data_6373
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H, 13C and 15N backbone resonance assignments of LexA catalytic domain with the
L89P/Q92W/D150H/E152A/K156A mutations
;
_BMRB_accession_number 6373
_BMRB_flat_file_name bmr6373.str
_Entry_type original
_Submission_date 2004-10-29
_Accession_date 2004-11-01
_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 Okon Mark . .
2 Pfuetzner Richard A. .
3 Vockovic Marija . .
4 Little John W. .
5 Strynadka Natalie C.J. .
6 McIntosh Lawrence P. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 125
"13C chemical shifts" 377
"15N chemical shifts" 125
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-06-03 original author .
stop_
_Original_release_date 2005-06-03
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: Backbone chemical shift assignments of the LexA
catalytic domain in its active conformation.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15929009
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Okon Mark . .
2 Pfuetzner Richard A. .
3 Vockovic Marija . .
4 Little John W. .
5 Strynadka Natalie C.J. .
6 McIntosh Lawrence P. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 31
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 371
_Page_last 372
_Year 2005
_Details .
save_
##################################
# Molecular system description #
##################################
save_molecular_system_LexA
_Saveframe_category molecular_system
_Mol_system_name 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant dimer'
_Abbreviation_common 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant dimer'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1' $catalytic_domain_of_LexA_mutant
'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 2' $catalytic_domain_of_LexA_mutant
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Magnetic_equivalence_ID
_Magnetically_equivalent_system_component
1 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1'
1 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 2'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_catalytic_domain_of_LexA_mutant
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant'
_Abbreviation_common 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant'
_Molecular_mass 14850
_Mol_thiol_state 'not present'
loop_
_Biological_function
repressor
stop_
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 135
_Mol_residue_sequence
;
LLQEEEEGLPLVGRVAAGEP
LPAQWHIEGHYQVDPSLFKP
NADFLLRVSGMSMKDIGIMD
GDLLAVHKTQDVRNGQVVVA
RIHDAVTVARLKKQGNKVEL
LPENSEFKPIVVDLRQQSFT
IEGLAVGVIRNGDWL
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 68 LEU 2 69 LEU 3 70 GLN 4 71 GLU 5 72 GLU
6 73 GLU 7 74 GLU 8 75 GLY 9 76 LEU 10 77 PRO
11 78 LEU 12 79 VAL 13 80 GLY 14 81 ARG 15 82 VAL
16 83 ALA 17 84 ALA 18 85 GLY 19 86 GLU 20 87 PRO
21 88 LEU 22 89 PRO 23 90 ALA 24 91 GLN 25 92 TRP
26 93 HIS 27 94 ILE 28 95 GLU 29 96 GLY 30 97 HIS
31 98 TYR 32 99 GLN 33 100 VAL 34 101 ASP 35 102 PRO
36 103 SER 37 104 LEU 38 105 PHE 39 106 LYS 40 107 PRO
41 108 ASN 42 109 ALA 43 110 ASP 44 111 PHE 45 112 LEU
46 113 LEU 47 114 ARG 48 115 VAL 49 116 SER 50 117 GLY
51 118 MET 52 119 SER 53 120 MET 54 121 LYS 55 122 ASP
56 123 ILE 57 124 GLY 58 125 ILE 59 126 MET 60 127 ASP
61 128 GLY 62 129 ASP 63 130 LEU 64 131 LEU 65 132 ALA
66 133 VAL 67 134 HIS 68 135 LYS 69 136 THR 70 137 GLN
71 138 ASP 72 139 VAL 73 140 ARG 74 141 ASN 75 142 GLY
76 143 GLN 77 144 VAL 78 145 VAL 79 146 VAL 80 147 ALA
81 148 ARG 82 149 ILE 83 150 HIS 84 151 ASP 85 152 ALA
86 153 VAL 87 154 THR 88 155 VAL 89 156 ALA 90 157 ARG
91 158 LEU 92 159 LYS 93 160 LYS 94 161 GLN 95 162 GLY
96 163 ASN 97 164 LYS 98 165 VAL 99 166 GLU 100 167 LEU
101 168 LEU 102 169 PRO 103 170 GLU 104 171 ASN 105 172 SER
106 173 GLU 107 174 PHE 108 175 LYS 109 176 PRO 110 177 ILE
111 178 VAL 112 179 VAL 113 180 ASP 114 181 LEU 115 182 ARG
116 183 GLN 117 184 GLN 118 185 SER 119 186 PHE 120 187 THR
121 188 ILE 122 189 GLU 123 190 GLY 124 191 LEU 125 192 ALA
126 193 VAL 127 194 GLY 128 195 VAL 129 196 ILE 130 197 ARG
131 198 ASN 132 199 GLY 133 200 ASP 134 201 TRP 135 202 LEU
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-28
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 1JHE "Lexa L89p Q92w E152a K156a Mutant" 100.00 135 99.26 99.26 4.56e-90
PDB 3JSO "Classic Protein With A New Twist: Crystal Structure Of A Lexa Repressor Dna Complex" 100.00 202 97.04 97.04 3.58e-86
PDB 3JSP "Classic Protein With A New Twist: Crystal Structure Of A Lexa Repressor Dna Complex" 100.00 202 97.04 97.04 3.58e-86
PDB 3K3R "Unrefined Crystal Structure Of A Lexa-dna Complex" 100.00 202 97.04 97.04 3.58e-86
GB KFH80209 "LexA repressor, partial [Escherichia coli]" 73.33 99 96.97 96.97 4.97e-60
GB KFH96244 "LexA repressor, partial [Escherichia coli]" 77.78 105 97.14 97.14 3.69e-65
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$catalytic_domain_of_LexA_mutant . . Bacteria . . .
