data_26822
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone 1H, 13C, and 15N Chemical Shift Assignments of Human integrin alpha1 I domain mutant E317A
;
_BMRB_accession_number 26822
_BMRB_flat_file_name bmr26822.str
_Entry_type original
_Submission_date 2016-06-20
_Accession_date 2016-06-20
_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 Nunes 'Ana Monica' . .
2 Zhu Jie . .
3 Jezioro Jacqueline . .
4 Minetti Conceicao A.S.A. .
5 Remeta David P. .
6 Farndale Richard W. .
7 Hamaia Samir W. .
8 Baum Jean . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 166
"13C chemical shifts" 475
"15N chemical shifts" 166
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2016-08-31 original BMRB .
stop_
_Original_release_date 2016-08-31
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Intrinsic local destabilization of the C-terminus predisposes integrin alpha1 I domain to a conformational switch induced by collagen binding
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 27342747
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Nunes 'Ana Monica' . .
2 Zhu Jie . .
3 Jezioro Jacqueline . .
4 Minetti Conceicao A.S.A. .
5 Remeta David P. .
6 Farndale Richard W. .
7 Hamaia Samir W. .
8 Baum Jean . .
stop_
_Journal_abbreviation 'Protein Sci.'
_Journal_volume 25
_Journal_issue 9
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1672
_Page_last 1681
_Year 2016
_Details .
loop_
_Keyword
NMR
'alpha1 I domain'
'binding energetics'
collagen
'conformational switch'
dynamics
'hydrogen-deuterium exchange'
integrin
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'a1I_E317A monomer'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
a1I_E317A $integrin_alpha1_I_domain_mutant_E317A
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_integrin_alpha1_I_domain_mutant_E317A
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common integrin_alpha1_I_domain_mutant_E317A
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 216
_Mol_residue_sequence
;
MNHHHHHHHHHHTSLYKKAG
FTQLDIVIVLDGSNSIYPWD
SVTAFLNDLLERMDIGPKQT
QVGIVQYGENVTHEFNLNKY
SSTEEVLVAAKKIVQRGGRQ
TMTALGIDTARKEAFTEARG
ARRGVKKVMVIVTDGESHDN
HRLKKVIQDCEDENIQRFSI
AILGSYNRGNLSTEKFVEEI
KSIASEPTEKHFFNVSDALA
LVTIVKTLGERIFALE
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 1 MET 2 2 ASN 3 3 HIS 4 4 HIS 5 5 HIS
6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS
11 11 HIS 12 12 HIS 13 13 THR 14 14 SER 15 15 LEU
16 16 TYR 17 17 LYS 18 18 LYS 19 19 ALA 20 20 GLY
21 21 PHE 22 141 THR 23 142 GLN 24 143 LEU 25 144 ASP
26 145 ILE 27 146 VAL 28 147 ILE 29 148 VAL 30 149 LEU
31 150 ASP 32 151 GLY 33 152 SER 34 153 ASN 35 154 SER
36 155 ILE 37 156 TYR 38 157 PRO 39 158 TRP 40 159 ASP
41 160 SER 42 161 VAL 43 162 THR 44 163 ALA 45 164 PHE
46 165 LEU 47 166 ASN 48 167 ASP 49 168 LEU 50 169 LEU
51 170 GLU 52 171 ARG 53 172 MET 54 173 ASP 55 174 ILE
56 175 GLY 57 176 PRO 58 177 LYS 59 178 GLN 60 179 THR
61 180 GLN 62 181 VAL 63 182 GLY 64 183 ILE 65 184 VAL
66 185 GLN 67 186 TYR 68 187 GLY 69 188 GLU 70 189 ASN
71 190 VAL 72 191 THR 73 192 HIS 74 193 GLU 75 194 PHE
76 195 ASN 77 196 LEU 78 197 ASN 79 198 LYS 80 199 TYR
81 200 SER 82 201 SER 83 202 THR 84 203 GLU 85 204 GLU
86 205 VAL 87 206 LEU 88 207 VAL 89 208 ALA 90 209 ALA
91 210 LYS 92 211 LYS 93 212 ILE 94 213 VAL 95 214 GLN
96 215 ARG 97 216 GLY 98 217 GLY 99 218 ARG 100 219 GLN
101 220 THR 102 221 MET 103 222 THR 104 223 ALA 105 224 LEU
106 225 GLY 107 226 ILE 108 227 ASP 109 228 THR 110 229 ALA
111 230 ARG 112 231 LYS 113 232 GLU 114 233 ALA 115 234 PHE
116 235 THR 117 236 GLU 118 237 ALA 119 238 ARG 120 239 GLY
121 240 ALA 122 241 ARG 123 242 ARG 124 243 GLY 125 244 VAL
126 245 LYS 127 246 LYS 128 247 VAL 129 248 MET 130 249 VAL
131 250 ILE 132 251 VAL 133 252 THR 134 253 ASP 135 254 GLY
136 255 GLU 137 256 SER 138 257 HIS 139 258 ASP 140 259 ASN
141 260 HIS 142 261 ARG 143 262 LEU 144 263 LYS 145 264 LYS
146 265 VAL 147 266 ILE 148 267 GLN 149 268 ASP 150 269 CYS
151 270 GLU 152 271 ASP 153 272 GLU 154 273 ASN 155 274 ILE
156 275 GLN 157 276 ARG 158 277 PHE 159 278 SER 160 279 ILE
161 280 ALA 162 281 ILE 163 282 LEU 164 283 GLY 165 284 SER
166 285 TYR 167 286 ASN 168 287 ARG 169 288 GLY 170 289 ASN
171 290 LEU 172 291 SER 173 292 THR 174 293 GLU 175 294 LYS
176 295 PHE 177 296 VAL 178 297 GLU 179 298 GLU 180 299 ILE
181 300 LYS 182 301 SER 183 302 ILE 184 303 ALA 185 304 SER
186 305 GLU 187 306 PRO 188 307 THR 189 308 GLU 190 309 LYS
191 310 HIS 192 311 PHE 193 312 PHE 194 313 ASN 195 314 VAL
196 315 SER 197 316 ASP 198 317 ALA 199 318 LEU 200 319 ALA
201 320 LEU 202 321 VAL 203 322 THR 204 323 ILE 205 324 VAL
206 325 LYS 207 326 THR 208 327 LEU 209 328 GLY 210 329 GLU
211 330 ARG 212 331 ILE 213 332 PHE 214 333 ALA 215 334 LEU
216 335 GLU
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
$integrin_alpha1_I_domain_mutant_E317A 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
$integrin_alpha1_I_domain_mutant_E317A 'recombinant technology' . Escherichia coli . pET_Dest_42
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
$integrin_alpha1_I_domain_mutant_E317A 0.45 mM '[U-99% 13C; U-99% 15N]'
'potassium phosphate' 50 mM 'natural abundance'
'sodium chloride' 140 mM 'natural abundance'
'Magnesium chloride' 5 mM 'natural abundance'
2-Mercaptoethanol 20 mM 'natural abundance'
H2O 95 % 'natural abundance'
D2O 5 % '[U-99% 2H]'
stop_
save_
############################
# Computer software used #
############################
save_CARA
_Saveframe_category software
_Name CARA
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Keller and Wuthrich' . .
