data_4815 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of Cardiotoxin in DPC-micelle ; _BMRB_accession_number 4815 _BMRB_flat_file_name bmr4815.str _Entry_type original _Submission_date 2000-08-28 _Accession_date 2000-08-28 _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 Dubovskii P. V. . 2 Dementieva D. V. . 3 Bocharov E. V. . 4 Utkin Yu. N. . 5 Arseniev A. S. . stop_ 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" 369 "coupling constants" 52 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-11-13 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4419 . stop_ _Original_release_date 2000-11-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Membrane Binding Motif of the P-type Cardiotoxin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11114253 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dubovskii P. V. . 2 Dementieva D. V. . 3 Bocharov E. V. . 4 Utkin Yu. N. . 5 Arseniev A. S. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 305 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 137 _Page_last 149 _Year 2001 _Details . loop_ _Keyword 'all-beta sheet protein' 'membrane perturbation' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Bartels C., Xia T.-H., Billeter M., Guentert P. & Wuethrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _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_ref-2 _Saveframe_category citation _Citation_full ; Guentert P., Mumenthaler C. & Wuethrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298. ; _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guentert P. . . 2 Mumenthaler C. . . 3 Wuethrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _Journal_issue 1 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ ################################## # Molecular system description # ################################## save_system_CTII _Saveframe_category molecular_system _Mol_system_name 'CYTOTOXIN 2' _Abbreviation_common CTII _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CYTOTOXIN 2' $CTII 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_CTII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'CYTOTOXIN 2' _Abbreviation_common CTII _Molecular_mass 6732 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; LKCKKLVPLFSKTCPAGKNL CYKMFMVAAPHVPVKRGCID VCPKSSLLVKYVCCNTDKCN ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 LYS 3 CYS 4 LYS 5 LYS 6 LEU 7 VAL 8 PRO 9 LEU 10 PHE 11 SER 12 LYS 13 THR 14 CYS 15 PRO 16 ALA 17 GLY 18 LYS 19 ASN 20 LEU 21 CYS 22 TYR 23 LYS 24 MET 25 PHE 26 MET 27 VAL 28 ALA 29 ALA 30 PRO 31 HIS 32 VAL 33 PRO 34 VAL 35 LYS 36 ARG 37 GLY 38 CYS 39 ILE 40 ASP 41 VAL 42 CYS 43 PRO 44 LYS 45 SER 46 SER 47 LEU 48 LEU 49 VAL 50 LYS 51 TYR 52 VAL 53 CYS 54 CYS 55 ASN 56 THR 57 ASP 58 LYS 59 CYS 60 ASN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P01441 'Cytotoxin-2 (Cytotoxin II) (CTII)' 100.00 60 100.00 100.00 9.02e-26 SWISS-PROT Q9PS34 Cytotoxin-Vc-5 100.00 60 98.33 100.00 1.34e-25 PDB 1FFJ 'Nmr Structure Of Cardiotoxin In Dpc-Micelle' 98.33 60 100.00 100.00 2.97e-25 GenBank AAB24494 'Vc-5=cytotoxin [Naja oxiana=snakes, venom, Peptide, 60 aa]' 100.00 60 98.33 100.00 1.34e-25 PDB 1CB9 'Nmr Structure With Tightly Bound Water Molecules Of Cytotoxin Ii (Cardiotoxin) From Naja Naja Oxiana In Aqueous Solution (Major Form).' 98.33 60 100.00 100.00 2.97e-25 PDB 1CCQ 'Nmr Structure With Tightly Bound Water Molecules Of Cytotoxin Ii (Cardiotoxin) From Naja Naja Oxiana In Aqueous Solution (Minor Form).' 98.33 60 100.00 100.00 2.97e-25 BMRB 4418 'cytotoxin 2' 100.00 60 100.00 100.00 9.02e-26 BMRB 4419 'cytotoxin 2' 100.00 60 100.00 100.00 9.02e-26 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 $CTII Snake 8657 Eukaryota Metazoa Naja oxiana venom 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 $CTII 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelles _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CTII 3.0 mM . 'perdeuterated dodecylphosphocholine' 120 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type micelles _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CTII 3.0 mM . 'perdeuterated dodecylphosphocholine' 120 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1A loop_ _Task 'data collection' stop_ _Details 'Varian software' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2.11 loop_ _Task 'data analysis' stop_ _Details . _Citation_label $ref-1 save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure calculation' stop_ _Details . _Citation_label $ref-2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 0.2 n/a temperature 318 0.5 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_chemical_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 'CYTOTOXIN 2' _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 LEU HA H 4.23 0.015 1 2 . 