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
$catalytic_domain_of_LexA_mutant 'recombinant technology' 'E. coli' Escherichia coli . .
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
$catalytic_domain_of_LexA_mutant 1 mM '[U-13C; U-15N]'
'Phosphate buffer' 20 mM .
stop_
save_
############################
# Computer software used #
############################
save_software
_Saveframe_category software
_Name VNMR
_Version 6.1C
loop_
_Vendor
_Address
_Electronic_address
VARIAN . .
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer VARIAN
_Model UNITY-INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_1H15N_HSQC_TROSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H15N HSQC TROSY'
_Sample_label .
save_
save_HNCA_TROSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HNCA TROSY'
_Sample_label .
save_
save_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_(HB)CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name (HB)CBCA(CO)NH
_Sample_label .
save_
save_HNCO_TROSY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HNCO TROSY'
_Sample_label .
save_
save_15N-edited_NOESY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-edited NOESY'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H15N HSQC TROSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HNCA TROSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name (HB)CBCA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HNCO TROSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-edited NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_conditions
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.0 0.1 pH
temperature 303 0.1 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 C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118
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 $sample_conditions
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'catalytic domain of LexA L89P/Q92W/D150H/E152A/K156A mutant, chain 1'
_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 LEU CA C 55.62 0.3 1
2 . 2 LEU C C 176.89 0.1 1
3 . 2 LEU CB C 42.43 0.3 1
4 . 3 GLN H H 8.50 0.02 1
5 . 3 GLN N N 121.62 0.1 1
6 . 3 GLN CA C 56.46 0.3 1
7 . 3 GLN CB C 29.71 0.3 1
8 . 4 GLU CA C 56.46 0.3 1
9 . 4 GLU C C 176.06 0.1 1
10 . 4 GLU CB C 29.61 0.3 1
11 . 5 GLU H H 8.51 0.02 1
12 . 5 GLU N N 121.02 0.1 1
13 . 5 GLU CA C 57.14 0.3 1
14 . 5 GLU C C 176.61 0.1 1
15 . 5 GLU CB C 30.16 0.3 1
16 . 6 GLU H H 8.29 0.02 1
17 . 6 GLU N N 120.41 0.1 1
18 . 6 GLU CA C 57.05 0.3 1
19 . 6 GLU C C 176.37 0.1 1
20 . 6 GLU CB C 30.47 0.3 1
21 . 7 GLU H H 8.08 0.02 1
22 . 7 GLU N N 120.75 0.1 1
23 . 7 GLU CA C 56.60 0.3 1
24 . 7 GLU C C 176.14 0.1 1
25 . 7 GLU CB C 30.68 0.3 1
26 . 8 GLY H H 8.15 0.02 1
27 . 8 GLY N N 107.40 0.1 1
28 . 8 GLY CA C 44.32 0.3 1
29 . 8 GLY C C 173.47 0.1 1
30 . 9 LEU H H 8.72 0.02 1
31 . 9 LEU N N 122.61 0.1 1
32 . 9 LEU CA C 52.09 0.3 1
33 . 9 LEU CB C 45.34 0.3 1
34 . 10 PRO CA C 62.45 0.3 1
