data_26058
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone 1H, 13C, and 15N Chemical Shift Assignments for a 58 truncated variant of the CI repressor from the temperated bacteriophage Tp901-1
;
_BMRB_accession_number 26058
_BMRB_flat_file_name bmr26058.str
_Entry_type original
_Submission_date 2016-05-18
_Accession_date 2016-05-18
_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 'Krighaar Rasmussen' Kim KKR .
2 Ringkjobing-Jensen Malene . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 117
"13C chemical shifts" 246
"15N chemical shifts" 117
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2016-10-12 update BMRB 'update entry citation'
2016-06-21 original author 'original release'
stop_
_Original_release_date 2016-06-21
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 27403839
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Rasmussen Kim K. .
2 Frandsen Kristian E.H. .
3 Erba Elisabetta B. .
4 Pedersen Margit . .
5 Varming Anders K. .
6 Hammer Karin . .
7 Kilstrup Mogens . .
8 Thulstrup Peter W. .
9 Blackledge Martin . .
10 Jensen Malene R. .
11 Leggio Leila L. .
stop_
_Journal_abbreviation 'Sci. Rep.'
_Journal_volume 6
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 29574
_Page_last 29574
_Year 2016
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'd58CI dimer'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'dimer d58CI, chain 1' $d58CI
'dimer d58CI, chain 2' $d58CI
stop_
_System_molecular_weight 30.088
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details 'Symmetric dimer'
save_
########################
# Monomeric polymers #
########################
save_d58CI
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common d58CI
_Molecular_mass .
_Mol_thiol_state 'not present'
loop_
_Biological_function
'Transcription repressor of the genetic switch from temperated TP901-1 bacteriophage'
stop_
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 130
_Mol_residue_sequence
;
MQTDTSNRLKQIMAERNLKQ
VDILNLSIPFQKKFGIKLSK
STLSQYVNSVQSPDQNRIYL
LAKTLGVSEAWLMGFDVPMV
ESSKIENDSENIEETITVMK
KLEEPRQKVVLDTAKIQLKE
QDRSHHHHHH
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLN 3 THR 4 ASP 5 THR
6 SER 7 ASN 8 ARG 9 LEU 10 LYS
11 GLN 12 ILE 13 MET 14 ALA 15 GLU
16 ARG 17 ASN 18 LEU 19 LYS 20 GLN
21 VAL 22 ASP 23 ILE 24 LEU 25 ASN
26 LEU 27 SER 28 ILE 29 PRO 30 PHE
31 GLN 32 LYS 33 LYS 34 PHE 35 GLY
36 ILE 37 LYS 38 LEU 39 SER 40 LYS
41 SER 42 THR 43 LEU 44 SER 45 GLN
46 TYR 47 VAL 48 ASN 49 SER 50 VAL
51 GLN 52 SER 53 PRO 54 ASP 55 GLN
56 ASN 57 ARG 58 ILE 59 TYR 60 LEU
61 LEU 62 ALA 63 LYS 64 THR 65 LEU
66 GLY 67 VAL 68 SER 69 GLU 70 ALA
71 TRP 72 LEU 73 MET 74 GLY 75 PHE
76 ASP 77 VAL 78 PRO 79 MET 80 VAL
81 GLU 82 SER 83 SER 84 LYS 85 ILE
86 GLU 87 ASN 88 ASP 89 SER 90 GLU
91 ASN 92 ILE 93 GLU 94 GLU 95 THR
96 ILE 97 THR 98 VAL 99 MET 100 LYS
101 LYS 102 LEU 103 GLU 104 GLU 105 PRO
106 ARG 107 GLN 108 LYS 109 VAL 110 VAL
111 LEU 112 ASP 113 THR 114 ALA 115 LYS
116 ILE 117 GLN 118 LEU 119 LYS 120 GLU
121 GLN 122 ASP 123 ARG 124 SER 125 HIS
126 HIS 127 HIS 128 HIS 129 HIS 130 HIS
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
$d58CI 'Lactococcus phage TP901-1' 35345 Viruses . bacteriophage TP901-1
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
$d58CI 'recombinant technology' . Escherichia coli . - -
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details 'd58CI in Tris buffer at pH. 6.5'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$d58CI 500 uM '[U-13C; U-15N]'
TRIS 20 mM 'natural abundance'
NaCl 100 mM 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_SPARKY
_Saveframe_category software
_Name SPARKY
_Version .