stop_
loop_
_Task
'chemical shift assignment'
'peak picking'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model 'Avance III'
_Field_strength 700
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D_HNCO_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCO'
_Sample_label $sample_1
save_
save_3D_HCACO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HCACO'
_Sample_label $sample_1
save_
save_3D_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label $sample_1
save_
save_3D_CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_Sample_label $sample_1
save_
save_3D_HN(COCA)CB_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(COCA)CB'
_Sample_label $sample_1
save_
save_2D_1H-15N_HSQC_NH2_only_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC NH2 only'
_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' 0.46 . M
pH 7.0 . pH
pressure 1 . atm
temperature 273 . 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
'3D HNCO'
'3D HNCACB'
'3D CBCA(CO)NH'
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 a1I_E317A
_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 14 14 SER H H 8.108 0.020 1
2 14 14 SER C C 177.227 0.3 1
3 14 14 SER CA C 58.075 0.3 1
4 14 14 SER N N 118.743 0.3 1
5 15 15 LEU H H 7.789 0.020 1
6 15 15 LEU C C 176.924 0.3 1
7 15 15 LEU CA C 55.284 0.3 1
8 15 15 LEU CB C 41.649 0.3 1
9 15 15 LEU N N 124.218 0.3 1
10 16 16 TYR H H 7.551 0.020 1
11 16 16 TYR C C 175.476 0.3 1
12 16 16 TYR CA C 57.265 0.3 1
13 16 16 TYR CB C 38.153 0.3 1
14 16 16 TYR N N 119.838 0.3 1
15 17 17 LYS H H 7.736 0.020 1
16 17 17 LYS C C 176.083 0.3 1
17 17 17 LYS CA C 55.750 0.3 1
18 17 17 LYS CB C 32.327 0.3 1
19 17 17 LYS N N 123.105 0.3 1
20 18 18 LYS H H 7.868 0.020 1
21 18 18 LYS C C 175.943 0.3 1
22 18 18 LYS CA C 55.782 0.3 1
23 18 18 LYS CB C 32.308 0.3 1
24 18 18 LYS N N 122.882 0.3 1
25 19 19 ALA H H 7.947 0.020 1
26 19 19 ALA C C 177.741 0.3 1
27 19 19 ALA CA C 52.254 0.3 1
28 19 19 ALA CB C 18.926 0.3 1
29 19 19 ALA N N 125.629 0.3 1
30 20 20 GLY H H 7.939 0.020 1
31 20 20 GLY C C 173.609 0.3 1
32 20 20 GLY CA C 44.679 0.3 1
33 20 20 GLY N N 108.480 0.3 1
34 21 21 PHE H H 7.903 0.020 1
35 21 21 PHE C C 175.640 0.3 1
36 21 21 PHE CA C 57.498 0.3 1
37 21 21 PHE CB C 39.319 0.3 1
38 21 21 PHE N N 120.878 0.3 1
39 141 22 THR H H 7.835 0.020 1
40 141 22 THR C C 174.460 0.3 1
41 141 22 THR CA C 61.576 0.3 1
42 141 22 THR CB C 69.617 0.3 1
43 141 22 THR N N 115.384 0.3 1
44 142 23 GLN H H 7.516 0.020 1
45 142 23 GLN C C 172.955 0.3 1
46 142 23 GLN CA C 55.633 0.3 1
47 142 23 GLN CB C 28.714 0.3 1
48 142 23 GLN N N 124.218 0.3 1
49 143 24 LEU H H 7.040 0.020 1
50 143 24 LEU C C 174.893 0.3 1
51 143 24 LEU CA C 54.002 0.3 1
52 143 24 LEU CB C 46.544 0.3 1
53 143 24 LEU N N 123.550 0.3 1
54 144 25 ASP H H 8.405 0.020 1
55 144 25 ASP C C 173.306 0.3 1
56 144 25 ASP CA C 53.931 0.3 1
57 144 25 ASP CB C 41.649 0.3 1
58 144 25 ASP N N 126.074 0.3 1
59 145 26 ILE H H 8.643 0.020 1
60 145 26 ILE C C 174.169 0.3 1
61 145 26 ILE CA C 59.246 0.3 1
62 145 26 ILE CB C 39.901 0.3 1
63 145 26 ILE N N 124.515 0.3 1
64 146 27 VAL H H 8.731 0.020 1
65 146 27 VAL C C 175.196 0.3 1
66 146 27 VAL CA C 59.263 0.3 1
67 146 27 VAL CB C 33.492 0.3 1
68 146 27 VAL N N 125.703 0.3 1
69 147 28 ILE H H 8.211 0.020 1
70 147 28 ILE C C 173.119 0.3 1
71 147 28 ILE CA C 59.263 0.3 1
72 147 28 ILE CB C 37.571 0.3 1
73 147 28 ILE N N 128.821 0.3 1
74 148 29 VAL H H 9.435 0.020 1
75 148 29 VAL C C 173.772 0.3 1
76 148 29 VAL CA C 60.994 0.3 1
77 148 29 VAL CB C 31.744 0.3 1
78 148 29 VAL N N 131.122 0.3 1
79 149 30 LEU H H 8.852 0.020 1
80 149 30 LEU C C 173.991 0.3 1
81 149 30 LEU CA C 52.894 0.3 1
82 149 30 LEU CB C 45.045 0.3 1
83 149 30 LEU N N 125.978 0.3 1
84 150 31 ASP H H 7.738 0.020 1
85 150 31 ASP N N 126.210 0.3 1
86 159 40 ASP H H 8.317 0.020 1
87 159 40 ASP C C 178.277 0.3 1
88 159 40 ASP CA C 55.633 0.3 1
89 159 40 ASP CB C 39.319 0.3 1
90 159 40 ASP N N 115.236 0.3 1
91 160 41 SER H H 7.260 0.020 1
92 160 41 SER CA C 61.693 0.3 1
