data_5184 #Corrected using PDB structure: 1J5JA # #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 # 11 Y HA 3.66 4.45 # 15 P HA 4.35 3.43 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 N/A N/A N/A N/A 0.20 # #bmr5184.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5184.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 #+/-0.05 N/A N/A N/A N/A +/-0.11 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.800 N/A N/A N/A N/A 0.784 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.155 N/A N/A N/A N/A 0.308 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for toxin BeKm from the Scorpion Buthus eupeus ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bocharov Eduard V. . 2 Maslennikov Innokenty V. . 3 Korolkova Yuliya V. . 4 Grishin Eugene V. . 5 Arseniev Alexandr S. . stop_ _BMRB_accession_number 5184 _BMRB_flat_file_name bmr5184.str _Entry_type new _Submission_date 2001-10-19 _Accession_date 2001-10-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 214 'coupling constants' 30 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Inverse active site of scorpion toxin BeKm ; _Citation_status 'in preparation' _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bocharov Eduard V. . 2 Maslennikov Innokenty V. . 3 Korolkova Yuliya V. . 4 Grishin Eugene V. . 5 Arseniev Alexandr S. . stop_ _Journal_abbreviation "Nat. Struct. Biol." _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year ? loop_ _Keyword "scorpion toxin BeKm" "potassium channel" "mutants" "activity" "NMR" "spatial structure" stop_ save_ ################################## # Molecular system description # ################################## save_system_BeKm _Saveframe_category molecular_system _Mol_system_name "toxin BeKm from the scorpion Buthus eupeus" _Abbreviation_common BeKm _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BeKm $BeKm stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function "Scorpion toxin BeKm is specific blocker of hERG1 potassium channels." stop_ save_ ######################## # Monomeric polymers # ######################## save_BeKm _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "scorpion toxin BeKm" _Name_variant . _Abbreviation_common BeKm _Molecular_mass 4092 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Sequence_citation_label $ref-5 ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; RPTDIKCSESYQCFPVCKSR FGKTNGRCVNGFCDCF ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 PRO 3 THR 4 ASP 5 ILE 6 LYS 7 CYS 8 SER 9 GLU 10 SER 11 TYR 12 GLN 13 CYS 14 PHE 15 PRO 16 VAL 17 CYS 18 LYS 19 SER 20 ARG 21 PHE 22 GLY 23 LYS 24 THR 25 ASN 26 GLY 27 ARG 28 CYS 29 VAL 30 ASN 31 GLY 32 PHE 33 CYS 34 ASP 35 CYS 36 PHE stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-06 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 1J5J "A Chain A, Solution Structure OfHerg-Specific Scorpion Toxin Bekm-1" 100.00 36 100 100 7e-17 PDB 1LGL "A Chain A, Solution Structure OfHerg-Specific Scorpion Toxin Bekm-1" 100.00 36 100 100 7e-17 GenBank AAK28021.1 "BeKm-1 toxin precursor [Mesobuthuseupeus]" 63.16 57 100 100 7e-17 SWISS-PROT Q9BKB7 "SEKM_BUTEU Neurotoxin BeKm-1 precursor(Gamma-KTx 2.1)" 63.16 57 100 100 7e-17 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _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 BeKm 7 CYS SG BeKm 28 CYS SG single disulfide BeKm 13 CYS SG BeKm 33 CYS SG single disulfide BeKm 17 CYS SG BeKm 35 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 _Secretion $BeKm "lesser Asian scorpion" 34648 Eukaryota Metazoa Buthus eupeus venom stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Cell_line $BeKm 'recombinant technology' "E. coli" Escherichia coli HB101 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 $BeKm 1.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2.11 loop_ _Task "peak assignments" stop_ _Citation_label $ref-1 save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task "structure calculation" stop_ _Citation_label $ref-2 save_ save_FANTOM _Saveframe_category software _Name FANTOM _Version 4 loop_ _Task "energy minimization" stop_ _Citation_label $ref-3 save_ save_MOLMOL _Saveframe_category software _Name MOLMOL _Version 2.5.1 loop_ _Task "visualization" "structure analysis" stop_ _Citation_label $ref-4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H COSY 1H TOCSY 1H NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.5 0.2 n/a temperature 303 0.5 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BeKm 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 ARG HA H 4.37 0.02 1 2 1 ARG HB2 H 1.90 0.02 1 3 1 ARG HB3 H 1.90 0.02 1 4 1 ARG HG2 H 1.64 0.02 1 5 1 ARG HG3 H 1.64 0.02 1 6 1 ARG HD2 H 3.06 0.02 1 7 1 ARG HD3 H 3.06 0.02 1 8 1 ARG HE H 7.09 0.02 1 9 2 PRO HA H 4.68 0.02 1 10 2 PRO HB2 H 1.90 0.02 1 11 2 PRO HB3 H 2.33 0.02 1 12 2 PRO HG2 H 1.98 0.02 1 13 2 PRO HG3 H 1.98 0.02 1 14 2 PRO HD2 H 3.58 0.02 1 15 2 PRO HD3 H 3.73 0.02 1 16 3 THR H H 7.72 0.02 1 17 3 THR HA H 4.69 0.02 1 18 3 THR HB H 4.26 0.02 1 19 3 THR HG2 H 0.87 0.02 1 20 4 ASP H H 8.33 0.02 1 21 4 ASP HA H 4.68 0.02 1 22 4 ASP HB2 H 2.99 0.02 1 23 4 ASP HB3 H 2.70 0.02 1 24 5 ILE H H 8.24 0.02 1 25 5 ILE HA H 4.12 0.02 1 26 5 ILE HB H 1.75 0.02 1 27 5 ILE HG2 H 0.93 0.02 1 28 5 ILE HG12 H 1.33 0.02 1 29 5 ILE HG13 H 1.65 0.02 1 30 5 ILE HD1 H 0.96 0.02 1 31 6 LYS H H 8.34 0.02 1 32 6 LYS HA H 4.41 0.02 1 33 6 LYS HB2 H 1.57 0.02 1 34 6 LYS HB3 H 1.57 0.02 1 35 6 LYS HG2 H 1.10 0.02 1 36 6 LYS HG3 H 1.10 0.02 1 37 6 LYS HD2 H 1.43 0.02 1 38 6 LYS HD3 H 1.43 0.02 1 39 7 CYS H H 8.00 0.02 1 40 7 CYS HA H 4.60 0.02 1 41 7 CYS HB2 H 2.95 0.02 1 42 7 CYS HB3 H 2.80 0.02 1 43 8 SER H H 9.29 0.02 1 44 8 SER HA H 4.54 0.02 1 45 8 SER HB2 H 3.75 0.02 1 46 8 SER HB3 H 3.87 0.02 1 47 9 GLU H H 7.66 0.02 1 48 9 GLU HA H 4.76 0.02 1 49 9 GLU HB2 H 1.31 0.02 1 50 9 GLU HB3 H 2.14 0.02 1 51 9 GLU HG2 H 2.41 0.02 1 52 9 GLU HG3 H 2.43 0.02 1 53 10 SER H H 9.33 0.02 1 54 10 SER HA H 3.91 0.02 1 55 10 SER HB2 H 4.18 0.02 1 56 10 SER HB3 H 4.02 0.02 1 57 11 TYR H H 8.35 0.02 1 58 11 TYR HA H 3.70 0.02 1 59 11 TYR HB2 H 3.13 0.02 1 60 11 TYR HB3 H 2.94 0.02 1 61 11 TYR HD1 H 7.06 0.02 1 62 11 TYR HD2 H 7.06 0.02 1 63 11 TYR HE1 H 6.81 0.02 1 64 11 TYR HE2 H 6.81 0.02 1 65 12 GLN H H 6.79 