data_4784
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H and 15N chemical shift assignments and interproton 3JHNHA coupling constants
of the DNA-binding domain of the tyrosine repressor from Haemophilus influenzae,
a transcription factor that belongs to the prokaryotic NtrC superfamily
;
_BMRB_accession_number 4784
_BMRB_flat_file_name bmr4784.str
_Entry_type original
_Submission_date 2000-07-13
_Accession_date 2000-07-13
_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 Wang Yunjun Y. .
2 Zhao Shimin S. .
3 Somerville Ronald L. .
4 Jardetzky Oleg O. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
coupling_constants 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 329
"15N chemical shifts" 63
"coupling constants" 34
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-07-17 original author .
stop_
_Original_release_date 2001-07-17
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Solution Structure of the DNA-binding Domain of the TyrR Protein of Haemophilus
influenzae
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21243163
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Wang Yunjun Y. .
2 Zhao Shimin S. .
3 Somerville Ronald L. .
4 Jardetzky Oleg O. .
stop_
_Journal_abbreviation 'Protein Sci.'
_Journal_name_full 'Protein Science'
_Journal_volume 10
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 592
_Page_last 598
_Year 2001
_Details .
loop_
_Keyword
'Tyr repressor'
NMR
'DNA-binding domain'
'Haemophilus influenzae'
Helix-turn-helix
stop_
save_
##################################
# Molecular system description #
##################################
save_system_TyrR
_Saveframe_category molecular_system
_Mol_system_name 'Tyrosine repressor'
_Abbreviation_common TyrR
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Tyr repressor DNA binding domain' $TyrR(258-318)
stop_
_System_molecular_weight 6878
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_TyrR(258-318)
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common repressor
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 61
_Mol_residue_sequence
;
SAVISLDEFENKTLDEIIGF
YEAQVLKLFYAEYPSTRKLA
QRLGVSHTAIANKLKQYGIG
K
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 ALA 3 VAL 4 ILE 5 SER
6 LEU 7 ASP 8 GLU 9 PHE 10 GLU
11 ASN 12 LYS 13 THR 14 LEU 15 ASP
16 GLU 17 ILE 18 ILE 19 GLY 20 PHE
21 TYR 22 GLU 23 ALA 24 GLN 25 VAL
26 LEU 27 LYS 28 LEU 29 PHE 30 TYR