35 . 10 PRO C C 176.73 0.1 1
36 . 10 PRO CB C 33.07 0.3 1
37 . 11 LEU H H 8.2 0.02 1
38 . 11 LEU N N 124.59 0.1 1
39 . 11 LEU CA C 53.7 0.3 1
40 . 11 LEU C C 177.39 0.1 1
41 . 11 LEU CB C 42.13 0.3 1
42 . 12 VAL H H 7.76 0.02 1
43 . 12 VAL N N 116.08 0.1 1
44 . 12 VAL CA C 60.24 0.3 1
45 . 12 VAL C C 173.14 0.1 1
46 . 12 VAL CB C 31.68 0.3 1
47 . 13 GLY H H 6.48 0.02 1
48 . 13 GLY N N 102.84 0.1 1
49 . 13 GLY CA C 44.82 0.3 1
50 . 13 GLY C C 172.13 0.1 1
51 . 14 ARG H H 8.57 0.02 1
52 . 14 ARG N N 120.18 0.1 1
53 . 14 ARG CA C 54.62 0.3 1
54 . 14 ARG C C 174.97 0.1 1
55 . 14 ARG CB C 34.47 0.3 1
56 . 15 VAL H H 8.42 0.02 1
57 . 15 VAL N N 116.64 0.1 1
58 . 15 VAL CA C 59.51 0.3 1
59 . 15 VAL C C 171.37 0.1 1
60 . 15 VAL CB C 34.93 0.3 1
61 . 16 ALA H H 6.79 0.02 1
62 . 16 ALA N N 129.17 0.1 1
63 . 16 ALA CA C 52.50 0.3 1
64 . 16 ALA C C 176.39 0.1 1
65 . 16 ALA CB C 22.33 0.3 1
66 . 17 ALA H H 8.67 0.02 1
67 . 17 ALA N N 131.09 0.1 1
68 . 17 ALA CA C 52.23 0.3 1
69 . 17 ALA C C 176.52 0.1 1
70 . 17 ALA CB C 18.11 0.3 1
71 . 18 GLY H H 6.53 0.02 1
72 . 18 GLY N N 104.93 0.1 1
73 . 18 GLY CA C 45.43 0.3 1
74 . 18 GLY C C 172.05 0.1 1
75 . 19 GLU H H 8.44 0.02 1
76 . 19 GLU N N 124.65 0.1 1
77 . 19 GLU CA C 54.8 0.3 1
78 . 19 GLU CB C 30.01 0.3 1
79 . 20 PRO CA C 64.14 0.3 1
80 . 20 PRO C C 175.61 0.1 1
81 . 20 PRO CB C 32.33 0.3 1
82 . 21 LEU H H 8.02 0.02 1
83 . 21 LEU N N 124.76 0.1 1
84 . 21 LEU CA C 51.16 0.3 1
85 . 21 LEU CB C 46.05 0.3 1
86 . 22 PRO CA C 63.39 0.3 1
87 . 22 PRO C C 176.11 0.1 1
88 . 22 PRO CB C 31.58 0.3 1
89 . 23 ALA H H 7.96 0.02 1
90 . 23 ALA N N 126.34 0.1 1
91 . 23 ALA CA C 52.89 0.3 1
92 . 23 ALA C C 175.55 0.1 1
93 . 23 ALA CB C 21.57 0.3 1
94 . 24 GLN H H 8.5 0.02 1
95 . 24 GLN N N 123.67 0.1 1
96 . 24 GLN CA C 54.69 0.3 1
97 . 24 GLN C C 175.61 0.1 1
98 . 24 GLN CB C 28.96 0.3 1
99 . 25 TRP H H 8.51 0.02 1
100 . 25 TRP N N 126.52 0.1 1
101 . 25 TRP CA C 56.02 0.3 1
102 . 25 TRP C C 176.74 0.1 1
103 . 25 TRP CB C 29.6 0.3 1
104 . 25 TRP NE1 N 126.62 0.1 1
105 . 25 TRP HE1 H 9.82 0.03 1
106 . 26 HIS H H 8.98 0.02 1
107 . 26 HIS N N 120.89 0.1 1
108 . 26 HIS CA C 55.84 0.3 1
109 . 26 HIS C C 173.46 0.1 1
110 . 26 HIS CB C 31.19 0.3 1
111 . 27 ILE H H 8.46 0.02 1
112 . 27 ILE N N 123.01 0.1 1
113 . 27 ILE CA C 64.23 0.3 1
114 . 27 ILE C C 176.28 0.1 1
115 . 27 ILE CB C 37.84 0.3 1
116 . 28 GLU H H 8.88 0.02 1
117 . 28 GLU N N 126.56 0.1 1
118 . 28 GLU CA C 56.32 0.3 1
119 . 28 GLU C C 175.94 0.1 1
120 . 28 GLU CB C 31.94 0.3 1
121 . 29 GLY H H 7.29 0.02 1
122 . 29 GLY N N 106.60 0.1 1
123 . 29 GLY CA C 44.84 0.3 1
124 . 29 GLY C C 172.62 0.1 1
125 . 30 HIS H H 8.29 0.02 1
126 . 30 HIS N N 117.12 0.1 1
127 . 30 HIS CA C 56.47 0.3 1
128 . 30 HIS C C 173.90 0.1 1
129 . 30 HIS CB C 33.14 0.3 1
130 . 31 TYR H H 9.0 0.02 1
131 . 31 TYR N N 120.62 0.1 1
132 . 31 TYR CA C 56.85 0.3 1
133 . 31 TYR C C 175.85 0.1 1
134 . 31 TYR CB C 41.75 0.3 1
135 . 32 GLN H H 9.57 0.02 1
136 . 32 GLN N N 126.16 0.1 1
