data_17499
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solid-state NMR assignment of the Ure2p prion C-terminal 70-354 in microcrystalline form.
;
_BMRB_accession_number 17499
_BMRB_flat_file_name bmr17499.str
_Entry_type original
_Submission_date 2011-03-01
_Accession_date 2011-03-01
_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 Habenstein Birgit . .
2 Wasmer Christian . .
3 Bousset Luc . .
4 Sourigues Yannick . .
5 Schuetz Anne . .
6 Loquet Antoine . .
7 Meier Beat H. .
8 Melki Ronald . .
9 Bockmann Anja . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"13C chemical shifts" 751
"15N chemical shifts" 192
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2012-03-08 update BMRB 'update entry citation'
2011-09-29 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 21805376
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Habenstein Birgit . .
2 Wasmer Christian . .
3 Bousset Luc . .
4 Sourigues Yannick . .
5 Schutz Anne . .
6 Loquet Antoine . .
7 Meier Beat H. .
8 Melki Ronald . .
9 Bockmann Anja . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 51
_Journal_issue 3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 235
_Page_last 243
_Year 2011
_Details .
loop_
_Keyword
'conformational heterogeneity'
fibrils
prion
'sequential assignment'
'solid-state NMR'
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name Ure2p70-354
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
Ure2p70-354 $Ure2p70-354
stop_
_System_molecular_weight 34053.46
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Ure2p70-354
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Ure2p70-354
_Molecular_mass .
_Mol_thiol_state 'not present'
loop_
_Biological_function
'nitrogen-dependent repression of the ureidosuccinate utilization pathway'
stop_
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 295
_Mol_residue_sequence
;
MNNDNENNIKNTLEQHRQQQ
QAFSDMSHVEYSRITKFFQE
QPLEGYTLFSHRSAPNGFKV
AIVLSELGFHYNTIFLDFNL
GEHRAPEFVSVNPNARVPAL
IDHGMDNLSIWESGAILLHL
VNKYYKETGNPLLWSDDLAD
QSQINAWLFFQTSGHAPMIG
QALHFRYFHSQKIASAVERY
TDEVRRVYGVVEMALAERRE
ALVMELDTENAAAYSAGTTP
MSQSRFFDYPVWLVGDKLTI
ADLAFVPWNNVVDRIGINIK
IEFPEVYKWTKHMMRRPAVI
KALRGERGSHHHHHH
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 69 MET 2 70 ASN 3 71 ASN 4 72 ASP 5 73 ASN
6 74 GLU 7 75 ASN 8 76 ASN 9 77 ILE 10 78 LYS
11 79 ASN 12 80 THR 13 81 LEU 14 82 GLU 15 83 GLN
16 84 HIS 17 85 ARG 18 86 GLN 19 87 GLN 20 88 GLN
21 89 GLN 22 90 ALA 23 91 PHE 24 92 SER 25 93 ASP
26 94 MET 27 95 SER 28 96 HIS 29 97 VAL 30 98 GLU
31 99 TYR 32 100 SER 33 101 ARG 34 102 ILE 35 103 THR
36 104 LYS 37 105 PHE 38 106 PHE 39 107 GLN 40 108 GLU
41 109 GLN 42 110 PRO 43 111 LEU 44 112 GLU 45 113 GLY
46 114 TYR 47 115 THR 48 116 LEU 49 117 PHE 50 118 SER
51 119 HIS 52 120 ARG 53 121 SER 54 122 ALA 55 123 PRO
56 124 ASN 57 125 GLY 58 126 PHE 59 127 LYS 60 128 VAL
61 129 ALA 62 130 ILE 63 131 VAL 64 132 LEU 65 133 SER
66 134 GLU 67 135 LEU 68 136 GLY 69 137 PHE 70 138 HIS
71 139 TYR 72 140 ASN 73 141 THR 74 142 ILE 75 143 PHE
76 144 LEU 77 145 ASP 78 146 PHE 79 147 ASN 80 148 LEU
81 149 GLY 82 150 GLU 83 151 HIS 84 152 ARG 85 153 ALA
86 154 PRO 87 155 GLU 88 156 PHE 89 157 VAL 90 158 SER
91 159 VAL 92 160 ASN 93 161 PRO 94 162 ASN 95 163 ALA
96 164 ARG 97 165 VAL 98 166 PRO 99 167 ALA 100 168 LEU
101 169 ILE 102 170 ASP 103 171 HIS 104 172 GLY 105 173 MET
106 174 ASP 107 175 ASN 108 176 LEU 109 177 SER 110 178 ILE
111 179 TRP 112 180 GLU 113 181 SER 114 182 GLY 115 183 ALA
116 184 ILE 117 185 LEU 118 186 LEU 119 187 HIS 120 188 LEU
121 189 VAL 122 190 ASN 123 191 LYS 124 192 TYR 125 193 TYR
126 194 LYS 127 195 GLU 128 196 THR 129 197 GLY 130 198 ASN
131 199 PRO 132 200 LEU 133 201 LEU 134 202 TRP 135 203 SER
136 204 ASP 137 205 ASP 138 206 LEU 139 207 ALA 140 208 ASP
141 209 GLN 142 210 SER 143 211 GLN 144 212 ILE 145 213 ASN
146 214 ALA 147 215 TRP 148 216 LEU 149 217 PHE 150 218 PHE
151 219 GLN 152 220 THR 153 221 SER 154 222 GLY 155 223 HIS
156 224 ALA 157 225 PRO 158 226 MET 159 227 ILE 160 228 GLY
161 229 GLN 162 230 ALA 163 231 LEU 164 232 HIS 165 233 PHE
166 234 ARG 167 235 TYR 168 236 PHE 169 237 HIS 170 238 SER
171 239 GLN 172 240 LYS 173 241 ILE 174 242 ALA 175 243 SER
176 244 ALA 177 245 VAL 178 246 GLU 179 247 ARG 180 248 TYR
181 249 THR 182 250 ASP 183 251 GLU 184 252 VAL 185 253 ARG
186 254 ARG 187 255 VAL 188 256 TYR 189 257 GLY 190 258 VAL
191 259 VAL 192 260 GLU 193 261 MET 194 262 ALA 195 263 LEU
196 264 ALA 197 265 GLU 198 266 ARG 199 267 ARG 200 268 GLU
201 269 ALA 202 270 LEU 203 271 VAL 204 272 MET 205 273 GLU
206 274 LEU 207 275 ASP 208 276 THR 209 277 GLU 210 278 ASN
211 279 ALA 212 280 ALA 213 281 ALA 214 282 TYR 215 283 SER
216 284 ALA 217 285 GLY 218 286 THR 219 287 THR 220 288 PRO
221 289 MET 222 290 SER 223 291 GLN 224 292 SER 225 293 ARG
226 294 PHE 227 295 PHE 228 296 ASP 229 297 TYR 230 298 PRO
231 299 VAL 232 300 TRP 233 301 LEU 234 302 VAL 235 303 GLY
236 304 ASP 237 305 LYS 238 306 LEU 239 307 THR 240 308 ILE
241 309 ALA 242 310 ASP 243 311 LEU 244 312 ALA 245 313 PHE
246 314 VAL 247 315 PRO 248 316 TRP 249 317 ASN 250 318 ASN
251 319 VAL 252 320 VAL 253 321 ASP 254 322 ARG 255 323 ILE
256 324 GLY 257 325 ILE 258 326 ASN 259 327 ILE 260 328 LYS
261 329 ILE 262 330 GLU 263 331 PHE 264 332 PRO 265 333 GLU
266 334 VAL 267 335 TYR 268 336 LYS 269 337 TRP 270 338 THR
271 339 LYS 272 340 HIS 273 341 MET 274 342 MET 275 343 ARG
276 344 ARG 277 345 PRO 278 346 ALA 279 347 VAL 280 348 ILE
281 349 LYS 282 350 ALA 283 351 LEU 284 352 ARG 285 353 GLY
