data_6991
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Phosphorylation of Cytoplasmic Tail of Tissue Factor and its Role in Modulating
;
_BMRB_accession_number 6991
_BMRB_flat_file_name bmr6991.str
_Entry_type original
_Submission_date 2006-02-15
_Accession_date 2006-02-15
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details 'This peptide is the unphosphorylated form of the Tissue Factor Cytoplasmic Domain'
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sen Mehmet . .
2 Agrawal Sameer . .
3 Craft John . .
4 Ruf Wolfram . .
5 Legge Glen B. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 2
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 104
"13C chemical shifts" 39
"15N chemical shifts" 19
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2019-09-13 update BMRB 'update entry citation'
2007-06-20 original author 'original release'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
6993 'Double phosphorylated variant of Tissue Factor Cytoplasmic Domain'
6996 'Single 253 phosphorylated variant of Tissue Factor Cytoplasmic Domain'
6998 'Single 258 phosphorylated variant of Tissue Factor Cytoplasmic Domain'
stop_
_Original_release_date 2006-02-15
save_
#############################
# Citation for this entry #
#############################
save_citation_for_TFCD
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 20076769
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sen Mehmet . .
2 Herzik Mark . .
3 Craft John W. .
4 Creath Andrea L. .
5 Agrawal Sameer . .
6 Ruf Wolfram . .
7 Legge Glen B. .
stop_
_Journal_abbreviation 'Open Spectrosc J.'
_Journal_name_full 'The open spectroscopy journal'
_Journal_volume 3
_Journal_issue .
_Journal_ISSN 1874-3838
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 58
_Page_last 64
_Year 2009
_Details .
loop_
_Keyword
'Homonuclear NMR'
NMR
'Tissue Factor'
phosphorylation
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name TFCD
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'TFCD, trans conformer' $Tissue_Factor_Cytoplasmic_Domain
'TFCD, cis conformer' $Tissue_Factor_Cytoplasmic_Domain
stop_
_System_molecular_weight 2060.3
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
'Cell signaling'
stop_
_Database_query_date .
_Details 'Synthetic Peptide of the unphosphorylated Tissue Factor Cytoplasmic Domain (TFCD)'
save_
########################
# Monomeric polymers #
########################
save_Tissue_Factor_Cytoplasmic_Domain
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common TFCD
_Molecular_mass 2060.3
_Mol_thiol_state 'all free'
loop_
_Biological_function
'Cell Signaling'
stop_
_Details 'Cis conformation of the Pro259 was assigned.'
##############################
# Polymer residue sequence #
##############################
_Residue_count 19
_Mol_residue_sequence
;
CRKAGVGQSWKENSPLNVS
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 245 CYS 2 246 ARG 3 247 LYS 4 248 ALA 5 249 GLY
6 250 VAL 7 251 GLY 8 252 GLN 9 253 SER 10 254 TRP
11 255 LYS 12 256 GLU 13 257 ASN 14 258 SER 15 259 PRO
16 260 LEU 17 261 ASN 18 262 VAL 19 263 SER
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Tissue_Factor_Cytoplasmic_Domain Human 9606 Eukaryota Metazoa Homo sapiens
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
$Tissue_Factor_Cytoplasmic_Domain 'chemical synthesis' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details
;
6mM TFCD in
10% D2O
pH 6.0
;
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Tissue_Factor_Cytoplasmic_Domain 6 mM .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRView
_Saveframe_category software
_Name NMRView
_Version .