loop_
_Vendor
_Address
_Electronic_address
Goddard . .
stop_
loop_
_Task
'chemical shift assignment'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity
_Field_strength 600
_Details .
save_
save_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $sample_1
save_
save_3D_HNCO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCO'
_Sample_label $sample_1
save_
save_3D_HCACO_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HCACO'
_Sample_label $sample_1
save_
save_3D_HNCA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCA'
_Sample_label $sample_1
save_
save_3D_HN(CO)CA_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(CO)CA'
_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
'ionic strength' 120 . mM
pH 6.5 . pH
pressure 1 . atm
temperature 311 . K
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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000
DSS N 15 'methyl protons' ppm 0.00 na 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_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
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 'dimer d58CI, 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 2 GLN C C 175.34 . .
2 2 2 GLN CA C 56.11 . .
3 3 3 THR H H 8.57 . .
4 3 3 THR C C 172.39 . .
5 3 3 THR CA C 59.83 . .
6 3 3 THR N N 119.28 . .
7 4 4 ASP H H 8.44 . .
8 4 4 ASP C C 176.55 . .
9 4 4 ASP CA C 53.19 . .
10 4 4 ASP N N 121.46 . .
11 5 5 THR H H 8.07 . .
12 5 5 THR C C 175.89 . .
13 5 5 THR CA C 66.16 . .
14 5 5 THR N N 116.08 . .
15 6 6 SER H H 8.36 . .
16 6 6 SER C C 176.14 . .
17 6 6 SER CA C 62.49 . .
18 6 6 SER N N 117.59 . .
19 7 7 ASN H H 7.89 . .
20 7 7 ASN C C 178.50 . .
21 7 7 ASN CA C 56.99 . .
22 7 7 ASN N N 118.84 . .
23 8 8 ARG H H 7.86 . .
24 8 8 ARG C C 178.57 . .
25 8 8 ARG CA C 58.11 . .
26 8 8 ARG N N 120.08 . .
27 9 9 LEU H H 8.59 . .
28 9 9 LEU C C 178.89 . .
29 9 9 LEU CA C 58.15 . .
30 9 9 LEU N N 118.55 . .
31 10 10 LYS H H 8.10 . .
32 10 10 LYS C C 179.68 . .
33 10 10 LYS CA C 60.82 . .
34 10 10 LYS N N 118.29 . .
35 11 11 GLN H H 8.31 . .
36 11 11 GLN C C 178.53 . .
37 11 11 GLN CA C 59.60 . .
38 11 11 GLN N N 121.35 . .
39 12 12 ILE H H 8.36 . .
40 12 12 ILE C C 177.72 . .
41 12 12 ILE CA C 63.70 . .
42 12 12 ILE N N 120.12 . .
43 13 13 MET H H 8.25 . .
44 13 13 MET C C 178.38 . .
45 13 13 MET CA C 61.08 . .
46 13 13 MET N N 119.38 . .
47 14 14 ALA H H 7.84 . .
48 14 14 ALA C C 180.72 . .
49 14 14 ALA CA C 55.01 . .
50 14 14 ALA N N 119.70 . .
51 15 15 GLU H H 8.57 . .
52 15 15 GLU C C 178.78 . .
53 15 15 GLU CA C 59.48 . .
54 15 15 GLU N N 117.43 . .
55 16 16 ARG H H 8.03 . .
56 16 16 ARG C C 175.04 . .
57 16 16 ARG CA C 55.84 . .
58 16 16 ARG N N 113.43 . .
59 17 17 ASN H H 7.61 . .
60 17 17 ASN C C 174.17 . .
61 17 17 ASN CA C 54.54 . .