286 354 GLU 287 355 ARG 288 356 GLY 289 357 SER 290 358 HIS
291 359 HIS 292 360 HIS 293 361 HIS 294 362 HIS 295 363 HIS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-10-14
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
BMRB 17570 "Ure2p prion" 96.61 354 100.00 100.00 0.00e+00
PDB 1G6W "Crystal Structure Of The Globular Region Of The Prion Protein Ure2 From The Yeast Saccaromyces Cerevisiae" 88.47 261 100.00 100.00 0.00e+00
PDB 1G6Y "Crystal Structure Of The Globular Region Of The Prion Protien Ure2 From Yeast Saccharomyces Cerevisiae" 88.47 261 100.00 100.00 0.00e+00
PDB 1HQO "Crystal Structure Of The Nitrogen Regulation Fragment Of The Yeast Prion Protein Ure2p" 87.46 258 97.29 97.29 0.00e+00
PDB 1JZR "Ure2p In Complex With Glutathione" 88.14 260 100.00 100.00 0.00e+00
PDB 1K0A "Ure2p In Complex With S-Hexylglutathione" 88.14 260 100.00 100.00 0.00e+00
PDB 1K0B "Ure2p In Complex With Glutathione" 88.14 260 100.00 100.00 0.00e+00
PDB 1K0C "Ure2p In Complex With S-P-Nitrobenzylglutathione" 88.14 260 100.00 100.00 0.00e+00
PDB 1K0D "Ure2p In Complex With Glutathione" 88.14 260 100.00 100.00 0.00e+00
DBJ BAM78703 "nitrogen catabolite repression transcriptional regulator [Saccharomyces pastorianus]" 96.61 344 97.89 99.65 0.00e+00
DBJ GAA25878 "K7_Ure2p [Saccharomyces cerevisiae Kyokai no. 7]" 96.61 354 100.00 100.00 0.00e+00
EMBL CAA93369 "N1165 [Saccharomyces cerevisiae]" 96.61 354 100.00 100.00 0.00e+00
EMBL CAA96134 "URE2 [Saccharomyces cerevisiae]" 96.61 354 100.00 100.00 0.00e+00
EMBL CAY82378 "Ure2p [Saccharomyces cerevisiae EC1118]" 96.61 354 100.00 100.00 0.00e+00
GB AAA35201 "glutathione transferase-like protein [Saccharomyces cerevisiae]" 96.61 354 100.00 100.00 0.00e+00
GB AAK51641 "Ure2p [Saccharomyces douglasii]" 96.27 359 99.30 99.65 0.00e+00
GB AAM91938 "Ure2p [Saccharomyces paradoxus]" 96.27 359 99.30 99.65 0.00e+00
GB AAM91939 "Ure2p [Saccharomyces bayanus]" 96.61 345 97.89 99.65 0.00e+00
GB AAM93167 "Ure2p [Saccharomyces cerevisiae]" 96.61 354 100.00 100.00 0.00e+00
REF NP_014170 "Ure2p [Saccharomyces cerevisiae S288c]" 96.61 354 100.00 100.00 0.00e+00
SP P23202 "RecName: Full=Transcriptional regulator URE2; AltName: Full=Disulfide reductase; AltName: Full=Glutathione peroxidase" 96.61 354 100.00 100.00 0.00e+00
SP Q7LLZ8 "RecName: Full=Protein URE2" 96.27 359 99.30 99.65 0.00e+00
SP Q8NJR6 "RecName: Full=Protein URE2" 96.61 345 97.89 99.65 0.00e+00
TPG DAA10329 "TPA: Ure2p [Saccharomyces cerevisiae S288c]" 96.61 354 100.00 100.00 0.00e+00
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Ure2p70-354 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Variant
_Vector_name
$Ure2p70-354 'recombinant technology' . Escherichia coli BL21 DE3 'pET 3A'
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solid
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$Ure2p70-354 . mg 20 40 '[U-100% 13C; U-100% 15N]'
KCl 75 mM . . 'natural abundance'
TRIS 20 mM . . 'natural abundance'
EGTA 1 mM . . 'natural abundance'
dithiothreitol 1 mM . . 'natural abundance'
DSS 0.5 mg . . 'natural abundance'
H2O 100 % . . 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_CCPNMR_Analysis
_Saveframe_category software
_Name ANALYSIS
_Version 2.1.1
loop_
_Vendor
_Address
_Electronic_address
CCPN . .
stop_
loop_
_Task
'chemical shift assignment'
stop_
_Details .
save_
save_TOPSPIN
_Saveframe_category software
_Name TOPSPIN
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Bruker Biospin' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 850
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D_NCACB_(DREAM)_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D NCACB (DREAM)'
_Sample_label $sample_1
save_
save_3D_N(CO)CACB_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D N(CO)CACB'
_Sample_label $sample_1
save_
save_3D_CAN(CO)CA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CAN(CO)CA'
_Sample_label $sample_1
save_
save_3D_CCC_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CCC'
_Sample_label $sample_1
save_
save_3D_NCACX_(DARR)_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D NCACX (DARR)'
_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
pH 7.5 . 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
_Indirect_shift_ratio_citation_label
_Correction_value_citation_label
DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $entry_citation $entry_citation
DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation
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 NCACB (DREAM)'
'3D N(CO)CACB'
'3D CAN(CO)CA'
'3D CCC'
'3D NCACX (DARR)'
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 Ure2p70-354
_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
1 113 45 GLY CA C 45.488 0.001 1
2 114 46 TYR C C 176.384 0.150 1
3 114 46 TYR CA C 57.306 0.125 1
4 114 46 TYR CB C 42.142 0.164 1
5 114 46 TYR CG C 130.118 0.150 1
6 114 46 TYR CD2 C 132.420 0.150 3
7 114 46 TYR CZ C 157.483 0.150 1
8 114 46 TYR N N 118.600 0.085 1
9 115 47 THR C C 172.221 0.016 1
10 115 47 THR CA C 63.460 0.139 1
11 115 47 THR CB C 69.403 0.158 1
12 115 47 THR CG2 C 21.393 0.028 1
13 115 47 THR N N 119.816 0.056 1
14 116 48 LEU CA C 52.825 0.055 1
15 116 48 LEU CB C 44.719 0.048 1
16 116 48 LEU CG C 27.737 0.037 1
17 116 48 LEU CD1 C 23.143 0.150 2
18 116 48 LEU CD2 C 25.192 0.150 2
19 116 48 LEU N N 129.345 0.070 1
20 117 49 PHE CA C 57.413 0.099 1
21 117 49 PHE CB C 40.225 0.146 1
22 117 49 PHE CG C 139.325 0.150 1
23 117 49 PHE CD2 C 131.227 0.150 3
24 117 49 PHE CE2 C 130.118 0.150 3