1 LEU HB2 H 1.60 0.015 1 3 . 1 LEU HB3 H 1.60 0.015 1 4 . 1 LEU HD1 H 0.81 0.015 2 5 . 1 LEU HD2 H 0.88 0.015 2 6 . 2 LYS H H 8.58 0.015 1 7 . 2 LYS HA H 5.50 0.015 1 8 . 2 LYS HB2 H 1.39 0.015 2 9 . 2 LYS HB3 H 1.52 0.015 2 10 . 2 LYS HG2 H 1.44 0.015 2 11 . 2 LYS HG3 H 1.50 0.015 2 12 . 2 LYS HD2 H 1.58 0.015 1 13 . 2 LYS HD3 H 1.58 0.015 1 14 . 2 LYS HE2 H 2.95 0.015 1 15 . 2 LYS HE3 H 2.95 0.015 1 16 . 3 CYS H H 8.63 0.015 1 17 . 3 CYS HA H 5.12 0.015 1 18 . 3 CYS HB2 H 2.40 0.015 2 19 . 3 CYS HB3 H 2.95 0.015 2 20 . 4 LYS H H 9.60 0.015 1 21 . 4 LYS HA H 4.36 0.015 1 22 . 4 LYS HB2 H 1.51 0.015 2 23 . 4 LYS HB3 H 1.64 0.015 2 24 . 4 LYS HG2 H 1.14 0.015 1 25 . 4 LYS HG3 H 1.14 0.015 1 26 . 4 LYS HD2 H 1.86 0.015 1 27 . 4 LYS HD3 H 1.86 0.015 1 28 . 5 LYS H H 7.55 0.015 1 29 . 5 LYS HA H 4.27 0.015 1 30 . 5 LYS HB2 H 1.67 0.015 2 31 . 5 LYS HB3 H 2.27 0.015 2 32 . 5 LYS HG2 H 1.34 0.015 2 33 . 5 LYS HG3 H 1.40 0.015 2 34 . 5 LYS HD2 H 1.70 0.015 1 35 . 5 LYS HD3 H 1.70 0.015 1 36 . 5 LYS HE2 H 2.99 0.015 2 37 . 5 LYS HE3 H 3.05 0.015 2 38 . 6 LEU H H 8.21 0.015 1 39 . 6 LEU HA H 3.69 0.015 1 40 . 6 LEU HB2 H 1.76 0.015 2 41 . 6 LEU HB3 H 1.88 0.015 2 42 . 6 LEU HG H 1.63 0.015 1 43 . 6 LEU HD1 H 0.91 0.015 2 44 . 6 LEU HD2 H 1.01 0.015 2 45 . 7 VAL H H 7.23 0.015 1 46 . 7 VAL HA H 4.44 0.015 1 47 . 7 VAL HB H 2.35 0.015 1 48 . 7 VAL HG1 H 1.00 0.015 2 49 . 8 PRO HA H 4.57 0.015 1 50 . 8 PRO HB2 H 1.85 0.015 2 51 . 8 PRO HB3 H 2.22 0.015 2 52 . 8 PRO HG2 H 2.01 0.015 2 53 . 8 PRO HG3 H 2.35 0.015 2 54 . 8 PRO HD2 H 3.57 0.015 2 55 . 8 PRO HD3 H 4.18 0.015 2 56 . 9 LEU H H 6.12 0.015 1 57 . 9 LEU HA H 4.07 0.015 1 58 . 9 LEU HB2 H 0.80 0.015 2 59 . 9 LEU HB3 H 1.22 0.015 2 60 . 9 LEU HG H 1.38 0.015 1 61 . 9 LEU HD1 H 0.78 0.015 2 62 . 9 LEU HD2 H 0.79 0.015 2 63 . 10 PHE H H 7.96 0.015 1 64 . 10 PHE HA H 5.08 0.015 1 65 . 10 PHE HB2 H 2.89 0.015 2 66 . 10 PHE HB3 H 3.47 0.015 2 67 . 10 PHE HD1 H 7.40 0.015 1 68 . 10 PHE HD2 H 7.40 0.015 1 69 . 10 PHE HE1 H 7.29 0.015 1 70 . 10 PHE HE2 H 7.29 0.015 1 71 . 10 PHE HZ H 7.21 0.015 1 72 . 11 SER H H 8.73 0.015 1 73 . 11 SER HA H 5.25 0.015 1 74 . 