62 17 17 ASN N N 118.09 . .
63 18 18 LEU H H 8.34 . .
64 18 18 LEU C C 176.78 . .
65 18 18 LEU CA C 53.62 . .
66 18 18 LEU N N 117.30 . .
67 19 19 LYS H H 9.39 . .
68 19 19 LYS C C 178.88 . .
69 19 19 LYS CA C 54.73 . .
70 19 19 LYS N N 120.36 . .
71 20 20 GLN H H 9.12 . .
72 20 20 GLN C C 178.91 . .
73 20 20 GLN CA C 61.98 . .
74 20 20 GLN N N 122.72 . .
75 21 21 VAL H H 8.25 . .
76 21 21 VAL C C 176.18 . .
77 21 21 VAL CA C 64.75 . .
78 21 21 VAL N N 114.50 . .
79 22 22 ASP H H 6.87 . .
80 22 22 ASP C C 178.71 . .
81 22 22 ASP CA C 57.61 . .
82 22 22 ASP N N 119.81 . .
83 23 23 ILE H H 7.45 . .
84 23 23 ILE C C 177.29 . .
85 23 23 ILE CA C 65.83 . .
86 23 23 ILE N N 118.72 . .
87 24 24 LEU H H 7.90 . .
88 24 24 LEU C C 180.83 . .
89 24 24 LEU CA C 57.92 . .
90 24 24 LEU N N 118.92 . .
91 25 25 ASN H H 8.55 . .
92 25 25 ASN C C 179.26 . .
93 25 25 ASN CA C 56.66 . .
94 25 25 ASN N N 119.23 . .
95 26 26 LEU H H 8.58 . .
96 26 26 LEU C C 178.94 . .
97 26 26 LEU CA C 57.65 . .
98 26 26 LEU N N 121.62 . .
99 27 27 SER H H 8.11 . .
100 27 27 SER C C 177.00 . .
101 27 27 SER CA C 60.60 . .
102 27 27 SER N N 111.70 . .
103 28 28 ILE H H 7.61 . .
104 28 28 ILE C C 175.23 . .
105 28 28 ILE CA C 66.88 . .
106 28 28 ILE N N 125.95 . .
107 29 29 PRO C C 179.75 . .
108 29 29 PRO CA C 65.56 . .
109 30 30 PHE H H 6.98 . .
110 30 30 PHE C C 176.94 . .
111 30 30 PHE CA C 61.28 . .
112 30 30 PHE N N 116.46 . .
113 31 31 GLN H H 8.88 . .
114 31 31 GLN C C 180.83 . .
115 31 31 GLN CA C 60.34 . .
116 31 31 GLN N N 122.27 . .
117 32 32 LYS H H 7.58 . .
118 32 32 LYS C C 178.44 . .
119 32 32 LYS CA C 58.86 . .
120 32 32 LYS N N 117.25 . .
121 33 33 LYS H H 7.59 . .
122 33 33 LYS C C 178.34 . .
123 33 33 LYS CA C 59.36 . .
124 33 33 LYS N N 119.03 . .
125 34 34 PHE H H 8.29 . .
126 34 34 PHE C C 176.77 . .
127 34 34 PHE CA C 56.11 . .
128 34 34 PHE N N 112.38 . .
129 35 35 GLY H H 7.87 . .
130 35 35 GLY C C 174.17 . .
131 35 35 GLY CA C 46.52 . .
132 35 35 GLY N N 109.44 . .
133 36 36 ILE H H 7.09 . .
134 36 36 ILE C C 173.50 . .
135 36 36 ILE CA C 60.24 . .
136 36 36 ILE N N 119.40 . .
137 37 37 LYS H H 8.16 . .
138 37 37 LYS C C 176.08 . .
139 37 37 LYS CA C 55.69 . .
140 37 37 LYS N N 123.90 . .
141 38 38 LEU H H 7.19 . .
142 38 38 LEU C C 173.49 . .
143 38 38 LEU CA C 54.61 . .
144 38 38 LEU N N 122.01 . .