93 160 41 SER CB C 62.742 0.3 1
94 160 41 SER N N 116.442 0.3 1
95 161 42 VAL H H 7.102 0.020 1
96 161 42 VAL C C 177.904 0.3 1
97 161 42 VAL CA C 65.631 0.3 1
98 161 42 VAL CB C 29.494 0.3 1
99 161 42 VAL N N 126.445 0.3 1
100 162 43 THR H H 7.408 0.020 1
101 162 43 THR C C 177.670 0.3 1
102 162 43 THR CA C 65.705 0.3 1
103 162 43 THR CB C 67.170 0.3 1
104 162 43 THR N N 112.126 0.3 1
105 163 44 ALA H H 7.513 0.020 1
106 163 44 ALA C C 178.534 0.3 1
107 163 44 ALA CA C 55.190 0.3 1
108 163 44 ALA CB C 17.760 0.3 1
109 163 44 ALA N N 126.014 0.3 1
110 164 45 PHE H H 6.767 0.020 1
111 164 45 PHE C C 174.939 0.3 1
112 164 45 PHE CA C 60.061 0.3 1
113 164 45 PHE CB C 38.153 0.3 1
114 164 45 PHE N N 119.319 0.3 1
115 165 46 LEU H H 7.595 0.020 1
116 165 46 LEU C C 177.717 0.3 1
117 165 46 LEU CA C 56.915 0.3 1
118 165 46 LEU CB C 41.416 0.3 1
119 165 46 LEU N N 117.092 0.3 1
120 166 47 ASN H H 7.859 0.020 1
121 166 47 ASN C C 175.546 0.3 1
122 166 47 ASN CA C 56.967 0.3 1
123 166 47 ASN CB C 39.901 0.3 1
124 166 47 ASN N N 116.572 0.3 1
125 167 48 ASP H H 7.943 0.020 1
126 167 48 ASP C C 177.951 0.3 1
127 167 48 ASP CA C 56.216 0.3 1
128 167 48 ASP CB C 39.202 0.3 1
129 167 48 ASP N N 118.432 0.3 1
130 168 49 LEU H H 7.657 0.020 1
131 168 49 LEU C C 177.717 0.3 1
132 168 49 LEU CA C 56.915 0.3 1
133 168 49 LEU CB C 42.232 0.3 1
134 168 49 LEU N N 120.284 0.3 1
135 169 50 LEU H H 7.806 0.020 1
136 169 50 LEU C C 179.024 0.3 1
137 169 50 LEU CA C 56.893 0.3 1
138 169 50 LEU CB C 40.484 0.3 1
139 169 50 LEU N N 117.240 0.3 1
140 170 51 GLU H H 7.912 0.020 1
141 170 51 GLU C C 176.573 0.3 1
142 170 51 GLU CA C 58.080 0.3 1
143 170 51 GLU CB C 28.248 0.3 1
144 170 51 GLU N N 115.681 0.3 1
145 171 52 ARG H H 6.380 0.020 1
146 171 52 ARG C C 175.686 0.3 1
147 171 52 ARG CA C 55.050 0.3 1
148 171 52 ARG CB C 29.414 0.3 1
149 171 52 ARG N N 115.087 0.3 1
150 172 53 MET H H 7.393 0.020 1
151 172 53 MET C C 174.449 0.3 1
152 172 53 MET CA C 55.190 0.3 1
153 172 53 MET CB C 33.492 0.3 1
154 172 53 MET N N 119.170 0.3 1
155 173 54 ASP H H 8.845 0.020 1
156 173 54 ASP C C 173.539 0.3 1
157 173 54 ASP CA C 52.820 0.3 1
158 173 54 ASP CB C 39.935 0.3 1
159 173 54 ASP N N 125.702 0.3 1
160 174 55 ILE H H 6.873 0.020 1
161 174 55 ILE C C 176.407 0.3 1
162 174 55 ILE CA C 57.498 0.3 1
163 174 55 ILE CB C 36.988 0.3 1
164 174 55 ILE N N 124.664 0.3 1
165 175 56 GLY H H 8.528 0.020 1
166 175 56 GLY C C 172.629 0.3 1
167 175 56 GLY CA C 44.679 0.3 1
168 175 56 GLY N N 113.825 0.3 1
169 177 58 LYS H H 8.018 0.020 1
170 177 58 LYS C C 176.153 0.3 1
171 177 58 LYS CA C 54.118 0.3 1
172 177 58 LYS CB C 31.716 0.3 1
173 177 58 LYS N N 118.131 0.3 1
174 178 59 GLN H H 7.384 0.020 1
175 178 59 GLN C C 175.593 0.3 1
176 178 59 GLN CA C 54.597 0.3 1
177 178 59 GLN CB C 28.598 0.3 1
178 178 59 GLN N N 123.179 0.3 1
179 179 60 THR H H 8.423 0.020 1
180 179 60 THR C C 172.450 0.3 1
181 179 60 THR CA C 63.324 0.3 1
182 179 60 THR CB C 69.034 0.3 1
183 179 60 THR N N 126.090 0.3 1
184 180 61 GLN H H 8.511 0.020 1
185 180 61 GLN C C 173.982 0.3 1
186 180 61 GLN CA C 54.584 0.3 1
187 180 61 GLN CB C 32.909 0.3 1
188 180 61 GLN N N 123.699 0.3 1
189 181 62 VAL H H 7.780 0.020 1
190 181 62 VAL C C 173.282 0.3 1
191 181 62 VAL CA C 59.246 0.3 1
192 181 62 VAL CB C 35.823 0.3 1
193 181 62 VAL N N 119.963 0.3 1
194 182 63 GLY H H 8.388 0.020 1
195 182 63 GLY C C 171.975 0.3 1
196 182 63 GLY CA C 42.931 0.3 1
197 182 63 GLY N N 111.672 0.3 1
198 183 64 ILE H H 6.921 0.020 1
199 183 64 ILE C C 173.912 0.3 1
200 183 64 ILE CA C 60.411 0.3 1
201 183 64 ILE CB C 40.484 0.3 1
202 183 64 ILE N N 116.709 0.3 1
203 184 65 VAL H H 8.942 0.020 1
204 184 65 VAL C C 173.165 0.3 1
205 184 65 VAL CA C 59.411 0.3 1
206 184 65 VAL CB C 34.678 0.3 1
207 184 65 VAL N N 128.821 0.3 1
208 185 66 GLN H H 8.961 0.020 1
209 185 66 GLN C C 174.029 0.3 1
210 185 66 GLN CA C 52.836 0.3 1
211 185 66 GLN CB C 31.511 0.3 1
212 185 66 GLN N N 126.776 0.3 1
213 186 67 TYR H H 9.161 0.020 1
214 186 67 TYR C C 172.115 0.3 1