31 ALA 32 GLU 33 TYR 34 PRO 35 SER
36 THR 37 ARG 38 LYS 39 LEU 40 ALA
41 GLN 42 ARG 43 LEU 44 GLY 45 VAL
46 SER 47 HIS 48 THR 49 ALA 50 ILE
51 ALA 52 ASN 53 LYS 54 LEU 55 LYS
56 GLN 57 TYR 58 GLY 59 ILE 60 GLY
61 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
PDB 1G2H "Solution Structure Of The Dna-Binding Domain Of The Tyrr Protein Of Haemophilus Influenzae" 100.00 61 100.00 100.00 3.55e-35
EMBL CBW28709 "transcriptional regulatory protein TyrR [Haemophilus influenzae 10810]" 100.00 318 100.00 100.00 9.91e-33
EMBL CBY81959 "Transcriptional regulatory protein TyrR [Haemophilus influenzae F3031]" 100.00 318 100.00 100.00 1.07e-32
EMBL CBY86469 "Transcriptional regulatory protein TyrR [Haemophilus influenzae F3047]" 100.00 318 98.36 98.36 4.05e-32
GB AAC22069 "transcriptional regulatory protein (tyrR) [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33
GB ADO80156 "Tyrosine repressor protein TyrR [Haemophilus influenzae R2866]" 100.00 318 100.00 100.00 1.11e-32
GB ADO95632 "Tyrosine repressor protein TyrR [Haemophilus influenzae R2846]" 100.00 318 100.00 100.00 1.06e-32
GB AIB45125 "Transcriptional repressor protein TyrR [Haemophilus influenzae CGSHiCZ412602]" 100.00 318 100.00 100.00 1.17e-32
GB EDJ91589 "transcriptional regulatory protein [Haemophilus influenzae R3021]" 100.00 318 100.00 100.00 1.08e-32
REF NP_438572 "transcriptional regulatory protein [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33
REF WP_005630049 "transcriptional regulator [Haemophilus haemolyticus]" 100.00 318 98.36 98.36 2.12e-31
REF WP_005634169 "transcriptional regulator [Haemophilus haemolyticus]" 100.00 318 98.36 98.36 1.83e-31
REF WP_005652170 "transcriptional regulator [Haemophilus influenzae]" 100.00 318 100.00 100.00 1.08e-32
REF WP_005656417 "transcriptional regulator [Haemophilus influenzae]" 100.00 318 100.00 100.00 1.02e-32
SP P44694 "RecName: Full=Transcriptional regulatory protein TyrR [Haemophilus influenzae Rd KW20]" 100.00 318 100.00 100.00 9.91e-33
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$TyrR(258-318) 'Haemophilus influenzae' 727 Eubacteria . Haemophilus influenzae
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Cell_line
_Vector_type
_Vector_name
$TyrR(258-318) 'recombinant technology' 'E. Coli' Escherichia coli . BL21 plasmid pZZ257
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
$TyrR(258-318) 2.0 mM [U-15N]
stop_
save_
#############################