11 SER HB2 H 3.56 0.015 2 75 . 11 SER HB3 H 3.64 0.015 2 76 . 12 LYS H H 8.90 0.015 1 77 . 12 LYS HA H 4.87 0.015 1 78 . 12 LYS HB2 H 1.78 0.015 2 79 . 12 LYS HB3 H 1.79 0.015 2 80 . 12 LYS HG2 H 1.29 0.015 2 81 . 12 LYS HG3 H 1.42 0.015 2 82 . 12 LYS HD2 H 1.73 0.015 2 83 . 12 LYS HD3 H 1.77 0.015 2 84 . 12 LYS HE2 H 3.05 0.015 1 85 . 12 LYS HE3 H 3.05 0.015 1 86 . 13 THR H H 8.70 0.015 1 87 . 13 THR HA H 4.59 0.015 1 88 . 13 THR HB H 4.08 0.015 1 89 . 13 THR HG2 H 1.28 0.015 1 90 . 14 CYS H H 9.09 0.015 1 91 . 14 CYS HA H 5.04 0.015 1 92 . 14 CYS HB2 H 2.83 0.015 2 93 . 14 CYS HB3 H 3.54 0.015 2 94 . 15 PRO HA H 4.64 0.015 1 95 . 15 PRO HB2 H 2.00 0.015 2 96 . 15 PRO HB3 H 2.43 0.015 2 97 . 15 PRO HG2 H 1.95 0.015 2 98 . 15 PRO HG3 H 2.22 0.015 2 99 . 15 PRO HD2 H 3.49 0.015 2 100 . 15 PRO HD3 H 4.01 0.015 2 101 . 16 ALA H H 8.33 0.015 1 102 . 16 ALA HA H 4.15 0.015 1 103 . 16 ALA HB H 1.41 0.015 1 104 . 17 GLY H H 8.67 0.015 1 105 . 17 GLY HA3 H 3.71 0.015 2 106 . 17 GLY HA2 H 4.30 0.015 2 107 . 18 LYS H H 7.62 0.015 1 108 . 18 LYS HA H 4.31 0.015 1 109 . 18 LYS HB2 H 1.94 0.015 1 110 . 18 LYS HB3 H 1.94 0.015 1 111 . 18 LYS HG2 H 1.13 0.015 2 112 . 18 LYS HG3 H 1.38 0.015 2 113 . 18 LYS HD2 H 1.55 0.015 1 114 . 18 LYS HD3 H 1.55 0.015 1 115 . 18 LYS HE2 H 2.99 0.015 1 116 . 18 LYS HE3 H 2.99 0.015 1 117 . 19 ASN H H 7.82 0.015 1 118 . 19 ASN HA H 4.93 0.015 1 119 . 19 ASN HB2 H 2.69 0.015 2 120 . 19 ASN HB3 H 3.06 0.015 2 121 . 19 ASN HD21 H 6.90 0.015 2 122 . 19 ASN HD22 H 7.41 0.015 2 123 . 20 LEU H H 8.20 0.015 1 124 . 20 LEU HA H 4.92 0.015 1 125 . 20 LEU HB2 H 1.41 0.015 2 126 . 20 LEU HB3 H 1.73 0.015 2 127 . 20 LEU HG H 1.58 0.015 1 128 . 20 LEU HD1 H 0.77 0.015 2 129 . 20 LEU HD2 H 0.89 0.015 2 130 . 21 CYS H H 9.02 0.015 1 131 . 21 CYS HA H 6.12 0.015 1 132 . 21 CYS HB2 H 2.97 0.015 2 133 . 21 CYS HB3 H 3.11 0.015 2 134 . 22 TYR H H 8.98 0.015 1 135 . 22 TYR HA H 6.13 0.015 1 136 . 22 TYR HB2 H 3.15 0.015 2 137 . 22 TYR HB3 H 2.97 0.015 2 138 . 22 TYR HD1 H 6.65 0.015 1 139 . 22 TYR HD2 H 6.65 0.015 1 140 . 22 TYR HE1 H 6.60 0.015 1 141 . 22 TYR HE2 H 6.60 0.015 1 142 . 23 LYS H H 9.07 0.015 1 143 . 23 LYS HA H 4.96 0.015 1 144 . 23 LYS HB2 H 1.67 0.015 2 145 . 23 LYS HB3 H 1.73 0.015 2 146 . 23 LYS HG2 H 1.43 0.015 2 147 . 23 LYS HG3 H 1.42 0.015 2 148 . 