215 186 67 TYR CA C 54.584 0.3 1
216 186 67 TYR CB C 43.416 0.3 1
217 186 67 TYR N N 126.286 0.3 1
218 187 68 GLY H H 7.483 0.020 1
219 187 68 GLY C C 173.306 0.3 1
220 187 68 GLY CA C 47.414 0.3 1
221 187 68 GLY N N 110.748 0.3 1
222 188 69 GLU H H 8.601 0.020 1
223 188 69 GLU C C 174.992 0.3 1
224 188 69 GLU CA C 57.485 0.3 1
225 188 69 GLU CB C 29.938 0.3 1
226 188 69 GLU N N 127.671 0.3 1
227 189 70 ASN H H 7.450 0.020 1
228 189 70 ASN C C 173.912 0.3 1
229 189 70 ASN CA C 50.506 0.3 1
230 189 70 ASN CB C 40.484 0.3 1
231 189 70 ASN N N 114.876 0.3 1
232 190 71 VAL H H 8.388 0.020 1
233 190 71 VAL C C 174.589 0.3 1
234 190 71 VAL CA C 61.576 0.3 1
235 190 71 VAL CB C 33.026 0.3 1
236 190 71 VAL N N 119.764 0.3 1
237 191 72 THR H H 8.801 0.020 1
238 191 72 THR C C 173.282 0.3 1
239 191 72 THR CA C 61.576 0.3 1
240 191 72 THR CB C 71.598 0.3 1
241 191 72 THR N N 123.624 0.3 1
242 192 73 HIS H H 8.713 0.020 1
243 192 73 HIS C C 175.406 0.3 1
244 192 73 HIS CA C 55.983 0.3 1
245 192 73 HIS CB C 29.996 0.3 1
246 192 73 HIS N N 127.626 0.3 1
247 193 74 GLU H H 8.582 0.020 1
248 193 74 GLU C C 178.768 0.3 1
249 193 74 GLU CA C 57.859 0.3 1
250 193 74 GLU CB C 27.816 0.3 1
251 193 74 GLU N N 129.044 0.3 1
252 194 75 PHE H H 6.917 0.020 1
253 194 75 PHE C C 174.052 0.3 1
254 194 75 PHE CA C 56.301 0.3 1
255 194 75 PHE CB C 39.901 0.3 1
256 194 75 PHE N N 107.367 0.3 1
257 195 76 ASN H H 7.983 0.020 1
258 195 76 ASN C C 176.153 0.3 1
259 195 76 ASN CA C 51.205 0.3 1
260 195 76 ASN CB C 38.736 0.3 1
261 195 76 ASN N N 120.642 0.3 1
262 196 77 LEU H H 8.888 0.020 1
263 196 77 LEU C C 175.943 0.3 1
264 196 77 LEU CA C 57.731 0.3 1
265 196 77 LEU CB C 42.897 0.3 1
266 196 77 LEU N N 124.218 0.3 1
267 197 78 ASN H H 7.093 0.020 1
268 197 78 ASN C C 176.854 0.3 1
269 197 78 ASN CA C 50.111 0.3 1
270 197 78 ASN CB C 37.905 0.3 1
271 197 78 ASN N N 109.594 0.3 1
272 198 79 LYS H H 7.525 0.020 1
273 198 79 LYS C C 176.177 0.3 1
274 198 79 LYS CA C 58.663 0.3 1
275 198 79 LYS CB C 31.977 0.3 1
276 198 79 LYS N N 123.030 0.3 1
277 199 80 TYR H H 8.458 0.020 1
278 199 80 TYR C C 176.273 0.3 1
279 199 80 TYR CA C 56.332 0.3 1
280 199 80 TYR CB C 39.901 0.3 1
281 199 80 TYR N N 116.572 0.3 1
282 200 81 SER H H 8.661 0.020 1
283 200 81 SER C C 171.718 0.3 1
284 200 81 SER CA C 56.819 0.3 1
285 200 81 SER CB C 63.907 0.3 1
286 200 81 SER N N 115.161 0.3 1
287 201 82 SER H H 6.979 0.020 1
288 201 82 SER C C 174.216 0.3 1
289 201 82 SER CA C 56.332 0.3 1
290 201 82 SER CB C 66.354 0.3 1
291 201 82 SER N N 112.334 0.3 1
292 202 83 THR H H 8.978 0.020 1
293 202 83 THR C C 175.430 0.3 1
294 202 83 THR CA C 66.937 0.3 1
295 202 83 THR CB C 68.685 0.3 1
296 202 83 THR N N 121.768 0.3 1
297 203 84 GLU H H 8.661 0.020 1
298 203 84 GLU C C 178.604 0.3 1
299 203 84 GLU CA C 59.828 0.3 1
300 203 84 GLU CB C 28.481 0.3 1
301 203 84 GLU N N 120.506 0.3 1
302 204 85 GLU H H 7.027 0.020 1
303 204 85 GLU C C 179.001 0.3 1
304 204 85 GLU CA C 58.663 0.3 1
305 204 85 GLU CB C 29.996 0.3 1
306 204 85 GLU N N 115.978 0.3 1
307 205 86 VAL H H 7.032 0.020 1
308 205 86 VAL C C 176.433 0.3 1
309 205 86 VAL CA C 65.072 0.3 1
310 205 86 VAL CB C 31.144 0.3 1
311 205 86 VAL N N 120.080 0.3 1
312 206 87 LEU H H 7.762 0.020 1
313 206 87 LEU C C 179.911 0.3 1
314 206 87 LEU CA C 57.381 0.3 1
315 206 87 LEU CB C 40.484 0.3 1
316 206 87 LEU N N 120.358 0.3 1
317 207 88 VAL H H 6.750 0.020 1
318 207 88 VAL C C 177.927 0.3 1
319 207 88 VAL CA C 65.655 0.3 1
320 207 88 VAL CB C 31.162 0.3 1
321 207 88 VAL N N 118.799 0.3 1
322 208 89 ALA H H 6.635 0.020 1
323 208 89 ALA C C 181.499 0.3 1
324 208 89 ALA CA C 54.118 0.3 1
325 208 89 ALA CB C 19.508 0.3 1
326 208 89 ALA N N 120.952 0.3 1
327 209 90 ALA H H 8.599 0.020 1
328 209 90 ALA C C 178.091 0.3 1
329 209 90 ALA CA C 54.597 0.3 1
330 209 90 ALA CB C 17.178 0.3 1
331 209 90 ALA N N 121.620 0.3 1
332 210 91 LYS H H 6.741 0.020 1
333 210 91 LYS C C 177.344 0.3 1
334 210 91 LYS CA C 57.498 0.3 1
335 210 91 LYS CB C 31.861 0.3 1