145 39 39 SER H H 8.18 . .
146 39 39 SER C C 174.37 . .
147 39 39 SER CA C 56.21 . .
148 39 39 SER N N 121.61 . .
149 40 40 LYS H H 8.94 . .
150 40 40 LYS C C 178.93 . .
151 40 40 LYS CA C 60.06 . .
152 40 40 LYS N N 121.55 . .
153 41 41 SER C C 177.00 . .
154 41 41 SER CA C 61.20 . .
155 42 42 THR H H 7.70 . .
156 42 42 THR C C 174.98 . .
157 42 42 THR CA C 66.28 . .
158 42 42 THR N N 120.46 . .
159 43 43 LEU H H 7.84 . .
160 43 43 LEU C C 178.04 . .
161 43 43 LEU CA C 58.55 . .
162 43 43 LEU N N 119.61 . .
163 44 44 SER H H 7.88 . .
164 44 44 SER C C 177.31 . .
165 44 44 SER CA C 61.52 . .
166 44 44 SER N N 112.75 . .
167 45 45 GLN H H 7.64 . .
168 45 45 GLN C C 179.32 . .
169 45 45 GLN CA C 59.36 . .
170 45 45 GLN N N 119.85 . .
171 46 46 TYR H H 8.03 . .
172 46 46 TYR C C 180.76 . .
173 46 46 TYR CA C 56.63 . .
174 46 46 TYR N N 118.92 . .
175 47 47 VAL H H 8.36 . .
176 47 47 VAL C C 176.47 . .
177 47 47 VAL CA C 66.84 . .
178 47 47 VAL N N 121.02 . .
179 48 48 ASN H H 8.07 . .
180 48 48 ASN C C 174.50 . .
181 48 48 ASN CA C 53.86 . .
182 48 48 ASN N N 114.96 . .
183 49 49 SER H H 7.64 . .
184 49 49 SER C C 174.11 . .
185 49 49 SER CA C 59.91 . .
186 49 49 SER N N 112.46 . .
187 50 50 VAL H H 8.44 . .
188 50 50 VAL C C 176.25 . .
189 50 50 VAL CA C 63.76 . .
190 50 50 VAL N N 118.46 . .
191 51 51 GLN H H 7.29 . .
192 51 51 GLN C C 174.81 . .
193 51 51 GLN CA C 54.57 . .
194 51 51 GLN N N 115.35 . .
195 52 52 SER H H 8.82 . .
196 52 52 SER C C 172.27 . .
197 52 52 SER CA C 56.25 . .
198 52 52 SER N N 119.41 . .
199 53 53 PRO C C 175.51 . .
200 53 53 PRO CA C 62.81 . .
201 54 54 ASP H H 7.16 . .
202 54 54 ASP C C 175.66 . .
203 54 54 ASP CA C 52.33 . .
204 54 54 ASP N N 118.95 . .
205 55 55 GLN H H 8.67 . .
206 55 55 GLN C C 178.55 . .
207 55 55 GLN CA C 59.64 . .
208 55 55 GLN N N 119.22 . .
209 56 56 ASN H H 8.42 . .
210 56 56 ASN C C 177.22 . .
211 56 56 ASN CA C 55.98 . .
212 56 56 ASN N N 116.55 . .
213 57 57 ARG H H 8.13 . .
214 57 57 ARG C C 179.08 . .
215 57 57 ARG CA C 60.62 . .
216 57 57 ARG N N 121.26 . .
217 58 58 ILE H H 8.38 . .
218 58 58 ILE C C 176.75 . .
219 58 58 ILE CA C 63.51 . .
220 58 58 ILE N N 122.09 . .
221 59 59 TYR H H 7.95 . .
222 59 59 TYR C C 176.92 . .
223 59 59 TYR CA C 62.02 . .
224 59 59 TYR N N 121.14 . .
225 60 60 LEU H H 8.11 . .
226 60 60 LEU C C 180.05 . .
227 60 60 LEU CA C 58.56 . .
228 60 60 LEU N N 116.46 . .
229 61 61 LEU H H 8.62 . .