25 117 49 PHE N N 125.624 0.170 1
26 118 50 SER C C 173.157 0.150 1
27 118 50 SER CA C 54.018 0.029 1
28 118 50 SER CB C 64.667 0.064 1
29 118 50 SER N N 115.877 0.063 1
30 122 54 ALA CA C 49.413 0.150 1
31 122 54 ALA CB C 20.146 0.150 1
32 122 54 ALA N N 124.540 0.150 1
33 123 55 PRO C C 178.813 0.153 1
34 123 55 PRO CA C 65.295 0.074 1
35 123 55 PRO CB C 31.772 0.064 1
36 123 55 PRO CG C 27.721 0.085 1
37 123 55 PRO CD C 50.640 0.162 1
38 123 55 PRO N N 139.728 0.076 1
39 124 56 ASN C C 175.722 0.150 1
40 124 56 ASN CA C 55.453 0.088 1
41 124 56 ASN CB C 37.947 0.175 1
42 124 56 ASN CG C 178.697 0.009 1
43 124 56 ASN N N 111.233 0.037 1
44 125 57 GLY CA C 47.256 0.108 1
45 125 57 GLY N N 106.940 0.051 1
46 126 58 PHE CA C 56.810 0.077 1
47 126 58 PHE CB C 39.994 0.150 1
48 126 58 PHE N N 122.259 0.044 1
49 127 59 LYS C C 176.421 0.014 1
50 127 59 LYS CA C 59.769 0.059 1
51 127 59 LYS CB C 32.843 0.063 1
52 127 59 LYS CG C 24.793 0.150 1
53 127 59 LYS CD C 29.681 0.150 1
54 127 59 LYS N N 116.975 0.150 1
55 128 60 VAL CA C 65.866 0.079 1
56 128 60 VAL CB C 31.278 0.013 1
57 128 60 VAL CG1 C 22.788 0.009 2
58 128 60 VAL CG2 C 24.351 0.046 2
59 128 60 VAL N N 114.713 0.180 1
60 129 61 ALA CA C 55.652 0.058 1
61 129 61 ALA CB C 18.092 0.026 1
62 129 61 ALA N N 122.227 0.132 1
63 130 62 ILE C C 176.121 0.150 1
64 130 62 ILE CA C 65.881 0.084 1
65 130 62 ILE CB C 38.087 0.074 1
66 130 62 ILE CG1 C 26.174 0.150 1
67 130 62 ILE CG2 C 19.431 0.069 1
68 130 62 ILE CD1 C 14.422 0.150 1
69 130 62 ILE N N 116.323 0.043 1
70 131 63 VAL CA C 67.776 0.058 1
71 131 63 VAL CB C 31.238 0.058 1
72 131 63 VAL CG1 C 21.544 0.150 2
73 131 63 VAL CG2 C 22.966 0.150 2
74 131 63 VAL N N 119.440 0.203 1
75 132 64 LEU CA C 59.053 0.040 1
76 132 64 LEU CB C 42.596 0.136 1
77 132 64 LEU CG C 25.609 0.028 1
78 132 64 LEU CD2 C 19.504 0.150 1
79 132 64 LEU N N 119.526 0.033 1
80 133 65 SER CA C 61.779 0.088 1
81 133 65 SER CB C 64.025 0.053 1
82 133 65 SER N N 111.399 0.314 1
83 134 66 GLU CA C 59.555 0.070 1
84 134 66 GLU CB C 31.021 0.098 1
85 134 66 GLU CG C 35.814 0.150 1
86 134 66 GLU CD C 182.019 0.150 1
87 134 66 GLU N N 123.124 0.033 1
88 135 67 LEU CA C 55.055 0.075 1
89 135 67 LEU CB C 40.737 0.115 1
90 135 67 LEU CG C 27.670 0.039 1
91 135 67 LEU CD2 C 25.878 0.037 1
92 135 67 LEU N N 115.902 0.116 1
93 136 68 GLY CA C 45.756 0.116 1
94 136 68 GLY N N 106.144 0.106 1
95 137 69 PHE CA C 54.510 0.035 1
96 137 69 PHE CB C 39.151 0.059 1
97 137 69 PHE CG C 138.827 0.150 1
98 137 69 PHE CE2 C 130.292 0.150 3
99 137 69 PHE N N 119.470 0.187 1
100 138 70 HIS CA C 56.567 0.101 1
101 138 70 HIS CB C 30.521 0.049 1
102 138 70 HIS CG C 134.615 0.150 1
103 138 70 HIS CD2 C 119.605 0.150 1
104 138 70 HIS N N 123.774 0.199 1
105 139 71 TYR CA C 54.563 0.072 1
106 139 71 TYR CB C 41.817 0.102 1
107 139 71 TYR CD1 C 134.540 0.150 3
108 139 71 TYR CE1 C 118.286 0.150 3
109 139 71 TYR CZ C 158.043 0.150 1
110 139 71 TYR N N 120.563 0.368 1
111 140 72 ASN C C 173.624 0.150 1
112 140 72 ASN CA C 51.521 0.052 1
113 140 72 ASN CB C 42.155 0.023 1
114 140 72 ASN CG C 174.028 0.150 1
115 140 72 ASN N N 117.579 0.057 1
116 141 73 THR CA C 61.562 0.064 1
117 141 73 THR CB C 69.552 0.127 1
118 141 73 THR CG2 C 20.690 0.181 1
119 141 73 THR N N 119.117 0.035 1
120 142 74 ILE CA C 60.137 0.236 1
121 142 74 ILE CB C 38.327 0.111 1
122 142 74 ILE CG1 C 26.620 0.209 1
123 142 74 ILE CG2 C 19.367 0.027 1
124 142 74 ILE CD1 C 14.686 0.035 1
125 142 74 ILE N N 128.437 0.153 1
126 143 75 PHE C C 176.969 0.150 1
127 143 75 PHE CA C 56.603 0.110 1
128 143 75 PHE CB C 37.758 0.048 1
129 143 75 PHE CD2 C 130.562 0.150 3
130 143 75 PHE CE2 C 131.365 0.150 3
131 143 75 PHE CZ C 129.493 0.150 1
132 143 75 PHE N N 128.179 0.152 1
133 145 77 ASP C C 176.845 0.054 1
134 145 77 ASP CA C 55.432 0.050 1
135 145 77 ASP CB C 36.841 0.067 1
136 145 77 ASP CG C 178.508 0.045 1
137 145 77 ASP N N 120.055 0.206 1
138 146 78 PHE C C 175.228 0.054 1
139 146 78 PHE CA C 54.432 0.105 1
140 146 78 PHE CB C 38.892 0.032 1
141 146 78 PHE CG C 138.352 0.150 1
142 146 78 PHE CD2 C 131.899 0.150 3
143 146 78 PHE CE2 C 130.063 0.163 3
144 146 78 PHE N N 113.440 0.183 1
145 147 79 ASN C C 175.250 0.150 1
146 147 79 ASN CA C 54.489 0.098 1
147 147 79 ASN CB C 36.459 0.150 1
148 147 79 ASN CG C 177.873 0.150 1
149 147 79 ASN N N 110.720 0.036 1
150 152 84 ARG C C 176.563 0.078 1
151 152 84 ARG CA C 53.269 0.129 1
152 152 84 ARG CB C 29.230 0.060 1
153 152 84 ARG N N 114.661 0.150 1
154 153 85 ALA C C 176.691 0.044 1
155 153 85 ALA CA C 50.535 0.143 1
156 153 85 ALA CB C 17.595 0.072 1
157 153 85 ALA N N 125.512 0.028 1
158 157 89 VAL C C 178.041 0.150 1
159 157 89 VAL CA C 64.235 0.085 1
160 157 89 VAL CB C 31.476 0.052 1
161 157 89 VAL CG1 C 21.543 0.150 2
162 157 89 VAL CG2 C 22.912 0.150 2
163 157 89 VAL N N 120.221 0.150 1
164 158 90 SER C C 175.644 0.150 1
165 158 90 SER CA C 61.096 0.131 1
166 158 90 SER CB C 63.035 0.121 1
167 158 90 SER N N 111.492 0.065 1
168 162 94 ASN C C 174.837 0.007 1
169 162 94 ASN CA C 52.426 0.129 1
170 162 94 ASN CB C 40.045 0.070 1
171 162 94 ASN CG C 180.256 0.150 1
172 162 94 ASN N N 111.704 0.150 1
173 163 95 ALA CA C 53.292 0.063 1
174 163 95 ALA CB C 17.359 0.025 1
175 163 95 ALA N N 115.503 0.100 1
176 164 96 ARG CA C 53.575 0.121 1
177 164 96 ARG CB C 32.939 0.034 1
178 164 96 ARG CD C 43.242 0.150 1
179 164 96 ARG N N 113.881 0.297 1
180 165 97 VAL C C 179.541 0.150 1
181 165 97 VAL CA C 64.909 0.032 1
182 165 97 VAL CB C 30.996 0.123 1