336 210 91 LYS N N 112.934 0.3 1
337 211 92 LYS H H 6.944 0.020 1
338 211 92 LYS C C 176.620 0.3 1
339 211 92 LYS CA C 55.284 0.3 1
340 211 92 LYS CB C 32.367 0.3 1
341 211 92 LYS N N 116.201 0.3 1
342 212 93 ILE H H 6.820 0.020 1
343 212 93 ILE C C 175.290 0.3 1
344 212 93 ILE CA C 62.742 0.3 1
345 212 93 ILE CB C 36.988 0.3 1
346 212 93 ILE N N 121.472 0.3 1
347 213 94 VAL H H 8.167 0.020 1
348 213 94 VAL C C 173.726 0.3 1
349 213 94 VAL CA C 59.246 0.3 1
350 213 94 VAL CB C 33.058 0.3 1
351 213 94 VAL N N 129.044 0.3 1
352 214 95 GLN H H 7.331 0.020 1
353 214 95 GLN C C 177.250 0.3 1
354 214 95 GLN CA C 55.167 0.3 1
355 214 95 GLN CB C 26.617 0.3 1
356 214 95 GLN N N 124.589 0.3 1
357 215 96 ARG H H 9.242 0.020 1
358 215 96 ARG C C 177.764 0.3 1
359 215 96 ARG CA C 56.915 0.3 1
360 215 96 ARG CB C 29.414 0.3 1
361 215 96 ARG N N 129.860 0.3 1
362 216 97 GLY H H 7.094 0.020 1
363 216 97 GLY C C 173.679 0.3 1
364 216 97 GLY CA C 45.145 0.3 1
365 216 97 GLY N N 108.222 0.3 1
366 217 98 GLY H H 7.399 0.020 1
367 217 98 GLY C C 173.656 0.3 1
368 217 98 GLY CA C 44.679 0.3 1
369 217 98 GLY N N 106.804 0.3 1
370 219 100 GLN H H 7.299 0.020 1
371 219 100 GLN C C 174.029 0.3 1
372 219 100 GLN CA C 51.205 0.3 1
373 219 100 GLN N N 117.483 0.3 1
374 225 106 GLY H H 8.167 0.020 1
375 225 106 GLY C C 173.936 0.3 1
376 225 106 GLY CA C 46.660 0.3 1
377 225 106 GLY N N 110.784 0.3 1
378 226 107 ILE H H 7.921 0.020 1
379 226 107 ILE C C 177.437 0.3 1
380 226 107 ILE CA C 65.631 0.3 1
381 226 107 ILE CB C 38.232 0.3 1
382 226 107 ILE N N 121.472 0.3 1
383 227 108 ASP H H 8.546 0.020 1
384 227 108 ASP C C 178.651 0.3 1
385 227 108 ASP CA C 57.032 0.3 1
386 227 108 ASP CB C 42.232 0.3 1
387 227 108 ASP N N 119.838 0.3 1
388 228 109 THR H H 8.074 0.020 1
389 228 109 THR CA C 66.937 0.3 1
390 228 109 THR CB C 67.636 0.3 1
391 228 109 THR N N 113.751 0.3 1
392 229 110 ALA H H 7.859 0.020 1
393 229 110 ALA C C 178.114 0.3 1
394 229 110 ALA CA C 55.167 0.3 1
395 229 110 ALA CB C 17.760 0.3 1
396 229 110 ALA N N 126.371 0.3 1
397 230 111 ARG H H 8.256 0.020 1
398 230 111 ARG C C 177.250 0.3 1
399 230 111 ARG CA C 60.411 0.3 1
400 230 111 ARG CB C 29.180 0.3 1
401 230 111 ARG N N 117.908 0.3 1
402 231 112 LYS H H 8.141 0.020 1
403 231 112 LYS C C 176.994 0.3 1
404 231 112 LYS CA C 58.080 0.3 1
405 231 112 LYS CB C 33.492 0.3 1
406 231 112 LYS N N 114.493 0.3 1
407 232 113 GLU H H 8.115 0.020 1
408 232 113 GLU C C 177.390 0.3 1
409 232 113 GLU CA C 56.449 0.3 1
410 232 113 GLU CB C 31.861 0.3 1
411 232 113 GLU N N 113.751 0.3 1
412 233 114 ALA H H 7.833 0.020 1
413 233 114 ALA C C 177.857 0.3 1
414 233 114 ALA CA C 55.167 0.3 1
415 233 114 ALA CB C 18.926 0.3 1
416 233 114 ALA N N 122.132 0.3 1
417 234 115 PHE H H 6.855 0.020 1
418 234 115 PHE C C 174.986 0.3 1
419 234 115 PHE CA C 57.148 0.3 1
420 234 115 PHE CB C 36.405 0.3 1
421 234 115 PHE N N 113.596 0.3 1
422 235 116 THR H H 6.750 0.020 1
423 235 116 THR C C 176.340 0.3 1
424 235 116 THR CA C 58.780 0.3 1
425 235 116 THR CB C 71.598 0.3 1
426 235 116 THR N N 107.292 0.3 1
427 236 117 GLU H H 8.883 0.020 1
428 236 117 GLU C C 180.612 0.3 1
429 236 117 GLU CB C 29.439 0.3 1
430 236 117 GLU N N 126.864 0.3 1
431 237 118 ALA H H 8.274 0.020 1
432 237 118 ALA C C 179.048 0.3 1
433 237 118 ALA CA C 54.002 0.3 1
434 237 118 ALA CB C 17.760 0.3 1
435 237 118 ALA N N 121.895 0.3 1
436 238 119 ARG H H 6.803 0.020 1
437 238 119 ARG C C 173.702 0.3 1
438 238 119 ARG CA C 55.866 0.3 1
439 238 119 ARG CB C 28.902 0.3 1
440 238 119 ARG N N 115.607 0.3 1
441 239 120 GLY H H 7.216 0.020 1
442 239 120 GLY C C 173.847 0.3 1
443 239 120 GLY CA C 45.262 0.3 1
444 239 120 GLY N N 103.284 0.3 1
445 240 121 ALA H H 7.542 0.020 1
446 240 121 ALA C C 177.881 0.3 1
447 240 121 ALA CA C 52.254 0.3 1
448 240 121 ALA CB C 17.178 0.3 1
449 240 121 ALA N N 124.738 0.3 1
450 241 122 ARG H H 9.172 0.020 1
451 241 122 ARG C C 176.387 0.3 1
452 241 122 ARG CA C 54.584 0.3 1
453 241 122 ARG CB C 31.744 0.3 1
454 241 122 ARG N N 126.445 0.3 1