loop_
_Task
'NMRView was used for Assignment'
stop_
_Details 'Johnson et al. Methods Mol. Bio. 2004'
save_
save_nmrpipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Task
'NMR data Processing'
stop_
_Details 'Delaglio et al J. Biomol. NMR 1995'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 800
_Details '800 and 600 MHz Bruker Avance spectrometers are used to acquire data'
save_
save_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 600
_Details '800 and 600 MHz Bruker Avance spectrometers are used to acquire data'
save_
#############################
# NMR applied experiments #
#############################
save_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_Sample_label $sample_1
save_
save_IP-COSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name IP-COSY
_Sample_label $sample_1
save_
save_ROESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name ROESY
_Sample_label $sample_1
save_
save_1H1H_NOESY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name 1H1H_NOESY
_Sample_label $sample_1
save_
save_1H15N_HSQC_5
_Saveframe_category NMR_applied_experiment
_Experiment_name 1H15N_HSQC
_Sample_label $sample_1
save_
save_1H13C_HSQC_6
_Saveframe_category NMR_applied_experiment
_Experiment_name 1H13C_HSQC
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_conditions_of_TFCD
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0 0 mM
pH 6.0 0.05 pH
pressure 1 0 atm
temperature 285 0.3 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_TMS
_Saveframe_category chemical_shift_reference
_Details
;
Carbon and Nitrogen dimension was referenced based of gyromagnetic ratio
relativity of these nuclei and proton.
;
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
TMS C 13 'methyl protons' ppm 0 external indirect . 'outside sample' . 0.251449520
TMS H 1 'methyl protons' ppm 0 external direct cylindrical 'outside sample' . 1.0
TMS N 15 'methyl protons' ppm 0 external indirect . 'outside sample' . 0.101329050
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_chem_shift_list_1_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Software_label
$NMRView
$nmrpipe
stop_
loop_
_Experiment_label
ROESY
IP-COSY
TOCSY
1H15N_HSQC
1H13C_HSQC
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_of_TFCD
_Chem_shift_reference_set_label $TMS
_Mol_system_component_name 'TFCD, trans conformer'
_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
1 247 3 LYS H H 8.53 0.02 1
2 247 3 LYS HA H 4.22 0.02 1
3 247 3 LYS HB2 H 1.75 0.02 2
4 247 3 LYS HB3 H 1.68 0.02 2
5 247 3 LYS HG2 H 1.39 0.02 1
6 247 3 LYS HG3 H 1.39 0.02 1
7 247 3 LYS CA C 56.3 0.10 1
8 247 3 LYS CG C 24.8 0.10 1
