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_