455 242 123 ARG H H 8.308 0.020 1
456 242 123 ARG C C 177.974 0.3 1
457 242 123 ARG CA C 56.915 0.3 1
458 242 123 ARG CB C 29.414 0.3 1
459 242 123 ARG N N 125.035 0.3 1
460 243 124 GLY H H 8.712 0.020 1
461 243 124 GLY C C 179.169 0.3 1
462 243 124 GLY CA C 45.448 0.3 1
463 243 124 GLY N N 113.818 0.3 1
464 244 125 VAL H H 7.032 0.020 1
465 244 125 VAL C C 175.756 0.3 1
466 244 125 VAL CA C 60.994 0.3 1
467 244 125 VAL CB C 31.162 0.3 1
468 244 125 VAL N N 119.881 0.3 1
469 245 126 LYS H H 8.097 0.020 1
470 245 126 LYS C C 173.819 0.3 1
471 245 126 LYS CA C 56.915 0.3 1
472 245 126 LYS CB C 32.560 0.3 1
473 245 126 LYS N N 129.563 0.3 1
474 246 127 LYS H H 8.071 0.020 1
475 246 127 LYS C C 175.967 0.3 1
476 246 127 LYS CA C 54.701 0.3 1
477 246 127 LYS CB C 34.191 0.3 1
478 246 127 LYS N N 125.154 0.3 1
479 247 128 VAL H H 8.705 0.020 1
480 247 128 VAL C C 173.586 0.3 1
481 247 128 VAL CA C 59.945 0.3 1
482 247 128 VAL CB C 35.823 0.3 1
483 247 128 VAL N N 123.996 0.3 1
484 248 129 MET H H 9.427 0.020 1
485 248 129 MET C C 174.846 0.3 1
486 248 129 MET CA C 53.069 0.3 1
487 248 129 MET CB C 38.386 0.3 1
488 248 129 MET N N 127.410 0.3 1
489 249 130 VAL H H 8.233 0.020 1
490 249 130 VAL C C 173.796 0.3 1
491 249 130 VAL CA C 60.411 0.3 1
492 249 130 VAL CB C 33.492 0.3 1
493 249 130 VAL N N 125.907 0.3 1
494 250 131 ILE H H 8.872 0.020 1
495 250 131 ILE C C 173.796 0.3 1
496 250 131 ILE CA C 60.447 0.3 1
497 250 131 ILE CB C 41.067 0.3 1
498 250 131 ILE N N 129.266 0.3 1
499 251 132 VAL H H 8.203 0.020 1
500 251 132 VAL C C 171.998 0.3 1
501 251 132 VAL CA C 55.190 0.3 1
502 251 132 VAL CB C 31.590 0.3 1
503 251 132 VAL N N 127.188 0.3 1
504 261 142 ARG H H 7.047 0.020 1
505 261 142 ARG CA C 55.633 0.3 1
506 261 142 ARG CB C 30.975 0.3 1
507 261 142 ARG N N 119.070 0.3 1
508 262 143 LEU H H 6.999 0.020 1
509 262 143 LEU C C 176.765 0.3 1
510 262 143 LEU CA C 58.078 0.3 1
511 262 143 LEU CB C 41.712 0.3 1
512 262 143 LEU N N 120.210 0.3 1
513 263 144 LYS H H 8.079 0.020 1
514 263 144 LYS C C 179.128 0.3 1
515 263 144 LYS CA C 59.828 0.3 1
516 263 144 LYS CB C 31.162 0.3 1
517 263 144 LYS N N 118.057 0.3 1
518 264 145 LYS H H 7.489 0.020 1
519 264 145 LYS C C 177.174 0.3 1
520 264 145 LYS CA C 57.614 0.3 1
521 264 145 LYS CB C 31.271 0.3 1
522 264 145 LYS N N 120.878 0.3 1
523 265 146 VAL H H 7.454 0.020 1
524 265 146 VAL C C 179.447 0.3 1
525 265 146 VAL CA C 65.189 0.3 1
526 265 146 VAL CB C 31.744 0.3 1
527 265 146 VAL N N 119.022 0.3 1
528 266 147 ILE H H 8.423 0.020 1
529 266 147 ILE C C 177.628 0.3 1
530 266 147 ILE CA C 63.324 0.3 1
531 266 147 ILE CB C 35.240 0.3 1
532 266 147 ILE N N 121.249 0.3 1
533 267 148 GLN H H 7.595 0.020 1
534 267 148 GLN C C 178.128 0.3 1
535 267 148 GLN CA C 58.080 0.3 1
536 267 148 GLN CB C 27.199 0.3 1
537 267 148 GLN N N 122.214 0.3 1
538 268 149 ASP H H 8.247 0.020 1
539 268 149 ASP C C 179.310 0.3 1
540 268 149 ASP CA C 57.498 0.3 1
541 268 149 ASP CB C 38.736 0.3 1
542 268 149 ASP N N 120.432 0.3 1
543 269 150 CYS H H 7.401 0.020 1
544 269 150 CYS C C 176.583 0.3 1
545 269 150 CYS CA C 63.907 0.3 1
546 269 150 CYS CB C 27.083 0.3 1
547 269 150 CYS N N 116.795 0.3 1
548 270 151 GLU H H 8.269 0.020 1
549 270 151 GLU C C 180.674 0.3 1
550 270 151 GLU CA C 58.663 0.3 1
551 270 151 GLU CB C 28.365 0.3 1
552 270 151 GLU N N 124.178 0.3 1
553 271 152 ASP H H 8.555 0.020 1
554 271 152 ASP C C 177.460 0.3 1
555 271 152 ASP CA C 56.332 0.3 1
556 271 152 ASP CB C 39.319 0.3 1
557 271 152 ASP N N 122.734 0.3 1
558 272 153 GLU H H 6.785 0.020 1
559 272 153 GLU C C 174.566 0.3 1
560 272 153 GLU CA C 55.750 0.3 1
561 272 153 GLU CB C 28.947 0.3 1
562 272 153 GLU N N 117.537 0.3 1
563 273 154 ASN H H 7.745 0.020 1
564 273 154 ASN C C 174.654 0.3 1
565 273 154 ASN CA C 54.002 0.3 1
566 273 154 ASN CB C 36.405 0.3 1
567 273 154 ASN N N 115.161 0.3 1
568 274 155 ILE H H 7.393 0.020 1
569 274 155 ILE C C 174.869 0.3 1
570 274 155 ILE CA C 60.994 0.3 1
571 274 155 ILE CB C 38.270 0.3 1
572 274 155 ILE N N 119.913 0.3 1