9 248 4 ALA H H 8.43 0.02 1
10 248 4 ALA HA H 4.23 0.02 1
11 248 4 ALA HB H 1.33 0.02 1
12 248 4 ALA CA C 52.5 0.10 1
13 248 4 ALA CB C 19.4 0.10 1
14 248 4 ALA N N 124.6 0.02 1
15 249 5 GLY H H 8.34 0.02 1
16 249 5 GLY HA2 H 3.91 0.02 2
17 249 5 GLY HA3 H 3.87 0.02 2
18 249 5 GLY CA C 45.1 0.10 1
19 249 5 GLY N N 108.7 0.10 1
20 250 6 VAL H H 8.07 0.02 1
21 250 6 VAL HA H 4.10 0.02 1
22 250 6 VAL HB H 2.06 0.02 1
23 250 6 VAL HG1 H 0.89 0.02 2
24 250 6 VAL HG2 H 0.89 0.02 2
25 250 6 VAL CA C 62.4 0.10 1
26 250 6 VAL CB C 32.6 0.10 1
27 250 6 VAL CG1 C 21.1 0.10 1
28 250 6 VAL N N 119.2 0.10 1
29 251 7 GLY H H 8.65 0.02 1
30 251 7 GLY HA2 H 3.92 0.02 1
31 251 7 GLY HA3 H 3.92 0.02 1
32 251 7 GLY CA C 45.1 0.10 1
33 251 7 GLY N N 113.0 0.10 1
34 252 8 GLN H H 8.24 0.10 1
35 252 8 GLN HA H 4.27 0.02 1
36 252 8 GLN HB2 H 1.91 0.02 2
37 252 8 GLN HB3 H 1.84 0.02 2
38 252 8 GLN HG2 H 2.21 0.02 1
39 252 8 GLN HG3 H 2.21 0.02 1
40 252 8 GLN HE21 H 6.85 0.02 2
41 252 8 GLN HE22 H 7.48 0.02 2
42 252 8 GLN CA C 55.7 0.10 1
43 252 8 GLN CB C 29.6 0.10 1
44 252 8 GLN CG C 33.6 0.10 1
45 252 8 GLN N N 119.7 0.10 1
46 252 8 GLN NE2 N 112.7 0.10 1
47 253 9 SER H H 8.39 0.02 1
48 253 9 SER HA H 4.38 0.02 1
49 253 9 SER HB2 H 3.80 0.02 1
50 253 9 SER HB3 H 3.80 0.02 1
51 253 9 SER CA C 58.3 0.10 1
52 253 9 SER N N 117.0 0.10 1
53 254 10 TRP H H 8.12 0.02 1
54 254 10 TRP HA H 4.60 0.02 1
55 254 10 TRP HB2 H 3.24 0.02 1
56 254 10 TRP HB3 H 3.24 0.02 1
57 254 10 TRP HD1 H 7.20 0.02 1
58 254 10 TRP HE1 H 10.14 0.02 1
59 254 10 TRP HE3 H 7.53 0.02 1
60 254 10 TRP HZ2 H 7.43 0.02 1
61 254 10 TRP HZ3 H 7.09 0.02 1
62 254 10 TRP HH2 H 7.17 0.02 1
63 254 10 TRP CA C 57.4 0.10 1
64 254 10 TRP CB C 29.6 0.10 1
65 254 10 TRP N N 123.1 0.10 1
66 254 10 TRP NE1 N 129.7 0.10 1
67 255 11 LYS H H 7.87 0.02 1
68 255 11 LYS HA H 4.08 0.02 1
69 255 11 LYS HB2 H 1.61 0.02 2
70 255 11 LYS HB3 H 1.5 0.02 2
71 255 11 LYS HG2 H 1.11 0.02 1
72 255 11 LYS HG3 H 1.11 0.02 1
73 255 11 LYS HD2 H 1.51 0.02 1
74 255 11 LYS HD3 H 1.51 0.02 1
75 255 11 LYS HE2 H 2.88 0.02 1
76 255 11 LYS HE3 H 2.88 0.02 1
77 255 11 LYS CA C 56.0 0.10 1
78 255 11 LYS CB C 33.4 0.10 1
79 255 11 LYS CG C 24.5 0.10 1
80 255 11 LYS CE C 42.0 0.10 1
81 255 11 LYS N N 123.2 0.10 1
82 256 12 GLU H H 8.20 0.02 1
83 256 12 GLU HA H 4.06 0.02 1
84 256 12 GLU HB2 H 1.87 0.02 2
85 256 12 GLU HB3 H 1.96 0.02 2
86 256 12 GLU HG2 H 2.21 0.02 1
87 256 12 GLU HG3 H 2.21 0.02 1
88 256 12 GLU CA C 56.5 0.10 1
89 256 12 GLU CB C 30.1 0.10 1
90 256 12 GLU CG C 36.1 0.10 1
91 256 12 GLU N N 121.7 0.10 1
92 257 13 ASN H H 8.46 0.02 1
93 257 13 ASN HA H 4.65 0.02 1
