data_4503 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Alpha-conotoxin SI ; _BMRB_accession_number 4503 _BMRB_flat_file_name bmr4503.str _Entry_type original _Submission_date 1999-10-08 _Accession_date 1999-12-06 _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 Benie A. J. . 2 Whitford D. . . 3 Hargittai B. . . 4 Barany G. . . 5 Janes R. W. . 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" 73 "13C chemical shifts" 37 "coupling constants" 18 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of Alpha-conotoxin SI' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20374965 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Benie A. J. . 2 Whitford D. . . 3 Hargittai B. . . 4 Barany G. . . 5 Janes R. W. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS Letters' _Journal_volume 476 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 287 _Page_last 295 _Year 2000 _Details . loop_ _Keyword conotoxin 'nicotinic acetylcholine receptor' toxin venom stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Delaglio, F. and Grzesiek, S. and Vuister, G. and Zhu, G. and Pfeifer, J. and Bax, A. NMRpipe - a multidimensional spectral processing system based on unix pipes. Journal of Biomolecular NMR (1995),6,277-293 ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F . . 2 Grzesiek S . . 3 Vuister G.W. W. . 4 Zhu G . . 5 Pfeifer J . . 6 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_citation_2 _Saveframe_category citation _Citation_full ; Bartels, C. and Xia, T. H. and Billeter, M. and Guntert, P. and Wuthrich, K. The program XEasy for computer-supported NMR spectral-analysis of biological macromolecules. Journal of Biomolecular NMR (1995),6,1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartels C. . . 2 Xia T.H. . . 3 Billeter M. . . 4 Guntert P. . . 5 Wuthrich K. . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_citation_3 _Saveframe_category citation _Citation_full ; Wishart, D. S. and Bigam, C. G. and Yao, J. and Abildgaard, F. and Dyson, H. J. and Oldfield, E. and Markley, J. L. and Sykes, B. D. 1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR. Journal of Biomolecular NMR (1995), 6, 135-140 ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart D.S. S. . 2 Bigam C.G. G. . 3 Yao J. . . 4 Abildgaard F. . . 5 Dyson H.J. J. . 6 Oldfield E. . . 7 Markley J.L. L. . 8 Sykes B.D. D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_SI _Saveframe_category molecular_system _Mol_system_name alpha-conotoxin_SI _Abbreviation_common SI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label conotoxin $SI 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_SI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common conotoxin _Name_variant none _Abbreviation_common SI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 14 _Mol_residue_sequence ICCNPACGPKYSCX loop_ _Residue_seq_code _Residue_label 1 ILE 2 CYS 3 CYS 4 ASN 5 PRO 6 ALA 7 CYS 8 GLY 9 PRO 10 LYS 11 TYR 12 SER 13 CYS 14 NH2 stop_ _Sequence_homology_query_date 2005-11-24 _Sequence_homology_query_revised_last_date 2005-11-22 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 4503 conotoxin 100.00 13 100 100 1.2 PDB 1HJE 'A Chain A, Crystal Structure OfAlpha-Conotoxin Si' 92.86 14 100 100 3.5 PDB 1QMW 'A Chain A, Solution Structure OfAlpha-Conotoxin Si' 92.86 14 100 100 3.5 SWISS-PROT P15471 'CXAS1_CONST Alpha-conotoxin SI precursor(S1)' 20.31 64 100 100 1.2 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 10:45:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 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 N HN1 ? ? SING N HN2 ? ? 