# Purity of the molecules #
#############################
save_mol_purity_list
_Saveframe_category sample_mol_purity
_Sample_label $sample_1
loop_
_Mol_label
_Mol_purity_value
_Mol_purity_value_units
_Mol_purity_measurement_method
$TyrR(258-318) 95 % 'SDS gel and mass spectrometry'
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model 'Unity plus'
_Field_strength 800
_Details .
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 0.1 n/a
temperature 298 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_one
_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
DSS H 1 'methyl protons' ppm 0 internal direct . . .
. N 15 . 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_assigned_chemical_shifts
_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_one
_Mol_system_component_name 'Tyr repressor DNA binding domain'
_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 . 2 ALA H H 8.77 0.02 1
2 . 2 ALA HA H 4.49 0.02 1
3 . 2 ALA HB H 1.47 0.02 1
4 . 2 ALA N N 124.75 0.02 1
5 . 3 VAL H H 8.32 0.02 1
6 . 3 VAL HA H 4.12 0.02 1
7 . 3 VAL HB H 2.01 0.02 1
8 . 3 VAL HG1 H 0.90 0.02 2
9 . 3 VAL HG2 H 0.95 0.02 2
10 . 3 VAL N N 121.44 0.02 1
11 . 4 ILE H H 8.19 0.02 1
12 . 4 ILE HA H 4.38 0.02 1
13 . 4 ILE HB H 1.80 0.02 1
14 . 4 ILE HG12 H 1.48 0.02 2
15 . 4 ILE HG13 H 1.14 0.02 2
16 . 4 ILE HG2 H 0.75 0.02 1
17 . 4 ILE HD1 H 0.89 0.02 1
18 . 4 ILE N N 120.51 0.02 1
19 . 5 SER H H 7.91 0.02 1
20 . 5 SER HA H 4.60 0.02 1
21 . 5 SER HB2 H 3.66 0.02 2
22 . 5 SER HB3 H 3.82 0.02 2
23 . 5 SER N N 113.81 0.02 1
24 . 6 LEU H H 8.80 0.02 1
25 . 6 LEU HA H 3.93 0.02 1
26 . 6 LEU HB2 H 1.61 0.02 2
27 . 6 LEU HG H 1.44 0.02 1
28 . 6 LEU HD1 H 0.55 0.02 2
29 . 6 LEU HD2 H 0.22 0.02 2
30 . 6 LEU N N 122.82 0.02 1
31 . 7 ASP H H 8.26 0.02 1
32 . 7 ASP HA H 4.27 0.02 1
33 . 7 ASP HB2 H 2.62 0.02 1
34 . 7 ASP HB3 H 2.53 0.02 1
35 . 7 ASP N N 119.35 0.02 1
36 . 8 GLU H H 7.42 0.02 1
37 . 8 GLU HA H 4.02 0.02 1
38 . 8 GLU HB2 H 1.81 0.02 2
39 . 8 GLU HB3 H 1.72 0.02 2
40 . 8 GLU HG2 H 1.94 0.02 2
41 . 8 GLU HG3 H 2.20 0.02 2
42 . 8 GLU N N 117.81 0.02 1
43 . 9 PHE H H 7.40 0.02 1
44 . 9 PHE HA H 4.90 0.02 1
45 . 9 PHE HB2 H 3.81 0.02 1
46 . 9 PHE HB3 H 3.00 0.02 1
47 . 9 PHE HD1 H 7.17 0.02 1
48 . 9 PHE HD2 H 7.17 0.02 1
49 . 9 PHE HE1 H 7.27 0.02 1
50 . 9 PHE HE2 H 7.27 0.02 1
51 . 9 PHE HZ H 7.25 0.02 1
52 . 9 PHE N N 116.27 0.02 1
53 . 10 GLU H H 7.34 0.02 1