137 . 32 GLN CA C 56.67 0.3 1
138 . 32 GLN C C 173.08 0.1 1
139 . 32 GLN CB C 27.08 0.3 1
140 . 33 VAL H H 7.56 0.02 1
141 . 33 VAL N N 125.38 0.1 1
142 . 33 VAL CA C 60.56 0.3 1
143 . 33 VAL C C 173.94 0.1 1
144 . 33 VAL CB C 35.94 0.3 1
145 . 34 ASP H H 7.56 0.02 1
146 . 34 ASP N N 126.81 0.1 1
147 . 34 ASP CA C 52.23 0.3 1
148 . 34 ASP CB C 43.11 0.3 1
149 . 35 PRO CA C 65.63 0.3 1
150 . 35 PRO C C 178.78 0.1 1
151 . 35 PRO CB C 33.26 0.3 1
152 . 36 SER H H 8.61 0.02 1
153 . 36 SER N N 110.89 0.1 1
154 . 36 SER CA C 59.48 0.3 1
155 . 36 SER C C 174.86 0.1 1
156 . 36 SER CB C 63.46 0.3 1
157 . 37 LEU H H 7.72 0.02 1
158 . 37 LEU N N 122.25 0.1 1
159 . 37 LEU CA C 57.13 0.3 1
160 . 37 LEU C C 176.03 0.1 1
161 . 37 LEU CB C 42.52 0.3 1
162 . 38 PHE H H 6.99 0.02 1
163 . 38 PHE N N 116.7 0.1 1
164 . 38 PHE CA C 55.51 0.3 1
165 . 38 PHE C C 173.02 0.1 1
166 . 38 PHE CB C 41.46 0.3 1
167 . 39 LYS H H 9.01 0.02 1
168 . 39 LYS N N 121.64 0.1 1
169 . 39 LYS CA C 53.46 0.3 1
170 . 39 LYS CB C 35.67 0.3 1
171 . 40 PRO CA C 63.29 0.3 1
172 . 40 PRO CB C 33.35 0.3 1
173 . 41 ASN H H 7.74 0.02 1
174 . 41 ASN N N 111.68 0.1 1
175 . 41 ASN CA C 53.9 0.3 1
176 . 41 ASN C C 175.29 0.1 1
177 . 41 ASN CB C 40.12 0.3 1
178 . 42 ALA H H 7.82 0.02 1
179 . 42 ALA N N 121.01 0.1 1
180 . 42 ALA CA C 52.38 0.3 1
181 . 42 ALA C C 175.35 0.1 1
182 . 42 ALA CB C 21.75 0.3 1
183 . 43 ASP H H 9.21 0.02 1
184 . 43 ASP N N 118.78 0.1 1
185 . 43 ASP CA C 56.26 0.3 1
186 . 43 ASP C C 175.78 0.1 1
187 . 43 ASP CB C 45.27 0.3 1
188 . 44 PHE H H 7.76 0.02 1
189 . 44 PHE N N 112.0 0.1 1
190 . 44 PHE CA C 56.66 0.3 1
191 . 44 PHE C C 171.61 0.1 1
192 . 44 PHE CB C 40.12 0.3 1
193 . 45 LEU H H 9.1 0.02 1
194 . 45 LEU N N 117.72 0.1 1
195 . 45 LEU CA C 52.76 0.3 1
196 . 45 LEU C C 175.56 0.1 1
197 . 45 LEU CB C 46.66 0.3 1
198 . 46 LEU H H 8.43 0.02 1
199 . 46 LEU N N 118.94 0.1 1
200 . 46 LEU CA C 52.66 0.3 1
201 . 46 LEU C C 175.06 0.1 1
202 . 46 LEU CB C 47.94 0.3 1
203 . 47 ARG H H 8.93 0.02 1
204 . 47 ARG N N 122.09 0.1 1
205 . 47 ARG CA C 54.92 0.3 1
206 . 47 ARG C C 175.63 0.1 1
207 . 47 ARG CB C 31.22 0.3 1
208 . 48 VAL H H 9.28 0.02 1
209 . 48 VAL N N 129.42 0.1 1
210 . 48 VAL CA C 63.78 0.3 1
211 . 48 VAL C C 176.94 0.1 1
212 . 48 VAL CB C 32.47 0.3 1
213 . 49 SER H H 8.92 0.02 1
214 . 49 SER N N 124.90 0.1 1
215 . 49 SER CA C 56.14 0.3 1
216 . 49 SER C C 174.72 0.1 1
217 . 49 SER CB C 64.43 0.3 1
218 . 50 GLY H H 10.08 0.02 1
219 . 50 GLY N N 119.56 0.1 1
220 . 50 GLY CA C 44.33 0.3 1
221 . 50 GLY C C 175.20 0.1 1
222 . 51 MET H H 7.94 0.02 1
223 . 51 MET N N 112.6 0.1 1
224 . 51 MET CA C 54.94 0.3 1
225 . 51 MET C C 179.86 0.1 1
226 . 51 MET CB C 33.42 0.3 1
227 . 52 SER H H 7.92 0.02 1
228 . 52 SER N N 119.61 0.1 1
229 . 52 SER CA C 62.81 0.3 1
230 . 52 SER C C 170.68 0.1 1
231 . 52 SER CB C 61.28 0.3 1
232 . 53 MET H H 8.27 0.02 1
233 . 53 MET N N 117.10 0.1 1
234 . 53 MET CA C 52.99 0.3 1
235 . 53 MET C C 176.15 0.1 1
