data_3435
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Proton NMR Conformational Study of an Annexin I Fragment: Influence of a
Phospholipidic Micellar Environment
;
_BMRB_accession_number 3435
_BMRB_flat_file_name bmr3435.str
_Entry_type update
_Submission_date 1995-07-31
_Accession_date 1996-03-25
_Entry_origination BMRB
_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 Macquaire Francois . .
2 Baleux Francoise . .
3 Huynh-Dinh Tam . .
4 Rouge Dominique . .
5 Neumann Jean-Michel . .
6 Sanson Alain . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 177
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-10 revision BMRB 'Updating non-standard residue'
1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format'
1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format'
1995-07-31 original BMRB 'Last release in original BMRB flat-file format'
2008-03-24 original author .
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full
;
Macquaire, Francois, Baleux, Francoise, Huynh-Dinh, Tam, Rouge, Dominique,
Neumann, Jean-Michel, Sanson, Alain,
"Proton NMR Conformational Study of an Annexin I Fragment: Influence of a
Phospholipidic Micellar Environment,"
Biochem. J. 32 (28), 7244-7254 (1993).
;
_Citation_title
;
Proton NMR Conformational Study of an Annexin I Fragment: Influence of a
Phospholipidic Micellar Environment
;
_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 Macquaire Francois . .
2 Baleux Francoise . .
3 Huynh-Dinh Tam . .
4 Rouge Dominique . .
5 Neumann Jean-Michel . .
6 Sanson Alain . .
stop_
_Journal_abbreviation 'Biochem. J.'
_Journal_volume 32
_Journal_issue 28
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 7244
_Page_last 7254
_Year 1993
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_annexin_I
_Saveframe_category molecular_system
_Mol_system_name 'annexin I'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'annexin I' $annexin_I
stop_
_System_molecular_weight .
_System_oligomer_state ?
_System_paramagnetic ?
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_annexin_I
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'annexin I'
_Name_variant 'residues 1-32'
_Molecular_mass .
_Mol_thiol_state .
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 32
_Mol_residue_sequence
;
XQWDADELRAAMKGLGTDED
TLIEILASRTNK
;
loop_
_Residue_seq_code
_Residue_label
1 AYA 2 GLN 3 TRP 4 ASP 5 ALA
6 ASP 7 GLU 8 LEU 9 ARG 10 ALA
11 ALA 12 MET 13 LYS 14 GLY 15 LEU
16 GLY 17 THR 18 ASP 19 GLU 20 ASP
21 THR 22 LEU 23 ILE 24 GLU 25 ILE
26 LEU 27 ALA 28 SER 29 ARG 30 THR
31 ASN 32 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-29
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 3436 "annexin I" 96.88 32 100.00 100.00 6.44e-12
BMRB 3437 "annexin I" 96.88 32 100.00 100.00 6.44e-12
DBJ BAG59381 "unnamed protein product [Homo sapiens]" 59.38 172 100.00 100.00 1.41e-02
stop_
save_
######################
# Polymer residues #
######################
save_chem_comp_AYA
_Saveframe_category polymer_residue
_Mol_type 'L-PEPTIDE LINKING'
_Name_common N-ACETYLALANINE
_BMRB_code AYA
_PDB_code AYA
_Standard_residue_derivative .
_Molecular_mass 131.130
_Mol_paramagnetic .
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
C C C . 0 . ?
CA CA C . 0 . ?
CB CB C . 0 . ?
CM CM C . 0 . ?
CT CT C . 0 . ?
H H H . 0 . ?
HA HA H . 0 . ?
HB1 HB1 H . 0 . ?
HB2 HB2 H . 0 . ?
HB3 HB3 H . 0 . ?
HM1 HM1 H . 0 . ?
HM2 HM2 H . 0 . ?
HM3 HM3 H . 0 . ?
HXT HXT H . 0 . ?
N N N . 0 . ?
O O O . 0 . ?
OT OT O . 0 . ?
OXT OXT O . 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 CA ? ?
SING N CT ? ?
SING N H ? ?
SING CA CB ? ?
SING CA C ? ?
SING CA HA ? ?
SING CB HB1 ? ?
SING CB HB2 ? ?
SING CB HB3 ? ?
DOUB C O ? ?
SING C OXT ? ?
SING OXT HXT ? ?
DOUB CT OT ? ?
SING CT CM ? ?
SING CM HM1 ? ?
SING CM HM2 ? ?
SING CM HM3 ? ?
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$annexin_I . . . . . .
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
$annexin_I 'not available' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_one
_Saveframe_category sample
_Sample_type solution
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_list
_Saveframe_category NMR_spectrometer
_Manufacturer .
_Model .
_Field_strength .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_condition_set_one
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.4 . na
temperature 293 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_reference_par_set_one
_Saveframe_category chemical_shift_reference
_Details 'The chemical shift reference is not available at this time.'
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
. H 1 . ppm . . . . . .