54 . 10 GLU HA H 4.08 0.02 1
55 . 10 GLU HB2 H 1.99 0.02 2
56 . 10 GLU HG2 H 2.10 0.02 2
57 . 10 GLU HG3 H 2.34 0.02 2
58 . 10 GLU N N 122.82 0.02 1
59 . 11 ASN H H 9.14 0.02 1
60 . 11 ASN HA H 4.44 0.02 1
61 . 11 ASN HB2 H 3.05 0.02 1
62 . 11 ASN HB3 H 3.14 0.02 1
63 . 11 ASN HD21 H 7.69 0.02 2
64 . 11 ASN HD22 H 7.02 0.02 2
65 . 11 ASN N N 117.81 0.02 1
66 . 11 ASN ND2 N 114.73 0.02 1
67 . 12 LYS H H 7.87 0.02 1
68 . 12 LYS HA H 4.97 0.02 1
69 . 12 LYS HB2 H 1.94 0.02 1
70 . 12 LYS HB3 H 1.88 0.02 1
71 . 12 LYS HG2 H 1.65 0.02 2
72 . 12 LYS HG3 H 1.53 0.02 2
73 . 12 LYS HD2 H 1.40 0.02 2
74 . 12 LYS HD3 H 1.31 0.02 2
75 . 12 LYS N N 117.42 0.02 1
76 . 13 THR H H 8.64 0.02 1
77 . 13 THR HA H 4.80 0.02 1
78 . 13 THR HB H 4.21 0.02 1
79 . 13 THR HG2 H 1.30 0.02 1
80 . 13 THR N N 111.64 0.02 1
81 . 14 LEU H H 8.87 0.02 1
82 . 14 LEU HA H 3.98 0.02 1
83 . 14 LEU HB2 H 1.88 0.02 2
84 . 14 LEU HD1 H 0.90 0.02 2
85 . 14 LEU HD2 H 0.97 0.02 2
86 . 14 LEU N N 120.12 0.02 1
87 . 15 ASP H H 8.53 0.02 1
88 . 15 ASP HA H 4.38 0.02 1
89 . 15 ASP HB2 H 2.55 0.02 1
90 . 15 ASP HB3 H 2.64 0.02 1
91 . 15 ASP N N 115.88 0.02 1
92 . 16 GLU H H 7.58 0.02 1
93 . 16 GLU HA H 4.13 0.02 1
94 . 16 GLU HB2 H 2.43 0.02 1
95 . 16 GLU HB3 H 2.29 0.02 1
96 . 16 GLU HG2 H 2.03 0.02 2
97 . 16 GLU HG3 H 2.18 0.02 2
98 . 16 GLU N N 120.51 0.02 1
99 . 17 ILE H H 8.44 0.02 1
100 . 17 ILE HA H 3.73 0.02 1
101 . 17 ILE HB H 1.96 0.02 1
102 . 17 ILE HG2 H 0.74 0.02 1
103 . 17 ILE HD1 H 0.46 0.02 1
104 . 17 ILE N N 122.44 0.02 1
105 . 18 ILE H H 8.85 0.02 1
106 . 18 ILE HA H 4.02 0.02 1
107 . 18 ILE HB H 2.22 0.02 1
108 . 18 ILE HG12 H 1.55 0.02 2
109 . 18 ILE HG13 H 1.77 0.02 2
110 . 18 ILE HG2 H 1.04 0.02 1
111 . 18 ILE HD1 H 0.82 0.02 1
112 . 18 ILE N N 119.74 0.02 1
113 . 19 GLY H H 8.36 0.02 1
114 . 19 GLY HA2 H 4.03 0.02 2
115 . 19 GLY HA3 H 4.20 0.02 2
116 . 19 GLY N N 108.91 0.02 1
117 . 20 PHE H H 8.16 0.02 1
118 . 20 PHE HA H 4.33 0.02 1
119 . 20 PHE HB2 H 3.42 0.02 1
120 . 20 PHE HB3 H 3.29 0.02 1
121 . 20 PHE HD1 H 7.45 0.02 1
122 . 20 PHE HD2 H 7.45 0.02 1
123 . 20 PHE HE1 H 7.42 0.02 1
124 . 20 PHE HE2 H 7.42 0.02 1
125 . 20 PHE N N 120.89 0.02 1
126 . 21 TYR H H 7.51 0.02 1
127 . 21 TYR HA H 4.05 0.02 1
128 . 21 TYR HB2 H 2.72 0.02 1
129 . 21 TYR HB3 H 2.90 0.02 1
130 . 21 TYR HD1 H 6.50 0.02 1
131 . 21 TYR HD2 H 6.50 0.02 1
132 . 21 TYR HE1 H 6.42 0.02 1
133 . 21 TYR HE2 H 6.42 0.02 1
