data_6511
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR structure of peptide SD
;
_BMRB_accession_number 6511
_BMRB_flat_file_name bmr6511.str
_Entry_type original
_Submission_date 2005-02-17
_Accession_date 2005-02-18
_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 Murata T. . .
2 Hemmi H. . .
3 Nakamura S. . .
4 Shimizu K. . .
5 Suzuki Y. . .
6 Yamaguchi I. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 52
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-09-22 original BMRB .
stop_
_Original_release_date 2005-02-18
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Structure, epitope mapping and docking simulation of a gibberellin mimic peptide
recognized by an anti-gibberellin A4 antibody 4-B8(8)/E9
;
_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 Murata T. . .
2 Hemmi H. . .
3 Nakamura S. . .
4 Shimizu K. . .
5 Suzuki Y. . .
6 Yamaguchi I. . .
stop_
_Journal_abbreviation 'FEBS J.'
_Journal_volume 272
_Journal_issue 19
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 4938
_Page_last 4948
_Year 2005
_Details .
loop_
_Keyword
STD-NMR
gibberellin
mimic
stop_
save_
##################################
# Molecular system description #
##################################
save_system_SD
_Saveframe_category molecular_system
_Mol_system_name 'peptide SD'
_Abbreviation_common SD
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'peptide SD' $SD_monomer
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_SD_monomer
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'peptide SD'
_Abbreviation_common SD
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 10
_Mol_residue_sequence
;
ACLPWSDGPC
;
loop_
_Residue_seq_code
_Residue_label
1 ALA 2 CYS 3 LEU 4 PRO 5 TRP
6 SER 7 ASP 8 GLY 9 PRO 10 CYS
stop_
_Sequence_homology_query_date 2005-11-24
_Sequence_homology_query_revised_last_date 2005-10-21
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Details
$SD_monomer 'not applicable' . . . . . 'gibberellin mimic peptide'
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
$SD_monomer '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
_Isotopic_labeling
$SD_monomer 5 mM .
'phosphate buffer' 50 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name xwinnmr
_Version 2.6
loop_
_Task
collection
processing
stop_
_Details Bruker
save_
save_Sparky
_Saveframe_category software
_Name SPARKY
_Version 3
loop_
_Task
'data analysis'
stop_
_Details 'Goddard and Kneller'
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
refinement
stop_
_Details Brunger
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 800
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_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_2D_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label .
save_
save_DQF-COSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label .
save_
save_2D_ROESY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 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 5.0 0.05 pH
pressure 1 . atm
temperature 298 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_
_Experiment_label
'2D NOESY'
'2D TOCSY'
DQF-COSY
'2D ROESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'peptide SD'
_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 ALA HA H 4.10 0.01 1
2 . 1 ALA HB H 1.50 0.01 1
3 . 2 CYS H H 8.76 0.01 1
4 . 2 CYS HA H 4.68 0.01 1
5 . 2 CYS HB2 H 2.95 0.01 1
6 . 2 CYS HB3 H 3.12 0.01 1
7 . 3 LEU H H 8.65 0.01 1
8 . 3 LEU HA H 4.52 0.01 1
9 . 3 LEU HB2 H 1.23 0.01 1
10 . 3 LEU HB3 H 0.72 0.01 1
11 . 3 LEU HG H 1.56 0.01 1
12 . 3 LEU HD1 H 0.85 0.01 2
13 . 3 LEU HD2 H 0.92 0.01 2
14 . 4 PRO HA H 4.24 0.01 1
15 . 4 PRO HB2 H 1.80 0.01 2
16 . 4 PRO HB3 H 2.20 0.01 2
17 . 4 PRO HG2 H 1.95 0.01 1
18 . 4 PRO HG3 H 2.00 0.01 1
19 . 4 PRO HD2 H 3.21 0.01 2
20 . 4 PRO HD3 H 3.69 0.01 2
21 . 5 TRP H H 7.04 0.01 1
22 . 5 TRP HA H 4.74 0.01 1
23 . 5 TRP HB2 H 3.33 0.01 2
24 . 5 TRP HB3 H 3.49 0.01 2
25 . 5 TRP HD1 H 7.22 0.01 1
26 . 5 TRP HE1 H 10.31 0.01 1
27 . 5 TRP HE3 H 7.67 0.01 1
28 . 5 TRP HZ2 H 7.55 0.01 1
29 . 5 TRP HZ3 H 7.23 0.01 1
30 . 5 TRP HH2 H 7.30 0.01 1
31 . 6 SER H H 7.62 0.01 1
32 . 6 SER HA H 4.42 0.01 1
33 . 6 SER HB2 H 3.77 0.01 1
34 . 6 SER HB3 H 3.77 0.01 1
35 . 7 ASP H H 8.48 0.01 1
36 . 7 ASP HA H 4.77 0.01 1
37 . 7 ASP HB2 H 2.74 0.01 2
38 . 7 ASP HB3 H 2.81 0.01 2
39 . 8 GLY H H 7.92 0.01 1
40 . 8 GLY HA2 H 4.05 0.01 2
41 . 8 GLY HA3 H 4.12 0.01 2
42 . 9 PRO HA H 4.43 0.01 1
43 . 9 PRO HB2 H 2.25 0.01 2
44 . 9 PRO HB3 H 1.93 0.01 2
45 . 9 PRO HG2 H 2.01 0.01 1
46 . 9 PRO HG3 H 2.01 0.01 1
47 . 9 PRO HD2 H 3.60 0.01 1
48 . 9 PRO HD3 H 3.60 0.01 1
49 . 10 CYS H H 8.16 0.01 1
50 . 10 CYS HA H 4.44 0.01 1
51 . 10 CYS HB2 H 3.06 0.01 1
52 . 10 CYS HB3 H 3.19 0.01 1
stop_
save_