236 . 53 MET CB C 31.32 0.3 1
237 . 54 LYS H H 9.45 0.02 1
238 . 54 LYS N N 121.01 0.1 1
239 . 54 LYS CA C 59.68 0.3 1
240 . 54 LYS C C 179.95 0.1 1
241 . 54 LYS CB C 33.41 0.3 1
242 . 55 ASP H H 7.33 0.02 1
243 . 55 ASP N N 119.87 0.1 1
244 . 55 ASP CA C 57.59 0.3 1
245 . 55 ASP C C 178.34 0.1 1
246 . 55 ASP CB C 39.53 0.3 1
247 . 56 ILE H H 7.35 0.02 1
248 . 56 ILE N N 108.47 0.1 1
249 . 56 ILE CA C 60.98 0.3 1
250 . 56 ILE C C 176.14 0.1 1
251 . 56 ILE CB C 37.99 0.3 1
252 . 57 GLY H H 8.27 0.02 1
253 . 57 GLY N N 108.90 0.1 1
254 . 57 GLY CA C 47.67 0.3 1
255 . 57 GLY C C 174.87 0.1 1
256 . 58 ILE H H 6.89 0.02 1
257 . 58 ILE N N 122.27 0.1 1
258 . 58 ILE CA C 61.32 0.3 1
259 . 58 ILE C C 173.92 0.1 1
260 . 58 ILE CB C 37.09 0.3 1
261 . 59 MET H H 9.21 0.02 1
262 . 59 MET N N 127.01 0.1 1
263 . 59 MET CA C 52.00 0.3 1
264 . 59 MET C C 175.4 0.1 1
265 . 59 MET CB C 34.57 0.3 1
266 . 60 ASP H H 6.99 0.02 1
267 . 60 ASP N N 120.12 0.1 1
268 . 60 ASP CA C 57.53 0.3 1
269 . 60 ASP C C 176.96 0.1 1
270 . 60 ASP CB C 43.50 0.3 1
271 . 61 GLY H H 9.05 0.02 1
272 . 61 GLY N N 116.7 0.1 1
273 . 61 GLY CA C 45.45 0.3 1
274 . 61 GLY C C 174.57 0.1 1
275 . 62 ASP H H 8.16 0.02 1
276 . 62 ASP N N 123.09 0.1 1
277 . 62 ASP CA C 55.86 0.3 1
278 . 62 ASP C C 174.91 0.1 1
279 . 62 ASP CB C 41.14 0.3 1
280 . 63 LEU H H 8.54 0.02 1
281 . 63 LEU N N 117.52 0.1 1
282 . 63 LEU CA C 53.55 0.3 1
283 . 63 LEU C C 174.75 0.1 1
284 . 63 LEU CB C 42.02 0.3 1
285 . 64 LEU H H 9.55 0.02 1
286 . 64 LEU N N 125.74 0.1 1
287 . 64 LEU CA C 53.01 0.3 1
288 . 64 LEU C C 174.93 0.1 1
289 . 64 LEU CB C 46.35 0.3 1
290 . 65 ALA H H 8.21 0.02 1
291 . 65 ALA N N 129.22 0.1 1
292 . 65 ALA CA C 50.9 0.3 1
293 . 65 ALA C C 176.38 0.1 1
294 . 65 ALA CB C 18.13 0.3 1
295 . 66 VAL H H 8.37 0.02 1
296 . 66 VAL N N 123.47 0.1 1
297 . 66 VAL CA C 60.84 0.3 1
298 . 66 VAL C C 174.75 0.1 1
299 . 66 VAL CB C 33.97 0.3 1
300 . 67 HIS H H 9.29 0.02 1
301 . 67 HIS N N 128.59 0.1 1
302 . 67 HIS CA C 54.40 0.3 1
303 . 67 HIS C C 174.01 0.1 1
304 . 67 HIS CB C 31.58 0.3 1
305 . 68 LYS H H 10.39 0.02 1
306 . 68 LYS N N 132.8 0.1 1
307 . 68 LYS CA C 58.00 0.3 1
308 . 68 LYS C C 174.09 0.1 1
309 . 68 LYS CB C 32.51 0.3 1
310 . 69 THR H H 7.16 0.02 1
311 . 69 THR N N 121.99 0.1 1
312 . 69 THR CA C 60.81 0.3 1
313 . 69 THR C C 170.51 0.1 1
314 . 69 THR CB C 67.31 0.3 1
315 . 70 GLN H H 8.24 0.02 1
316 . 70 GLN N N 119.12 0.1 1
317 . 70 GLN CA C 55.48 0.3 1
318 . 70 GLN C C 175.87 0.1 1
319 . 70 GLN CB C 30.55 0.3 1
320 . 71 ASP H H 8.90 0.02 1
321 . 71 ASP N N 125.94 0.1 1
322 . 71 ASP CA C 54.11 0.3 1
323 . 71 ASP C C 174.12 0.1 1
324 . 71 ASP CB C 40.25 0.3 1
325 . 72 VAL H H 7.41 0.02 1
326 . 72 VAL N N 114.4 0.1 1
327 . 72 VAL CA C 59.31 0.3 1
328 . 72 VAL C C 174.97 0.1 1
329 . 72 VAL CB C 35.20 0.3 1
330 . 73 ARG H H 8.77 0.02 1
331 . 73 ARG N N 121.0 0.1 1
332 . 73 ARG CA C 53.79 0.3 1
333 . 73 ARG C C 175.11 0.1 1
334 . 73 ARG CB C 33.67 0.3 1
335 . 74 ASN H H 8.49 0.02 1