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_assignment_data_set_one
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_one
stop_
_Sample_conditions_label $sample_condition_set_one
_Chem_shift_reference_set_label $chem_shift_reference_par_set_one
_Mol_system_component_name 'annexin I'
_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 AYA H H 8.3 . 1
2 . 1 AYA HA H 4.22 . 1
3 . 1 AYA HB1 H 1.27 . 1
4 . 1 AYA HB2 H 1.27 . 1
5 . 1 AYA HB3 H 1.27 . 1
6 . 2 GLN H H 8.29 . 1
7 . 2 GLN HA H 4.29 . 1
8 . 2 GLN HB2 H 1.96 . 2
9 . 2 GLN HB3 H 1.86 . 2
10 . 2 GLN HG2 H 2.24 . 2
11 . 2 GLN HG3 H 2.17 . 2
12 . 2 GLN HE21 H 7.53 . 2
13 . 2 GLN HE22 H 6.86 . 2
14 . 3 TRP H H 8.14 . 1
15 . 3 TRP HA H 4.74 . 1
16 . 3 TRP HB2 H 3.32 . 2
17 . 3 TRP HB3 H 3.21 . 2
18 . 3 TRP HD1 H 7.27 . 1
19 . 3 TRP HE1 H 10.18 . 1
20 . 3 TRP HE3 H 7.61 . 1
21 . 3 TRP HZ2 H 7.48 . 1
22 . 3 TRP HZ3 H 7.12 . 1
23 . 3 TRP HH2 H 7.22 . 1
24 . 4 ASP H H 8.39 . 1
25 . 4 ASP HA H 4.61 . 1
26 . 4 ASP HB2 H 2.68 . 2
27 . 4 ASP HB3 H 2.64 . 2
28 . 5 ALA H H 8.35 . 1
29 . 5 ALA HA H 4.1 . 1
30 . 5 ALA HB H 1.46 . 1
31 . 6 ASP H H 8.36 . 1
32 . 6 ASP HA H 4.51 . 1
33 . 6 ASP HB2 H 2.76 . 2
34 . 6 ASP HB3 H 2.73 . 2
35 . 7 GLU H H 8.45 . 1
36 . 7 GLU HA H 4.12 . 1
37 . 7 GLU HB2 H 2.11 . 1
38 . 7 GLU HB3 H 2.11 . 1
39 . 7 GLU HG2 H 2.37 . 2
40 . 7 GLU HG3 H 2.26 . 2
41 . 8 LEU H H 8.18 . 1
42 . 8 LEU HA H 4.16 . 1
43 . 8 LEU HB2 H 1.73 . 2
44 . 8 LEU HB3 H 1.64 . 2
45 . 8 LEU HD1 H .83 . 1
46 . 8 LEU HD2 H .83 . 1
47 . 9 ARG H H 8.08 . 1
48 . 9 ARG HA H 4.08 . 1
49 . 9 ARG HB2 H 1.9 . 1
50 . 9 ARG HB3 H 1.9 . 1
51 . 9 ARG HG2 H 1.74 . 2
52 . 9 ARG HG3 H 1.62 . 2
53 . 9 ARG HD2 H 3.23 . 1
54 . 9 ARG HD3 H 3.23 . 1
55 . 10 ALA H H 8.04 . 1
56 . 10 ALA HA H 4.19 . 1
57 . 10 ALA HB H 1.48 . 1
58 . 11 ALA H H 8 . 1
59 . 11 ALA HA H 4.25 . 1
60 . 11 ALA HB H 1.46 . 1
61 . 12 MET H H 8.06 . 1
62 . 12 MET HA H 4.35 . 1
63 . 12 MET HB2 H 2.16 . 2
64 . 12 MET HB3 H 2.1 . 2
65 . 12 MET HG2 H 2.68 . 2
66 . 12 MET HG3 H 2.55 . 2
67 . 13 LYS H H 8.05 . 1
68 . 13 LYS HA H 4.28 . 1
69 . 13 LYS HB2 H 1.88 . 1
70 . 13 LYS HB3 H 1.88 . 1
71 . 13 LYS HG2 H 1.55 . 2
72 . 13 LYS HG3 H 1.49 . 2
73 . 13 LYS HD2 H 1.71 . 1
74 . 13 LYS HD3 H 1.71 . 1
75 . 13 LYS HE2 H 3.02 . 1
76 . 13 LYS HE3 H 3.02 . 1
77 . 14 GLY H H 8.44 . 1
78 . 14 GLY HA2 H 3.99 . 1
79 . 14 GLY HA3 H 3.99 . 1
80 . 15 LEU H H 8.1 . 1
81 . 15 LEU HA H 4.42 . 1
82 . 15 LEU HB2 H 1.77 . 2
83 . 15 LEU HB3 H 1.68 . 2
84 . 15 LEU HG H 1.65 . 1