183 165 97 VAL CG1 C 17.377 0.059 2
184 165 97 VAL CG2 C 24.234 0.060 2
185 165 97 VAL N N 107.524 0.016 1
186 166 98 PRO C C 175.006 0.074 1
187 166 98 PRO CA C 61.485 0.189 1
188 166 98 PRO CB C 36.957 0.091 1
189 166 98 PRO CG C 23.869 0.098 1
190 166 98 PRO CD C 50.165 0.117 1
191 166 98 PRO N N 128.638 0.150 1
192 167 99 ALA CA C 51.813 0.089 1
193 167 99 ALA CB C 22.496 0.123 1
194 167 99 ALA N N 116.265 0.066 1
195 168 100 LEU C C 175.374 0.150 1
196 168 100 LEU CA C 52.635 0.142 1
197 168 100 LEU CB C 48.224 0.103 1
198 168 100 LEU CG C 27.359 0.018 1
199 168 100 LEU CD1 C 26.755 0.073 2
200 168 100 LEU CD2 C 26.261 0.030 2
201 168 100 LEU N N 124.877 0.079 1
202 169 101 ILE C C 175.340 0.024 1
203 169 101 ILE CA C 59.307 0.149 1
204 169 101 ILE CB C 42.368 0.069 1
205 169 101 ILE CG1 C 25.467 0.088 1
206 169 101 ILE N N 123.170 0.176 1
207 170 102 ASP C C 176.698 0.052 1
208 170 102 ASP CA C 51.543 0.090 1
209 170 102 ASP CB C 40.961 0.077 1
210 170 102 ASP CG C 179.581 0.056 1
211 170 102 ASP N N 126.004 0.173 1
212 171 103 HIS CA C 59.527 0.064 1
213 171 103 HIS CB C 27.711 0.108 1
214 171 103 HIS CG C 129.275 0.035 1
215 171 103 HIS CD2 C 128.341 0.033 1
216 171 103 HIS CE1 C 139.096 0.150 1
217 171 103 HIS N N 122.365 0.077 1
218 172 104 GLY CA C 45.881 0.082 1
219 172 104 GLY N N 106.040 0.148 1
220 173 105 MET C C 175.127 0.055 1
221 173 105 MET CA C 54.514 0.064 1
222 173 105 MET CB C 31.678 0.078 1
223 173 105 MET CG C 32.829 0.045 1
224 173 105 MET N N 122.116 0.055 1
225 174 106 ASP C C 175.306 0.150 1
226 174 106 ASP CA C 55.016 0.154 1
227 174 106 ASP CB C 39.032 0.027 1
228 174 106 ASP CG C 177.845 0.150 1
229 174 106 ASP N N 116.888 0.055 1
230 175 107 ASN C C 173.475 0.123 1
231 175 107 ASN CA C 54.579 0.071 1
232 175 107 ASN CB C 36.160 0.236 1
233 175 107 ASN CG C 177.950 0.092 1
234 175 107 ASN N N 110.603 0.196 1
235 176 108 LEU C C 175.305 0.062 1
236 176 108 LEU CA C 55.696 0.077 1
237 176 108 LEU CB C 44.140 0.069 1
238 176 108 LEU CG C 26.979 0.081 1
239 176 108 LEU CD2 C 22.774 0.074 1
240 176 108 LEU N N 122.442 0.116 1
241 177 109 SER CA C 55.863 0.103 1
242 177 109 SER CB C 64.671 0.026 1
243 177 109 SER N N 121.777 0.242 1
244 178 110 ILE CA C 62.359 0.059 1
245 178 110 ILE CB C 40.878 0.150 1
246 178 110 ILE N N 124.396 0.071 1
247 179 111 TRP CA C 54.054 0.182 1
248 179 111 TRP CB C 30.067 0.208 1
249 179 111 TRP N N 125.455 0.069 1
250 180 112 GLU CA C 57.074 0.154 1
251 180 112 GLU CB C 29.004 0.092 1
252 180 112 GLU CG C 34.140 0.090 1
253 180 112 GLU CD C 180.352 0.032 1
254 180 112 GLU N N 118.192 0.155 1
255 181 113 SER CA C 62.122 0.091 1
256 181 113 SER CB C 63.163 0.073 1
257 181 113 SER N N 121.866 0.220 1
258 182 114 GLY CA C 46.445 0.058 1
259 182 114 GLY N N 110.851 0.067 1
260 183 115 ALA C C 180.854 0.150 1
261 183 115 ALA CA C 54.017 0.082 1
262 183 115 ALA CB C 17.675 0.018 1
263 183 115 ALA N N 120.668 0.013 1
264 184 116 ILE C C 176.842 0.062 1
265 184 116 ILE CA C 66.003 0.096 1
266 184 116 ILE CB C 37.218 0.070 1
267 184 116 ILE CG1 C 28.692 0.106 1
268 184 116 ILE CG2 C 21.128 0.044 1
269 184 116 ILE CD1 C 14.464 0.094 1
270 184 116 ILE N N 119.914 0.041 1
271 185 117 LEU CA C 59.882 0.074 1
272 185 117 LEU CB C 40.344 0.116 1
273 185 117 LEU CG C 29.740 0.146 1
274 185 117 LEU CD2 C 24.339 0.071 1
275 185 117 LEU N N 119.854 0.078 1
276 186 118 LEU C C 179.616 0.150 1
277 186 118 LEU CA C 57.206 0.126 1
278 186 118 LEU CB C 41.992 0.065 1
279 186 118 LEU CG C 27.520 0.045 1
280 186 118 LEU CD2 C 22.111 0.065 1
281 186 118 LEU N N 114.785 0.070 1
282 187 119 HIS C C 177.123 0.051 1
283 187 119 HIS CA C 60.739 0.076 1
284 187 119 HIS CB C 31.675 0.129 1
285 187 119 HIS CG C 137.129 0.042 1
286 187 119 HIS CD2 C 115.147 0.131 1
287 187 119 HIS CE1 C 138.571 0.150 1
288 187 119 HIS N N 122.316 0.139 1
289 188 120 LEU C C 179.498 0.150 1
290 188 120 LEU CA C 57.995 0.085 1
291 188 120 LEU CB C 41.435 0.048 1
292 188 120 LEU CG C 25.903 0.090 1
293 188 120 LEU CD2 C 21.747 0.134 1
294 188 120 LEU N N 115.368 0.079 1
295 189 121 VAL C C 179.266 0.131 1
296 189 121 VAL CA C 65.207 0.066 1
297 189 121 VAL CB C 30.668 0.174 1
298 189 121 VAL CG1 C 16.249 0.150 2
299 189 121 VAL CG2 C 24.140 0.157 2
300 189 121 VAL N N 108.643 0.073 1
301 190 122 ASN C C 175.911 0.150 1
302 190 122 ASN CA C 57.032 0.107 1
303 190 122 ASN CB C 39.856 0.101 1
304 190 122 ASN CG C 178.326 0.020 1
305 190 122 ASN N N 121.171 0.184 1
306 191 123 LYS CA C 59.271 0.125 1
307 191 123 LYS CB C 32.286 0.100 1
308 191 123 LYS CG C 24.972 0.034 1
309 191 123 LYS CD C 29.102 0.112 1
310 191 123 LYS CE C 41.888 0.035 1
311 191 123 LYS N N 119.599 0.149 1
312 195 127 GLU C C 178.599 0.085 1
313 195 127 GLU CA C 59.072 0.033 1
314 195 127 GLU CB C 30.412 0.030 1
315 195 127 GLU CG C 36.318 0.150 1
316 195 127 GLU CD C 184.083 0.150 1
317 195 127 GLU N N 119.774 0.150 1
318 196 128 THR C C 176.768 0.057 1
319 196 128 THR CB C 72.399 0.077 1
320 196 128 THR CA C 62.587 0.188 1
321 196 128 THR CG2 C 19.624 0.122 1
322 196 128 THR N N 105.591 0.107 1
323 197 129 GLY C C 172.399 0.150 1
324 197 129 GLY CA C 45.728 0.028 1
325 197 129 GLY N N 112.544 0.063 1
326 198 130 ASN C C 172.761 0.150 1
327 198 130 ASN CA C 48.953 0.160 1
328 198 130 ASN CB C 40.511 0.093 1
329 198 130 ASN CG C 176.803 0.150 1
330 198 130 ASN N N 120.937 0.082 1
331 199 131 PRO CA C 61.559 0.154 1
332 199 131 PRO CB C 31.947 0.075 1
333 199 131 PRO CG C 26.844 0.099 1
334 199 131 PRO CD C 50.199 0.122 1
335 199 131 PRO N N 138.208 0.065 1