336 . 74 ASN N N 118.48 0.1 1
337 . 74 ASN CA C 54.14 0.3 1
338 . 74 ASN C C 177.02 0.1 1
339 . 74 ASN CB C 38.00 0.3 1
340 . 75 GLY H H 9.38 0.02 1
341 . 75 GLY N N 110.75 0.1 1
342 . 75 GLY CA C 45.5 0.3 1
343 . 75 GLY C C 174.63 0.1 1
344 . 76 GLN H H 7.79 0.02 1
345 . 76 GLN N N 119.16 0.1 1
346 . 76 GLN CA C 56.41 0.3 1
347 . 76 GLN C C 175.06 0.1 1
348 . 76 GLN CB C 29.46 0.3 1
349 . 77 VAL H H 8.67 0.02 1
350 . 77 VAL N N 122.19 0.1 1
351 . 77 VAL CA C 57.38 0.3 1
352 . 77 VAL C C 174.52 0.1 1
353 . 77 VAL CB C 30.03 0.3 1
354 . 78 VAL H H 8.92 0.02 1
355 . 78 VAL N N 120.14 0.1 1
356 . 78 VAL CA C 58.48 0.3 1
357 . 78 VAL C C 173.44 0.1 1
358 . 78 VAL CB C 35.94 0.3 1
359 . 79 VAL H H 8.21 0.02 1
360 . 79 VAL N N 118.2 0.1 1
361 . 79 VAL CA C 61.26 0.3 1
362 . 79 VAL C C 174.74 0.1 1
363 . 79 VAL CB C 32.36 0.3 1
364 . 80 ALA H H 9.12 0.02 1
365 . 80 ALA N N 130.64 0.1 1
366 . 80 ALA CA C 50.30 0.3 1
367 . 80 ALA C C 173.5 0.1 1
368 . 80 ALA CB C 24.38 0.3 1
369 . 81 ARG H H 8.97 0.02 1
370 . 81 ARG N N 121.84 0.1 1
371 . 81 ARG CA C 54.01 0.3 1
372 . 81 ARG C C 174.62 0.1 1
373 . 81 ARG CB C 33.58 0.3 1
374 . 82 ILE H H 9.19 0.02 1
375 . 82 ILE N N 127.78 0.1 1
376 . 82 ILE CA C 60.80 0.3 1
377 . 82 ILE C C 177.24 0.3 1
378 . 82 ILE CB C 40.17 0.3 1
379 . 83 HIS H H 8.90 0.02 1
380 . 83 HIS N N 126.12 0.1 1
381 . 83 HIS CA C 59.36 0.3 1
382 . 83 HIS C C 173.34 0.1 1
383 . 83 HIS CB C 28.9 0.3 1
384 . 84 ASP H H 8.48 0.02 1
385 . 84 ASP N N 121.15 0.1 1
386 . 84 ASP CA C 57.68 0.3 1
387 . 84 ASP C C 174.70 0.1 1
388 . 84 ASP CB C 39.7 0.3 1
389 . 85 ALA H H 7.97 0.02 1
390 . 85 ALA N N 124.7 0.1 1
391 . 85 ALA CA C 51.75 0.3 1
392 . 85 ALA C C 175.75 0.1 1
393 . 85 ALA CB C 22.18 0.3 1
394 . 86 VAL H H 8.64 0.02 1
395 . 86 VAL N N 114.88 0.1 1
396 . 86 VAL CA C 59.44 0.3 1
397 . 86 VAL C C 175.86 0.1 1
398 . 86 VAL CB C 35.96 0.3 1
399 . 87 THR H H 8.84 0.02 1
400 . 87 THR N N 119.61 0.1 1
401 . 87 THR CA C 59.59 0.3 1
402 . 87 THR C C 170.25 0.1 1
403 . 87 THR CB C 71.81 0.3 1
404 . 88 VAL H H 8.14 0.02 1
405 . 88 VAL N N 124.90 0.1 1
406 . 88 VAL CA C 57.57 0.3 1
407 . 88 VAL C C 171.99 0.1 1
408 . 88 VAL CB C 33.89 0.3 1
409 . 89 ALA H H 8.50 0.02 1
410 . 89 ALA N N 125.95 0.1 1
411 . 89 ALA CA C 51.28 0.3 1
412 . 89 ALA C C 175.16 0.1 1
413 . 89 ALA CB C 24.21 0.3 1
414 . 90 ARG H H 9.24 0.02 1
415 . 90 ARG N N 119.79 0.1 1
416 . 90 ARG CA C 56.30 0.3 1
417 . 90 ARG C C 176.21 0.1 1
418 . 90 ARG CB C 31.71 0.3 1
419 . 91 LEU H H 8.51 0.02 1
420 . 91 LEU N N 126.63 0.1 1
421 . 91 LEU CA C 56.06 0.3 1
422 . 91 LEU C C 177.09 0.1 1
423 . 91 LEU CB C 44.64 0.3 1
424 . 92 LYS H H 8.82 0.02 1
425 . 92 LYS N N 128.66 0.1 1
426 . 92 LYS CA C 56.82 0.3 1
427 . 92 LYS C C 173.86 0.1 1
428 . 92 LYS CB C 34.91 0.3 1
429 . 93 LYS H H 9.40 0.02 1
430 . 93 LYS N N 129.43 0.1 1
431 . 93 LYS CA C 56.21 0.3 1
432 . 93 LYS C C 175.83 0.1 1
433 . 93 LYS CB C 35.09 0.3 1
434 . 94 GLN H H 8.79 0.02 1