0.02 1 66 12 GLN HA H 3.93 0.02 1 67 12 GLN HB2 H 2.21 0.02 1 68 12 GLN HB3 H 2.01 0.02 1 69 12 GLN HG2 H 2.29 0.02 1 70 12 GLN HG3 H 1.47 0.02 1 71 12 GLN HE21 H 7.30 0.02 1 72 12 GLN HE22 H 6.83 0.02 1 73 13 CYS H H 7.84 0.02 1 74 13 CYS HA H 4.58 0.02 1 75 13 CYS HB2 H 2.61 0.02 1 76 13 CYS HB3 H 2.95 0.02 1 77 14 PHE H H 7.28 0.02 1 78 14 PHE HA H 4.32 0.02 1 79 14 PHE HB2 H 3.29 0.02 1 80 14 PHE HB3 H 3.36 0.02 1 81 14 PHE HD1 H 7.26 0.02 1 82 14 PHE HD2 H 7.26 0.02 1 83 14 PHE HE1 H 7.52 0.02 1 84 14 PHE HE2 H 7.52 0.02 1 85 14 PHE HZ H 7.42 0.02 1 86 15 PRO HA H 4.39 0.02 1 87 15 PRO HB2 H 1.99 0.02 1 88 15 PRO HB3 H 2.38 0.02 1 89 15 PRO HG2 H 2.13 0.02 1 90 15 PRO HG3 H 2.13 0.02 1 91 15 PRO HD2 H 3.86 0.02 1 92 15 PRO HD3 H 3.86 0.02 1 93 16 VAL H H 6.63 0.02 1 94 16 VAL HA H 4.11 0.02 1 95 16 VAL HB H 2.17 0.02 1 96 16 VAL HG1 H 1.09 0.02 1 97 16 VAL HG2 H 1.14 0.02 1 98 17 CYS H H 8.46 0.02 1 99 17 CYS HA H 4.76 0.02 1 100 17 CYS HB2 H 2.75 0.02 1 101 17 CYS HB3 H 2.86 0.02 1 102 18 LYS H H 7.66 0.02 1 103 18 LYS HA H 4.24 0.02 1 104 18 LYS HB2 H 1.83 0.02 1 105 18 LYS HB3 H 1.83 0.02 1 106 18 LYS HG2 H 1.28 0.02 1 107 18 LYS HG3 H 1.35 0.02 1 108 18 LYS HD2 H 1.53 0.02 1 109 18 LYS HD3 H 1.53 0.02 1 110 19 SER H H 8.35 0.02 1 111 19 SER HA H 4.18 0.02 1 112 19 SER HB2 H 3.98 0.02 1 113 19 SER HB3 H 3.98 0.02 1 114 20 ARG H H 8.44 0.02 1 115 20 ARG HA H 4.19 0.02 1 116 20 ARG HB2 H 1.15 0.02 1 117 20 ARG HB3 H 1.53 0.02 1 118 20 ARG HG2 H 1.38 0.02 1 119 20 ARG HG3 H 1.05 0.02 1 120 20 ARG HD2 H 2.92 0.02 1 121 20 ARG HD3 H 2.92 0.02 1 122 20 ARG HE H 7.08 0.02 1 123 21 PHE H H 6.94 0.02 1 124 21 PHE HA H 4.92 0.02 1 125 21 PHE HB2 H 3.06 0.02 1 126 21 PHE HB3 H 3.44 0.02 1 127 21 PHE HD1 H 7.40 0.02 1 128 21 PHE HD2 H 7.40 0.02 1 129 21 PHE HE1 H 7.26 0.02 1 130 21 PHE HE2 H 7.26 0.02 1 131 21 PHE HZ H 7.35 0.02 1 132 22 GLY H H 7.69 0.02 1 133 22 GLY HA2 H 4.02 0.02 1 134 22 GLY HA3 H 4.02 0.02 1 135 23 LYS H H 7.79 0.02 1 136 23 LYS HA H 4.72 0.02 1 137 23 LYS HB2 H 1.38 0.02 1 138 23 LYS HB3 H 2.09 0.02 1 139 23 LYS HG2 H 1.13 0.02 1 140 23 LYS HG3 H 1.41 0.02 1 141 23 LYS HD2 H 1.64 0.02 1 142 23 LYS HD3 H 1.64 0.02 1 143 23 LYS HE2 H 2.98 0.02 1 144 23 LYS HE3 H 2.98 0.02 1 145 24 THR H H 8.46 0.02 1 146 24 THR HA H 4.05 0.02 1 147 24 THR HB H 4.30 0.02 1 148 24 THR HG2 H 1.13 0.02 1 149 25 ASN H H 7.80 0.02 1 150 25 ASN HA H 4.67 0.02 1 151 25 ASN HB2 H 1.64 0.02 1 152 25 ASN HB3 H 1.68 0.02 1 153 25 ASN HD21 H 7.36 0.02 1 154 25 ASN HD22 H 6.81 0.02 1 155 26 GLY H H 7.08 0.02 1 156 26 GLY HA2 H 5.01 0.02 1 157 26 GLY HA3 H 3.31 0.02 1 158 27 ARG H H 8.77 0.02 1 159 27 ARG HA H 4.64 0.02 1 160 27 ARG HB2 H 1.86 0.02 1 161 27 ARG HB3 H 1.86 0.02 1 162 27 ARG HG2 H 1.62 0.02 1 163 27 ARG HG3 H 1.66 0.02 1 164 27 ARG HD2 H 3.14 0.02 1 165 27 ARG HD3 H 3.14 0.02 1 166 27 ARG HE H 7.18 0.02 1 167 28 CYS H H 8.89 0.02 1 168 28 CYS HA H 4.80 0.02 1 169 28 CYS HB2 H 2.26 0.02 1 170 28 CYS HB3 H 2.78 0.02 1 171 29 VAL H H 9.07 0.02 1 172 29 VAL HA H 4.24 0.02 1 173 29 VAL HB H 2.03 0.02 1 174 29 VAL HG1 H 0.91 0.02 1 175 29 VAL HG2 H 0.87 0.02 1 176 30 ASN H H 