230 61 61 LEU C C 177.29 . .
231 61 61 LEU CA C 58.28 . .
232 61 61 LEU N N 120.62 . .
233 62 62 ALA H H 8.81 . .
234 62 62 ALA C C 180.13 . .
235 62 62 ALA CA C 56.08 . .
236 62 62 ALA N N 123.92 . .
237 63 63 LYS H H 7.77 . .
238 63 63 LYS C C 178.76 . .
239 63 63 LYS CA C 57.22 . .
240 63 63 LYS N N 115.80 . .
241 64 64 THR H H 7.67 . .
242 64 64 THR C C 175.43 . .
243 64 64 THR CA C 66.93 . .
244 64 64 THR N N 115.33 . .
245 65 65 LEU H H 7.77 . .
246 65 65 LEU C C 176.51 . .
247 65 65 LEU CA C 54.90 . .
248 65 65 LEU N N 115.90 . .
249 66 66 GLY H H 7.86 . .
250 66 66 GLY C C 175.71 . .
251 66 66 GLY CA C 46.54 . .
252 66 66 GLY N N 110.79 . .
253 67 67 VAL H H 7.98 . .
254 67 67 VAL C C 174.47 . .
255 67 67 VAL CA C 58.20 . .
256 67 67 VAL N N 110.80 . .
257 68 68 SER H H 8.50 . .
258 68 68 SER C C 176.25 . .
259 68 68 SER CA C 57.66 . .
260 68 68 SER N N 114.76 . .
261 69 69 GLU H H 9.32 . .
262 69 69 GLU C C 178.10 . .
263 69 69 GLU CA C 60.98 . .
264 69 69 GLU N N 126.75 . .
265 70 70 ALA H H 8.29 . .
266 70 70 ALA C C 179.24 . .
267 70 70 ALA CA C 55.33 . .
268 70 70 ALA N N 119.38 . .
269 71 71 TRP H H 7.67 . .
270 71 71 TRP C C 181.35 . .
271 71 71 TRP CA C 62.33 . .
272 71 71 TRP N N 119.33 . .
273 72 72 LEU H H 8.29 . .
274 72 72 LEU C C 177.08 . .
275 72 72 LEU CA C 57.70 . .
276 72 72 LEU N N 121.91 . .
277 73 73 MET H H 7.84 . .
278 73 73 MET C C 175.35 . .
279 73 73 MET CA C 57.38 . .
280 73 73 MET N N 115.13 . .
281 74 74 GLY H H 7.50 . .
282 74 74 GLY C C 174.02 . .
283 74 74 GLY CA C 44.02 . .
284 74 74 GLY N N 103.64 . .
285 75 75 PHE H H 7.61 . .
286 75 75 PHE C C 175.93 . .
287 75 75 PHE CA C 58.57 . .
288 75 75 PHE N N 118.53 . .
289 76 76 ASP H H 9.01 . .
290 76 76 ASP C C 174.68 . .
291 76 76 ASP CA C 53.73 . .
292 76 76 ASP N N 123.20 . .
293 77 77 VAL H H 7.64 . .
294 77 77 VAL C C 173.68 . .
295 77 77 VAL CA C 58.33 . .
296 77 77 VAL N N 117.46 . .
297 78 78 PRO C C 176.42 . .
298 78 78 PRO CA C 63.21 . .
299 79 79 MET H H 8.11 . .
300 79 79 MET C C 175.01 . .
301 79 79 MET CA C 58.81 . .
302 79 79 MET N N 121.49 . .
303 80 80 VAL H H 7.19 . .
304 80 80 VAL C C 175.65 . .
305 80 80 VAL CA C 60.77 . .
306 80 80 VAL N N 111.95 . .
307 81 81 GLU H H 8.43 . .
308 81 81 GLU C C 176.35 . .
309 81 81 GLU CA C 56.68 . .
310 81 81 GLU N N 124.85 . .
311 82 82 SER H H 8.35 . .
312 82 82 SER C C 174.56 . .
313 82 82 SER CA C 58.62 . .