435 . 94 GLN N N 127.31 0.1 1
436 . 94 GLN CA C 55.84 0.3 1
437 . 94 GLN CB C 31.13 0.3 1
438 . 96 ASN CA C 54.05 0.3 1
439 . 96 ASN C C 173.15 0.1 1
440 . 96 ASN CB C 39.56 0.3 1
441 . 97 LYS H H 7.85 0.02 1
442 . 97 LYS N N 119.8 0.1 1
443 . 97 LYS CA C 55.25 0.3 1
444 . 97 LYS C C 174.8 0.1 1
445 . 97 LYS CB C 35.04 0.3 1
446 . 98 VAL H H 8.76 0.02 1
447 . 98 VAL N N 124.47 0.1 1
448 . 98 VAL CA C 61.38 0.3 1
449 . 98 VAL C C 173.84 0.1 1
450 . 98 VAL CB C 34.80 0.3 1
451 . 99 GLU H H 8.78 0.02 1
452 . 99 GLU N N 125.55 0.1 1
453 . 99 GLU CA C 54.94 0.3 1
454 . 99 GLU C C 174.35 0.1 1
455 . 99 GLU CB C 33.25 0.3 1
456 . 100 LEU H H 9.04 0.02 1
457 . 100 LEU N N 124.29 0.1 1
458 . 100 LEU CA C 52.73 0.3 1
459 . 100 LEU C C 176.49 0.1 1
460 . 100 LEU CB C 41.3 0.3 1
461 . 101 LEU H H 9.65 0.02 1
462 . 101 LEU N N 127.38 0.1 1
463 . 101 LEU CA C 52.98 0.3 1
464 . 101 LEU CB C 42.66 0.3 1
465 . 102 PRO CA C 61.8 0.3 1
466 . 102 PRO C C 175.79 0.1 1
467 . 102 PRO CB C 32.7 0.3 1
468 . 103 GLU H H 8.6 0.02 1
469 . 103 GLU N N 123.88 0.1 1
470 . 103 GLU CA C 54.87 0.3 1
471 . 103 GLU C C 173.52 0.1 1
472 . 103 GLU CB C 29.71 0.3 1
473 . 104 ASN H H 6.92 0.02 1
474 . 104 ASN N N 115.51 0.1 1
475 . 104 ASN CA C 54.72 0.3 1
476 . 104 ASN C C 176.88 0.1 1
477 . 104 ASN CB C 39.01 0.3 1
478 . 105 SER H H 9.38 0.02 1
479 . 105 SER N N 123.47 0.1 1
480 . 105 SER CA C 61.45 0.3 1
481 . 105 SER C C 175.26 0.1 1
482 . 105 SER CB C 63.28 0.3 1
483 . 106 GLU H H 8.59 0.02 1
484 . 106 GLU N N 119.77 0.1 1
485 . 106 GLU CA C 57.22 0.3 1
486 . 106 GLU C C 174.24 0.1 1
487 . 106 GLU CB C 30.1 0.3 1
488 . 107 PHE H H 8.20 0.02 1
489 . 107 PHE N N 120.17 0.1 1
490 . 107 PHE CA C 57.37 0.3 1
491 . 107 PHE C C 174.12 0.1 1
492 . 107 PHE CB C 41.4 0.3 1
493 . 108 LYS H H 8.63 0.02 1
494 . 108 LYS N N 120.19 0.1 1
495 . 108 LYS CA C 53.27 0.3 1
496 . 108 LYS CB C 33.23 0.3 1
497 . 109 PRO CA C 63.39 0.3 1
498 . 109 PRO C C 176.25 0.1 1
499 . 109 PRO CB C 33.07 0.3 1
500 . 110 ILE H H 8.09 0.02 1
501 . 110 ILE N N 123.90 0.1 1
502 . 110 ILE CA C 61.22 0.3 1
503 . 110 ILE C C 174.87 0.1 1
504 . 110 ILE CB C 40.44 0.3 1
505 . 111 VAL H H 8.54 0.02 1
506 . 111 VAL N N 127.36 0.1 1
507 . 111 VAL CA C 61.55 0.3 1
508 . 111 VAL C C 175.54 0.1 1
509 . 111 VAL CB C 33.29 0.3 1
510 . 112 VAL H H 9.29 0.02 1
511 . 112 VAL N N 128.84 0.1 1
512 . 112 VAL CA C 60.94 0.3 1
513 . 112 VAL C C 174.05 0.1 1
514 . 112 VAL CB C 34.89 0.3 1
515 . 113 ASP H H 8.64 0.02 1
516 . 113 ASP N N 126.12 0.1 1
517 . 113 ASP CA C 59.27 0.3 1
518 . 113 ASP C C 177.58 0.1 1
519 . 113 ASP CB C 40.37 0.3 1
520 . 114 LEU H H 8.93 0.02 1
521 . 114 LEU N N 126.13 0.1 1
522 . 114 LEU CA C 57.04 0.3 1
523 . 114 LEU C C 178.63 0.1 1
524 . 114 LEU CB C 41.86 0.3 1
525 . 115 ARG H H 8.7 0.02 1
526 . 115 ARG N N 116.45 0.1 1
527 . 115 ARG CA C 57.66 0.3 1
528 . 115 ARG C C 177.55 0.1 1
529 . 115 ARG CB C 30.54 0.3 1
530 . 116 GLN H H 7.59 0.02 1
531 . 116 GLN N N 114.37 0.1 1
