data_15095
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1
;
_BMRB_accession_number 15095
_BMRB_flat_file_name bmr15095.str
_Entry_type new
_Submission_date 2007-01-04
_Accession_date 2007-01-04
_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 Zhou Chen-Jie . .
2 Hu Hong-Yu . .
3 Lin Dong-Hai . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 65
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2010-05-25 update BMRB 'update entity name'
2010-01-26 update BMRB 'complete entry citation'
2009-09-29 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 19762560
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Xie Yuan-Yuan . .
2 Zhou Chen-Jie . .
3 Zhou Zi-Ren . .
4 Hong Jing . .
5 Che Mei-Xia . .
6 Fu Qing-Shan . .
7 Song Ai-Xin . .
8 Lin Dong-Hai . .
9 Hu Hong-Yu . .
stop_
_Journal_abbreviation 'FASEB J.'
_Journal_name_full 'The FASEB journal : official publication of the Federation of American Societies for Experimental Biology'
_Journal_volume 24
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 196
_Page_last 205
_Year 2010
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'Alpha-Syn12 bound with Synphilin-1'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
Alpha-Syn12 $entity
Synphilin-1 $Synphilin
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic ?
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_entity
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Alpha-Syn12
_Molecular_mass 1357.708
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 12
_Mol_residue_sequence MDVFMKGLSKAK
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ASP 3 VAL 4 PHE 5 MET
6 LYS 7 GLY 8 LEU 9 SER 10 LYS
11 ALA 12 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
#############
# Ligands #
#############
save_Synphilin
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "Synphilin (Synphilin-1)"
_BMRB_code .
_PDB_code Synphilin
_Molecular_mass .
_Mol_charge 0
_Mol_paramagnetic .
_Mol_aromatic .
_Details .
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 . . ? ?
DOUB . . ? ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Details
$entity . . . . . . 'The N-terminal 12 residues of alpha-synuclein'
$Synphilin . . . . . . 'The middle part of Synphilin-1 fused with GB1'
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
_Details
$entity 'chemical synthesis' . . . . . 'The N-terminal 12 residues of alpha-synuclein'
$Synphilin 'recombinant technology' . . . . . 'The middle part of Synphilin-1 fused with GB1'
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
$entity 1 mM 'natural abundance'
'sodium phosphate' 20 mM 'natural abundance'
'sodium chloride' 50 mM 'natural abundance'
$Synphilin 0.1 mM 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_NMRDraw
_Saveframe_category software
_Name NMRDraw
_Version 2.3
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
save_SPARKY
_Saveframe_category software
_Name SPARKY
_Version 3.110
loop_
_Vendor
_Address
_Electronic_address
Goddard . .
stop_
loop_
_Task
'peak picking'
'chemical shift assignment'
stop_
_Details .
save_
save_ARIA
_Saveframe_category software
_Name ARIA
_Version 2.0
loop_
_Vendor
_Address
_Electronic_address
'Linge, O'Donoghue and Nilges' . .
stop_
loop_
_Task
'data analysis'
'structure solution'
refinement
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_nmr_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-1H_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H TOCSY'
_Sample_label $sample_1
save_
save_2D_1H-1H_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
temperature 298 . K
pH 6.5 . pH
pressure 1 . atm
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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 0.00 internal direct . . . 1.000000000
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_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-1H TOCSY'
'2D 1H-1H NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name Alpha-Syn12
_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 1 MET HA H 4.064 0.003 .
2 1 1 MET HB2 H 2.112 0.012 .
3 1 1 MET HG2 H 2.571 0.001 .
4 1 1 MET HG3 H 2.564 0.005 .
5 2 2 ASP H H 7.877 0.000 .
6 2 2 ASP HA H 4.700 0.007 .
7 2 2 ASP HB2 H 2.614 0.000 .
8 2 2 ASP HB3 H 2.553 0.010 .
9 3 3 VAL H H 8.209 0.005 .
10 3 3 VAL HA H 4.023 0.004 .
11 3 3 VAL HB H 2.013 0.004 .
12 3 3 VAL HG1 H 0.832 0.005 .
13 4 4 PHE H H 8.307 0.007 .
14 4 4 PHE HA H 4.611 0.004 .
15 4 4 PHE HB2 H 3.118 0.008 .
16 4 4 PHE HB3 H 3.057 0.007 .
17 4 4 PHE HD2 H 7.267 0.008 .
18 4 4 PHE HE2 H 7.348 0.008 .
19 4 4 PHE HZ H 7.298 0.011 .
20 5 5 MET H H 8.181 0.010 .
21 5 5 MET HA H 4.393 0.006 .
22 5 5 MET HB2 H 2.073 0.026 .
23 5 5 MET HB3 H 1.963 0.011 .
24 5 5 MET HG2 H 2.534 0.007 .
25 5 5 MET HG3 H 2.467 0.007 .
26 6 6 LYS H H 8.233 0.005 .
27 6 6 LYS HA H 4.209 0.005 .
28 6 6 LYS HB2 H 1.835 0.005 .
29 6 6 LYS HG2 H 1.467 0.000 .
30 6 6 LYS HD2 H 1.774 0.010 .
31 6 6 LYS HE2 H 2.996 0.000 .
32 6 6 LYS HE3 H 3.001 0.002 .
33 7 7 GLY H H 8.387 0.005 .
34 7 7 GLY HA2 H 3.938 0.006 .
35 7 7 GLY HA3 H 3.860 0.000 .
36 8 8 LEU H H 8.033 0.003 .
37 8 8 LEU HA H 4.385 0.005 .
38 8 8 LEU HB2 H 1.616 0.004 .
39 8 8 LEU HD1 H 0.915 0.007 .
40 8 8 LEU HD2 H 0.870 0.008 .
41 9 9 SER H H 8.294 0.007 .
42 9 9 SER HA H 4.423 0.010 .
43 9 9 SER HB2 H 3.845 0.003 .
44 10 10 LYS H H 8.306 0.006 .
45 10 10 LYS HA H 4.339 0.006 .
46 10 10 LYS HB2 H 1.850 0.009 .
47 10 10 LYS HG2 H 1.434 0.008 .
48 10 10 LYS HG3 H 1.392 0.002 .
49 10 10 LYS HD2 H 1.712 0.008 .
50 10 10 LYS HD3 H 1.696 0.006 .
51 10 10 LYS HE2 H 3.048 0.026 .
52 10 10 LYS HE3 H 2.992 0.003 .
53 11 11 ALA H H 8.301 0.001 .
54 11 11 ALA HA H 4.292 0.007 .
55 11 11 ALA HB H 1.386 0.002 .
56 12 12 LYS H H 7.885 0.005 .
57 12 12 LYS HA H 4.124 0.004 .
58 12 12 LYS HB2 H 1.805 0.007 .
59 12 12 LYS HB3 H 1.808 0.000 .
60 12 12 LYS HG2 H 1.404 0.009 .
61 12 12 LYS HG3 H 1.391 0.004 .
62 12 12 LYS HD2 H 1.702 0.006 .
63 12 12 LYS HD3 H 1.686 0.006 .
64 12 12 LYS HE2 H 3.001 0.002 .
65 12 12 LYS HE3 H 2.985 0.009 .
stop_
save_