23 LYS HD2 H 1.70 0.015 1 149 . 23 LYS HD3 H 1.70 0.015 1 150 . 23 LYS HE2 H 2.93 0.015 1 151 . 23 LYS HE3 H 2.93 0.015 1 152 . 24 MET H H 8.47 0.015 1 153 . 24 MET HA H 5.21 0.015 1 154 . 24 MET HB2 H 1.36 0.015 2 155 . 24 MET HB3 H 1.91 0.015 2 156 . 24 MET HG2 H 1.59 0.015 1 157 . 24 MET HG3 H 1.59 0.015 1 158 . 24 MET HE H 1.94 0.015 1 159 . 25 PHE H H 9.01 0.015 1 160 . 25 PHE HA H 5.01 0.015 1 161 . 25 PHE HB2 H 2.89 0.015 1 162 . 25 PHE HB3 H 2.89 0.015 1 163 . 25 PHE HD1 H 6.92 0.015 1 164 . 25 PHE HD2 H 6.92 0.015 1 165 . 25 PHE HE1 H 7.07 0.015 1 166 . 25 PHE HE2 H 7.07 0.015 1 167 . 25 PHE HZ H 7.24 0.015 1 168 . 26 MET H H 10.13 0.015 1 169 . 26 MET HA H 5.13 0.015 1 170 . 26 MET HB2 H 2.09 0.015 2 171 . 26 MET HB3 H 2.24 0.015 2 172 . 26 MET HG2 H 2.67 0.015 2 173 . 26 MET HG3 H 2.70 0.015 2 174 . 27 VAL H H 8.27 0.015 1 175 . 27 VAL HA H 3.65 0.015 1 176 . 27 VAL HB H 2.09 0.015 1 177 . 27 VAL HG1 H 1.01 0.015 1 178 . 27 VAL HG2 H 1.01 0.015 1 179 . 28 ALA H H 8.10 0.015 1 180 . 28 ALA HA H 4.30 0.015 1 181 . 28 ALA HB H 1.46 0.015 1 182 . 29 ALA H H 7.58 0.015 1 183 . 29 ALA HA H 4.95 0.015 1 184 . 29 ALA HB H 1.36 0.015 1 185 . 30 PRO HA H 4.33 0.015 1 186 . 30 PRO HB2 H 1.50 0.015 2 187 . 30 PRO HB3 H 1.57 0.015 2 188 . 30 PRO HG2 H 1.94 0.015 1 189 . 30 PRO HG3 H 1.94 0.015 1 190 . 30 PRO HD2 H 3.59 0.015 2 191 . 30 PRO HD3 H 3.55 0.015 2 192 . 31 HIS H H 8.64 0.015 1 193 . 31 HIS HA H 4.53 0.015 1 194 . 31 HIS HB2 H 3.15 0.015 2 195 . 31 HIS HB3 H 3.35 0.015 2 196 . 31 HIS HD2 H 7.14 0.015 1 197 . 31 HIS HE1 H 8.14 0.015 1 198 . 32 VAL H H 7.57 0.015 1 199 . 32 VAL HA H 4.66 0.015 1 200 . 32 VAL HB H 2.20 0.015 1 201 . 32 VAL HG1 H 0.90 0.015 2 202 . 32 VAL HG2 H 0.97 0.015 2 203 . 33 PRO HA H 4.39 0.015 1 204 . 33 PRO HB2 H 1.73 0.015 2 205 . 33 PRO HB3 H 1.70 0.015 2 206 . 33 PRO HG2 H 1.73 0.015 2 207 . 33 PRO HG3 H 1.97 0.015 2 208 . 33 PRO HD2 H 3.61 0.015 2 209 . 33 PRO HD3 H 3.98 0.015 2 210 . 34 VAL H H 8.20 0.015 1 211 . 34 VAL HA H 4.40 0.015 1 212 . 34 VAL HB H 2.38 0.015 1 213 . 34 VAL HG1 H 0.89 0.015 2 214 . 34 VAL HG2 H 1.07 0.015 2 215 . 35 LYS H H 7.26 0.015 1 216 . 35 LYS HA H 4.51 0.015 1 217 . 35 LYS HB2 H 1.85 0.015 2 218 . 35 LYS HB3 H 2.01 0.015 2 219 . 35 LYS HG2 H 1.66 0.015 2 220 . 35 LYS HG3 H 1.88 0.015 2 221 . 35 LYS HD2 H 1.76 0.015 2 222 . 