9.35 0.02 1 177 30 ASN HA H 4.33 0.02 1 178 30 ASN HB2 H 2.87 0.02 1 179 30 ASN HB3 H 3.16 0.02 1 180 30 ASN HD21 H 7.65 0.02 1 181 30 ASN HD22 H 6.89 0.02 1 182 31 GLY H H 7.94 0.02 1 183 31 GLY HA2 H 3.75 0.02 1 184 31 GLY HA3 H 3.86 0.02 1 185 32 PHE H H 7.67 0.02 1 186 32 PHE HA H 5.45 0.02 1 187 32 PHE HB2 H 2.68 0.02 1 188 32 PHE HB3 H 3.20 0.02 1 189 32 PHE HD1 H 7.06 0.02 1 190 32 PHE HD2 H 7.06 0.02 1 191 32 PHE HE1 H 7.27 0.02 1 192 32 PHE HE2 H 7.27 0.02 1 193 32 PHE HZ H 7.25 0.02 1 194 33 CYS H H 9.03 0.02 1 195 33 CYS HA H 4.92 0.02 1 196 33 CYS HB2 H 2.76 0.02 1 197 33 CYS HB3 H 2.56 0.02 1 198 34 ASP H H 9.65 0.02 1 199 34 ASP HA H 5.13 0.02 1 200 34 ASP HB2 H 2.56 0.02 1 201 34 ASP HB3 H 2.85 0.02 1 202 35 CYS H H 8.06 0.02 1 203 35 CYS HA H 5.49 0.02 1 204 35 CYS HB2 H 2.35 0.02 1 205 35 CYS HB3 H 2.86 0.02 1 206 36 PHE H H 8.25 0.02 1 207 36 PHE HA H 4.53 0.02 1 208 36 PHE HB2 H 3.06 0.02 1 209 36 PHE HB3 H 2.94 0.02 1 210 36 PHE HD1 H 7.00 0.02 1 211 36 PHE HD2 H 7.00 0.02 1 212 36 PHE HE1 H 7.02 0.02 1 213 36 PHE HE2 H 7.02 0.02 1 214 36 PHE HZ H 7.09 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name BeKm loop_ _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_value_error 3JHNHA 3 THR H 3 THR HA 9.5 1.0 3JHNHA 4 ASP H 4 ASP HA 8.5 1.0 3JHNHA 5 ILE H 5 ILE HA 7.5 1.0 3JHNHA 6 LYS H 6 LYS HA 5.0 1.0 3JHNHA 7 CYS H 7 CYS HA 8.0 1.0 3JHNHA 8 SER H 8 SER HA 8.3 1.0 3JHNHA 9 GLU H 9 GLU HA 5.5 1.0 3JHNHA 10 SER H 10 SER HA 5.0 1.0 3JHNHA 11 TYR H 11 TYR HA 4.0 1.0 3JHNHA 12 GLN H 12 GLN HA 6.0 1.0 3JHNHA 13 CYS H 13 CYS HA 6.5 1.0 3JHNHA 14 PHE H 14 PHE HA 4.0 1.0 3JHNHA 16 VAL H 16 VAL HA 5.0 1.0 3JHNHA 17 CYS H 17 CYS HA 4.5 1.0 3JHNHA 18 LYS H 18 LYS HA 4.0 1.0 3JHNHA 19 SER H 19 SER HA 5.5 1.0 3JHNHA 20 ARG H 20 ARG HA 7.5 1.0 3JHNHA 21 PHE H 21 PHE HA 7.5 1.0 3JHNHA 23 LYS H 23 LYS HA 8.0 1.0 3JHNHA 24 THR H 24 THR HA 8.5 1.0 3JHNHA 25 ASN H 25 ASN HA 7.5 1.0 3JHNHA 27 ARG H 27 ARG HA 8.8 1.0 3JHNHA 28 CYS H 28 CYS HA 8.2 1.0 3JHNHA 29 VAL H 29 VAL HA 10.4 1.0 3JHNHA 30 ASN H 30 ASN HA 6.5 1.0 3JHNHA 32 PHE H 32 PHE HA 10.5 1.0 3JHNHA 33 CYS H 33 CYS HA 4.5 1.0 3JHNHA 34 ASP H 34 ASP HA 9.0 1.0 3JHNHA 35 CYS H 35 CYS HA 10.0 1.0 3JHNHA 36 PHE H 36 PHE HA 7.0 1.0 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _PubMed_ID . _Citation_full ; Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10. ; save_ save_ref-2 _Saveframe_category citation _PubMed_ID . _Citation_full ; Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298. ; save_ save_ref-3 _Saveframe_category citation _PubMed_ID . _Citation_full ; Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694. ; save_ save_ref-4 _Saveframe_category citation _PubMed_ID 9367762 _Citation_full ; Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55. ; save_ save_ref-5 _Saveframe_category citation _PubMed_ID 11136720 _Citation_full ; Korolkova YV, Kozlov SA, Lipkin AV, Pluzhnikov KA, Hadley JK, Filippov AK, Brown DA, Angelo K, Strobaek D, Jespersen T, Olesen SP, Jensen BS, Grishin EV. An ERG channel inhibitor from the scorpion Buthus eupeus. J. Biol. Chem. 2001 Mar 30;276(13):9868-76 ; save_