134 . 21 TYR N N 120.12 0.02 1
135 . 22 GLU H H 9.26 0.02 1
136 . 22 GLU HA H 3.38 0.02 1
137 . 22 GLU HB2 H 2.22 0.02 1
138 . 22 GLU HB3 H 2.29 0.02 1
139 . 22 GLU HG2 H 1.99 0.02 2
140 . 22 GLU HG3 H 2.06 0.02 2
141 . 22 GLU N N 119.74 0.02 1
142 . 23 ALA H H 7.84 0.02 1
143 . 23 ALA HA H 3.18 0.02 1
144 . 23 ALA HB H 0.85 0.02 1
145 . 23 ALA N N 118.96 0.02 1
146 . 24 GLN H H 7.19 0.02 1
147 . 24 GLN HA H 3.77 0.02 1
148 . 24 GLN HB2 H 1.89 0.02 2
149 . 24 GLN HB3 H 2.00 0.02 2
150 . 24 GLN HG2 H 2.06 0.02 2
151 . 24 GLN HG3 H 2.18 0.02 2
152 . 24 GLN HE21 H 6.64 0.02 2
153 . 24 GLN HE22 H 6.91 0.02 2
154 . 24 GLN N N 116.27 0.02 1
155 . 24 GLN NE2 N 112.09 0.02 1
156 . 25 VAL H H 8.16 0.02 1
157 . 25 VAL HA H 3.30 0.02 1
158 . 25 VAL HB H 1.82 0.02 1
159 . 25 VAL HG1 H 0.62 0.02 1
160 . 25 VAL HG2 H 0.25 0.02 1
161 . 25 VAL N N 120.51 0.02 1
162 . 26 LEU H H 8.72 0.02 1
163 . 26 LEU HA H 4.08 0.02 1
164 . 26 LEU HB2 H 1.15 0.02 2
165 . 26 LEU HG H 1.83 0.02 1
166 . 26 LEU HD1 H 0.84 0.02 2
167 . 26 LEU HD2 H 0.72 0.02 2
168 . 26 LEU N N 118.22 0.02 1
169 . 27 LYS H H 8.17 0.02 1
170 . 27 LYS HA H 3.89 0.02 1
171 . 27 LYS HB2 H 1.88 0.02 2
172 . 27 LYS N N 120.12 0.02 1
173 . 28 LEU H H 7.51 0.02 1
174 . 28 LEU HA H 4.13 0.02 1
175 . 28 LEU HB2 H 1.70 0.02 2
176 . 28 LEU HB3 H 1.75 0.02 2
177 . 28 LEU HG H 1.50 0.02 1
178 . 28 LEU HD1 H 0.74 0.02 2
179 . 28 LEU HD2 H 0.82 0.02 2
180 . 28 LEU N N 120.12 0.02 1
181 . 29 PHE H H 8.50 0.02 1
182 . 29 PHE HA H 4.22 0.02 1
183 . 29 PHE HB2 H 2.96 0.02 1
184 . 29 PHE HB3 H 3.14 0.02 1
185 . 29 PHE HD1 H 7.35 0.02 1
186 . 29 PHE HD2 H 7.35 0.02 1
187 . 29 PHE HE1 H 7.08 0.02 1
188 . 29 PHE HE2 H 7.08 0.02 1
189 . 29 PHE N N 116.65 0.02 1
190 . 30 TYR H H 9.23 0.02 1
191 . 30 TYR HA H 4.31 0.02 1
192 . 30 TYR HB2 H 3.08 0.02 1
193 . 30 TYR HB3 H 2.93 0.02 1
194 . 30 TYR HD1 H 7.02 0.02 1
195 . 30 TYR HD2 H 7.02 0.02 1
196 . 30 TYR HE1 H 6.69 0.02 1
197 . 30 TYR HE2 H 6.69 0.02 1
198 . 30 TYR N N 121.28 0.02 1
199 . 31 ALA H H 7.12 0.02 1
200 . 31 ALA HA H 3.99 0.02 1
201 . 31 ALA HB H 1.52 0.02 1
202 . 31 ALA N N 116.27 0.02 1
203 . 32 GLU H H 6.99 0.02 1
204 . 32 GLU HA H 4.13 0.02 1
205 . 32 GLU HB2 H 1.78 0.02 2
206 . 32 GLU HG2 H 2.00 0.02 2
207 . 32 GLU N N 115.48 0.02 1
208 . 33 TYR H H 8.19 0.02 1
209 . 33 TYR HA H 4.80 0.02 1
210 . 33 TYR HB2 H 3.15 0.02 1
211 . 33 TYR HB3 H 2.62 0.02 1
212 . 33 TYR HD1 H 7.35 0.02 1