94 257 13 ASN HB2 H 2.78 0.02 2
95 257 13 ASN HB3 H 2.70 0.02 2
96 257 13 ASN HD21 H 6.90 0.02 2
97 257 13 ASN HD22 H 7.60 0.02 2
98 257 13 ASN CA C 53.1 0.10 1
99 257 13 ASN CB C 38.7 0.10 1
100 257 13 ASN N N 119.7 0.10 1
101 257 13 ASN ND2 N 112.9 0.10 1
102 258 14 SER H H 8.21 0.02 1
103 258 14 SER HA H 4.69 0.02 1
104 258 14 SER HB2 H 3.78 0.02 1
105 258 14 SER HB3 H 3.78 0.02 1
106 258 14 SER CA C 56.4 0.10 1
107 258 14 SER CB C 63.4 0.10 1
108 258 14 SER N N 117.4 0.10 1
109 259 15 PRO HA H 4.38 0.02 1
110 259 15 PRO HB2 H 2.25 0.02 2
111 259 15 PRO HB3 H 1.89 0.02 2
112 259 15 PRO HG2 H 1.96 0.02 1
113 259 15 PRO HG3 H 1.96 0.02 1
114 259 15 PRO HD2 H 3.78 0.02 2
115 259 15 PRO HD3 H 3.83 0.02 2
116 259 15 PRO CA C 63.3 0.10 1
117 260 16 LEU H H 8.24 0.02 1
118 260 16 LEU HA H 4.24 0.02 1
119 260 16 LEU HB2 H 1.55 0.02 1
120 260 16 LEU HB3 H 1.55 0.02 1
121 260 16 LEU HG H 1.61 0.02 1
122 260 16 LEU HD2 H 0.82 0.02 2
123 260 16 LEU HD1 H 0.87 0.02 2
124 260 16 LEU CA C 55.3 0.10 1
125 260 16 LEU CB C 42.3 0.10 1
126 260 16 LEU CG C 27.1 0.10 1
127 260 16 LEU CD1 C 23.5 0.10 1
128 260 16 LEU CD2 C 23.5 0.10 1
129 260 16 LEU N N 121.3 0.10 1
130 261 17 ASN H H 8.34 0.02 1
131 261 17 ASN HA H 4.69 0.02 1
132 261 17 ASN HB2 H 2.80 0.02 2
133 261 17 ASN HB3 H 2.70 0.02 2
134 261 17 ASN HD21 H 6.89 0.02 2
135 261 17 ASN HD22 H 7.60 0.02 2
136 261 17 ASN CA C 53.1 0.10 1
137 261 17 ASN CB C 38.7 0.10 1
138 261 17 ASN N N 119.5 0.10 1
139 261 17 ASN ND2 N 113.1 0.10 1
140 262 18 VAL H H 8.13 0.02 1
141 262 18 VAL HA H 4.15 0.02 1
142 262 18 VAL HB H 2.12 0.02 1
143 262 18 VAL HG1 H 0.89 0.02 1
144 262 18 VAL HG2 H 0.89 0.02 1
145 262 18 VAL CA C 62.22 0.10 1
146 262 18 VAL CB C 32.75 0.10 1
147 262 18 VAL CG1 C 20.37 0.10 1
148 262 18 VAL N N 120.3 0.10 1
149 263 19 SER H H 8.36 0.02 1
150 263 19 SER HA H 4.38 0.02 1
151 263 19 SER HB2 H 3.86 0.02 1
152 263 19 SER HB3 H 3.86 0.02 1
153 263 19 SER CA C 58.3 0.10 1
154 263 19 SER CB C 63.7 0.10 1
155 263 19 SER N N 119.7 0.10 1
stop_
save_
save_chem_shift_list_1_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Software_label
$NMRView
$nmrpipe
stop_
loop_
_Experiment_label
ROESY
IP-COSY
TOCSY
1H15N_HSQC
1H13C_HSQC
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_of_TFCD
_Chem_shift_reference_set_label $TMS
_Mol_system_component_name 'TFCD, cis conformer'
_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
1 259 15 PRO HA H 4.72 0.02 1
2 259 15 PRO HB2 H 2.09 0.02 1
3 259 15 PRO HB3 H 2.30 0.02 1
4 259 15 PRO HG2 H 1.91 0.02 1
5 259 15 PRO HG3 H 1.78 0.02 1
6 259 15 PRO HD2 H 3.47 0.02 1
7 259 15 PRO HD3 H 3.47 0.02 1
stop_
save_