573 275 156 GLN H H 7.947 0.020 1
574 275 156 GLN C C 175.033 0.3 1
575 275 156 GLN CA C 55.633 0.3 1
576 275 156 GLN CB C 28.831 0.3 1
577 275 156 GLN N N 132.904 0.3 1
578 276 157 ARG H H 8.853 0.020 1
579 276 157 ARG C C 175.220 0.3 1
580 276 157 ARG CA C 55.116 0.3 1
581 276 157 ARG CB C 30.605 0.3 1
582 276 157 ARG N N 125.509 0.3 1
583 277 158 PHE H H 8.898 0.020 1
584 277 158 PHE C C 175.103 0.3 1
585 277 158 PHE CA C 56.332 0.3 1
586 277 158 PHE CB C 41.183 0.3 1
587 277 158 PHE N N 123.105 0.3 1
588 278 159 SER H H 9.189 0.020 1
589 278 159 SER C C 171.532 0.3 1
590 278 159 SER CA C 55.167 0.3 1
591 278 159 SER CB C 66.820 0.3 1
592 278 159 SER N N 118.131 0.3 1
593 279 160 ILE H H 8.625 0.020 1
594 279 160 ILE C C 173.539 0.3 1
595 279 160 ILE CA C 59.364 0.3 1
596 279 160 ILE CB C 39.905 0.3 1
597 279 160 ILE N N 123.253 0.3 1
598 280 161 ALA H H 8.194 0.020 1
599 280 161 ALA C C 175.523 0.3 1
600 280 161 ALA CA C 49.340 0.3 1
601 280 161 ALA CB C 19.497 0.3 1
602 280 161 ALA N N 127.703 0.3 1
603 281 162 ILE H H 8.472 0.020 1
604 281 162 ILE C C 177.180 0.3 1
605 281 162 ILE CA C 54.597 0.3 1
606 281 162 ILE CB C 32.974 0.3 1
607 281 162 ILE N N 123.536 0.3 1
608 282 163 LEU H H 8.395 0.020 1
609 282 163 LEU CA C 56.301 0.3 1
610 282 163 LEU CB C 41.105 0.3 1
611 282 163 LEU N N 126.634 0.3 1
612 293 174 GLU H H 7.785 0.020 1
613 293 174 GLU C C 178.436 0.3 1
614 293 174 GLU CA C 60.003 0.3 1
615 293 174 GLU CB C 28.828 0.3 1
616 293 174 GLU N N 122.642 0.3 1
617 294 175 LYS H H 7.940 0.020 1
618 294 175 LYS C C 178.931 0.3 1
619 294 175 LYS CA C 58.663 0.3 1
620 294 175 LYS CB C 31.162 0.3 1
621 294 175 LYS N N 120.134 0.3 1
622 295 176 PHE H H 7.824 0.020 1
623 295 176 PHE C C 176.013 0.3 1
624 295 176 PHE CA C 58.684 0.3 1
625 295 176 PHE CB C 38.432 0.3 1
626 295 176 PHE N N 122.437 0.3 1
627 296 177 VAL H H 8.115 0.020 1
628 296 177 VAL C C 177.265 0.3 1
629 296 177 VAL CA C 66.937 0.3 1
630 296 177 VAL CB C 30.579 0.3 1
631 296 177 VAL N N 119.096 0.3 1
632 297 178 GLU H H 7.428 0.020 1
633 297 178 GLU C C 178.931 0.3 1
634 297 178 GLU CA C 58.780 0.3 1
635 297 178 GLU CB C 28.831 0.3 1
636 297 178 GLU N N 117.908 0.3 1
637 298 179 GLU H H 7.727 0.020 1
638 298 179 GLU C C 179.211 0.3 1
639 298 179 GLU CA C 59.353 0.3 1
640 298 179 GLU CB C 29.245 0.3 1
641 298 179 GLU N N 121.917 0.3 1
642 299 180 ILE H H 7.909 0.020 1
643 299 180 ILE C C 180.331 0.3 1
644 299 180 ILE CA C 61.576 0.3 1
645 299 180 ILE CB C 32.974 0.3 1
646 299 180 ILE N N 120.033 0.3 1
647 300 181 LYS H H 8.273 0.020 1
648 300 181 LYS C C 178.231 0.3 1
649 300 181 LYS CA C 59.945 0.3 1
650 300 181 LYS CB C 31.744 0.3 1
651 300 181 LYS N N 126.000 0.3 1
652 301 182 SER H H 7.151 0.020 1
653 301 182 SER C C 174.654 0.3 1
654 301 182 SER CA C 60.411 0.3 1
655 301 182 SER CB C 62.159 0.3 1
656 301 182 SER N N 113.935 0.3 1
657 302 183 ILE H H 6.828 0.020 1
658 302 183 ILE C C 175.266 0.3 1
659 302 183 ILE CA C 62.742 0.3 1
660 302 183 ILE CB C 38.736 0.3 1
661 302 183 ILE N N 121.805 0.3 1
662 303 184 ALA H H 6.591 0.020 1
663 303 184 ALA C C 178.137 0.3 1
664 303 184 ALA CA C 51.671 0.3 1
665 303 184 ALA CB C 18.809 0.3 1
666 303 184 ALA N N 122.511 0.3 1
667 304 185 SER H H 8.245 0.020 1
668 304 185 SER CA C 61.632 0.3 1
669 304 185 SER CB C 61.632 0.3 1
670 304 185 SER N N 121.798 0.3 1
671 305 186 GLU H H 7.815 0.020 1
672 305 186 GLU C C 176.363 0.3 1
673 305 186 GLU CA C 53.487 0.3 1
674 305 186 GLU CB C 28.754 0.3 1
675 305 186 GLU N N 118.502 0.3 1
676 308 189 GLU H H 9.048 0.020 1
677 308 189 GLU C C 177.344 0.3 1
678 308 189 GLU CA C 58.663 0.3 1
679 308 189 GLU CB C 28.248 0.3 1
680 308 189 GLU N N 119.690 0.3 1
681 309 190 LYS H H 6.821 0.020 1
682 309 190 LYS C C 175.850 0.3 1
683 309 190 LYS CA C 55.750 0.3 1
684 309 190 LYS CB C 33.123 0.3 1
685 309 190 LYS N N 115.436 0.3 1
686 310 191 HIS H H 6.793 0.020 1
687 310 191 HIS C C 172.115 0.3 1
688 310 191 HIS CA C 57.485 0.3 1
689 310 191 HIS CB C 31.123 0.3 1
690 310 191 HIS N N 115.289 0.3 1