314 82 82 SER N N 117.98 . .
315 83 83 SER H H 8.33 . .
316 83 83 SER C C 174.22 . .
317 83 83 SER CA C 58.62 . .
318 83 83 SER N N 117.97 . .
319 84 84 LYS H H 8.20 . .
320 84 84 LYS C C 176.22 . .
321 84 84 LYS CA C 56.46 . .
322 84 84 LYS N N 123.17 . .
323 85 85 ILE H H 8.10 . .
324 85 85 ILE C C 176.15 . .
325 85 85 ILE CA C 61.29 . .
326 85 85 ILE N N 122.45 . .
327 86 86 GLU H H 8.40 . .
328 86 86 GLU C C 175.96 . .
329 86 86 GLU CA C 56.65 . .
330 86 86 GLU N N 124.79 . .
331 87 87 ASN H H 8.43 . .
332 87 87 ASN C C 174.86 . .
333 87 87 ASN CA C 53.69 . .
334 87 87 ASN N N 119.91 . .
335 88 88 ASP H H 8.36 . .
336 88 88 ASP C C 176.31 . .
337 88 88 ASP CA C 54.95 . .
338 88 88 ASP N N 121.00 . .
339 89 89 SER H H 8.20 . .
340 89 89 SER C C 175.43 . .
341 89 89 SER CA C 58.22 . .
342 89 89 SER N N 115.10 . .
343 90 90 GLU H H 8.82 . .
344 90 90 GLU C C 178.00 . .
345 90 90 GLU CA C 59.27 . .
346 90 90 GLU N N 125.15 . .
347 91 91 ASN H H 8.46 . .
348 91 91 ASN C C 178.60 . .
349 91 91 ASN CA C 56.37 . .
350 91 91 ASN N N 115.80 . .
351 92 92 ILE H H 7.89 . .
352 92 92 ILE C C 176.70 . .
353 92 92 ILE CA C 65.94 . .
354 92 92 ILE N N 122.31 . .
355 93 93 GLU H H 8.16 . .
356 93 93 GLU C C 179.65 . .
357 93 93 GLU CA C 60.18 . .
358 93 93 GLU N N 119.83 . .
359 94 94 GLU H H 8.34 . .
360 94 94 GLU C C 178.48 . .
361 94 94 GLU CA C 59.59 . .
362 94 94 GLU N N 118.00 . .
363 95 95 THR H H 7.64 . .
364 95 95 THR C C 176.47 . .
365 95 95 THR CA C 68.39 . .
366 95 95 THR N N 117.00 . .
367 96 96 ILE H H 8.31 . .
368 96 96 ILE C C 177.09 . .
369 96 96 ILE CA C 66.01 . .
370 96 96 ILE N N 121.80 . .
371 97 97 THR H H 7.75 . .
372 97 97 THR C C 176.64 . .
373 97 97 THR CA C 66.85 . .
374 97 97 THR N N 114.95 . .
375 98 98 VAL H H 7.73 . .
376 98 98 VAL C C 178.39 . .
377 98 98 VAL CA C 66.60 . .
378 98 98 VAL N N 119.91 . .
379 99 99 MET H H 8.94 . .
380 99 99 MET C C 178.90 . .
381 99 99 MET CA C 60.43 . .
382 99 99 MET N N 117.19 . .
383 100 100 LYS H H 8.07 . .
384 100 100 LYS C C 177.69 . .
385 100 100 LYS CA C 59.48 . .
386 100 100 LYS N N 116.63 . .
387 101 101 LYS H H 7.63 . .
388 101 101 LYS C C 177.05 . .
389 101 101 LYS CA C 56.47 . .
390 101 101 LYS N N 116.61 . .
391 102 102 LEU H H 7.56 . .
392 102 102 LEU C C 177.42 . .
393 102 102 LEU CA C 54.08 . .
394 102 102 LEU N N 119.98 . .
395 103 103 GLU H H 9.06 . .
396 103 103 GLU C C 178.42 . .
397 103 103 GLU CA C 56.04 . .