85 . 15 LEU HD1 H .94 . 2
86 . 15 LEU HD2 H .9 . 2
87 . 16 GLY H H 8.5 . 1
88 . 16 GLY HA2 H 4.05 . 1
89 . 16 GLY HA3 H 4.05 . 1
90 . 17 THR H H 8.1 . 1
91 . 17 THR HA H 4.45 . 1
92 . 17 THR HB H 4.26 . 1
93 . 17 THR HG2 H 1.21 . 1
94 . 18 ASP H H 8.52 . 1
95 . 18 ASP HA H 4.65 . 1
96 . 18 ASP HB2 H 2.79 . 2
97 . 18 ASP HB3 H 2.75 . 2
98 . 19 GLU H H 8.57 . 1
99 . 19 GLU HA H 4.17 . 1
100 . 19 GLU HB2 H 2.1 . 2
101 . 19 GLU HB3 H 2 . 2
102 . 19 GLU HG2 H 2.3 . 1
103 . 19 GLU HG3 H 2.3 . 1
104 . 20 ASP H H 8.39 . 1
105 . 20 ASP HA H 4.57 . 1
106 . 20 ASP HB2 H 2.74 . 2
107 . 20 ASP HB3 H 2.71 . 2
108 . 21 THR H H 8.09 . 1
109 . 21 THR HA H 4.18 . 1
110 . 21 THR HB H 4.14 . 1
111 . 21 THR HG2 H 1.26 . 1
112 . 22 LEU H H 8.1 . 1
113 . 22 LEU HA H 4.22 . 1
114 . 22 LEU HB2 H 1.67 . 1
115 . 22 LEU HB3 H 1.67 . 1
116 . 22 LEU HD1 H .92 . 2
117 . 22 LEU HD2 H .88 . 2
118 . 23 ILE H H 8.06 . 1
119 . 23 ILE HA H 4.89 . 1
120 . 23 ILE HB H 1.94 . 1
121 . 23 ILE HG12 H 1.91 . 2
122 . 23 ILE HG13 H 1.25 . 2
123 . 23 ILE HG2 H .95 . 1
124 . 23 ILE HD1 H .9 . 1
125 . 24 GLU H H 8.12 . 1
126 . 24 GLU HA H 4.21 . 1
127 . 24 GLU HB2 H 2.08 . 1
128 . 24 GLU HB3 H 2.08 . 1
129 . 24 GLU HG2 H 2.33 . 2
130 . 24 GLU HG3 H 2.25 . 2
131 . 25 ILE H H 8.19 . 1
132 . 25 ILE HA H 3.97 . 1
133 . 25 ILE HB H 1.95 . 1
134 . 25 ILE HG12 H 1.65 . 2
135 . 25 ILE HG13 H 1.2 . 2
136 . 25 ILE HG2 H .9 . 1
137 . 25 ILE HD1 H .86 . 1
138 . 26 LEU H H 8.33 . 1
139 . 26 LEU HA H 4.2 . 1
140 . 26 LEU HB2 H 1.74 . 1
141 . 26 LEU HB3 H 1.74 . 1
142 . 26 LEU HG H 1.54 . 1
143 . 26 LEU HD1 H .84 . 1
144 . 26 LEU HD2 H .84 . 1
145 . 27 ALA H H 8.26 . 1
146 . 27 ALA HA H 4.29 . 1
147 . 27 ALA HB H 1.49 . 1
148 . 28 SER H H 8.05 . 1
149 . 28 SER HA H 4.44 . 1
150 . 28 SER HB2 H 2.99 . 1
151 . 28 SER HB3 H 2.99 . 1
152 . 29 ARG H H 8.08 . 1
153 . 29 ARG HA H 4.46 . 1
154 . 29 ARG HB2 H 1.99 . 2
155 . 29 ARG HB3 H 1.86 . 2
156 . 29 ARG HG2 H 1.75 . 2
157 . 29 ARG HG3 H 1.71 . 2
158 . 29 ARG HD2 H 3.2 . 1
159 . 29 ARG HD3 H 3.2 . 1
160 . 30 THR H H 8.14 . 1
161 . 30 THR HA H 4.27 . 1
162 . 30 THR HB H 4.38 . 1
163 . 30 THR HG2 H 1.26 . 1
164 . 31 ASN H H 8.46 . 1
165 . 31 ASN HA H 4.8 . 1
166 . 31 ASN HB2 H 2.89 . 2
167 . 31 ASN HB3 H 2.81 . 2
168 . 32 LYS H H 7.99 . 1
169 . 32 LYS HA H 4.18 . 1
170 . 32 LYS HB2 H 1.85 . 1
171 . 32 LYS HB3 H 1.85 . 1
172 . 32 LYS HG2 H 1.42 . 1
173 . 32 LYS HG3 H 1.42 . 1
174 . 32 LYS HD2 H 1.71 . 1
175 . 32 LYS HD3 H 1.71 . 1
176 . 32 LYS HE2 H 3.03 . 1
177 . 32 LYS HE3 H 3.03 . 1
stop_
save_