336 200 132 LEU C C 177.090 0.085 1
337 200 132 LEU CA C 56.943 0.097 1
338 200 132 LEU CB C 43.251 0.038 1
339 200 132 LEU CG C 26.827 0.072 1
340 200 132 LEU N N 129.468 0.213 1
341 201 133 LEU C C 176.842 0.084 1
342 201 133 LEU CA C 56.254 0.112 1
343 201 133 LEU CB C 40.916 0.052 1
344 201 133 LEU CG C 26.964 0.093 1
345 201 133 LEU CD2 C 22.748 0.058 1
346 201 133 LEU N N 115.165 0.315 1
347 202 134 TRP C C 173.836 0.150 1
348 202 134 TRP CA C 53.492 0.086 1
349 202 134 TRP CB C 34.205 0.138 1
350 202 134 TRP CD2 C 128.099 0.150 1
351 202 134 TRP N N 122.631 0.178 1
352 203 135 SER C C 172.284 0.080 1
353 203 135 SER CA C 57.376 0.139 1
354 203 135 SER CB C 63.669 0.072 1
355 203 135 SER N N 113.454 0.029 1
356 204 136 ASP CA C 53.075 0.120 1
357 204 136 ASP CB C 40.378 0.160 1
358 204 136 ASP CG C 180.215 0.150 1
359 204 136 ASP N N 121.519 0.213 1
360 205 137 ASP C C 175.987 0.074 1
361 205 137 ASP CA C 52.760 0.051 1
362 205 137 ASP CB C 43.797 0.136 1
363 205 137 ASP CG C 180.049 0.150 1
364 205 137 ASP N N 123.309 0.134 1
365 206 138 LEU CA C 58.602 0.052 1
366 206 138 LEU CB C 41.865 0.172 1
367 206 138 LEU CG C 27.249 0.099 1
368 206 138 LEU N N 128.762 0.141 1
369 207 139 ALA CA C 55.859 0.050 1
370 207 139 ALA CB C 18.673 0.025 1
371 207 139 ALA N N 119.808 0.115 1
372 208 140 ASP CA C 57.182 0.060 1
373 208 140 ASP CB C 39.664 0.061 1
374 208 140 ASP CG C 179.407 0.150 1
375 208 140 ASP N N 118.582 0.163 1
376 209 141 GLN CA C 59.962 0.107 1
377 209 141 GLN CB C 27.016 0.058 1
378 209 141 GLN CG C 32.696 0.159 1
379 209 141 GLN CD C 179.009 0.033 1
380 209 141 GLN N N 118.742 0.178 1
381 210 142 SER C C 175.929 0.150 1
382 210 142 SER CA C 61.458 0.282 1
383 210 142 SER CB C 62.638 0.067 1
384 210 142 SER N N 117.792 0.086 1
385 211 143 GLN C C 177.981 0.150 1
386 211 143 GLN CA C 58.793 0.129 1
387 211 143 GLN CB C 29.664 0.023 1
388 211 143 GLN CD C 180.501 0.150 1
389 211 143 GLN N N 121.394 0.151 1
390 212 144 ILE C C 178.808 0.114 1
391 212 144 ILE CA C 66.233 0.144 1
392 212 144 ILE CB C 38.772 0.094 1
393 212 144 ILE CG1 C 29.695 0.164 1
394 212 144 ILE CG2 C 17.451 0.090 1
395 212 144 ILE CD1 C 15.389 0.066 1
396 212 144 ILE N N 120.724 0.177 1
397 213 145 ASN C C 174.349 0.150 1
398 213 145 ASN CA C 55.460 0.078 1
399 213 145 ASN CB C 36.650 0.042 1
400 213 145 ASN CG C 178.226 0.150 1
401 213 145 ASN N N 117.150 0.150 1
402 214 146 ALA C C 178.091 0.060 1
403 214 146 ALA CA C 56.484 0.101 1
404 214 146 ALA CB C 16.199 0.055 1
405 214 146 ALA N N 127.562 0.029 1
406 215 147 TRP C C 178.507 0.026 1
407 215 147 TRP CA C 60.961 0.066 1
408 215 147 TRP CB C 31.440 0.174 1
409 215 147 TRP CG C 111.470 0.265 1
410 215 147 TRP CD2 C 129.581 0.038 1
411 215 147 TRP CE2 C 140.105 0.150 1
412 215 147 TRP N N 116.123 0.046 1
413 216 148 LEU CA C 58.418 0.107 1
414 216 148 LEU CB C 43.575 0.088 1
415 216 148 LEU CG C 27.152 0.027 1
416 216 148 LEU CD1 C 23.870 0.063 2
417 216 148 LEU CD2 C 26.239 0.063 2
418 216 148 LEU N N 121.439 0.065 1
419 221 153 SER C C 178.465 0.020 1
420 221 153 SER CA C 59.673 0.082 1
421 221 153 SER CB C 64.460 0.064 1
422 221 153 SER N N 114.164 0.078 1
423 222 154 GLY CA C 44.779 0.047 1
424 222 154 GLY N N 111.149 0.089 1
425 223 155 HIS CA C 58.144 0.053 1
426 223 155 HIS CB C 29.813 0.026 1
427 223 155 HIS N N 120.343 0.157 1
428 224 156 ALA C C 176.015 0.173 1
429 224 156 ALA CA C 56.397 0.147 1
430 224 156 ALA CB C 15.686 0.118 1
431 224 156 ALA N N 121.537 0.071 1
432 225 157 PRO C C 180.093 0.150 1
433 225 157 PRO CA C 65.666 0.104 1
434 225 157 PRO CB C 30.744 0.133 1
435 225 157 PRO CG C 29.629 0.094 1
436 225 157 PRO CD C 51.219 0.113 1
437 225 157 PRO N N 134.319 0.112 1
438 226 158 MET C C 178.264 0.087 1
439 226 158 MET CA C 56.796 0.096 1
440 226 158 MET CB C 34.577 0.048 1
441 226 158 MET CG C 33.000 0.137 1
442 226 158 MET N N 112.809 0.177 1
443 227 159 ILE C C 178.540 0.105 1
444 227 159 ILE CA C 66.281 0.096 1
445 227 159 ILE CB C 37.680 0.203 1
446 227 159 ILE CG1 C 30.706 0.097 1
447 227 159 ILE CG2 C 17.849 0.141 1
448 227 159 ILE CD1 C 14.414 0.063 1
449 227 159 ILE N N 121.483 0.100 1
450 228 160 GLY CA C 47.516 0.079 1
451 228 160 GLY N N 104.325 0.133 1
452 229 161 GLN C C 177.588 0.066 1
453 229 161 GLN CA C 56.761 0.108 1
454 229 161 GLN CB C 24.266 0.101 1
455 229 161 GLN CG C 31.962 0.188 1
456 229 161 GLN CD C 180.268 0.036 1
457 229 161 GLN N N 119.882 0.099 1
458 230 162 ALA CA C 56.577 0.069 1
459 230 162 ALA CB C 19.038 0.024 1
460 230 162 ALA N N 122.201 0.133 1
461 231 163 LEU C C 178.970 0.094 1
462 231 163 LEU CA C 58.351 0.063 1
463 231 163 LEU CB C 42.895 0.035 1
464 231 163 LEU CG C 27.149 0.088 1
465 231 163 LEU N N 116.718 0.036 1
466 232 164 HIS CA C 61.705 0.150 1
467 232 164 HIS CB C 30.856 0.150 1
468 232 164 HIS N N 117.211 0.150 1
469 238 170 SER C C 173.746 0.059 1
470 238 170 SER CA C 60.991 0.081 1
471 238 170 SER CB C 62.712 0.077 1
472 238 170 SER N N 119.589 0.079 1
473 239 171 GLN C C 174.738 0.018 1
474 239 171 GLN CA C 54.210 0.093 1
475 239 171 GLN CB C 32.369 0.046 1
476 239 171 GLN CG C 33.688 0.101 1
477 239 171 GLN CD C 180.289 0.150 1
478 239 171 GLN N N 117.282 0.153 1
479 240 172 LYS C C 176.000 0.055 1
480 240 172 LYS CA C 55.988 0.111 1
481 240 172 LYS CB C 31.534 0.071 1
482 240 172 LYS CG C 24.287 0.150 1
483 240 172 LYS CD C 28.930 0.175 1
484 240 172 LYS CE C 39.811 0.150 1
485 240 172 LYS N N 125.028 0.133 1
486 241 173 ILE C C 176.137 0.150 1
487 241 173 ILE CA C 59.706 0.164 1