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 conotoxin 3 CYS SG conotoxin 13 CYS SG single disulfide conotoxin 2 CYS SG conotoxin 7 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 _Organ _Secretion _Details $SI 'Striated Cone' 6493 Eukaryota Metazoa Conus striatus 'venom duct' 'venom component' 'Synthesised by Solid Phase Peptide Chemistry' 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 $SI 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Adjusted to pH4.2 with HCl' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $SI . mM 4.9 5.1 . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'Data processing' stop_ _Details . _Citation_label $citation_1 save_ save_XEasy _Saveframe_category software _Name XEasy _Version . loop_ _Task 'Data analysis' stop_ _Details 'Made use of the external program INFIT' _Citation_label $citation_2 save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version . loop_ _Task 'Data analysis and Processing' stop_ _Details 'Made use of the optional DECO module' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_2D_J_resolved_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D J resolved' _Sample_label $sample_1 save_ save_LED_6 _Saveframe_category NMR_applied_experiment _Experiment_name LED _Sample_label $sample_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D J resolved' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name LED _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 0.01 n/a temperature 283 0.1 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 _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value H2O H 1 proton ppm 4.91 internal direct . . . . . temperature 0.21 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_3 . . 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name conotoxin _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 ILE CA C 60.9 0.1 1 2 . 1 ILE HA H 3.74 0.02 1 3 . 1 ILE CB C 39.2 0.1 1 4 . 1 ILE HB H 1.95 0.02 1 5 . 1 ILE HG2 H 0.94 0.02 1 6 . 1 ILE CG2 C 17.4 0.1 1 7 . 1 ILE CG1 C 26.7 0.1 1 8 . 1 ILE HG12 H 1.15 0.02 2 9 . 1 ILE HG13 H 1.46 0.02 2 10 . 1 ILE HD1 H 0.83 0.02 1 11 . 1 ILE CD1 C 13.3 0.1 1 12 . 2 CYS H H 8.85 0.02 1 13 . 2 CYS CA C 59.4 0.1 1 14 . 2 CYS HA H 4.50 0.02 1 15 . 2 CYS CB C 36.8 0.1 1 16 . 2 CYS HB2 H 2.60 0.02 2 17 . 2 CYS HB3 H 3.54 0.02 2 18 . 3 CYS H H 9.31 0.02 1 19 . 3 CYS CA C 54.5 0.1 1 20 . 3 CYS HA H 4.65 0.02 1 21 . 3 CYS CB C 42.3 0.1 1 22 . 3 CYS HB2 H 2.78 0.02 2 23 . 3 CYS HB3 H 3.27 0.02 2 24 . 4 ASN H H 7.37 0.02 1 25 . 4 ASN CA C 52.5 0.1 1 26 . 4 ASN HA H 5.17 0.02 1 27 . 4 ASN CB C 40.6 0.1 1 28 . 4 ASN HB2 H 2.85 0.02 1 29 . 4 ASN HB3 H 2.85 0.02 1 30 . 4 ASN HD21 H 6.95 0.02 2 31 . 4 ASN HD22 H 7.84 0.02 2 32 . 5 PRO CD C 51.6 0.1 1 33 . 5 PRO CA C 65.6 0.1 1 34 . 