data_4847 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of alpha-conotoxin Im1 point mutation variant D5N ; _BMRB_accession_number 4847 _BMRB_flat_file_name bmr4847.str _Entry_type original _Submission_date 2000-10-04 _Accession_date 2000-10-04 _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 Rogers Jessica P. . 2 Luginbuhl Peter . . 3 Pemberton Karen . . 4 Harty Patrick . . 5 Wemmer David E. . 6 Stevens Raymond C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 4420 'alpha-conotoxin Im1' 4845 'alpha-conotoxin Im1(R11E)' 4846 'alpha-conotoxin Im1(R7L)' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure-activity Relationships in a Peptidic Alpha7 Nicotinic Acetylcholine Receptor Antagonist ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rogers Jessica P. . 2 Luginbuhl Peter . . 3 Pemberton Karen . . 4 Harty Patrick . . 5 Wemmer David E. . 6 Stevens Raymond C. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 304 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 911 _Page_last 926 _Year 2000 _Details . loop_ _Keyword 'alpha-conotoxin Im1' 'peptide toxin' 'neuronal nicotinic acetylcholine receptor' 'competitive antagonist' 'NMR solution structure' stop_ save_ ################################## # Molecular system description # ################################## save_Im1(D5N) _Saveframe_category molecular_system _Mol_system_name 'alpha-conotoxin Im1(D5N)' _Abbreviation_common Im1(D5N) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Im1(D5N) $D5N 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_D5N _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'alpha-conotoxin Im1(D5N)' _Abbreviation_common Im1(D5N) _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details 'amidated C-terminus' ############################## # Polymer residue sequence # ############################## _Residue_count 13 _Mol_residue_sequence GCCSNPRCAWRCX loop_ _Residue_seq_code _Residue_label 1 GLY 2 CYS 3 CYS 4 SER 5 ASN 6 PRO 7 ARG 8 CYS 9 ALA 10 TRP 11 ARG 12 CYS 13 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 4847 'alpha-conotoxin Im1(D5N)' 100.00 12 100 100 2.1 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 Thu Jul 14 16:09:34 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 Im1(D5N) 2 CYS SG Im1(D5N) 8 CYS SG single disulfide Im1(D5N) 3 CYS SG Im1(D5N) 12 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 $D5N . 35631 Eukaryota Metazoa Conus imperialis 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 $D5N 'chemical synthesis' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $D5N . mM 2 3 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 400 _Details . save_ ############################# # NMR applied experiments # ############################# save_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $SAMPLE_1 save_ save_ROESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $SAMPLE_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $SAMPLE_1 save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_CONDITIONS_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.1 0.2 n/a temperature 298 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 H2O H 1 protons ppm 4.75 internal direct spherical internal parallel_to_Bo 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_LIST_FOR_Im1(D5N) _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $SAMPLE_1 stop_ _Sample_conditions_label $CONDITIONS_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Im1(D5N) _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 GLY HA2 H 3.850 . 1 2 . 1 GLY HA3 H 3.893 . 1 3 . 2 CYS H H 8.805 . 1 4 . 2 CYS HA H 4.555 . 1 5 . 2 CYS HB2 H 2.906 . 1 6 . 2 CYS HB3 H 3.292 . 1 7 . 3 CYS H H 8.357 . 1 8 . 3 CYS HA H 4.369 . 1 9 . 3 CYS HB2 H 2.856 . 1 10 . 3 CYS HB3 H 3.471 . 1 11 . 4 SER H H 8.178 . 1 12 . 4 SER HA H 4.372 . 1 13 . 4 SER HB2 H 3.960 . 1 14 . 4 SER HB3 H 4.011 . 1 15 . 5 ASN H H 8.029 . 1 16 . 5 ASN HA H 5.153 . 1 17 . 5 ASN HB2 H 2.858 . 1 18 . 5 ASN HB3 H 3.141 . 1 19 . 5 ASN HD21 H 7.670 . 1 20 . 5 ASN HD22 H 6.888 . 1 21 . 6 PRO HA H 4.360 . 1 22 . 6 PRO HB2 H 1.955 . 1 23 . 6 PRO HB3 H 2.449 . 1 24 . 6 PRO HG2 H 2.070 . 1 25 . 6 PRO HG3 H 2.070 . 1 26 . 6 PRO HD2 H 3.856 . 1 27 . 6 PRO HD3 H 3.970 . 1 28 . 7 ARG H H 8.078 . 1 29 . 7 ARG HA H 4.324 . 1 30 . 7 ARG HB2 H 1.942 . 1 31 . 7 ARG HB3 H 1.749 . 1 32 . 7 ARG HG2 H 1.686 . 1 33 . 7 ARG HG3 H 1.686 . 1 34 . 7 ARG HD2 H 3.219 . 1 35 . 7 ARG HD3 H 3.219 . 1 36 . 7 ARG HE H 7.229 . 1 37 . 7 ARG HH11 H 6.682 . 1 38 . 7 ARG HH12 H 6.682 . 1 39 . 8 CYS H H 7.931 . 1 40 . 8 CYS HA H 4.232 . 1 41 . 8 CYS HB2 H 3.052 . 1 42 . 8 CYS HB3 H 3.345 . 1 43 . 9 ALA H H 8.075 . 1 44 . 9 ALA HA H 4.158 . 1 45 . 9 ALA HB H 1.350 . 1 46 . 10 TRP H H 7.703 . 1 47 . 10 TRP HA H 4.581 . 1 48 . 10 TRP HB3 H 3.377 . 1 49 . 10 TRP HB2 H 3.295 . 1 50 . 10 TRP HD1 H 7.294 . 1 51 . 10 TRP HE3 H 7.527 . 1 52 . 10 TRP HE1 H 10.064 . 1 53 . 10 TRP HZ3 H 7.115 . 1 54 . 10 TRP HZ2 H 7.520 . 1 55 . 10 TRP HH2 H 7.187 . 1 56 . 11 ARG H H 7.865 . 1 57 . 11 ARG HA H 3.981 . 1 58 . 11 ARG HB2 H 1.540 . 1 59 . 11 ARG HB3 H 1.540 . 1 60 . 11 ARG HG2 H 0.922 . 1 61 . 11 ARG HG3 H 0.922 . 1 62 . 11 ARG HD2 H 3.002 . 1 63 . 11 ARG HD3 H 3.002 . 1 64 . 11 ARG HE H 7.029 . 1 65 . 11 ARG HH11 H 6.626 . 1 66 . 11 ARG HH12 H 6.626 . 1 67 . 12 CYS H H 8.135 . 1 68 . 12 CYS HA H 4.586 . 1 69 . 12 CYS HB2 H 3.191 . 1 70 . 12 CYS HB3 H 3.311 . 1 71 . 13 NH2 HN1 H 7.380 . 1 72 . 13 NH2 HN2 H 7.258 . 1 stop_ save_