488 241 173 ILE CB C 38.237 0.079 1
489 241 173 ILE CG1 C 26.258 0.111 1
490 241 173 ILE CG2 C 19.341 0.069 1
491 241 173 ILE CD1 C 14.684 0.041 1
492 241 173 ILE N N 129.965 0.149 1
493 242 174 ALA C C 180.580 0.006 1
494 242 174 ALA CA C 56.269 0.047 1
495 242 174 ALA CB C 18.196 0.081 1
496 242 174 ALA N N 133.068 0.050 1
497 243 175 SER CA C 61.137 0.001 1
498 243 175 SER CB C 61.382 0.181 1
499 243 175 SER N N 112.095 0.065 1
500 244 176 ALA C C 177.639 0.048 1
501 244 176 ALA CA C 54.902 0.074 1
502 244 176 ALA CB C 17.282 0.038 1
503 244 176 ALA N N 127.197 0.134 1
504 245 177 VAL CA C 68.160 0.114 1
505 245 177 VAL CB C 32.174 0.050 1
506 245 177 VAL CG1 C 22.029 0.042 2
507 245 177 VAL CG2 C 22.778 0.078 2
508 245 177 VAL N N 117.272 0.067 1
509 246 178 GLU CA C 59.022 0.063 1
510 246 178 GLU CB C 29.777 0.071 1
511 246 178 GLU CD C 184.022 0.033 1
512 246 178 GLU N N 119.480 0.173 1
513 247 179 ARG C C 179.108 0.022 1
514 247 179 ARG CA C 58.761 0.037 1
515 247 179 ARG CB C 28.879 0.060 1
516 247 179 ARG CG C 26.069 0.049 1
517 247 179 ARG CD C 43.317 0.150 1
518 247 179 ARG N N 117.377 0.114 1
519 248 180 TYR C C 179.257 0.150 1
520 248 180 TYR CA C 63.446 0.134 1
521 248 180 TYR CB C 38.867 0.067 1
522 248 180 TYR CG C 131.564 0.150 1
523 248 180 TYR CE1 C 117.098 0.150 3
524 248 180 TYR CE2 C 120.289 0.150 3
525 248 180 TYR CZ C 158.908 0.150 1
526 248 180 TYR N N 114.901 0.175 1
527 249 181 THR CA C 68.034 0.236 1
528 249 181 THR CB C 68.368 0.103 1
529 249 181 THR N N 117.598 0.228 1
530 250 182 ASP C C 178.164 0.065 1
531 250 182 ASP CA C 57.585 0.076 1
532 250 182 ASP CB C 39.472 0.018 1
533 250 182 ASP CG C 179.786 0.052 1
534 250 182 ASP N N 121.950 0.029 1
535 251 183 GLU C C 178.096 0.150 1
536 251 183 GLU CA C 57.923 0.050 1
537 251 183 GLU CB C 29.752 0.034 1
538 251 183 GLU CG C 34.690 0.150 1
539 251 183 GLU CD C 180.666 0.150 1
540 251 183 GLU N N 120.598 0.072 1
541 252 184 VAL C C 178.566 0.159 1
542 252 184 VAL CA C 67.720 0.092 1
543 252 184 VAL CB C 31.256 0.170 1
544 252 184 VAL CG1 C 24.239 0.116 2
545 252 184 VAL CG2 C 21.504 0.062 2
546 252 184 VAL N N 120.207 0.310 1
547 253 185 ARG C C 179.452 0.088 1
548 253 185 ARG CA C 62.236 0.045 1
549 253 185 ARG CB C 30.276 0.062 1
550 253 185 ARG CD C 43.049 0.150 1
551 253 185 ARG N N 118.711 0.096 1
552 254 186 ARG C C 180.307 0.150 1
553 254 186 ARG CA C 60.416 0.110 1
554 254 186 ARG CB C 29.859 0.013 1
555 254 186 ARG CD C 42.138 0.150 1
556 254 186 ARG N N 124.220 0.088 1
557 256 188 TYR C C 177.736 0.043 1
558 256 188 TYR CA C 64.093 0.096 1
559 256 188 TYR CB C 35.789 0.084 1
560 256 188 TYR CZ C 157.079 0.150 1
561 256 188 TYR N N 118.873 0.048 1
562 257 189 GLY C C 176.675 0.065 1
563 257 189 GLY CA C 47.439 0.056 1
564 257 189 GLY N N 107.687 0.180 1
565 258 190 VAL C C 178.392 0.150 1
566 258 190 VAL CA C 66.560 0.085 1
567 258 190 VAL CB C 31.672 0.144 1
568 258 190 VAL CG1 C 21.003 0.081 2
569 258 190 VAL CG2 C 22.283 0.121 2
570 258 190 VAL N N 124.239 0.329 1
571 259 191 VAL CA C 66.736 0.069 1
572 259 191 VAL CB C 31.778 0.060 1
573 259 191 VAL CG2 C 22.591 0.168 1
574 259 191 VAL N N 120.383 0.041 1
575 260 192 GLU CA C 59.674 0.074 1
576 260 192 GLU CB C 30.087 0.100 1
577 260 192 GLU CG C 37.712 0.112 1
578 260 192 GLU CD C 182.546 0.150 1
579 260 192 GLU N N 120.462 0.112 1
580 261 193 MET CA C 58.382 0.094 1
581 261 193 MET CB C 32.366 0.031 1
582 261 193 MET N N 116.236 0.100 1
583 262 194 ALA CA C 55.294 0.141 1
584 262 194 ALA CB C 18.561 0.018 1
585 262 194 ALA N N 123.279 0.056 1
586 263 195 LEU CA C 57.905 0.085 1
587 263 195 LEU CB C 41.678 0.112 1
588 263 195 LEU CG C 25.740 0.153 1
589 263 195 LEU CD2 C 19.813 0.103 1
590 263 195 LEU N N 120.686 0.074 1
591 264 196 ALA C C 179.119 0.150 1
592 264 196 ALA CA C 55.558 0.049 1
593 264 196 ALA CB C 18.155 0.037 1
594 264 196 ALA N N 121.278 0.101 1
595 265 197 GLU CA C 59.449 0.103 1
596 265 197 GLU CB C 29.313 0.106 1
597 265 197 GLU CG C 36.262 0.153 1
598 265 197 GLU CD C 183.978 0.076 1
599 265 197 GLU N N 119.238 0.095 1
600 266 198 ARG CA C 58.368 0.027 1
601 266 198 ARG CB C 28.821 0.113 1
602 266 198 ARG CD C 42.658 0.150 1
603 266 198 ARG CG C 26.590 0.036 1
604 266 198 ARG N N 120.520 0.177 1
605 267 199 ARG C C 179.296 0.150 1
606 267 199 ARG CA C 58.246 0.110 1
607 267 199 ARG CB C 28.640 0.070 1
608 267 199 ARG CD C 42.078 0.150 1
609 267 199 ARG CG C 26.041 0.092 1
610 267 199 ARG N N 121.170 0.379 1
611 268 200 GLU CA C 59.774 0.074 1
612 268 200 GLU CB C 29.229 0.114 1
613 268 200 GLU CG C 36.598 0.004 1
614 268 200 GLU CD C 183.550 0.053 1
615 268 200 GLU N N 118.935 0.016 1
616 269 201 ALA CA C 54.914 0.093 1
617 269 201 ALA CB C 18.213 0.037 1
618 269 201 ALA N N 118.427 0.114 1
619 270 202 LEU C C 178.780 0.039 1
620 270 202 LEU CA C 58.515 0.090 1
621 270 202 LEU CB C 42.435 0.129 1
622 270 202 LEU CG C 26.823 0.047 1
623 270 202 LEU CD2 C 25.876 0.042 1
624 270 202 LEU N N 120.662 0.026 1
625 271 203 VAL CA C 67.382 0.117 1
626 271 203 VAL CB C 31.693 0.052 1
627 271 203 VAL CG2 C 22.608 0.074 1
628 271 203 VAL N N 119.194 0.036 1
629 275 207 ASP C C 175.572 0.150 1
630 275 207 ASP CA C 50.733 0.022 1
631 275 207 ASP CB C 38.499 0.049 1
632 275 207 ASP CG C 176.823 0.150 1
633 275 207 ASP N N 129.630 0.150 1
634 276 208 THR C C 174.977 0.200 1
635 276 208 THR CA C 63.172 0.070 1
636 276 208 THR CB C 68.960 0.044 1
637 276 208 THR CG2 C 22.066 0.150 1
638 276 208 THR N N 111.980 0.036 1
639 277 209 GLU CA C 55.168 0.106 1