5 PRO HA H 4.30 0.02 1 35 . 5 PRO CB C 32.3 0.1 1 36 . 5 PRO HB2 H 1.94 0.02 1 37 . 5 PRO HB3 H 2.36 0.02 1 38 . 5 PRO CG C 27.9 0.1 1 39 . 5 PRO HG2 H 1.96 0.02 1 40 . 5 PRO HG3 H 2.08 0.02 1 41 . 5 PRO HD2 H 3.75 0.02 2 42 . 5 PRO HD3 H 3.91 0.02 2 43 . 6 ALA H H 8.54 0.02 1 44 . 6 ALA CA C 53.6 0.1 1 45 . 6 ALA HA H 4.30 0.02 1 46 . 6 ALA HB H 1.38 0.02 1 47 . 6 ALA CB C 18.2 0.1 1 48 . 7 CYS H H 8.10 0.02 1 49 . 7 CYS CA C 59.2 0.1 1 50 . 7 CYS HA H 4.31 0.02 1 51 . 7 CYS CB C 44.5 0.1 1 52 . 7 CYS HB2 H 2.67 0.02 2 53 . 7 CYS HB3 H 3.42 0.02 2 54 . 8 GLY H H 8.11 0.02 1 55 . 8 GLY CA C 45.7 0.1 1 56 . 8 GLY HA3 H 3.74 0.02 2 57 . 8 GLY HA2 H 4.23 0.02 2 58 . 9 PRO CD C 51.4 0.1 1 59 . 9 PRO CA C 64.4 0.1 1 60 . 9 PRO HA H 4.50 0.02 1 61 . 9 PRO CB C 32.3 0.1 1 62 . 9 PRO HB2 H 2.37 0.02 1 63 . 9 PRO HB3 H 2.37 0.02 1 64 . 9 PRO CG C 27.3 0.1 1 65 . 9 PRO HG2 H 2.02 0.02 1 66 . 9 PRO HG3 H 2.02 0.02 1 67 . 9 PRO HD2 H 3.77 0.02 2 68 . 9 PRO HD3 H 3.98 0.02 2 69 . 10 LYS H H 7.73 0.02 1 70 . 10 LYS CA C 55.8 0.1 1 71 . 10 LYS HA H 4.35 0.02 1 72 . 10 LYS CB C 32.4 0.1 1 73 . 10 LYS HB2 H 1.82 0.02 1 74 . 10 LYS HB3 H 1.98 0.02 1 75 . 10 LYS CG C 25.6 0.1 1 76 . 10 LYS HG2 H 1.39 0.02 1 77 . 10 LYS HG3 H 1.46 0.02 1 78 . 10 LYS CD C 29.2 0.1 1 79 . 10 LYS HD2 H 1.66 0.02 1 80 . 10 LYS HD3 H 1.66 0.02 1 81 . 10 LYS CE C 42.4 0.1 1 82 . 10 LYS HE2 H 2.98 0.02 1 83 . 10 LYS HE3 H 2.98 0.02 1 84 . 10 LYS HZ H 7.59 0.02 2 85 . 11 TYR H H 7.74 0.02 1 86 . 11 TYR CA C 59.7 0.1 1 87 . 11 TYR HA H 4.44 0.02 1 88 . 11 TYR CB C 38.9 0.1 1 89 . 11 TYR HB2 H 2.93 0.02 2 90 . 11 TYR HB3 H 3.05 0.02 2 91 . 11 TYR HD1 H 7.01 0.02 1 92 . 11 TYR HD2 H 7.01 0.02 1 93 . 11 TYR HE1 H 6.63 0.02 1 94 . 11 TYR HE2 H 6.63 0.02 1 95 . 11 TYR CD1 C 133.7 0.1 1 96 . 11 TYR CE1 C 118.1 0.1 1 97 . 12 SER H H 8.43 0.02 1 98 . 12 SER CA C 58.5 0.1 1 99 . 12 SER HA H 4.23 0.02 1 100 . 12 SER CB C 63.4 0.1 1 101 . 12 SER HB2 H 3.64 0.02 1 102 . 12 SER HB3 H 3.85 0.02 1 103 . 13 CYS H H 8.70 0.02 1 104 . 13 CYS CA C 56.8 0.1 1 105 . 13 CYS HA H 4.57 0.02 1 106 . 13 CYS CB C 46.1 0.1 1 107 . 13 CYS HB2 H 2.78 0.02 2 108 . 13 CYS HB3 H 3.21 0.02 2 109 . 14 NH2 HN1 H 7.36 0.02 1 110 . 14 NH2 HN2 H 7.59 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name conotoxin _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 2 CYS H 2 CYS HA 7.8 . . 0.1 2 3JHNHA 3 CYS H 3 CYS HA 8.4 . . 0.1 3 3JHNHA 4 ASN H 4 ASN HA 8.2 . . 0.1 4 3JHNHA 6 ALA H 6 ALA HA 6.1 . . 0.1 5 3JHNHA 7 CYS H 7 CYS HA 4.6 . . 0.1 6 3JHNHA 10 LYS H 10 LYS HA 8.8 . . 0.1 7 3JHNHA 11 TYR H 11 TYR HA 4.9 . . 0.1 8 3JHNHA 12 SER H 12 SER HA 6.1 . . 0.1 9 3JHNHA 13 CYS H 13 CYS HA 10.2 . . 0.1 stop_ save_ save_coupling_constants_set_2 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name conotoxin _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 2 CYS H 2 CYS HA 7.2 . . 0.1 2 3JHNHA 3 CYS H 3 CYS HA 9.4 . . 0.1 3 3JHNHA 4 ASN H 4 ASN HA 8.2 . . 0.1 4 3JHNHA 6 ALA H 6 ALA HA 6.1 . . 0.1 5 3JHNHA 7 CYS H 7 CYS HA 5.2 . . 0.1 6 3JHNHA 10 LYS H 10 LYS HA 8.7 . . 0.1 7 3JHNHA 11 TYR H 11 TYR HA 4.7 . . 0.1 8 3JHNHA 12 SER H 12 SER HA 6.8 . . 0.1 9 3JHNHA 13 CYS H 13 CYS HA 10.2 . . 0.1 stop_ save_