213 . 33 TYR HD2 H 7.35 0.02 1
214 . 33 TYR HE1 H 6.93 0.02 1
215 . 33 TYR HE2 H 6.93 0.02 1
216 . 33 TYR N N 118.19 0.02 1
217 . 34 PRO HA H 4.02 0.02 1
218 . 34 PRO HB2 H 1.98 0.02 2
219 . 34 PRO HB3 H 1.94 0.02 2
220 . 34 PRO HG2 H 1.73 0.02 2
221 . 34 PRO HG3 H 1.81 0.02 2
222 . 34 PRO HD2 H 3.12 0.02 2
223 . 34 PRO HD3 H 3.45 0.02 2
224 . 35 SER H H 8.20 0.02 1
225 . 35 SER HA H 4.92 0.02 1
226 . 35 SER HB2 H 3.80 0.02 2
227 . 35 SER HB3 H 4.17 0.02 2
228 . 35 SER N N 115.49 0.02 1
229 . 36 THR HA H 3.95 0.02 1
230 . 36 THR HB H 4.24 0.02 1
231 . 36 THR HG2 H 1.30 0.02 1
232 . 36 THR N N 125.13 0.02 1
233 . 37 ARG H H 8.41 0.02 1
234 . 37 ARG HA H 3.92 0.02 1
235 . 37 ARG HB2 H 1.72 0.02 2
236 . 37 ARG HB3 H 1.56 0.02 2
237 . 37 ARG HG2 H 1.33 0.02 2
238 . 37 ARG HD2 H 3.07 0.02 1
239 . 37 ARG HD3 H 3.07 0.02 1
240 . 37 ARG N N 123.59 0.02 1
241 . 38 LYS H H 7.69 0.02 1
242 . 38 LYS HA H 4.14 0.02 1
243 . 38 LYS HB2 H 1.97 0.02 2
244 . 38 LYS HB3 H 1.73 0.02 2
245 . 38 LYS HG2 H 1.55 0.02 2
246 . 38 LYS N N 119.74 0.02 1
247 . 39 LEU H H 8.60 0.02 1
248 . 39 LEU HA H 3.75 0.02 1
249 . 39 LEU HB2 H 2.24 0.02 2
250 . 39 LEU HG H 1.76 0.02 1
251 . 39 LEU HD1 H 1.01 0.02 2
252 . 39 LEU HD2 H 1.05 0.02 2
253 . 39 LEU N N 121.66 0.02 1
254 . 40 ALA H H 8.32 0.02 1
255 . 40 ALA HA H 3.76 0.02 1
256 . 40 ALA HB H 1.58 0.02 1
257 . 40 ALA N N 120.89 0.02 1
258 . 41 GLN H H 7.39 0.02 1
259 . 41 GLN HA H 4.06 0.02 1
260 . 41 GLN HB2 H 2.13 0.02 1
261 . 41 GLN HB3 H 2.19 0.02 1
262 . 41 GLN HG2 H 2.38 0.02 2
263 . 41 GLN HG3 H 2.54 0.02 2
264 . 41 GLN HE21 H 7.53 0.02 1
265 . 41 GLN HE22 H 6.89 0.02 1
266 . 41 GLN N N 115.49 0.02 1
267 . 41 GLN NE2 N 111.87 0.02 1
268 . 42 ARG H H 7.89 0.02 1
269 . 42 ARG HA H 4.20 0.02 1
270 . 42 ARG HB2 H 1.58 0.02 2
271 . 42 ARG N N 119.35 0.02 1
272 . 43 LEU H H 8.10 0.02 1
273 . 43 LEU HA H 4.26 0.02 1
274 . 43 LEU HB2 H 1.49 0.02 2
275 . 43 LEU HB3 H 1.64 0.02 2
276 . 43 LEU HG H 1.07 0.02 1
277 . 43 LEU HD1 H -0.20 0.02 2
278 . 43 LEU HD2 H 0.38 0.02 2
279 . 43 LEU N N 113.27 0.02 1
280 . 44 GLY H H 7.87 0.02 1
281 . 44 GLY HA2 H 3.87 0.02 2
282 . 44 GLY HA3 H 4.06 0.02 2
283 . 44 GLY N N 110.48 0.02 1
284 . 45 VAL H H 7.73 0.02 1
285 . 45 VAL HA H 4.68 0.02 1
286 . 45 VAL HB H 2.05 0.02 1
287 . 45 VAL HG1 H 0.78 0.02 1
288 . 45 VAL HG2 H 0.97 0.02 1
289 . 45 VAL N N 113.59 0.02 1
290 . 46 SER H H 8.48 0.02 1
291 . 46 SER HA H 4.46 0.02 1