398 103 103 GLU N N 121.46 . .
399 104 104 GLU H H 9.19 . .
400 104 104 GLU C C 174.94 . .
401 104 104 GLU CA C 62.70 . .
402 104 104 GLU N N 124.51 . .
403 105 105 PRO C C 179.71 . .
404 105 105 PRO CA C 66.10 . .
405 106 106 ARG H H 7.18 . .
406 106 106 ARG C C 178.76 . .
407 106 106 ARG CA C 59.36 . .
408 106 106 ARG N N 114.85 . .
409 107 107 GLN H H 8.06 . .
410 107 107 GLN C C 179.09 . .
411 107 107 GLN CA C 59.57 . .
412 107 107 GLN N N 118.94 . .
413 108 108 LYS H H 7.68 . .
414 108 108 LYS C C 177.55 . .
415 108 108 LYS CA C 59.59 . .
416 108 108 LYS N N 116.79 . .
417 109 109 VAL H H 7.01 . .
418 109 109 VAL C C 179.48 . .
419 109 109 VAL CA C 66.11 . .
420 109 109 VAL N N 118.64 . .
421 110 110 VAL H H 7.34 . .
422 110 110 VAL C C 176.93 . .
423 110 110 VAL CA C 67.44 . .
424 110 110 VAL N N 122.54 . .
425 111 111 LEU H H 7.90 . .
426 111 111 LEU C C 178.48 . .
427 111 111 LEU CA C 58.48 . .
428 111 111 LEU N N 121.88 . .
429 112 112 ASP H H 8.87 . .
430 112 112 ASP C C 179.55 . .
431 112 112 ASP CA C 57.96 . .
432 112 112 ASP N N 119.07 . .
433 113 113 THR H H 8.03 . .
434 113 113 THR C C 175.95 . .
435 113 113 THR CA C 67.39 . .
436 113 113 THR N N 117.24 . .
437 114 114 ALA H H 8.44 . .
438 114 114 ALA C C 178.48 . .
439 114 114 ALA CA C 56.10 . .
440 114 114 ALA N N 125.34 . .
441 115 115 LYS H H 8.50 . .
442 115 115 LYS C C 180.12 . .
443 115 115 LYS CA C 61.03 . .
444 115 115 LYS N N 116.85 . .
445 116 116 ILE H H 8.31 . .
446 116 116 ILE C C 178.61 . .
447 116 116 ILE CA C 64.96 . .
448 116 116 ILE N N 122.70 . .
449 117 117 GLN H H 8.28 . .
450 117 117 GLN C C 177.78 . .
451 117 117 GLN CA C 58.46 . .
452 117 117 GLN N N 118.81 . .
453 118 118 LEU H H 8.08 . .
454 118 118 LEU C C 177.77 . .
455 118 118 LEU CA C 57.89 . .
456 118 118 LEU N N 120.81 . .
457 119 119 LYS H H 7.80 . .
458 119 119 LYS C C 179.97 . .
459 119 119 LYS CA C 59.62 . .
460 119 119 LYS N N 119.78 . .
461 120 120 GLU H H 8.28 . .
462 120 120 GLU C C 179.31 . .
463 120 120 GLU CA C 59.43 . .
464 120 120 GLU N N 118.79 . .
465 121 121 GLN H H 8.43 . .
466 121 121 GLN C C 178.59 . .
467 121 121 GLN CA C 59.82 . .
468 121 121 GLN N N 122.37 . .
469 122 122 ASP H H 8.55 . .
470 122 122 ASP C C 178.46 . .
471 122 122 ASP CA C 57.11 . .
472 122 122 ASP N N 119.64 . .
473 123 123 ARG H H 7.80 . .
474 123 123 ARG C C 177.95 . .
475 123 123 ARG CA C 58.36 . .
476 123 123 ARG N N 118.97 . .
477 124 124 SER H H 7.92 . .
478 124 124 SER C C 174.89 . .
479 124 124 SER CA C 60.12 . .
480 124 124 SER N N 114.62 . .
stop_
save_