640 277 209 GLU CD C 182.282 0.016 1
641 277 209 GLU N N 117.031 0.165 1
642 283 215 SER C C 171.914 0.052 1
643 283 215 SER CA C 57.067 0.140 1
644 283 215 SER CB C 63.947 0.137 1
645 283 215 SER N N 110.893 0.150 1
646 284 216 ALA C C 178.347 0.070 1
647 284 216 ALA CA C 52.792 0.153 1
648 284 216 ALA CB C 19.528 0.035 1
649 284 216 ALA N N 121.066 0.150 1
650 285 217 GLY C C 177.951 0.052 1
651 285 217 GLY CA C 45.635 0.058 1
652 285 217 GLY N N 105.701 0.078 1
653 286 218 THR C C 177.850 0.013 1
654 286 218 THR CA C 65.204 0.159 1
655 286 218 THR CB C 68.575 0.064 1
656 286 218 THR N N 112.422 0.241 1
657 287 219 THR C C 171.810 0.043 1
658 287 219 THR CA C 59.565 0.077 1
659 287 219 THR CB C 72.840 0.021 1
660 287 219 THR CG2 C 21.824 0.150 1
661 287 219 THR N N 117.125 0.184 1
662 288 220 PRO C C 177.186 0.043 1
663 288 220 PRO CA C 62.456 0.091 1
664 288 220 PRO CB C 32.113 0.048 1
665 288 220 PRO CG C 27.307 0.109 1
666 288 220 PRO CD C 51.536 0.053 1
667 288 220 PRO N N 140.685 0.201 1
668 289 221 MET C C 177.925 0.122 1
669 289 221 MET CB C 32.528 0.176 1
670 289 221 MET CG C 30.249 0.171 1
671 289 221 MET CA C 56.474 0.100 1
672 289 221 MET N N 113.668 0.150 1
673 290 222 SER CA C 61.251 0.143 1
674 290 222 SER CB C 62.975 0.150 1
675 290 222 SER N N 116.596 0.286 1
676 291 223 GLN CA C 59.705 0.064 1
677 291 223 GLN CB C 26.899 0.043 1
678 291 223 GLN CG C 32.693 0.150 1
679 291 223 GLN N N 117.929 0.150 1
680 292 224 SER C C 175.999 0.112 1
681 292 224 SER CA C 61.757 0.070 1
682 292 224 SER CB C 62.939 0.121 1
683 292 224 SER N N 113.445 0.141 1
684 293 225 ARG CA C 57.777 0.088 1
685 293 225 ARG CB C 30.637 0.106 1
686 293 225 ARG CD C 43.300 0.150 1
687 293 225 ARG N N 119.501 0.137 1
688 298 230 PRO C C 178.757 0.101 1
689 298 230 PRO CA C 65.098 0.130 1
690 298 230 PRO CB C 30.137 0.049 1
691 298 230 PRO CG C 26.919 0.089 1
692 298 230 PRO CD C 50.932 0.098 1
693 298 230 PRO N N 141.568 0.150 1
694 299 231 VAL CA C 59.767 0.080 1
695 299 231 VAL CB C 33.604 0.107 1
696 299 231 VAL CG2 C 24.267 0.150 1
697 299 231 VAL N N 117.038 0.048 1
698 300 232 TRP CA C 53.373 0.061 1
699 300 232 TRP CB C 34.999 0.116 1
700 300 232 TRP CG C 112.459 0.150 1
701 300 232 TRP CE2 C 139.085 0.150 1
702 300 232 TRP N N 121.952 0.133 1
703 301 233 LEU CA C 59.193 0.079 1
704 301 233 LEU CB C 42.337 0.117 1
705 301 233 LEU CG C 25.957 0.111 1
706 301 233 LEU CD2 C 19.654 0.082 1
707 301 233 LEU N N 123.036 0.203 1
708 302 234 VAL CA C 61.964 0.063 1
709 302 234 VAL CB C 34.840 0.129 1
710 302 234 VAL CG2 C 21.179 0.086 1
711 302 234 VAL N N 120.293 0.243 1
712 303 235 GLY C C 173.912 0.101 1
713 303 235 GLY CA C 46.444 0.107 1
714 303 235 GLY N N 112.402 0.170 1
715 305 237 LYS C C 175.079 0.028 1
716 305 237 LYS CA C 54.621 0.132 1
717 305 237 LYS CB C 36.399 0.135 1
718 305 237 LYS CG C 23.542 0.014 1
719 305 237 LYS CD C 29.547 0.187 1
720 305 237 LYS N N 116.444 0.062 1
721 306 238 LEU CA C 55.250 0.065 1
722 306 238 LEU CB C 40.629 0.068 1
723 306 238 LEU CD2 C 25.873 0.150 1
724 306 238 LEU N N 115.582 0.193 1
725 307 239 THR C C 176.761 0.150 1
726 307 239 THR CA C 60.381 0.089 1
727 307 239 THR CB C 76.410 0.078 1
728 307 239 THR CG2 C 21.464 0.106 1
729 307 239 THR N N 115.498 0.239 1
730 308 240 ILE C C 175.854 0.150 1
731 308 240 ILE CA C 65.933 0.099 1
732 308 240 ILE CB C 38.817 0.109 1
733 308 240 ILE CG1 C 25.133 0.123 1
734 308 240 ILE CG2 C 21.599 0.067 1
735 308 240 ILE CD1 C 15.414 0.037 1
736 308 240 ILE N N 110.630 0.128 1
737 309 241 ALA C C 176.732 0.082 1
738 309 241 ALA CA C 55.482 0.078 1
739 309 241 ALA CB C 19.208 0.109 1
740 309 241 ALA N N 120.014 0.100 1
741 310 242 ASP C C 178.519 0.078 1
742 310 242 ASP CA C 57.139 0.080 1
743 310 242 ASP CB C 43.855 0.115 1
744 310 242 ASP CG C 179.728 0.039 1
745 310 242 ASP N N 112.043 0.072 1
746 311 243 LEU CA C 56.833 0.096 1
747 311 243 LEU CB C 42.304 0.108 1
748 311 243 LEU CG C 26.178 0.097 1
749 311 243 LEU CD2 C 21.741 0.105 1
750 311 243 LEU N N 113.006 0.131 1
751 312 244 ALA CA C 54.727 0.054 1
752 312 244 ALA CB C 17.911 0.038 1
753 312 244 ALA N N 116.838 0.177 1
754 313 245 PHE CA C 60.662 0.089 1
755 313 245 PHE CB C 40.512 0.091 1
756 313 245 PHE CG C 141.651 0.150 1
757 313 245 PHE CD2 C 135.953 0.150 3
758 313 245 PHE CE1 C 130.133 0.150 3
759 313 245 PHE CE2 C 132.522 0.150 3
760 313 245 PHE CZ C 128.723 0.150 1
761 313 245 PHE N N 106.344 0.089 1
762 314 246 VAL CA C 69.141 0.076 1
763 314 246 VAL CB C 30.439 0.108 1
764 314 246 VAL CG2 C 26.211 0.150 1
765 314 246 VAL N N 118.247 0.314 1
766 315 247 PRO C C 178.488 0.150 1
767 315 247 PRO CA C 65.065 0.125 1
768 315 247 PRO CB C 32.103 0.106 1
769 315 247 PRO CG C 28.954 0.052 1
770 315 247 PRO CD C 49.168 0.084 1
771 315 247 PRO N N 132.102 0.195 1
772 316 248 TRP CA C 58.873 0.075 1
773 316 248 TRP CB C 30.791 0.195 1
774 316 248 TRP CG C 112.467 0.150 1
775 316 248 TRP N N 115.503 0.150 1
776 319 251 VAL CA C 61.555 0.109 1
777 319 251 VAL CB C 33.407 0.111 1
778 319 251 VAL CG1 C 20.286 0.030 2
779 319 251 VAL CG2 C 20.909 0.074 2
780 319 251 VAL N N 111.027 0.150 1
781 320 252 VAL CA C 65.693 0.118 1
782 320 252 VAL CB C 31.512 0.120 1
783 320 252 VAL CG1 C 18.907 0.074 2
784 320 252 VAL CG2 C 22.885 0.170 2
785 320 252 VAL N N 112.078 0.065 1
786 321 253 ASP C C 178.318 0.150 1
787 321 253 ASP CA C 56.630 0.097 1
788 321 253 ASP CB C 38.370 0.150 1
789 321 253 ASP CG C 180.047 0.150 1
790 321 253 ASP N N 123.369 0.280 1
791 322 254 ARG CA C 57.787 0.162 1
792 322 254 ARG CB C 30.711 0.152 1