292 . 46 SER HB2 H 4.00 0.02 2
293 . 46 SER HB3 H 4.32 0.02 2
294 . 46 SER N N 116.65 0.02 1
295 . 47 HIS H H 9.10 0.02 1
296 . 47 HIS HA H 4.09 0.02 1
297 . 47 HIS HB2 H 3.17 0.02 1
298 . 47 HIS HB3 H 3.19 0.02 1
299 . 47 HIS HD2 H 6.81 0.02 1
300 . 47 HIS HE1 H 7.73 0.02 1
301 . 47 HIS N N 121.78 0.02 1
302 . 48 THR H H 7.98 0.02 1
303 . 48 THR HA H 3.98 0.02 1
304 . 48 THR HB H 3.79 0.02 1
305 . 48 THR HG2 H 1.14 0.02 1
306 . 48 THR N N 130.24 0.02 1
307 . 49 ALA H H 7.71 0.02 1
308 . 49 ALA HA H 4.15 0.02 1
309 . 49 ALA HB H 1.44 0.02 1
310 . 49 ALA N N 124.75 0.02 1
311 . 50 ILE H H 8.02 0.02 1
312 . 50 ILE HA H 3.95 0.02 1
313 . 50 ILE HB H 1.96 0.02 1
314 . 50 ILE HG12 H 1.58 0.02 2
315 . 50 ILE HG2 H 1.08 0.02 1
316 . 50 ILE HD1 H 0.78 0.02 1
317 . 50 ILE N N 117.04 0.02 1
318 . 51 ALA H H 8.31 0.02 1
319 . 51 ALA HA H 3.96 0.02 1
320 . 51 ALA HB H 1.41 0.02 1
321 . 51 ALA N N 124.36 0.02 1
322 . 52 ASN H H 8.04 0.02 1
323 . 52 ASN HA H 4.42 0.02 1
324 . 52 ASN HB2 H 2.78 0.02 1
325 . 52 ASN HB3 H 2.89 0.02 1
326 . 52 ASN HD21 H 7.55 0.02 2
327 . 52 ASN HD22 H 6.90 0.02 2
328 . 52 ASN N N 116.65 0.02 1
329 . 53 LYS H H 7.94 0.02 1
330 . 53 LYS HA H 3.89 0.02 1
331 . 53 LYS HB2 H 1.91 0.02 2
332 . 53 LYS HB3 H 1.62 0.02 2
333 . 53 LYS HG2 H 1.52 0.02 2
334 . 53 LYS HG3 H 1.42 0.02 2
335 . 53 LYS N N 122.05 0.02 1
336 . 54 LEU H H 8.55 0.02 1
337 . 54 LEU HA H 3.86 0.02 1
338 . 54 LEU HG H 1.94 0.02 1
339 . 54 LEU HD1 H 0.70 0.02 2
340 . 54 LEU HD2 H 0.54 0.02 2
341 . 54 LEU N N 117.42 0.02 1
342 . 55 LYS H H 7.44 0.02 1
343 . 55 LYS HA H 4.10 0.02 1
344 . 55 LYS HB2 H 1.89 0.02 2
345 . 55 LYS HB3 H 1.68 0.02 2
346 . 55 LYS HG2 H 1.52 0.02 2
347 . 55 LYS HG3 H 1.41 0.02 2
348 . 55 LYS N N 117.42 0.02 1
349 . 56 GLN H H 8.12 0.02 1
350 . 56 GLN HA H 3.86 0.02 1
351 . 56 GLN HB2 H 1.89 0.02 2
352 . 56 GLN HB3 H 1.68 0.02 2
353 . 56 GLN HG2 H 1.93 0.02 1
354 . 56 GLN HG3 H 1.76 0.02 1
355 . 56 GLN HE21 H 6.95 0.02 2
356 . 56 GLN HE22 H 6.70 0.02 2
357 . 56 GLN NE2 N 110.40 0.02 1
358 . 56 GLN N N 121.28 0.02 1
359 . 57 TYR H H 7.56 0.02 1
360 . 57 TYR HA H 4.89 0.02 1
361 . 57 TYR HB2 H 2.57 0.02 1
362 . 57 TYR HB3 H 3.38 0.02 1
363 . 57 TYR HD1 H 7.00 0.02 1
364 . 57 TYR HD2 H 7.00 0.02 1
365 . 57 TYR HE1 H 6.59 0.02 1
366 . 57 TYR HE2 H 6.59 0.02 1
367 . 57 TYR N N 114.34 0.02 1
368 . 58 GLY H H 7.84 0.02 1
369 . 58 GLY HA2 H 3.90 0.02 2
370 . 58 GLY HA3 H 3.95 0.02 2