532 . 116 GLN CA C 56.17 0.3 1
533 . 116 GLN C C 175.40 0.1 1
534 . 116 GLN CB C 32.11 0.3 1
535 . 117 GLN H H 7.95 0.02 1
536 . 117 GLN N N 117.65 0.1 1
537 . 117 GLN CA C 55.29 0.3 1
538 . 117 GLN C C 174.48 0.1 1
539 . 117 GLN CB C 32.49 0.3 1
540 . 118 SER H H 8.1 0.02 1
541 . 118 SER N N 116.36 0.1 1
542 . 118 SER CA C 58.3 0.3 1
543 . 118 SER C C 173.11 0.1 1
544 . 118 SER CB C 63.84 0.3 1
545 . 119 PHE H H 8.23 0.02 1
546 . 119 PHE N N 126.6 0.1 1
547 . 119 PHE CA C 57.62 0.3 1
548 . 119 PHE C C 174.15 0.1 1
549 . 119 PHE CB C 43.56 0.3 1
550 . 120 THR H H 8.37 0.02 1
551 . 120 THR N N 122.47 0.1 1
552 . 120 THR CA C 61.07 0.3 1
553 . 120 THR C C 172.23 0.1 1
554 . 120 THR CB C 72.13 0.3 1
555 . 121 ILE H H 8.69 0.02 1
556 . 121 ILE N N 125.95 0.1 1
557 . 121 ILE CA C 59.52 0.3 1
558 . 121 ILE C C 175.59 0.1 1
559 . 121 ILE CB C 37.24 0.3 1
560 . 122 GLU H H 8.85 0.02 1
561 . 122 GLU N N 125.52 0.1 1
562 . 122 GLU CA C 56.06 0.3 1
563 . 122 GLU C C 177.91 0.1 1
564 . 122 GLU CB C 30.32 0.3 1
565 . 123 GLY H H 7.46 0.02 1
566 . 123 GLY N N 102.98 0.1 1
567 . 123 GLY CA C 45.89 0.3 1
568 . 123 GLY C C 169.66 0.1 1
569 . 124 LEU H H 8.75 0.02 1
570 . 124 LEU N N 121.02 0.1 1
571 . 124 LEU CA C 53.00 0.3 1
572 . 124 LEU C C 175.76 0.1 1
573 . 124 LEU CB C 47.58 0.3 1
574 . 125 ALA H H 8.82 0.02 1
575 . 125 ALA N N 129.61 0.1 1
576 . 125 ALA CA C 52.43 0.3 1
577 . 125 ALA C C 176.58 0.1 1
578 . 125 ALA CB C 19.63 0.3 1
579 . 126 VAL H H 8.68 0.02 1
580 . 126 VAL N N 113.21 0.1 1
581 . 126 VAL CA C 60.68 0.3 1
582 . 126 VAL C C 175.16 0.1 1
583 . 126 VAL CB C 33.85 0.3 1
584 . 127 GLY H H 7.27 0.02 1
585 . 127 GLY N N 106.71 0.1 1
586 . 127 GLY CA C 46.46 0.3 1
587 . 127 GLY C C 171.57 0.1 1
588 . 128 VAL H H 8.52 0.02 1
589 . 128 VAL N N 117.45 0.1 1
590 . 128 VAL CA C 60.47 0.3 1
591 . 128 VAL C C 174.44 0.1 1
592 . 128 VAL CB C 37.94 0.3 1
593 . 129 ILE H H 9.26 0.02 1
594 . 129 ILE N N 124.09 0.1 1
595 . 129 ILE CA C 60.71 0.3 1
596 . 129 ILE C C 173.12 0.1 1
597 . 129 ILE CB C 42.16 0.3 1
598 . 130 ARG H H 9.34 0.02 1
599 . 130 ARG N N 128.5 0.1 1
600 . 130 ARG CA C 54.97 0.3 1
601 . 130 ARG C C 175.04 0.1 1
602 . 130 ARG CB C 33.53 0.3 1
603 . 131 ASN H H 8.52 0.02 1
604 . 131 ASN N N 124.76 0.1 1
605 . 131 ASN CA C 52.5 0.3 1
606 . 131 ASN C C 175.19 0.1 1
607 . 131 ASN CB C 39.33 0.3 1
608 . 132 GLY H H 7.76 0.02 1
609 . 132 GLY N N 109.11 0.1 1
610 . 132 GLY CA C 45.4 0.3 1
611 . 132 GLY C C 173.28 0.1 1
612 . 133 ASP H H 8.13 0.02 1
613 . 133 ASP N N 119.50 0.1 1
614 . 133 ASP CA C 54.96 0.3 1
615 . 133 ASP C C 176.06 0.1 1
616 . 133 ASP CB C 41.59 0.3 1
617 . 134 TRP H H 7.85 0.02 1
618 . 134 TRP N N 119.44 0.1 1
619 . 134 TRP CA C 57.17 0.3 1
620 . 134 TRP C C 175.28 0.1 1
621 . 134 TRP CB C 29.77 0.3 1
622 . 134 TRP NE1 N 129.16 0.1 1
623 . 134 TRP HE1 H 9.89 0.03 1
624 . 135 LEU H H 7.80 0.02 1
625 . 135 LEU N N 128.95 0.1 1
626 . 135 LEU CA C 57.09 0.3 1
627 . 135 LEU CB C 43.78 0.3 1
stop_
save_