793 322 254 ARG CG C 27.339 0.164 1
794 322 254 ARG CD C 43.373 0.170 1
795 322 254 ARG N N 119.651 0.159 1
796 323 255 ILE CA C 60.170 0.117 1
797 323 255 ILE CB C 37.285 0.100 1
798 323 255 ILE CG1 C 27.343 0.057 1
799 323 255 ILE CG2 C 18.127 0.094 1
800 323 255 ILE CD1 C 15.704 0.080 1
801 323 255 ILE N N 109.386 0.125 1
802 324 256 GLY C C 173.729 0.014 1
803 324 256 GLY CA C 46.190 0.175 1
804 324 256 GLY N N 108.507 0.229 1
805 325 257 ILE CA C 60.559 0.110 1
806 325 257 ILE CB C 38.584 0.086 1
807 325 257 ILE CG1 C 27.582 0.085 1
808 325 257 ILE CG2 C 16.800 0.030 1
809 325 257 ILE CD1 C 15.144 0.041 1
810 325 257 ILE N N 119.546 0.141 1
811 326 258 ASN C C 175.032 0.150 1
812 326 258 ASN CA C 50.668 0.096 1
813 326 258 ASN CB C 38.400 0.068 1
814 326 258 ASN CG C 176.774 0.150 1
815 326 258 ASN N N 128.844 0.107 1
816 327 259 ILE C C 178.621 0.150 1
817 327 259 ILE CA C 66.684 0.146 1
818 327 259 ILE CB C 37.805 0.059 1
819 327 259 ILE CG1 C 28.804 0.031 1
820 327 259 ILE CG2 C 18.279 0.004 1
821 327 259 ILE CD1 C 13.490 0.030 1
822 327 259 ILE N N 122.776 0.180 1
823 328 260 LYS C C 176.647 0.150 1
824 328 260 LYS CA C 59.802 0.118 1
825 328 260 LYS CB C 32.689 0.195 1
826 328 260 LYS CG C 24.601 0.144 1
827 328 260 LYS CD C 29.309 0.116 1
828 328 260 LYS CE C 42.068 0.007 1
829 328 260 LYS N N 117.385 0.100 1
830 329 261 ILE CA C 60.985 0.188 1
831 329 261 ILE CB C 38.799 0.081 1
832 329 261 ILE CG1 C 27.687 0.070 1
833 329 261 ILE CG2 C 17.004 0.084 1
834 329 261 ILE CD1 C 15.211 0.150 1
835 329 261 ILE N N 111.172 0.039 1
836 330 262 GLU C C 176.677 0.150 1
837 330 262 GLU CA C 59.496 0.094 1
838 330 262 GLU CB C 33.522 0.107 1
839 330 262 GLU CG C 38.416 0.082 1
840 330 262 GLU CD C 184.042 0.022 1
841 330 262 GLU N N 117.422 0.087 1
842 331 263 PHE C C 173.587 0.150 1
843 331 263 PHE CA C 55.253 0.164 1
844 331 263 PHE CB C 40.477 0.097 1
845 331 263 PHE CG C 139.945 0.150 1
846 331 263 PHE CE2 C 132.739 0.080 3
847 331 263 PHE CZ C 129.915 0.150 1
848 331 263 PHE N N 115.507 0.230 1
849 332 264 PRO C C 181.019 0.150 1
850 332 264 PRO CA C 65.866 0.087 1
851 332 264 PRO CB C 32.682 0.097 1
852 332 264 PRO CG C 27.545 0.088 1
853 332 264 PRO CD C 49.770 0.117 1
854 332 264 PRO N N 135.634 0.153 1
855 333 265 GLU C C 181.019 0.150 1
856 333 265 GLU CA C 59.482 0.075 1
857 333 265 GLU CB C 27.671 0.054 1
858 333 265 GLU CG C 35.796 0.080 1
859 333 265 GLU CD C 183.323 0.100 1
860 333 265 GLU N N 124.223 0.149 1
861 334 266 VAL C C 180.197 0.150 1
862 334 266 VAL CA C 65.852 0.138 1
863 334 266 VAL CB C 30.523 0.074 1
864 334 266 VAL CG1 C 22.832 0.084 2
865 334 266 VAL CG2 C 21.629 0.094 2
866 334 266 VAL N N 128.296 0.091 1
867 335 267 TYR C C 176.490 0.020 1
868 335 267 TYR CA C 62.443 0.092 1
869 335 267 TYR CB C 37.910 0.068 1
870 335 267 TYR CG C 129.274 0.054 1
871 335 267 TYR CD1 C 132.682 0.150 3
872 335 267 TYR CD2 C 133.074 0.027 3
873 335 267 TYR CE1 C 118.307 0.150 3
874 335 267 TYR CE2 C 118.616 0.088 3
875 335 267 TYR CZ C 157.660 0.055 1
876 335 267 TYR N N 123.760 0.084 1
877 336 268 LYS CA C 60.558 0.090 1
878 336 268 LYS CB C 32.330 0.194 1
879 336 268 LYS CG C 25.064 0.150 1
880 336 268 LYS CE C 42.726 0.150 1
881 336 268 LYS N N 119.431 0.092 1
882 337 269 TRP CA C 59.160 0.077 1
883 337 269 TRP CB C 31.001 0.065 1
884 337 269 TRP CG C 108.612 0.150 1
885 337 269 TRP CD1 C 130.141 0.137 1
886 337 269 TRP CD2 C 132.622 0.170 1
887 337 269 TRP CE2 C 139.371 0.121 1
888 337 269 TRP CZ2 C 114.609 0.150 1
889 337 269 TRP CH2 C 123.652 0.150 1
890 337 269 TRP N N 122.609 0.090 1
891 338 270 THR C C 176.599 0.017 1
892 338 270 THR CA C 67.904 0.080 1
893 338 270 THR CB C 69.160 0.067 1
894 338 270 THR CG2 C 21.367 0.150 1
895 338 270 THR N N 115.290 0.174 1
896 339 271 LYS CA C 59.165 0.065 1
897 339 271 LYS CB C 30.731 0.081 1
898 339 271 LYS CG C 23.848 0.024 1
899 339 271 LYS CD C 27.470 0.150 1
900 339 271 LYS CE C 43.018 0.150 1
901 339 271 LYS N N 121.806 0.196 1
902 343 275 ARG CA C 56.911 0.115 1
903 343 275 ARG CB C 31.800 0.121 1
904 343 275 ARG CG C 28.133 0.043 1
905 343 275 ARG CD C 43.973 0.150 1
906 343 275 ARG N N 116.010 0.150 1
907 344 276 ARG CA C 55.186 0.072 1
908 344 276 ARG CB C 29.503 0.041 1
909 344 276 ARG CG C 28.123 0.150 1
910 344 276 ARG CD C 42.732 0.022 1
911 344 276 ARG N N 120.926 0.051 1
912 345 277 PRO CA C 65.578 0.051 1
913 345 277 PRO CB C 32.170 0.103 1
914 345 277 PRO CG C 27.784 0.067 1
915 345 277 PRO CD C 50.805 0.072 1
916 345 277 PRO N N 137.402 0.080 1
917 346 278 ALA C C 180.187 0.017 1
918 346 278 ALA CA C 55.066 0.107 1
919 346 278 ALA CB C 17.769 0.064 1
920 346 278 ALA N N 118.499 0.128 1
921 347 279 VAL C C 176.813 0.074 1
922 347 279 VAL CA C 66.330 0.063 1
923 347 279 VAL CB C 31.733 0.041 1
924 347 279 VAL CG1 C 22.300 0.049 2
925 347 279 VAL CG2 C 22.825 0.074 2
926 347 279 VAL N N 119.402 0.145 1
927 348 280 ILE C C 179.191 0.150 1
928 348 280 ILE CA C 65.081 0.093 1
929 348 280 ILE CB C 38.696 0.046 1
930 348 280 ILE CG1 C 29.641 0.036 1
931 348 280 ILE CG2 C 17.031 0.150 1
932 348 280 ILE CD1 C 14.156 0.150 1
933 348 280 ILE N N 118.660 0.044 1
934 349 281 LYS C C 179.208 0.059 1
935 349 281 LYS CA C 59.430 0.097 1
936 349 281 LYS CB C 32.904 0.050 1
937 349 281 LYS CG C 24.682 0.030 1
938 349 281 LYS CD C 30.024 0.150 1
939 349 281 LYS CE C 42.097 0.150 1
940 349 281 LYS N N 117.443 0.272 1
941 350 282 ALA CA C 54.584 0.073 1
942 350 282 ALA CB C 19.383 0.052 1
943 350 282 ALA N N 121.341 0.114 1
stop_
save_