GLY H H 8.89 0.000 1 84 20 GLY HA2 H 4.24 0.000 1 85 20 GLY HA3 H 3.66 0.000 1 86 21 LEU H H 7.82 0.000 1 87 21 LEU HA H 5.13 0.000 1 88 21 LEU HB2 H 2.08 0.000 1 89 21 LEU HB3 H 0.96 0.000 1 90 21 LEU HG H 1.25 0.000 1 91 21 LEU HD1 H 0.65 0.000 1 92 21 LEU HD2 H 0.37 0.000 1 93 22 GLU H H 9.38 0.000 1 94 22 GLU HA H 4.67 0.000 1 95 22 GLU HB2 H 1.96 0.000 1 96 22 GLU HB3 H 1.81 0.000 1 97 23 CYS H H 8.94 0.000 1 98 23 CYS HA H 4.77 0.000 1 99 23 CYS HB2 H 3.14 0.000 1 100 23 CYS HB3 H 2.75 0.000 1 101 24 TRP H H 9.40 0.000 1 102 24 TRP HA H 4.87 0.000 1 103 24 TRP HB2 H 3.41 0.000 1 104 24 TRP HB3 H 3.02 0.000 1 105 24 TRP HD1 H 7.12 0.001 1 106 24 TRP HE1 H 10.18 0.000 1 107 24 TRP HZ2 H 7.15 0.000 1 108 24 TRP HH2 H 7.56 0.000 1 109 25 LYS H H 8.09 0.000 1 110 25 LYS HA H 4.18 0.001 1 111 26 ARG H H 7.60 0.000 1 112 26 ARG HA H 3.98 0.001 1 113 26 ARG HE H 7.02 0.000 1 114 27 ARG H H 8.38 0.000 1 115 27 ARG HA H 4.34 0.001 1 116 27 ARG HB2 H 1.87 0.004 1 117 27 ARG HB3 H 1.79 0.007 1 118 29 SER H H 8.02 0.000 1 119 29 SER HA H 4.37 0.000 1 120 29 SER HB2 H 3.76 0.000 1 121 29 SER HB3 H 3.61 0.002 1 122 30 PHE H H 7.86 0.000 1 123 30 PHE HA H 4.78 0.000 1 124 30 PHE HB2 H 3.18 0.003 1 125 30 PHE HB3 H 3.05 0.001 1 126 30 PHE HZ H 7.29 0.000 1 127 31 GLU H H 8.58 0.000 1 128 31 GLU HA H 4.28 0.000 1 129 31 GLU HG2 H 1.64 0.001 1 130 31 GLU HG3 H 1.45 0.001 1 131 32 VAL H H 8.37 0.001 1 132 32 VAL HA H 5.05 0.000 1 133 32 VAL HB H 1.78 0.000 1 134 32 VAL HG1 H 0.89 0.000 1 135 32 VAL HG2 H 0.82 0.000 1 136 33 CYS H H 8.22 0.000 1 137 33 CYS HA H 5.12 0.000 1 138 33 CYS HB2 H 2.96 0.000 1 139 33 CYS HB3 H 2.54 0.000 1 140 34 VAL H H 9.56 0.000 1 141 34 VAL HA H 4.50 0.004 1 142 34 VAL HB H 2.16 0.005 1 143 34 VAL HG1 H 1.03 0.003 1 144 34 VAL HG2 H 0.83 0.003 1 145 35 PRO HA H 4.36 0.000 1 146 35 PRO HB2 H 2.24 0.000 1 147 35 PRO HB3 H 1.80 0.000 1 148 35 PRO HG2 H 2.09 0.000 1 149 35 PRO HG3 H 1.56 0.001 1 150 35 PRO HD2 H 3.45 0.000 1 151 35 PRO HD3 H 2.77 0.000 1 152 36 LYS H H 8.02 0.000 1 153 36 LYS HA H 4.14 0.000 1 154 36 LYS HB2 H 1.66 0.000 1 155 36 LYS HB3 H 1.44 0.001 1 156 36 LYS HG2 H 1.25 0.000 1 157 36 LYS HG3 H 1.16 0.000 1 158 37 THR H H 8.28 0.000 1 159 37 THR HA H 4.51 0.001 1 160 37 THR HB H 4.08 0.000 1 161 37 THR HG2 H 1.17 0.000 1 162 38 PRO HA H 4.39 0.001 1 163 38 PRO HD2 H 3.82 0.000 1 164 38 PRO HD3 H 3.66 0.000 1 165 39 LYS H H 8.52 0.000 1 166 39 LYS HA H 4.06 0.005 1 167 40 THR H H 7.77 0.000 1 168 40 THR HA H 4.23 0.000 1 169 40 THR HB H 4.17 0.000 1 170 40 THR HG2 H 1.14 0.000 1 stop_ save_