35 LYS HD3 H 1.78 0.015 2 223 . 35 LYS HE2 H 3.08 0.015 2 224 . 35 LYS HE3 H 3.13 0.015 2 225 . 36 ARG H H 8.11 0.015 1 226 . 36 ARG HA H 4.40 0.015 1 227 . 36 ARG HB2 H 1.21 0.015 2 228 . 36 ARG HB3 H 1.60 0.015 2 229 . 36 ARG HG2 H 1.36 0.015 2 230 . 36 ARG HG3 H 1.70 0.015 2 231 . 36 ARG HD2 H 2.95 0.015 2 232 . 36 ARG HD3 H 3.30 0.015 2 233 . 36 ARG HE H 7.32 0.015 1 234 . 37 GLY H H 6.54 0.015 1 235 . 37 GLY HA3 H 3.83 0.015 2 236 . 37 GLY HA2 H 4.26 0.015 2 237 . 38 CYS H H 8.70 0.015 1 238 . 38 CYS HA H 5.97 0.015 1 239 . 38 CYS HB2 H 2.94 0.015 2 240 . 38 CYS HB3 H 3.53 0.015 2 241 . 39 ILE H H 9.85 0.015 1 242 . 39 ILE HA H 4.46 0.015 1 243 . 39 ILE HB H 1.80 0.015 1 244 . 39 ILE HG2 H 1.42 0.015 1 245 . 39 ILE HG12 H 0.62 0.015 1 246 . 39 ILE HG13 H 0.62 0.015 1 247 . 39 ILE HD1 H 0.50 0.015 1 248 . 40 ASP H H 8.77 0.015 1 249 . 40 ASP HA H 4.91 0.015 1 250 . 40 ASP HB2 H 2.82 0.015 1 251 . 40 ASP HB3 H 2.82 0.015 1 252 . 41 VAL H H 7.70 0.015 1 253 . 41 VAL HA H 4.07 0.015 1 254 . 41 VAL HB H 1.78 0.015 1 255 . 41 VAL HG1 H 0.78 0.015 1 256 . 41 VAL HG2 H 0.78 0.015 1 257 . 42 CYS H H 8.79 0.015 1 258 . 42 CYS HA H 4.51 0.015 1 259 . 42 CYS HB2 H 2.78 0.015 2 260 . 42 CYS HB3 H 3.10 0.015 2 261 . 43 PRO HA H 4.10 0.015 1 262 . 43 PRO HB2 H 0.42 0.015 2 263 . 43 PRO HB3 H 1.77 0.015 2 264 . 43 PRO HG2 H 0.57 0.015 2 265 . 43 PRO HG3 H 1.25 0.015 2 266 . 43 PRO HD2 H 2.52 0.015 2 267 . 43 PRO HD3 H 3.91 0.015 2 268 . 44 LYS H H 7.89 0.015 1 269 . 44 LYS HA H 4.24 0.015 1 270 . 44 LYS HB2 H 1.75 0.015 2 271 . 44 LYS HB3 H 1.87 0.015 2 272 . 44 LYS HG2 H 1.59 0.015 1 273 . 44 LYS HG3 H 1.59 0.015 1 274 . 44 LYS HD2 H 1.62 0.015 1 275 . 44 LYS HD3 H 1.62 0.015 1 276 . 44 LYS HE2 H 3.06 0.015 1 277 . 44 LYS HE3 H 3.06 0.015 1 278 . 45 SER H H 8.41 0.015 1 279 . 45 SER HA H 4.80 0.015 1 280 . 45 SER HB2 H 4.08 0.015 2 281 . 45 SER HB3 H 4.43 0.015 2 282 . 46 SER H H 9.34 0.015 1 283 . 46 SER HA H 5.00 0.015 1 284 . 46 SER HB2 H 4.48 0.015 2 285 . 46 SER HB3 H 3.99 0.015 2 286 . 47 LEU H H 8.23 0.015 1 287 . 47 LEU HA H 4.24 0.015 1 288 . 47 LEU HB2 H 1.68 0.015 2 289 . 47 LEU HB3 H 1.84 0.015 2 290 . 47 LEU HG H 1.78 0.015 1 291 . 47 LEU HD1 H 0.98 0.015 2 292 . 47 LEU HD2 H 1.02 0.015 2 293 . 48 LEU H H 8.18 0.015 1 294 . 48 LEU HA H 4.54 0.015 1 295 . 