691 311 192 PHE H H 7.489 0.020 1
692 311 192 PHE CA C 55.190 0.3 1
693 311 192 PHE CB C 41.120 0.3 1
694 311 192 PHE N N 120.210 0.3 1
695 313 194 ASN H H 8.002 0.020 1
696 313 194 ASN C C 173.959 0.3 1
697 313 194 ASN CA C 51.088 0.3 1
698 313 194 ASN CB C 40.834 0.3 1
699 313 194 ASN N N 117.847 0.3 1
700 314 195 VAL H H 8.335 0.020 1
701 314 195 VAL C C 175.850 0.3 1
702 314 195 VAL CA C 58.596 0.3 1
703 314 195 VAL CB C 34.604 0.3 1
704 314 195 VAL N N 116.943 0.3 1
705 315 196 SER H H 8.511 0.020 1
706 315 196 SER CA C 61.632 0.3 1
707 315 196 SER CB C 62.595 0.3 1
708 315 196 SER N N 118.576 0.3 1
709 316 197 ASP H H 6.992 0.020 1
710 316 197 ASP C C 175.360 0.3 1
711 316 197 ASP CA C 52.836 0.3 1
712 316 197 ASP CB C 42.232 0.3 1
713 316 197 ASP N N 114.048 0.3 1
714 317 198 ALA H H 8.740 0.020 1
715 317 198 ALA C C 179.538 0.3 1
716 317 198 ALA CA C 54.667 0.3 1
717 317 198 ALA CB C 17.050 0.3 1
718 317 198 ALA N N 122.734 0.3 1
719 318 199 LEU H H 7.639 0.020 1
720 318 199 LEU C C 178.114 0.3 1
721 318 199 LEU CA C 57.559 0.3 1
722 318 199 LEU CB C 40.454 0.3 1
723 318 199 LEU N N 118.576 0.3 1
724 319 200 ALA H H 7.285 0.020 1
725 319 200 ALA C C 179.768 0.3 1
726 319 200 ALA CA C 51.088 0.3 1
727 319 200 ALA CB C 18.926 0.3 1
728 319 200 ALA N N 118.129 0.3 1
729 320 201 LEU H H 7.648 0.020 1
730 320 201 LEU C C 177.997 0.3 1
731 320 201 LEU CA C 58.663 0.3 1
732 320 201 LEU CB C 39.901 0.3 1
733 320 201 LEU N N 124.738 0.3 1
734 321 202 VAL H H 7.084 0.020 1
735 321 202 VAL C C 177.868 0.3 1
736 321 202 VAL CA C 64.490 0.3 1
737 321 202 VAL CB C 31.162 0.3 1
738 321 202 VAL N N 108.521 0.3 1
739 322 203 THR H H 7.498 0.020 1
740 322 203 THR C C 176.620 0.3 1
741 322 203 THR CA C 63.790 0.3 1
742 322 203 THR CB C 69.267 0.3 1
743 322 203 THR N N 111.450 0.3 1
744 323 204 ILE H H 6.891 0.020 1
745 323 204 ILE C C 175.756 0.3 1
746 323 204 ILE CA C 60.411 0.3 1
747 323 204 ILE CB C 38.153 0.3 1
748 323 204 ILE N N 113.009 0.3 1
749 324 205 VAL H H 6.659 0.020 1
750 324 205 VAL C C 176.760 0.3 1
751 324 205 VAL CA C 66.937 0.3 1
752 324 205 VAL CB C 31.162 0.3 1
753 324 205 VAL N N 120.878 0.3 1
754 325 206 LYS H H 8.203 0.020 1
755 325 206 LYS C C 178.552 0.3 1
756 325 206 LYS CA C 59.828 0.3 1
757 325 206 LYS CB C 31.162 0.3 1
758 325 206 LYS N N 121.843 0.3 1
759 326 207 THR H H 7.639 0.020 1
760 326 207 THR C C 175.710 0.3 1
761 326 207 THR CA C 65.655 0.3 1
762 326 207 THR CB C 68.102 0.3 1
763 326 207 THR N N 116.572 0.3 1
764 327 208 LEU H H 8.150 0.020 1
765 327 208 LEU C C 177.689 0.3 1
766 327 208 LEU CA C 58.080 0.3 1
767 327 208 LEU CB C 40.484 0.3 1
768 327 208 LEU N N 122.214 0.3 1
769 328 209 GLY H H 8.159 0.020 1
770 328 209 GLY C C 175.243 0.3 1
771 328 209 GLY CA C 47.010 0.3 1
772 328 209 GLY N N 104.917 0.3 1
773 329 210 GLU H H 7.532 0.020 1
774 329 210 GLU C C 179.398 0.3 1
775 329 210 GLU CA C 58.670 0.3 1
776 329 210 GLU CB C 28.831 0.3 1
777 329 210 GLU N N 119.842 0.3 1
778 330 211 ARG H H 7.710 0.020 1
779 330 211 ARG C C 178.954 0.3 1
780 330 211 ARG CA C 58.197 0.3 1
781 330 211 ARG CB C 30.462 0.3 1
782 330 211 ARG N N 118.205 0.3 1
783 331 212 ILE H H 7.877 0.020 1
784 331 212 ILE C C 176.134 0.3 1
785 331 212 ILE CA C 65.538 0.3 1
786 331 212 ILE CB C 37.571 0.3 1
787 331 212 ILE N N 121.148 0.3 1
788 332 213 PHE H H 6.842 0.020 1
789 332 213 PHE C C 174.869 0.3 1
790 332 213 PHE CA C 58.663 0.3 1
791 332 213 PHE CB C 38.153 0.3 1
792 332 213 PHE N N 113.119 0.3 1
793 333 214 ALA H H 7.064 0.020 1
794 333 214 ALA C C 177.414 0.3 1
795 333 214 ALA CA C 52.254 0.3 1
796 333 214 ALA CB C 18.343 0.3 1
797 333 214 ALA N N 122.711 0.3 1
798 334 215 LEU H H 8.000 0.020 1
799 334 215 LEU C C 176.363 0.3 1
800 334 215 LEU CA C 55.167 0.3 1
801 334 215 LEU CB C 41.766 0.3 1
802 334 215 LEU N N 121.768 0.3 1
803 335 216 GLU H H 7.489 0.020 1
804 335 216 GLU C C 180.682 0.3 1
805 335 216 GLU CA C 57.381 0.3 1
806 335 216 GLU CB C 31.162 0.3 1
807 335 216 GLU N N 125.703 0.3 1
stop_
save_