371 . 58 GLY N N 111.25 0.02 1
372 . 59 ILE H H 8.28 0.02 1
373 . 59 ILE HA H 3.88 0.02 1
374 . 59 ILE HB H 1.48 0.02 1
375 . 59 ILE HG12 H 1.52 0.02 2
376 . 59 ILE HG13 H 1.44 0.02 2
377 . 59 ILE HG2 H 0.42 0.02 1
378 . 59 ILE HD1 H 0.84 0.02 1
379 . 59 ILE N N 120.89 0.02 1
380 . 60 GLY H H 8.22 0.02 1
381 . 60 GLY HA2 H 3.68 0.02 2
382 . 60 GLY HA3 H 3.79 0.02 2
383 . 60 GLY N N 113.57 0.02 1
384 . 61 LYS H H 7.65 0.02 1
385 . 61 LYS HA H 4.18 0.02 1
386 . 61 LYS HB2 H 1.83 0.02 2
387 . 61 LYS HB3 H 1.73 0.02 2
388 . 61 LYS HG2 H 1.70 0.02 2
389 . 61 LYS HG3 H 1.40 0.02 2
390 . 61 LYS HD2 H 1.48 0.02 2
391 . 61 LYS HE2 H 3.00 0.02 2
392 . 61 LYS N N 124.75 0.02 1
stop_
save_
########################
# Coupling constants #
########################
save_coupling_constants
_Saveframe_category coupling_constants
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_1
_Spectrometer_frequency_1H 800
_Mol_system_component_name 'Tyr repressor DNA binding domain'
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 5 SER H 5 SER HA 4.4 . . 0.5
2 3JHNHA 6 LEU H 6 LEU HA 7.5 . . 0.5
3 3JHNHA 10 GLU H 10 GLU HA 10.0 . . 0.5
4 3JHNHA 11 ASN H 11 ASN HA 7.8 . . 0.5
5 3JHNHA 13 THR H 13 THR HA 5.8 . . 0.5
6 3JHNHA 14 LEU H 14 LEU HA 5.0 . . 0.5
7 3JHNHA 15 ASP H 15 ASP HA 4.4 . . 0.5
8 3JHNHA 16 GLU H 16 GLU HA 5.4 . . 0.5
9 3JHNHA 17 ILE H 17 ILE HA 4.6 . . 0.5
10 3JHNHA 18 ILE H 18 ILE HA 8.0 . . 0.5
11 3JHNHA 22 GLU H 22 GLU HA 5.4 . . 0.5
12 3JHNHA 23 ALA H 23 ALA HA 4.6 . . 0.5
13 3JHNHA 25 VAL H 25 VAL HA 4.3 . . 0.5
14 3JHNHA 26 LEU H 26 LEU HA 5.5 . . 0.5
15 3JHNHA 27 LYS H 27 LYS HA 4.6 . . 0.5
16 3JHNHA 30 TYR H 30 TYR HA 5.4 . . 0.5
17 3JHNHA 32 GLU H 32 GLU HA 9.7 . . 0.5
18 3JHNHA 33 TYR H 33 TYR HA 7.7 . . 0.5
19 3JHNHA 35 SER H 35 SER HA 5.0 . . 0.5
20 3JHNHA 36 THR H 36 THR HA 4.2 . . 0.5
21 3JHNHA 37 ARG H 37 ARG HA 5.3 . . 0.5
22 3JHNHA 38 LYS H 38 LYS HA 6.2 . . 0.5
23 3JHNHA 39 LEU H 39 LEU HA 5.9 . . 0.5
24 3JHNHA 41 GLN H 41 GLN HA 4.5 . . 0.5
25 3JHNHA 43 LEU H 43 LEU HA 6.9 . . 0.5
26 3JHNHA 45 VAL H 45 VAL HA 7.2 . . 0.5
27 3JHNHA 48 THR H 48 THR HA 5.1 . . 0.5
28 3JHNHA 49 ALA H 49 ALA HA 4.5 . . 0.5
29 3JHNHA 50 ILE H 50 ILE HA 5.0 . . 0.5
30 3JHNHA 52 ASN H 52 ASN HA 4.1 . . 0.5
31 3JHNHA 53 LYS H 53 LYS HA 4.6 . . 0.5
32 3JHNHA 54 LEU H 54 LEU HA 4.7 . . 0.5
33 3JHNHA 57 TYR H 57 TYR HA 5.8 . . 0.5
34 3JHNHA 61 LYS H 61 LYS HA 5.5 . . 0.5
stop_
save_