48 LEU HB2 H 1.64 0.015 2 296 . 48 LEU HB3 H 1.83 0.015 2 297 . 48 LEU HG H 1.76 0.015 1 298 . 48 LEU HD1 H 0.93 0.015 2 299 . 48 LEU HD2 H 1.02 0.015 2 300 . 49 VAL H H 7.45 0.015 1 301 . 49 VAL HA H 4.98 0.015 1 302 . 49 VAL HB H 1.90 0.015 1 303 . 49 VAL HG1 H 0.80 0.015 2 304 . 49 VAL HG2 H 0.89 0.015 2 305 . 50 LYS H H 8.70 0.015 1 306 . 50 LYS HA H 4.80 0.015 1 307 . 50 LYS HB2 H 1.38 0.015 2 308 . 50 LYS HB3 H 1.49 0.015 2 309 . 50 LYS HG2 H 1.18 0.015 1 310 . 50 LYS HG3 H 1.18 0.015 1 311 . 50 LYS HD2 H 1.67 0.015 2 312 . 50 LYS HD3 H 1.68 0.015 2 313 . 50 LYS HE2 H 2.85 0.015 2 314 . 50 LYS HE3 H 2.94 0.015 2 315 . 51 TYR H H 8.29 0.015 1 316 . 51 TYR HA H 5.30 0.015 1 317 . 51 TYR HB2 H 2.66 0.015 2 318 . 51 TYR HB3 H 2.84 0.015 2 319 . 51 TYR HD1 H 6.75 0.015 1 320 . 51 TYR HD2 H 6.75 0.015 1 321 . 51 TYR HE1 H 6.52 0.015 1 322 . 51 TYR HE2 H 6.52 0.015 1 323 . 52 VAL H H 8.89 0.015 1 324 . 52 VAL HA H 4.55 0.015 1 325 . 52 VAL HB H 2.08 0.015 1 326 . 52 VAL HG1 H 1.09 0.015 2 327 . 52 VAL HG2 H 1.19 0.015 2 328 . 53 CYS H H 9.26 0.015 1 329 . 53 CYS HA H 5.92 0.015 1 330 . 53 CYS HB2 H 3.08 0.015 2 331 . 53 CYS HB3 H 3.81 0.015 2 332 . 54 CYS H H 9.17 0.015 1 333 . 54 CYS HA H 5.13 0.015 1 334 . 54 CYS HB2 H 3.47 0.015 2 335 . 54 CYS HB3 H 3.68 0.015 2 336 . 55 ASN H H 8.55 0.015 1 337 . 55 ASN HA H 5.20 0.015 1 338 . 55 ASN HB2 H 2.69 0.015 2 339 . 55 ASN HB3 H 3.42 0.015 2 340 . 55 ASN HD21 H 7.46 0.015 2 341 . 55 ASN HD22 H 6.72 0.015 2 342 . 56 THR H H 7.59 0.015 1 343 . 56 THR HA H 4.76 0.015 1 344 . 56 THR HB H 4.33 0.015 1 345 . 56 THR HG2 H 1.25 0.015 1 346 . 57 ASP H H 8.17 0.015 1 347 . 57 ASP HA H 4.86 0.015 1 348 . 57 ASP HB2 H 2.38 0.015 2 349 . 57 ASP HB3 H 2.60 0.015 2 350 . 58 LYS H H 9.74 0.015 1 351 . 58 LYS HA H 3.53 0.015 1 352 . 58 LYS HB2 H 1.93 0.015 1 353 . 58 LYS HB3 H 1.93 0.015 1 354 . 58 LYS HG2 H 1.04 0.015 2 355 . 58 LYS HG3 H 1.25 0.015 2 356 . 58 LYS HD2 H 1.69 0.015 1 357 . 58 LYS HD3 H 1.69 0.015 1 358 . 58 LYS HE2 H 2.88 0.015 1 359 . 58 LYS HE3 H 2.88 0.015 1 360 . 59 CYS H H 7.68 0.015 1 361 . 59 CYS HA H 4.51 0.015 1 362 . 59 CYS HB2 H 3.45 0.015 2 363 . 59 CYS HB3 H 3.68 0.015 2 364 . 60 ASN H H 8.99 0.015 1 365 . 60 ASN HA H 4.40 0.015 1 366 . 60 ASN HB2 H 2.22 0.015 2 367 . 60 ASN HB3 H 2.65 0.015 2 368 . 60 ASN HD21 H 7.32 0.015 2 369 . 60 ASN HD22 H 7.51 0.015 2 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 600 _Mol_system_component_name 'CYTOTOXIN 2' _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 LYS H 2 LYS HA 10.0 . . 1.0 2 3JHNHA 3 CYS H 3 CYS HA 10.0 . . 1.0 3 3JHNHA 4 LYS H 4 LYS HA 9.0 . . 1.0 4 3JHNHA 5 LYS H 5 LYS HA 9.0 . . 1.0 5 3JHNHA 6 LEU H 6 LEU HA 4.0 . . 1.0 6 3JHNHA 7 VAL H 7 VAL HA 9.0 . . 1.0 7 3JHNHA 9 LEU H 9 LEU HA 9.0 . . 1.0 8 3JHNHA 10 PHE H 10 PHE HA 10.0 . . 1.0 9 3JHNHA 11 SER H 11 SER HA 10.0 . . 1.0 10 3JHNHA 12 LYS H 12 LYS HA 9.0 . . 1.0 11 3JHNHA 13 THR H 13 THR HA 7.0 . . 1.0 12 3JHNHA 14 CYS H 14 CYS HA 5.0 . . 1.0 13 3JHNHA 16 ALA H 16 ALA HA 4.0 . . 1.0 14 3JHNHA 18 LYS H 18 LYS HA 10.0 . . 1.0 15 3JHNHA 19 ASN H 19 ASN HA 10.0 . . 1.0 16 3JHNHA 20 LEU H 20 LEU HA 10.0 . . 1.0 17 3JHNHA 21 CYS H 21 CYS HA 9.0 . . 1.0 18 3JHNHA 22 TYR H 22 TYR HA 10.0 . . 1.0 19 3JHNHA 23 LYS H 23 LYS HA 10.0 . . 1.0 20 3JHNHA 24 MET H 24 MET HA 10.0 . . 1.0 21 3JHNHA 25 PHE H 25 PHE HA 9.0 . . 1.0 22 3JHNHA 26 MET H 26 MET HA 9.0 . . 1.0 23 3JHNHA 27 VAL H 27 VAL HA 5.0 . . 1.0 24 3JHNHA 28 ALA H 28 ALA HA 5.0 . . 1.0 25 3JHNHA 29 ALA H 29 ALA HA 6.0 . . 1.0 26 3JHNHA 31 HIS H 31 HIS HA 8.0 . . 1.0 27 3JHNHA 32 VAL H 32 VAL HA 8.0 . . 1.0 28 3JHNHA 34 VAL H 34 VAL HA 10.0 . . 1.0 29 3JHNHA 35 LYS H 35 LYS HA 7.0 . . 1.0 30 3JHNHA 36 ARG H 36 ARG HA 8.0 . . 1.0 31 3JHNHA 38 CYS H 38 CYS HA 10.0 . . 1.0 32 3JHNHA 39 ILE H 39 ILE HA 6.0 . . 1.0 33 3JHNHA 40 ASP H 40 ASP HA 9.0 . . 1.0 34 3JHNHA 41 VAL H 41 VAL HA 10.0 . . 1.0 35 3JHNHA 42 CYS H 42 CYS HA 6.0 . . 1.0 36 3JHNHA 44 LYS H 44 LYS HA 6.0 . . 1.0 37 3JHNHA 45 SER H 45 SER HA 6.0 . . 1.0 38 3JHNHA 46 SER H 46 SER HA 10.0 . . 1.0 39 3JHNHA 47 LEU H 47 LEU HA 7.0 . . 1.0 40 3JHNHA 48 LEU H 48 LEU HA 8.0 . . 1.0 41 3JHNHA 49 VAL H 49 VAL HA 10.0 . . 1.0 42 3JHNHA 50 LYS H 50 LYS HA 9.0 . . 1.0 43 3JHNHA 51 TYR H 51 TYR HA 10.0 . . 1.0 44 3JHNHA 52 VAL H 52 VAL HA 10.0 . . 1.0 45 3JHNHA 53 CYS H 53 CYS HA 10.0 . . 1.0 46 3JHNHA 54 CYS H 54 CYS HA 8.0 . . 1.0 47 3JHNHA 55 ASN H 55 ASN HA 10.0 . . 1.0 48 3JHNHA 56 THR H 56 THR HA 10.0 . . 1.0 49 3JHNHA 57 ASP H 57 ASP HA 6.0 . . 1.0 50 3JHNHA 58 LYS H 58 LYS HA 8.0 . . 1.0 51 3JHNHA 59 CYS H 59 CYS HA 7.0 . . 1.0 52 3JHNHA 60 ASN H 60 ASN HA 8.0 . . 1.0 stop_ save_